data_9EMI
# 
_entry.id   9EMI 
# 
_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   9EMI         pdb_00009emi 10.2210/pdb9emi/pdb 
WWPDB D_1292137165 ?            ?                   
# 
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                        9EMI 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-08 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'KOD-H4, apo structure'                                   8S87 unspecified 
PDB 'KOD-H4, DNA:DNA, binary,'                                8S8T unspecified 
PDB 'KOD-H4, DNA:DNA, ternary, non-hydrolyzable triphosphate' 8S84 unspecified 
PDB 'KOD-H4, binary, one HNA nucleotide'                      9EMF unspecified 
PDB 'KOD-H4, binary, two HNA nucleotides'                     9EMH unspecified 
# 
_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(*(6HA)P*(6HA)P*(6HC)P*(6HT)P*(6HG)P*(6HT)P*GP*GP*CP*CP*GP*TP*GP*GP*TP*C)-3')
;
5014.349  1  ?       ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                                                                               62.068    3  ? ? ? 
? 
5 non-polymer syn 'MAGNESIUM ION'                                                                              24.305    2  ? ? ? 
? 
6 non-polymer syn "2'-deoxy-5'-O-[(R)-hydroxy{[(R)-hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl]guanosine" 506.196   1  ? ? ? 
? 
7 water       nat water                                                                                        18.015    32 ? ? ? 
? 
# 
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 yes '(6HA)(6HA)(6HC)(6HT)(6HG)(6HT)(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 1,2-ETHANEDIOL                                                                               EDO 
5 'MAGNESIUM ION'                                                                              MG  
6 "2'-deoxy-5'-O-[(R)-hydroxy{[(R)-hydroxy(phosphonooxy)phosphoryl]amino}phosphoryl]guanosine" XG4 
7 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   6HA n 
3 2   6HA n 
3 3   6HC n 
3 4   6HT n 
3 5   6HG n 
3 6   6HT 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 
6HA 'DNA linking'       n "1',5'-ANHYDRO-2',3'-DIDEOXY-2'-(ADENIN-9-YL)-6'-O-PHOSPHORYL-D-ARABINO-HEXITOL"             ? 
'C11 H16 N5 O6 P'   345.248 
6HC 'DNA linking'       n "1',5'-ANHYDRO-2',3'-DIDEOXY-2'-(CYTOSIN-1-YL)-6'-O-PHOSPHORYL-D-ARABINO-HEXITOL"            ? 
'C10 H16 N3 O7 P'   321.224 
6HG 'DNA linking'       n "1',5'-ANHYDRO-2',3'-DIDEOXY-2'-(GUANIN-9-YL)-6'-O-PHOSPHORYL-D-ARABINO-HEXITOL"             ? 
'C11 H16 N5 O7 P'   361.248 
6HT 'DNA linking'       n "1',5'-ANHYDRO-2',3'-DIDEOXY-2'-(THYMIN-1-YL)-6'-O-PHOSPHORYL-D-ARABINO-HEXITOL"             ? 
'C11 H17 N2 O8 P'   336.235 
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 
EDO non-polymer         . 1,2-ETHANEDIOL                                                                               
'ETHYLENE GLYCOL' 'C2 H6 O2'          62.068  
GLN 'L-peptide linking' y GLUTAMINE                                                                                    ? 
'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                              ? 
'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                                                                      ? 
'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                    ? 
'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                                                                                        ? 'H2 O' 
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                   ? 
'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                      ? 
'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                                                                                       ? 
'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                                                                                   ? 
'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'                                                                              ? 'Mg 2' 
24.305  
PHE 'L-peptide linking' y PHENYLALANINE                                                                                ? 
'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                                                                                      ? 
'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                                                                                       ? 
'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                                                                                    ? 
'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                   ? 
'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                     ? 
'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                                                                                       ? 
'C5 H11 N O2'       117.146 
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   6HA 1   1   1   6HA 6HA T . n 
C 3 2   6HA 2   2   2   6HA 6HA T . n 
C 3 3   6HC 3   3   3   6HC 6HC T . n 
C 3 4   6HT 4   4   4   6HT 6HT T . n 
C 3 5   6HG 5   5   5   6HG 6HG T . n 
C 3 6   6HT 6   6   6   6HT 6HT 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 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 6HC ? ? 6HC ? ? 'SUBJECT OF INVESTIGATION' ? 
2 6HA ? ? 6HA ? ? 'SUBJECT OF INVESTIGATION' ? 
3 6HG ? ? 6HG ? ? 'SUBJECT OF INVESTIGATION' ? 
4 6HT ? ? 6HT ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 4 EDO 1  801 4  EDO EDO A . 
E 5 MG  1  802 15 MG  MG  A . 
F 6 XG4 1  803 14 XG4 XG4 A . 
G 4 EDO 1  101 8  EDO EDO P . 
H 5 MG  1  102 16 MG  MG  P . 
I 4 EDO 1  101 7  EDO EDO T . 
J 7 HOH 1  901 20 HOH HOH A . 
J 7 HOH 2  902 13 HOH HOH A . 
J 7 HOH 3  903 11 HOH HOH A . 
J 7 HOH 4  904 5  HOH HOH A . 
J 7 HOH 5  905 8  HOH HOH A . 
J 7 HOH 6  906 22 HOH HOH A . 
J 7 HOH 7  907 3  HOH HOH A . 
J 7 HOH 8  908 19 HOH HOH A . 
J 7 HOH 9  909 1  HOH HOH A . 
J 7 HOH 10 910 17 HOH HOH A . 
J 7 HOH 11 911 23 HOH HOH A . 
J 7 HOH 12 912 6  HOH HOH A . 
J 7 HOH 13 913 12 HOH HOH A . 
J 7 HOH 14 914 27 HOH HOH A . 
J 7 HOH 15 915 10 HOH HOH A . 
J 7 HOH 16 916 29 HOH HOH A . 
J 7 HOH 17 917 2  HOH HOH A . 
J 7 HOH 18 918 16 HOH HOH A . 
J 7 HOH 19 919 32 HOH HOH A . 
J 7 HOH 20 920 7  HOH HOH A . 
J 7 HOH 21 921 14 HOH HOH A . 
J 7 HOH 22 922 4  HOH HOH A . 
J 7 HOH 23 923 15 HOH HOH A . 
J 7 HOH 24 924 18 HOH HOH A . 
J 7 HOH 25 925 9  HOH HOH A . 
J 7 HOH 26 926 26 HOH HOH A . 
J 7 HOH 27 927 31 HOH HOH A . 
J 7 HOH 28 928 24 HOH HOH A . 
J 7 HOH 29 929 21 HOH HOH A . 
J 7 HOH 30 930 25 HOH HOH A . 
K 7 HOH 1  201 30 HOH HOH T . 
K 7 HOH 2  202 28 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                     9EMI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     111.454 
_cell.length_a_esd                 ? 
_cell.length_b                     151.548 
_cell.length_b_esd                 ? 
_cell.length_c                     70.406 
_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                         9EMI 
_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                   9EMI 
_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          58.87 
_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    
;10% w/v PEG 8000, 20% v/v ethylene glycol 0.02 M D-glucose, 0.02 M D-mannose, 0.02 M D-galactose,  0.02 M L-fucose, 0.02 M  D-xylose, 0.02 M N-acetyl-D-glucosamine , 0.1 M bicine/Trizma base pH 8.5
;
_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         2023-07-13 
_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   0.976250 
_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                        'EMBL/DESY, HAMBURG BEAMLINE X13' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976250 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X13 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EMI 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.26 
_reflns.d_resolution_low                               46.809 
_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                                     101092 
_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                           93.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.44 
_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                                   0.996 
_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                                    2.26 
_reflns_shell.d_res_low                                     2.40 
_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                             17452 
_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                                  0.237 
_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                                 9EMI 
_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                            2.27 
_refine.ls_d_res_low                             41.04 
_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                     98883 
_refine.ls_number_reflns_R_free                  3816 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.75 
_refine.ls_percent_reflns_R_free                 3.86 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2357 
_refine.ls_R_factor_R_free                       0.2654 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2345 
_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                          1.30 
_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                 36.18 
_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                            0.49 
_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.pdbx_number_atoms_protein        6200 
_refine_hist.pdbx_number_atoms_nucleic_acid   625 
_refine_hist.pdbx_number_atoms_ligand         14 
_refine_hist.number_atoms_solvent             32 
_refine_hist.number_atoms_total               6871 
_refine_hist.d_res_high                       2.27 
_refine_hist.d_res_low                        41.04 
# 
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  ? 7055 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.641  ? 9627 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.695 ? 1128 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.044  ? 1030 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 1128 ? 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' 2.27 2.30  . . 122 2990 79.00  . . . . 0.5065 . . . . . . . . . . . 0.5091 
'X-RAY DIFFRACTION' 2.30 2.33  . . 150 3761 99.00  . . . . 0.4590 . . . . . . . . . . . 0.4680 
'X-RAY DIFFRACTION' 2.33 2.36  . . 150 3782 100.00 . . . . 0.4447 . . . . . . . . . . . 0.4516 
'X-RAY DIFFRACTION' 2.36 2.39  . . 151 3804 100.00 . . . . 0.4404 . . . . . . . . . . . 0.4352 
'X-RAY DIFFRACTION' 2.39 2.43  . . 153 3809 100.00 . . . . 0.4241 . . . . . . . . . . . 0.4115 
'X-RAY DIFFRACTION' 2.43 2.47  . . 153 3751 100.00 . . . . 0.3916 . . . . . . . . . . . 0.4462 
'X-RAY DIFFRACTION' 2.47 2.51  . . 154 3816 100.00 . . . . 0.3844 . . . . . . . . . . . 0.4042 
'X-RAY DIFFRACTION' 2.51 2.55  . . 155 3760 100.00 . . . . 0.3618 . . . . . . . . . . . 0.3405 
'X-RAY DIFFRACTION' 2.55 2.60  . . 148 3814 100.00 . . . . 0.3729 . . . . . . . . . . . 0.4051 
'X-RAY DIFFRACTION' 2.60 2.65  . . 147 3715 98.00  . . . . 0.3560 . . . . . . . . . . . 0.4289 
'X-RAY DIFFRACTION' 2.65 2.70  . . 61  1442 38.00  . . . . 0.3706 . . . . . . . . . . . 0.4083 
'X-RAY DIFFRACTION' 2.70 2.76  . . 151 3771 100.00 . . . . 0.3243 . . . . . . . . . . . 0.3728 
'X-RAY DIFFRACTION' 2.76 2.82  . . 156 3803 100.00 . . . . 0.3265 . . . . . . . . . . . 0.3265 
'X-RAY DIFFRACTION' 2.82 2.89  . . 151 3769 100.00 . . . . 0.3224 . . . . . . . . . . . 0.3484 
'X-RAY DIFFRACTION' 2.89 2.97  . . 148 3784 100.00 . . . . 0.3177 . . . . . . . . . . . 0.3877 
'X-RAY DIFFRACTION' 2.97 3.06  . . 156 3850 100.00 . . . . 0.2944 . . . . . . . . . . . 0.3175 
'X-RAY DIFFRACTION' 3.06 3.16  . . 152 3749 100.00 . . . . 0.2765 . . . . . . . . . . . 0.3253 
'X-RAY DIFFRACTION' 3.16 3.27  . . 147 3824 100.00 . . . . 0.2653 . . . . . . . . . . . 0.3278 
'X-RAY DIFFRACTION' 3.27 3.40  . . 152 3782 100.00 . . . . 0.2436 . . . . . . . . . . . 0.3525 
'X-RAY DIFFRACTION' 3.40 3.56  . . 90  2104 55.00  . . . . 0.2446 . . . . . . . . . . . 0.2550 
'X-RAY DIFFRACTION' 3.56 3.74  . . 98  2454 65.00  . . . . 0.2224 . . . . . . . . . . . 0.2415 
'X-RAY DIFFRACTION' 3.75 3.98  . . 110 2795 73.00  . . . . 0.2042 . . . . . . . . . . . 0.2294 
'X-RAY DIFFRACTION' 3.98 4.29  . . 153 3787 100.00 . . . . 0.1734 . . . . . . . . . . . 0.2044 
'X-RAY DIFFRACTION' 4.29 4.72  . . 152 3787 100.00 . . . . 0.1525 . . . . . . . . . . . 0.2202 
'X-RAY DIFFRACTION' 4.72 5.40  . . 153 3774 100.00 . . . . 0.1648 . . . . . . . . . . . 0.1870 
'X-RAY DIFFRACTION' 5.40 6.80  . . 150 3783 100.00 . . . . 0.1860 . . . . . . . . . . . 0.2382 
'X-RAY DIFFRACTION' 6.80 41.04 . . 153 3807 100.00 . . . . 0.1555 . . . . . . . . . . . 0.1359 
# 
_struct.entry_id                     9EMI 
_struct.title                        
'KOD-H4 DNA polymerase mutant in a ternary complex containing six HNA nucleotides and a 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        9EMI 
_struct_keywords.text            
'Polymerase, XNA, modified nucleotides, Reverse transcriptase, HNA, non-hydrolyzable triphosphate, 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 5 ? 
F N N 6 ? 
G N N 4 ? 
H N N 5 ? 
I N N 4 ? 
J N N 7 ? 
K N N 7 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP D0VWU9_THEKO D0VWU9 ? 1 
;MILDTDYITEDGKPVIRIFKKENGEFKIEYDRTFEPYFYALLKDDSAIEEVKKITAERHGTVVTVKRVEKVQKKFLGRPV
EVWKLYFTHPQDVPAIRDKIREHPAVIDIYEYDIPFAKRYLIDKGLVPMEGDEELKMLAFDIETLYEEGEEFAEGPILMI
SYADEEGARVITWKNVDLPYVDVVSTEREMIKRFLRVVKEKDPDVLITYNGDNFDFAYLKKRCEKLGINFALGRDGSEPK
IQRMGDRFAVEVKGRIHFDLYPVIRRTINLPTYTLEAVYEAVFGQPKEKVYAEEITTAWETGENLERVARYSMEDAKVTY
ELGKEFLPMEAQLSRLIGQSLWDVSRSSTGNLVEWFLLRKAYERNELAPNKPDEKELARRRQSYEGGYVKEPERGLWENI
VYLDFRSLYPSIIITHNVSPDTLNREGCKEYDVAPQVGHRFCKDFPGFIPSLLGDLLEERQKIKKKMKATIDPIERKLLD
YRQRAIKILANSYYGYYGYARARWYCKECAESVTAWGREYITMTIKEIEEKYGFKVIYSDTDGFFATIPGADAETVKKKA
MEFLKYINAKLPGALELEYEGFYERGFFVTKKKYAVIDEEGKITTRGLEIVRRDWSEIAKETQARVLEALLKDGDVEKAV
RIVKEVTEKLSKYEVPPEKLVIHEQITRDLKDYKATGPHVAVAKRLAARGVKIRPGTVISYIVLKGSGRIGDRAIPFDEF
DPTKHKYDAEYYIENQVLPAVERILRAFGYRKEDLRYQKTRQVGLSAWLKPKGT
;
1 
2 PDB 9EMI         9EMI   ? 2 ? 1 
3 PDB 9EMI         9EMI   ? 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 9EMI A 1 ? 774 ? D0VWU9 1 ? 774 ? 1 774 
2 2 9EMI P 1 ? 13  ? 9EMI   1 ? 13  ? 1 13  
3 3 9EMI T 1 ? 16  ? 9EMI   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 9EMI GLN A 93  ? UNP D0VWU9 VAL 93  conflict 93  1  
1 9EMI THR A 114 ? UNP D0VWU9 ILE 114 conflict 114 2  
1 9EMI ALA A 141 ? UNP D0VWU9 ASP 141 conflict 141 3  
1 9EMI ALA A 143 ? UNP D0VWU9 GLU 143 conflict 143 4  
1 9EMI HIS A 147 ? UNP D0VWU9 GLU 147 conflict 147 5  
1 9EMI LYS A 383 ? UNP D0VWU9 SER 383 conflict 383 6  
1 9EMI GLY A 429 ? UNP D0VWU9 LYS 429 conflict 429 7  
1 9EMI LEU A 445 ? UNP D0VWU9 PHE 445 conflict 445 8  
1 9EMI LEU A 485 ? UNP D0VWU9 ALA 485 conflict 485 9  
1 9EMI VAL A 493 ? UNP D0VWU9 TYR 493 conflict 493 10 
1 9EMI HIS A 496 ? UNP D0VWU9 TYR 496 conflict 496 11 
1 9EMI MET A 497 ? UNP D0VWU9 TYR 497 conflict 497 12 
1 9EMI PHE A 499 ? UNP D0VWU9 TYR 499 conflict 499 13 
1 9EMI GLU A 500 ? UNP D0VWU9 ALA 500 conflict 500 14 
1 9EMI ASN A 501 ? UNP D0VWU9 ARG 501 conflict 501 15 
1 9EMI LEU A 521 ? UNP D0VWU9 ILE 521 conflict 521 16 
1 9EMI LYS A 584 ? UNP D0VWU9 GLU 584 conflict 584 17 
1 9EMI LYS A 664 ? UNP D0VWU9 GLU 664 conflict 664 18 
1 9EMI ARG A 726 ? UNP D0VWU9 LYS 726 conflict 726 19 
1 9EMI LYS A 735 ? UNP D0VWU9 ASN 735 conflict 735 20 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 8830  ? 
1 MORE         -25   ? 
1 'SSA (A^2)'  35670 ? 
# 
_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 
# 
_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]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ALA A 47  ? LYS A 52  ? ALA A 47  LYS A 52  1 ? 6  
HELX_P HELX_P2  AA2 GLN A 91  ? HIS A 103 ? GLN A 91  HIS A 103 1 ? 13 
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 347 ? SER A 340 SER A 347 1 ? 8  
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 GLY A 447 ? THR A 470 ? GLY A 447 THR A 470 1 ? 24 
HELX_P HELX_P15 AB6 ASP A 472 ? MET A 497 ? ASP A 472 MET A 497 1 ? 26 
HELX_P HELX_P16 AB7 CYS A 506 ? LYS A 531 ? CYS A 506 LYS A 531 1 ? 26 
HELX_P HELX_P17 AB8 ASP A 552 ? LEU A 571 ? ASP A 552 LEU A 571 1 ? 20 
HELX_P HELX_P18 AB9 LEU A 608 ? ARG A 612 ? LEU A 608 ARG A 612 5 ? 5  
HELX_P HELX_P19 AC1 SER A 616 ? GLY A 634 ? SER A 616 GLY A 634 1 ? 19 
HELX_P HELX_P20 AC2 ASP A 635 ? LYS A 652 ? ASP A 635 LYS A 652 1 ? 18 
HELX_P HELX_P21 AC3 PRO A 656 ? VAL A 661 ? PRO A 656 VAL A 661 5 ? 6  
HELX_P HELX_P22 AC4 ASP A 669 ? TYR A 673 ? ASP A 669 TYR A 673 5 ? 5  
HELX_P HELX_P23 AC5 GLY A 677 ? ARG A 689 ? GLY A 677 ARG A 689 1 ? 13 
HELX_P HELX_P24 AC6 ARG A 709 ? ASP A 712 ? ARG A 709 ASP A 712 5 ? 4  
HELX_P HELX_P25 AC7 ASP A 718 ? PHE A 720 ? ASP A 718 PHE A 720 5 ? 3  
HELX_P HELX_P26 AC8 ASP A 728 ? LYS A 735 ? ASP A 728 LYS A 735 1 ? 8  
HELX_P HELX_P27 AC9 GLN A 736 ? ARG A 746 ? GLN A 736 ARG A 746 1 ? 11 
HELX_P HELX_P28 AD1 ALA A 747 ? GLY A 749 ? ALA A 747 GLY A 749 5 ? 3  
HELX_P HELX_P29 AD2 ARG A 751 ? LEU A 755 ? ARG A 751 LEU A 755 5 ? 5  
# 
_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 428 SG    ? ? ? 1_555 A CYS 442 SG  ? ? A CYS 428 A CYS 442 1_555 ? ? ? ? ? ? ?            2.037 ? ? 
disulf2  disulf ?    ? A CYS 506 SG    ? ? ? 1_555 A CYS 509 SG  ? ? A CYS 506 A CYS 509 1_555 ? ? ? ? ? ? ?            2.039 ? ? 
covale1  covale both ? C 6HA 1   "O3'" ? ? ? 1_555 C 6HA 2   P   ? ? T 6HA 1   T 6HA 2   1_555 ? ? ? ? ? ? ?            1.559 ? ? 
covale2  covale both ? C 6HA 2   "O3'" ? ? ? 1_555 C 6HC 3   P   ? ? T 6HA 2   T 6HC 3   1_555 ? ? ? ? ? ? ?            1.559 ? ? 
covale3  covale both ? C 6HC 3   "O3'" ? ? ? 1_555 C 6HT 4   P   ? ? T 6HC 3   T 6HT 4   1_555 ? ? ? ? ? ? ?            1.557 ? ? 
covale4  covale both ? C 6HT 4   "O3'" ? ? ? 1_555 C 6HG 5   P   ? ? T 6HT 4   T 6HG 5   1_555 ? ? ? ? ? ? ?            1.559 ? ? 
covale5  covale both ? C 6HG 5   "O3'" ? ? ? 1_555 C 6HT 6   P   ? ? T 6HG 5   T 6HT 6   1_555 ? ? ? ? ? ? ?            1.557 ? ? 
covale6  covale both ? C 6HT 6   "O3'" ? ? ? 1_555 C DG  7   P   ? ? T 6HT 6   T DG  7   1_555 ? ? ? ? ? ? ?            1.601 ? ? 
metalc1  metalc ?    ? A ASP 404 OD2   ? ? ? 1_555 E MG  .   MG  ? ? A ASP 404 A MG  802 1_555 ? ? ? ? ? ? ?            2.700 ? ? 
metalc2  metalc ?    ? A PHE 405 O     ? ? ? 1_555 E MG  .   MG  ? ? A PHE 405 A MG  802 1_555 ? ? ? ? ? ? ?            2.996 ? ? 
metalc3  metalc ?    ? A GLU 580 OE2   ? ? ? 1_555 E MG  .   MG  ? ? A GLU 580 A MG  802 1_555 ? ? ? ? ? ? ?            2.459 ? ? 
metalc4  metalc ?    ? E MG  .   MG    ? ? ? 1_555 F XG4 .   O1G ? ? A MG  802 A XG4 803 1_555 ? ? ? ? ? ? ?            2.821 ? ? 
metalc5  metalc ?    ? E MG  .   MG    ? ? ? 1_555 J HOH .   O   ? ? A MG  802 A HOH 904 1_555 ? ? ? ? ? ? ?            2.352 ? ? 
metalc6  metalc ?    ? E MG  .   MG    ? ? ? 1_555 J HOH .   O   ? ? A MG  802 A HOH 905 1_555 ? ? ? ? ? ? ?            2.489 ? ? 
metalc7  metalc ?    ? F XG4 .   O2A   ? ? ? 1_555 H MG  .   MG  ? ? A XG4 803 P MG  102 1_555 ? ? ? ? ? ? ?            2.184 ? ? 
metalc8  metalc ?    ? J HOH .   O     ? ? ? 1_555 H MG  .   MG  ? ? A HOH 914 P MG  102 1_555 ? ? ? ? ? ? ?            2.206 ? ? 
metalc9  metalc ?    ? J HOH .   O     ? ? ? 1_555 H MG  .   MG  ? ? A HOH 926 P MG  102 1_555 ? ? ? ? ? ? ?            2.218 ? ? 
metalc10 metalc ?    ? B DA  13  "O3'" ? ? ? 1_555 H MG  .   MG  ? ? P DA  13  P MG  102 1_555 ? ? ? ? ? ? ?            2.297 ? ? 
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 6HT 6   N3  ? ? P DA  11  T 6HT 6   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog30 hydrog ?    ? B DA  11  N6    ? ? ? 1_555 C 6HT 6   O4  ? ? P DA  11  T 6HT 6   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog31 hydrog ?    ? B DC  12  N3    ? ? ? 1_555 C 6HG 5   N1  ? ? P DC  12  T 6HG 5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog32 hydrog ?    ? B DC  12  N4    ? ? ? 1_555 C 6HG 5   O6  ? ? P DC  12  T 6HG 5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog33 hydrog ?    ? B DC  12  O2    ? ? ? 1_555 C 6HG 5   N2  ? ? P DC  12  T 6HG 5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog34 hydrog ?    ? B DA  13  N1    ? ? ? 1_555 C 6HT 4   N3  ? ? P DA  13  T 6HT 4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog35 hydrog ?    ? B DA  13  N6    ? ? ? 1_555 C 6HT 4   O4  ? ? P DA  13  T 6HT 4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
hydrog ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  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 84.5  ? 
2  OD2 ? A ASP 404 ? A ASP 404 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 OE2   ? A GLU 580 ? A GLU 580 ? 1_555 80.9  ? 
3  O   ? A PHE 405 ? A PHE 405 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 OE2   ? A GLU 580 ? A GLU 580 ? 1_555 120.1 ? 
4  OD2 ? A ASP 404 ? A ASP 404 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 O1G   ? F XG4 .   ? A XG4 803 ? 1_555 113.3 ? 
5  O   ? A PHE 405 ? A PHE 405 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 O1G   ? F XG4 .   ? A XG4 803 ? 1_555 144.6 ? 
6  OE2 ? A GLU 580 ? A GLU 580 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 O1G   ? F XG4 .   ? A XG4 803 ? 1_555 93.6  ? 
7  OD2 ? A ASP 404 ? A ASP 404 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 O     ? J HOH .   ? A HOH 904 ? 1_555 63.7  ? 
8  O   ? A PHE 405 ? A PHE 405 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 O     ? J HOH .   ? A HOH 904 ? 1_555 147.6 ? 
9  OE2 ? A GLU 580 ? A GLU 580 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 O     ? J HOH .   ? A HOH 904 ? 1_555 63.3  ? 
10 O1G ? F XG4 .   ? A XG4 803 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 O     ? J HOH .   ? A HOH 904 ? 1_555 55.4  ? 
11 OD2 ? A ASP 404 ? A ASP 404 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 O     ? J HOH .   ? A HOH 905 ? 1_555 138.5 ? 
12 O   ? A PHE 405 ? A PHE 405 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 O     ? J HOH .   ? A HOH 905 ? 1_555 123.5 ? 
13 OE2 ? A GLU 580 ? A GLU 580 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 O     ? J HOH .   ? A HOH 905 ? 1_555 59.2  ? 
14 O1G ? F XG4 .   ? A XG4 803 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 O     ? J HOH .   ? A HOH 905 ? 1_555 63.0  ? 
15 O   ? J HOH .   ? A HOH 904 ? 1_555 MG ? E MG . ? A MG 802 ? 1_555 O     ? J HOH .   ? A HOH 905 ? 1_555 87.0  ? 
16 O2A ? F XG4 .   ? A XG4 803 ? 1_555 MG ? H MG . ? P MG 102 ? 1_555 O     ? J HOH .   ? A HOH 914 ? 1_555 74.6  ? 
17 O2A ? F XG4 .   ? A XG4 803 ? 1_555 MG ? H MG . ? P MG 102 ? 1_555 O     ? J HOH .   ? A HOH 926 ? 1_555 148.1 ? 
18 O   ? J HOH .   ? A HOH 914 ? 1_555 MG ? H MG . ? P MG 102 ? 1_555 O     ? J HOH .   ? A HOH 926 ? 1_555 89.4  ? 
19 O2A ? F XG4 .   ? A XG4 803 ? 1_555 MG ? H MG . ? P MG 102 ? 1_555 "O3'" ? B DA  13  ? P DA  13  ? 1_555 98.9  ? 
20 O   ? J HOH .   ? A HOH 914 ? 1_555 MG ? H MG . ? P MG 102 ? 1_555 "O3'" ? B DA  13  ? P DA  13  ? 1_555 165.0 ? 
21 O   ? J HOH .   ? A HOH 926 ? 1_555 MG ? H MG . ? P MG 102 ? 1_555 "O3'" ? B DA  13  ? P DA  13  ? 1_555 89.6  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 428 ? CYS A 442 ? CYS A 428 ? 1_555 CYS A 442 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 506 ? CYS A 509 ? CYS A 506 ? 1_555 CYS A 509 ? 1_555 SG SG . . . None '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 ALA A 56  ? GLU A 57  ? ALA A 56  GLU A 57  
AA3 2 VAL A 62  ? VAL A 63  ? VAL A 62  VAL A 63  
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 ? MET A 244 ? LYS A 240 MET A 244 
AA5 2 ARG A 247 ? GLU A 251 ? ARG A 247 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 ? ILE A 597 ? LYS A 593 ILE A 597 
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 GLU A 10  ? N GLU A 10  O LYS A 13  ? O LYS A 13  
AA1 2 3 N LYS A 20  ? N LYS A 20  O LYS A 27  ? O LYS A 27  
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 THR A 172 ? N THR A 172 
AA4 2 3 O ARG A 169 ? O ARG A 169 N TYR A 162 ? N TYR A 162 
AA4 3 4 O ALA A 163 ? O ALA A 163 N ALA A 139 ? N ALA A 139 
AA4 4 5 N PHE A 140 ? N PHE A 140 O ILE A 207 ? O ILE A 207 
AA4 5 6 N THR A 208 ? N THR A 208 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 ILE A 400 ? N ILE A 400 O TYR A 583 ? O TYR A 583 
AA6 4 5 N ARG A 585 ? N ARG A 585 O ILE A 597 ? O ILE A 597 
AA6 5 6 N TYR A 594 ? N TYR A 594 O ARG A 606 ? O ARG A 606 
AA7 1 2 N ASP A 432 ? N ASP A 432 O PHE A 441 ? O PHE A 441 
AA8 1 2 N ILE A 662 ? N ILE A 662 O TYR A 701 ? O TYR A 701 
AA8 2 3 N ILE A 702 ? N ILE A 702 O ILE A 715 ? O ILE A 715 
# 
_pdbx_entry_details.entry_id                   9EMI 
_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   NH1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ARG 
_pdbx_validate_close_contact.auth_seq_id_1    58 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OD2 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   ASP 
_pdbx_validate_close_contact.auth_seq_id_2    92 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.14 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 "C3'" T 6HC 3 ? ? "O3'" T 6HC 3 ? ? P   T 6HT 4 ? ? 134.40 119.70 14.70 1.20 Y 
2 1 "O3'" T 6HC 3 ? ? P     T 6HT 4 ? ? OP1 T 6HT 4 ? ? 119.95 110.50 9.45  1.10 Y 
3 1 "C3'" T 6HG 5 ? ? "O3'" T 6HG 5 ? ? P   T 6HT 6 ? ? 129.05 119.70 9.35  1.20 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 58  ? ? -109.37 -79.43  
2  1 ASP A 164 ? ? -152.93 -149.95 
3  1 PHE A 214 ? ? -147.64 -73.70  
4  1 GLU A 393 ? ? -65.34  86.35   
5  1 GLN A 436 ? ? 62.12   -65.04  
6  1 ILE A 471 ? ? -90.05  -64.59  
7  1 CYS A 506 ? ? -162.64 93.32   
8  1 ASP A 540 ? ? -91.79  -133.00 
9  1 PRO A 549 ? ? -55.49  104.77  
10 1 ASP A 598 ? ? -89.38  -154.35 
11 1 ASP A 633 ? ? -152.10 4.33    
12 1 PRO A 695 ? ? -56.13  105.20  
13 1 ARG A 709 ? ? -30.91  110.85  
14 1 LYS A 735 ? ? -144.16 17.10   
15 1 GLN A 736 ? ? -139.29 -56.23  
# 
_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         -27.8382 
_pdbx_refine_tls.origin_y         21.2684 
_pdbx_refine_tls.origin_z         -16.8289 
_pdbx_refine_tls.T[1][1]          0.3858 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0421 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0066 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.4230 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0343 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.4716 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.3166 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0101 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0429 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.1104 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.5602 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.7440 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0141 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0926 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.2172 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0101 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0539 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0349 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.1131 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0401 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0365 
_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 
# 
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 
6HA P      P  N N 1   
6HA OP1    O  N N 2   
6HA OP2    O  N N 3   
6HA OP3    O  N N 4   
6HA "O5'"  O  N N 5   
6HA "C5'"  C  N N 6   
6HA "C4'"  C  N R 7   
6HA "O4'"  O  N N 8   
6HA "C3'"  C  N S 9   
6HA "O3'"  O  N N 10  
6HA "C2'"  C  N N 11  
6HA "C1'"  C  N S 12  
6HA "C6'"  C  N N 13  
6HA N9     N  Y N 14  
6HA C8     C  Y N 15  
6HA N7     N  Y N 16  
6HA C5     C  Y N 17  
6HA C6     C  Y N 18  
6HA N6     N  N N 19  
6HA N1     N  Y N 20  
6HA C2     C  Y N 21  
6HA N3     N  Y N 22  
6HA C4     C  Y N 23  
6HA HOP2   H  N N 24  
6HA HOP3   H  N N 25  
6HA "H5'"  H  N N 26  
6HA "H5''" H  N N 27  
6HA "H4'"  H  N N 28  
6HA "H3'"  H  N N 29  
6HA "HO3'" H  N N 30  
6HA "H2'"  H  N N 31  
6HA "H2''" H  N N 32  
6HA "H1'"  H  N N 33  
6HA "H6'1" H  N N 34  
6HA "H6'2" H  N N 35  
6HA H8     H  N N 36  
6HA H61    H  N N 37  
6HA H62    H  N N 38  
6HA H2     H  N N 39  
6HC P      P  N N 40  
6HC OP1    O  N N 41  
6HC OP2    O  N N 42  
6HC OP3    O  N N 43  
6HC "O5'"  O  N N 44  
6HC "C5'"  C  N N 45  
6HC "C4'"  C  N R 46  
6HC "O4'"  O  N N 47  
6HC "C3'"  C  N S 48  
6HC "O3'"  O  N N 49  
6HC "C2'"  C  N N 50  
6HC "C1'"  C  N S 51  
6HC "C6'"  C  N N 52  
6HC N1     N  N N 53  
6HC C2     C  N N 54  
6HC O2     O  N N 55  
6HC N3     N  N N 56  
6HC C4     C  N N 57  
6HC N4     N  N N 58  
6HC C5     C  N N 59  
6HC C6     C  N N 60  
6HC HOP2   H  N N 61  
6HC HOP3   H  N N 62  
6HC "H5'"  H  N N 63  
6HC "H5''" H  N N 64  
6HC "H4'"  H  N N 65  
6HC "H3'"  H  N N 66  
6HC "HO3'" H  N N 67  
6HC "H2'"  H  N N 68  
6HC "H2''" H  N N 69  
6HC "H1'"  H  N N 70  
6HC "H6'1" H  N N 71  
6HC "H6'2" H  N N 72  
6HC H41    H  N N 73  
6HC H42    H  N N 74  
6HC H5     H  N N 75  
6HC H6     H  N N 76  
6HG P      P  N N 77  
6HG OP1    O  N N 78  
6HG OP2    O  N N 79  
6HG OP3    O  N N 80  
6HG "O5'"  O  N N 81  
6HG "C5'"  C  N N 82  
6HG "C4'"  C  N R 83  
6HG "O4'"  O  N N 84  
6HG "C3'"  C  N S 85  
6HG "O3'"  O  N N 86  
6HG "C2'"  C  N N 87  
6HG "C1'"  C  N S 88  
6HG "C6'"  C  N N 89  
6HG N9     N  Y N 90  
6HG C8     C  Y N 91  
6HG N7     N  Y N 92  
6HG C5     C  Y N 93  
6HG C6     C  N N 94  
6HG O6     O  N N 95  
6HG N1     N  N N 96  
6HG C2     C  N N 97  
6HG N2     N  N N 98  
6HG N3     N  N N 99  
6HG C4     C  Y N 100 
6HG HOP2   H  N N 101 
6HG HOP3   H  N N 102 
6HG "H5'"  H  N N 103 
6HG "H5''" H  N N 104 
6HG "H4'"  H  N N 105 
6HG "H3'"  H  N N 106 
6HG "HO3'" H  N N 107 
6HG "H2'"  H  N N 108 
6HG "H2''" H  N N 109 
6HG "H1'"  H  N N 110 
6HG "H6'1" H  N N 111 
6HG "H6'2" H  N N 112 
6HG H8     H  N N 113 
6HG H1     H  N N 114 
6HG H21    H  N N 115 
6HG H22    H  N N 116 
6HT P      P  N N 117 
6HT OP1    O  N N 118 
6HT OP2    O  N N 119 
6HT OP3    O  N N 120 
6HT "O5'"  O  N N 121 
6HT "C5'"  C  N N 122 
6HT "C4'"  C  N R 123 
6HT "O4'"  O  N N 124 
6HT "C3'"  C  N S 125 
6HT "O3'"  O  N N 126 
6HT "C2'"  C  N N 127 
6HT "C1'"  C  N S 128 
6HT "C6'"  C  N N 129 
6HT N1     N  N N 130 
6HT C2     C  N N 131 
6HT O2     O  N N 132 
6HT N3     N  N N 133 
6HT C4     C  N N 134 
6HT O4     O  N N 135 
6HT C5     C  N N 136 
6HT C5M    C  N N 137 
6HT C6     C  N N 138 
6HT HOP2   H  N N 139 
6HT HOP3   H  N N 140 
6HT "H5'"  H  N N 141 
6HT "H5''" H  N N 142 
6HT "H4'"  H  N N 143 
6HT "H3'"  H  N N 144 
6HT "HO3'" H  N N 145 
6HT "H2'"  H  N N 146 
6HT "H2''" H  N N 147 
6HT "H1'"  H  N N 148 
6HT "H6'1" H  N N 149 
6HT "H6'2" H  N N 150 
6HT H3     H  N N 151 
6HT H71    H  N N 152 
6HT H72    H  N N 153 
6HT H73    H  N N 154 
6HT H6     H  N N 155 
ALA N      N  N N 156 
ALA CA     C  N S 157 
ALA C      C  N N 158 
ALA O      O  N N 159 
ALA CB     C  N N 160 
ALA OXT    O  N N 161 
ALA H      H  N N 162 
ALA H2     H  N N 163 
ALA HA     H  N N 164 
ALA HB1    H  N N 165 
ALA HB2    H  N N 166 
ALA HB3    H  N N 167 
ALA HXT    H  N N 168 
ARG N      N  N N 169 
ARG CA     C  N S 170 
ARG C      C  N N 171 
ARG O      O  N N 172 
ARG CB     C  N N 173 
ARG CG     C  N N 174 
ARG CD     C  N N 175 
ARG NE     N  N N 176 
ARG CZ     C  N N 177 
ARG NH1    N  N N 178 
ARG NH2    N  N N 179 
ARG OXT    O  N N 180 
ARG H      H  N N 181 
ARG H2     H  N N 182 
ARG HA     H  N N 183 
ARG HB2    H  N N 184 
ARG HB3    H  N N 185 
ARG HG2    H  N N 186 
ARG HG3    H  N N 187 
ARG HD2    H  N N 188 
ARG HD3    H  N N 189 
ARG HE     H  N N 190 
ARG HH11   H  N N 191 
ARG HH12   H  N N 192 
ARG HH21   H  N N 193 
ARG HH22   H  N N 194 
ARG HXT    H  N N 195 
ASN N      N  N N 196 
ASN CA     C  N S 197 
ASN C      C  N N 198 
ASN O      O  N N 199 
ASN CB     C  N N 200 
ASN CG     C  N N 201 
ASN OD1    O  N N 202 
ASN ND2    N  N N 203 
ASN OXT    O  N N 204 
ASN H      H  N N 205 
ASN H2     H  N N 206 
ASN HA     H  N N 207 
ASN HB2    H  N N 208 
ASN HB3    H  N N 209 
ASN HD21   H  N N 210 
ASN HD22   H  N N 211 
ASN HXT    H  N N 212 
ASP N      N  N N 213 
ASP CA     C  N S 214 
ASP C      C  N N 215 
ASP O      O  N N 216 
ASP CB     C  N N 217 
ASP CG     C  N N 218 
ASP OD1    O  N N 219 
ASP OD2    O  N N 220 
ASP OXT    O  N N 221 
ASP H      H  N N 222 
ASP H2     H  N N 223 
ASP HA     H  N N 224 
ASP HB2    H  N N 225 
ASP HB3    H  N N 226 
ASP HD2    H  N N 227 
ASP HXT    H  N N 228 
CYS N      N  N N 229 
CYS CA     C  N R 230 
CYS C      C  N N 231 
CYS O      O  N N 232 
CYS CB     C  N N 233 
CYS SG     S  N N 234 
CYS OXT    O  N N 235 
CYS H      H  N N 236 
CYS H2     H  N N 237 
CYS HA     H  N N 238 
CYS HB2    H  N N 239 
CYS HB3    H  N N 240 
CYS HG     H  N N 241 
CYS HXT    H  N N 242 
DA  OP3    O  N N 243 
DA  P      P  N N 244 
DA  OP1    O  N N 245 
DA  OP2    O  N N 246 
DA  "O5'"  O  N N 247 
DA  "C5'"  C  N N 248 
DA  "C4'"  C  N R 249 
DA  "O4'"  O  N N 250 
DA  "C3'"  C  N S 251 
DA  "O3'"  O  N N 252 
DA  "C2'"  C  N N 253 
DA  "C1'"  C  N R 254 
DA  N9     N  Y N 255 
DA  C8     C  Y N 256 
DA  N7     N  Y N 257 
DA  C5     C  Y N 258 
DA  C6     C  Y N 259 
DA  N6     N  N N 260 
DA  N1     N  Y N 261 
DA  C2     C  Y N 262 
DA  N3     N  Y N 263 
DA  C4     C  Y N 264 
DA  HOP3   H  N N 265 
DA  HOP2   H  N N 266 
DA  "H5'"  H  N N 267 
DA  "H5''" H  N N 268 
DA  "H4'"  H  N N 269 
DA  "H3'"  H  N N 270 
DA  "HO3'" H  N N 271 
DA  "H2'"  H  N N 272 
DA  "H2''" H  N N 273 
DA  "H1'"  H  N N 274 
DA  H8     H  N N 275 
DA  H61    H  N N 276 
DA  H62    H  N N 277 
DA  H2     H  N N 278 
DC  OP3    O  N N 279 
DC  P      P  N N 280 
DC  OP1    O  N N 281 
DC  OP2    O  N N 282 
DC  "O5'"  O  N N 283 
DC  "C5'"  C  N N 284 
DC  "C4'"  C  N R 285 
DC  "O4'"  O  N N 286 
DC  "C3'"  C  N S 287 
DC  "O3'"  O  N N 288 
DC  "C2'"  C  N N 289 
DC  "C1'"  C  N R 290 
DC  N1     N  N N 291 
DC  C2     C  N N 292 
DC  O2     O  N N 293 
DC  N3     N  N N 294 
DC  C4     C  N N 295 
DC  N4     N  N N 296 
DC  C5     C  N N 297 
DC  C6     C  N N 298 
DC  HOP3   H  N N 299 
DC  HOP2   H  N N 300 
DC  "H5'"  H  N N 301 
DC  "H5''" H  N N 302 
DC  "H4'"  H  N N 303 
DC  "H3'"  H  N N 304 
DC  "HO3'" H  N N 305 
DC  "H2'"  H  N N 306 
DC  "H2''" H  N N 307 
DC  "H1'"  H  N N 308 
DC  H41    H  N N 309 
DC  H42    H  N N 310 
DC  H5     H  N N 311 
DC  H6     H  N N 312 
DG  OP3    O  N N 313 
DG  P      P  N N 314 
DG  OP1    O  N N 315 
DG  OP2    O  N N 316 
DG  "O5'"  O  N N 317 
DG  "C5'"  C  N N 318 
DG  "C4'"  C  N R 319 
DG  "O4'"  O  N N 320 
DG  "C3'"  C  N S 321 
DG  "O3'"  O  N N 322 
DG  "C2'"  C  N N 323 
DG  "C1'"  C  N R 324 
DG  N9     N  Y N 325 
DG  C8     C  Y N 326 
DG  N7     N  Y N 327 
DG  C5     C  Y N 328 
DG  C6     C  N N 329 
DG  O6     O  N N 330 
DG  N1     N  N N 331 
DG  C2     C  N N 332 
DG  N2     N  N N 333 
DG  N3     N  N N 334 
DG  C4     C  Y N 335 
DG  HOP3   H  N N 336 
DG  HOP2   H  N N 337 
DG  "H5'"  H  N N 338 
DG  "H5''" H  N N 339 
DG  "H4'"  H  N N 340 
DG  "H3'"  H  N N 341 
DG  "HO3'" H  N N 342 
DG  "H2'"  H  N N 343 
DG  "H2''" H  N N 344 
DG  "H1'"  H  N N 345 
DG  H8     H  N N 346 
DG  H1     H  N N 347 
DG  H21    H  N N 348 
DG  H22    H  N N 349 
DT  OP3    O  N N 350 
DT  P      P  N N 351 
DT  OP1    O  N N 352 
DT  OP2    O  N N 353 
DT  "O5'"  O  N N 354 
DT  "C5'"  C  N N 355 
DT  "C4'"  C  N R 356 
DT  "O4'"  O  N N 357 
DT  "C3'"  C  N S 358 
DT  "O3'"  O  N N 359 
DT  "C2'"  C  N N 360 
DT  "C1'"  C  N R 361 
DT  N1     N  N N 362 
DT  C2     C  N N 363 
DT  O2     O  N N 364 
DT  N3     N  N N 365 
DT  C4     C  N N 366 
DT  O4     O  N N 367 
DT  C5     C  N N 368 
DT  C7     C  N N 369 
DT  C6     C  N N 370 
DT  HOP3   H  N N 371 
DT  HOP2   H  N N 372 
DT  "H5'"  H  N N 373 
DT  "H5''" H  N N 374 
DT  "H4'"  H  N N 375 
DT  "H3'"  H  N N 376 
DT  "HO3'" H  N N 377 
DT  "H2'"  H  N N 378 
DT  "H2''" H  N N 379 
DT  "H1'"  H  N N 380 
DT  H3     H  N N 381 
DT  H71    H  N N 382 
DT  H72    H  N N 383 
DT  H73    H  N N 384 
DT  H6     H  N N 385 
EDO C1     C  N N 386 
EDO O1     O  N N 387 
EDO C2     C  N N 388 
EDO O2     O  N N 389 
EDO H11    H  N N 390 
EDO H12    H  N N 391 
EDO HO1    H  N N 392 
EDO H21    H  N N 393 
EDO H22    H  N N 394 
EDO HO2    H  N N 395 
GLN N      N  N N 396 
GLN CA     C  N S 397 
GLN C      C  N N 398 
GLN O      O  N N 399 
GLN CB     C  N N 400 
GLN CG     C  N N 401 
GLN CD     C  N N 402 
GLN OE1    O  N N 403 
GLN NE2    N  N N 404 
GLN OXT    O  N N 405 
GLN H      H  N N 406 
GLN H2     H  N N 407 
GLN HA     H  N N 408 
GLN HB2    H  N N 409 
GLN HB3    H  N N 410 
GLN HG2    H  N N 411 
GLN HG3    H  N N 412 
GLN HE21   H  N N 413 
GLN HE22   H  N N 414 
GLN HXT    H  N N 415 
GLU N      N  N N 416 
GLU CA     C  N S 417 
GLU C      C  N N 418 
GLU O      O  N N 419 
GLU CB     C  N N 420 
GLU CG     C  N N 421 
GLU CD     C  N N 422 
GLU OE1    O  N N 423 
GLU OE2    O  N N 424 
GLU OXT    O  N N 425 
GLU H      H  N N 426 
GLU H2     H  N N 427 
GLU HA     H  N N 428 
GLU HB2    H  N N 429 
GLU HB3    H  N N 430 
GLU HG2    H  N N 431 
GLU HG3    H  N N 432 
GLU HE2    H  N N 433 
GLU HXT    H  N N 434 
GLY N      N  N N 435 
GLY CA     C  N N 436 
GLY C      C  N N 437 
GLY O      O  N N 438 
GLY OXT    O  N N 439 
GLY H      H  N N 440 
GLY H2     H  N N 441 
GLY HA2    H  N N 442 
GLY HA3    H  N N 443 
GLY HXT    H  N N 444 
HIS N      N  N N 445 
HIS CA     C  N S 446 
HIS C      C  N N 447 
HIS O      O  N N 448 
HIS CB     C  N N 449 
HIS CG     C  Y N 450 
HIS ND1    N  Y N 451 
HIS CD2    C  Y N 452 
HIS CE1    C  Y N 453 
HIS NE2    N  Y N 454 
HIS OXT    O  N N 455 
HIS H      H  N N 456 
HIS H2     H  N N 457 
HIS HA     H  N N 458 
HIS HB2    H  N N 459 
HIS HB3    H  N N 460 
HIS HD1    H  N N 461 
HIS HD2    H  N N 462 
HIS HE1    H  N N 463 
HIS HE2    H  N N 464 
HIS HXT    H  N N 465 
HOH O      O  N N 466 
HOH H1     H  N N 467 
HOH H2     H  N N 468 
ILE N      N  N N 469 
ILE CA     C  N S 470 
ILE C      C  N N 471 
ILE O      O  N N 472 
ILE CB     C  N S 473 
ILE CG1    C  N N 474 
ILE CG2    C  N N 475 
ILE CD1    C  N N 476 
ILE OXT    O  N N 477 
ILE H      H  N N 478 
ILE H2     H  N N 479 
ILE HA     H  N N 480 
ILE HB     H  N N 481 
ILE HG12   H  N N 482 
ILE HG13   H  N N 483 
ILE HG21   H  N N 484 
ILE HG22   H  N N 485 
ILE HG23   H  N N 486 
ILE HD11   H  N N 487 
ILE HD12   H  N N 488 
ILE HD13   H  N N 489 
ILE HXT    H  N N 490 
LEU N      N  N N 491 
LEU CA     C  N S 492 
LEU C      C  N N 493 
LEU O      O  N N 494 
LEU CB     C  N N 495 
LEU CG     C  N N 496 
LEU CD1    C  N N 497 
LEU CD2    C  N N 498 
LEU OXT    O  N N 499 
LEU H      H  N N 500 
LEU H2     H  N N 501 
LEU HA     H  N N 502 
LEU HB2    H  N N 503 
LEU HB3    H  N N 504 
LEU HG     H  N N 505 
LEU HD11   H  N N 506 
LEU HD12   H  N N 507 
LEU HD13   H  N N 508 
LEU HD21   H  N N 509 
LEU HD22   H  N N 510 
LEU HD23   H  N N 511 
LEU HXT    H  N N 512 
LYS N      N  N N 513 
LYS CA     C  N S 514 
LYS C      C  N N 515 
LYS O      O  N N 516 
LYS CB     C  N N 517 
LYS CG     C  N N 518 
LYS CD     C  N N 519 
LYS CE     C  N N 520 
LYS NZ     N  N N 521 
LYS OXT    O  N N 522 
LYS H      H  N N 523 
LYS H2     H  N N 524 
LYS HA     H  N N 525 
LYS HB2    H  N N 526 
LYS HB3    H  N N 527 
LYS HG2    H  N N 528 
LYS HG3    H  N N 529 
LYS HD2    H  N N 530 
LYS HD3    H  N N 531 
LYS HE2    H  N N 532 
LYS HE3    H  N N 533 
LYS HZ1    H  N N 534 
LYS HZ2    H  N N 535 
LYS HZ3    H  N N 536 
LYS HXT    H  N N 537 
MET N      N  N N 538 
MET CA     C  N S 539 
MET C      C  N N 540 
MET O      O  N N 541 
MET CB     C  N N 542 
MET CG     C  N N 543 
MET SD     S  N N 544 
MET CE     C  N N 545 
MET OXT    O  N N 546 
MET H      H  N N 547 
MET H2     H  N N 548 
MET HA     H  N N 549 
MET HB2    H  N N 550 
MET HB3    H  N N 551 
MET HG2    H  N N 552 
MET HG3    H  N N 553 
MET HE1    H  N N 554 
MET HE2    H  N N 555 
MET HE3    H  N N 556 
MET HXT    H  N N 557 
MG  MG     MG N N 558 
PHE N      N  N N 559 
PHE CA     C  N S 560 
PHE C      C  N N 561 
PHE O      O  N N 562 
PHE CB     C  N N 563 
PHE CG     C  Y N 564 
PHE CD1    C  Y N 565 
PHE CD2    C  Y N 566 
PHE CE1    C  Y N 567 
PHE CE2    C  Y N 568 
PHE CZ     C  Y N 569 
PHE OXT    O  N N 570 
PHE H      H  N N 571 
PHE H2     H  N N 572 
PHE HA     H  N N 573 
PHE HB2    H  N N 574 
PHE HB3    H  N N 575 
PHE HD1    H  N N 576 
PHE HD2    H  N N 577 
PHE HE1    H  N N 578 
PHE HE2    H  N N 579 
PHE HZ     H  N N 580 
PHE HXT    H  N N 581 
PRO N      N  N N 582 
PRO CA     C  N S 583 
PRO C      C  N N 584 
PRO O      O  N N 585 
PRO CB     C  N N 586 
PRO CG     C  N N 587 
PRO CD     C  N N 588 
PRO OXT    O  N N 589 
PRO H      H  N N 590 
PRO HA     H  N N 591 
PRO HB2    H  N N 592 
PRO HB3    H  N N 593 
PRO HG2    H  N N 594 
PRO HG3    H  N N 595 
PRO HD2    H  N N 596 
PRO HD3    H  N N 597 
PRO HXT    H  N N 598 
SER N      N  N N 599 
SER CA     C  N S 600 
SER C      C  N N 601 
SER O      O  N N 602 
SER CB     C  N N 603 
SER OG     O  N N 604 
SER OXT    O  N N 605 
SER H      H  N N 606 
SER H2     H  N N 607 
SER HA     H  N N 608 
SER HB2    H  N N 609 
SER HB3    H  N N 610 
SER HG     H  N N 611 
SER HXT    H  N N 612 
THR N      N  N N 613 
THR CA     C  N S 614 
THR C      C  N N 615 
THR O      O  N N 616 
THR CB     C  N R 617 
THR OG1    O  N N 618 
THR CG2    C  N N 619 
THR OXT    O  N N 620 
THR H      H  N N 621 
THR H2     H  N N 622 
THR HA     H  N N 623 
THR HB     H  N N 624 
THR HG1    H  N N 625 
THR HG21   H  N N 626 
THR HG22   H  N N 627 
THR HG23   H  N N 628 
THR HXT    H  N N 629 
TRP N      N  N N 630 
TRP CA     C  N S 631 
TRP C      C  N N 632 
TRP O      O  N N 633 
TRP CB     C  N N 634 
TRP CG     C  Y N 635 
TRP CD1    C  Y N 636 
TRP CD2    C  Y N 637 
TRP NE1    N  Y N 638 
TRP CE2    C  Y N 639 
TRP CE3    C  Y N 640 
TRP CZ2    C  Y N 641 
TRP CZ3    C  Y N 642 
TRP CH2    C  Y N 643 
TRP OXT    O  N N 644 
TRP H      H  N N 645 
TRP H2     H  N N 646 
TRP HA     H  N N 647 
TRP HB2    H  N N 648 
TRP HB3    H  N N 649 
TRP HD1    H  N N 650 
TRP HE1    H  N N 651 
TRP HE3    H  N N 652 
TRP HZ2    H  N N 653 
TRP HZ3    H  N N 654 
TRP HH2    H  N N 655 
TRP HXT    H  N N 656 
TYR N      N  N N 657 
TYR CA     C  N S 658 
TYR C      C  N N 659 
TYR O      O  N N 660 
TYR CB     C  N N 661 
TYR CG     C  Y N 662 
TYR CD1    C  Y N 663 
TYR CD2    C  Y N 664 
TYR CE1    C  Y N 665 
TYR CE2    C  Y N 666 
TYR CZ     C  Y N 667 
TYR OH     O  N N 668 
TYR OXT    O  N N 669 
TYR H      H  N N 670 
TYR H2     H  N N 671 
TYR HA     H  N N 672 
TYR HB2    H  N N 673 
TYR HB3    H  N N 674 
TYR HD1    H  N N 675 
TYR HD2    H  N N 676 
TYR HE1    H  N N 677 
TYR HE2    H  N N 678 
TYR HH     H  N N 679 
TYR HXT    H  N N 680 
VAL N      N  N N 681 
VAL CA     C  N S 682 
VAL C      C  N N 683 
VAL O      O  N N 684 
VAL CB     C  N N 685 
VAL CG1    C  N N 686 
VAL CG2    C  N N 687 
VAL OXT    O  N N 688 
VAL H      H  N N 689 
VAL H2     H  N N 690 
VAL HA     H  N N 691 
VAL HB     H  N N 692 
VAL HG11   H  N N 693 
VAL HG12   H  N N 694 
VAL HG13   H  N N 695 
VAL HG21   H  N N 696 
VAL HG22   H  N N 697 
VAL HG23   H  N N 698 
VAL HXT    H  N N 699 
XG4 N1     N  N N 700 
XG4 C2     C  N N 701 
XG4 N2     N  N N 702 
XG4 N3     N  N N 703 
XG4 C4     C  Y N 704 
XG4 C5     C  Y N 705 
XG4 C6     C  N N 706 
XG4 O6     O  N N 707 
XG4 N7     N  Y N 708 
XG4 C8     C  Y N 709 
XG4 N9     N  Y N 710 
XG4 PA     P  N N 711 
XG4 PB     P  N N 712 
XG4 PG     P  N N 713 
XG4 "C1'"  C  N R 714 
XG4 O1A    O  N N 715 
XG4 O1B    O  N N 716 
XG4 O1G    O  N N 717 
XG4 "C2'"  C  N N 718 
XG4 O2A    O  N N 719 
XG4 O2B    O  N N 720 
XG4 O2G    O  N N 721 
XG4 "C3'"  C  N S 722 
XG4 "O3'"  O  N N 723 
XG4 N3A    N  N N 724 
XG4 O3B    O  N N 725 
XG4 O3G    O  N N 726 
XG4 "C4'"  C  N R 727 
XG4 "O4'"  O  N N 728 
XG4 "C5'"  C  N N 729 
XG4 "O5'"  O  N N 730 
XG4 HN1    H  N N 731 
XG4 HN2    H  N N 732 
XG4 HN2A   H  N N 733 
XG4 H8     H  N N 734 
XG4 "H1'"  H  N N 735 
XG4 "H2'"  H  N N 736 
XG4 "H2'A" H  N N 737 
XG4 HO2A   H  N N 738 
XG4 HO2B   H  N N 739 
XG4 HO2G   H  N N 740 
XG4 "H3'"  H  N N 741 
XG4 "HO3'" H  N N 742 
XG4 HN3A   H  N N 743 
XG4 HO3G   H  N N 744 
XG4 "H4'"  H  N N 745 
XG4 "H5'"  H  N N 746 
XG4 "H5'A" H  N N 747 
# 
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 
6HA P     OP1    doub N N 1   
6HA P     OP2    sing N N 2   
6HA P     OP3    sing N N 3   
6HA P     "O5'"  sing N N 4   
6HA OP2   HOP2   sing N N 5   
6HA OP3   HOP3   sing N N 6   
6HA "O5'" "C5'"  sing N N 7   
6HA "C5'" "C4'"  sing N N 8   
6HA "C5'" "H5'"  sing N N 9   
6HA "C5'" "H5''" sing N N 10  
6HA "C4'" "O4'"  sing N N 11  
6HA "C4'" "C3'"  sing N N 12  
6HA "C4'" "H4'"  sing N N 13  
6HA "O4'" "C6'"  sing N N 14  
6HA "C3'" "O3'"  sing N N 15  
6HA "C3'" "C2'"  sing N N 16  
6HA "C3'" "H3'"  sing N N 17  
6HA "O3'" "HO3'" sing N N 18  
6HA "C2'" "C1'"  sing N N 19  
6HA "C2'" "H2'"  sing N N 20  
6HA "C2'" "H2''" sing N N 21  
6HA "C1'" "C6'"  sing N N 22  
6HA "C1'" N9     sing N N 23  
6HA "C1'" "H1'"  sing N N 24  
6HA "C6'" "H6'1" sing N N 25  
6HA "C6'" "H6'2" sing N N 26  
6HA N9    C8     sing Y N 27  
6HA N9    C4     sing Y N 28  
6HA C8    N7     doub Y N 29  
6HA C8    H8     sing N N 30  
6HA N7    C5     sing Y N 31  
6HA C5    C6     sing Y N 32  
6HA C5    C4     doub Y N 33  
6HA C6    N6     sing N N 34  
6HA C6    N1     doub Y N 35  
6HA N6    H61    sing N N 36  
6HA N6    H62    sing N N 37  
6HA N1    C2     sing Y N 38  
6HA C2    N3     doub Y N 39  
6HA C2    H2     sing N N 40  
6HA N3    C4     sing Y N 41  
6HC P     OP1    doub N N 42  
6HC P     OP2    sing N N 43  
6HC P     OP3    sing N N 44  
6HC P     "O5'"  sing N N 45  
6HC OP2   HOP2   sing N N 46  
6HC OP3   HOP3   sing N N 47  
6HC "O5'" "C5'"  sing N N 48  
6HC "C5'" "C4'"  sing N N 49  
6HC "C5'" "H5'"  sing N N 50  
6HC "C5'" "H5''" sing N N 51  
6HC "C4'" "O4'"  sing N N 52  
6HC "C4'" "C3'"  sing N N 53  
6HC "C4'" "H4'"  sing N N 54  
6HC "O4'" "C6'"  sing N N 55  
6HC "C3'" "O3'"  sing N N 56  
6HC "C3'" "C2'"  sing N N 57  
6HC "C3'" "H3'"  sing N N 58  
6HC "O3'" "HO3'" sing N N 59  
6HC "C2'" "C1'"  sing N N 60  
6HC "C2'" "H2'"  sing N N 61  
6HC "C2'" "H2''" sing N N 62  
6HC "C1'" "C6'"  sing N N 63  
6HC "C1'" N1     sing N N 64  
6HC "C1'" "H1'"  sing N N 65  
6HC "C6'" "H6'1" sing N N 66  
6HC "C6'" "H6'2" sing N N 67  
6HC N1    C2     sing N N 68  
6HC N1    C6     sing N N 69  
6HC C2    O2     doub N N 70  
6HC C2    N3     sing N N 71  
6HC N3    C4     doub N N 72  
6HC C4    N4     sing N N 73  
6HC C4    C5     sing N N 74  
6HC N4    H41    sing N N 75  
6HC N4    H42    sing N N 76  
6HC C5    C6     doub N N 77  
6HC C5    H5     sing N N 78  
6HC C6    H6     sing N N 79  
6HG P     OP1    doub N N 80  
6HG P     OP2    sing N N 81  
6HG P     OP3    sing N N 82  
6HG P     "O5'"  sing N N 83  
6HG OP2   HOP2   sing N N 84  
6HG OP3   HOP3   sing N N 85  
6HG "O5'" "C5'"  sing N N 86  
6HG "C5'" "C4'"  sing N N 87  
6HG "C5'" "H5'"  sing N N 88  
6HG "C5'" "H5''" sing N N 89  
6HG "C4'" "O4'"  sing N N 90  
6HG "C4'" "C3'"  sing N N 91  
6HG "C4'" "H4'"  sing N N 92  
6HG "O4'" "C6'"  sing N N 93  
6HG "C3'" "O3'"  sing N N 94  
6HG "C3'" "C2'"  sing N N 95  
6HG "C3'" "H3'"  sing N N 96  
6HG "O3'" "HO3'" sing N N 97  
6HG "C2'" "C1'"  sing N N 98  
6HG "C2'" "H2'"  sing N N 99  
6HG "C2'" "H2''" sing N N 100 
6HG "C1'" "C6'"  sing N N 101 
6HG "C1'" N9     sing N N 102 
6HG "C1'" "H1'"  sing N N 103 
6HG "C6'" "H6'1" sing N N 104 
6HG "C6'" "H6'2" sing N N 105 
6HG N9    C8     sing Y N 106 
6HG N9    C4     sing Y N 107 
6HG C8    N7     doub Y N 108 
6HG C8    H8     sing N N 109 
6HG N7    C5     sing Y N 110 
6HG C5    C6     sing N N 111 
6HG C5    C4     doub Y N 112 
6HG C6    O6     doub N N 113 
6HG C6    N1     sing N N 114 
6HG N1    C2     sing N N 115 
6HG N1    H1     sing N N 116 
6HG C2    N2     sing N N 117 
6HG C2    N3     doub N N 118 
6HG N2    H21    sing N N 119 
6HG N2    H22    sing N N 120 
6HG N3    C4     sing N N 121 
6HT P     OP1    doub N N 122 
6HT P     OP2    sing N N 123 
6HT P     OP3    sing N N 124 
6HT P     "O5'"  sing N N 125 
6HT OP2   HOP2   sing N N 126 
6HT OP3   HOP3   sing N N 127 
6HT "O5'" "C5'"  sing N N 128 
6HT "C5'" "C4'"  sing N N 129 
6HT "C5'" "H5'"  sing N N 130 
6HT "C5'" "H5''" sing N N 131 
6HT "C4'" "O4'"  sing N N 132 
6HT "C4'" "C3'"  sing N N 133 
6HT "C4'" "H4'"  sing N N 134 
6HT "O4'" "C6'"  sing N N 135 
6HT "C3'" "O3'"  sing N N 136 
6HT "C3'" "C2'"  sing N N 137 
6HT "C3'" "H3'"  sing N N 138 
6HT "O3'" "HO3'" sing N N 139 
6HT "C2'" "C1'"  sing N N 140 
6HT "C2'" "H2'"  sing N N 141 
6HT "C2'" "H2''" sing N N 142 
6HT "C1'" "C6'"  sing N N 143 
6HT "C1'" N1     sing N N 144 
6HT "C1'" "H1'"  sing N N 145 
6HT "C6'" "H6'1" sing N N 146 
6HT "C6'" "H6'2" sing N N 147 
6HT N1    C2     sing N N 148 
6HT N1    C6     sing N N 149 
6HT C2    O2     doub N N 150 
6HT C2    N3     sing N N 151 
6HT N3    C4     sing N N 152 
6HT N3    H3     sing N N 153 
6HT C4    O4     doub N N 154 
6HT C4    C5     sing N N 155 
6HT C5    C5M    sing N N 156 
6HT C5    C6     doub N N 157 
6HT C5M   H71    sing N N 158 
6HT C5M   H72    sing N N 159 
6HT C5M   H73    sing N N 160 
6HT C6    H6     sing N N 161 
ALA N     CA     sing N N 162 
ALA N     H      sing N N 163 
ALA N     H2     sing N N 164 
ALA CA    C      sing N N 165 
ALA CA    CB     sing N N 166 
ALA CA    HA     sing N N 167 
ALA C     O      doub N N 168 
ALA C     OXT    sing N N 169 
ALA CB    HB1    sing N N 170 
ALA CB    HB2    sing N N 171 
ALA CB    HB3    sing N N 172 
ALA OXT   HXT    sing N N 173 
ARG N     CA     sing N N 174 
ARG N     H      sing N N 175 
ARG N     H2     sing N N 176 
ARG CA    C      sing N N 177 
ARG CA    CB     sing N N 178 
ARG CA    HA     sing N N 179 
ARG C     O      doub N N 180 
ARG C     OXT    sing N N 181 
ARG CB    CG     sing N N 182 
ARG CB    HB2    sing N N 183 
ARG CB    HB3    sing N N 184 
ARG CG    CD     sing N N 185 
ARG CG    HG2    sing N N 186 
ARG CG    HG3    sing N N 187 
ARG CD    NE     sing N N 188 
ARG CD    HD2    sing N N 189 
ARG CD    HD3    sing N N 190 
ARG NE    CZ     sing N N 191 
ARG NE    HE     sing N N 192 
ARG CZ    NH1    sing N N 193 
ARG CZ    NH2    doub N N 194 
ARG NH1   HH11   sing N N 195 
ARG NH1   HH12   sing N N 196 
ARG NH2   HH21   sing N N 197 
ARG NH2   HH22   sing N N 198 
ARG OXT   HXT    sing N N 199 
ASN N     CA     sing N N 200 
ASN N     H      sing N N 201 
ASN N     H2     sing N N 202 
ASN CA    C      sing N N 203 
ASN CA    CB     sing N N 204 
ASN CA    HA     sing N N 205 
ASN C     O      doub N N 206 
ASN C     OXT    sing N N 207 
ASN CB    CG     sing N N 208 
ASN CB    HB2    sing N N 209 
ASN CB    HB3    sing N N 210 
ASN CG    OD1    doub N N 211 
ASN CG    ND2    sing N N 212 
ASN ND2   HD21   sing N N 213 
ASN ND2   HD22   sing N N 214 
ASN OXT   HXT    sing N N 215 
ASP N     CA     sing N N 216 
ASP N     H      sing N N 217 
ASP N     H2     sing N N 218 
ASP CA    C      sing N N 219 
ASP CA    CB     sing N N 220 
ASP CA    HA     sing N N 221 
ASP C     O      doub N N 222 
ASP C     OXT    sing N N 223 
ASP CB    CG     sing N N 224 
ASP CB    HB2    sing N N 225 
ASP CB    HB3    sing N N 226 
ASP CG    OD1    doub N N 227 
ASP CG    OD2    sing N N 228 
ASP OD2   HD2    sing N N 229 
ASP OXT   HXT    sing N N 230 
CYS N     CA     sing N N 231 
CYS N     H      sing N N 232 
CYS N     H2     sing N N 233 
CYS CA    C      sing N N 234 
CYS CA    CB     sing N N 235 
CYS CA    HA     sing N N 236 
CYS C     O      doub N N 237 
CYS C     OXT    sing N N 238 
CYS CB    SG     sing N N 239 
CYS CB    HB2    sing N N 240 
CYS CB    HB3    sing N N 241 
CYS SG    HG     sing N N 242 
CYS OXT   HXT    sing N N 243 
DA  OP3   P      sing N N 244 
DA  OP3   HOP3   sing N N 245 
DA  P     OP1    doub N N 246 
DA  P     OP2    sing N N 247 
DA  P     "O5'"  sing N N 248 
DA  OP2   HOP2   sing N N 249 
DA  "O5'" "C5'"  sing N N 250 
DA  "C5'" "C4'"  sing N N 251 
DA  "C5'" "H5'"  sing N N 252 
DA  "C5'" "H5''" sing N N 253 
DA  "C4'" "O4'"  sing N N 254 
DA  "C4'" "C3'"  sing N N 255 
DA  "C4'" "H4'"  sing N N 256 
DA  "O4'" "C1'"  sing N N 257 
DA  "C3'" "O3'"  sing N N 258 
DA  "C3'" "C2'"  sing N N 259 
DA  "C3'" "H3'"  sing N N 260 
DA  "O3'" "HO3'" sing N N 261 
DA  "C2'" "C1'"  sing N N 262 
DA  "C2'" "H2'"  sing N N 263 
DA  "C2'" "H2''" sing N N 264 
DA  "C1'" N9     sing N N 265 
DA  "C1'" "H1'"  sing N N 266 
DA  N9    C8     sing Y N 267 
DA  N9    C4     sing Y N 268 
DA  C8    N7     doub Y N 269 
DA  C8    H8     sing N N 270 
DA  N7    C5     sing Y N 271 
DA  C5    C6     sing Y N 272 
DA  C5    C4     doub Y N 273 
DA  C6    N6     sing N N 274 
DA  C6    N1     doub Y N 275 
DA  N6    H61    sing N N 276 
DA  N6    H62    sing N N 277 
DA  N1    C2     sing Y N 278 
DA  C2    N3     doub Y N 279 
DA  C2    H2     sing N N 280 
DA  N3    C4     sing Y N 281 
DC  OP3   P      sing N N 282 
DC  OP3   HOP3   sing N N 283 
DC  P     OP1    doub N N 284 
DC  P     OP2    sing N N 285 
DC  P     "O5'"  sing N N 286 
DC  OP2   HOP2   sing N N 287 
DC  "O5'" "C5'"  sing N N 288 
DC  "C5'" "C4'"  sing N N 289 
DC  "C5'" "H5'"  sing N N 290 
DC  "C5'" "H5''" sing N N 291 
DC  "C4'" "O4'"  sing N N 292 
DC  "C4'" "C3'"  sing N N 293 
DC  "C4'" "H4'"  sing N N 294 
DC  "O4'" "C1'"  sing N N 295 
DC  "C3'" "O3'"  sing N N 296 
DC  "C3'" "C2'"  sing N N 297 
DC  "C3'" "H3'"  sing N N 298 
DC  "O3'" "HO3'" sing N N 299 
DC  "C2'" "C1'"  sing N N 300 
DC  "C2'" "H2'"  sing N N 301 
DC  "C2'" "H2''" sing N N 302 
DC  "C1'" N1     sing N N 303 
DC  "C1'" "H1'"  sing N N 304 
DC  N1    C2     sing N N 305 
DC  N1    C6     sing N N 306 
DC  C2    O2     doub N N 307 
DC  C2    N3     sing N N 308 
DC  N3    C4     doub N N 309 
DC  C4    N4     sing N N 310 
DC  C4    C5     sing N N 311 
DC  N4    H41    sing N N 312 
DC  N4    H42    sing N N 313 
DC  C5    C6     doub N N 314 
DC  C5    H5     sing N N 315 
DC  C6    H6     sing N N 316 
DG  OP3   P      sing N N 317 
DG  OP3   HOP3   sing N N 318 
DG  P     OP1    doub N N 319 
DG  P     OP2    sing N N 320 
DG  P     "O5'"  sing N N 321 
DG  OP2   HOP2   sing N N 322 
DG  "O5'" "C5'"  sing N N 323 
DG  "C5'" "C4'"  sing N N 324 
DG  "C5'" "H5'"  sing N N 325 
DG  "C5'" "H5''" sing N N 326 
DG  "C4'" "O4'"  sing N N 327 
DG  "C4'" "C3'"  sing N N 328 
DG  "C4'" "H4'"  sing N N 329 
DG  "O4'" "C1'"  sing N N 330 
DG  "C3'" "O3'"  sing N N 331 
DG  "C3'" "C2'"  sing N N 332 
DG  "C3'" "H3'"  sing N N 333 
DG  "O3'" "HO3'" sing N N 334 
DG  "C2'" "C1'"  sing N N 335 
DG  "C2'" "H2'"  sing N N 336 
DG  "C2'" "H2''" sing N N 337 
DG  "C1'" N9     sing N N 338 
DG  "C1'" "H1'"  sing N N 339 
DG  N9    C8     sing Y N 340 
DG  N9    C4     sing Y N 341 
DG  C8    N7     doub Y N 342 
DG  C8    H8     sing N N 343 
DG  N7    C5     sing Y N 344 
DG  C5    C6     sing N N 345 
DG  C5    C4     doub Y N 346 
DG  C6    O6     doub N N 347 
DG  C6    N1     sing N N 348 
DG  N1    C2     sing N N 349 
DG  N1    H1     sing N N 350 
DG  C2    N2     sing N N 351 
DG  C2    N3     doub N N 352 
DG  N2    H21    sing N N 353 
DG  N2    H22    sing N N 354 
DG  N3    C4     sing N N 355 
DT  OP3   P      sing N N 356 
DT  OP3   HOP3   sing N N 357 
DT  P     OP1    doub N N 358 
DT  P     OP2    sing N N 359 
DT  P     "O5'"  sing N N 360 
DT  OP2   HOP2   sing N N 361 
DT  "O5'" "C5'"  sing N N 362 
DT  "C5'" "C4'"  sing N N 363 
DT  "C5'" "H5'"  sing N N 364 
DT  "C5'" "H5''" sing N N 365 
DT  "C4'" "O4'"  sing N N 366 
DT  "C4'" "C3'"  sing N N 367 
DT  "C4'" "H4'"  sing N N 368 
DT  "O4'" "C1'"  sing N N 369 
DT  "C3'" "O3'"  sing N N 370 
DT  "C3'" "C2'"  sing N N 371 
DT  "C3'" "H3'"  sing N N 372 
DT  "O3'" "HO3'" sing N N 373 
DT  "C2'" "C1'"  sing N N 374 
DT  "C2'" "H2'"  sing N N 375 
DT  "C2'" "H2''" sing N N 376 
DT  "C1'" N1     sing N N 377 
DT  "C1'" "H1'"  sing N N 378 
DT  N1    C2     sing N N 379 
DT  N1    C6     sing N N 380 
DT  C2    O2     doub N N 381 
DT  C2    N3     sing N N 382 
DT  N3    C4     sing N N 383 
DT  N3    H3     sing N N 384 
DT  C4    O4     doub N N 385 
DT  C4    C5     sing N N 386 
DT  C5    C7     sing N N 387 
DT  C5    C6     doub N N 388 
DT  C7    H71    sing N N 389 
DT  C7    H72    sing N N 390 
DT  C7    H73    sing N N 391 
DT  C6    H6     sing N N 392 
EDO C1    O1     sing N N 393 
EDO C1    C2     sing N N 394 
EDO C1    H11    sing N N 395 
EDO C1    H12    sing N N 396 
EDO O1    HO1    sing N N 397 
EDO C2    O2     sing N N 398 
EDO C2    H21    sing N N 399 
EDO C2    H22    sing N N 400 
EDO O2    HO2    sing N N 401 
GLN N     CA     sing N N 402 
GLN N     H      sing N N 403 
GLN N     H2     sing N N 404 
GLN CA    C      sing N N 405 
GLN CA    CB     sing N N 406 
GLN CA    HA     sing N N 407 
GLN C     O      doub N N 408 
GLN C     OXT    sing N N 409 
GLN CB    CG     sing N N 410 
GLN CB    HB2    sing N N 411 
GLN CB    HB3    sing N N 412 
GLN CG    CD     sing N N 413 
GLN CG    HG2    sing N N 414 
GLN CG    HG3    sing N N 415 
GLN CD    OE1    doub N N 416 
GLN CD    NE2    sing N N 417 
GLN NE2   HE21   sing N N 418 
GLN NE2   HE22   sing N N 419 
GLN OXT   HXT    sing N N 420 
GLU N     CA     sing N N 421 
GLU N     H      sing N N 422 
GLU N     H2     sing N N 423 
GLU CA    C      sing N N 424 
GLU CA    CB     sing N N 425 
GLU CA    HA     sing N N 426 
GLU C     O      doub N N 427 
GLU C     OXT    sing N N 428 
GLU CB    CG     sing N N 429 
GLU CB    HB2    sing N N 430 
GLU CB    HB3    sing N N 431 
GLU CG    CD     sing N N 432 
GLU CG    HG2    sing N N 433 
GLU CG    HG3    sing N N 434 
GLU CD    OE1    doub N N 435 
GLU CD    OE2    sing N N 436 
GLU OE2   HE2    sing N N 437 
GLU OXT   HXT    sing N N 438 
GLY N     CA     sing N N 439 
GLY N     H      sing N N 440 
GLY N     H2     sing N N 441 
GLY CA    C      sing N N 442 
GLY CA    HA2    sing N N 443 
GLY CA    HA3    sing N N 444 
GLY C     O      doub N N 445 
GLY C     OXT    sing N N 446 
GLY OXT   HXT    sing N N 447 
HIS N     CA     sing N N 448 
HIS N     H      sing N N 449 
HIS N     H2     sing N N 450 
HIS CA    C      sing N N 451 
HIS CA    CB     sing N N 452 
HIS CA    HA     sing N N 453 
HIS C     O      doub N N 454 
HIS C     OXT    sing N N 455 
HIS CB    CG     sing N N 456 
HIS CB    HB2    sing N N 457 
HIS CB    HB3    sing N N 458 
HIS CG    ND1    sing Y N 459 
HIS CG    CD2    doub Y N 460 
HIS ND1   CE1    doub Y N 461 
HIS ND1   HD1    sing N N 462 
HIS CD2   NE2    sing Y N 463 
HIS CD2   HD2    sing N N 464 
HIS CE1   NE2    sing Y N 465 
HIS CE1   HE1    sing N N 466 
HIS NE2   HE2    sing N N 467 
HIS OXT   HXT    sing N N 468 
HOH O     H1     sing N N 469 
HOH O     H2     sing N N 470 
ILE N     CA     sing N N 471 
ILE N     H      sing N N 472 
ILE N     H2     sing N N 473 
ILE CA    C      sing N N 474 
ILE CA    CB     sing N N 475 
ILE CA    HA     sing N N 476 
ILE C     O      doub N N 477 
ILE C     OXT    sing N N 478 
ILE CB    CG1    sing N N 479 
ILE CB    CG2    sing N N 480 
ILE CB    HB     sing N N 481 
ILE CG1   CD1    sing N N 482 
ILE CG1   HG12   sing N N 483 
ILE CG1   HG13   sing N N 484 
ILE CG2   HG21   sing N N 485 
ILE CG2   HG22   sing N N 486 
ILE CG2   HG23   sing N N 487 
ILE CD1   HD11   sing N N 488 
ILE CD1   HD12   sing N N 489 
ILE CD1   HD13   sing N N 490 
ILE OXT   HXT    sing N N 491 
LEU N     CA     sing N N 492 
LEU N     H      sing N N 493 
LEU N     H2     sing N N 494 
LEU CA    C      sing N N 495 
LEU CA    CB     sing N N 496 
LEU CA    HA     sing N N 497 
LEU C     O      doub N N 498 
LEU C     OXT    sing N N 499 
LEU CB    CG     sing N N 500 
LEU CB    HB2    sing N N 501 
LEU CB    HB3    sing N N 502 
LEU CG    CD1    sing N N 503 
LEU CG    CD2    sing N N 504 
LEU CG    HG     sing N N 505 
LEU CD1   HD11   sing N N 506 
LEU CD1   HD12   sing N N 507 
LEU CD1   HD13   sing N N 508 
LEU CD2   HD21   sing N N 509 
LEU CD2   HD22   sing N N 510 
LEU CD2   HD23   sing N N 511 
LEU OXT   HXT    sing N N 512 
LYS N     CA     sing N N 513 
LYS N     H      sing N N 514 
LYS N     H2     sing N N 515 
LYS CA    C      sing N N 516 
LYS CA    CB     sing N N 517 
LYS CA    HA     sing N N 518 
LYS C     O      doub N N 519 
LYS C     OXT    sing N N 520 
LYS CB    CG     sing N N 521 
LYS CB    HB2    sing N N 522 
LYS CB    HB3    sing N N 523 
LYS CG    CD     sing N N 524 
LYS CG    HG2    sing N N 525 
LYS CG    HG3    sing N N 526 
LYS CD    CE     sing N N 527 
LYS CD    HD2    sing N N 528 
LYS CD    HD3    sing N N 529 
LYS CE    NZ     sing N N 530 
LYS CE    HE2    sing N N 531 
LYS CE    HE3    sing N N 532 
LYS NZ    HZ1    sing N N 533 
LYS NZ    HZ2    sing N N 534 
LYS NZ    HZ3    sing N N 535 
LYS OXT   HXT    sing N N 536 
MET N     CA     sing N N 537 
MET N     H      sing N N 538 
MET N     H2     sing N N 539 
MET CA    C      sing N N 540 
MET CA    CB     sing N N 541 
MET CA    HA     sing N N 542 
MET C     O      doub N N 543 
MET C     OXT    sing N N 544 
MET CB    CG     sing N N 545 
MET CB    HB2    sing N N 546 
MET CB    HB3    sing N N 547 
MET CG    SD     sing N N 548 
MET CG    HG2    sing N N 549 
MET CG    HG3    sing N N 550 
MET SD    CE     sing N N 551 
MET CE    HE1    sing N N 552 
MET CE    HE2    sing N N 553 
MET CE    HE3    sing N N 554 
MET OXT   HXT    sing N N 555 
PHE N     CA     sing N N 556 
PHE N     H      sing N N 557 
PHE N     H2     sing N N 558 
PHE CA    C      sing N N 559 
PHE CA    CB     sing N N 560 
PHE CA    HA     sing N N 561 
PHE C     O      doub N N 562 
PHE C     OXT    sing N N 563 
PHE CB    CG     sing N N 564 
PHE CB    HB2    sing N N 565 
PHE CB    HB3    sing N N 566 
PHE CG    CD1    doub Y N 567 
PHE CG    CD2    sing Y N 568 
PHE CD1   CE1    sing Y N 569 
PHE CD1   HD1    sing N N 570 
PHE CD2   CE2    doub Y N 571 
PHE CD2   HD2    sing N N 572 
PHE CE1   CZ     doub Y N 573 
PHE CE1   HE1    sing N N 574 
PHE CE2   CZ     sing Y N 575 
PHE CE2   HE2    sing N N 576 
PHE CZ    HZ     sing N N 577 
PHE OXT   HXT    sing N N 578 
PRO N     CA     sing N N 579 
PRO N     CD     sing N N 580 
PRO N     H      sing N N 581 
PRO CA    C      sing N N 582 
PRO CA    CB     sing N N 583 
PRO CA    HA     sing N N 584 
PRO C     O      doub N N 585 
PRO C     OXT    sing N N 586 
PRO CB    CG     sing N N 587 
PRO CB    HB2    sing N N 588 
PRO CB    HB3    sing N N 589 
PRO CG    CD     sing N N 590 
PRO CG    HG2    sing N N 591 
PRO CG    HG3    sing N N 592 
PRO CD    HD2    sing N N 593 
PRO CD    HD3    sing N N 594 
PRO OXT   HXT    sing N N 595 
SER N     CA     sing N N 596 
SER N     H      sing N N 597 
SER N     H2     sing N N 598 
SER CA    C      sing N N 599 
SER CA    CB     sing N N 600 
SER CA    HA     sing N N 601 
SER C     O      doub N N 602 
SER C     OXT    sing N N 603 
SER CB    OG     sing N N 604 
SER CB    HB2    sing N N 605 
SER CB    HB3    sing N N 606 
SER OG    HG     sing N N 607 
SER OXT   HXT    sing N N 608 
THR N     CA     sing N N 609 
THR N     H      sing N N 610 
THR N     H2     sing N N 611 
THR CA    C      sing N N 612 
THR CA    CB     sing N N 613 
THR CA    HA     sing N N 614 
THR C     O      doub N N 615 
THR C     OXT    sing N N 616 
THR CB    OG1    sing N N 617 
THR CB    CG2    sing N N 618 
THR CB    HB     sing N N 619 
THR OG1   HG1    sing N N 620 
THR CG2   HG21   sing N N 621 
THR CG2   HG22   sing N N 622 
THR CG2   HG23   sing N N 623 
THR OXT   HXT    sing N N 624 
TRP N     CA     sing N N 625 
TRP N     H      sing N N 626 
TRP N     H2     sing N N 627 
TRP CA    C      sing N N 628 
TRP CA    CB     sing N N 629 
TRP CA    HA     sing N N 630 
TRP C     O      doub N N 631 
TRP C     OXT    sing N N 632 
TRP CB    CG     sing N N 633 
TRP CB    HB2    sing N N 634 
TRP CB    HB3    sing N N 635 
TRP CG    CD1    doub Y N 636 
TRP CG    CD2    sing Y N 637 
TRP CD1   NE1    sing Y N 638 
TRP CD1   HD1    sing N N 639 
TRP CD2   CE2    doub Y N 640 
TRP CD2   CE3    sing Y N 641 
TRP NE1   CE2    sing Y N 642 
TRP NE1   HE1    sing N N 643 
TRP CE2   CZ2    sing Y N 644 
TRP CE3   CZ3    doub Y N 645 
TRP CE3   HE3    sing N N 646 
TRP CZ2   CH2    doub Y N 647 
TRP CZ2   HZ2    sing N N 648 
TRP CZ3   CH2    sing Y N 649 
TRP CZ3   HZ3    sing N N 650 
TRP CH2   HH2    sing N N 651 
TRP OXT   HXT    sing N N 652 
TYR N     CA     sing N N 653 
TYR N     H      sing N N 654 
TYR N     H2     sing N N 655 
TYR CA    C      sing N N 656 
TYR CA    CB     sing N N 657 
TYR CA    HA     sing N N 658 
TYR C     O      doub N N 659 
TYR C     OXT    sing N N 660 
TYR CB    CG     sing N N 661 
TYR CB    HB2    sing N N 662 
TYR CB    HB3    sing N N 663 
TYR CG    CD1    doub Y N 664 
TYR CG    CD2    sing Y N 665 
TYR CD1   CE1    sing Y N 666 
TYR CD1   HD1    sing N N 667 
TYR CD2   CE2    doub Y N 668 
TYR CD2   HD2    sing N N 669 
TYR CE1   CZ     doub Y N 670 
TYR CE1   HE1    sing N N 671 
TYR CE2   CZ     sing Y N 672 
TYR CE2   HE2    sing N N 673 
TYR CZ    OH     sing N N 674 
TYR OH    HH     sing N N 675 
TYR OXT   HXT    sing N N 676 
VAL N     CA     sing N N 677 
VAL N     H      sing N N 678 
VAL N     H2     sing N N 679 
VAL CA    C      sing N N 680 
VAL CA    CB     sing N N 681 
VAL CA    HA     sing N N 682 
VAL C     O      doub N N 683 
VAL C     OXT    sing N N 684 
VAL CB    CG1    sing N N 685 
VAL CB    CG2    sing N N 686 
VAL CB    HB     sing N N 687 
VAL CG1   HG11   sing N N 688 
VAL CG1   HG12   sing N N 689 
VAL CG1   HG13   sing N N 690 
VAL CG2   HG21   sing N N 691 
VAL CG2   HG22   sing N N 692 
VAL CG2   HG23   sing N N 693 
VAL OXT   HXT    sing N N 694 
XG4 C2    N1     sing N N 695 
XG4 N1    C6     sing N N 696 
XG4 N1    HN1    sing N N 697 
XG4 N3    C2     doub N N 698 
XG4 N2    C2     sing N N 699 
XG4 N2    HN2    sing N N 700 
XG4 N2    HN2A   sing N N 701 
XG4 N3    C4     sing N N 702 
XG4 N9    C4     sing Y N 703 
XG4 C4    C5     doub Y N 704 
XG4 C5    N7     sing Y N 705 
XG4 C5    C6     sing N N 706 
XG4 C6    O6     doub N N 707 
XG4 C8    N7     doub Y N 708 
XG4 N9    C8     sing Y N 709 
XG4 C8    H8     sing N N 710 
XG4 "C1'" N9     sing N N 711 
XG4 "O5'" PA     sing N N 712 
XG4 O1A   PA     doub N N 713 
XG4 PA    O2A    sing N N 714 
XG4 PA    N3A    sing N N 715 
XG4 O1B   PB     doub N N 716 
XG4 N3A   PB     sing N N 717 
XG4 PB    O2B    sing N N 718 
XG4 PB    O3B    sing N N 719 
XG4 O1G   PG     doub N N 720 
XG4 PG    O3B    sing N N 721 
XG4 PG    O2G    sing N N 722 
XG4 PG    O3G    sing N N 723 
XG4 "O4'" "C1'"  sing N N 724 
XG4 "C1'" "C2'"  sing N N 725 
XG4 "C1'" "H1'"  sing N N 726 
XG4 "C2'" "C3'"  sing N N 727 
XG4 "C2'" "H2'"  sing N N 728 
XG4 "C2'" "H2'A" sing N N 729 
XG4 O2A   HO2A   sing N N 730 
XG4 O2B   HO2B   sing N N 731 
XG4 O2G   HO2G   sing N N 732 
XG4 "C4'" "C3'"  sing N N 733 
XG4 "C3'" "O3'"  sing N N 734 
XG4 "C3'" "H3'"  sing N N 735 
XG4 "O3'" "HO3'" sing N N 736 
XG4 N3A   HN3A   sing N N 737 
XG4 O3G   HO3G   sing N N 738 
XG4 "O4'" "C4'"  sing N N 739 
XG4 "C4'" "C5'"  sing N N 740 
XG4 "C4'" "H4'"  sing N N 741 
XG4 "C5'" "O5'"  sing N N 742 
XG4 "C5'" "H5'"  sing N N 743 
XG4 "C5'" "H5'A" sing N N 744 
# 
loop_
_ndb_struct_conf_na.entry_id 
_ndb_struct_conf_na.feature 
9EMI 'double helix'        
9EMI '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 -0.213 -0.221 -0.093 -4.985 -10.879 -1.659  1  P_DG1:DC16_T  P 1  ? T 16 ? 19 1 
1 B DA 2  1_555 C DT  15 1_555 0.281  0.016  -0.268 -9.713 -9.939  -14.478 2  P_DA2:DT15_T  P 2  ? T 15 ? 20 1 
1 B DC 3  1_555 C DG  14 1_555 0.202  -0.150 -0.224 -7.394 -5.071  0.452   3  P_DC3:DG14_T  P 3  ? T 14 ? 19 1 
1 B DC 4  1_555 C DG  13 1_555 0.221  -0.139 -0.106 -1.249 -4.680  3.710   4  P_DC4:DG13_T  P 4  ? T 13 ? 19 1 
1 B DA 5  1_555 C DT  12 1_555 0.108  -0.078 0.073  -3.806 -4.314  -1.212  5  P_DA5:DT12_T  P 5  ? T 12 ? 20 1 
1 B DC 6  1_555 C DG  11 1_555 0.228  -0.125 -0.021 -0.282 -3.210  2.201   6  P_DC6:DG11_T  P 6  ? T 11 ? 19 1 
1 B DG 7  1_555 C DC  10 1_555 -0.213 -0.160 0.228  -4.622 -3.599  -1.858  7  P_DG7:DC10_T  P 7  ? T 10 ? 19 1 
1 B DG 8  1_555 C DC  9  1_555 -0.215 -0.131 0.079  -2.497 -0.208  2.459   8  P_DG8:DC9_T   P 8  ? T 9  ? 19 1 
1 B DC 9  1_555 C DG  8  1_555 0.173  -0.144 0.295  -0.468 2.089   -0.324  9  P_DC9:DG8_T   P 9  ? T 8  ? 19 1 
1 B DC 10 1_555 C DG  7  1_555 0.215  -0.215 0.471  5.740  0.999   1.870   10 P_DC10:DG7_T  P 10 ? T 7  ? 19 1 
1 B DA 11 1_555 C 6HT 6  1_555 0.070  -0.333 0.237  2.116  -3.133  1.786   11 P_DA11:6HT6_T P 11 ? T 6  ? 20 1 
1 B DC 12 1_555 C 6HG 5  1_555 0.305  -0.308 0.056  -0.761 -1.237  -3.028  12 P_DC12:6HG5_T P 12 ? T 5  ? 19 1 
1 B DA 13 1_555 C 6HT 4  1_555 0.331  -0.429 -0.276 3.080  3.953   -4.627  13 P_DA13:6HT4_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 -1.664 0.313  3.276 -4.725 0.199 38.038 0.451  1.924  3.452 0.304 
7.215  38.320 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 1.189  -0.076 3.172 -1.043 0.708 33.549 -0.243 -2.222 3.132 1.227 
1.806  33.572 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 -0.119 0.293  3.308 -2.555 3.983 29.365 -0.280 -0.315 3.315 7.793 
4.998  29.735 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 -0.617 1.096  3.457 -2.981 1.619 40.961 1.374  0.533  3.530 2.308 
4.250  41.095 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 0.080  -0.521 3.273 0.419  2.580 26.848 -1.770 -0.066 3.210 5.539 
-0.900 26.973 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 -0.511 1.319  3.502 -5.431 1.835 41.743 1.629  0.101  3.590 2.561 
7.579  42.117 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 0.793  -0.501 3.344 -0.453 4.028 33.237 -1.541 -1.453 3.251 7.009 
0.789  33.476 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 -0.544 -0.582 3.387 0.999  4.707 30.288 -2.047 1.230  3.242 8.938 
-1.897 30.659 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 0.804  -0.238 3.331 -0.266 2.528 31.438 -0.915 -1.530 3.295 4.656 
0.490  31.538 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 6HT 6  1_555 -0.382 -1.084 3.262 -2.279 4.726 30.292 -2.950 0.284  3.081 8.960 
4.321  30.732 10 PP_DC10DA11:6HT6DG7_TT  P 10 ? T 7  ? P 11 ? T 6  ? 
1 B DA 11 1_555 C 6HT 6  1_555 B DC 12 1_555 C 6HG 5  1_555 -0.679 -0.920 3.548 -0.321 3.316 38.848 -1.808 0.975  3.466 4.975 
0.481  38.985 11 PP_DA11DC12:6HG56HT6_TT P 11 ? T 6  ? P 12 ? T 5  ? 
1 B DC 12 1_555 C 6HG 5  1_555 B DA 13 1_555 C 6HT 4  1_555 -0.283 -0.204 3.420 1.895  0.479 33.344 -0.438 0.819  3.397 0.834 
-3.298 33.399 12 PP_DC12DA13:6HT46HG5_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                    9EMI 
_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]   0.008972 
_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]   0.006599 
_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]   0.014203 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . MET A 1 1   ? -34.443 49.629  -16.570 1.00 86.98  ? 1   MET A N     1 
ATOM   2    C  CA    . MET A 1 1   ? -33.989 48.249  -16.691 1.00 69.78  ? 1   MET A CA    1 
ATOM   3    C  C     . MET A 1 1   ? -34.775 47.516  -17.773 1.00 65.71  ? 1   MET A C     1 
ATOM   4    O  O     . MET A 1 1   ? -35.995 47.382  -17.682 1.00 67.39  ? 1   MET A O     1 
ATOM   5    C  CB    . MET A 1 1   ? -34.123 47.521  -15.352 1.00 71.86  ? 1   MET A CB    1 
ATOM   6    C  CG    . MET A 1 1   ? -33.746 46.050  -15.398 1.00 66.28  ? 1   MET A CG    1 
ATOM   7    S  SD    . MET A 1 1   ? -34.525 45.093  -14.085 1.00 69.20  ? 1   MET A SD    1 
ATOM   8    C  CE    . MET A 1 1   ? -33.164 44.928  -12.934 1.00 64.97  ? 1   MET A CE    1 
ATOM   9    N  N     . ILE A 1 2   ? -34.067 47.046  -18.797 1.00 61.73  ? 2   ILE A N     1 
ATOM   10   C  CA    . ILE A 1 2   ? -34.716 46.371  -19.915 1.00 57.07  ? 2   ILE A CA    1 
ATOM   11   C  C     . ILE A 1 2   ? -35.214 45.010  -19.447 1.00 59.57  ? 2   ILE A C     1 
ATOM   12   O  O     . ILE A 1 2   ? -34.432 44.169  -18.988 1.00 61.80  ? 2   ILE A O     1 
ATOM   13   C  CB    . ILE A 1 2   ? -33.759 46.236  -21.107 1.00 55.14  ? 2   ILE A CB    1 
ATOM   14   C  CG1   . ILE A 1 2   ? -33.759 47.520  -21.935 1.00 57.12  ? 2   ILE A CG1   1 
ATOM   15   C  CG2   . ILE A 1 2   ? -34.160 45.068  -21.996 1.00 51.26  ? 2   ILE A CG2   1 
ATOM   16   C  CD1   . ILE A 1 2   ? -32.413 47.863  -22.523 1.00 53.55  ? 2   ILE A CD1   1 
ATOM   17   N  N     . LEU A 1 3   ? -36.526 44.793  -19.545 1.00 62.17  ? 3   LEU A N     1 
ATOM   18   C  CA    . LEU A 1 3   ? -37.076 43.481  -19.232 1.00 55.05  ? 3   LEU A CA    1 
ATOM   19   C  C     . LEU A 1 3   ? -36.940 42.533  -20.416 1.00 55.92  ? 3   LEU A C     1 
ATOM   20   O  O     . LEU A 1 3   ? -36.380 41.439  -20.281 1.00 64.42  ? 3   LEU A O     1 
ATOM   21   C  CB    . LEU A 1 3   ? -38.542 43.603  -18.808 1.00 53.67  ? 3   LEU A CB    1 
ATOM   22   C  CG    . LEU A 1 3   ? -38.827 44.327  -17.491 1.00 60.61  ? 3   LEU A CG    1 
ATOM   23   C  CD1   . LEU A 1 3   ? -40.249 44.046  -17.030 1.00 56.63  ? 3   LEU A CD1   1 
ATOM   24   C  CD2   . LEU A 1 3   ? -37.822 43.920  -16.423 1.00 56.64  ? 3   LEU A CD2   1 
ATOM   25   N  N     . ASP A 1 4   ? -37.428 42.937  -21.585 1.00 53.37  ? 4   ASP A N     1 
ATOM   26   C  CA    . ASP A 1 4   ? -37.403 42.051  -22.745 1.00 51.58  ? 4   ASP A CA    1 
ATOM   27   C  C     . ASP A 1 4   ? -37.599 42.876  -24.011 1.00 50.59  ? 4   ASP A C     1 
ATOM   28   O  O     . ASP A 1 4   ? -37.751 44.099  -23.963 1.00 44.51  ? 4   ASP A O     1 
ATOM   29   C  CB    . ASP A 1 4   ? -38.470 40.957  -22.623 1.00 62.39  ? 4   ASP A CB    1 
ATOM   30   C  CG    . ASP A 1 4   ? -38.065 39.667  -23.311 1.00 75.79  ? 4   ASP A CG    1 
ATOM   31   O  OD1   . ASP A 1 4   ? -37.545 39.734  -24.445 1.00 63.26  ? 4   ASP A OD1   1 
ATOM   32   O  OD2   . ASP A 1 4   ? -38.265 38.586  -22.717 1.00 76.26  ? 4   ASP A OD2   1 
ATOM   33   N  N     . THR A 1 5   ? -37.581 42.190  -25.155 1.00 47.86  ? 5   THR A N     1 
ATOM   34   C  CA    . THR A 1 5   ? -37.819 42.804  -26.454 1.00 46.53  ? 5   THR A CA    1 
ATOM   35   C  C     . THR A 1 5   ? -38.601 41.841  -27.334 1.00 44.94  ? 5   THR A C     1 
ATOM   36   O  O     . THR A 1 5   ? -38.483 40.620  -27.205 1.00 40.53  ? 5   THR A O     1 
ATOM   37   C  CB    . THR A 1 5   ? -36.515 43.179  -27.185 1.00 48.20  ? 5   THR A CB    1 
ATOM   38   O  OG1   . THR A 1 5   ? -35.757 41.993  -27.455 1.00 47.00  ? 5   THR A OG1   1 
ATOM   39   C  CG2   . THR A 1 5   ? -35.671 44.154  -26.370 1.00 47.39  ? 5   THR A CG2   1 
ATOM   40   N  N     . ASP A 1 6   ? -39.405 42.408  -28.229 1.00 39.80  ? 6   ASP A N     1 
ATOM   41   C  CA    . ASP A 1 6   ? -39.996 41.650  -29.329 1.00 41.85  ? 6   ASP A CA    1 
ATOM   42   C  C     . ASP A 1 6   ? -40.225 42.607  -30.493 1.00 42.60  ? 6   ASP A C     1 
ATOM   43   O  O     . ASP A 1 6   ? -39.702 43.723  -30.508 1.00 41.89  ? 6   ASP A O     1 
ATOM   44   C  CB    . ASP A 1 6   ? -41.275 40.916  -28.888 1.00 51.69  ? 6   ASP A CB    1 
ATOM   45   C  CG    . ASP A 1 6   ? -42.434 41.854  -28.549 1.00 54.99  ? 6   ASP A CG    1 
ATOM   46   O  OD1   . ASP A 1 6   ? -42.310 43.089  -28.681 1.00 56.84  ? 6   ASP A OD1   1 
ATOM   47   O  OD2   . ASP A 1 6   ? -43.498 41.333  -28.153 1.00 52.74  ? 6   ASP A OD2   1 
ATOM   48   N  N     . TYR A 1 7   ? -41.015 42.177  -31.474 1.00 43.06  ? 7   TYR A N     1 
ATOM   49   C  CA    . TYR A 1 7   ? -41.376 43.068  -32.566 1.00 48.51  ? 7   TYR A CA    1 
ATOM   50   C  C     . TYR A 1 7   ? -42.785 42.752  -33.042 1.00 48.47  ? 7   TYR A C     1 
ATOM   51   O  O     . TYR A 1 7   ? -43.238 41.606  -32.986 1.00 47.05  ? 7   TYR A O     1 
ATOM   52   C  CB    . TYR A 1 7   ? -40.382 42.979  -33.734 1.00 43.37  ? 7   TYR A CB    1 
ATOM   53   C  CG    . TYR A 1 7   ? -40.618 41.846  -34.716 1.00 46.94  ? 7   TYR A CG    1 
ATOM   54   C  CD1   . TYR A 1 7   ? -39.999 40.613  -34.547 1.00 46.61  ? 7   TYR A CD1   1 
ATOM   55   C  CD2   . TYR A 1 7   ? -41.431 42.023  -35.832 1.00 49.40  ? 7   TYR A CD2   1 
ATOM   56   C  CE1   . TYR A 1 7   ? -40.200 39.582  -35.447 1.00 43.87  ? 7   TYR A CE1   1 
ATOM   57   C  CE2   . TYR A 1 7   ? -41.640 40.997  -36.734 1.00 49.85  ? 7   TYR A CE2   1 
ATOM   58   C  CZ    . TYR A 1 7   ? -41.022 39.780  -36.538 1.00 54.17  ? 7   TYR A CZ    1 
ATOM   59   O  OH    . TYR A 1 7   ? -41.228 38.760  -37.439 1.00 56.32  ? 7   TYR A OH    1 
ATOM   60   N  N     . ILE A 1 8   ? -43.471 43.794  -33.507 1.00 49.65  ? 8   ILE A N     1 
ATOM   61   C  CA    . ILE A 1 8   ? -44.761 43.661  -34.167 1.00 50.32  ? 8   ILE A CA    1 
ATOM   62   C  C     . ILE A 1 8   ? -44.608 44.116  -35.615 1.00 52.09  ? 8   ILE A C     1 
ATOM   63   O  O     . ILE A 1 8   ? -43.582 44.667  -36.014 1.00 49.30  ? 8   ILE A O     1 
ATOM   64   C  CB    . ILE A 1 8   ? -45.876 44.453  -33.458 1.00 47.30  ? 8   ILE A CB    1 
ATOM   65   C  CG1   . ILE A 1 8   ? -45.527 45.943  -33.402 1.00 54.84  ? 8   ILE A CG1   1 
ATOM   66   C  CG2   . ILE A 1 8   ? -46.130 43.891  -32.068 1.00 46.80  ? 8   ILE A CG2   1 
ATOM   67   C  CD1   . ILE A 1 8   ? -46.543 46.782  -32.654 1.00 52.03  ? 8   ILE A CD1   1 
ATOM   68   N  N     . THR A 1 9   ? -45.649 43.871  -36.404 1.00 43.27  ? 9   THR A N     1 
ATOM   69   C  CA    . THR A 1 9   ? -45.671 44.240  -37.816 1.00 44.48  ? 9   THR A CA    1 
ATOM   70   C  C     . THR A 1 9   ? -46.700 45.347  -38.007 1.00 56.01  ? 9   THR A C     1 
ATOM   71   O  O     . THR A 1 9   ? -47.906 45.108  -37.900 1.00 58.87  ? 9   THR A O     1 
ATOM   72   C  CB    . THR A 1 9   ? -45.990 43.034  -38.695 1.00 51.88  ? 9   THR A CB    1 
ATOM   73   O  OG1   . THR A 1 9   ? -44.979 42.034  -38.523 1.00 54.67  ? 9   THR A OG1   1 
ATOM   74   C  CG2   . THR A 1 9   ? -46.040 43.445  -40.158 1.00 52.31  ? 9   THR A CG2   1 
ATOM   75   N  N     . GLU A 1 10  ? -46.223 46.553  -38.289 1.00 55.40  ? 10  GLU A N     1 
ATOM   76   C  CA    . GLU A 1 10  ? -47.070 47.718  -38.506 1.00 56.37  ? 10  GLU A CA    1 
ATOM   77   C  C     . GLU A 1 10  ? -46.983 48.097  -39.980 1.00 59.94  ? 10  GLU A C     1 
ATOM   78   O  O     . GLU A 1 10  ? -45.929 48.545  -40.450 1.00 55.52  ? 10  GLU A O     1 
ATOM   79   C  CB    . GLU A 1 10  ? -46.637 48.868  -37.603 1.00 49.86  ? 10  GLU A CB    1 
ATOM   80   C  CG    . GLU A 1 10  ? -47.617 50.013  -37.520 1.00 63.70  ? 10  GLU A CG    1 
ATOM   81   C  CD    . GLU A 1 10  ? -47.392 50.867  -36.290 1.00 78.98  ? 10  GLU A CD    1 
ATOM   82   O  OE1   . GLU A 1 10  ? -47.881 50.486  -35.206 1.00 83.21  ? 10  GLU A OE1   1 
ATOM   83   O  OE2   . GLU A 1 10  ? -46.718 51.913  -36.405 1.00 76.80  ? 10  GLU A OE2   1 
ATOM   84   N  N     . ASP A 1 11  ? -48.087 47.900  -40.706 1.00 63.02  ? 11  ASP A N     1 
ATOM   85   C  CA    . ASP A 1 11  ? -48.160 48.195  -42.138 1.00 61.47  ? 11  ASP A CA    1 
ATOM   86   C  C     . ASP A 1 11  ? -47.033 47.506  -42.902 1.00 62.81  ? 11  ASP A C     1 
ATOM   87   O  O     . ASP A 1 11  ? -46.388 48.094  -43.772 1.00 63.83  ? 11  ASP A O     1 
ATOM   88   C  CB    . ASP A 1 11  ? -48.152 49.703  -42.390 1.00 65.60  ? 11  ASP A CB    1 
ATOM   89   C  CG    . ASP A 1 11  ? -49.499 50.347  -42.119 1.00 71.40  ? 11  ASP A CG    1 
ATOM   90   O  OD1   . ASP A 1 11  ? -50.480 50.005  -42.816 1.00 61.89  ? 11  ASP A OD1   1 
ATOM   91   O  OD2   . ASP A 1 11  ? -49.576 51.195  -41.205 1.00 85.45  ? 11  ASP A OD2   1 
ATOM   92   N  N     . GLY A 1 12  ? -46.788 46.242  -42.564 1.00 67.20  ? 12  GLY A N     1 
ATOM   93   C  CA    . GLY A 1 12  ? -45.761 45.461  -43.216 1.00 58.84  ? 12  GLY A CA    1 
ATOM   94   C  C     . GLY A 1 12  ? -44.344 45.757  -42.779 1.00 55.10  ? 12  GLY A C     1 
ATOM   95   O  O     . GLY A 1 12  ? -43.411 45.156  -43.327 1.00 52.25  ? 12  GLY A O     1 
ATOM   96   N  N     . LYS A 1 13  ? -44.146 46.656  -41.807 1.00 51.88  ? 13  LYS A N     1 
ATOM   97   C  CA    . LYS A 1 13  ? -42.803 47.006  -41.377 1.00 51.43  ? 13  LYS A CA    1 
ATOM   98   C  C     . LYS A 1 13  ? -42.558 46.559  -39.938 1.00 52.45  ? 13  LYS A C     1 
ATOM   99   O  O     . LYS A 1 13  ? -43.475 46.567  -39.113 1.00 48.83  ? 13  LYS A O     1 
ATOM   100  C  CB    . LYS A 1 13  ? -42.568 48.517  -41.488 1.00 48.04  ? 13  LYS A CB    1 
ATOM   101  C  CG    . LYS A 1 13  ? -42.907 49.091  -42.853 1.00 52.01  ? 13  LYS A CG    1 
ATOM   102  C  CD    . LYS A 1 13  ? -42.048 50.299  -43.181 1.00 62.07  ? 13  LYS A CD    1 
ATOM   103  C  CE    . LYS A 1 13  ? -41.518 50.222  -44.603 1.00 74.31  ? 13  LYS A CE    1 
ATOM   104  N  NZ    . LYS A 1 13  ? -42.504 49.592  -45.525 1.00 63.63  ? 13  LYS A NZ    1 
ATOM   105  N  N     . PRO A 1 14  ? -41.331 46.165  -39.603 1.00 46.40  ? 14  PRO A N     1 
ATOM   106  C  CA    . PRO A 1 14  ? -41.046 45.723  -38.233 1.00 42.09  ? 14  PRO A CA    1 
ATOM   107  C  C     . PRO A 1 14  ? -40.972 46.902  -37.277 1.00 42.68  ? 14  PRO A C     1 
ATOM   108  O  O     . PRO A 1 14  ? -40.406 47.952  -37.592 1.00 48.65  ? 14  PRO A O     1 
ATOM   109  C  CB    . PRO A 1 14  ? -39.679 45.032  -38.355 1.00 47.84  ? 14  PRO A CB    1 
ATOM   110  C  CG    . PRO A 1 14  ? -39.340 45.032  -39.830 1.00 54.95  ? 14  PRO A CG    1 
ATOM   111  C  CD    . PRO A 1 14  ? -40.128 46.133  -40.446 1.00 51.94  ? 14  PRO A CD    1 
ATOM   112  N  N     . VAL A 1 15  ? -41.557 46.720  -36.096 1.00 42.55  ? 15  VAL A N     1 
ATOM   113  C  CA    . VAL A 1 15  ? -41.505 47.703  -35.023 1.00 44.72  ? 15  VAL A CA    1 
ATOM   114  C  C     . VAL A 1 15  ? -41.011 46.976  -33.783 1.00 53.54  ? 15  VAL A C     1 
ATOM   115  O  O     . VAL A 1 15  ? -41.724 46.128  -33.230 1.00 54.52  ? 15  VAL A O     1 
ATOM   116  C  CB    . VAL A 1 15  ? -42.865 48.363  -34.761 1.00 54.01  ? 15  VAL A CB    1 
ATOM   117  C  CG1   . VAL A 1 15  ? -42.745 49.386  -33.641 1.00 49.71  ? 15  VAL A CG1   1 
ATOM   118  C  CG2   . VAL A 1 15  ? -43.392 49.016  -36.027 1.00 47.94  ? 15  VAL A CG2   1 
ATOM   119  N  N     . ILE A 1 16  ? -39.785 47.287  -33.361 1.00 46.77  ? 16  ILE A N     1 
ATOM   120  C  CA    . ILE A 1 16  ? -39.223 46.698  -32.156 1.00 45.63  ? 16  ILE A CA    1 
ATOM   121  C  C     . ILE A 1 16  ? -39.894 47.315  -30.937 1.00 47.53  ? 16  ILE A C     1 
ATOM   122  O  O     . ILE A 1 16  ? -40.053 48.541  -30.847 1.00 51.00  ? 16  ILE A O     1 
ATOM   123  C  CB    . ILE A 1 16  ? -37.700 46.906  -32.119 1.00 46.39  ? 16  ILE A CB    1 
ATOM   124  C  CG1   . ILE A 1 16  ? -36.991 45.895  -33.026 1.00 45.63  ? 16  ILE A CG1   1 
ATOM   125  C  CG2   . ILE A 1 16  ? -37.171 46.816  -30.694 1.00 43.78  ? 16  ILE A CG2   1 
ATOM   126  C  CD1   . ILE A 1 16  ? -36.910 44.495  -32.450 1.00 44.79  ? 16  ILE A CD1   1 
ATOM   127  N  N     . ARG A 1 17  ? -40.306 46.464  -30.002 1.00 42.51  ? 17  ARG A N     1 
ATOM   128  C  CA    . ARG A 1 17  ? -40.794 46.876  -28.695 1.00 49.02  ? 17  ARG A CA    1 
ATOM   129  C  C     . ARG A 1 17  ? -39.784 46.450  -27.640 1.00 46.39  ? 17  ARG A C     1 
ATOM   130  O  O     . ARG A 1 17  ? -39.387 45.279  -27.593 1.00 48.64  ? 17  ARG A O     1 
ATOM   131  C  CB    . ARG A 1 17  ? -42.159 46.258  -28.389 1.00 43.78  ? 17  ARG A CB    1 
ATOM   132  C  CG    . ARG A 1 17  ? -43.278 46.714  -29.299 1.00 55.32  ? 17  ARG A CG    1 
ATOM   133  C  CD    . ARG A 1 17  ? -44.271 45.590  -29.523 1.00 57.11  ? 17  ARG A CD    1 
ATOM   134  N  NE    . ARG A 1 17  ? -45.155 45.403  -28.378 1.00 59.65  ? 17  ARG A NE    1 
ATOM   135  C  CZ    . ARG A 1 17  ? -45.730 44.253  -28.054 1.00 61.36  ? 17  ARG A CZ    1 
ATOM   136  N  NH1   . ARG A 1 17  ? -45.525 43.153  -28.760 1.00 52.22  ? 17  ARG A NH1   1 
ATOM   137  N  NH2   . ARG A 1 17  ? -46.530 44.205  -26.992 1.00 63.09  ? 17  ARG A NH2   1 
ATOM   138  N  N     . ILE A 1 18  ? -39.374 47.400  -26.804 1.00 43.81  ? 18  ILE A N     1 
ATOM   139  C  CA    . ILE A 1 18  ? -38.475 47.163  -25.680 1.00 50.38  ? 18  ILE A CA    1 
ATOM   140  C  C     . ILE A 1 18  ? -39.285 47.366  -24.406 1.00 54.57  ? 18  ILE A C     1 
ATOM   141  O  O     . ILE A 1 18  ? -39.626 48.501  -24.052 1.00 53.44  ? 18  ILE A O     1 
ATOM   142  C  CB    . ILE A 1 18  ? -37.254 48.094  -25.719 1.00 48.67  ? 18  ILE A CB    1 
ATOM   143  C  CG1   . ILE A 1 18  ? -36.537 47.979  -27.064 1.00 50.73  ? 18  ILE A CG1   1 
ATOM   144  C  CG2   . ILE A 1 18  ? -36.290 47.772  -24.588 1.00 47.89  ? 18  ILE A CG2   1 
ATOM   145  C  CD1   . ILE A 1 18  ? -36.617 49.232  -27.901 1.00 56.87  ? 18  ILE A CD1   1 
ATOM   146  N  N     . PHE A 1 19  ? -39.615 46.263  -23.733 1.00 53.47  ? 19  PHE A N     1 
ATOM   147  C  CA    . PHE A 1 19  ? -40.323 46.308  -22.461 1.00 52.64  ? 19  PHE A CA    1 
ATOM   148  C  C     . PHE A 1 19  ? -39.319 46.519  -21.338 1.00 56.19  ? 19  PHE A C     1 
ATOM   149  O  O     . PHE A 1 19  ? -38.370 45.736  -21.196 1.00 57.57  ? 19  PHE A O     1 
ATOM   150  C  CB    . PHE A 1 19  ? -41.094 45.008  -22.228 1.00 48.42  ? 19  PHE A CB    1 
ATOM   151  C  CG    . PHE A 1 19  ? -41.933 44.575  -23.394 1.00 53.74  ? 19  PHE A CG    1 
ATOM   152  C  CD1   . PHE A 1 19  ? -43.245 45.000  -23.525 1.00 53.63  ? 19  PHE A CD1   1 
ATOM   153  C  CD2   . PHE A 1 19  ? -41.407 43.735  -24.360 1.00 54.60  ? 19  PHE A CD2   1 
ATOM   154  C  CE1   . PHE A 1 19  ? -44.013 44.596  -24.602 1.00 52.92  ? 19  PHE A CE1   1 
ATOM   155  C  CE2   . PHE A 1 19  ? -42.168 43.330  -25.438 1.00 56.82  ? 19  PHE A CE2   1 
ATOM   156  C  CZ    . PHE A 1 19  ? -43.472 43.759  -25.559 1.00 56.54  ? 19  PHE A CZ    1 
ATOM   157  N  N     . LYS A 1 20  ? -39.540 47.561  -20.532 1.00 57.26  ? 20  LYS A N     1 
ATOM   158  C  CA    . LYS A 1 20  ? -38.590 47.972  -19.509 1.00 62.90  ? 20  LYS A CA    1 
ATOM   159  C  C     . LYS A 1 20  ? -39.338 48.462  -18.276 1.00 64.18  ? 20  LYS A C     1 
ATOM   160  O  O     . LYS A 1 20  ? -40.543 48.717  -18.311 1.00 62.19  ? 20  LYS A O     1 
ATOM   161  C  CB    . LYS A 1 20  ? -37.658 49.071  -20.037 1.00 62.80  ? 20  LYS A CB    1 
ATOM   162  C  CG    . LYS A 1 20  ? -38.302 49.937  -21.111 1.00 67.86  ? 20  LYS A CG    1 
ATOM   163  C  CD    . LYS A 1 20  ? -37.275 50.448  -22.109 1.00 62.81  ? 20  LYS A CD    1 
ATOM   164  C  CE    . LYS A 1 20  ? -36.641 51.743  -21.635 1.00 70.22  ? 20  LYS A CE    1 
ATOM   165  N  NZ    . LYS A 1 20  ? -36.606 52.762  -22.721 1.00 71.43  ? 20  LYS A NZ    1 
ATOM   166  N  N     . LYS A 1 21  ? -38.594 48.609  -17.180 1.00 69.90  ? 21  LYS A N     1 
ATOM   167  C  CA    . LYS A 1 21  ? -39.112 49.146  -15.925 1.00 76.46  ? 21  LYS A CA    1 
ATOM   168  C  C     . LYS A 1 21  ? -38.192 50.274  -15.480 1.00 79.08  ? 21  LYS A C     1 
ATOM   169  O  O     . LYS A 1 21  ? -37.065 50.021  -15.044 1.00 79.28  ? 21  LYS A O     1 
ATOM   170  C  CB    . LYS A 1 21  ? -39.206 48.062  -14.851 1.00 76.36  ? 21  LYS A CB    1 
ATOM   171  C  CG    . LYS A 1 21  ? -40.310 48.296  -13.838 1.00 80.27  ? 21  LYS A CG    1 
ATOM   172  C  CD    . LYS A 1 21  ? -39.938 47.727  -12.480 1.00 81.83  ? 21  LYS A CD    1 
ATOM   173  C  CE    . LYS A 1 21  ? -41.078 47.888  -11.488 1.00 82.30  ? 21  LYS A CE    1 
ATOM   174  N  NZ    . LYS A 1 21  ? -42.405 47.675  -12.126 1.00 75.66  ? 21  LYS A NZ    1 
ATOM   175  N  N     . GLU A 1 22  ? -38.666 51.513  -15.587 1.00 84.08  ? 22  GLU A N     1 
ATOM   176  C  CA    . GLU A 1 22  ? -37.883 52.688  -15.230 1.00 92.91  ? 22  GLU A CA    1 
ATOM   177  C  C     . GLU A 1 22  ? -38.627 53.497  -14.177 1.00 93.56  ? 22  GLU A C     1 
ATOM   178  O  O     . GLU A 1 22  ? -39.819 53.783  -14.334 1.00 90.62  ? 22  GLU A O     1 
ATOM   179  C  CB    . GLU A 1 22  ? -37.589 53.552  -16.459 1.00 94.35  ? 22  GLU A CB    1 
ATOM   180  C  CG    . GLU A 1 22  ? -36.226 54.223  -16.425 1.00 107.25 ? 22  GLU A CG    1 
ATOM   181  C  CD    . GLU A 1 22  ? -35.598 54.338  -17.799 1.00 117.27 ? 22  GLU A CD    1 
ATOM   182  O  OE1   . GLU A 1 22  ? -36.348 54.357  -18.797 1.00 105.50 ? 22  GLU A OE1   1 
ATOM   183  O  OE2   . GLU A 1 22  ? -34.354 54.405  -17.880 1.00 122.62 ? 22  GLU A OE2   1 
ATOM   184  N  N     . ASN A 1 23  ? -37.917 53.848  -13.102 1.00 94.26  ? 23  ASN A N     1 
ATOM   185  C  CA    . ASN A 1 23  ? -38.465 54.654  -12.009 1.00 96.05  ? 23  ASN A CA    1 
ATOM   186  C  C     . ASN A 1 23  ? -39.745 54.039  -11.449 1.00 92.31  ? 23  ASN A C     1 
ATOM   187  O  O     . ASN A 1 23  ? -40.714 54.736  -11.139 1.00 96.88  ? 23  ASN A O     1 
ATOM   188  C  CB    . ASN A 1 23  ? -38.701 56.096  -12.456 1.00 101.16 ? 23  ASN A CB    1 
ATOM   189  C  CG    . ASN A 1 23  ? -37.414 56.888  -12.560 1.00 113.43 ? 23  ASN A CG    1 
ATOM   190  O  OD1   . ASN A 1 23  ? -36.489 56.695  -11.771 1.00 127.51 ? 23  ASN A OD1   1 
ATOM   191  N  ND2   . ASN A 1 23  ? -37.348 57.787  -13.536 1.00 114.75 ? 23  ASN A ND2   1 
ATOM   192  N  N     . GLY A 1 24  ? -39.747 52.714  -11.316 1.00 88.95  ? 24  GLY A N     1 
ATOM   193  C  CA    . GLY A 1 24  ? -40.899 52.014  -10.787 1.00 85.60  ? 24  GLY A CA    1 
ATOM   194  C  C     . GLY A 1 24  ? -42.108 51.983  -11.692 1.00 88.46  ? 24  GLY A C     1 
ATOM   195  O  O     . GLY A 1 24  ? -43.197 51.626  -11.232 1.00 83.66  ? 24  GLY A O     1 
ATOM   196  N  N     . GLU A 1 25  ? -41.958 52.345  -12.964 1.00 89.35  ? 25  GLU A N     1 
ATOM   197  C  CA    . GLU A 1 25  ? -43.059 52.342  -13.916 1.00 83.83  ? 25  GLU A CA    1 
ATOM   198  C  C     . GLU A 1 25  ? -42.692 51.491  -15.123 1.00 78.44  ? 25  GLU A C     1 
ATOM   199  O  O     . GLU A 1 25  ? -41.570 51.572  -15.634 1.00 76.80  ? 25  GLU A O     1 
ATOM   200  C  CB    . GLU A 1 25  ? -43.411 53.768  -14.360 1.00 87.56  ? 25  GLU A CB    1 
ATOM   201  C  CG    . GLU A 1 25  ? -44.196 53.844  -15.661 1.00 94.76  ? 25  GLU A CG    1 
ATOM   202  C  CD    . GLU A 1 25  ? -45.040 55.098  -15.761 1.00 113.14 ? 25  GLU A CD    1 
ATOM   203  O  OE1   . GLU A 1 25  ? -44.510 56.139  -16.202 1.00 104.67 ? 25  GLU A OE1   1 
ATOM   204  O  OE2   . GLU A 1 25  ? -46.235 55.042  -15.399 1.00 141.08 ? 25  GLU A OE2   1 
ATOM   205  N  N     . PHE A 1 26  ? -43.640 50.669  -15.567 1.00 68.08  ? 26  PHE A N     1 
ATOM   206  C  CA    . PHE A 1 26  ? -43.438 49.830  -16.740 1.00 66.64  ? 26  PHE A CA    1 
ATOM   207  C  C     . PHE A 1 26  ? -43.623 50.669  -17.998 1.00 66.08  ? 26  PHE A C     1 
ATOM   208  O  O     . PHE A 1 26  ? -44.671 51.297  -18.185 1.00 71.77  ? 26  PHE A O     1 
ATOM   209  C  CB    . PHE A 1 26  ? -44.410 48.651  -16.726 1.00 62.38  ? 26  PHE A CB    1 
ATOM   210  C  CG    . PHE A 1 26  ? -44.482 47.906  -18.030 1.00 63.00  ? 26  PHE A CG    1 
ATOM   211  C  CD1   . PHE A 1 26  ? -43.489 47.007  -18.385 1.00 63.21  ? 26  PHE A CD1   1 
ATOM   212  C  CD2   . PHE A 1 26  ? -45.540 48.106  -18.902 1.00 63.47  ? 26  PHE A CD2   1 
ATOM   213  C  CE1   . PHE A 1 26  ? -43.551 46.320  -19.583 1.00 60.51  ? 26  PHE A CE1   1 
ATOM   214  C  CE2   . PHE A 1 26  ? -45.607 47.422  -20.101 1.00 62.49  ? 26  PHE A CE2   1 
ATOM   215  C  CZ    . PHE A 1 26  ? -44.611 46.528  -20.442 1.00 60.39  ? 26  PHE A CZ    1 
ATOM   216  N  N     . LYS A 1 27  ? -42.608 50.681  -18.858 1.00 62.47  ? 27  LYS A N     1 
ATOM   217  C  CA    . LYS A 1 27  ? -42.645 51.426  -20.105 1.00 66.13  ? 27  LYS A CA    1 
ATOM   218  C  C     . LYS A 1 27  ? -42.364 50.499  -21.281 1.00 65.88  ? 27  LYS A C     1 
ATOM   219  O  O     . LYS A 1 27  ? -41.742 49.438  -21.140 1.00 66.80  ? 27  LYS A O     1 
ATOM   220  C  CB    . LYS A 1 27  ? -41.632 52.581  -20.101 1.00 69.00  ? 27  LYS A CB    1 
ATOM   221  C  CG    . LYS A 1 27  ? -41.441 53.256  -18.751 1.00 76.32  ? 27  LYS A CG    1 
ATOM   222  C  CD    . LYS A 1 27  ? -40.633 54.538  -18.889 1.00 84.78  ? 27  LYS A CD    1 
ATOM   223  C  CE    . LYS A 1 27  ? -41.064 55.580  -17.867 1.00 90.64  ? 27  LYS A CE    1 
ATOM   224  N  NZ    . LYS A 1 27  ? -40.301 55.471  -16.594 1.00 92.98  ? 27  LYS A NZ    1 
ATOM   225  N  N     . ILE A 1 28  ? -42.840 50.920  -22.450 1.00 64.20  ? 28  ILE A N     1 
ATOM   226  C  CA    . ILE A 1 28  ? -42.642 50.206  -23.705 1.00 58.65  ? 28  ILE A CA    1 
ATOM   227  C  C     . ILE A 1 28  ? -42.037 51.191  -24.696 1.00 68.92  ? 28  ILE A C     1 
ATOM   228  O  O     . ILE A 1 28  ? -42.733 52.090  -25.186 1.00 70.30  ? 28  ILE A O     1 
ATOM   229  C  CB    . ILE A 1 28  ? -43.947 49.618  -24.256 1.00 58.31  ? 28  ILE A CB    1 
ATOM   230  C  CG1   . ILE A 1 28  ? -44.522 48.592  -23.279 1.00 60.90  ? 28  ILE A CG1   1 
ATOM   231  C  CG2   . ILE A 1 28  ? -43.710 48.995  -25.627 1.00 56.03  ? 28  ILE A CG2   1 
ATOM   232  C  CD1   . ILE A 1 28  ? -45.604 47.718  -23.873 1.00 55.40  ? 28  ILE A CD1   1 
ATOM   233  N  N     . GLU A 1 29  ? -40.749 51.032  -24.984 1.00 59.24  ? 29  GLU A N     1 
ATOM   234  C  CA    . GLU A 1 29  ? -40.095 51.850  -25.994 1.00 56.11  ? 29  GLU A CA    1 
ATOM   235  C  C     . GLU A 1 29  ? -40.326 51.251  -27.375 1.00 52.96  ? 29  GLU A C     1 
ATOM   236  O  O     . GLU A 1 29  ? -40.234 50.036  -27.562 1.00 55.98  ? 29  GLU A O     1 
ATOM   237  C  CB    . GLU A 1 29  ? -38.596 51.956  -25.708 1.00 55.38  ? 29  GLU A CB    1 
ATOM   238  C  CG    . GLU A 1 29  ? -37.912 53.131  -26.385 1.00 61.23  ? 29  GLU A CG    1 
ATOM   239  C  CD    . GLU A 1 29  ? -36.419 52.920  -26.555 1.00 78.37  ? 29  GLU A CD    1 
ATOM   240  O  OE1   . GLU A 1 29  ? -35.767 52.460  -25.593 1.00 74.17  ? 29  GLU A OE1   1 
ATOM   241  O  OE2   . GLU A 1 29  ? -35.897 53.214  -27.651 1.00 83.20  ? 29  GLU A OE2   1 
ATOM   242  N  N     . TYR A 1 30  ? -40.633 52.106  -28.342 1.00 55.35  ? 30  TYR A N     1 
ATOM   243  C  CA    . TYR A 1 30  ? -40.867 51.677  -29.713 1.00 50.20  ? 30  TYR A CA    1 
ATOM   244  C  C     . TYR A 1 30  ? -39.719 52.130  -30.604 1.00 49.23  ? 30  TYR A C     1 
ATOM   245  O  O     . TYR A 1 30  ? -39.152 53.209  -30.404 1.00 57.14  ? 30  TYR A O     1 
ATOM   246  C  CB    . TYR A 1 30  ? -42.194 52.224  -30.241 1.00 56.28  ? 30  TYR A CB    1 
ATOM   247  C  CG    . TYR A 1 30  ? -43.406 51.662  -29.529 1.00 62.50  ? 30  TYR A CG    1 
ATOM   248  C  CD1   . TYR A 1 30  ? -43.916 52.275  -28.392 1.00 57.86  ? 30  TYR A CD1   1 
ATOM   249  C  CD2   . TYR A 1 30  ? -44.033 50.512  -29.991 1.00 53.61  ? 30  TYR A CD2   1 
ATOM   250  C  CE1   . TYR A 1 30  ? -45.020 51.763  -27.738 1.00 54.41  ? 30  TYR A CE1   1 
ATOM   251  C  CE2   . TYR A 1 30  ? -45.136 49.993  -29.346 1.00 55.61  ? 30  TYR A CE2   1 
ATOM   252  C  CZ    . TYR A 1 30  ? -45.626 50.622  -28.220 1.00 62.32  ? 30  TYR A CZ    1 
ATOM   253  O  OH    . TYR A 1 30  ? -46.727 50.105  -27.575 1.00 58.13  ? 30  TYR A OH    1 
ATOM   254  N  N     . ASP A 1 31  ? -39.373 51.294  -31.581 1.00 50.57  ? 31  ASP A N     1 
ATOM   255  C  CA    . ASP A 1 31  ? -38.282 51.592  -32.508 1.00 50.46  ? 31  ASP A CA    1 
ATOM   256  C  C     . ASP A 1 31  ? -38.674 51.092  -33.891 1.00 47.37  ? 31  ASP A C     1 
ATOM   257  O  O     . ASP A 1 31  ? -38.802 49.883  -34.103 1.00 48.43  ? 31  ASP A O     1 
ATOM   258  C  CB    . ASP A 1 31  ? -36.976 50.948  -32.044 1.00 51.53  ? 31  ASP A CB    1 
ATOM   259  C  CG    . ASP A 1 31  ? -35.752 51.595  -32.664 1.00 53.86  ? 31  ASP A CG    1 
ATOM   260  O  OD1   . ASP A 1 31  ? -35.891 52.275  -33.703 1.00 51.39  ? 31  ASP A OD1   1 
ATOM   261  O  OD2   . ASP A 1 31  ? -34.646 51.423  -32.107 1.00 54.62  ? 31  ASP A OD2   1 
ATOM   262  N  N     . ARG A 1 32  ? -38.857 52.015  -34.835 1.00 51.91  ? 32  ARG A N     1 
ATOM   263  C  CA    . ARG A 1 32  ? -39.217 51.662  -36.201 1.00 52.13  ? 32  ARG A CA    1 
ATOM   264  C  C     . ARG A 1 32  ? -38.064 51.874  -37.175 1.00 51.73  ? 32  ARG A C     1 
ATOM   265  O  O     . ARG A 1 32  ? -38.279 51.889  -38.391 1.00 56.01  ? 32  ARG A O     1 
ATOM   266  C  CB    . ARG A 1 32  ? -40.443 52.458  -36.648 1.00 61.84  ? 32  ARG A CB    1 
ATOM   267  C  CG    . ARG A 1 32  ? -41.428 52.762  -35.529 1.00 58.89  ? 32  ARG A CG    1 
ATOM   268  C  CD    . ARG A 1 32  ? -42.566 53.645  -36.020 1.00 52.86  ? 32  ARG A CD    1 
ATOM   269  N  NE    . ARG A 1 32  ? -43.859 53.195  -35.519 1.00 64.97  ? 32  ARG A NE    1 
ATOM   270  C  CZ    . ARG A 1 32  ? -44.321 53.452  -34.303 1.00 68.59  ? 32  ARG A CZ    1 
ATOM   271  N  NH1   . ARG A 1 32  ? -43.619 54.159  -33.432 1.00 55.07  ? 32  ARG A NH1   1 
ATOM   272  N  NH2   . ARG A 1 32  ? -45.516 52.986  -33.952 1.00 80.27  ? 32  ARG A NH2   1 
ATOM   273  N  N     . THR A 1 33  ? -36.842 52.029  -36.666 1.00 56.86  ? 33  THR A N     1 
ATOM   274  C  CA    . THR A 1 33  ? -35.686 52.315  -37.501 1.00 56.69  ? 33  THR A CA    1 
ATOM   275  C  C     . THR A 1 33  ? -34.741 51.134  -37.669 1.00 56.41  ? 33  THR A C     1 
ATOM   276  O  O     . THR A 1 33  ? -33.780 51.239  -38.439 1.00 56.58  ? 33  THR A O     1 
ATOM   277  C  CB    . THR A 1 33  ? -34.904 53.507  -36.930 1.00 59.57  ? 33  THR A CB    1 
ATOM   278  O  OG1   . THR A 1 33  ? -34.243 53.111  -35.721 1.00 59.32  ? 33  THR A OG1   1 
ATOM   279  C  CG2   . THR A 1 33  ? -35.843 54.664  -36.634 1.00 61.42  ? 33  THR A CG2   1 
ATOM   280  N  N     . PHE A 1 34  ? -34.979 50.020  -36.982 1.00 53.36  ? 34  PHE A N     1 
ATOM   281  C  CA    . PHE A 1 34  ? -34.106 48.859  -37.102 1.00 51.60  ? 34  PHE A CA    1 
ATOM   282  C  C     . PHE A 1 34  ? -34.465 48.060  -38.350 1.00 54.95  ? 34  PHE A C     1 
ATOM   283  O  O     . PHE A 1 34  ? -35.619 47.656  -38.529 1.00 55.04  ? 34  PHE A O     1 
ATOM   284  C  CB    . PHE A 1 34  ? -34.207 47.979  -35.858 1.00 50.86  ? 34  PHE A CB    1 
ATOM   285  C  CG    . PHE A 1 34  ? -33.030 47.064  -35.670 1.00 58.12  ? 34  PHE A CG    1 
ATOM   286  C  CD1   . PHE A 1 34  ? -31.744 47.573  -35.604 1.00 56.89  ? 34  PHE A CD1   1 
ATOM   287  C  CD2   . PHE A 1 34  ? -33.210 45.695  -35.565 1.00 50.22  ? 34  PHE A CD2   1 
ATOM   288  C  CE1   . PHE A 1 34  ? -30.659 46.733  -35.433 1.00 53.37  ? 34  PHE A CE1   1 
ATOM   289  C  CE2   . PHE A 1 34  ? -32.131 44.851  -35.396 1.00 57.61  ? 34  PHE A CE2   1 
ATOM   290  C  CZ    . PHE A 1 34  ? -30.853 45.371  -35.329 1.00 53.51  ? 34  PHE A CZ    1 
ATOM   291  N  N     . GLU A 1 35  ? -33.472 47.827  -39.209 1.00 50.96  ? 35  GLU A N     1 
ATOM   292  C  CA    . GLU A 1 35  ? -33.685 47.150  -40.480 1.00 52.59  ? 35  GLU A CA    1 
ATOM   293  C  C     . GLU A 1 35  ? -33.092 45.751  -40.447 1.00 53.48  ? 35  GLU A C     1 
ATOM   294  O  O     . GLU A 1 35  ? -31.933 45.586  -40.046 1.00 58.46  ? 35  GLU A O     1 
ATOM   295  C  CB    . GLU A 1 35  ? -33.058 47.951  -41.628 1.00 57.99  ? 35  GLU A CB    1 
ATOM   296  C  CG    . GLU A 1 35  ? -33.001 49.451  -41.384 1.00 68.37  ? 35  GLU A CG    1 
ATOM   297  C  CD    . GLU A 1 35  ? -32.144 50.176  -42.403 1.00 73.52  ? 35  GLU A CD    1 
ATOM   298  O  OE1   . GLU A 1 35  ? -32.485 50.141  -43.605 1.00 72.13  ? 35  GLU A OE1   1 
ATOM   299  O  OE2   . GLU A 1 35  ? -31.125 50.778  -42.003 1.00 69.99  ? 35  GLU A OE2   1 
ATOM   300  N  N     . PRO A 1 36  ? -33.842 44.730  -40.858 1.00 53.11  ? 36  PRO A N     1 
ATOM   301  C  CA    . PRO A 1 36  ? -33.282 43.375  -40.903 1.00 54.35  ? 36  PRO A CA    1 
ATOM   302  C  C     . PRO A 1 36  ? -32.250 43.237  -42.011 1.00 51.37  ? 36  PRO A C     1 
ATOM   303  O  O     . PRO A 1 36  ? -32.308 43.922  -43.035 1.00 52.35  ? 36  PRO A O     1 
ATOM   304  C  CB    . PRO A 1 36  ? -34.507 42.494  -41.173 1.00 52.09  ? 36  PRO A CB    1 
ATOM   305  C  CG    . PRO A 1 36  ? -35.480 43.406  -41.849 1.00 52.38  ? 36  PRO A CG    1 
ATOM   306  C  CD    . PRO A 1 36  ? -35.265 44.758  -41.235 1.00 52.71  ? 36  PRO A CD    1 
ATOM   307  N  N     . TYR A 1 37  ? -31.299 42.327  -41.800 1.00 50.28  ? 37  TYR A N     1 
ATOM   308  C  CA    . TYR A 1 37  ? -30.199 42.164  -42.741 1.00 50.72  ? 37  TYR A CA    1 
ATOM   309  C  C     . TYR A 1 37  ? -29.524 40.819  -42.519 1.00 49.32  ? 37  TYR A C     1 
ATOM   310  O  O     . TYR A 1 37  ? -29.703 40.173  -41.483 1.00 46.13  ? 37  TYR A O     1 
ATOM   311  C  CB    . TYR A 1 37  ? -29.172 43.295  -42.596 1.00 53.90  ? 37  TYR A CB    1 
ATOM   312  C  CG    . TYR A 1 37  ? -28.400 43.257  -41.292 1.00 51.93  ? 37  TYR A CG    1 
ATOM   313  C  CD1   . TYR A 1 37  ? -28.869 43.921  -40.165 1.00 48.22  ? 37  TYR A CD1   1 
ATOM   314  C  CD2   . TYR A 1 37  ? -27.201 42.557  -41.188 1.00 49.38  ? 37  TYR A CD2   1 
ATOM   315  C  CE1   . TYR A 1 37  ? -28.171 43.887  -38.973 1.00 45.25  ? 37  TYR A CE1   1 
ATOM   316  C  CE2   . TYR A 1 37  ? -26.498 42.517  -39.999 1.00 43.65  ? 37  TYR A CE2   1 
ATOM   317  C  CZ    . TYR A 1 37  ? -26.987 43.184  -38.896 1.00 50.23  ? 37  TYR A CZ    1 
ATOM   318  O  OH    . TYR A 1 37  ? -26.289 43.148  -37.712 1.00 49.82  ? 37  TYR A OH    1 
ATOM   319  N  N     . PHE A 1 38  ? -28.741 40.410  -43.517 1.00 51.58  ? 38  PHE A N     1 
ATOM   320  C  CA    . PHE A 1 38  ? -27.728 39.376  -43.315 1.00 55.09  ? 38  PHE A CA    1 
ATOM   321  C  C     . PHE A 1 38  ? -26.600 39.584  -44.320 1.00 52.01  ? 38  PHE A C     1 
ATOM   322  O  O     . PHE A 1 38  ? -26.721 40.365  -45.265 1.00 52.92  ? 38  PHE A O     1 
ATOM   323  C  CB    . PHE A 1 38  ? -28.325 37.952  -43.369 1.00 49.21  ? 38  PHE A CB    1 
ATOM   324  C  CG    . PHE A 1 38  ? -28.920 37.556  -44.700 1.00 56.31  ? 38  PHE A CG    1 
ATOM   325  C  CD1   . PHE A 1 38  ? -28.117 37.304  -45.803 1.00 54.44  ? 38  PHE A CD1   1 
ATOM   326  C  CD2   . PHE A 1 38  ? -30.289 37.376  -44.827 1.00 56.36  ? 38  PHE A CD2   1 
ATOM   327  C  CE1   . PHE A 1 38  ? -28.670 36.922  -47.013 1.00 58.18  ? 38  PHE A CE1   1 
ATOM   328  C  CE2   . PHE A 1 38  ? -30.847 36.987  -46.033 1.00 49.00  ? 38  PHE A CE2   1 
ATOM   329  C  CZ    . PHE A 1 38  ? -30.036 36.763  -47.128 1.00 54.08  ? 38  PHE A CZ    1 
ATOM   330  N  N     . TYR A 1 39  ? -25.483 38.890  -44.104 1.00 52.71  ? 39  TYR A N     1 
ATOM   331  C  CA    . TYR A 1 39  ? -24.280 39.129  -44.888 1.00 55.73  ? 39  TYR A CA    1 
ATOM   332  C  C     . TYR A 1 39  ? -24.145 38.107  -46.011 1.00 54.94  ? 39  TYR A C     1 
ATOM   333  O  O     . TYR A 1 39  ? -24.570 36.958  -45.881 1.00 56.63  ? 39  TYR A O     1 
ATOM   334  C  CB    . TYR A 1 39  ? -23.038 39.083  -43.996 1.00 50.67  ? 39  TYR A CB    1 
ATOM   335  C  CG    . TYR A 1 39  ? -23.078 40.061  -42.843 1.00 46.66  ? 39  TYR A CG    1 
ATOM   336  C  CD1   . TYR A 1 39  ? -22.830 41.412  -43.043 1.00 44.01  ? 39  TYR A CD1   1 
ATOM   337  C  CD2   . TYR A 1 39  ? -23.365 39.632  -41.554 1.00 46.39  ? 39  TYR A CD2   1 
ATOM   338  C  CE1   . TYR A 1 39  ? -22.865 42.308  -41.993 1.00 43.82  ? 39  TYR A CE1   1 
ATOM   339  C  CE2   . TYR A 1 39  ? -23.402 40.521  -40.497 1.00 43.79  ? 39  TYR A CE2   1 
ATOM   340  C  CZ    . TYR A 1 39  ? -23.151 41.856  -40.722 1.00 43.78  ? 39  TYR A CZ    1 
ATOM   341  O  OH    . TYR A 1 39  ? -23.189 42.741  -39.670 1.00 51.19  ? 39  TYR A OH    1 
ATOM   342  N  N     . ALA A 1 40  ? -23.532 38.536  -47.115 1.00 56.78  ? 40  ALA A N     1 
ATOM   343  C  CA    . ALA A 1 40  ? -23.260 37.657  -48.245 1.00 60.41  ? 40  ALA A CA    1 
ATOM   344  C  C     . ALA A 1 40  ? -21.843 37.889  -48.751 1.00 66.46  ? 40  ALA A C     1 
ATOM   345  O  O     . ALA A 1 40  ? -21.363 39.027  -48.776 1.00 64.47  ? 40  ALA A O     1 
ATOM   346  C  CB    . ALA A 1 40  ? -24.264 37.879  -49.384 1.00 52.19  ? 40  ALA A CB    1 
ATOM   347  N  N     . LEU A 1 41  ? -21.177 36.811  -49.164 1.00 68.58  ? 41  LEU A N     1 
ATOM   348  C  CA    . LEU A 1 41  ? -19.805 36.880  -49.654 1.00 64.44  ? 41  LEU A CA    1 
ATOM   349  C  C     . LEU A 1 41  ? -19.788 36.566  -51.145 1.00 71.39  ? 41  LEU A C     1 
ATOM   350  O  O     . LEU A 1 41  ? -20.212 35.481  -51.559 1.00 74.99  ? 41  LEU A O     1 
ATOM   351  C  CB    . LEU A 1 41  ? -18.904 35.910  -48.890 1.00 64.43  ? 41  LEU A CB    1 
ATOM   352  C  CG    . LEU A 1 41  ? -17.403 35.950  -49.188 1.00 65.75  ? 41  LEU A CG    1 
ATOM   353  C  CD1   . LEU A 1 41  ? -16.919 37.376  -49.421 1.00 68.66  ? 41  LEU A CD1   1 
ATOM   354  C  CD2   . LEU A 1 41  ? -16.633 35.297  -48.053 1.00 58.71  ? 41  LEU A CD2   1 
ATOM   355  N  N     . LEU A 1 42  ? -19.293 37.508  -51.943 1.00 73.11  ? 42  LEU A N     1 
ATOM   356  C  CA    . LEU A 1 42  ? -19.187 37.353  -53.385 1.00 79.68  ? 42  LEU A CA    1 
ATOM   357  C  C     . LEU A 1 42  ? -17.727 37.201  -53.794 1.00 85.06  ? 42  LEU A C     1 
ATOM   358  O  O     . LEU A 1 42  ? -16.813 37.645  -53.094 1.00 93.03  ? 42  LEU A O     1 
ATOM   359  C  CB    . LEU A 1 42  ? -19.798 38.551  -54.119 1.00 82.18  ? 42  LEU A CB    1 
ATOM   360  C  CG    . LEU A 1 42  ? -21.072 39.173  -53.550 1.00 81.96  ? 42  LEU A CG    1 
ATOM   361  C  CD1   . LEU A 1 42  ? -21.489 40.375  -54.385 1.00 85.36  ? 42  LEU A CD1   1 
ATOM   362  C  CD2   . LEU A 1 42  ? -22.190 38.148  -53.490 1.00 84.91  ? 42  LEU A CD2   1 
ATOM   363  N  N     . LYS A 1 43  ? -17.516 36.559  -54.946 1.00 83.77  ? 43  LYS A N     1 
ATOM   364  C  CA    . LYS A 1 43  ? -16.171 36.443  -55.495 1.00 90.12  ? 43  LYS A CA    1 
ATOM   365  C  C     . LYS A 1 43  ? -15.757 37.680  -56.276 1.00 97.59  ? 43  LYS A C     1 
ATOM   366  O  O     . LYS A 1 43  ? -14.556 37.942  -56.409 1.00 100.17 ? 43  LYS A O     1 
ATOM   367  C  CB    . LYS A 1 43  ? -16.062 35.213  -56.399 1.00 92.63  ? 43  LYS A CB    1 
ATOM   368  C  CG    . LYS A 1 43  ? -17.363 34.789  -57.064 1.00 88.57  ? 43  LYS A CG    1 
ATOM   369  C  CD    . LYS A 1 43  ? -17.137 33.578  -57.954 1.00 90.47  ? 43  LYS A CD    1 
ATOM   370  C  CE    . LYS A 1 43  ? -18.434 33.094  -58.575 1.00 94.45  ? 43  LYS A CE    1 
ATOM   371  N  NZ    . LYS A 1 43  ? -18.209 32.079  -59.641 1.00 99.11  ? 43  LYS A NZ    1 
ATOM   372  N  N     . ASP A 1 44  ? -16.720 38.441  -56.790 1.00 102.13 ? 44  ASP A N     1 
ATOM   373  C  CA    . ASP A 1 44  ? -16.459 39.686  -57.494 1.00 106.79 ? 44  ASP A CA    1 
ATOM   374  C  C     . ASP A 1 44  ? -17.389 40.756  -56.942 1.00 107.72 ? 44  ASP A C     1 
ATOM   375  O  O     . ASP A 1 44  ? -18.539 40.471  -56.596 1.00 99.51  ? 44  ASP A O     1 
ATOM   376  C  CB    . ASP A 1 44  ? -16.650 39.512  -59.017 1.00 107.61 ? 44  ASP A CB    1 
ATOM   377  C  CG    . ASP A 1 44  ? -16.681 40.835  -59.772 1.00 112.02 ? 44  ASP A CG    1 
ATOM   378  O  OD1   . ASP A 1 44  ? -17.658 41.601  -59.628 1.00 117.97 ? 44  ASP A OD1   1 
ATOM   379  O  OD2   . ASP A 1 44  ? -15.713 41.113  -60.509 1.00 108.11 ? 44  ASP A OD2   1 
ATOM   380  N  N     . ASP A 1 45  ? -16.881 41.988  -56.855 1.00 126.39 ? 45  ASP A N     1 
ATOM   381  C  CA    . ASP A 1 45  ? -17.671 43.076  -56.288 1.00 116.84 ? 45  ASP A CA    1 
ATOM   382  C  C     . ASP A 1 45  ? -18.841 43.444  -57.195 1.00 110.57 ? 45  ASP A C     1 
ATOM   383  O  O     . ASP A 1 45  ? -19.994 43.493  -56.749 1.00 122.84 ? 45  ASP A O     1 
ATOM   384  C  CB    . ASP A 1 45  ? -16.778 44.291  -56.035 1.00 119.79 ? 45  ASP A CB    1 
ATOM   385  C  CG    . ASP A 1 45  ? -15.380 43.904  -55.590 1.00 128.98 ? 45  ASP A CG    1 
ATOM   386  O  OD1   . ASP A 1 45  ? -15.253 43.211  -54.559 1.00 134.90 ? 45  ASP A OD1   1 
ATOM   387  O  OD2   . ASP A 1 45  ? -14.409 44.286  -56.277 1.00 111.45 ? 45  ASP A OD2   1 
ATOM   388  N  N     . SER A 1 46  ? -18.563 43.690  -58.480 1.00 106.36 ? 46  SER A N     1 
ATOM   389  C  CA    . SER A 1 46  ? -19.602 44.119  -59.411 1.00 105.72 ? 46  SER A CA    1 
ATOM   390  C  C     . SER A 1 46  ? -20.749 43.120  -59.515 1.00 100.68 ? 46  SER A C     1 
ATOM   391  O  O     . SER A 1 46  ? -21.851 43.501  -59.927 1.00 100.96 ? 46  SER A O     1 
ATOM   392  C  CB    . SER A 1 46  ? -18.996 44.360  -60.795 1.00 105.20 ? 46  SER A CB    1 
ATOM   393  O  OG    . SER A 1 46  ? -18.182 43.269  -61.190 1.00 107.23 ? 46  SER A OG    1 
ATOM   394  N  N     . ALA A 1 47  ? -20.520 41.858  -59.138 1.00 99.07  ? 47  ALA A N     1 
ATOM   395  C  CA    . ALA A 1 47  ? -21.591 40.867  -59.131 1.00 92.69  ? 47  ALA A CA    1 
ATOM   396  C  C     . ALA A 1 47  ? -22.779 41.306  -58.287 1.00 95.26  ? 47  ALA A C     1 
ATOM   397  O  O     . ALA A 1 47  ? -23.895 40.814  -58.500 1.00 94.96  ? 47  ALA A O     1 
ATOM   398  C  CB    . ALA A 1 47  ? -21.059 39.525  -58.622 1.00 89.93  ? 47  ALA A CB    1 
ATOM   399  N  N     . ILE A 1 48  ? -22.568 42.233  -57.346 1.00 92.48  ? 48  ILE A N     1 
ATOM   400  C  CA    . ILE A 1 48  ? -23.666 42.736  -56.526 1.00 93.72  ? 48  ILE A CA    1 
ATOM   401  C  C     . ILE A 1 48  ? -24.782 43.302  -57.396 1.00 93.59  ? 48  ILE A C     1 
ATOM   402  O  O     . ILE A 1 48  ? -25.953 43.296  -56.993 1.00 91.97  ? 48  ILE A O     1 
ATOM   403  C  CB    . ILE A 1 48  ? -23.145 43.782  -55.518 1.00 85.57  ? 48  ILE A CB    1 
ATOM   404  C  CG1   . ILE A 1 48  ? -24.224 44.119  -54.488 1.00 82.28  ? 48  ILE A CG1   1 
ATOM   405  C  CG2   . ILE A 1 48  ? -22.695 45.047  -56.231 1.00 81.23  ? 48  ILE A CG2   1 
ATOM   406  C  CD1   . ILE A 1 48  ? -24.339 43.107  -53.376 1.00 79.56  ? 48  ILE A CD1   1 
ATOM   407  N  N     . GLU A 1 49  ? -24.451 43.773  -58.605 1.00 98.38  ? 49  GLU A N     1 
ATOM   408  C  CA    . GLU A 1 49  ? -25.473 44.317  -59.495 1.00 99.62  ? 49  GLU A CA    1 
ATOM   409  C  C     . GLU A 1 49  ? -26.581 43.308  -59.762 1.00 101.55 ? 49  GLU A C     1 
ATOM   410  O  O     . GLU A 1 49  ? -27.740 43.696  -59.950 1.00 100.17 ? 49  GLU A O     1 
ATOM   411  C  CB    . GLU A 1 49  ? -24.845 44.777  -60.814 1.00 107.74 ? 49  GLU A CB    1 
ATOM   412  C  CG    . GLU A 1 49  ? -24.515 43.650  -61.787 1.00 120.83 ? 49  GLU A CG    1 
ATOM   413  C  CD    . GLU A 1 49  ? -24.522 44.099  -63.234 1.00 129.61 ? 49  GLU A CD    1 
ATOM   414  O  OE1   . GLU A 1 49  ? -24.516 45.323  -63.479 1.00 134.28 ? 49  GLU A OE1   1 
ATOM   415  O  OE2   . GLU A 1 49  ? -24.541 43.225  -64.127 1.00 127.66 ? 49  GLU A OE2   1 
ATOM   416  N  N     . GLU A 1 50  ? -26.253 42.015  -59.772 1.00 101.76 ? 50  GLU A N     1 
ATOM   417  C  CA    . GLU A 1 50  ? -27.268 40.984  -59.920 1.00 105.45 ? 50  GLU A CA    1 
ATOM   418  C  C     . GLU A 1 50  ? -27.802 40.498  -58.585 1.00 100.02 ? 50  GLU A C     1 
ATOM   419  O  O     . GLU A 1 50  ? -28.940 40.020  -58.525 1.00 93.91  ? 50  GLU A O     1 
ATOM   420  C  CB    . GLU A 1 50  ? -26.709 39.796  -60.710 1.00 112.04 ? 50  GLU A CB    1 
ATOM   421  C  CG    . GLU A 1 50  ? -26.946 39.888  -62.209 1.00 118.27 ? 50  GLU A CG    1 
ATOM   422  C  CD    . GLU A 1 50  ? -27.418 38.578  -62.805 1.00 125.88 ? 50  GLU A CD    1 
ATOM   423  O  OE1   . GLU A 1 50  ? -26.825 37.527  -62.483 1.00 117.82 ? 50  GLU A OE1   1 
ATOM   424  O  OE2   . GLU A 1 50  ? -28.378 38.599  -63.604 1.00 136.71 ? 50  GLU A OE2   1 
ATOM   425  N  N     . VAL A 1 51  ? -27.014 40.626  -57.515 1.00 97.01  ? 51  VAL A N     1 
ATOM   426  C  CA    . VAL A 1 51  ? -27.466 40.173  -56.203 1.00 95.81  ? 51  VAL A CA    1 
ATOM   427  C  C     . VAL A 1 51  ? -28.672 40.986  -55.750 1.00 98.17  ? 51  VAL A C     1 
ATOM   428  O  O     . VAL A 1 51  ? -29.593 40.461  -55.111 1.00 90.83  ? 51  VAL A O     1 
ATOM   429  C  CB    . VAL A 1 51  ? -26.309 40.239  -55.188 1.00 91.35  ? 51  VAL A CB    1 
ATOM   430  C  CG1   . VAL A 1 51  ? -26.793 39.868  -53.794 1.00 84.70  ? 51  VAL A CG1   1 
ATOM   431  C  CG2   . VAL A 1 51  ? -25.176 39.321  -55.625 1.00 94.62  ? 51  VAL A CG2   1 
ATOM   432  N  N     . LYS A 1 52  ? -28.697 42.275  -56.092 1.00 91.29  ? 52  LYS A N     1 
ATOM   433  C  CA    . LYS A 1 52  ? -29.842 43.119  -55.776 1.00 92.61  ? 52  LYS A CA    1 
ATOM   434  C  C     . LYS A 1 52  ? -31.098 42.720  -56.537 1.00 89.06  ? 52  LYS A C     1 
ATOM   435  O  O     . LYS A 1 52  ? -32.180 43.224  -56.215 1.00 84.49  ? 52  LYS A O     1 
ATOM   436  C  CB    . LYS A 1 52  ? -29.514 44.583  -56.077 1.00 89.50  ? 52  LYS A CB    1 
ATOM   437  C  CG    . LYS A 1 52  ? -28.211 45.073  -55.470 1.00 87.29  ? 52  LYS A CG    1 
ATOM   438  C  CD    . LYS A 1 52  ? -28.165 46.593  -55.411 1.00 91.44  ? 52  LYS A CD    1 
ATOM   439  C  CE    . LYS A 1 52  ? -27.186 47.159  -56.431 1.00 89.12  ? 52  LYS A CE    1 
ATOM   440  N  NZ    . LYS A 1 52  ? -27.708 47.062  -57.824 1.00 91.87  ? 52  LYS A NZ    1 
ATOM   441  N  N     . LYS A 1 53  ? -30.989 41.832  -57.525 1.00 90.99  ? 53  LYS A N     1 
ATOM   442  C  CA    . LYS A 1 53  ? -32.099 41.564  -58.425 1.00 86.11  ? 53  LYS A CA    1 
ATOM   443  C  C     . LYS A 1 53  ? -32.881 40.302  -58.087 1.00 89.49  ? 53  LYS A C     1 
ATOM   444  O  O     . LYS A 1 53  ? -34.035 40.184  -58.517 1.00 90.64  ? 53  LYS A O     1 
ATOM   445  C  CB    . LYS A 1 53  ? -31.597 41.467  -59.871 1.00 94.25  ? 53  LYS A CB    1 
ATOM   446  C  CG    . LYS A 1 53  ? -31.655 42.783  -60.631 1.00 93.66  ? 53  LYS A CG    1 
ATOM   447  C  CD    . LYS A 1 53  ? -31.022 42.658  -62.008 1.00 98.12  ? 53  LYS A CD    1 
ATOM   448  C  CE    . LYS A 1 53  ? -31.799 41.688  -62.885 1.00 98.72  ? 53  LYS A CE    1 
ATOM   449  N  NZ    . LYS A 1 53  ? -31.849 42.134  -64.305 1.00 99.05  ? 53  LYS A NZ    1 
ATOM   450  N  N     . ILE A 1 54  ? -32.300 39.356  -57.345 1.00 88.03  ? 54  ILE A N     1 
ATOM   451  C  CA    . ILE A 1 54  ? -33.035 38.141  -57.013 1.00 88.68  ? 54  ILE A CA    1 
ATOM   452  C  C     . ILE A 1 54  ? -34.198 38.485  -56.095 1.00 82.91  ? 54  ILE A C     1 
ATOM   453  O  O     . ILE A 1 54  ? -34.032 39.162  -55.072 1.00 82.87  ? 54  ILE A O     1 
ATOM   454  C  CB    . ILE A 1 54  ? -32.125 37.077  -56.377 1.00 90.33  ? 54  ILE A CB    1 
ATOM   455  C  CG1   . ILE A 1 54  ? -30.832 36.888  -57.169 1.00 87.04  ? 54  ILE A CG1   1 
ATOM   456  C  CG2   . ILE A 1 54  ? -32.856 35.749  -56.258 1.00 104.16 ? 54  ILE A CG2   1 
ATOM   457  C  CD1   . ILE A 1 54  ? -29.657 37.546  -56.544 1.00 89.22  ? 54  ILE A CD1   1 
ATOM   458  N  N     . THR A 1 55  ? -35.387 38.028  -56.469 1.00 84.71  ? 55  THR A N     1 
ATOM   459  C  CA    . THR A 1 55  ? -36.587 38.177  -55.667 1.00 83.35  ? 55  THR A CA    1 
ATOM   460  C  C     . THR A 1 55  ? -37.103 36.795  -55.296 1.00 82.69  ? 55  THR A C     1 
ATOM   461  O  O     . THR A 1 55  ? -36.626 35.771  -55.792 1.00 81.26  ? 55  THR A O     1 
ATOM   462  C  CB    . THR A 1 55  ? -37.666 38.963  -56.423 1.00 87.37  ? 55  THR A CB    1 
ATOM   463  O  OG1   . THR A 1 55  ? -37.744 38.495  -57.775 1.00 93.74  ? 55  THR A OG1   1 
ATOM   464  C  CG2   . THR A 1 55  ? -37.332 40.447  -56.434 1.00 84.13  ? 55  THR A CG2   1 
ATOM   465  N  N     . ALA A 1 56  ? -38.084 36.777  -54.402 1.00 87.98  ? 56  ALA A N     1 
ATOM   466  C  CA    . ALA A 1 56  ? -38.769 35.539  -54.048 1.00 93.29  ? 56  ALA A CA    1 
ATOM   467  C  C     . ALA A 1 56  ? -40.203 35.881  -53.667 1.00 91.85  ? 56  ALA A C     1 
ATOM   468  O  O     . ALA A 1 56  ? -40.674 36.999  -53.896 1.00 89.10  ? 56  ALA A O     1 
ATOM   469  C  CB    . ALA A 1 56  ? -38.030 34.801  -52.926 1.00 86.00  ? 56  ALA A CB    1 
ATOM   470  N  N     . GLU A 1 57  ? -40.885 34.931  -53.031 1.00 100.46 ? 57  GLU A N     1 
ATOM   471  C  CA    . GLU A 1 57  ? -42.260 35.122  -52.595 1.00 105.60 ? 57  GLU A CA    1 
ATOM   472  C  C     . GLU A 1 57  ? -42.417 34.602  -51.171 1.00 106.50 ? 57  GLU A C     1 
ATOM   473  O  O     . GLU A 1 57  ? -41.747 33.648  -50.758 1.00 106.94 ? 57  GLU A O     1 
ATOM   474  C  CB    . GLU A 1 57  ? -43.237 34.437  -53.594 1.00 110.26 ? 57  GLU A CB    1 
ATOM   475  C  CG    . GLU A 1 57  ? -43.580 32.971  -53.339 1.00 126.53 ? 57  GLU A CG    1 
ATOM   476  C  CD    . GLU A 1 57  ? -44.539 32.755  -52.185 1.00 133.31 ? 57  GLU A CD    1 
ATOM   477  O  OE1   . GLU A 1 57  ? -44.571 31.631  -51.638 1.00 140.80 ? 57  GLU A OE1   1 
ATOM   478  O  OE2   . GLU A 1 57  ? -45.296 33.696  -51.859 1.00 119.29 ? 57  GLU A OE2   1 
ATOM   479  N  N     . ARG A 1 58  ? -43.299 35.260  -50.416 1.00 105.89 ? 58  ARG A N     1 
ATOM   480  C  CA    . ARG A 1 58  ? -43.615 34.844  -49.054 1.00 107.58 ? 58  ARG A CA    1 
ATOM   481  C  C     . ARG A 1 58  ? -45.023 34.265  -48.980 1.00 110.85 ? 58  ARG A C     1 
ATOM   482  O  O     . ARG A 1 58  ? -45.197 33.043  -48.956 1.00 117.50 ? 58  ARG A O     1 
ATOM   483  C  CB    . ARG A 1 58  ? -43.486 36.016  -48.078 1.00 99.62  ? 58  ARG A CB    1 
ATOM   484  C  CG    . ARG A 1 58  ? -42.955 35.615  -46.713 1.00 90.96  ? 58  ARG A CG    1 
ATOM   485  C  CD    . ARG A 1 58  ? -42.387 36.809  -45.975 1.00 83.97  ? 58  ARG A CD    1 
ATOM   486  N  NE    . ARG A 1 58  ? -43.450 37.706  -45.541 1.00 102.37 ? 58  ARG A NE    1 
ATOM   487  C  CZ    . ARG A 1 58  ? -43.294 39.004  -45.328 1.00 83.58  ? 58  ARG A CZ    1 
ATOM   488  N  NH1   . ARG A 1 58  ? -42.121 39.592  -45.482 1.00 81.52  ? 58  ARG A NH1   1 
ATOM   489  N  NH2   . ARG A 1 58  ? -44.340 39.728  -44.939 1.00 87.64  ? 58  ARG A NH2   1 
ATOM   490  N  N     . HIS A 1 59  ? -46.033 35.137  -48.938 1.00 111.44 ? 59  HIS A N     1 
ATOM   491  C  CA    . HIS A 1 59  ? -47.443 34.736  -48.927 1.00 107.37 ? 59  HIS A CA    1 
ATOM   492  C  C     . HIS A 1 59  ? -48.178 35.461  -50.057 1.00 104.14 ? 59  HIS A C     1 
ATOM   493  O  O     . HIS A 1 59  ? -49.107 36.238  -49.838 1.00 100.07 ? 59  HIS A O     1 
ATOM   494  C  CB    . HIS A 1 59  ? -48.091 35.019  -47.569 1.00 102.64 ? 59  HIS A CB    1 
ATOM   495  C  CG    . HIS A 1 59  ? -47.832 33.958  -46.548 1.00 115.12 ? 59  HIS A CG    1 
ATOM   496  N  ND1   . HIS A 1 59  ? -46.818 33.035  -46.682 1.00 123.58 ? 59  HIS A ND1   1 
ATOM   497  C  CD2   . HIS A 1 59  ? -48.450 33.671  -45.378 1.00 118.54 ? 59  HIS A CD2   1 
ATOM   498  C  CE1   . HIS A 1 59  ? -46.822 32.224  -45.640 1.00 120.61 ? 59  HIS A CE1   1 
ATOM   499  N  NE2   . HIS A 1 59  ? -47.802 32.589  -44.833 1.00 122.50 ? 59  HIS A NE2   1 
ATOM   500  N  N     . GLY A 1 60  ? -47.741 35.195  -51.284 1.00 107.63 ? 60  GLY A N     1 
ATOM   501  C  CA    . GLY A 1 60  ? -48.160 35.927  -52.473 1.00 109.63 ? 60  GLY A CA    1 
ATOM   502  C  C     . GLY A 1 60  ? -47.384 37.212  -52.712 1.00 112.94 ? 60  GLY A C     1 
ATOM   503  O  O     . GLY A 1 60  ? -47.157 37.601  -53.860 1.00 111.19 ? 60  GLY A O     1 
ATOM   504  N  N     . THR A 1 61  ? -46.977 37.881  -51.637 1.00 121.11 ? 61  THR A N     1 
ATOM   505  C  CA    . THR A 1 61  ? -46.172 39.086  -51.754 1.00 115.04 ? 61  THR A CA    1 
ATOM   506  C  C     . THR A 1 61  ? -44.789 38.748  -52.298 1.00 111.55 ? 61  THR A C     1 
ATOM   507  O  O     . THR A 1 61  ? -44.248 37.665  -52.056 1.00 110.63 ? 61  THR A O     1 
ATOM   508  C  CB    . THR A 1 61  ? -46.038 39.771  -50.395 1.00 111.98 ? 61  THR A CB    1 
ATOM   509  O  OG1   . THR A 1 61  ? -45.983 38.781  -49.359 1.00 108.70 ? 61  THR A OG1   1 
ATOM   510  C  CG2   . THR A 1 61  ? -47.220 40.694  -50.141 1.00 105.92 ? 61  THR A CG2   1 
ATOM   511  N  N     . VAL A 1 62  ? -44.218 39.686  -53.040 1.00 106.71 ? 62  VAL A N     1 
ATOM   512  C  CA    . VAL A 1 62  ? -42.865 39.549  -53.565 1.00 97.93  ? 62  VAL A CA    1 
ATOM   513  C  C     . VAL A 1 62  ? -41.892 40.140  -52.554 1.00 100.45 ? 62  VAL A C     1 
ATOM   514  O  O     . VAL A 1 62  ? -42.188 41.141  -51.889 1.00 98.66  ? 62  VAL A O     1 
ATOM   515  C  CB    . VAL A 1 62  ? -42.746 40.208  -54.958 1.00 91.78  ? 62  VAL A CB    1 
ATOM   516  C  CG1   . VAL A 1 62  ? -42.439 41.703  -54.861 1.00 84.44  ? 62  VAL A CG1   1 
ATOM   517  C  CG2   . VAL A 1 62  ? -41.702 39.487  -55.810 1.00 97.81  ? 62  VAL A CG2   1 
ATOM   518  N  N     . VAL A 1 63  ? -40.744 39.486  -52.392 1.00 93.95  ? 63  VAL A N     1 
ATOM   519  C  CA    . VAL A 1 63  ? -39.712 39.932  -51.464 1.00 85.05  ? 63  VAL A CA    1 
ATOM   520  C  C     . VAL A 1 63  ? -38.474 40.267  -52.277 1.00 82.41  ? 63  VAL A C     1 
ATOM   521  O  O     . VAL A 1 63  ? -38.014 39.447  -53.082 1.00 78.90  ? 63  VAL A O     1 
ATOM   522  C  CB    . VAL A 1 63  ? -39.395 38.875  -50.390 1.00 83.86  ? 63  VAL A CB    1 
ATOM   523  C  CG1   . VAL A 1 63  ? -40.489 38.854  -49.351 1.00 81.13  ? 63  VAL A CG1   1 
ATOM   524  C  CG2   . VAL A 1 63  ? -39.209 37.509  -50.999 1.00 88.14  ? 63  VAL A CG2   1 
ATOM   525  N  N     . THR A 1 64  ? -37.956 41.478  -52.073 1.00 80.19  ? 64  THR A N     1 
ATOM   526  C  CA    . THR A 1 64  ? -36.837 42.021  -52.823 1.00 80.93  ? 64  THR A CA    1 
ATOM   527  C  C     . THR A 1 64  ? -35.746 42.446  -51.851 1.00 74.42  ? 64  THR A C     1 
ATOM   528  O  O     . THR A 1 64  ? -36.002 42.710  -50.675 1.00 74.94  ? 64  THR A O     1 
ATOM   529  C  CB    . THR A 1 64  ? -37.261 43.229  -53.682 1.00 76.47  ? 64  THR A CB    1 
ATOM   530  O  OG1   . THR A 1 64  ? -37.245 44.414  -52.874 1.00 74.77  ? 64  THR A OG1   1 
ATOM   531  C  CG2   . THR A 1 64  ? -38.660 43.030  -54.234 1.00 78.55  ? 64  THR A CG2   1 
ATOM   532  N  N     . VAL A 1 65  ? -34.518 42.516  -52.358 1.00 73.43  ? 65  VAL A N     1 
ATOM   533  C  CA    . VAL A 1 65  ? -33.412 43.068  -51.584 1.00 76.21  ? 65  VAL A CA    1 
ATOM   534  C  C     . VAL A 1 65  ? -33.608 44.580  -51.513 1.00 75.74  ? 65  VAL A C     1 
ATOM   535  O  O     . VAL A 1 65  ? -33.541 45.269  -52.534 1.00 84.13  ? 65  VAL A O     1 
ATOM   536  C  CB    . VAL A 1 65  ? -32.057 42.707  -52.201 1.00 75.26  ? 65  VAL A CB    1 
ATOM   537  C  CG1   . VAL A 1 65  ? -30.921 43.233  -51.338 1.00 76.52  ? 65  VAL A CG1   1 
ATOM   538  C  CG2   . VAL A 1 65  ? -31.948 41.201  -52.383 1.00 74.74  ? 65  VAL A CG2   1 
ATOM   539  N  N     . LYS A 1 66  ? -33.870 45.098  -50.312 1.00 66.60  ? 66  LYS A N     1 
ATOM   540  C  CA    . LYS A 1 66  ? -34.153 46.518  -50.140 1.00 63.96  ? 66  LYS A CA    1 
ATOM   541  C  C     . LYS A 1 66  ? -32.942 47.365  -50.510 1.00 71.75  ? 66  LYS A C     1 
ATOM   542  O  O     . LYS A 1 66  ? -32.981 48.116  -51.490 1.00 72.95  ? 66  LYS A O     1 
ATOM   543  C  CB    . LYS A 1 66  ? -34.591 46.806  -48.702 1.00 65.52  ? 66  LYS A CB    1 
ATOM   544  C  CG    . LYS A 1 66  ? -34.715 48.287  -48.376 1.00 73.83  ? 66  LYS A CG    1 
ATOM   545  C  CD    . LYS A 1 66  ? -35.466 48.510  -47.072 1.00 72.65  ? 66  LYS A CD    1 
ATOM   546  C  CE    . LYS A 1 66  ? -34.798 49.585  -46.227 1.00 81.32  ? 66  LYS A CE    1 
ATOM   547  N  NZ    . LYS A 1 66  ? -35.141 49.461  -44.783 1.00 81.82  ? 66  LYS A NZ    1 
ATOM   548  N  N     . ARG A 1 67  ? -31.860 47.249  -49.742 1.00 71.16  ? 67  ARG A N     1 
ATOM   549  C  CA    . ARG A 1 67  ? -30.641 47.990  -50.029 1.00 70.10  ? 67  ARG A CA    1 
ATOM   550  C  C     . ARG A 1 67  ? -29.441 47.142  -49.636 1.00 71.47  ? 67  ARG A C     1 
ATOM   551  O  O     . ARG A 1 67  ? -29.530 46.286  -48.752 1.00 69.96  ? 67  ARG A O     1 
ATOM   552  C  CB    . ARG A 1 67  ? -30.608 49.338  -49.296 1.00 68.45  ? 67  ARG A CB    1 
ATOM   553  C  CG    . ARG A 1 67  ? -30.670 49.226  -47.782 1.00 71.65  ? 67  ARG A CG    1 
ATOM   554  C  CD    . ARG A 1 67  ? -30.962 50.569  -47.133 1.00 76.91  ? 67  ARG A CD    1 
ATOM   555  N  NE    . ARG A 1 67  ? -30.314 50.700  -45.833 1.00 75.20  ? 67  ARG A NE    1 
ATOM   556  C  CZ    . ARG A 1 67  ? -29.041 51.030  -45.660 1.00 80.31  ? 67  ARG A CZ    1 
ATOM   557  N  NH1   . ARG A 1 67  ? -28.244 51.275  -46.687 1.00 78.53  ? 67  ARG A NH1   1 
ATOM   558  N  NH2   . ARG A 1 67  ? -28.556 51.118  -44.425 1.00 74.92  ? 67  ARG A NH2   1 
ATOM   559  N  N     . VAL A 1 68  ? -28.318 47.386  -50.309 1.00 70.31  ? 68  VAL A N     1 
ATOM   560  C  CA    . VAL A 1 68  ? -27.077 46.677  -50.039 1.00 71.62  ? 68  VAL A CA    1 
ATOM   561  C  C     . VAL A 1 68  ? -26.039 47.680  -49.554 1.00 74.29  ? 68  VAL A C     1 
ATOM   562  O  O     . VAL A 1 68  ? -26.161 48.890  -49.757 1.00 71.78  ? 68  VAL A O     1 
ATOM   563  C  CB    . VAL A 1 68  ? -26.559 45.909  -51.272 1.00 73.60  ? 68  VAL A CB    1 
ATOM   564  C  CG1   . VAL A 1 68  ? -27.647 45.005  -51.829 1.00 71.32  ? 68  VAL A CG1   1 
ATOM   565  C  CG2   . VAL A 1 68  ? -26.066 46.879  -52.334 1.00 77.61  ? 68  VAL A CG2   1 
ATOM   566  N  N     . GLU A 1 69  ? -25.006 47.157  -48.895 1.00 69.26  ? 69  GLU A N     1 
ATOM   567  C  CA    . GLU A 1 69  ? -23.961 48.014  -48.351 1.00 68.06  ? 69  GLU A CA    1 
ATOM   568  C  C     . GLU A 1 69  ? -22.677 47.210  -48.207 1.00 73.22  ? 69  GLU A C     1 
ATOM   569  O  O     . GLU A 1 69  ? -22.680 46.142  -47.592 1.00 75.09  ? 69  GLU A O     1 
ATOM   570  C  CB    . GLU A 1 69  ? -24.393 48.600  -47.002 1.00 64.83  ? 69  GLU A CB    1 
ATOM   571  C  CG    . GLU A 1 69  ? -23.277 49.243  -46.200 1.00 77.94  ? 69  GLU A CG    1 
ATOM   572  C  CD    . GLU A 1 69  ? -23.803 50.052  -45.030 1.00 81.00  ? 69  GLU A CD    1 
ATOM   573  O  OE1   . GLU A 1 69  ? -24.532 51.038  -45.270 1.00 87.99  ? 69  GLU A OE1   1 
ATOM   574  O  OE2   . GLU A 1 69  ? -23.492 49.701  -43.873 1.00 77.58  ? 69  GLU A OE2   1 
ATOM   575  N  N     . LYS A 1 70  ? -21.587 47.722  -48.771 1.00 69.15  ? 70  LYS A N     1 
ATOM   576  C  CA    . LYS A 1 70  ? -20.297 47.051  -48.669 1.00 65.58  ? 70  LYS A CA    1 
ATOM   577  C  C     . LYS A 1 70  ? -19.675 47.325  -47.305 1.00 67.23  ? 70  LYS A C     1 
ATOM   578  O  O     . LYS A 1 70  ? -19.599 48.479  -46.871 1.00 72.91  ? 70  LYS A O     1 
ATOM   579  C  CB    . LYS A 1 70  ? -19.370 47.524  -49.787 1.00 75.46  ? 70  LYS A CB    1 
ATOM   580  C  CG    . LYS A 1 70  ? -18.088 46.727  -49.920 1.00 78.58  ? 70  LYS A CG    1 
ATOM   581  C  CD    . LYS A 1 70  ? -16.906 47.649  -50.166 1.00 81.14  ? 70  LYS A CD    1 
ATOM   582  C  CE    . LYS A 1 70  ? -16.709 47.905  -51.650 1.00 84.18  ? 70  LYS A CE    1 
ATOM   583  N  NZ    . LYS A 1 70  ? -16.057 49.218  -51.913 1.00 91.42  ? 70  LYS A NZ    1 
ATOM   584  N  N     . VAL A 1 71  ? -19.226 46.267  -46.627 1.00 59.54  ? 71  VAL A N     1 
ATOM   585  C  CA    . VAL A 1 71  ? -18.715 46.380  -45.267 1.00 63.80  ? 71  VAL A CA    1 
ATOM   586  C  C     . VAL A 1 71  ? -17.455 45.530  -45.147 1.00 68.22  ? 71  VAL A C     1 
ATOM   587  O  O     . VAL A 1 71  ? -17.286 44.534  -45.856 1.00 72.24  ? 71  VAL A O     1 
ATOM   588  C  CB    . VAL A 1 71  ? -19.805 45.970  -44.241 1.00 65.31  ? 71  VAL A CB    1 
ATOM   589  C  CG1   . VAL A 1 71  ? -19.211 45.427  -42.953 1.00 72.11  ? 71  VAL A CG1   1 
ATOM   590  C  CG2   . VAL A 1 71  ? -20.727 47.147  -43.948 1.00 67.62  ? 71  VAL A CG2   1 
ATOM   591  N  N     . GLN A 1 72  ? -16.540 45.957  -44.278 1.00 57.03  ? 72  GLN A N     1 
ATOM   592  C  CA    . GLN A 1 72  ? -15.312 45.225  -43.992 1.00 56.05  ? 72  GLN A CA    1 
ATOM   593  C  C     . GLN A 1 72  ? -15.422 44.583  -42.614 1.00 56.72  ? 72  GLN A C     1 
ATOM   594  O  O     . GLN A 1 72  ? -15.642 45.280  -41.617 1.00 53.57  ? 72  GLN A O     1 
ATOM   595  C  CB    . GLN A 1 72  ? -14.099 46.152  -44.058 1.00 60.72  ? 72  GLN A CB    1 
ATOM   596  C  CG    . GLN A 1 72  ? -12.809 45.459  -44.456 1.00 76.08  ? 72  GLN A CG    1 
ATOM   597  C  CD    . GLN A 1 72  ? -11.592 46.336  -44.238 1.00 78.77  ? 72  GLN A CD    1 
ATOM   598  O  OE1   . GLN A 1 72  ? -11.714 47.516  -43.910 1.00 86.79  ? 72  GLN A OE1   1 
ATOM   599  N  NE2   . GLN A 1 72  ? -10.410 45.756  -44.394 1.00 85.01  ? 72  GLN A NE2   1 
ATOM   600  N  N     . LYS A 1 73  ? -15.262 43.263  -42.558 1.00 52.91  ? 73  LYS A N     1 
ATOM   601  C  CA    . LYS A 1 73  ? -15.347 42.525  -41.304 1.00 58.60  ? 73  LYS A CA    1 
ATOM   602  C  C     . LYS A 1 73  ? -14.124 41.625  -41.171 1.00 64.03  ? 73  LYS A C     1 
ATOM   603  O  O     . LYS A 1 73  ? -13.227 41.633  -42.015 1.00 70.19  ? 73  LYS A O     1 
ATOM   604  C  CB    . LYS A 1 73  ? -16.649 41.715  -41.223 1.00 56.30  ? 73  LYS A CB    1 
ATOM   605  C  CG    . LYS A 1 73  ? -17.911 42.553  -41.393 1.00 55.84  ? 73  LYS A CG    1 
ATOM   606  C  CD    . LYS A 1 73  ? -19.180 41.752  -41.129 1.00 47.63  ? 73  LYS A CD    1 
ATOM   607  C  CE    . LYS A 1 73  ? -19.432 41.584  -39.638 1.00 39.07  ? 73  LYS A CE    1 
ATOM   608  N  NZ    . LYS A 1 73  ? -19.821 42.869  -38.996 1.00 51.02  ? 73  LYS A NZ    1 
ATOM   609  N  N     . LYS A 1 74  ? -14.082 40.848  -40.090 1.00 60.72  ? 74  LYS A N     1 
ATOM   610  C  CA    . LYS A 1 74  ? -12.973 39.939  -39.819 1.00 60.85  ? 74  LYS A CA    1 
ATOM   611  C  C     . LYS A 1 74  ? -13.509 38.513  -39.791 1.00 66.78  ? 74  LYS A C     1 
ATOM   612  O  O     . LYS A 1 74  ? -14.239 38.135  -38.869 1.00 70.33  ? 74  LYS A O     1 
ATOM   613  C  CB    . LYS A 1 74  ? -12.280 40.284  -38.502 1.00 65.85  ? 74  LYS A CB    1 
ATOM   614  C  CG    . LYS A 1 74  ? -11.797 41.722  -38.405 1.00 70.96  ? 74  LYS A CG    1 
ATOM   615  C  CD    . LYS A 1 74  ? -11.932 42.251  -36.984 1.00 76.84  ? 74  LYS A CD    1 
ATOM   616  C  CE    . LYS A 1 74  ? -10.817 41.724  -36.093 1.00 82.18  ? 74  LYS A CE    1 
ATOM   617  N  NZ    . LYS A 1 74  ? -11.012 42.101  -34.664 1.00 71.40  ? 74  LYS A NZ    1 
ATOM   618  N  N     . PHE A 1 75  ? -13.146 37.727  -40.798 1.00 68.46  ? 75  PHE A N     1 
ATOM   619  C  CA    . PHE A 1 75  ? -13.460 36.306  -40.842 1.00 63.99  ? 75  PHE A CA    1 
ATOM   620  C  C     . PHE A 1 75  ? -12.175 35.520  -40.641 1.00 76.49  ? 75  PHE A C     1 
ATOM   621  O  O     . PHE A 1 75  ? -11.154 35.839  -41.258 1.00 87.72  ? 75  PHE A O     1 
ATOM   622  C  CB    . PHE A 1 75  ? -14.120 35.924  -42.167 1.00 63.10  ? 75  PHE A CB    1 
ATOM   623  C  CG    . PHE A 1 75  ? -15.005 34.715  -42.070 1.00 68.81  ? 75  PHE A CG    1 
ATOM   624  C  CD1   . PHE A 1 75  ? -15.895 34.573  -41.017 1.00 61.50  ? 75  PHE A CD1   1 
ATOM   625  C  CD2   . PHE A 1 75  ? -14.940 33.717  -43.026 1.00 66.72  ? 75  PHE A CD2   1 
ATOM   626  C  CE1   . PHE A 1 75  ? -16.709 33.461  -40.926 1.00 60.36  ? 75  PHE A CE1   1 
ATOM   627  C  CE2   . PHE A 1 75  ? -15.751 32.602  -42.940 1.00 66.33  ? 75  PHE A CE2   1 
ATOM   628  C  CZ    . PHE A 1 75  ? -16.637 32.474  -41.889 1.00 60.26  ? 75  PHE A CZ    1 
ATOM   629  N  N     . LEU A 1 76  ? -12.239 34.491  -39.791 1.00 70.12  ? 76  LEU A N     1 
ATOM   630  C  CA    . LEU A 1 76  ? -11.078 33.715  -39.357 1.00 80.85  ? 76  LEU A CA    1 
ATOM   631  C  C     . LEU A 1 76  ? -9.885  34.614  -39.040 1.00 83.32  ? 76  LEU A C     1 
ATOM   632  O  O     . LEU A 1 76  ? -8.744  34.287  -39.379 1.00 83.87  ? 76  LEU A O     1 
ATOM   633  C  CB    . LEU A 1 76  ? -10.706 32.647  -40.398 1.00 84.39  ? 76  LEU A CB    1 
ATOM   634  C  CG    . LEU A 1 76  ? -10.473 32.936  -41.888 1.00 104.95 ? 76  LEU A CG    1 
ATOM   635  C  CD1   . LEU A 1 76  ? -8.985  33.002  -42.233 1.00 87.53  ? 76  LEU A CD1   1 
ATOM   636  C  CD2   . LEU A 1 76  ? -11.184 31.905  -42.754 1.00 91.44  ? 76  LEU A CD2   1 
ATOM   637  N  N     . GLY A 1 77  ? -10.144 35.745  -38.378 1.00 88.55  ? 77  GLY A N     1 
ATOM   638  C  CA    . GLY A 1 77  ? -9.106  36.673  -37.983 1.00 87.91  ? 77  GLY A CA    1 
ATOM   639  C  C     . GLY A 1 77  ? -8.618  37.610  -39.066 1.00 86.76  ? 77  GLY A C     1 
ATOM   640  O  O     . GLY A 1 77  ? -8.022  38.645  -38.747 1.00 93.83  ? 77  GLY A O     1 
ATOM   641  N  N     . ARG A 1 78  ? -8.853  37.290  -40.333 1.00 82.61  ? 78  ARG A N     1 
ATOM   642  C  CA    . ARG A 1 78  ? -8.400  38.015  -41.511 1.00 82.78  ? 78  ARG A CA    1 
ATOM   643  C  C     . ARG A 1 78  ? -9.466  39.002  -41.984 1.00 83.62  ? 78  ARG A C     1 
ATOM   644  O  O     . ARG A 1 78  ? -10.661 38.695  -41.941 1.00 76.40  ? 78  ARG A O     1 
ATOM   645  C  CB    . ARG A 1 78  ? -8.072  37.044  -42.640 1.00 86.48  ? 78  ARG A CB    1 
ATOM   646  C  CG    . ARG A 1 78  ? -6.682  36.438  -42.551 1.00 91.30  ? 78  ARG A CG    1 
ATOM   647  C  CD    . ARG A 1 78  ? -5.634  37.419  -43.057 1.00 91.96  ? 78  ARG A CD    1 
ATOM   648  N  NE    . ARG A 1 78  ? -4.358  37.338  -42.351 1.00 103.32 ? 78  ARG A NE    1 
ATOM   649  C  CZ    . ARG A 1 78  ? -3.575  36.266  -42.307 1.00 95.75  ? 78  ARG A CZ    1 
ATOM   650  N  NH1   . ARG A 1 78  ? -3.891  35.146  -42.937 1.00 95.36  ? 78  ARG A NH1   1 
ATOM   651  N  NH2   . ARG A 1 78  ? -2.435  36.326  -41.625 1.00 89.83  ? 78  ARG A NH2   1 
ATOM   652  N  N     . PRO A 1 79  ? -9.052  40.187  -42.433 1.00 85.17  ? 79  PRO A N     1 
ATOM   653  C  CA    . PRO A 1 79  ? -10.019 41.142  -42.987 1.00 77.83  ? 79  PRO A CA    1 
ATOM   654  C  C     . PRO A 1 79  ? -10.625 40.623  -44.281 1.00 72.92  ? 79  PRO A C     1 
ATOM   655  O  O     . PRO A 1 79  ? -9.950  39.994  -45.098 1.00 76.57  ? 79  PRO A O     1 
ATOM   656  C  CB    . PRO A 1 79  ? -9.179  42.403  -43.229 1.00 80.18  ? 79  PRO A CB    1 
ATOM   657  C  CG    . PRO A 1 79  ? -7.959  42.228  -42.376 1.00 80.74  ? 79  PRO A CG    1 
ATOM   658  C  CD    . PRO A 1 79  ? -7.696  40.755  -42.362 1.00 82.14  ? 79  PRO A CD    1 
ATOM   659  N  N     . VAL A 1 80  ? -11.916 40.898  -44.462 1.00 67.73  ? 80  VAL A N     1 
ATOM   660  C  CA    . VAL A 1 80  ? -12.648 40.437  -45.633 1.00 69.53  ? 80  VAL A CA    1 
ATOM   661  C  C     . VAL A 1 80  ? -13.750 41.440  -45.947 1.00 70.07  ? 80  VAL A C     1 
ATOM   662  O  O     . VAL A 1 80  ? -14.234 42.162  -45.069 1.00 63.10  ? 80  VAL A O     1 
ATOM   663  C  CB    . VAL A 1 80  ? -13.220 39.014  -45.421 1.00 69.23  ? 80  VAL A CB    1 
ATOM   664  C  CG1   . VAL A 1 80  ? -14.488 39.058  -44.578 1.00 57.22  ? 80  VAL A CG1   1 
ATOM   665  C  CG2   . VAL A 1 80  ? -13.475 38.334  -46.759 1.00 69.25  ? 80  VAL A CG2   1 
ATOM   666  N  N     . GLU A 1 81  ? -14.129 41.493  -47.221 1.00 70.95  ? 81  GLU A N     1 
ATOM   667  C  CA    . GLU A 1 81  ? -15.176 42.383  -47.703 1.00 68.02  ? 81  GLU A CA    1 
ATOM   668  C  C     . GLU A 1 81  ? -16.461 41.584  -47.876 1.00 65.69  ? 81  GLU A C     1 
ATOM   669  O  O     . GLU A 1 81  ? -16.500 40.624  -48.653 1.00 66.23  ? 81  GLU A O     1 
ATOM   670  C  CB    . GLU A 1 81  ? -14.768 43.040  -49.021 1.00 73.82  ? 81  GLU A CB    1 
ATOM   671  C  CG    . GLU A 1 81  ? -15.165 44.502  -49.132 1.00 80.21  ? 81  GLU A CG    1 
ATOM   672  C  CD    . GLU A 1 81  ? -14.586 45.171  -50.363 1.00 94.76  ? 81  GLU A CD    1 
ATOM   673  O  OE1   . GLU A 1 81  ? -14.993 44.808  -51.487 1.00 88.15  ? 81  GLU A OE1   1 
ATOM   674  O  OE2   . GLU A 1 81  ? -13.727 46.065  -50.207 1.00 105.05 ? 81  GLU A OE2   1 
ATOM   675  N  N     . VAL A 1 82  ? -17.504 41.981  -47.153 1.00 64.51  ? 82  VAL A N     1 
ATOM   676  C  CA    . VAL A 1 82  ? -18.795 41.313  -47.191 1.00 68.27  ? 82  VAL A CA    1 
ATOM   677  C  C     . VAL A 1 82  ? -19.844 42.330  -47.627 1.00 67.69  ? 82  VAL A C     1 
ATOM   678  O  O     . VAL A 1 82  ? -19.616 43.544  -47.612 1.00 64.50  ? 82  VAL A O     1 
ATOM   679  C  CB    . VAL A 1 82  ? -19.152 40.689  -45.825 1.00 60.39  ? 82  VAL A CB    1 
ATOM   680  C  CG1   . VAL A 1 82  ? -19.827 41.713  -44.920 1.00 73.92  ? 82  VAL A CG1   1 
ATOM   681  C  CG2   . VAL A 1 82  ? -20.013 39.453  -46.001 1.00 68.05  ? 82  VAL A CG2   1 
ATOM   682  N  N     . TRP A 1 83  ? -21.004 41.822  -48.035 1.00 61.93  ? 83  TRP A N     1 
ATOM   683  C  CA    . TRP A 1 83  ? -22.107 42.663  -48.478 1.00 67.62  ? 83  TRP A CA    1 
ATOM   684  C  C     . TRP A 1 83  ? -23.261 42.496  -47.498 1.00 63.99  ? 83  TRP A C     1 
ATOM   685  O  O     . TRP A 1 83  ? -23.865 41.420  -47.418 1.00 59.43  ? 83  TRP A O     1 
ATOM   686  C  CB    . TRP A 1 83  ? -22.531 42.306  -49.899 1.00 67.69  ? 83  TRP A CB    1 
ATOM   687  C  CG    . TRP A 1 83  ? -21.651 42.911  -50.947 1.00 73.84  ? 83  TRP A CG    1 
ATOM   688  C  CD1   . TRP A 1 83  ? -20.639 42.296  -51.622 1.00 78.20  ? 83  TRP A CD1   1 
ATOM   689  C  CD2   . TRP A 1 83  ? -21.701 44.256  -51.436 1.00 75.65  ? 83  TRP A CD2   1 
ATOM   690  N  NE1   . TRP A 1 83  ? -20.057 43.172  -52.505 1.00 79.57  ? 83  TRP A NE1   1 
ATOM   691  C  CE2   . TRP A 1 83  ? -20.691 44.383  -52.411 1.00 77.06  ? 83  TRP A CE2   1 
ATOM   692  C  CE3   . TRP A 1 83  ? -22.503 45.364  -51.148 1.00 75.11  ? 83  TRP A CE3   1 
ATOM   693  C  CZ2   . TRP A 1 83  ? -20.461 45.573  -53.097 1.00 78.25  ? 83  TRP A CZ2   1 
ATOM   694  C  CZ3   . TRP A 1 83  ? -22.273 46.545  -51.830 1.00 76.25  ? 83  TRP A CZ3   1 
ATOM   695  C  CH2   . TRP A 1 83  ? -21.261 46.639  -52.793 1.00 77.07  ? 83  TRP A CH2   1 
ATOM   696  N  N     . LYS A 1 84  ? -23.528 43.548  -46.729 1.00 60.81  ? 84  LYS A N     1 
ATOM   697  C  CA    . LYS A 1 84  ? -24.721 43.622  -45.901 1.00 63.20  ? 84  LYS A CA    1 
ATOM   698  C  C     . LYS A 1 84  ? -25.937 43.788  -46.802 1.00 61.13  ? 84  LYS A C     1 
ATOM   699  O  O     . LYS A 1 84  ? -26.028 44.766  -47.553 1.00 58.96  ? 84  LYS A O     1 
ATOM   700  C  CB    . LYS A 1 84  ? -24.600 44.801  -44.937 1.00 61.29  ? 84  LYS A CB    1 
ATOM   701  C  CG    . LYS A 1 84  ? -25.253 44.617  -43.582 1.00 60.44  ? 84  LYS A CG    1 
ATOM   702  C  CD    . LYS A 1 84  ? -24.859 45.756  -42.650 1.00 53.01  ? 84  LYS A CD    1 
ATOM   703  C  CE    . LYS A 1 84  ? -25.579 45.667  -41.316 1.00 56.60  ? 84  LYS A CE    1 
ATOM   704  N  NZ    . LYS A 1 84  ? -25.208 46.786  -40.407 1.00 52.38  ? 84  LYS A NZ    1 
ATOM   705  N  N     . LEU A 1 85  ? -26.860 42.830  -46.746 1.00 59.99  ? 85  LEU A N     1 
ATOM   706  C  CA    . LEU A 1 85  ? -28.102 42.871  -47.504 1.00 59.26  ? 85  LEU A CA    1 
ATOM   707  C  C     . LEU A 1 85  ? -29.231 43.173  -46.532 1.00 57.36  ? 85  LEU A C     1 
ATOM   708  O  O     . LEU A 1 85  ? -29.485 42.383  -45.612 1.00 55.90  ? 85  LEU A O     1 
ATOM   709  C  CB    . LEU A 1 85  ? -28.356 41.546  -48.223 1.00 57.59  ? 85  LEU A CB    1 
ATOM   710  C  CG    . LEU A 1 85  ? -27.246 40.971  -49.107 1.00 64.44  ? 85  LEU A CG    1 
ATOM   711  C  CD1   . LEU A 1 85  ? -27.820 39.943  -50.068 1.00 62.06  ? 85  LEU A CD1   1 
ATOM   712  C  CD2   . LEU A 1 85  ? -26.524 42.070  -49.870 1.00 64.67  ? 85  LEU A CD2   1 
ATOM   713  N  N     . TYR A 1 86  ? -29.885 44.316  -46.728 1.00 61.23  ? 86  TYR A N     1 
ATOM   714  C  CA    . TYR A 1 86  ? -31.019 44.735  -45.919 1.00 59.61  ? 86  TYR A CA    1 
ATOM   715  C  C     . TYR A 1 86  ? -32.324 44.282  -46.562 1.00 56.71  ? 86  TYR A C     1 
ATOM   716  O  O     . TYR A 1 86  ? -32.411 44.102  -47.780 1.00 57.60  ? 86  TYR A O     1 
ATOM   717  C  CB    . TYR A 1 86  ? -31.035 46.256  -45.750 1.00 59.87  ? 86  TYR A CB    1 
ATOM   718  C  CG    . TYR A 1 86  ? -29.888 46.819  -44.940 1.00 60.46  ? 86  TYR A CG    1 
ATOM   719  C  CD1   . TYR A 1 86  ? -29.976 46.930  -43.558 1.00 59.67  ? 86  TYR A CD1   1 
ATOM   720  C  CD2   . TYR A 1 86  ? -28.722 47.254  -45.558 1.00 63.96  ? 86  TYR A CD2   1 
ATOM   721  C  CE1   . TYR A 1 86  ? -28.933 47.452  -42.814 1.00 60.89  ? 86  TYR A CE1   1 
ATOM   722  C  CE2   . TYR A 1 86  ? -27.673 47.777  -44.821 1.00 63.71  ? 86  TYR A CE2   1 
ATOM   723  C  CZ    . TYR A 1 86  ? -27.784 47.873  -43.450 1.00 62.42  ? 86  TYR A CZ    1 
ATOM   724  O  OH    . TYR A 1 86  ? -26.745 48.393  -42.712 1.00 60.02  ? 86  TYR A OH    1 
ATOM   725  N  N     . PHE A 1 87  ? -33.347 44.107  -45.729 1.00 53.45  ? 87  PHE A N     1 
ATOM   726  C  CA    . PHE A 1 87  ? -34.656 43.675  -46.195 1.00 59.88  ? 87  PHE A CA    1 
ATOM   727  C  C     . PHE A 1 87  ? -35.731 44.500  -45.505 1.00 59.70  ? 87  PHE A C     1 
ATOM   728  O  O     . PHE A 1 87  ? -35.462 45.264  -44.575 1.00 62.26  ? 87  PHE A O     1 
ATOM   729  C  CB    . PHE A 1 87  ? -34.871 42.177  -45.946 1.00 55.29  ? 87  PHE A CB    1 
ATOM   730  C  CG    . PHE A 1 87  ? -33.838 41.308  -46.596 1.00 60.13  ? 87  PHE A CG    1 
ATOM   731  C  CD1   . PHE A 1 87  ? -34.007 40.864  -47.897 1.00 61.60  ? 87  PHE A CD1   1 
ATOM   732  C  CD2   . PHE A 1 87  ? -32.687 40.953  -45.915 1.00 56.36  ? 87  PHE A CD2   1 
ATOM   733  C  CE1   . PHE A 1 87  ? -33.051 40.072  -48.502 1.00 63.98  ? 87  PHE A CE1   1 
ATOM   734  C  CE2   . PHE A 1 87  ? -31.727 40.164  -46.514 1.00 53.64  ? 87  PHE A CE2   1 
ATOM   735  C  CZ    . PHE A 1 87  ? -31.909 39.721  -47.809 1.00 58.97  ? 87  PHE A CZ    1 
ATOM   736  N  N     . THR A 1 88  ? -36.967 44.339  -45.977 1.00 64.13  ? 88  THR A N     1 
ATOM   737  C  CA    . THR A 1 88  ? -38.083 45.081  -45.402 1.00 53.88  ? 88  THR A CA    1 
ATOM   738  C  C     . THR A 1 88  ? -38.534 44.469  -44.081 1.00 55.90  ? 88  THR A C     1 
ATOM   739  O  O     . THR A 1 88  ? -38.681 45.176  -43.079 1.00 51.24  ? 88  THR A O     1 
ATOM   740  C  CB    . THR A 1 88  ? -39.246 45.130  -46.394 1.00 58.75  ? 88  THR A CB    1 
ATOM   741  O  OG1   . THR A 1 88  ? -38.787 45.664  -47.642 1.00 61.73  ? 88  THR A OG1   1 
ATOM   742  C  CG2   . THR A 1 88  ? -40.372 45.999  -45.854 1.00 59.30  ? 88  THR A CG2   1 
ATOM   743  N  N     . HIS A 1 89  ? -38.747 43.157  -44.061 1.00 57.35  ? 89  HIS A N     1 
ATOM   744  C  CA    . HIS A 1 89  ? -39.270 42.450  -42.905 1.00 56.77  ? 89  HIS A CA    1 
ATOM   745  C  C     . HIS A 1 89  ? -38.381 41.257  -42.592 1.00 55.92  ? 89  HIS A C     1 
ATOM   746  O  O     . HIS A 1 89  ? -37.829 40.638  -43.507 1.00 57.30  ? 89  HIS A O     1 
ATOM   747  C  CB    . HIS A 1 89  ? -40.708 41.975  -43.167 1.00 56.33  ? 89  HIS A CB    1 
ATOM   748  C  CG    . HIS A 1 89  ? -41.515 41.768  -41.925 1.00 54.61  ? 89  HIS A CG    1 
ATOM   749  N  ND1   . HIS A 1 89  ? -41.564 40.560  -41.262 1.00 54.29  ? 89  HIS A ND1   1 
ATOM   750  C  CD2   . HIS A 1 89  ? -42.297 42.617  -41.218 1.00 53.80  ? 89  HIS A CD2   1 
ATOM   751  C  CE1   . HIS A 1 89  ? -42.345 40.673  -40.202 1.00 59.29  ? 89  HIS A CE1   1 
ATOM   752  N  NE2   . HIS A 1 89  ? -42.803 41.912  -40.153 1.00 58.69  ? 89  HIS A NE2   1 
ATOM   753  N  N     . PRO A 1 90  ? -38.215 40.915  -41.308 1.00 51.62  ? 90  PRO A N     1 
ATOM   754  C  CA    . PRO A 1 90  ? -37.374 39.751  -40.975 1.00 55.25  ? 90  PRO A CA    1 
ATOM   755  C  C     . PRO A 1 90  ? -37.859 38.464  -41.616 1.00 59.57  ? 90  PRO A C     1 
ATOM   756  O  O     . PRO A 1 90  ? -37.039 37.634  -42.029 1.00 62.56  ? 90  PRO A O     1 
ATOM   757  C  CB    . PRO A 1 90  ? -37.449 39.686  -39.443 1.00 55.90  ? 90  PRO A CB    1 
ATOM   758  C  CG    . PRO A 1 90  ? -37.895 41.034  -39.010 1.00 52.31  ? 90  PRO A CG    1 
ATOM   759  C  CD    . PRO A 1 90  ? -38.733 41.592  -40.109 1.00 50.19  ? 90  PRO A CD    1 
ATOM   760  N  N     . GLN A 1 91  ? -39.178 38.283  -41.727 1.00 57.73  ? 91  GLN A N     1 
ATOM   761  C  CA    . GLN A 1 91  ? -39.726 37.087  -42.354 1.00 61.14  ? 91  GLN A CA    1 
ATOM   762  C  C     . GLN A 1 91  ? -39.351 36.969  -43.826 1.00 62.36  ? 91  GLN A C     1 
ATOM   763  O  O     . GLN A 1 91  ? -39.555 35.900  -44.412 1.00 69.13  ? 91  GLN A O     1 
ATOM   764  C  CB    . GLN A 1 91  ? -41.248 37.066  -42.187 1.00 64.34  ? 91  GLN A CB    1 
ATOM   765  C  CG    . GLN A 1 91  ? -41.702 37.206  -40.740 1.00 60.33  ? 91  GLN A CG    1 
ATOM   766  C  CD    . GLN A 1 91  ? -43.177 36.913  -40.555 1.00 70.37  ? 91  GLN A CD    1 
ATOM   767  O  OE1   . GLN A 1 91  ? -43.840 36.399  -41.457 1.00 74.02  ? 91  GLN A OE1   1 
ATOM   768  N  NE2   . GLN A 1 91  ? -43.701 37.241  -39.378 1.00 59.17  ? 91  GLN A NE2   1 
ATOM   769  N  N     . ASP A 1 92  ? -38.808 38.031  -44.432 1.00 61.39  ? 92  ASP A N     1 
ATOM   770  C  CA    . ASP A 1 92  ? -38.283 37.920  -45.788 1.00 69.12  ? 92  ASP A CA    1 
ATOM   771  C  C     . ASP A 1 92  ? -37.049 37.031  -45.838 1.00 66.91  ? 92  ASP A C     1 
ATOM   772  O  O     . ASP A 1 92  ? -36.814 36.359  -46.849 1.00 70.48  ? 92  ASP A O     1 
ATOM   773  C  CB    . ASP A 1 92  ? -37.938 39.302  -46.343 1.00 73.95  ? 92  ASP A CB    1 
ATOM   774  C  CG    . ASP A 1 92  ? -39.115 40.248  -46.324 1.00 79.89  ? 92  ASP A CG    1 
ATOM   775  O  OD1   . ASP A 1 92  ? -38.899 41.457  -46.104 1.00 76.52  ? 92  ASP A OD1   1 
ATOM   776  O  OD2   . ASP A 1 92  ? -40.255 39.787  -46.521 1.00 73.01  ? 92  ASP A OD2   1 
ATOM   777  N  N     . GLN A 1 93  ? -36.257 37.012  -44.765 1.00 59.99  ? 93  GLN A N     1 
ATOM   778  C  CA    . GLN A 1 93  ? -34.988 36.284  -44.793 1.00 66.40  ? 93  GLN A CA    1 
ATOM   779  C  C     . GLN A 1 93  ? -35.168 34.780  -44.965 1.00 67.92  ? 93  GLN A C     1 
ATOM   780  O  O     . GLN A 1 93  ? -34.477 34.197  -45.819 1.00 61.21  ? 93  GLN A O     1 
ATOM   781  C  CB    . GLN A 1 93  ? -34.172 36.614  -43.538 1.00 58.45  ? 93  GLN A CB    1 
ATOM   782  C  CG    . GLN A 1 93  ? -33.912 38.096  -43.336 1.00 56.82  ? 93  GLN A CG    1 
ATOM   783  C  CD    . GLN A 1 93  ? -33.047 38.373  -42.122 1.00 60.91  ? 93  GLN A CD    1 
ATOM   784  O  OE1   . GLN A 1 93  ? -33.046 39.481  -41.587 1.00 56.05  ? 93  GLN A OE1   1 
ATOM   785  N  NE2   . GLN A 1 93  ? -32.303 37.364  -41.682 1.00 64.30  ? 93  GLN A NE2   1 
ATOM   786  N  N     . PRO A 1 94  ? -36.043 34.092  -44.219 1.00 66.32  ? 94  PRO A N     1 
ATOM   787  C  CA    . PRO A 1 94  ? -36.197 32.645  -44.448 1.00 67.81  ? 94  PRO A CA    1 
ATOM   788  C  C     . PRO A 1 94  ? -36.693 32.299  -45.840 1.00 71.09  ? 94  PRO A C     1 
ATOM   789  O  O     . PRO A 1 94  ? -36.464 31.173  -46.298 1.00 81.33  ? 94  PRO A O     1 
ATOM   790  C  CB    . PRO A 1 94  ? -37.211 32.217  -43.376 1.00 61.40  ? 94  PRO A CB    1 
ATOM   791  C  CG    . PRO A 1 94  ? -37.840 33.474  -42.895 1.00 67.97  ? 94  PRO A CG    1 
ATOM   792  C  CD    . PRO A 1 94  ? -36.812 34.535  -43.042 1.00 62.43  ? 94  PRO A CD    1 
ATOM   793  N  N     . ALA A 1 95  ? -37.354 33.226  -46.531 1.00 68.32  ? 95  ALA A N     1 
ATOM   794  C  CA    . ALA A 1 95  ? -37.921 32.935  -47.841 1.00 70.91  ? 95  ALA A CA    1 
ATOM   795  C  C     . ALA A 1 95  ? -36.970 33.228  -48.993 1.00 70.17  ? 95  ALA A C     1 
ATOM   796  O  O     . ALA A 1 95  ? -37.153 32.671  -50.082 1.00 71.44  ? 95  ALA A O     1 
ATOM   797  C  CB    . ALA A 1 95  ? -39.216 33.728  -48.043 1.00 72.21  ? 95  ALA A CB    1 
ATOM   798  N  N     . ILE A 1 96  ? -35.964 34.075  -48.789 1.00 64.71  ? 96  ILE A N     1 
ATOM   799  C  CA    . ILE A 1 96  ? -35.070 34.473  -49.868 1.00 70.53  ? 96  ILE A CA    1 
ATOM   800  C  C     . ILE A 1 96  ? -33.647 33.955  -49.683 1.00 75.30  ? 96  ILE A C     1 
ATOM   801  O  O     . ILE A 1 96  ? -32.912 33.854  -50.679 1.00 72.10  ? 96  ILE A O     1 
ATOM   802  C  CB    . ILE A 1 96  ? -35.064 36.007  -50.044 1.00 67.02  ? 96  ILE A CB    1 
ATOM   803  C  CG1   . ILE A 1 96  ? -34.492 36.402  -51.409 1.00 69.86  ? 96  ILE A CG1   1 
ATOM   804  C  CG2   . ILE A 1 96  ? -34.279 36.673  -48.920 1.00 67.54  ? 96  ILE A CG2   1 
ATOM   805  C  CD1   . ILE A 1 96  ? -34.264 37.892  -51.572 1.00 65.60  ? 96  ILE A CD1   1 
ATOM   806  N  N     . ARG A 1 97  ? -33.246 33.598  -48.457 1.00 71.63  ? 97  ARG A N     1 
ATOM   807  C  CA    . ARG A 1 97  ? -31.852 33.255  -48.186 1.00 70.11  ? 97  ARG A CA    1 
ATOM   808  C  C     . ARG A 1 97  ? -31.345 32.178  -49.138 1.00 74.13  ? 97  ARG A C     1 
ATOM   809  O  O     . ARG A 1 97  ? -30.297 32.341  -49.775 1.00 76.94  ? 97  ARG A O     1 
ATOM   810  C  CB    . ARG A 1 97  ? -31.688 32.815  -46.727 1.00 71.74  ? 97  ARG A CB    1 
ATOM   811  C  CG    . ARG A 1 97  ? -32.608 31.687  -46.277 1.00 77.40  ? 97  ARG A CG    1 
ATOM   812  C  CD    . ARG A 1 97  ? -32.214 31.161  -44.906 1.00 77.87  ? 97  ARG A CD    1 
ATOM   813  N  NE    . ARG A 1 97  ? -32.921 29.931  -44.572 1.00 83.74  ? 97  ARG A NE    1 
ATOM   814  C  CZ    . ARG A 1 97  ? -33.505 29.695  -43.405 1.00 92.82  ? 97  ARG A CZ    1 
ATOM   815  N  NH1   . ARG A 1 97  ? -33.483 30.587  -42.429 1.00 81.47  ? 97  ARG A NH1   1 
ATOM   816  N  NH2   . ARG A 1 97  ? -34.126 28.534  -43.213 1.00 93.42  ? 97  ARG A NH2   1 
ATOM   817  N  N     . ASP A 1 98  ? -32.095 31.079  -49.270 1.00 74.01  ? 98  ASP A N     1 
ATOM   818  C  CA    . ASP A 1 98  ? -31.677 30.004  -50.162 1.00 81.40  ? 98  ASP A CA    1 
ATOM   819  C  C     . ASP A 1 98  ? -31.501 30.509  -51.588 1.00 82.09  ? 98  ASP A C     1 
ATOM   820  O  O     . ASP A 1 98  ? -30.498 30.199  -52.241 1.00 82.25  ? 98  ASP A O     1 
ATOM   821  C  CB    . ASP A 1 98  ? -32.685 28.855  -50.115 1.00 83.11  ? 98  ASP A CB    1 
ATOM   822  C  CG    . ASP A 1 98  ? -32.673 28.123  -48.785 1.00 92.41  ? 98  ASP A CG    1 
ATOM   823  O  OD1   . ASP A 1 98  ? -31.614 28.105  -48.122 1.00 88.25  ? 98  ASP A OD1   1 
ATOM   824  O  OD2   . ASP A 1 98  ? -33.722 27.563  -48.404 1.00 105.75 ? 98  ASP A OD2   1 
ATOM   825  N  N     . LYS A 1 99  ? -32.448 31.316  -52.076 1.00 76.85  ? 99  LYS A N     1 
ATOM   826  C  CA    . LYS A 1 99  ? -32.326 31.853  -53.428 1.00 78.43  ? 99  LYS A CA    1 
ATOM   827  C  C     . LYS A 1 99  ? -31.069 32.696  -53.582 1.00 79.49  ? 99  LYS A C     1 
ATOM   828  O  O     . LYS A 1 99  ? -30.486 32.749  -54.671 1.00 80.27  ? 99  LYS A O     1 
ATOM   829  C  CB    . LYS A 1 99  ? -33.565 32.672  -53.787 1.00 76.60  ? 99  LYS A CB    1 
ATOM   830  C  CG    . LYS A 1 99  ? -34.109 32.381  -55.174 1.00 79.55  ? 99  LYS A CG    1 
ATOM   831  C  CD    . LYS A 1 99  ? -35.612 32.593  -55.238 1.00 87.07  ? 99  LYS A CD    1 
ATOM   832  C  CE    . LYS A 1 99  ? -36.089 32.703  -56.677 1.00 87.53  ? 99  LYS A CE    1 
ATOM   833  N  NZ    . LYS A 1 99  ? -35.625 31.558  -57.508 1.00 93.70  ? 99  LYS A NZ    1 
ATOM   834  N  N     . ILE A 1 100 ? -30.633 33.355  -52.508 1.00 77.61  ? 100 ILE A N     1 
ATOM   835  C  CA    . ILE A 1 100 ? -29.369 34.079  -52.563 1.00 78.42  ? 100 ILE A CA    1 
ATOM   836  C  C     . ILE A 1 100 ? -28.206 33.097  -52.616 1.00 82.78  ? 100 ILE A C     1 
ATOM   837  O  O     . ILE A 1 100 ? -27.255 33.280  -53.385 1.00 82.40  ? 100 ILE A O     1 
ATOM   838  C  CB    . ILE A 1 100 ? -29.254 35.042  -51.368 1.00 76.61  ? 100 ILE A CB    1 
ATOM   839  C  CG1   . ILE A 1 100 ? -29.983 36.353  -51.663 1.00 77.41  ? 100 ILE A CG1   1 
ATOM   840  C  CG2   . ILE A 1 100 ? -27.802 35.350  -51.072 1.00 79.15  ? 100 ILE A CG2   1 
ATOM   841  C  CD1   . ILE A 1 100 ? -29.496 37.046  -52.913 1.00 91.61  ? 100 ILE A CD1   1 
ATOM   842  N  N     . ARG A 1 101 ? -28.279 32.024  -51.823 1.00 83.84  ? 101 ARG A N     1 
ATOM   843  C  CA    . ARG A 1 101 ? -27.183 31.063  -51.755 1.00 82.02  ? 101 ARG A CA    1 
ATOM   844  C  C     . ARG A 1 101 ? -27.045 30.258  -53.042 1.00 85.62  ? 101 ARG A C     1 
ATOM   845  O  O     . ARG A 1 101 ? -25.927 29.877  -53.411 1.00 81.84  ? 101 ARG A O     1 
ATOM   846  C  CB    . ARG A 1 101 ? -27.382 30.130  -50.559 1.00 80.02  ? 101 ARG A CB    1 
ATOM   847  C  CG    . ARG A 1 101 ? -26.097 29.531  -50.007 1.00 76.37  ? 101 ARG A CG    1 
ATOM   848  C  CD    . ARG A 1 101 ? -26.211 29.237  -48.516 1.00 68.87  ? 101 ARG A CD    1 
ATOM   849  N  NE    . ARG A 1 101 ? -27.569 28.874  -48.124 1.00 91.98  ? 101 ARG A NE    1 
ATOM   850  C  CZ    . ARG A 1 101 ? -27.908 28.422  -46.924 1.00 99.26  ? 101 ARG A CZ    1 
ATOM   851  N  NH1   . ARG A 1 101 ? -27.009 28.266  -45.965 1.00 88.51  ? 101 ARG A NH1   1 
ATOM   852  N  NH2   . ARG A 1 101 ? -29.180 28.123  -46.678 1.00 83.64  ? 101 ARG A NH2   1 
ATOM   853  N  N     . GLU A 1 102 ? -28.155 29.985  -53.737 1.00 88.09  ? 102 GLU A N     1 
ATOM   854  C  CA    . GLU A 1 102 ? -28.073 29.244  -54.993 1.00 88.36  ? 102 GLU A CA    1 
ATOM   855  C  C     . GLU A 1 102 ? -27.305 30.006  -56.062 1.00 85.62  ? 102 GLU A C     1 
ATOM   856  O  O     . GLU A 1 102 ? -26.793 29.385  -57.000 1.00 90.17  ? 102 GLU A O     1 
ATOM   857  C  CB    . GLU A 1 102 ? -29.470 28.911  -55.530 1.00 93.71  ? 102 GLU A CB    1 
ATOM   858  C  CG    . GLU A 1 102 ? -30.427 28.266  -54.540 1.00 91.89  ? 102 GLU A CG    1 
ATOM   859  C  CD    . GLU A 1 102 ? -29.966 26.905  -54.059 1.00 105.07 ? 102 GLU A CD    1 
ATOM   860  O  OE1   . GLU A 1 102 ? -29.179 26.249  -54.773 1.00 115.72 ? 102 GLU A OE1   1 
ATOM   861  O  OE2   . GLU A 1 102 ? -30.394 26.491  -52.960 1.00 103.77 ? 102 GLU A OE2   1 
ATOM   862  N  N     . HIS A 1 103 ? -27.220 31.326  -55.946 1.00 85.50  ? 103 HIS A N     1 
ATOM   863  C  CA    . HIS A 1 103 ? -26.566 32.125  -56.971 1.00 89.77  ? 103 HIS A CA    1 
ATOM   864  C  C     . HIS A 1 103 ? -25.093 31.740  -57.075 1.00 92.73  ? 103 HIS A C     1 
ATOM   865  O  O     . HIS A 1 103 ? -24.421 31.593  -56.044 1.00 89.20  ? 103 HIS A O     1 
ATOM   866  C  CB    . HIS A 1 103 ? -26.701 33.614  -56.658 1.00 89.54  ? 103 HIS A CB    1 
ATOM   867  C  CG    . HIS A 1 103 ? -26.628 34.493  -57.868 1.00 87.40  ? 103 HIS A CG    1 
ATOM   868  N  ND1   . HIS A 1 103 ? -25.451 35.063  -58.303 1.00 84.76  ? 103 HIS A ND1   1 
ATOM   869  C  CD2   . HIS A 1 103 ? -27.585 34.898  -58.736 1.00 87.60  ? 103 HIS A CD2   1 
ATOM   870  C  CE1   . HIS A 1 103 ? -25.686 35.782  -59.386 1.00 89.57  ? 103 HIS A CE1   1 
ATOM   871  N  NE2   . HIS A 1 103 ? -26.973 35.698  -59.670 1.00 93.19  ? 103 HIS A NE2   1 
ATOM   872  N  N     . PRO A 1 104 ? -24.559 31.561  -58.285 1.00 96.77  ? 104 PRO A N     1 
ATOM   873  C  CA    . PRO A 1 104 ? -23.144 31.183  -58.400 1.00 92.78  ? 104 PRO A CA    1 
ATOM   874  C  C     . PRO A 1 104 ? -22.199 32.276  -57.941 1.00 90.57  ? 104 PRO A C     1 
ATOM   875  O  O     . PRO A 1 104 ? -21.106 31.966  -57.453 1.00 90.25  ? 104 PRO A O     1 
ATOM   876  C  CB    . PRO A 1 104 ? -22.980 30.885  -59.895 1.00 94.48  ? 104 PRO A CB    1 
ATOM   877  C  CG    . PRO A 1 104 ? -24.049 31.690  -60.556 1.00 91.27  ? 104 PRO A CG    1 
ATOM   878  C  CD    . PRO A 1 104 ? -25.209 31.699  -59.599 1.00 91.74  ? 104 PRO A CD    1 
ATOM   879  N  N     . ALA A 1 105 ? -22.590 33.546  -58.071 1.00 91.46  ? 105 ALA A N     1 
ATOM   880  C  CA    . ALA A 1 105 ? -21.691 34.640  -57.727 1.00 92.20  ? 105 ALA A CA    1 
ATOM   881  C  C     . ALA A 1 105 ? -21.455 34.754  -56.227 1.00 88.82  ? 105 ALA A C     1 
ATOM   882  O  O     . ALA A 1 105 ? -20.509 35.433  -55.812 1.00 83.71  ? 105 ALA A O     1 
ATOM   883  C  CB    . ALA A 1 105 ? -22.235 35.962  -58.269 1.00 89.61  ? 105 ALA A CB    1 
ATOM   884  N  N     . VAL A 1 106 ? -22.283 34.114  -55.405 1.00 88.05  ? 106 VAL A N     1 
ATOM   885  C  CA    . VAL A 1 106 ? -22.120 34.147  -53.957 1.00 89.66  ? 106 VAL A CA    1 
ATOM   886  C  C     . VAL A 1 106 ? -21.372 32.896  -53.521 1.00 81.71  ? 106 VAL A C     1 
ATOM   887  O  O     . VAL A 1 106 ? -21.548 31.814  -54.097 1.00 88.40  ? 106 VAL A O     1 
ATOM   888  C  CB    . VAL A 1 106 ? -23.478 34.268  -53.233 1.00 84.21  ? 106 VAL A CB    1 
ATOM   889  C  CG1   . VAL A 1 106 ? -24.367 35.289  -53.932 1.00 84.57  ? 106 VAL A CG1   1 
ATOM   890  C  CG2   . VAL A 1 106 ? -24.175 32.918  -53.127 1.00 91.36  ? 106 VAL A CG2   1 
ATOM   891  N  N     . ILE A 1 107 ? -20.505 33.052  -52.527 1.00 75.96  ? 107 ILE A N     1 
ATOM   892  C  CA    . ILE A 1 107 ? -19.832 31.910  -51.920 1.00 72.68  ? 107 ILE A CA    1 
ATOM   893  C  C     . ILE A 1 107 ? -20.640 31.355  -50.760 1.00 71.92  ? 107 ILE A C     1 
ATOM   894  O  O     . ILE A 1 107 ? -20.827 30.141  -50.640 1.00 79.27  ? 107 ILE A O     1 
ATOM   895  C  CB    . ILE A 1 107 ? -18.408 32.301  -51.471 1.00 70.12  ? 107 ILE A CB    1 
ATOM   896  C  CG1   . ILE A 1 107 ? -17.505 32.544  -52.679 1.00 69.54  ? 107 ILE A CG1   1 
ATOM   897  C  CG2   . ILE A 1 107 ? -17.813 31.233  -50.573 1.00 67.03  ? 107 ILE A CG2   1 
ATOM   898  C  CD1   . ILE A 1 107 ? -17.255 33.988  -52.955 1.00 74.61  ? 107 ILE A CD1   1 
ATOM   899  N  N     . ASP A 1 108 ? -21.138 32.238  -49.901 1.00 68.59  ? 108 ASP A N     1 
ATOM   900  C  CA    . ASP A 1 108 ? -21.882 31.834  -48.718 1.00 64.31  ? 108 ASP A CA    1 
ATOM   901  C  C     . ASP A 1 108 ? -22.614 33.051  -48.170 1.00 60.79  ? 108 ASP A C     1 
ATOM   902  O  O     . ASP A 1 108 ? -22.396 34.188  -48.606 1.00 58.80  ? 108 ASP A O     1 
ATOM   903  C  CB    . ASP A 1 108 ? -20.959 31.226  -47.657 1.00 67.51  ? 108 ASP A CB    1 
ATOM   904  C  CG    . ASP A 1 108 ? -21.663 30.206  -46.786 1.00 77.38  ? 108 ASP A CG    1 
ATOM   905  O  OD1   . ASP A 1 108 ? -22.837 29.889  -47.074 1.00 74.39  ? 108 ASP A OD1   1 
ATOM   906  O  OD2   . ASP A 1 108 ? -21.041 29.720  -45.817 1.00 74.39  ? 108 ASP A OD2   1 
ATOM   907  N  N     . ILE A 1 109 ? -23.497 32.790  -47.211 1.00 61.85  ? 109 ILE A N     1 
ATOM   908  C  CA    . ILE A 1 109 ? -24.220 33.825  -46.490 1.00 60.27  ? 109 ILE A CA    1 
ATOM   909  C  C     . ILE A 1 109 ? -24.048 33.577  -45.000 1.00 60.43  ? 109 ILE A C     1 
ATOM   910  O  O     . ILE A 1 109 ? -23.817 32.447  -44.559 1.00 59.63  ? 109 ILE A O     1 
ATOM   911  C  CB    . ILE A 1 109 ? -25.711 33.873  -46.888 1.00 62.23  ? 109 ILE A CB    1 
ATOM   912  C  CG1   . ILE A 1 109 ? -26.317 32.470  -46.906 1.00 64.64  ? 109 ILE A CG1   1 
ATOM   913  C  CG2   . ILE A 1 109 ? -25.869 34.521  -48.241 1.00 57.26  ? 109 ILE A CG2   1 
ATOM   914  C  CD1   . ILE A 1 109 ? -27.817 32.454  -46.696 1.00 68.23  ? 109 ILE A CD1   1 
ATOM   915  N  N     . TYR A 1 110 ? -24.147 34.651  -44.223 1.00 55.80  ? 110 TYR A N     1 
ATOM   916  C  CA    . TYR A 1 110 ? -23.790 34.614  -42.815 1.00 53.46  ? 110 TYR A CA    1 
ATOM   917  C  C     . TYR A 1 110 ? -24.784 35.426  -41.999 1.00 55.50  ? 110 TYR A C     1 
ATOM   918  O  O     . TYR A 1 110 ? -25.332 36.432  -42.467 1.00 56.43  ? 110 TYR A O     1 
ATOM   919  C  CB    . TYR A 1 110 ? -22.366 35.145  -42.585 1.00 54.12  ? 110 TYR A CB    1 
ATOM   920  C  CG    . TYR A 1 110 ? -21.314 34.480  -43.449 1.00 53.94  ? 110 TYR A CG    1 
ATOM   921  C  CD1   . TYR A 1 110 ? -20.674 33.320  -43.030 1.00 55.54  ? 110 TYR A CD1   1 
ATOM   922  C  CD2   . TYR A 1 110 ? -20.961 35.013  -44.684 1.00 52.98  ? 110 TYR A CD2   1 
ATOM   923  C  CE1   . TYR A 1 110 ? -19.713 32.709  -43.817 1.00 62.59  ? 110 TYR A CE1   1 
ATOM   924  C  CE2   . TYR A 1 110 ? -20.002 34.409  -45.476 1.00 60.69  ? 110 TYR A CE2   1 
ATOM   925  C  CZ    . TYR A 1 110 ? -19.381 33.258  -45.038 1.00 62.84  ? 110 TYR A CZ    1 
ATOM   926  O  OH    . TYR A 1 110 ? -18.427 32.654  -45.824 1.00 62.89  ? 110 TYR A OH    1 
ATOM   927  N  N     . GLU A 1 111 ? -25.005 34.963  -40.767 1.00 51.24  ? 111 GLU A N     1 
ATOM   928  C  CA    . GLU A 1 111 ? -25.845 35.642  -39.783 1.00 53.67  ? 111 GLU A CA    1 
ATOM   929  C  C     . GLU A 1 111 ? -27.244 35.900  -40.338 1.00 53.65  ? 111 GLU A C     1 
ATOM   930  O  O     . GLU A 1 111 ? -27.778 37.008  -40.268 1.00 54.77  ? 111 GLU A O     1 
ATOM   931  C  CB    . GLU A 1 111 ? -25.182 36.935  -39.306 1.00 50.50  ? 111 GLU A CB    1 
ATOM   932  C  CG    . GLU A 1 111 ? -23.739 36.740  -38.853 1.00 56.72  ? 111 GLU A CG    1 
ATOM   933  C  CD    . GLU A 1 111 ? -23.186 37.929  -38.089 1.00 57.80  ? 111 GLU A CD    1 
ATOM   934  O  OE1   . GLU A 1 111 ? -23.983 38.792  -37.664 1.00 52.75  ? 111 GLU A OE1   1 
ATOM   935  O  OE2   . GLU A 1 111 ? -21.950 37.998  -37.910 1.00 52.51  ? 111 GLU A OE2   1 
ATOM   936  N  N     . TYR A 1 112 ? -27.843 34.845  -40.891 1.00 60.16  ? 112 TYR A N     1 
ATOM   937  C  CA    . TYR A 1 112 ? -29.150 34.927  -41.527 1.00 59.81  ? 112 TYR A CA    1 
ATOM   938  C  C     . TYR A 1 112 ? -30.268 34.328  -40.687 1.00 58.62  ? 112 TYR A C     1 
ATOM   939  O  O     . TYR A 1 112 ? -31.442 34.540  -41.008 1.00 60.73  ? 112 TYR A O     1 
ATOM   940  C  CB    . TYR A 1 112 ? -29.108 34.232  -42.895 1.00 57.88  ? 112 TYR A CB    1 
ATOM   941  C  CG    . TYR A 1 112 ? -28.570 32.817  -42.851 1.00 69.16  ? 112 TYR A CG    1 
ATOM   942  C  CD1   . TYR A 1 112 ? -27.292 32.529  -43.311 1.00 69.69  ? 112 TYR A CD1   1 
ATOM   943  C  CD2   . TYR A 1 112 ? -29.347 31.765  -42.373 1.00 69.34  ? 112 TYR A CD2   1 
ATOM   944  C  CE1   . TYR A 1 112 ? -26.794 31.239  -43.284 1.00 86.82  ? 112 TYR A CE1   1 
ATOM   945  C  CE2   . TYR A 1 112 ? -28.857 30.474  -42.340 1.00 85.04  ? 112 TYR A CE2   1 
ATOM   946  C  CZ    . TYR A 1 112 ? -27.581 30.216  -42.797 1.00 78.13  ? 112 TYR A CZ    1 
ATOM   947  O  OH    . TYR A 1 112 ? -27.091 28.930  -42.767 1.00 77.53  ? 112 TYR A OH    1 
ATOM   948  N  N     . ASP A 1 113 ? -29.939 33.587  -39.631 1.00 60.31  ? 113 ASP A N     1 
ATOM   949  C  CA    . ASP A 1 113 ? -30.930 32.869  -38.842 1.00 63.06  ? 113 ASP A CA    1 
ATOM   950  C  C     . ASP A 1 113 ? -31.100 33.444  -37.442 1.00 56.33  ? 113 ASP A C     1 
ATOM   951  O  O     . ASP A 1 113 ? -31.786 32.837  -36.614 1.00 58.67  ? 113 ASP A O     1 
ATOM   952  C  CB    . ASP A 1 113 ? -30.556 31.386  -38.759 1.00 67.51  ? 113 ASP A CB    1 
ATOM   953  C  CG    . ASP A 1 113 ? -29.141 31.167  -38.254 1.00 81.68  ? 113 ASP A CG    1 
ATOM   954  O  OD1   . ASP A 1 113 ? -28.371 32.150  -38.175 1.00 69.72  ? 113 ASP A OD1   1 
ATOM   955  O  OD2   . ASP A 1 113 ? -28.797 30.010  -37.933 1.00 82.62  ? 113 ASP A OD2   1 
ATOM   956  N  N     . THR A 1 114 ? -30.502 34.592  -37.158 1.00 52.69  ? 114 THR A N     1 
ATOM   957  C  CA    . THR A 1 114 ? -30.601 35.166  -35.821 1.00 53.25  ? 114 THR A CA    1 
ATOM   958  C  C     . THR A 1 114 ? -31.924 35.910  -35.675 1.00 52.18  ? 114 THR A C     1 
ATOM   959  O  O     . THR A 1 114 ? -32.264 36.729  -36.535 1.00 51.35  ? 114 THR A O     1 
ATOM   960  C  CB    . THR A 1 114 ? -29.432 36.109  -35.549 1.00 53.16  ? 114 THR A CB    1 
ATOM   961  O  OG1   . THR A 1 114 ? -29.415 37.148  -36.534 1.00 67.65  ? 114 THR A OG1   1 
ATOM   962  C  CG2   . THR A 1 114 ? -28.113 35.348  -35.606 1.00 54.58  ? 114 THR A CG2   1 
ATOM   963  N  N     . PRO A 1 115 ? -32.690 35.655  -34.612 1.00 53.65  ? 115 PRO A N     1 
ATOM   964  C  CA    . PRO A 1 115 ? -34.004 36.298  -34.476 1.00 46.98  ? 115 PRO A CA    1 
ATOM   965  C  C     . PRO A 1 115 ? -33.889 37.813  -34.379 1.00 46.59  ? 115 PRO A C     1 
ATOM   966  O  O     . PRO A 1 115 ? -32.876 38.358  -33.936 1.00 47.69  ? 115 PRO A O     1 
ATOM   967  C  CB    . PRO A 1 115 ? -34.566 35.694  -33.182 1.00 39.65  ? 115 PRO A CB    1 
ATOM   968  C  CG    . PRO A 1 115 ? -33.788 34.429  -32.978 1.00 54.23  ? 115 PRO A CG    1 
ATOM   969  C  CD    . PRO A 1 115 ? -32.418 34.712  -33.516 1.00 49.03  ? 115 PRO A CD    1 
ATOM   970  N  N     . PHE A 1 116 ? -34.965 38.488  -34.786 1.00 47.21  ? 116 PHE A N     1 
ATOM   971  C  CA    . PHE A 1 116 ? -34.923 39.936  -34.974 1.00 45.12  ? 116 PHE A CA    1 
ATOM   972  C  C     . PHE A 1 116 ? -34.719 40.673  -33.654 1.00 47.67  ? 116 PHE A C     1 
ATOM   973  O  O     . PHE A 1 116 ? -33.865 41.561  -33.556 1.00 44.47  ? 116 PHE A O     1 
ATOM   974  C  CB    . PHE A 1 116 ? -36.207 40.397  -35.665 1.00 45.91  ? 116 PHE A CB    1 
ATOM   975  C  CG    . PHE A 1 116 ? -36.176 41.827  -36.117 1.00 56.18  ? 116 PHE A CG    1 
ATOM   976  C  CD1   . PHE A 1 116 ? -35.263 42.246  -37.072 1.00 55.31  ? 116 PHE A CD1   1 
ATOM   977  C  CD2   . PHE A 1 116 ? -37.071 42.750  -35.600 1.00 44.64  ? 116 PHE A CD2   1 
ATOM   978  C  CE1   . PHE A 1 116 ? -35.236 43.561  -37.495 1.00 54.19  ? 116 PHE A CE1   1 
ATOM   979  C  CE2   . PHE A 1 116 ? -37.048 44.066  -36.020 1.00 48.28  ? 116 PHE A CE2   1 
ATOM   980  C  CZ    . PHE A 1 116 ? -36.129 44.472  -36.968 1.00 52.23  ? 116 PHE A CZ    1 
ATOM   981  N  N     . ALA A 1 117 ? -35.494 40.321  -32.623 1.00 47.19  ? 117 ALA A N     1 
ATOM   982  C  CA    . ALA A 1 117 ? -35.414 41.047  -31.357 1.00 47.38  ? 117 ALA A CA    1 
ATOM   983  C  C     . ALA A 1 117 ? -34.070 40.831  -30.668 1.00 43.20  ? 117 ALA A C     1 
ATOM   984  O  O     . ALA A 1 117 ? -33.508 41.762  -30.075 1.00 47.42  ? 117 ALA A O     1 
ATOM   985  C  CB    . ALA A 1 117 ? -36.563 40.628  -30.440 1.00 35.20  ? 117 ALA A CB    1 
ATOM   986  N  N     . LYS A 1 118 ? -33.526 39.614  -30.746 1.00 44.39  ? 118 LYS A N     1 
ATOM   987  C  CA    . LYS A 1 118 ? -32.226 39.356  -30.135 1.00 48.04  ? 118 LYS A CA    1 
ATOM   988  C  C     . LYS A 1 118 ? -31.103 40.025  -30.923 1.00 44.84  ? 118 LYS A C     1 
ATOM   989  O  O     . LYS A 1 118 ? -30.133 40.524  -30.335 1.00 46.83  ? 118 LYS A O     1 
ATOM   990  C  CB    . LYS A 1 118 ? -32.001 37.850  -30.018 1.00 45.64  ? 118 LYS A CB    1 
ATOM   991  C  CG    . LYS A 1 118 ? -32.895 37.193  -28.974 1.00 46.59  ? 118 LYS A CG    1 
ATOM   992  C  CD    . LYS A 1 118 ? -33.162 35.733  -29.291 1.00 55.12  ? 118 LYS A CD    1 
ATOM   993  C  CE    . LYS A 1 118 ? -34.000 35.085  -28.201 1.00 66.95  ? 118 LYS A CE    1 
ATOM   994  N  NZ    . LYS A 1 118 ? -34.015 33.601  -28.312 1.00 78.96  ? 118 LYS A NZ    1 
ATOM   995  N  N     . ARG A 1 119 ? -31.223 40.059  -32.253 1.00 45.86  ? 119 ARG A N     1 
ATOM   996  C  CA    . ARG A 1 119 ? -30.271 40.820  -33.055 1.00 43.11  ? 119 ARG A CA    1 
ATOM   997  C  C     . ARG A 1 119 ? -30.331 42.302  -32.707 1.00 50.04  ? 119 ARG A C     1 
ATOM   998  O  O     . ARG A 1 119 ? -29.304 42.989  -32.715 1.00 49.95  ? 119 ARG A O     1 
ATOM   999  C  CB    . ARG A 1 119 ? -30.535 40.605  -34.548 1.00 45.18  ? 119 ARG A CB    1 
ATOM   1000 C  CG    . ARG A 1 119 ? -29.721 41.524  -35.461 1.00 50.61  ? 119 ARG A CG    1 
ATOM   1001 C  CD    . ARG A 1 119 ? -28.980 40.756  -36.557 1.00 51.57  ? 119 ARG A CD    1 
ATOM   1002 N  NE    . ARG A 1 119 ? -28.038 39.775  -36.025 1.00 74.61  ? 119 ARG A NE    1 
ATOM   1003 C  CZ    . ARG A 1 119 ? -26.825 40.059  -35.568 1.00 73.54  ? 119 ARG A CZ    1 
ATOM   1004 N  NH1   . ARG A 1 119 ? -26.367 41.300  -35.543 1.00 58.12  ? 119 ARG A NH1   1 
ATOM   1005 N  NH2   . ARG A 1 119 ? -26.050 39.072  -35.126 1.00 60.77  ? 119 ARG A NH2   1 
ATOM   1006 N  N     . TYR A 1 120 ? -31.525 42.812  -32.394 1.00 45.56  ? 120 TYR A N     1 
ATOM   1007 C  CA    . TYR A 1 120 ? -31.636 44.193  -31.935 1.00 46.69  ? 120 TYR A CA    1 
ATOM   1008 C  C     . TYR A 1 120 ? -30.928 44.384  -30.601 1.00 43.69  ? 120 TYR A C     1 
ATOM   1009 O  O     . TYR A 1 120 ? -30.232 45.385  -30.396 1.00 43.28  ? 120 TYR A O     1 
ATOM   1010 C  CB    . TYR A 1 120 ? -33.107 44.596  -31.820 1.00 44.74  ? 120 TYR A CB    1 
ATOM   1011 C  CG    . TYR A 1 120 ? -33.325 46.019  -31.351 1.00 41.39  ? 120 TYR A CG    1 
ATOM   1012 C  CD1   . TYR A 1 120 ? -33.411 47.065  -32.262 1.00 38.67  ? 120 TYR A CD1   1 
ATOM   1013 C  CD2   . TYR A 1 120 ? -33.450 46.316  -30.000 1.00 39.26  ? 120 TYR A CD2   1 
ATOM   1014 C  CE1   . TYR A 1 120 ? -33.611 48.365  -31.838 1.00 42.23  ? 120 TYR A CE1   1 
ATOM   1015 C  CE2   . TYR A 1 120 ? -33.651 47.614  -29.567 1.00 42.88  ? 120 TYR A CE2   1 
ATOM   1016 C  CZ    . TYR A 1 120 ? -33.731 48.633  -30.490 1.00 44.08  ? 120 TYR A CZ    1 
ATOM   1017 O  OH    . TYR A 1 120 ? -33.931 49.925  -30.061 1.00 51.30  ? 120 TYR A OH    1 
ATOM   1018 N  N     . LEU A 1 121 ? -31.112 43.439  -29.674 1.00 38.54  ? 121 LEU A N     1 
ATOM   1019 C  CA    . LEU A 1 121 ? -30.407 43.508  -28.396 1.00 43.12  ? 121 LEU A CA    1 
ATOM   1020 C  C     . LEU A 1 121 ? -28.896 43.560  -28.597 1.00 52.34  ? 121 LEU A C     1 
ATOM   1021 O  O     . LEU A 1 121 ? -28.196 44.318  -27.914 1.00 48.11  ? 121 LEU A O     1 
ATOM   1022 C  CB    . LEU A 1 121 ? -30.776 42.310  -27.521 1.00 40.73  ? 121 LEU A CB    1 
ATOM   1023 C  CG    . LEU A 1 121 ? -32.021 42.422  -26.644 1.00 50.12  ? 121 LEU A CG    1 
ATOM   1024 C  CD1   . LEU A 1 121 ? -32.161 41.180  -25.780 1.00 47.76  ? 121 LEU A CD1   1 
ATOM   1025 C  CD2   . LEU A 1 121 ? -31.961 43.676  -25.788 1.00 49.69  ? 121 LEU A CD2   1 
ATOM   1026 N  N     . ILE A 1 122 ? -28.376 42.759  -29.527 1.00 44.94  ? 122 ILE A N     1 
ATOM   1027 C  CA    . ILE A 1 122 ? -26.928 42.690  -29.715 1.00 50.28  ? 122 ILE A CA    1 
ATOM   1028 C  C     . ILE A 1 122 ? -26.416 43.939  -30.429 1.00 53.39  ? 122 ILE A C     1 
ATOM   1029 O  O     . ILE A 1 122 ? -25.452 44.575  -29.987 1.00 49.40  ? 122 ILE A O     1 
ATOM   1030 C  CB    . ILE A 1 122 ? -26.544 41.405  -30.471 1.00 51.47  ? 122 ILE A CB    1 
ATOM   1031 C  CG1   . ILE A 1 122 ? -26.537 40.210  -29.519 1.00 43.69  ? 122 ILE A CG1   1 
ATOM   1032 C  CG2   . ILE A 1 122 ? -25.177 41.548  -31.120 1.00 45.31  ? 122 ILE A CG2   1 
ATOM   1033 C  CD1   . ILE A 1 122 ? -26.779 38.887  -30.207 1.00 45.90  ? 122 ILE A CD1   1 
ATOM   1034 N  N     . ASP A 1 123 ? -27.056 44.311  -31.542 1.00 50.41  ? 123 ASP A N     1 
ATOM   1035 C  CA    . ASP A 1 123 ? -26.565 45.423  -32.352 1.00 49.82  ? 123 ASP A CA    1 
ATOM   1036 C  C     . ASP A 1 123 ? -26.634 46.740  -31.593 1.00 49.08  ? 123 ASP A C     1 
ATOM   1037 O  O     . ASP A 1 123 ? -25.724 47.571  -31.692 1.00 56.03  ? 123 ASP A O     1 
ATOM   1038 C  CB    . ASP A 1 123 ? -27.363 45.516  -33.650 1.00 47.23  ? 123 ASP A CB    1 
ATOM   1039 C  CG    . ASP A 1 123 ? -26.988 44.436  -34.641 1.00 50.39  ? 123 ASP A CG    1 
ATOM   1040 O  OD1   . ASP A 1 123 ? -26.387 43.425  -34.217 1.00 50.36  ? 123 ASP A OD1   1 
ATOM   1041 O  OD2   . ASP A 1 123 ? -27.297 44.594  -35.841 1.00 50.00  ? 123 ASP A OD2   1 
ATOM   1042 N  N     . LYS A 1 124 ? -27.706 46.954  -30.837 1.00 48.05  ? 124 LYS A N     1 
ATOM   1043 C  CA    . LYS A 1 124 ? -27.852 48.170  -30.048 1.00 48.96  ? 124 LYS A CA    1 
ATOM   1044 C  C     . LYS A 1 124 ? -27.016 48.155  -28.774 1.00 49.20  ? 124 LYS A C     1 
ATOM   1045 O  O     . LYS A 1 124 ? -27.050 49.135  -28.023 1.00 53.77  ? 124 LYS A O     1 
ATOM   1046 C  CB    . LYS A 1 124 ? -29.326 48.394  -29.696 1.00 52.12  ? 124 LYS A CB    1 
ATOM   1047 C  CG    . LYS A 1 124 ? -29.946 49.627  -30.335 1.00 56.87  ? 124 LYS A CG    1 
ATOM   1048 C  CD    . LYS A 1 124 ? -30.065 49.484  -31.845 1.00 55.85  ? 124 LYS A CD    1 
ATOM   1049 C  CE    . LYS A 1 124 ? -30.497 50.796  -32.486 1.00 59.38  ? 124 LYS A CE    1 
ATOM   1050 N  NZ    . LYS A 1 124 ? -30.382 50.762  -33.969 1.00 64.28  ? 124 LYS A NZ    1 
ATOM   1051 N  N     . GLY A 1 125 ? -26.274 47.080  -28.514 1.00 50.41  ? 125 GLY A N     1 
ATOM   1052 C  CA    . GLY A 1 125 ? -25.467 47.002  -27.307 1.00 49.25  ? 125 GLY A CA    1 
ATOM   1053 C  C     . GLY A 1 125 ? -26.263 47.078  -26.024 1.00 49.92  ? 125 GLY A C     1 
ATOM   1054 O  O     . GLY A 1 125 ? -25.766 47.604  -25.022 1.00 51.92  ? 125 GLY A O     1 
ATOM   1055 N  N     . LEU A 1 126 ? -27.490 46.567  -26.025 1.00 53.67  ? 126 LEU A N     1 
ATOM   1056 C  CA    . LEU A 1 126 ? -28.349 46.621  -24.852 1.00 49.62  ? 126 LEU A CA    1 
ATOM   1057 C  C     . LEU A 1 126 ? -28.199 45.351  -24.025 1.00 44.66  ? 126 LEU A C     1 
ATOM   1058 O  O     . LEU A 1 126 ? -28.049 44.253  -24.570 1.00 45.94  ? 126 LEU A O     1 
ATOM   1059 C  CB    . LEU A 1 126 ? -29.809 46.812  -25.262 1.00 52.60  ? 126 LEU A CB    1 
ATOM   1060 C  CG    . LEU A 1 126 ? -30.085 48.057  -26.106 1.00 58.17  ? 126 LEU A CG    1 
ATOM   1061 C  CD1   . LEU A 1 126 ? -31.525 48.070  -26.591 1.00 44.40  ? 126 LEU A CD1   1 
ATOM   1062 C  CD2   . LEU A 1 126 ? -29.760 49.320  -25.323 1.00 52.98  ? 126 LEU A CD2   1 
ATOM   1063 N  N     . VAL A 1 127 ? -28.238 45.510  -22.707 1.00 51.50  ? 127 VAL A N     1 
ATOM   1064 C  CA    . VAL A 1 127 ? -28.104 44.409  -21.764 1.00 46.68  ? 127 VAL A CA    1 
ATOM   1065 C  C     . VAL A 1 127 ? -29.324 44.423  -20.851 1.00 51.75  ? 127 VAL A C     1 
ATOM   1066 O  O     . VAL A 1 127 ? -29.539 45.396  -20.124 1.00 53.17  ? 127 VAL A O     1 
ATOM   1067 C  CB    . VAL A 1 127 ? -26.812 44.505  -20.936 1.00 50.09  ? 127 VAL A CB    1 
ATOM   1068 C  CG1   . VAL A 1 127 ? -26.736 43.356  -19.939 1.00 50.46  ? 127 VAL A CG1   1 
ATOM   1069 C  CG2   . VAL A 1 127 ? -25.595 44.512  -21.847 1.00 46.52  ? 127 VAL A CG2   1 
ATOM   1070 N  N     . PRO A 1 128 ? -30.146 43.381  -20.850 1.00 47.27  ? 128 PRO A N     1 
ATOM   1071 C  CA    . PRO A 1 128 ? -31.310 43.352  -19.960 1.00 54.08  ? 128 PRO A CA    1 
ATOM   1072 C  C     . PRO A 1 128 ? -30.903 43.057  -18.522 1.00 52.87  ? 128 PRO A C     1 
ATOM   1073 O  O     . PRO A 1 128 ? -29.763 42.696  -18.228 1.00 57.03  ? 128 PRO A O     1 
ATOM   1074 C  CB    . PRO A 1 128 ? -32.169 42.224  -20.540 1.00 52.97  ? 128 PRO A CB    1 
ATOM   1075 C  CG    . PRO A 1 128 ? -31.195 41.324  -21.212 1.00 52.39  ? 128 PRO A CG    1 
ATOM   1076 C  CD    . PRO A 1 128 ? -30.066 42.186  -21.707 1.00 48.09  ? 128 PRO A CD    1 
ATOM   1077 N  N     . MET A 1 129 ? -31.871 43.237  -17.620 1.00 58.43  ? 129 MET A N     1 
ATOM   1078 C  CA    . MET A 1 129 ? -31.708 42.932  -16.197 1.00 61.11  ? 129 MET A CA    1 
ATOM   1079 C  C     . MET A 1 129 ? -30.608 43.773  -15.552 1.00 63.43  ? 129 MET A C     1 
ATOM   1080 O  O     . MET A 1 129 ? -29.974 43.346  -14.584 1.00 69.57  ? 129 MET A O     1 
ATOM   1081 C  CB    . MET A 1 129 ? -31.433 41.440  -15.980 1.00 54.14  ? 129 MET A CB    1 
ATOM   1082 C  CG    . MET A 1 129 ? -32.615 40.526  -16.275 1.00 53.75  ? 129 MET A CG    1 
ATOM   1083 S  SD    . MET A 1 129 ? -34.215 41.354  -16.302 1.00 56.41  ? 129 MET A SD    1 
ATOM   1084 C  CE    . MET A 1 129 ? -34.554 41.488  -14.547 1.00 45.34  ? 129 MET A CE    1 
ATOM   1085 N  N     . GLU A 1 130 ? -30.370 44.970  -16.078 1.00 64.72  ? 130 GLU A N     1 
ATOM   1086 C  CA    . GLU A 1 130 ? -29.321 45.851  -15.579 1.00 69.80  ? 130 GLU A CA    1 
ATOM   1087 C  C     . GLU A 1 130 ? -29.937 46.981  -14.764 1.00 72.41  ? 130 GLU A C     1 
ATOM   1088 O  O     . GLU A 1 130 ? -30.897 47.619  -15.207 1.00 83.43  ? 130 GLU A O     1 
ATOM   1089 C  CB    . GLU A 1 130 ? -28.498 46.423  -16.734 1.00 66.89  ? 130 GLU A CB    1 
ATOM   1090 C  CG    . GLU A 1 130 ? -27.034 46.643  -16.402 1.00 80.06  ? 130 GLU A CG    1 
ATOM   1091 C  CD    . GLU A 1 130 ? -26.144 46.558  -17.625 1.00 95.20  ? 130 GLU A CD    1 
ATOM   1092 O  OE1   . GLU A 1 130 ? -26.461 47.213  -18.640 1.00 75.48  ? 130 GLU A OE1   1 
ATOM   1093 O  OE2   . GLU A 1 130 ? -25.127 45.835  -17.571 1.00 98.90  ? 130 GLU A OE2   1 
ATOM   1094 N  N     . GLY A 1 131 ? -29.383 47.227  -13.581 1.00 71.75  ? 131 GLY A N     1 
ATOM   1095 C  CA    . GLY A 1 131 ? -29.812 48.317  -12.732 1.00 74.65  ? 131 GLY A CA    1 
ATOM   1096 C  C     . GLY A 1 131 ? -30.198 47.840  -11.350 1.00 87.28  ? 131 GLY A C     1 
ATOM   1097 O  O     . GLY A 1 131 ? -30.125 46.657  -11.021 1.00 82.91  ? 131 GLY A O     1 
ATOM   1098 N  N     . ASP A 1 132 ? -30.611 48.801  -10.525 1.00 93.17  ? 132 ASP A N     1 
ATOM   1099 C  CA    . ASP A 1 132 ? -31.071 48.536  -9.169  1.00 91.76  ? 132 ASP A CA    1 
ATOM   1100 C  C     . ASP A 1 132 ? -32.584 48.407  -9.076  1.00 91.17  ? 132 ASP A C     1 
ATOM   1101 O  O     . ASP A 1 132 ? -33.109 48.215  -7.974  1.00 87.54  ? 132 ASP A O     1 
ATOM   1102 C  CB    . ASP A 1 132 ? -30.599 49.644  -8.219  1.00 100.92 ? 132 ASP A CB    1 
ATOM   1103 C  CG    . ASP A 1 132 ? -29.128 49.971  -8.385  1.00 119.42 ? 132 ASP A CG    1 
ATOM   1104 O  OD1   . ASP A 1 132 ? -28.310 49.029  -8.456  1.00 122.48 ? 132 ASP A OD1   1 
ATOM   1105 O  OD2   . ASP A 1 132 ? -28.789 51.172  -8.437  1.00 115.71 ? 132 ASP A OD2   1 
ATOM   1106 N  N     . GLU A 1 133 ? -33.292 48.511  -10.199 1.00 90.24  ? 133 GLU A N     1 
ATOM   1107 C  CA    . GLU A 1 133 ? -34.748 48.478  -10.182 1.00 85.68  ? 133 GLU A CA    1 
ATOM   1108 C  C     . GLU A 1 133 ? -35.256 47.142  -9.659  1.00 81.45  ? 133 GLU A C     1 
ATOM   1109 O  O     . GLU A 1 133 ? -34.854 46.078  -10.138 1.00 86.19  ? 133 GLU A O     1 
ATOM   1110 C  CB    . GLU A 1 133 ? -35.294 48.736  -11.585 1.00 83.28  ? 133 GLU A CB    1 
ATOM   1111 C  CG    . GLU A 1 133 ? -35.546 50.199  -11.881 1.00 87.94  ? 133 GLU A CG    1 
ATOM   1112 C  CD    . GLU A 1 133 ? -36.973 50.608  -11.588 1.00 96.04  ? 133 GLU A CD    1 
ATOM   1113 O  OE1   . GLU A 1 133 ? -37.581 50.042  -10.654 1.00 100.47 ? 133 GLU A OE1   1 
ATOM   1114 O  OE2   . GLU A 1 133 ? -37.488 51.500  -12.289 1.00 97.52  ? 133 GLU A OE2   1 
ATOM   1115 N  N     . GLU A 1 134 ? -36.143 47.203  -8.671  1.00 79.04  ? 134 GLU A N     1 
ATOM   1116 C  CA    . GLU A 1 134 ? -36.745 46.013  -8.088  1.00 87.25  ? 134 GLU A CA    1 
ATOM   1117 C  C     . GLU A 1 134 ? -38.094 45.753  -8.742  1.00 82.31  ? 134 GLU A C     1 
ATOM   1118 O  O     . GLU A 1 134 ? -38.924 46.661  -8.850  1.00 78.99  ? 134 GLU A O     1 
ATOM   1119 C  CB    . GLU A 1 134 ? -36.907 46.162  -6.574  1.00 89.38  ? 134 GLU A CB    1 
ATOM   1120 C  CG    . GLU A 1 134 ? -37.639 45.001  -5.906  1.00 105.59 ? 134 GLU A CG    1 
ATOM   1121 C  CD    . GLU A 1 134 ? -36.752 43.786  -5.671  1.00 113.19 ? 134 GLU A CD    1 
ATOM   1122 O  OE1   . GLU A 1 134 ? -36.058 43.347  -6.614  1.00 97.03  ? 134 GLU A OE1   1 
ATOM   1123 O  OE2   . GLU A 1 134 ? -36.754 43.264  -4.536  1.00 106.06 ? 134 GLU A OE2   1 
ATOM   1124 N  N     . LEU A 1 135 ? -38.303 44.518  -9.181  1.00 77.96  ? 135 LEU A N     1 
ATOM   1125 C  CA    . LEU A 1 135 ? -39.544 44.126  -9.826  1.00 71.87  ? 135 LEU A CA    1 
ATOM   1126 C  C     . LEU A 1 135 ? -40.517 43.557  -8.804  1.00 67.39  ? 135 LEU A C     1 
ATOM   1127 O  O     . LEU A 1 135 ? -40.118 43.006  -7.774  1.00 69.61  ? 135 LEU A O     1 
ATOM   1128 C  CB    . LEU A 1 135 ? -39.280 43.090  -10.920 1.00 63.77  ? 135 LEU A CB    1 
ATOM   1129 C  CG    . LEU A 1 135 ? -37.946 43.196  -11.659 1.00 68.69  ? 135 LEU A CG    1 
ATOM   1130 C  CD1   . LEU A 1 135 ? -37.662 41.922  -12.439 1.00 57.63  ? 135 LEU A CD1   1 
ATOM   1131 C  CD2   . LEU A 1 135 ? -37.946 44.402  -12.583 1.00 72.82  ? 135 LEU A CD2   1 
ATOM   1132 N  N     . LYS A 1 136 ? -41.806 43.703  -9.095  1.00 57.77  ? 136 LYS A N     1 
ATOM   1133 C  CA    . LYS A 1 136 ? -42.847 43.063  -8.306  1.00 60.25  ? 136 LYS A CA    1 
ATOM   1134 C  C     . LYS A 1 136 ? -43.131 41.684  -8.886  1.00 57.35  ? 136 LYS A C     1 
ATOM   1135 O  O     . LYS A 1 136 ? -43.273 41.533  -10.105 1.00 55.36  ? 136 LYS A O     1 
ATOM   1136 C  CB    . LYS A 1 136 ? -44.119 43.911  -8.285  1.00 62.20  ? 136 LYS A CB    1 
ATOM   1137 C  CG    . LYS A 1 136 ? -45.229 43.326  -7.429  1.00 66.49  ? 136 LYS A CG    1 
ATOM   1138 C  CD    . LYS A 1 136 ? -45.981 44.406  -6.671  1.00 82.37  ? 136 LYS A CD    1 
ATOM   1139 C  CE    . LYS A 1 136 ? -47.164 44.917  -7.471  1.00 73.92  ? 136 LYS A CE    1 
ATOM   1140 N  NZ    . LYS A 1 136 ? -48.453 44.764  -6.740  1.00 71.97  ? 136 LYS A NZ    1 
ATOM   1141 N  N     . MET A 1 137 ? -43.202 40.682  -8.016  1.00 53.62  ? 137 MET A N     1 
ATOM   1142 C  CA    . MET A 1 137 ? -43.401 39.305  -8.433  1.00 55.34  ? 137 MET A CA    1 
ATOM   1143 C  C     . MET A 1 137 ? -44.697 38.756  -7.855  1.00 51.93  ? 137 MET A C     1 
ATOM   1144 O  O     . MET A 1 137 ? -45.141 39.161  -6.776  1.00 43.89  ? 137 MET A O     1 
ATOM   1145 C  CB    . MET A 1 137 ? -42.227 38.425  -8.001  1.00 48.16  ? 137 MET A CB    1 
ATOM   1146 C  CG    . MET A 1 137 ? -40.882 38.929  -8.484  1.00 59.06  ? 137 MET A CG    1 
ATOM   1147 S  SD    . MET A 1 137 ? -39.520 37.902  -7.919  1.00 65.54  ? 137 MET A SD    1 
ATOM   1148 C  CE    . MET A 1 137 ? -38.982 38.864  -6.513  1.00 57.72  ? 137 MET A CE    1 
ATOM   1149 N  N     . LEU A 1 138 ? -45.298 37.824  -8.590  1.00 46.53  ? 138 LEU A N     1 
ATOM   1150 C  CA    . LEU A 1 138 ? -46.516 37.148  -8.160  1.00 50.18  ? 138 LEU A CA    1 
ATOM   1151 C  C     . LEU A 1 138 ? -46.403 35.682  -8.539  1.00 46.29  ? 138 LEU A C     1 
ATOM   1152 O  O     . LEU A 1 138 ? -46.278 35.359  -9.723  1.00 42.63  ? 138 LEU A O     1 
ATOM   1153 C  CB    . LEU A 1 138 ? -47.755 37.773  -8.806  1.00 47.54  ? 138 LEU A CB    1 
ATOM   1154 C  CG    . LEU A 1 138 ? -49.096 37.198  -8.355  1.00 49.62  ? 138 LEU A CG    1 
ATOM   1155 C  CD1   . LEU A 1 138 ? -49.330 37.503  -6.885  1.00 53.63  ? 138 LEU A CD1   1 
ATOM   1156 C  CD2   . LEU A 1 138 ? -50.229 37.740  -9.212  1.00 56.00  ? 138 LEU A CD2   1 
ATOM   1157 N  N     . ALA A 1 139 ? -46.423 34.798  -7.550  1.00 43.61  ? 139 ALA A N     1 
ATOM   1158 C  CA    . ALA A 1 139 ? -46.380 33.369  -7.809  1.00 50.81  ? 139 ALA A CA    1 
ATOM   1159 C  C     . ALA A 1 139 ? -47.793 32.805  -7.809  1.00 55.02  ? 139 ALA A C     1 
ATOM   1160 O  O     . ALA A 1 139 ? -48.673 33.301  -7.103  1.00 47.39  ? 139 ALA A O     1 
ATOM   1161 C  CB    . ALA A 1 139 ? -45.533 32.648  -6.762  1.00 49.16  ? 139 ALA A CB    1 
ATOM   1162 N  N     . PHE A 1 140 ? -48.010 31.762  -8.607  1.00 51.85  ? 140 PHE A N     1 
ATOM   1163 C  CA    . PHE A 1 140 ? -49.329 31.142  -8.607  1.00 52.52  ? 140 PHE A CA    1 
ATOM   1164 C  C     . PHE A 1 140 ? -49.236 29.657  -8.927  1.00 50.53  ? 140 PHE A C     1 
ATOM   1165 O  O     . PHE A 1 140 ? -48.307 29.200  -9.598  1.00 47.23  ? 140 PHE A O     1 
ATOM   1166 C  CB    . PHE A 1 140 ? -50.288 31.845  -9.582  1.00 50.96  ? 140 PHE A CB    1 
ATOM   1167 C  CG    . PHE A 1 140 ? -50.069 31.494  -11.028 1.00 51.45  ? 140 PHE A CG    1 
ATOM   1168 C  CD1   . PHE A 1 140 ? -50.744 30.432  -11.612 1.00 52.32  ? 140 PHE A CD1   1 
ATOM   1169 C  CD2   . PHE A 1 140 ? -49.211 32.246  -11.811 1.00 50.24  ? 140 PHE A CD2   1 
ATOM   1170 C  CE1   . PHE A 1 140 ? -50.548 30.113  -12.942 1.00 51.00  ? 140 PHE A CE1   1 
ATOM   1171 C  CE2   . PHE A 1 140 ? -49.014 31.935  -13.144 1.00 52.25  ? 140 PHE A CE2   1 
ATOM   1172 C  CZ    . PHE A 1 140 ? -49.683 30.866  -13.709 1.00 49.30  ? 140 PHE A CZ    1 
ATOM   1173 N  N     . ALA A 1 141 ? -50.225 28.915  -8.432  1.00 55.52  ? 141 ALA A N     1 
ATOM   1174 C  CA    . ALA A 1 141 ? -50.365 27.487  -8.677  1.00 50.69  ? 141 ALA A CA    1 
ATOM   1175 C  C     . ALA A 1 141 ? -51.845 27.158  -8.823  1.00 61.87  ? 141 ALA A C     1 
ATOM   1176 O  O     . ALA A 1 141 ? -52.719 27.962  -8.487  1.00 55.10  ? 141 ALA A O     1 
ATOM   1177 C  CB    . ALA A 1 141 ? -49.733 26.657  -7.555  1.00 42.62  ? 141 ALA A CB    1 
ATOM   1178 N  N     . ILE A 1 142 ? -52.129 25.961  -9.338  1.00 56.48  ? 142 ILE A N     1 
ATOM   1179 C  CA    . ILE A 1 142 ? -53.499 25.512  -9.541  1.00 58.16  ? 142 ILE A CA    1 
ATOM   1180 C  C     . ILE A 1 142 ? -53.661 24.101  -8.992  1.00 59.30  ? 142 ILE A C     1 
ATOM   1181 O  O     . ILE A 1 142 ? -52.697 23.346  -8.845  1.00 60.23  ? 142 ILE A O     1 
ATOM   1182 C  CB    . ILE A 1 142 ? -53.926 25.553  -11.028 1.00 59.44  ? 142 ILE A CB    1 
ATOM   1183 C  CG1   . ILE A 1 142 ? -53.276 24.407  -11.807 1.00 54.72  ? 142 ILE A CG1   1 
ATOM   1184 C  CG2   . ILE A 1 142 ? -53.600 26.903  -11.653 1.00 55.40  ? 142 ILE A CG2   1 
ATOM   1185 C  CD1   . ILE A 1 142 ? -53.440 24.519  -13.307 1.00 60.07  ? 142 ILE A CD1   1 
ATOM   1186 N  N     . ALA A 1 143 ? -54.908 23.757  -8.683  1.00 62.95  ? 143 ALA A N     1 
ATOM   1187 C  CA    . ALA A 1 143 ? -55.292 22.416  -8.268  1.00 65.15  ? 143 ALA A CA    1 
ATOM   1188 C  C     . ALA A 1 143 ? -56.288 21.857  -9.273  1.00 71.51  ? 143 ALA A C     1 
ATOM   1189 O  O     . ALA A 1 143 ? -57.217 22.554  -9.692  1.00 69.05  ? 143 ALA A O     1 
ATOM   1190 C  CB    . ALA A 1 143 ? -55.903 22.419  -6.862  1.00 67.56  ? 143 ALA A CB    1 
ATOM   1191 N  N     . THR A 1 144 ? -56.096 20.598  -9.659  1.00 81.05  ? 144 THR A N     1 
ATOM   1192 C  CA    . THR A 1 144 ? -56.859 20.005  -10.746 1.00 77.94  ? 144 THR A CA    1 
ATOM   1193 C  C     . THR A 1 144 ? -57.560 18.721  -10.322 1.00 74.84  ? 144 THR A C     1 
ATOM   1194 O  O     . THR A 1 144 ? -57.124 18.018  -9.407  1.00 73.15  ? 144 THR A O     1 
ATOM   1195 C  CB    . THR A 1 144 ? -55.970 19.714  -11.956 1.00 80.40  ? 144 THR A CB    1 
ATOM   1196 O  OG1   . THR A 1 144 ? -56.804 19.483  -13.092 1.00 99.79  ? 144 THR A OG1   1 
ATOM   1197 C  CG2   . THR A 1 144 ? -55.083 18.496  -11.712 1.00 81.39  ? 144 THR A CG2   1 
ATOM   1198 N  N     . LEU A 1 145 ? -58.655 18.420  -11.018 1.00 78.46  ? 145 LEU A N     1 
ATOM   1199 C  CA    . LEU A 1 145 ? -59.441 17.218  -10.768 1.00 80.22  ? 145 LEU A CA    1 
ATOM   1200 C  C     . LEU A 1 145 ? -58.926 16.129  -11.697 1.00 79.32  ? 145 LEU A C     1 
ATOM   1201 O  O     . LEU A 1 145 ? -59.166 16.171  -12.908 1.00 78.90  ? 145 LEU A O     1 
ATOM   1202 C  CB    . LEU A 1 145 ? -60.929 17.485  -10.988 1.00 72.78  ? 145 LEU A CB    1 
ATOM   1203 C  CG    . LEU A 1 145 ? -61.943 16.377  -10.669 1.00 83.70  ? 145 LEU A CG    1 
ATOM   1204 C  CD1   . LEU A 1 145 ? -62.241 15.488  -11.876 1.00 80.09  ? 145 LEU A CD1   1 
ATOM   1205 C  CD2   . LEU A 1 145 ? -61.478 15.539  -9.487  1.00 85.90  ? 145 LEU A CD2   1 
ATOM   1206 N  N     . TYR A 1 146 ? -58.217 15.156  -11.134 1.00 79.43  ? 146 TYR A N     1 
ATOM   1207 C  CA    . TYR A 1 146 ? -57.541 14.132  -11.918 1.00 81.07  ? 146 TYR A CA    1 
ATOM   1208 C  C     . TYR A 1 146 ? -58.143 12.770  -11.613 1.00 87.28  ? 146 TYR A C     1 
ATOM   1209 O  O     . TYR A 1 146 ? -58.123 12.319  -10.463 1.00 87.80  ? 146 TYR A O     1 
ATOM   1210 C  CB    . TYR A 1 146 ? -56.036 14.127  -11.633 1.00 86.54  ? 146 TYR A CB    1 
ATOM   1211 C  CG    . TYR A 1 146 ? -55.310 12.972  -12.282 1.00 85.74  ? 146 TYR A CG    1 
ATOM   1212 C  CD1   . TYR A 1 146 ? -54.977 13.006  -13.630 1.00 88.02  ? 146 TYR A CD1   1 
ATOM   1213 C  CD2   . TYR A 1 146 ? -54.965 11.842  -11.550 1.00 82.43  ? 146 TYR A CD2   1 
ATOM   1214 C  CE1   . TYR A 1 146 ? -54.317 11.948  -14.231 1.00 90.95  ? 146 TYR A CE1   1 
ATOM   1215 C  CE2   . TYR A 1 146 ? -54.307 10.780  -12.142 1.00 83.50  ? 146 TYR A CE2   1 
ATOM   1216 C  CZ    . TYR A 1 146 ? -53.985 10.838  -13.482 1.00 90.48  ? 146 TYR A CZ    1 
ATOM   1217 O  OH    . TYR A 1 146 ? -53.329 9.781   -14.070 1.00 90.94  ? 146 TYR A OH    1 
ATOM   1218 N  N     . HIS A 1 147 ? -58.687 12.129  -12.641 1.00 97.12  ? 147 HIS A N     1 
ATOM   1219 C  CA    . HIS A 1 147 ? -58.952 10.699  -12.639 1.00 101.62 ? 147 HIS A CA    1 
ATOM   1220 C  C     . HIS A 1 147 ? -58.006 10.041  -13.632 1.00 104.81 ? 147 HIS A C     1 
ATOM   1221 O  O     . HIS A 1 147 ? -57.748 10.585  -14.710 1.00 102.96 ? 147 HIS A O     1 
ATOM   1222 C  CB    . HIS A 1 147 ? -60.406 10.380  -13.010 1.00 96.33  ? 147 HIS A CB    1 
ATOM   1223 C  CG    . HIS A 1 147 ? -61.407 10.842  -11.997 1.00 96.53  ? 147 HIS A CG    1 
ATOM   1224 N  ND1   . HIS A 1 147 ? -62.283 11.880  -12.233 1.00 95.40  ? 147 HIS A ND1   1 
ATOM   1225 C  CD2   . HIS A 1 147 ? -61.669 10.406  -10.742 1.00 98.63  ? 147 HIS A CD2   1 
ATOM   1226 C  CE1   . HIS A 1 147 ? -63.043 12.061  -11.168 1.00 102.04 ? 147 HIS A CE1   1 
ATOM   1227 N  NE2   . HIS A 1 147 ? -62.690 11.181  -10.249 1.00 104.59 ? 147 HIS A NE2   1 
ATOM   1228 N  N     . GLU A 1 148 ? -57.472 8.883   -13.260 1.00 109.18 ? 148 GLU A N     1 
ATOM   1229 C  CA    . GLU A 1 148 ? -56.565 8.168   -14.147 1.00 105.06 ? 148 GLU A CA    1 
ATOM   1230 C  C     . GLU A 1 148 ? -57.331 7.620   -15.346 1.00 110.74 ? 148 GLU A C     1 
ATOM   1231 O  O     . GLU A 1 148 ? -58.362 6.958   -15.190 1.00 105.25 ? 148 GLU A O     1 
ATOM   1232 C  CB    . GLU A 1 148 ? -55.869 7.040   -13.386 1.00 111.31 ? 148 GLU A CB    1 
ATOM   1233 C  CG    . GLU A 1 148 ? -54.647 6.467   -14.078 1.00 108.73 ? 148 GLU A CG    1 
ATOM   1234 C  CD    . GLU A 1 148 ? -54.630 4.953   -14.036 1.00 121.66 ? 148 GLU A CD    1 
ATOM   1235 O  OE1   . GLU A 1 148 ? -54.381 4.322   -15.083 1.00 124.18 ? 148 GLU A OE1   1 
ATOM   1236 O  OE2   . GLU A 1 148 ? -54.870 4.392   -12.947 1.00 125.94 ? 148 GLU A OE2   1 
ATOM   1237 N  N     . GLY A 1 149 ? -56.837 7.916   -16.552 1.00 107.28 ? 149 GLY A N     1 
ATOM   1238 C  CA    . GLY A 1 149 ? -57.429 7.453   -17.788 1.00 101.97 ? 149 GLY A CA    1 
ATOM   1239 C  C     . GLY A 1 149 ? -57.971 8.563   -18.667 1.00 107.95 ? 149 GLY A C     1 
ATOM   1240 O  O     . GLY A 1 149 ? -58.047 8.388   -19.890 1.00 105.88 ? 149 GLY A O     1 
ATOM   1241 N  N     . GLU A 1 150 ? -58.353 9.694   -18.075 1.00 122.06 ? 150 GLU A N     1 
ATOM   1242 C  CA    . GLU A 1 150 ? -58.883 10.793  -18.868 1.00 113.31 ? 150 GLU A CA    1 
ATOM   1243 C  C     . GLU A 1 150 ? -57.786 11.408  -19.735 1.00 104.95 ? 150 GLU A C     1 
ATOM   1244 O  O     . GLU A 1 150 ? -56.594 11.144  -19.563 1.00 108.86 ? 150 GLU A O     1 
ATOM   1245 C  CB    . GLU A 1 150 ? -59.491 11.886  -17.984 1.00 116.84 ? 150 GLU A CB    1 
ATOM   1246 C  CG    . GLU A 1 150 ? -60.178 11.431  -16.709 1.00 121.30 ? 150 GLU A CG    1 
ATOM   1247 C  CD    . GLU A 1 150 ? -60.640 12.607  -15.872 1.00 126.89 ? 150 GLU A CD    1 
ATOM   1248 O  OE1   . GLU A 1 150 ? -60.090 12.818  -14.768 1.00 125.10 ? 150 GLU A OE1   1 
ATOM   1249 O  OE2   . GLU A 1 150 ? -61.568 13.311  -16.322 1.00 129.89 ? 150 GLU A OE2   1 
ATOM   1250 N  N     . GLU A 1 151 ? -58.207 12.250  -20.675 1.00 100.11 ? 151 GLU A N     1 
ATOM   1251 C  CA    . GLU A 1 151 ? -57.269 13.060  -21.433 1.00 98.01  ? 151 GLU A CA    1 
ATOM   1252 C  C     . GLU A 1 151 ? -56.863 14.284  -20.614 1.00 95.35  ? 151 GLU A C     1 
ATOM   1253 O  O     . GLU A 1 151 ? -57.331 14.500  -19.492 1.00 91.58  ? 151 GLU A O     1 
ATOM   1254 C  CB    . GLU A 1 151 ? -57.871 13.467  -22.776 1.00 98.96  ? 151 GLU A CB    1 
ATOM   1255 C  CG    . GLU A 1 151 ? -58.818 12.442  -23.378 1.00 106.04 ? 151 GLU A CG    1 
ATOM   1256 C  CD    . GLU A 1 151 ? -59.573 12.987  -24.573 1.00 108.31 ? 151 GLU A CD    1 
ATOM   1257 O  OE1   . GLU A 1 151 ? -59.579 12.333  -25.639 1.00 113.02 ? 151 GLU A OE1   1 
ATOM   1258 O  OE2   . GLU A 1 151 ? -60.165 14.077  -24.438 1.00 110.00 ? 151 GLU A OE2   1 
ATOM   1259 N  N     . PHE A 1 152 ? -55.982 15.099  -21.187 1.00 94.79  ? 152 PHE A N     1 
ATOM   1260 C  CA    . PHE A 1 152 ? -55.450 16.250  -20.472 1.00 86.64  ? 152 PHE A CA    1 
ATOM   1261 C  C     . PHE A 1 152 ? -56.504 17.346  -20.365 1.00 81.85  ? 152 PHE A C     1 
ATOM   1262 O  O     . PHE A 1 152 ? -57.193 17.659  -21.341 1.00 84.40  ? 152 PHE A O     1 
ATOM   1263 C  CB    . PHE A 1 152 ? -54.202 16.776  -21.179 1.00 82.17  ? 152 PHE A CB    1 
ATOM   1264 C  CG    . PHE A 1 152 ? -53.609 17.997  -20.535 1.00 81.70  ? 152 PHE A CG    1 
ATOM   1265 C  CD1   . PHE A 1 152 ? -52.893 17.895  -19.354 1.00 84.40  ? 152 PHE A CD1   1 
ATOM   1266 C  CD2   . PHE A 1 152 ? -53.764 19.246  -21.113 1.00 79.78  ? 152 PHE A CD2   1 
ATOM   1267 C  CE1   . PHE A 1 152 ? -52.346 19.015  -18.759 1.00 73.60  ? 152 PHE A CE1   1 
ATOM   1268 C  CE2   . PHE A 1 152 ? -53.219 20.371  -20.522 1.00 75.52  ? 152 PHE A CE2   1 
ATOM   1269 C  CZ    . PHE A 1 152 ? -52.509 20.255  -19.343 1.00 71.95  ? 152 PHE A CZ    1 
ATOM   1270 N  N     . ALA A 1 153 ? -56.634 17.910  -19.163 1.00 81.39  ? 153 ALA A N     1 
ATOM   1271 C  CA    . ALA A 1 153 ? -57.486 19.069  -18.896 1.00 80.18  ? 153 ALA A CA    1 
ATOM   1272 C  C     . ALA A 1 153 ? -58.966 18.766  -19.113 1.00 87.02  ? 153 ALA A C     1 
ATOM   1273 O  O     . ALA A 1 153 ? -59.752 19.666  -19.418 1.00 82.41  ? 153 ALA A O     1 
ATOM   1274 C  CB    . ALA A 1 153 ? -57.062 20.279  -19.733 1.00 78.83  ? 153 ALA A CB    1 
ATOM   1275 N  N     . GLU A 1 154 ? -59.367 17.502  -18.958 1.00 83.15  ? 154 GLU A N     1 
ATOM   1276 C  CA    . GLU A 1 154 ? -60.793 17.195  -18.958 1.00 102.32 ? 154 GLU A CA    1 
ATOM   1277 C  C     . GLU A 1 154 ? -61.464 17.721  -17.698 1.00 96.20  ? 154 GLU A C     1 
ATOM   1278 O  O     . GLU A 1 154 ? -62.466 18.442  -17.770 1.00 83.13  ? 154 GLU A O     1 
ATOM   1279 C  CB    . GLU A 1 154 ? -61.028 15.691  -19.088 1.00 110.33 ? 154 GLU A CB    1 
ATOM   1280 C  CG    . GLU A 1 154 ? -61.592 15.288  -20.437 1.00 116.56 ? 154 GLU A CG    1 
ATOM   1281 C  CD    . GLU A 1 154 ? -61.515 13.802  -20.688 1.00 120.32 ? 154 GLU A CD    1 
ATOM   1282 O  OE1   . GLU A 1 154 ? -61.757 13.031  -19.736 1.00 121.09 ? 154 GLU A OE1   1 
ATOM   1283 O  OE2   . GLU A 1 154 ? -61.252 13.403  -21.840 1.00 128.63 ? 154 GLU A OE2   1 
ATOM   1284 N  N     . GLY A 1 155 ? -60.937 17.351  -16.535 1.00 87.30  ? 155 GLY A N     1 
ATOM   1285 C  CA    . GLY A 1 155 ? -61.440 17.848  -15.280 1.00 77.55  ? 155 GLY A CA    1 
ATOM   1286 C  C     . GLY A 1 155 ? -61.198 19.336  -15.136 1.00 81.85  ? 155 GLY A C     1 
ATOM   1287 O  O     . GLY A 1 155 ? -60.258 19.895  -15.710 1.00 77.04  ? 155 GLY A O     1 
ATOM   1288 N  N     . PRO A 1 156 ? -62.048 20.008  -14.370 1.00 82.80  ? 156 PRO A N     1 
ATOM   1289 C  CA    . PRO A 1 156 ? -61.906 21.454  -14.191 1.00 71.89  ? 156 PRO A CA    1 
ATOM   1290 C  C     . PRO A 1 156 ? -60.830 21.784  -13.164 1.00 74.41  ? 156 PRO A C     1 
ATOM   1291 O  O     . PRO A 1 156 ? -60.331 20.924  -12.438 1.00 72.32  ? 156 PRO A O     1 
ATOM   1292 C  CB    . PRO A 1 156 ? -63.291 21.877  -13.695 1.00 70.31  ? 156 PRO A CB    1 
ATOM   1293 C  CG    . PRO A 1 156 ? -63.776 20.683  -12.942 1.00 69.71  ? 156 PRO A CG    1 
ATOM   1294 C  CD    . PRO A 1 156 ? -63.229 19.476  -13.667 1.00 69.24  ? 156 PRO A CD    1 
ATOM   1295 N  N     . ILE A 1 157 ? -60.472 23.064  -13.123 1.00 73.89  ? 157 ILE A N     1 
ATOM   1296 C  CA    . ILE A 1 157 ? -59.597 23.572  -12.074 1.00 66.40  ? 157 ILE A CA    1 
ATOM   1297 C  C     . ILE A 1 157 ? -60.440 23.839  -10.835 1.00 68.39  ? 157 ILE A C     1 
ATOM   1298 O  O     . ILE A 1 157 ? -61.514 24.447  -10.920 1.00 70.87  ? 157 ILE A O     1 
ATOM   1299 C  CB    . ILE A 1 157 ? -58.862 24.842  -12.532 1.00 64.07  ? 157 ILE A CB    1 
ATOM   1300 C  CG1   . ILE A 1 157 ? -57.969 24.552  -13.738 1.00 64.28  ? 157 ILE A CG1   1 
ATOM   1301 C  CG2   . ILE A 1 157 ? -58.025 25.411  -11.400 1.00 63.38  ? 157 ILE A CG2   1 
ATOM   1302 C  CD1   . ILE A 1 157 ? -57.912 25.690  -14.729 1.00 61.77  ? 157 ILE A CD1   1 
ATOM   1303 N  N     . LEU A 1 158 ? -59.963 23.377  -9.682  1.00 66.32  ? 158 LEU A N     1 
ATOM   1304 C  CA    . LEU A 1 158 ? -60.700 23.507  -8.429  1.00 66.04  ? 158 LEU A CA    1 
ATOM   1305 C  C     . LEU A 1 158 ? -60.306 24.761  -7.664  1.00 69.26  ? 158 LEU A C     1 
ATOM   1306 O  O     . LEU A 1 158 ? -61.172 25.525  -7.228  1.00 64.40  ? 158 LEU A O     1 
ATOM   1307 C  CB    . LEU A 1 158 ? -60.483 22.273  -7.542  1.00 70.59  ? 158 LEU A CB    1 
ATOM   1308 C  CG    . LEU A 1 158 ? -60.954 20.886  -7.990  1.00 75.67  ? 158 LEU A CG    1 
ATOM   1309 C  CD1   . LEU A 1 158 ? -60.244 20.440  -9.229  1.00 75.13  ? 158 LEU A CD1   1 
ATOM   1310 C  CD2   . LEU A 1 158 ? -60.704 19.877  -6.886  1.00 73.96  ? 158 LEU A CD2   1 
ATOM   1311 N  N     . MET A 1 159 ? -59.008 24.977  -7.480  1.00 64.91  ? 159 MET A N     1 
ATOM   1312 C  CA    . MET A 1 159 ? -58.504 26.147  -6.781  1.00 62.75  ? 159 MET A CA    1 
ATOM   1313 C  C     . MET A 1 159 ? -57.368 26.765  -7.578  1.00 60.41  ? 159 MET A C     1 
ATOM   1314 O  O     . MET A 1 159 ? -56.589 26.057  -8.222  1.00 64.57  ? 159 MET A O     1 
ATOM   1315 C  CB    . MET A 1 159 ? -58.018 25.797  -5.369  1.00 62.24  ? 159 MET A CB    1 
ATOM   1316 C  CG    . MET A 1 159 ? -58.755 24.642  -4.712  1.00 59.64  ? 159 MET A CG    1 
ATOM   1317 S  SD    . MET A 1 159 ? -57.984 24.151  -3.161  1.00 64.80  ? 159 MET A SD    1 
ATOM   1318 C  CE    . MET A 1 159 ? -59.407 23.565  -2.247  1.00 60.91  ? 159 MET A CE    1 
ATOM   1319 N  N     . ILE A 1 160 ? -57.295 28.089  -7.544  1.00 59.20  ? 160 ILE A N     1 
ATOM   1320 C  CA    . ILE A 1 160 ? -56.166 28.840  -8.081  1.00 59.28  ? 160 ILE A CA    1 
ATOM   1321 C  C     . ILE A 1 160 ? -55.595 29.660  -6.936  1.00 58.71  ? 160 ILE A C     1 
ATOM   1322 O  O     . ILE A 1 160 ? -56.291 30.508  -6.367  1.00 60.11  ? 160 ILE A O     1 
ATOM   1323 C  CB    . ILE A 1 160 ? -56.571 29.739  -9.259  1.00 59.72  ? 160 ILE A CB    1 
ATOM   1324 C  CG1   . ILE A 1 160 ? -57.025 28.887  -10.447 1.00 58.23  ? 160 ILE A CG1   1 
ATOM   1325 C  CG2   . ILE A 1 160 ? -55.414 30.649  -9.658  1.00 57.23  ? 160 ILE A CG2   1 
ATOM   1326 C  CD1   . ILE A 1 160 ? -57.584 29.696  -11.599 1.00 55.08  ? 160 ILE A CD1   1 
ATOM   1327 N  N     . SER A 1 161 ? -54.349 29.387  -6.572  1.00 55.31  ? 161 SER A N     1 
ATOM   1328 C  CA    . SER A 1 161 ? -53.704 30.058  -5.455  1.00 52.74  ? 161 SER A CA    1 
ATOM   1329 C  C     . SER A 1 161 ? -52.625 30.996  -5.975  1.00 57.28  ? 161 SER A C     1 
ATOM   1330 O  O     . SER A 1 161 ? -51.953 30.695  -6.965  1.00 55.13  ? 161 SER A O     1 
ATOM   1331 C  CB    . SER A 1 161 ? -53.101 29.044  -4.479  1.00 54.32  ? 161 SER A CB    1 
ATOM   1332 O  OG    . SER A 1 161 ? -52.168 28.199  -5.129  1.00 57.44  ? 161 SER A OG    1 
ATOM   1333 N  N     . TYR A 1 162 ? -52.476 32.138  -5.310  1.00 55.01  ? 162 TYR A N     1 
ATOM   1334 C  CA    . TYR A 1 162 ? -51.427 33.089  -5.639  1.00 51.57  ? 162 TYR A CA    1 
ATOM   1335 C  C     . TYR A 1 162 ? -50.770 33.572  -4.354  1.00 56.11  ? 162 TYR A C     1 
ATOM   1336 O  O     . TYR A 1 162 ? -51.301 33.401  -3.254  1.00 52.90  ? 162 TYR A O     1 
ATOM   1337 C  CB    . TYR A 1 162 ? -51.960 34.277  -6.457  1.00 55.74  ? 162 TYR A CB    1 
ATOM   1338 C  CG    . TYR A 1 162 ? -53.043 35.077  -5.772  1.00 60.15  ? 162 TYR A CG    1 
ATOM   1339 C  CD1   . TYR A 1 162 ? -54.380 34.723  -5.902  1.00 63.28  ? 162 TYR A CD1   1 
ATOM   1340 C  CD2   . TYR A 1 162 ? -52.732 36.196  -5.010  1.00 58.58  ? 162 TYR A CD2   1 
ATOM   1341 C  CE1   . TYR A 1 162 ? -55.377 35.453  -5.282  1.00 64.37  ? 162 TYR A CE1   1 
ATOM   1342 C  CE2   . TYR A 1 162 ? -53.723 36.934  -4.386  1.00 60.26  ? 162 TYR A CE2   1 
ATOM   1343 C  CZ    . TYR A 1 162 ? -55.044 36.558  -4.526  1.00 66.38  ? 162 TYR A CZ    1 
ATOM   1344 O  OH    . TYR A 1 162 ? -56.033 37.287  -3.908  1.00 64.77  ? 162 TYR A OH    1 
ATOM   1345 N  N     . ALA A 1 163 ? -49.590 34.165  -4.511  1.00 54.59  ? 163 ALA A N     1 
ATOM   1346 C  CA    . ALA A 1 163 ? -48.798 34.597  -3.369  1.00 55.38  ? 163 ALA A CA    1 
ATOM   1347 C  C     . ALA A 1 163 ? -47.847 35.704  -3.797  1.00 59.35  ? 163 ALA A C     1 
ATOM   1348 O  O     . ALA A 1 163 ? -47.331 35.696  -4.920  1.00 57.17  ? 163 ALA A O     1 
ATOM   1349 C  CB    . ALA A 1 163 ? -48.011 33.430  -2.761  1.00 46.54  ? 163 ALA A CB    1 
ATOM   1350 N  N     . ASP A 1 164 ? -47.629 36.657  -2.894  1.00 63.46  ? 164 ASP A N     1 
ATOM   1351 C  CA    . ASP A 1 164 ? -46.647 37.712  -3.104  1.00 57.96  ? 164 ASP A CA    1 
ATOM   1352 C  C     . ASP A 1 164 ? -46.128 38.221  -1.766  1.00 68.66  ? 164 ASP A C     1 
ATOM   1353 O  O     . ASP A 1 164 ? -46.080 37.471  -0.785  1.00 68.33  ? 164 ASP A O     1 
ATOM   1354 C  CB    . ASP A 1 164 ? -47.241 38.856  -3.932  1.00 58.65  ? 164 ASP A CB    1 
ATOM   1355 C  CG    . ASP A 1 164 ? -48.465 39.486  -3.284  1.00 68.13  ? 164 ASP A CG    1 
ATOM   1356 O  OD1   . ASP A 1 164 ? -48.812 39.124  -2.138  1.00 73.04  ? 164 ASP A OD1   1 
ATOM   1357 O  OD2   . ASP A 1 164 ? -49.083 40.358  -3.928  1.00 68.58  ? 164 ASP A OD2   1 
ATOM   1358 N  N     . GLU A 1 165 ? -45.746 39.497  -1.711  1.00 72.40  ? 165 GLU A N     1 
ATOM   1359 C  CA    . GLU A 1 165 ? -45.265 40.064  -0.459  1.00 78.22  ? 165 GLU A CA    1 
ATOM   1360 C  C     . GLU A 1 165 ? -46.380 40.240  0.563   1.00 81.33  ? 165 GLU A C     1 
ATOM   1361 O  O     . GLU A 1 165 ? -46.096 40.321  1.762   1.00 83.12  ? 165 GLU A O     1 
ATOM   1362 C  CB    . GLU A 1 165 ? -44.577 41.404  -0.719  1.00 80.40  ? 165 GLU A CB    1 
ATOM   1363 C  CG    . GLU A 1 165 ? -43.362 41.667  0.162   1.00 91.42  ? 165 GLU A CG    1 
ATOM   1364 C  CD    . GLU A 1 165 ? -42.340 40.543  0.118   1.00 96.36  ? 165 GLU A CD    1 
ATOM   1365 O  OE1   . GLU A 1 165 ? -42.450 39.597  0.928   1.00 109.20 ? 165 GLU A OE1   1 
ATOM   1366 O  OE2   . GLU A 1 165 ? -41.427 40.605  -0.731  1.00 107.18 ? 165 GLU A OE2   1 
ATOM   1367 N  N     . GLU A 1 166 ? -47.636 40.292  0.123   1.00 76.51  ? 166 GLU A N     1 
ATOM   1368 C  CA    . GLU A 1 166 ? -48.757 40.514  1.026   1.00 80.61  ? 166 GLU A CA    1 
ATOM   1369 C  C     . GLU A 1 166 ? -49.279 39.233  1.663   1.00 75.17  ? 166 GLU A C     1 
ATOM   1370 O  O     . GLU A 1 166 ? -50.051 39.308  2.625   1.00 74.79  ? 166 GLU A O     1 
ATOM   1371 C  CB    . GLU A 1 166 ? -49.904 41.213  0.284   1.00 80.23  ? 166 GLU A CB    1 
ATOM   1372 C  CG    . GLU A 1 166 ? -49.496 42.396  -0.608  1.00 93.21  ? 166 GLU A CG    1 
ATOM   1373 C  CD    . GLU A 1 166 ? -48.580 43.414  0.067   1.00 113.25 ? 166 GLU A CD    1 
ATOM   1374 O  OE1   . GLU A 1 166 ? -48.565 43.508  1.314   1.00 120.63 ? 166 GLU A OE1   1 
ATOM   1375 O  OE2   . GLU A 1 166 ? -47.861 44.127  -0.667  1.00 117.02 ? 166 GLU A OE2   1 
ATOM   1376 N  N     . GLY A 1 167 ? -48.891 38.068  1.154   1.00 71.77  ? 167 GLY A N     1 
ATOM   1377 C  CA    . GLY A 1 167 ? -49.330 36.795  1.677   1.00 69.08  ? 167 GLY A CA    1 
ATOM   1378 C  C     . GLY A 1 167 ? -49.818 35.894  0.567   1.00 66.69  ? 167 GLY A C     1 
ATOM   1379 O  O     . GLY A 1 167 ? -49.619 36.161  -0.623  1.00 64.54  ? 167 GLY A O     1 
ATOM   1380 N  N     . ALA A 1 168 ? -50.473 34.805  0.961   1.00 60.15  ? 168 ALA A N     1 
ATOM   1381 C  CA    . ALA A 1 168 ? -50.972 33.806  0.029   1.00 62.85  ? 168 ALA A CA    1 
ATOM   1382 C  C     . ALA A 1 168 ? -52.489 33.717  0.128   1.00 62.18  ? 168 ALA A C     1 
ATOM   1383 O  O     . ALA A 1 168 ? -53.058 33.829  1.218   1.00 62.80  ? 168 ALA A O     1 
ATOM   1384 C  CB    . ALA A 1 168 ? -50.346 32.433  0.301   1.00 58.44  ? 168 ALA A CB    1 
ATOM   1385 N  N     . ARG A 1 169 ? -53.139 33.519  -1.017  1.00 57.44  ? 169 ARG A N     1 
ATOM   1386 C  CA    . ARG A 1 169 ? -54.590 33.419  -1.076  1.00 63.94  ? 169 ARG A CA    1 
ATOM   1387 C  C     . ARG A 1 169 ? -54.993 32.344  -2.075  1.00 57.84  ? 169 ARG A C     1 
ATOM   1388 O  O     . ARG A 1 169 ? -54.341 32.147  -3.102  1.00 57.63  ? 169 ARG A O     1 
ATOM   1389 C  CB    . ARG A 1 169 ? -55.239 34.756  -1.464  1.00 66.86  ? 169 ARG A CB    1 
ATOM   1390 C  CG    . ARG A 1 169 ? -55.086 35.851  -0.422  1.00 64.68  ? 169 ARG A CG    1 
ATOM   1391 C  CD    . ARG A 1 169 ? -56.161 36.915  -0.576  1.00 71.22  ? 169 ARG A CD    1 
ATOM   1392 N  NE    . ARG A 1 169 ? -57.470 36.452  -0.127  1.00 61.05  ? 169 ARG A NE    1 
ATOM   1393 C  CZ    . ARG A 1 169 ? -57.822 36.313  1.144   1.00 66.82  ? 169 ARG A CZ    1 
ATOM   1394 N  NH1   . ARG A 1 169 ? -56.983 36.590  2.129   1.00 64.07  ? 169 ARG A NH1   1 
ATOM   1395 N  NH2   . ARG A 1 169 ? -59.049 35.890  1.435   1.00 68.48  ? 169 ARG A NH2   1 
ATOM   1396 N  N     . VAL A 1 170 ? -56.084 31.652  -1.760  1.00 59.11  ? 170 VAL A N     1 
ATOM   1397 C  CA    . VAL A 1 170 ? -56.660 30.624  -2.618  1.00 59.85  ? 170 VAL A CA    1 
ATOM   1398 C  C     . VAL A 1 170 ? -58.007 31.126  -3.118  1.00 66.66  ? 170 VAL A C     1 
ATOM   1399 O  O     . VAL A 1 170 ? -58.721 31.822  -2.391  1.00 60.57  ? 170 VAL A O     1 
ATOM   1400 C  CB    . VAL A 1 170 ? -56.811 29.290  -1.857  1.00 63.08  ? 170 VAL A CB    1 
ATOM   1401 C  CG1   . VAL A 1 170 ? -57.415 28.214  -2.751  1.00 59.14  ? 170 VAL A CG1   1 
ATOM   1402 C  CG2   . VAL A 1 170 ? -55.468 28.839  -1.303  1.00 60.65  ? 170 VAL A CG2   1 
ATOM   1403 N  N     . ILE A 1 171 ? -58.345 30.795  -4.362  1.00 65.34  ? 171 ILE A N     1 
ATOM   1404 C  CA    . ILE A 1 171 ? -59.652 31.085  -4.940  1.00 58.83  ? 171 ILE A CA    1 
ATOM   1405 C  C     . ILE A 1 171 ? -60.273 29.764  -5.358  1.00 70.30  ? 171 ILE A C     1 
ATOM   1406 O  O     . ILE A 1 171 ? -59.653 28.997  -6.104  1.00 72.11  ? 171 ILE A O     1 
ATOM   1407 C  CB    . ILE A 1 171 ? -59.548 32.033  -6.149  1.00 60.90  ? 171 ILE A CB    1 
ATOM   1408 C  CG1   . ILE A 1 171 ? -58.822 33.322  -5.771  1.00 61.62  ? 171 ILE A CG1   1 
ATOM   1409 C  CG2   . ILE A 1 171 ? -60.931 32.338  -6.705  1.00 65.72  ? 171 ILE A CG2   1 
ATOM   1410 C  CD1   . ILE A 1 171 ? -58.274 34.069  -6.965  1.00 58.08  ? 171 ILE A CD1   1 
ATOM   1411 N  N     . THR A 1 172 ? -61.491 29.499  -4.891  1.00 68.35  ? 172 THR A N     1 
ATOM   1412 C  CA    . THR A 1 172 ? -62.132 28.230  -5.215  1.00 69.48  ? 172 THR A CA    1 
ATOM   1413 C  C     . THR A 1 172 ? -63.638 28.425  -5.326  1.00 72.55  ? 172 THR A C     1 
ATOM   1414 O  O     . THR A 1 172 ? -64.202 29.374  -4.778  1.00 71.10  ? 172 THR A O     1 
ATOM   1415 C  CB    . THR A 1 172 ? -61.803 27.154  -4.172  1.00 65.96  ? 172 THR A CB    1 
ATOM   1416 O  OG1   . THR A 1 172 ? -62.445 25.924  -4.529  1.00 74.28  ? 172 THR A OG1   1 
ATOM   1417 C  CG2   . THR A 1 172 ? -62.279 27.585  -2.799  1.00 67.89  ? 172 THR A CG2   1 
ATOM   1418 N  N     . TRP A 1 173 ? -64.288 27.509  -6.050  1.00 69.22  ? 173 TRP A N     1 
ATOM   1419 C  CA    . TRP A 1 173 ? -65.732 27.563  -6.253  1.00 78.21  ? 173 TRP A CA    1 
ATOM   1420 C  C     . TRP A 1 173 ? -66.483 26.535  -5.409  1.00 81.57  ? 173 TRP A C     1 
ATOM   1421 O  O     . TRP A 1 173 ? -67.584 26.111  -5.779  1.00 73.16  ? 173 TRP A O     1 
ATOM   1422 C  CB    . TRP A 1 173 ? -66.086 27.411  -7.735  1.00 77.31  ? 173 TRP A CB    1 
ATOM   1423 C  CG    . TRP A 1 173 ? -65.510 26.213  -8.437  1.00 78.65  ? 173 TRP A CG    1 
ATOM   1424 C  CD1   . TRP A 1 173 ? -64.195 25.973  -8.714  1.00 75.37  ? 173 TRP A CD1   1 
ATOM   1425 C  CD2   . TRP A 1 173 ? -66.241 25.108  -8.986  1.00 81.32  ? 173 TRP A CD2   1 
ATOM   1426 N  NE1   . TRP A 1 173 ? -64.061 24.781  -9.386  1.00 76.26  ? 173 TRP A NE1   1 
ATOM   1427 C  CE2   . TRP A 1 173 ? -65.303 24.232  -9.567  1.00 80.58  ? 173 TRP A CE2   1 
ATOM   1428 C  CE3   . TRP A 1 173 ? -67.598 24.772  -9.035  1.00 76.56  ? 173 TRP A CE3   1 
ATOM   1429 C  CZ2   . TRP A 1 173 ? -65.678 23.041  -10.189 1.00 82.71  ? 173 TRP A CZ2   1 
ATOM   1430 C  CZ3   . TRP A 1 173 ? -67.968 23.590  -9.651  1.00 75.26  ? 173 TRP A CZ3   1 
ATOM   1431 C  CH2   . TRP A 1 173 ? -67.011 22.738  -10.218 1.00 81.91  ? 173 TRP A CH2   1 
ATOM   1432 N  N     . LYS A 1 174 ? -65.906 26.129  -4.279  1.00 79.98  ? 174 LYS A N     1 
ATOM   1433 C  CA    . LYS A 1 174 ? -66.624 25.437  -3.217  1.00 82.66  ? 174 LYS A CA    1 
ATOM   1434 C  C     . LYS A 1 174 ? -66.281 26.090  -1.887  1.00 80.49  ? 174 LYS A C     1 
ATOM   1435 O  O     . LYS A 1 174 ? -65.187 26.633  -1.706  1.00 85.80  ? 174 LYS A O     1 
ATOM   1436 C  CB    . LYS A 1 174 ? -66.297 23.937  -3.161  1.00 82.52  ? 174 LYS A CB    1 
ATOM   1437 C  CG    . LYS A 1 174 ? -67.047 23.101  -4.179  1.00 85.39  ? 174 LYS A CG    1 
ATOM   1438 C  CD    . LYS A 1 174 ? -67.854 21.987  -3.553  1.00 94.55  ? 174 LYS A CD    1 
ATOM   1439 C  CE    . LYS A 1 174 ? -69.015 21.599  -4.450  1.00 104.83 ? 174 LYS A CE    1 
ATOM   1440 N  NZ    . LYS A 1 174 ? -69.700 20.377  -3.963  1.00 104.62 ? 174 LYS A NZ    1 
ATOM   1441 N  N     . ASN A 1 175 ? -67.223 26.020  -0.954  1.00 78.38  ? 175 ASN A N     1 
ATOM   1442 C  CA    . ASN A 1 175 ? -67.098 26.749  0.300   1.00 83.25  ? 175 ASN A CA    1 
ATOM   1443 C  C     . ASN A 1 175 ? -66.072 26.072  1.201   1.00 83.09  ? 175 ASN A C     1 
ATOM   1444 O  O     . ASN A 1 175 ? -66.208 24.890  1.534   1.00 83.87  ? 175 ASN A O     1 
ATOM   1445 C  CB    . ASN A 1 175 ? -68.457 26.830  0.991   1.00 84.97  ? 175 ASN A CB    1 
ATOM   1446 C  CG    . ASN A 1 175 ? -68.363 27.351  2.411   1.00 91.13  ? 175 ASN A CG    1 
ATOM   1447 O  OD1   . ASN A 1 175 ? -67.460 28.117  2.747   1.00 100.24 ? 175 ASN A OD1   1 
ATOM   1448 N  ND2   . ASN A 1 175 ? -69.300 26.935  3.255   1.00 99.43  ? 175 ASN A ND2   1 
ATOM   1449 N  N     . VAL A 1 176 ? -65.038 26.821  1.580   1.00 81.11  ? 176 VAL A N     1 
ATOM   1450 C  CA    . VAL A 1 176 ? -64.071 26.409  2.589   1.00 77.23  ? 176 VAL A CA    1 
ATOM   1451 C  C     . VAL A 1 176 ? -63.955 27.542  3.599   1.00 80.83  ? 176 VAL A C     1 
ATOM   1452 O  O     . VAL A 1 176 ? -63.827 28.709  3.213   1.00 85.08  ? 176 VAL A O     1 
ATOM   1453 C  CB    . VAL A 1 176 ? -62.693 26.084  1.978   1.00 74.49  ? 176 VAL A CB    1 
ATOM   1454 C  CG1   . VAL A 1 176 ? -61.714 25.671  3.065   1.00 76.69  ? 176 VAL A CG1   1 
ATOM   1455 C  CG2   . VAL A 1 176 ? -62.817 24.993  0.926   1.00 69.28  ? 176 VAL A CG2   1 
ATOM   1456 N  N     . ASP A 1 177 ? -64.012 27.205  4.887   1.00 83.44  ? 177 ASP A N     1 
ATOM   1457 C  CA    . ASP A 1 177 ? -63.976 28.210  5.950   1.00 91.24  ? 177 ASP A CA    1 
ATOM   1458 C  C     . ASP A 1 177 ? -62.531 28.396  6.395   1.00 83.31  ? 177 ASP A C     1 
ATOM   1459 O  O     . ASP A 1 177 ? -62.047 27.730  7.311   1.00 83.34  ? 177 ASP A O     1 
ATOM   1460 C  CB    . ASP A 1 177 ? -64.874 27.803  7.111   1.00 87.08  ? 177 ASP A CB    1 
ATOM   1461 C  CG    . ASP A 1 177 ? -65.158 28.953  8.060   1.00 97.52  ? 177 ASP A CG    1 
ATOM   1462 O  OD1   . ASP A 1 177 ? -65.250 30.106  7.588   1.00 110.21 ? 177 ASP A OD1   1 
ATOM   1463 O  OD2   . ASP A 1 177 ? -65.290 28.704  9.276   1.00 104.71 ? 177 ASP A OD2   1 
ATOM   1464 N  N     . LEU A 1 178 ? -61.835 29.320  5.738   1.00 85.21  ? 178 LEU A N     1 
ATOM   1465 C  CA    . LEU A 1 178 ? -60.457 29.647  6.074   1.00 85.04  ? 178 LEU A CA    1 
ATOM   1466 C  C     . LEU A 1 178 ? -60.250 31.133  5.831   1.00 93.36  ? 178 LEU A C     1 
ATOM   1467 O  O     . LEU A 1 178 ? -60.966 31.729  5.018   1.00 87.16  ? 178 LEU A O     1 
ATOM   1468 C  CB    . LEU A 1 178 ? -59.461 28.821  5.247   1.00 78.63  ? 178 LEU A CB    1 
ATOM   1469 C  CG    . LEU A 1 178 ? -59.192 27.403  5.751   1.00 77.02  ? 178 LEU A CG    1 
ATOM   1470 C  CD1   . LEU A 1 178 ? -58.220 26.682  4.831   1.00 72.40  ? 178 LEU A CD1   1 
ATOM   1471 C  CD2   . LEU A 1 178 ? -58.671 27.432  7.180   1.00 71.25  ? 178 LEU A CD2   1 
ATOM   1472 N  N     . PRO A 1 179 ? -59.300 31.765  6.527   1.00 82.52  ? 179 PRO A N     1 
ATOM   1473 C  CA    . PRO A 1 179 ? -59.125 33.218  6.373   1.00 80.51  ? 179 PRO A CA    1 
ATOM   1474 C  C     . PRO A 1 179 ? -58.453 33.634  5.072   1.00 78.96  ? 179 PRO A C     1 
ATOM   1475 O  O     . PRO A 1 179 ? -58.460 34.831  4.757   1.00 88.07  ? 179 PRO A O     1 
ATOM   1476 C  CB    . PRO A 1 179 ? -58.266 33.600  7.585   1.00 79.74  ? 179 PRO A CB    1 
ATOM   1477 C  CG    . PRO A 1 179 ? -57.542 32.352  7.946   1.00 81.19  ? 179 PRO A CG    1 
ATOM   1478 C  CD    . PRO A 1 179 ? -58.453 31.211  7.600   1.00 73.81  ? 179 PRO A CD    1 
ATOM   1479 N  N     . TYR A 1 180 ? -57.884 32.704  4.306   1.00 69.09  ? 180 TYR A N     1 
ATOM   1480 C  CA    . TYR A 1 180 ? -57.185 33.053  3.075   1.00 68.07  ? 180 TYR A CA    1 
ATOM   1481 C  C     . TYR A 1 180 ? -57.843 32.476  1.828   1.00 70.04  ? 180 TYR A C     1 
ATOM   1482 O  O     . TYR A 1 180 ? -57.222 32.477  0.758   1.00 65.57  ? 180 TYR A O     1 
ATOM   1483 C  CB    . TYR A 1 180 ? -55.721 32.605  3.146   1.00 65.54  ? 180 TYR A CB    1 
ATOM   1484 C  CG    . TYR A 1 180 ? -55.527 31.160  3.548   1.00 66.89  ? 180 TYR A CG    1 
ATOM   1485 C  CD1   . TYR A 1 180 ? -55.623 30.138  2.613   1.00 65.29  ? 180 TYR A CD1   1 
ATOM   1486 C  CD2   . TYR A 1 180 ? -55.235 30.818  4.863   1.00 68.70  ? 180 TYR A CD2   1 
ATOM   1487 C  CE1   . TYR A 1 180 ? -55.443 28.817  2.975   1.00 68.23  ? 180 TYR A CE1   1 
ATOM   1488 C  CE2   . TYR A 1 180 ? -55.053 29.500  5.235   1.00 72.16  ? 180 TYR A CE2   1 
ATOM   1489 C  CZ    . TYR A 1 180 ? -55.157 28.505  4.286   1.00 71.47  ? 180 TYR A CZ    1 
ATOM   1490 O  OH    . TYR A 1 180 ? -54.977 27.191  4.650   1.00 70.54  ? 180 TYR A OH    1 
ATOM   1491 N  N     . VAL A 1 181 ? -59.078 31.993  1.926   1.00 70.65  ? 181 VAL A N     1 
ATOM   1492 C  CA    . VAL A 1 181 ? -59.794 31.428  0.789   1.00 70.27  ? 181 VAL A CA    1 
ATOM   1493 C  C     . VAL A 1 181 ? -60.899 32.391  0.377   1.00 73.29  ? 181 VAL A C     1 
ATOM   1494 O  O     . VAL A 1 181 ? -61.604 32.950  1.226   1.00 72.50  ? 181 VAL A O     1 
ATOM   1495 C  CB    . VAL A 1 181 ? -60.370 30.034  1.108   1.00 75.75  ? 181 VAL A CB    1 
ATOM   1496 C  CG1   . VAL A 1 181 ? -61.089 30.055  2.431   1.00 77.52  ? 181 VAL A CG1   1 
ATOM   1497 C  CG2   . VAL A 1 181 ? -61.308 29.574  0.006   1.00 72.33  ? 181 VAL A CG2   1 
ATOM   1498 N  N     . ASP A 1 182 ? -61.033 32.592  -0.930  1.00 70.03  ? 182 ASP A N     1 
ATOM   1499 C  CA    . ASP A 1 182 ? -62.102 33.378  -1.526  1.00 70.30  ? 182 ASP A CA    1 
ATOM   1500 C  C     . ASP A 1 182 ? -62.976 32.438  -2.345  1.00 67.83  ? 182 ASP A C     1 
ATOM   1501 O  O     . ASP A 1 182 ? -62.492 31.780  -3.277  1.00 63.36  ? 182 ASP A O     1 
ATOM   1502 C  CB    . ASP A 1 182 ? -61.536 34.502  -2.393  1.00 70.77  ? 182 ASP A CB    1 
ATOM   1503 C  CG    . ASP A 1 182 ? -60.666 35.463  -1.602  1.00 76.59  ? 182 ASP A CG    1 
ATOM   1504 O  OD1   . ASP A 1 182 ? -60.843 35.546  -0.368  1.00 72.50  ? 182 ASP A OD1   1 
ATOM   1505 O  OD2   . ASP A 1 182 ? -59.804 36.130  -2.213  1.00 80.36  ? 182 ASP A OD2   1 
ATOM   1506 N  N     . VAL A 1 183 ? -64.254 32.368  -1.986  1.00 74.25  ? 183 VAL A N     1 
ATOM   1507 C  CA    . VAL A 1 183 ? -65.204 31.457  -2.610  1.00 70.06  ? 183 VAL A CA    1 
ATOM   1508 C  C     . VAL A 1 183 ? -65.948 32.201  -3.708  1.00 69.92  ? 183 VAL A C     1 
ATOM   1509 O  O     . VAL A 1 183 ? -66.470 33.299  -3.483  1.00 71.99  ? 183 VAL A O     1 
ATOM   1510 C  CB    . VAL A 1 183 ? -66.183 30.880  -1.572  1.00 74.05  ? 183 VAL A CB    1 
ATOM   1511 C  CG1   . VAL A 1 183 ? -66.953 29.707  -2.159  1.00 72.37  ? 183 VAL A CG1   1 
ATOM   1512 C  CG2   . VAL A 1 183 ? -65.436 30.460  -0.314  1.00 71.02  ? 183 VAL A CG2   1 
ATOM   1513 N  N     . VAL A 1 184 ? -65.990 31.605  -4.897  1.00 69.57  ? 184 VAL A N     1 
ATOM   1514 C  CA    . VAL A 1 184 ? -66.773 32.138  -6.005  1.00 74.10  ? 184 VAL A CA    1 
ATOM   1515 C  C     . VAL A 1 184 ? -67.824 31.105  -6.387  1.00 76.60  ? 184 VAL A C     1 
ATOM   1516 O  O     . VAL A 1 184 ? -67.945 30.060  -5.739  1.00 79.34  ? 184 VAL A O     1 
ATOM   1517 C  CB    . VAL A 1 184 ? -65.884 32.503  -7.207  1.00 69.95  ? 184 VAL A CB    1 
ATOM   1518 C  CG1   . VAL A 1 184 ? -64.846 33.540  -6.802  1.00 67.40  ? 184 VAL A CG1   1 
ATOM   1519 C  CG2   . VAL A 1 184 ? -65.215 31.259  -7.762  1.00 70.43  ? 184 VAL A CG2   1 
ATOM   1520 N  N     . SER A 1 185 ? -68.584 31.384  -7.445  1.00 74.49  ? 185 SER A N     1 
ATOM   1521 C  CA    . SER A 1 185 ? -69.702 30.525  -7.814  1.00 93.95  ? 185 SER A CA    1 
ATOM   1522 C  C     . SER A 1 185 ? -69.278 29.372  -8.720  1.00 82.71  ? 185 SER A C     1 
ATOM   1523 O  O     . SER A 1 185 ? -69.617 28.215  -8.452  1.00 77.49  ? 185 SER A O     1 
ATOM   1524 C  CB    . SER A 1 185 ? -70.800 31.360  -8.484  1.00 89.50  ? 185 SER A CB    1 
ATOM   1525 O  OG    . SER A 1 185 ? -70.499 31.614  -9.845  1.00 103.56 ? 185 SER A OG    1 
ATOM   1526 N  N     . THR A 1 186 ? -68.548 29.665  -9.794  1.00 77.04  ? 186 THR A N     1 
ATOM   1527 C  CA    . THR A 1 186 ? -68.169 28.663  -10.782 1.00 74.99  ? 186 THR A CA    1 
ATOM   1528 C  C     . THR A 1 186 ? -66.666 28.722  -11.031 1.00 80.98  ? 186 THR A C     1 
ATOM   1529 O  O     . THR A 1 186 ? -65.953 29.578  -10.499 1.00 77.94  ? 186 THR A O     1 
ATOM   1530 C  CB    . THR A 1 186 ? -68.932 28.857  -12.102 1.00 85.04  ? 186 THR A CB    1 
ATOM   1531 O  OG1   . THR A 1 186 ? -68.400 29.989  -12.802 1.00 70.23  ? 186 THR A OG1   1 
ATOM   1532 C  CG2   . THR A 1 186 ? -70.424 29.060  -11.853 1.00 75.92  ? 186 THR A CG2   1 
ATOM   1533 N  N     . GLU A 1 187 ? -66.190 27.786  -11.856 1.00 78.36  ? 187 GLU A N     1 
ATOM   1534 C  CA    . GLU A 1 187 ? -64.797 27.801  -12.288 1.00 72.17  ? 187 GLU A CA    1 
ATOM   1535 C  C     . GLU A 1 187 ? -64.510 29.012  -13.170 1.00 76.08  ? 187 GLU A C     1 
ATOM   1536 O  O     . GLU A 1 187 ? -63.426 29.608  -13.091 1.00 75.69  ? 187 GLU A O     1 
ATOM   1537 C  CB    . GLU A 1 187 ? -64.477 26.499  -13.025 1.00 70.34  ? 187 GLU A CB    1 
ATOM   1538 C  CG    . GLU A 1 187 ? -63.360 26.602  -14.047 1.00 85.60  ? 187 GLU A CG    1 
ATOM   1539 C  CD    . GLU A 1 187 ? -63.043 25.269  -14.701 1.00 91.97  ? 187 GLU A CD    1 
ATOM   1540 O  OE1   . GLU A 1 187 ? -63.922 24.728  -15.404 1.00 80.04  ? 187 GLU A OE1   1 
ATOM   1541 O  OE2   . GLU A 1 187 ? -61.911 24.770  -14.524 1.00 81.29  ? 187 GLU A OE2   1 
ATOM   1542 N  N     . ARG A 1 188 ? -65.474 29.382  -14.017 1.00 77.18  ? 188 ARG A N     1 
ATOM   1543 C  CA    . ARG A 1 188 ? -65.337 30.577  -14.843 1.00 83.03  ? 188 ARG A CA    1 
ATOM   1544 C  C     . ARG A 1 188 ? -65.078 31.807  -13.983 1.00 75.36  ? 188 ARG A C     1 
ATOM   1545 O  O     . ARG A 1 188 ? -64.176 32.605  -14.270 1.00 73.38  ? 188 ARG A O     1 
ATOM   1546 C  CB    . ARG A 1 188 ? -66.602 30.766  -15.683 1.00 88.30  ? 188 ARG A CB    1 
ATOM   1547 C  CG    . ARG A 1 188 ? -66.356 31.033  -17.156 1.00 90.38  ? 188 ARG A CG    1 
ATOM   1548 C  CD    . ARG A 1 188 ? -67.639 31.427  -17.864 1.00 86.43  ? 188 ARG A CD    1 
ATOM   1549 N  NE    . ARG A 1 188 ? -67.383 32.243  -19.045 1.00 88.98  ? 188 ARG A NE    1 
ATOM   1550 C  CZ    . ARG A 1 188 ? -67.480 33.565  -19.077 1.00 82.82  ? 188 ARG A CZ    1 
ATOM   1551 N  NH1   . ARG A 1 188 ? -67.820 34.260  -18.004 1.00 76.93  ? 188 ARG A NH1   1 
ATOM   1552 N  NH2   . ARG A 1 188 ? -67.228 34.207  -20.215 1.00 73.96  ? 188 ARG A NH2   1 
ATOM   1553 N  N     . GLU A 1 189 ? -65.866 31.974  -12.918 1.00 73.78  ? 189 GLU A N     1 
ATOM   1554 C  CA    . GLU A 1 189 ? -65.691 33.123  -12.039 1.00 76.91  ? 189 GLU A CA    1 
ATOM   1555 C  C     . GLU A 1 189 ? -64.341 33.077  -11.336 1.00 70.71  ? 189 GLU A C     1 
ATOM   1556 O  O     . GLU A 1 189 ? -63.720 34.119  -11.106 1.00 68.09  ? 189 GLU A O     1 
ATOM   1557 C  CB    . GLU A 1 189 ? -66.829 33.183  -11.019 1.00 77.82  ? 189 GLU A CB    1 
ATOM   1558 C  CG    . GLU A 1 189 ? -67.475 34.554  -10.879 1.00 87.85  ? 189 GLU A CG    1 
ATOM   1559 C  CD    . GLU A 1 189 ? -68.035 35.081  -12.188 1.00 103.49 ? 189 GLU A CD    1 
ATOM   1560 O  OE1   . GLU A 1 189 ? -68.542 34.273  -12.997 1.00 111.88 ? 189 GLU A OE1   1 
ATOM   1561 O  OE2   . GLU A 1 189 ? -67.975 36.309  -12.405 1.00 102.82 ? 189 GLU A OE2   1 
ATOM   1562 N  N     . MET A 1 190 ? -63.863 31.877  -11.000 1.00 67.40  ? 190 MET A N     1 
ATOM   1563 C  CA    . MET A 1 190 ? -62.558 31.755  -10.356 1.00 69.73  ? 190 MET A CA    1 
ATOM   1564 C  C     . MET A 1 190 ? -61.440 32.202  -11.291 1.00 63.98  ? 190 MET A C     1 
ATOM   1565 O  O     . MET A 1 190 ? -60.541 32.956  -10.893 1.00 62.04  ? 190 MET A O     1 
ATOM   1566 C  CB    . MET A 1 190 ? -62.333 30.313  -9.904  1.00 65.90  ? 190 MET A CB    1 
ATOM   1567 C  CG    . MET A 1 190 ? -60.900 30.021  -9.505  1.00 64.33  ? 190 MET A CG    1 
ATOM   1568 S  SD    . MET A 1 190 ? -60.612 28.269  -9.216  1.00 55.47  ? 190 MET A SD    1 
ATOM   1569 C  CE    . MET A 1 190 ? -60.871 27.618  -10.863 1.00 59.33  ? 190 MET A CE    1 
ATOM   1570 N  N     . ILE A 1 191 ? -61.475 31.738  -12.542 1.00 62.64  ? 191 ILE A N     1 
ATOM   1571 C  CA    . ILE A 1 191 ? -60.450 32.134  -13.504 1.00 64.88  ? 191 ILE A CA    1 
ATOM   1572 C  C     . ILE A 1 191 ? -60.514 33.635  -13.764 1.00 65.56  ? 191 ILE A C     1 
ATOM   1573 O  O     . ILE A 1 191 ? -59.480 34.315  -13.830 1.00 61.23  ? 191 ILE A O     1 
ATOM   1574 C  CB    . ILE A 1 191 ? -60.596 31.322  -14.804 1.00 64.16  ? 191 ILE A CB    1 
ATOM   1575 C  CG1   . ILE A 1 191 ? -60.335 29.837  -14.535 1.00 66.12  ? 191 ILE A CG1   1 
ATOM   1576 C  CG2   . ILE A 1 191 ? -59.643 31.842  -15.868 1.00 66.48  ? 191 ILE A CG2   1 
ATOM   1577 C  CD1   . ILE A 1 191 ? -60.591 28.941  -15.729 1.00 68.87  ? 191 ILE A CD1   1 
ATOM   1578 N  N     . LYS A 1 192 ? -61.727 34.180  -13.899 1.00 64.23  ? 192 LYS A N     1 
ATOM   1579 C  CA    . LYS A 1 192 ? -61.866 35.617  -14.109 1.00 66.17  ? 192 LYS A CA    1 
ATOM   1580 C  C     . LYS A 1 192 ? -61.342 36.403  -12.913 1.00 64.33  ? 192 LYS A C     1 
ATOM   1581 O  O     . LYS A 1 192 ? -60.723 37.462  -13.077 1.00 60.16  ? 192 LYS A O     1 
ATOM   1582 C  CB    . LYS A 1 192 ? -63.328 35.970  -14.382 1.00 72.85  ? 192 LYS A CB    1 
ATOM   1583 C  CG    . LYS A 1 192 ? -63.776 35.704  -15.811 1.00 71.76  ? 192 LYS A CG    1 
ATOM   1584 C  CD    . LYS A 1 192 ? -65.290 35.810  -15.961 1.00 81.89  ? 192 LYS A CD    1 
ATOM   1585 C  CE    . LYS A 1 192 ? -65.917 36.617  -14.833 1.00 85.06  ? 192 LYS A CE    1 
ATOM   1586 N  NZ    . LYS A 1 192 ? -67.110 37.382  -15.286 1.00 83.17  ? 192 LYS A NZ    1 
ATOM   1587 N  N     . ARG A 1 193 ? -61.568 35.896  -11.700 1.00 60.07  ? 193 ARG A N     1 
ATOM   1588 C  CA    . ARG A 1 193 ? -61.069 36.585  -10.518 1.00 62.42  ? 193 ARG A CA    1 
ATOM   1589 C  C     . ARG A 1 193 ? -59.550 36.544  -10.461 1.00 61.99  ? 193 ARG A C     1 
ATOM   1590 O  O     . ARG A 1 193 ? -58.918 37.529  -10.071 1.00 64.05  ? 193 ARG A O     1 
ATOM   1591 C  CB    . ARG A 1 193 ? -61.665 35.978  -9.250  1.00 61.81  ? 193 ARG A CB    1 
ATOM   1592 C  CG    . ARG A 1 193 ? -61.458 36.852  -8.026  1.00 66.23  ? 193 ARG A CG    1 
ATOM   1593 C  CD    . ARG A 1 193 ? -61.376 36.035  -6.750  1.00 76.75  ? 193 ARG A CD    1 
ATOM   1594 N  NE    . ARG A 1 193 ? -61.279 36.885  -5.569  1.00 80.17  ? 193 ARG A NE    1 
ATOM   1595 C  CZ    . ARG A 1 193 ? -62.282 37.595  -5.069  1.00 78.20  ? 193 ARG A CZ    1 
ATOM   1596 N  NH1   . ARG A 1 193 ? -63.487 37.572  -5.614  1.00 70.43  ? 193 ARG A NH1   1 
ATOM   1597 N  NH2   . ARG A 1 193 ? -62.070 38.346  -3.991  1.00 82.67  ? 193 ARG A NH2   1 
ATOM   1598 N  N     . PHE A 1 194 ? -58.945 35.416  -10.839 1.00 57.10  ? 194 PHE A N     1 
ATOM   1599 C  CA    . PHE A 1 194 ? -57.487 35.371  -10.903 1.00 64.07  ? 194 PHE A CA    1 
ATOM   1600 C  C     . PHE A 1 194 ? -56.956 36.369  -11.926 1.00 63.24  ? 194 PHE A C     1 
ATOM   1601 O  O     . PHE A 1 194 ? -55.943 37.041  -11.687 1.00 61.09  ? 194 PHE A O     1 
ATOM   1602 C  CB    . PHE A 1 194 ? -57.007 33.958  -11.234 1.00 59.40  ? 194 PHE A CB    1 
ATOM   1603 C  CG    . PHE A 1 194 ? -55.520 33.856  -11.411 1.00 60.69  ? 194 PHE A CG    1 
ATOM   1604 C  CD1   . PHE A 1 194 ? -54.662 34.193  -10.376 1.00 61.22  ? 194 PHE A CD1   1 
ATOM   1605 C  CD2   . PHE A 1 194 ? -54.979 33.442  -12.615 1.00 60.42  ? 194 PHE A CD2   1 
ATOM   1606 C  CE1   . PHE A 1 194 ? -53.291 34.108  -10.538 1.00 61.06  ? 194 PHE A CE1   1 
ATOM   1607 C  CE2   . PHE A 1 194 ? -53.611 33.354  -12.784 1.00 59.00  ? 194 PHE A CE2   1 
ATOM   1608 C  CZ    . PHE A 1 194 ? -52.766 33.688  -11.744 1.00 60.47  ? 194 PHE A CZ    1 
ATOM   1609 N  N     . LEU A 1 195 ? -57.634 36.481  -13.073 1.00 63.21  ? 195 LEU A N     1 
ATOM   1610 C  CA    . LEU A 1 195 ? -57.246 37.477  -14.070 1.00 59.27  ? 195 LEU A CA    1 
ATOM   1611 C  C     . LEU A 1 195 ? -57.326 38.883  -13.498 1.00 66.01  ? 195 LEU A C     1 
ATOM   1612 O  O     . LEU A 1 195 ? -56.447 39.716  -13.745 1.00 65.69  ? 195 LEU A O     1 
ATOM   1613 C  CB    . LEU A 1 195 ? -58.133 37.366  -15.311 1.00 63.82  ? 195 LEU A CB    1 
ATOM   1614 C  CG    . LEU A 1 195 ? -57.609 36.493  -16.449 1.00 81.06  ? 195 LEU A CG    1 
ATOM   1615 C  CD1   . LEU A 1 195 ? -56.936 35.277  -15.869 1.00 76.96  ? 195 LEU A CD1   1 
ATOM   1616 C  CD2   . LEU A 1 195 ? -58.735 36.082  -17.386 1.00 76.68  ? 195 LEU A CD2   1 
ATOM   1617 N  N     . ARG A 1 196 ? -58.382 39.164  -12.734 1.00 65.09  ? 196 ARG A N     1 
ATOM   1618 C  CA    . ARG A 1 196 ? -58.528 40.480  -12.124 1.00 69.72  ? 196 ARG A CA    1 
ATOM   1619 C  C     . ARG A 1 196 ? -57.436 40.735  -11.091 1.00 64.41  ? 196 ARG A C     1 
ATOM   1620 O  O     . ARG A 1 196 ? -56.921 41.854  -10.992 1.00 64.54  ? 196 ARG A O     1 
ATOM   1621 C  CB    . ARG A 1 196 ? -59.911 40.613  -11.491 1.00 66.99  ? 196 ARG A CB    1 
ATOM   1622 C  CG    . ARG A 1 196 ? -60.633 41.898  -11.851 1.00 74.71  ? 196 ARG A CG    1 
ATOM   1623 C  CD    . ARG A 1 196 ? -61.946 42.012  -11.098 1.00 82.20  ? 196 ARG A CD    1 
ATOM   1624 N  NE    . ARG A 1 196 ? -61.786 42.702  -9.824  1.00 97.76  ? 196 ARG A NE    1 
ATOM   1625 C  CZ    . ARG A 1 196 ? -62.032 42.155  -8.641  1.00 102.79 ? 196 ARG A CZ    1 
ATOM   1626 N  NH1   . ARG A 1 196 ? -62.452 40.905  -8.532  1.00 89.87  ? 196 ARG A NH1   1 
ATOM   1627 N  NH2   . ARG A 1 196 ? -61.850 42.880  -7.541  1.00 105.74 ? 196 ARG A NH2   1 
ATOM   1628 N  N     . VAL A 1 197 ? -57.073 39.712  -10.312 1.00 64.38  ? 197 VAL A N     1 
ATOM   1629 C  CA    . VAL A 1 197 ? -55.980 39.854  -9.349  1.00 67.75  ? 197 VAL A CA    1 
ATOM   1630 C  C     . VAL A 1 197 ? -54.681 40.195  -10.066 1.00 62.78  ? 197 VAL A C     1 
ATOM   1631 O  O     . VAL A 1 197 ? -53.941 41.095  -9.651  1.00 61.48  ? 197 VAL A O     1 
ATOM   1632 C  CB    . VAL A 1 197 ? -55.830 38.582  -8.495  1.00 65.37  ? 197 VAL A CB    1 
ATOM   1633 C  CG1   . VAL A 1 197 ? -54.721 38.771  -7.474  1.00 61.08  ? 197 VAL A CG1   1 
ATOM   1634 C  CG2   . VAL A 1 197 ? -57.121 38.278  -7.770  1.00 62.68  ? 197 VAL A CG2   1 
ATOM   1635 N  N     . VAL A 1 198 ? -54.386 39.487  -11.159 1.00 58.56  ? 198 VAL A N     1 
ATOM   1636 C  CA    . VAL A 1 198 ? -53.152 39.764  -11.891 1.00 65.66  ? 198 VAL A CA    1 
ATOM   1637 C  C     . VAL A 1 198 ? -53.186 41.167  -12.485 1.00 67.60  ? 198 VAL A C     1 
ATOM   1638 O  O     . VAL A 1 198 ? -52.202 41.914  -12.406 1.00 62.04  ? 198 VAL A O     1 
ATOM   1639 C  CB    . VAL A 1 198 ? -52.911 38.694  -12.970 1.00 62.52  ? 198 VAL A CB    1 
ATOM   1640 C  CG1   . VAL A 1 198 ? -51.670 39.037  -13.773 1.00 59.08  ? 198 VAL A CG1   1 
ATOM   1641 C  CG2   . VAL A 1 198 ? -52.775 37.320  -12.335 1.00 59.78  ? 198 VAL A CG2   1 
ATOM   1642 N  N     . LYS A 1 199 ? -54.320 41.553  -13.073 1.00 65.39  ? 199 LYS A N     1 
ATOM   1643 C  CA    . LYS A 1 199 ? -54.424 42.867  -13.701 1.00 64.32  ? 199 LYS A CA    1 
ATOM   1644 C  C     . LYS A 1 199 ? -54.293 43.985  -12.674 1.00 63.93  ? 199 LYS A C     1 
ATOM   1645 O  O     . LYS A 1 199 ? -53.692 45.029  -12.954 1.00 67.67  ? 199 LYS A O     1 
ATOM   1646 C  CB    . LYS A 1 199 ? -55.749 42.977  -14.456 1.00 68.75  ? 199 LYS A CB    1 
ATOM   1647 C  CG    . LYS A 1 199 ? -55.709 43.868  -15.689 1.00 71.28  ? 199 LYS A CG    1 
ATOM   1648 C  CD    . LYS A 1 199 ? -57.079 43.943  -16.349 1.00 85.85  ? 199 LYS A CD    1 
ATOM   1649 C  CE    . LYS A 1 199 ? -57.980 44.956  -15.655 1.00 82.12  ? 199 LYS A CE    1 
ATOM   1650 N  NZ    . LYS A 1 199 ? -57.213 46.110  -15.112 1.00 98.90  ? 199 LYS A NZ    1 
ATOM   1651 N  N     . GLU A 1 200 ? -54.841 43.782  -11.474 1.00 68.67  ? 200 GLU A N     1 
ATOM   1652 C  CA    . GLU A 1 200 ? -54.760 44.805  -10.438 1.00 71.39  ? 200 GLU A CA    1 
ATOM   1653 C  C     . GLU A 1 200 ? -53.359 44.884  -9.848  1.00 67.18  ? 200 GLU A C     1 
ATOM   1654 O  O     . GLU A 1 200 ? -52.820 45.981  -9.655  1.00 66.15  ? 200 GLU A O     1 
ATOM   1655 C  CB    . GLU A 1 200 ? -55.789 44.517  -9.345  1.00 75.06  ? 200 GLU A CB    1 
ATOM   1656 C  CG    . GLU A 1 200 ? -55.716 45.455  -8.154  1.00 94.77  ? 200 GLU A CG    1 
ATOM   1657 C  CD    . GLU A 1 200 ? -57.017 45.508  -7.377  1.00 121.61 ? 200 GLU A CD    1 
ATOM   1658 O  OE1   . GLU A 1 200 ? -58.044 45.022  -7.897  1.00 111.98 ? 200 GLU A OE1   1 
ATOM   1659 O  OE2   . GLU A 1 200 ? -57.013 46.035  -6.244  1.00 126.80 ? 200 GLU A OE2   1 
ATOM   1660 N  N     . LYS A 1 201 ? -52.752 43.734  -9.553  1.00 64.91  ? 201 LYS A N     1 
ATOM   1661 C  CA    . LYS A 1 201 ? -51.415 43.740  -8.973  1.00 70.35  ? 201 LYS A CA    1 
ATOM   1662 C  C     . LYS A 1 201 ? -50.361 44.125  -10.001 1.00 62.74  ? 201 LYS A C     1 
ATOM   1663 O  O     . LYS A 1 201 ? -49.375 44.784  -9.654  1.00 57.57  ? 201 LYS A O     1 
ATOM   1664 C  CB    . LYS A 1 201 ? -51.105 42.372  -8.365  1.00 67.22  ? 201 LYS A CB    1 
ATOM   1665 C  CG    . LYS A 1 201 ? -52.048 41.985  -7.236  1.00 63.47  ? 201 LYS A CG    1 
ATOM   1666 C  CD    . LYS A 1 201 ? -51.444 40.937  -6.318  1.00 58.54  ? 201 LYS A CD    1 
ATOM   1667 C  CE    . LYS A 1 201 ? -52.126 40.957  -4.959  1.00 50.66  ? 201 LYS A CE    1 
ATOM   1668 N  NZ    . LYS A 1 201 ? -51.473 40.055  -3.973  1.00 65.86  ? 201 LYS A NZ    1 
ATOM   1669 N  N     . ASP A 1 202 ? -50.560 43.743  -11.259 1.00 59.96  ? 202 ASP A N     1 
ATOM   1670 C  CA    . ASP A 1 202 ? -49.644 44.063  -12.348 1.00 64.44  ? 202 ASP A CA    1 
ATOM   1671 C  C     . ASP A 1 202 ? -48.194 43.702  -12.008 1.00 66.37  ? 202 ASP A C     1 
ATOM   1672 O  O     . ASP A 1 202 ? -47.332 44.581  -11.930 1.00 59.97  ? 202 ASP A O     1 
ATOM   1673 C  CB    . ASP A 1 202 ? -49.754 45.533  -12.728 1.00 66.66  ? 202 ASP A CB    1 
ATOM   1674 C  CG    . ASP A 1 202 ? -49.115 45.838  -14.070 1.00 73.15  ? 202 ASP A CG    1 
ATOM   1675 O  OD1   . ASP A 1 202 ? -48.905 44.893  -14.858 1.00 80.00  ? 202 ASP A OD1   1 
ATOM   1676 O  OD2   . ASP A 1 202 ? -48.817 47.022  -14.333 1.00 73.92  ? 202 ASP A OD2   1 
ATOM   1677 N  N     . PRO A 1 203 ? -47.895 42.421  -11.800 1.00 67.26  ? 203 PRO A N     1 
ATOM   1678 C  CA    . PRO A 1 203 ? -46.519 42.043  -11.472 1.00 58.66  ? 203 PRO A CA    1 
ATOM   1679 C  C     . PRO A 1 203 ? -45.631 42.096  -12.702 1.00 56.70  ? 203 PRO A C     1 
ATOM   1680 O  O     . PRO A 1 203 ? -46.087 41.948  -13.838 1.00 54.62  ? 203 PRO A O     1 
ATOM   1681 C  CB    . PRO A 1 203 ? -46.662 40.609  -10.955 1.00 54.36  ? 203 PRO A CB    1 
ATOM   1682 C  CG    . PRO A 1 203 ? -47.828 40.077  -11.717 1.00 59.62  ? 203 PRO A CG    1 
ATOM   1683 C  CD    . PRO A 1 203 ? -48.776 41.243  -11.904 1.00 65.82  ? 203 PRO A CD    1 
ATOM   1684 N  N     . ASP A 1 204 ? -44.341 42.324  -12.462 1.00 56.00  ? 204 ASP A N     1 
ATOM   1685 C  CA    . ASP A 1 204 ? -43.372 42.234  -13.545 1.00 52.57  ? 204 ASP A CA    1 
ATOM   1686 C  C     . ASP A 1 204 ? -42.977 40.790  -13.813 1.00 52.77  ? 204 ASP A C     1 
ATOM   1687 O  O     . ASP A 1 204 ? -42.600 40.450  -14.940 1.00 48.20  ? 204 ASP A O     1 
ATOM   1688 C  CB    . ASP A 1 204 ? -42.135 43.066  -13.215 1.00 56.44  ? 204 ASP A CB    1 
ATOM   1689 C  CG    . ASP A 1 204 ? -42.479 44.490  -12.836 1.00 62.33  ? 204 ASP A CG    1 
ATOM   1690 O  OD1   . ASP A 1 204 ? -43.080 45.203  -13.668 1.00 59.61  ? 204 ASP A OD1   1 
ATOM   1691 O  OD2   . ASP A 1 204 ? -42.159 44.890  -11.698 1.00 59.03  ? 204 ASP A OD2   1 
ATOM   1692 N  N     . VAL A 1 205 ? -43.071 39.934  -12.799 1.00 47.18  ? 205 VAL A N     1 
ATOM   1693 C  CA    . VAL A 1 205 ? -42.668 38.539  -12.894 1.00 49.50  ? 205 VAL A CA    1 
ATOM   1694 C  C     . VAL A 1 205 ? -43.821 37.671  -12.414 1.00 44.95  ? 205 VAL A C     1 
ATOM   1695 O  O     . VAL A 1 205 ? -44.401 37.931  -11.353 1.00 46.80  ? 205 VAL A O     1 
ATOM   1696 C  CB    . VAL A 1 205 ? -41.400 38.253  -12.067 1.00 47.81  ? 205 VAL A CB    1 
ATOM   1697 C  CG1   . VAL A 1 205 ? -41.047 36.772  -12.127 1.00 44.73  ? 205 VAL A CG1   1 
ATOM   1698 C  CG2   . VAL A 1 205 ? -40.243 39.112  -12.552 1.00 49.03  ? 205 VAL A CG2   1 
ATOM   1699 N  N     . LEU A 1 206 ? -44.157 36.652  -13.198 1.00 38.54  ? 206 LEU A N     1 
ATOM   1700 C  CA    . LEU A 1 206 ? -45.120 35.632  -12.801 1.00 49.47  ? 206 LEU A CA    1 
ATOM   1701 C  C     . LEU A 1 206 ? -44.358 34.341  -12.535 1.00 44.36  ? 206 LEU A C     1 
ATOM   1702 O  O     . LEU A 1 206 ? -43.753 33.777  -13.450 1.00 43.61  ? 206 LEU A O     1 
ATOM   1703 C  CB    . LEU A 1 206 ? -46.187 35.424  -13.876 1.00 45.53  ? 206 LEU A CB    1 
ATOM   1704 C  CG    . LEU A 1 206 ? -47.332 36.439  -13.901 1.00 46.86  ? 206 LEU A CG    1 
ATOM   1705 C  CD1   . LEU A 1 206 ? -47.991 36.476  -15.274 1.00 54.57  ? 206 LEU A CD1   1 
ATOM   1706 C  CD2   . LEU A 1 206 ? -48.352 36.130  -12.816 1.00 50.63  ? 206 LEU A CD2   1 
ATOM   1707 N  N     . ILE A 1 207 ? -44.393 33.881  -11.289 1.00 43.58  ? 207 ILE A N     1 
ATOM   1708 C  CA    . ILE A 1 207 ? -43.598 32.745  -10.836 1.00 44.55  ? 207 ILE A CA    1 
ATOM   1709 C  C     . ILE A 1 207 ? -44.459 31.490  -10.843 1.00 49.05  ? 207 ILE A C     1 
ATOM   1710 O  O     . ILE A 1 207 ? -45.562 31.468  -10.274 1.00 48.17  ? 207 ILE A O     1 
ATOM   1711 C  CB    . ILE A 1 207 ? -43.011 32.997  -9.438  1.00 44.60  ? 207 ILE A CB    1 
ATOM   1712 C  CG1   . ILE A 1 207 ? -42.395 34.396  -9.365  1.00 47.80  ? 207 ILE A CG1   1 
ATOM   1713 C  CG2   . ILE A 1 207 ? -41.976 31.934  -9.098  1.00 46.12  ? 207 ILE A CG2   1 
ATOM   1714 C  CD1   . ILE A 1 207 ? -41.878 34.764  -7.993  1.00 48.29  ? 207 ILE A CD1   1 
ATOM   1715 N  N     . THR A 1 208 ? -43.957 30.445  -11.500 1.00 49.43  ? 208 THR A N     1 
ATOM   1716 C  CA    . THR A 1 208 ? -44.603 29.142  -11.515 1.00 44.44  ? 208 THR A CA    1 
ATOM   1717 C  C     . THR A 1 208 ? -43.564 28.059  -11.269 1.00 48.92  ? 208 THR A C     1 
ATOM   1718 O  O     . THR A 1 208 ? -42.356 28.287  -11.381 1.00 47.79  ? 208 THR A O     1 
ATOM   1719 C  CB    . THR A 1 208 ? -45.315 28.853  -12.849 1.00 52.23  ? 208 THR A CB    1 
ATOM   1720 O  OG1   . THR A 1 208 ? -44.348 28.454  -13.829 1.00 44.60  ? 208 THR A OG1   1 
ATOM   1721 C  CG2   . THR A 1 208 ? -46.075 30.072  -13.350 1.00 47.73  ? 208 THR A CG2   1 
ATOM   1722 N  N     . TYR A 1 209 ? -44.054 26.869  -10.929 1.00 49.55  ? 209 TYR A N     1 
ATOM   1723 C  CA    . TYR A 1 209 ? -43.239 25.660  -10.872 1.00 50.40  ? 209 TYR A CA    1 
ATOM   1724 C  C     . TYR A 1 209 ? -43.775 24.697  -11.923 1.00 55.07  ? 209 TYR A C     1 
ATOM   1725 O  O     . TYR A 1 209 ? -44.859 24.128  -11.753 1.00 57.58  ? 209 TYR A O     1 
ATOM   1726 C  CB    . TYR A 1 209 ? -43.262 25.027  -9.482  1.00 54.09  ? 209 TYR A CB    1 
ATOM   1727 C  CG    . TYR A 1 209 ? -42.185 23.984  -9.289  1.00 55.92  ? 209 TYR A CG    1 
ATOM   1728 C  CD1   . TYR A 1 209 ? -40.842 24.319  -9.401  1.00 53.53  ? 209 TYR A CD1   1 
ATOM   1729 C  CD2   . TYR A 1 209 ? -42.509 22.662  -9.014  1.00 61.44  ? 209 TYR A CD2   1 
ATOM   1730 C  CE1   . TYR A 1 209 ? -39.851 23.369  -9.233  1.00 62.21  ? 209 TYR A CE1   1 
ATOM   1731 C  CE2   . TYR A 1 209 ? -41.525 21.704  -8.845  1.00 57.06  ? 209 TYR A CE2   1 
ATOM   1732 C  CZ    . TYR A 1 209 ? -40.198 22.064  -8.955  1.00 63.47  ? 209 TYR A CZ    1 
ATOM   1733 O  OH    . TYR A 1 209 ? -39.214 21.118  -8.789  1.00 54.06  ? 209 TYR A OH    1 
ATOM   1734 N  N     . ASN A 1 210 ? -43.017 24.528  -13.008 1.00 52.91  ? 210 ASN A N     1 
ATOM   1735 C  CA    . ASN A 1 210 ? -43.420 23.710  -14.154 1.00 54.78  ? 210 ASN A CA    1 
ATOM   1736 C  C     . ASN A 1 210 ? -44.677 24.257  -14.826 1.00 56.48  ? 210 ASN A C     1 
ATOM   1737 O  O     . ASN A 1 210 ? -45.439 23.511  -15.445 1.00 60.45  ? 210 ASN A O     1 
ATOM   1738 C  CB    . ASN A 1 210 ? -43.615 22.242  -13.761 1.00 61.72  ? 210 ASN A CB    1 
ATOM   1739 C  CG    . ASN A 1 210 ? -43.556 21.310  -14.954 1.00 67.30  ? 210 ASN A CG    1 
ATOM   1740 O  OD1   . ASN A 1 210 ? -42.831 21.563  -15.917 1.00 67.86  ? 210 ASN A OD1   1 
ATOM   1741 N  ND2   . ASN A 1 210 ? -44.327 20.229  -14.900 1.00 72.39  ? 210 ASN A ND2   1 
ATOM   1742 N  N     . GLY A 1 211 ? -44.905 25.567  -14.715 1.00 54.65  ? 211 GLY A N     1 
ATOM   1743 C  CA    . GLY A 1 211 ? -45.988 26.187  -15.457 1.00 50.14  ? 211 GLY A CA    1 
ATOM   1744 C  C     . GLY A 1 211 ? -45.774 26.184  -16.956 1.00 57.10  ? 211 GLY A C     1 
ATOM   1745 O  O     . GLY A 1 211 ? -46.734 26.374  -17.710 1.00 58.38  ? 211 GLY A O     1 
ATOM   1746 N  N     . ASP A 1 212 ? -44.532 25.970  -17.402 1.00 53.87  ? 212 ASP A N     1 
ATOM   1747 C  CA    . ASP A 1 212 ? -44.252 25.890  -18.831 1.00 53.12  ? 212 ASP A CA    1 
ATOM   1748 C  C     . ASP A 1 212 ? -44.931 24.687  -19.470 1.00 53.25  ? 212 ASP A C     1 
ATOM   1749 O  O     . ASP A 1 212 ? -45.286 24.731  -20.654 1.00 55.68  ? 212 ASP A O     1 
ATOM   1750 C  CB    . ASP A 1 212 ? -42.742 25.815  -19.067 1.00 48.93  ? 212 ASP A CB    1 
ATOM   1751 C  CG    . ASP A 1 212 ? -42.118 27.170  -19.339 1.00 55.07  ? 212 ASP A CG    1 
ATOM   1752 O  OD1   . ASP A 1 212 ? -42.863 28.139  -19.596 1.00 48.85  ? 212 ASP A OD1   1 
ATOM   1753 O  OD2   . ASP A 1 212 ? -40.872 27.263  -19.299 1.00 58.37  ? 212 ASP A OD2   1 
ATOM   1754 N  N     . ASN A 1 213 ? -45.118 23.606  -18.713 1.00 49.13  ? 213 ASN A N     1 
ATOM   1755 C  CA    . ASN A 1 213 ? -45.602 22.351  -19.274 1.00 61.95  ? 213 ASN A CA    1 
ATOM   1756 C  C     . ASN A 1 213 ? -46.871 21.839  -18.604 1.00 61.39  ? 213 ASN A C     1 
ATOM   1757 O  O     . ASN A 1 213 ? -47.266 20.695  -18.854 1.00 64.05  ? 213 ASN A O     1 
ATOM   1758 C  CB    . ASN A 1 213 ? -44.504 21.286  -19.196 1.00 59.30  ? 213 ASN A CB    1 
ATOM   1759 C  CG    . ASN A 1 213 ? -43.262 21.675  -19.972 1.00 68.08  ? 213 ASN A CG    1 
ATOM   1760 O  OD1   . ASN A 1 213 ? -43.215 21.550  -21.196 1.00 71.65  ? 213 ASN A OD1   1 
ATOM   1761 N  ND2   . ASN A 1 213 ? -42.248 22.157  -19.262 1.00 67.74  ? 213 ASN A ND2   1 
ATOM   1762 N  N     . PHE A 1 214 ? -47.525 22.643  -17.767 1.00 60.18  ? 214 PHE A N     1 
ATOM   1763 C  CA    . PHE A 1 214 ? -48.761 22.191  -17.140 1.00 63.55  ? 214 PHE A CA    1 
ATOM   1764 C  C     . PHE A 1 214 ? -49.748 23.325  -16.896 1.00 61.55  ? 214 PHE A C     1 
ATOM   1765 O  O     . PHE A 1 214 ? -50.758 23.433  -17.599 1.00 65.56  ? 214 PHE A O     1 
ATOM   1766 C  CB    . PHE A 1 214 ? -48.470 21.480  -15.817 1.00 64.57  ? 214 PHE A CB    1 
ATOM   1767 C  CG    . PHE A 1 214 ? -49.703 20.957  -15.133 1.00 69.60  ? 214 PHE A CG    1 
ATOM   1768 C  CD1   . PHE A 1 214 ? -50.355 19.833  -15.614 1.00 69.64  ? 214 PHE A CD1   1 
ATOM   1769 C  CD2   . PHE A 1 214 ? -50.221 21.599  -14.018 1.00 66.34  ? 214 PHE A CD2   1 
ATOM   1770 C  CE1   . PHE A 1 214 ? -51.494 19.354  -14.992 1.00 76.00  ? 214 PHE A CE1   1 
ATOM   1771 C  CE2   . PHE A 1 214 ? -51.360 21.124  -13.393 1.00 72.77  ? 214 PHE A CE2   1 
ATOM   1772 C  CZ    . PHE A 1 214 ? -51.996 20.001  -13.880 1.00 76.14  ? 214 PHE A CZ    1 
ATOM   1773 N  N     . ASP A 1 215 ? -49.460 24.167  -15.899 1.00 59.57  ? 215 ASP A N     1 
ATOM   1774 C  CA    . ASP A 1 215 ? -50.445 25.125  -15.401 1.00 61.31  ? 215 ASP A CA    1 
ATOM   1775 C  C     . ASP A 1 215 ? -50.994 26.003  -16.521 1.00 64.75  ? 215 ASP A C     1 
ATOM   1776 O  O     . ASP A 1 215 ? -52.209 26.213  -16.627 1.00 64.07  ? 215 ASP A O     1 
ATOM   1777 C  CB    . ASP A 1 215 ? -49.822 25.986  -14.299 1.00 60.85  ? 215 ASP A CB    1 
ATOM   1778 C  CG    . ASP A 1 215 ? -49.132 25.160  -13.227 1.00 61.12  ? 215 ASP A CG    1 
ATOM   1779 O  OD1   . ASP A 1 215 ? -48.145 24.470  -13.554 1.00 66.03  ? 215 ASP A OD1   1 
ATOM   1780 O  OD2   . ASP A 1 215 ? -49.567 25.207  -12.056 1.00 58.79  ? 215 ASP A OD2   1 
ATOM   1781 N  N     . PHE A 1 216 ? -50.112 26.515  -17.382 1.00 60.30  ? 216 PHE A N     1 
ATOM   1782 C  CA    . PHE A 1 216 ? -50.558 27.446  -18.414 1.00 59.82  ? 216 PHE A CA    1 
ATOM   1783 C  C     . PHE A 1 216 ? -51.362 26.740  -19.499 1.00 60.35  ? 216 PHE A C     1 
ATOM   1784 O  O     . PHE A 1 216 ? -52.392 27.256  -19.944 1.00 58.84  ? 216 PHE A O     1 
ATOM   1785 C  CB    . PHE A 1 216 ? -49.362 28.181  -19.012 1.00 59.85  ? 216 PHE A CB    1 
ATOM   1786 C  CG    . PHE A 1 216 ? -49.034 29.464  -18.308 1.00 57.55  ? 216 PHE A CG    1 
ATOM   1787 C  CD1   . PHE A 1 216 ? -49.850 30.573  -18.451 1.00 58.16  ? 216 PHE A CD1   1 
ATOM   1788 C  CD2   . PHE A 1 216 ? -47.918 29.560  -17.497 1.00 50.45  ? 216 PHE A CD2   1 
ATOM   1789 C  CE1   . PHE A 1 216 ? -49.555 31.757  -17.802 1.00 59.24  ? 216 PHE A CE1   1 
ATOM   1790 C  CE2   . PHE A 1 216 ? -47.617 30.741  -16.846 1.00 52.52  ? 216 PHE A CE2   1 
ATOM   1791 C  CZ    . PHE A 1 216 ? -48.437 31.841  -16.999 1.00 53.05  ? 216 PHE A CZ    1 
ATOM   1792 N  N     . ALA A 1 217 ? -50.917 25.558  -19.935 1.00 61.37  ? 217 ALA A N     1 
ATOM   1793 C  CA    . ALA A 1 217 ? -51.666 24.819  -20.948 1.00 63.65  ? 217 ALA A CA    1 
ATOM   1794 C  C     . ALA A 1 217 ? -53.016 24.358  -20.409 1.00 68.07  ? 217 ALA A C     1 
ATOM   1795 O  O     . ALA A 1 217 ? -54.025 24.376  -21.130 1.00 66.45  ? 217 ALA A O     1 
ATOM   1796 C  CB    . ALA A 1 217 ? -50.845 23.627  -21.439 1.00 54.65  ? 217 ALA A CB    1 
ATOM   1797 N  N     . TYR A 1 218 ? -53.049 23.945  -19.141 1.00 63.15  ? 218 TYR A N     1 
ATOM   1798 C  CA    . TYR A 1 218 ? -54.308 23.583  -18.500 1.00 68.54  ? 218 TYR A CA    1 
ATOM   1799 C  C     . TYR A 1 218 ? -55.261 24.770  -18.463 1.00 67.14  ? 218 TYR A C     1 
ATOM   1800 O  O     . TYR A 1 218 ? -56.435 24.654  -18.843 1.00 68.30  ? 218 TYR A O     1 
ATOM   1801 C  CB    . TYR A 1 218 ? -54.037 23.064  -17.087 1.00 65.01  ? 218 TYR A CB    1 
ATOM   1802 C  CG    . TYR A 1 218 ? -55.105 22.132  -16.584 1.00 74.86  ? 218 TYR A CG    1 
ATOM   1803 C  CD1   . TYR A 1 218 ? -54.828 20.793  -16.350 1.00 79.22  ? 218 TYR A CD1   1 
ATOM   1804 C  CD2   . TYR A 1 218 ? -56.394 22.587  -16.351 1.00 78.13  ? 218 TYR A CD2   1 
ATOM   1805 C  CE1   . TYR A 1 218 ? -55.807 19.932  -15.902 1.00 79.48  ? 218 TYR A CE1   1 
ATOM   1806 C  CE2   . TYR A 1 218 ? -57.375 21.739  -15.901 1.00 77.70  ? 218 TYR A CE2   1 
ATOM   1807 C  CZ    . TYR A 1 218 ? -57.082 20.412  -15.685 1.00 81.57  ? 218 TYR A CZ    1 
ATOM   1808 O  OH    . TYR A 1 218 ? -58.063 19.565  -15.221 1.00 86.05  ? 218 TYR A OH    1 
ATOM   1809 N  N     . LEU A 1 219 ? -54.772 25.920  -17.990 1.00 63.69  ? 219 LEU A N     1 
ATOM   1810 C  CA    . LEU A 1 219 ? -55.599 27.118  -17.965 1.00 60.84  ? 219 LEU A CA    1 
ATOM   1811 C  C     . LEU A 1 219 ? -56.053 27.511  -19.364 1.00 68.70  ? 219 LEU A C     1 
ATOM   1812 O  O     . LEU A 1 219 ? -57.164 28.016  -19.529 1.00 73.58  ? 219 LEU A O     1 
ATOM   1813 C  CB    . LEU A 1 219 ? -54.838 28.268  -17.306 1.00 62.47  ? 219 LEU A CB    1 
ATOM   1814 C  CG    . LEU A 1 219 ? -55.143 28.493  -15.824 1.00 59.32  ? 219 LEU A CG    1 
ATOM   1815 C  CD1   . LEU A 1 219 ? -53.974 29.180  -15.138 1.00 67.82  ? 219 LEU A CD1   1 
ATOM   1816 C  CD2   . LEU A 1 219 ? -56.418 29.302  -15.659 1.00 61.70  ? 219 LEU A CD2   1 
ATOM   1817 N  N     . LYS A 1 220 ? -55.225 27.264  -20.380 1.00 69.55  ? 220 LYS A N     1 
ATOM   1818 C  CA    . LYS A 1 220 ? -55.613 27.573  -21.754 1.00 74.17  ? 220 LYS A CA    1 
ATOM   1819 C  C     . LYS A 1 220 ? -56.774 26.696  -22.211 1.00 71.82  ? 220 LYS A C     1 
ATOM   1820 O  O     . LYS A 1 220 ? -57.760 27.193  -22.773 1.00 66.38  ? 220 LYS A O     1 
ATOM   1821 C  CB    . LYS A 1 220 ? -54.410 27.399  -22.682 1.00 56.96  ? 220 LYS A CB    1 
ATOM   1822 C  CG    . LYS A 1 220 ? -54.647 27.847  -24.113 1.00 59.73  ? 220 LYS A CG    1 
ATOM   1823 C  CD    . LYS A 1 220 ? -53.616 27.241  -25.050 1.00 64.77  ? 220 LYS A CD    1 
ATOM   1824 C  CE    . LYS A 1 220 ? -53.629 27.922  -26.408 1.00 73.42  ? 220 LYS A CE    1 
ATOM   1825 N  NZ    . LYS A 1 220 ? -53.046 27.052  -27.467 1.00 78.65  ? 220 LYS A NZ    1 
ATOM   1826 N  N     . LYS A 1 221 ? -56.661 25.383  -21.992 1.00 69.89  ? 221 LYS A N     1 
ATOM   1827 C  CA    . LYS A 1 221 ? -57.744 24.473  -22.358 1.00 78.77  ? 221 LYS A CA    1 
ATOM   1828 C  C     . LYS A 1 221 ? -59.040 24.844  -21.647 1.00 83.28  ? 221 LYS A C     1 
ATOM   1829 O  O     . LYS A 1 221 ? -60.114 24.875  -22.264 1.00 84.62  ? 221 LYS A O     1 
ATOM   1830 C  CB    . LYS A 1 221 ? -57.354 23.031  -22.035 1.00 80.87  ? 221 LYS A CB    1 
ATOM   1831 C  CG    . LYS A 1 221 ? -57.705 22.025  -23.121 1.00 87.10  ? 221 LYS A CG    1 
ATOM   1832 C  CD    . LYS A 1 221 ? -56.472 21.610  -23.907 1.00 93.78  ? 221 LYS A CD    1 
ATOM   1833 C  CE    . LYS A 1 221 ? -56.775 20.455  -24.848 1.00 90.38  ? 221 LYS A CE    1 
ATOM   1834 N  NZ    . LYS A 1 221 ? -55.529 19.839  -25.385 1.00 89.02  ? 221 LYS A NZ    1 
ATOM   1835 N  N     . ARG A 1 222 ? -58.961 25.144  -20.349 1.00 77.01  ? 222 ARG A N     1 
ATOM   1836 C  CA    . ARG A 1 222 ? -60.179 25.491  -19.624 1.00 74.01  ? 222 ARG A CA    1 
ATOM   1837 C  C     . ARG A 1 222 ? -60.726 26.844  -20.066 1.00 78.16  ? 222 ARG A C     1 
ATOM   1838 O  O     . ARG A 1 222 ? -61.945 27.020  -20.167 1.00 87.03  ? 222 ARG A O     1 
ATOM   1839 C  CB    . ARG A 1 222 ? -59.923 25.469  -18.119 1.00 73.44  ? 222 ARG A CB    1 
ATOM   1840 C  CG    . ARG A 1 222 ? -59.267 24.189  -17.637 1.00 71.61  ? 222 ARG A CG    1 
ATOM   1841 C  CD    . ARG A 1 222 ? -60.120 22.973  -17.934 1.00 66.82  ? 222 ARG A CD    1 
ATOM   1842 N  NE    . ARG A 1 222 ? -61.478 23.121  -17.426 1.00 77.71  ? 222 ARG A NE    1 
ATOM   1843 C  CZ    . ARG A 1 222 ? -62.433 22.212  -17.569 1.00 76.99  ? 222 ARG A CZ    1 
ATOM   1844 N  NH1   . ARG A 1 222 ? -62.215 21.073  -18.206 1.00 73.20  ? 222 ARG A NH1   1 
ATOM   1845 N  NH2   . ARG A 1 222 ? -63.637 22.451  -17.058 1.00 74.49  ? 222 ARG A NH2   1 
ATOM   1846 N  N     . CYS A 1 223 ? -59.846 27.806  -20.359 1.00 77.64  ? 223 CYS A N     1 
ATOM   1847 C  CA    . CYS A 1 223 ? -60.293 29.131  -20.772 1.00 80.59  ? 223 CYS A CA    1 
ATOM   1848 C  C     . CYS A 1 223 ? -60.995 29.080  -22.121 1.00 84.08  ? 223 CYS A C     1 
ATOM   1849 O  O     . CYS A 1 223 ? -61.960 29.818  -22.351 1.00 85.21  ? 223 CYS A O     1 
ATOM   1850 C  CB    . CYS A 1 223 ? -59.103 30.091  -20.825 1.00 77.43  ? 223 CYS A CB    1 
ATOM   1851 S  SG    . CYS A 1 223 ? -58.683 30.895  -19.258 1.00 75.81  ? 223 CYS A SG    1 
ATOM   1852 N  N     . GLU A 1 224 ? -60.524 28.222  -23.030 1.00 87.59  ? 224 GLU A N     1 
ATOM   1853 C  CA    . GLU A 1 224 ? -61.221 28.090  -24.304 1.00 95.82  ? 224 GLU A CA    1 
ATOM   1854 C  C     . GLU A 1 224 ? -62.485 27.249  -24.173 1.00 95.72  ? 224 GLU A C     1 
ATOM   1855 O  O     . GLU A 1 224 ? -63.441 27.462  -24.927 1.00 93.62  ? 224 GLU A O     1 
ATOM   1856 C  CB    . GLU A 1 224 ? -60.299 27.496  -25.373 1.00 113.70 ? 224 GLU A CB    1 
ATOM   1857 C  CG    . GLU A 1 224 ? -59.744 26.122  -25.053 1.00 114.53 ? 224 GLU A CG    1 
ATOM   1858 C  CD    . GLU A 1 224 ? -59.664 25.228  -26.275 1.00 134.95 ? 224 GLU A CD    1 
ATOM   1859 O  OE1   . GLU A 1 224 ? -60.173 25.632  -27.341 1.00 155.91 ? 224 GLU A OE1   1 
ATOM   1860 O  OE2   . GLU A 1 224 ? -59.097 24.120  -26.167 1.00 115.54 ? 224 GLU A OE2   1 
ATOM   1861 N  N     . LYS A 1 225 ? -62.519 26.303  -23.228 1.00 94.23  ? 225 LYS A N     1 
ATOM   1862 C  CA    . LYS A 1 225 ? -63.732 25.512  -23.044 1.00 87.35  ? 225 LYS A CA    1 
ATOM   1863 C  C     . LYS A 1 225 ? -64.857 26.328  -22.415 1.00 87.53  ? 225 LYS A C     1 
ATOM   1864 O  O     . LYS A 1 225 ? -66.034 26.009  -22.614 1.00 94.15  ? 225 LYS A O     1 
ATOM   1865 C  CB    . LYS A 1 225 ? -63.437 24.275  -22.197 1.00 87.35  ? 225 LYS A CB    1 
ATOM   1866 C  CG    . LYS A 1 225 ? -63.033 23.060  -23.017 1.00 96.20  ? 225 LYS A CG    1 
ATOM   1867 C  CD    . LYS A 1 225 ? -63.655 21.785  -22.472 1.00 95.59  ? 225 LYS A CD    1 
ATOM   1868 C  CE    . LYS A 1 225 ? -62.613 20.689  -22.316 1.00 96.38  ? 225 LYS A CE    1 
ATOM   1869 N  NZ    . LYS A 1 225 ? -62.829 19.886  -21.082 1.00 96.95  ? 225 LYS A NZ    1 
ATOM   1870 N  N     . LEU A 1 226 ? -64.525 27.375  -21.661 1.00 88.09  ? 226 LEU A N     1 
ATOM   1871 C  CA    . LEU A 1 226 ? -65.527 28.229  -21.036 1.00 84.57  ? 226 LEU A CA    1 
ATOM   1872 C  C     . LEU A 1 226 ? -65.587 29.624  -21.642 1.00 85.35  ? 226 LEU A C     1 
ATOM   1873 O  O     . LEU A 1 226 ? -66.355 30.462  -21.156 1.00 81.29  ? 226 LEU A O     1 
ATOM   1874 C  CB    . LEU A 1 226 ? -65.272 28.334  -19.527 1.00 85.91  ? 226 LEU A CB    1 
ATOM   1875 C  CG    . LEU A 1 226 ? -64.713 27.089  -18.838 1.00 85.61  ? 226 LEU A CG    1 
ATOM   1876 C  CD1   . LEU A 1 226 ? -64.141 27.446  -17.476 1.00 79.92  ? 226 LEU A CD1   1 
ATOM   1877 C  CD2   . LEU A 1 226 ? -65.779 26.013  -18.716 1.00 82.60  ? 226 LEU A CD2   1 
ATOM   1878 N  N     . GLY A 1 227 ? -64.802 29.899  -22.680 1.00 82.58  ? 227 GLY A N     1 
ATOM   1879 C  CA    . GLY A 1 227 ? -64.854 31.182  -23.353 1.00 83.19  ? 227 GLY A CA    1 
ATOM   1880 C  C     . GLY A 1 227 ? -64.338 32.343  -22.531 1.00 87.18  ? 227 GLY A C     1 
ATOM   1881 O  O     . GLY A 1 227 ? -65.044 33.339  -22.339 1.00 85.33  ? 227 GLY A O     1 
ATOM   1882 N  N     . ILE A 1 228 ? -63.107 32.231  -22.041 1.00 84.20  ? 228 ILE A N     1 
ATOM   1883 C  CA    . ILE A 1 228 ? -62.457 33.288  -21.278 1.00 83.44  ? 228 ILE A CA    1 
ATOM   1884 C  C     . ILE A 1 228 ? -61.254 33.784  -22.064 1.00 86.76  ? 228 ILE A C     1 
ATOM   1885 O  O     . ILE A 1 228 ? -60.490 32.986  -22.618 1.00 85.82  ? 228 ILE A O     1 
ATOM   1886 C  CB    . ILE A 1 228 ? -62.020 32.807  -19.880 1.00 86.36  ? 228 ILE A CB    1 
ATOM   1887 C  CG1   . ILE A 1 228 ? -63.128 31.988  -19.216 1.00 85.23  ? 228 ILE A CG1   1 
ATOM   1888 C  CG2   . ILE A 1 228 ? -61.623 33.995  -19.011 1.00 87.77  ? 228 ILE A CG2   1 
ATOM   1889 C  CD1   . ILE A 1 228 ? -63.000 31.912  -17.710 1.00 84.72  ? 228 ILE A CD1   1 
ATOM   1890 N  N     . ASN A 1 229 ? -61.088 35.102  -22.114 1.00 85.41  ? 229 ASN A N     1 
ATOM   1891 C  CA    . ASN A 1 229 ? -59.900 35.711  -22.700 1.00 87.23  ? 229 ASN A CA    1 
ATOM   1892 C  C     . ASN A 1 229 ? -58.819 35.771  -21.628 1.00 84.15  ? 229 ASN A C     1 
ATOM   1893 O  O     . ASN A 1 229 ? -58.912 36.561  -20.684 1.00 81.47  ? 229 ASN A O     1 
ATOM   1894 C  CB    . ASN A 1 229 ? -60.214 37.099  -23.250 1.00 92.58  ? 229 ASN A CB    1 
ATOM   1895 C  CG    . ASN A 1 229 ? -59.355 37.454  -24.442 1.00 92.57  ? 229 ASN A CG    1 
ATOM   1896 O  OD1   . ASN A 1 229 ? -58.678 38.482  -24.450 1.00 100.28 ? 229 ASN A OD1   1 
ATOM   1897 N  ND2   . ASN A 1 229 ? -59.363 36.594  -25.454 1.00 98.52  ? 229 ASN A ND2   1 
ATOM   1898 N  N     . PHE A 1 230 ? -57.793 34.931  -21.774 1.00 83.81  ? 230 PHE A N     1 
ATOM   1899 C  CA    . PHE A 1 230 ? -56.732 34.803  -20.775 1.00 77.05  ? 230 PHE A CA    1 
ATOM   1900 C  C     . PHE A 1 230 ? -55.720 35.945  -20.909 1.00 74.33  ? 230 PHE A C     1 
ATOM   1901 O  O     . PHE A 1 230 ? -54.518 35.743  -21.073 1.00 72.98  ? 230 PHE A O     1 
ATOM   1902 C  CB    . PHE A 1 230 ? -56.057 33.444  -20.916 1.00 79.23  ? 230 PHE A CB    1 
ATOM   1903 C  CG    . PHE A 1 230 ? -55.441 32.930  -19.646 1.00 87.32  ? 230 PHE A CG    1 
ATOM   1904 C  CD1   . PHE A 1 230 ? -54.211 32.290  -19.674 1.00 83.39  ? 230 PHE A CD1   1 
ATOM   1905 C  CD2   . PHE A 1 230 ? -56.090 33.070  -18.433 1.00 82.67  ? 230 PHE A CD2   1 
ATOM   1906 C  CE1   . PHE A 1 230 ? -53.638 31.810  -18.515 1.00 94.13  ? 230 PHE A CE1   1 
ATOM   1907 C  CE2   . PHE A 1 230 ? -55.518 32.584  -17.267 1.00 80.23  ? 230 PHE A CE2   1 
ATOM   1908 C  CZ    . PHE A 1 230 ? -54.294 31.959  -17.309 1.00 74.01  ? 230 PHE A CZ    1 
ATOM   1909 N  N     . ALA A 1 231 ? -56.235 37.173  -20.825 1.00 71.28  ? 231 ALA A N     1 
ATOM   1910 C  CA    . ALA A 1 231 ? -55.432 38.374  -21.065 1.00 72.63  ? 231 ALA A CA    1 
ATOM   1911 C  C     . ALA A 1 231 ? -54.533 38.653  -19.859 1.00 73.69  ? 231 ALA A C     1 
ATOM   1912 O  O     . ALA A 1 231 ? -54.731 39.592  -19.085 1.00 89.24  ? 231 ALA A O     1 
ATOM   1913 C  CB    . ALA A 1 231 ? -56.331 39.562  -21.379 1.00 74.29  ? 231 ALA A CB    1 
ATOM   1914 N  N     . LEU A 1 232 ? -53.513 37.804  -19.709 1.00 67.42  ? 232 LEU A N     1 
ATOM   1915 C  CA    . LEU A 1 232 ? -52.519 38.027  -18.666 1.00 63.80  ? 232 LEU A CA    1 
ATOM   1916 C  C     . LEU A 1 232 ? -51.444 39.009  -19.105 1.00 58.39  ? 232 LEU A C     1 
ATOM   1917 O  O     . LEU A 1 232 ? -50.862 39.699  -18.261 1.00 66.97  ? 232 LEU A O     1 
ATOM   1918 C  CB    . LEU A 1 232 ? -51.864 36.709  -18.255 1.00 62.80  ? 232 LEU A CB    1 
ATOM   1919 C  CG    . LEU A 1 232 ? -52.638 35.789  -17.315 1.00 67.71  ? 232 LEU A CG    1 
ATOM   1920 C  CD1   . LEU A 1 232 ? -51.841 34.518  -17.083 1.00 66.37  ? 232 LEU A CD1   1 
ATOM   1921 C  CD2   . LEU A 1 232 ? -52.949 36.483  -16.000 1.00 56.56  ? 232 LEU A CD2   1 
ATOM   1922 N  N     . GLY A 1 233 ? -51.164 39.082  -20.404 1.00 57.41  ? 233 GLY A N     1 
ATOM   1923 C  CA    . GLY A 1 233 ? -50.136 39.988  -20.879 1.00 71.45  ? 233 GLY A CA    1 
ATOM   1924 C  C     . GLY A 1 233 ? -50.493 41.439  -20.618 1.00 71.10  ? 233 GLY A C     1 
ATOM   1925 O  O     . GLY A 1 233 ? -51.661 41.833  -20.638 1.00 68.99  ? 233 GLY A O     1 
ATOM   1926 N  N     . ARG A 1 234 ? -49.459 42.244  -20.365 1.00 68.65  ? 234 ARG A N     1 
ATOM   1927 C  CA    . ARG A 1 234 ? -49.670 43.660  -20.088 1.00 68.18  ? 234 ARG A CA    1 
ATOM   1928 C  C     . ARG A 1 234 ? -50.233 44.402  -21.291 1.00 74.31  ? 234 ARG A C     1 
ATOM   1929 O  O     . ARG A 1 234 ? -50.816 45.479  -21.125 1.00 78.77  ? 234 ARG A O     1 
ATOM   1930 C  CB    . ARG A 1 234 ? -48.360 44.304  -19.635 1.00 66.24  ? 234 ARG A CB    1 
ATOM   1931 C  CG    . ARG A 1 234 ? -48.094 44.173  -18.143 1.00 68.36  ? 234 ARG A CG    1 
ATOM   1932 C  CD    . ARG A 1 234 ? -47.243 45.320  -17.630 1.00 59.80  ? 234 ARG A CD    1 
ATOM   1933 N  NE    . ARG A 1 234 ? -45.891 44.886  -17.301 1.00 61.30  ? 234 ARG A NE    1 
ATOM   1934 C  CZ    . ARG A 1 234 ? -45.377 44.888  -16.079 1.00 58.86  ? 234 ARG A CZ    1 
ATOM   1935 N  NH1   . ARG A 1 234 ? -46.076 45.300  -15.035 1.00 47.59  ? 234 ARG A NH1   1 
ATOM   1936 N  NH2   . ARG A 1 234 ? -44.127 44.469  -15.901 1.00 65.11  ? 234 ARG A NH2   1 
ATOM   1937 N  N     . ASP A 1 235 ? -50.074 43.854  -22.494 1.00 75.25  ? 235 ASP A N     1 
ATOM   1938 C  CA    . ASP A 1 235 ? -50.645 44.433  -23.701 1.00 79.93  ? 235 ASP A CA    1 
ATOM   1939 C  C     . ASP A 1 235 ? -51.999 43.832  -24.057 1.00 75.93  ? 235 ASP A C     1 
ATOM   1940 O  O     . ASP A 1 235 ? -52.493 44.062  -25.165 1.00 79.31  ? 235 ASP A O     1 
ATOM   1941 C  CB    . ASP A 1 235 ? -49.674 44.268  -24.875 1.00 79.48  ? 235 ASP A CB    1 
ATOM   1942 C  CG    . ASP A 1 235 ? -49.518 42.821  -25.306 1.00 81.85  ? 235 ASP A CG    1 
ATOM   1943 O  OD1   . ASP A 1 235 ? -49.708 41.921  -24.460 1.00 80.53  ? 235 ASP A OD1   1 
ATOM   1944 O  OD2   . ASP A 1 235 ? -49.203 42.585  -26.492 1.00 78.53  ? 235 ASP A OD2   1 
ATOM   1945 N  N     . GLY A 1 236 ? -52.604 43.068  -23.150 1.00 75.03  ? 236 GLY A N     1 
ATOM   1946 C  CA    . GLY A 1 236 ? -53.892 42.457  -23.394 1.00 75.56  ? 236 GLY A CA    1 
ATOM   1947 C  C     . GLY A 1 236 ? -53.850 41.097  -24.057 1.00 79.85  ? 236 GLY A C     1 
ATOM   1948 O  O     . GLY A 1 236 ? -54.910 40.483  -24.240 1.00 80.54  ? 236 GLY A O     1 
ATOM   1949 N  N     . SER A 1 237 ? -52.670 40.605  -24.422 1.00 69.43  ? 237 SER A N     1 
ATOM   1950 C  CA    . SER A 1 237 ? -52.559 39.315  -25.080 1.00 69.62  ? 237 SER A CA    1 
ATOM   1951 C  C     . SER A 1 237 ? -52.631 38.182  -24.059 1.00 63.04  ? 237 SER A C     1 
ATOM   1952 O  O     . SER A 1 237 ? -52.578 38.394  -22.844 1.00 69.43  ? 237 SER A O     1 
ATOM   1953 C  CB    . SER A 1 237 ? -51.256 39.229  -25.873 1.00 73.25  ? 237 SER A CB    1 
ATOM   1954 O  OG    . SER A 1 237 ? -50.136 39.196  -25.006 1.00 63.81  ? 237 SER A OG    1 
ATOM   1955 N  N     . GLU A 1 238 ? -52.753 36.964  -24.569 1.00 60.15  ? 238 GLU A N     1 
ATOM   1956 C  CA    . GLU A 1 238 ? -52.769 35.765  -23.749 1.00 67.75  ? 238 GLU A CA    1 
ATOM   1957 C  C     . GLU A 1 238 ? -51.454 35.002  -23.889 1.00 67.34  ? 238 GLU A C     1 
ATOM   1958 O  O     . GLU A 1 238 ? -50.693 35.229  -24.836 1.00 64.78  ? 238 GLU A O     1 
ATOM   1959 C  CB    . GLU A 1 238 ? -53.954 34.861  -24.126 1.00 67.87  ? 238 GLU A CB    1 
ATOM   1960 C  CG    . GLU A 1 238 ? -54.296 34.814  -25.602 1.00 78.64  ? 238 GLU A CG    1 
ATOM   1961 C  CD    . GLU A 1 238 ? -55.639 34.153  -25.857 1.00 92.58  ? 238 GLU A CD    1 
ATOM   1962 O  OE1   . GLU A 1 238 ? -56.312 33.770  -24.875 1.00 88.96  ? 238 GLU A OE1   1 
ATOM   1963 O  OE2   . GLU A 1 238 ? -56.024 34.015  -27.037 1.00 98.57  ? 238 GLU A OE2   1 
ATOM   1964 N  N     . PRO A 1 239 ? -51.140 34.117  -22.939 1.00 64.26  ? 239 PRO A N     1 
ATOM   1965 C  CA    . PRO A 1 239 ? -49.857 33.402  -22.975 1.00 62.58  ? 239 PRO A CA    1 
ATOM   1966 C  C     . PRO A 1 239 ? -49.575 32.752  -24.322 1.00 66.29  ? 239 PRO A C     1 
ATOM   1967 O  O     . PRO A 1 239 ? -50.409 32.035  -24.876 1.00 70.19  ? 239 PRO A O     1 
ATOM   1968 C  CB    . PRO A 1 239 ? -50.018 32.354  -21.871 1.00 60.73  ? 239 PRO A CB    1 
ATOM   1969 C  CG    . PRO A 1 239 ? -50.918 33.000  -20.885 1.00 64.28  ? 239 PRO A CG    1 
ATOM   1970 C  CD    . PRO A 1 239 ? -51.838 33.916  -21.656 1.00 67.92  ? 239 PRO A CD    1 
ATOM   1971 N  N     . LYS A 1 240 ? -48.379 33.014  -24.845 1.00 66.60  ? 240 LYS A N     1 
ATOM   1972 C  CA    . LYS A 1 240 ? -47.933 32.478  -26.125 1.00 71.96  ? 240 LYS A CA    1 
ATOM   1973 C  C     . LYS A 1 240 ? -47.099 31.227  -25.873 1.00 73.43  ? 240 LYS A C     1 
ATOM   1974 O  O     . LYS A 1 240 ? -46.115 31.273  -25.128 1.00 76.83  ? 240 LYS A O     1 
ATOM   1975 C  CB    . LYS A 1 240 ? -47.120 33.521  -26.892 1.00 79.32  ? 240 LYS A CB    1 
ATOM   1976 C  CG    . LYS A 1 240 ? -47.357 33.531  -28.391 1.00 100.42 ? 240 LYS A CG    1 
ATOM   1977 C  CD    . LYS A 1 240 ? -46.225 34.243  -29.119 1.00 102.40 ? 240 LYS A CD    1 
ATOM   1978 C  CE    . LYS A 1 240 ? -46.469 34.280  -30.620 1.00 117.79 ? 240 LYS A CE    1 
ATOM   1979 N  NZ    . LYS A 1 240 ? -47.365 35.403  -31.011 1.00 119.98 ? 240 LYS A NZ    1 
ATOM   1980 N  N     . ILE A 1 241 ? -47.482 30.124  -26.493 1.00 71.87  ? 241 ILE A N     1 
ATOM   1981 C  CA    . ILE A 1 241 ? -46.771 28.861  -26.333 1.00 73.98  ? 241 ILE A CA    1 
ATOM   1982 C  C     . ILE A 1 241 ? -45.703 28.761  -27.413 1.00 81.05  ? 241 ILE A C     1 
ATOM   1983 O  O     . ILE A 1 241 ? -45.952 29.069  -28.584 1.00 86.85  ? 241 ILE A O     1 
ATOM   1984 C  CB    . ILE A 1 241 ? -47.743 27.665  -26.389 1.00 76.28  ? 241 ILE A CB    1 
ATOM   1985 C  CG1   . ILE A 1 241 ? -48.686 27.667  -25.178 1.00 75.33  ? 241 ILE A CG1   1 
ATOM   1986 C  CG2   . ILE A 1 241 ? -46.979 26.350  -26.456 1.00 75.72  ? 241 ILE A CG2   1 
ATOM   1987 C  CD1   . ILE A 1 241 ? -49.975 28.450  -25.381 1.00 73.85  ? 241 ILE A CD1   1 
ATOM   1988 N  N     . GLN A 1 242 ? -44.502 28.341  -27.018 1.00 85.29  ? 242 GLN A N     1 
ATOM   1989 C  CA    . GLN A 1 242 ? -43.379 28.221  -27.934 1.00 89.26  ? 242 GLN A CA    1 
ATOM   1990 C  C     . GLN A 1 242 ? -42.677 26.890  -27.698 1.00 90.91  ? 242 GLN A C     1 
ATOM   1991 O  O     . GLN A 1 242 ? -42.804 26.276  -26.637 1.00 85.07  ? 242 GLN A O     1 
ATOM   1992 C  CB    . GLN A 1 242 ? -42.388 29.382  -27.766 1.00 88.26  ? 242 GLN A CB    1 
ATOM   1993 C  CG    . GLN A 1 242 ? -42.940 30.738  -28.177 1.00 94.75  ? 242 GLN A CG    1 
ATOM   1994 C  CD    . GLN A 1 242 ? -41.879 31.819  -28.170 1.00 103.11 ? 242 GLN A CD    1 
ATOM   1995 O  OE1   . GLN A 1 242 ? -40.774 31.616  -27.666 1.00 101.96 ? 242 GLN A OE1   1 
ATOM   1996 N  NE2   . GLN A 1 242 ? -42.211 32.979  -28.725 1.00 115.48 ? 242 GLN A NE2   1 
ATOM   1997 N  N     . ARG A 1 243 ? -41.929 26.456  -28.706 1.00 99.41  ? 243 ARG A N     1 
ATOM   1998 C  CA    . ARG A 1 243 ? -41.166 25.217  -28.628 1.00 104.08 ? 243 ARG A CA    1 
ATOM   1999 C  C     . ARG A 1 243 ? -39.842 25.452  -27.911 1.00 100.01 ? 243 ARG A C     1 
ATOM   2000 O  O     . ARG A 1 243 ? -39.195 26.486  -28.103 1.00 102.12 ? 243 ARG A O     1 
ATOM   2001 C  CB    . ARG A 1 243 ? -40.917 24.682  -30.038 1.00 114.26 ? 243 ARG A CB    1 
ATOM   2002 C  CG    . ARG A 1 243 ? -40.726 23.179  -30.154 1.00 119.49 ? 243 ARG A CG    1 
ATOM   2003 C  CD    . ARG A 1 243 ? -40.382 22.813  -31.595 1.00 132.18 ? 243 ARG A CD    1 
ATOM   2004 N  NE    . ARG A 1 243 ? -39.217 23.527  -32.111 1.00 144.41 ? 243 ARG A NE    1 
ATOM   2005 C  CZ    . ARG A 1 243 ? -37.987 23.442  -31.619 1.00 134.36 ? 243 ARG A CZ    1 
ATOM   2006 N  NH1   . ARG A 1 243 ? -37.687 22.602  -30.644 1.00 127.45 ? 243 ARG A NH1   1 
ATOM   2007 N  NH2   . ARG A 1 243 ? -37.025 24.199  -32.141 1.00 127.61 ? 243 ARG A NH2   1 
ATOM   2008 N  N     . MET A 1 244 ? -39.430 24.485  -27.087 1.00 94.83  ? 244 MET A N     1 
ATOM   2009 C  CA    . MET A 1 244 ? -38.159 24.551  -26.366 1.00 93.22  ? 244 MET A CA    1 
ATOM   2010 C  C     . MET A 1 244 ? -37.452 23.203  -26.482 1.00 91.92  ? 244 MET A C     1 
ATOM   2011 O  O     . MET A 1 244 ? -37.114 22.556  -25.490 1.00 92.01  ? 244 MET A O     1 
ATOM   2012 C  CB    . MET A 1 244 ? -38.359 24.928  -24.900 1.00 85.46  ? 244 MET A CB    1 
ATOM   2013 C  CG    . MET A 1 244 ? -37.177 25.660  -24.283 1.00 79.16  ? 244 MET A CG    1 
ATOM   2014 S  SD    . MET A 1 244 ? -37.081 27.381  -24.805 1.00 85.50  ? 244 MET A SD    1 
ATOM   2015 C  CE    . MET A 1 244 ? -35.374 27.475  -25.341 1.00 66.17  ? 244 MET A CE    1 
ATOM   2016 N  N     . GLY A 1 245 ? -37.222 22.782  -27.723 1.00 97.83  ? 245 GLY A N     1 
ATOM   2017 C  CA    . GLY A 1 245 ? -36.696 21.459  -27.993 1.00 99.07  ? 245 GLY A CA    1 
ATOM   2018 C  C     . GLY A 1 245 ? -37.790 20.414  -27.961 1.00 101.06 ? 245 GLY A C     1 
ATOM   2019 O  O     . GLY A 1 245 ? -38.679 20.411  -28.818 1.00 103.86 ? 245 GLY A O     1 
ATOM   2020 N  N     . ASP A 1 246 ? -37.742 19.526  -26.970 1.00 97.25  ? 246 ASP A N     1 
ATOM   2021 C  CA    . ASP A 1 246 ? -38.778 18.518  -26.784 1.00 99.95  ? 246 ASP A CA    1 
ATOM   2022 C  C     . ASP A 1 246 ? -39.926 19.010  -25.912 1.00 105.00 ? 246 ASP A C     1 
ATOM   2023 O  O     . ASP A 1 246 ? -41.053 18.514  -26.042 1.00 110.07 ? 246 ASP A O     1 
ATOM   2024 C  CB    . ASP A 1 246 ? -38.162 17.253  -26.181 1.00 99.53  ? 246 ASP A CB    1 
ATOM   2025 C  CG    . ASP A 1 246 ? -37.421 17.527  -24.887 1.00 93.94  ? 246 ASP A CG    1 
ATOM   2026 O  OD1   . ASP A 1 246 ? -37.297 18.711  -24.509 1.00 102.00 ? 246 ASP A OD1   1 
ATOM   2027 O  OD2   . ASP A 1 246 ? -36.958 16.560  -24.248 1.00 84.83  ? 246 ASP A OD2   1 
ATOM   2028 N  N     . ARG A 1 247 ? -39.676 19.979  -25.036 1.00 97.45  ? 247 ARG A N     1 
ATOM   2029 C  CA    . ARG A 1 247 ? -40.709 20.521  -24.173 1.00 91.53  ? 247 ARG A CA    1 
ATOM   2030 C  C     . ARG A 1 247 ? -41.257 21.826  -24.749 1.00 87.68  ? 247 ARG A C     1 
ATOM   2031 O  O     . ARG A 1 247 ? -40.906 22.260  -25.855 1.00 87.61  ? 247 ARG A O     1 
ATOM   2032 C  CB    . ARG A 1 247 ? -40.180 20.746  -22.752 1.00 87.40  ? 247 ARG A CB    1 
ATOM   2033 C  CG    . ARG A 1 247 ? -39.277 19.662  -22.193 1.00 90.91  ? 247 ARG A CG    1 
ATOM   2034 C  CD    . ARG A 1 247 ? -38.211 20.285  -21.300 1.00 90.19  ? 247 ARG A CD    1 
ATOM   2035 N  NE    . ARG A 1 247 ? -37.837 19.452  -20.161 1.00 103.10 ? 247 ARG A NE    1 
ATOM   2036 C  CZ    . ARG A 1 247 ? -37.138 18.327  -20.238 1.00 96.62  ? 247 ARG A CZ    1 
ATOM   2037 N  NH1   . ARG A 1 247 ? -36.721 17.847  -21.399 1.00 92.85  ? 247 ARG A NH1   1 
ATOM   2038 N  NH2   . ARG A 1 247 ? -36.842 17.669  -19.120 1.00 90.96  ? 247 ARG A NH2   1 
ATOM   2039 N  N     . PHE A 1 248 ? -42.115 22.477  -23.976 1.00 82.10  ? 248 PHE A N     1 
ATOM   2040 C  CA    . PHE A 1 248 ? -42.717 23.740  -24.357 1.00 81.02  ? 248 PHE A CA    1 
ATOM   2041 C  C     . PHE A 1 248 ? -42.321 24.818  -23.359 1.00 68.98  ? 248 PHE A C     1 
ATOM   2042 O  O     . PHE A 1 248 ? -41.830 24.535  -22.262 1.00 64.72  ? 248 PHE A O     1 
ATOM   2043 C  CB    . PHE A 1 248 ? -44.243 23.621  -24.431 1.00 82.12  ? 248 PHE A CB    1 
ATOM   2044 C  CG    . PHE A 1 248 ? -44.720 22.507  -25.318 1.00 95.49  ? 248 PHE A CG    1 
ATOM   2045 C  CD1   . PHE A 1 248 ? -45.267 21.357  -24.771 1.00 99.16  ? 248 PHE A CD1   1 
ATOM   2046 C  CD2   . PHE A 1 248 ? -44.620 22.607  -26.696 1.00 98.16  ? 248 PHE A CD2   1 
ATOM   2047 C  CE1   . PHE A 1 248 ? -45.708 20.326  -25.581 1.00 99.52  ? 248 PHE A CE1   1 
ATOM   2048 C  CE2   . PHE A 1 248 ? -45.060 21.579  -27.513 1.00 105.72 ? 248 PHE A CE2   1 
ATOM   2049 C  CZ    . PHE A 1 248 ? -45.604 20.437  -26.953 1.00 98.03  ? 248 PHE A CZ    1 
ATOM   2050 N  N     . ALA A 1 249 ? -42.531 26.067  -23.764 1.00 66.21  ? 249 ALA A N     1 
ATOM   2051 C  CA    . ALA A 1 249 ? -42.315 27.220  -22.906 1.00 63.09  ? 249 ALA A CA    1 
ATOM   2052 C  C     . ALA A 1 249 ? -43.457 28.200  -23.125 1.00 60.66  ? 249 ALA A C     1 
ATOM   2053 O  O     . ALA A 1 249 ? -44.105 28.200  -24.173 1.00 69.08  ? 249 ALA A O     1 
ATOM   2054 C  CB    . ALA A 1 249 ? -40.962 27.890  -23.180 1.00 64.53  ? 249 ALA A CB    1 
ATOM   2055 N  N     . VAL A 1 250 ? -43.708 29.036  -22.122 1.00 57.17  ? 250 VAL A N     1 
ATOM   2056 C  CA    . VAL A 1 250 ? -44.862 29.928  -22.125 1.00 54.00  ? 250 VAL A CA    1 
ATOM   2057 C  C     . VAL A 1 250 ? -44.384 31.353  -21.885 1.00 53.73  ? 250 VAL A C     1 
ATOM   2058 O  O     . VAL A 1 250 ? -43.765 31.639  -20.853 1.00 51.28  ? 250 VAL A O     1 
ATOM   2059 C  CB    . VAL A 1 250 ? -45.903 29.522  -21.069 1.00 48.96  ? 250 VAL A CB    1 
ATOM   2060 C  CG1   . VAL A 1 250 ? -47.039 30.526  -21.035 1.00 50.42  ? 250 VAL A CG1   1 
ATOM   2061 C  CG2   . VAL A 1 250 ? -46.429 28.125  -21.358 1.00 48.37  ? 250 VAL A CG2   1 
ATOM   2062 N  N     . GLU A 1 251 ? -44.679 32.243  -22.828 1.00 55.15  ? 251 GLU A N     1 
ATOM   2063 C  CA    . GLU A 1 251 ? -44.400 33.664  -22.698 1.00 54.79  ? 251 GLU A CA    1 
ATOM   2064 C  C     . GLU A 1 251 ? -45.657 34.412  -22.274 1.00 58.35  ? 251 GLU A C     1 
ATOM   2065 O  O     . GLU A 1 251 ? -46.779 34.035  -22.626 1.00 59.59  ? 251 GLU A O     1 
ATOM   2066 C  CB    . GLU A 1 251 ? -43.885 34.245  -24.017 1.00 64.08  ? 251 GLU A CB    1 
ATOM   2067 C  CG    . GLU A 1 251 ? -42.442 33.916  -24.323 1.00 75.63  ? 251 GLU A CG    1 
ATOM   2068 C  CD    . GLU A 1 251 ? -41.769 34.976  -25.168 1.00 98.94  ? 251 GLU A CD    1 
ATOM   2069 O  OE1   . GLU A 1 251 ? -42.349 35.370  -26.201 1.00 89.64  ? 251 GLU A OE1   1 
ATOM   2070 O  OE2   . GLU A 1 251 ? -40.658 35.412  -24.799 1.00 111.65 ? 251 GLU A OE2   1 
ATOM   2071 N  N     . VAL A 1 252 ? -45.455 35.484  -21.512 1.00 52.86  ? 252 VAL A N     1 
ATOM   2072 C  CA    . VAL A 1 252 ? -46.516 36.412  -21.129 1.00 53.62  ? 252 VAL A CA    1 
ATOM   2073 C  C     . VAL A 1 252 ? -45.983 37.811  -21.426 1.00 53.80  ? 252 VAL A C     1 
ATOM   2074 O  O     . VAL A 1 252 ? -45.170 38.344  -20.664 1.00 54.20  ? 252 VAL A O     1 
ATOM   2075 C  CB    . VAL A 1 252 ? -46.922 36.266  -19.657 1.00 57.55  ? 252 VAL A CB    1 
ATOM   2076 C  CG1   . VAL A 1 252 ? -47.948 37.327  -19.279 1.00 55.99  ? 252 VAL A CG1   1 
ATOM   2077 C  CG2   . VAL A 1 252 ? -47.470 34.870  -19.392 1.00 56.32  ? 252 VAL A CG2   1 
ATOM   2078 N  N     . LYS A 1 253 ? -46.437 38.407  -22.532 1.00 53.17  ? 253 LYS A N     1 
ATOM   2079 C  CA    . LYS A 1 253 ? -45.881 39.669  -23.011 1.00 54.64  ? 253 LYS A CA    1 
ATOM   2080 C  C     . LYS A 1 253 ? -45.999 40.764  -21.955 1.00 60.26  ? 253 LYS A C     1 
ATOM   2081 O  O     . LYS A 1 253 ? -46.928 40.781  -21.144 1.00 60.78  ? 253 LYS A O     1 
ATOM   2082 C  CB    . LYS A 1 253 ? -46.580 40.100  -24.303 1.00 56.28  ? 253 LYS A CB    1 
ATOM   2083 C  CG    . LYS A 1 253 ? -46.277 39.215  -25.500 1.00 60.41  ? 253 LYS A CG    1 
ATOM   2084 C  CD    . LYS A 1 253 ? -44.845 39.394  -25.969 1.00 58.92  ? 253 LYS A CD    1 
ATOM   2085 C  CE    . LYS A 1 253 ? -44.495 38.352  -27.016 1.00 70.63  ? 253 LYS A CE    1 
ATOM   2086 N  NZ    . LYS A 1 253 ? -44.228 38.974  -28.342 1.00 75.18  ? 253 LYS A NZ    1 
ATOM   2087 N  N     . GLY A 1 254 ? -45.034 41.687  -21.975 1.00 56.06  ? 254 GLY A N     1 
ATOM   2088 C  CA    . GLY A 1 254 ? -44.905 42.704  -20.960 1.00 60.12  ? 254 GLY A CA    1 
ATOM   2089 C  C     . GLY A 1 254 ? -44.453 42.215  -19.601 1.00 58.52  ? 254 GLY A C     1 
ATOM   2090 O  O     . GLY A 1 254 ? -44.049 43.034  -18.774 1.00 56.64  ? 254 GLY A O     1 
ATOM   2091 N  N     . ARG A 1 255 ? -44.498 40.915  -19.339 1.00 61.13  ? 255 ARG A N     1 
ATOM   2092 C  CA    . ARG A 1 255 ? -44.067 40.340  -18.076 1.00 54.62  ? 255 ARG A CA    1 
ATOM   2093 C  C     . ARG A 1 255 ? -42.969 39.316  -18.329 1.00 54.80  ? 255 ARG A C     1 
ATOM   2094 O  O     . ARG A 1 255 ? -42.615 39.016  -19.472 1.00 52.21  ? 255 ARG A O     1 
ATOM   2095 C  CB    . ARG A 1 255 ? -45.247 39.686  -17.347 1.00 56.40  ? 255 ARG A CB    1 
ATOM   2096 C  CG    . ARG A 1 255 ? -46.248 40.666  -16.778 1.00 58.69  ? 255 ARG A CG    1 
ATOM   2097 C  CD    . ARG A 1 255 ? -47.412 39.955  -16.111 1.00 67.04  ? 255 ARG A CD    1 
ATOM   2098 N  NE    . ARG A 1 255 ? -48.281 40.894  -15.410 1.00 68.59  ? 255 ARG A NE    1 
ATOM   2099 C  CZ    . ARG A 1 255 ? -49.308 41.534  -15.958 1.00 64.40  ? 255 ARG A CZ    1 
ATOM   2100 N  NH1   . ARG A 1 255 ? -49.644 41.354  -17.225 1.00 63.07  ? 255 ARG A NH1   1 
ATOM   2101 N  NH2   . ARG A 1 255 ? -50.016 42.378  -15.213 1.00 69.54  ? 255 ARG A NH2   1 
ATOM   2102 N  N     . ILE A 1 256 ? -42.427 38.773  -17.244 1.00 45.61  ? 256 ILE A N     1 
ATOM   2103 C  CA    . ILE A 1 256 ? -41.432 37.710  -17.310 1.00 47.98  ? 256 ILE A CA    1 
ATOM   2104 C  C     . ILE A 1 256 ? -42.026 36.494  -16.615 1.00 42.29  ? 256 ILE A C     1 
ATOM   2105 O  O     . ILE A 1 256 ? -42.258 36.520  -15.400 1.00 46.13  ? 256 ILE A O     1 
ATOM   2106 C  CB    . ILE A 1 256 ? -40.099 38.123  -16.668 1.00 51.57  ? 256 ILE A CB    1 
ATOM   2107 C  CG1   . ILE A 1 256 ? -39.448 39.260  -17.457 1.00 49.19  ? 256 ILE A CG1   1 
ATOM   2108 C  CG2   . ILE A 1 256 ? -39.146 36.931  -16.576 1.00 48.74  ? 256 ILE A CG2   1 
ATOM   2109 C  CD1   . ILE A 1 256 ? -39.055 38.883  -18.872 1.00 62.20  ? 256 ILE A CD1   1 
ATOM   2110 N  N     . HIS A 1 257 ? -42.310 35.442  -17.379 1.00 42.19  ? 257 HIS A N     1 
ATOM   2111 C  CA    . HIS A 1 257 ? -42.771 34.191  -16.785 1.00 45.86  ? 257 HIS A CA    1 
ATOM   2112 C  C     . HIS A 1 257 ? -41.553 33.418  -16.295 1.00 47.71  ? 257 HIS A C     1 
ATOM   2113 O  O     . HIS A 1 257 ? -40.785 32.879  -17.097 1.00 38.05  ? 257 HIS A O     1 
ATOM   2114 C  CB    . HIS A 1 257 ? -43.581 33.368  -17.781 1.00 43.90  ? 257 HIS A CB    1 
ATOM   2115 C  CG    . HIS A 1 257 ? -43.872 31.976  -17.312 1.00 38.70  ? 257 HIS A CG    1 
ATOM   2116 N  ND1   . HIS A 1 257 ? -43.968 30.905  -18.174 1.00 42.59  ? 257 HIS A ND1   1 
ATOM   2117 C  CD2   . HIS A 1 257 ? -44.076 31.479  -16.069 1.00 37.51  ? 257 HIS A CD2   1 
ATOM   2118 C  CE1   . HIS A 1 257 ? -44.223 29.808  -17.482 1.00 46.45  ? 257 HIS A CE1   1 
ATOM   2119 N  NE2   . HIS A 1 257 ? -44.291 30.129  -16.202 1.00 39.61  ? 257 HIS A NE2   1 
ATOM   2120 N  N     . PHE A 1 258 ? -41.374 33.373  -14.978 1.00 45.08  ? 258 PHE A N     1 
ATOM   2121 C  CA    . PHE A 1 258 ? -40.263 32.673  -14.342 1.00 43.25  ? 258 PHE A CA    1 
ATOM   2122 C  C     . PHE A 1 258 ? -40.765 31.300  -13.902 1.00 44.03  ? 258 PHE A C     1 
ATOM   2123 O  O     . PHE A 1 258 ? -41.470 31.173  -12.895 1.00 47.84  ? 258 PHE A O     1 
ATOM   2124 C  CB    . PHE A 1 258 ? -39.726 33.486  -13.168 1.00 45.99  ? 258 PHE A CB    1 
ATOM   2125 C  CG    . PHE A 1 258 ? -38.377 33.039  -12.680 1.00 51.42  ? 258 PHE A CG    1 
ATOM   2126 C  CD1   . PHE A 1 258 ? -37.279 33.063  -13.522 1.00 49.53  ? 258 PHE A CD1   1 
ATOM   2127 C  CD2   . PHE A 1 258 ? -38.203 32.614  -11.372 1.00 49.25  ? 258 PHE A CD2   1 
ATOM   2128 C  CE1   . PHE A 1 258 ? -36.035 32.659  -13.075 1.00 58.35  ? 258 PHE A CE1   1 
ATOM   2129 C  CE2   . PHE A 1 258 ? -36.962 32.210  -10.919 1.00 54.13  ? 258 PHE A CE2   1 
ATOM   2130 C  CZ    . PHE A 1 258 ? -35.877 32.233  -11.771 1.00 57.13  ? 258 PHE A CZ    1 
ATOM   2131 N  N     . ASP A 1 259 ? -40.426 30.275  -14.680 1.00 45.12  ? 259 ASP A N     1 
ATOM   2132 C  CA    . ASP A 1 259 ? -40.683 28.894  -14.297 1.00 46.20  ? 259 ASP A CA    1 
ATOM   2133 C  C     . ASP A 1 259 ? -39.472 28.381  -13.532 1.00 49.92  ? 259 ASP A C     1 
ATOM   2134 O  O     . ASP A 1 259 ? -38.371 28.291  -14.087 1.00 47.09  ? 259 ASP A O     1 
ATOM   2135 C  CB    . ASP A 1 259 ? -40.963 28.020  -15.519 1.00 42.65  ? 259 ASP A CB    1 
ATOM   2136 C  CG    . ASP A 1 259 ? -41.397 26.608  -15.142 1.00 51.72  ? 259 ASP A CG    1 
ATOM   2137 O  OD1   . ASP A 1 259 ? -41.506 26.310  -13.933 1.00 45.62  ? 259 ASP A OD1   1 
ATOM   2138 O  OD2   . ASP A 1 259 ? -41.634 25.793  -16.058 1.00 55.74  ? 259 ASP A OD2   1 
ATOM   2139 N  N     . LEU A 1 260 ? -39.677 28.049  -12.259 1.00 47.47  ? 260 LEU A N     1 
ATOM   2140 C  CA    . LEU A 1 260 ? -38.557 27.649  -11.419 1.00 48.73  ? 260 LEU A CA    1 
ATOM   2141 C  C     . LEU A 1 260 ? -37.989 26.298  -11.830 1.00 51.10  ? 260 LEU A C     1 
ATOM   2142 O  O     . LEU A 1 260 ? -36.789 26.067  -11.662 1.00 57.67  ? 260 LEU A O     1 
ATOM   2143 C  CB    . LEU A 1 260 ? -38.988 27.616  -9.954  1.00 50.49  ? 260 LEU A CB    1 
ATOM   2144 C  CG    . LEU A 1 260 ? -39.102 28.973  -9.260  1.00 52.91  ? 260 LEU A CG    1 
ATOM   2145 C  CD1   . LEU A 1 260 ? -40.123 28.913  -8.135  1.00 48.44  ? 260 LEU A CD1   1 
ATOM   2146 C  CD2   . LEU A 1 260 ? -37.747 29.416  -8.740  1.00 53.27  ? 260 LEU A CD2   1 
ATOM   2147 N  N     . TYR A 1 261 ? -38.818 25.418  -12.397 1.00 53.52  ? 261 TYR A N     1 
ATOM   2148 C  CA    . TYR A 1 261 ? -38.425 24.019  -12.571 1.00 56.96  ? 261 TYR A CA    1 
ATOM   2149 C  C     . TYR A 1 261 ? -37.120 23.836  -13.339 1.00 59.51  ? 261 TYR A C     1 
ATOM   2150 O  O     . TYR A 1 261 ? -36.224 23.144  -12.822 1.00 62.66  ? 261 TYR A O     1 
ATOM   2151 C  CB    . TYR A 1 261 ? -39.572 23.241  -13.227 1.00 55.49  ? 261 TYR A CB    1 
ATOM   2152 C  CG    . TYR A 1 261 ? -39.265 21.777  -13.436 1.00 62.60  ? 261 TYR A CG    1 
ATOM   2153 C  CD1   . TYR A 1 261 ? -39.281 20.887  -12.370 1.00 68.45  ? 261 TYR A CD1   1 
ATOM   2154 C  CD2   . TYR A 1 261 ? -38.953 21.286  -14.696 1.00 66.14  ? 261 TYR A CD2   1 
ATOM   2155 C  CE1   . TYR A 1 261 ? -38.998 19.546  -12.556 1.00 73.09  ? 261 TYR A CE1   1 
ATOM   2156 C  CE2   . TYR A 1 261 ? -38.669 19.949  -14.891 1.00 73.12  ? 261 TYR A CE2   1 
ATOM   2157 C  CZ    . TYR A 1 261 ? -38.692 19.083  -13.818 1.00 78.88  ? 261 TYR A CZ    1 
ATOM   2158 O  OH    . TYR A 1 261 ? -38.409 17.751  -14.010 1.00 92.93  ? 261 TYR A OH    1 
ATOM   2159 N  N     . PRO A 1 262 ? -36.936 24.387  -14.548 1.00 59.50  ? 262 PRO A N     1 
ATOM   2160 C  CA    . PRO A 1 262 ? -35.643 24.181  -15.224 1.00 55.21  ? 262 PRO A CA    1 
ATOM   2161 C  C     . PRO A 1 262 ? -34.484 24.810  -14.476 1.00 57.56  ? 262 PRO A C     1 
ATOM   2162 O  O     . PRO A 1 262 ? -33.387 24.239  -14.448 1.00 69.01  ? 262 PRO A O     1 
ATOM   2163 C  CB    . PRO A 1 262 ? -35.857 24.826  -16.601 1.00 54.38  ? 262 PRO A CB    1 
ATOM   2164 C  CG    . PRO A 1 262 ? -36.946 25.812  -16.392 1.00 53.91  ? 262 PRO A CG    1 
ATOM   2165 C  CD    . PRO A 1 262 ? -37.853 25.201  -15.370 1.00 51.94  ? 262 PRO A CD    1 
ATOM   2166 N  N     . VAL A 1 263 ? -34.707 25.966  -13.846 1.00 55.63  ? 263 VAL A N     1 
ATOM   2167 C  CA    . VAL A 1 263 ? -33.646 26.627  -13.089 1.00 61.18  ? 263 VAL A CA    1 
ATOM   2168 C  C     . VAL A 1 263 ? -33.165 25.730  -11.954 1.00 64.92  ? 263 VAL A C     1 
ATOM   2169 O  O     . VAL A 1 263 ? -31.959 25.536  -11.758 1.00 68.62  ? 263 VAL A O     1 
ATOM   2170 C  CB    . VAL A 1 263 ? -34.134 27.989  -12.564 1.00 55.17  ? 263 VAL A CB    1 
ATOM   2171 C  CG1   . VAL A 1 263 ? -33.115 28.588  -11.609 1.00 63.30  ? 263 VAL A CG1   1 
ATOM   2172 C  CG2   . VAL A 1 263 ? -34.410 28.936  -13.722 1.00 55.42  ? 263 VAL A CG2   1 
ATOM   2173 N  N     . ILE A 1 264 ? -34.105 25.162  -11.195 1.00 58.97  ? 264 ILE A N     1 
ATOM   2174 C  CA    . ILE A 1 264 ? -33.741 24.302  -10.074 1.00 66.20  ? 264 ILE A CA    1 
ATOM   2175 C  C     . ILE A 1 264 ? -33.076 23.027  -10.575 1.00 68.62  ? 264 ILE A C     1 
ATOM   2176 O  O     . ILE A 1 264 ? -32.052 22.590  -10.036 1.00 62.77  ? 264 ILE A O     1 
ATOM   2177 C  CB    . ILE A 1 264 ? -34.973 23.983  -9.210  1.00 66.72  ? 264 ILE A CB    1 
ATOM   2178 C  CG1   . ILE A 1 264 ? -35.761 25.253  -8.895  1.00 61.33  ? 264 ILE A CG1   1 
ATOM   2179 C  CG2   . ILE A 1 264 ? -34.548 23.283  -7.931  1.00 59.84  ? 264 ILE A CG2   1 
ATOM   2180 C  CD1   . ILE A 1 264 ? -34.978 26.286  -8.143  1.00 58.67  ? 264 ILE A CD1   1 
ATOM   2181 N  N     . ARG A 1 265 ? -33.653 22.406  -11.609 1.00 62.89  ? 265 ARG A N     1 
ATOM   2182 C  CA    . ARG A 1 265 ? -33.083 21.173  -12.140 1.00 69.14  ? 265 ARG A CA    1 
ATOM   2183 C  C     . ARG A 1 265 ? -31.664 21.386  -12.652 1.00 73.09  ? 265 ARG A C     1 
ATOM   2184 O  O     . ARG A 1 265 ? -30.818 20.492  -12.530 1.00 77.98  ? 265 ARG A O     1 
ATOM   2185 C  CB    . ARG A 1 265 ? -33.986 20.623  -13.248 1.00 67.80  ? 265 ARG A CB    1 
ATOM   2186 C  CG    . ARG A 1 265 ? -33.301 19.684  -14.227 1.00 84.58  ? 265 ARG A CG    1 
ATOM   2187 C  CD    . ARG A 1 265 ? -33.367 18.249  -13.740 1.00 92.18  ? 265 ARG A CD    1 
ATOM   2188 N  NE    . ARG A 1 265 ? -34.738 17.757  -13.679 1.00 95.13  ? 265 ARG A NE    1 
ATOM   2189 C  CZ    . ARG A 1 265 ? -35.145 16.604  -14.190 1.00 96.26  ? 265 ARG A CZ    1 
ATOM   2190 N  NH1   . ARG A 1 265 ? -34.304 15.781  -14.794 1.00 92.83  ? 265 ARG A NH1   1 
ATOM   2191 N  NH2   . ARG A 1 265 ? -36.428 16.267  -14.091 1.00 87.19  ? 265 ARG A NH2   1 
ATOM   2192 N  N     . ARG A 1 266 ? -31.377 22.569  -13.196 1.00 74.12  ? 266 ARG A N     1 
ATOM   2193 C  CA    . ARG A 1 266 ? -30.061 22.877  -13.732 1.00 67.19  ? 266 ARG A CA    1 
ATOM   2194 C  C     . ARG A 1 266 ? -29.086 23.382  -12.676 1.00 66.78  ? 266 ARG A C     1 
ATOM   2195 O  O     . ARG A 1 266 ? -27.871 23.318  -12.895 1.00 71.34  ? 266 ARG A O     1 
ATOM   2196 C  CB    . ARG A 1 266 ? -30.203 23.917  -14.850 1.00 67.15  ? 266 ARG A CB    1 
ATOM   2197 C  CG    . ARG A 1 266 ? -28.979 24.118  -15.720 1.00 77.37  ? 266 ARG A CG    1 
ATOM   2198 C  CD    . ARG A 1 266 ? -29.057 25.463  -16.416 1.00 75.99  ? 266 ARG A CD    1 
ATOM   2199 N  NE    . ARG A 1 266 ? -29.022 26.560  -15.456 1.00 95.40  ? 266 ARG A NE    1 
ATOM   2200 C  CZ    . ARG A 1 266 ? -29.652 27.716  -15.613 1.00 87.80  ? 266 ARG A CZ    1 
ATOM   2201 N  NH1   . ARG A 1 266 ? -30.396 27.960  -16.681 1.00 66.53  ? 266 ARG A NH1   1 
ATOM   2202 N  NH2   . ARG A 1 266 ? -29.539 28.648  -14.672 1.00 73.28  ? 266 ARG A NH2   1 
ATOM   2203 N  N     . THR A 1 267 ? -29.581 23.872  -11.540 1.00 71.09  ? 267 THR A N     1 
ATOM   2204 C  CA    . THR A 1 267 ? -28.728 24.434  -10.497 1.00 64.02  ? 267 THR A CA    1 
ATOM   2205 C  C     . THR A 1 267 ? -28.402 23.435  -9.392  1.00 64.98  ? 267 THR A C     1 
ATOM   2206 O  O     . THR A 1 267 ? -27.241 23.311  -8.994  1.00 73.04  ? 267 THR A O     1 
ATOM   2207 C  CB    . THR A 1 267 ? -29.391 25.678  -9.894  1.00 70.43  ? 267 THR A CB    1 
ATOM   2208 O  OG1   . THR A 1 267 ? -29.538 26.681  -10.907 1.00 84.19  ? 267 THR A OG1   1 
ATOM   2209 C  CG2   . THR A 1 267 ? -28.548 26.237  -8.757  1.00 76.55  ? 267 THR A CG2   1 
ATOM   2210 N  N     . ILE A 1 268 ? -29.404 22.719  -8.885  1.00 69.73  ? 268 ILE A N     1 
ATOM   2211 C  CA    . ILE A 1 268 ? -29.233 21.780  -7.782  1.00 73.00  ? 268 ILE A CA    1 
ATOM   2212 C  C     . ILE A 1 268 ? -29.508 20.371  -8.285  1.00 75.77  ? 268 ILE A C     1 
ATOM   2213 O  O     . ILE A 1 268 ? -30.401 20.160  -9.114  1.00 74.17  ? 268 ILE A O     1 
ATOM   2214 C  CB    . ILE A 1 268 ? -30.157 22.127  -6.598  1.00 67.58  ? 268 ILE A CB    1 
ATOM   2215 C  CG1   . ILE A 1 268 ? -30.091 23.624  -6.290  1.00 70.25  ? 268 ILE A CG1   1 
ATOM   2216 C  CG2   . ILE A 1 268 ? -29.786 21.308  -5.369  1.00 71.10  ? 268 ILE A CG2   1 
ATOM   2217 C  CD1   . ILE A 1 268 ? -30.637 23.995  -4.927  1.00 69.41  ? 268 ILE A CD1   1 
ATOM   2218 N  N     . ASN A 1 269 ? -28.737 19.407  -7.785  1.00 79.51  ? 269 ASN A N     1 
ATOM   2219 C  CA    . ASN A 1 269 ? -28.924 17.999  -8.113  1.00 97.61  ? 269 ASN A CA    1 
ATOM   2220 C  C     . ASN A 1 269 ? -29.604 17.301  -6.941  1.00 78.25  ? 269 ASN A C     1 
ATOM   2221 O  O     . ASN A 1 269 ? -29.043 17.229  -5.842  1.00 68.33  ? 269 ASN A O     1 
ATOM   2222 C  CB    . ASN A 1 269 ? -27.594 17.323  -8.442  1.00 96.77  ? 269 ASN A CB    1 
ATOM   2223 C  CG    . ASN A 1 269 ? -27.775 15.914  -8.979  1.00 96.80  ? 269 ASN A CG    1 
ATOM   2224 O  OD1   . ASN A 1 269 ? -28.188 15.720  -10.124 1.00 96.03  ? 269 ASN A OD1   1 
ATOM   2225 N  ND2   . ASN A 1 269 ? -27.473 14.922  -8.151  1.00 91.60  ? 269 ASN A ND2   1 
ATOM   2226 N  N     . LEU A 1 270 ? -30.802 16.789  -7.181  1.00 76.88  ? 270 LEU A N     1 
ATOM   2227 C  CA    . LEU A 1 270 ? -31.616 16.111  -6.187  1.00 70.69  ? 270 LEU A CA    1 
ATOM   2228 C  C     . LEU A 1 270 ? -32.073 14.773  -6.742  1.00 65.91  ? 270 LEU A C     1 
ATOM   2229 O  O     . LEU A 1 270 ? -32.155 14.592  -7.962  1.00 68.74  ? 270 LEU A O     1 
ATOM   2230 C  CB    . LEU A 1 270 ? -32.839 16.958  -5.805  1.00 75.16  ? 270 LEU A CB    1 
ATOM   2231 C  CG    . LEU A 1 270 ? -32.640 18.193  -4.922  1.00 69.42  ? 270 LEU A CG    1 
ATOM   2232 C  CD1   . LEU A 1 270 ? -33.945 18.538  -4.220  1.00 71.59  ? 270 LEU A CD1   1 
ATOM   2233 C  CD2   . LEU A 1 270 ? -31.528 17.976  -3.911  1.00 59.93  ? 270 LEU A CD2   1 
ATOM   2234 N  N     . PRO A 1 271 ? -32.371 13.805  -5.870  1.00 65.14  ? 271 PRO A N     1 
ATOM   2235 C  CA    . PRO A 1 271 ? -32.961 12.546  -6.363  1.00 66.24  ? 271 PRO A CA    1 
ATOM   2236 C  C     . PRO A 1 271 ? -34.299 12.750  -7.050  1.00 73.41  ? 271 PRO A C     1 
ATOM   2237 O  O     . PRO A 1 271 ? -34.546 12.163  -8.111  1.00 67.01  ? 271 PRO A O     1 
ATOM   2238 C  CB    . PRO A 1 271 ? -33.093 11.699  -5.088  1.00 62.92  ? 271 PRO A CB    1 
ATOM   2239 C  CG    . PRO A 1 271 ? -33.018 12.676  -3.953  1.00 65.68  ? 271 PRO A CG    1 
ATOM   2240 C  CD    . PRO A 1 271 ? -32.112 13.768  -4.421  1.00 60.69  ? 271 PRO A CD    1 
ATOM   2241 N  N     . THR A 1 272 ? -35.173 13.571  -6.469  1.00 73.46  ? 272 THR A N     1 
ATOM   2242 C  CA    . THR A 1 272 ? -36.434 13.948  -7.087  1.00 67.53  ? 272 THR A CA    1 
ATOM   2243 C  C     . THR A 1 272 ? -36.558 15.463  -7.080  1.00 67.91  ? 272 THR A C     1 
ATOM   2244 O  O     . THR A 1 272 ? -35.977 16.146  -6.231  1.00 69.23  ? 272 THR A O     1 
ATOM   2245 C  CB    . THR A 1 272 ? -37.638 13.329  -6.365  1.00 70.13  ? 272 THR A CB    1 
ATOM   2246 O  OG1   . THR A 1 272 ? -37.562 13.627  -4.965  1.00 82.02  ? 272 THR A OG1   1 
ATOM   2247 C  CG2   . THR A 1 272 ? -37.663 11.822  -6.563  1.00 64.59  ? 272 THR A CG2   1 
ATOM   2248 N  N     . TYR A 1 273 ? -37.325 15.984  -8.033  1.00 67.25  ? 273 TYR A N     1 
ATOM   2249 C  CA    . TYR A 1 273 ? -37.504 17.419  -8.204  1.00 63.02  ? 273 TYR A CA    1 
ATOM   2250 C  C     . TYR A 1 273 ? -38.954 17.825  -7.971  1.00 64.73  ? 273 TYR A C     1 
ATOM   2251 O  O     . TYR A 1 273 ? -39.518 18.643  -8.701  1.00 63.97  ? 273 TYR A O     1 
ATOM   2252 C  CB    . TYR A 1 273 ? -37.030 17.860  -9.586  1.00 63.98  ? 273 TYR A CB    1 
ATOM   2253 C  CG    . TYR A 1 273 ? -35.526 17.869  -9.724  1.00 75.04  ? 273 TYR A CG    1 
ATOM   2254 C  CD1   . TYR A 1 273 ? -34.754 18.836  -9.092  1.00 72.28  ? 273 TYR A CD1   1 
ATOM   2255 C  CD2   . TYR A 1 273 ? -34.875 16.895  -10.468 1.00 76.22  ? 273 TYR A CD2   1 
ATOM   2256 C  CE1   . TYR A 1 273 ? -33.377 18.842  -9.214  1.00 71.99  ? 273 TYR A CE1   1 
ATOM   2257 C  CE2   . TYR A 1 273 ? -33.502 16.890  -10.592 1.00 77.05  ? 273 TYR A CE2   1 
ATOM   2258 C  CZ    . TYR A 1 273 ? -32.758 17.866  -9.966  1.00 78.57  ? 273 TYR A CZ    1 
ATOM   2259 O  OH    . TYR A 1 273 ? -31.390 17.856  -10.097 1.00 78.75  ? 273 TYR A OH    1 
ATOM   2260 N  N     . THR A 1 274 ? -39.577 17.249  -6.949  1.00 58.39  ? 274 THR A N     1 
ATOM   2261 C  CA    . THR A 1 274 ? -40.900 17.684  -6.539  1.00 57.70  ? 274 THR A CA    1 
ATOM   2262 C  C     . THR A 1 274 ? -40.802 18.991  -5.765  1.00 58.91  ? 274 THR A C     1 
ATOM   2263 O  O     . THR A 1 274 ? -39.774 19.299  -5.154  1.00 58.21  ? 274 THR A O     1 
ATOM   2264 C  CB    . THR A 1 274 ? -41.578 16.619  -5.678  1.00 57.40  ? 274 THR A CB    1 
ATOM   2265 O  OG1   . THR A 1 274 ? -40.978 16.605  -4.377  1.00 61.09  ? 274 THR A OG1   1 
ATOM   2266 C  CG2   . THR A 1 274 ? -41.427 15.249  -6.317  1.00 57.48  ? 274 THR A CG2   1 
ATOM   2267 N  N     . LEU A 1 275 ? -41.889 19.767  -5.805  1.00 61.96  ? 275 LEU A N     1 
ATOM   2268 C  CA    . LEU A 1 275 ? -41.914 21.049  -5.106  1.00 59.60  ? 275 LEU A CA    1 
ATOM   2269 C  C     . LEU A 1 275 ? -41.588 20.878  -3.629  1.00 57.60  ? 275 LEU A C     1 
ATOM   2270 O  O     . LEU A 1 275 ? -40.857 21.688  -3.046  1.00 53.87  ? 275 LEU A O     1 
ATOM   2271 C  CB    . LEU A 1 275 ? -43.281 21.712  -5.281  1.00 57.14  ? 275 LEU A CB    1 
ATOM   2272 C  CG    . LEU A 1 275 ? -43.434 23.136  -4.744  1.00 57.10  ? 275 LEU A CG    1 
ATOM   2273 C  CD1   . LEU A 1 275 ? -42.254 24.001  -5.163  1.00 54.42  ? 275 LEU A CD1   1 
ATOM   2274 C  CD2   . LEU A 1 275 ? -44.745 23.744  -5.216  1.00 55.05  ? 275 LEU A CD2   1 
ATOM   2275 N  N     . GLU A 1 276 ? -42.111 19.817  -3.011  1.00 52.17  ? 276 GLU A N     1 
ATOM   2276 C  CA    . GLU A 1 276 ? -41.824 19.555  -1.605  1.00 61.61  ? 276 GLU A CA    1 
ATOM   2277 C  C     . GLU A 1 276 ? -40.334 19.317  -1.386  1.00 65.20  ? 276 GLU A C     1 
ATOM   2278 O  O     . GLU A 1 276 ? -39.723 19.910  -0.489  1.00 62.59  ? 276 GLU A O     1 
ATOM   2279 C  CB    . GLU A 1 276 ? -42.642 18.354  -1.124  1.00 58.95  ? 276 GLU A CB    1 
ATOM   2280 C  CG    . GLU A 1 276 ? -44.145 18.603  -1.038  1.00 64.85  ? 276 GLU A CG    1 
ATOM   2281 C  CD    . GLU A 1 276 ? -44.821 18.635  -2.398  1.00 69.03  ? 276 GLU A CD    1 
ATOM   2282 O  OE1   . GLU A 1 276 ? -44.417 17.853  -3.286  1.00 68.41  ? 276 GLU A OE1   1 
ATOM   2283 O  OE2   . GLU A 1 276 ? -45.759 19.440  -2.579  1.00 62.97  ? 276 GLU A OE2   1 
ATOM   2284 N  N     . ALA A 1 277 ? -39.730 18.457  -2.212  1.00 60.60  ? 277 ALA A N     1 
ATOM   2285 C  CA    . ALA A 1 277 ? -38.311 18.150  -2.058  1.00 58.62  ? 277 ALA A CA    1 
ATOM   2286 C  C     . ALA A 1 277 ? -37.444 19.366  -2.351  1.00 61.67  ? 277 ALA A C     1 
ATOM   2287 O  O     . ALA A 1 277 ? -36.467 19.624  -1.639  1.00 62.36  ? 277 ALA A O     1 
ATOM   2288 C  CB    . ALA A 1 277 ? -37.921 16.986  -2.969  1.00 50.61  ? 277 ALA A CB    1 
ATOM   2289 N  N     . VAL A 1 278 ? -37.784 20.124  -3.396  1.00 58.80  ? 278 VAL A N     1 
ATOM   2290 C  CA    . VAL A 1 278 ? -37.011 21.315  -3.738  1.00 55.46  ? 278 VAL A CA    1 
ATOM   2291 C  C     . VAL A 1 278 ? -37.071 22.335  -2.609  1.00 60.57  ? 278 VAL A C     1 
ATOM   2292 O  O     . VAL A 1 278 ? -36.054 22.936  -2.236  1.00 62.68  ? 278 VAL A O     1 
ATOM   2293 C  CB    . VAL A 1 278 ? -37.515 21.907  -5.067  1.00 55.00  ? 278 VAL A CB    1 
ATOM   2294 C  CG1   . VAL A 1 278 ? -36.947 23.299  -5.278  1.00 59.21  ? 278 VAL A CG1   1 
ATOM   2295 C  CG2   . VAL A 1 278 ? -37.146 20.990  -6.222  1.00 59.12  ? 278 VAL A CG2   1 
ATOM   2296 N  N     . TYR A 1 279 ? -38.263 22.546  -2.045  1.00 61.64  ? 279 TYR A N     1 
ATOM   2297 C  CA    . TYR A 1 279 ? -38.396 23.485  -0.937  1.00 63.85  ? 279 TYR A CA    1 
ATOM   2298 C  C     . TYR A 1 279 ? -37.613 23.012  0.281   1.00 64.54  ? 279 TYR A C     1 
ATOM   2299 O  O     . TYR A 1 279 ? -36.914 23.806  0.922   1.00 61.22  ? 279 TYR A O     1 
ATOM   2300 C  CB    . TYR A 1 279 ? -39.871 23.677  -0.588  1.00 56.41  ? 279 TYR A CB    1 
ATOM   2301 C  CG    . TYR A 1 279 ? -40.106 24.595  0.589   1.00 55.96  ? 279 TYR A CG    1 
ATOM   2302 C  CD1   . TYR A 1 279 ? -39.968 25.971  0.458   1.00 53.61  ? 279 TYR A CD1   1 
ATOM   2303 C  CD2   . TYR A 1 279 ? -40.466 24.088  1.830   1.00 63.10  ? 279 TYR A CD2   1 
ATOM   2304 C  CE1   . TYR A 1 279 ? -40.181 26.817  1.532   1.00 49.42  ? 279 TYR A CE1   1 
ATOM   2305 C  CE2   . TYR A 1 279 ? -40.682 24.925  2.910   1.00 63.61  ? 279 TYR A CE2   1 
ATOM   2306 C  CZ    . TYR A 1 279 ? -40.537 26.288  2.755   1.00 58.30  ? 279 TYR A CZ    1 
ATOM   2307 O  OH    . TYR A 1 279 ? -40.751 27.125  3.827   1.00 69.12  ? 279 TYR A OH    1 
ATOM   2308 N  N     . GLU A 1 280 ? -37.711 21.720  0.611   1.00 61.12  ? 280 GLU A N     1 
ATOM   2309 C  CA    . GLU A 1 280 ? -36.986 21.195  1.764   1.00 74.51  ? 280 GLU A CA    1 
ATOM   2310 C  C     . GLU A 1 280 ? -35.479 21.241  1.552   1.00 70.40  ? 280 GLU A C     1 
ATOM   2311 O  O     . GLU A 1 280 ? -34.721 21.307  2.525   1.00 72.17  ? 280 GLU A O     1 
ATOM   2312 C  CB    . GLU A 1 280 ? -37.436 19.763  2.060   1.00 84.00  ? 280 GLU A CB    1 
ATOM   2313 C  CG    . GLU A 1 280 ? -37.050 19.259  3.445   1.00 87.24  ? 280 GLU A CG    1 
ATOM   2314 C  CD    . GLU A 1 280 ? -37.402 17.797  3.653   1.00 97.79  ? 280 GLU A CD    1 
ATOM   2315 O  OE1   . GLU A 1 280 ? -37.160 16.987  2.734   1.00 103.94 ? 280 GLU A OE1   1 
ATOM   2316 O  OE2   . GLU A 1 280 ? -37.922 17.458  4.737   1.00 100.21 ? 280 GLU A OE2   1 
ATOM   2317 N  N     . ALA A 1 281 ? -35.026 21.202  0.299   1.00 66.80  ? 281 ALA A N     1 
ATOM   2318 C  CA    . ALA A 1 281 ? -33.597 21.292  0.033   1.00 64.76  ? 281 ALA A CA    1 
ATOM   2319 C  C     . ALA A 1 281 ? -33.101 22.729  0.115   1.00 70.30  ? 281 ALA A C     1 
ATOM   2320 O  O     . ALA A 1 281 ? -32.027 22.986  0.670   1.00 68.38  ? 281 ALA A O     1 
ATOM   2321 C  CB    . ALA A 1 281 ? -33.279 20.700  -1.340  1.00 59.34  ? 281 ALA A CB    1 
ATOM   2322 N  N     . VAL A 1 282 ? -33.868 23.677  -0.423  1.00 72.62  ? 282 VAL A N     1 
ATOM   2323 C  CA    . VAL A 1 282 ? -33.403 25.061  -0.457  1.00 63.60  ? 282 VAL A CA    1 
ATOM   2324 C  C     . VAL A 1 282 ? -33.539 25.721  0.910   1.00 63.02  ? 282 VAL A C     1 
ATOM   2325 O  O     . VAL A 1 282 ? -32.686 26.522  1.310   1.00 66.80  ? 282 VAL A O     1 
ATOM   2326 C  CB    . VAL A 1 282 ? -34.155 25.846  -1.547  1.00 60.65  ? 282 VAL A CB    1 
ATOM   2327 C  CG1   . VAL A 1 282 ? -33.735 27.309  -1.538  1.00 59.82  ? 282 VAL A CG1   1 
ATOM   2328 C  CG2   . VAL A 1 282 ? -33.896 25.228  -2.911  1.00 58.92  ? 282 VAL A CG2   1 
ATOM   2329 N  N     . PHE A 1 283 ? -34.596 25.396  1.657   1.00 65.98  ? 283 PHE A N     1 
ATOM   2330 C  CA    . PHE A 1 283 ? -34.884 26.085  2.906   1.00 67.62  ? 283 PHE A CA    1 
ATOM   2331 C  C     . PHE A 1 283 ? -34.814 25.205  4.145   1.00 76.17  ? 283 PHE A C     1 
ATOM   2332 O  O     . PHE A 1 283 ? -34.877 25.739  5.259   1.00 76.32  ? 283 PHE A O     1 
ATOM   2333 C  CB    . PHE A 1 283 ? -36.272 26.741  2.841   1.00 61.10  ? 283 PHE A CB    1 
ATOM   2334 C  CG    . PHE A 1 283 ? -36.367 27.854  1.840   1.00 61.97  ? 283 PHE A CG    1 
ATOM   2335 C  CD1   . PHE A 1 283 ? -35.933 29.129  2.161   1.00 66.34  ? 283 PHE A CD1   1 
ATOM   2336 C  CD2   . PHE A 1 283 ? -36.881 27.625  0.575   1.00 60.79  ? 283 PHE A CD2   1 
ATOM   2337 C  CE1   . PHE A 1 283 ? -36.017 30.158  1.241   1.00 68.88  ? 283 PHE A CE1   1 
ATOM   2338 C  CE2   . PHE A 1 283 ? -36.967 28.649  -0.350  1.00 60.12  ? 283 PHE A CE2   1 
ATOM   2339 C  CZ    . PHE A 1 283 ? -36.535 29.917  -0.016  1.00 65.55  ? 283 PHE A CZ    1 
ATOM   2340 N  N     . GLY A 1 284 ? -34.694 23.886  3.996   1.00 79.32  ? 284 GLY A N     1 
ATOM   2341 C  CA    . GLY A 1 284 ? -34.575 22.995  5.130   1.00 84.83  ? 284 GLY A CA    1 
ATOM   2342 C  C     . GLY A 1 284 ? -35.871 22.645  5.825   1.00 87.07  ? 284 GLY A C     1 
ATOM   2343 O  O     . GLY A 1 284 ? -35.918 21.638  6.542   1.00 93.55  ? 284 GLY A O     1 
ATOM   2344 N  N     . GLN A 1 285 ? -36.925 23.434  5.641   1.00 84.51  ? 285 GLN A N     1 
ATOM   2345 C  CA    . GLN A 1 285 ? -38.133 23.037  6.351   1.00 89.51  ? 285 GLN A CA    1 
ATOM   2346 C  C     . GLN A 1 285 ? -39.013 22.164  5.459   1.00 91.64  ? 285 GLN A C     1 
ATOM   2347 O  O     . GLN A 1 285 ? -39.142 22.432  4.261   1.00 95.11  ? 285 GLN A O     1 
ATOM   2348 C  CB    . GLN A 1 285 ? -38.917 24.262  6.808   1.00 88.61  ? 285 GLN A CB    1 
ATOM   2349 C  CG    . GLN A 1 285 ? -38.356 24.944  8.052   1.00 94.49  ? 285 GLN A CG    1 
ATOM   2350 C  CD    . GLN A 1 285 ? -37.913 23.961  9.125   1.00 101.87 ? 285 GLN A CD    1 
ATOM   2351 O  OE1   . GLN A 1 285 ? -38.700 23.571  9.986   1.00 102.64 ? 285 GLN A OE1   1 
ATOM   2352 N  NE2   . GLN A 1 285 ? -36.637 23.585  9.098   1.00 104.61 ? 285 GLN A NE2   1 
ATOM   2353 N  N     . PRO A 1 286 ? -39.617 21.120  6.019   1.00 87.84  ? 286 PRO A N     1 
ATOM   2354 C  CA    . PRO A 1 286 ? -40.421 20.208  5.202   1.00 83.21  ? 286 PRO A CA    1 
ATOM   2355 C  C     . PRO A 1 286 ? -41.720 20.854  4.749   1.00 79.89  ? 286 PRO A C     1 
ATOM   2356 O  O     . PRO A 1 286 ? -42.172 21.867  5.288   1.00 76.18  ? 286 PRO A O     1 
ATOM   2357 C  CB    . PRO A 1 286 ? -40.688 19.030  6.143   1.00 79.89  ? 286 PRO A CB    1 
ATOM   2358 C  CG    . PRO A 1 286 ? -40.635 19.634  7.505   1.00 87.61  ? 286 PRO A CG    1 
ATOM   2359 C  CD    . PRO A 1 286 ? -39.596 20.722  7.438   1.00 88.18  ? 286 PRO A CD    1 
ATOM   2360 N  N     . LYS A 1 287 ? -42.323 20.240  3.734   1.00 73.37  ? 287 LYS A N     1 
ATOM   2361 C  CA    . LYS A 1 287 ? -43.591 20.701  3.182   1.00 68.53  ? 287 LYS A CA    1 
ATOM   2362 C  C     . LYS A 1 287 ? -44.462 19.487  2.909   1.00 68.49  ? 287 LYS A C     1 
ATOM   2363 O  O     . LYS A 1 287 ? -44.060 18.592  2.160   1.00 67.48  ? 287 LYS A O     1 
ATOM   2364 C  CB    . LYS A 1 287 ? -43.376 21.511  1.901   1.00 64.61  ? 287 LYS A CB    1 
ATOM   2365 C  CG    . LYS A 1 287 ? -44.654 22.070  1.306   1.00 65.49  ? 287 LYS A CG    1 
ATOM   2366 C  CD    . LYS A 1 287 ? -44.571 22.140  -0.208  1.00 62.27  ? 287 LYS A CD    1 
ATOM   2367 C  CE    . LYS A 1 287 ? -45.764 22.878  -0.784  1.00 61.83  ? 287 LYS A CE    1 
ATOM   2368 N  NZ    . LYS A 1 287 ? -46.737 21.944  -1.411  1.00 68.25  ? 287 LYS A NZ    1 
ATOM   2369 N  N     . GLU A 1 288 ? -45.646 19.455  3.516   1.00 69.46  ? 288 GLU A N     1 
ATOM   2370 C  CA    . GLU A 1 288 ? -46.538 18.318  3.350   1.00 68.14  ? 288 GLU A CA    1 
ATOM   2371 C  C     . GLU A 1 288 ? -47.055 18.244  1.919   1.00 66.76  ? 288 GLU A C     1 
ATOM   2372 O  O     . GLU A 1 288 ? -47.403 19.260  1.312   1.00 67.60  ? 288 GLU A O     1 
ATOM   2373 C  CB    . GLU A 1 288 ? -47.712 18.410  4.325   1.00 73.30  ? 288 GLU A CB    1 
ATOM   2374 C  CG    . GLU A 1 288 ? -48.610 17.182  4.322   1.00 81.48  ? 288 GLU A CG    1 
ATOM   2375 C  CD    . GLU A 1 288 ? -49.642 17.206  5.432   1.00 92.57  ? 288 GLU A CD    1 
ATOM   2376 O  OE1   . GLU A 1 288 ? -50.373 18.212  5.545   1.00 100.42 ? 288 GLU A OE1   1 
ATOM   2377 O  OE2   . GLU A 1 288 ? -49.726 16.216  6.189   1.00 96.19  ? 288 GLU A OE2   1 
ATOM   2378 N  N     . LYS A 1 289 ? -47.097 17.030  1.381   1.00 68.32  ? 289 LYS A N     1 
ATOM   2379 C  CA    . LYS A 1 289 ? -47.615 16.777  0.045   1.00 70.00  ? 289 LYS A CA    1 
ATOM   2380 C  C     . LYS A 1 289 ? -48.997 16.145  0.151   1.00 68.52  ? 289 LYS A C     1 
ATOM   2381 O  O     . LYS A 1 289 ? -49.204 15.225  0.949   1.00 71.12  ? 289 LYS A O     1 
ATOM   2382 C  CB    . LYS A 1 289 ? -46.672 15.862  -0.741  1.00 64.65  ? 289 LYS A CB    1 
ATOM   2383 C  CG    . LYS A 1 289 ? -47.308 15.191  -1.955  1.00 65.42  ? 289 LYS A CG    1 
ATOM   2384 C  CD    . LYS A 1 289 ? -47.679 16.204  -3.030  1.00 64.74  ? 289 LYS A CD    1 
ATOM   2385 C  CE    . LYS A 1 289 ? -47.342 15.686  -4.420  1.00 70.10  ? 289 LYS A CE    1 
ATOM   2386 N  NZ    . LYS A 1 289 ? -48.214 16.288  -5.467  1.00 52.08  ? 289 LYS A NZ    1 
ATOM   2387 N  N     . VAL A 1 290 ? -49.938 16.649  -0.641  1.00 66.64  ? 290 VAL A N     1 
ATOM   2388 C  CA    . VAL A 1 290 ? -51.270 16.068  -0.754  1.00 71.26  ? 290 VAL A CA    1 
ATOM   2389 C  C     . VAL A 1 290 ? -51.423 15.567  -2.182  1.00 70.20  ? 290 VAL A C     1 
ATOM   2390 O  O     . VAL A 1 290 ? -51.253 16.336  -3.136  1.00 67.82  ? 290 VAL A O     1 
ATOM   2391 C  CB    . VAL A 1 290 ? -52.372 17.078  -0.396  1.00 68.27  ? 290 VAL A CB    1 
ATOM   2392 C  CG1   . VAL A 1 290 ? -53.738 16.438  -0.545  1.00 73.84  ? 290 VAL A CG1   1 
ATOM   2393 C  CG2   . VAL A 1 290 ? -52.177 17.597  1.020   1.00 69.78  ? 290 VAL A CG2   1 
ATOM   2394 N  N     . TYR A 1 291 ? -51.729 14.283  -2.328  1.00 71.77  ? 291 TYR A N     1 
ATOM   2395 C  CA    . TYR A 1 291 ? -51.759 13.638  -3.631  1.00 73.51  ? 291 TYR A CA    1 
ATOM   2396 C  C     . TYR A 1 291 ? -53.115 13.832  -4.304  1.00 70.49  ? 291 TYR A C     1 
ATOM   2397 O  O     . TYR A 1 291 ? -54.115 14.169  -3.665  1.00 74.33  ? 291 TYR A O     1 
ATOM   2398 C  CB    . TYR A 1 291 ? -51.428 12.151  -3.495  1.00 72.78  ? 291 TYR A CB    1 
ATOM   2399 C  CG    . TYR A 1 291 ? -50.105 11.902  -2.804  1.00 70.34  ? 291 TYR A CG    1 
ATOM   2400 C  CD1   . TYR A 1 291 ? -50.033 11.764  -1.423  1.00 71.10  ? 291 TYR A CD1   1 
ATOM   2401 C  CD2   . TYR A 1 291 ? -48.924 11.824  -3.532  1.00 69.16  ? 291 TYR A CD2   1 
ATOM   2402 C  CE1   . TYR A 1 291 ? -48.824 11.545  -0.788  1.00 73.64  ? 291 TYR A CE1   1 
ATOM   2403 C  CE2   . TYR A 1 291 ? -47.710 11.605  -2.905  1.00 69.49  ? 291 TYR A CE2   1 
ATOM   2404 C  CZ    . TYR A 1 291 ? -47.666 11.466  -1.534  1.00 71.55  ? 291 TYR A CZ    1 
ATOM   2405 O  OH    . TYR A 1 291 ? -46.461 11.249  -0.906  1.00 72.00  ? 291 TYR A OH    1 
ATOM   2406 N  N     . ALA A 1 292 ? -53.132 13.609  -5.623  1.00 70.67  ? 292 ALA A N     1 
ATOM   2407 C  CA    . ALA A 1 292 ? -54.308 13.931  -6.426  1.00 73.84  ? 292 ALA A CA    1 
ATOM   2408 C  C     . ALA A 1 292 ? -55.521 13.103  -6.026  1.00 82.90  ? 292 ALA A C     1 
ATOM   2409 O  O     . ALA A 1 292 ? -56.657 13.579  -6.135  1.00 84.06  ? 292 ALA A O     1 
ATOM   2410 C  CB    . ALA A 1 292 ? -54.002 13.729  -7.910  1.00 70.27  ? 292 ALA A CB    1 
ATOM   2411 N  N     . GLU A 1 293 ? -55.307 11.866  -5.575  1.00 81.59  ? 293 GLU A N     1 
ATOM   2412 C  CA    . GLU A 1 293 ? -56.425 11.030  -5.151  1.00 78.85  ? 293 GLU A CA    1 
ATOM   2413 C  C     . GLU A 1 293 ? -57.145 11.648  -3.960  1.00 72.27  ? 293 GLU A C     1 
ATOM   2414 O  O     . GLU A 1 293 ? -58.383 11.682  -3.916  1.00 74.77  ? 293 GLU A O     1 
ATOM   2415 C  CB    . GLU A 1 293 ? -55.935 9.619   -4.805  1.00 89.18  ? 293 GLU A CB    1 
ATOM   2416 C  CG    . GLU A 1 293 ? -55.386 8.764   -5.966  1.00 90.27  ? 293 GLU A CG    1 
ATOM   2417 C  CD    . GLU A 1 293 ? -54.315 9.440   -6.814  1.00 101.31 ? 293 GLU A CD    1 
ATOM   2418 O  OE1   . GLU A 1 293 ? -54.133 9.018   -7.976  1.00 106.40 ? 293 GLU A OE1   1 
ATOM   2419 O  OE2   . GLU A 1 293 ? -53.633 10.366  -6.319  1.00 108.18 ? 293 GLU A OE2   1 
ATOM   2420 N  N     . GLU A 1 294 ? -56.379 12.144  -2.986  1.00 73.60  ? 294 GLU A N     1 
ATOM   2421 C  CA    . GLU A 1 294 ? -56.969 12.769  -1.809  1.00 77.06  ? 294 GLU A CA    1 
ATOM   2422 C  C     . GLU A 1 294 ? -57.840 13.954  -2.200  1.00 77.15  ? 294 GLU A C     1 
ATOM   2423 O  O     . GLU A 1 294 ? -58.980 14.075  -1.741  1.00 74.36  ? 294 GLU A O     1 
ATOM   2424 C  CB    . GLU A 1 294 ? -55.869 13.212  -0.844  1.00 75.82  ? 294 GLU A CB    1 
ATOM   2425 C  CG    . GLU A 1 294 ? -54.850 12.139  -0.508  1.00 80.41  ? 294 GLU A CG    1 
ATOM   2426 C  CD    . GLU A 1 294 ? -53.819 12.619  0.495   1.00 88.01  ? 294 GLU A CD    1 
ATOM   2427 O  OE1   . GLU A 1 294 ? -54.142 12.664  1.701   1.00 91.85  ? 294 GLU A OE1   1 
ATOM   2428 O  OE2   . GLU A 1 294 ? -52.690 12.955  0.078   1.00 81.93  ? 294 GLU A OE2   1 
ATOM   2429 N  N     . ILE A 1 295 ? -57.322 14.837  -3.056  1.00 73.96  ? 295 ILE A N     1 
ATOM   2430 C  CA    . ILE A 1 295 ? -58.075 16.037  -3.403  1.00 74.22  ? 295 ILE A CA    1 
ATOM   2431 C  C     . ILE A 1 295 ? -59.265 15.692  -4.291  1.00 74.92  ? 295 ILE A C     1 
ATOM   2432 O  O     . ILE A 1 295 ? -60.318 16.335  -4.202  1.00 73.48  ? 295 ILE A O     1 
ATOM   2433 C  CB    . ILE A 1 295 ? -57.151 17.085  -4.054  1.00 75.53  ? 295 ILE A CB    1 
ATOM   2434 C  CG1   . ILE A 1 295 ? -56.819 16.720  -5.497  1.00 78.99  ? 295 ILE A CG1   1 
ATOM   2435 C  CG2   . ILE A 1 295 ? -55.862 17.223  -3.270  1.00 72.28  ? 295 ILE A CG2   1 
ATOM   2436 C  CD1   . ILE A 1 295 ? -56.783 17.917  -6.397  1.00 78.97  ? 295 ILE A CD1   1 
ATOM   2437 N  N     . THR A 1 296 ? -59.143 14.658  -5.126  1.00 77.94  ? 296 THR A N     1 
ATOM   2438 C  CA    . THR A 1 296 ? -60.274 14.228  -5.941  1.00 76.78  ? 296 THR A CA    1 
ATOM   2439 C  C     . THR A 1 296 ? -61.415 13.718  -5.069  1.00 75.12  ? 296 THR A C     1 
ATOM   2440 O  O     . THR A 1 296 ? -62.577 14.097  -5.263  1.00 75.50  ? 296 THR A O     1 
ATOM   2441 C  CB    . THR A 1 296 ? -59.830 13.153  -6.934  1.00 79.37  ? 296 THR A CB    1 
ATOM   2442 O  OG1   . THR A 1 296 ? -58.975 13.738  -7.925  1.00 81.19  ? 296 THR A OG1   1 
ATOM   2443 C  CG2   . THR A 1 296 ? -61.034 12.510  -7.610  1.00 81.66  ? 296 THR A CG2   1 
ATOM   2444 N  N     . THR A 1 297 ? -61.101 12.856  -4.097  1.00 68.80  ? 297 THR A N     1 
ATOM   2445 C  CA    . THR A 1 297 ? -62.147 12.377  -3.197  1.00 79.46  ? 297 THR A CA    1 
ATOM   2446 C  C     . THR A 1 297 ? -62.691 13.506  -2.330  1.00 80.01  ? 297 THR A C     1 
ATOM   2447 O  O     . THR A 1 297 ? -63.895 13.556  -2.052  1.00 73.21  ? 297 THR A O     1 
ATOM   2448 C  CB    . THR A 1 297 ? -61.624 11.233  -2.327  1.00 71.82  ? 297 THR A CB    1 
ATOM   2449 O  OG1   . THR A 1 297 ? -60.633 11.730  -1.419  1.00 88.26  ? 297 THR A OG1   1 
ATOM   2450 C  CG2   . THR A 1 297 ? -61.029 10.129  -3.194  1.00 70.75  ? 297 THR A CG2   1 
ATOM   2451 N  N     . ALA A 1 298 ? -61.824 14.432  -1.909  1.00 78.83  ? 298 ALA A N     1 
ATOM   2452 C  CA    . ALA A 1 298 ? -62.267 15.552  -1.086  1.00 78.11  ? 298 ALA A CA    1 
ATOM   2453 C  C     . ALA A 1 298 ? -63.200 16.478  -1.852  1.00 71.95  ? 298 ALA A C     1 
ATOM   2454 O  O     . ALA A 1 298 ? -64.104 17.076  -1.258  1.00 74.58  ? 298 ALA A O     1 
ATOM   2455 C  CB    . ALA A 1 298 ? -61.056 16.328  -0.569  1.00 70.87  ? 298 ALA A CB    1 
ATOM   2456 N  N     . TRP A 1 299 ? -62.997 16.613  -3.161  1.00 70.39  ? 299 TRP A N     1 
ATOM   2457 C  CA    . TRP A 1 299 ? -63.874 17.447  -3.971  1.00 74.73  ? 299 TRP A CA    1 
ATOM   2458 C  C     . TRP A 1 299 ? -65.184 16.735  -4.281  1.00 78.16  ? 299 TRP A C     1 
ATOM   2459 O  O     . TRP A 1 299 ? -66.263 17.330  -4.178  1.00 87.42  ? 299 TRP A O     1 
ATOM   2460 C  CB    . TRP A 1 299 ? -63.166 17.834  -5.265  1.00 76.45  ? 299 TRP A CB    1 
ATOM   2461 C  CG    . TRP A 1 299 ? -63.924 18.805  -6.098  1.00 75.93  ? 299 TRP A CG    1 
ATOM   2462 C  CD1   . TRP A 1 299 ? -64.693 18.524  -7.188  1.00 77.65  ? 299 TRP A CD1   1 
ATOM   2463 C  CD2   . TRP A 1 299 ? -63.959 20.226  -5.937  1.00 80.78  ? 299 TRP A CD2   1 
ATOM   2464 N  NE1   . TRP A 1 299 ? -65.220 19.680  -7.706  1.00 74.70  ? 299 TRP A NE1   1 
ATOM   2465 C  CE2   . TRP A 1 299 ? -64.782 20.741  -6.957  1.00 77.67  ? 299 TRP A CE2   1 
ATOM   2466 C  CE3   . TRP A 1 299 ? -63.378 21.114  -5.026  1.00 81.99  ? 299 TRP A CE3   1 
ATOM   2467 C  CZ2   . TRP A 1 299 ? -65.041 22.101  -7.089  1.00 80.29  ? 299 TRP A CZ2   1 
ATOM   2468 C  CZ3   . TRP A 1 299 ? -63.634 22.467  -5.161  1.00 83.37  ? 299 TRP A CZ3   1 
ATOM   2469 C  CH2   . TRP A 1 299 ? -64.450 22.947  -6.191  1.00 79.70  ? 299 TRP A CH2   1 
ATOM   2470 N  N     . GLU A 1 300 ? -65.107 15.460  -4.676  1.00 85.93  ? 300 GLU A N     1 
ATOM   2471 C  CA    . GLU A 1 300 ? -66.317 14.730  -5.039  1.00 84.70  ? 300 GLU A CA    1 
ATOM   2472 C  C     . GLU A 1 300 ? -67.214 14.489  -3.833  1.00 80.38  ? 300 GLU A C     1 
ATOM   2473 O  O     . GLU A 1 300 ? -68.441 14.442  -3.976  1.00 90.54  ? 300 GLU A O     1 
ATOM   2474 C  CB    . GLU A 1 300 ? -65.953 13.403  -5.707  1.00 90.96  ? 300 GLU A CB    1 
ATOM   2475 C  CG    . GLU A 1 300 ? -65.234 13.555  -7.041  1.00 99.56  ? 300 GLU A CG    1 
ATOM   2476 C  CD    . GLU A 1 300 ? -64.949 12.223  -7.710  1.00 103.07 ? 300 GLU A CD    1 
ATOM   2477 O  OE1   . GLU A 1 300 ? -64.540 11.276  -7.005  1.00 97.97  ? 300 GLU A OE1   1 
ATOM   2478 O  OE2   . GLU A 1 300 ? -65.132 12.123  -8.941  1.00 104.26 ? 300 GLU A OE2   1 
ATOM   2479 N  N     . THR A 1 301 ? -66.630 14.346  -2.643  1.00 79.90  ? 301 THR A N     1 
ATOM   2480 C  CA    . THR A 1 301 ? -67.404 14.118  -1.431  1.00 78.01  ? 301 THR A CA    1 
ATOM   2481 C  C     . THR A 1 301 ? -67.638 15.382  -0.613  1.00 85.52  ? 301 THR A C     1 
ATOM   2482 O  O     . THR A 1 301 ? -68.553 15.400  0.217   1.00 85.32  ? 301 THR A O     1 
ATOM   2483 C  CB    . THR A 1 301 ? -66.712 13.070  -0.552  1.00 82.08  ? 301 THR A CB    1 
ATOM   2484 O  OG1   . THR A 1 301 ? -65.355 13.466  -0.316  1.00 82.80  ? 301 THR A OG1   1 
ATOM   2485 C  CG2   . THR A 1 301 ? -66.728 11.711  -1.235  1.00 86.07  ? 301 THR A CG2   1 
ATOM   2486 N  N     . GLY A 1 302 ? -66.844 16.429  -0.825  1.00 86.08  ? 302 GLY A N     1 
ATOM   2487 C  CA    . GLY A 1 302 ? -67.039 17.680  -0.121  1.00 83.14  ? 302 GLY A CA    1 
ATOM   2488 C  C     . GLY A 1 302 ? -66.493 17.726  1.288   1.00 78.79  ? 302 GLY A C     1 
ATOM   2489 O  O     . GLY A 1 302 ? -66.836 18.649  2.036   1.00 88.40  ? 302 GLY A O     1 
ATOM   2490 N  N     . GLU A 1 303 ? -65.654 16.770  1.675   1.00 75.52  ? 303 GLU A N     1 
ATOM   2491 C  CA    . GLU A 1 303 ? -65.087 16.716  3.012   1.00 78.79  ? 303 GLU A CA    1 
ATOM   2492 C  C     . GLU A 1 303 ? -63.579 16.913  2.944   1.00 82.27  ? 303 GLU A C     1 
ATOM   2493 O  O     . GLU A 1 303 ? -62.947 16.658  1.917   1.00 82.08  ? 303 GLU A O     1 
ATOM   2494 C  CB    . GLU A 1 303 ? -65.410 15.381  3.692   1.00 83.96  ? 303 GLU A CB    1 
ATOM   2495 C  CG    . GLU A 1 303 ? -65.334 14.192  2.750   1.00 87.55  ? 303 GLU A CG    1 
ATOM   2496 C  CD    . GLU A 1 303 ? -65.750 12.891  3.404   1.00 103.38 ? 303 GLU A CD    1 
ATOM   2497 O  OE1   . GLU A 1 303 ? -66.705 12.904  4.211   1.00 91.37  ? 303 GLU A OE1   1 
ATOM   2498 O  OE2   . GLU A 1 303 ? -65.122 11.852  3.109   1.00 109.01 ? 303 GLU A OE2   1 
ATOM   2499 N  N     . ASN A 1 304 ? -63.011 17.380  4.058   1.00 84.47  ? 304 ASN A N     1 
ATOM   2500 C  CA    . ASN A 1 304 ? -61.565 17.568  4.196   1.00 89.95  ? 304 ASN A CA    1 
ATOM   2501 C  C     . ASN A 1 304 ? -61.011 18.543  3.159   1.00 89.24  ? 304 ASN A C     1 
ATOM   2502 O  O     . ASN A 1 304 ? -59.845 18.452  2.769   1.00 86.02  ? 304 ASN A O     1 
ATOM   2503 C  CB    . ASN A 1 304 ? -60.822 16.230  4.117   1.00 98.15  ? 304 ASN A CB    1 
ATOM   2504 C  CG    . ASN A 1 304 ? -60.142 15.860  5.419   1.00 113.09 ? 304 ASN A CG    1 
ATOM   2505 O  OD1   . ASN A 1 304 ? -59.599 16.718  6.115   1.00 107.11 ? 304 ASN A OD1   1 
ATOM   2506 N  ND2   . ASN A 1 304 ? -60.167 14.576  5.755   1.00 116.30 ? 304 ASN A ND2   1 
ATOM   2507 N  N     . LEU A 1 305 ? -61.839 19.487  2.706   1.00 80.46  ? 305 LEU A N     1 
ATOM   2508 C  CA    . LEU A 1 305 ? -61.399 20.437  1.690   1.00 76.18  ? 305 LEU A CA    1 
ATOM   2509 C  C     . LEU A 1 305 ? -60.418 21.463  2.240   1.00 73.08  ? 305 LEU A C     1 
ATOM   2510 O  O     . LEU A 1 305 ? -59.641 22.038  1.468   1.00 70.99  ? 305 LEU A O     1 
ATOM   2511 C  CB    . LEU A 1 305 ? -62.607 21.147  1.078   1.00 76.43  ? 305 LEU A CB    1 
ATOM   2512 C  CG    . LEU A 1 305 ? -63.295 20.425  -0.082  1.00 77.99  ? 305 LEU A CG    1 
ATOM   2513 C  CD1   . LEU A 1 305 ? -64.487 21.229  -0.578  1.00 79.77  ? 305 LEU A CD1   1 
ATOM   2514 C  CD2   . LEU A 1 305 ? -62.310 20.163  -1.213  1.00 64.55  ? 305 LEU A CD2   1 
ATOM   2515 N  N     . GLU A 1 306 ? -60.438 21.707  3.553   1.00 72.75  ? 306 GLU A N     1 
ATOM   2516 C  CA    . GLU A 1 306 ? -59.495 22.649  4.145   1.00 74.10  ? 306 GLU A CA    1 
ATOM   2517 C  C     . GLU A 1 306 ? -58.059 22.166  3.992   1.00 81.11  ? 306 GLU A C     1 
ATOM   2518 O  O     . GLU A 1 306 ? -57.142 22.982  3.850   1.00 75.98  ? 306 GLU A O     1 
ATOM   2519 C  CB    . GLU A 1 306 ? -59.840 22.870  5.618   1.00 83.42  ? 306 GLU A CB    1 
ATOM   2520 C  CG    . GLU A 1 306 ? -61.307 22.619  5.943   1.00 97.68  ? 306 GLU A CG    1 
ATOM   2521 C  CD    . GLU A 1 306 ? -61.763 23.337  7.198   1.00 107.11 ? 306 GLU A CD    1 
ATOM   2522 O  OE1   . GLU A 1 306 ? -60.921 23.572  8.090   1.00 115.95 ? 306 GLU A OE1   1 
ATOM   2523 O  OE2   . GLU A 1 306 ? -62.965 23.665  7.293   1.00 97.70  ? 306 GLU A OE2   1 
ATOM   2524 N  N     . ARG A 1 307 ? -57.849 20.849  3.996   1.00 86.00  ? 307 ARG A N     1 
ATOM   2525 C  CA    . ARG A 1 307 ? -56.515 20.305  3.764   1.00 74.32  ? 307 ARG A CA    1 
ATOM   2526 C  C     . ARG A 1 307 ? -56.031 20.623  2.352   1.00 71.79  ? 307 ARG A C     1 
ATOM   2527 O  O     . ARG A 1 307 ? -54.866 20.991  2.151   1.00 65.51  ? 307 ARG A O     1 
ATOM   2528 C  CB    . ARG A 1 307 ? -56.532 18.796  4.017   1.00 75.20  ? 307 ARG A CB    1 
ATOM   2529 C  CG    . ARG A 1 307 ? -55.261 18.052  3.651   1.00 84.29  ? 307 ARG A CG    1 
ATOM   2530 C  CD    . ARG A 1 307 ? -55.420 16.562  3.940   1.00 80.25  ? 307 ARG A CD    1 
ATOM   2531 N  NE    . ARG A 1 307 ? -54.237 15.793  3.575   1.00 84.00  ? 307 ARG A NE    1 
ATOM   2532 C  CZ    . ARG A 1 307 ? -53.130 15.731  4.301   1.00 89.22  ? 307 ARG A CZ    1 
ATOM   2533 N  NH1   . ARG A 1 307 ? -53.021 16.374  5.452   1.00 95.90  ? 307 ARG A NH1   1 
ATOM   2534 N  NH2   . ARG A 1 307 ? -52.107 15.003  3.863   1.00 89.88  ? 307 ARG A NH2   1 
ATOM   2535 N  N     . VAL A 1 308 ? -56.920 20.512  1.363   1.00 69.39  ? 308 VAL A N     1 
ATOM   2536 C  CA    . VAL A 1 308 ? -56.548 20.837  -0.011  1.00 67.94  ? 308 VAL A CA    1 
ATOM   2537 C  C     . VAL A 1 308 ? -56.305 22.335  -0.159  1.00 66.26  ? 308 VAL A C     1 
ATOM   2538 O  O     . VAL A 1 308 ? -55.408 22.766  -0.898  1.00 64.07  ? 308 VAL A O     1 
ATOM   2539 C  CB    . VAL A 1 308 ? -57.630 20.336  -0.984  1.00 62.88  ? 308 VAL A CB    1 
ATOM   2540 C  CG1   . VAL A 1 308 ? -57.184 20.524  -2.425  1.00 52.08  ? 308 VAL A CG1   1 
ATOM   2541 C  CG2   . VAL A 1 308 ? -57.959 18.877  -0.704  1.00 65.68  ? 308 VAL A CG2   1 
ATOM   2542 N  N     . ALA A 1 309 ? -57.098 23.153  0.538   1.00 64.60  ? 309 ALA A N     1 
ATOM   2543 C  CA    . ALA A 1 309 ? -56.862 24.594  0.520   1.00 65.53  ? 309 ALA A CA    1 
ATOM   2544 C  C     . ALA A 1 309 ? -55.501 24.933  1.115   1.00 61.02  ? 309 ALA A C     1 
ATOM   2545 O  O     . ALA A 1 309 ? -54.774 25.780  0.580   1.00 60.27  ? 309 ALA A O     1 
ATOM   2546 C  CB    . ALA A 1 309 ? -57.976 25.321  1.272   1.00 66.44  ? 309 ALA A CB    1 
ATOM   2547 N  N     . ARG A 1 310 ? -55.144 24.280  2.225   1.00 60.63  ? 310 ARG A N     1 
ATOM   2548 C  CA    . ARG A 1 310 ? -53.815 24.447  2.802   1.00 62.67  ? 310 ARG A CA    1 
ATOM   2549 C  C     . ARG A 1 310 ? -52.729 24.043  1.816   1.00 63.95  ? 310 ARG A C     1 
ATOM   2550 O  O     . ARG A 1 310 ? -51.713 24.733  1.689   1.00 60.89  ? 310 ARG A O     1 
ATOM   2551 C  CB    . ARG A 1 310 ? -53.686 23.622  4.081   1.00 69.28  ? 310 ARG A CB    1 
ATOM   2552 C  CG    . ARG A 1 310 ? -53.590 24.433  5.360   1.00 71.21  ? 310 ARG A CG    1 
ATOM   2553 C  CD    . ARG A 1 310 ? -52.834 23.672  6.443   1.00 82.33  ? 310 ARG A CD    1 
ATOM   2554 N  NE    . ARG A 1 310 ? -53.029 22.228  6.360   1.00 90.18  ? 310 ARG A NE    1 
ATOM   2555 C  CZ    . ARG A 1 310 ? -54.145 21.595  6.699   1.00 90.49  ? 310 ARG A CZ    1 
ATOM   2556 N  NH1   . ARG A 1 310 ? -55.202 22.248  7.155   1.00 79.27  ? 310 ARG A NH1   1 
ATOM   2557 N  NH2   . ARG A 1 310 ? -54.202 20.272  6.574   1.00 92.15  ? 310 ARG A NH2   1 
ATOM   2558 N  N     . TYR A 1 311 ? -52.919 22.916  1.124   1.00 66.10  ? 311 TYR A N     1 
ATOM   2559 C  CA    . TYR A 1 311 ? -51.914 22.464  0.165   1.00 60.57  ? 311 TYR A CA    1 
ATOM   2560 C  C     . TYR A 1 311 ? -51.719 23.484  -0.951  1.00 59.00  ? 311 TYR A C     1 
ATOM   2561 O  O     . TYR A 1 311 ? -50.583 23.791  -1.328  1.00 58.39  ? 311 TYR A O     1 
ATOM   2562 C  CB    . TYR A 1 311 ? -52.304 21.102  -0.411  1.00 62.00  ? 311 TYR A CB    1 
ATOM   2563 C  CG    . TYR A 1 311 ? -51.385 20.615  -1.510  1.00 63.55  ? 311 TYR A CG    1 
ATOM   2564 C  CD1   . TYR A 1 311 ? -50.147 20.062  -1.212  1.00 63.22  ? 311 TYR A CD1   1 
ATOM   2565 C  CD2   . TYR A 1 311 ? -51.756 20.707  -2.846  1.00 68.57  ? 311 TYR A CD2   1 
ATOM   2566 C  CE1   . TYR A 1 311 ? -49.303 19.616  -2.212  1.00 65.41  ? 311 TYR A CE1   1 
ATOM   2567 C  CE2   . TYR A 1 311 ? -50.917 20.264  -3.854  1.00 63.14  ? 311 TYR A CE2   1 
ATOM   2568 C  CZ    . TYR A 1 311 ? -49.694 19.720  -3.530  1.00 64.62  ? 311 TYR A CZ    1 
ATOM   2569 O  OH    . TYR A 1 311 ? -48.857 19.278  -4.529  1.00 86.66  ? 311 TYR A OH    1 
ATOM   2570 N  N     . SER A 1 312 ? -52.817 24.032  -1.481  1.00 56.36  ? 312 SER A N     1 
ATOM   2571 C  CA    . SER A 1 312 ? -52.710 25.027  -2.549  1.00 56.83  ? 312 SER A CA    1 
ATOM   2572 C  C     . SER A 1 312 ? -52.045 26.309  -2.055  1.00 58.04  ? 312 SER A C     1 
ATOM   2573 O  O     . SER A 1 312 ? -51.183 26.883  -2.743  1.00 54.73  ? 312 SER A O     1 
ATOM   2574 C  CB    . SER A 1 312 ? -54.096 25.329  -3.120  1.00 61.46  ? 312 SER A CB    1 
ATOM   2575 O  OG    . SER A 1 312 ? -54.008 25.857  -4.433  1.00 66.10  ? 312 SER A OG    1 
ATOM   2576 N  N     . MET A 1 313 ? -52.442 26.778  -0.868  1.00 55.02  ? 313 MET A N     1 
ATOM   2577 C  CA    . MET A 1 313 ? -51.843 27.983  -0.308  1.00 56.07  ? 313 MET A CA    1 
ATOM   2578 C  C     . MET A 1 313 ? -50.347 27.791  -0.092  1.00 60.35  ? 313 MET A C     1 
ATOM   2579 O  O     . MET A 1 313 ? -49.545 28.667  -0.441  1.00 53.77  ? 313 MET A O     1 
ATOM   2580 C  CB    . MET A 1 313 ? -52.568 28.351  0.992   1.00 53.40  ? 313 MET A CB    1 
ATOM   2581 C  CG    . MET A 1 313 ? -51.976 29.477  1.857   1.00 54.49  ? 313 MET A CG    1 
ATOM   2582 S  SD    . MET A 1 313 ? -50.377 29.216  2.658   1.00 74.74  ? 313 MET A SD    1 
ATOM   2583 C  CE    . MET A 1 313 ? -50.856 28.191  4.047   1.00 58.59  ? 313 MET A CE    1 
ATOM   2584 N  N     . GLU A 1 314 ? -49.954 26.642  0.463   1.00 56.96  ? 314 GLU A N     1 
ATOM   2585 C  CA    . GLU A 1 314 ? -48.542 26.373  0.705   1.00 57.21  ? 314 GLU A CA    1 
ATOM   2586 C  C     . GLU A 1 314 ? -47.775 26.245  -0.602  1.00 59.82  ? 314 GLU A C     1 
ATOM   2587 O  O     . GLU A 1 314 ? -46.617 26.669  -0.687  1.00 58.50  ? 314 GLU A O     1 
ATOM   2588 C  CB    . GLU A 1 314 ? -48.390 25.109  1.546   1.00 58.99  ? 314 GLU A CB    1 
ATOM   2589 C  CG    . GLU A 1 314 ? -48.808 25.280  2.995   1.00 58.61  ? 314 GLU A CG    1 
ATOM   2590 C  CD    . GLU A 1 314 ? -48.278 24.177  3.887   1.00 69.97  ? 314 GLU A CD    1 
ATOM   2591 O  OE1   . GLU A 1 314 ? -47.497 23.334  3.396   1.00 75.34  ? 314 GLU A OE1   1 
ATOM   2592 O  OE2   . GLU A 1 314 ? -48.647 24.150  5.080   1.00 88.68  ? 314 GLU A OE2   1 
ATOM   2593 N  N     . ASP A 1 315 ? -48.396 25.658  -1.628  1.00 53.07  ? 315 ASP A N     1 
ATOM   2594 C  CA    . ASP A 1 315 ? -47.778 25.625  -2.949  1.00 54.93  ? 315 ASP A CA    1 
ATOM   2595 C  C     . ASP A 1 315 ? -47.434 27.031  -3.417  1.00 56.83  ? 315 ASP A C     1 
ATOM   2596 O  O     . ASP A 1 315 ? -46.281 27.322  -3.763  1.00 56.49  ? 315 ASP A O     1 
ATOM   2597 C  CB    . ASP A 1 315 ? -48.716 24.942  -3.946  1.00 54.86  ? 315 ASP A CB    1 
ATOM   2598 C  CG    . ASP A 1 315 ? -48.358 23.489  -4.190  1.00 65.13  ? 315 ASP A CG    1 
ATOM   2599 O  OD1   . ASP A 1 315 ? -47.767 22.859  -3.288  1.00 68.46  ? 315 ASP A OD1   1 
ATOM   2600 O  OD2   . ASP A 1 315 ? -48.672 22.972  -5.283  1.00 64.74  ? 315 ASP A OD2   1 
ATOM   2601 N  N     . ALA A 1 316 ? -48.433 27.921  -3.429  1.00 53.28  ? 316 ALA A N     1 
ATOM   2602 C  CA    . ALA A 1 316 ? -48.191 29.294  -3.868  1.00 54.61  ? 316 ALA A CA    1 
ATOM   2603 C  C     . ALA A 1 316 ? -47.109 29.965  -3.027  1.00 50.97  ? 316 ALA A C     1 
ATOM   2604 O  O     . ALA A 1 316 ? -46.213 30.632  -3.563  1.00 51.95  ? 316 ALA A O     1 
ATOM   2605 C  CB    . ALA A 1 316 ? -49.490 30.099  -3.813  1.00 51.95  ? 316 ALA A CB    1 
ATOM   2606 N  N     . LYS A 1 317 ? -47.165 29.776  -1.706  1.00 50.52  ? 317 LYS A N     1 
ATOM   2607 C  CA    . LYS A 1 317 ? -46.212 30.423  -0.809  1.00 57.28  ? 317 LYS A CA    1 
ATOM   2608 C  C     . LYS A 1 317 ? -44.783 29.962  -1.086  1.00 54.25  ? 317 LYS A C     1 
ATOM   2609 O  O     . LYS A 1 317 ? -43.860 30.783  -1.189  1.00 54.76  ? 317 LYS A O     1 
ATOM   2610 C  CB    . LYS A 1 317 ? -46.608 30.140  0.641   1.00 55.84  ? 317 LYS A CB    1 
ATOM   2611 C  CG    . LYS A 1 317 ? -45.871 30.966  1.678   1.00 72.76  ? 317 LYS A CG    1 
ATOM   2612 C  CD    . LYS A 1 317 ? -46.729 31.164  2.919   1.00 76.72  ? 317 LYS A CD    1 
ATOM   2613 C  CE    . LYS A 1 317 ? -45.875 31.373  4.159   1.00 89.61  ? 317 LYS A CE    1 
ATOM   2614 N  NZ    . LYS A 1 317 ? -44.538 30.725  4.040   1.00 80.10  ? 317 LYS A NZ    1 
ATOM   2615 N  N     . VAL A 1 318 ? -44.580 28.646  -1.214  1.00 53.39  ? 318 VAL A N     1 
ATOM   2616 C  CA    . VAL A 1 318 ? -43.224 28.142  -1.399  1.00 52.71  ? 318 VAL A CA    1 
ATOM   2617 C  C     . VAL A 1 318 ? -42.700 28.489  -2.784  1.00 54.78  ? 318 VAL A C     1 
ATOM   2618 O  O     . VAL A 1 318 ? -41.503 28.750  -2.944  1.00 54.41  ? 318 VAL A O     1 
ATOM   2619 C  CB    . VAL A 1 318 ? -43.142 26.625  -1.128  1.00 49.97  ? 318 VAL A CB    1 
ATOM   2620 C  CG1   . VAL A 1 318 ? -43.572 26.309  0.297   1.00 50.41  ? 318 VAL A CG1   1 
ATOM   2621 C  CG2   . VAL A 1 318 ? -43.960 25.834  -2.143  1.00 55.28  ? 318 VAL A CG2   1 
ATOM   2622 N  N     . THR A 1 319 ? -43.564 28.519  -3.807  1.00 49.81  ? 319 THR A N     1 
ATOM   2623 C  CA    . THR A 1 319 ? -43.076 28.964  -5.110  1.00 53.00  ? 319 THR A CA    1 
ATOM   2624 C  C     . THR A 1 319 ? -42.687 30.438  -5.075  1.00 51.69  ? 319 THR A C     1 
ATOM   2625 O  O     . THR A 1 319 ? -41.702 30.834  -5.709  1.00 53.41  ? 319 THR A O     1 
ATOM   2626 C  CB    . THR A 1 319 ? -44.102 28.699  -6.214  1.00 41.53  ? 319 THR A CB    1 
ATOM   2627 O  OG1   . THR A 1 319 ? -45.209 29.598  -6.089  1.00 65.16  ? 319 THR A OG1   1 
ATOM   2628 C  CG2   . THR A 1 319 ? -44.558 27.245  -6.208  1.00 43.12  ? 319 THR A CG2   1 
ATOM   2629 N  N     . TYR A 1 320 ? -43.421 31.264  -4.321  1.00 51.52  ? 320 TYR A N     1 
ATOM   2630 C  CA    . TYR A 1 320 ? -43.026 32.667  -4.203  1.00 51.79  ? 320 TYR A CA    1 
ATOM   2631 C  C     . TYR A 1 320 ? -41.679 32.806  -3.501  1.00 55.86  ? 320 TYR A C     1 
ATOM   2632 O  O     . TYR A 1 320 ? -40.826 33.596  -3.925  1.00 54.54  ? 320 TYR A O     1 
ATOM   2633 C  CB    . TYR A 1 320 ? -44.094 33.464  -3.461  1.00 49.98  ? 320 TYR A CB    1 
ATOM   2634 C  CG    . TYR A 1 320 ? -43.718 34.917  -3.299  1.00 56.12  ? 320 TYR A CG    1 
ATOM   2635 C  CD1   . TYR A 1 320 ? -43.697 35.774  -4.392  1.00 52.98  ? 320 TYR A CD1   1 
ATOM   2636 C  CD2   . TYR A 1 320 ? -43.369 35.430  -2.058  1.00 60.91  ? 320 TYR A CD2   1 
ATOM   2637 C  CE1   . TYR A 1 320 ? -43.345 37.105  -4.253  1.00 54.07  ? 320 TYR A CE1   1 
ATOM   2638 C  CE2   . TYR A 1 320 ? -43.016 36.759  -1.906  1.00 63.80  ? 320 TYR A CE2   1 
ATOM   2639 C  CZ    . TYR A 1 320 ? -43.007 37.592  -3.006  1.00 60.48  ? 320 TYR A CZ    1 
ATOM   2640 O  OH    . TYR A 1 320 ? -42.656 38.915  -2.854  1.00 69.33  ? 320 TYR A OH    1 
ATOM   2641 N  N     . GLU A 1 321 ? -41.472 32.051  -2.420  1.00 54.00  ? 321 GLU A N     1 
ATOM   2642 C  CA    . GLU A 1 321 ? -40.198 32.130  -1.709  1.00 57.76  ? 321 GLU A CA    1 
ATOM   2643 C  C     . GLU A 1 321 ? -39.044 31.641  -2.583  1.00 59.54  ? 321 GLU A C     1 
ATOM   2644 O  O     . GLU A 1 321 ? -37.969 32.258  -2.615  1.00 59.77  ? 321 GLU A O     1 
ATOM   2645 C  CB    . GLU A 1 321 ? -40.272 31.329  -0.410  1.00 59.71  ? 321 GLU A CB    1 
ATOM   2646 C  CG    . GLU A 1 321 ? -41.274 31.878  0.597   1.00 69.60  ? 321 GLU A CG    1 
ATOM   2647 C  CD    . GLU A 1 321 ? -40.658 32.884  1.551   1.00 98.79  ? 321 GLU A CD    1 
ATOM   2648 O  OE1   . GLU A 1 321 ? -39.653 32.543  2.208   1.00 99.95  ? 321 GLU A OE1   1 
ATOM   2649 O  OE2   . GLU A 1 321 ? -41.182 34.014  1.646   1.00 95.82  ? 321 GLU A OE2   1 
ATOM   2650 N  N     . LEU A 1 322 ? -39.253 30.541  -3.310  1.00 56.97  ? 322 LEU A N     1 
ATOM   2651 C  CA    . LEU A 1 322 ? -38.214 30.039  -4.203  1.00 56.11  ? 322 LEU A CA    1 
ATOM   2652 C  C     . LEU A 1 322 ? -37.910 31.040  -5.311  1.00 58.65  ? 322 LEU A C     1 
ATOM   2653 O  O     . LEU A 1 322 ? -36.749 31.212  -5.699  1.00 58.08  ? 322 LEU A O     1 
ATOM   2654 C  CB    . LEU A 1 322 ? -38.634 28.693  -4.791  1.00 50.46  ? 322 LEU A CB    1 
ATOM   2655 C  CG    . LEU A 1 322 ? -38.607 27.506  -3.825  1.00 53.37  ? 322 LEU A CG    1 
ATOM   2656 C  CD1   . LEU A 1 322 ? -39.514 26.389  -4.317  1.00 49.15  ? 322 LEU A CD1   1 
ATOM   2657 C  CD2   . LEU A 1 322 ? -37.185 26.996  -3.627  1.00 59.61  ? 322 LEU A CD2   1 
ATOM   2658 N  N     . GLY A 1 323 ? -38.939 31.711  -5.833  1.00 54.32  ? 323 GLY A N     1 
ATOM   2659 C  CA    . GLY A 1 323 ? -38.701 32.745  -6.825  1.00 53.12  ? 323 GLY A CA    1 
ATOM   2660 C  C     . GLY A 1 323 ? -37.895 33.899  -6.263  1.00 58.29  ? 323 GLY A C     1 
ATOM   2661 O  O     . GLY A 1 323 ? -36.956 34.382  -6.900  1.00 57.23  ? 323 GLY A O     1 
ATOM   2662 N  N     . LYS A 1 324 ? -38.247 34.351  -5.057  1.00 59.79  ? 324 LYS A N     1 
ATOM   2663 C  CA    . LYS A 1 324 ? -37.472 35.404  -4.408  1.00 61.64  ? 324 LYS A CA    1 
ATOM   2664 C  C     . LYS A 1 324 ? -36.014 34.992  -4.247  1.00 63.07  ? 324 LYS A C     1 
ATOM   2665 O  O     . LYS A 1 324 ? -35.106 35.818  -4.399  1.00 70.53  ? 324 LYS A O     1 
ATOM   2666 C  CB    . LYS A 1 324 ? -38.089 35.755  -3.052  1.00 62.75  ? 324 LYS A CB    1 
ATOM   2667 C  CG    . LYS A 1 324 ? -37.626 37.090  -2.472  1.00 79.18  ? 324 LYS A CG    1 
ATOM   2668 C  CD    . LYS A 1 324 ? -37.281 38.094  -3.565  1.00 103.51 ? 324 LYS A CD    1 
ATOM   2669 C  CE    . LYS A 1 324 ? -36.231 39.098  -3.110  1.00 81.88  ? 324 LYS A CE    1 
ATOM   2670 N  NZ    . LYS A 1 324 ? -36.744 40.010  -2.050  1.00 93.83  ? 324 LYS A NZ    1 
ATOM   2671 N  N     . GLU A 1 325 ? -35.767 33.715  -3.955  1.00 59.51  ? 325 GLU A N     1 
ATOM   2672 C  CA    . GLU A 1 325 ? -34.387 33.280  -3.761  1.00 63.43  ? 325 GLU A CA    1 
ATOM   2673 C  C     . GLU A 1 325 ? -33.629 33.158  -5.082  1.00 65.48  ? 325 GLU A C     1 
ATOM   2674 O  O     . GLU A 1 325 ? -32.444 33.503  -5.151  1.00 67.71  ? 325 GLU A O     1 
ATOM   2675 C  CB    . GLU A 1 325 ? -34.351 31.953  -3.000  1.00 68.08  ? 325 GLU A CB    1 
ATOM   2676 C  CG    . GLU A 1 325 ? -32.957 31.347  -2.871  1.00 77.82  ? 325 GLU A CG    1 
ATOM   2677 C  CD    . GLU A 1 325 ? -32.235 31.785  -1.608  1.00 87.18  ? 325 GLU A CD    1 
ATOM   2678 O  OE1   . GLU A 1 325 ? -32.161 33.007  -1.356  1.00 98.46  ? 325 GLU A OE1   1 
ATOM   2679 O  OE2   . GLU A 1 325 ? -31.736 30.909  -0.869  1.00 92.72  ? 325 GLU A OE2   1 
ATOM   2680 N  N     . PHE A 1 326 ? -34.290 32.691  -6.144  1.00 60.98  ? 326 PHE A N     1 
ATOM   2681 C  CA    . PHE A 1 326 ? -33.579 32.300  -7.357  1.00 51.69  ? 326 PHE A CA    1 
ATOM   2682 C  C     . PHE A 1 326 ? -33.594 33.342  -8.472  1.00 55.25  ? 326 PHE A C     1 
ATOM   2683 O  O     . PHE A 1 326 ? -32.749 33.261  -9.370  1.00 63.39  ? 326 PHE A O     1 
ATOM   2684 C  CB    . PHE A 1 326 ? -34.151 30.984  -7.901  1.00 51.32  ? 326 PHE A CB    1 
ATOM   2685 C  CG    . PHE A 1 326 ? -33.652 29.764  -7.179  1.00 57.15  ? 326 PHE A CG    1 
ATOM   2686 C  CD1   . PHE A 1 326 ? -34.303 29.297  -6.049  1.00 65.54  ? 326 PHE A CD1   1 
ATOM   2687 C  CD2   . PHE A 1 326 ? -32.529 29.088  -7.627  1.00 59.46  ? 326 PHE A CD2   1 
ATOM   2688 C  CE1   . PHE A 1 326 ? -33.843 28.176  -5.379  1.00 69.03  ? 326 PHE A CE1   1 
ATOM   2689 C  CE2   . PHE A 1 326 ? -32.064 27.967  -6.963  1.00 62.21  ? 326 PHE A CE2   1 
ATOM   2690 C  CZ    . PHE A 1 326 ? -32.721 27.511  -5.837  1.00 68.90  ? 326 PHE A CZ    1 
ATOM   2691 N  N     . LEU A 1 327 ? -34.513 34.315  -8.452  1.00 58.95  ? 327 LEU A N     1 
ATOM   2692 C  CA    . LEU A 1 327 ? -34.585 35.258  -9.569  1.00 59.30  ? 327 LEU A CA    1 
ATOM   2693 C  C     . LEU A 1 327 ? -33.398 36.214  -9.621  1.00 57.19  ? 327 LEU A C     1 
ATOM   2694 O  O     . LEU A 1 327 ? -32.835 36.400  -10.715 1.00 56.24  ? 327 LEU A O     1 
ATOM   2695 C  CB    . LEU A 1 327 ? -35.915 36.015  -9.531  1.00 52.33  ? 327 LEU A CB    1 
ATOM   2696 C  CG    . LEU A 1 327 ? -36.088 37.055  -10.641 1.00 54.31  ? 327 LEU A CG    1 
ATOM   2697 C  CD1   . LEU A 1 327 ? -37.464 36.940  -11.265 1.00 66.30  ? 327 LEU A CD1   1 
ATOM   2698 C  CD2   . LEU A 1 327 ? -35.857 38.468  -10.114 1.00 59.11  ? 327 LEU A CD2   1 
ATOM   2699 N  N     . PRO A 1 328 ? -32.982 36.870  -8.528  1.00 58.02  ? 328 PRO A N     1 
ATOM   2700 C  CA    . PRO A 1 328 ? -31.800 37.745  -8.621  1.00 70.33  ? 328 PRO A CA    1 
ATOM   2701 C  C     . PRO A 1 328 ? -30.558 37.007  -9.069  1.00 61.70  ? 328 PRO A C     1 
ATOM   2702 O  O     . PRO A 1 328 ? -29.639 37.624  -9.619  1.00 62.49  ? 328 PRO A O     1 
ATOM   2703 C  CB    . PRO A 1 328 ? -31.643 38.281  -7.192  1.00 65.53  ? 328 PRO A CB    1 
ATOM   2704 C  CG    . PRO A 1 328 ? -32.988 38.129  -6.580  1.00 65.13  ? 328 PRO A CG    1 
ATOM   2705 C  CD    . PRO A 1 328 ? -33.529 36.861  -7.159  1.00 58.66  ? 328 PRO A CD    1 
ATOM   2706 N  N     . MET A 1 329 ? -30.516 35.695  -8.856  1.00 61.00  ? 329 MET A N     1 
ATOM   2707 C  CA    . MET A 1 329 ? -29.378 34.892  -9.275  1.00 65.11  ? 329 MET A CA    1 
ATOM   2708 C  C     . MET A 1 329 ? -29.393 34.667  -10.783 1.00 66.22  ? 329 MET A C     1 
ATOM   2709 O  O     . MET A 1 329 ? -28.365 34.812  -11.453 1.00 65.40  ? 329 MET A O     1 
ATOM   2710 C  CB    . MET A 1 329 ? -29.400 33.565  -8.522  1.00 65.00  ? 329 MET A CB    1 
ATOM   2711 C  CG    . MET A 1 329 ? -29.523 33.705  -7.008  1.00 73.42  ? 329 MET A CG    1 
ATOM   2712 S  SD    . MET A 1 329 ? -27.941 33.566  -6.148  1.00 116.81 ? 329 MET A SD    1 
ATOM   2713 C  CE    . MET A 1 329 ? -27.988 34.985  -5.058  1.00 80.80  ? 329 MET A CE    1 
ATOM   2714 N  N     . GLU A 1 330 ? -30.556 34.311  -11.337 1.00 57.76  ? 330 GLU A N     1 
ATOM   2715 C  CA    . GLU A 1 330 ? -30.677 34.137  -12.781 1.00 51.46  ? 330 GLU A CA    1 
ATOM   2716 C  C     . GLU A 1 330 ? -30.572 35.462  -13.529 1.00 53.44  ? 330 GLU A C     1 
ATOM   2717 O  O     . GLU A 1 330 ? -30.232 35.470  -14.720 1.00 49.72  ? 330 GLU A O     1 
ATOM   2718 C  CB    . GLU A 1 330 ? -31.998 33.445  -13.114 1.00 60.31  ? 330 GLU A CB    1 
ATOM   2719 C  CG    . GLU A 1 330 ? -31.991 31.939  -12.912 1.00 60.04  ? 330 GLU A CG    1 
ATOM   2720 C  CD    . GLU A 1 330 ? -31.098 31.222  -13.902 1.00 64.04  ? 330 GLU A CD    1 
ATOM   2721 O  OE1   . GLU A 1 330 ? -31.483 31.124  -15.087 1.00 61.05  ? 330 GLU A OE1   1 
ATOM   2722 O  OE2   . GLU A 1 330 ? -30.014 30.753  -13.497 1.00 68.24  ? 330 GLU A OE2   1 
ATOM   2723 N  N     . ALA A 1 331 ? -30.856 36.581  -12.860 1.00 53.65  ? 331 ALA A N     1 
ATOM   2724 C  CA    . ALA A 1 331 ? -30.613 37.880  -13.475 1.00 55.44  ? 331 ALA A CA    1 
ATOM   2725 C  C     . ALA A 1 331 ? -29.132 38.087  -13.765 1.00 58.09  ? 331 ALA A C     1 
ATOM   2726 O  O     . ALA A 1 331 ? -28.776 38.762  -14.739 1.00 54.16  ? 331 ALA A O     1 
ATOM   2727 C  CB    . ALA A 1 331 ? -31.146 38.994  -12.575 1.00 53.31  ? 331 ALA A CB    1 
ATOM   2728 N  N     . GLN A 1 332 ? -28.253 37.506  -12.944 1.00 58.74  ? 332 GLN A N     1 
ATOM   2729 C  CA    . GLN A 1 332 ? -26.824 37.570  -13.233 1.00 56.59  ? 332 GLN A CA    1 
ATOM   2730 C  C     . GLN A 1 332 ? -26.486 36.800  -14.504 1.00 50.06  ? 332 GLN A C     1 
ATOM   2731 O  O     . GLN A 1 332 ? -25.650 37.242  -15.298 1.00 50.04  ? 332 GLN A O     1 
ATOM   2732 C  CB    . GLN A 1 332 ? -26.022 37.037  -12.048 1.00 54.58  ? 332 GLN A CB    1 
ATOM   2733 C  CG    . GLN A 1 332 ? -26.187 37.852  -10.778 1.00 61.46  ? 332 GLN A CG    1 
ATOM   2734 C  CD    . GLN A 1 332 ? -25.070 37.609  -9.784  1.00 94.37  ? 332 GLN A CD    1 
ATOM   2735 O  OE1   . GLN A 1 332 ? -24.211 38.465  -9.574  1.00 97.06  ? 332 GLN A OE1   1 
ATOM   2736 N  NE2   . GLN A 1 332 ? -25.075 36.432  -9.166  1.00 95.42  ? 332 GLN A NE2   1 
ATOM   2737 N  N     . LEU A 1 333 ? -27.126 35.645  -14.714 1.00 49.69  ? 333 LEU A N     1 
ATOM   2738 C  CA    . LEU A 1 333 ? -26.969 34.934  -15.980 1.00 47.11  ? 333 LEU A CA    1 
ATOM   2739 C  C     . LEU A 1 333 ? -27.457 35.784  -17.145 1.00 46.63  ? 333 LEU A C     1 
ATOM   2740 O  O     . LEU A 1 333 ? -26.824 35.825  -18.208 1.00 46.69  ? 333 LEU A O     1 
ATOM   2741 C  CB    . LEU A 1 333 ? -27.730 33.609  -15.935 1.00 44.94  ? 333 LEU A CB    1 
ATOM   2742 C  CG    . LEU A 1 333 ? -27.554 32.668  -17.130 1.00 45.33  ? 333 LEU A CG    1 
ATOM   2743 C  CD1   . LEU A 1 333 ? -26.079 32.388  -17.400 1.00 46.20  ? 333 LEU A CD1   1 
ATOM   2744 C  CD2   . LEU A 1 333 ? -28.325 31.374  -16.920 1.00 42.45  ? 333 LEU A CD2   1 
ATOM   2745 N  N     . SER A 1 334 ? -28.592 36.462  -16.960 1.00 50.05  ? 334 SER A N     1 
ATOM   2746 C  CA    . SER A 1 334 ? -29.113 37.341  -18.004 1.00 48.01  ? 334 SER A CA    1 
ATOM   2747 C  C     . SER A 1 334 ? -28.113 38.438  -18.352 1.00 42.76  ? 334 SER A C     1 
ATOM   2748 O  O     . SER A 1 334 ? -27.897 38.741  -19.532 1.00 43.45  ? 334 SER A O     1 
ATOM   2749 C  CB    . SER A 1 334 ? -30.445 37.947  -17.562 1.00 49.51  ? 334 SER A CB    1 
ATOM   2750 O  OG    . SER A 1 334 ? -31.066 38.650  -18.625 1.00 45.61  ? 334 SER A OG    1 
ATOM   2751 N  N     . ARG A 1 335 ? -27.492 39.043  -17.337 1.00 44.71  ? 335 ARG A N     1 
ATOM   2752 C  CA    . ARG A 1 335 ? -26.487 40.075  -17.589 1.00 56.05  ? 335 ARG A CA    1 
ATOM   2753 C  C     . ARG A 1 335 ? -25.243 39.495  -18.255 1.00 43.91  ? 335 ARG A C     1 
ATOM   2754 O  O     . ARG A 1 335 ? -24.653 40.127  -19.139 1.00 45.24  ? 335 ARG A O     1 
ATOM   2755 C  CB    . ARG A 1 335 ? -26.104 40.774  -16.285 1.00 54.23  ? 335 ARG A CB    1 
ATOM   2756 C  CG    . ARG A 1 335 ? -27.208 41.601  -15.661 1.00 56.89  ? 335 ARG A CG    1 
ATOM   2757 C  CD    . ARG A 1 335 ? -26.641 42.542  -14.615 1.00 64.15  ? 335 ARG A CD    1 
ATOM   2758 N  NE    . ARG A 1 335 ? -26.497 41.889  -13.320 1.00 70.27  ? 335 ARG A NE    1 
ATOM   2759 C  CZ    . ARG A 1 335 ? -27.488 41.704  -12.459 1.00 83.93  ? 335 ARG A CZ    1 
ATOM   2760 N  NH1   . ARG A 1 335 ? -28.715 42.129  -12.716 1.00 68.10  ? 335 ARG A NH1   1 
ATOM   2761 N  NH2   . ARG A 1 335 ? -27.242 41.082  -11.310 1.00 87.95  ? 335 ARG A NH2   1 
ATOM   2762 N  N     . LEU A 1 336 ? -24.826 38.297  -17.841 1.00 39.70  ? 336 LEU A N     1 
ATOM   2763 C  CA    . LEU A 1 336 ? -23.613 37.697  -18.388 1.00 44.14  ? 336 LEU A CA    1 
ATOM   2764 C  C     . LEU A 1 336 ? -23.775 37.341  -19.860 1.00 48.16  ? 336 LEU A C     1 
ATOM   2765 O  O     . LEU A 1 336 ? -22.872 37.588  -20.666 1.00 45.09  ? 336 LEU A O     1 
ATOM   2766 C  CB    . LEU A 1 336 ? -23.234 36.458  -17.580 1.00 49.84  ? 336 LEU A CB    1 
ATOM   2767 C  CG    . LEU A 1 336 ? -21.839 35.905  -17.860 1.00 52.08  ? 336 LEU A CG    1 
ATOM   2768 C  CD1   . LEU A 1 336 ? -20.803 36.996  -17.661 1.00 43.65  ? 336 LEU A CD1   1 
ATOM   2769 C  CD2   . LEU A 1 336 ? -21.550 34.705  -16.972 1.00 51.86  ? 336 LEU A CD2   1 
ATOM   2770 N  N     . ILE A 1 337 ? -24.911 36.748  -20.228 1.00 46.69  ? 337 ILE A N     1 
ATOM   2771 C  CA    . ILE A 1 337 ? -25.125 36.348  -21.616 1.00 41.51  ? 337 ILE A CA    1 
ATOM   2772 C  C     . ILE A 1 337 ? -25.653 37.487  -22.484 1.00 39.09  ? 337 ILE A C     1 
ATOM   2773 O  O     . ILE A 1 337 ? -25.481 37.451  -23.712 1.00 41.91  ? 337 ILE A O     1 
ATOM   2774 C  CB    . ILE A 1 337 ? -26.074 35.136  -21.681 1.00 46.36  ? 337 ILE A CB    1 
ATOM   2775 C  CG1   . ILE A 1 337 ? -25.675 34.104  -20.628 1.00 44.88  ? 337 ILE A CG1   1 
ATOM   2776 C  CG2   . ILE A 1 337 ? -26.059 34.496  -23.065 1.00 43.69  ? 337 ILE A CG2   1 
ATOM   2777 C  CD1   . ILE A 1 337 ? -24.362 33.408  -20.927 1.00 44.64  ? 337 ILE A CD1   1 
ATOM   2778 N  N     . GLY A 1 338 ? -26.270 38.503  -21.887 1.00 42.72  ? 338 GLY A N     1 
ATOM   2779 C  CA    . GLY A 1 338 ? -26.825 39.591  -22.665 1.00 43.77  ? 338 GLY A CA    1 
ATOM   2780 C  C     . GLY A 1 338 ? -28.147 39.279  -23.325 1.00 43.94  ? 338 GLY A C     1 
ATOM   2781 O  O     . GLY A 1 338 ? -28.473 39.874  -24.359 1.00 44.01  ? 338 GLY A O     1 
ATOM   2782 N  N     . GLN A 1 339 ? -28.920 38.353  -22.763 1.00 43.45  ? 339 GLN A N     1 
ATOM   2783 C  CA    . GLN A 1 339 ? -30.234 37.998  -23.275 1.00 45.04  ? 339 GLN A CA    1 
ATOM   2784 C  C     . GLN A 1 339 ? -31.236 38.022  -22.130 1.00 48.82  ? 339 GLN A C     1 
ATOM   2785 O  O     . GLN A 1 339 ? -30.869 38.104  -20.955 1.00 44.96  ? 339 GLN A O     1 
ATOM   2786 C  CB    . GLN A 1 339 ? -30.220 36.623  -23.957 1.00 48.27  ? 339 GLN A CB    1 
ATOM   2787 C  CG    . GLN A 1 339 ? -29.328 36.563  -25.189 1.00 45.16  ? 339 GLN A CG    1 
ATOM   2788 C  CD    . GLN A 1 339 ? -29.743 37.561  -26.248 1.00 49.72  ? 339 GLN A CD    1 
ATOM   2789 O  OE1   . GLN A 1 339 ? -30.928 37.710  -26.544 1.00 53.92  ? 339 GLN A OE1   1 
ATOM   2790 N  NE2   . GLN A 1 339 ? -28.768 38.254  -26.824 1.00 47.59  ? 339 GLN A NE2   1 
ATOM   2791 N  N     . SER A 1 340 ? -32.517 37.952  -22.487 1.00 50.95  ? 340 SER A N     1 
ATOM   2792 C  CA    . SER A 1 340 ? -33.579 38.129  -21.507 1.00 49.38  ? 340 SER A CA    1 
ATOM   2793 C  C     . SER A 1 340 ? -33.552 37.022  -20.460 1.00 46.88  ? 340 SER A C     1 
ATOM   2794 O  O     . SER A 1 340 ? -33.127 35.893  -20.722 1.00 40.27  ? 340 SER A O     1 
ATOM   2795 C  CB    . SER A 1 340 ? -34.941 38.156  -22.198 1.00 49.05  ? 340 SER A CB    1 
ATOM   2796 O  OG    . SER A 1 340 ? -35.396 36.842  -22.465 1.00 50.75  ? 340 SER A OG    1 
ATOM   2797 N  N     . LEU A 1 341 ? -34.009 37.370  -19.255 1.00 37.43  ? 341 LEU A N     1 
ATOM   2798 C  CA    . LEU A 1 341 ? -34.124 36.387  -18.182 1.00 42.91  ? 341 LEU A CA    1 
ATOM   2799 C  C     . LEU A 1 341 ? -34.987 35.205  -18.609 1.00 52.05  ? 341 LEU A C     1 
ATOM   2800 O  O     . LEU A 1 341 ? -34.659 34.047  -18.317 1.00 52.36  ? 341 LEU A O     1 
ATOM   2801 C  CB    . LEU A 1 341 ? -34.700 37.058  -16.935 1.00 43.04  ? 341 LEU A CB    1 
ATOM   2802 C  CG    . LEU A 1 341 ? -35.116 36.163  -15.769 1.00 53.62  ? 341 LEU A CG    1 
ATOM   2803 C  CD1   . LEU A 1 341 ? -33.940 35.340  -15.296 1.00 57.47  ? 341 LEU A CD1   1 
ATOM   2804 C  CD2   . LEU A 1 341 ? -35.675 37.002  -14.633 1.00 60.77  ? 341 LEU A CD2   1 
ATOM   2805 N  N     . TRP A 1 342 ? -36.089 35.482  -19.312 1.00 48.16  ? 342 TRP A N     1 
ATOM   2806 C  CA    . TRP A 1 342 ? -36.948 34.416  -19.817 1.00 48.14  ? 342 TRP A CA    1 
ATOM   2807 C  C     . TRP A 1 342 ? -36.169 33.445  -20.693 1.00 47.14  ? 342 TRP A C     1 
ATOM   2808 O  O     . TRP A 1 342 ? -36.387 32.229  -20.633 1.00 44.63  ? 342 TRP A O     1 
ATOM   2809 C  CB    . TRP A 1 342 ? -38.114 35.019  -20.601 1.00 50.96  ? 342 TRP A CB    1 
ATOM   2810 C  CG    . TRP A 1 342 ? -39.185 34.035  -20.930 1.00 50.18  ? 342 TRP A CG    1 
ATOM   2811 C  CD1   . TRP A 1 342 ? -40.346 33.829  -20.245 1.00 50.32  ? 342 TRP A CD1   1 
ATOM   2812 C  CD2   . TRP A 1 342 ? -39.200 33.117  -22.030 1.00 55.66  ? 342 TRP A CD2   1 
ATOM   2813 N  NE1   . TRP A 1 342 ? -41.082 32.837  -20.847 1.00 54.64  ? 342 TRP A NE1   1 
ATOM   2814 C  CE2   . TRP A 1 342 ? -40.400 32.385  -21.946 1.00 57.74  ? 342 TRP A CE2   1 
ATOM   2815 C  CE3   . TRP A 1 342 ? -38.315 32.844  -23.079 1.00 53.48  ? 342 TRP A CE3   1 
ATOM   2816 C  CZ2   . TRP A 1 342 ? -40.736 31.396  -22.868 1.00 57.31  ? 342 TRP A CZ2   1 
ATOM   2817 C  CZ3   . TRP A 1 342 ? -38.651 31.863  -23.993 1.00 55.43  ? 342 TRP A CZ3   1 
ATOM   2818 C  CH2   . TRP A 1 342 ? -39.852 31.153  -23.883 1.00 59.64  ? 342 TRP A CH2   1 
ATOM   2819 N  N     . ASP A 1 343 ? -35.256 33.963  -21.515 1.00 49.57  ? 343 ASP A N     1 
ATOM   2820 C  CA    . ASP A 1 343 ? -34.497 33.105  -22.418 1.00 48.50  ? 343 ASP A CA    1 
ATOM   2821 C  C     . ASP A 1 343 ? -33.437 32.312  -21.662 1.00 47.09  ? 343 ASP A C     1 
ATOM   2822 O  O     . ASP A 1 343 ? -33.359 31.084  -21.785 1.00 47.97  ? 343 ASP A O     1 
ATOM   2823 C  CB    . ASP A 1 343 ? -33.858 33.944  -23.526 1.00 54.81  ? 343 ASP A CB    1 
ATOM   2824 C  CG    . ASP A 1 343 ? -34.839 34.305  -24.626 1.00 72.38  ? 343 ASP A CG    1 
ATOM   2825 O  OD1   . ASP A 1 343 ? -35.162 33.425  -25.451 1.00 64.58  ? 343 ASP A OD1   1 
ATOM   2826 O  OD2   . ASP A 1 343 ? -35.286 35.471  -24.668 1.00 82.80  ? 343 ASP A OD2   1 
ATOM   2827 N  N     . VAL A 1 344 ? -32.611 32.998  -20.867 1.00 47.36  ? 344 VAL A N     1 
ATOM   2828 C  CA    . VAL A 1 344 ? -31.498 32.322  -20.211 1.00 49.96  ? 344 VAL A CA    1 
ATOM   2829 C  C     . VAL A 1 344 ? -31.971 31.359  -19.133 1.00 47.84  ? 344 VAL A C     1 
ATOM   2830 O  O     . VAL A 1 344 ? -31.222 30.454  -18.749 1.00 54.76  ? 344 VAL A O     1 
ATOM   2831 C  CB    . VAL A 1 344 ? -30.508 33.347  -19.626 1.00 43.84  ? 344 VAL A CB    1 
ATOM   2832 C  CG1   . VAL A 1 344 ? -30.127 34.372  -20.681 1.00 39.73  ? 344 VAL A CG1   1 
ATOM   2833 C  CG2   . VAL A 1 344 ? -31.097 34.026  -18.402 1.00 43.18  ? 344 VAL A CG2   1 
ATOM   2834 N  N     . SER A 1 345 ? -33.199 31.516  -18.635 1.00 48.14  ? 345 SER A N     1 
ATOM   2835 C  CA    . SER A 1 345 ? -33.683 30.594  -17.614 1.00 48.14  ? 345 SER A CA    1 
ATOM   2836 C  C     . SER A 1 345 ? -34.031 29.231  -18.200 1.00 48.28  ? 345 SER A C     1 
ATOM   2837 O  O     . SER A 1 345 ? -33.980 28.222  -17.488 1.00 53.73  ? 345 SER A O     1 
ATOM   2838 C  CB    . SER A 1 345 ? -34.895 31.189  -16.903 1.00 48.45  ? 345 SER A CB    1 
ATOM   2839 O  OG    . SER A 1 345 ? -35.900 31.538  -17.837 1.00 43.10  ? 345 SER A OG    1 
ATOM   2840 N  N     . ARG A 1 346 ? -34.377 29.175  -19.489 1.00 44.89  ? 346 ARG A N     1 
ATOM   2841 C  CA    . ARG A 1 346 ? -34.789 27.929  -20.120 1.00 47.60  ? 346 ARG A CA    1 
ATOM   2842 C  C     . ARG A 1 346 ? -33.831 27.430  -21.189 1.00 51.67  ? 346 ARG A C     1 
ATOM   2843 O  O     . ARG A 1 346 ? -33.924 26.262  -21.577 1.00 57.85  ? 346 ARG A O     1 
ATOM   2844 C  CB    . ARG A 1 346 ? -36.180 28.084  -20.750 1.00 52.97  ? 346 ARG A CB    1 
ATOM   2845 C  CG    . ARG A 1 346 ? -37.107 28.996  -19.976 1.00 52.64  ? 346 ARG A CG    1 
ATOM   2846 C  CD    . ARG A 1 346 ? -38.375 29.287  -20.759 1.00 53.17  ? 346 ARG A CD    1 
ATOM   2847 N  NE    . ARG A 1 346 ? -39.544 29.368  -19.892 1.00 50.19  ? 346 ARG A NE    1 
ATOM   2848 C  CZ    . ARG A 1 346 ? -39.806 30.382  -19.079 1.00 46.06  ? 346 ARG A CZ    1 
ATOM   2849 N  NH1   . ARG A 1 346 ? -38.995 31.423  -18.989 1.00 45.52  ? 346 ARG A NH1   1 
ATOM   2850 N  NH2   . ARG A 1 346 ? -40.907 30.349  -18.333 1.00 46.52  ? 346 ARG A NH2   1 
ATOM   2851 N  N     . SER A 1 347 ? -32.927 28.273  -21.674 1.00 58.07  ? 347 SER A N     1 
ATOM   2852 C  CA    . SER A 1 347 ? -32.047 27.889  -22.765 1.00 59.96  ? 347 SER A CA    1 
ATOM   2853 C  C     . SER A 1 347 ? -30.945 26.958  -22.271 1.00 56.99  ? 347 SER A C     1 
ATOM   2854 O  O     . SER A 1 347 ? -30.512 27.024  -21.117 1.00 52.80  ? 347 SER A O     1 
ATOM   2855 C  CB    . SER A 1 347 ? -31.444 29.132  -23.417 1.00 57.29  ? 347 SER A CB    1 
ATOM   2856 O  OG    . SER A 1 347 ? -30.929 28.842  -24.702 1.00 78.99  ? 347 SER A OG    1 
ATOM   2857 N  N     . SER A 1 348 ? -30.500 26.075  -23.161 1.00 54.18  ? 348 SER A N     1 
ATOM   2858 C  CA    . SER A 1 348 ? -29.445 25.131  -22.827 1.00 55.75  ? 348 SER A CA    1 
ATOM   2859 C  C     . SER A 1 348 ? -28.102 25.848  -22.701 1.00 53.38  ? 348 SER A C     1 
ATOM   2860 O  O     . SER A 1 348 ? -27.946 27.014  -23.076 1.00 51.48  ? 348 SER A O     1 
ATOM   2861 C  CB    . SER A 1 348 ? -29.355 24.033  -23.884 1.00 55.93  ? 348 SER A CB    1 
ATOM   2862 O  OG    . SER A 1 348 ? -28.777 24.529  -25.078 1.00 54.07  ? 348 SER A OG    1 
ATOM   2863 N  N     . THR A 1 349 ? -27.117 25.124  -22.164 1.00 46.72  ? 349 THR A N     1 
ATOM   2864 C  CA    . THR A 1 349 ? -25.787 25.700  -21.988 1.00 50.64  ? 349 THR A CA    1 
ATOM   2865 C  C     . THR A 1 349 ? -25.162 26.068  -23.328 1.00 41.66  ? 349 THR A C     1 
ATOM   2866 O  O     . THR A 1 349 ? -24.543 27.131  -23.465 1.00 44.68  ? 349 THR A O     1 
ATOM   2867 C  CB    . THR A 1 349 ? -24.887 24.724  -21.231 1.00 50.33  ? 349 THR A CB    1 
ATOM   2868 O  OG1   . THR A 1 349 ? -25.490 24.389  -19.976 1.00 54.92  ? 349 THR A OG1   1 
ATOM   2869 C  CG2   . THR A 1 349 ? -23.529 25.352  -20.972 1.00 47.03  ? 349 THR A CG2   1 
ATOM   2870 N  N     . GLY A 1 350 ? -25.321 25.202  -24.331 1.00 46.15  ? 350 GLY A N     1 
ATOM   2871 C  CA    . GLY A 1 350 ? -24.750 25.484  -25.638 1.00 40.27  ? 350 GLY A CA    1 
ATOM   2872 C  C     . GLY A 1 350 ? -25.305 26.748  -26.264 1.00 46.82  ? 350 GLY A C     1 
ATOM   2873 O  O     . GLY A 1 350 ? -24.564 27.534  -26.857 1.00 50.39  ? 350 GLY A O     1 
ATOM   2874 N  N     . ASN A 1 351 ? -26.615 26.968  -26.134 1.00 48.16  ? 351 ASN A N     1 
ATOM   2875 C  CA    . ASN A 1 351 ? -27.212 28.176  -26.695 1.00 47.95  ? 351 ASN A CA    1 
ATOM   2876 C  C     . ASN A 1 351 ? -26.777 29.417  -25.923 1.00 41.50  ? 351 ASN A C     1 
ATOM   2877 O  O     . ASN A 1 351 ? -26.579 30.484  -26.516 1.00 49.65  ? 351 ASN A O     1 
ATOM   2878 C  CB    . ASN A 1 351 ? -28.733 28.050  -26.712 1.00 56.76  ? 351 ASN A CB    1 
ATOM   2879 C  CG    . ASN A 1 351 ? -29.223 27.086  -27.770 1.00 67.69  ? 351 ASN A CG    1 
ATOM   2880 O  OD1   . ASN A 1 351 ? -28.436 26.556  -28.556 1.00 69.64  ? 351 ASN A OD1   1 
ATOM   2881 N  ND2   . ASN A 1 351 ? -30.530 26.849  -27.796 1.00 65.81  ? 351 ASN A ND2   1 
ATOM   2882 N  N     . LEU A 1 352 ? -26.627 29.298  -24.601 1.00 37.47  ? 352 LEU A N     1 
ATOM   2883 C  CA    . LEU A 1 352 ? -26.043 30.384  -23.818 1.00 46.53  ? 352 LEU A CA    1 
ATOM   2884 C  C     . LEU A 1 352 ? -24.660 30.749  -24.343 1.00 49.33  ? 352 LEU A C     1 
ATOM   2885 O  O     . LEU A 1 352 ? -24.346 31.930  -24.551 1.00 48.97  ? 352 LEU A O     1 
ATOM   2886 C  CB    . LEU A 1 352 ? -25.961 29.985  -22.343 1.00 42.81  ? 352 LEU A CB    1 
ATOM   2887 C  CG    . LEU A 1 352 ? -27.073 30.397  -21.377 1.00 44.04  ? 352 LEU A CG    1 
ATOM   2888 C  CD1   . LEU A 1 352 ? -28.424 29.947  -21.874 1.00 58.63  ? 352 LEU A CD1   1 
ATOM   2889 C  CD2   . LEU A 1 352 ? -26.799 29.825  -19.994 1.00 46.07  ? 352 LEU A CD2   1 
ATOM   2890 N  N     . VAL A 1 353 ? -23.817 29.737  -24.561 1.00 43.55  ? 353 VAL A N     1 
ATOM   2891 C  CA    . VAL A 1 353 ? -22.471 29.983  -25.065 1.00 41.75  ? 353 VAL A CA    1 
ATOM   2892 C  C     . VAL A 1 353 ? -22.529 30.619  -26.446 1.00 48.52  ? 353 VAL A C     1 
ATOM   2893 O  O     . VAL A 1 353 ? -21.766 31.543  -26.751 1.00 47.17  ? 353 VAL A O     1 
ATOM   2894 C  CB    . VAL A 1 353 ? -21.661 28.674  -25.075 1.00 42.01  ? 353 VAL A CB    1 
ATOM   2895 C  CG1   . VAL A 1 353 ? -20.395 28.830  -25.904 1.00 46.20  ? 353 VAL A CG1   1 
ATOM   2896 C  CG2   . VAL A 1 353 ? -21.322 28.270  -23.661 1.00 43.52  ? 353 VAL A CG2   1 
ATOM   2897 N  N     . GLU A 1 354 ? -23.439 30.146  -27.300 1.00 41.69  ? 354 GLU A N     1 
ATOM   2898 C  CA    . GLU A 1 354 ? -23.517 30.683  -28.653 1.00 48.94  ? 354 GLU A CA    1 
ATOM   2899 C  C     . GLU A 1 354 ? -23.959 32.141  -28.646 1.00 54.14  ? 354 GLU A C     1 
ATOM   2900 O  O     . GLU A 1 354 ? -23.446 32.949  -29.425 1.00 46.43  ? 354 GLU A O     1 
ATOM   2901 C  CB    . GLU A 1 354 ? -24.452 29.829  -29.508 1.00 50.95  ? 354 GLU A CB    1 
ATOM   2902 C  CG    . GLU A 1 354 ? -23.763 28.618  -30.119 1.00 57.52  ? 354 GLU A CG    1 
ATOM   2903 C  CD    . GLU A 1 354 ? -23.955 28.530  -31.619 1.00 66.14  ? 354 GLU A CD    1 
ATOM   2904 O  OE1   . GLU A 1 354 ? -24.659 29.397  -32.179 1.00 80.50  ? 354 GLU A OE1   1 
ATOM   2905 O  OE2   . GLU A 1 354 ? -23.390 27.605  -32.240 1.00 53.19  ? 354 GLU A OE2   1 
ATOM   2906 N  N     A TRP A 1 355 ? -24.903 32.496  -27.772 0.51 54.56  ? 355 TRP A N     1 
ATOM   2907 N  N     B TRP A 1 355 ? -24.898 32.500  -27.769 0.49 55.34  ? 355 TRP A N     1 
ATOM   2908 C  CA    A TRP A 1 355 ? -25.331 33.889  -27.672 0.51 52.59  ? 355 TRP A CA    1 
ATOM   2909 C  CA    B TRP A 1 355 ? -25.322 33.895  -27.686 0.49 51.86  ? 355 TRP A CA    1 
ATOM   2910 C  C     A TRP A 1 355 ? -24.209 34.773  -27.139 0.51 55.56  ? 355 TRP A C     1 
ATOM   2911 C  C     B TRP A 1 355 ? -24.207 34.779  -27.137 0.49 56.19  ? 355 TRP A C     1 
ATOM   2912 O  O     A TRP A 1 355 ? -23.987 35.882  -27.646 0.51 62.10  ? 355 TRP A O     1 
ATOM   2913 O  O     B TRP A 1 355 ? -23.986 35.892  -27.635 0.49 58.40  ? 355 TRP A O     1 
ATOM   2914 C  CB    A TRP A 1 355 ? -26.571 33.994  -26.784 0.51 54.59  ? 355 TRP A CB    1 
ATOM   2915 C  CB    B TRP A 1 355 ? -26.582 34.012  -26.829 0.49 52.50  ? 355 TRP A CB    1 
ATOM   2916 C  CG    A TRP A 1 355 ? -27.832 33.552  -27.464 0.51 56.23  ? 355 TRP A CG    1 
ATOM   2917 C  CG    B TRP A 1 355 ? -27.823 33.604  -27.559 0.49 60.01  ? 355 TRP A CG    1 
ATOM   2918 C  CD1   A TRP A 1 355 ? -28.095 33.588  -28.803 0.51 58.02  ? 355 TRP A CD1   1 
ATOM   2919 C  CD1   B TRP A 1 355 ? -28.654 32.567  -27.248 0.49 56.66  ? 355 TRP A CD1   1 
ATOM   2920 C  CD2   A TRP A 1 355 ? -29.001 33.004  -26.840 0.51 57.19  ? 355 TRP A CD2   1 
ATOM   2921 C  CD2   B TRP A 1 355 ? -28.369 34.217  -28.733 0.49 56.93  ? 355 TRP A CD2   1 
ATOM   2922 N  NE1   A TRP A 1 355 ? -29.355 33.099  -29.051 0.51 55.32  ? 355 TRP A NE1   1 
ATOM   2923 N  NE1   B TRP A 1 355 ? -29.686 32.499  -28.153 0.49 55.34  ? 355 TRP A NE1   1 
ATOM   2924 C  CE2   A TRP A 1 355 ? -29.932 32.734  -27.863 0.51 55.63  ? 355 TRP A CE2   1 
ATOM   2925 C  CE2   B TRP A 1 355 ? -29.534 33.502  -29.075 0.49 55.65  ? 355 TRP A CE2   1 
ATOM   2926 C  CE3   A TRP A 1 355 ? -29.350 32.717  -25.517 0.51 56.54  ? 355 TRP A CE3   1 
ATOM   2927 C  CE3   B TRP A 1 355 ? -27.988 35.304  -29.527 0.49 48.93  ? 355 TRP A CE3   1 
ATOM   2928 C  CZ2   A TRP A 1 355 ? -31.189 32.190  -27.604 0.51 56.02  ? 355 TRP A CZ2   1 
ATOM   2929 C  CZ2   B TRP A 1 355 ? -30.319 33.836  -30.175 0.49 50.88  ? 355 TRP A CZ2   1 
ATOM   2930 C  CZ3   A TRP A 1 355 ? -30.599 32.178  -25.262 0.51 54.50  ? 355 TRP A CZ3   1 
ATOM   2931 C  CZ3   B TRP A 1 355 ? -28.769 35.634  -30.618 0.49 50.48  ? 355 TRP A CZ3   1 
ATOM   2932 C  CH2   A TRP A 1 355 ? -31.503 31.920  -26.301 0.51 51.79  ? 355 TRP A CH2   1 
ATOM   2933 C  CH2   B TRP A 1 355 ? -29.921 34.903  -30.932 0.49 51.52  ? 355 TRP A CH2   1 
ATOM   2934 N  N     . PHE A 1 356 ? -23.492 34.299  -26.115 1.00 46.71  ? 356 PHE A N     1 
ATOM   2935 C  CA    . PHE A 1 356 ? -22.350 35.047  -25.594 1.00 52.23  ? 356 PHE A CA    1 
ATOM   2936 C  C     . PHE A 1 356 ? -21.294 35.261  -26.675 1.00 46.56  ? 356 PHE A C     1 
ATOM   2937 O  O     . PHE A 1 356 ? -20.776 36.374  -26.845 1.00 50.07  ? 356 PHE A O     1 
ATOM   2938 C  CB    . PHE A 1 356 ? -21.763 34.301  -24.394 1.00 47.60  ? 356 PHE A CB    1 
ATOM   2939 C  CG    . PHE A 1 356 ? -20.532 34.936  -23.814 1.00 52.26  ? 356 PHE A CG    1 
ATOM   2940 C  CD1   . PHE A 1 356 ? -20.629 36.020  -22.956 1.00 50.72  ? 356 PHE A CD1   1 
ATOM   2941 C  CD2   . PHE A 1 356 ? -19.275 34.435  -24.111 1.00 50.44  ? 356 PHE A CD2   1 
ATOM   2942 C  CE1   . PHE A 1 356 ? -19.495 36.598  -22.415 1.00 46.91  ? 356 PHE A CE1   1 
ATOM   2943 C  CE2   . PHE A 1 356 ? -18.137 35.009  -23.575 1.00 46.19  ? 356 PHE A CE2   1 
ATOM   2944 C  CZ    . PHE A 1 356 ? -18.248 36.091  -22.726 1.00 43.93  ? 356 PHE A CZ    1 
ATOM   2945 N  N     . LEU A 1 357 ? -20.990 34.209  -27.439 1.00 48.04  ? 357 LEU A N     1 
ATOM   2946 C  CA    . LEU A 1 357 ? -19.986 34.307  -28.491 1.00 48.29  ? 357 LEU A CA    1 
ATOM   2947 C  C     . LEU A 1 357 ? -20.456 35.211  -29.622 1.00 50.08  ? 357 LEU A C     1 
ATOM   2948 O  O     . LEU A 1 357 ? -19.655 35.946  -30.203 1.00 42.60  ? 357 LEU A O     1 
ATOM   2949 C  CB    . LEU A 1 357 ? -19.649 32.914  -29.023 1.00 44.13  ? 357 LEU A CB    1 
ATOM   2950 C  CG    . LEU A 1 357 ? -18.868 31.981  -28.093 1.00 45.15  ? 357 LEU A CG    1 
ATOM   2951 C  CD1   . LEU A 1 357 ? -18.694 30.612  -28.731 1.00 44.22  ? 357 LEU A CD1   1 
ATOM   2952 C  CD2   . LEU A 1 357 ? -17.521 32.578  -27.729 1.00 42.08  ? 357 LEU A CD2   1 
ATOM   2953 N  N     . LEU A 1 358 ? -21.751 35.178  -29.947 1.00 46.52  ? 358 LEU A N     1 
ATOM   2954 C  CA    . LEU A 1 358 ? -22.273 36.049  -30.993 1.00 45.55  ? 358 LEU A CA    1 
ATOM   2955 C  C     . LEU A 1 358 ? -22.189 37.511  -30.580 1.00 42.55  ? 358 LEU A C     1 
ATOM   2956 O  O     . LEU A 1 358 ? -21.801 38.370  -31.384 1.00 35.82  ? 358 LEU A O     1 
ATOM   2957 C  CB    . LEU A 1 358 ? -23.715 35.660  -31.320 1.00 47.46  ? 358 LEU A CB    1 
ATOM   2958 C  CG    . LEU A 1 358 ? -23.926 34.785  -32.556 1.00 55.30  ? 358 LEU A CG    1 
ATOM   2959 C  CD1   . LEU A 1 358 ? -25.357 34.278  -32.606 1.00 62.87  ? 358 LEU A CD1   1 
ATOM   2960 C  CD2   . LEU A 1 358 ? -23.593 35.561  -33.818 1.00 68.09  ? 358 LEU A CD2   1 
ATOM   2961 N  N     . ARG A 1 359 ? -22.541 37.812  -29.328 1.00 38.22  ? 359 ARG A N     1 
ATOM   2962 C  CA    . ARG A 1 359 ? -22.418 39.182  -28.840 1.00 40.50  ? 359 ARG A CA    1 
ATOM   2963 C  C     . ARG A 1 359 ? -20.962 39.639  -28.874 1.00 50.13  ? 359 ARG A C     1 
ATOM   2964 O  O     . ARG A 1 359 ? -20.649 40.738  -29.356 1.00 45.02  ? 359 ARG A O     1 
ATOM   2965 C  CB    . ARG A 1 359 ? -23.001 39.280  -27.429 1.00 37.06  ? 359 ARG A CB    1 
ATOM   2966 C  CG    . ARG A 1 359 ? -22.374 40.339  -26.549 1.00 54.17  ? 359 ARG A CG    1 
ATOM   2967 C  CD    . ARG A 1 359 ? -23.263 41.561  -26.450 1.00 47.14  ? 359 ARG A CD    1 
ATOM   2968 N  NE    . ARG A 1 359 ? -24.628 41.222  -26.065 1.00 48.48  ? 359 ARG A NE    1 
ATOM   2969 C  CZ    . ARG A 1 359 ? -25.596 42.113  -25.901 1.00 49.82  ? 359 ARG A CZ    1 
ATOM   2970 N  NH1   . ARG A 1 359 ? -25.378 43.407  -26.065 1.00 47.12  ? 359 ARG A NH1   1 
ATOM   2971 N  NH2   . ARG A 1 359 ? -26.813 41.696  -25.562 1.00 44.27  ? 359 ARG A NH2   1 
ATOM   2972 N  N     . LYS A 1 360 ? -20.049 38.787  -28.395 1.00 50.16  ? 360 LYS A N     1 
ATOM   2973 C  CA    . LYS A 1 360 ? -18.631 39.136  -28.416 1.00 46.35  ? 360 LYS A CA    1 
ATOM   2974 C  C     . LYS A 1 360 ? -18.128 39.337  -29.841 1.00 47.90  ? 360 LYS A C     1 
ATOM   2975 O  O     . LYS A 1 360 ? -17.338 40.251  -30.104 1.00 45.17  ? 360 LYS A O     1 
ATOM   2976 C  CB    . LYS A 1 360 ? -17.818 38.056  -27.706 1.00 43.12  ? 360 LYS A CB    1 
ATOM   2977 C  CG    . LYS A 1 360 ? -17.996 38.044  -26.196 1.00 46.56  ? 360 LYS A CG    1 
ATOM   2978 C  CD    . LYS A 1 360 ? -17.566 39.364  -25.578 1.00 44.73  ? 360 LYS A CD    1 
ATOM   2979 C  CE    . LYS A 1 360 ? -17.702 39.333  -24.064 1.00 48.15  ? 360 LYS A CE    1 
ATOM   2980 N  NZ    . LYS A 1 360 ? -17.526 40.680  -23.456 1.00 70.90  ? 360 LYS A NZ    1 
ATOM   2981 N  N     . ALA A 1 361 ? -18.583 38.500  -30.778 1.00 40.91  ? 361 ALA A N     1 
ATOM   2982 C  CA    . ALA A 1 361 ? -18.160 38.630  -32.167 1.00 48.91  ? 361 ALA A CA    1 
ATOM   2983 C  C     . ALA A 1 361 ? -18.654 39.935  -32.772 1.00 50.73  ? 361 ALA A C     1 
ATOM   2984 O  O     . ALA A 1 361 ? -17.925 40.589  -33.528 1.00 49.62  ? 361 ALA A O     1 
ATOM   2985 C  CB    . ALA A 1 361 ? -18.663 37.442  -32.985 1.00 38.84  ? 361 ALA A CB    1 
ATOM   2986 N  N     . TYR A 1 362 ? -19.891 40.326  -32.461 1.00 41.16  ? 362 TYR A N     1 
ATOM   2987 C  CA    . TYR A 1 362 ? -20.370 41.623  -32.924 1.00 47.39  ? 362 TYR A CA    1 
ATOM   2988 C  C     . TYR A 1 362 ? -19.535 42.750  -32.334 1.00 45.40  ? 362 TYR A C     1 
ATOM   2989 O  O     . TYR A 1 362 ? -19.251 43.744  -33.014 1.00 36.52  ? 362 TYR A O     1 
ATOM   2990 C  CB    . TYR A 1 362 ? -21.845 41.815  -32.572 1.00 41.17  ? 362 TYR A CB    1 
ATOM   2991 C  CG    . TYR A 1 362 ? -22.434 43.082  -33.159 1.00 44.09  ? 362 TYR A CG    1 
ATOM   2992 C  CD1   . TYR A 1 362 ? -22.934 43.102  -34.455 1.00 48.20  ? 362 TYR A CD1   1 
ATOM   2993 C  CD2   . TYR A 1 362 ? -22.479 44.259  -32.421 1.00 41.21  ? 362 TYR A CD2   1 
ATOM   2994 C  CE1   . TYR A 1 362 ? -23.470 44.258  -34.998 1.00 48.04  ? 362 TYR A CE1   1 
ATOM   2995 C  CE2   . TYR A 1 362 ? -23.010 45.419  -32.955 1.00 45.20  ? 362 TYR A CE2   1 
ATOM   2996 C  CZ    . TYR A 1 362 ? -23.505 45.412  -34.243 1.00 51.14  ? 362 TYR A CZ    1 
ATOM   2997 O  OH    . TYR A 1 362 ? -24.037 46.565  -34.777 1.00 61.57  ? 362 TYR A OH    1 
ATOM   2998 N  N     . GLU A 1 363 ? -19.127 42.611  -31.070 1.00 46.49  ? 363 GLU A N     1 
ATOM   2999 C  CA    . GLU A 1 363 ? -18.324 43.658  -30.447 1.00 45.90  ? 363 GLU A CA    1 
ATOM   3000 C  C     . GLU A 1 363 ? -16.991 43.853  -31.161 1.00 44.82  ? 363 GLU A C     1 
ATOM   3001 O  O     . GLU A 1 363 ? -16.486 44.979  -31.223 1.00 43.82  ? 363 GLU A O     1 
ATOM   3002 C  CB    . GLU A 1 363 ? -18.095 43.341  -28.970 1.00 49.27  ? 363 GLU A CB    1 
ATOM   3003 C  CG    . GLU A 1 363 ? -19.360 43.392  -28.128 1.00 50.17  ? 363 GLU A CG    1 
ATOM   3004 C  CD    . GLU A 1 363 ? -19.103 43.052  -26.675 1.00 59.10  ? 363 GLU A CD    1 
ATOM   3005 O  OE1   . GLU A 1 363 ? -17.940 42.750  -26.333 1.00 63.92  ? 363 GLU A OE1   1 
ATOM   3006 O  OE2   . GLU A 1 363 ? -20.063 43.081  -25.878 1.00 49.82  ? 363 GLU A OE2   1 
ATOM   3007 N  N     . ARG A 1 364 ? -16.411 42.784  -31.711 1.00 47.94  ? 364 ARG A N     1 
ATOM   3008 C  CA    . ARG A 1 364 ? -15.114 42.859  -32.373 1.00 50.47  ? 364 ARG A CA    1 
ATOM   3009 C  C     . ARG A 1 364 ? -15.219 42.884  -33.894 1.00 52.98  ? 364 ARG A C     1 
ATOM   3010 O  O     . ARG A 1 364 ? -14.205 42.693  -34.573 1.00 59.88  ? 364 ARG A O     1 
ATOM   3011 C  CB    . ARG A 1 364 ? -14.224 41.689  -31.948 1.00 46.25  ? 364 ARG A CB    1 
ATOM   3012 C  CG    . ARG A 1 364 ? -14.432 41.206  -30.525 1.00 54.82  ? 364 ARG A CG    1 
ATOM   3013 C  CD    . ARG A 1 364 ? -13.863 42.176  -29.507 1.00 70.11  ? 364 ARG A CD    1 
ATOM   3014 N  NE    . ARG A 1 364 ? -14.204 41.783  -28.145 1.00 87.27  ? 364 ARG A NE    1 
ATOM   3015 C  CZ    . ARG A 1 364 ? -13.516 40.908  -27.424 1.00 86.48  ? 364 ARG A CZ    1 
ATOM   3016 N  NH1   . ARG A 1 364 ? -12.442 40.304  -27.908 1.00 67.94  ? 364 ARG A NH1   1 
ATOM   3017 N  NH2   . ARG A 1 364 ? -13.915 40.633  -26.185 1.00 70.79  ? 364 ARG A NH2   1 
ATOM   3018 N  N     . ASN A 1 365 ? -16.416 43.110  -34.441 1.00 51.32  ? 365 ASN A N     1 
ATOM   3019 C  CA    . ASN A 1 365 ? -16.636 43.129  -35.891 1.00 54.10  ? 365 ASN A CA    1 
ATOM   3020 C  C     . ASN A 1 365 ? -16.169 41.830  -36.545 1.00 54.31  ? 365 ASN A C     1 
ATOM   3021 O  O     . ASN A 1 365 ? -15.648 41.825  -37.662 1.00 49.49  ? 365 ASN A O     1 
ATOM   3022 C  CB    . ASN A 1 365 ? -15.962 44.339  -36.543 1.00 54.56  ? 365 ASN A CB    1 
ATOM   3023 C  CG    . ASN A 1 365 ? -16.741 44.869  -37.730 1.00 66.63  ? 365 ASN A CG    1 
ATOM   3024 O  OD1   . ASN A 1 365 ? -16.698 44.301  -38.821 1.00 66.65  ? 365 ASN A OD1   1 
ATOM   3025 N  ND2   . ASN A 1 365 ? -17.464 45.965  -37.522 1.00 80.08  ? 365 ASN A ND2   1 
ATOM   3026 N  N     . GLU A 1 366 ? -16.359 40.716  -35.844 1.00 53.52  ? 366 GLU A N     1 
ATOM   3027 C  CA    . GLU A 1 366 ? -15.990 39.400  -36.346 1.00 52.27  ? 366 GLU A CA    1 
ATOM   3028 C  C     . GLU A 1 366 ? -17.212 38.755  -36.986 1.00 52.73  ? 366 GLU A C     1 
ATOM   3029 O  O     . GLU A 1 366 ? -18.249 38.596  -36.333 1.00 50.14  ? 366 GLU A O     1 
ATOM   3030 C  CB    . GLU A 1 366 ? -15.445 38.523  -35.220 1.00 51.15  ? 366 GLU A CB    1 
ATOM   3031 C  CG    . GLU A 1 366 ? -14.195 39.072  -34.549 1.00 62.50  ? 366 GLU A CG    1 
ATOM   3032 C  CD    . GLU A 1 366 ? -12.921 38.455  -35.092 1.00 71.14  ? 366 GLU A CD    1 
ATOM   3033 O  OE1   . GLU A 1 366 ? -12.971 37.841  -36.178 1.00 71.55  ? 366 GLU A OE1   1 
ATOM   3034 O  OE2   . GLU A 1 366 ? -11.869 38.584  -34.432 1.00 84.58  ? 366 GLU A OE2   1 
ATOM   3035 N  N     . LEU A 1 367 ? -17.091 38.394  -38.260 1.00 53.65  ? 367 LEU A N     1 
ATOM   3036 C  CA    . LEU A 1 367 ? -18.179 37.726  -38.961 1.00 48.09  ? 367 LEU A CA    1 
ATOM   3037 C  C     . LEU A 1 367 ? -18.415 36.351  -38.349 1.00 51.58  ? 367 LEU A C     1 
ATOM   3038 O  O     . LEU A 1 367 ? -17.499 35.525  -38.289 1.00 47.07  ? 367 LEU A O     1 
ATOM   3039 C  CB    . LEU A 1 367 ? -17.854 37.607  -40.447 1.00 54.27  ? 367 LEU A CB    1 
ATOM   3040 C  CG    . LEU A 1 367 ? -18.997 37.156  -41.355 1.00 57.62  ? 367 LEU A CG    1 
ATOM   3041 C  CD1   . LEU A 1 367 ? -20.109 38.190  -41.358 1.00 51.39  ? 367 LEU A CD1   1 
ATOM   3042 C  CD2   . LEU A 1 367 ? -18.486 36.906  -42.764 1.00 59.26  ? 367 LEU A CD2   1 
ATOM   3043 N  N     . ALA A 1 368 ? -19.636 36.105  -37.897 1.00 53.83  ? 368 ALA A N     1 
ATOM   3044 C  CA    . ALA A 1 368 ? -19.938 34.849  -37.220 1.00 48.01  ? 368 ALA A CA    1 
ATOM   3045 C  C     . ALA A 1 368 ? -19.966 33.701  -38.222 1.00 47.62  ? 368 ALA A C     1 
ATOM   3046 O  O     . ALA A 1 368 ? -20.622 33.810  -39.265 1.00 52.34  ? 368 ALA A O     1 
ATOM   3047 C  CB    . ALA A 1 368 ? -21.274 34.943  -36.492 1.00 52.81  ? 368 ALA A CB    1 
ATOM   3048 N  N     . PRO A 1 369 ? -19.273 32.597  -37.953 1.00 48.86  ? 369 PRO A N     1 
ATOM   3049 C  CA    . PRO A 1 369 ? -19.387 31.423  -38.824 1.00 51.27  ? 369 PRO A CA    1 
ATOM   3050 C  C     . PRO A 1 369 ? -20.781 30.821  -38.750 1.00 51.75  ? 369 PRO A C     1 
ATOM   3051 O  O     . PRO A 1 369 ? -21.541 31.050  -37.807 1.00 49.57  ? 369 PRO A O     1 
ATOM   3052 C  CB    . PRO A 1 369 ? -18.335 30.453  -38.271 1.00 49.86  ? 369 PRO A CB    1 
ATOM   3053 C  CG    . PRO A 1 369 ? -17.481 31.266  -37.342 1.00 54.01  ? 369 PRO A CG    1 
ATOM   3054 C  CD    . PRO A 1 369 ? -18.342 32.375  -36.837 1.00 50.38  ? 369 PRO A CD    1 
ATOM   3055 N  N     . ASN A 1 370 ? -21.111 30.038  -39.769 1.00 51.98  ? 370 ASN A N     1 
ATOM   3056 C  CA    . ASN A 1 370 ? -22.437 29.450  -39.869 1.00 52.34  ? 370 ASN A CA    1 
ATOM   3057 C  C     . ASN A 1 370 ? -22.489 28.094  -39.175 1.00 54.21  ? 370 ASN A C     1 
ATOM   3058 O  O     . ASN A 1 370 ? -21.472 27.425  -38.978 1.00 52.15  ? 370 ASN A O     1 
ATOM   3059 C  CB    . ASN A 1 370 ? -22.854 29.300  -41.331 1.00 50.08  ? 370 ASN A CB    1 
ATOM   3060 C  CG    . ASN A 1 370 ? -23.057 30.634  -42.017 1.00 56.22  ? 370 ASN A CG    1 
ATOM   3061 O  OD1   . ASN A 1 370 ? -23.561 31.584  -41.415 1.00 58.77  ? 370 ASN A OD1   1 
ATOM   3062 N  ND2   . ASN A 1 370 ? -22.672 30.712  -43.285 1.00 60.95  ? 370 ASN A ND2   1 
ATOM   3063 N  N     . LYS A 1 371 ? -23.702 27.696  -38.803 1.00 61.57  ? 371 LYS A N     1 
ATOM   3064 C  CA    . LYS A 1 371 ? -23.915 26.364  -38.269 1.00 56.33  ? 371 LYS A CA    1 
ATOM   3065 C  C     . LYS A 1 371 ? -23.681 25.327  -39.368 1.00 52.66  ? 371 LYS A C     1 
ATOM   3066 O  O     . LYS A 1 371 ? -23.884 25.608  -40.552 1.00 54.98  ? 371 LYS A O     1 
ATOM   3067 C  CB    . LYS A 1 371 ? -25.328 26.233  -37.709 1.00 50.98  ? 371 LYS A CB    1 
ATOM   3068 C  CG    . LYS A 1 371 ? -25.571 27.062  -36.456 1.00 57.25  ? 371 LYS A CG    1 
ATOM   3069 C  CD    . LYS A 1 371 ? -26.080 26.205  -35.308 1.00 59.91  ? 371 LYS A CD    1 
ATOM   3070 C  CE    . LYS A 1 371 ? -26.399 27.054  -34.086 1.00 65.59  ? 371 LYS A CE    1 
ATOM   3071 N  NZ    . LYS A 1 371 ? -26.163 26.313  -32.815 1.00 67.22  ? 371 LYS A NZ    1 
ATOM   3072 N  N     . PRO A 1 372 ? -23.240 24.126  -39.006 1.00 54.73  ? 372 PRO A N     1 
ATOM   3073 C  CA    . PRO A 1 372 ? -22.887 23.138  -40.030 1.00 63.42  ? 372 PRO A CA    1 
ATOM   3074 C  C     . PRO A 1 372 ? -24.117 22.580  -40.725 1.00 71.92  ? 372 PRO A C     1 
ATOM   3075 O  O     . PRO A 1 372 ? -25.195 22.464  -40.137 1.00 66.70  ? 372 PRO A O     1 
ATOM   3076 C  CB    . PRO A 1 372 ? -22.170 22.045  -39.229 1.00 65.97  ? 372 PRO A CB    1 
ATOM   3077 C  CG    . PRO A 1 372 ? -22.756 22.161  -37.861 1.00 60.97  ? 372 PRO A CG    1 
ATOM   3078 C  CD    . PRO A 1 372 ? -22.970 23.631  -37.646 1.00 58.36  ? 372 PRO A CD    1 
ATOM   3079 N  N     . ASP A 1 373 ? -23.944 22.231  -41.998 1.00 78.47  ? 373 ASP A N     1 
ATOM   3080 C  CA    . ASP A 1 373 ? -24.970 21.482  -42.706 1.00 81.28  ? 373 ASP A CA    1 
ATOM   3081 C  C     . ASP A 1 373 ? -24.825 19.995  -42.386 1.00 86.22  ? 373 ASP A C     1 
ATOM   3082 O  O     . ASP A 1 373 ? -24.009 19.588  -41.554 1.00 81.74  ? 373 ASP A O     1 
ATOM   3083 C  CB    . ASP A 1 373 ? -24.911 21.770  -44.208 1.00 80.48  ? 373 ASP A CB    1 
ATOM   3084 C  CG    . ASP A 1 373 ? -23.639 21.260  -44.870 1.00 90.13  ? 373 ASP A CG    1 
ATOM   3085 O  OD1   . ASP A 1 373 ? -23.326 20.055  -44.768 1.00 94.38  ? 373 ASP A OD1   1 
ATOM   3086 O  OD2   . ASP A 1 373 ? -22.950 22.079  -45.512 1.00 95.26  ? 373 ASP A OD2   1 
ATOM   3087 N  N     . GLU A 1 374 ? -25.622 19.166  -43.063 1.00 91.09  ? 374 GLU A N     1 
ATOM   3088 C  CA    . GLU A 1 374 ? -25.672 17.747  -42.722 1.00 90.50  ? 374 GLU A CA    1 
ATOM   3089 C  C     . GLU A 1 374 ? -24.352 17.052  -43.033 1.00 85.53  ? 374 GLU A C     1 
ATOM   3090 O  O     . GLU A 1 374 ? -23.836 16.282  -42.214 1.00 87.84  ? 374 GLU A O     1 
ATOM   3091 C  CB    . GLU A 1 374 ? -26.833 17.074  -43.456 1.00 92.93  ? 374 GLU A CB    1 
ATOM   3092 C  CG    . GLU A 1 374 ? -28.167 17.815  -43.355 1.00 96.54  ? 374 GLU A CG    1 
ATOM   3093 C  CD    . GLU A 1 374 ? -28.401 18.449  -41.991 1.00 99.21  ? 374 GLU A CD    1 
ATOM   3094 O  OE1   . GLU A 1 374 ? -28.027 19.628  -41.804 1.00 97.44  ? 374 GLU A OE1   1 
ATOM   3095 O  OE2   . GLU A 1 374 ? -28.956 17.768  -41.104 1.00 97.86  ? 374 GLU A OE2   1 
ATOM   3096 N  N     . LYS A 1 375 ? -23.785 17.314  -44.213 1.00 86.77  ? 375 LYS A N     1 
ATOM   3097 C  CA    . LYS A 1 375 ? -22.503 16.709  -44.566 1.00 91.11  ? 375 LYS A CA    1 
ATOM   3098 C  C     . LYS A 1 375 ? -21.394 17.189  -43.637 1.00 90.32  ? 375 LYS A C     1 
ATOM   3099 O  O     . LYS A 1 375 ? -20.534 16.402  -43.218 1.00 90.60  ? 375 LYS A O     1 
ATOM   3100 C  CB    . LYS A 1 375 ? -22.156 17.030  -46.019 1.00 93.75  ? 375 LYS A CB    1 
ATOM   3101 C  CG    . LYS A 1 375 ? -23.299 16.808  -46.994 1.00 96.39  ? 375 LYS A CG    1 
ATOM   3102 C  CD    . LYS A 1 375 ? -22.806 16.192  -48.291 1.00 98.93  ? 375 LYS A CD    1 
ATOM   3103 C  CE    . LYS A 1 375 ? -22.766 17.225  -49.405 1.00 109.25 ? 375 LYS A CE    1 
ATOM   3104 N  NZ    . LYS A 1 375 ? -24.128 17.707  -49.770 1.00 111.72 ? 375 LYS A NZ    1 
ATOM   3105 N  N     . GLU A 1 376 ? -21.396 18.481  -43.305 1.00 89.41  ? 376 GLU A N     1 
ATOM   3106 C  CA    . GLU A 1 376 ? -20.368 19.002  -42.413 1.00 86.91  ? 376 GLU A CA    1 
ATOM   3107 C  C     . GLU A 1 376 ? -20.551 18.463  -41.001 1.00 80.99  ? 376 GLU A C     1 
ATOM   3108 O  O     . GLU A 1 376 ? -19.567 18.177  -40.310 1.00 87.33  ? 376 GLU A O     1 
ATOM   3109 C  CB    . GLU A 1 376 ? -20.380 20.531  -42.418 1.00 87.60  ? 376 GLU A CB    1 
ATOM   3110 C  CG    . GLU A 1 376 ? -20.424 21.208  -43.801 1.00 94.52  ? 376 GLU A CG    1 
ATOM   3111 C  CD    . GLU A 1 376 ? -19.755 20.425  -44.933 1.00 109.97 ? 376 GLU A CD    1 
ATOM   3112 O  OE1   . GLU A 1 376 ? -18.671 19.835  -44.729 1.00 117.58 ? 376 GLU A OE1   1 
ATOM   3113 O  OE2   . GLU A 1 376 ? -20.333 20.398  -46.041 1.00 101.46 ? 376 GLU A OE2   1 
ATOM   3114 N  N     . LEU A 1 377 ? -21.801 18.317  -40.557 1.00 81.79  ? 377 LEU A N     1 
ATOM   3115 C  CA    . LEU A 1 377 ? -22.059 17.625  -39.299 1.00 80.85  ? 377 LEU A CA    1 
ATOM   3116 C  C     . LEU A 1 377 ? -21.506 16.207  -39.339 1.00 89.22  ? 377 LEU A C     1 
ATOM   3117 O  O     . LEU A 1 377 ? -20.987 15.704  -38.336 1.00 87.11  ? 377 LEU A O     1 
ATOM   3118 C  CB    . LEU A 1 377 ? -23.560 17.604  -39.007 1.00 81.35  ? 377 LEU A CB    1 
ATOM   3119 C  CG    . LEU A 1 377 ? -24.116 18.678  -38.072 1.00 77.36  ? 377 LEU A CG    1 
ATOM   3120 C  CD1   . LEU A 1 377 ? -25.621 18.533  -37.930 1.00 77.00  ? 377 LEU A CD1   1 
ATOM   3121 C  CD2   . LEU A 1 377 ? -23.445 18.602  -36.722 1.00 74.33  ? 377 LEU A CD2   1 
ATOM   3122 N  N     . ALA A 1 378 ? -21.603 15.551  -40.499 1.00 85.61  ? 378 ALA A N     1 
ATOM   3123 C  CA    . ALA A 1 378 ? -21.066 14.201  -40.637 1.00 86.81  ? 378 ALA A CA    1 
ATOM   3124 C  C     . ALA A 1 378 ? -19.548 14.191  -40.507 1.00 90.53  ? 378 ALA A C     1 
ATOM   3125 O  O     . ALA A 1 378 ? -18.986 13.311  -39.843 1.00 104.74 ? 378 ALA A O     1 
ATOM   3126 C  CB    . ALA A 1 378 ? -21.495 13.601  -41.975 1.00 85.45  ? 378 ALA A CB    1 
ATOM   3127 N  N     . ARG A 1 379 ? -18.865 15.158  -41.128 1.00 88.92  ? 379 ARG A N     1 
ATOM   3128 C  CA    . ARG A 1 379 ? -17.410 15.211  -41.002 1.00 82.68  ? 379 ARG A CA    1 
ATOM   3129 C  C     . ARG A 1 379 ? -16.993 15.410  -39.550 1.00 83.07  ? 379 ARG A C     1 
ATOM   3130 O  O     . ARG A 1 379 ? -16.006 14.821  -39.092 1.00 90.74  ? 379 ARG A O     1 
ATOM   3131 C  CB    . ARG A 1 379 ? -16.830 16.324  -41.879 1.00 85.33  ? 379 ARG A CB    1 
ATOM   3132 C  CG    . ARG A 1 379 ? -15.485 16.858  -41.376 1.00 83.32  ? 379 ARG A CG    1 
ATOM   3133 C  CD    . ARG A 1 379 ? -15.085 18.180  -42.019 1.00 90.08  ? 379 ARG A CD    1 
ATOM   3134 N  NE    . ARG A 1 379 ? -15.598 19.325  -41.276 1.00 102.71 ? 379 ARG A NE    1 
ATOM   3135 C  CZ    . ARG A 1 379 ? -16.614 20.080  -41.672 1.00 95.55  ? 379 ARG A CZ    1 
ATOM   3136 N  NH1   . ARG A 1 379 ? -17.225 19.865  -42.825 1.00 96.66  ? 379 ARG A NH1   1 
ATOM   3137 N  NH2   . ARG A 1 379 ? -17.022 21.079  -40.894 1.00 84.15  ? 379 ARG A NH2   1 
ATOM   3138 N  N     . ARG A 1 380 ? -17.747 16.215  -38.804 1.00 78.57  ? 380 ARG A N     1 
ATOM   3139 C  CA    . ARG A 1 380 ? -17.415 16.525  -37.420 1.00 78.20  ? 380 ARG A CA    1 
ATOM   3140 C  C     . ARG A 1 380 ? -17.735 15.393  -36.453 1.00 80.98  ? 380 ARG A C     1 
ATOM   3141 O  O     . ARG A 1 380 ? -17.570 15.574  -35.242 1.00 81.31  ? 380 ARG A O     1 
ATOM   3142 C  CB    . ARG A 1 380 ? -18.146 17.796  -36.981 1.00 72.42  ? 380 ARG A CB    1 
ATOM   3143 C  CG    . ARG A 1 380 ? -17.869 18.997  -37.864 1.00 68.30  ? 380 ARG A CG    1 
ATOM   3144 C  CD    . ARG A 1 380 ? -18.645 20.216  -37.400 1.00 64.32  ? 380 ARG A CD    1 
ATOM   3145 N  NE    . ARG A 1 380 ? -18.267 21.416  -38.137 1.00 61.05  ? 380 ARG A NE    1 
ATOM   3146 C  CZ    . ARG A 1 380 ? -18.714 22.634  -37.865 1.00 57.81  ? 380 ARG A CZ    1 
ATOM   3147 N  NH1   . ARG A 1 380 ? -19.566 22.854  -36.875 1.00 54.41  ? 380 ARG A NH1   1 
ATOM   3148 N  NH2   . ARG A 1 380 ? -18.299 23.657  -38.606 1.00 57.52  ? 380 ARG A NH2   1 
ATOM   3149 N  N     . ARG A 1 381 ? -18.186 14.238  -36.943 1.00 85.85  ? 381 ARG A N     1 
ATOM   3150 C  CA    . ARG A 1 381 ? -18.403 13.090  -36.072 1.00 87.16  ? 381 ARG A CA    1 
ATOM   3151 C  C     . ARG A 1 381 ? -17.083 12.375  -35.819 1.00 95.09  ? 381 ARG A C     1 
ATOM   3152 O  O     . ARG A 1 381 ? -16.971 11.165  -36.042 1.00 96.66  ? 381 ARG A O     1 
ATOM   3153 C  CB    . ARG A 1 381 ? -19.427 12.132  -36.682 1.00 86.07  ? 381 ARG A CB    1 
ATOM   3154 C  CG    . ARG A 1 381 ? -20.726 12.800  -37.083 1.00 89.25  ? 381 ARG A CG    1 
ATOM   3155 C  CD    . ARG A 1 381 ? -21.703 12.869  -35.915 1.00 94.24  ? 381 ARG A CD    1 
ATOM   3156 N  NE    . ARG A 1 381 ? -22.868 13.713  -36.174 1.00 107.96 ? 381 ARG A NE    1 
ATOM   3157 C  CZ    . ARG A 1 381 ? -23.717 13.571  -37.185 1.00 103.08 ? 381 ARG A CZ    1 
ATOM   3158 N  NH1   . ARG A 1 381 ? -23.615 12.571  -38.048 1.00 97.22  ? 381 ARG A NH1   1 
ATOM   3159 N  NH2   . ARG A 1 381 ? -24.708 14.447  -37.326 1.00 89.43  ? 381 ARG A NH2   1 
ATOM   3160 N  N     . GLN A 1 382 ? -16.081 13.117  -35.358 1.00 111.80 ? 382 GLN A N     1 
ATOM   3161 C  CA    . GLN A 1 382 ? -14.753 12.586  -35.110 1.00 107.00 ? 382 GLN A CA    1 
ATOM   3162 C  C     . GLN A 1 382 ? -14.605 12.210  -33.639 1.00 103.79 ? 382 GLN A C     1 
ATOM   3163 O  O     . GLN A 1 382 ? -15.551 12.278  -32.850 1.00 106.00 ? 382 GLN A O     1 
ATOM   3164 C  CB    . GLN A 1 382 ? -13.686 13.600  -35.527 1.00 103.29 ? 382 GLN A CB    1 
ATOM   3165 C  CG    . GLN A 1 382 ? -13.491 13.710  -37.027 1.00 110.09 ? 382 GLN A CG    1 
ATOM   3166 C  CD    . GLN A 1 382 ? -12.728 12.534  -37.600 1.00 127.92 ? 382 GLN A CD    1 
ATOM   3167 O  OE1   . GLN A 1 382 ? -13.236 11.806  -38.453 1.00 129.50 ? 382 GLN A OE1   1 
ATOM   3168 N  NE2   . GLN A 1 382 ? -11.498 12.344  -37.136 1.00 123.25 ? 382 GLN A NE2   1 
ATOM   3169 N  N     . LYS A 1 383 ? -13.391 11.815  -33.268 1.00 97.06  ? 383 LYS A N     1 
ATOM   3170 C  CA    . LYS A 1 383 ? -13.095 11.391  -31.908 1.00 90.53  ? 383 LYS A CA    1 
ATOM   3171 C  C     . LYS A 1 383 ? -11.688 11.837  -31.548 1.00 87.58  ? 383 LYS A C     1 
ATOM   3172 O  O     . LYS A 1 383 ? -10.743 11.577  -32.299 1.00 99.11  ? 383 LYS A O     1 
ATOM   3173 C  CB    . LYS A 1 383 ? -13.220 9.870   -31.766 1.00 94.94  ? 383 LYS A CB    1 
ATOM   3174 C  CG    . LYS A 1 383 ? -12.834 9.109   -33.026 1.00 98.22  ? 383 LYS A CG    1 
ATOM   3175 C  CD    . LYS A 1 383 ? -13.359 7.682   -33.007 1.00 99.39  ? 383 LYS A CD    1 
ATOM   3176 C  CE    . LYS A 1 383 ? -12.950 6.959   -31.732 1.00 101.73 ? 383 LYS A CE    1 
ATOM   3177 N  NZ    . LYS A 1 383 ? -11.476 6.754   -31.652 1.00 100.64 ? 383 LYS A NZ    1 
ATOM   3178 N  N     . TYR A 1 384 ? -11.551 12.511  -30.410 1.00 81.97  ? 384 TYR A N     1 
ATOM   3179 C  CA    . TYR A 1 384 ? -10.252 12.935  -29.915 1.00 73.01  ? 384 TYR A CA    1 
ATOM   3180 C  C     . TYR A 1 384 ? -10.107 12.529  -28.456 1.00 71.45  ? 384 TYR A C     1 
ATOM   3181 O  O     . TYR A 1 384 ? -11.092 12.352  -27.735 1.00 69.24  ? 384 TYR A O     1 
ATOM   3182 C  CB    . TYR A 1 384 ? -10.043 14.451  -30.085 1.00 70.28  ? 384 TYR A CB    1 
ATOM   3183 C  CG    . TYR A 1 384 ? -10.995 15.341  -29.309 1.00 63.80  ? 384 TYR A CG    1 
ATOM   3184 C  CD1   . TYR A 1 384 ? -12.270 15.620  -29.789 1.00 59.48  ? 384 TYR A CD1   1 
ATOM   3185 C  CD2   . TYR A 1 384 ? -10.605 15.930  -28.113 1.00 62.66  ? 384 TYR A CD2   1 
ATOM   3186 C  CE1   . TYR A 1 384 ? -13.134 16.446  -29.088 1.00 59.16  ? 384 TYR A CE1   1 
ATOM   3187 C  CE2   . TYR A 1 384 ? -11.460 16.754  -27.406 1.00 61.96  ? 384 TYR A CE2   1 
ATOM   3188 C  CZ    . TYR A 1 384 ? -12.723 17.011  -27.897 1.00 64.87  ? 384 TYR A CZ    1 
ATOM   3189 O  OH    . TYR A 1 384 ? -13.574 17.834  -27.191 1.00 51.92  ? 384 TYR A OH    1 
ATOM   3190 N  N     . GLU A 1 385 ? -8.856  12.369  -28.032 1.00 79.58  ? 385 GLU A N     1 
ATOM   3191 C  CA    . GLU A 1 385 ? -8.578  11.918  -26.678 1.00 85.48  ? 385 GLU A CA    1 
ATOM   3192 C  C     . GLU A 1 385 ? -8.966  12.991  -25.664 1.00 82.87  ? 385 GLU A C     1 
ATOM   3193 O  O     . GLU A 1 385 ? -9.170  14.160  -25.998 1.00 74.17  ? 385 GLU A O     1 
ATOM   3194 C  CB    . GLU A 1 385 ? -7.101  11.553  -26.526 1.00 78.86  ? 385 GLU A CB    1 
ATOM   3195 C  CG    . GLU A 1 385 ? -6.862  10.259  -25.767 1.00 81.16  ? 385 GLU A CG    1 
ATOM   3196 C  CD    . GLU A 1 385 ? -5.486  10.197  -25.137 1.00 85.24  ? 385 GLU A CD    1 
ATOM   3197 O  OE1   . GLU A 1 385 ? -4.486  10.281  -25.882 1.00 88.97  ? 385 GLU A OE1   1 
ATOM   3198 O  OE2   . GLU A 1 385 ? -5.404  10.066  -23.898 1.00 82.28  ? 385 GLU A OE2   1 
ATOM   3199 N  N     . GLY A 1 386 ? -9.078  12.574  -24.407 1.00 81.11  ? 386 GLY A N     1 
ATOM   3200 C  CA    . GLY A 1 386 ? -9.475  13.485  -23.353 1.00 68.91  ? 386 GLY A CA    1 
ATOM   3201 C  C     . GLY A 1 386 ? -8.416  13.659  -22.286 1.00 70.76  ? 386 GLY A C     1 
ATOM   3202 O  O     . GLY A 1 386 ? -7.216  13.596  -22.573 1.00 66.31  ? 386 GLY A O     1 
ATOM   3203 N  N     . GLY A 1 387 ? -8.849  13.888  -21.049 1.00 61.57  ? 387 GLY A N     1 
ATOM   3204 C  CA    . GLY A 1 387 ? -7.910  14.067  -19.966 1.00 60.54  ? 387 GLY A CA    1 
ATOM   3205 C  C     . GLY A 1 387 ? -7.298  12.762  -19.496 1.00 70.97  ? 387 GLY A C     1 
ATOM   3206 O  O     . GLY A 1 387 ? -7.866  11.680  -19.645 1.00 74.81  ? 387 GLY A O     1 
ATOM   3207 N  N     . TYR A 1 388 ? -6.106  12.878  -18.919 1.00 67.23  ? 388 TYR A N     1 
ATOM   3208 C  CA    . TYR A 1 388 ? -5.415  11.725  -18.363 1.00 68.54  ? 388 TYR A CA    1 
ATOM   3209 C  C     . TYR A 1 388 ? -6.049  11.326  -17.038 1.00 63.95  ? 388 TYR A C     1 
ATOM   3210 O  O     . TYR A 1 388 ? -6.483  12.178  -16.260 1.00 65.45  ? 388 TYR A O     1 
ATOM   3211 C  CB    . TYR A 1 388 ? -3.931  12.037  -18.166 1.00 67.83  ? 388 TYR A CB    1 
ATOM   3212 C  CG    . TYR A 1 388 ? -3.197  11.059  -17.272 1.00 77.77  ? 388 TYR A CG    1 
ATOM   3213 C  CD1   . TYR A 1 388 ? -2.809  11.417  -15.986 1.00 70.42  ? 388 TYR A CD1   1 
ATOM   3214 C  CD2   . TYR A 1 388 ? -2.891  9.779   -17.716 1.00 75.86  ? 388 TYR A CD2   1 
ATOM   3215 C  CE1   . TYR A 1 388 ? -2.137  10.526  -15.168 1.00 68.02  ? 388 TYR A CE1   1 
ATOM   3216 C  CE2   . TYR A 1 388 ? -2.220  8.882   -16.905 1.00 74.17  ? 388 TYR A CE2   1 
ATOM   3217 C  CZ    . TYR A 1 388 ? -1.846  9.261   -15.633 1.00 72.61  ? 388 TYR A CZ    1 
ATOM   3218 O  OH    . TYR A 1 388 ? -1.177  8.371   -14.824 1.00 79.75  ? 388 TYR A OH    1 
ATOM   3219 N  N     . VAL A 1 389 ? -6.116  10.022  -16.790 1.00 68.86  ? 389 VAL A N     1 
ATOM   3220 C  CA    . VAL A 1 389 ? -6.627  9.504   -15.524 1.00 78.62  ? 389 VAL A CA    1 
ATOM   3221 C  C     . VAL A 1 389 ? -5.922  8.185   -15.237 1.00 77.09  ? 389 VAL A C     1 
ATOM   3222 O  O     . VAL A 1 389 ? -5.779  7.338   -16.125 1.00 86.14  ? 389 VAL A O     1 
ATOM   3223 C  CB    . VAL A 1 389 ? -8.164  9.347   -15.542 1.00 70.50  ? 389 VAL A CB    1 
ATOM   3224 C  CG1   . VAL A 1 389 ? -8.611  8.413   -16.655 1.00 72.99  ? 389 VAL A CG1   1 
ATOM   3225 C  CG2   . VAL A 1 389 ? -8.674  8.870   -14.187 1.00 58.88  ? 389 VAL A CG2   1 
ATOM   3226 N  N     . LYS A 1 390 ? -5.457  8.025   -14.004 1.00 80.76  ? 390 LYS A N     1 
ATOM   3227 C  CA    . LYS A 1 390 ? -4.670  6.870   -13.607 1.00 84.50  ? 390 LYS A CA    1 
ATOM   3228 C  C     . LYS A 1 390 ? -5.474  5.971   -12.680 1.00 82.31  ? 390 LYS A C     1 
ATOM   3229 O  O     . LYS A 1 390 ? -6.334  6.435   -11.926 1.00 80.37  ? 390 LYS A O     1 
ATOM   3230 C  CB    . LYS A 1 390 ? -3.375  7.301   -12.913 1.00 91.13  ? 390 LYS A CB    1 
ATOM   3231 C  CG    . LYS A 1 390 ? -3.588  8.112   -11.645 1.00 87.69  ? 390 LYS A CG    1 
ATOM   3232 C  CD    . LYS A 1 390 ? -2.310  8.210   -10.825 1.00 81.74  ? 390 LYS A CD    1 
ATOM   3233 C  CE    . LYS A 1 390 ? -1.711  6.838   -10.561 1.00 94.14  ? 390 LYS A CE    1 
ATOM   3234 N  NZ    . LYS A 1 390 ? -0.959  6.794   -9.276  1.00 91.39  ? 390 LYS A NZ    1 
ATOM   3235 N  N     . GLU A 1 391 ? -5.187  4.678   -12.749 1.00 75.49  ? 391 GLU A N     1 
ATOM   3236 C  CA    . GLU A 1 391 ? -5.777  3.733   -11.816 1.00 70.90  ? 391 GLU A CA    1 
ATOM   3237 C  C     . GLU A 1 391 ? -5.298  4.064   -10.409 1.00 70.97  ? 391 GLU A C     1 
ATOM   3238 O  O     . GLU A 1 391 ? -4.081  4.079   -10.165 1.00 71.08  ? 391 GLU A O     1 
ATOM   3239 C  CB    . GLU A 1 391 ? -5.409  2.300   -12.185 1.00 67.71  ? 391 GLU A CB    1 
ATOM   3240 C  CG    . GLU A 1 391 ? -6.454  1.608   -13.042 1.00 73.26  ? 391 GLU A CG    1 
ATOM   3241 C  CD    . GLU A 1 391 ? -7.742  1.339   -12.287 1.00 77.11  ? 391 GLU A CD    1 
ATOM   3242 O  OE1   . GLU A 1 391 ? -7.689  1.194   -11.046 1.00 77.37  ? 391 GLU A OE1   1 
ATOM   3243 O  OE2   . GLU A 1 391 ? -8.810  1.282   -12.933 1.00 85.58  ? 391 GLU A OE2   1 
ATOM   3244 N  N     . PRO A 1 392 ? -6.197  4.340   -9.469  1.00 70.74  ? 392 PRO A N     1 
ATOM   3245 C  CA    . PRO A 1 392 ? -5.759  4.782   -8.143  1.00 68.35  ? 392 PRO A CA    1 
ATOM   3246 C  C     . PRO A 1 392 ? -5.053  3.668   -7.392  1.00 76.31  ? 392 PRO A C     1 
ATOM   3247 O  O     . PRO A 1 392 ? -5.366  2.485   -7.544  1.00 78.79  ? 392 PRO A O     1 
ATOM   3248 C  CB    . PRO A 1 392 ? -7.068  5.171   -7.440  1.00 67.42  ? 392 PRO A CB    1 
ATOM   3249 C  CG    . PRO A 1 392 ? -8.135  5.128   -8.497  1.00 74.17  ? 392 PRO A CG    1 
ATOM   3250 C  CD    . PRO A 1 392 ? -7.657  4.189   -9.547  1.00 71.06  ? 392 PRO A CD    1 
ATOM   3251 N  N     . GLU A 1 393 ? -4.078  4.063   -6.579  1.00 73.36  ? 393 GLU A N     1 
ATOM   3252 C  CA    . GLU A 1 393 ? -3.505  3.140   -5.611  1.00 72.56  ? 393 GLU A CA    1 
ATOM   3253 C  C     . GLU A 1 393 ? -4.590  2.787   -4.603  1.00 76.81  ? 393 GLU A C     1 
ATOM   3254 O  O     . GLU A 1 393 ? -4.703  3.436   -3.558  1.00 74.45  ? 393 GLU A O     1 
ATOM   3255 C  CB    . GLU A 1 393 ? -2.290  3.760   -4.924  1.00 71.40  ? 393 GLU A CB    1 
ATOM   3256 C  CG    . GLU A 1 393 ? -1.204  4.223   -5.877  1.00 77.61  ? 393 GLU A CG    1 
ATOM   3257 C  CD    . GLU A 1 393 ? -0.569  3.078   -6.638  1.00 79.84  ? 393 GLU A CD    1 
ATOM   3258 O  OE1   . GLU A 1 393 ? -0.391  1.995   -6.043  1.00 91.45  ? 393 GLU A OE1   1 
ATOM   3259 O  OE2   . GLU A 1 393 ? -0.244  3.263   -7.829  1.00 86.08  ? 393 GLU A OE2   1 
ATOM   3260 N  N     . ARG A 1 394 ? -5.398  1.774   -4.923  1.00 77.46  ? 394 ARG A N     1 
ATOM   3261 C  CA    . ARG A 1 394 ? -6.627  1.511   -4.185  1.00 81.96  ? 394 ARG A CA    1 
ATOM   3262 C  C     . ARG A 1 394 ? -6.347  1.263   -2.711  1.00 74.40  ? 394 ARG A C     1 
ATOM   3263 O  O     . ARG A 1 394 ? -5.317  0.696   -2.332  1.00 84.94  ? 394 ARG A O     1 
ATOM   3264 C  CB    . ARG A 1 394 ? -7.365  0.299   -4.753  1.00 88.26  ? 394 ARG A CB    1 
ATOM   3265 C  CG    . ARG A 1 394 ? -7.393  0.185   -6.252  1.00 90.10  ? 394 ARG A CG    1 
ATOM   3266 C  CD    . ARG A 1 394 ? -8.267  -0.972  -6.795  1.00 109.31 ? 394 ARG A CD    1 
ATOM   3267 N  NE    . ARG A 1 394 ? -9.673  -0.990  -6.381  1.00 122.19 ? 394 ARG A NE    1 
ATOM   3268 C  CZ    . ARG A 1 394 ? -10.142 -1.309  -5.176  1.00 111.84 ? 394 ARG A CZ    1 
ATOM   3269 N  NH1   . ARG A 1 394 ? -9.370  -1.848  -4.239  1.00 115.65 ? 394 ARG A NH1   1 
ATOM   3270 N  NH2   . ARG A 1 394 ? -11.435 -1.133  -4.919  1.00 83.37  ? 394 ARG A NH2   1 
ATOM   3271 N  N     . GLY A 1 395 ? -7.287  1.689   -1.874  1.00 77.94  ? 395 GLY A N     1 
ATOM   3272 C  CA    . GLY A 1 395 ? -7.171  1.437   -0.454  1.00 73.27  ? 395 GLY A CA    1 
ATOM   3273 C  C     . GLY A 1 395 ? -7.191  2.700   0.377   1.00 76.15  ? 395 GLY A C     1 
ATOM   3274 O  O     . GLY A 1 395 ? -7.646  3.751   -0.085  1.00 77.41  ? 395 GLY A O     1 
ATOM   3275 N  N     . LEU A 1 396 ? -6.687  2.608   1.604   1.00 74.78  ? 396 LEU A N     1 
ATOM   3276 C  CA    . LEU A 1 396 ? -6.729  3.701   2.564   1.00 80.96  ? 396 LEU A CA    1 
ATOM   3277 C  C     . LEU A 1 396 ? -5.341  4.310   2.713   1.00 80.84  ? 396 LEU A C     1 
ATOM   3278 O  O     . LEU A 1 396 ? -4.348  3.584   2.833   1.00 81.18  ? 396 LEU A O     1 
ATOM   3279 C  CB    . LEU A 1 396 ? -7.249  3.211   3.919   1.00 83.31  ? 396 LEU A CB    1 
ATOM   3280 C  CG    . LEU A 1 396 ? -7.206  4.191   5.092   1.00 91.73  ? 396 LEU A CG    1 
ATOM   3281 C  CD1   . LEU A 1 396 ? -8.360  5.176   5.010   1.00 80.85  ? 396 LEU A CD1   1 
ATOM   3282 C  CD2   . LEU A 1 396 ? -7.234  3.442   6.418   1.00 89.92  ? 396 LEU A CD2   1 
ATOM   3283 N  N     . TRP A 1 397 ? -5.279  5.640   2.699   1.00 82.54  ? 397 TRP A N     1 
ATOM   3284 C  CA    . TRP A 1 397 ? -4.042  6.388   2.845   1.00 86.42  ? 397 TRP A CA    1 
ATOM   3285 C  C     . TRP A 1 397 ? -4.236  7.483   3.883   1.00 88.15  ? 397 TRP A C     1 
ATOM   3286 O  O     . TRP A 1 397 ? -5.363  7.851   4.225   1.00 84.58  ? 397 TRP A O     1 
ATOM   3287 C  CB    . TRP A 1 397 ? -3.591  7.011   1.516   1.00 76.24  ? 397 TRP A CB    1 
ATOM   3288 C  CG    . TRP A 1 397 ? -3.323  6.015   0.440   1.00 77.58  ? 397 TRP A CG    1 
ATOM   3289 C  CD1   . TRP A 1 397 ? -4.244  5.280   -0.248  1.00 75.46  ? 397 TRP A CD1   1 
ATOM   3290 C  CD2   . TRP A 1 397 ? -2.042  5.637   -0.073  1.00 71.53  ? 397 TRP A CD2   1 
ATOM   3291 N  NE1   . TRP A 1 397 ? -3.614  4.469   -1.160  1.00 76.76  ? 397 TRP A NE1   1 
ATOM   3292 C  CE2   . TRP A 1 397 ? -2.261  4.670   -1.071  1.00 72.12  ? 397 TRP A CE2   1 
ATOM   3293 C  CE3   . TRP A 1 397 ? -0.731  6.024   0.216   1.00 76.55  ? 397 TRP A CE3   1 
ATOM   3294 C  CZ2   . TRP A 1 397 ? -1.217  4.082   -1.779  1.00 80.93  ? 397 TRP A CZ2   1 
ATOM   3295 C  CZ3   . TRP A 1 397 ? 0.304   5.441   -0.492  1.00 75.32  ? 397 TRP A CZ3   1 
ATOM   3296 C  CH2   . TRP A 1 397 ? 0.055   4.482   -1.479  1.00 76.47  ? 397 TRP A CH2   1 
ATOM   3297 N  N     . GLU A 1 398 ? -3.117  8.012   4.371   1.00 88.33  ? 398 GLU A N     1 
ATOM   3298 C  CA    . GLU A 1 398 ? -3.115  9.050   5.390   1.00 88.55  ? 398 GLU A CA    1 
ATOM   3299 C  C     . GLU A 1 398 ? -2.200  10.189  4.962   1.00 88.35  ? 398 GLU A C     1 
ATOM   3300 O  O     . GLU A 1 398 ? -1.262  9.993   4.184   1.00 89.24  ? 398 GLU A O     1 
ATOM   3301 C  CB    . GLU A 1 398 ? -2.662  8.506   6.758   1.00 93.19  ? 398 GLU A CB    1 
ATOM   3302 C  CG    . GLU A 1 398 ? -3.025  7.048   7.029   1.00 104.04 ? 398 GLU A CG    1 
ATOM   3303 C  CD    . GLU A 1 398 ? -2.038  6.060   6.426   1.00 120.11 ? 398 GLU A CD    1 
ATOM   3304 O  OE1   . GLU A 1 398 ? -1.662  6.222   5.244   1.00 112.24 ? 398 GLU A OE1   1 
ATOM   3305 O  OE2   . GLU A 1 398 ? -1.640  5.114   7.137   1.00 131.58 ? 398 GLU A OE2   1 
ATOM   3306 N  N     . ASN A 1 399 ? -2.487  11.383  5.485   1.00 83.73  ? 399 ASN A N     1 
ATOM   3307 C  CA    . ASN A 1 399 ? -1.695  12.586  5.226   1.00 81.22  ? 399 ASN A CA    1 
ATOM   3308 C  C     . ASN A 1 399 ? -1.593  12.869  3.726   1.00 80.17  ? 399 ASN A C     1 
ATOM   3309 O  O     . ASN A 1 399 ? -0.516  12.839  3.129   1.00 82.50  ? 399 ASN A O     1 
ATOM   3310 C  CB    . ASN A 1 399 ? -0.305  12.475  5.863   1.00 84.88  ? 399 ASN A CB    1 
ATOM   3311 C  CG    . ASN A 1 399 ? -0.365  12.337  7.369   1.00 93.65  ? 399 ASN A CG    1 
ATOM   3312 O  OD1   . ASN A 1 399 ? -1.195  12.962  8.029   1.00 101.86 ? 399 ASN A OD1   1 
ATOM   3313 N  ND2   . ASN A 1 399 ? 0.519   11.515  7.924   1.00 90.89  ? 399 ASN A ND2   1 
ATOM   3314 N  N     . ILE A 1 400 ? -2.743  13.165  3.128   1.00 75.70  ? 400 ILE A N     1 
ATOM   3315 C  CA    . ILE A 1 400 ? -2.863  13.353  1.687   1.00 71.90  ? 400 ILE A CA    1 
ATOM   3316 C  C     . ILE A 1 400 ? -3.012  14.837  1.384   1.00 69.91  ? 400 ILE A C     1 
ATOM   3317 O  O     . ILE A 1 400 ? -3.695  15.567  2.112   1.00 67.85  ? 400 ILE A O     1 
ATOM   3318 C  CB    . ILE A 1 400 ? -4.056  12.561  1.120   1.00 77.55  ? 400 ILE A CB    1 
ATOM   3319 C  CG1   . ILE A 1 400 ? -4.125  11.172  1.755   1.00 76.60  ? 400 ILE A CG1   1 
ATOM   3320 C  CG2   . ILE A 1 400 ? -3.955  12.457  -0.394  1.00 75.67  ? 400 ILE A CG2   1 
ATOM   3321 C  CD1   . ILE A 1 400 ? -5.070  10.230  1.047   1.00 83.02  ? 400 ILE A CD1   1 
ATOM   3322 N  N     . VAL A 1 401 ? -2.372  15.279  0.303   1.00 62.74  ? 401 VAL A N     1 
ATOM   3323 C  CA    . VAL A 1 401 ? -2.525  16.631  -0.220  1.00 66.06  ? 401 VAL A CA    1 
ATOM   3324 C  C     . VAL A 1 401 ? -3.085  16.539  -1.631  1.00 63.09  ? 401 VAL A C     1 
ATOM   3325 O  O     . VAL A 1 401 ? -2.628  15.722  -2.439  1.00 64.11  ? 401 VAL A O     1 
ATOM   3326 C  CB    . VAL A 1 401 ? -1.194  17.414  -0.219  1.00 60.11  ? 401 VAL A CB    1 
ATOM   3327 C  CG1   . VAL A 1 401 ? -0.871  17.922  1.175   1.00 70.94  ? 401 VAL A CG1   1 
ATOM   3328 C  CG2   . VAL A 1 401 ? -0.062  16.549  -0.752  1.00 67.21  ? 401 VAL A CG2   1 
ATOM   3329 N  N     . TYR A 1 402 ? -4.075  17.376  -1.924  1.00 52.61  ? 402 TYR A N     1 
ATOM   3330 C  CA    . TYR A 1 402 ? -4.649  17.478  -3.259  1.00 60.74  ? 402 TYR A CA    1 
ATOM   3331 C  C     . TYR A 1 402 ? -4.135  18.754  -3.913  1.00 59.80  ? 402 TYR A C     1 
ATOM   3332 O  O     . TYR A 1 402 ? -4.343  19.854  -3.388  1.00 58.20  ? 402 TYR A O     1 
ATOM   3333 C  CB    . TYR A 1 402 ? -6.178  17.475  -3.209  1.00 58.75  ? 402 TYR A CB    1 
ATOM   3334 C  CG    . TYR A 1 402 ? -6.829  17.561  -4.574  1.00 59.33  ? 402 TYR A CG    1 
ATOM   3335 C  CD1   . TYR A 1 402 ? -6.624  16.571  -5.527  1.00 58.74  ? 402 TYR A CD1   1 
ATOM   3336 C  CD2   . TYR A 1 402 ? -7.640  18.637  -4.914  1.00 62.67  ? 402 TYR A CD2   1 
ATOM   3337 C  CE1   . TYR A 1 402 ? -7.212  16.646  -6.779  1.00 59.20  ? 402 TYR A CE1   1 
ATOM   3338 C  CE2   . TYR A 1 402 ? -8.233  18.721  -6.164  1.00 70.50  ? 402 TYR A CE2   1 
ATOM   3339 C  CZ    . TYR A 1 402 ? -8.015  17.723  -7.092  1.00 68.25  ? 402 TYR A CZ    1 
ATOM   3340 O  OH    . TYR A 1 402 ? -8.601  17.801  -8.336  1.00 69.30  ? 402 TYR A OH    1 
ATOM   3341 N  N     . LEU A 1 403 ? -3.460  18.605  -5.047  1.00 58.46  ? 403 LEU A N     1 
ATOM   3342 C  CA    . LEU A 1 403 ? -2.935  19.733  -5.803  1.00 55.80  ? 403 LEU A CA    1 
ATOM   3343 C  C     . LEU A 1 403 ? -3.573  19.723  -7.180  1.00 59.23  ? 403 LEU A C     1 
ATOM   3344 O  O     . LEU A 1 403 ? -3.585  18.684  -7.847  1.00 58.22  ? 403 LEU A O     1 
ATOM   3345 C  CB    . LEU A 1 403 ? -1.410  19.661  -5.929  1.00 50.45  ? 403 LEU A CB    1 
ATOM   3346 C  CG    . LEU A 1 403 ? -0.601  19.370  -4.664  1.00 57.13  ? 403 LEU A CG    1 
ATOM   3347 C  CD1   . LEU A 1 403 ? 0.891   19.380  -4.974  1.00 53.36  ? 403 LEU A CD1   1 
ATOM   3348 C  CD2   . LEU A 1 403 ? -0.932  20.371  -3.567  1.00 53.46  ? 403 LEU A CD2   1 
ATOM   3349 N  N     . ASP A 1 404 ? -4.096  20.869  -7.613  1.00 53.13  ? 404 ASP A N     1 
ATOM   3350 C  CA    . ASP A 1 404 ? -4.742  20.914  -8.921  1.00 58.78  ? 404 ASP A CA    1 
ATOM   3351 C  C     . ASP A 1 404 ? -4.485  22.251  -9.600  1.00 55.78  ? 404 ASP A C     1 
ATOM   3352 O  O     . ASP A 1 404 ? -4.128  23.240  -8.960  1.00 54.38  ? 404 ASP A O     1 
ATOM   3353 C  CB    . ASP A 1 404 ? -6.254  20.630  -8.823  1.00 56.61  ? 404 ASP A CB    1 
ATOM   3354 C  CG    . ASP A 1 404 ? -7.034  21.785  -8.234  1.00 65.86  ? 404 ASP A CG    1 
ATOM   3355 O  OD1   . ASP A 1 404 ? -6.424  22.620  -7.543  1.00 74.77  ? 404 ASP A OD1   1 
ATOM   3356 O  OD2   . ASP A 1 404 ? -8.262  21.858  -8.457  1.00 73.23  ? 404 ASP A OD2   1 
ATOM   3357 N  N     . PHE A 1 405 ? -4.651  22.262  -10.918 1.00 51.82  ? 405 PHE A N     1 
ATOM   3358 C  CA    . PHE A 1 405 ? -4.428  23.473  -11.688 1.00 54.84  ? 405 PHE A CA    1 
ATOM   3359 C  C     . PHE A 1 405 ? -5.621  24.415  -11.561 1.00 59.90  ? 405 PHE A C     1 
ATOM   3360 O  O     . PHE A 1 405 ? -6.744  24.006  -11.250 1.00 61.61  ? 405 PHE A O     1 
ATOM   3361 C  CB    . PHE A 1 405 ? -4.177  23.139  -13.160 1.00 56.31  ? 405 PHE A CB    1 
ATOM   3362 C  CG    . PHE A 1 405 ? -2.903  22.377  -13.405 1.00 56.12  ? 405 PHE A CG    1 
ATOM   3363 C  CD1   . PHE A 1 405 ? -1.694  23.041  -13.531 1.00 59.81  ? 405 PHE A CD1   1 
ATOM   3364 C  CD2   . PHE A 1 405 ? -2.917  20.997  -13.514 1.00 50.47  ? 405 PHE A CD2   1 
ATOM   3365 C  CE1   . PHE A 1 405 ? -0.522  22.340  -13.760 1.00 61.25  ? 405 PHE A CE1   1 
ATOM   3366 C  CE2   . PHE A 1 405 ? -1.749  20.291  -13.742 1.00 58.30  ? 405 PHE A CE2   1 
ATOM   3367 C  CZ    . PHE A 1 405 ? -0.551  20.964  -13.864 1.00 56.06  ? 405 PHE A CZ    1 
ATOM   3368 N  N     . ARG A 1 406 ? -5.363  25.697  -11.806 1.00 57.20  ? 406 ARG A N     1 
ATOM   3369 C  CA    . ARG A 1 406 ? -6.415  26.705  -11.843 1.00 55.94  ? 406 ARG A CA    1 
ATOM   3370 C  C     . ARG A 1 406 ? -6.944  26.792  -13.268 1.00 57.47  ? 406 ARG A C     1 
ATOM   3371 O  O     . ARG A 1 406 ? -6.223  27.223  -14.175 1.00 53.49  ? 406 ARG A O     1 
ATOM   3372 C  CB    . ARG A 1 406 ? -5.897  28.063  -11.379 1.00 62.32  ? 406 ARG A CB    1 
ATOM   3373 C  CG    . ARG A 1 406 ? -6.830  29.204  -11.753 1.00 57.88  ? 406 ARG A CG    1 
ATOM   3374 C  CD    . ARG A 1 406 ? -6.249  30.557  -11.404 1.00 64.75  ? 406 ARG A CD    1 
ATOM   3375 N  NE    . ARG A 1 406 ? -6.007  30.689  -9.974  1.00 69.36  ? 406 ARG A NE    1 
ATOM   3376 C  CZ    . ARG A 1 406 ? -5.049  31.438  -9.447  1.00 86.32  ? 406 ARG A CZ    1 
ATOM   3377 N  NH1   . ARG A 1 406 ? -4.225  32.140  -10.207 1.00 85.99  ? 406 ARG A NH1   1 
ATOM   3378 N  NH2   . ARG A 1 406 ? -4.916  31.485  -8.124  1.00 95.95  ? 406 ARG A NH2   1 
ATOM   3379 N  N     . SER A 1 407 ? -8.205  26.395  -13.459 1.00 50.26  ? 407 SER A N     1 
ATOM   3380 C  CA    . SER A 1 407 ? -8.872  26.460  -14.756 1.00 47.88  ? 407 SER A CA    1 
ATOM   3381 C  C     . SER A 1 407 ? -7.970  25.933  -15.863 1.00 52.52  ? 407 SER A C     1 
ATOM   3382 O  O     . SER A 1 407 ? -7.535  26.698  -16.731 1.00 52.30  ? 407 SER A O     1 
ATOM   3383 C  CB    . SER A 1 407 ? -9.312  27.894  -15.059 1.00 53.13  ? 407 SER A CB    1 
ATOM   3384 O  OG    . SER A 1 407 ? -10.014 28.447  -13.959 1.00 56.58  ? 407 SER A OG    1 
ATOM   3385 N  N     . LEU A 1 408 ? -7.690  24.628  -15.832 1.00 52.28  ? 408 LEU A N     1 
ATOM   3386 C  CA    . LEU A 1 408 ? -6.669  24.038  -16.692 1.00 49.17  ? 408 LEU A CA    1 
ATOM   3387 C  C     . LEU A 1 408 ? -6.898  24.377  -18.162 1.00 50.65  ? 408 LEU A C     1 
ATOM   3388 O  O     . LEU A 1 408 ? -6.026  24.945  -18.826 1.00 46.40  ? 408 LEU A O     1 
ATOM   3389 C  CB    . LEU A 1 408 ? -6.642  22.522  -16.487 1.00 51.31  ? 408 LEU A CB    1 
ATOM   3390 C  CG    . LEU A 1 408 ? -5.607  21.739  -17.294 1.00 47.41  ? 408 LEU A CG    1 
ATOM   3391 C  CD1   . LEU A 1 408 ? -4.224  22.383  -17.189 1.00 48.07  ? 408 LEU A CD1   1 
ATOM   3392 C  CD2   . LEU A 1 408 ? -5.570  20.288  -16.853 1.00 49.33  ? 408 LEU A CD2   1 
ATOM   3393 N  N     . TYR A 1 409 ? -8.078  24.038  -18.689 1.00 49.50  ? 409 TYR A N     1 
ATOM   3394 C  CA    . TYR A 1 409 ? -8.293  24.186  -20.128 1.00 49.20  ? 409 TYR A CA    1 
ATOM   3395 C  C     . TYR A 1 409 ? -8.362  25.649  -20.554 1.00 49.29  ? 409 TYR A C     1 
ATOM   3396 O  O     . TYR A 1 409 ? -7.745  26.001  -21.578 1.00 44.45  ? 409 TYR A O     1 
ATOM   3397 C  CB    . TYR A 1 409 ? -9.538  23.398  -20.548 1.00 49.27  ? 409 TYR A CB    1 
ATOM   3398 C  CG    . TYR A 1 409 ? -9.338  21.898  -20.604 1.00 57.58  ? 409 TYR A CG    1 
ATOM   3399 C  CD1   . TYR A 1 409 ? -8.206  21.299  -20.054 1.00 47.75  ? 409 TYR A CD1   1 
ATOM   3400 C  CD2   . TYR A 1 409 ? -10.300 21.077  -21.165 1.00 47.64  ? 409 TYR A CD2   1 
ATOM   3401 C  CE1   . TYR A 1 409 ? -8.033  19.928  -20.094 1.00 48.08  ? 409 TYR A CE1   1 
ATOM   3402 C  CE2   . TYR A 1 409 ? -10.140 19.707  -21.207 1.00 42.40  ? 409 TYR A CE2   1 
ATOM   3403 C  CZ    . TYR A 1 409 ? -9.005  19.136  -20.671 1.00 49.36  ? 409 TYR A CZ    1 
ATOM   3404 O  OH    . TYR A 1 409 ? -8.846  17.769  -20.713 1.00 47.86  ? 409 TYR A OH    1 
ATOM   3405 N  N     . PRO A 1 410 ? -9.080  26.540  -19.857 1.00 51.67  ? 410 PRO A N     1 
ATOM   3406 C  CA    . PRO A 1 410 ? -9.016  27.957  -20.250 1.00 45.44  ? 410 PRO A CA    1 
ATOM   3407 C  C     . PRO A 1 410 ? -7.628  28.553  -20.115 1.00 43.75  ? 410 PRO A C     1 
ATOM   3408 O  O     . PRO A 1 410 ? -7.223  29.365  -20.957 1.00 44.20  ? 410 PRO A O     1 
ATOM   3409 C  CB    . PRO A 1 410 ? -10.022 28.631  -19.303 1.00 40.82  ? 410 PRO A CB    1 
ATOM   3410 C  CG    . PRO A 1 410 ? -10.958 27.547  -18.911 1.00 44.23  ? 410 PRO A CG    1 
ATOM   3411 C  CD    . PRO A 1 410 ? -10.103 26.320  -18.817 1.00 48.57  ? 410 PRO A CD    1 
ATOM   3412 N  N     . SER A 1 411 ? -6.882  28.172  -19.075 1.00 41.49  ? 411 SER A N     1 
ATOM   3413 C  CA    . SER A 1 411 ? -5.518  28.669  -18.930 1.00 49.33  ? 411 SER A CA    1 
ATOM   3414 C  C     . SER A 1 411 ? -4.635  28.193  -20.076 1.00 44.64  ? 411 SER A C     1 
ATOM   3415 O  O     . SER A 1 411 ? -3.768  28.934  -20.549 1.00 45.89  ? 411 SER A O     1 
ATOM   3416 C  CB    . SER A 1 411 ? -4.935  28.236  -17.586 1.00 53.14  ? 411 SER A CB    1 
ATOM   3417 O  OG    . SER A 1 411 ? -5.686  28.782  -16.515 1.00 47.55  ? 411 SER A OG    1 
ATOM   3418 N  N     . ILE A 1 412 ? -4.846  26.963  -20.543 1.00 40.90  ? 412 ILE A N     1 
ATOM   3419 C  CA    . ILE A 1 412 ? -4.109  26.473  -21.704 1.00 43.69  ? 412 ILE A CA    1 
ATOM   3420 C  C     . ILE A 1 412 ? -4.461  27.297  -22.936 1.00 46.69  ? 412 ILE A C     1 
ATOM   3421 O  O     . ILE A 1 412 ? -3.579  27.751  -23.679 1.00 51.39  ? 412 ILE A O     1 
ATOM   3422 C  CB    . ILE A 1 412 ? -4.401  24.980  -21.926 1.00 48.19  ? 412 ILE A CB    1 
ATOM   3423 C  CG1   . ILE A 1 412 ? -3.714  24.143  -20.847 1.00 46.69  ? 412 ILE A CG1   1 
ATOM   3424 C  CG2   . ILE A 1 412 ? -3.976  24.556  -23.324 1.00 44.74  ? 412 ILE A CG2   1 
ATOM   3425 C  CD1   . ILE A 1 412 ? -4.059  22.679  -20.910 1.00 44.93  ? 412 ILE A CD1   1 
ATOM   3426 N  N     . ILE A 1 413 ? -5.762  27.497  -23.168 1.00 42.96  ? 413 ILE A N     1 
ATOM   3427 C  CA    . ILE A 1 413 ? -6.214  28.276  -24.321 1.00 43.51  ? 413 ILE A CA    1 
ATOM   3428 C  C     . ILE A 1 413 ? -5.592  29.666  -24.306 1.00 42.79  ? 413 ILE A C     1 
ATOM   3429 O  O     . ILE A 1 413 ? -5.150  30.178  -25.342 1.00 39.70  ? 413 ILE A O     1 
ATOM   3430 C  CB    . ILE A 1 413 ? -7.752  28.349  -24.344 1.00 41.86  ? 413 ILE A CB    1 
ATOM   3431 C  CG1   . ILE A 1 413 ? -8.342  27.010  -24.775 1.00 43.82  ? 413 ILE A CG1   1 
ATOM   3432 C  CG2   . ILE A 1 413 ? -8.226  29.463  -25.265 1.00 39.55  ? 413 ILE A CG2   1 
ATOM   3433 C  CD1   . ILE A 1 413 ? -9.693  26.726  -24.176 1.00 45.23  ? 413 ILE A CD1   1 
ATOM   3434 N  N     . ILE A 1 414 ? -5.539  30.292  -23.130 1.00 39.20  ? 414 ILE A N     1 
ATOM   3435 C  CA    . ILE A 1 414 ? -4.989  31.640  -23.024 1.00 42.47  ? 414 ILE A CA    1 
ATOM   3436 C  C     . ILE A 1 414 ? -3.479  31.620  -23.237 1.00 48.98  ? 414 ILE A C     1 
ATOM   3437 O  O     . ILE A 1 414 ? -2.929  32.449  -23.971 1.00 41.96  ? 414 ILE A O     1 
ATOM   3438 C  CB    . ILE A 1 414 ? -5.355  32.258  -21.664 1.00 42.36  ? 414 ILE A CB    1 
ATOM   3439 C  CG1   . ILE A 1 414 ? -6.862  32.485  -21.571 1.00 43.01  ? 414 ILE A CG1   1 
ATOM   3440 C  CG2   . ILE A 1 414 ? -4.601  33.560  -21.443 1.00 44.56  ? 414 ILE A CG2   1 
ATOM   3441 C  CD1   . ILE A 1 414 ? -7.355  32.628  -20.157 1.00 42.52  ? 414 ILE A CD1   1 
ATOM   3442 N  N     . THR A 1 415 ? -2.790  30.667  -22.606 1.00 44.89  ? 415 THR A N     1 
ATOM   3443 C  CA    . THR A 1 415 ? -1.332  30.655  -22.630 1.00 46.99  ? 415 THR A CA    1 
ATOM   3444 C  C     . THR A 1 415 ? -0.799  30.383  -24.030 1.00 50.43  ? 415 THR A C     1 
ATOM   3445 O  O     . THR A 1 415 ? 0.193   30.991  -24.450 1.00 53.75  ? 415 THR A O     1 
ATOM   3446 C  CB    . THR A 1 415 ? -0.808  29.612  -21.644 1.00 49.18  ? 415 THR A CB    1 
ATOM   3447 O  OG1   . THR A 1 415 ? -1.322  29.893  -20.336 1.00 47.34  ? 415 THR A OG1   1 
ATOM   3448 C  CG2   . THR A 1 415 ? 0.715   29.623  -21.601 1.00 52.14  ? 415 THR A CG2   1 
ATOM   3449 N  N     . HIS A 1 416 ? -1.441  29.484  -24.772 1.00 52.19  ? 416 HIS A N     1 
ATOM   3450 C  CA    . HIS A 1 416 ? -0.952  29.108  -26.091 1.00 49.09  ? 416 HIS A CA    1 
ATOM   3451 C  C     . HIS A 1 416 ? -1.783  29.694  -27.226 1.00 54.74  ? 416 HIS A C     1 
ATOM   3452 O  O     . HIS A 1 416 ? -1.609  29.284  -28.379 1.00 47.83  ? 416 HIS A O     1 
ATOM   3453 C  CB    . HIS A 1 416 ? -0.883  27.586  -26.200 1.00 53.40  ? 416 HIS A CB    1 
ATOM   3454 C  CG    . HIS A 1 416 ? 0.006   26.954  -25.174 1.00 59.86  ? 416 HIS A CG    1 
ATOM   3455 N  ND1   . HIS A 1 416 ? 1.239   27.471  -24.841 1.00 65.00  ? 416 HIS A ND1   1 
ATOM   3456 C  CD2   . HIS A 1 416 ? -0.166  25.862  -24.393 1.00 61.50  ? 416 HIS A CD2   1 
ATOM   3457 C  CE1   . HIS A 1 416 ? 1.794   26.717  -23.909 1.00 55.97  ? 416 HIS A CE1   1 
ATOM   3458 N  NE2   . HIS A 1 416 ? 0.962   25.734  -23.619 1.00 64.10  ? 416 HIS A NE2   1 
ATOM   3459 N  N     . ASN A 1 417 ? -2.670  30.649  -26.929 1.00 54.01  ? 417 ASN A N     1 
ATOM   3460 C  CA    . ASN A 1 417 ? -3.463  31.345  -27.946 1.00 48.88  ? 417 ASN A CA    1 
ATOM   3461 C  C     . ASN A 1 417 ? -4.256  30.363  -28.803 1.00 46.48  ? 417 ASN A C     1 
ATOM   3462 O  O     . ASN A 1 417 ? -4.352  30.511  -30.023 1.00 43.09  ? 417 ASN A O     1 
ATOM   3463 C  CB    . ASN A 1 417 ? -2.581  32.239  -28.821 1.00 50.00  ? 417 ASN A CB    1 
ATOM   3464 C  CG    . ASN A 1 417 ? -3.275  33.521  -29.226 1.00 48.04  ? 417 ASN A CG    1 
ATOM   3465 O  OD1   . ASN A 1 417 ? -4.035  34.101  -28.451 1.00 49.09  ? 417 ASN A OD1   1 
ATOM   3466 N  ND2   . ASN A 1 417 ? -3.014  33.974  -30.447 1.00 51.10  ? 417 ASN A ND2   1 
ATOM   3467 N  N     . VAL A 1 418 ? -4.828  29.349  -28.158 1.00 42.93  ? 418 VAL A N     1 
ATOM   3468 C  CA    . VAL A 1 418 ? -5.594  28.335  -28.873 1.00 47.09  ? 418 VAL A CA    1 
ATOM   3469 C  C     . VAL A 1 418 ? -6.914  28.943  -29.328 1.00 49.07  ? 418 VAL A C     1 
ATOM   3470 O  O     . VAL A 1 418 ? -7.739  29.363  -28.507 1.00 45.47  ? 418 VAL A O     1 
ATOM   3471 C  CB    . VAL A 1 418 ? -5.821  27.101  -27.994 1.00 51.86  ? 418 VAL A CB    1 
ATOM   3472 C  CG1   . VAL A 1 418 ? -6.680  26.083  -28.722 1.00 44.72  ? 418 VAL A CG1   1 
ATOM   3473 C  CG2   . VAL A 1 418 ? -4.485  26.492  -27.589 1.00 49.96  ? 418 VAL A CG2   1 
ATOM   3474 N  N     . SER A 1 419 ? -7.118  28.995  -30.643 1.00 43.45  ? 419 SER A N     1 
ATOM   3475 C  CA    . SER A 1 419 ? -8.316  29.579  -31.230 1.00 45.49  ? 419 SER A CA    1 
ATOM   3476 C  C     . SER A 1 419 ? -8.421  29.159  -32.690 1.00 48.31  ? 419 SER A C     1 
ATOM   3477 O  O     . SER A 1 419 ? -7.393  28.967  -33.353 1.00 48.73  ? 419 SER A O     1 
ATOM   3478 C  CB    . SER A 1 419 ? -8.285  31.104  -31.113 1.00 46.83  ? 419 SER A CB    1 
ATOM   3479 O  OG    . SER A 1 419 ? -9.555  31.669  -31.390 1.00 55.88  ? 419 SER A OG    1 
ATOM   3480 N  N     . PRO A 1 420 ? -9.634  28.998  -33.226 1.00 52.46  ? 420 PRO A N     1 
ATOM   3481 C  CA    . PRO A 1 420 ? -9.757  28.644  -34.650 1.00 48.95  ? 420 PRO A CA    1 
ATOM   3482 C  C     . PRO A 1 420 ? -9.125  29.663  -35.580 1.00 48.62  ? 420 PRO A C     1 
ATOM   3483 O  O     . PRO A 1 420 ? -8.675  29.296  -36.673 1.00 48.95  ? 420 PRO A O     1 
ATOM   3484 C  CB    . PRO A 1 420 ? -11.276 28.556  -34.858 1.00 45.52  ? 420 PRO A CB    1 
ATOM   3485 C  CG    . PRO A 1 420 ? -11.835 28.309  -33.497 1.00 51.15  ? 420 PRO A CG    1 
ATOM   3486 C  CD    . PRO A 1 420 ? -10.943 29.055  -32.554 1.00 45.35  ? 420 PRO A CD    1 
ATOM   3487 N  N     . ASP A 1 421 ? -9.070  30.932  -35.178 1.00 49.01  ? 421 ASP A N     1 
ATOM   3488 C  CA    . ASP A 1 421 ? -8.484  31.975  -36.010 1.00 53.76  ? 421 ASP A CA    1 
ATOM   3489 C  C     . ASP A 1 421 ? -6.964  32.031  -35.920 1.00 49.38  ? 421 ASP A C     1 
ATOM   3490 O  O     . ASP A 1 421 ? -6.345  32.802  -36.662 1.00 61.22  ? 421 ASP A O     1 
ATOM   3491 C  CB    . ASP A 1 421 ? -9.075  33.336  -35.630 1.00 44.34  ? 421 ASP A CB    1 
ATOM   3492 C  CG    . ASP A 1 421 ? -9.159  33.534  -34.130 1.00 48.06  ? 421 ASP A CG    1 
ATOM   3493 O  OD1   . ASP A 1 421 ? -9.911  32.784  -33.477 1.00 46.88  ? 421 ASP A OD1   1 
ATOM   3494 O  OD2   . ASP A 1 421 ? -8.476  34.439  -33.603 1.00 53.92  ? 421 ASP A OD2   1 
ATOM   3495 N  N     . THR A 1 422 ? -6.347  31.242  -35.041 1.00 49.43  ? 422 THR A N     1 
ATOM   3496 C  CA    . THR A 1 422 ? -4.896  31.209  -34.910 1.00 53.57  ? 422 THR A CA    1 
ATOM   3497 C  C     . THR A 1 422 ? -4.289  29.877  -35.328 1.00 57.99  ? 422 THR A C     1 
ATOM   3498 O  O     . THR A 1 422 ? -3.062  29.741  -35.316 1.00 53.00  ? 422 THR A O     1 
ATOM   3499 C  CB    . THR A 1 422 ? -4.481  31.524  -33.468 1.00 48.93  ? 422 THR A CB    1 
ATOM   3500 O  OG1   . THR A 1 422 ? -4.876  30.448  -32.608 1.00 50.37  ? 422 THR A OG1   1 
ATOM   3501 C  CG2   . THR A 1 422 ? -5.125  32.813  -32.994 1.00 48.31  ? 422 THR A CG2   1 
ATOM   3502 N  N     . LEU A 1 423 ? -5.108  28.896  -35.698 1.00 57.71  ? 423 LEU A N     1 
ATOM   3503 C  CA    . LEU A 1 423 ? -4.609  27.568  -36.030 1.00 54.99  ? 423 LEU A CA    1 
ATOM   3504 C  C     . LEU A 1 423 ? -3.981  27.577  -37.419 1.00 58.85  ? 423 LEU A C     1 
ATOM   3505 O  O     . LEU A 1 423 ? -4.641  27.933  -38.401 1.00 63.34  ? 423 LEU A O     1 
ATOM   3506 C  CB    . LEU A 1 423 ? -5.742  26.548  -35.959 1.00 53.80  ? 423 LEU A CB    1 
ATOM   3507 C  CG    . LEU A 1 423 ? -5.443  25.174  -36.558 1.00 60.62  ? 423 LEU A CG    1 
ATOM   3508 C  CD1   . LEU A 1 423 ? -4.520  24.376  -35.648 1.00 59.95  ? 423 LEU A CD1   1 
ATOM   3509 C  CD2   . LEU A 1 423 ? -6.735  24.420  -36.819 1.00 54.50  ? 423 LEU A CD2   1 
ATOM   3510 N  N     . ASN A 1 424 ? -2.708  27.181  -37.495 1.00 55.53  ? 424 ASN A N     1 
ATOM   3511 C  CA    . ASN A 1 424 ? -1.985  27.055  -38.763 1.00 57.21  ? 424 ASN A CA    1 
ATOM   3512 C  C     . ASN A 1 424 ? -2.053  28.344  -39.577 1.00 62.83  ? 424 ASN A C     1 
ATOM   3513 O  O     . ASN A 1 424 ? -2.194  28.326  -40.802 1.00 67.54  ? 424 ASN A O     1 
ATOM   3514 C  CB    . ASN A 1 424 ? -2.510  25.872  -39.578 1.00 59.68  ? 424 ASN A CB    1 
ATOM   3515 C  CG    . ASN A 1 424 ? -2.564  24.589  -38.774 1.00 74.29  ? 424 ASN A CG    1 
ATOM   3516 O  OD1   . ASN A 1 424 ? -3.521  23.821  -38.875 1.00 92.26  ? 424 ASN A OD1   1 
ATOM   3517 N  ND2   . ASN A 1 424 ? -1.531  24.346  -37.975 1.00 67.30  ? 424 ASN A ND2   1 
ATOM   3518 N  N     . ARG A 1 425 ? -1.950  29.477  -38.887 1.00 62.56  ? 425 ARG A N     1 
ATOM   3519 C  CA    . ARG A 1 425 ? -2.054  30.784  -39.526 1.00 70.24  ? 425 ARG A CA    1 
ATOM   3520 C  C     . ARG A 1 425 ? -0.737  31.103  -40.223 1.00 72.60  ? 425 ARG A C     1 
ATOM   3521 O  O     . ARG A 1 425 ? 0.283   31.332  -39.565 1.00 78.13  ? 425 ARG A O     1 
ATOM   3522 C  CB    . ARG A 1 425 ? -2.411  31.849  -38.493 1.00 71.69  ? 425 ARG A CB    1 
ATOM   3523 C  CG    . ARG A 1 425 ? -2.446  33.266  -39.034 1.00 81.98  ? 425 ARG A CG    1 
ATOM   3524 C  CD    . ARG A 1 425 ? -2.684  34.263  -37.912 1.00 78.85  ? 425 ARG A CD    1 
ATOM   3525 N  NE    . ARG A 1 425 ? -3.538  35.368  -38.327 1.00 96.38  ? 425 ARG A NE    1 
ATOM   3526 C  CZ    . ARG A 1 425 ? -3.099  36.580  -38.637 1.00 95.99  ? 425 ARG A CZ    1 
ATOM   3527 N  NH1   . ARG A 1 425 ? -1.811  36.880  -38.594 1.00 88.84  ? 425 ARG A NH1   1 
ATOM   3528 N  NH2   . ARG A 1 425 ? -3.973  37.514  -39.001 1.00 94.95  ? 425 ARG A NH2   1 
ATOM   3529 N  N     . GLU A 1 426 ? -0.759  31.115  -41.554 1.00 76.64  ? 426 GLU A N     1 
ATOM   3530 C  CA    . GLU A 1 426 ? 0.450   31.358  -42.330 1.00 80.30  ? 426 GLU A CA    1 
ATOM   3531 C  C     . GLU A 1 426 ? 0.988   32.761  -42.078 1.00 80.21  ? 426 GLU A C     1 
ATOM   3532 O  O     . GLU A 1 426 ? 0.233   33.737  -42.048 1.00 74.82  ? 426 GLU A O     1 
ATOM   3533 C  CB    . GLU A 1 426 ? 0.163   31.179  -43.823 1.00 80.87  ? 426 GLU A CB    1 
ATOM   3534 C  CG    . GLU A 1 426 ? 0.038   29.738  -44.290 1.00 89.31  ? 426 GLU A CG    1 
ATOM   3535 C  CD    . GLU A 1 426 ? -0.383  29.640  -45.747 1.00 113.09 ? 426 GLU A CD    1 
ATOM   3536 O  OE1   . GLU A 1 426 ? -0.568  30.698  -46.386 1.00 117.43 ? 426 GLU A OE1   1 
ATOM   3537 O  OE2   . GLU A 1 426 ? -0.531  28.508  -46.254 1.00 105.90 ? 426 GLU A OE2   1 
ATOM   3538 N  N     . GLY A 1 427 ? 2.304   32.857  -41.887 1.00 77.57  ? 427 GLY A N     1 
ATOM   3539 C  CA    . GLY A 1 427 ? 2.989   34.133  -41.904 1.00 74.91  ? 427 GLY A CA    1 
ATOM   3540 C  C     . GLY A 1 427 ? 3.345   34.737  -40.561 1.00 73.99  ? 427 GLY A C     1 
ATOM   3541 O  O     . GLY A 1 427 ? 3.946   35.818  -40.538 1.00 69.57  ? 427 GLY A O     1 
ATOM   3542 N  N     . CYS A 1 428 ? 2.991   34.099  -39.448 1.00 87.56  ? 428 CYS A N     1 
ATOM   3543 C  CA    . CYS A 1 428 ? 3.380   34.650  -38.158 1.00 76.47  ? 428 CYS A CA    1 
ATOM   3544 C  C     . CYS A 1 428 ? 4.802   34.224  -37.805 1.00 76.89  ? 428 CYS A C     1 
ATOM   3545 O  O     . CYS A 1 428 ? 5.370   33.298  -38.393 1.00 71.28  ? 428 CYS A O     1 
ATOM   3546 C  CB    . CYS A 1 428 ? 2.428   34.204  -37.046 1.00 85.27  ? 428 CYS A CB    1 
ATOM   3547 S  SG    . CYS A 1 428 ? 0.768   34.900  -37.028 1.00 113.30 ? 428 CYS A SG    1 
ATOM   3548 N  N     . GLY A 1 429 ? 5.373   34.910  -36.817 1.00 72.74  ? 429 GLY A N     1 
ATOM   3549 C  CA    . GLY A 1 429 ? 6.750   34.673  -36.432 1.00 72.40  ? 429 GLY A CA    1 
ATOM   3550 C  C     . GLY A 1 429 ? 6.922   33.884  -35.151 1.00 66.26  ? 429 GLY A C     1 
ATOM   3551 O  O     . GLY A 1 429 ? 8.008   33.358  -34.891 1.00 66.47  ? 429 GLY A O     1 
ATOM   3552 N  N     . GLU A 1 430 ? 5.869   33.795  -34.338 1.00 61.87  ? 430 GLU A N     1 
ATOM   3553 C  CA    . GLU A 1 430 ? 5.914   33.067  -33.074 1.00 56.63  ? 430 GLU A CA    1 
ATOM   3554 C  C     . GLU A 1 430 ? 4.779   32.057  -33.033 1.00 68.28  ? 430 GLU A C     1 
ATOM   3555 O  O     . GLU A 1 430 ? 3.604   32.440  -33.034 1.00 71.60  ? 430 GLU A O     1 
ATOM   3556 C  CB    . GLU A 1 430 ? 5.827   34.021  -31.877 1.00 58.14  ? 430 GLU A CB    1 
ATOM   3557 C  CG    . GLU A 1 430 ? 5.989   33.321  -30.532 1.00 67.27  ? 430 GLU A CG    1 
ATOM   3558 C  CD    . GLU A 1 430 ? 6.216   34.288  -29.388 1.00 74.07  ? 430 GLU A CD    1 
ATOM   3559 O  OE1   . GLU A 1 430 ? 6.255   35.509  -29.641 1.00 91.83  ? 430 GLU A OE1   1 
ATOM   3560 O  OE2   . GLU A 1 430 ? 6.355   33.825  -28.236 1.00 83.02  ? 430 GLU A OE2   1 
ATOM   3561 N  N     . TYR A 1 431 ? 5.131   30.774  -32.993 1.00 62.87  ? 431 TYR A N     1 
ATOM   3562 C  CA    . TYR A 1 431 ? 4.171   29.682  -32.990 1.00 63.21  ? 431 TYR A CA    1 
ATOM   3563 C  C     . TYR A 1 431 ? 4.285   28.880  -31.701 1.00 63.05  ? 431 TYR A C     1 
ATOM   3564 O  O     . TYR A 1 431 ? 5.342   28.838  -31.065 1.00 64.05  ? 431 TYR A O     1 
ATOM   3565 C  CB    . TYR A 1 431 ? 4.387   28.738  -34.187 1.00 72.85  ? 431 TYR A CB    1 
ATOM   3566 C  CG    . TYR A 1 431 ? 3.914   29.281  -35.515 1.00 89.21  ? 431 TYR A CG    1 
ATOM   3567 C  CD1   . TYR A 1 431 ? 3.465   30.584  -35.631 1.00 83.91  ? 431 TYR A CD1   1 
ATOM   3568 C  CD2   . TYR A 1 431 ? 3.931   28.492  -36.659 1.00 102.10 ? 431 TYR A CD2   1 
ATOM   3569 C  CE1   . TYR A 1 431 ? 3.037   31.082  -36.835 1.00 78.65  ? 431 TYR A CE1   1 
ATOM   3570 C  CE2   . TYR A 1 431 ? 3.503   28.991  -37.879 1.00 103.13 ? 431 TYR A CE2   1 
ATOM   3571 C  CZ    . TYR A 1 431 ? 3.057   30.293  -37.956 1.00 84.83  ? 431 TYR A CZ    1 
ATOM   3572 O  OH    . TYR A 1 431 ? 2.625   30.820  -39.152 1.00 67.32  ? 431 TYR A OH    1 
ATOM   3573 N  N     . ASP A 1 432 ? 3.180   28.241  -31.324 1.00 65.49  ? 432 ASP A N     1 
ATOM   3574 C  CA    . ASP A 1 432 ? 3.165   27.251  -30.254 1.00 61.24  ? 432 ASP A CA    1 
ATOM   3575 C  C     . ASP A 1 432 ? 2.622   25.945  -30.812 1.00 59.72  ? 432 ASP A C     1 
ATOM   3576 O  O     . ASP A 1 432 ? 1.567   25.935  -31.454 1.00 64.91  ? 432 ASP A O     1 
ATOM   3577 C  CB    . ASP A 1 432 ? 2.327   27.721  -29.063 1.00 63.41  ? 432 ASP A CB    1 
ATOM   3578 C  CG    . ASP A 1 432 ? 3.155   28.454  -28.024 1.00 64.08  ? 432 ASP A CG    1 
ATOM   3579 O  OD1   . ASP A 1 432 ? 4.312   28.816  -28.331 1.00 67.38  ? 432 ASP A OD1   1 
ATOM   3580 O  OD2   . ASP A 1 432 ? 2.649   28.678  -26.904 1.00 60.77  ? 432 ASP A OD2   1 
ATOM   3581 N  N     . VAL A 1 433 ? 3.344   24.852  -30.576 1.00 61.39  ? 433 VAL A N     1 
ATOM   3582 C  CA    . VAL A 1 433 ? 3.026   23.547  -31.147 1.00 61.23  ? 433 VAL A CA    1 
ATOM   3583 C  C     . VAL A 1 433 ? 2.492   22.643  -30.046 1.00 63.16  ? 433 VAL A C     1 
ATOM   3584 O  O     . VAL A 1 433 ? 3.135   22.475  -29.002 1.00 59.55  ? 433 VAL A O     1 
ATOM   3585 C  CB    . VAL A 1 433 ? 4.253   22.914  -31.825 1.00 61.65  ? 433 VAL A CB    1 
ATOM   3586 C  CG1   . VAL A 1 433 ? 3.821   21.801  -32.765 1.00 65.14  ? 433 VAL A CG1   1 
ATOM   3587 C  CG2   . VAL A 1 433 ? 5.038   23.969  -32.577 1.00 63.31  ? 433 VAL A CG2   1 
ATOM   3588 N  N     . ALA A 1 434 ? 1.326   22.047  -30.291 1.00 59.92  ? 434 ALA A N     1 
ATOM   3589 C  CA    . ALA A 1 434 ? 0.679   21.187  -29.311 1.00 53.89  ? 434 ALA A CA    1 
ATOM   3590 C  C     . ALA A 1 434 ? 1.370   19.825  -29.254 1.00 57.00  ? 434 ALA A C     1 
ATOM   3591 O  O     . ALA A 1 434 ? 1.797   19.299  -30.286 1.00 58.43  ? 434 ALA A O     1 
ATOM   3592 C  CB    . ALA A 1 434 ? -0.794  21.001  -29.653 1.00 52.12  ? 434 ALA A CB    1 
ATOM   3593 N  N     . PRO A 1 435 ? 1.492   19.237  -28.065 1.00 57.90  ? 435 PRO A N     1 
ATOM   3594 C  CA    . PRO A 1 435 ? 2.091   17.902  -27.962 1.00 56.61  ? 435 PRO A CA    1 
ATOM   3595 C  C     . PRO A 1 435 ? 1.254   16.862  -28.691 1.00 68.43  ? 435 PRO A C     1 
ATOM   3596 O  O     . PRO A 1 435 ? 0.035   16.996  -28.824 1.00 59.39  ? 435 PRO A O     1 
ATOM   3597 C  CB    . PRO A 1 435 ? 2.120   17.636  -26.451 1.00 56.84  ? 435 PRO A CB    1 
ATOM   3598 C  CG    . PRO A 1 435 ? 1.169   18.629  -25.853 1.00 55.92  ? 435 PRO A CG    1 
ATOM   3599 C  CD    . PRO A 1 435 ? 1.191   19.820  -26.748 1.00 54.72  ? 435 PRO A CD    1 
ATOM   3600 N  N     . GLN A 1 436 ? 1.933   15.815  -29.168 1.00 57.14  ? 436 GLN A N     1 
ATOM   3601 C  CA    . GLN A 1 436 ? 1.312   14.681  -29.851 1.00 60.60  ? 436 GLN A CA    1 
ATOM   3602 C  C     . GLN A 1 436 ? 0.604   15.088  -31.141 1.00 66.09  ? 436 GLN A C     1 
ATOM   3603 O  O     . GLN A 1 436 ? 1.009   14.670  -32.231 1.00 63.85  ? 436 GLN A O     1 
ATOM   3604 C  CB    . GLN A 1 436 ? 0.327   13.957  -28.925 1.00 63.16  ? 436 GLN A CB    1 
ATOM   3605 C  CG    . GLN A 1 436 ? 0.844   13.708  -27.516 1.00 73.30  ? 436 GLN A CG    1 
ATOM   3606 C  CD    . GLN A 1 436 ? -0.167  12.987  -26.642 1.00 90.92  ? 436 GLN A CD    1 
ATOM   3607 O  OE1   . GLN A 1 436 ? -0.351  13.330  -25.474 1.00 80.94  ? 436 GLN A OE1   1 
ATOM   3608 N  NE2   . GLN A 1 436 ? -0.827  11.981  -27.205 1.00 85.49  ? 436 GLN A NE2   1 
ATOM   3609 N  N     . VAL A 1 437 ? -0.456  15.894  -31.030 1.00 59.32  ? 437 VAL A N     1 
ATOM   3610 C  CA    . VAL A 1 437 ? -1.279  16.199  -32.197 1.00 58.72  ? 437 VAL A CA    1 
ATOM   3611 C  C     . VAL A 1 437 ? -0.556  17.143  -33.152 1.00 63.34  ? 437 VAL A C     1 
ATOM   3612 O  O     . VAL A 1 437 ? -0.845  17.157  -34.355 1.00 66.95  ? 437 VAL A O     1 
ATOM   3613 C  CB    . VAL A 1 437 ? -2.638  16.769  -31.753 1.00 60.30  ? 437 VAL A CB    1 
ATOM   3614 C  CG1   . VAL A 1 437 ? -3.522  15.655  -31.211 1.00 56.77  ? 437 VAL A CG1   1 
ATOM   3615 C  CG2   . VAL A 1 437 ? -2.448  17.858  -30.710 1.00 56.54  ? 437 VAL A CG2   1 
ATOM   3616 N  N     . GLY A 1 438 ? 0.376   17.947  -32.645 1.00 59.67  ? 438 GLY A N     1 
ATOM   3617 C  CA    . GLY A 1 438 ? 1.243   18.746  -33.490 1.00 53.43  ? 438 GLY A CA    1 
ATOM   3618 C  C     . GLY A 1 438 ? 0.629   19.986  -34.101 1.00 63.78  ? 438 GLY A C     1 
ATOM   3619 O  O     . GLY A 1 438 ? 1.252   20.589  -34.982 1.00 63.61  ? 438 GLY A O     1 
ATOM   3620 N  N     . HIS A 1 439 ? -0.561  20.393  -33.668 1.00 55.60  ? 439 HIS A N     1 
ATOM   3621 C  CA    . HIS A 1 439 ? -1.173  21.598  -34.213 1.00 60.20  ? 439 HIS A CA    1 
ATOM   3622 C  C     . HIS A 1 439 ? -0.424  22.839  -33.742 1.00 58.69  ? 439 HIS A C     1 
ATOM   3623 O  O     . HIS A 1 439 ? -0.019  22.936  -32.580 1.00 56.63  ? 439 HIS A O     1 
ATOM   3624 C  CB    . HIS A 1 439 ? -2.643  21.684  -33.802 1.00 59.68  ? 439 HIS A CB    1 
ATOM   3625 C  CG    . HIS A 1 439 ? -3.439  20.468  -34.158 1.00 56.71  ? 439 HIS A CG    1 
ATOM   3626 N  ND1   . HIS A 1 439 ? -3.637  20.066  -35.461 1.00 56.37  ? 439 HIS A ND1   1 
ATOM   3627 C  CD2   . HIS A 1 439 ? -4.083  19.565  -33.383 1.00 50.60  ? 439 HIS A CD2   1 
ATOM   3628 C  CE1   . HIS A 1 439 ? -4.370  18.967  -35.474 1.00 57.37  ? 439 HIS A CE1   1 
ATOM   3629 N  NE2   . HIS A 1 439 ? -4.654  18.642  -34.226 1.00 56.26  ? 439 HIS A NE2   1 
ATOM   3630 N  N     . ARG A 1 440 ? -0.241  23.792  -34.653 1.00 55.29  ? 440 ARG A N     1 
ATOM   3631 C  CA    . ARG A 1 440 ? 0.482   25.023  -34.367 1.00 62.34  ? 440 ARG A CA    1 
ATOM   3632 C  C     . ARG A 1 440 ? -0.485  26.197  -34.296 1.00 54.49  ? 440 ARG A C     1 
ATOM   3633 O  O     . ARG A 1 440 ? -1.467  26.255  -35.042 1.00 64.35  ? 440 ARG A O     1 
ATOM   3634 C  CB    . ARG A 1 440 ? 1.554   25.300  -35.426 1.00 59.46  ? 440 ARG A CB    1 
ATOM   3635 C  CG    . ARG A 1 440 ? 1.961   24.088  -36.241 1.00 68.96  ? 440 ARG A CG    1 
ATOM   3636 C  CD    . ARG A 1 440 ? 3.067   24.439  -37.221 1.00 84.47  ? 440 ARG A CD    1 
ATOM   3637 N  NE    . ARG A 1 440 ? 4.388   24.197  -36.654 1.00 89.98  ? 440 ARG A NE    1 
ATOM   3638 C  CZ    . ARG A 1 440 ? 5.499   24.086  -37.369 1.00 97.15  ? 440 ARG A CZ    1 
ATOM   3639 N  NH1   . ARG A 1 440 ? 5.487   24.194  -38.687 1.00 106.81 ? 440 ARG A NH1   1 
ATOM   3640 N  NH2   . ARG A 1 440 ? 6.652   23.860  -36.745 1.00 102.90 ? 440 ARG A NH2   1 
ATOM   3641 N  N     . PHE A 1 441 ? -0.192  27.134  -33.399 1.00 58.21  ? 441 PHE A N     1 
ATOM   3642 C  CA    . PHE A 1 441 ? -1.028  28.306  -33.181 1.00 58.11  ? 441 PHE A CA    1 
ATOM   3643 C  C     . PHE A 1 441 ? -0.156  29.551  -33.175 1.00 58.44  ? 441 PHE A C     1 
ATOM   3644 O  O     . PHE A 1 441 ? 0.859   29.599  -32.470 1.00 60.93  ? 441 PHE A O     1 
ATOM   3645 C  CB    . PHE A 1 441 ? -1.805  28.189  -31.865 1.00 48.19  ? 441 PHE A CB    1 
ATOM   3646 C  CG    . PHE A 1 441 ? -2.645  26.947  -31.771 1.00 56.91  ? 441 PHE A CG    1 
ATOM   3647 C  CD1   . PHE A 1 441 ? -2.116  25.773  -31.262 1.00 55.98  ? 441 PHE A CD1   1 
ATOM   3648 C  CD2   . PHE A 1 441 ? -3.962  26.952  -32.200 1.00 59.27  ? 441 PHE A CD2   1 
ATOM   3649 C  CE1   . PHE A 1 441 ? -2.884  24.628  -31.178 1.00 56.30  ? 441 PHE A CE1   1 
ATOM   3650 C  CE2   . PHE A 1 441 ? -4.737  25.810  -32.119 1.00 57.94  ? 441 PHE A CE2   1 
ATOM   3651 C  CZ    . PHE A 1 441 ? -4.196  24.646  -31.607 1.00 60.32  ? 441 PHE A CZ    1 
ATOM   3652 N  N     . CYS A 1 442 ? -0.549  30.545  -33.970 1.00 56.17  ? 442 CYS A N     1 
ATOM   3653 C  CA    . CYS A 1 442 ? 0.177   31.806  -34.032 1.00 58.27  ? 442 CYS A CA    1 
ATOM   3654 C  C     . CYS A 1 442 ? -0.046  32.613  -32.760 1.00 60.99  ? 442 CYS A C     1 
ATOM   3655 O  O     . CYS A 1 442 ? -1.151  32.646  -32.209 1.00 56.26  ? 442 CYS A O     1 
ATOM   3656 C  CB    . CYS A 1 442 ? -0.266  32.613  -35.257 1.00 66.46  ? 442 CYS A CB    1 
ATOM   3657 S  SG    . CYS A 1 442 ? 0.075   34.399  -35.179 1.00 95.51  ? 442 CYS A SG    1 
ATOM   3658 N  N     . LYS A 1 443 ? 1.015   33.271  -32.292 1.00 58.04  ? 443 LYS A N     1 
ATOM   3659 C  CA    . LYS A 1 443 ? 0.956   34.069  -31.074 1.00 57.63  ? 443 LYS A CA    1 
ATOM   3660 C  C     . LYS A 1 443 ? 1.158   35.555  -31.333 1.00 57.49  ? 443 LYS A C     1 
ATOM   3661 O  O     . LYS A 1 443 ? 1.243   36.332  -30.374 1.00 63.50  ? 443 LYS A O     1 
ATOM   3662 C  CB    . LYS A 1 443 ? 1.993   33.576  -30.064 1.00 63.78  ? 443 LYS A CB    1 
ATOM   3663 C  CG    . LYS A 1 443 ? 2.066   32.070  -29.950 1.00 60.28  ? 443 LYS A CG    1 
ATOM   3664 C  CD    . LYS A 1 443 ? 2.540   31.659  -28.572 1.00 64.19  ? 443 LYS A CD    1 
ATOM   3665 C  CE    . LYS A 1 443 ? 1.535   32.033  -27.499 1.00 53.87  ? 443 LYS A CE    1 
ATOM   3666 N  NZ    . LYS A 1 443 ? 2.215   32.323  -26.207 1.00 66.47  ? 443 LYS A NZ    1 
ATOM   3667 N  N     . ASP A 1 444 ? 1.244   35.973  -32.597 1.00 59.88  ? 444 ASP A N     1 
ATOM   3668 C  CA    . ASP A 1 444 ? 1.439   37.388  -32.891 1.00 66.35  ? 444 ASP A CA    1 
ATOM   3669 C  C     . ASP A 1 444 ? 0.223   38.205  -32.475 1.00 67.09  ? 444 ASP A C     1 
ATOM   3670 O  O     . ASP A 1 444 ? 0.350   39.215  -31.774 1.00 73.80  ? 444 ASP A O     1 
ATOM   3671 C  CB    . ASP A 1 444 ? 1.739   37.580  -34.378 1.00 73.13  ? 444 ASP A CB    1 
ATOM   3672 C  CG    . ASP A 1 444 ? 3.028   36.902  -34.806 1.00 72.96  ? 444 ASP A CG    1 
ATOM   3673 O  OD1   . ASP A 1 444 ? 3.645   36.205  -33.971 1.00 67.75  ? 444 ASP A OD1   1 
ATOM   3674 O  OD2   . ASP A 1 444 ? 3.426   37.070  -35.976 1.00 77.54  ? 444 ASP A OD2   1 
ATOM   3675 N  N     . LEU A 1 445 ? -0.965  37.780  -32.894 1.00 69.79  ? 445 LEU A N     1 
ATOM   3676 C  CA    . LEU A 1 445 ? -2.198  38.450  -32.526 1.00 68.83  ? 445 LEU A CA    1 
ATOM   3677 C  C     . LEU A 1 445 ? -3.001  37.568  -31.585 1.00 58.73  ? 445 LEU A C     1 
ATOM   3678 O  O     . LEU A 1 445 ? -3.144  36.366  -31.847 1.00 57.09  ? 445 LEU A O     1 
ATOM   3679 C  CB    . LEU A 1 445 ? -3.031  38.782  -33.769 1.00 74.26  ? 445 LEU A CB    1 
ATOM   3680 C  CG    . LEU A 1 445 ? -2.557  39.965  -34.620 1.00 88.31  ? 445 LEU A CG    1 
ATOM   3681 C  CD1   . LEU A 1 445 ? -2.071  41.110  -33.739 1.00 76.39  ? 445 LEU A CD1   1 
ATOM   3682 C  CD2   . LEU A 1 445 ? -1.474  39.540  -35.608 1.00 83.61  ? 445 LEU A CD2   1 
ATOM   3683 N  N     . PRO A 1 446 ? -3.525  38.114  -30.490 1.00 61.89  ? 446 PRO A N     1 
ATOM   3684 C  CA    . PRO A 1 446 ? -4.317  37.292  -29.567 1.00 59.83  ? 446 PRO A CA    1 
ATOM   3685 C  C     . PRO A 1 446 ? -5.606  36.815  -30.220 1.00 50.39  ? 446 PRO A C     1 
ATOM   3686 O  O     . PRO A 1 446 ? -6.259  37.552  -30.961 1.00 56.69  ? 446 PRO A O     1 
ATOM   3687 C  CB    . PRO A 1 446 ? -4.599  38.240  -28.395 1.00 53.25  ? 446 PRO A CB    1 
ATOM   3688 C  CG    . PRO A 1 446 ? -4.462  39.611  -28.975 1.00 54.51  ? 446 PRO A CG    1 
ATOM   3689 C  CD    . PRO A 1 446 ? -3.408  39.510  -30.036 1.00 60.41  ? 446 PRO A CD    1 
ATOM   3690 N  N     . GLY A 1 447 ? -5.965  35.562  -29.936 1.00 47.97  ? 447 GLY A N     1 
ATOM   3691 C  CA    . GLY A 1 447 ? -7.134  34.973  -30.549 1.00 56.95  ? 447 GLY A CA    1 
ATOM   3692 C  C     . GLY A 1 447 ? -8.436  35.398  -29.892 1.00 41.15  ? 447 GLY A C     1 
ATOM   3693 O  O     . GLY A 1 447 ? -8.474  35.897  -28.769 1.00 41.92  ? 447 GLY A O     1 
ATOM   3694 N  N     . PHE A 1 448 ? -9.523  35.181  -30.632 1.00 46.73  ? 448 PHE A N     1 
ATOM   3695 C  CA    . PHE A 1 448 ? -10.863 35.508  -30.150 1.00 44.79  ? 448 PHE A CA    1 
ATOM   3696 C  C     . PHE A 1 448 ? -11.163 34.795  -28.834 1.00 47.57  ? 448 PHE A C     1 
ATOM   3697 O  O     . PHE A 1 448 ? -11.365 35.432  -27.786 1.00 43.84  ? 448 PHE A O     1 
ATOM   3698 C  CB    . PHE A 1 448 ? -11.872 35.125  -31.236 1.00 48.62  ? 448 PHE A CB    1 
ATOM   3699 C  CG    . PHE A 1 448 ? -13.294 35.475  -30.917 1.00 56.77  ? 448 PHE A CG    1 
ATOM   3700 C  CD1   . PHE A 1 448 ? -13.636 36.741  -30.476 1.00 60.98  ? 448 PHE A CD1   1 
ATOM   3701 C  CD2   . PHE A 1 448 ? -14.298 34.535  -31.090 1.00 48.00  ? 448 PHE A CD2   1 
ATOM   3702 C  CE1   . PHE A 1 448 ? -14.954 37.058  -30.198 1.00 58.60  ? 448 PHE A CE1   1 
ATOM   3703 C  CE2   . PHE A 1 448 ? -15.614 34.845  -30.814 1.00 50.46  ? 448 PHE A CE2   1 
ATOM   3704 C  CZ    . PHE A 1 448 ? -15.944 36.107  -30.368 1.00 49.17  ? 448 PHE A CZ    1 
ATOM   3705 N  N     . ILE A 1 449 ? -11.175 33.459  -28.877 1.00 43.37  ? 449 ILE A N     1 
ATOM   3706 C  CA    . ILE A 1 449 ? -11.468 32.680  -27.674 1.00 44.59  ? 449 ILE A CA    1 
ATOM   3707 C  C     . ILE A 1 449 ? -10.499 32.974  -26.540 1.00 48.71  ? 449 ILE A C     1 
ATOM   3708 O  O     . ILE A 1 449 ? -10.957 33.125  -25.391 1.00 45.33  ? 449 ILE A O     1 
ATOM   3709 C  CB    . ILE A 1 449 ? -11.526 31.176  -28.027 1.00 44.86  ? 449 ILE A CB    1 
ATOM   3710 C  CG1   . ILE A 1 449 ? -12.512 30.934  -29.171 1.00 47.12  ? 449 ILE A CG1   1 
ATOM   3711 C  CG2   . ILE A 1 449 ? -11.892 30.355  -26.802 1.00 36.11  ? 449 ILE A CG2   1 
ATOM   3712 C  CD1   . ILE A 1 449 ? -13.949 31.232  -28.811 1.00 47.05  ? 449 ILE A CD1   1 
ATOM   3713 N  N     . PRO A 1 450 ? -9.173  33.041  -26.753 1.00 46.23  ? 450 PRO A N     1 
ATOM   3714 C  CA    . PRO A 1 450 ? -8.290  33.406  -25.632 1.00 44.50  ? 450 PRO A CA    1 
ATOM   3715 C  C     . PRO A 1 450 ? -8.623  34.752  -25.021 1.00 38.87  ? 450 PRO A C     1 
ATOM   3716 O  O     . PRO A 1 450 ? -8.561  34.893  -23.796 1.00 42.23  ? 450 PRO A O     1 
ATOM   3717 C  CB    . PRO A 1 450 ? -6.883  33.407  -26.251 1.00 41.16  ? 450 PRO A CB    1 
ATOM   3718 C  CG    . PRO A 1 450 ? -6.988  32.736  -27.548 1.00 42.77  ? 450 PRO A CG    1 
ATOM   3719 C  CD    . PRO A 1 450 ? -8.417  32.558  -27.926 1.00 47.20  ? 450 PRO A CD    1 
ATOM   3720 N  N     . SER A 1 451 ? -8.983  35.747  -25.835 1.00 37.45  ? 451 SER A N     1 
ATOM   3721 C  CA    . SER A 1 451 ? -9.308  37.063  -25.289 1.00 42.07  ? 451 SER A CA    1 
ATOM   3722 C  C     . SER A 1 451 ? -10.543 36.996  -24.400 1.00 48.94  ? 451 SER A C     1 
ATOM   3723 O  O     . SER A 1 451 ? -10.535 37.493  -23.260 1.00 49.36  ? 451 SER A O     1 
ATOM   3724 C  CB    . SER A 1 451 ? -9.513  38.067  -26.423 1.00 46.59  ? 451 SER A CB    1 
ATOM   3725 O  OG    . SER A 1 451 ? -8.629  37.811  -27.500 1.00 61.88  ? 451 SER A OG    1 
ATOM   3726 N  N     . LEU A 1 452 ? -11.623 36.387  -24.907 1.00 47.09  ? 452 LEU A N     1 
ATOM   3727 C  CA    . LEU A 1 452 ? -12.832 36.272  -24.093 1.00 45.70  ? 452 LEU A CA    1 
ATOM   3728 C  C     . LEU A 1 452 ? -12.563 35.490  -22.812 1.00 46.28  ? 452 LEU A C     1 
ATOM   3729 O  O     . LEU A 1 452 ? -13.009 35.888  -21.727 1.00 48.51  ? 452 LEU A O     1 
ATOM   3730 C  CB    . LEU A 1 452 ? -13.962 35.618  -24.891 1.00 42.16  ? 452 LEU A CB    1 
ATOM   3731 C  CG    . LEU A 1 452 ? -14.007 35.925  -26.386 1.00 48.70  ? 452 LEU A CG    1 
ATOM   3732 C  CD1   . LEU A 1 452 ? -14.865 34.917  -27.133 1.00 47.60  ? 452 LEU A CD1   1 
ATOM   3733 C  CD2   . LEU A 1 452 ? -14.483 37.343  -26.630 1.00 57.04  ? 452 LEU A CD2   1 
ATOM   3734 N  N     . LEU A 1 453 ? -11.815 34.387  -22.914 1.00 41.88  ? 453 LEU A N     1 
ATOM   3735 C  CA    . LEU A 1 453 ? -11.547 33.565  -21.739 1.00 42.19  ? 453 LEU A CA    1 
ATOM   3736 C  C     . LEU A 1 453 ? -10.684 34.306  -20.726 1.00 45.81  ? 453 LEU A C     1 
ATOM   3737 O  O     . LEU A 1 453 ? -10.877 34.157  -19.515 1.00 44.75  ? 453 LEU A O     1 
ATOM   3738 C  CB    . LEU A 1 453 ? -10.877 32.258  -22.159 1.00 41.01  ? 453 LEU A CB    1 
ATOM   3739 C  CG    . LEU A 1 453 ? -11.794 31.180  -22.732 1.00 46.27  ? 453 LEU A CG    1 
ATOM   3740 C  CD1   . LEU A 1 453 ? -11.110 29.829  -22.656 1.00 42.00  ? 453 LEU A CD1   1 
ATOM   3741 C  CD2   . LEU A 1 453 ? -13.132 31.154  -22.002 1.00 46.23  ? 453 LEU A CD2   1 
ATOM   3742 N  N     . GLY A 1 454 ? -9.722  35.101  -21.198 1.00 45.04  ? 454 GLY A N     1 
ATOM   3743 C  CA    . GLY A 1 454 ? -8.907  35.876  -20.280 1.00 38.91  ? 454 GLY A CA    1 
ATOM   3744 C  C     . GLY A 1 454 ? -9.725  36.901  -19.524 1.00 46.92  ? 454 GLY A C     1 
ATOM   3745 O  O     . GLY A 1 454 ? -9.604  37.034  -18.302 1.00 47.90  ? 454 GLY A O     1 
ATOM   3746 N  N     . ASP A 1 455 ? -10.578 37.639  -20.244 1.00 50.42  ? 455 ASP A N     1 
ATOM   3747 C  CA    . ASP A 1 455 ? -11.479 38.569  -19.566 1.00 52.64  ? 455 ASP A CA    1 
ATOM   3748 C  C     . ASP A 1 455 ? -12.340 37.846  -18.536 1.00 49.34  ? 455 ASP A C     1 
ATOM   3749 O  O     . ASP A 1 455 ? -12.516 38.329  -17.409 1.00 55.91  ? 455 ASP A O     1 
ATOM   3750 C  CB    . ASP A 1 455 ? -12.357 39.297  -20.583 1.00 59.79  ? 455 ASP A CB    1 
ATOM   3751 C  CG    . ASP A 1 455 ? -11.567 40.244  -21.461 1.00 64.79  ? 455 ASP A CG    1 
ATOM   3752 O  OD1   . ASP A 1 455 ? -10.540 40.776  -20.988 1.00 88.26  ? 455 ASP A OD1   1 
ATOM   3753 O  OD2   . ASP A 1 455 ? -11.975 40.460  -22.621 1.00 70.72  ? 455 ASP A OD2   1 
ATOM   3754 N  N     . LEU A 1 456 ? -12.864 36.671  -18.898 1.00 46.57  ? 456 LEU A N     1 
ATOM   3755 C  CA    . LEU A 1 456 ? -13.757 35.946  -17.999 1.00 48.68  ? 456 LEU A CA    1 
ATOM   3756 C  C     . LEU A 1 456 ? -13.026 35.474  -16.745 1.00 49.19  ? 456 LEU A C     1 
ATOM   3757 O  O     . LEU A 1 456 ? -13.540 35.609  -15.629 1.00 50.18  ? 456 LEU A O     1 
ATOM   3758 C  CB    . LEU A 1 456 ? -14.391 34.765  -18.735 1.00 47.04  ? 456 LEU A CB    1 
ATOM   3759 C  CG    . LEU A 1 456 ? -15.833 34.957  -19.208 1.00 49.83  ? 456 LEU A CG    1 
ATOM   3760 C  CD1   . LEU A 1 456 ? -15.978 36.255  -19.984 1.00 57.54  ? 456 LEU A CD1   1 
ATOM   3761 C  CD2   . LEU A 1 456 ? -16.272 33.775  -20.055 1.00 48.70  ? 456 LEU A CD2   1 
ATOM   3762 N  N     . LEU A 1 457 ? -11.827 34.910  -16.908 1.00 46.91  ? 457 LEU A N     1 
ATOM   3763 C  CA    . LEU A 1 457 ? -11.075 34.438  -15.748 1.00 49.72  ? 457 LEU A CA    1 
ATOM   3764 C  C     . LEU A 1 457 ? -10.641 35.600  -14.862 1.00 50.23  ? 457 LEU A C     1 
ATOM   3765 O  O     . LEU A 1 457 ? -10.634 35.480  -13.630 1.00 49.23  ? 457 LEU A O     1 
ATOM   3766 C  CB    . LEU A 1 457 ? -9.865  33.618  -16.195 1.00 47.23  ? 457 LEU A CB    1 
ATOM   3767 C  CG    . LEU A 1 457 ? -10.140 32.303  -16.930 1.00 50.53  ? 457 LEU A CG    1 
ATOM   3768 C  CD1   . LEU A 1 457 ? -8.867  31.479  -17.044 1.00 46.76  ? 457 LEU A CD1   1 
ATOM   3769 C  CD2   . LEU A 1 457 ? -11.236 31.504  -16.239 1.00 48.39  ? 457 LEU A CD2   1 
ATOM   3770 N  N     . GLU A 1 458 ? -10.292 36.739  -15.467 1.00 48.92  ? 458 GLU A N     1 
ATOM   3771 C  CA    . GLU A 1 458 ? -9.959  37.920  -14.676 1.00 55.93  ? 458 GLU A CA    1 
ATOM   3772 C  C     . GLU A 1 458 ? -11.153 38.369  -13.843 1.00 59.27  ? 458 GLU A C     1 
ATOM   3773 O  O     . GLU A 1 458 ? -11.021 38.660  -12.645 1.00 60.28  ? 458 GLU A O     1 
ATOM   3774 C  CB    . GLU A 1 458 ? -9.485  39.040  -15.601 1.00 59.36  ? 458 GLU A CB    1 
ATOM   3775 C  CG    . GLU A 1 458 ? -8.893  40.241  -14.887 1.00 76.98  ? 458 GLU A CG    1 
ATOM   3776 C  CD    . GLU A 1 458 ? -8.335  41.264  -15.856 1.00 97.81  ? 458 GLU A CD    1 
ATOM   3777 O  OE1   . GLU A 1 458 ? -8.454  41.046  -17.081 1.00 96.53  ? 458 GLU A OE1   1 
ATOM   3778 O  OE2   . GLU A 1 458 ? -7.781  42.284  -15.395 1.00 102.48 ? 458 GLU A OE2   1 
ATOM   3779 N  N     . GLU A 1 459 ? -12.336 38.420  -14.462 1.00 62.21  ? 459 GLU A N     1 
ATOM   3780 C  CA    . GLU A 1 459 ? -13.535 38.812  -13.727 1.00 61.05  ? 459 GLU A CA    1 
ATOM   3781 C  C     . GLU A 1 459 ? -13.850 37.820  -12.612 1.00 55.93  ? 459 GLU A C     1 
ATOM   3782 O  O     . GLU A 1 459 ? -14.230 38.219  -11.505 1.00 56.23  ? 459 GLU A O     1 
ATOM   3783 C  CB    . GLU A 1 459 ? -14.719 38.942  -14.686 1.00 65.37  ? 459 GLU A CB    1 
ATOM   3784 C  CG    . GLU A 1 459 ? -16.023 39.356  -14.019 1.00 69.82  ? 459 GLU A CG    1 
ATOM   3785 C  CD    . GLU A 1 459 ? -16.099 40.849  -13.750 1.00 91.26  ? 459 GLU A CD    1 
ATOM   3786 O  OE1   . GLU A 1 459 ? -15.189 41.586  -14.189 1.00 92.63  ? 459 GLU A OE1   1 
ATOM   3787 O  OE2   . GLU A 1 459 ? -17.071 41.285  -13.098 1.00 95.13  ? 459 GLU A OE2   1 
ATOM   3788 N  N     . ARG A 1 460 ? -13.693 36.521  -12.885 1.00 49.69  ? 460 ARG A N     1 
ATOM   3789 C  CA    . ARG A 1 460 ? -13.958 35.513  -11.862 1.00 52.55  ? 460 ARG A CA    1 
ATOM   3790 C  C     . ARG A 1 460 ? -13.006 35.661  -10.682 1.00 64.27  ? 460 ARG A C     1 
ATOM   3791 O  O     . ARG A 1 460 ? -13.419 35.531  -9.522  1.00 66.58  ? 460 ARG A O     1 
ATOM   3792 C  CB    . ARG A 1 460 ? -13.849 34.112  -12.463 1.00 58.26  ? 460 ARG A CB    1 
ATOM   3793 C  CG    . ARG A 1 460 ? -13.840 32.993  -11.431 1.00 60.70  ? 460 ARG A CG    1 
ATOM   3794 C  CD    . ARG A 1 460 ? -14.686 31.814  -11.880 1.00 59.32  ? 460 ARG A CD    1 
ATOM   3795 N  NE    . ARG A 1 460 ? -14.905 30.859  -10.800 1.00 64.88  ? 460 ARG A NE    1 
ATOM   3796 C  CZ    . ARG A 1 460 ? -14.224 29.732  -10.645 1.00 66.12  ? 460 ARG A CZ    1 
ATOM   3797 N  NH1   . ARG A 1 460 ? -13.271 29.378  -11.492 1.00 71.12  ? 460 ARG A NH1   1 
ATOM   3798 N  NH2   . ARG A 1 460 ? -14.506 28.940  -9.615  1.00 64.30  ? 460 ARG A NH2   1 
ATOM   3799 N  N     . GLN A 1 461 ? -11.726 35.928  -10.954 1.00 65.18  ? 461 GLN A N     1 
ATOM   3800 C  CA    . GLN A 1 461 ? -10.779 36.128  -9.863  1.00 64.73  ? 461 GLN A CA    1 
ATOM   3801 C  C     . GLN A 1 461 ? -11.121 37.376  -9.059  1.00 62.34  ? 461 GLN A C     1 
ATOM   3802 O  O     . GLN A 1 461 ? -11.033 37.367  -7.825  1.00 71.49  ? 461 GLN A O     1 
ATOM   3803 C  CB    . GLN A 1 461 ? -9.353  36.203  -10.407 1.00 73.37  ? 461 GLN A CB    1 
ATOM   3804 C  CG    . GLN A 1 461 ? -8.710  34.841  -10.621 1.00 79.48  ? 461 GLN A CG    1 
ATOM   3805 C  CD    . GLN A 1 461 ? -8.745  33.977  -9.373  1.00 82.69  ? 461 GLN A CD    1 
ATOM   3806 O  OE1   . GLN A 1 461 ? -8.365  34.417  -8.287  1.00 88.75  ? 461 GLN A OE1   1 
ATOM   3807 N  NE2   . GLN A 1 461 ? -9.206  32.740  -9.522  1.00 74.33  ? 461 GLN A NE2   1 
ATOM   3808 N  N     . LYS A 1 462 ? -11.526 38.456  -9.736  1.00 63.09  ? 462 LYS A N     1 
ATOM   3809 C  CA    . LYS A 1 462 ? -11.964 39.652  -9.019  1.00 67.56  ? 462 LYS A CA    1 
ATOM   3810 C  C     . LYS A 1 462 ? -13.167 39.355  -8.129  1.00 71.48  ? 462 LYS A C     1 
ATOM   3811 O  O     . LYS A 1 462 ? -13.261 39.861  -7.002  1.00 76.29  ? 462 LYS A O     1 
ATOM   3812 C  CB    . LYS A 1 462 ? -12.301 40.766  -10.011 1.00 68.22  ? 462 LYS A CB    1 
ATOM   3813 C  CG    . LYS A 1 462 ? -11.111 41.602  -10.445 1.00 74.19  ? 462 LYS A CG    1 
ATOM   3814 C  CD    . LYS A 1 462 ? -11.211 41.970  -11.917 1.00 80.18  ? 462 LYS A CD    1 
ATOM   3815 C  CE    . LYS A 1 462 ? -11.749 43.380  -12.099 1.00 96.92  ? 462 LYS A CE    1 
ATOM   3816 N  NZ    . LYS A 1 462 ? -11.708 43.815  -13.523 1.00 90.51  ? 462 LYS A NZ    1 
ATOM   3817 N  N     . ILE A 1 463 ? -14.095 38.531  -8.620  1.00 72.30  ? 463 ILE A N     1 
ATOM   3818 C  CA    . ILE A 1 463 ? -15.287 38.195  -7.846  1.00 68.80  ? 463 ILE A CA    1 
ATOM   3819 C  C     . ILE A 1 463 ? -14.910 37.380  -6.614  1.00 74.40  ? 463 ILE A C     1 
ATOM   3820 O  O     . ILE A 1 463 ? -15.384 37.647  -5.503  1.00 80.33  ? 463 ILE A O     1 
ATOM   3821 C  CB    . ILE A 1 463 ? -16.304 37.449  -8.728  1.00 68.23  ? 463 ILE A CB    1 
ATOM   3822 C  CG1   . ILE A 1 463 ? -17.101 38.439  -9.579  1.00 69.10  ? 463 ILE A CG1   1 
ATOM   3823 C  CG2   . ILE A 1 463 ? -17.239 36.610  -7.878  1.00 60.79  ? 463 ILE A CG2   1 
ATOM   3824 C  CD1   . ILE A 1 463 ? -17.896 37.781  -10.683 1.00 70.15  ? 463 ILE A CD1   1 
ATOM   3825 N  N     . LYS A 1 464 ? -14.059 36.366  -6.795  1.00 71.25  ? 464 LYS A N     1 
ATOM   3826 C  CA    . LYS A 1 464 ? -13.614 35.569  -5.654  1.00 74.75  ? 464 LYS A CA    1 
ATOM   3827 C  C     . LYS A 1 464 ? -12.839 36.412  -4.650  1.00 82.21  ? 464 LYS A C     1 
ATOM   3828 O  O     . LYS A 1 464 ? -12.903 36.151  -3.442  1.00 92.28  ? 464 LYS A O     1 
ATOM   3829 C  CB    . LYS A 1 464 ? -12.764 34.388  -6.126  1.00 67.45  ? 464 LYS A CB    1 
ATOM   3830 C  CG    . LYS A 1 464 ? -13.432 33.521  -7.179  1.00 69.20  ? 464 LYS A CG    1 
ATOM   3831 C  CD    . LYS A 1 464 ? -12.551 32.350  -7.585  1.00 64.06  ? 464 LYS A CD    1 
ATOM   3832 C  CE    . LYS A 1 464 ? -12.905 31.096  -6.799  1.00 75.07  ? 464 LYS A CE    1 
ATOM   3833 N  NZ    . LYS A 1 464 ? -11.806 30.089  -6.821  1.00 74.57  ? 464 LYS A NZ    1 
ATOM   3834 N  N     . LYS A 1 465 ? -12.108 37.423  -5.124  1.00 77.80  ? 465 LYS A N     1 
ATOM   3835 C  CA    . LYS A 1 465 ? -11.413 38.326  -4.213  1.00 86.20  ? 465 LYS A CA    1 
ATOM   3836 C  C     . LYS A 1 465 ? -12.402 39.148  -3.397  1.00 91.80  ? 465 LYS A C     1 
ATOM   3837 O  O     . LYS A 1 465 ? -12.301 39.218  -2.166  1.00 96.09  ? 465 LYS A O     1 
ATOM   3838 C  CB    . LYS A 1 465 ? -10.471 39.240  -4.998  1.00 84.48  ? 465 LYS A CB    1 
ATOM   3839 C  CG    . LYS A 1 465 ? -9.611  40.142  -4.128  1.00 79.55  ? 465 LYS A CG    1 
ATOM   3840 C  CD    . LYS A 1 465 ? -8.231  40.346  -4.734  1.00 84.66  ? 465 LYS A CD    1 
ATOM   3841 C  CE    . LYS A 1 465 ? -7.465  41.443  -4.008  1.00 80.65  ? 465 LYS A CE    1 
ATOM   3842 N  NZ    . LYS A 1 465 ? -7.227  41.107  -2.577  1.00 77.11  ? 465 LYS A NZ    1 
ATOM   3843 N  N     . LYS A 1 466 ? -13.369 39.782  -4.068  1.00 94.75  ? 466 LYS A N     1 
ATOM   3844 C  CA    . LYS A 1 466 ? -14.362 40.582  -3.359  1.00 96.54  ? 466 LYS A CA    1 
ATOM   3845 C  C     . LYS A 1 466 ? -15.248 39.742  -2.448  1.00 103.95 ? 466 LYS A C     1 
ATOM   3846 O  O     . LYS A 1 466 ? -15.841 40.287  -1.511  1.00 111.61 ? 466 LYS A O     1 
ATOM   3847 C  CB    . LYS A 1 466 ? -15.231 41.359  -4.349  1.00 90.26  ? 466 LYS A CB    1 
ATOM   3848 C  CG    . LYS A 1 466 ? -14.487 42.441  -5.108  1.00 92.77  ? 466 LYS A CG    1 
ATOM   3849 C  CD    . LYS A 1 466 ? -15.448 43.480  -5.662  1.00 101.78 ? 466 LYS A CD    1 
ATOM   3850 C  CE    . LYS A 1 466 ? -16.165 44.221  -4.542  1.00 97.07  ? 466 LYS A CE    1 
ATOM   3851 N  NZ    . LYS A 1 466 ? -16.783 45.493  -5.012  1.00 88.59  ? 466 LYS A NZ    1 
ATOM   3852 N  N     . MET A 1 467 ? -15.354 38.434  -2.702  1.00 102.67 ? 467 MET A N     1 
ATOM   3853 C  CA    . MET A 1 467 ? -16.163 37.578  -1.838  1.00 120.66 ? 467 MET A CA    1 
ATOM   3854 C  C     . MET A 1 467 ? -15.604 37.507  -0.422  1.00 117.45 ? 467 MET A C     1 
ATOM   3855 O  O     . MET A 1 467 ? -16.365 37.333  0.537   1.00 120.90 ? 467 MET A O     1 
ATOM   3856 C  CB    . MET A 1 467 ? -16.262 36.173  -2.431  1.00 107.08 ? 467 MET A CB    1 
ATOM   3857 C  CG    . MET A 1 467 ? -17.611 35.846  -3.048  1.00 94.19  ? 467 MET A CG    1 
ATOM   3858 S  SD    . MET A 1 467 ? -17.593 34.279  -3.943  1.00 105.05 ? 467 MET A SD    1 
ATOM   3859 C  CE    . MET A 1 467 ? -16.719 33.233  -2.782  1.00 97.68  ? 467 MET A CE    1 
ATOM   3860 N  N     . LYS A 1 468 ? -14.283 37.633  -0.268  1.00 113.81 ? 468 LYS A N     1 
ATOM   3861 C  CA    . LYS A 1 468 ? -13.683 37.531  1.058   1.00 109.67 ? 468 LYS A CA    1 
ATOM   3862 C  C     . LYS A 1 468 ? -14.008 38.751  1.912   1.00 110.91 ? 468 LYS A C     1 
ATOM   3863 O  O     . LYS A 1 468 ? -14.192 38.633  3.128   1.00 109.92 ? 468 LYS A O     1 
ATOM   3864 C  CB    . LYS A 1 468 ? -12.170 37.346  0.936   1.00 106.01 ? 468 LYS A CB    1 
ATOM   3865 C  CG    . LYS A 1 468 ? -11.732 35.962  0.466   1.00 109.59 ? 468 LYS A CG    1 
ATOM   3866 C  CD    . LYS A 1 468 ? -12.790 34.900  0.738   1.00 113.23 ? 468 LYS A CD    1 
ATOM   3867 C  CE    . LYS A 1 468 ? -12.203 33.500  0.658   1.00 114.02 ? 468 LYS A CE    1 
ATOM   3868 N  NZ    . LYS A 1 468 ? -11.795 33.146  -0.730  1.00 106.96 ? 468 LYS A NZ    1 
ATOM   3869 N  N     . ALA A 1 469 ? -14.082 39.928  1.295   1.00 113.20 ? 469 ALA A N     1 
ATOM   3870 C  CA    . ALA A 1 469 ? -14.407 41.159  2.002   1.00 116.10 ? 469 ALA A CA    1 
ATOM   3871 C  C     . ALA A 1 469 ? -15.896 41.477  1.991   1.00 126.42 ? 469 ALA A C     1 
ATOM   3872 O  O     . ALA A 1 469 ? -16.299 42.504  2.548   1.00 125.54 ? 469 ALA A O     1 
ATOM   3873 C  CB    . ALA A 1 469 ? -13.627 42.333  1.401   1.00 102.12 ? 469 ALA A CB    1 
ATOM   3874 N  N     . THR A 1 470 ? -16.719 40.627  1.380   1.00 143.16 ? 470 THR A N     1 
ATOM   3875 C  CA    . THR A 1 470 ? -18.149 40.893  1.287   1.00 141.33 ? 470 THR A CA    1 
ATOM   3876 C  C     . THR A 1 470 ? -18.810 40.752  2.653   1.00 140.36 ? 470 THR A C     1 
ATOM   3877 O  O     . THR A 1 470 ? -18.668 39.723  3.322   1.00 145.13 ? 470 THR A O     1 
ATOM   3878 C  CB    . THR A 1 470 ? -18.799 39.940  0.284   1.00 136.56 ? 470 THR A CB    1 
ATOM   3879 O  OG1   . THR A 1 470 ? -18.269 40.185  -1.024  1.00 148.20 ? 470 THR A OG1   1 
ATOM   3880 C  CG2   . THR A 1 470 ? -20.306 40.141  0.258   1.00 129.96 ? 470 THR A CG2   1 
ATOM   3881 N  N     . ILE A 1 471 ? -19.538 41.790  3.064   1.00 128.54 ? 471 ILE A N     1 
ATOM   3882 C  CA    . ILE A 1 471 ? -20.202 41.809  4.363   1.00 128.87 ? 471 ILE A CA    1 
ATOM   3883 C  C     . ILE A 1 471 ? -21.605 41.230  4.230   1.00 130.06 ? 471 ILE A C     1 
ATOM   3884 O  O     . ILE A 1 471 ? -21.916 40.188  4.816   1.00 127.18 ? 471 ILE A O     1 
ATOM   3885 C  CB    . ILE A 1 471 ? -20.249 43.235  4.941   1.00 124.34 ? 471 ILE A CB    1 
ATOM   3886 C  CG1   . ILE A 1 471 ? -18.834 43.802  5.078   1.00 118.91 ? 471 ILE A CG1   1 
ATOM   3887 C  CG2   . ILE A 1 471 ? -20.965 43.244  6.282   1.00 122.13 ? 471 ILE A CG2   1 
ATOM   3888 C  CD1   . ILE A 1 471 ? -18.795 45.301  5.282   1.00 110.70 ? 471 ILE A CD1   1 
ATOM   3889 N  N     . ASP A 1 472 ? -22.459 41.912  3.466   1.00 122.34 ? 472 ASP A N     1 
ATOM   3890 C  CA    . ASP A 1 472 ? -23.828 41.484  3.206   1.00 116.49 ? 472 ASP A CA    1 
ATOM   3891 C  C     . ASP A 1 472 ? -23.831 40.070  2.636   1.00 118.89 ? 472 ASP A C     1 
ATOM   3892 O  O     . ASP A 1 472 ? -23.364 39.852  1.511   1.00 117.75 ? 472 ASP A O     1 
ATOM   3893 C  CB    . ASP A 1 472 ? -24.506 42.470  2.252   1.00 108.04 ? 472 ASP A CB    1 
ATOM   3894 C  CG    . ASP A 1 472 ? -25.979 42.172  2.037   1.00 117.02 ? 472 ASP A CG    1 
ATOM   3895 O  OD1   . ASP A 1 472 ? -26.524 41.273  2.710   1.00 121.22 ? 472 ASP A OD1   1 
ATOM   3896 O  OD2   . ASP A 1 472 ? -26.592 42.839  1.177   1.00 117.41 ? 472 ASP A OD2   1 
ATOM   3897 N  N     . PRO A 1 473 ? -24.343 39.085  3.382   1.00 122.82 ? 473 PRO A N     1 
ATOM   3898 C  CA    . PRO A 1 473 ? -24.264 37.693  2.907   1.00 121.98 ? 473 PRO A CA    1 
ATOM   3899 C  C     . PRO A 1 473 ? -25.117 37.420  1.682   1.00 116.24 ? 473 PRO A C     1 
ATOM   3900 O  O     . PRO A 1 473 ? -24.807 36.494  0.921   1.00 115.87 ? 473 PRO A O     1 
ATOM   3901 C  CB    . PRO A 1 473 ? -24.741 36.885  4.121   1.00 120.50 ? 473 PRO A CB    1 
ATOM   3902 C  CG    . PRO A 1 473 ? -25.637 37.823  4.850   1.00 121.27 ? 473 PRO A CG    1 
ATOM   3903 C  CD    . PRO A 1 473 ? -25.031 39.188  4.680   1.00 118.80 ? 473 PRO A CD    1 
ATOM   3904 N  N     . ILE A 1 474 ? -26.191 38.184  1.475   1.00 117.30 ? 474 ILE A N     1 
ATOM   3905 C  CA    . ILE A 1 474 ? -26.931 38.083  0.221   1.00 123.98 ? 474 ILE A CA    1 
ATOM   3906 C  C     . ILE A 1 474 ? -26.011 38.407  -0.950  1.00 115.83 ? 474 ILE A C     1 
ATOM   3907 O  O     . ILE A 1 474 ? -26.030 37.730  -1.988  1.00 120.14 ? 474 ILE A O     1 
ATOM   3908 C  CB    . ILE A 1 474 ? -28.172 38.998  0.256   1.00 127.56 ? 474 ILE A CB    1 
ATOM   3909 C  CG1   . ILE A 1 474 ? -29.420 38.204  0.664   1.00 115.25 ? 474 ILE A CG1   1 
ATOM   3910 C  CG2   . ILE A 1 474 ? -28.394 39.679  -1.090  1.00 117.69 ? 474 ILE A CG2   1 
ATOM   3911 C  CD1   . ILE A 1 474 ? -29.311 37.504  2.004   1.00 107.16 ? 474 ILE A CD1   1 
ATOM   3912 N  N     . GLU A 1 475 ? -25.157 39.421  -0.787  1.00 112.10 ? 475 GLU A N     1 
ATOM   3913 C  CA    . GLU A 1 475 ? -24.149 39.697  -1.804  1.00 105.73 ? 475 GLU A CA    1 
ATOM   3914 C  C     . GLU A 1 475 ? -23.169 38.539  -1.939  1.00 99.65  ? 475 GLU A C     1 
ATOM   3915 O  O     . GLU A 1 475 ? -22.732 38.220  -3.047  1.00 90.82  ? 475 GLU A O     1 
ATOM   3916 C  CB    . GLU A 1 475 ? -23.405 40.988  -1.474  1.00 104.10 ? 475 GLU A CB    1 
ATOM   3917 C  CG    . GLU A 1 475 ? -24.310 42.162  -1.165  1.00 112.61 ? 475 GLU A CG    1 
ATOM   3918 C  CD    . GLU A 1 475 ? -24.404 43.157  -2.304  1.00 113.79 ? 475 GLU A CD    1 
ATOM   3919 O  OE1   . GLU A 1 475 ? -24.367 42.732  -3.477  1.00 114.40 ? 475 GLU A OE1   1 
ATOM   3920 O  OE2   . GLU A 1 475 ? -24.514 44.369  -2.023  1.00 107.79 ? 475 GLU A OE2   1 
ATOM   3921 N  N     . ARG A 1 476 ? -22.784 37.917  -0.821  1.00 102.12 ? 476 ARG A N     1 
ATOM   3922 C  CA    . ARG A 1 476 ? -21.895 36.761  -0.899  1.00 104.46 ? 476 ARG A CA    1 
ATOM   3923 C  C     . ARG A 1 476 ? -22.499 35.678  -1.784  1.00 98.15  ? 476 ARG A C     1 
ATOM   3924 O  O     . ARG A 1 476 ? -21.826 35.136  -2.669  1.00 106.87 ? 476 ARG A O     1 
ATOM   3925 C  CB    . ARG A 1 476 ? -21.600 36.218  0.501   1.00 110.57 ? 476 ARG A CB    1 
ATOM   3926 C  CG    . ARG A 1 476 ? -21.334 34.718  0.533   1.00 114.56 ? 476 ARG A CG    1 
ATOM   3927 C  CD    . ARG A 1 476 ? -20.035 34.378  1.248   1.00 115.76 ? 476 ARG A CD    1 
ATOM   3928 N  NE    . ARG A 1 476 ? -19.551 33.052  0.879   1.00 124.09 ? 476 ARG A NE    1 
ATOM   3929 C  CZ    . ARG A 1 476 ? -18.450 32.492  1.362   1.00 122.33 ? 476 ARG A CZ    1 
ATOM   3930 N  NH1   . ARG A 1 476 ? -17.691 33.112  2.249   1.00 121.97 ? 476 ARG A NH1   1 
ATOM   3931 N  NH2   . ARG A 1 476 ? -18.102 31.279  0.942   1.00 112.18 ? 476 ARG A NH2   1 
ATOM   3932 N  N     . LYS A 1 477 ? -23.781 35.370  -1.571  1.00 95.36  ? 477 LYS A N     1 
ATOM   3933 C  CA    . LYS A 1 477 ? -24.474 34.418  -2.436  1.00 91.80  ? 477 LYS A CA    1 
ATOM   3934 C  C     . LYS A 1 477 ? -24.474 34.891  -3.886  1.00 84.98  ? 477 LYS A C     1 
ATOM   3935 O  O     . LYS A 1 477 ? -24.266 34.093  -4.810  1.00 91.97  ? 477 LYS A O     1 
ATOM   3936 C  CB    . LYS A 1 477 ? -25.906 34.216  -1.940  1.00 98.96  ? 477 LYS A CB    1 
ATOM   3937 C  CG    . LYS A 1 477 ? -26.119 32.970  -1.097  1.00 94.76  ? 477 LYS A CG    1 
ATOM   3938 C  CD    . LYS A 1 477 ? -27.565 32.501  -1.168  1.00 96.36  ? 477 LYS A CD    1 
ATOM   3939 C  CE    . LYS A 1 477 ? -28.417 33.171  -0.101  1.00 91.62  ? 477 LYS A CE    1 
ATOM   3940 N  NZ    . LYS A 1 477 ? -29.340 32.205  0.556   1.00 90.41  ? 477 LYS A NZ    1 
ATOM   3941 N  N     . LEU A 1 478 ? -24.706 36.190  -4.100  1.00 84.34  ? 478 LEU A N     1 
ATOM   3942 C  CA    . LEU A 1 478 ? -24.751 36.733  -5.455  1.00 84.69  ? 478 LEU A CA    1 
ATOM   3943 C  C     . LEU A 1 478 ? -23.428 36.516  -6.184  1.00 82.62  ? 478 LEU A C     1 
ATOM   3944 O  O     . LEU A 1 478 ? -23.400 35.963  -7.291  1.00 80.30  ? 478 LEU A O     1 
ATOM   3945 C  CB    . LEU A 1 478 ? -25.101 38.221  -5.412  1.00 82.13  ? 478 LEU A CB    1 
ATOM   3946 C  CG    . LEU A 1 478 ? -26.581 38.591  -5.557  1.00 88.79  ? 478 LEU A CG    1 
ATOM   3947 C  CD1   . LEU A 1 478 ? -26.761 40.101  -5.515  1.00 77.76  ? 478 LEU A CD1   1 
ATOM   3948 C  CD2   . LEU A 1 478 ? -27.159 38.018  -6.840  1.00 75.52  ? 478 LEU A CD2   1 
ATOM   3949 N  N     . LEU A 1 479 ? -22.316 36.951  -5.581  1.00 83.40  ? 479 LEU A N     1 
ATOM   3950 C  CA    . LEU A 1 479 ? -21.033 36.783  -6.258  1.00 77.15  ? 479 LEU A CA    1 
ATOM   3951 C  C     . LEU A 1 479 ? -20.612 35.318  -6.343  1.00 77.17  ? 479 LEU A C     1 
ATOM   3952 O  O     . LEU A 1 479 ? -19.921 34.943  -7.295  1.00 76.09  ? 479 LEU A O     1 
ATOM   3953 C  CB    . LEU A 1 479 ? -19.901 37.604  -5.610  1.00 74.04  ? 479 LEU A CB    1 
ATOM   3954 C  CG    . LEU A 1 479 ? -19.881 39.134  -5.390  1.00 72.38  ? 479 LEU A CG    1 
ATOM   3955 C  CD1   . LEU A 1 479 ? -20.306 39.886  -6.657  1.00 70.73  ? 479 LEU A CD1   1 
ATOM   3956 C  CD2   . LEU A 1 479 ? -20.560 39.691  -4.144  1.00 86.75  ? 479 LEU A CD2   1 
ATOM   3957 N  N     . ASP A 1 480 ? -21.014 34.470  -5.390  1.00 74.97  ? 480 ASP A N     1 
ATOM   3958 C  CA    . ASP A 1 480 ? -20.720 33.045  -5.527  1.00 78.85  ? 480 ASP A CA    1 
ATOM   3959 C  C     . ASP A 1 480 ? -21.408 32.469  -6.758  1.00 83.39  ? 480 ASP A C     1 
ATOM   3960 O  O     . ASP A 1 480 ? -20.789 31.756  -7.561  1.00 80.23  ? 480 ASP A O     1 
ATOM   3961 C  CB    . ASP A 1 480 ? -21.141 32.297  -4.264  1.00 78.14  ? 480 ASP A CB    1 
ATOM   3962 C  CG    . ASP A 1 480 ? -20.708 30.841  -4.279  1.00 85.66  ? 480 ASP A CG    1 
ATOM   3963 O  OD1   . ASP A 1 480 ? -21.411 30.011  -4.899  1.00 84.36  ? 480 ASP A OD1   1 
ATOM   3964 O  OD2   . ASP A 1 480 ? -19.661 30.529  -3.675  1.00 87.87  ? 480 ASP A OD2   1 
ATOM   3965 N  N     . TYR A 1 481 ? -22.697 32.774  -6.925  1.00 94.84  ? 481 TYR A N     1 
ATOM   3966 C  CA    . TYR A 1 481 ? -23.409 32.314  -8.110  1.00 96.30  ? 481 TYR A CA    1 
ATOM   3967 C  C     . TYR A 1 481 ? -22.789 32.901  -9.374  1.00 87.27  ? 481 TYR A C     1 
ATOM   3968 O  O     . TYR A 1 481 ? -22.639 32.196  -10.376 1.00 86.60  ? 481 TYR A O     1 
ATOM   3969 C  CB    . TYR A 1 481 ? -24.903 32.642  -7.958  1.00 87.81  ? 481 TYR A CB    1 
ATOM   3970 C  CG    . TYR A 1 481 ? -25.855 31.967  -8.939  1.00 88.18  ? 481 TYR A CG    1 
ATOM   3971 C  CD1   . TYR A 1 481 ? -26.983 31.292  -8.483  1.00 89.26  ? 481 TYR A CD1   1 
ATOM   3972 C  CD2   . TYR A 1 481 ? -25.685 32.095  -10.318 1.00 95.57  ? 481 TYR A CD2   1 
ATOM   3973 C  CE1   . TYR A 1 481 ? -27.869 30.690  -9.367  1.00 82.79  ? 481 TYR A CE1   1 
ATOM   3974 C  CE2   . TYR A 1 481 ? -26.567 31.508  -11.208 1.00 79.54  ? 481 TYR A CE2   1 
ATOM   3975 C  CZ    . TYR A 1 481 ? -27.656 30.810  -10.733 1.00 82.69  ? 481 TYR A CZ    1 
ATOM   3976 O  OH    . TYR A 1 481 ? -28.527 30.232  -11.631 1.00 96.31  ? 481 TYR A OH    1 
ATOM   3977 N  N     . ARG A 1 482 ? -22.354 34.166  -9.328  1.00 77.19  ? 482 ARG A N     1 
ATOM   3978 C  CA    . ARG A 1 482 ? -21.762 34.779  -10.518 1.00 75.12  ? 482 ARG A CA    1 
ATOM   3979 C  C     . ARG A 1 482 ? -20.444 34.109  -10.906 1.00 72.13  ? 482 ARG A C     1 
ATOM   3980 O  O     . ARG A 1 482 ? -20.200 33.851  -12.091 1.00 64.59  ? 482 ARG A O     1 
ATOM   3981 C  CB    . ARG A 1 482 ? -21.556 36.278  -10.301 1.00 69.44  ? 482 ARG A CB    1 
ATOM   3982 C  CG    . ARG A 1 482 ? -21.576 37.076  -11.598 1.00 67.31  ? 482 ARG A CG    1 
ATOM   3983 C  CD    . ARG A 1 482 ? -21.436 38.572  -11.355 1.00 70.09  ? 482 ARG A CD    1 
ATOM   3984 N  NE    . ARG A 1 482 ? -20.467 39.187  -12.255 1.00 89.24  ? 482 ARG A NE    1 
ATOM   3985 C  CZ    . ARG A 1 482 ? -20.653 39.364  -13.557 1.00 90.92  ? 482 ARG A CZ    1 
ATOM   3986 N  NH1   . ARG A 1 482 ? -21.776 38.995  -14.153 1.00 83.93  ? 482 ARG A NH1   1 
ATOM   3987 N  NH2   . ARG A 1 482 ? -19.688 39.927  -14.280 1.00 84.04  ? 482 ARG A NH2   1 
ATOM   3988 N  N     . GLN A 1 483 ? -19.576 33.829  -9.931  1.00 62.74  ? 483 GLN A N     1 
ATOM   3989 C  CA    . GLN A 1 483 ? -18.318 33.167  -10.261 1.00 65.15  ? 483 GLN A CA    1 
ATOM   3990 C  C     . GLN A 1 483 ? -18.560 31.743  -10.745 1.00 61.36  ? 483 GLN A C     1 
ATOM   3991 O  O     . GLN A 1 483 ? -17.862 31.264  -11.649 1.00 60.70  ? 483 GLN A O     1 
ATOM   3992 C  CB    . GLN A 1 483 ? -17.360 33.196  -9.064  1.00 64.37  ? 483 GLN A CB    1 
ATOM   3993 C  CG    . GLN A 1 483 ? -17.803 32.411  -7.841  1.00 71.60  ? 483 GLN A CG    1 
ATOM   3994 C  CD    . GLN A 1 483 ? -17.335 30.968  -7.866  1.00 69.25  ? 483 GLN A CD    1 
ATOM   3995 O  OE1   . GLN A 1 483 ? -16.409 30.616  -8.596  1.00 67.82  ? 483 GLN A OE1   1 
ATOM   3996 N  NE2   . GLN A 1 483 ? -17.980 30.124  -7.070  1.00 67.10  ? 483 GLN A NE2   1 
ATOM   3997 N  N     . ARG A 1 484 ? -19.561 31.055  -10.183 1.00 62.08  ? 484 ARG A N     1 
ATOM   3998 C  CA    . ARG A 1 484 ? -19.918 29.740  -10.708 1.00 61.81  ? 484 ARG A CA    1 
ATOM   3999 C  C     . ARG A 1 484 ? -20.398 29.839  -12.154 1.00 60.58  ? 484 ARG A C     1 
ATOM   4000 O  O     . ARG A 1 484 ? -20.081 28.977  -12.985 1.00 57.83  ? 484 ARG A O     1 
ATOM   4001 C  CB    . ARG A 1 484 ? -20.981 29.093  -9.822  1.00 68.17  ? 484 ARG A CB    1 
ATOM   4002 C  CG    . ARG A 1 484 ? -20.602 27.716  -9.297  1.00 77.14  ? 484 ARG A CG    1 
ATOM   4003 C  CD    . ARG A 1 484 ? -21.831 26.927  -8.876  1.00 83.22  ? 484 ARG A CD    1 
ATOM   4004 N  NE    . ARG A 1 484 ? -22.707 26.631  -10.004 1.00 104.31 ? 484 ARG A NE    1 
ATOM   4005 C  CZ    . ARG A 1 484 ? -24.011 26.871  -10.025 1.00 96.26  ? 484 ARG A CZ    1 
ATOM   4006 N  NH1   . ARG A 1 484 ? -24.631 27.413  -8.989  1.00 93.24  ? 484 ARG A NH1   1 
ATOM   4007 N  NH2   . ARG A 1 484 ? -24.712 26.558  -11.112 1.00 83.54  ? 484 ARG A NH2   1 
ATOM   4008 N  N     . LEU A 1 485 ? -21.163 30.888  -12.471 1.00 59.37  ? 485 LEU A N     1 
ATOM   4009 C  CA    . LEU A 1 485 ? -21.579 31.134  -13.850 1.00 53.90  ? 485 LEU A CA    1 
ATOM   4010 C  C     . LEU A 1 485 ? -20.386 31.308  -14.770 1.00 55.40  ? 485 LEU A C     1 
ATOM   4011 O  O     . LEU A 1 485 ? -20.337 30.718  -15.854 1.00 48.91  ? 485 LEU A O     1 
ATOM   4012 C  CB    . LEU A 1 485 ? -22.475 32.369  -13.933 1.00 54.52  ? 485 LEU A CB    1 
ATOM   4013 C  CG    . LEU A 1 485 ? -23.829 32.207  -13.267 1.00 64.74  ? 485 LEU A CG    1 
ATOM   4014 C  CD1   . LEU A 1 485 ? -24.748 33.373  -13.581 1.00 59.24  ? 485 LEU A CD1   1 
ATOM   4015 C  CD2   . LEU A 1 485 ? -24.403 30.910  -13.787 1.00 52.42  ? 485 LEU A CD2   1 
ATOM   4016 N  N     . ILE A 1 486 ? -19.434 32.151  -14.371 1.00 53.77  ? 486 ILE A N     1 
ATOM   4017 C  CA    . ILE A 1 486 ? -18.267 32.391  -15.214 1.00 46.34  ? 486 ILE A CA    1 
ATOM   4018 C  C     . ILE A 1 486 ? -17.484 31.101  -15.418 1.00 47.95  ? 486 ILE A C     1 
ATOM   4019 O  O     . ILE A 1 486 ? -16.991 30.823  -16.518 1.00 47.81  ? 486 ILE A O     1 
ATOM   4020 C  CB    . ILE A 1 486 ? -17.385 33.497  -14.610 1.00 54.27  ? 486 ILE A CB    1 
ATOM   4021 C  CG1   . ILE A 1 486 ? -18.228 34.717  -14.232 1.00 52.09  ? 486 ILE A CG1   1 
ATOM   4022 C  CG2   . ILE A 1 486 ? -16.285 33.877  -15.587 1.00 47.09  ? 486 ILE A CG2   1 
ATOM   4023 C  CD1   . ILE A 1 486 ? -18.339 35.758  -15.320 1.00 57.39  ? 486 ILE A CD1   1 
ATOM   4024 N  N     . LYS A 1 487 ? -17.365 30.289  -14.365 1.00 46.96  ? 487 LYS A N     1 
ATOM   4025 C  CA    . LYS A 1 487 ? -16.636 29.028  -14.476 1.00 43.75  ? 487 LYS A CA    1 
ATOM   4026 C  C     . LYS A 1 487 ? -17.316 28.084  -15.463 1.00 47.54  ? 487 LYS A C     1 
ATOM   4027 O  O     . LYS A 1 487 ? -16.666 27.524  -16.362 1.00 47.48  ? 487 LYS A O     1 
ATOM   4028 C  CB    . LYS A 1 487 ? -16.512 28.395  -13.089 1.00 55.18  ? 487 LYS A CB    1 
ATOM   4029 C  CG    . LYS A 1 487 ? -16.758 26.900  -13.024 1.00 60.29  ? 487 LYS A CG    1 
ATOM   4030 C  CD    . LYS A 1 487 ? -16.257 26.326  -11.710 1.00 62.76  ? 487 LYS A CD    1 
ATOM   4031 C  CE    . LYS A 1 487 ? -16.062 24.827  -11.801 1.00 63.19  ? 487 LYS A CE    1 
ATOM   4032 N  NZ    . LYS A 1 487 ? -15.040 24.343  -10.835 1.00 65.19  ? 487 LYS A NZ    1 
ATOM   4033 N  N     . ILE A 1 488 ? -18.633 27.902  -15.315 1.00 46.59  ? 488 ILE A N     1 
ATOM   4034 C  CA    . ILE A 1 488 ? -19.366 27.026  -16.224 1.00 46.39  ? 488 ILE A CA    1 
ATOM   4035 C  C     . ILE A 1 488 ? -19.296 27.561  -17.646 1.00 43.13  ? 488 ILE A C     1 
ATOM   4036 O  O     . ILE A 1 488 ? -19.144 26.797  -18.607 1.00 44.25  ? 488 ILE A O     1 
ATOM   4037 C  CB    . ILE A 1 488 ? -20.822 26.856  -15.751 1.00 50.67  ? 488 ILE A CB    1 
ATOM   4038 C  CG1   . ILE A 1 488 ? -20.861 26.278  -14.335 1.00 57.04  ? 488 ILE A CG1   1 
ATOM   4039 C  CG2   . ILE A 1 488 ? -21.595 25.964  -16.709 1.00 47.28  ? 488 ILE A CG2   1 
ATOM   4040 C  CD1   . ILE A 1 488 ? -22.255 25.936  -13.855 1.00 74.46  ? 488 ILE A CD1   1 
ATOM   4041 N  N     . LEU A 1 489 ? -19.373 28.883  -17.803 1.00 43.84  ? 489 LEU A N     1 
ATOM   4042 C  CA    . LEU A 1 489 ? -19.355 29.471  -19.134 1.00 46.56  ? 489 LEU A CA    1 
ATOM   4043 C  C     . LEU A 1 489 ? -17.998 29.288  -19.803 1.00 45.68  ? 489 LEU A C     1 
ATOM   4044 O  O     . LEU A 1 489 ? -17.933 29.002  -21.000 1.00 44.27  ? 489 LEU A O     1 
ATOM   4045 C  CB    . LEU A 1 489 ? -19.733 30.951  -19.056 1.00 45.50  ? 489 LEU A CB    1 
ATOM   4046 C  CG    . LEU A 1 489 ? -19.645 31.759  -20.351 1.00 48.74  ? 489 LEU A CG    1 
ATOM   4047 C  CD1   . LEU A 1 489 ? -20.567 31.177  -21.411 1.00 40.93  ? 489 LEU A CD1   1 
ATOM   4048 C  CD2   . LEU A 1 489 ? -19.979 33.218  -20.089 1.00 45.93  ? 489 LEU A CD2   1 
ATOM   4049 N  N     . ALA A 1 490 ? -16.903 29.420  -19.051 1.00 46.69  ? 490 ALA A N     1 
ATOM   4050 C  CA    . ALA A 1 490 ? -15.583 29.217  -19.645 1.00 43.09  ? 490 ALA A CA    1 
ATOM   4051 C  C     . ALA A 1 490 ? -15.363 27.757  -20.027 1.00 43.53  ? 490 ALA A C     1 
ATOM   4052 O  O     . ALA A 1 490 ? -14.858 27.461  -21.123 1.00 41.57  ? 490 ALA A O     1 
ATOM   4053 C  CB    . ALA A 1 490 ? -14.495 29.690  -18.684 1.00 39.68  ? 490 ALA A CB    1 
ATOM   4054 N  N     . ASN A 1 491 ? -15.740 26.827  -19.142 1.00 40.07  ? 491 ASN A N     1 
ATOM   4055 C  CA    . ASN A 1 491 ? -15.609 25.412  -19.484 1.00 43.54  ? 491 ASN A CA    1 
ATOM   4056 C  C     . ASN A 1 491 ? -16.463 25.064  -20.699 1.00 45.73  ? 491 ASN A C     1 
ATOM   4057 O  O     . ASN A 1 491 ? -16.042 24.292  -21.573 1.00 42.22  ? 491 ASN A O     1 
ATOM   4058 C  CB    . ASN A 1 491 ? -15.986 24.549  -18.280 1.00 43.42  ? 491 ASN A CB    1 
ATOM   4059 C  CG    . ASN A 1 491 ? -14.954 24.621  -17.162 1.00 53.74  ? 491 ASN A CG    1 
ATOM   4060 O  OD1   . ASN A 1 491 ? -13.856 25.152  -17.346 1.00 51.47  ? 491 ASN A OD1   1 
ATOM   4061 N  ND2   . ASN A 1 491 ? -15.310 24.101  -15.994 1.00 56.15  ? 491 ASN A ND2   1 
ATOM   4062 N  N     . SER A 1 492 ? -17.654 25.658  -20.794 1.00 44.68  ? 492 SER A N     1 
ATOM   4063 C  CA    . SER A 1 492 ? -18.517 25.394  -21.935 1.00 48.36  ? 492 SER A CA    1 
ATOM   4064 C  C     . SER A 1 492 ? -18.006 26.078  -23.196 1.00 49.23  ? 492 SER A C     1 
ATOM   4065 O  O     . SER A 1 492 ? -18.258 25.595  -24.300 1.00 43.46  ? 492 SER A O     1 
ATOM   4066 C  CB    . SER A 1 492 ? -19.941 25.834  -21.613 1.00 44.27  ? 492 SER A CB    1 
ATOM   4067 O  OG    . SER A 1 492 ? -20.361 25.293  -20.373 1.00 53.96  ? 492 SER A OG    1 
ATOM   4068 N  N     . VAL A 1 493 ? -17.282 27.190  -23.057 1.00 45.76  ? 493 VAL A N     1 
ATOM   4069 C  CA    . VAL A 1 493 ? -16.638 27.796  -24.217 1.00 44.00  ? 493 VAL A CA    1 
ATOM   4070 C  C     . VAL A 1 493 ? -15.552 26.876  -24.755 1.00 43.71  ? 493 VAL A C     1 
ATOM   4071 O  O     . VAL A 1 493 ? -15.401 26.719  -25.973 1.00 41.44  ? 493 VAL A O     1 
ATOM   4072 C  CB    . VAL A 1 493 ? -16.087 29.191  -23.866 1.00 45.68  ? 493 VAL A CB    1 
ATOM   4073 C  CG1   . VAL A 1 493 ? -15.070 29.643  -24.904 1.00 46.04  ? 493 VAL A CG1   1 
ATOM   4074 C  CG2   . VAL A 1 493 ? -17.221 30.197  -23.786 1.00 41.36  ? 493 VAL A CG2   1 
ATOM   4075 N  N     . TYR A 1 494 ? -14.789 26.235  -23.864 1.00 37.41  ? 494 TYR A N     1 
ATOM   4076 C  CA    . TYR A 1 494 ? -13.867 25.205  -24.341 1.00 39.51  ? 494 TYR A CA    1 
ATOM   4077 C  C     . TYR A 1 494 ? -14.626 24.100  -25.066 1.00 46.87  ? 494 TYR A C     1 
ATOM   4078 O  O     . TYR A 1 494 ? -14.283 23.730  -26.195 1.00 43.71  ? 494 TYR A O     1 
ATOM   4079 C  CB    . TYR A 1 494 ? -13.051 24.598  -23.201 1.00 42.59  ? 494 TYR A CB    1 
ATOM   4080 C  CG    . TYR A 1 494 ? -12.635 23.174  -23.532 1.00 42.54  ? 494 TYR A CG    1 
ATOM   4081 C  CD1   . TYR A 1 494 ? -11.664 22.920  -24.497 1.00 44.62  ? 494 TYR A CD1   1 
ATOM   4082 C  CD2   . TYR A 1 494 ? -13.242 22.086  -22.914 1.00 42.88  ? 494 TYR A CD2   1 
ATOM   4083 C  CE1   . TYR A 1 494 ? -11.298 21.626  -24.821 1.00 43.72  ? 494 TYR A CE1   1 
ATOM   4084 C  CE2   . TYR A 1 494 ? -12.883 20.790  -23.234 1.00 49.06  ? 494 TYR A CE2   1 
ATOM   4085 C  CZ    . TYR A 1 494 ? -11.909 20.566  -24.184 1.00 42.99  ? 494 TYR A CZ    1 
ATOM   4086 O  OH    . TYR A 1 494 ? -11.552 19.275  -24.497 1.00 48.16  ? 494 TYR A OH    1 
ATOM   4087 N  N     . GLY A 1 495 ? -15.662 23.552  -24.420 1.00 47.46  ? 495 GLY A N     1 
ATOM   4088 C  CA    . GLY A 1 495 ? -16.401 22.452  -25.024 1.00 43.80  ? 495 GLY A CA    1 
ATOM   4089 C  C     . GLY A 1 495 ? -17.057 22.818  -26.342 1.00 43.88  ? 495 GLY A C     1 
ATOM   4090 O  O     . GLY A 1 495 ? -17.276 21.953  -27.194 1.00 43.16  ? 495 GLY A O     1 
ATOM   4091 N  N     . HIS A 1 496 ? -17.378 24.099  -26.524 1.00 38.73  ? 496 HIS A N     1 
ATOM   4092 C  CA    . HIS A 1 496 ? -17.984 24.569  -27.764 1.00 44.09  ? 496 HIS A CA    1 
ATOM   4093 C  C     . HIS A 1 496 ? -17.097 24.253  -28.961 1.00 47.03  ? 496 HIS A C     1 
ATOM   4094 O  O     . HIS A 1 496 ? -17.592 23.886  -30.032 1.00 48.31  ? 496 HIS A O     1 
ATOM   4095 C  CB    . HIS A 1 496 ? -18.253 26.073  -27.645 1.00 43.19  ? 496 HIS A CB    1 
ATOM   4096 C  CG    . HIS A 1 496 ? -18.719 26.725  -28.910 1.00 47.40  ? 496 HIS A CG    1 
ATOM   4097 N  ND1   . HIS A 1 496 ? -20.052 26.946  -29.186 1.00 52.52  ? 496 HIS A ND1   1 
ATOM   4098 C  CD2   . HIS A 1 496 ? -18.029 27.228  -29.961 1.00 54.61  ? 496 HIS A CD2   1 
ATOM   4099 C  CE1   . HIS A 1 496 ? -20.163 27.549  -30.356 1.00 52.49  ? 496 HIS A CE1   1 
ATOM   4100 N  NE2   . HIS A 1 496 ? -18.951 27.729  -30.849 1.00 46.92  ? 496 HIS A NE2   1 
ATOM   4101 N  N     . MET A 1 497 ? -15.778 24.356  -28.790 1.00 48.78  ? 497 MET A N     1 
ATOM   4102 C  CA    . MET A 1 497 ? -14.866 24.101  -29.898 1.00 44.82  ? 497 MET A CA    1 
ATOM   4103 C  C     . MET A 1 497 ? -14.894 22.650  -30.359 1.00 47.27  ? 497 MET A C     1 
ATOM   4104 O  O     . MET A 1 497 ? -14.458 22.361  -31.479 1.00 43.78  ? 497 MET A O     1 
ATOM   4105 C  CB    . MET A 1 497 ? -13.445 24.502  -29.504 1.00 51.26  ? 497 MET A CB    1 
ATOM   4106 C  CG    . MET A 1 497 ? -13.290 25.992  -29.262 1.00 51.88  ? 497 MET A CG    1 
ATOM   4107 S  SD    . MET A 1 497 ? -11.581 26.542  -29.327 1.00 56.25  ? 497 MET A SD    1 
ATOM   4108 C  CE    . MET A 1 497 ? -11.105 26.372  -27.608 1.00 42.79  ? 497 MET A CE    1 
ATOM   4109 N  N     . GLY A 1 498 ? -15.400 21.736  -29.535 1.00 48.00  ? 498 GLY A N     1 
ATOM   4110 C  CA    . GLY A 1 498 ? -15.477 20.341  -29.919 1.00 45.63  ? 498 GLY A CA    1 
ATOM   4111 C  C     . GLY A 1 498 ? -16.896 19.838  -30.090 1.00 53.74  ? 498 GLY A C     1 
ATOM   4112 O  O     . GLY A 1 498 ? -17.140 18.629  -30.046 1.00 57.99  ? 498 GLY A O     1 
ATOM   4113 N  N     . PHE A 1 499 ? -17.842 20.754  -30.291 1.00 51.38  ? 499 PHE A N     1 
ATOM   4114 C  CA    . PHE A 1 499 ? -19.251 20.413  -30.438 1.00 56.13  ? 499 PHE A CA    1 
ATOM   4115 C  C     . PHE A 1 499 ? -19.645 20.456  -31.909 1.00 58.56  ? 499 PHE A C     1 
ATOM   4116 O  O     . PHE A 1 499 ? -19.333 21.423  -32.612 1.00 54.11  ? 499 PHE A O     1 
ATOM   4117 C  CB    . PHE A 1 499 ? -20.127 21.360  -29.617 1.00 49.60  ? 499 PHE A CB    1 
ATOM   4118 C  CG    . PHE A 1 499 ? -21.600 21.149  -29.815 1.00 62.91  ? 499 PHE A CG    1 
ATOM   4119 C  CD1   . PHE A 1 499 ? -22.207 19.978  -29.387 1.00 65.59  ? 499 PHE A CD1   1 
ATOM   4120 C  CD2   . PHE A 1 499 ? -22.386 22.131  -30.396 1.00 64.59  ? 499 PHE A CD2   1 
ATOM   4121 C  CE1   . PHE A 1 499 ? -23.561 19.780  -29.556 1.00 64.22  ? 499 PHE A CE1   1 
ATOM   4122 C  CE2   . PHE A 1 499 ? -23.746 21.941  -30.564 1.00 69.40  ? 499 PHE A CE2   1 
ATOM   4123 C  CZ    . PHE A 1 499 ? -24.333 20.763  -30.144 1.00 63.79  ? 499 PHE A CZ    1 
ATOM   4124 N  N     . GLU A 1 500 ? -20.350 19.416  -32.359 1.00 62.25  ? 500 GLU A N     1 
ATOM   4125 C  CA    . GLU A 1 500 ? -20.600 19.236  -33.787 1.00 61.82  ? 500 GLU A CA    1 
ATOM   4126 C  C     . GLU A 1 500 ? -21.382 20.405  -34.376 1.00 60.70  ? 500 GLU A C     1 
ATOM   4127 O  O     . GLU A 1 500 ? -21.028 20.930  -35.437 1.00 55.08  ? 500 GLU A O     1 
ATOM   4128 C  CB    . GLU A 1 500 ? -21.337 17.918  -34.024 1.00 71.28  ? 500 GLU A CB    1 
ATOM   4129 C  CG    . GLU A 1 500 ? -20.541 16.679  -33.661 1.00 88.64  ? 500 GLU A CG    1 
ATOM   4130 C  CD    . GLU A 1 500 ? -20.891 16.150  -32.284 1.00 111.32 ? 500 GLU A CD    1 
ATOM   4131 O  OE1   . GLU A 1 500 ? -20.051 16.268  -31.365 1.00 105.84 ? 500 GLU A OE1   1 
ATOM   4132 O  OE2   . GLU A 1 500 ? -22.011 15.621  -32.119 1.00 104.12 ? 500 GLU A OE2   1 
ATOM   4133 N  N     . ASN A 1 501 ? -22.451 20.831  -33.703 1.00 58.77  ? 501 ASN A N     1 
ATOM   4134 C  CA    . ASN A 1 501 ? -23.303 21.901  -34.206 1.00 59.30  ? 501 ASN A CA    1 
ATOM   4135 C  C     . ASN A 1 501 ? -22.884 23.279  -33.702 1.00 57.24  ? 501 ASN A C     1 
ATOM   4136 O  O     . ASN A 1 501 ? -23.702 24.206  -33.702 1.00 58.12  ? 501 ASN A O     1 
ATOM   4137 C  CB    . ASN A 1 501 ? -24.765 21.629  -33.843 1.00 52.71  ? 501 ASN A CB    1 
ATOM   4138 C  CG    . ASN A 1 501 ? -25.737 22.305  -34.792 1.00 57.11  ? 501 ASN A CG    1 
ATOM   4139 O  OD1   . ASN A 1 501 ? -25.521 22.338  -36.004 1.00 54.37  ? 501 ASN A OD1   1 
ATOM   4140 N  ND2   . ASN A 1 501 ? -26.814 22.854  -34.241 1.00 58.29  ? 501 ASN A ND2   1 
ATOM   4141 N  N     . ALA A 1 502 ? -21.633 23.439  -33.284 1.00 59.77  ? 502 ALA A N     1 
ATOM   4142 C  CA    . ALA A 1 502 ? -21.155 24.713  -32.771 1.00 52.43  ? 502 ALA A CA    1 
ATOM   4143 C  C     . ALA A 1 502 ? -20.622 25.581  -33.902 1.00 48.67  ? 502 ALA A C     1 
ATOM   4144 O  O     . ALA A 1 502 ? -20.010 25.082  -34.851 1.00 52.79  ? 502 ALA A O     1 
ATOM   4145 C  CB    . ALA A 1 502 ? -20.067 24.496  -31.724 1.00 51.26  ? 502 ALA A CB    1 
ATOM   4146 N  N     . ARG A 1 503 ? -20.863 26.889  -33.791 1.00 45.16  ? 503 ARG A N     1 
ATOM   4147 C  CA    . ARG A 1 503 ? -20.401 27.825  -34.812 1.00 52.80  ? 503 ARG A CA    1 
ATOM   4148 C  C     . ARG A 1 503 ? -18.879 27.897  -34.845 1.00 50.94  ? 503 ARG A C     1 
ATOM   4149 O  O     . ARG A 1 503 ? -18.261 27.712  -35.899 1.00 50.99  ? 503 ARG A O     1 
ATOM   4150 C  CB    . ARG A 1 503 ? -20.999 29.208  -34.559 1.00 47.87  ? 503 ARG A CB    1 
ATOM   4151 C  CG    . ARG A 1 503 ? -22.340 29.436  -35.232 1.00 58.98  ? 503 ARG A CG    1 
ATOM   4152 C  CD    . ARG A 1 503 ? -22.902 30.804  -34.884 1.00 57.65  ? 503 ARG A CD    1 
ATOM   4153 N  NE    . ARG A 1 503 ? -24.315 30.742  -34.532 1.00 62.97  ? 503 ARG A NE    1 
ATOM   4154 C  CZ    . ARG A 1 503 ? -25.304 31.046  -35.361 1.00 73.01  ? 503 ARG A CZ    1 
ATOM   4155 N  NH1   . ARG A 1 503 ? -25.069 31.445  -36.601 1.00 64.77  ? 503 ARG A NH1   1 
ATOM   4156 N  NH2   . ARG A 1 503 ? -26.561 30.948  -34.935 1.00 79.28  ? 503 ARG A NH2   1 
ATOM   4157 N  N     . TRP A 1 504 ? -18.259 28.169  -33.701 1.00 43.16  ? 504 TRP A N     1 
ATOM   4158 C  CA    . TRP A 1 504 ? -16.803 28.244  -33.597 1.00 53.06  ? 504 TRP A CA    1 
ATOM   4159 C  C     . TRP A 1 504 ? -16.195 26.875  -33.307 1.00 54.20  ? 504 TRP A C     1 
ATOM   4160 O  O     . TRP A 1 504 ? -15.404 26.695  -32.384 1.00 50.48  ? 504 TRP A O     1 
ATOM   4161 C  CB    . TRP A 1 504 ? -16.415 29.263  -32.532 1.00 45.52  ? 504 TRP A CB    1 
ATOM   4162 C  CG    . TRP A 1 504 ? -16.560 30.677  -33.003 1.00 49.22  ? 504 TRP A CG    1 
ATOM   4163 C  CD1   . TRP A 1 504 ? -15.617 31.429  -33.640 1.00 48.37  ? 504 TRP A CD1   1 
ATOM   4164 C  CD2   . TRP A 1 504 ? -17.727 31.503  -32.896 1.00 52.13  ? 504 TRP A CD2   1 
ATOM   4165 N  NE1   . TRP A 1 504 ? -16.119 32.676  -33.925 1.00 48.27  ? 504 TRP A NE1   1 
ATOM   4166 C  CE2   . TRP A 1 504 ? -17.413 32.746  -33.479 1.00 50.70  ? 504 TRP A CE2   1 
ATOM   4167 C  CE3   . TRP A 1 504 ? -19.003 31.313  -32.358 1.00 48.13  ? 504 TRP A CE3   1 
ATOM   4168 C  CZ2   . TRP A 1 504 ? -18.330 33.794  -33.541 1.00 47.92  ? 504 TRP A CZ2   1 
ATOM   4169 C  CZ3   . TRP A 1 504 ? -19.911 32.354  -32.422 1.00 45.25  ? 504 TRP A CZ3   1 
ATOM   4170 C  CH2   . TRP A 1 504 ? -19.571 33.578  -33.008 1.00 49.95  ? 504 TRP A CH2   1 
ATOM   4171 N  N     . TYR A 1 505 ? -16.578 25.892  -34.117 1.00 51.44  ? 505 TYR A N     1 
ATOM   4172 C  CA    . TYR A 1 505 ? -16.076 24.536  -33.955 1.00 51.10  ? 505 TYR A CA    1 
ATOM   4173 C  C     . TYR A 1 505 ? -14.625 24.446  -34.411 1.00 50.70  ? 505 TYR A C     1 
ATOM   4174 O  O     . TYR A 1 505 ? -14.229 25.058  -35.407 1.00 47.29  ? 505 TYR A O     1 
ATOM   4175 C  CB    . TYR A 1 505 ? -16.949 23.563  -34.748 1.00 47.26  ? 505 TYR A CB    1 
ATOM   4176 C  CG    . TYR A 1 505 ? -16.411 22.152  -34.854 1.00 50.28  ? 505 TYR A CG    1 
ATOM   4177 C  CD1   . TYR A 1 505 ? -16.582 21.241  -33.820 1.00 53.31  ? 505 TYR A CD1   1 
ATOM   4178 C  CD2   . TYR A 1 505 ? -15.752 21.724  -35.999 1.00 50.06  ? 505 TYR A CD2   1 
ATOM   4179 C  CE1   . TYR A 1 505 ? -16.102 19.946  -33.919 1.00 54.80  ? 505 TYR A CE1   1 
ATOM   4180 C  CE2   . TYR A 1 505 ? -15.266 20.433  -36.106 1.00 53.30  ? 505 TYR A CE2   1 
ATOM   4181 C  CZ    . TYR A 1 505 ? -15.445 19.548  -35.064 1.00 51.95  ? 505 TYR A CZ    1 
ATOM   4182 O  OH    . TYR A 1 505 ? -14.965 18.263  -35.169 1.00 56.52  ? 505 TYR A OH    1 
ATOM   4183 N  N     . CYS A 1 506 ? -13.826 23.679  -33.666 1.00 47.38  ? 506 CYS A N     1 
ATOM   4184 C  CA    . CYS A 1 506 ? -12.419 23.468  -34.019 1.00 46.18  ? 506 CYS A CA    1 
ATOM   4185 C  C     . CYS A 1 506 ? -11.942 22.235  -33.243 1.00 44.58  ? 506 CYS A C     1 
ATOM   4186 O  O     . CYS A 1 506 ? -11.516 22.345  -32.094 1.00 47.85  ? 506 CYS A O     1 
ATOM   4187 C  CB    . CYS A 1 506 ? -11.567 24.685  -33.708 1.00 54.80  ? 506 CYS A CB    1 
ATOM   4188 S  SG    . CYS A 1 506 ? -9.792  24.467  -34.003 1.00 67.82  ? 506 CYS A SG    1 
ATOM   4189 N  N     . LYS A 1 507 ? -12.032 21.069  -33.889 1.00 46.65  ? 507 LYS A N     1 
ATOM   4190 C  CA    . LYS A 1 507 ? -11.589 19.834  -33.247 1.00 56.95  ? 507 LYS A CA    1 
ATOM   4191 C  C     . LYS A 1 507 ? -10.093 19.871  -32.961 1.00 56.42  ? 507 LYS A C     1 
ATOM   4192 O  O     . LYS A 1 507 ? -9.636  19.380  -31.919 1.00 53.40  ? 507 LYS A O     1 
ATOM   4193 C  CB    . LYS A 1 507 ? -11.950 18.635  -34.126 1.00 50.67  ? 507 LYS A CB    1 
ATOM   4194 C  CG    . LYS A 1 507 ? -11.203 17.353  -33.799 1.00 58.19  ? 507 LYS A CG    1 
ATOM   4195 C  CD    . LYS A 1 507 ? -11.112 16.451  -35.021 1.00 70.82  ? 507 LYS A CD    1 
ATOM   4196 C  CE    . LYS A 1 507 ? -9.667  16.208  -35.430 1.00 79.53  ? 507 LYS A CE    1 
ATOM   4197 N  NZ    . LYS A 1 507 ? -8.905  15.480  -34.379 1.00 78.64  ? 507 LYS A NZ    1 
ATOM   4198 N  N     . GLU A 1 508 ? -9.314  20.457  -33.875 1.00 45.17  ? 508 GLU A N     1 
ATOM   4199 C  CA    . GLU A 1 508 ? -7.879  20.593  -33.653 1.00 58.93  ? 508 GLU A CA    1 
ATOM   4200 C  C     . GLU A 1 508 ? -7.593  21.389  -32.386 1.00 54.38  ? 508 GLU A C     1 
ATOM   4201 O  O     . GLU A 1 508 ? -6.733  21.004  -31.586 1.00 49.92  ? 508 GLU A O     1 
ATOM   4202 C  CB    . GLU A 1 508 ? -7.221  21.254  -34.864 1.00 58.01  ? 508 GLU A CB    1 
ATOM   4203 C  CG    . GLU A 1 508 ? -7.422  20.498  -36.169 1.00 61.95  ? 508 GLU A CG    1 
ATOM   4204 C  CD    . GLU A 1 508 ? -8.632  20.980  -36.948 1.00 75.24  ? 508 GLU A CD    1 
ATOM   4205 O  OE1   . GLU A 1 508 ? -9.582  21.499  -36.321 1.00 71.48  ? 508 GLU A OE1   1 
ATOM   4206 O  OE2   . GLU A 1 508 ? -8.635  20.835  -38.189 1.00 82.81  ? 508 GLU A OE2   1 
ATOM   4207 N  N     . CYS A 1 509 ? -8.318  22.491  -32.179 1.00 43.52  ? 509 CYS A N     1 
ATOM   4208 C  CA    . CYS A 1 509 ? -8.126  23.302  -30.980 1.00 43.02  ? 509 CYS A CA    1 
ATOM   4209 C  C     . CYS A 1 509 ? -8.410  22.497  -29.716 1.00 46.79  ? 509 CYS A C     1 
ATOM   4210 O  O     . CYS A 1 509 ? -7.631  22.526  -28.755 1.00 47.84  ? 509 CYS A O     1 
ATOM   4211 C  CB    . CYS A 1 509 ? -9.023  24.542  -31.037 1.00 42.61  ? 509 CYS A CB    1 
ATOM   4212 S  SG    . CYS A 1 509 ? -8.877  25.552  -32.539 1.00 53.46  ? 509 CYS A SG    1 
ATOM   4213 N  N     . ALA A 1 510 ? -9.526  21.764  -29.701 1.00 43.86  ? 510 ALA A N     1 
ATOM   4214 C  CA    . ALA A 1 510 ? -9.917  21.035  -28.499 1.00 47.19  ? 510 ALA A CA    1 
ATOM   4215 C  C     . ALA A 1 510 ? -8.934  19.912  -28.186 1.00 48.83  ? 510 ALA A C     1 
ATOM   4216 O  O     . ALA A 1 510 ? -8.527  19.732  -27.028 1.00 50.86  ? 510 ALA A O     1 
ATOM   4217 C  CB    . ALA A 1 510 ? -11.334 20.486  -28.661 1.00 54.99  ? 510 ALA A CB    1 
ATOM   4218 N  N     . GLU A 1 511 ? -8.540  19.141  -29.205 1.00 49.82  ? 511 GLU A N     1 
ATOM   4219 C  CA    . GLU A 1 511 ? -7.592  18.061  -28.956 1.00 54.68  ? 511 GLU A CA    1 
ATOM   4220 C  C     . GLU A 1 511 ? -6.212  18.600  -28.597 1.00 48.91  ? 511 GLU A C     1 
ATOM   4221 O  O     . GLU A 1 511 ? -5.497  17.981  -27.799 1.00 55.58  ? 511 GLU A O     1 
ATOM   4222 C  CB    . GLU A 1 511 ? -7.525  17.118  -30.160 1.00 48.61  ? 511 GLU A CB    1 
ATOM   4223 C  CG    . GLU A 1 511 ? -6.820  17.661  -31.386 1.00 61.88  ? 511 GLU A CG    1 
ATOM   4224 C  CD    . GLU A 1 511 ? -6.743  16.631  -32.496 1.00 68.95  ? 511 GLU A CD    1 
ATOM   4225 O  OE1   . GLU A 1 511 ? -7.048  15.449  -32.228 1.00 71.16  ? 511 GLU A OE1   1 
ATOM   4226 O  OE2   . GLU A 1 511 ? -6.378  16.997  -33.633 1.00 72.37  ? 511 GLU A OE2   1 
ATOM   4227 N  N     . SER A 1 512 ? -5.833  19.763  -29.132 1.00 53.05  ? 512 SER A N     1 
ATOM   4228 C  CA    . SER A 1 512 ? -4.601  20.405  -28.693 1.00 54.87  ? 512 SER A CA    1 
ATOM   4229 C  C     . SER A 1 512 ? -4.676  20.757  -27.214 1.00 52.70  ? 512 SER A C     1 
ATOM   4230 O  O     . SER A 1 512 ? -3.740  20.488  -26.451 1.00 50.75  ? 512 SER A O     1 
ATOM   4231 C  CB    . SER A 1 512 ? -4.334  21.652  -29.535 1.00 45.78  ? 512 SER A CB    1 
ATOM   4232 O  OG    . SER A 1 512 ? -4.207  21.319  -30.906 1.00 51.10  ? 512 SER A OG    1 
ATOM   4233 N  N     . VAL A 1 513 ? -5.792  21.358  -26.793 1.00 51.58  ? 513 VAL A N     1 
ATOM   4234 C  CA    . VAL A 1 513 ? -5.966  21.736  -25.390 1.00 49.71  ? 513 VAL A CA    1 
ATOM   4235 C  C     . VAL A 1 513 ? -5.841  20.513  -24.489 1.00 52.29  ? 513 VAL A C     1 
ATOM   4236 O  O     . VAL A 1 513 ? -5.149  20.537  -23.461 1.00 52.72  ? 513 VAL A O     1 
ATOM   4237 C  CB    . VAL A 1 513 ? -7.320  22.441  -25.194 1.00 45.51  ? 513 VAL A CB    1 
ATOM   4238 C  CG1   . VAL A 1 513 ? -7.657  22.559  -23.712 1.00 45.47  ? 513 VAL A CG1   1 
ATOM   4239 C  CG2   . VAL A 1 513 ? -7.302  23.805  -25.853 1.00 46.00  ? 513 VAL A CG2   1 
ATOM   4240 N  N     . THR A 1 514 ? -6.509  19.420  -24.864 1.00 54.42  ? 514 THR A N     1 
ATOM   4241 C  CA    . THR A 1 514 ? -6.485  18.244  -24.000 1.00 52.77  ? 514 THR A CA    1 
ATOM   4242 C  C     . THR A 1 514 ? -5.109  17.578  -23.988 1.00 52.94  ? 514 THR A C     1 
ATOM   4243 O  O     . THR A 1 514 ? -4.687  17.054  -22.948 1.00 57.00  ? 514 THR A O     1 
ATOM   4244 C  CB    . THR A 1 514 ? -7.586  17.262  -24.412 1.00 55.72  ? 514 THR A CB    1 
ATOM   4245 O  OG1   . THR A 1 514 ? -7.742  16.270  -23.392 1.00 78.91  ? 514 THR A OG1   1 
ATOM   4246 C  CG2   . THR A 1 514 ? -7.268  16.584  -25.723 1.00 50.40  ? 514 THR A CG2   1 
ATOM   4247 N  N     . ALA A 1 515 ? -4.379  17.621  -25.109 1.00 54.12  ? 515 ALA A N     1 
ATOM   4248 C  CA    . ALA A 1 515 ? -3.017  17.098  -25.112 1.00 53.28  ? 515 ALA A CA    1 
ATOM   4249 C  C     . ALA A 1 515 ? -2.105  17.936  -24.224 1.00 50.59  ? 515 ALA A C     1 
ATOM   4250 O  O     . ALA A 1 515 ? -1.272  17.390  -23.487 1.00 56.49  ? 515 ALA A O     1 
ATOM   4251 C  CB    . ALA A 1 515 ? -2.478  17.043  -26.540 1.00 55.55  ? 515 ALA A CB    1 
ATOM   4252 N  N     . TRP A 1 516 ? -2.242  19.264  -24.289 1.00 53.15  ? 516 TRP A N     1 
ATOM   4253 C  CA    . TRP A 1 516 ? -1.509  20.135  -23.375 1.00 52.69  ? 516 TRP A CA    1 
ATOM   4254 C  C     . TRP A 1 516 ? -1.791  19.755  -21.928 1.00 52.79  ? 516 TRP A C     1 
ATOM   4255 O  O     . TRP A 1 516 ? -0.869  19.642  -21.111 1.00 54.82  ? 516 TRP A O     1 
ATOM   4256 C  CB    . TRP A 1 516 ? -1.886  21.602  -23.603 1.00 59.91  ? 516 TRP A CB    1 
ATOM   4257 C  CG    . TRP A 1 516 ? -1.331  22.271  -24.835 1.00 69.36  ? 516 TRP A CG    1 
ATOM   4258 C  CD1   . TRP A 1 516 ? -2.032  22.667  -25.938 1.00 73.53  ? 516 TRP A CD1   1 
ATOM   4259 C  CD2   . TRP A 1 516 ? 0.027   22.664  -25.066 1.00 65.14  ? 516 TRP A CD2   1 
ATOM   4260 N  NE1   . TRP A 1 516 ? -1.195  23.262  -26.848 1.00 65.20  ? 516 TRP A NE1   1 
ATOM   4261 C  CE2   . TRP A 1 516 ? 0.075   23.273  -26.337 1.00 61.49  ? 516 TRP A CE2   1 
ATOM   4262 C  CE3   . TRP A 1 516 ? 1.207   22.551  -24.327 1.00 57.07  ? 516 TRP A CE3   1 
ATOM   4263 C  CZ2   . TRP A 1 516 ? 1.253   23.767  -26.882 1.00 61.65  ? 516 TRP A CZ2   1 
ATOM   4264 C  CZ3   . TRP A 1 516 ? 2.378   23.042  -24.872 1.00 92.89  ? 516 TRP A CZ3   1 
ATOM   4265 C  CH2   . TRP A 1 516 ? 2.393   23.641  -26.137 1.00 93.26  ? 516 TRP A CH2   1 
ATOM   4266 N  N     . GLY A 1 517 ? -3.071  19.578  -21.588 1.00 53.15  ? 517 GLY A N     1 
ATOM   4267 C  CA    . GLY A 1 517 ? -3.422  19.235  -20.217 1.00 46.17  ? 517 GLY A CA    1 
ATOM   4268 C  C     . GLY A 1 517 ? -2.801  17.928  -19.762 1.00 48.28  ? 517 GLY A C     1 
ATOM   4269 O  O     . GLY A 1 517 ? -2.254  17.838  -18.656 1.00 49.31  ? 517 GLY A O     1 
ATOM   4270 N  N     . ARG A 1 518 ? -2.881  16.898  -20.609 1.00 45.35  ? 518 ARG A N     1 
ATOM   4271 C  CA    . ARG A 1 518 ? -2.238  15.626  -20.296 1.00 53.25  ? 518 ARG A CA    1 
ATOM   4272 C  C     . ARG A 1 518 ? -0.747  15.815  -20.041 1.00 56.61  ? 518 ARG A C     1 
ATOM   4273 O  O     . ARG A 1 518 ? -0.206  15.325  -19.039 1.00 49.33  ? 518 ARG A O     1 
ATOM   4274 C  CB    . ARG A 1 518 ? -2.461  14.636  -21.438 1.00 56.36  ? 518 ARG A CB    1 
ATOM   4275 C  CG    . ARG A 1 518 ? -3.831  13.992  -21.455 1.00 60.40  ? 518 ARG A CG    1 
ATOM   4276 C  CD    . ARG A 1 518 ? -3.948  13.031  -22.622 1.00 57.89  ? 518 ARG A CD    1 
ATOM   4277 N  NE    . ARG A 1 518 ? -4.683  13.622  -23.733 1.00 66.14  ? 518 ARG A NE    1 
ATOM   4278 C  CZ    . ARG A 1 518 ? -4.265  13.615  -24.991 1.00 66.59  ? 518 ARG A CZ    1 
ATOM   4279 N  NH1   . ARG A 1 518 ? -3.115  13.060  -25.333 1.00 65.05  ? 518 ARG A NH1   1 
ATOM   4280 N  NH2   . ARG A 1 518 ? -5.022  14.177  -25.928 1.00 70.78  ? 518 ARG A NH2   1 
ATOM   4281 N  N     . GLU A 1 519 ? -0.065  16.523  -20.948 1.00 48.87  ? 519 GLU A N     1 
ATOM   4282 C  CA    . GLU A 1 519 ? 1.375   16.723  -20.808 1.00 55.35  ? 519 GLU A CA    1 
ATOM   4283 C  C     . GLU A 1 519 ? 1.707   17.422  -19.498 1.00 57.65  ? 519 GLU A C     1 
ATOM   4284 O  O     . GLU A 1 519 ? 2.593   16.985  -18.755 1.00 52.97  ? 519 GLU A O     1 
ATOM   4285 C  CB    . GLU A 1 519 ? 1.921   17.527  -21.988 1.00 59.84  ? 519 GLU A CB    1 
ATOM   4286 C  CG    . GLU A 1 519 ? 3.428   17.755  -21.920 1.00 77.99  ? 519 GLU A CG    1 
ATOM   4287 C  CD    . GLU A 1 519 ? 3.862   19.050  -22.584 1.00 96.43  ? 519 GLU A CD    1 
ATOM   4288 O  OE1   . GLU A 1 519 ? 3.815   19.133  -23.829 1.00 91.90  ? 519 GLU A OE1   1 
ATOM   4289 O  OE2   . GLU A 1 519 ? 4.251   19.989  -21.857 1.00 91.49  ? 519 GLU A OE2   1 
ATOM   4290 N  N     . TYR A 1 520 ? 0.999   18.513  -19.196 1.00 56.06  ? 520 TYR A N     1 
ATOM   4291 C  CA    . TYR A 1 520 ? 1.310   19.290  -18.001 1.00 52.28  ? 520 TYR A CA    1 
ATOM   4292 C  C     . TYR A 1 520 ? 1.067   18.481  -16.733 1.00 58.36  ? 520 TYR A C     1 
ATOM   4293 O  O     . TYR A 1 520 ? 1.884   18.509  -15.802 1.00 60.97  ? 520 TYR A O     1 
ATOM   4294 C  CB    . TYR A 1 520 ? 0.490   20.580  -17.983 1.00 49.66  ? 520 TYR A CB    1 
ATOM   4295 C  CG    . TYR A 1 520 ? 1.007   21.652  -18.919 1.00 61.61  ? 520 TYR A CG    1 
ATOM   4296 C  CD1   . TYR A 1 520 ? 2.255   22.231  -18.724 1.00 62.24  ? 520 TYR A CD1   1 
ATOM   4297 C  CD2   . TYR A 1 520 ? 0.248   22.085  -19.997 1.00 53.72  ? 520 TYR A CD2   1 
ATOM   4298 C  CE1   . TYR A 1 520 ? 2.728   23.211  -19.578 1.00 59.37  ? 520 TYR A CE1   1 
ATOM   4299 C  CE2   . TYR A 1 520 ? 0.712   23.060  -20.856 1.00 61.63  ? 520 TYR A CE2   1 
ATOM   4300 C  CZ    . TYR A 1 520 ? 1.951   23.621  -20.642 1.00 58.75  ? 520 TYR A CZ    1 
ATOM   4301 O  OH    . TYR A 1 520 ? 2.411   24.594  -21.499 1.00 65.54  ? 520 TYR A OH    1 
ATOM   4302 N  N     . LEU A 1 521 ? -0.041  17.737  -16.681 1.00 51.20  ? 521 LEU A N     1 
ATOM   4303 C  CA    . LEU A 1 521 ? -0.346  16.979  -15.472 1.00 57.23  ? 521 LEU A CA    1 
ATOM   4304 C  C     . LEU A 1 521 ? 0.651   15.843  -15.264 1.00 54.58  ? 521 LEU A C     1 
ATOM   4305 O  O     . LEU A 1 521 ? 1.147   15.637  -14.146 1.00 51.91  ? 521 LEU A O     1 
ATOM   4306 C  CB    . LEU A 1 521 ? -1.774  16.444  -15.532 1.00 47.94  ? 521 LEU A CB    1 
ATOM   4307 C  CG    . LEU A 1 521 ? -2.148  15.516  -14.380 1.00 51.81  ? 521 LEU A CG    1 
ATOM   4308 C  CD1   . LEU A 1 521 ? -2.101  16.256  -13.053 1.00 45.90  ? 521 LEU A CD1   1 
ATOM   4309 C  CD2   . LEU A 1 521 ? -3.519  14.936  -14.622 1.00 58.31  ? 521 LEU A CD2   1 
ATOM   4310 N  N     . THR A 1 522 ? 0.957   15.088  -16.326 1.00 48.40  ? 522 THR A N     1 
ATOM   4311 C  CA    . THR A 1 522 ? 1.940   14.018  -16.187 1.00 60.82  ? 522 THR A CA    1 
ATOM   4312 C  C     . THR A 1 522 ? 3.318   14.570  -15.845 1.00 56.51  ? 522 THR A C     1 
ATOM   4313 O  O     . THR A 1 522 ? 4.067   13.943  -15.085 1.00 57.90  ? 522 THR A O     1 
ATOM   4314 C  CB    . THR A 1 522 ? 2.002   13.174  -17.462 1.00 60.07  ? 522 THR A CB    1 
ATOM   4315 O  OG1   . THR A 1 522 ? 2.340   14.005  -18.580 1.00 59.25  ? 522 THR A OG1   1 
ATOM   4316 C  CG2   . THR A 1 522 ? 0.663   12.493  -17.717 1.00 58.98  ? 522 THR A CG2   1 
ATOM   4317 N  N     . MET A 1 523 ? 3.661   15.747  -16.375 1.00 59.68  ? 523 MET A N     1 
ATOM   4318 C  CA    . MET A 1 523 ? 4.924   16.389  -16.029 1.00 62.85  ? 523 MET A CA    1 
ATOM   4319 C  C     . MET A 1 523 ? 4.975   16.721  -14.544 1.00 60.25  ? 523 MET A C     1 
ATOM   4320 O  O     . MET A 1 523 ? 5.971   16.440  -13.867 1.00 69.82  ? 523 MET A O     1 
ATOM   4321 C  CB    . MET A 1 523 ? 5.101   17.644  -16.891 1.00 57.72  ? 523 MET A CB    1 
ATOM   4322 C  CG    . MET A 1 523 ? 6.428   18.391  -16.760 1.00 71.31  ? 523 MET A CG    1 
ATOM   4323 S  SD    . MET A 1 523 ? 6.674   19.297  -15.216 1.00 77.38  ? 523 MET A SD    1 
ATOM   4324 C  CE    . MET A 1 523 ? 5.596   20.707  -15.454 1.00 71.74  ? 523 MET A CE    1 
ATOM   4325 N  N     . THR A 1 524 ? 3.909   17.335  -14.023 1.00 60.88  ? 524 THR A N     1 
ATOM   4326 C  CA    . THR A 1 524 ? 3.884   17.684  -12.606 1.00 59.39  ? 524 THR A CA    1 
ATOM   4327 C  C     . THR A 1 524 ? 3.968   16.440  -11.732 1.00 60.54  ? 524 THR A C     1 
ATOM   4328 O  O     . THR A 1 524 ? 4.637   16.450  -10.693 1.00 63.22  ? 524 THR A O     1 
ATOM   4329 C  CB    . THR A 1 524 ? 2.623   18.484  -12.282 1.00 59.54  ? 524 THR A CB    1 
ATOM   4330 O  OG1   . THR A 1 524 ? 1.478   17.809  -12.813 1.00 62.92  ? 524 THR A OG1   1 
ATOM   4331 C  CG2   . THR A 1 524 ? 2.710   19.878  -12.883 1.00 62.85  ? 524 THR A CG2   1 
ATOM   4332 N  N     . ILE A 1 525 ? 3.304   15.356  -12.142 1.00 65.68  ? 525 ILE A N     1 
ATOM   4333 C  CA    . ILE A 1 525 ? 3.374   14.111  -11.378 1.00 63.70  ? 525 ILE A CA    1 
ATOM   4334 C  C     . ILE A 1 525 ? 4.802   13.573  -11.367 1.00 63.62  ? 525 ILE A C     1 
ATOM   4335 O  O     . ILE A 1 525 ? 5.347   13.215  -10.311 1.00 56.58  ? 525 ILE A O     1 
ATOM   4336 C  CB    . ILE A 1 525 ? 2.385   13.078  -11.946 1.00 61.17  ? 525 ILE A CB    1 
ATOM   4337 C  CG1   . ILE A 1 525 ? 0.963   13.394  -11.478 1.00 57.37  ? 525 ILE A CG1   1 
ATOM   4338 C  CG2   . ILE A 1 525 ? 2.796   11.663  -11.545 1.00 52.59  ? 525 ILE A CG2   1 
ATOM   4339 C  CD1   . ILE A 1 525 ? -0.117  12.791  -12.349 1.00 50.90  ? 525 ILE A CD1   1 
ATOM   4340 N  N     . LYS A 1 526 ? 5.425   13.500  -12.547 1.00 57.74  ? 526 LYS A N     1 
ATOM   4341 C  CA    . LYS A 1 526 ? 6.797   13.012  -12.633 1.00 68.75  ? 526 LYS A CA    1 
ATOM   4342 C  C     . LYS A 1 526 ? 7.733   13.847  -11.770 1.00 69.56  ? 526 LYS A C     1 
ATOM   4343 O  O     . LYS A 1 526 ? 8.607   13.303  -11.085 1.00 68.52  ? 526 LYS A O     1 
ATOM   4344 C  CB    . LYS A 1 526 ? 7.265   13.015  -14.088 1.00 73.46  ? 526 LYS A CB    1 
ATOM   4345 C  CG    . LYS A 1 526 ? 8.737   12.670  -14.267 1.00 80.91  ? 526 LYS A CG    1 
ATOM   4346 C  CD    . LYS A 1 526 ? 9.011   12.066  -15.636 1.00 91.70  ? 526 LYS A CD    1 
ATOM   4347 C  CE    . LYS A 1 526 ? 10.298  12.617  -16.233 1.00 94.21  ? 526 LYS A CE    1 
ATOM   4348 N  NZ    . LYS A 1 526 ? 10.183  14.064  -16.579 1.00 97.92  ? 526 LYS A NZ    1 
ATOM   4349 N  N     . GLU A 1 527 ? 7.555   15.169  -11.775 1.00 68.74  ? 527 GLU A N     1 
ATOM   4350 C  CA    . GLU A 1 527 ? 8.454   16.030  -11.013 1.00 69.84  ? 527 GLU A CA    1 
ATOM   4351 C  C     . GLU A 1 527 ? 8.227   15.888  -9.513  1.00 71.72  ? 527 GLU A C     1 
ATOM   4352 O  O     . GLU A 1 527 ? 9.191   15.839  -8.740  1.00 76.31  ? 527 GLU A O     1 
ATOM   4353 C  CB    . GLU A 1 527 ? 8.291   17.485  -11.449 1.00 72.17  ? 527 GLU A CB    1 
ATOM   4354 C  CG    . GLU A 1 527 ? 8.754   17.754  -12.870 1.00 73.41  ? 527 GLU A CG    1 
ATOM   4355 C  CD    . GLU A 1 527 ? 10.229  18.095  -12.954 1.00 83.73  ? 527 GLU A CD    1 
ATOM   4356 O  OE1   . GLU A 1 527 ? 10.787  18.593  -11.953 1.00 84.08  ? 527 GLU A OE1   1 
ATOM   4357 O  OE2   . GLU A 1 527 ? 10.831  17.869  -14.025 1.00 91.45  ? 527 GLU A OE2   1 
ATOM   4358 N  N     . ILE A 1 528 ? 6.965   15.819  -9.078  1.00 67.95  ? 528 ILE A N     1 
ATOM   4359 C  CA    . ILE A 1 528 ? 6.702   15.687  -7.649  1.00 63.42  ? 528 ILE A CA    1 
ATOM   4360 C  C     . ILE A 1 528 ? 7.169   14.331  -7.139  1.00 67.16  ? 528 ILE A C     1 
ATOM   4361 O  O     . ILE A 1 528 ? 7.497   14.186  -5.955  1.00 68.06  ? 528 ILE A O     1 
ATOM   4362 C  CB    . ILE A 1 528 ? 5.211   15.926  -7.340  1.00 63.84  ? 528 ILE A CB    1 
ATOM   4363 C  CG1   . ILE A 1 528 ? 5.008   16.172  -5.845  1.00 60.94  ? 528 ILE A CG1   1 
ATOM   4364 C  CG2   . ILE A 1 528 ? 4.361   14.751  -7.782  1.00 63.66  ? 528 ILE A CG2   1 
ATOM   4365 C  CD1   . ILE A 1 528 ? 3.652   16.737  -5.497  1.00 66.17  ? 528 ILE A CD1   1 
ATOM   4366 N  N     . GLU A 1 529 ? 7.224   13.320  -8.009  1.00 68.56  ? 529 GLU A N     1 
ATOM   4367 C  CA    . GLU A 1 529 ? 7.666   12.010  -7.545  1.00 75.67  ? 529 GLU A CA    1 
ATOM   4368 C  C     . GLU A 1 529 ? 9.187   11.891  -7.559  1.00 74.36  ? 529 GLU A C     1 
ATOM   4369 O  O     . GLU A 1 529 ? 9.794   11.496  -6.557  1.00 74.04  ? 529 GLU A O     1 
ATOM   4370 C  CB    . GLU A 1 529 ? 7.028   10.908  -8.392  1.00 74.93  ? 529 GLU A CB    1 
ATOM   4371 C  CG    . GLU A 1 529 ? 5.549   10.701  -8.105  1.00 72.94  ? 529 GLU A CG    1 
ATOM   4372 C  CD    . GLU A 1 529 ? 5.012   9.407   -8.683  1.00 73.87  ? 529 GLU A CD    1 
ATOM   4373 O  OE1   . GLU A 1 529 ? 5.388   9.064   -9.824  1.00 81.09  ? 529 GLU A OE1   1 
ATOM   4374 O  OE2   . GLU A 1 529 ? 4.212   8.735   -7.997  1.00 69.46  ? 529 GLU A OE2   1 
ATOM   4375 N  N     . GLU A 1 530 ? 9.822   12.240  -8.680  1.00 74.35  ? 530 GLU A N     1 
ATOM   4376 C  CA    . GLU A 1 530 ? 11.256  12.003  -8.820  1.00 79.71  ? 530 GLU A CA    1 
ATOM   4377 C  C     . GLU A 1 530 ? 12.087  12.951  -7.965  1.00 83.63  ? 530 GLU A C     1 
ATOM   4378 O  O     . GLU A 1 530 ? 13.141  12.555  -7.455  1.00 84.05  ? 530 GLU A O     1 
ATOM   4379 C  CB    . GLU A 1 530 ? 11.670  12.130  -10.286 1.00 79.18  ? 530 GLU A CB    1 
ATOM   4380 C  CG    . GLU A 1 530 ? 11.018  11.118  -11.212 1.00 85.50  ? 530 GLU A CG    1 
ATOM   4381 C  CD    . GLU A 1 530 ? 11.510  11.242  -12.641 1.00 99.91  ? 530 GLU A CD    1 
ATOM   4382 O  OE1   . GLU A 1 530 ? 12.334  12.142  -12.910 1.00 85.31  ? 530 GLU A OE1   1 
ATOM   4383 O  OE2   . GLU A 1 530 ? 11.073  10.441  -13.494 1.00 109.02 ? 530 GLU A OE2   1 
ATOM   4384 N  N     . LYS A 1 531 ? 11.642  14.196  -7.796  1.00 81.66  ? 531 LYS A N     1 
ATOM   4385 C  CA    . LYS A 1 531 ? 12.465  15.218  -7.167  1.00 80.94  ? 531 LYS A CA    1 
ATOM   4386 C  C     . LYS A 1 531 ? 12.003  15.621  -5.775  1.00 77.78  ? 531 LYS A C     1 
ATOM   4387 O  O     . LYS A 1 531 ? 12.732  16.347  -5.090  1.00 87.37  ? 531 LYS A O     1 
ATOM   4388 C  CB    . LYS A 1 531 ? 12.529  16.464  -8.061  1.00 82.22  ? 531 LYS A CB    1 
ATOM   4389 C  CG    . LYS A 1 531 ? 12.796  16.143  -9.521  1.00 82.77  ? 531 LYS A CG    1 
ATOM   4390 C  CD    . LYS A 1 531 ? 13.432  17.313  -10.246 1.00 81.45  ? 531 LYS A CD    1 
ATOM   4391 C  CE    . LYS A 1 531 ? 13.711  16.965  -11.698 1.00 88.02  ? 531 LYS A CE    1 
ATOM   4392 N  NZ    . LYS A 1 531 ? 13.699  18.166  -12.577 1.00 92.02  ? 531 LYS A NZ    1 
ATOM   4393 N  N     . TYR A 1 532 ? 10.826  15.179  -5.333  1.00 77.73  ? 532 TYR A N     1 
ATOM   4394 C  CA    . TYR A 1 532 ? 10.375  15.470  -3.982  1.00 73.68  ? 532 TYR A CA    1 
ATOM   4395 C  C     . TYR A 1 532 ? 9.922   14.237  -3.215  1.00 71.03  ? 532 TYR A C     1 
ATOM   4396 O  O     . TYR A 1 532 ? 9.430   14.376  -2.090  1.00 78.02  ? 532 TYR A O     1 
ATOM   4397 C  CB    . TYR A 1 532 ? 9.243   16.509  -4.001  1.00 72.01  ? 532 TYR A CB    1 
ATOM   4398 C  CG    . TYR A 1 532 ? 9.745   17.927  -4.155  1.00 66.91  ? 532 TYR A CG    1 
ATOM   4399 C  CD1   . TYR A 1 532 ? 10.141  18.415  -5.395  1.00 70.76  ? 532 TYR A CD1   1 
ATOM   4400 C  CD2   . TYR A 1 532 ? 9.844   18.771  -3.058  1.00 71.28  ? 532 TYR A CD2   1 
ATOM   4401 C  CE1   . TYR A 1 532 ? 10.609  19.708  -5.539  1.00 72.92  ? 532 TYR A CE1   1 
ATOM   4402 C  CE2   . TYR A 1 532 ? 10.312  20.065  -3.192  1.00 78.56  ? 532 TYR A CE2   1 
ATOM   4403 C  CZ    . TYR A 1 532 ? 10.693  20.529  -4.434  1.00 75.74  ? 532 TYR A CZ    1 
ATOM   4404 O  OH    . TYR A 1 532 ? 11.158  21.816  -4.572  1.00 73.97  ? 532 TYR A OH    1 
ATOM   4405 N  N     . GLY A 1 533 ? 10.076  13.042  -3.781  1.00 73.26  ? 533 GLY A N     1 
ATOM   4406 C  CA    . GLY A 1 533 ? 9.771   11.825  -3.057  1.00 75.17  ? 533 GLY A CA    1 
ATOM   4407 C  C     . GLY A 1 533 ? 8.307   11.585  -2.773  1.00 80.94  ? 533 GLY A C     1 
ATOM   4408 O  O     . GLY A 1 533 ? 7.983   10.814  -1.866  1.00 79.53  ? 533 GLY A O     1 
ATOM   4409 N  N     . PHE A 1 534 ? 7.408   12.223  -3.517  1.00 76.50  ? 534 PHE A N     1 
ATOM   4410 C  CA    . PHE A 1 534 ? 5.987   11.990  -3.329  1.00 73.70  ? 534 PHE A CA    1 
ATOM   4411 C  C     . PHE A 1 534 ? 5.558   10.709  -4.038  1.00 77.60  ? 534 PHE A C     1 
ATOM   4412 O  O     . PHE A 1 534 ? 6.251   10.187  -4.916  1.00 73.08  ? 534 PHE A O     1 
ATOM   4413 C  CB    . PHE A 1 534 ? 5.166   13.168  -3.859  1.00 73.01  ? 534 PHE A CB    1 
ATOM   4414 C  CG    . PHE A 1 534 ? 4.980   14.281  -2.866  1.00 75.92  ? 534 PHE A CG    1 
ATOM   4415 C  CD1   . PHE A 1 534 ? 5.975   15.226  -2.669  1.00 76.91  ? 534 PHE A CD1   1 
ATOM   4416 C  CD2   . PHE A 1 534 ? 3.806   14.390  -2.139  1.00 70.77  ? 534 PHE A CD2   1 
ATOM   4417 C  CE1   . PHE A 1 534 ? 5.805   16.253  -1.758  1.00 73.74  ? 534 PHE A CE1   1 
ATOM   4418 C  CE2   . PHE A 1 534 ? 3.631   15.415  -1.227  1.00 70.04  ? 534 PHE A CE2   1 
ATOM   4419 C  CZ    . PHE A 1 534 ? 4.631   16.347  -1.037  1.00 74.17  ? 534 PHE A CZ    1 
ATOM   4420 N  N     . LYS A 1 535 ? 4.396   10.199  -3.638  1.00 79.06  ? 535 LYS A N     1 
ATOM   4421 C  CA    . LYS A 1 535 ? 3.737   9.097   -4.327  1.00 73.07  ? 535 LYS A CA    1 
ATOM   4422 C  C     . LYS A 1 535 ? 2.325   9.536   -4.678  1.00 73.85  ? 535 LYS A C     1 
ATOM   4423 O  O     . LYS A 1 535 ? 1.541   9.887   -3.790  1.00 72.07  ? 535 LYS A O     1 
ATOM   4424 C  CB    . LYS A 1 535 ? 3.712   7.829   -3.472  1.00 70.65  ? 535 LYS A CB    1 
ATOM   4425 C  CG    . LYS A 1 535 ? 3.855   6.547   -4.282  1.00 78.52  ? 535 LYS A CG    1 
ATOM   4426 C  CD    . LYS A 1 535 ? 2.500   5.974   -4.669  1.00 73.65  ? 535 LYS A CD    1 
ATOM   4427 C  CE    . LYS A 1 535 ? 2.648   4.707   -5.501  1.00 73.52  ? 535 LYS A CE    1 
ATOM   4428 N  NZ    . LYS A 1 535 ? 3.302   4.975   -6.811  1.00 67.33  ? 535 LYS A NZ    1 
ATOM   4429 N  N     . VAL A 1 536 ? 2.008   9.526   -5.967  1.00 71.09  ? 536 VAL A N     1 
ATOM   4430 C  CA    . VAL A 1 536 ? 0.688   9.935   -6.429  1.00 69.54  ? 536 VAL A CA    1 
ATOM   4431 C  C     . VAL A 1 536 ? -0.281  8.778   -6.223  1.00 67.50  ? 536 VAL A C     1 
ATOM   4432 O  O     . VAL A 1 536 ? -0.137  7.716   -6.839  1.00 69.19  ? 536 VAL A O     1 
ATOM   4433 C  CB    . VAL A 1 536 ? 0.728   10.371  -7.900  1.00 68.45  ? 536 VAL A CB    1 
ATOM   4434 C  CG1   . VAL A 1 536 ? -0.668  10.721  -8.382  1.00 63.08  ? 536 VAL A CG1   1 
ATOM   4435 C  CG2   . VAL A 1 536 ? 1.675   11.550  -8.072  1.00 66.99  ? 536 VAL A CG2   1 
ATOM   4436 N  N     . ILE A 1 537 ? -1.266  8.978   -5.348  1.00 66.11  ? 537 ILE A N     1 
ATOM   4437 C  CA    . ILE A 1 537 ? -2.269  7.948   -5.101  1.00 67.10  ? 537 ILE A CA    1 
ATOM   4438 C  C     . ILE A 1 537 ? -3.275  7.895   -6.242  1.00 72.43  ? 537 ILE A C     1 
ATOM   4439 O  O     . ILE A 1 537 ? -3.553  6.827   -6.801  1.00 72.68  ? 537 ILE A O     1 
ATOM   4440 C  CB    . ILE A 1 537 ? -2.970  8.194   -3.752  1.00 65.29  ? 537 ILE A CB    1 
ATOM   4441 C  CG1   . ILE A 1 537 ? -1.963  8.163   -2.603  1.00 68.57  ? 537 ILE A CG1   1 
ATOM   4442 C  CG2   . ILE A 1 537 ? -4.079  7.176   -3.533  1.00 69.57  ? 537 ILE A CG2   1 
ATOM   4443 C  CD1   . ILE A 1 537 ? -1.678  9.521   -2.016  1.00 71.52  ? 537 ILE A CD1   1 
ATOM   4444 N  N     . TYR A 1 538 ? -3.835  9.047   -6.602  1.00 67.50  ? 538 TYR A N     1 
ATOM   4445 C  CA    . TYR A 1 538 ? -4.868  9.133   -7.621  1.00 64.21  ? 538 TYR A CA    1 
ATOM   4446 C  C     . TYR A 1 538 ? -4.695  10.450  -8.363  1.00 59.37  ? 538 TYR A C     1 
ATOM   4447 O  O     . TYR A 1 538 ? -4.157  11.415  -7.817  1.00 57.27  ? 538 TYR A O     1 
ATOM   4448 C  CB    . TYR A 1 538 ? -6.264  9.027   -6.991  1.00 61.41  ? 538 TYR A CB    1 
ATOM   4449 C  CG    . TYR A 1 538 ? -7.418  9.189   -7.952  1.00 62.20  ? 538 TYR A CG    1 
ATOM   4450 C  CD1   . TYR A 1 538 ? -7.489  8.443   -9.121  1.00 65.03  ? 538 TYR A CD1   1 
ATOM   4451 C  CD2   . TYR A 1 538 ? -8.448  10.078  -7.679  1.00 61.13  ? 538 TYR A CD2   1 
ATOM   4452 C  CE1   . TYR A 1 538 ? -8.550  8.585   -9.995  1.00 66.63  ? 538 TYR A CE1   1 
ATOM   4453 C  CE2   . TYR A 1 538 ? -9.511  10.227  -8.544  1.00 61.30  ? 538 TYR A CE2   1 
ATOM   4454 C  CZ    . TYR A 1 538 ? -9.558  9.480   -9.700  1.00 65.10  ? 538 TYR A CZ    1 
ATOM   4455 O  OH    . TYR A 1 538 ? -10.619 9.631   -10.562 1.00 64.31  ? 538 TYR A OH    1 
ATOM   4456 N  N     . SER A 1 539 ? -5.140  10.481  -9.615  1.00 60.72  ? 539 SER A N     1 
ATOM   4457 C  CA    . SER A 1 539 ? -4.988  11.674  -10.441 1.00 63.41  ? 539 SER A CA    1 
ATOM   4458 C  C     . SER A 1 539 ? -6.064  11.680  -11.512 1.00 62.20  ? 539 SER A C     1 
ATOM   4459 O  O     . SER A 1 539 ? -6.100  10.779  -12.355 1.00 67.58  ? 539 SER A O     1 
ATOM   4460 C  CB    . SER A 1 539 ? -3.598  11.724  -11.079 1.00 62.30  ? 539 SER A CB    1 
ATOM   4461 O  OG    . SER A 1 539 ? -3.500  12.798  -11.996 1.00 59.63  ? 539 SER A OG    1 
ATOM   4462 N  N     . ASP A 1 540 ? -6.931  12.691  -11.484 1.00 62.95  ? 540 ASP A N     1 
ATOM   4463 C  CA    . ASP A 1 540 ? -7.905  12.850  -12.555 1.00 67.18  ? 540 ASP A CA    1 
ATOM   4464 C  C     . ASP A 1 540 ? -7.328  13.760  -13.631 1.00 55.75  ? 540 ASP A C     1 
ATOM   4465 O  O     . ASP A 1 540 ? -6.175  13.579  -14.028 1.00 87.24  ? 540 ASP A O     1 
ATOM   4466 C  CB    . ASP A 1 540 ? -9.232  13.388  -12.021 1.00 65.15  ? 540 ASP A CB    1 
ATOM   4467 C  CG    . ASP A 1 540 ? -10.430 12.754  -12.707 1.00 71.96  ? 540 ASP A CG    1 
ATOM   4468 O  OD1   . ASP A 1 540 ? -10.450 12.731  -13.957 1.00 55.97  ? 540 ASP A OD1   1 
ATOM   4469 O  OD2   . ASP A 1 540 ? -11.341 12.268  -12.003 1.00 67.59  ? 540 ASP A OD2   1 
ATOM   4470 N  N     . THR A 1 541 ? -8.092  14.744  -14.100 1.00 54.89  ? 541 THR A N     1 
ATOM   4471 C  CA    . THR A 1 541 ? -7.695  15.453  -15.312 1.00 59.93  ? 541 THR A CA    1 
ATOM   4472 C  C     . THR A 1 541 ? -6.882  16.716  -15.049 1.00 63.94  ? 541 THR A C     1 
ATOM   4473 O  O     . THR A 1 541 ? -6.102  17.126  -15.917 1.00 55.84  ? 541 THR A O     1 
ATOM   4474 C  CB    . THR A 1 541 ? -8.931  15.807  -16.147 1.00 66.39  ? 541 THR A CB    1 
ATOM   4475 O  OG1   . THR A 1 541 ? -8.560  15.907  -17.526 1.00 74.79  ? 541 THR A OG1   1 
ATOM   4476 C  CG2   . THR A 1 541 ? -9.523  17.136  -15.713 1.00 60.52  ? 541 THR A CG2   1 
ATOM   4477 N  N     . ASP A 1 542 ? -7.031  17.344  -13.879 1.00 59.85  ? 542 ASP A N     1 
ATOM   4478 C  CA    . ASP A 1 542 ? -6.385  18.624  -13.616 1.00 52.87  ? 542 ASP A CA    1 
ATOM   4479 C  C     . ASP A 1 542 ? -5.677  18.658  -12.269 1.00 53.60  ? 542 ASP A C     1 
ATOM   4480 O  O     . ASP A 1 542 ? -5.240  19.732  -11.843 1.00 50.21  ? 542 ASP A O     1 
ATOM   4481 C  CB    . ASP A 1 542 ? -7.402  19.771  -13.686 1.00 60.69  ? 542 ASP A CB    1 
ATOM   4482 C  CG    . ASP A 1 542 ? -8.505  19.635  -12.654 1.00 58.05  ? 542 ASP A CG    1 
ATOM   4483 O  OD1   . ASP A 1 542 ? -8.772  18.496  -12.222 1.00 57.23  ? 542 ASP A OD1   1 
ATOM   4484 O  OD2   . ASP A 1 542 ? -9.096  20.666  -12.270 1.00 63.17  ? 542 ASP A OD2   1 
ATOM   4485 N  N     . GLY A 1 543 ? -5.558  17.524  -11.590 1.00 48.39  ? 543 GLY A N     1 
ATOM   4486 C  CA    . GLY A 1 543 ? -4.919  17.507  -10.289 1.00 52.52  ? 543 GLY A CA    1 
ATOM   4487 C  C     . GLY A 1 543 ? -4.674  16.086  -9.840  1.00 56.89  ? 543 GLY A C     1 
ATOM   4488 O  O     . GLY A 1 543 ? -4.992  15.122  -10.541 1.00 60.49  ? 543 GLY A O     1 
ATOM   4489 N  N     . PHE A 1 544 ? -4.100  15.971  -8.646  1.00 53.31  ? 544 PHE A N     1 
ATOM   4490 C  CA    . PHE A 1 544 ? -3.779  14.664  -8.094  1.00 52.02  ? 544 PHE A CA    1 
ATOM   4491 C  C     . PHE A 1 544 ? -3.697  14.745  -6.577  1.00 53.28  ? 544 PHE A C     1 
ATOM   4492 O  O     . PHE A 1 544 ? -3.479  15.813  -5.993  1.00 54.43  ? 544 PHE A O     1 
ATOM   4493 C  CB    . PHE A 1 544 ? -2.471  14.113  -8.674  1.00 56.11  ? 544 PHE A CB    1 
ATOM   4494 C  CG    . PHE A 1 544 ? -1.278  14.999  -8.443  1.00 56.49  ? 544 PHE A CG    1 
ATOM   4495 C  CD1   . PHE A 1 544 ? -0.516  14.872  -7.293  1.00 50.83  ? 544 PHE A CD1   1 
ATOM   4496 C  CD2   . PHE A 1 544 ? -0.910  15.948  -9.382  1.00 58.47  ? 544 PHE A CD2   1 
ATOM   4497 C  CE1   . PHE A 1 544 ? 0.580   15.683  -7.078  1.00 61.25  ? 544 PHE A CE1   1 
ATOM   4498 C  CE2   . PHE A 1 544 ? 0.189   16.761  -9.173  1.00 56.75  ? 544 PHE A CE2   1 
ATOM   4499 C  CZ    . PHE A 1 544 ? 0.934   16.627  -8.019  1.00 58.94  ? 544 PHE A CZ    1 
ATOM   4500 N  N     . PHE A 1 545 ? -3.879  13.584  -5.953  1.00 54.85  ? 545 PHE A N     1 
ATOM   4501 C  CA    . PHE A 1 545 ? -3.645  13.383  -4.532  1.00 55.74  ? 545 PHE A CA    1 
ATOM   4502 C  C     . PHE A 1 545 ? -2.285  12.722  -4.357  1.00 61.46  ? 545 PHE A C     1 
ATOM   4503 O  O     . PHE A 1 545 ? -1.952  11.776  -5.080  1.00 59.80  ? 545 PHE A O     1 
ATOM   4504 C  CB    . PHE A 1 545 ? -4.733  12.503  -3.914  1.00 55.67  ? 545 PHE A CB    1 
ATOM   4505 C  CG    . PHE A 1 545 ? -6.112  13.100  -3.975  1.00 61.91  ? 545 PHE A CG    1 
ATOM   4506 C  CD1   . PHE A 1 545 ? -6.924  12.892  -5.079  1.00 61.33  ? 545 PHE A CD1   1 
ATOM   4507 C  CD2   . PHE A 1 545 ? -6.604  13.850  -2.920  1.00 63.38  ? 545 PHE A CD2   1 
ATOM   4508 C  CE1   . PHE A 1 545 ? -8.197  13.432  -5.135  1.00 61.07  ? 545 PHE A CE1   1 
ATOM   4509 C  CE2   . PHE A 1 545 ? -7.877  14.392  -2.971  1.00 65.13  ? 545 PHE A CE2   1 
ATOM   4510 C  CZ    . PHE A 1 545 ? -8.673  14.183  -4.080  1.00 61.37  ? 545 PHE A CZ    1 
ATOM   4511 N  N     . ALA A 1 546 ? -1.502  13.218  -3.402  1.00 64.76  ? 546 ALA A N     1 
ATOM   4512 C  CA    . ALA A 1 546 ? -0.164  12.697  -3.166  1.00 66.32  ? 546 ALA A CA    1 
ATOM   4513 C  C     . ALA A 1 546 ? 0.130   12.709  -1.673  1.00 68.38  ? 546 ALA A C     1 
ATOM   4514 O  O     . ALA A 1 546 ? -0.580  13.331  -0.879  1.00 72.82  ? 546 ALA A O     1 
ATOM   4515 C  CB    . ALA A 1 546 ? 0.896   13.499  -3.932  1.00 64.61  ? 546 ALA A CB    1 
ATOM   4516 N  N     . THR A 1 547 ? 1.195   12.003  -1.298  1.00 70.58  ? 547 THR A N     1 
ATOM   4517 C  CA    . THR A 1 547 ? 1.625   11.941  0.091   1.00 73.38  ? 547 THR A CA    1 
ATOM   4518 C  C     . THR A 1 547 ? 3.076   11.487  0.134   1.00 77.00  ? 547 THR A C     1 
ATOM   4519 O  O     . THR A 1 547 ? 3.602   10.934  -0.835  1.00 75.30  ? 547 THR A O     1 
ATOM   4520 C  CB    . THR A 1 547 ? 0.747   10.993  0.916   1.00 78.54  ? 547 THR A CB    1 
ATOM   4521 O  OG1   . THR A 1 547 ? 1.026   11.175  2.311   1.00 73.75  ? 547 THR A OG1   1 
ATOM   4522 C  CG2   . THR A 1 547 ? 1.024   9.545   0.538   1.00 81.24  ? 547 THR A CG2   1 
ATOM   4523 N  N     . ILE A 1 548 ? 3.719   11.746  1.270   1.00 80.53  ? 548 ILE A N     1 
ATOM   4524 C  CA    . ILE A 1 548 ? 5.049   11.211  1.559   1.00 76.59  ? 548 ILE A CA    1 
ATOM   4525 C  C     . ILE A 1 548 ? 4.860   9.885   2.282   1.00 79.05  ? 548 ILE A C     1 
ATOM   4526 O  O     . ILE A 1 548 ? 4.361   9.878   3.422   1.00 73.82  ? 548 ILE A O     1 
ATOM   4527 C  CB    . ILE A 1 548 ? 5.887   12.181  2.405   1.00 78.23  ? 548 ILE A CB    1 
ATOM   4528 C  CG1   . ILE A 1 548 ? 6.175   13.489  1.667   1.00 77.56  ? 548 ILE A CG1   1 
ATOM   4529 C  CG2   . ILE A 1 548 ? 7.219   11.550  2.734   1.00 82.71  ? 548 ILE A CG2   1 
ATOM   4530 C  CD1   . ILE A 1 548 ? 6.212   13.359  0.170   1.00 80.02  ? 548 ILE A CD1   1 
ATOM   4531 N  N     . PRO A 1 549 ? 5.225   8.754   1.678   1.00 84.79  ? 549 PRO A N     1 
ATOM   4532 C  CA    . PRO A 1 549 ? 5.046   7.462   2.351   1.00 81.50  ? 549 PRO A CA    1 
ATOM   4533 C  C     . PRO A 1 549 ? 5.725   7.424   3.710   1.00 84.62  ? 549 PRO A C     1 
ATOM   4534 O  O     . PRO A 1 549 ? 6.952   7.334   3.799   1.00 80.96  ? 549 PRO A O     1 
ATOM   4535 C  CB    . PRO A 1 549 ? 5.683   6.467   1.372   1.00 90.80  ? 549 PRO A CB    1 
ATOM   4536 C  CG    . PRO A 1 549 ? 5.596   7.143   0.043   1.00 96.15  ? 549 PRO A CG    1 
ATOM   4537 C  CD    . PRO A 1 549 ? 5.785   8.604   0.323   1.00 101.56 ? 549 PRO A CD    1 
ATOM   4538 N  N     . GLY A 1 550 ? 4.930   7.514   4.773   1.00 87.26  ? 550 GLY A N     1 
ATOM   4539 C  CA    . GLY A 1 550 ? 5.461   7.504   6.121   1.00 83.28  ? 550 GLY A CA    1 
ATOM   4540 C  C     . GLY A 1 550 ? 6.092   8.818   6.527   1.00 83.50  ? 550 GLY A C     1 
ATOM   4541 O  O     . GLY A 1 550 ? 7.320   8.937   6.560   1.00 104.11 ? 550 GLY A O     1 
ATOM   4542 N  N     . ALA A 1 551 ? 5.267   9.814   6.840   1.00 89.91  ? 551 ALA A N     1 
ATOM   4543 C  CA    . ALA A 1 551 ? 5.779   11.113  7.256   1.00 82.83  ? 551 ALA A CA    1 
ATOM   4544 C  C     . ALA A 1 551 ? 4.691   11.860  8.011   1.00 80.92  ? 551 ALA A C     1 
ATOM   4545 O  O     . ALA A 1 551 ? 3.499   11.575  7.868   1.00 90.56  ? 551 ALA A O     1 
ATOM   4546 C  CB    . ALA A 1 551 ? 6.259   11.941  6.063   1.00 81.52  ? 551 ALA A CB    1 
ATOM   4547 N  N     . ASP A 1 552 ? 5.127   12.826  8.817   1.00 83.28  ? 552 ASP A N     1 
ATOM   4548 C  CA    . ASP A 1 552 ? 4.208   13.706  9.520   1.00 89.13  ? 552 ASP A CA    1 
ATOM   4549 C  C     . ASP A 1 552 ? 3.395   14.517  8.517   1.00 86.74  ? 552 ASP A C     1 
ATOM   4550 O  O     . ASP A 1 552 ? 3.822   14.760  7.385   1.00 83.65  ? 552 ASP A O     1 
ATOM   4551 C  CB    . ASP A 1 552 ? 4.995   14.632  10.466  1.00 92.09  ? 552 ASP A CB    1 
ATOM   4552 C  CG    . ASP A 1 552 ? 4.105   15.587  11.268  1.00 101.04 ? 552 ASP A CG    1 
ATOM   4553 O  OD1   . ASP A 1 552 ? 3.309   16.351  10.690  1.00 101.17 ? 552 ASP A OD1   1 
ATOM   4554 O  OD2   . ASP A 1 552 ? 4.213   15.550  12.514  1.00 114.68 ? 552 ASP A OD2   1 
ATOM   4555 N  N     . ALA A 1 553 ? 2.205   14.938  8.951   1.00 89.11  ? 553 ALA A N     1 
ATOM   4556 C  CA    . ALA A 1 553 ? 1.370   15.800  8.122   1.00 87.14  ? 553 ALA A CA    1 
ATOM   4557 C  C     . ALA A 1 553 ? 2.082   17.107  7.790   1.00 92.84  ? 553 ALA A C     1 
ATOM   4558 O  O     . ALA A 1 553 ? 2.023   17.589  6.649   1.00 86.88  ? 553 ALA A O     1 
ATOM   4559 C  CB    . ALA A 1 553 ? 0.049   16.075  8.837   1.00 85.11  ? 553 ALA A CB    1 
ATOM   4560 N  N     . GLU A 1 554 ? 2.764   17.692  8.778   1.00 93.61  ? 554 GLU A N     1 
ATOM   4561 C  CA    . GLU A 1 554 ? 3.470   18.947  8.548   1.00 103.44 ? 554 GLU A CA    1 
ATOM   4562 C  C     . GLU A 1 554 ? 4.579   18.776  7.520   1.00 95.52  ? 554 GLU A C     1 
ATOM   4563 O  O     . GLU A 1 554 ? 4.830   19.676  6.712   1.00 89.32  ? 554 GLU A O     1 
ATOM   4564 C  CB    . GLU A 1 554 ? 4.033   19.482  9.866   1.00 100.10 ? 554 GLU A CB    1 
ATOM   4565 C  CG    . GLU A 1 554 ? 3.781   20.968  10.101  1.00 115.91 ? 554 GLU A CG    1 
ATOM   4566 C  CD    . GLU A 1 554 ? 2.361   21.393  9.762   1.00 126.15 ? 554 GLU A CD    1 
ATOM   4567 O  OE1   . GLU A 1 554 ? 1.406   20.707  10.191  1.00 124.14 ? 554 GLU A OE1   1 
ATOM   4568 O  OE2   . GLU A 1 554 ? 2.200   22.417  9.065   1.00 110.43 ? 554 GLU A OE2   1 
ATOM   4569 N  N     . THR A 1 555 ? 5.250   17.622  7.529   1.00 86.46  ? 555 THR A N     1 
ATOM   4570 C  CA    . THR A 1 555 ? 6.298   17.366  6.546   1.00 81.52  ? 555 THR A CA    1 
ATOM   4571 C  C     . THR A 1 555 ? 5.724   17.314  5.135   1.00 81.37  ? 555 THR A C     1 
ATOM   4572 O  O     . THR A 1 555 ? 6.281   17.909  4.202   1.00 82.25  ? 555 THR A O     1 
ATOM   4573 C  CB    . THR A 1 555 ? 7.025   16.063  6.882   1.00 83.11  ? 555 THR A CB    1 
ATOM   4574 O  OG1   . THR A 1 555 ? 7.247   15.988  8.296   1.00 86.04  ? 555 THR A OG1   1 
ATOM   4575 C  CG2   . THR A 1 555 ? 8.364   16.000  6.164   1.00 81.03  ? 555 THR A CG2   1 
ATOM   4576 N  N     . VAL A 1 556 ? 4.607   16.601  4.963   1.00 80.27  ? 556 VAL A N     1 
ATOM   4577 C  CA    . VAL A 1 556 ? 3.953   16.534  3.659   1.00 78.56  ? 556 VAL A CA    1 
ATOM   4578 C  C     . VAL A 1 556 ? 3.546   17.927  3.199   1.00 77.83  ? 556 VAL A C     1 
ATOM   4579 O  O     . VAL A 1 556 ? 3.763   18.301  2.040   1.00 77.00  ? 556 VAL A O     1 
ATOM   4580 C  CB    . VAL A 1 556 ? 2.743   15.581  3.717   1.00 79.33  ? 556 VAL A CB    1 
ATOM   4581 C  CG1   . VAL A 1 556 ? 1.893   15.713  2.460   1.00 69.96  ? 556 VAL A CG1   1 
ATOM   4582 C  CG2   . VAL A 1 556 ? 3.202   14.145  3.911   1.00 77.82  ? 556 VAL A CG2   1 
ATOM   4583 N  N     . LYS A 1 557 ? 2.963   18.720  4.102   1.00 76.15  ? 557 LYS A N     1 
ATOM   4584 C  CA    . LYS A 1 557 ? 2.519   20.063  3.738   1.00 79.05  ? 557 LYS A CA    1 
ATOM   4585 C  C     . LYS A 1 557 ? 3.697   20.942  3.327   1.00 79.10  ? 557 LYS A C     1 
ATOM   4586 O  O     . LYS A 1 557 ? 3.635   21.663  2.322   1.00 77.75  ? 557 LYS A O     1 
ATOM   4587 C  CB    . LYS A 1 557 ? 1.759   20.690  4.908   1.00 82.49  ? 557 LYS A CB    1 
ATOM   4588 C  CG    . LYS A 1 557 ? 0.406   20.053  5.187   1.00 78.79  ? 557 LYS A CG    1 
ATOM   4589 C  CD    . LYS A 1 557 ? -0.120  20.451  6.559   1.00 83.67  ? 557 LYS A CD    1 
ATOM   4590 C  CE    . LYS A 1 557 ? -0.852  19.298  7.231   1.00 88.17  ? 557 LYS A CE    1 
ATOM   4591 N  NZ    . LYS A 1 557 ? -1.684  19.754  8.381   1.00 88.39  ? 557 LYS A NZ    1 
ATOM   4592 N  N     . LYS A 1 558 ? 4.786   20.888  4.095   1.00 73.39  ? 558 LYS A N     1 
ATOM   4593 C  CA    . LYS A 1 558 ? 5.957   21.712  3.811   1.00 77.72  ? 558 LYS A CA    1 
ATOM   4594 C  C     . LYS A 1 558 ? 6.580   21.337  2.470   1.00 77.90  ? 558 LYS A C     1 
ATOM   4595 O  O     . LYS A 1 558 ? 6.913   22.210  1.652   1.00 80.33  ? 558 LYS A O     1 
ATOM   4596 C  CB    . LYS A 1 558 ? 6.957   21.552  4.958   1.00 82.74  ? 558 LYS A CB    1 
ATOM   4597 C  CG    . LYS A 1 558 ? 8.211   22.399  4.892   1.00 85.19  ? 558 LYS A CG    1 
ATOM   4598 C  CD    . LYS A 1 558 ? 9.411   21.552  4.515   1.00 96.29  ? 558 LYS A CD    1 
ATOM   4599 C  CE    . LYS A 1 558 ? 10.632  22.413  4.288   1.00 94.36  ? 558 LYS A CE    1 
ATOM   4600 N  NZ    . LYS A 1 558 ? 10.480  23.297  3.112   1.00 90.24  ? 558 LYS A NZ    1 
ATOM   4601 N  N     . LYS A 1 559 ? 6.741   20.035  2.224   1.00 80.69  ? 559 LYS A N     1 
ATOM   4602 C  CA    . LYS A 1 559 ? 7.313   19.599  0.957   1.00 82.77  ? 559 LYS A CA    1 
ATOM   4603 C  C     . LYS A 1 559 ? 6.394   19.928  -0.213  1.00 73.30  ? 559 LYS A C     1 
ATOM   4604 O  O     . LYS A 1 559 ? 6.876   20.248  -1.306  1.00 67.38  ? 559 LYS A O     1 
ATOM   4605 C  CB    . LYS A 1 559 ? 7.616   18.101  1.003   1.00 83.43  ? 559 LYS A CB    1 
ATOM   4606 C  CG    . LYS A 1 559 ? 8.757   17.738  1.944   1.00 87.75  ? 559 LYS A CG    1 
ATOM   4607 C  CD    . LYS A 1 559 ? 10.027  18.507  1.604   1.00 83.49  ? 559 LYS A CD    1 
ATOM   4608 C  CE    . LYS A 1 559 ? 11.002  18.519  2.773   1.00 96.06  ? 559 LYS A CE    1 
ATOM   4609 N  NZ    . LYS A 1 559 ? 12.309  19.132  2.400   1.00 91.06  ? 559 LYS A NZ    1 
ATOM   4610 N  N     . ALA A 1 560 ? 5.075   19.874  -0.004  1.00 73.76  ? 560 ALA A N     1 
ATOM   4611 C  CA    . ALA A 1 560 ? 4.149   20.271  -1.058  1.00 72.65  ? 560 ALA A CA    1 
ATOM   4612 C  C     . ALA A 1 560 ? 4.273   21.757  -1.366  1.00 72.01  ? 560 ALA A C     1 
ATOM   4613 O  O     . ALA A 1 560 ? 4.205   22.161  -2.532  1.00 65.83  ? 560 ALA A O     1 
ATOM   4614 C  CB    . ALA A 1 560 ? 2.716   19.920  -0.661  1.00 69.91  ? 560 ALA A CB    1 
ATOM   4615 N  N     . MET A 1 561 ? 4.460   22.585  -0.336  1.00 72.54  ? 561 MET A N     1 
ATOM   4616 C  CA    . MET A 1 561 ? 4.679   24.012  -0.565  1.00 73.59  ? 561 MET A CA    1 
ATOM   4617 C  C     . MET A 1 561 ? 5.945   24.244  -1.386  1.00 70.49  ? 561 MET A C     1 
ATOM   4618 O  O     . MET A 1 561 ? 5.955   25.047  -2.334  1.00 75.26  ? 561 MET A O     1 
ATOM   4619 C  CB    . MET A 1 561 ? 4.768   24.749  0.772   1.00 71.88  ? 561 MET A CB    1 
ATOM   4620 C  CG    . MET A 1 561 ? 3.465   24.813  1.550   1.00 76.03  ? 561 MET A CG    1 
ATOM   4621 S  SD    . MET A 1 561 ? 2.039   25.228  0.530   1.00 84.67  ? 561 MET A SD    1 
ATOM   4622 C  CE    . MET A 1 561 ? 0.698   24.683  1.586   1.00 82.75  ? 561 MET A CE    1 
ATOM   4623 N  N     . GLU A 1 562 ? 7.033   23.558  -1.018  1.00 63.27  ? 562 GLU A N     1 
ATOM   4624 C  CA    . GLU A 1 562 ? 8.263   23.645  -1.804  1.00 73.58  ? 562 GLU A CA    1 
ATOM   4625 C  C     . GLU A 1 562 ? 8.018   23.268  -3.260  1.00 71.78  ? 562 GLU A C     1 
ATOM   4626 O  O     . GLU A 1 562 ? 8.410   24.001  -4.181  1.00 69.59  ? 562 GLU A O     1 
ATOM   4627 C  CB    . GLU A 1 562 ? 9.345   22.740  -1.220  1.00 76.47  ? 562 GLU A CB    1 
ATOM   4628 C  CG    . GLU A 1 562 ? 9.995   23.224  0.046   1.00 82.74  ? 562 GLU A CG    1 
ATOM   4629 C  CD    . GLU A 1 562 ? 11.357  22.587  0.248   1.00 99.79  ? 562 GLU A CD    1 
ATOM   4630 O  OE1   . GLU A 1 562 ? 11.730  21.718  -0.570  1.00 99.74  ? 562 GLU A OE1   1 
ATOM   4631 O  OE2   . GLU A 1 562 ? 12.050  22.949  1.220   1.00 120.23 ? 562 GLU A OE2   1 
ATOM   4632 N  N     . PHE A 1 563 ? 7.401   22.103  -3.485  1.00 68.31  ? 563 PHE A N     1 
ATOM   4633 C  CA    . PHE A 1 563 ? 7.156   21.656  -4.850  1.00 62.81  ? 563 PHE A CA    1 
ATOM   4634 C  C     . PHE A 1 563 ? 6.281   22.641  -5.605  1.00 63.77  ? 563 PHE A C     1 
ATOM   4635 O  O     . PHE A 1 563 ? 6.463   22.829  -6.810  1.00 64.40  ? 563 PHE A O     1 
ATOM   4636 C  CB    . PHE A 1 563 ? 6.507   20.273  -4.860  1.00 61.91  ? 563 PHE A CB    1 
ATOM   4637 C  CG    . PHE A 1 563 ? 5.980   19.875  -6.207  1.00 64.08  ? 563 PHE A CG    1 
ATOM   4638 C  CD1   . PHE A 1 563 ? 6.847   19.470  -7.208  1.00 60.41  ? 563 PHE A CD1   1 
ATOM   4639 C  CD2   . PHE A 1 563 ? 4.624   19.935  -6.486  1.00 58.70  ? 563 PHE A CD2   1 
ATOM   4640 C  CE1   . PHE A 1 563 ? 6.372   19.118  -8.457  1.00 62.56  ? 563 PHE A CE1   1 
ATOM   4641 C  CE2   . PHE A 1 563 ? 4.141   19.582  -7.733  1.00 61.93  ? 563 PHE A CE2   1 
ATOM   4642 C  CZ    . PHE A 1 563 ? 5.017   19.173  -8.720  1.00 65.84  ? 563 PHE A CZ    1 
ATOM   4643 N  N     . LEU A 1 564 ? 5.328   23.273  -4.922  1.00 61.71  ? 564 LEU A N     1 
ATOM   4644 C  CA    . LEU A 1 564 ? 4.478   24.255  -5.580  1.00 65.99  ? 564 LEU A CA    1 
ATOM   4645 C  C     . LEU A 1 564 ? 5.294   25.441  -6.065  1.00 63.91  ? 564 LEU A C     1 
ATOM   4646 O  O     . LEU A 1 564 ? 5.179   25.853  -7.224  1.00 60.28  ? 564 LEU A O     1 
ATOM   4647 C  CB    . LEU A 1 564 ? 3.375   24.709  -4.631  1.00 59.97  ? 564 LEU A CB    1 
ATOM   4648 C  CG    . LEU A 1 564 ? 2.189   23.752  -4.573  1.00 63.71  ? 564 LEU A CG    1 
ATOM   4649 C  CD1   . LEU A 1 564 ? 1.262   24.170  -3.464  1.00 64.38  ? 564 LEU A CD1   1 
ATOM   4650 C  CD2   . LEU A 1 564 ? 1.463   23.722  -5.907  1.00 56.65  ? 564 LEU A CD2   1 
ATOM   4651 N  N     . LYS A 1 565 ? 6.129   26.004  -5.187  1.00 59.95  ? 565 LYS A N     1 
ATOM   4652 C  CA    . LYS A 1 565 ? 6.981   27.116  -5.606  1.00 70.12  ? 565 LYS A CA    1 
ATOM   4653 C  C     . LYS A 1 565 ? 7.851   26.719  -6.796  1.00 67.22  ? 565 LYS A C     1 
ATOM   4654 O  O     . LYS A 1 565 ? 7.941   27.449  -7.794  1.00 57.88  ? 565 LYS A O     1 
ATOM   4655 C  CB    . LYS A 1 565 ? 7.849   27.590  -4.440  1.00 64.54  ? 565 LYS A CB    1 
ATOM   4656 C  CG    . LYS A 1 565 ? 8.440   28.979  -4.648  1.00 79.64  ? 565 LYS A CG    1 
ATOM   4657 C  CD    . LYS A 1 565 ? 8.839   29.625  -3.331  1.00 87.15  ? 565 LYS A CD    1 
ATOM   4658 C  CE    . LYS A 1 565 ? 10.190  30.318  -3.437  1.00 91.51  ? 565 LYS A CE    1 
ATOM   4659 N  NZ    . LYS A 1 565 ? 10.064  31.797  -3.320  1.00 99.18  ? 565 LYS A NZ    1 
ATOM   4660 N  N     . TYR A 1 566 ? 8.466   25.536  -6.720  1.00 64.03  ? 566 TYR A N     1 
ATOM   4661 C  CA    . TYR A 1 566 ? 9.366   25.082  -7.778  1.00 59.88  ? 566 TYR A CA    1 
ATOM   4662 C  C     . TYR A 1 566 ? 8.627   24.895  -9.103  1.00 67.17  ? 566 TYR A C     1 
ATOM   4663 O  O     . TYR A 1 566 ? 9.018   25.457  -10.137 1.00 60.85  ? 566 TYR A O     1 
ATOM   4664 C  CB    . TYR A 1 566 ? 10.047  23.786  -7.329  1.00 67.19  ? 566 TYR A CB    1 
ATOM   4665 C  CG    . TYR A 1 566 ? 10.622  22.925  -8.431  1.00 74.42  ? 566 TYR A CG    1 
ATOM   4666 C  CD1   . TYR A 1 566 ? 11.895  23.162  -8.935  1.00 71.87  ? 566 TYR A CD1   1 
ATOM   4667 C  CD2   . TYR A 1 566 ? 9.902   21.855  -8.947  1.00 71.08  ? 566 TYR A CD2   1 
ATOM   4668 C  CE1   . TYR A 1 566 ? 12.427  22.366  -9.934  1.00 75.72  ? 566 TYR A CE1   1 
ATOM   4669 C  CE2   . TYR A 1 566 ? 10.424  21.056  -9.945  1.00 76.35  ? 566 TYR A CE2   1 
ATOM   4670 C  CZ    . TYR A 1 566 ? 11.686  21.315  -10.435 1.00 81.48  ? 566 TYR A CZ    1 
ATOM   4671 O  OH    . TYR A 1 566 ? 12.204  20.517  -11.430 1.00 85.26  ? 566 TYR A OH    1 
ATOM   4672 N  N     . ILE A 1 567 ? 7.542   24.118  -9.087  1.00 64.93  ? 567 ILE A N     1 
ATOM   4673 C  CA    . ILE A 1 567 ? 6.838   23.780  -10.318 1.00 57.44  ? 567 ILE A CA    1 
ATOM   4674 C  C     . ILE A 1 567 ? 6.130   24.996  -10.898 1.00 57.19  ? 567 ILE A C     1 
ATOM   4675 O  O     . ILE A 1 567 ? 5.953   25.089  -12.119 1.00 60.67  ? 567 ILE A O     1 
ATOM   4676 C  CB    . ILE A 1 567 ? 5.863   22.611  -10.067 1.00 60.30  ? 567 ILE A CB    1 
ATOM   4677 C  CG1   . ILE A 1 567 ? 5.597   21.844  -11.364 1.00 61.71  ? 567 ILE A CG1   1 
ATOM   4678 C  CG2   . ILE A 1 567 ? 4.558   23.099  -9.450  1.00 63.21  ? 567 ILE A CG2   1 
ATOM   4679 C  CD1   . ILE A 1 567 ? 6.785   21.049  -11.854 1.00 68.67  ? 567 ILE A CD1   1 
ATOM   4680 N  N     . ASN A 1 568 ? 5.725   25.954  -10.057 1.00 57.37  ? 568 ASN A N     1 
ATOM   4681 C  CA    . ASN A 1 568 ? 5.093   27.157  -10.577 1.00 58.26  ? 568 ASN A CA    1 
ATOM   4682 C  C     . ASN A 1 568 ? 6.119   28.111  -11.166 1.00 66.74  ? 568 ASN A C     1 
ATOM   4683 O  O     . ASN A 1 568 ? 5.804   28.847  -12.109 1.00 64.12  ? 568 ASN A O     1 
ATOM   4684 C  CB    . ASN A 1 568 ? 4.283   27.843  -9.478  1.00 62.57  ? 568 ASN A CB    1 
ATOM   4685 C  CG    . ASN A 1 568 ? 2.896   27.244  -9.318  1.00 60.79  ? 568 ASN A CG    1 
ATOM   4686 O  OD1   . ASN A 1 568 ? 2.304   26.751  -10.280 1.00 52.39  ? 568 ASN A OD1   1 
ATOM   4687 N  ND2   . ASN A 1 568 ? 2.376   27.276  -8.097  1.00 57.03  ? 568 ASN A ND2   1 
ATOM   4688 N  N     . ALA A 1 569 ? 7.345   28.115  -10.633 1.00 69.69  ? 569 ALA A N     1 
ATOM   4689 C  CA    . ALA A 1 569 ? 8.434   28.774  -11.342 1.00 71.31  ? 569 ALA A CA    1 
ATOM   4690 C  C     . ALA A 1 569 ? 8.673   28.116  -12.695 1.00 69.15  ? 569 ALA A C     1 
ATOM   4691 O  O     . ALA A 1 569 ? 8.952   28.799  -13.688 1.00 73.11  ? 569 ALA A O     1 
ATOM   4692 C  CB    . ALA A 1 569 ? 9.708   28.747  -10.498 1.00 79.46  ? 569 ALA A CB    1 
ATOM   4693 N  N     . LYS A 1 570 ? 8.555   26.788  -12.756 1.00 68.54  ? 570 LYS A N     1 
ATOM   4694 C  CA    . LYS A 1 570 ? 8.755   26.067  -14.009 1.00 67.43  ? 570 LYS A CA    1 
ATOM   4695 C  C     . LYS A 1 570 ? 7.552   26.131  -14.947 1.00 69.08  ? 570 LYS A C     1 
ATOM   4696 O  O     . LYS A 1 570 ? 7.696   25.812  -16.132 1.00 69.25  ? 570 LYS A O     1 
ATOM   4697 C  CB    . LYS A 1 570 ? 9.097   24.602  -13.719 1.00 70.44  ? 570 LYS A CB    1 
ATOM   4698 C  CG    . LYS A 1 570 ? 9.936   23.930  -14.794 1.00 72.89  ? 570 LYS A CG    1 
ATOM   4699 C  CD    . LYS A 1 570 ? 10.899  22.914  -14.199 1.00 82.58  ? 570 LYS A CD    1 
ATOM   4700 C  CE    . LYS A 1 570 ? 11.953  23.589  -13.339 1.00 92.21  ? 570 LYS A CE    1 
ATOM   4701 N  NZ    . LYS A 1 570 ? 13.093  22.677  -13.048 1.00 85.48  ? 570 LYS A NZ    1 
ATOM   4702 N  N     . LEU A 1 571 ? 6.381   26.538  -14.460 1.00 69.10  ? 571 LEU A N     1 
ATOM   4703 C  CA    . LEU A 1 571 ? 5.197   26.481  -15.312 1.00 66.92  ? 571 LEU A CA    1 
ATOM   4704 C  C     . LEU A 1 571 ? 5.016   27.795  -16.072 1.00 62.68  ? 571 LEU A C     1 
ATOM   4705 O  O     . LEU A 1 571 ? 5.239   28.871  -15.510 1.00 67.09  ? 571 LEU A O     1 
ATOM   4706 C  CB    . LEU A 1 571 ? 3.952   26.197  -14.478 1.00 65.89  ? 571 LEU A CB    1 
ATOM   4707 C  CG    . LEU A 1 571 ? 3.547   24.728  -14.339 1.00 61.86  ? 571 LEU A CG    1 
ATOM   4708 C  CD1   . LEU A 1 571 ? 2.284   24.600  -13.505 1.00 64.18  ? 571 LEU A CD1   1 
ATOM   4709 C  CD2   . LEU A 1 571 ? 3.359   24.081  -15.702 1.00 65.30  ? 571 LEU A CD2   1 
ATOM   4710 N  N     . PRO A 1 572 ? 4.609   27.734  -17.339 1.00 61.00  ? 572 PRO A N     1 
ATOM   4711 C  CA    . PRO A 1 572 ? 4.531   28.944  -18.161 1.00 59.51  ? 572 PRO A CA    1 
ATOM   4712 C  C     . PRO A 1 572 ? 3.150   29.578  -18.192 1.00 58.68  ? 572 PRO A C     1 
ATOM   4713 O  O     . PRO A 1 572 ? 2.119   28.914  -18.063 1.00 55.25  ? 572 PRO A O     1 
ATOM   4714 C  CB    . PRO A 1 572 ? 4.904   28.419  -19.553 1.00 58.99  ? 572 PRO A CB    1 
ATOM   4715 C  CG    . PRO A 1 572 ? 4.309   27.039  -19.567 1.00 55.98  ? 572 PRO A CG    1 
ATOM   4716 C  CD    . PRO A 1 572 ? 4.360   26.520  -18.137 1.00 58.34  ? 572 PRO A CD    1 
ATOM   4717 N  N     . GLY A 1 573 ? 3.153   30.896  -18.377 1.00 58.86  ? 573 GLY A N     1 
ATOM   4718 C  CA    . GLY A 1 573 ? 1.924   31.631  -18.630 1.00 53.08  ? 573 GLY A CA    1 
ATOM   4719 C  C     . GLY A 1 573 ? 0.933   31.535  -17.488 1.00 54.36  ? 573 GLY A C     1 
ATOM   4720 O  O     . GLY A 1 573 ? 1.291   31.584  -16.306 1.00 52.03  ? 573 GLY A O     1 
ATOM   4721 N  N     . ALA A 1 574 ? -0.340  31.391  -17.850 1.00 53.34  ? 574 ALA A N     1 
ATOM   4722 C  CA    . ALA A 1 574 ? -1.436  31.332  -16.892 1.00 58.47  ? 574 ALA A CA    1 
ATOM   4723 C  C     . ALA A 1 574 ? -1.571  29.972  -16.223 1.00 58.02  ? 574 ALA A C     1 
ATOM   4724 O  O     . ALA A 1 574 ? -2.543  29.754  -15.492 1.00 54.89  ? 574 ALA A O     1 
ATOM   4725 C  CB    . ALA A 1 574 ? -2.753  31.704  -17.578 1.00 43.93  ? 574 ALA A CB    1 
ATOM   4726 N  N     . LEU A 1 575 ? -0.632  29.057  -16.452 1.00 56.67  ? 575 LEU A N     1 
ATOM   4727 C  CA    . LEU A 1 575 ? -0.697  27.733  -15.849 1.00 56.25  ? 575 LEU A CA    1 
ATOM   4728 C  C     . LEU A 1 575 ? -0.102  27.780  -14.449 1.00 52.51  ? 575 LEU A C     1 
ATOM   4729 O  O     . LEU A 1 575 ? 1.049   28.191  -14.267 1.00 69.36  ? 575 LEU A O     1 
ATOM   4730 C  CB    . LEU A 1 575 ? 0.032   26.712  -16.717 1.00 58.60  ? 575 LEU A CB    1 
ATOM   4731 C  CG    . LEU A 1 575 ? -0.863  26.124  -17.807 1.00 65.83  ? 575 LEU A CG    1 
ATOM   4732 C  CD1   . LEU A 1 575 ? -0.683  26.861  -19.130 1.00 59.17  ? 575 LEU A CD1   1 
ATOM   4733 C  CD2   . LEU A 1 575 ? -0.612  24.641  -17.963 1.00 64.71  ? 575 LEU A CD2   1 
ATOM   4734 N  N     . GLU A 1 576 ? -0.885  27.350  -13.464 1.00 58.78  ? 576 GLU A N     1 
ATOM   4735 C  CA    . GLU A 1 576 ? -0.499  27.466  -12.067 1.00 64.13  ? 576 GLU A CA    1 
ATOM   4736 C  C     . GLU A 1 576 ? -1.046  26.275  -11.296 1.00 62.78  ? 576 GLU A C     1 
ATOM   4737 O  O     . GLU A 1 576 ? -2.222  25.928  -11.440 1.00 55.58  ? 576 GLU A O     1 
ATOM   4738 C  CB    . GLU A 1 576 ? -1.023  28.777  -11.470 1.00 61.16  ? 576 GLU A CB    1 
ATOM   4739 C  CG    . GLU A 1 576 ? -0.471  29.114  -10.096 1.00 77.07  ? 576 GLU A CG    1 
ATOM   4740 C  CD    . GLU A 1 576 ? -1.221  30.258  -9.441  1.00 100.29 ? 576 GLU A CD    1 
ATOM   4741 O  OE1   . GLU A 1 576 ? -2.046  30.899  -10.127 1.00 86.80  ? 576 GLU A OE1   1 
ATOM   4742 O  OE2   . GLU A 1 576 ? -0.987  30.515  -8.241  1.00 108.55 ? 576 GLU A OE2   1 
ATOM   4743 N  N     . LEU A 1 577 ? -0.191  25.654  -10.489 1.00 60.52  ? 577 LEU A N     1 
ATOM   4744 C  CA    . LEU A 1 577 ? -0.598  24.585  -9.591  1.00 55.65  ? 577 LEU A CA    1 
ATOM   4745 C  C     . LEU A 1 577 ? -0.957  25.182  -8.236  1.00 59.24  ? 577 LEU A C     1 
ATOM   4746 O  O     . LEU A 1 577 ? -0.264  26.075  -7.741  1.00 63.88  ? 577 LEU A O     1 
ATOM   4747 C  CB    . LEU A 1 577 ? 0.525   23.558  -9.435  1.00 54.21  ? 577 LEU A CB    1 
ATOM   4748 C  CG    . LEU A 1 577 ? 0.166   22.129  -9.016  1.00 57.83  ? 577 LEU A CG    1 
ATOM   4749 C  CD1   . LEU A 1 577 ? -1.210  21.746  -9.516  1.00 48.22  ? 577 LEU A CD1   1 
ATOM   4750 C  CD2   . LEU A 1 577 ? 1.210   21.135  -9.509  1.00 57.03  ? 577 LEU A CD2   1 
ATOM   4751 N  N     . GLU A 1 578 ? -2.039  24.686  -7.636  1.00 54.84  ? 578 GLU A N     1 
ATOM   4752 C  CA    . GLU A 1 578 ? -2.542  25.218  -6.380  1.00 61.25  ? 578 GLU A CA    1 
ATOM   4753 C  C     . GLU A 1 578 ? -2.731  24.102  -5.366  1.00 62.54  ? 578 GLU A C     1 
ATOM   4754 O  O     . GLU A 1 578 ? -3.155  22.989  -5.712  1.00 66.36  ? 578 GLU A O     1 
ATOM   4755 C  CB    . GLU A 1 578 ? -3.877  25.950  -6.564  1.00 68.59  ? 578 GLU A CB    1 
ATOM   4756 C  CG    . GLU A 1 578 ? -4.010  26.746  -7.843  1.00 75.81  ? 578 GLU A CG    1 
ATOM   4757 C  CD    . GLU A 1 578 ? -4.996  27.885  -7.702  1.00 84.46  ? 578 GLU A CD    1 
ATOM   4758 O  OE1   . GLU A 1 578 ? -4.667  28.873  -7.011  1.00 92.08  ? 578 GLU A OE1   1 
ATOM   4759 O  OE2   . GLU A 1 578 ? -6.108  27.784  -8.260  1.00 79.98  ? 578 GLU A OE2   1 
ATOM   4760 N  N     . TYR A 1 579 ? -2.419  24.430  -4.112  1.00 61.12  ? 579 TYR A N     1 
ATOM   4761 C  CA    . TYR A 1 579 ? -2.691  23.590  -2.951  1.00 70.87  ? 579 TYR A CA    1 
ATOM   4762 C  C     . TYR A 1 579 ? -4.142  23.798  -2.537  1.00 73.72  ? 579 TYR A C     1 
ATOM   4763 O  O     . TYR A 1 579 ? -4.497  24.853  -2.001  1.00 75.29  ? 579 TYR A O     1 
ATOM   4764 C  CB    . TYR A 1 579 ? -1.732  23.959  -1.822  1.00 70.83  ? 579 TYR A CB    1 
ATOM   4765 C  CG    . TYR A 1 579 ? -2.055  23.404  -0.455  1.00 78.99  ? 579 TYR A CG    1 
ATOM   4766 C  CD1   . TYR A 1 579 ? -1.671  22.120  -0.094  1.00 79.99  ? 579 TYR A CD1   1 
ATOM   4767 C  CD2   . TYR A 1 579 ? -2.714  24.181  0.489   1.00 79.33  ? 579 TYR A CD2   1 
ATOM   4768 C  CE1   . TYR A 1 579 ? -1.952  21.618  1.163   1.00 80.84  ? 579 TYR A CE1   1 
ATOM   4769 C  CE2   . TYR A 1 579 ? -3.000  23.688  1.745   1.00 80.05  ? 579 TYR A CE2   1 
ATOM   4770 C  CZ    . TYR A 1 579 ? -2.617  22.407  2.077   1.00 78.92  ? 579 TYR A CZ    1 
ATOM   4771 O  OH    . TYR A 1 579 ? -2.900  21.917  3.329   1.00 93.58  ? 579 TYR A OH    1 
ATOM   4772 N  N     . GLU A 1 580 ? -4.987  22.803  -2.792  1.00 69.23  ? 580 GLU A N     1 
ATOM   4773 C  CA    . GLU A 1 580 ? -6.408  22.955  -2.506  1.00 73.82  ? 580 GLU A CA    1 
ATOM   4774 C  C     . GLU A 1 580 ? -6.895  21.894  -1.529  1.00 68.76  ? 580 GLU A C     1 
ATOM   4775 O  O     . GLU A 1 580 ? -7.841  21.154  -1.821  1.00 82.21  ? 580 GLU A O     1 
ATOM   4776 C  CB    . GLU A 1 580 ? -7.218  22.916  -3.804  1.00 72.34  ? 580 GLU A CB    1 
ATOM   4777 C  CG    . GLU A 1 580 ? -6.727  23.913  -4.844  1.00 85.18  ? 580 GLU A CG    1 
ATOM   4778 C  CD    . GLU A 1 580 ? -7.851  24.708  -5.482  1.00 91.40  ? 580 GLU A CD    1 
ATOM   4779 O  OE1   . GLU A 1 580 ? -8.624  25.344  -4.736  1.00 95.62  ? 580 GLU A OE1   1 
ATOM   4780 O  OE2   . GLU A 1 580 ? -7.952  24.713  -6.727  1.00 71.62  ? 580 GLU A OE2   1 
ATOM   4781 N  N     . GLY A 1 581 ? -6.255  21.817  -0.368  1.00 68.50  ? 581 GLY A N     1 
ATOM   4782 C  CA    . GLY A 1 581 ? -6.764  20.951  0.687   1.00 62.94  ? 581 GLY A CA    1 
ATOM   4783 C  C     . GLY A 1 581 ? -5.769  19.905  1.147   1.00 69.83  ? 581 GLY A C     1 
ATOM   4784 O  O     . GLY A 1 581 ? -5.110  19.234  0.352   1.00 72.58  ? 581 GLY A O     1 
ATOM   4785 N  N     . PHE A 1 582 ? -5.650  19.782  2.465   1.00 69.52  ? 582 PHE A N     1 
ATOM   4786 C  CA    . PHE A 1 582 ? -5.001  18.647  3.099   1.00 67.84  ? 582 PHE A CA    1 
ATOM   4787 C  C     . PHE A 1 582 ? -6.072  17.781  3.743   1.00 68.33  ? 582 PHE A C     1 
ATOM   4788 O  O     . PHE A 1 582 ? -7.073  18.293  4.256   1.00 69.95  ? 582 PHE A O     1 
ATOM   4789 C  CB    . PHE A 1 582 ? -3.983  19.090  4.153   1.00 72.09  ? 582 PHE A CB    1 
ATOM   4790 C  CG    . PHE A 1 582 ? -3.325  17.949  4.876   1.00 73.07  ? 582 PHE A CG    1 
ATOM   4791 C  CD1   . PHE A 1 582 ? -2.178  17.362  4.369   1.00 77.37  ? 582 PHE A CD1   1 
ATOM   4792 C  CD2   . PHE A 1 582 ? -3.853  17.461  6.061   1.00 75.31  ? 582 PHE A CD2   1 
ATOM   4793 C  CE1   . PHE A 1 582 ? -1.572  16.311  5.028   1.00 79.55  ? 582 PHE A CE1   1 
ATOM   4794 C  CE2   . PHE A 1 582 ? -3.251  16.410  6.721   1.00 81.26  ? 582 PHE A CE2   1 
ATOM   4795 C  CZ    . PHE A 1 582 ? -2.111  15.838  6.205   1.00 81.79  ? 582 PHE A CZ    1 
ATOM   4796 N  N     . TYR A 1 583 ? -5.863  16.471  3.715   1.00 70.90  ? 583 TYR A N     1 
ATOM   4797 C  CA    . TYR A 1 583 ? -6.838  15.526  4.236   1.00 75.86  ? 583 TYR A CA    1 
ATOM   4798 C  C     . TYR A 1 583 ? -6.133  14.530  5.138   1.00 77.06  ? 583 TYR A C     1 
ATOM   4799 O  O     . TYR A 1 583 ? -5.142  13.914  4.733   1.00 73.54  ? 583 TYR A O     1 
ATOM   4800 C  CB    . TYR A 1 583 ? -7.569  14.819  3.094   1.00 68.61  ? 583 TYR A CB    1 
ATOM   4801 C  CG    . TYR A 1 583 ? -8.245  15.800  2.169   1.00 70.35  ? 583 TYR A CG    1 
ATOM   4802 C  CD1   . TYR A 1 583 ? -9.375  16.497  2.575   1.00 67.40  ? 583 TYR A CD1   1 
ATOM   4803 C  CD2   . TYR A 1 583 ? -7.732  16.060  0.905   1.00 68.01  ? 583 TYR A CD2   1 
ATOM   4804 C  CE1   . TYR A 1 583 ? -9.991  17.409  1.740   1.00 61.95  ? 583 TYR A CE1   1 
ATOM   4805 C  CE2   . TYR A 1 583 ? -8.341  16.972  0.063   1.00 67.09  ? 583 TYR A CE2   1 
ATOM   4806 C  CZ    . TYR A 1 583 ? -9.470  17.642  0.485   1.00 62.39  ? 583 TYR A CZ    1 
ATOM   4807 O  OH    . TYR A 1 583 ? -10.077 18.550  -0.351  1.00 62.57  ? 583 TYR A OH    1 
ATOM   4808 N  N     . LYS A 1 584 ? -6.639  14.394  6.366   1.00 84.72  ? 584 LYS A N     1 
ATOM   4809 C  CA    . LYS A 1 584 ? -6.057  13.447  7.309   1.00 80.53  ? 584 LYS A CA    1 
ATOM   4810 C  C     . LYS A 1 584 ? -6.005  12.049  6.712   1.00 82.37  ? 584 LYS A C     1 
ATOM   4811 O  O     . LYS A 1 584 ? -4.960  11.390  6.738   1.00 83.70  ? 584 LYS A O     1 
ATOM   4812 C  CB    . LYS A 1 584 ? -6.850  13.442  8.617   1.00 90.38  ? 584 LYS A CB    1 
ATOM   4813 C  CG    . LYS A 1 584 ? -6.211  12.594  9.710   1.00 101.12 ? 584 LYS A CG    1 
ATOM   4814 C  CD    . LYS A 1 584 ? -6.917  12.758  11.047  1.00 106.87 ? 584 LYS A CD    1 
ATOM   4815 C  CE    . LYS A 1 584 ? -6.929  11.447  11.820  1.00 100.49 ? 584 LYS A CE    1 
ATOM   4816 N  NZ    . LYS A 1 584 ? -7.888  11.476  12.959  1.00 95.40  ? 584 LYS A NZ    1 
ATOM   4817 N  N     . ARG A 1 585 ? -7.124  11.577  6.159   1.00 83.89  ? 585 ARG A N     1 
ATOM   4818 C  CA    . ARG A 1 585 ? -7.152  10.233  5.593   1.00 82.62  ? 585 ARG A CA    1 
ATOM   4819 C  C     . ARG A 1 585 ? -7.985  10.222  4.319   1.00 78.40  ? 585 ARG A C     1 
ATOM   4820 O  O     . ARG A 1 585 ? -8.699  11.177  4.004   1.00 73.64  ? 585 ARG A O     1 
ATOM   4821 C  CB    . ARG A 1 585 ? -7.684  9.202   6.602   1.00 83.05  ? 585 ARG A CB    1 
ATOM   4822 C  CG    . ARG A 1 585 ? -6.861  9.096   7.882   1.00 90.58  ? 585 ARG A CG    1 
ATOM   4823 C  CD    . ARG A 1 585 ? -7.084  7.779   8.601   1.00 88.57  ? 585 ARG A CD    1 
ATOM   4824 N  NE    . ARG A 1 585 ? -8.330  7.780   9.356   1.00 101.06 ? 585 ARG A NE    1 
ATOM   4825 C  CZ    . ARG A 1 585 ? -8.401  7.838   10.679  1.00 104.51 ? 585 ARG A CZ    1 
ATOM   4826 N  NH1   . ARG A 1 585 ? -7.313  7.902   11.428  1.00 105.81 ? 585 ARG A NH1   1 
ATOM   4827 N  NH2   . ARG A 1 585 ? -9.595  7.833   11.265  1.00 109.42 ? 585 ARG A NH2   1 
ATOM   4828 N  N     . GLY A 1 586 ? -7.878  9.123   3.578   1.00 78.80  ? 586 GLY A N     1 
ATOM   4829 C  CA    . GLY A 1 586 ? -8.594  8.999   2.324   1.00 71.12  ? 586 GLY A CA    1 
ATOM   4830 C  C     . GLY A 1 586 ? -8.647  7.589   1.773   1.00 76.95  ? 586 GLY A C     1 
ATOM   4831 O  O     . GLY A 1 586 ? -7.620  6.917   1.658   1.00 76.11  ? 586 GLY A O     1 
ATOM   4832 N  N     . PHE A 1 587 ? -9.845  7.135   1.419   1.00 75.76  ? 587 PHE A N     1 
ATOM   4833 C  CA    . PHE A 1 587 ? -10.062 5.815   0.845   1.00 72.23  ? 587 PHE A CA    1 
ATOM   4834 C  C     . PHE A 1 587 ? -10.410 5.971   -0.630  1.00 68.20  ? 587 PHE A C     1 
ATOM   4835 O  O     . PHE A 1 587 ? -11.410 6.610   -0.970  1.00 67.55  ? 587 PHE A O     1 
ATOM   4836 C  CB    . PHE A 1 587 ? -11.175 5.074   1.585   1.00 68.89  ? 587 PHE A CB    1 
ATOM   4837 C  CG    . PHE A 1 587 ? -11.211 3.602   1.303   1.00 71.50  ? 587 PHE A CG    1 
ATOM   4838 C  CD1   . PHE A 1 587 ? -10.423 2.727   2.031   1.00 74.80  ? 587 PHE A CD1   1 
ATOM   4839 C  CD2   . PHE A 1 587 ? -12.030 3.092   0.311   1.00 68.32  ? 587 PHE A CD2   1 
ATOM   4840 C  CE1   . PHE A 1 587 ? -10.451 1.370   1.776   1.00 72.28  ? 587 PHE A CE1   1 
ATOM   4841 C  CE2   . PHE A 1 587 ? -12.062 1.736   0.052   1.00 73.08  ? 587 PHE A CE2   1 
ATOM   4842 C  CZ    . PHE A 1 587 ? -11.271 0.875   0.785   1.00 71.13  ? 587 PHE A CZ    1 
ATOM   4843 N  N     . PHE A 1 588 ? -9.590  5.383   -1.496  1.00 72.19  ? 588 PHE A N     1 
ATOM   4844 C  CA    . PHE A 1 588 ? -9.776  5.448   -2.942  1.00 70.11  ? 588 PHE A CA    1 
ATOM   4845 C  C     . PHE A 1 588 ? -10.194 4.068   -3.431  1.00 70.62  ? 588 PHE A C     1 
ATOM   4846 O  O     . PHE A 1 588 ? -9.414  3.111   -3.336  1.00 70.58  ? 588 PHE A O     1 
ATOM   4847 C  CB    . PHE A 1 588 ? -8.493  5.903   -3.635  1.00 66.75  ? 588 PHE A CB    1 
ATOM   4848 C  CG    . PHE A 1 588 ? -8.029  7.267   -3.216  1.00 67.20  ? 588 PHE A CG    1 
ATOM   4849 C  CD1   . PHE A 1 588 ? -7.329  7.443   -2.033  1.00 69.25  ? 588 PHE A CD1   1 
ATOM   4850 C  CD2   . PHE A 1 588 ? -8.285  8.371   -4.009  1.00 62.42  ? 588 PHE A CD2   1 
ATOM   4851 C  CE1   . PHE A 1 588 ? -6.902  8.697   -1.647  1.00 65.57  ? 588 PHE A CE1   1 
ATOM   4852 C  CE2   . PHE A 1 588 ? -7.860  9.627   -3.628  1.00 64.87  ? 588 PHE A CE2   1 
ATOM   4853 C  CZ    . PHE A 1 588 ? -7.167  9.790   -2.445  1.00 62.57  ? 588 PHE A CZ    1 
ATOM   4854 N  N     . VAL A 1 589 ? -11.423 3.959   -3.945  1.00 70.65  ? 589 VAL A N     1 
ATOM   4855 C  CA    . VAL A 1 589 ? -11.913 2.664   -4.405  1.00 72.96  ? 589 VAL A CA    1 
ATOM   4856 C  C     . VAL A 1 589 ? -11.458 2.396   -5.833  1.00 69.56  ? 589 VAL A C     1 
ATOM   4857 O  O     . VAL A 1 589 ? -10.881 1.345   -6.132  1.00 70.23  ? 589 VAL A O     1 
ATOM   4858 C  CB    . VAL A 1 589 ? -13.449 2.602   -4.284  1.00 66.97  ? 589 VAL A CB    1 
ATOM   4859 C  CG1   . VAL A 1 589 ? -14.024 1.588   -5.267  1.00 70.26  ? 589 VAL A CG1   1 
ATOM   4860 C  CG2   . VAL A 1 589 ? -13.862 2.266   -2.863  1.00 69.68  ? 589 VAL A CG2   1 
ATOM   4861 N  N     . THR A 1 590 ? -11.697 3.347   -6.725  1.00 66.07  ? 590 THR A N     1 
ATOM   4862 C  CA    . THR A 1 590 ? -11.431 3.184   -8.149  1.00 68.10  ? 590 THR A CA    1 
ATOM   4863 C  C     . THR A 1 590 ? -11.499 4.564   -8.792  1.00 64.88  ? 590 THR A C     1 
ATOM   4864 O  O     . THR A 1 590 ? -11.777 5.569   -8.127  1.00 60.11  ? 590 THR A O     1 
ATOM   4865 C  CB    . THR A 1 590 ? -12.421 2.205   -8.786  1.00 77.61  ? 590 THR A CB    1 
ATOM   4866 O  OG1   . THR A 1 590 ? -11.846 1.621   -9.964  1.00 82.72  ? 590 THR A OG1   1 
ATOM   4867 C  CG2   . THR A 1 590 ? -13.733 2.902   -9.118  1.00 64.30  ? 590 THR A CG2   1 
ATOM   4868 N  N     . LYS A 1 591 ? -11.224 4.606   -10.095 1.00 60.71  ? 591 LYS A N     1 
ATOM   4869 C  CA    . LYS A 1 591 ? -11.281 5.855   -10.840 1.00 61.94  ? 591 LYS A CA    1 
ATOM   4870 C  C     . LYS A 1 591 ? -12.641 6.515   -10.665 1.00 63.90  ? 591 LYS A C     1 
ATOM   4871 O  O     . LYS A 1 591 ? -13.682 5.864   -10.783 1.00 66.03  ? 591 LYS A O     1 
ATOM   4872 C  CB    . LYS A 1 591 ? -10.999 5.589   -12.319 1.00 63.85  ? 591 LYS A CB    1 
ATOM   4873 C  CG    . LYS A 1 591 ? -9.709  4.824   -12.568 1.00 70.35  ? 591 LYS A CG    1 
ATOM   4874 C  CD    . LYS A 1 591 ? -9.001  5.304   -13.823 1.00 70.56  ? 591 LYS A CD    1 
ATOM   4875 C  CE    . LYS A 1 591 ? -8.746  4.160   -14.789 1.00 74.68  ? 591 LYS A CE    1 
ATOM   4876 N  NZ    . LYS A 1 591 ? -8.955  4.576   -16.202 1.00 80.14  ? 591 LYS A NZ    1 
ATOM   4877 N  N     . LYS A 1 592 ? -12.617 7.813   -10.359 1.00 62.32  ? 592 LYS A N     1 
ATOM   4878 C  CA    . LYS A 1 592 ? -13.806 8.626   -10.117 1.00 63.03  ? 592 LYS A CA    1 
ATOM   4879 C  C     . LYS A 1 592 ? -14.577 8.200   -8.870  1.00 62.08  ? 592 LYS A C     1 
ATOM   4880 O  O     . LYS A 1 592 ? -15.732 8.593   -8.699  1.00 61.79  ? 592 LYS A O     1 
ATOM   4881 C  CB    . LYS A 1 592 ? -14.748 8.626   -11.331 1.00 56.94  ? 592 LYS A CB    1 
ATOM   4882 C  CG    . LYS A 1 592 ? -14.064 8.879   -12.661 1.00 56.06  ? 592 LYS A CG    1 
ATOM   4883 C  CD    . LYS A 1 592 ? -14.093 10.350  -13.036 1.00 57.13  ? 592 LYS A CD    1 
ATOM   4884 C  CE    . LYS A 1 592 ? -13.808 10.540  -14.513 1.00 61.15  ? 592 LYS A CE    1 
ATOM   4885 N  NZ    . LYS A 1 592 ? -12.803 11.607  -14.769 1.00 66.99  ? 592 LYS A NZ    1 
ATOM   4886 N  N     . LYS A 1 593 ? -13.975 7.410   -7.978  1.00 60.04  ? 593 LYS A N     1 
ATOM   4887 C  CA    . LYS A 1 593 ? -14.681 6.922   -6.794  1.00 63.48  ? 593 LYS A CA    1 
ATOM   4888 C  C     . LYS A 1 593 ? -13.737 6.910   -5.597  1.00 59.67  ? 593 LYS A C     1 
ATOM   4889 O  O     . LYS A 1 593 ? -12.859 6.044   -5.490  1.00 55.30  ? 593 LYS A O     1 
ATOM   4890 C  CB    . LYS A 1 593 ? -15.277 5.535   -7.042  1.00 66.64  ? 593 LYS A CB    1 
ATOM   4891 C  CG    . LYS A 1 593 ? -16.644 5.578   -7.720  1.00 65.58  ? 593 LYS A CG    1 
ATOM   4892 C  CD    . LYS A 1 593 ? -17.339 4.223   -7.690  1.00 72.69  ? 593 LYS A CD    1 
ATOM   4893 C  CE    . LYS A 1 593 ? -18.265 4.046   -8.888  1.00 73.14  ? 593 LYS A CE    1 
ATOM   4894 N  NZ    . LYS A 1 593 ? -19.699 3.947   -8.494  1.00 68.59  ? 593 LYS A NZ    1 
ATOM   4895 N  N     . TYR A 1 594 ? -13.937 7.857   -4.684  1.00 64.17  ? 594 TYR A N     1 
ATOM   4896 C  CA    . TYR A 1 594 ? -13.101 7.948   -3.494  1.00 62.93  ? 594 TYR A CA    1 
ATOM   4897 C  C     . TYR A 1 594 ? -13.827 8.759   -2.426  1.00 64.72  ? 594 TYR A C     1 
ATOM   4898 O  O     . TYR A 1 594 ? -14.937 9.256   -2.632  1.00 63.16  ? 594 TYR A O     1 
ATOM   4899 C  CB    . TYR A 1 594 ? -11.734 8.557   -3.828  1.00 62.08  ? 594 TYR A CB    1 
ATOM   4900 C  CG    . TYR A 1 594 ? -11.779 9.978   -4.352  1.00 58.92  ? 594 TYR A CG    1 
ATOM   4901 C  CD1   . TYR A 1 594 ? -11.728 11.063  -3.485  1.00 60.20  ? 594 TYR A CD1   1 
ATOM   4902 C  CD2   . TYR A 1 594 ? -11.860 10.233  -5.715  1.00 59.56  ? 594 TYR A CD2   1 
ATOM   4903 C  CE1   . TYR A 1 594 ? -11.763 12.362  -3.960  1.00 58.28  ? 594 TYR A CE1   1 
ATOM   4904 C  CE2   . TYR A 1 594 ? -11.895 11.530  -6.199  1.00 65.74  ? 594 TYR A CE2   1 
ATOM   4905 C  CZ    . TYR A 1 594 ? -11.846 12.590  -5.318  1.00 65.52  ? 594 TYR A CZ    1 
ATOM   4906 O  OH    . TYR A 1 594 ? -11.882 13.880  -5.797  1.00 63.27  ? 594 TYR A OH    1 
ATOM   4907 N  N     . ALA A 1 595 ? -13.180 8.876   -1.270  1.00 62.97  ? 595 ALA A N     1 
ATOM   4908 C  CA    . ALA A 1 595 ? -13.689 9.665   -0.159  1.00 66.57  ? 595 ALA A CA    1 
ATOM   4909 C  C     . ALA A 1 595 ? -12.506 10.101  0.691   1.00 69.95  ? 595 ALA A C     1 
ATOM   4910 O  O     . ALA A 1 595 ? -11.547 9.348   0.858   1.00 65.36  ? 595 ALA A O     1 
ATOM   4911 C  CB    . ALA A 1 595 ? -14.698 8.874   0.682   1.00 63.33  ? 595 ALA A CB    1 
ATOM   4912 N  N     . VAL A 1 596 ? -12.563 11.328  1.200   1.00 69.33  ? 596 VAL A N     1 
ATOM   4913 C  CA    . VAL A 1 596 ? -11.473 11.897  1.980   1.00 69.93  ? 596 VAL A CA    1 
ATOM   4914 C  C     . VAL A 1 596 ? -12.029 12.538  3.244   1.00 75.11  ? 596 VAL A C     1 
ATOM   4915 O  O     . VAL A 1 596 ? -13.192 12.953  3.301   1.00 79.37  ? 596 VAL A O     1 
ATOM   4916 C  CB    . VAL A 1 596 ? -10.646 12.928  1.173   1.00 64.37  ? 596 VAL A CB    1 
ATOM   4917 C  CG1   . VAL A 1 596 ? -10.140 12.318  -0.129  1.00 59.90  ? 596 VAL A CG1   1 
ATOM   4918 C  CG2   . VAL A 1 596 ? -11.465 14.175  0.897   1.00 63.32  ? 596 VAL A CG2   1 
ATOM   4919 N  N     . ILE A 1 597 ? -11.183 12.600  4.271   1.00 73.76  ? 597 ILE A N     1 
ATOM   4920 C  CA    . ILE A 1 597 ? -11.490 13.261  5.531   1.00 73.71  ? 597 ILE A CA    1 
ATOM   4921 C  C     . ILE A 1 597 ? -10.342 14.203  5.871   1.00 83.79  ? 597 ILE A C     1 
ATOM   4922 O  O     . ILE A 1 597 ? -9.169  13.796  5.875   1.00 85.85  ? 597 ILE A O     1 
ATOM   4923 C  CB    . ILE A 1 597 ? -11.738 12.255  6.674   1.00 79.55  ? 597 ILE A CB    1 
ATOM   4924 C  CG1   . ILE A 1 597 ? -12.116 12.987  7.962   1.00 86.00  ? 597 ILE A CG1   1 
ATOM   4925 C  CG2   . ILE A 1 597 ? -10.545 11.337  6.890   1.00 81.65  ? 597 ILE A CG2   1 
ATOM   4926 C  CD1   . ILE A 1 597 ? -13.250 12.345  8.712   1.00 87.64  ? 597 ILE A CD1   1 
ATOM   4927 N  N     . ASP A 1 598 ? -10.687 15.460  6.146   1.00 80.68  ? 598 ASP A N     1 
ATOM   4928 C  CA    . ASP A 1 598 ? -9.726  16.513  6.439   1.00 85.65  ? 598 ASP A CA    1 
ATOM   4929 C  C     . ASP A 1 598 ? -9.447  16.546  7.945   1.00 95.33  ? 598 ASP A C     1 
ATOM   4930 O  O     . ASP A 1 598 ? -9.603  15.540  8.642   1.00 102.21 ? 598 ASP A O     1 
ATOM   4931 C  CB    . ASP A 1 598 ? -10.243 17.852  5.896   1.00 82.79  ? 598 ASP A CB    1 
ATOM   4932 C  CG    . ASP A 1 598 ? -11.574 18.263  6.504   1.00 93.02  ? 598 ASP A CG    1 
ATOM   4933 O  OD1   . ASP A 1 598 ? -12.106 17.520  7.357   1.00 97.88  ? 598 ASP A OD1   1 
ATOM   4934 O  OD2   . ASP A 1 598 ? -12.091 19.336  6.129   1.00 92.23  ? 598 ASP A OD2   1 
ATOM   4935 N  N     . GLU A 1 599 ? -9.041  17.706  8.463   1.00 99.64  ? 599 GLU A N     1 
ATOM   4936 C  CA    . GLU A 1 599 ? -8.619  17.793  9.856   1.00 105.94 ? 599 GLU A CA    1 
ATOM   4937 C  C     . GLU A 1 599 ? -9.800  17.984  10.800  1.00 107.53 ? 599 GLU A C     1 
ATOM   4938 O  O     . GLU A 1 599 ? -9.824  17.403  11.890  1.00 113.60 ? 599 GLU A O     1 
ATOM   4939 C  CB    . GLU A 1 599 ? -7.613  18.932  10.027  1.00 107.10 ? 599 GLU A CB    1 
ATOM   4940 C  CG    . GLU A 1 599 ? -6.475  18.911  9.017   1.00 108.60 ? 599 GLU A CG    1 
ATOM   4941 C  CD    . GLU A 1 599 ? -5.116  18.763  9.675   1.00 123.40 ? 599 GLU A CD    1 
ATOM   4942 O  OE1   . GLU A 1 599 ? -4.910  19.351  10.757  1.00 132.41 ? 599 GLU A OE1   1 
ATOM   4943 O  OE2   . GLU A 1 599 ? -4.255  18.056  9.114   1.00 110.81 ? 599 GLU A OE2   1 
ATOM   4944 N  N     . GLU A 1 600 ? -10.785 18.791  10.404  1.00 108.63 ? 600 GLU A N     1 
ATOM   4945 C  CA    . GLU A 1 600 ? -11.907 19.101  11.280  1.00 107.80 ? 600 GLU A CA    1 
ATOM   4946 C  C     . GLU A 1 600 ? -12.973 18.013  11.304  1.00 103.16 ? 600 GLU A C     1 
ATOM   4947 O  O     . GLU A 1 600 ? -13.862 18.062  12.161  1.00 103.70 ? 600 GLU A O     1 
ATOM   4948 C  CB    . GLU A 1 600 ? -12.541 20.433  10.872  1.00 108.81 ? 600 GLU A CB    1 
ATOM   4949 C  CG    . GLU A 1 600 ? -11.532 21.524  10.547  1.00 110.08 ? 600 GLU A CG    1 
ATOM   4950 C  CD    . GLU A 1 600 ? -11.675 22.737  11.445  1.00 124.04 ? 600 GLU A CD    1 
ATOM   4951 O  OE1   . GLU A 1 600 ? -12.262 22.602  12.540  1.00 124.43 ? 600 GLU A OE1   1 
ATOM   4952 O  OE2   . GLU A 1 600 ? -11.201 23.826  11.058  1.00 126.28 ? 600 GLU A OE2   1 
ATOM   4953 N  N     . GLY A 1 601 ? -12.912 17.043  10.401  1.00 98.62  ? 601 GLY A N     1 
ATOM   4954 C  CA    . GLY A 1 601 ? -13.868 15.959  10.382  1.00 95.26  ? 601 GLY A CA    1 
ATOM   4955 C  C     . GLY A 1 601 ? -14.933 16.039  9.312   1.00 97.45  ? 601 GLY A C     1 
ATOM   4956 O  O     . GLY A 1 601 ? -15.987 15.415  9.474   1.00 106.57 ? 601 GLY A O     1 
ATOM   4957 N  N     . LYS A 1 602 ? -14.701 16.787  8.237   1.00 94.52  ? 602 LYS A N     1 
ATOM   4958 C  CA    . LYS A 1 602 ? -15.644 16.868  7.130   1.00 85.90  ? 602 LYS A CA    1 
ATOM   4959 C  C     . LYS A 1 602 ? -15.294 15.810  6.092   1.00 90.85  ? 602 LYS A C     1 
ATOM   4960 O  O     . LYS A 1 602 ? -14.144 15.726  5.646   1.00 89.04  ? 602 LYS A O     1 
ATOM   4961 C  CB    . LYS A 1 602 ? -15.618 18.259  6.497   1.00 80.36  ? 602 LYS A CB    1 
ATOM   4962 C  CG    . LYS A 1 602 ? -16.970 18.743  5.999   1.00 83.94  ? 602 LYS A CG    1 
ATOM   4963 C  CD    . LYS A 1 602 ? -16.830 19.584  4.740   1.00 83.20  ? 602 LYS A CD    1 
ATOM   4964 C  CE    . LYS A 1 602 ? -18.166 19.751  4.035   1.00 76.86  ? 602 LYS A CE    1 
ATOM   4965 N  NZ    . LYS A 1 602 ? -18.886 18.455  3.896   1.00 82.38  ? 602 LYS A NZ    1 
ATOM   4966 N  N     . ILE A 1 603 ? -16.283 15.005  5.710   1.00 86.91  ? 603 ILE A N     1 
ATOM   4967 C  CA    . ILE A 1 603 ? -16.077 13.908  4.771   1.00 85.21  ? 603 ILE A CA    1 
ATOM   4968 C  C     . ILE A 1 603 ? -16.523 14.375  3.395   1.00 86.07  ? 603 ILE A C     1 
ATOM   4969 O  O     . ILE A 1 603 ? -17.660 14.834  3.226   1.00 80.84  ? 603 ILE A O     1 
ATOM   4970 C  CB    . ILE A 1 603 ? -16.844 12.633  5.180   1.00 87.76  ? 603 ILE A CB    1 
ATOM   4971 C  CG1   . ILE A 1 603 ? -16.347 12.018  6.500   1.00 84.04  ? 603 ILE A CG1   1 
ATOM   4972 C  CG2   . ILE A 1 603 ? -16.776 11.595  4.066   1.00 79.34  ? 603 ILE A CG2   1 
ATOM   4973 C  CD1   . ILE A 1 603 ? -16.640 12.821  7.749   1.00 92.38  ? 603 ILE A CD1   1 
ATOM   4974 N  N     . THR A 1 604 ? -15.634 14.261  2.411   1.00 79.53  ? 604 THR A N     1 
ATOM   4975 C  CA    . THR A 1 604 ? -15.947 14.562  1.020   1.00 71.86  ? 604 THR A CA    1 
ATOM   4976 C  C     . THR A 1 604 ? -15.976 13.255  0.241   1.00 73.85  ? 604 THR A C     1 
ATOM   4977 O  O     . THR A 1 604 ? -14.986 12.519  0.227   1.00 74.30  ? 604 THR A O     1 
ATOM   4978 C  CB    . THR A 1 604 ? -14.920 15.520  0.417   1.00 68.41  ? 604 THR A CB    1 
ATOM   4979 O  OG1   . THR A 1 604 ? -14.554 16.506  1.391   1.00 72.54  ? 604 THR A OG1   1 
ATOM   4980 C  CG2   . THR A 1 604 ? -15.496 16.205  -0.806  1.00 68.16  ? 604 THR A CG2   1 
ATOM   4981 N  N     . THR A 1 605 ? -17.105 12.967  -0.402  1.00 70.88  ? 605 THR A N     1 
ATOM   4982 C  CA    . THR A 1 605 ? -17.293 11.726  -1.140  1.00 72.70  ? 605 THR A CA    1 
ATOM   4983 C  C     . THR A 1 605 ? -17.495 12.038  -2.615  1.00 70.03  ? 605 THR A C     1 
ATOM   4984 O  O     . THR A 1 605 ? -18.290 12.918  -2.964  1.00 64.13  ? 605 THR A O     1 
ATOM   4985 C  CB    . THR A 1 605 ? -18.487 10.940  -0.597  1.00 71.33  ? 605 THR A CB    1 
ATOM   4986 O  OG1   . THR A 1 605 ? -19.689 11.691  -0.804  1.00 87.91  ? 605 THR A OG1   1 
ATOM   4987 C  CG2   . THR A 1 605 ? -18.314 10.676  0.890   1.00 66.29  ? 605 THR A CG2   1 
ATOM   4988 N  N     . ARG A 1 606 ? -16.785 11.309  -3.476  1.00 65.37  ? 606 ARG A N     1 
ATOM   4989 C  CA    . ARG A 1 606 ? -16.828 11.523  -4.914  1.00 65.89  ? 606 ARG A CA    1 
ATOM   4990 C  C     . ARG A 1 606 ? -17.128 10.207  -5.612  1.00 59.56  ? 606 ARG A C     1 
ATOM   4991 O  O     . ARG A 1 606 ? -16.417 9.216   -5.407  1.00 61.75  ? 606 ARG A O     1 
ATOM   4992 C  CB    . ARG A 1 606 ? -15.499 12.091  -5.422  1.00 62.73  ? 606 ARG A CB    1 
ATOM   4993 C  CG    . ARG A 1 606 ? -15.164 13.475  -4.887  1.00 64.38  ? 606 ARG A CG    1 
ATOM   4994 C  CD    . ARG A 1 606 ? -15.927 14.553  -5.637  1.00 68.80  ? 606 ARG A CD    1 
ATOM   4995 N  NE    . ARG A 1 606 ? -16.543 15.519  -4.737  1.00 76.36  ? 606 ARG A NE    1 
ATOM   4996 C  CZ    . ARG A 1 606 ? -16.037 16.713  -4.460  1.00 79.78  ? 606 ARG A CZ    1 
ATOM   4997 N  NH1   . ARG A 1 606 ? -14.895 17.120  -4.991  1.00 79.67  ? 606 ARG A NH1   1 
ATOM   4998 N  NH2   . ARG A 1 606 ? -16.694 17.520  -3.632  1.00 87.04  ? 606 ARG A NH2   1 
ATOM   4999 N  N     . GLY A 1 607 ? -18.185 10.200  -6.422  1.00 59.69  ? 607 GLY A N     1 
ATOM   5000 C  CA    . GLY A 1 607 ? -18.476 9.088   -7.309  1.00 61.22  ? 607 GLY A CA    1 
ATOM   5001 C  C     . GLY A 1 607 ? -19.145 7.902   -6.650  1.00 63.50  ? 607 GLY A C     1 
ATOM   5002 O  O     . GLY A 1 607 ? -19.818 7.111   -7.319  1.00 60.02  ? 607 GLY A O     1 
ATOM   5003 N  N     . LEU A 1 608 ? -18.970 7.771   -5.338  1.00 55.35  ? 608 LEU A N     1 
ATOM   5004 C  CA    . LEU A 1 608 ? -19.503 6.621   -4.626  1.00 61.11  ? 608 LEU A CA    1 
ATOM   5005 C  C     . LEU A 1 608 ? -21.030 6.620   -4.662  1.00 64.60  ? 608 LEU A C     1 
ATOM   5006 O  O     . LEU A 1 608 ? -21.679 7.623   -4.971  1.00 63.75  ? 608 LEU A O     1 
ATOM   5007 C  CB    . LEU A 1 608 ? -18.997 6.601   -3.184  1.00 56.72  ? 608 LEU A CB    1 
ATOM   5008 C  CG    . LEU A 1 608 ? -17.474 6.544   -3.056  1.00 67.64  ? 608 LEU A CG    1 
ATOM   5009 C  CD1   . LEU A 1 608 ? -17.048 6.723   -1.615  1.00 62.05  ? 608 LEU A CD1   1 
ATOM   5010 C  CD2   . LEU A 1 608 ? -16.945 5.232   -3.615  1.00 60.55  ? 608 LEU A CD2   1 
ATOM   5011 N  N     . GLU A 1 609 ? -21.602 5.458   -4.340  1.00 60.49  ? 609 GLU A N     1 
ATOM   5012 C  CA    . GLU A 1 609 ? -23.047 5.280   -4.418  1.00 59.53  ? 609 GLU A CA    1 
ATOM   5013 C  C     . GLU A 1 609 ? -23.798 6.201   -3.466  1.00 62.15  ? 609 GLU A C     1 
ATOM   5014 O  O     . GLU A 1 609 ? -25.004 6.405   -3.639  1.00 63.46  ? 609 GLU A O     1 
ATOM   5015 C  CB    . GLU A 1 609 ? -23.407 3.821   -4.129  1.00 50.73  ? 609 GLU A CB    1 
ATOM   5016 C  CG    . GLU A 1 609 ? -22.917 2.837   -5.182  1.00 55.64  ? 609 GLU A CG    1 
ATOM   5017 C  CD    . GLU A 1 609 ? -21.439 2.517   -5.059  1.00 70.52  ? 609 GLU A CD    1 
ATOM   5018 O  OE1   . GLU A 1 609 ? -20.881 2.692   -3.956  1.00 63.75  ? 609 GLU A OE1   1 
ATOM   5019 O  OE2   . GLU A 1 609 ? -20.834 2.095   -6.068  1.00 69.87  ? 609 GLU A OE2   1 
ATOM   5020 N  N     . ILE A 1 610 ? -23.110 6.763   -2.471  1.00 61.73  ? 610 ILE A N     1 
ATOM   5021 C  CA    . ILE A 1 610 ? -23.752 7.663   -1.518  1.00 63.68  ? 610 ILE A CA    1 
ATOM   5022 C  C     . ILE A 1 610 ? -24.265 8.921   -2.213  1.00 64.70  ? 610 ILE A C     1 
ATOM   5023 O  O     . ILE A 1 610 ? -25.285 9.493   -1.808  1.00 62.43  ? 610 ILE A O     1 
ATOM   5024 C  CB    . ILE A 1 610 ? -22.763 7.989   -0.379  1.00 63.83  ? 610 ILE A CB    1 
ATOM   5025 C  CG1   . ILE A 1 610 ? -23.199 9.225   0.409   1.00 86.79  ? 610 ILE A CG1   1 
ATOM   5026 C  CG2   . ILE A 1 610 ? -21.360 8.173   -0.930  1.00 71.95  ? 610 ILE A CG2   1 
ATOM   5027 C  CD1   . ILE A 1 610 ? -22.429 9.420   1.695   1.00 88.07  ? 610 ILE A CD1   1 
ATOM   5028 N  N     . VAL A 1 611 ? -23.591 9.358   -3.280  1.00 62.87  ? 611 VAL A N     1 
ATOM   5029 C  CA    . VAL A 1 611 ? -23.964 10.582  -3.980  1.00 63.59  ? 611 VAL A CA    1 
ATOM   5030 C  C     . VAL A 1 611 ? -24.823 10.322  -5.208  1.00 63.83  ? 611 VAL A C     1 
ATOM   5031 O  O     . VAL A 1 611 ? -25.219 11.277  -5.889  1.00 71.91  ? 611 VAL A O     1 
ATOM   5032 C  CB    . VAL A 1 611 ? -22.713 11.392  -4.378  1.00 64.14  ? 611 VAL A CB    1 
ATOM   5033 C  CG1   . VAL A 1 611 ? -21.747 11.475  -3.213  1.00 57.77  ? 611 VAL A CG1   1 
ATOM   5034 C  CG2   . VAL A 1 611 ? -22.039 10.772  -5.595  1.00 60.68  ? 611 VAL A CG2   1 
ATOM   5035 N  N     . ARG A 1 612 ? -25.126 9.066   -5.513  1.00 59.84  ? 612 ARG A N     1 
ATOM   5036 C  CA    . ARG A 1 612 ? -25.854 8.715   -6.724  1.00 64.94  ? 612 ARG A CA    1 
ATOM   5037 C  C     . ARG A 1 612 ? -27.341 8.576   -6.427  1.00 63.92  ? 612 ARG A C     1 
ATOM   5038 O  O     . ARG A 1 612 ? -27.729 8.005   -5.405  1.00 66.75  ? 612 ARG A O     1 
ATOM   5039 C  CB    . ARG A 1 612 ? -25.312 7.416   -7.323  1.00 63.49  ? 612 ARG A CB    1 
ATOM   5040 C  CG    . ARG A 1 612 ? -23.822 7.456   -7.631  1.00 65.36  ? 612 ARG A CG    1 
ATOM   5041 C  CD    . ARG A 1 612 ? -23.397 6.274   -8.486  1.00 62.79  ? 612 ARG A CD    1 
ATOM   5042 N  NE    . ARG A 1 612 ? -24.320 6.041   -9.590  1.00 56.30  ? 612 ARG A NE    1 
ATOM   5043 C  CZ    . ARG A 1 612 ? -24.032 6.258   -10.866 1.00 63.60  ? 612 ARG A CZ    1 
ATOM   5044 N  NH1   . ARG A 1 612 ? -22.854 6.732   -11.238 1.00 64.87  ? 612 ARG A NH1   1 
ATOM   5045 N  NH2   . ARG A 1 612 ? -24.949 5.995   -11.792 1.00 60.86  ? 612 ARG A NH2   1 
ATOM   5046 N  N     . ARG A 1 613 ? -28.171 9.097   -7.334  1.00 61.07  ? 613 ARG A N     1 
ATOM   5047 C  CA    . ARG A 1 613 ? -29.618 9.045   -7.146  1.00 68.19  ? 613 ARG A CA    1 
ATOM   5048 C  C     . ARG A 1 613 ? -30.187 7.655   -7.418  1.00 66.98  ? 613 ARG A C     1 
ATOM   5049 O  O     . ARG A 1 613 ? -31.157 7.248   -6.767  1.00 70.41  ? 613 ARG A O     1 
ATOM   5050 C  CB    . ARG A 1 613 ? -30.292 10.089  -8.043  1.00 62.90  ? 613 ARG A CB    1 
ATOM   5051 C  CG    . ARG A 1 613 ? -31.624 9.659   -8.640  1.00 68.44  ? 613 ARG A CG    1 
ATOM   5052 C  CD    . ARG A 1 613 ? -31.840 10.258  -10.021 1.00 69.47  ? 613 ARG A CD    1 
ATOM   5053 N  NE    . ARG A 1 613 ? -31.976 11.709  -9.974  1.00 82.71  ? 613 ARG A NE    1 
ATOM   5054 C  CZ    . ARG A 1 613 ? -31.490 12.536  -10.889 1.00 77.64  ? 613 ARG A CZ    1 
ATOM   5055 N  NH1   . ARG A 1 613 ? -30.828 12.089  -11.943 1.00 67.85  ? 613 ARG A NH1   1 
ATOM   5056 N  NH2   . ARG A 1 613 ? -31.673 13.846  -10.742 1.00 77.93  ? 613 ARG A NH2   1 
ATOM   5057 N  N     . ASP A 1 614 ? -29.593 6.907   -8.350  1.00 67.14  ? 614 ASP A N     1 
ATOM   5058 C  CA    . ASP A 1 614 ? -30.106 5.605   -8.764  1.00 58.13  ? 614 ASP A CA    1 
ATOM   5059 C  C     . ASP A 1 614 ? -29.809 4.488   -7.765  1.00 59.23  ? 614 ASP A C     1 
ATOM   5060 O  O     . ASP A 1 614 ? -29.905 3.311   -8.133  1.00 63.37  ? 614 ASP A O     1 
ATOM   5061 C  CB    . ASP A 1 614 ? -29.542 5.234   -10.138 1.00 64.51  ? 614 ASP A CB    1 
ATOM   5062 C  CG    . ASP A 1 614 ? -28.059 5.524   -10.255 1.00 69.59  ? 614 ASP A CG    1 
ATOM   5063 O  OD1   . ASP A 1 614 ? -27.451 5.930   -9.241  1.00 65.06  ? 614 ASP A OD1   1 
ATOM   5064 O  OD2   . ASP A 1 614 ? -27.502 5.348   -11.358 1.00 82.95  ? 614 ASP A OD2   1 
ATOM   5065 N  N     . TRP A 1 615 ? -29.456 4.812   -6.526  1.00 58.65  ? 615 TRP A N     1 
ATOM   5066 C  CA    . TRP A 1 615 ? -29.199 3.813   -5.500  1.00 61.02  ? 615 TRP A CA    1 
ATOM   5067 C  C     . TRP A 1 615 ? -30.165 4.015   -4.340  1.00 62.80  ? 615 TRP A C     1 
ATOM   5068 O  O     . TRP A 1 615 ? -30.653 5.123   -4.106  1.00 72.36  ? 615 TRP A O     1 
ATOM   5069 C  CB    . TRP A 1 615 ? -27.746 3.880   -5.013  1.00 58.05  ? 615 TRP A CB    1 
ATOM   5070 C  CG    . TRP A 1 615 ? -26.800 3.217   -5.964  1.00 59.25  ? 615 TRP A CG    1 
ATOM   5071 C  CD1   . TRP A 1 615 ? -26.279 3.750   -7.108  1.00 57.58  ? 615 TRP A CD1   1 
ATOM   5072 C  CD2   . TRP A 1 615 ? -26.278 1.886   -5.868  1.00 59.95  ? 615 TRP A CD2   1 
ATOM   5073 N  NE1   . TRP A 1 615 ? -25.459 2.836   -7.726  1.00 58.34  ? 615 TRP A NE1   1 
ATOM   5074 C  CE2   . TRP A 1 615 ? -25.444 1.683   -6.986  1.00 58.90  ? 615 TRP A CE2   1 
ATOM   5075 C  CE3   . TRP A 1 615 ? -26.433 0.847   -4.945  1.00 54.62  ? 615 TRP A CE3   1 
ATOM   5076 C  CZ2   . TRP A 1 615 ? -24.764 0.487   -7.202  1.00 59.96  ? 615 TRP A CZ2   1 
ATOM   5077 C  CZ3   . TRP A 1 615 ? -25.760 -0.340  -5.163  1.00 54.00  ? 615 TRP A CZ3   1 
ATOM   5078 C  CH2   . TRP A 1 615 ? -24.936 -0.511  -6.282  1.00 57.52  ? 615 TRP A CH2   1 
ATOM   5079 N  N     . SER A 1 616 ? -30.452 2.931   -3.627  1.00 61.62  ? 616 SER A N     1 
ATOM   5080 C  CA    . SER A 1 616 ? -31.434 2.990   -2.555  1.00 63.15  ? 616 SER A CA    1 
ATOM   5081 C  C     . SER A 1 616 ? -30.875 3.733   -1.347  1.00 62.20  ? 616 SER A C     1 
ATOM   5082 O  O     . SER A 1 616 ? -29.665 3.757   -1.106  1.00 65.06  ? 616 SER A O     1 
ATOM   5083 C  CB    . SER A 1 616 ? -31.869 1.584   -2.149  1.00 64.05  ? 616 SER A CB    1 
ATOM   5084 O  OG    . SER A 1 616 ? -30.769 0.837   -1.663  1.00 72.86  ? 616 SER A OG    1 
ATOM   5085 N  N     . GLU A 1 617 ? -31.782 4.345   -0.580  1.00 66.16  ? 617 GLU A N     1 
ATOM   5086 C  CA    . GLU A 1 617 ? -31.371 5.130   0.579   1.00 65.52  ? 617 GLU A CA    1 
ATOM   5087 C  C     . GLU A 1 617 ? -30.729 4.263   1.653   1.00 63.22  ? 617 GLU A C     1 
ATOM   5088 O  O     . GLU A 1 617 ? -29.818 4.721   2.352   1.00 70.45  ? 617 GLU A O     1 
ATOM   5089 C  CB    . GLU A 1 617 ? -32.571 5.888   1.150   1.00 72.81  ? 617 GLU A CB    1 
ATOM   5090 C  CG    . GLU A 1 617 ? -32.256 6.739   2.369   1.00 73.14  ? 617 GLU A CG    1 
ATOM   5091 C  CD    . GLU A 1 617 ? -31.192 7.784   2.091   1.00 93.07  ? 617 GLU A CD    1 
ATOM   5092 O  OE1   . GLU A 1 617 ? -31.322 8.515   1.086   1.00 89.53  ? 617 GLU A OE1   1 
ATOM   5093 O  OE2   . GLU A 1 617 ? -30.225 7.873   2.877   1.00 87.80  ? 617 GLU A OE2   1 
ATOM   5094 N  N     . ILE A 1 618 ? -31.182 3.017   1.802   1.00 63.00  ? 618 ILE A N     1 
ATOM   5095 C  CA    . ILE A 1 618 ? -30.574 2.129   2.788   1.00 66.75  ? 618 ILE A CA    1 
ATOM   5096 C  C     . ILE A 1 618 ? -29.115 1.859   2.431   1.00 64.94  ? 618 ILE A C     1 
ATOM   5097 O  O     . ILE A 1 618 ? -28.235 1.872   3.302   1.00 68.94  ? 618 ILE A O     1 
ATOM   5098 C  CB    . ILE A 1 618 ? -31.396 0.829   2.921   1.00 62.98  ? 618 ILE A CB    1 
ATOM   5099 C  CG1   . ILE A 1 618 ? -30.888 -0.023  4.087   1.00 68.87  ? 618 ILE A CG1   1 
ATOM   5100 C  CG2   . ILE A 1 618 ? -31.414 0.037   1.617   1.00 61.48  ? 618 ILE A CG2   1 
ATOM   5101 C  CD1   . ILE A 1 618 ? -30.799 0.723   5.397   1.00 71.57  ? 618 ILE A CD1   1 
ATOM   5102 N  N     . ALA A 1 619 ? -28.828 1.668   1.140   1.00 66.79  ? 619 ALA A N     1 
ATOM   5103 C  CA    . ALA A 1 619 ? -27.453 1.434   0.714   1.00 65.33  ? 619 ALA A CA    1 
ATOM   5104 C  C     . ALA A 1 619 ? -26.594 2.677   0.908   1.00 67.81  ? 619 ALA A C     1 
ATOM   5105 O  O     . ALA A 1 619 ? -25.466 2.583   1.406   1.00 66.30  ? 619 ALA A O     1 
ATOM   5106 C  CB    . ALA A 1 619 ? -27.426 0.982   -0.746  1.00 57.01  ? 619 ALA A CB    1 
ATOM   5107 N  N     . LYS A 1 620 ? -27.112 3.849   0.521   1.00 67.23  ? 620 LYS A N     1 
ATOM   5108 C  CA    . LYS A 1 620 ? -26.380 5.095   0.736   1.00 64.51  ? 620 LYS A CA    1 
ATOM   5109 C  C     . LYS A 1 620 ? -26.045 5.282   2.208   1.00 72.25  ? 620 LYS A C     1 
ATOM   5110 O  O     . LYS A 1 620 ? -24.903 5.590   2.563   1.00 67.77  ? 620 LYS A O     1 
ATOM   5111 C  CB    . LYS A 1 620 ? -27.191 6.294   0.248   1.00 66.33  ? 620 LYS A CB    1 
ATOM   5112 C  CG    . LYS A 1 620 ? -27.657 6.271   -1.186  1.00 61.90  ? 620 LYS A CG    1 
ATOM   5113 C  CD    . LYS A 1 620 ? -28.765 7.304   -1.339  1.00 67.59  ? 620 LYS A CD    1 
ATOM   5114 C  CE    . LYS A 1 620 ? -29.202 7.471   -2.773  1.00 63.53  ? 620 LYS A CE    1 
ATOM   5115 N  NZ    . LYS A 1 620 ? -28.882 8.830   -3.290  1.00 66.51  ? 620 LYS A NZ    1 
ATOM   5116 N  N     . GLU A 1 621 ? -27.043 5.118   3.079   1.00 69.60  ? 621 GLU A N     1 
ATOM   5117 C  CA    . GLU A 1 621 ? -26.842 5.359   4.503   1.00 74.27  ? 621 GLU A CA    1 
ATOM   5118 C  C     . GLU A 1 621 ? -25.866 4.354   5.102   1.00 74.23  ? 621 GLU A C     1 
ATOM   5119 O  O     . GLU A 1 621 ? -25.008 4.724   5.916   1.00 71.04  ? 621 GLU A O     1 
ATOM   5120 C  CB    . GLU A 1 621 ? -28.193 5.320   5.219   1.00 75.96  ? 621 GLU A CB    1 
ATOM   5121 C  CG    . GLU A 1 621 ? -28.145 4.916   6.680   1.00 90.14  ? 621 GLU A CG    1 
ATOM   5122 C  CD    . GLU A 1 621 ? -29.512 4.979   7.336   1.00 97.73  ? 621 GLU A CD    1 
ATOM   5123 O  OE1   . GLU A 1 621 ? -30.513 5.162   6.610   1.00 91.32  ? 621 GLU A OE1   1 
ATOM   5124 O  OE2   . GLU A 1 621 ? -29.588 4.845   8.576   1.00 103.44 ? 621 GLU A OE2   1 
ATOM   5125 N  N     . THR A 1 622 ? -25.964 3.083   4.700   1.00 70.79  ? 622 THR A N     1 
ATOM   5126 C  CA    . THR A 1 622 ? -25.037 2.076   5.206   1.00 74.05  ? 622 THR A CA    1 
ATOM   5127 C  C     . THR A 1 622 ? -23.610 2.376   4.762   1.00 69.71  ? 622 THR A C     1 
ATOM   5128 O  O     . THR A 1 622 ? -22.672 2.321   5.568   1.00 70.25  ? 622 THR A O     1 
ATOM   5129 C  CB    . THR A 1 622 ? -25.469 0.684   4.739   1.00 74.16  ? 622 THR A CB    1 
ATOM   5130 O  OG1   . THR A 1 622 ? -26.852 0.482   5.058   1.00 73.83  ? 622 THR A OG1   1 
ATOM   5131 C  CG2   . THR A 1 622 ? -24.638 -0.393  5.422   1.00 66.80  ? 622 THR A CG2   1 
ATOM   5132 N  N     . GLN A 1 623 ? -23.427 2.704   3.480   1.00 67.46  ? 623 GLN A N     1 
ATOM   5133 C  CA    . GLN A 1 623 ? -22.094 3.037   2.990   1.00 66.69  ? 623 GLN A CA    1 
ATOM   5134 C  C     . GLN A 1 623 ? -21.552 4.283   3.676   1.00 74.04  ? 623 GLN A C     1 
ATOM   5135 O  O     . GLN A 1 623 ? -20.356 4.364   3.975   1.00 76.55  ? 623 GLN A O     1 
ATOM   5136 C  CB    . GLN A 1 623 ? -22.122 3.227   1.473   1.00 61.29  ? 623 GLN A CB    1 
ATOM   5137 C  CG    . GLN A 1 623 ? -20.746 3.387   0.850   1.00 57.44  ? 623 GLN A CG    1 
ATOM   5138 C  CD    . GLN A 1 623 ? -20.803 3.615   -0.646  1.00 57.92  ? 623 GLN A CD    1 
ATOM   5139 O  OE1   . GLN A 1 623 ? -21.186 4.690   -1.108  1.00 60.17  ? 623 GLN A OE1   1 
ATOM   5140 N  NE2   . GLN A 1 623 ? -20.417 2.602   -1.414  1.00 55.98  ? 623 GLN A NE2   1 
ATOM   5141 N  N     . ALA A 1 624 ? -22.423 5.257   3.951   1.00 74.66  ? 624 ALA A N     1 
ATOM   5142 C  CA    . ALA A 1 624 ? -21.994 6.482   4.615   1.00 74.85  ? 624 ALA A CA    1 
ATOM   5143 C  C     . ALA A 1 624 ? -21.519 6.203   6.034   1.00 75.24  ? 624 ALA A C     1 
ATOM   5144 O  O     . ALA A 1 624 ? -20.463 6.689   6.453   1.00 74.40  ? 624 ALA A O     1 
ATOM   5145 C  CB    . ALA A 1 624 ? -23.135 7.499   4.622   1.00 73.07  ? 624 ALA A CB    1 
ATOM   5146 N  N     . ARG A 1 625 ? -22.291 5.420   6.793   1.00 77.01  ? 625 ARG A N     1 
ATOM   5147 C  CA    . ARG A 1 625 ? -21.888 5.099   8.158   1.00 74.46  ? 625 ARG A CA    1 
ATOM   5148 C  C     . ARG A 1 625 ? -20.621 4.251   8.176   1.00 77.19  ? 625 ARG A C     1 
ATOM   5149 O  O     . ARG A 1 625 ? -19.767 4.418   9.056   1.00 79.80  ? 625 ARG A O     1 
ATOM   5150 C  CB    . ARG A 1 625 ? -23.027 4.392   8.890   1.00 81.43  ? 625 ARG A CB    1 
ATOM   5151 C  CG    . ARG A 1 625 ? -24.288 5.232   9.012   1.00 81.02  ? 625 ARG A CG    1 
ATOM   5152 C  CD    . ARG A 1 625 ? -25.497 4.366   9.296   1.00 77.95  ? 625 ARG A CD    1 
ATOM   5153 N  NE    . ARG A 1 625 ? -25.450 3.805   10.640  1.00 83.89  ? 625 ARG A NE    1 
ATOM   5154 C  CZ    . ARG A 1 625 ? -26.175 2.771   11.046  1.00 82.18  ? 625 ARG A CZ    1 
ATOM   5155 N  NH1   . ARG A 1 625 ? -27.017 2.156   10.232  1.00 83.92  ? 625 ARG A NH1   1 
ATOM   5156 N  NH2   . ARG A 1 625 ? -26.051 2.344   12.299  1.00 72.17  ? 625 ARG A NH2   1 
ATOM   5157 N  N     . VAL A 1 626 ? -20.472 3.348   7.203   1.00 73.47  ? 626 VAL A N     1 
ATOM   5158 C  CA    . VAL A 1 626 ? -19.255 2.545   7.112   1.00 77.01  ? 626 VAL A CA    1 
ATOM   5159 C  C     . VAL A 1 626 ? -18.049 3.438   6.839   1.00 76.89  ? 626 VAL A C     1 
ATOM   5160 O  O     . VAL A 1 626 ? -17.006 3.330   7.498   1.00 75.43  ? 626 VAL A O     1 
ATOM   5161 C  CB    . VAL A 1 626 ? -19.415 1.462   6.030   1.00 72.83  ? 626 VAL A CB    1 
ATOM   5162 C  CG1   . VAL A 1 626 ? -18.072 1.106   5.432   1.00 65.24  ? 626 VAL A CG1   1 
ATOM   5163 C  CG2   . VAL A 1 626 ? -20.090 0.230   6.611   1.00 77.14  ? 626 VAL A CG2   1 
ATOM   5164 N  N     . LEU A 1 627 ? -18.177 4.337   5.860   1.00 75.17  ? 627 LEU A N     1 
ATOM   5165 C  CA    . LEU A 1 627 ? -17.090 5.255   5.544   1.00 73.09  ? 627 LEU A CA    1 
ATOM   5166 C  C     . LEU A 1 627 ? -16.765 6.160   6.720   1.00 81.11  ? 627 LEU A C     1 
ATOM   5167 O  O     . LEU A 1 627 ? -15.599 6.509   6.927   1.00 83.02  ? 627 LEU A O     1 
ATOM   5168 C  CB    . LEU A 1 627 ? -17.453 6.090   4.320   1.00 66.47  ? 627 LEU A CB    1 
ATOM   5169 C  CG    . LEU A 1 627 ? -17.003 5.531   2.974   1.00 63.37  ? 627 LEU A CG    1 
ATOM   5170 C  CD1   . LEU A 1 627 ? -17.351 6.512   1.878   1.00 60.45  ? 627 LEU A CD1   1 
ATOM   5171 C  CD2   . LEU A 1 627 ? -15.509 5.241   2.989   1.00 63.60  ? 627 LEU A CD2   1 
ATOM   5172 N  N     . GLU A 1 628 ? -17.775 6.551   7.499   1.00 75.80  ? 628 GLU A N     1 
ATOM   5173 C  CA    . GLU A 1 628 ? -17.510 7.361   8.682   1.00 81.48  ? 628 GLU A CA    1 
ATOM   5174 C  C     . GLU A 1 628 ? -16.737 6.568   9.726   1.00 86.77  ? 628 GLU A C     1 
ATOM   5175 O  O     . GLU A 1 628 ? -15.773 7.075   10.308  1.00 92.22  ? 628 GLU A O     1 
ATOM   5176 C  CB    . GLU A 1 628 ? -18.818 7.889   9.267   1.00 83.34  ? 628 GLU A CB    1 
ATOM   5177 C  CG    . GLU A 1 628 ? -18.646 9.130   10.127  1.00 86.62  ? 628 GLU A CG    1 
ATOM   5178 C  CD    . GLU A 1 628 ? -19.435 9.059   11.418  1.00 95.48  ? 628 GLU A CD    1 
ATOM   5179 O  OE1   . GLU A 1 628 ? -19.526 7.957   12.000  1.00 97.20  ? 628 GLU A OE1   1 
ATOM   5180 O  OE2   . GLU A 1 628 ? -19.962 10.105  11.852  1.00 98.12  ? 628 GLU A OE2   1 
ATOM   5181 N  N     . ALA A 1 629 ? -17.143 5.320   9.974   1.00 85.58  ? 629 ALA A N     1 
ATOM   5182 C  CA    . ALA A 1 629 ? -16.399 4.476   10.904  1.00 90.24  ? 629 ALA A CA    1 
ATOM   5183 C  C     . ALA A 1 629 ? -14.963 4.265   10.440  1.00 94.50  ? 629 ALA A C     1 
ATOM   5184 O  O     . ALA A 1 629 ? -14.057 4.114   11.267  1.00 102.96 ? 629 ALA A O     1 
ATOM   5185 C  CB    . ALA A 1 629 ? -17.104 3.131   11.078  1.00 90.62  ? 629 ALA A CB    1 
ATOM   5186 N  N     . LEU A 1 630 ? -14.738 4.252   9.125   1.00 88.46  ? 630 LEU A N     1 
ATOM   5187 C  CA    . LEU A 1 630 ? -13.385 4.088   8.603   1.00 87.18  ? 630 LEU A CA    1 
ATOM   5188 C  C     . LEU A 1 630 ? -12.561 5.368   8.722   1.00 91.79  ? 630 LEU A C     1 
ATOM   5189 O  O     . LEU A 1 630 ? -11.378 5.315   9.077   1.00 88.79  ? 630 LEU A O     1 
ATOM   5190 C  CB    . LEU A 1 630 ? -13.439 3.638   7.144   1.00 83.49  ? 630 LEU A CB    1 
ATOM   5191 C  CG    . LEU A 1 630 ? -13.256 2.150   6.849   1.00 87.08  ? 630 LEU A CG    1 
ATOM   5192 C  CD1   . LEU A 1 630 ? -14.512 1.362   7.178   1.00 87.75  ? 630 LEU A CD1   1 
ATOM   5193 C  CD2   . LEU A 1 630 ? -12.883 1.973   5.389   1.00 88.34  ? 630 LEU A CD2   1 
ATOM   5194 N  N     . LEU A 1 631 ? -13.165 6.519   8.433   1.00 89.47  ? 631 LEU A N     1 
ATOM   5195 C  CA    . LEU A 1 631 ? -12.424 7.764   8.282   1.00 88.37  ? 631 LEU A CA    1 
ATOM   5196 C  C     . LEU A 1 631 ? -12.314 8.575   9.567   1.00 96.28  ? 631 LEU A C     1 
ATOM   5197 O  O     . LEU A 1 631 ? -11.415 9.417   9.670   1.00 98.18  ? 631 LEU A O     1 
ATOM   5198 C  CB    . LEU A 1 631 ? -13.077 8.631   7.198   1.00 86.81  ? 631 LEU A CB    1 
ATOM   5199 C  CG    . LEU A 1 631 ? -12.547 8.536   5.762   1.00 79.43  ? 631 LEU A CG    1 
ATOM   5200 C  CD1   . LEU A 1 631 ? -12.232 7.100   5.369   1.00 81.15  ? 631 LEU A CD1   1 
ATOM   5201 C  CD2   . LEU A 1 631 ? -13.537 9.157   4.786   1.00 72.92  ? 631 LEU A CD2   1 
ATOM   5202 N  N     . LYS A 1 632 ? -13.196 8.353   10.543  1.00 97.08  ? 632 LYS A N     1 
ATOM   5203 C  CA    . LYS A 1 632 ? -13.166 9.124   11.779  1.00 105.66 ? 632 LYS A CA    1 
ATOM   5204 C  C     . LYS A 1 632 ? -12.242 8.522   12.825  1.00 118.63 ? 632 LYS A C     1 
ATOM   5205 O  O     . LYS A 1 632 ? -11.645 9.264   13.614  1.00 122.13 ? 632 LYS A O     1 
ATOM   5206 C  CB    . LYS A 1 632 ? -14.578 9.244   12.358  1.00 109.48 ? 632 LYS A CB    1 
ATOM   5207 C  CG    . LYS A 1 632 ? -15.296 10.534  11.999  1.00 102.90 ? 632 LYS A CG    1 
ATOM   5208 C  CD    . LYS A 1 632 ? -14.634 11.740  12.645  1.00 100.04 ? 632 LYS A CD    1 
ATOM   5209 C  CE    . LYS A 1 632 ? -15.640 12.853  12.892  1.00 101.00 ? 632 LYS A CE    1 
ATOM   5210 N  NZ    . LYS A 1 632 ? -16.656 12.939  11.805  1.00 99.99  ? 632 LYS A NZ    1 
ATOM   5211 N  N     . ASP A 1 633 ? -12.110 7.199   12.851  1.00 131.33 ? 633 ASP A N     1 
ATOM   5212 C  CA    . ASP A 1 633 ? -11.247 6.557   13.835  1.00 142.01 ? 633 ASP A CA    1 
ATOM   5213 C  C     . ASP A 1 633 ? -10.672 5.227   13.371  1.00 144.04 ? 633 ASP A C     1 
ATOM   5214 O  O     . ASP A 1 633 ? -9.992  4.572   14.166  1.00 164.40 ? 633 ASP A O     1 
ATOM   5215 C  CB    . ASP A 1 633 ? -12.016 6.361   15.151  1.00 152.45 ? 633 ASP A CB    1 
ATOM   5216 C  CG    . ASP A 1 633 ? -13.241 5.486   14.983  1.00 157.78 ? 633 ASP A CG    1 
ATOM   5217 O  OD1   . ASP A 1 633 ? -13.903 5.586   13.929  1.00 144.09 ? 633 ASP A OD1   1 
ATOM   5218 O  OD2   . ASP A 1 633 ? -13.543 4.699   15.905  1.00 166.71 ? 633 ASP A OD2   1 
ATOM   5219 N  N     . GLY A 1 634 ? -10.907 4.804   12.134  1.00 119.19 ? 634 GLY A N     1 
ATOM   5220 C  CA    . GLY A 1 634 ? -10.377 3.534   11.666  1.00 114.06 ? 634 GLY A CA    1 
ATOM   5221 C  C     . GLY A 1 634 ? -10.956 2.326   12.369  1.00 115.32 ? 634 GLY A C     1 
ATOM   5222 O  O     . GLY A 1 634 ? -10.222 1.376   12.668  1.00 109.69 ? 634 GLY A O     1 
ATOM   5223 N  N     . ASP A 1 635 ? -12.262 2.336   12.637  1.00 128.26 ? 635 ASP A N     1 
ATOM   5224 C  CA    . ASP A 1 635 ? -12.926 1.248   13.354  1.00 129.93 ? 635 ASP A CA    1 
ATOM   5225 C  C     . ASP A 1 635 ? -13.554 0.309   12.326  1.00 125.76 ? 635 ASP A C     1 
ATOM   5226 O  O     . ASP A 1 635 ? -14.745 0.376   12.022  1.00 113.81 ? 635 ASP A O     1 
ATOM   5227 C  CB    . ASP A 1 635 ? -13.961 1.805   14.328  1.00 124.48 ? 635 ASP A CB    1 
ATOM   5228 C  CG    . ASP A 1 635 ? -13.882 1.159   15.695  1.00 127.93 ? 635 ASP A CG    1 
ATOM   5229 O  OD1   . ASP A 1 635 ? -13.649 -0.063  15.761  1.00 124.24 ? 635 ASP A OD1   1 
ATOM   5230 O  OD2   . ASP A 1 635 ? -14.058 1.873   16.704  1.00 137.88 ? 635 ASP A OD2   1 
ATOM   5231 N  N     . VAL A 1 636 ? -12.721 -0.586  11.786  1.00 109.90 ? 636 VAL A N     1 
ATOM   5232 C  CA    . VAL A 1 636 ? -13.189 -1.537  10.778  1.00 104.20 ? 636 VAL A CA    1 
ATOM   5233 C  C     . VAL A 1 636 ? -14.250 -2.463  11.364  1.00 99.70  ? 636 VAL A C     1 
ATOM   5234 O  O     . VAL A 1 636 ? -15.235 -2.811  10.694  1.00 99.49  ? 636 VAL A O     1 
ATOM   5235 C  CB    . VAL A 1 636 ? -11.997 -2.328  10.202  1.00 95.97  ? 636 VAL A CB    1 
ATOM   5236 C  CG1   . VAL A 1 636 ? -12.338 -2.898  8.830   1.00 92.11  ? 636 VAL A CG1   1 
ATOM   5237 C  CG2   . VAL A 1 636 ? -10.750 -1.452  10.135  1.00 92.51  ? 636 VAL A CG2   1 
ATOM   5238 N  N     . GLU A 1 637 ? -14.066 -2.875  12.622  1.00 102.50 ? 637 GLU A N     1 
ATOM   5239 C  CA    . GLU A 1 637 ? -15.051 -3.729  13.280  1.00 103.81 ? 637 GLU A CA    1 
ATOM   5240 C  C     . GLU A 1 637 ? -16.400 -3.029  13.385  1.00 103.18 ? 637 GLU A C     1 
ATOM   5241 O  O     . GLU A 1 637 ? -17.449 -3.660  13.209  1.00 97.50  ? 637 GLU A O     1 
ATOM   5242 C  CB    . GLU A 1 637 ? -14.534 -4.168  14.660  1.00 114.45 ? 637 GLU A CB    1 
ATOM   5243 C  CG    . GLU A 1 637 ? -14.363 -3.060  15.717  1.00 123.56 ? 637 GLU A CG    1 
ATOM   5244 C  CD    . GLU A 1 637 ? -15.615 -2.769  16.544  1.00 141.50 ? 637 GLU A CD    1 
ATOM   5245 O  OE1   . GLU A 1 637 ? -16.737 -3.088  16.105  1.00 139.53 ? 637 GLU A OE1   1 
ATOM   5246 O  OE2   . GLU A 1 637 ? -15.471 -2.204  17.649  1.00 131.35 ? 637 GLU A OE2   1 
ATOM   5247 N  N     . LYS A 1 638 ? -16.399 -1.727  13.682  1.00 106.50 ? 638 LYS A N     1 
ATOM   5248 C  CA    . LYS A 1 638 ? -17.666 -1.011  13.768  1.00 101.51 ? 638 LYS A CA    1 
ATOM   5249 C  C     . LYS A 1 638 ? -18.396 -1.055  12.434  1.00 96.05  ? 638 LYS A C     1 
ATOM   5250 O  O     . LYS A 1 638 ? -19.607 -1.281  12.392  1.00 95.63  ? 638 LYS A O     1 
ATOM   5251 C  CB    . LYS A 1 638 ? -17.433 0.432   14.225  1.00 104.84 ? 638 LYS A CB    1 
ATOM   5252 C  CG    . LYS A 1 638 ? -18.716 1.227   14.494  1.00 101.39 ? 638 LYS A CG    1 
ATOM   5253 C  CD    . LYS A 1 638 ? -18.631 2.016   15.800  1.00 104.18 ? 638 LYS A CD    1 
ATOM   5254 C  CE    . LYS A 1 638 ? -19.498 1.391   16.886  1.00 104.91 ? 638 LYS A CE    1 
ATOM   5255 N  NZ    . LYS A 1 638 ? -19.473 2.187   18.145  1.00 101.27 ? 638 LYS A NZ    1 
ATOM   5256 N  N     . ALA A 1 639 ? -17.662 -0.903  11.330  1.00 92.77  ? 639 ALA A N     1 
ATOM   5257 C  CA    . ALA A 1 639 ? -18.274 -0.970  10.006  1.00 89.82  ? 639 ALA A CA    1 
ATOM   5258 C  C     . ALA A 1 639 ? -18.815 -2.365  9.700   1.00 92.42  ? 639 ALA A C     1 
ATOM   5259 O  O     . ALA A 1 639 ? -19.915 -2.501  9.143   1.00 91.44  ? 639 ALA A O     1 
ATOM   5260 C  CB    . ALA A 1 639 ? -17.261 -0.542  8.946   1.00 86.80  ? 639 ALA A CB    1 
ATOM   5261 N  N     . VAL A 1 640 ? -18.057 -3.416  10.040  1.00 92.95  ? 640 VAL A N     1 
ATOM   5262 C  CA    . VAL A 1 640 ? -18.544 -4.769  9.766   1.00 91.53  ? 640 VAL A CA    1 
ATOM   5263 C  C     . VAL A 1 640 ? -19.799 -5.054  10.590  1.00 90.99  ? 640 VAL A C     1 
ATOM   5264 O  O     . VAL A 1 640 ? -20.752 -5.682  10.105  1.00 89.65  ? 640 VAL A O     1 
ATOM   5265 C  CB    . VAL A 1 640 ? -17.431 -5.818  9.990   1.00 91.91  ? 640 VAL A CB    1 
ATOM   5266 C  CG1   . VAL A 1 640 ? -17.341 -6.269  11.443  1.00 98.44  ? 640 VAL A CG1   1 
ATOM   5267 C  CG2   . VAL A 1 640 ? -17.638 -7.024  9.075   1.00 90.08  ? 640 VAL A CG2   1 
ATOM   5268 N  N     . ARG A 1 641 ? -19.852 -4.544  11.824  1.00 90.83  ? 641 ARG A N     1 
ATOM   5269 C  CA    . ARG A 1 641 ? -21.074 -4.681  12.608  1.00 89.66  ? 641 ARG A CA    1 
ATOM   5270 C  C     . ARG A 1 641 ? -22.218 -3.880  12.000  1.00 92.34  ? 641 ARG A C     1 
ATOM   5271 O  O     . ARG A 1 641 ? -23.367 -4.327  12.024  1.00 93.11  ? 641 ARG A O     1 
ATOM   5272 C  CB    . ARG A 1 641 ? -20.851 -4.251  14.057  1.00 91.36  ? 641 ARG A CB    1 
ATOM   5273 C  CG    . ARG A 1 641 ? -19.922 -5.137  14.855  1.00 97.63  ? 641 ARG A CG    1 
ATOM   5274 C  CD    . ARG A 1 641 ? -19.407 -4.384  16.055  1.00 102.54 ? 641 ARG A CD    1 
ATOM   5275 N  NE    . ARG A 1 641 ? -20.394 -3.449  16.580  1.00 103.33 ? 641 ARG A NE    1 
ATOM   5276 C  CZ    . ARG A 1 641 ? -20.095 -2.286  17.143  1.00 102.66 ? 641 ARG A CZ    1 
ATOM   5277 N  NH1   . ARG A 1 641 ? -18.844 -1.865  17.238  1.00 106.27 ? 641 ARG A NH1   1 
ATOM   5278 N  NH2   . ARG A 1 641 ? -21.075 -1.525  17.622  1.00 101.21 ? 641 ARG A NH2   1 
ATOM   5279 N  N     . ILE A 1 642 ? -21.934 -2.687  11.470  1.00 90.41  ? 642 ILE A N     1 
ATOM   5280 C  CA    . ILE A 1 642 ? -22.987 -1.891  10.843  1.00 89.87  ? 642 ILE A CA    1 
ATOM   5281 C  C     . ILE A 1 642 ? -23.615 -2.662  9.689   1.00 87.75  ? 642 ILE A C     1 
ATOM   5282 O  O     . ILE A 1 642 ? -24.844 -2.736  9.565   1.00 83.63  ? 642 ILE A O     1 
ATOM   5283 C  CB    . ILE A 1 642 ? -22.444 -0.527  10.377  1.00 90.17  ? 642 ILE A CB    1 
ATOM   5284 C  CG1   . ILE A 1 642 ? -21.944 0.306   11.563  1.00 93.31  ? 642 ILE A CG1   1 
ATOM   5285 C  CG2   . ILE A 1 642 ? -23.505 0.225   9.577   1.00 83.54  ? 642 ILE A CG2   1 
ATOM   5286 C  CD1   . ILE A 1 642 ? -22.940 1.317   12.096  1.00 93.29  ? 642 ILE A CD1   1 
ATOM   5287 N  N     . VAL A 1 643 ? -22.782 -3.255  8.830   1.00 84.47  ? 643 VAL A N     1 
ATOM   5288 C  CA    . VAL A 1 643 ? -23.341 -3.952  7.672   1.00 86.55  ? 643 VAL A CA    1 
ATOM   5289 C  C     . VAL A 1 643 ? -24.089 -5.212  8.112   1.00 89.43  ? 643 VAL A C     1 
ATOM   5290 O  O     . VAL A 1 643 ? -25.152 -5.532  7.565   1.00 84.23  ? 643 VAL A O     1 
ATOM   5291 C  CB    . VAL A 1 643 ? -22.257 -4.251  6.615   1.00 85.93  ? 643 VAL A CB    1 
ATOM   5292 C  CG1   . VAL A 1 643 ? -21.021 -4.843  7.231   1.00 92.33  ? 643 VAL A CG1   1 
ATOM   5293 C  CG2   . VAL A 1 643 ? -22.804 -5.164  5.515   1.00 88.94  ? 643 VAL A CG2   1 
ATOM   5294 N  N     . LYS A 1 644 ? -23.583 -5.925  9.129   1.00 86.37  ? 644 LYS A N     1 
ATOM   5295 C  CA    . LYS A 1 644 ? -24.319 -7.091  9.625   1.00 91.49  ? 644 LYS A CA    1 
ATOM   5296 C  C     . LYS A 1 644 ? -25.672 -6.696  10.217  1.00 87.52  ? 644 LYS A C     1 
ATOM   5297 O  O     . LYS A 1 644 ? -26.686 -7.362  9.968   1.00 89.18  ? 644 LYS A O     1 
ATOM   5298 C  CB    . LYS A 1 644 ? -23.486 -7.851  10.659  1.00 93.58  ? 644 LYS A CB    1 
ATOM   5299 C  CG    . LYS A 1 644 ? -22.156 -8.368  10.129  1.00 107.01 ? 644 LYS A CG    1 
ATOM   5300 C  CD    . LYS A 1 644 ? -21.298 -8.979  11.230  1.00 104.39 ? 644 LYS A CD    1 
ATOM   5301 C  CE    . LYS A 1 644 ? -20.467 -10.143 10.705  1.00 102.81 ? 644 LYS A CE    1 
ATOM   5302 N  NZ    . LYS A 1 644 ? -21.208 -10.953 9.700   1.00 103.34 ? 644 LYS A NZ    1 
ATOM   5303 N  N     . GLU A 1 645 ? -25.710 -5.617  11.003  1.00 88.99  ? 645 GLU A N     1 
ATOM   5304 C  CA    . GLU A 1 645 ? -26.970 -5.178  11.598  1.00 99.98  ? 645 GLU A CA    1 
ATOM   5305 C  C     . GLU A 1 645 ? -27.954 -4.716  10.531  1.00 84.83  ? 645 GLU A C     1 
ATOM   5306 O  O     . GLU A 1 645 ? -29.150 -5.025  10.605  1.00 90.35  ? 645 GLU A O     1 
ATOM   5307 C  CB    . GLU A 1 645 ? -26.716 -4.061  12.612  1.00 104.25 ? 645 GLU A CB    1 
ATOM   5308 C  CG    . GLU A 1 645 ? -25.812 -4.455  13.773  1.00 104.17 ? 645 GLU A CG    1 
ATOM   5309 C  CD    . GLU A 1 645 ? -25.627 -3.333  14.778  1.00 108.55 ? 645 GLU A CD    1 
ATOM   5310 O  OE1   . GLU A 1 645 ? -25.993 -2.182  14.462  1.00 109.68 ? 645 GLU A OE1   1 
ATOM   5311 O  OE2   . GLU A 1 645 ? -25.100 -3.601  15.880  1.00 103.98 ? 645 GLU A OE2   1 
ATOM   5312 N  N     . VAL A 1 646 ? -27.472 -3.981  9.527   1.00 86.68  ? 646 VAL A N     1 
ATOM   5313 C  CA    . VAL A 1 646 ? -28.359 -3.506  8.471   1.00 82.38  ? 646 VAL A CA    1 
ATOM   5314 C  C     . VAL A 1 646 ? -28.891 -4.678  7.653   1.00 81.83  ? 646 VAL A C     1 
ATOM   5315 O  O     . VAL A 1 646 ? -30.069 -4.701  7.273   1.00 83.04  ? 646 VAL A O     1 
ATOM   5316 C  CB    . VAL A 1 646 ? -27.632 -2.472  7.592   1.00 74.92  ? 646 VAL A CB    1 
ATOM   5317 C  CG1   . VAL A 1 646 ? -28.412 -2.207  6.316   1.00 72.53  ? 646 VAL A CG1   1 
ATOM   5318 C  CG2   . VAL A 1 646 ? -27.421 -1.177  8.364   1.00 74.44  ? 646 VAL A CG2   1 
ATOM   5319 N  N     . THR A 1 647 ? -28.049 -5.683  7.391   1.00 79.49  ? 647 THR A N     1 
ATOM   5320 C  CA    . THR A 1 647 ? -28.520 -6.827  6.619   1.00 81.25  ? 647 THR A CA    1 
ATOM   5321 C  C     . THR A 1 647 ? -29.511 -7.668  7.420   1.00 87.91  ? 647 THR A C     1 
ATOM   5322 O  O     . THR A 1 647 ? -30.461 -8.213  6.844   1.00 87.64  ? 647 THR A O     1 
ATOM   5323 C  CB    . THR A 1 647 ? -27.331 -7.664  6.123   1.00 85.17  ? 647 THR A CB    1 
ATOM   5324 O  OG1   . THR A 1 647 ? -27.718 -8.409  4.963   1.00 89.90  ? 647 THR A OG1   1 
ATOM   5325 C  CG2   . THR A 1 647 ? -26.831 -8.637  7.181   1.00 89.77  ? 647 THR A CG2   1 
ATOM   5326 N  N     . GLU A 1 648 ? -29.345 -7.749  8.746   1.00 87.68  ? 648 GLU A N     1 
ATOM   5327 C  CA    . GLU A 1 648 ? -30.347 -8.445  9.550   1.00 91.67  ? 648 GLU A CA    1 
ATOM   5328 C  C     . GLU A 1 648 ? -31.657 -7.667  9.580   1.00 97.45  ? 648 GLU A C     1 
ATOM   5329 O  O     . GLU A 1 648 ? -32.741 -8.260  9.509   1.00 90.73  ? 648 GLU A O     1 
ATOM   5330 C  CB    . GLU A 1 648 ? -29.831 -8.684  10.969  1.00 101.83 ? 648 GLU A CB    1 
ATOM   5331 C  CG    . GLU A 1 648 ? -30.925 -9.103  11.948  1.00 110.03 ? 648 GLU A CG    1 
ATOM   5332 C  CD    . GLU A 1 648 ? -30.514 -8.955  13.399  1.00 128.05 ? 648 GLU A CD    1 
ATOM   5333 O  OE1   . GLU A 1 648 ? -29.330 -8.652  13.657  1.00 132.79 ? 648 GLU A OE1   1 
ATOM   5334 O  OE2   . GLU A 1 648 ? -31.378 -9.145  14.282  1.00 111.57 ? 648 GLU A OE2   1 
ATOM   5335 N  N     . LYS A 1 649 ? -31.577 -6.336  9.680   1.00 92.37  ? 649 LYS A N     1 
ATOM   5336 C  CA    . LYS A 1 649 ? -32.778 -5.509  9.610   1.00 88.63  ? 649 LYS A CA    1 
ATOM   5337 C  C     . LYS A 1 649 ? -33.513 -5.717  8.293   1.00 86.89  ? 649 LYS A C     1 
ATOM   5338 O  O     . LYS A 1 649 ? -34.746 -5.808  8.267   1.00 85.22  ? 649 LYS A O     1 
ATOM   5339 C  CB    . LYS A 1 649 ? -32.409 -4.036  9.786   1.00 88.46  ? 649 LYS A CB    1 
ATOM   5340 C  CG    . LYS A 1 649 ? -32.618 -3.495  11.190  1.00 92.93  ? 649 LYS A CG    1 
ATOM   5341 C  CD    . LYS A 1 649 ? -32.577 -1.975  11.201  1.00 93.63  ? 649 LYS A CD    1 
ATOM   5342 C  CE    . LYS A 1 649 ? -33.266 -1.409  12.429  1.00 95.45  ? 649 LYS A CE    1 
ATOM   5343 N  NZ    . LYS A 1 649 ? -34.233 -0.336  12.068  1.00 92.31  ? 649 LYS A NZ    1 
ATOM   5344 N  N     . LEU A 1 650 ? -32.769 -5.791  7.187   1.00 85.69  ? 650 LEU A N     1 
ATOM   5345 C  CA    . LEU A 1 650 ? -33.392 -6.039  5.890   1.00 81.89  ? 650 LEU A CA    1 
ATOM   5346 C  C     . LEU A 1 650 ? -34.036 -7.419  5.840   1.00 88.73  ? 650 LEU A C     1 
ATOM   5347 O  O     . LEU A 1 650 ? -35.155 -7.571  5.333   1.00 83.58  ? 650 LEU A O     1 
ATOM   5348 C  CB    . LEU A 1 650 ? -32.358 -5.895  4.774   1.00 78.73  ? 650 LEU A CB    1 
ATOM   5349 C  CG    . LEU A 1 650 ? -31.893 -4.493  4.374   1.00 81.02  ? 650 LEU A CG    1 
ATOM   5350 C  CD1   . LEU A 1 650 ? -31.482 -4.469  2.911   1.00 71.72  ? 650 LEU A CD1   1 
ATOM   5351 C  CD2   . LEU A 1 650 ? -32.987 -3.477  4.625   1.00 74.86  ? 650 LEU A CD2   1 
ATOM   5352 N  N     . SER A 1 651 ? -33.347 -8.439  6.363   1.00 88.72  ? 651 SER A N     1 
ATOM   5353 C  CA    . SER A 1 651 ? -33.859 -9.803  6.265   1.00 80.97  ? 651 SER A CA    1 
ATOM   5354 C  C     . SER A 1 651 ? -35.173 -9.964  7.020   1.00 88.31  ? 651 SER A C     1 
ATOM   5355 O  O     . SER A 1 651 ? -36.072 -10.685 6.571   1.00 89.93  ? 651 SER A O     1 
ATOM   5356 C  CB    . SER A 1 651 ? -32.818 -10.794 6.785   1.00 79.33  ? 651 SER A CB    1 
ATOM   5357 O  OG    . SER A 1 651 ? -32.770 -10.787 8.201   1.00 89.44  ? 651 SER A OG    1 
ATOM   5358 N  N     . LYS A 1 652 ? -35.307 -9.300  8.166   1.00 91.33  ? 652 LYS A N     1 
ATOM   5359 C  CA    . LYS A 1 652 ? -36.516 -9.383  8.974   1.00 85.25  ? 652 LYS A CA    1 
ATOM   5360 C  C     . LYS A 1 652 ? -37.580 -8.378  8.551   1.00 88.85  ? 652 LYS A C     1 
ATOM   5361 O  O     . LYS A 1 652 ? -38.550 -8.179  9.289   1.00 93.01  ? 652 LYS A O     1 
ATOM   5362 C  CB    . LYS A 1 652 ? -36.175 -9.189  10.454  1.00 84.80  ? 652 LYS A CB    1 
ATOM   5363 C  CG    . LYS A 1 652 ? -35.088 -10.121 10.963  1.00 82.92  ? 652 LYS A CG    1 
ATOM   5364 C  CD    . LYS A 1 652 ? -34.677 -9.774  12.384  1.00 87.74  ? 652 LYS A CD    1 
ATOM   5365 C  CE    . LYS A 1 652 ? -35.587 -10.441 13.401  1.00 87.71  ? 652 LYS A CE    1 
ATOM   5366 N  NZ    . LYS A 1 652 ? -35.006 -11.711 13.920  1.00 93.07  ? 652 LYS A NZ    1 
ATOM   5367 N  N     . TYR A 1 653 ? -37.423 -7.751  7.385   1.00 91.53  ? 653 TYR A N     1 
ATOM   5368 C  CA    . TYR A 1 653 ? -38.376 -6.769  6.868   1.00 93.39  ? 653 TYR A CA    1 
ATOM   5369 C  C     . TYR A 1 653 ? -38.644 -5.674  7.899   1.00 95.00  ? 653 TYR A C     1 
ATOM   5370 O  O     . TYR A 1 653 ? -39.787 -5.301  8.171   1.00 98.12  ? 653 TYR A O     1 
ATOM   5371 C  CB    . TYR A 1 653 ? -39.676 -7.443  6.424   1.00 91.67  ? 653 TYR A CB    1 
ATOM   5372 C  CG    . TYR A 1 653 ? -39.479 -8.515  5.376   1.00 104.81 ? 653 TYR A CG    1 
ATOM   5373 C  CD1   . TYR A 1 653 ? -39.166 -9.821  5.736   1.00 98.52  ? 653 TYR A CD1   1 
ATOM   5374 C  CD2   . TYR A 1 653 ? -39.582 -8.217  4.024   1.00 104.17 ? 653 TYR A CD2   1 
ATOM   5375 C  CE1   . TYR A 1 653 ? -38.978 -10.802 4.780   1.00 99.36  ? 653 TYR A CE1   1 
ATOM   5376 C  CE2   . TYR A 1 653 ? -39.392 -9.190  3.060   1.00 101.64 ? 653 TYR A CE2   1 
ATOM   5377 C  CZ    . TYR A 1 653 ? -39.092 -10.481 3.444   1.00 104.06 ? 653 TYR A CZ    1 
ATOM   5378 O  OH    . TYR A 1 653 ? -38.904 -11.452 2.488   1.00 109.09 ? 653 TYR A OH    1 
ATOM   5379 N  N     . GLU A 1 654 ? -37.561 -5.154  8.473   1.00 103.38 ? 654 GLU A N     1 
ATOM   5380 C  CA    . GLU A 1 654 ? -37.630 -4.192  9.564   1.00 94.01  ? 654 GLU A CA    1 
ATOM   5381 C  C     . GLU A 1 654 ? -37.277 -2.774  9.140   1.00 89.51  ? 654 GLU A C     1 
ATOM   5382 O  O     . GLU A 1 654 ? -37.347 -1.860  9.968   1.00 100.54 ? 654 GLU A O     1 
ATOM   5383 C  CB    . GLU A 1 654 ? -36.702 -4.630  10.702  1.00 101.24 ? 654 GLU A CB    1 
ATOM   5384 C  CG    . GLU A 1 654 ? -37.322 -4.569  12.084  1.00 106.28 ? 654 GLU A CG    1 
ATOM   5385 C  CD    . GLU A 1 654 ? -36.429 -5.186  13.142  1.00 112.79 ? 654 GLU A CD    1 
ATOM   5386 O  OE1   . GLU A 1 654 ? -35.193 -5.033  13.042  1.00 106.83 ? 654 GLU A OE1   1 
ATOM   5387 O  OE2   . GLU A 1 654 ? -36.961 -5.830  14.071  1.00 109.06 ? 654 GLU A OE2   1 
ATOM   5388 N  N     . VAL A 1 655 ? -36.900 -2.564  7.883   1.00 87.52  ? 655 VAL A N     1 
ATOM   5389 C  CA    . VAL A 1 655 ? -36.469 -1.250  7.413   1.00 86.02  ? 655 VAL A CA    1 
ATOM   5390 C  C     . VAL A 1 655 ? -37.617 -0.588  6.659   1.00 85.28  ? 655 VAL A C     1 
ATOM   5391 O  O     . VAL A 1 655 ? -38.296 -1.249  5.859   1.00 81.87  ? 655 VAL A O     1 
ATOM   5392 C  CB    . VAL A 1 655 ? -35.203 -1.366  6.547   1.00 82.55  ? 655 VAL A CB    1 
ATOM   5393 C  CG1   . VAL A 1 655 ? -35.052 -0.163  5.627   1.00 73.97  ? 655 VAL A CG1   1 
ATOM   5394 C  CG2   . VAL A 1 655 ? -33.976 -1.513  7.436   1.00 83.28  ? 655 VAL A CG2   1 
ATOM   5395 N  N     . PRO A 1 656 ? -37.881 0.696   6.896   1.00 85.96  ? 656 PRO A N     1 
ATOM   5396 C  CA    . PRO A 1 656 ? -38.979 1.380   6.201   1.00 84.38  ? 656 PRO A CA    1 
ATOM   5397 C  C     . PRO A 1 656 ? -38.779 1.357   4.697   1.00 83.97  ? 656 PRO A C     1 
ATOM   5398 O  O     . PRO A 1 656 ? -37.672 1.623   4.204   1.00 79.40  ? 656 PRO A O     1 
ATOM   5399 C  CB    . PRO A 1 656 ? -38.906 2.813   6.749   1.00 78.29  ? 656 PRO A CB    1 
ATOM   5400 C  CG    . PRO A 1 656 ? -38.211 2.684   8.058   1.00 78.53  ? 656 PRO A CG    1 
ATOM   5401 C  CD    . PRO A 1 656 ? -37.226 1.567   7.888   1.00 82.40  ? 656 PRO A CD    1 
ATOM   5402 N  N     . PRO A 1 657 ? -39.830 1.049   3.933   1.00 81.69  ? 657 PRO A N     1 
ATOM   5403 C  CA    . PRO A 1 657 ? -39.683 0.999   2.468   1.00 78.01  ? 657 PRO A CA    1 
ATOM   5404 C  C     . PRO A 1 657 ? -39.350 2.341   1.842   1.00 75.03  ? 657 PRO A C     1 
ATOM   5405 O  O     . PRO A 1 657 ? -38.924 2.373   0.681   1.00 73.25  ? 657 PRO A O     1 
ATOM   5406 C  CB    . PRO A 1 657 ? -41.050 0.483   1.995   1.00 75.32  ? 657 PRO A CB    1 
ATOM   5407 C  CG    . PRO A 1 657 ? -41.989 0.816   3.110   1.00 75.07  ? 657 PRO A CG    1 
ATOM   5408 C  CD    . PRO A 1 657 ? -41.189 0.692   4.369   1.00 77.12  ? 657 PRO A CD    1 
ATOM   5409 N  N     . GLU A 1 658 ? -39.531 3.447   2.567   1.00 76.69  ? 658 GLU A N     1 
ATOM   5410 C  CA    . GLU A 1 658 ? -39.167 4.752   2.023   1.00 76.52  ? 658 GLU A CA    1 
ATOM   5411 C  C     . GLU A 1 658 ? -37.667 4.835   1.768   1.00 81.54  ? 658 GLU A C     1 
ATOM   5412 O  O     . GLU A 1 658 ? -37.225 5.476   0.806   1.00 77.23  ? 658 GLU A O     1 
ATOM   5413 C  CB    . GLU A 1 658 ? -39.617 5.864   2.972   1.00 81.76  ? 658 GLU A CB    1 
ATOM   5414 C  CG    . GLU A 1 658 ? -41.127 5.986   3.118   1.00 91.40  ? 658 GLU A CG    1 
ATOM   5415 C  CD    . GLU A 1 658 ? -41.703 5.004   4.123   1.00 103.71 ? 658 GLU A CD    1 
ATOM   5416 O  OE1   . GLU A 1 658 ? -40.937 4.494   4.966   1.00 89.40  ? 658 GLU A OE1   1 
ATOM   5417 O  OE2   . GLU A 1 658 ? -42.925 4.741   4.071   1.00 101.99 ? 658 GLU A OE2   1 
ATOM   5418 N  N     . LYS A 1 659 ? -36.868 4.187   2.615   1.00 75.00  ? 659 LYS A N     1 
ATOM   5419 C  CA    . LYS A 1 659 ? -35.427 4.096   2.410   1.00 78.43  ? 659 LYS A CA    1 
ATOM   5420 C  C     . LYS A 1 659 ? -35.047 3.075   1.346   1.00 74.09  ? 659 LYS A C     1 
ATOM   5421 O  O     . LYS A 1 659 ? -33.857 2.797   1.168   1.00 63.80  ? 659 LYS A O     1 
ATOM   5422 C  CB    . LYS A 1 659 ? -34.723 3.741   3.723   1.00 74.62  ? 659 LYS A CB    1 
ATOM   5423 C  CG    . LYS A 1 659 ? -35.026 4.670   4.887   1.00 76.52  ? 659 LYS A CG    1 
ATOM   5424 C  CD    . LYS A 1 659 ? -34.368 4.161   6.163   1.00 73.56  ? 659 LYS A CD    1 
ATOM   5425 C  CE    . LYS A 1 659 ? -34.183 5.270   7.184   1.00 80.93  ? 659 LYS A CE    1 
ATOM   5426 N  NZ    . LYS A 1 659 ? -33.037 4.991   8.093   1.00 81.94  ? 659 LYS A NZ    1 
ATOM   5427 N  N     . LEU A 1 660 ? -36.024 2.515   0.632   1.00 74.99  ? 660 LEU A N     1 
ATOM   5428 C  CA    . LEU A 1 660 ? -35.777 1.411   -0.287  1.00 67.49  ? 660 LEU A CA    1 
ATOM   5429 C  C     . LEU A 1 660 ? -36.077 1.775   -1.733  1.00 61.08  ? 660 LEU A C     1 
ATOM   5430 O  O     . LEU A 1 660 ? -36.019 0.904   -2.609  1.00 56.66  ? 660 LEU A O     1 
ATOM   5431 C  CB    . LEU A 1 660 ? -36.607 0.200   0.129   1.00 61.15  ? 660 LEU A CB    1 
ATOM   5432 C  CG    . LEU A 1 660 ? -35.827 -0.805  0.968   1.00 68.70  ? 660 LEU A CG    1 
ATOM   5433 C  CD1   . LEU A 1 660 ? -36.661 -2.033  1.236   1.00 68.70  ? 660 LEU A CD1   1 
ATOM   5434 C  CD2   . LEU A 1 660 ? -34.535 -1.164  0.278   1.00 69.42  ? 660 LEU A CD2   1 
ATOM   5435 N  N     . VAL A 1 661 ? -36.395 3.030   -2.006  1.00 63.88  ? 661 VAL A N     1 
ATOM   5436 C  CA    . VAL A 1 661 ? -36.849 3.456   -3.322  1.00 66.56  ? 661 VAL A CA    1 
ATOM   5437 C  C     . VAL A 1 661 ? -35.645 3.766   -4.195  1.00 60.10  ? 661 VAL A C     1 
ATOM   5438 O  O     . VAL A 1 661 ? -34.673 4.386   -3.745  1.00 59.41  ? 661 VAL A O     1 
ATOM   5439 C  CB    . VAL A 1 661 ? -37.782 4.676   -3.204  1.00 64.15  ? 661 VAL A CB    1 
ATOM   5440 C  CG1   . VAL A 1 661 ? -38.251 5.121   -4.574  1.00 54.34  ? 661 VAL A CG1   1 
ATOM   5441 C  CG2   . VAL A 1 661 ? -38.962 4.350   -2.306  1.00 68.19  ? 661 VAL A CG2   1 
ATOM   5442 N  N     . ILE A 1 662 ? -35.705 3.328   -5.450  1.00 56.76  ? 662 ILE A N     1 
ATOM   5443 C  CA    . ILE A 1 662 ? -34.695 3.643   -6.451  1.00 60.85  ? 662 ILE A CA    1 
ATOM   5444 C  C     . ILE A 1 662 ? -35.292 4.655   -7.417  1.00 60.81  ? 662 ILE A C     1 
ATOM   5445 O  O     . ILE A 1 662 ? -36.370 4.423   -7.981  1.00 65.70  ? 662 ILE A O     1 
ATOM   5446 C  CB    . ILE A 1 662 ? -34.219 2.383   -7.195  1.00 62.49  ? 662 ILE A CB    1 
ATOM   5447 C  CG1   . ILE A 1 662 ? -33.486 1.444   -6.237  1.00 59.23  ? 662 ILE A CG1   1 
ATOM   5448 C  CG2   . ILE A 1 662 ? -33.320 2.760   -8.363  1.00 59.90  ? 662 ILE A CG2   1 
ATOM   5449 C  CD1   . ILE A 1 662 ? -33.492 -0.001  -6.679  1.00 59.11  ? 662 ILE A CD1   1 
ATOM   5450 N  N     . HIS A 1 663 ? -34.600 5.781   -7.590  1.00 65.47  ? 663 HIS A N     1 
ATOM   5451 C  CA    . HIS A 1 663 ? -35.017 6.836   -8.504  1.00 64.95  ? 663 HIS A CA    1 
ATOM   5452 C  C     . HIS A 1 663 ? -34.135 6.787   -9.746  1.00 64.25  ? 663 HIS A C     1 
ATOM   5453 O  O     . HIS A 1 663 ? -32.910 6.922   -9.648  1.00 59.10  ? 663 HIS A O     1 
ATOM   5454 C  CB    . HIS A 1 663 ? -34.925 8.214   -7.847  1.00 60.22  ? 663 HIS A CB    1 
ATOM   5455 C  CG    . HIS A 1 663 ? -35.452 8.263   -6.446  1.00 62.21  ? 663 HIS A CG    1 
ATOM   5456 N  ND1   . HIS A 1 663 ? -36.758 8.592   -6.152  1.00 59.68  ? 663 HIS A ND1   1 
ATOM   5457 C  CD2   . HIS A 1 663 ? -34.844 8.041   -5.256  1.00 63.72  ? 663 HIS A CD2   1 
ATOM   5458 C  CE1   . HIS A 1 663 ? -36.934 8.562   -4.843  1.00 57.18  ? 663 HIS A CE1   1 
ATOM   5459 N  NE2   . HIS A 1 663 ? -35.789 8.231   -4.276  1.00 63.10  ? 663 HIS A NE2   1 
ATOM   5460 N  N     . LYS A 1 664 ? -34.755 6.592   -10.906 1.00 63.12  ? 664 LYS A N     1 
ATOM   5461 C  CA    . LYS A 1 664 ? -34.043 6.585   -12.176 1.00 63.30  ? 664 LYS A CA    1 
ATOM   5462 C  C     . LYS A 1 664 ? -34.833 7.399   -13.187 1.00 61.18  ? 664 LYS A C     1 
ATOM   5463 O  O     . LYS A 1 664 ? -36.064 7.385   -13.180 1.00 60.49  ? 664 LYS A O     1 
ATOM   5464 C  CB    . LYS A 1 664 ? -33.821 5.157   -12.692 1.00 70.35  ? 664 LYS A CB    1 
ATOM   5465 C  CG    . LYS A 1 664 ? -32.657 5.027   -13.664 1.00 66.52  ? 664 LYS A CG    1 
ATOM   5466 C  CD    . LYS A 1 664 ? -32.028 3.643   -13.614 1.00 65.35  ? 664 LYS A CD    1 
ATOM   5467 C  CE    . LYS A 1 664 ? -31.943 3.115   -12.191 1.00 65.18  ? 664 LYS A CE    1 
ATOM   5468 N  NZ    . LYS A 1 664 ? -31.144 1.861   -12.119 1.00 71.59  ? 664 LYS A NZ    1 
ATOM   5469 N  N     . GLN A 1 665 ? -34.124 8.106   -14.056 1.00 62.65  ? 665 GLN A N     1 
ATOM   5470 C  CA    . GLN A 1 665 ? -34.736 9.050   -14.977 1.00 65.98  ? 665 GLN A CA    1 
ATOM   5471 C  C     . GLN A 1 665 ? -34.773 8.474   -16.386 1.00 70.12  ? 665 GLN A C     1 
ATOM   5472 O  O     . GLN A 1 665 ? -33.790 7.895   -16.857 1.00 74.58  ? 665 GLN A O     1 
ATOM   5473 C  CB    . GLN A 1 665 ? -33.973 10.376  -14.960 1.00 67.58  ? 665 GLN A CB    1 
ATOM   5474 C  CG    . GLN A 1 665 ? -34.168 11.252  -16.175 1.00 74.28  ? 665 GLN A CG    1 
ATOM   5475 C  CD    . GLN A 1 665 ? -33.569 12.629  -15.978 1.00 86.83  ? 665 GLN A CD    1 
ATOM   5476 O  OE1   . GLN A 1 665 ? -34.277 13.635  -15.986 1.00 93.59  ? 665 GLN A OE1   1 
ATOM   5477 N  NE2   . GLN A 1 665 ? -32.256 12.678  -15.786 1.00 76.67  ? 665 GLN A NE2   1 
ATOM   5478 N  N     . ILE A 1 666 ? -35.916 8.625   -17.050 1.00 73.99  ? 666 ILE A N     1 
ATOM   5479 C  CA    . ILE A 1 666 ? -36.053 8.271   -18.458 1.00 74.59  ? 666 ILE A CA    1 
ATOM   5480 C  C     . ILE A 1 666 ? -35.617 9.463   -19.297 1.00 72.00  ? 666 ILE A C     1 
ATOM   5481 O  O     . ILE A 1 666 ? -36.048 10.596  -19.056 1.00 76.14  ? 666 ILE A O     1 
ATOM   5482 C  CB    . ILE A 1 666 ? -37.497 7.864   -18.789 1.00 76.33  ? 666 ILE A CB    1 
ATOM   5483 C  CG1   . ILE A 1 666 ? -38.473 8.691   -17.961 1.00 78.28  ? 666 ILE A CG1   1 
ATOM   5484 C  CG2   . ILE A 1 666 ? -37.706 6.374   -18.558 1.00 78.90  ? 666 ILE A CG2   1 
ATOM   5485 C  CD1   . ILE A 1 666 ? -39.898 8.417   -18.287 1.00 97.94  ? 666 ILE A CD1   1 
ATOM   5486 N  N     . THR A 1 667 ? -34.764 9.208   -20.288 1.00 76.09  ? 667 THR A N     1 
ATOM   5487 C  CA    . THR A 1 667 ? -34.142 10.269  -21.064 1.00 79.12  ? 667 THR A CA    1 
ATOM   5488 C  C     . THR A 1 667 ? -34.674 10.389  -22.484 1.00 74.37  ? 667 THR A C     1 
ATOM   5489 O  O     . THR A 1 667 ? -34.320 11.350  -23.176 1.00 84.10  ? 667 THR A O     1 
ATOM   5490 C  CB    . THR A 1 667 ? -32.621 10.057  -21.121 1.00 74.37  ? 667 THR A CB    1 
ATOM   5491 O  OG1   . THR A 1 667 ? -32.312 9.117   -22.157 1.00 74.00  ? 667 THR A OG1   1 
ATOM   5492 C  CG2   . THR A 1 667 ? -32.105 9.525   -19.793 1.00 64.08  ? 667 THR A CG2   1 
ATOM   5493 N  N     . ARG A 1 668 ? -35.496 9.449   -22.943 1.00 80.38  ? 668 ARG A N     1 
ATOM   5494 C  CA    . ARG A 1 668 ? -35.993 9.452   -24.312 1.00 85.81  ? 668 ARG A CA    1 
ATOM   5495 C  C     . ARG A 1 668 ? -37.460 9.048   -24.310 1.00 85.63  ? 668 ARG A C     1 
ATOM   5496 O  O     . ARG A 1 668 ? -38.059 8.788   -23.262 1.00 82.25  ? 668 ARG A O     1 
ATOM   5497 C  CB    . ARG A 1 668 ? -35.177 8.509   -25.206 1.00 83.87  ? 668 ARG A CB    1 
ATOM   5498 C  CG    . ARG A 1 668 ? -33.687 8.792   -25.240 1.00 88.25  ? 668 ARG A CG    1 
ATOM   5499 C  CD    . ARG A 1 668 ? -32.898 7.539   -24.899 1.00 90.30  ? 668 ARG A CD    1 
ATOM   5500 N  NE    . ARG A 1 668 ? -32.943 6.546   -25.965 1.00 96.97  ? 668 ARG A NE    1 
ATOM   5501 C  CZ    . ARG A 1 668 ? -32.104 5.527   -26.073 1.00 92.98  ? 668 ARG A CZ    1 
ATOM   5502 N  NH1   . ARG A 1 668 ? -31.144 5.325   -25.185 1.00 84.83  ? 668 ARG A NH1   1 
ATOM   5503 N  NH2   . ARG A 1 668 ? -32.229 4.689   -27.099 1.00 99.28  ? 668 ARG A NH2   1 
ATOM   5504 N  N     . ASP A 1 669 ? -38.043 9.006   -25.504 1.00 93.77  ? 669 ASP A N     1 
ATOM   5505 C  CA    . ASP A 1 669 ? -39.379 8.456   -25.668 1.00 101.08 ? 669 ASP A CA    1 
ATOM   5506 C  C     . ASP A 1 669 ? -39.333 6.942   -25.508 1.00 92.45  ? 669 ASP A C     1 
ATOM   5507 O  O     . ASP A 1 669 ? -38.418 6.280   -26.008 1.00 97.49  ? 669 ASP A O     1 
ATOM   5508 C  CB    . ASP A 1 669 ? -39.938 8.830   -27.040 1.00 113.15 ? 669 ASP A CB    1 
ATOM   5509 C  CG    . ASP A 1 669 ? -40.473 10.250  -27.087 1.00 121.42 ? 669 ASP A CG    1 
ATOM   5510 O  OD1   . ASP A 1 669 ? -41.162 10.664  -26.130 1.00 112.56 ? 669 ASP A OD1   1 
ATOM   5511 O  OD2   . ASP A 1 669 ? -40.199 10.954  -28.082 1.00 125.22 ? 669 ASP A OD2   1 
ATOM   5512 N  N     . LEU A 1 670 ? -40.329 6.391   -24.805 1.00 84.19  ? 670 LEU A N     1 
ATOM   5513 C  CA    . LEU A 1 670 ? -40.328 4.960   -24.512 1.00 86.42  ? 670 LEU A CA    1 
ATOM   5514 C  C     . LEU A 1 670 ? -40.280 4.118   -25.780 1.00 88.28  ? 670 LEU A C     1 
ATOM   5515 O  O     . LEU A 1 670 ? -39.810 2.975   -25.747 1.00 92.09  ? 670 LEU A O     1 
ATOM   5516 C  CB    . LEU A 1 670 ? -41.557 4.582   -23.686 1.00 83.38  ? 670 LEU A CB    1 
ATOM   5517 C  CG    . LEU A 1 670 ? -41.813 5.358   -22.395 1.00 82.93  ? 670 LEU A CG    1 
ATOM   5518 C  CD1   . LEU A 1 670 ? -43.195 5.021   -21.860 1.00 77.92  ? 670 LEU A CD1   1 
ATOM   5519 C  CD2   . LEU A 1 670 ? -40.739 5.062   -21.361 1.00 79.83  ? 670 LEU A CD2   1 
ATOM   5520 N  N     . LYS A 1 671 ? -40.762 4.659   -26.901 1.00 89.55  ? 671 LYS A N     1 
ATOM   5521 C  CA    . LYS A 1 671 ? -40.703 3.923   -28.160 1.00 94.26  ? 671 LYS A CA    1 
ATOM   5522 C  C     . LYS A 1 671 ? -39.261 3.672   -28.586 1.00 92.29  ? 671 LYS A C     1 
ATOM   5523 O  O     . LYS A 1 671 ? -38.936 2.599   -29.107 1.00 91.14  ? 671 LYS A O     1 
ATOM   5524 C  CB    . LYS A 1 671 ? -41.456 4.688   -29.248 1.00 90.51  ? 671 LYS A CB    1 
ATOM   5525 C  CG    . LYS A 1 671 ? -42.666 5.464   -28.749 1.00 94.99  ? 671 LYS A CG    1 
ATOM   5526 C  CD    . LYS A 1 671 ? -42.884 6.726   -29.570 1.00 101.21 ? 671 LYS A CD    1 
ATOM   5527 C  CE    . LYS A 1 671 ? -43.708 7.754   -28.809 1.00 104.97 ? 671 LYS A CE    1 
ATOM   5528 N  NZ    . LYS A 1 671 ? -43.061 8.178   -27.537 1.00 96.68  ? 671 LYS A NZ    1 
ATOM   5529 N  N     . ASP A 1 672 ? -38.382 4.648   -28.365 1.00 92.25  ? 672 ASP A N     1 
ATOM   5530 C  CA    . ASP A 1 672 ? -37.004 4.588   -28.829 1.00 97.10  ? 672 ASP A CA    1 
ATOM   5531 C  C     . ASP A 1 672 ? -36.077 3.860   -27.862 1.00 93.61  ? 672 ASP A C     1 
ATOM   5532 O  O     . ASP A 1 672 ? -34.859 3.869   -28.067 1.00 91.28  ? 672 ASP A O     1 
ATOM   5533 C  CB    . ASP A 1 672 ? -36.478 6.003   -29.088 1.00 95.84  ? 672 ASP A CB    1 
ATOM   5534 C  CG    . ASP A 1 672 ? -36.959 6.570   -30.410 1.00 99.63  ? 672 ASP A CG    1 
ATOM   5535 O  OD1   . ASP A 1 672 ? -37.897 7.395   -30.399 1.00 95.80  ? 672 ASP A OD1   1 
ATOM   5536 O  OD2   . ASP A 1 672 ? -36.402 6.190   -31.462 1.00 105.44 ? 672 ASP A OD2   1 
ATOM   5537 N  N     . TYR A 1 673 ? -36.618 3.236   -26.819 1.00 88.61  ? 673 TYR A N     1 
ATOM   5538 C  CA    . TYR A 1 673 ? -35.795 2.490   -25.877 1.00 87.77  ? 673 TYR A CA    1 
ATOM   5539 C  C     . TYR A 1 673 ? -35.574 1.078   -26.406 1.00 86.78  ? 673 TYR A C     1 
ATOM   5540 O  O     . TYR A 1 673 ? -36.535 0.326   -26.602 1.00 92.52  ? 673 TYR A O     1 
ATOM   5541 C  CB    . TYR A 1 673 ? -36.452 2.453   -24.500 1.00 86.27  ? 673 TYR A CB    1 
ATOM   5542 C  CG    . TYR A 1 673 ? -36.000 3.551   -23.562 1.00 89.44  ? 673 TYR A CG    1 
ATOM   5543 C  CD1   . TYR A 1 673 ? -36.056 3.377   -22.194 1.00 92.30  ? 673 TYR A CD1   1 
ATOM   5544 C  CD2   . TYR A 1 673 ? -35.525 4.764   -24.044 1.00 94.10  ? 673 TYR A CD2   1 
ATOM   5545 C  CE1   . TYR A 1 673 ? -35.654 4.367   -21.326 1.00 91.10  ? 673 TYR A CE1   1 
ATOM   5546 C  CE2   . TYR A 1 673 ? -35.120 5.761   -23.179 1.00 90.01  ? 673 TYR A CE2   1 
ATOM   5547 C  CZ    . TYR A 1 673 ? -35.186 5.557   -21.822 1.00 83.67  ? 673 TYR A CZ    1 
ATOM   5548 O  OH    . TYR A 1 673 ? -34.782 6.543   -20.954 1.00 88.06  ? 673 TYR A OH    1 
ATOM   5549 N  N     . LYS A 1 674 ? -34.310 0.717   -26.634 1.00 85.09  ? 674 LYS A N     1 
ATOM   5550 C  CA    . LYS A 1 674 ? -33.995 -0.626  -27.109 1.00 83.19  ? 674 LYS A CA    1 
ATOM   5551 C  C     . LYS A 1 674 ? -33.898 -1.611  -25.950 1.00 83.88  ? 674 LYS A C     1 
ATOM   5552 O  O     . LYS A 1 674 ? -34.537 -2.669  -25.968 1.00 90.36  ? 674 LYS A O     1 
ATOM   5553 C  CB    . LYS A 1 674 ? -32.694 -0.607  -27.912 1.00 89.30  ? 674 LYS A CB    1 
ATOM   5554 C  CG    . LYS A 1 674 ? -32.585 0.557   -28.884 1.00 95.24  ? 674 LYS A CG    1 
ATOM   5555 C  CD    . LYS A 1 674 ? -31.298 0.482   -29.689 1.00 97.82  ? 674 LYS A CD    1 
ATOM   5556 C  CE    . LYS A 1 674 ? -30.161 1.199   -28.977 1.00 106.94 ? 674 LYS A CE    1 
ATOM   5557 N  NZ    . LYS A 1 674 ? -29.496 2.200   -29.856 1.00 101.53 ? 674 LYS A NZ    1 
ATOM   5558 N  N     . ALA A 1 675 ? -33.104 -1.281  -24.936 1.00 83.90  ? 675 ALA A N     1 
ATOM   5559 C  CA    . ALA A 1 675 ? -32.983 -2.094  -23.734 1.00 83.61  ? 675 ALA A CA    1 
ATOM   5560 C  C     . ALA A 1 675 ? -33.903 -1.520  -22.664 1.00 88.21  ? 675 ALA A C     1 
ATOM   5561 O  O     . ALA A 1 675 ? -33.782 -0.345  -22.300 1.00 85.35  ? 675 ALA A O     1 
ATOM   5562 C  CB    . ALA A 1 675 ? -31.536 -2.134  -23.242 1.00 80.01  ? 675 ALA A CB    1 
ATOM   5563 N  N     . THR A 1 676 ? -34.820 -2.346  -22.166 1.00 87.25  ? 676 THR A N     1 
ATOM   5564 C  CA    . THR A 1 676 ? -35.840 -1.908  -21.216 1.00 90.23  ? 676 THR A CA    1 
ATOM   5565 C  C     . THR A 1 676 ? -35.434 -2.371  -19.820 1.00 85.54  ? 676 THR A C     1 
ATOM   5566 O  O     . THR A 1 676 ? -35.574 -3.548  -19.477 1.00 81.45  ? 676 THR A O     1 
ATOM   5567 C  CB    . THR A 1 676 ? -37.212 -2.450  -21.606 1.00 83.26  ? 676 THR A CB    1 
ATOM   5568 O  OG1   . THR A 1 676 ? -37.287 -3.843  -21.283 1.00 97.64  ? 676 THR A OG1   1 
ATOM   5569 C  CG2   . THR A 1 676 ? -37.436 -2.277  -23.099 1.00 80.45  ? 676 THR A CG2   1 
ATOM   5570 N  N     . GLY A 1 677 ? -34.929 -1.438  -19.016 1.00 80.81  ? 677 GLY A N     1 
ATOM   5571 C  CA    . GLY A 1 677 ? -34.573 -1.719  -17.648 1.00 73.51  ? 677 GLY A CA    1 
ATOM   5572 C  C     . GLY A 1 677 ? -35.773 -1.675  -16.725 1.00 74.18  ? 677 GLY A C     1 
ATOM   5573 O  O     . GLY A 1 677 ? -36.921 -1.534  -17.161 1.00 86.96  ? 677 GLY A O     1 
ATOM   5574 N  N     . PRO A 1 678 ? -35.523 -1.802  -15.418 1.00 72.08  ? 678 PRO A N     1 
ATOM   5575 C  CA    . PRO A 1 678 ? -36.646 -1.803  -14.460 1.00 71.38  ? 678 PRO A CA    1 
ATOM   5576 C  C     . PRO A 1 678 ? -37.448 -0.511  -14.471 1.00 69.12  ? 678 PRO A C     1 
ATOM   5577 O  O     . PRO A 1 678 ? -38.687 -0.549  -14.540 1.00 69.31  ? 678 PRO A O     1 
ATOM   5578 C  CB    . PRO A 1 678 ? -35.946 -2.039  -13.114 1.00 69.41  ? 678 PRO A CB    1 
ATOM   5579 C  CG    . PRO A 1 678 ? -34.649 -2.705  -13.470 1.00 68.79  ? 678 PRO A CG    1 
ATOM   5580 C  CD    . PRO A 1 678 ? -34.235 -2.101  -14.772 1.00 78.78  ? 678 PRO A CD    1 
ATOM   5581 N  N     . HIS A 1 679 ? -36.774 0.640   -14.395 1.00 71.85  ? 679 HIS A N     1 
ATOM   5582 C  CA    . HIS A 1 679 ? -37.487 1.908   -14.503 1.00 69.32  ? 679 HIS A CA    1 
ATOM   5583 C  C     . HIS A 1 679 ? -38.184 2.033   -15.850 1.00 69.95  ? 679 HIS A C     1 
ATOM   5584 O  O     . HIS A 1 679 ? -39.286 2.587   -15.929 1.00 71.02  ? 679 HIS A O     1 
ATOM   5585 C  CB    . HIS A 1 679 ? -36.529 3.080   -14.268 1.00 64.75  ? 679 HIS A CB    1 
ATOM   5586 C  CG    . HIS A 1 679 ? -35.585 3.341   -15.402 1.00 70.55  ? 679 HIS A CG    1 
ATOM   5587 N  ND1   . HIS A 1 679 ? -34.640 2.425   -15.811 1.00 69.88  ? 679 HIS A ND1   1 
ATOM   5588 C  CD2   . HIS A 1 679 ? -35.429 4.424   -16.201 1.00 71.35  ? 679 HIS A CD2   1 
ATOM   5589 C  CE1   . HIS A 1 679 ? -33.947 2.930   -16.817 1.00 72.73  ? 679 HIS A CE1   1 
ATOM   5590 N  NE2   . HIS A 1 679 ? -34.408 4.141   -17.075 1.00 69.20  ? 679 HIS A NE2   1 
ATOM   5591 N  N     . VAL A 1 680 ? -37.579 1.489   -16.909 1.00 69.91  ? 680 VAL A N     1 
ATOM   5592 C  CA    . VAL A 1 680 ? -38.232 1.464   -18.215 1.00 74.04  ? 680 VAL A CA    1 
ATOM   5593 C  C     . VAL A 1 680 ? -39.502 0.629   -18.170 1.00 72.26  ? 680 VAL A C     1 
ATOM   5594 O  O     . VAL A 1 680 ? -40.529 1.008   -18.742 1.00 78.82  ? 680 VAL A O     1 
ATOM   5595 C  CB    . VAL A 1 680 ? -37.266 0.938   -19.289 1.00 81.09  ? 680 VAL A CB    1 
ATOM   5596 C  CG1   . VAL A 1 680 ? -37.896 1.076   -20.660 1.00 82.70  ? 680 VAL A CG1   1 
ATOM   5597 C  CG2   . VAL A 1 680 ? -35.946 1.677   -19.215 1.00 78.21  ? 680 VAL A CG2   1 
ATOM   5598 N  N     . ALA A 1 681 ? -39.448 -0.532  -17.515 1.00 73.41  ? 681 ALA A N     1 
ATOM   5599 C  CA    . ALA A 1 681 ? -40.626 -1.390  -17.440 1.00 75.35  ? 681 ALA A CA    1 
ATOM   5600 C  C     . ALA A 1 681 ? -41.750 -0.713  -16.667 1.00 79.29  ? 681 ALA A C     1 
ATOM   5601 O  O     . ALA A 1 681 ? -42.920 -0.764  -17.074 1.00 82.19  ? 681 ALA A O     1 
ATOM   5602 C  CB    . ALA A 1 681 ? -40.256 -2.727  -16.800 1.00 64.70  ? 681 ALA A CB    1 
ATOM   5603 N  N     . VAL A 1 682 ? -41.410 -0.065  -15.550 1.00 74.17  ? 682 VAL A N     1 
ATOM   5604 C  CA    . VAL A 1 682 ? -42.418 0.662   -14.786 1.00 75.16  ? 682 VAL A CA    1 
ATOM   5605 C  C     . VAL A 1 682 ? -43.009 1.788   -15.626 1.00 79.32  ? 682 VAL A C     1 
ATOM   5606 O  O     . VAL A 1 682 ? -44.230 1.998   -15.640 1.00 81.20  ? 682 VAL A O     1 
ATOM   5607 C  CB    . VAL A 1 682 ? -41.816 1.188   -13.469 1.00 71.01  ? 682 VAL A CB    1 
ATOM   5608 C  CG1   . VAL A 1 682 ? -42.607 2.380   -12.960 1.00 70.11  ? 682 VAL A CG1   1 
ATOM   5609 C  CG2   . VAL A 1 682 ? -41.774 0.083   -12.425 1.00 70.46  ? 682 VAL A CG2   1 
ATOM   5610 N  N     . ALA A 1 683 ? -42.158 2.519   -16.354 1.00 76.81  ? 683 ALA A N     1 
ATOM   5611 C  CA    . ALA A 1 683 ? -42.644 3.609   -17.193 1.00 80.04  ? 683 ALA A CA    1 
ATOM   5612 C  C     . ALA A 1 683 ? -43.557 3.096   -18.298 1.00 87.59  ? 683 ALA A C     1 
ATOM   5613 O  O     . ALA A 1 683 ? -44.555 3.740   -18.637 1.00 94.04  ? 683 ALA A O     1 
ATOM   5614 C  CB    . ALA A 1 683 ? -41.467 4.376   -17.792 1.00 74.51  ? 683 ALA A CB    1 
ATOM   5615 N  N     . LYS A 1 684 ? -43.232 1.937   -18.873 1.00 86.33  ? 684 LYS A N     1 
ATOM   5616 C  CA    . LYS A 1 684 ? -44.052 1.396   -19.951 1.00 86.49  ? 684 LYS A CA    1 
ATOM   5617 C  C     . LYS A 1 684 ? -45.402 0.923   -19.432 1.00 94.56  ? 684 LYS A C     1 
ATOM   5618 O  O     . LYS A 1 684 ? -46.430 1.137   -20.084 1.00 92.94  ? 684 LYS A O     1 
ATOM   5619 C  CB    . LYS A 1 684 ? -43.311 0.265   -20.661 1.00 86.16  ? 684 LYS A CB    1 
ATOM   5620 C  CG    . LYS A 1 684 ? -42.164 0.755   -21.530 1.00 87.31  ? 684 LYS A CG    1 
ATOM   5621 C  CD    . LYS A 1 684 ? -41.958 -0.128  -22.747 1.00 91.43  ? 684 LYS A CD    1 
ATOM   5622 C  CE    . LYS A 1 684 ? -40.484 -0.428  -22.953 1.00 85.01  ? 684 LYS A CE    1 
ATOM   5623 N  NZ    . LYS A 1 684 ? -40.190 -0.855  -24.347 1.00 87.77  ? 684 LYS A NZ    1 
ATOM   5624 N  N     . ARG A 1 685 ? -45.428 0.295   -18.254 1.00 90.02  ? 685 ARG A N     1 
ATOM   5625 C  CA    . ARG A 1 685 ? -46.712 -0.063  -17.656 1.00 84.94  ? 685 ARG A CA    1 
ATOM   5626 C  C     . ARG A 1 685 ? -47.534 1.182   -17.334 1.00 91.07  ? 685 ARG A C     1 
ATOM   5627 O  O     . ARG A 1 685 ? -48.752 1.214   -17.566 1.00 88.11  ? 685 ARG A O     1 
ATOM   5628 C  CB    . ARG A 1 685 ? -46.495 -0.908  -16.403 1.00 77.45  ? 685 ARG A CB    1 
ATOM   5629 C  CG    . ARG A 1 685 ? -46.840 -2.375  -16.590 1.00 79.22  ? 685 ARG A CG    1 
ATOM   5630 C  CD    . ARG A 1 685 ? -45.642 -3.268  -16.330 1.00 83.95  ? 685 ARG A CD    1 
ATOM   5631 N  NE    . ARG A 1 685 ? -45.171 -3.156  -14.955 1.00 87.14  ? 685 ARG A NE    1 
ATOM   5632 C  CZ    . ARG A 1 685 ? -43.933 -3.428  -14.565 1.00 85.60  ? 685 ARG A CZ    1 
ATOM   5633 N  NH1   . ARG A 1 685 ? -43.014 -3.842  -15.421 1.00 78.34  ? 685 ARG A NH1   1 
ATOM   5634 N  NH2   . ARG A 1 685 ? -43.611 -3.284  -13.283 1.00 85.64  ? 685 ARG A NH2   1 
ATOM   5635 N  N     . LEU A 1 686 ? -46.882 2.224   -16.812 1.00 87.96  ? 686 LEU A N     1 
ATOM   5636 C  CA    . LEU A 1 686 ? -47.586 3.466   -16.506 1.00 89.66  ? 686 LEU A CA    1 
ATOM   5637 C  C     . LEU A 1 686 ? -48.172 4.091   -17.766 1.00 91.06  ? 686 LEU A C     1 
ATOM   5638 O  O     . LEU A 1 686 ? -49.316 4.562   -17.761 1.00 89.72  ? 686 LEU A O     1 
ATOM   5639 C  CB    . LEU A 1 686 ? -46.637 4.443   -15.813 1.00 85.53  ? 686 LEU A CB    1 
ATOM   5640 C  CG    . LEU A 1 686 ? -47.122 5.080   -14.511 1.00 84.92  ? 686 LEU A CG    1 
ATOM   5641 C  CD1   . LEU A 1 686 ? -47.487 4.010   -13.495 1.00 82.20  ? 686 LEU A CD1   1 
ATOM   5642 C  CD2   . LEU A 1 686 ? -46.061 6.014   -13.950 1.00 79.29  ? 686 LEU A CD2   1 
ATOM   5643 N  N     . ALA A 1 687 ? -47.403 4.104   -18.857 1.00 90.52  ? 687 ALA A N     1 
ATOM   5644 C  CA    . ALA A 1 687 ? -47.916 4.630   -20.117 1.00 90.50  ? 687 ALA A CA    1 
ATOM   5645 C  C     . ALA A 1 687 ? -49.056 3.769   -20.642 1.00 90.16  ? 687 ALA A C     1 
ATOM   5646 O  O     . ALA A 1 687 ? -50.001 4.281   -21.253 1.00 90.65  ? 687 ALA A O     1 
ATOM   5647 C  CB    . ALA A 1 687 ? -46.791 4.725   -21.147 1.00 81.06  ? 687 ALA A CB    1 
ATOM   5648 N  N     . ALA A 1 688 ? -48.981 2.453   -20.419 1.00 87.09  ? 688 ALA A N     1 
ATOM   5649 C  CA    . ALA A 1 688 ? -50.091 1.576   -20.777 1.00 96.49  ? 688 ALA A CA    1 
ATOM   5650 C  C     . ALA A 1 688 ? -51.337 1.898   -19.963 1.00 101.16 ? 688 ALA A C     1 
ATOM   5651 O  O     . ALA A 1 688 ? -52.459 1.642   -20.415 1.00 96.17  ? 688 ALA A O     1 
ATOM   5652 C  CB    . ALA A 1 688 ? -49.693 0.113   -20.585 1.00 91.95  ? 688 ALA A CB    1 
ATOM   5653 N  N     . ARG A 1 689 ? -51.162 2.451   -18.764 1.00 110.44 ? 689 ARG A N     1 
ATOM   5654 C  CA    . ARG A 1 689 ? -52.286 2.911   -17.958 1.00 99.47  ? 689 ARG A CA    1 
ATOM   5655 C  C     . ARG A 1 689 ? -52.725 4.332   -18.304 1.00 96.41  ? 689 ARG A C     1 
ATOM   5656 O  O     . ARG A 1 689 ? -53.576 4.890   -17.605 1.00 97.41  ? 689 ARG A O     1 
ATOM   5657 C  CB    . ARG A 1 689 ? -51.941 2.826   -16.470 1.00 101.44 ? 689 ARG A CB    1 
ATOM   5658 C  CG    . ARG A 1 689 ? -52.159 1.451   -15.865 1.00 106.27 ? 689 ARG A CG    1 
ATOM   5659 C  CD    . ARG A 1 689 ? -51.259 1.231   -14.664 1.00 109.25 ? 689 ARG A CD    1 
ATOM   5660 N  NE    . ARG A 1 689 ? -51.284 2.372   -13.758 1.00 107.53 ? 689 ARG A NE    1 
ATOM   5661 C  CZ    . ARG A 1 689 ? -51.284 2.277   -12.435 1.00 113.60 ? 689 ARG A CZ    1 
ATOM   5662 N  NH1   . ARG A 1 689 ? -51.258 1.103   -11.826 1.00 122.15 ? 689 ARG A NH1   1 
ATOM   5663 N  NH2   . ARG A 1 689 ? -51.311 3.389   -11.706 1.00 112.16 ? 689 ARG A NH2   1 
ATOM   5664 N  N     . GLY A 1 690 ? -52.175 4.926   -19.357 1.00 95.15  ? 690 GLY A N     1 
ATOM   5665 C  CA    . GLY A 1 690 ? -52.566 6.275   -19.730 1.00 88.88  ? 690 GLY A CA    1 
ATOM   5666 C  C     . GLY A 1 690 ? -52.032 7.353   -18.812 1.00 90.78  ? 690 GLY A C     1 
ATOM   5667 O  O     . GLY A 1 690 ? -52.774 8.273   -18.443 1.00 88.12  ? 690 GLY A O     1 
ATOM   5668 N  N     . VAL A 1 691 ? -50.762 7.259   -18.428 1.00 93.04  ? 691 VAL A N     1 
ATOM   5669 C  CA    . VAL A 1 691 ? -50.105 8.253   -17.586 1.00 84.41  ? 691 VAL A CA    1 
ATOM   5670 C  C     . VAL A 1 691 ? -49.069 8.980   -18.429 1.00 85.68  ? 691 VAL A C     1 
ATOM   5671 O  O     . VAL A 1 691 ? -48.337 8.353   -19.205 1.00 84.86  ? 691 VAL A O     1 
ATOM   5672 C  CB    . VAL A 1 691 ? -49.458 7.605   -16.346 1.00 80.97  ? 691 VAL A CB    1 
ATOM   5673 C  CG1   . VAL A 1 691 ? -48.838 8.665   -15.448 1.00 81.30  ? 691 VAL A CG1   1 
ATOM   5674 C  CG2   . VAL A 1 691 ? -50.486 6.786   -15.581 1.00 89.66  ? 691 VAL A CG2   1 
ATOM   5675 N  N     . LYS A 1 692 ? -49.014 10.303  -18.284 1.00 87.80  ? 692 LYS A N     1 
ATOM   5676 C  CA    . LYS A 1 692 ? -48.083 11.109  -19.064 1.00 89.04  ? 692 LYS A CA    1 
ATOM   5677 C  C     . LYS A 1 692 ? -46.649 10.767  -18.679 1.00 91.58  ? 692 LYS A C     1 
ATOM   5678 O  O     . LYS A 1 692 ? -46.261 10.897  -17.513 1.00 96.43  ? 692 LYS A O     1 
ATOM   5679 C  CB    . LYS A 1 692 ? -48.354 12.596  -18.852 1.00 89.86  ? 692 LYS A CB    1 
ATOM   5680 C  CG    . LYS A 1 692 ? -48.032 13.452  -20.068 1.00 97.21  ? 692 LYS A CG    1 
ATOM   5681 C  CD    . LYS A 1 692 ? -47.317 14.733  -19.674 1.00 95.25  ? 692 LYS A CD    1 
ATOM   5682 C  CE    . LYS A 1 692 ? -47.407 15.776  -20.777 1.00 96.59  ? 692 LYS A CE    1 
ATOM   5683 N  NZ    . LYS A 1 692 ? -47.322 17.163  -20.241 1.00 80.57  ? 692 LYS A NZ    1 
ATOM   5684 N  N     . ILE A 1 693 ? -45.866 10.331  -19.662 1.00 93.26  ? 693 ILE A N     1 
ATOM   5685 C  CA    . ILE A 1 693 ? -44.471 9.955   -19.465 1.00 94.93  ? 693 ILE A CA    1 
ATOM   5686 C  C     . ILE A 1 693 ? -43.663 10.586  -20.591 1.00 95.73  ? 693 ILE A C     1 
ATOM   5687 O  O     . ILE A 1 693 ? -43.942 10.342  -21.771 1.00 98.46  ? 693 ILE A O     1 
ATOM   5688 C  CB    . ILE A 1 693 ? -44.289 8.428   -19.436 1.00 93.23  ? 693 ILE A CB    1 
ATOM   5689 C  CG1   . ILE A 1 693 ? -44.499 7.895   -18.017 1.00 84.62  ? 693 ILE A CG1   1 
ATOM   5690 C  CG2   . ILE A 1 693 ? -42.920 8.035   -19.951 1.00 89.62  ? 693 ILE A CG2   1 
ATOM   5691 C  CD1   . ILE A 1 693 ? -43.496 8.423   -17.016 1.00 84.33  ? 693 ILE A CD1   1 
ATOM   5692 N  N     . ARG A 1 694 ? -42.681 11.401  -20.232 1.00 92.93  ? 694 ARG A N     1 
ATOM   5693 C  CA    . ARG A 1 694 ? -41.930 12.202  -21.184 1.00 102.87 ? 694 ARG A CA    1 
ATOM   5694 C  C     . ARG A 1 694 ? -40.467 12.214  -20.774 1.00 98.85  ? 694 ARG A C     1 
ATOM   5695 O  O     . ARG A 1 694 ? -40.140 11.946  -19.613 1.00 91.53  ? 694 ARG A O     1 
ATOM   5696 C  CB    . ARG A 1 694 ? -42.476 13.637  -21.246 1.00 104.64 ? 694 ARG A CB    1 
ATOM   5697 C  CG    . ARG A 1 694 ? -43.335 13.932  -22.470 1.00 117.81 ? 694 ARG A CG    1 
ATOM   5698 C  CD    . ARG A 1 694 ? -42.524 14.594  -23.574 1.00 126.10 ? 694 ARG A CD    1 
ATOM   5699 N  NE    . ARG A 1 694 ? -43.363 15.098  -24.655 1.00 141.13 ? 694 ARG A NE    1 
ATOM   5700 C  CZ    . ARG A 1 694 ? -43.781 16.352  -24.757 1.00 139.00 ? 694 ARG A CZ    1 
ATOM   5701 N  NH1   . ARG A 1 694 ? -43.458 17.264  -23.854 1.00 127.20 ? 694 ARG A NH1   1 
ATOM   5702 N  NH2   . ARG A 1 694 ? -44.536 16.702  -25.795 1.00 130.83 ? 694 ARG A NH2   1 
ATOM   5703 N  N     . PRO A 1 695 ? -39.553 12.497  -21.718 1.00 90.10  ? 695 PRO A N     1 
ATOM   5704 C  CA    . PRO A 1 695 ? -38.135 12.633  -21.354 1.00 81.00  ? 695 PRO A CA    1 
ATOM   5705 C  C     . PRO A 1 695 ? -37.901 13.676  -20.274 1.00 87.60  ? 695 PRO A C     1 
ATOM   5706 O  O     . PRO A 1 695 ? -37.964 14.882  -20.535 1.00 91.97  ? 695 PRO A O     1 
ATOM   5707 C  CB    . PRO A 1 695 ? -37.472 13.042  -22.675 1.00 76.70  ? 695 PRO A CB    1 
ATOM   5708 C  CG    . PRO A 1 695 ? -38.350 12.471  -23.724 1.00 91.76  ? 695 PRO A CG    1 
ATOM   5709 C  CD    . PRO A 1 695 ? -39.751 12.506  -23.179 1.00 95.79  ? 695 PRO A CD    1 
ATOM   5710 N  N     . GLY A 1 696 ? -37.633 13.219  -19.054 1.00 83.80  ? 696 GLY A N     1 
ATOM   5711 C  CA    . GLY A 1 696 ? -37.381 14.123  -17.950 1.00 79.07  ? 696 GLY A CA    1 
ATOM   5712 C  C     . GLY A 1 696 ? -37.951 13.639  -16.633 1.00 78.99  ? 696 GLY A C     1 
ATOM   5713 O  O     . GLY A 1 696 ? -37.383 13.908  -15.570 1.00 81.10  ? 696 GLY A O     1 
ATOM   5714 N  N     . THR A 1 697 ? -39.072 12.924  -16.688 1.00 75.81  ? 697 THR A N     1 
ATOM   5715 C  CA    . THR A 1 697 ? -39.707 12.440  -15.470 1.00 75.44  ? 697 THR A CA    1 
ATOM   5716 C  C     . THR A 1 697 ? -38.838 11.384  -14.794 1.00 78.80  ? 697 THR A C     1 
ATOM   5717 O  O     . THR A 1 697 ? -38.075 10.662  -15.441 1.00 71.66  ? 697 THR A O     1 
ATOM   5718 C  CB    . THR A 1 697 ? -41.092 11.866  -15.773 1.00 76.50  ? 697 THR A CB    1 
ATOM   5719 O  OG1   . THR A 1 697 ? -40.978 10.475  -16.096 1.00 71.83  ? 697 THR A OG1   1 
ATOM   5720 C  CG2   . THR A 1 697 ? -41.735 12.603  -16.939 1.00 82.79  ? 697 THR A CG2   1 
ATOM   5721 N  N     . VAL A 1 698 ? -38.961 11.302  -13.472 1.00 72.55  ? 698 VAL A N     1 
ATOM   5722 C  CA    . VAL A 1 698 ? -38.155 10.406  -12.652 1.00 61.73  ? 698 VAL A CA    1 
ATOM   5723 C  C     . VAL A 1 698 ? -39.066 9.311   -12.114 1.00 66.23  ? 698 VAL A C     1 
ATOM   5724 O  O     . VAL A 1 698 ? -40.048 9.595   -11.416 1.00 66.78  ? 698 VAL A O     1 
ATOM   5725 C  CB    . VAL A 1 698 ? -37.455 11.162  -11.510 1.00 67.50  ? 698 VAL A CB    1 
ATOM   5726 C  CG1   . VAL A 1 698 ? -37.172 10.233  -10.334 1.00 67.76  ? 698 VAL A CG1   1 
ATOM   5727 C  CG2   . VAL A 1 698 ? -36.170 11.811  -12.009 1.00 67.82  ? 698 VAL A CG2   1 
ATOM   5728 N  N     . ILE A 1 699 ? -38.752 8.065   -12.456 1.00 65.70  ? 699 ILE A N     1 
ATOM   5729 C  CA    . ILE A 1 699 ? -39.461 6.901   -11.943 1.00 62.33  ? 699 ILE A CA    1 
ATOM   5730 C  C     . ILE A 1 699 ? -38.839 6.502   -10.613 1.00 65.99  ? 699 ILE A C     1 
ATOM   5731 O  O     . ILE A 1 699 ? -37.624 6.289   -10.521 1.00 67.61  ? 699 ILE A O     1 
ATOM   5732 C  CB    . ILE A 1 699 ? -39.397 5.739   -12.947 1.00 63.16  ? 699 ILE A CB    1 
ATOM   5733 C  CG1   . ILE A 1 699 ? -40.287 6.030   -14.153 1.00 67.25  ? 699 ILE A CG1   1 
ATOM   5734 C  CG2   . ILE A 1 699 ? -39.772 4.425   -12.279 1.00 61.73  ? 699 ILE A CG2   1 
ATOM   5735 C  CD1   . ILE A 1 699 ? -39.511 6.186   -15.430 1.00 72.89  ? 699 ILE A CD1   1 
ATOM   5736 N  N     . SER A 1 700 ? -39.672 6.392   -9.584  1.00 65.22  ? 700 SER A N     1 
ATOM   5737 C  CA    . SER A 1 700 ? -39.243 5.972   -8.254  1.00 66.79  ? 700 SER A CA    1 
ATOM   5738 C  C     . SER A 1 700 ? -39.944 4.658   -7.938  1.00 64.49  ? 700 SER A C     1 
ATOM   5739 O  O     . SER A 1 700 ? -41.164 4.634   -7.745  1.00 71.36  ? 700 SER A O     1 
ATOM   5740 C  CB    . SER A 1 700 ? -39.568 7.044   -7.216  1.00 65.81  ? 700 SER A CB    1 
ATOM   5741 O  OG    . SER A 1 700 ? -39.155 8.323   -7.665  1.00 58.81  ? 700 SER A OG    1 
ATOM   5742 N  N     . TYR A 1 701 ? -39.182 3.567   -7.892  1.00 60.28  ? 701 TYR A N     1 
ATOM   5743 C  CA    . TYR A 1 701 ? -39.775 2.241   -7.778  1.00 64.75  ? 701 TYR A CA    1 
ATOM   5744 C  C     . TYR A 1 701 ? -39.166 1.455   -6.624  1.00 66.24  ? 701 TYR A C     1 
ATOM   5745 O  O     . TYR A 1 701 ? -38.110 1.799   -6.084  1.00 66.90  ? 701 TYR A O     1 
ATOM   5746 C  CB    . TYR A 1 701 ? -39.632 1.439   -9.085  1.00 63.73  ? 701 TYR A CB    1 
ATOM   5747 C  CG    . TYR A 1 701 ? -38.206 1.136   -9.502  1.00 64.95  ? 701 TYR A CG    1 
ATOM   5748 C  CD1   . TYR A 1 701 ? -37.551 -0.000  -9.041  1.00 63.12  ? 701 TYR A CD1   1 
ATOM   5749 C  CD2   . TYR A 1 701 ? -37.523 1.977   -10.371 1.00 64.00  ? 701 TYR A CD2   1 
ATOM   5750 C  CE1   . TYR A 1 701 ? -36.252 -0.283  -9.423  1.00 64.31  ? 701 TYR A CE1   1 
ATOM   5751 C  CE2   . TYR A 1 701 ? -36.222 1.701   -10.759 1.00 68.66  ? 701 TYR A CE2   1 
ATOM   5752 C  CZ    . TYR A 1 701 ? -35.593 0.570   -10.282 1.00 66.39  ? 701 TYR A CZ    1 
ATOM   5753 O  OH    . TYR A 1 701 ? -34.301 0.289   -10.665 1.00 63.15  ? 701 TYR A OH    1 
ATOM   5754 N  N     . ILE A 1 702 ? -39.874 0.386   -6.259  1.00 64.39  ? 702 ILE A N     1 
ATOM   5755 C  CA    . ILE A 1 702 ? -39.422 -0.609  -5.294  1.00 65.94  ? 702 ILE A CA    1 
ATOM   5756 C  C     . ILE A 1 702 ? -39.493 -1.980  -5.952  1.00 67.24  ? 702 ILE A C     1 
ATOM   5757 O  O     . ILE A 1 702 ? -40.444 -2.280  -6.687  1.00 70.64  ? 702 ILE A O     1 
ATOM   5758 C  CB    . ILE A 1 702 ? -40.259 -0.587  -3.996  1.00 66.20  ? 702 ILE A CB    1 
ATOM   5759 C  CG1   . ILE A 1 702 ? -39.945 0.655   -3.162  1.00 84.44  ? 702 ILE A CG1   1 
ATOM   5760 C  CG2   . ILE A 1 702 ? -40.028 -1.847  -3.166  1.00 66.97  ? 702 ILE A CG2   1 
ATOM   5761 C  CD1   . ILE A 1 702 ? -40.246 0.474   -1.681  1.00 73.32  ? 702 ILE A CD1   1 
ATOM   5762 N  N     . VAL A 1 703 ? -38.476 -2.802  -5.694  1.00 61.62  ? 703 VAL A N     1 
ATOM   5763 C  CA    . VAL A 1 703 ? -38.444 -4.190  -6.138  1.00 67.11  ? 703 VAL A CA    1 
ATOM   5764 C  C     . VAL A 1 703 ? -39.140 -5.049  -5.090  1.00 67.30  ? 703 VAL A C     1 
ATOM   5765 O  O     . VAL A 1 703 ? -38.834 -4.957  -3.895  1.00 70.26  ? 703 VAL A O     1 
ATOM   5766 C  CB    . VAL A 1 703 ? -36.996 -4.659  -6.364  1.00 65.08  ? 703 VAL A CB    1 
ATOM   5767 C  CG1   . VAL A 1 703 ? -36.949 -6.166  -6.587  1.00 68.16  ? 703 VAL A CG1   1 
ATOM   5768 C  CG2   . VAL A 1 703 ? -36.372 -3.916  -7.534  1.00 62.22  ? 703 VAL A CG2   1 
ATOM   5769 N  N     . LEU A 1 704 ? -40.073 -5.884  -5.534  1.00 67.86  ? 704 LEU A N     1 
ATOM   5770 C  CA    . LEU A 1 704 ? -40.863 -6.729  -4.653  1.00 70.20  ? 704 LEU A CA    1 
ATOM   5771 C  C     . LEU A 1 704 ? -40.389 -8.173  -4.748  1.00 71.17  ? 704 LEU A C     1 
ATOM   5772 O  O     . LEU A 1 704 ? -39.762 -8.584  -5.728  1.00 73.90  ? 704 LEU A O     1 
ATOM   5773 C  CB    . LEU A 1 704 ? -42.352 -6.649  -5.008  1.00 68.39  ? 704 LEU A CB    1 
ATOM   5774 C  CG    . LEU A 1 704 ? -43.146 -5.427  -4.542  1.00 69.22  ? 704 LEU A CG    1 
ATOM   5775 C  CD1   . LEU A 1 704 ? -42.822 -5.056  -3.112  1.00 77.41  ? 704 LEU A CD1   1 
ATOM   5776 C  CD2   . LEU A 1 704 ? -42.847 -4.268  -5.455  1.00 72.11  ? 704 LEU A CD2   1 
ATOM   5777 N  N     . LYS A 1 705 ? -40.700 -8.942  -3.708  1.00 73.61  ? 705 LYS A N     1 
ATOM   5778 C  CA    . LYS A 1 705 ? -40.418 -10.371 -3.709  1.00 75.14  ? 705 LYS A CA    1 
ATOM   5779 C  C     . LYS A 1 705 ? -41.157 -11.039 -4.859  1.00 89.36  ? 705 LYS A C     1 
ATOM   5780 O  O     . LYS A 1 705 ? -42.386 -10.948 -4.950  1.00 88.41  ? 705 LYS A O     1 
ATOM   5781 C  CB    . LYS A 1 705 ? -40.841 -10.981 -2.375  1.00 73.36  ? 705 LYS A CB    1 
ATOM   5782 C  CG    . LYS A 1 705 ? -39.916 -12.047 -1.833  1.00 78.67  ? 705 LYS A CG    1 
ATOM   5783 C  CD    . LYS A 1 705 ? -40.634 -12.901 -0.800  1.00 81.18  ? 705 LYS A CD    1 
ATOM   5784 C  CE    . LYS A 1 705 ? -39.663 -13.651 0.093   1.00 79.84  ? 705 LYS A CE    1 
ATOM   5785 N  NZ    . LYS A 1 705 ? -40.047 -13.539 1.526   1.00 85.50  ? 705 LYS A NZ    1 
ATOM   5786 N  N     . GLY A 1 706 ? -40.418 -11.710 -5.743  1.00 101.18 ? 706 GLY A N     1 
ATOM   5787 C  CA    . GLY A 1 706 ? -41.075 -12.323 -6.882  1.00 117.98 ? 706 GLY A CA    1 
ATOM   5788 C  C     . GLY A 1 706 ? -40.209 -13.086 -7.865  1.00 126.95 ? 706 GLY A C     1 
ATOM   5789 O  O     . GLY A 1 706 ? -39.222 -13.734 -7.492  1.00 119.95 ? 706 GLY A O     1 
ATOM   5790 N  N     . SER A 1 707 ? -40.579 -12.983 -9.143  1.00 141.99 ? 707 SER A N     1 
ATOM   5791 C  CA    . SER A 1 707 ? -40.149 -13.909 -10.190 1.00 125.07 ? 707 SER A CA    1 
ATOM   5792 C  C     . SER A 1 707 ? -39.061 -13.263 -11.045 1.00 115.51 ? 707 SER A C     1 
ATOM   5793 O  O     . SER A 1 707 ? -39.341 -12.612 -12.055 1.00 111.74 ? 707 SER A O     1 
ATOM   5794 C  CB    . SER A 1 707 ? -41.343 -14.324 -11.046 1.00 119.34 ? 707 SER A CB    1 
ATOM   5795 O  OG    . SER A 1 707 ? -42.016 -13.192 -11.571 1.00 111.95 ? 707 SER A OG    1 
ATOM   5796 N  N     . GLY A 1 708 ? -37.814 -13.463 -10.637 1.00 111.89 ? 708 GLY A N     1 
ATOM   5797 C  CA    . GLY A 1 708 ? -36.675 -13.164 -11.491 1.00 110.67 ? 708 GLY A CA    1 
ATOM   5798 C  C     . GLY A 1 708 ? -36.605 -11.712 -11.914 1.00 113.29 ? 708 GLY A C     1 
ATOM   5799 O  O     . GLY A 1 708 ? -36.432 -10.812 -11.082 1.00 128.50 ? 708 GLY A O     1 
ATOM   5800 N  N     . ARG A 1 709 ? -36.736 -11.495 -13.230 1.00 95.57  ? 709 ARG A N     1 
ATOM   5801 C  CA    . ARG A 1 709 ? -36.615 -10.198 -13.896 1.00 84.96  ? 709 ARG A CA    1 
ATOM   5802 C  C     . ARG A 1 709 ? -37.059 -9.046  -13.006 1.00 84.86  ? 709 ARG A C     1 
ATOM   5803 O  O     . ARG A 1 709 ? -38.249 -8.919  -12.699 1.00 86.45  ? 709 ARG A O     1 
ATOM   5804 C  CB    . ARG A 1 709 ? -37.427 -10.193 -15.192 1.00 82.25  ? 709 ARG A CB    1 
ATOM   5805 C  CG    . ARG A 1 709 ? -36.602 -10.013 -16.459 1.00 79.72  ? 709 ARG A CG    1 
ATOM   5806 C  CD    . ARG A 1 709 ? -37.047 -10.967 -17.560 1.00 82.41  ? 709 ARG A CD    1 
ATOM   5807 N  NE    . ARG A 1 709 ? -37.379 -10.267 -18.795 1.00 89.71  ? 709 ARG A NE    1 
ATOM   5808 C  CZ    . ARG A 1 709 ? -38.543 -9.677  -19.035 1.00 84.32  ? 709 ARG A CZ    1 
ATOM   5809 N  NH1   . ARG A 1 709 ? -39.520 -9.688  -18.144 1.00 82.62  ? 709 ARG A NH1   1 
ATOM   5810 N  NH2   . ARG A 1 709 ? -38.733 -9.067  -20.202 1.00 84.53  ? 709 ARG A NH2   1 
ATOM   5811 N  N     . ILE A 1 710 ? -36.102 -8.216  -12.580 1.00 79.37  ? 710 ILE A N     1 
ATOM   5812 C  CA    . ILE A 1 710 ? -36.387 -7.191  -11.578 1.00 79.62  ? 710 ILE A CA    1 
ATOM   5813 C  C     . ILE A 1 710 ? -37.504 -6.274  -12.060 1.00 75.60  ? 710 ILE A C     1 
ATOM   5814 O  O     . ILE A 1 710 ? -38.423 -5.936  -11.301 1.00 79.21  ? 710 ILE A O     1 
ATOM   5815 C  CB    . ILE A 1 710 ? -35.106 -6.402  -11.238 1.00 75.92  ? 710 ILE A CB    1 
ATOM   5816 C  CG1   . ILE A 1 710 ? -34.377 -7.023  -10.044 1.00 77.66  ? 710 ILE A CG1   1 
ATOM   5817 C  CG2   . ILE A 1 710 ? -35.432 -4.957  -10.909 1.00 69.03  ? 710 ILE A CG2   1 
ATOM   5818 C  CD1   . ILE A 1 710 ? -33.941 -8.450  -10.257 1.00 77.76  ? 710 ILE A CD1   1 
ATOM   5819 N  N     . GLY A 1 711 ? -37.463 -5.884  -13.337 1.00 72.38  ? 711 GLY A N     1 
ATOM   5820 C  CA    . GLY A 1 711 ? -38.504 -5.041  -13.897 1.00 74.21  ? 711 GLY A CA    1 
ATOM   5821 C  C     . GLY A 1 711 ? -39.891 -5.644  -13.821 1.00 74.06  ? 711 GLY A C     1 
ATOM   5822 O  O     . GLY A 1 711 ? -40.881 -4.906  -13.848 1.00 75.35  ? 711 GLY A O     1 
ATOM   5823 N  N     . ASP A 1 712 ? -39.987 -6.972  -13.724 1.00 78.04  ? 712 ASP A N     1 
ATOM   5824 C  CA    . ASP A 1 712 ? -41.289 -7.610  -13.573 1.00 80.57  ? 712 ASP A CA    1 
ATOM   5825 C  C     . ASP A 1 712 ? -41.848 -7.445  -12.166 1.00 80.56  ? 712 ASP A C     1 
ATOM   5826 O  O     . ASP A 1 712 ? -43.072 -7.411  -11.993 1.00 79.94  ? 712 ASP A O     1 
ATOM   5827 C  CB    . ASP A 1 712 ? -41.197 -9.099  -13.921 1.00 76.94  ? 712 ASP A CB    1 
ATOM   5828 C  CG    . ASP A 1 712 ? -41.025 -9.345  -15.409 1.00 71.99  ? 712 ASP A CG    1 
ATOM   5829 O  OD1   . ASP A 1 712 ? -41.313 -8.427  -16.205 1.00 75.15  ? 712 ASP A OD1   1 
ATOM   5830 O  OD2   . ASP A 1 712 ? -40.611 -10.462 -15.783 1.00 80.50  ? 712 ASP A OD2   1 
ATOM   5831 N  N     . ARG A 1 713 ? -40.984 -7.340  -11.154 1.00 76.09  ? 713 ARG A N     1 
ATOM   5832 C  CA    . ARG A 1 713 ? -41.424 -7.272  -9.766  1.00 73.33  ? 713 ARG A CA    1 
ATOM   5833 C  C     . ARG A 1 713 ? -41.237 -5.886  -9.157  1.00 72.61  ? 713 ARG A C     1 
ATOM   5834 O  O     . ARG A 1 713 ? -41.267 -5.744  -7.931  1.00 74.83  ? 713 ARG A O     1 
ATOM   5835 C  CB    . ARG A 1 713 ? -40.697 -8.321  -8.923  1.00 78.95  ? 713 ARG A CB    1 
ATOM   5836 C  CG    . ARG A 1 713 ? -39.345 -8.761  -9.470  1.00 88.31  ? 713 ARG A CG    1 
ATOM   5837 C  CD    . ARG A 1 713 ? -38.586 -9.554  -8.417  1.00 92.44  ? 713 ARG A CD    1 
ATOM   5838 N  NE    . ARG A 1 713 ? -37.332 -10.117 -8.902  1.00 96.73  ? 713 ARG A NE    1 
ATOM   5839 C  CZ    . ARG A 1 713 ? -36.293 -10.392 -8.126  1.00 96.60  ? 713 ARG A CZ    1 
ATOM   5840 N  NH1   . ARG A 1 713 ? -36.304 -10.115 -6.834  1.00 87.93  ? 713 ARG A NH1   1 
ATOM   5841 N  NH2   . ARG A 1 713 ? -35.214 -10.959 -8.660  1.00 107.25 ? 713 ARG A NH2   1 
ATOM   5842 N  N     . ALA A 1 714 ? -41.054 -4.861  -9.984  1.00 67.47  ? 714 ALA A N     1 
ATOM   5843 C  CA    . ALA A 1 714 ? -40.845 -3.498  -9.518  1.00 73.49  ? 714 ALA A CA    1 
ATOM   5844 C  C     . ALA A 1 714 ? -42.099 -2.673  -9.772  1.00 76.36  ? 714 ALA A C     1 
ATOM   5845 O  O     . ALA A 1 714 ? -42.661 -2.712  -10.872 1.00 74.18  ? 714 ALA A O     1 
ATOM   5846 C  CB    . ALA A 1 714 ? -39.641 -2.858  -10.214 1.00 68.63  ? 714 ALA A CB    1 
ATOM   5847 N  N     . ILE A 1 715 ? -42.532 -1.931  -8.758  1.00 77.91  ? 715 ILE A N     1 
ATOM   5848 C  CA    . ILE A 1 715 ? -43.696 -1.055  -8.908  1.00 74.14  ? 715 ILE A CA    1 
ATOM   5849 C  C     . ILE A 1 715 ? -43.351 0.340   -8.401  1.00 73.25  ? 715 ILE A C     1 
ATOM   5850 O  O     . ILE A 1 715 ? -42.460 0.485   -7.551  1.00 67.75  ? 715 ILE A O     1 
ATOM   5851 C  CB    . ILE A 1 715 ? -44.929 -1.606  -8.171  1.00 75.89  ? 715 ILE A CB    1 
ATOM   5852 C  CG1   . ILE A 1 715 ? -44.669 -1.674  -6.666  1.00 75.70  ? 715 ILE A CG1   1 
ATOM   5853 C  CG2   . ILE A 1 715 ? -45.327 -2.968  -8.720  1.00 76.44  ? 715 ILE A CG2   1 
ATOM   5854 C  CD1   . ILE A 1 715 ? -45.926 -1.670  -5.820  1.00 78.18  ? 715 ILE A CD1   1 
ATOM   5855 N  N     . PRO A 1 716 ? -44.024 1.388   -8.880  1.00 79.05  ? 716 PRO A N     1 
ATOM   5856 C  CA    . PRO A 1 716 ? -43.800 2.724   -8.316  1.00 75.24  ? 716 PRO A CA    1 
ATOM   5857 C  C     . PRO A 1 716 ? -44.128 2.748   -6.831  1.00 76.13  ? 716 PRO A C     1 
ATOM   5858 O  O     . PRO A 1 716 ? -45.029 2.050   -6.360  1.00 78.26  ? 716 PRO A O     1 
ATOM   5859 C  CB    . PRO A 1 716 ? -44.755 3.618   -9.116  1.00 76.81  ? 716 PRO A CB    1 
ATOM   5860 C  CG    . PRO A 1 716 ? -45.076 2.844   -10.351 1.00 77.01  ? 716 PRO A CG    1 
ATOM   5861 C  CD    . PRO A 1 716 ? -45.011 1.402   -9.973  1.00 75.91  ? 716 PRO A CD    1 
ATOM   5862 N  N     . PHE A 1 717 ? -43.378 3.565   -6.088  1.00 77.25  ? 717 PHE A N     1 
ATOM   5863 C  CA    . PHE A 1 717 ? -43.508 3.560   -4.636  1.00 79.58  ? 717 PHE A CA    1 
ATOM   5864 C  C     . PHE A 1 717 ? -44.855 4.091   -4.164  1.00 77.43  ? 717 PHE A C     1 
ATOM   5865 O  O     . PHE A 1 717 ? -45.292 3.739   -3.063  1.00 77.00  ? 717 PHE A O     1 
ATOM   5866 C  CB    . PHE A 1 717 ? -42.380 4.369   -3.997  1.00 72.56  ? 717 PHE A CB    1 
ATOM   5867 C  CG    . PHE A 1 717 ? -42.374 4.305   -2.499  1.00 71.56  ? 717 PHE A CG    1 
ATOM   5868 C  CD1   . PHE A 1 717 ? -42.445 3.087   -1.849  1.00 70.77  ? 717 PHE A CD1   1 
ATOM   5869 C  CD2   . PHE A 1 717 ? -42.303 5.460   -1.740  1.00 74.25  ? 717 PHE A CD2   1 
ATOM   5870 C  CE1   . PHE A 1 717 ? -42.440 3.016   -0.470  1.00 74.91  ? 717 PHE A CE1   1 
ATOM   5871 C  CE2   . PHE A 1 717 ? -42.297 5.397   -0.359  1.00 78.74  ? 717 PHE A CE2   1 
ATOM   5872 C  CZ    . PHE A 1 717 ? -42.366 4.173   0.276   1.00 75.36  ? 717 PHE A CZ    1 
ATOM   5873 N  N     . ASP A 1 718 ? -45.522 4.926   -4.963  1.00 83.37  ? 718 ASP A N     1 
ATOM   5874 C  CA    . ASP A 1 718 ? -46.838 5.416   -4.562  1.00 89.07  ? 718 ASP A CA    1 
ATOM   5875 C  C     . ASP A 1 718 ? -47.869 4.296   -4.509  1.00 82.18  ? 718 ASP A C     1 
ATOM   5876 O  O     . ASP A 1 718 ? -48.844 4.391   -3.755  1.00 88.52  ? 718 ASP A O     1 
ATOM   5877 C  CB    . ASP A 1 718 ? -47.301 6.533   -5.501  1.00 89.54  ? 718 ASP A CB    1 
ATOM   5878 C  CG    . ASP A 1 718 ? -47.334 6.110   -6.964  1.00 103.88 ? 718 ASP A CG    1 
ATOM   5879 O  OD1   . ASP A 1 718 ? -47.371 7.017   -7.824  1.00 110.40 ? 718 ASP A OD1   1 
ATOM   5880 O  OD2   . ASP A 1 718 ? -47.311 4.899   -7.266  1.00 108.03 ? 718 ASP A OD2   1 
ATOM   5881 N  N     . GLU A 1 719 ? -47.677 3.242   -5.300  1.00 85.02  ? 719 GLU A N     1 
ATOM   5882 C  CA    . GLU A 1 719 ? -48.579 2.100   -5.332  1.00 80.12  ? 719 GLU A CA    1 
ATOM   5883 C  C     . GLU A 1 719 ? -48.215 1.030   -4.312  1.00 81.08  ? 719 GLU A C     1 
ATOM   5884 O  O     . GLU A 1 719 ? -48.824 -0.044  -4.318  1.00 87.06  ? 719 GLU A O     1 
ATOM   5885 C  CB    . GLU A 1 719 ? -48.602 1.483   -6.734  1.00 78.49  ? 719 GLU A CB    1 
ATOM   5886 C  CG    . GLU A 1 719 ? -49.126 2.405   -7.824  1.00 88.15  ? 719 GLU A CG    1 
ATOM   5887 C  CD    . GLU A 1 719 ? -48.741 1.941   -9.217  1.00 93.90  ? 719 GLU A CD    1 
ATOM   5888 O  OE1   . GLU A 1 719 ? -48.557 0.720   -9.412  1.00 94.64  ? 719 GLU A OE1   1 
ATOM   5889 O  OE2   . GLU A 1 719 ? -48.615 2.798   -10.115 1.00 93.32  ? 719 GLU A OE2   1 
ATOM   5890 N  N     . PHE A 1 720 ? -47.239 1.290   -3.445  1.00 83.47  ? 720 PHE A N     1 
ATOM   5891 C  CA    . PHE A 1 720 ? -46.813 0.302   -2.461  1.00 86.67  ? 720 PHE A CA    1 
ATOM   5892 C  C     . PHE A 1 720 ? -47.770 0.312   -1.275  1.00 97.14  ? 720 PHE A C     1 
ATOM   5893 O  O     . PHE A 1 720 ? -47.868 1.313   -0.556  1.00 98.56  ? 720 PHE A O     1 
ATOM   5894 C  CB    . PHE A 1 720 ? -45.384 0.582   -2.002  1.00 80.65  ? 720 PHE A CB    1 
ATOM   5895 C  CG    . PHE A 1 720 ? -44.877 -0.385  -0.966  1.00 82.62  ? 720 PHE A CG    1 
ATOM   5896 C  CD1   . PHE A 1 720 ? -44.337 -1.604  -1.343  1.00 82.29  ? 720 PHE A CD1   1 
ATOM   5897 C  CD2   . PHE A 1 720 ? -44.939 -0.075  0.383   1.00 83.84  ? 720 PHE A CD2   1 
ATOM   5898 C  CE1   . PHE A 1 720 ? -43.869 -2.495  -0.394  1.00 81.45  ? 720 PHE A CE1   1 
ATOM   5899 C  CE2   . PHE A 1 720 ? -44.475 -0.963  1.336   1.00 82.25  ? 720 PHE A CE2   1 
ATOM   5900 C  CZ    . PHE A 1 720 ? -43.939 -2.175  0.947   1.00 79.19  ? 720 PHE A CZ    1 
ATOM   5901 N  N     . ASP A 1 721 ? -48.474 -0.798  -1.075  1.00 108.12 ? 721 ASP A N     1 
ATOM   5902 C  CA    . ASP A 1 721 ? -49.340 -0.984  0.084   1.00 127.66 ? 721 ASP A CA    1 
ATOM   5903 C  C     . ASP A 1 721 ? -48.698 -1.998  1.017   1.00 117.95 ? 721 ASP A C     1 
ATOM   5904 O  O     . ASP A 1 721 ? -48.621 -3.186  0.665   1.00 116.20 ? 721 ASP A O     1 
ATOM   5905 C  CB    . ASP A 1 721 ? -50.730 -1.460  -0.340  1.00 134.58 ? 721 ASP A CB    1 
ATOM   5906 C  CG    . ASP A 1 721 ? -51.533 -0.378  -1.030  1.00 151.52 ? 721 ASP A CG    1 
ATOM   5907 O  OD1   . ASP A 1 721 ? -51.133 0.803   -0.956  1.00 158.17 ? 721 ASP A OD1   1 
ATOM   5908 O  OD2   . ASP A 1 721 ? -52.568 -0.709  -1.646  1.00 133.85 ? 721 ASP A OD2   1 
ATOM   5909 N  N     . PRO A 1 722 ? -48.228 -1.593  2.199   1.00 108.19 ? 722 PRO A N     1 
ATOM   5910 C  CA    . PRO A 1 722 ? -47.581 -2.558  3.106   1.00 105.44 ? 722 PRO A CA    1 
ATOM   5911 C  C     . PRO A 1 722 ? -48.435 -3.774  3.417   1.00 112.41 ? 722 PRO A C     1 
ATOM   5912 O  O     . PRO A 1 722 ? -47.892 -4.853  3.688   1.00 111.39 ? 722 PRO A O     1 
ATOM   5913 C  CB    . PRO A 1 722 ? -47.318 -1.722  4.366   1.00 101.12 ? 722 PRO A CB    1 
ATOM   5914 C  CG    . PRO A 1 722 ? -47.205 -0.320  3.868   1.00 102.89 ? 722 PRO A CG    1 
ATOM   5915 C  CD    . PRO A 1 722 ? -48.168 -0.214  2.716   1.00 104.48 ? 722 PRO A CD    1 
ATOM   5916 N  N     . THR A 1 723 ? -49.761 -3.633  3.374   1.00 116.19 ? 723 THR A N     1 
ATOM   5917 C  CA    . THR A 1 723 ? -50.642 -4.747  3.707   1.00 120.41 ? 723 THR A CA    1 
ATOM   5918 C  C     . THR A 1 723 ? -50.479 -5.899  2.722   1.00 121.90 ? 723 THR A C     1 
ATOM   5919 O  O     . THR A 1 723 ? -50.400 -7.066  3.122   1.00 123.06 ? 723 THR A O     1 
ATOM   5920 C  CB    . THR A 1 723 ? -52.093 -4.266  3.740   1.00 122.33 ? 723 THR A CB    1 
ATOM   5921 O  OG1   . THR A 1 723 ? -52.577 -4.110  2.401   1.00 128.82 ? 723 THR A OG1   1 
ATOM   5922 C  CG2   . THR A 1 723 ? -52.189 -2.932  4.461   1.00 115.63 ? 723 THR A CG2   1 
ATOM   5923 N  N     . LYS A 1 724 ? -50.419 -5.592  1.424   1.00 125.82 ? 724 LYS A N     1 
ATOM   5924 C  CA    . LYS A 1 724 ? -50.370 -6.619  0.389   1.00 115.19 ? 724 LYS A CA    1 
ATOM   5925 C  C     . LYS A 1 724 ? -49.071 -6.585  -0.410  1.00 108.44 ? 724 LYS A C     1 
ATOM   5926 O  O     . LYS A 1 724 ? -49.027 -7.102  -1.530  1.00 104.91 ? 724 LYS A O     1 
ATOM   5927 C  CB    . LYS A 1 724 ? -51.563 -6.484  -0.560  1.00 112.38 ? 724 LYS A CB    1 
ATOM   5928 C  CG    . LYS A 1 724 ? -52.175 -5.092  -0.599  1.00 114.63 ? 724 LYS A CG    1 
ATOM   5929 C  CD    . LYS A 1 724 ? -53.499 -5.091  -1.348  1.00 116.22 ? 724 LYS A CD    1 
ATOM   5930 C  CE    . LYS A 1 724 ? -54.597 -5.762  -0.538  1.00 108.89 ? 724 LYS A CE    1 
ATOM   5931 N  NZ    . LYS A 1 724 ? -55.931 -5.627  -1.186  1.00 93.92  ? 724 LYS A NZ    1 
ATOM   5932 N  N     . HIS A 1 725 ? -48.010 -5.989  0.133   1.00 105.89 ? 725 HIS A N     1 
ATOM   5933 C  CA    . HIS A 1 725 ? -46.748 -5.898  -0.587  1.00 94.96  ? 725 HIS A CA    1 
ATOM   5934 C  C     . HIS A 1 725 ? -45.587 -6.163  0.356   1.00 87.87  ? 725 HIS A C     1 
ATOM   5935 O  O     . HIS A 1 725 ? -45.615 -5.765  1.524   1.00 90.17  ? 725 HIS A O     1 
ATOM   5936 C  CB    . HIS A 1 725 ? -46.578 -4.526  -1.252  1.00 93.48  ? 725 HIS A CB    1 
ATOM   5937 C  CG    . HIS A 1 725 ? -47.455 -4.323  -2.447  1.00 92.29  ? 725 HIS A CG    1 
ATOM   5938 N  ND1   . HIS A 1 725 ? -48.292 -3.237  -2.581  1.00 91.78  ? 725 HIS A ND1   1 
ATOM   5939 C  CD2   . HIS A 1 725 ? -47.629 -5.071  -3.563  1.00 90.47  ? 725 HIS A CD2   1 
ATOM   5940 C  CE1   . HIS A 1 725 ? -48.941 -3.322  -3.729  1.00 95.70  ? 725 HIS A CE1   1 
ATOM   5941 N  NE2   . HIS A 1 725 ? -48.557 -4.425  -4.344  1.00 89.96  ? 725 HIS A NE2   1 
ATOM   5942 N  N     . ARG A 1 726 ? -44.565 -6.837  -0.166  1.00 88.66  ? 726 ARG A N     1 
ATOM   5943 C  CA    . ARG A 1 726 ? -43.360 -7.159  0.589   1.00 83.25  ? 726 ARG A CA    1 
ATOM   5944 C  C     . ARG A 1 726 ? -42.163 -6.969  -0.326  1.00 77.22  ? 726 ARG A C     1 
ATOM   5945 O  O     . ARG A 1 726 ? -42.050 -7.656  -1.346  1.00 71.13  ? 726 ARG A O     1 
ATOM   5946 C  CB    . ARG A 1 726 ? -43.409 -8.593  1.119   1.00 85.54  ? 726 ARG A CB    1 
ATOM   5947 C  CG    . ARG A 1 726 ? -42.728 -8.779  2.455   1.00 93.29  ? 726 ARG A CG    1 
ATOM   5948 C  CD    . ARG A 1 726 ? -43.041 -10.145 3.044   1.00 103.84 ? 726 ARG A CD    1 
ATOM   5949 N  NE    . ARG A 1 726 ? -42.996 -10.152 4.502   1.00 108.65 ? 726 ARG A NE    1 
ATOM   5950 C  CZ    . ARG A 1 726 ? -43.781 -9.430  5.292   1.00 111.10 ? 726 ARG A CZ    1 
ATOM   5951 N  NH1   . ARG A 1 726 ? -44.733 -8.650  4.803   1.00 104.50 ? 726 ARG A NH1   1 
ATOM   5952 N  NH2   . ARG A 1 726 ? -43.613 -9.499  6.609   1.00 117.07 ? 726 ARG A NH2   1 
ATOM   5953 N  N     . TYR A 1 727 ? -41.277 -6.043  0.031   1.00 73.37  ? 727 TYR A N     1 
ATOM   5954 C  CA    . TYR A 1 727 ? -40.128 -5.780  -0.820  1.00 72.63  ? 727 TYR A CA    1 
ATOM   5955 C  C     . TYR A 1 727 ? -39.179 -6.974  -0.821  1.00 75.23  ? 727 TYR A C     1 
ATOM   5956 O  O     . TYR A 1 727 ? -39.149 -7.784  0.110   1.00 73.36  ? 727 TYR A O     1 
ATOM   5957 C  CB    . TYR A 1 727 ? -39.392 -4.515  -0.376  1.00 70.64  ? 727 TYR A CB    1 
ATOM   5958 C  CG    . TYR A 1 727 ? -39.038 -4.440  1.095   1.00 71.26  ? 727 TYR A CG    1 
ATOM   5959 C  CD1   . TYR A 1 727 ? -38.001 -5.199  1.626   1.00 72.05  ? 727 TYR A CD1   1 
ATOM   5960 C  CD2   . TYR A 1 727 ? -39.715 -3.575  1.944   1.00 74.63  ? 727 TYR A CD2   1 
ATOM   5961 C  CE1   . TYR A 1 727 ? -37.666 -5.114  2.965   1.00 77.63  ? 727 TYR A CE1   1 
ATOM   5962 C  CE2   . TYR A 1 727 ? -39.386 -3.483  3.283   1.00 71.91  ? 727 TYR A CE2   1 
ATOM   5963 C  CZ    . TYR A 1 727 ? -38.363 -4.254  3.787   1.00 81.25  ? 727 TYR A CZ    1 
ATOM   5964 O  OH    . TYR A 1 727 ? -38.037 -4.160  5.120   1.00 88.40  ? 727 TYR A OH    1 
ATOM   5965 N  N     . ASP A 1 728 ? -38.401 -7.080  -1.895  1.00 69.13  ? 728 ASP A N     1 
ATOM   5966 C  CA    . ASP A 1 728 ? -37.451 -8.179  -2.045  1.00 71.79  ? 728 ASP A CA    1 
ATOM   5967 C  C     . ASP A 1 728 ? -36.231 -7.870  -1.190  1.00 68.47  ? 728 ASP A C     1 
ATOM   5968 O  O     . ASP A 1 728 ? -35.282 -7.215  -1.626  1.00 68.26  ? 728 ASP A O     1 
ATOM   5969 C  CB    . ASP A 1 728 ? -37.080 -8.382  -3.507  1.00 72.59  ? 728 ASP A CB    1 
ATOM   5970 C  CG    . ASP A 1 728 ? -36.424 -9.724  -3.758  1.00 77.48  ? 728 ASP A CG    1 
ATOM   5971 O  OD1   . ASP A 1 728 ? -35.531 -10.117 -2.977  1.00 84.91  ? 728 ASP A OD1   1 
ATOM   5972 O  OD2   . ASP A 1 728 ? -36.829 -10.405 -4.722  1.00 94.03  ? 728 ASP A OD2   1 
ATOM   5973 N  N     . ALA A 1 729 ? -36.265 -8.350  0.055   1.00 72.46  ? 729 ALA A N     1 
ATOM   5974 C  CA    . ALA A 1 729 ? -35.143 -8.137  0.961   1.00 74.02  ? 729 ALA A CA    1 
ATOM   5975 C  C     . ALA A 1 729 ? -33.863 -8.739  0.398   1.00 78.40  ? 729 ALA A C     1 
ATOM   5976 O  O     . ALA A 1 729 ? -32.785 -8.145  0.518   1.00 70.53  ? 729 ALA A O     1 
ATOM   5977 C  CB    . ALA A 1 729 ? -35.458 -8.728  2.335   1.00 71.46  ? 729 ALA A CB    1 
ATOM   5978 N  N     . GLU A 1 730 ? -33.965 -9.912  -0.232  1.00 75.08  ? 730 GLU A N     1 
ATOM   5979 C  CA    . GLU A 1 730 ? -32.787 -10.545 -0.815  1.00 74.08  ? 730 GLU A CA    1 
ATOM   5980 C  C     . GLU A 1 730 ? -32.175 -9.678  -1.907  1.00 74.72  ? 730 GLU A C     1 
ATOM   5981 O  O     . GLU A 1 730 ? -30.947 -9.621  -2.046  1.00 78.50  ? 730 GLU A O     1 
ATOM   5982 C  CB    . GLU A 1 730 ? -33.149 -11.926 -1.364  1.00 82.17  ? 730 GLU A CB    1 
ATOM   5983 C  CG    . GLU A 1 730 ? -32.187 -13.034 -0.953  1.00 99.50  ? 730 GLU A CG    1 
ATOM   5984 C  CD    . GLU A 1 730 ? -32.216 -13.321 0.538   1.00 115.72 ? 730 GLU A CD    1 
ATOM   5985 O  OE1   . GLU A 1 730 ? -33.228 -12.993 1.194   1.00 115.12 ? 730 GLU A OE1   1 
ATOM   5986 O  OE2   . GLU A 1 730 ? -31.221 -13.874 1.054   1.00 112.38 ? 730 GLU A OE2   1 
ATOM   5987 N  N     . TYR A 1 731 ? -33.011 -8.990  -2.689  1.00 72.03  ? 731 TYR A N     1 
ATOM   5988 C  CA    . TYR A 1 731 ? -32.485 -8.117  -3.734  1.00 73.31  ? 731 TYR A CA    1 
ATOM   5989 C  C     . TYR A 1 731 ? -31.666 -6.982  -3.134  1.00 70.37  ? 731 TYR A C     1 
ATOM   5990 O  O     . TYR A 1 731 ? -30.520 -6.746  -3.533  1.00 72.31  ? 731 TYR A O     1 
ATOM   5991 C  CB    . TYR A 1 731 ? -33.622 -7.557  -4.589  1.00 67.89  ? 731 TYR A CB    1 
ATOM   5992 C  CG    . TYR A 1 731 ? -33.174 -6.440  -5.508  1.00 63.13  ? 731 TYR A CG    1 
ATOM   5993 C  CD1   . TYR A 1 731 ? -32.575 -6.720  -6.730  1.00 64.19  ? 731 TYR A CD1   1 
ATOM   5994 C  CD2   . TYR A 1 731 ? -33.338 -5.107  -5.150  1.00 63.32  ? 731 TYR A CD2   1 
ATOM   5995 C  CE1   . TYR A 1 731 ? -32.157 -5.704  -7.570  1.00 67.39  ? 731 TYR A CE1   1 
ATOM   5996 C  CE2   . TYR A 1 731 ? -32.921 -4.086  -5.982  1.00 63.73  ? 731 TYR A CE2   1 
ATOM   5997 C  CZ    . TYR A 1 731 ? -32.333 -4.390  -7.191  1.00 65.20  ? 731 TYR A CZ    1 
ATOM   5998 O  OH    . TYR A 1 731 ? -31.920 -3.374  -8.020  1.00 70.12  ? 731 TYR A OH    1 
ATOM   5999 N  N     . TYR A 1 732 ? -32.241 -6.263  -2.173  1.00 66.14  ? 732 TYR A N     1 
ATOM   6000 C  CA    . TYR A 1 732 ? -31.562 -5.119  -1.583  1.00 67.48  ? 732 TYR A CA    1 
ATOM   6001 C  C     . TYR A 1 732 ? -30.440 -5.514  -0.632  1.00 68.26  ? 732 TYR A C     1 
ATOM   6002 O  O     . TYR A 1 732 ? -29.652 -4.648  -0.239  1.00 57.71  ? 732 TYR A O     1 
ATOM   6003 C  CB    . TYR A 1 732 ? -32.577 -4.232  -0.861  1.00 63.03  ? 732 TYR A CB    1 
ATOM   6004 C  CG    . TYR A 1 732 ? -33.585 -3.592  -1.792  1.00 65.91  ? 732 TYR A CG    1 
ATOM   6005 C  CD1   . TYR A 1 732 ? -33.222 -2.532  -2.614  1.00 64.36  ? 732 TYR A CD1   1 
ATOM   6006 C  CD2   . TYR A 1 732 ? -34.899 -4.042  -1.844  1.00 64.10  ? 732 TYR A CD2   1 
ATOM   6007 C  CE1   . TYR A 1 732 ? -34.138 -1.939  -3.463  1.00 66.07  ? 732 TYR A CE1   1 
ATOM   6008 C  CE2   . TYR A 1 732 ? -35.823 -3.455  -2.692  1.00 64.93  ? 732 TYR A CE2   1 
ATOM   6009 C  CZ    . TYR A 1 732 ? -35.436 -2.404  -3.499  1.00 65.43  ? 732 TYR A CZ    1 
ATOM   6010 O  OH    . TYR A 1 732 ? -36.348 -1.814  -4.345  1.00 64.40  ? 732 TYR A OH    1 
ATOM   6011 N  N     . ILE A 1 733 ? -30.345 -6.788  -0.254  1.00 73.73  ? 733 ILE A N     1 
ATOM   6012 C  CA    . ILE A 1 733 ? -29.220 -7.271  0.538   1.00 72.20  ? 733 ILE A CA    1 
ATOM   6013 C  C     . ILE A 1 733 ? -28.093 -7.662  -0.407  1.00 73.83  ? 733 ILE A C     1 
ATOM   6014 O  O     . ILE A 1 733 ? -27.035 -7.024  -0.430  1.00 68.21  ? 733 ILE A O     1 
ATOM   6015 C  CB    . ILE A 1 733 ? -29.621 -8.461  1.430   1.00 74.34  ? 733 ILE A CB    1 
ATOM   6016 C  CG1   . ILE A 1 733 ? -30.485 -7.991  2.600   1.00 78.64  ? 733 ILE A CG1   1 
ATOM   6017 C  CG2   . ILE A 1 733 ? -28.382 -9.191  1.940   1.00 64.62  ? 733 ILE A CG2   1 
ATOM   6018 C  CD1   . ILE A 1 733 ? -30.656 -9.026  3.693   1.00 73.16  ? 733 ILE A CD1   1 
ATOM   6019 N  N     . GLU A 1 734 ? -28.323 -8.705  -1.206  1.00 75.01  ? 734 GLU A N     1 
ATOM   6020 C  CA    . GLU A 1 734 ? -27.280 -9.268  -2.051  1.00 81.77  ? 734 GLU A CA    1 
ATOM   6021 C  C     . GLU A 1 734 ? -26.909 -8.371  -3.224  1.00 78.14  ? 734 GLU A C     1 
ATOM   6022 O  O     . GLU A 1 734 ? -25.913 -8.653  -3.901  1.00 86.64  ? 734 GLU A O     1 
ATOM   6023 C  CB    . GLU A 1 734 ? -27.722 -10.635 -2.576  1.00 79.93  ? 734 GLU A CB    1 
ATOM   6024 C  CG    . GLU A 1 734 ? -27.563 -11.774 -1.581  1.00 92.82  ? 734 GLU A CG    1 
ATOM   6025 C  CD    . GLU A 1 734 ? -26.212 -11.767 -0.896  1.00 97.24  ? 734 GLU A CD    1 
ATOM   6026 O  OE1   . GLU A 1 734 ? -25.185 -11.783 -1.608  1.00 90.30  ? 734 GLU A OE1   1 
ATOM   6027 O  OE2   . GLU A 1 734 ? -26.178 -11.753 0.353   1.00 100.36 ? 734 GLU A OE2   1 
ATOM   6028 N  N     . LYS A 1 735 ? -27.669 -7.298  -3.482  1.00 71.31  ? 735 LYS A N     1 
ATOM   6029 C  CA    . LYS A 1 735 ? -27.434 -6.550  -4.713  1.00 72.45  ? 735 LYS A CA    1 
ATOM   6030 C  C     . LYS A 1 735 ? -27.630 -5.041  -4.564  1.00 67.45  ? 735 LYS A C     1 
ATOM   6031 O  O     . LYS A 1 735 ? -27.770 -4.353  -5.582  1.00 65.40  ? 735 LYS A O     1 
ATOM   6032 C  CB    . LYS A 1 735 ? -28.350 -7.098  -5.815  1.00 72.57  ? 735 LYS A CB    1 
ATOM   6033 C  CG    . LYS A 1 735 ? -27.796 -8.340  -6.507  1.00 84.13  ? 735 LYS A CG    1 
ATOM   6034 C  CD    . LYS A 1 735 ? -28.631 -8.737  -7.709  1.00 85.24  ? 735 LYS A CD    1 
ATOM   6035 C  CE    . LYS A 1 735 ? -29.085 -7.514  -8.468  1.00 88.69  ? 735 LYS A CE    1 
ATOM   6036 N  NZ    . LYS A 1 735 ? -27.911 -6.806  -9.051  1.00 88.18  ? 735 LYS A NZ    1 
ATOM   6037 N  N     . GLN A 1 736 ? -27.642 -4.503  -3.344  1.00 62.36  ? 736 GLN A N     1 
ATOM   6038 C  CA    . GLN A 1 736 ? -27.730 -3.060  -3.157  1.00 63.97  ? 736 GLN A CA    1 
ATOM   6039 C  C     . GLN A 1 736 ? -26.807 -2.607  -2.034  1.00 60.31  ? 736 GLN A C     1 
ATOM   6040 O  O     . GLN A 1 736 ? -25.943 -1.750  -2.240  1.00 62.12  ? 736 GLN A O     1 
ATOM   6041 C  CB    . GLN A 1 736 ? -29.173 -2.634  -2.866  1.00 68.50  ? 736 GLN A CB    1 
ATOM   6042 C  CG    . GLN A 1 736 ? -29.975 -2.251  -4.106  1.00 61.13  ? 736 GLN A CG    1 
ATOM   6043 C  CD    . GLN A 1 736 ? -29.784 -0.801  -4.501  1.00 60.53  ? 736 GLN A CD    1 
ATOM   6044 O  OE1   . GLN A 1 736 ? -29.475 0.046   -3.664  1.00 64.99  ? 736 GLN A OE1   1 
ATOM   6045 N  NE2   . GLN A 1 736 ? -29.962 -0.507  -5.784  1.00 60.69  ? 736 GLN A NE2   1 
ATOM   6046 N  N     . VAL A 1 737 ? -26.978 -3.181  -0.844  1.00 53.98  ? 737 VAL A N     1 
ATOM   6047 C  CA    . VAL A 1 737 ? -26.150 -2.797  0.294   1.00 64.67  ? 737 VAL A CA    1 
ATOM   6048 C  C     . VAL A 1 737 ? -24.810 -3.522  0.255   1.00 70.11  ? 737 VAL A C     1 
ATOM   6049 O  O     . VAL A 1 737 ? -23.743 -2.898  0.350   1.00 63.45  ? 737 VAL A O     1 
ATOM   6050 C  CB    . VAL A 1 737 ? -26.901 -3.071  1.610   1.00 61.29  ? 737 VAL A CB    1 
ATOM   6051 C  CG1   . VAL A 1 737 ? -25.967 -2.905  2.799   1.00 62.40  ? 737 VAL A CG1   1 
ATOM   6052 C  CG2   . VAL A 1 737 ? -28.107 -2.153  1.733   1.00 64.77  ? 737 VAL A CG2   1 
ATOM   6053 N  N     . LEU A 1 738 ? -24.850 -4.849  0.119   1.00 66.48  ? 738 LEU A N     1 
ATOM   6054 C  CA    . LEU A 1 738 ? -23.623 -5.642  0.146   1.00 67.78  ? 738 LEU A CA    1 
ATOM   6055 C  C     . LEU A 1 738 ? -22.647 -5.264  -0.959  1.00 75.25  ? 738 LEU A C     1 
ATOM   6056 O  O     . LEU A 1 738 ? -21.449 -5.121  -0.662  1.00 68.67  ? 738 LEU A O     1 
ATOM   6057 C  CB    . LEU A 1 738 ? -23.971 -7.135  0.099   1.00 66.03  ? 738 LEU A CB    1 
ATOM   6058 C  CG    . LEU A 1 738 ? -23.957 -7.895  1.426   1.00 78.84  ? 738 LEU A CG    1 
ATOM   6059 C  CD1   . LEU A 1 738 ? -22.536 -8.278  1.799   1.00 85.13  ? 738 LEU A CD1   1 
ATOM   6060 C  CD2   . LEU A 1 738 ? -24.604 -7.079  2.536   1.00 76.77  ? 738 LEU A CD2   1 
ATOM   6061 N  N     . PRO A 1 739 ? -23.053 -5.103  -2.225  1.00 69.33  ? 739 PRO A N     1 
ATOM   6062 C  CA    . PRO A 1 739 ? -22.078 -4.653  -3.231  1.00 69.34  ? 739 PRO A CA    1 
ATOM   6063 C  C     . PRO A 1 739 ? -21.541 -3.262  -2.957  1.00 75.97  ? 739 PRO A C     1 
ATOM   6064 O  O     . PRO A 1 739 ? -20.388 -2.973  -3.298  1.00 76.59  ? 739 PRO A O     1 
ATOM   6065 C  CB    . PRO A 1 739 ? -22.875 -4.702  -4.542  1.00 66.91  ? 739 PRO A CB    1 
ATOM   6066 C  CG    . PRO A 1 739 ? -23.976 -5.659  -4.279  1.00 68.46  ? 739 PRO A CG    1 
ATOM   6067 C  CD    . PRO A 1 739 ? -24.348 -5.429  -2.850  1.00 68.34  ? 739 PRO A CD    1 
ATOM   6068 N  N     . ALA A 1 740 ? -22.344 -2.390  -2.341  1.00 74.27  ? 740 ALA A N     1 
ATOM   6069 C  CA    . ALA A 1 740 ? -21.885 -1.034  -2.065  1.00 68.01  ? 740 ALA A CA    1 
ATOM   6070 C  C     . ALA A 1 740 ? -20.824 -1.018  -0.974  1.00 67.76  ? 740 ALA A C     1 
ATOM   6071 O  O     . ALA A 1 740 ? -19.858 -0.250  -1.053  1.00 68.19  ? 740 ALA A O     1 
ATOM   6072 C  CB    . ALA A 1 740 ? -23.067 -0.146  -1.677  1.00 60.48  ? 740 ALA A CB    1 
ATOM   6073 N  N     . VAL A 1 741 ? -20.979 -1.856  0.054   1.00 71.90  ? 741 VAL A N     1 
ATOM   6074 C  CA    . VAL A 1 741 ? -19.989 -1.884  1.127   1.00 71.93  ? 741 VAL A CA    1 
ATOM   6075 C  C     . VAL A 1 741 ? -18.827 -2.831  0.841   1.00 71.84  ? 741 VAL A C     1 
ATOM   6076 O  O     . VAL A 1 741 ? -17.771 -2.711  1.482   1.00 69.56  ? 741 VAL A O     1 
ATOM   6077 C  CB    . VAL A 1 741 ? -20.631 -2.263  2.474   1.00 70.55  ? 741 VAL A CB    1 
ATOM   6078 C  CG1   . VAL A 1 741 ? -21.543 -1.146  2.960   1.00 64.71  ? 741 VAL A CG1   1 
ATOM   6079 C  CG2   . VAL A 1 741 ? -21.380 -3.582  2.360   1.00 70.65  ? 741 VAL A CG2   1 
ATOM   6080 N  N     . GLU A 1 742 ? -18.985 -3.759  -0.104  1.00 74.06  ? 742 GLU A N     1 
ATOM   6081 C  CA    . GLU A 1 742 ? -17.943 -4.748  -0.355  1.00 74.69  ? 742 GLU A CA    1 
ATOM   6082 C  C     . GLU A 1 742 ? -16.742 -4.126  -1.054  1.00 81.31  ? 742 GLU A C     1 
ATOM   6083 O  O     . GLU A 1 742 ? -15.594 -4.428  -0.706  1.00 75.32  ? 742 GLU A O     1 
ATOM   6084 C  CB    . GLU A 1 742 ? -18.523 -5.900  -1.176  1.00 87.57  ? 742 GLU A CB    1 
ATOM   6085 C  CG    . GLU A 1 742 ? -17.503 -6.872  -1.738  1.00 90.61  ? 742 GLU A CG    1 
ATOM   6086 C  CD    . GLU A 1 742 ? -17.424 -6.805  -3.248  1.00 104.87 ? 742 GLU A CD    1 
ATOM   6087 O  OE1   . GLU A 1 742 ? -16.299 -6.783  -3.785  1.00 103.09 ? 742 GLU A OE1   1 
ATOM   6088 O  OE2   . GLU A 1 742 ? -18.489 -6.763  -3.899  1.00 98.08  ? 742 GLU A OE2   1 
ATOM   6089 N  N     . ARG A 1 743 ? -16.985 -3.251  -2.035  1.00 72.88  ? 743 ARG A N     1 
ATOM   6090 C  CA    . ARG A 1 743 ? -15.886 -2.590  -2.730  1.00 76.11  ? 743 ARG A CA    1 
ATOM   6091 C  C     . ARG A 1 743 ? -15.003 -1.797  -1.780  1.00 71.42  ? 743 ARG A C     1 
ATOM   6092 O  O     . ARG A 1 743 ? -13.846 -1.518  -2.111  1.00 72.31  ? 743 ARG A O     1 
ATOM   6093 C  CB    . ARG A 1 743 ? -16.422 -1.662  -3.817  1.00 77.53  ? 743 ARG A CB    1 
ATOM   6094 C  CG    . ARG A 1 743 ? -17.531 -2.256  -4.652  1.00 64.75  ? 743 ARG A CG    1 
ATOM   6095 C  CD    . ARG A 1 743 ? -18.315 -1.158  -5.338  1.00 71.31  ? 743 ARG A CD    1 
ATOM   6096 N  NE    . ARG A 1 743 ? -19.212 -1.692  -6.352  1.00 74.10  ? 743 ARG A NE    1 
ATOM   6097 C  CZ    . ARG A 1 743 ? -20.531 -1.578  -6.309  1.00 78.46  ? 743 ARG A CZ    1 
ATOM   6098 N  NH1   . ARG A 1 743 ? -21.139 -0.937  -5.325  1.00 82.14  ? 743 ARG A NH1   1 
ATOM   6099 N  NH2   . ARG A 1 743 ? -21.260 -2.125  -7.275  1.00 76.51  ? 743 ARG A NH2   1 
ATOM   6100 N  N     . ILE A 1 744 ? -15.523 -1.430  -0.614  1.00 69.38  ? 744 ILE A N     1 
ATOM   6101 C  CA    . ILE A 1 744 ? -14.741 -0.721  0.387   1.00 69.72  ? 744 ILE A CA    1 
ATOM   6102 C  C     . ILE A 1 744 ? -14.094 -1.688  1.367   1.00 74.75  ? 744 ILE A C     1 
ATOM   6103 O  O     . ILE A 1 744 ? -12.885 -1.632  1.608   1.00 72.17  ? 744 ILE A O     1 
ATOM   6104 C  CB    . ILE A 1 744 ? -15.634 0.303   1.117   1.00 70.49  ? 744 ILE A CB    1 
ATOM   6105 C  CG1   . ILE A 1 744 ? -16.164 1.339   0.125   1.00 65.28  ? 744 ILE A CG1   1 
ATOM   6106 C  CG2   . ILE A 1 744 ? -14.864 0.969   2.249   1.00 73.85  ? 744 ILE A CG2   1 
ATOM   6107 C  CD1   . ILE A 1 744 ? -16.722 2.577   0.776   1.00 67.86  ? 744 ILE A CD1   1 
ATOM   6108 N  N     . LEU A 1 745 ? -14.880 -2.601  1.936   1.00 77.87  ? 745 LEU A N     1 
ATOM   6109 C  CA    . LEU A 1 745 ? -14.381 -3.460  3.003   1.00 71.95  ? 745 LEU A CA    1 
ATOM   6110 C  C     . LEU A 1 745 ? -13.535 -4.621  2.495   1.00 74.14  ? 745 LEU A C     1 
ATOM   6111 O  O     . LEU A 1 745 ? -12.992 -5.368  3.317   1.00 74.25  ? 745 LEU A O     1 
ATOM   6112 C  CB    . LEU A 1 745 ? -15.544 -3.993  3.850   1.00 72.35  ? 745 LEU A CB    1 
ATOM   6113 C  CG    . LEU A 1 745 ? -16.093 -3.103  4.976   1.00 76.39  ? 745 LEU A CG    1 
ATOM   6114 C  CD1   . LEU A 1 745 ? -15.293 -3.296  6.254   1.00 84.33  ? 745 LEU A CD1   1 
ATOM   6115 C  CD2   . LEU A 1 745 ? -16.111 -1.636  4.589   1.00 78.08  ? 745 LEU A CD2   1 
ATOM   6116 N  N     . ARG A 1 746 ? -13.402 -4.794  1.175   1.00 74.96  ? 746 ARG A N     1 
ATOM   6117 C  CA    . ARG A 1 746 ? -12.487 -5.809  0.665   1.00 74.68  ? 746 ARG A CA    1 
ATOM   6118 C  C     . ARG A 1 746 ? -11.037 -5.447  0.959   1.00 81.06  ? 746 ARG A C     1 
ATOM   6119 O  O     . ARG A 1 746 ? -10.194 -6.341  1.099   1.00 80.90  ? 746 ARG A O     1 
ATOM   6120 C  CB    . ARG A 1 746 ? -12.684 -5.996  -0.840  1.00 75.61  ? 746 ARG A CB    1 
ATOM   6121 C  CG    . ARG A 1 746 ? -12.196 -4.809  -1.655  1.00 79.30  ? 746 ARG A CG    1 
ATOM   6122 C  CD    . ARG A 1 746 ? -12.975 -4.627  -2.934  1.00 88.22  ? 746 ARG A CD    1 
ATOM   6123 N  NE    . ARG A 1 746 ? -13.208 -5.892  -3.616  1.00 92.60  ? 746 ARG A NE    1 
ATOM   6124 C  CZ    . ARG A 1 746 ? -13.704 -5.995  -4.840  1.00 96.84  ? 746 ARG A CZ    1 
ATOM   6125 N  NH1   . ARG A 1 746 ? -14.040 -4.925  -5.541  1.00 89.67  ? 746 ARG A NH1   1 
ATOM   6126 N  NH2   . ARG A 1 746 ? -13.875 -7.202  -5.372  1.00 102.51 ? 746 ARG A NH2   1 
ATOM   6127 N  N     . ALA A 1 747 ? -10.727 -4.150  1.057   1.00 84.14  ? 747 ALA A N     1 
ATOM   6128 C  CA    . ALA A 1 747 ? -9.381  -3.690  1.376   1.00 84.28  ? 747 ALA A CA    1 
ATOM   6129 C  C     . ALA A 1 747 ? -8.922  -4.096  2.772   1.00 83.23  ? 747 ALA A C     1 
ATOM   6130 O  O     . ALA A 1 747 ? -7.768  -3.812  3.118   1.00 87.15  ? 747 ALA A O     1 
ATOM   6131 C  CB    . ALA A 1 747 ? -9.298  -2.163  1.228   1.00 73.06  ? 747 ALA A CB    1 
ATOM   6132 N  N     . PHE A 1 748 ? -9.774  -4.736  3.579   1.00 78.94  ? 748 PHE A N     1 
ATOM   6133 C  CA    . PHE A 1 748 ? -9.411  -5.201  4.915   1.00 72.64  ? 748 PHE A CA    1 
ATOM   6134 C  C     . PHE A 1 748 ? -9.579  -6.706  5.055   1.00 77.69  ? 748 PHE A C     1 
ATOM   6135 O  O     . PHE A 1 748 ? -9.499  -7.227  6.172   1.00 84.30  ? 748 PHE A O     1 
ATOM   6136 C  CB    . PHE A 1 748 ? -10.241 -4.474  5.984   1.00 78.48  ? 748 PHE A CB    1 
ATOM   6137 C  CG    . PHE A 1 748 ? -10.149 -2.972  5.897   1.00 85.26  ? 748 PHE A CG    1 
ATOM   6138 C  CD1   . PHE A 1 748 ? -9.151  -2.281  6.566   1.00 80.99  ? 748 PHE A CD1   1 
ATOM   6139 C  CD2   . PHE A 1 748 ? -11.057 -2.254  5.134   1.00 79.97  ? 748 PHE A CD2   1 
ATOM   6140 C  CE1   . PHE A 1 748 ? -9.063  -0.903  6.478   1.00 78.38  ? 748 PHE A CE1   1 
ATOM   6141 C  CE2   . PHE A 1 748 ? -10.971 -0.878  5.041   1.00 82.11  ? 748 PHE A CE2   1 
ATOM   6142 C  CZ    . PHE A 1 748 ? -9.975  -0.201  5.714   1.00 84.33  ? 748 PHE A CZ    1 
ATOM   6143 N  N     . GLY A 1 749 ? -9.811  -7.411  3.946   1.00 75.94  ? 749 GLY A N     1 
ATOM   6144 C  CA    . GLY A 1 749 ? -9.889  -8.854  3.928   1.00 79.18  ? 749 GLY A CA    1 
ATOM   6145 C  C     . GLY A 1 749 ? -11.279 -9.439  4.036   1.00 83.23  ? 749 GLY A C     1 
ATOM   6146 O  O     . GLY A 1 749 ? -11.412 -10.667 4.012   1.00 86.98  ? 749 GLY A O     1 
ATOM   6147 N  N     . TYR A 1 750 ? -12.316 -8.611  4.153   1.00 79.54  ? 750 TYR A N     1 
ATOM   6148 C  CA    . TYR A 1 750 ? -13.678 -9.110  4.316   1.00 87.82  ? 750 TYR A CA    1 
ATOM   6149 C  C     . TYR A 1 750 ? -14.289 -9.425  2.955   1.00 84.68  ? 750 TYR A C     1 
ATOM   6150 O  O     . TYR A 1 750 ? -14.342 -8.558  2.075   1.00 78.55  ? 750 TYR A O     1 
ATOM   6151 C  CB    . TYR A 1 750 ? -14.541 -8.088  5.053   1.00 85.51  ? 750 TYR A CB    1 
ATOM   6152 C  CG    . TYR A 1 750 ? -14.164 -7.872  6.501   1.00 89.79  ? 750 TYR A CG    1 
ATOM   6153 C  CD1   . TYR A 1 750 ? -14.606 -8.740  7.491   1.00 92.36  ? 750 TYR A CD1   1 
ATOM   6154 C  CD2   . TYR A 1 750 ? -13.379 -6.791  6.880   1.00 86.76  ? 750 TYR A CD2   1 
ATOM   6155 C  CE1   . TYR A 1 750 ? -14.269 -8.543  8.816   1.00 94.59  ? 750 TYR A CE1   1 
ATOM   6156 C  CE2   . TYR A 1 750 ? -13.037 -6.586  8.204   1.00 88.81  ? 750 TYR A CE2   1 
ATOM   6157 C  CZ    . TYR A 1 750 ? -13.484 -7.465  9.167   1.00 92.54  ? 750 TYR A CZ    1 
ATOM   6158 O  OH    . TYR A 1 750 ? -13.147 -7.266  10.485  1.00 93.57  ? 750 TYR A OH    1 
ATOM   6159 N  N     . ARG A 1 751 ? -14.749 -10.662 2.781   1.00 88.35  ? 751 ARG A N     1 
ATOM   6160 C  CA    . ARG A 1 751 ? -15.558 -11.019 1.629   1.00 97.05  ? 751 ARG A CA    1 
ATOM   6161 C  C     . ARG A 1 751 ? -17.025 -10.733 1.940   1.00 98.33  ? 751 ARG A C     1 
ATOM   6162 O  O     . ARG A 1 751 ? -17.379 -10.292 3.037   1.00 98.23  ? 751 ARG A O     1 
ATOM   6163 C  CB    . ARG A 1 751 ? -15.345 -12.484 1.248   1.00 98.94  ? 751 ARG A CB    1 
ATOM   6164 C  CG    . ARG A 1 751 ? -13.929 -12.992 1.468   1.00 94.96  ? 751 ARG A CG    1 
ATOM   6165 C  CD    . ARG A 1 751 ? -13.435 -13.783 0.264   1.00 99.18  ? 751 ARG A CD    1 
ATOM   6166 N  NE    . ARG A 1 751 ? -13.518 -13.009 -0.969  1.00 109.63 ? 751 ARG A NE    1 
ATOM   6167 C  CZ    . ARG A 1 751 ? -13.894 -13.503 -2.141  1.00 96.06  ? 751 ARG A CZ    1 
ATOM   6168 N  NH1   . ARG A 1 751 ? -14.227 -14.776 -2.280  1.00 97.35  ? 751 ARG A NH1   1 
ATOM   6169 N  NH2   . ARG A 1 751 ? -13.938 -12.700 -3.200  1.00 89.38  ? 751 ARG A NH2   1 
ATOM   6170 N  N     . LYS A 1 752 ? -17.897 -10.986 0.961   1.00 98.47  ? 752 LYS A N     1 
ATOM   6171 C  CA    . LYS A 1 752 ? -19.319 -10.721 1.156   1.00 100.43 ? 752 LYS A CA    1 
ATOM   6172 C  C     . LYS A 1 752 ? -19.895 -11.589 2.269   1.00 106.69 ? 752 LYS A C     1 
ATOM   6173 O  O     . LYS A 1 752 ? -20.785 -11.155 3.010   1.00 101.72 ? 752 LYS A O     1 
ATOM   6174 C  CB    . LYS A 1 752 ? -20.083 -10.956 -0.147  1.00 90.89  ? 752 LYS A CB    1 
ATOM   6175 C  CG    . LYS A 1 752 ? -19.788 -9.954  -1.248  1.00 97.51  ? 752 LYS A CG    1 
ATOM   6176 C  CD    . LYS A 1 752 ? -21.008 -9.103  -1.555  1.00 88.47  ? 752 LYS A CD    1 
ATOM   6177 C  CE    . LYS A 1 752 ? -21.049 -8.706  -3.022  1.00 85.11  ? 752 LYS A CE    1 
ATOM   6178 N  NZ    . LYS A 1 752 ? -21.360 -9.870  -3.899  1.00 86.05  ? 752 LYS A NZ    1 
ATOM   6179 N  N     . GLU A 1 753 ? -19.391 -12.815 2.408   1.00 109.07 ? 753 GLU A N     1 
ATOM   6180 C  CA    . GLU A 1 753 ? -19.984 -13.744 3.359   1.00 109.62 ? 753 GLU A CA    1 
ATOM   6181 C  C     . GLU A 1 753 ? -19.649 -13.375 4.798   1.00 106.82 ? 753 GLU A C     1 
ATOM   6182 O  O     . GLU A 1 753 ? -20.388 -13.745 5.719   1.00 112.32 ? 753 GLU A O     1 
ATOM   6183 C  CB    . GLU A 1 753 ? -19.528 -15.170 3.049   1.00 111.26 ? 753 GLU A CB    1 
ATOM   6184 C  CG    . GLU A 1 753 ? -20.115 -15.821 1.775   1.00 115.51 ? 753 GLU A CG    1 
ATOM   6185 C  CD    . GLU A 1 753 ? -20.038 -14.973 0.497   1.00 128.57 ? 753 GLU A CD    1 
ATOM   6186 O  OE1   . GLU A 1 753 ? -19.243 -14.011 0.419   1.00 123.58 ? 753 GLU A OE1   1 
ATOM   6187 O  OE2   . GLU A 1 753 ? -20.820 -15.275 -0.436  1.00 132.93 ? 753 GLU A OE2   1 
ATOM   6188 N  N     . ASP A 1 754 ? -18.543 -12.672 5.014   1.00 107.58 ? 754 ASP A N     1 
ATOM   6189 C  CA    . ASP A 1 754 ? -18.205 -12.158 6.334   1.00 111.08 ? 754 ASP A CA    1 
ATOM   6190 C  C     . ASP A 1 754 ? -19.006 -10.912 6.705   1.00 108.27 ? 754 ASP A C     1 
ATOM   6191 O  O     . ASP A 1 754 ? -18.705 -10.279 7.725   1.00 107.36 ? 754 ASP A O     1 
ATOM   6192 C  CB    . ASP A 1 754 ? -16.706 -11.853 6.410   1.00 106.67 ? 754 ASP A CB    1 
ATOM   6193 C  CG    . ASP A 1 754 ? -15.867 -12.877 5.671   1.00 107.82 ? 754 ASP A CG    1 
ATOM   6194 O  OD1   . ASP A 1 754 ? -15.428 -13.859 6.307   1.00 115.23 ? 754 ASP A OD1   1 
ATOM   6195 O  OD2   . ASP A 1 754 ? -15.645 -12.703 4.455   1.00 119.04 ? 754 ASP A OD2   1 
ATOM   6196 N  N     . LEU A 1 755 ? -20.014 -10.549 5.907   1.00 113.72 ? 755 LEU A N     1 
ATOM   6197 C  CA    . LEU A 1 755 ? -20.787 -9.335  6.127   1.00 111.53 ? 755 LEU A CA    1 
ATOM   6198 C  C     . LEU A 1 755 ? -22.281 -9.567  6.306   1.00 113.39 ? 755 LEU A C     1 
ATOM   6199 O  O     . LEU A 1 755 ? -22.944 -8.720  6.916   1.00 109.33 ? 755 LEU A O     1 
ATOM   6200 C  CB    . LEU A 1 755 ? -20.586 -8.354  4.960   1.00 103.32 ? 755 LEU A CB    1 
ATOM   6201 C  CG    . LEU A 1 755 ? -19.146 -8.057  4.536   1.00 102.70 ? 755 LEU A CG    1 
ATOM   6202 C  CD1   . LEU A 1 755 ? -19.110 -7.438  3.146   1.00 94.87  ? 755 LEU A CD1   1 
ATOM   6203 C  CD2   . LEU A 1 755 ? -18.458 -7.151  5.543   1.00 96.68  ? 755 LEU A CD2   1 
ATOM   6204 N  N     . ARG A 1 756 ? -22.828 -10.667 5.798   1.00 111.75 ? 756 ARG A N     1 
ATOM   6205 C  CA    . ARG A 1 756 ? -24.263 -10.910 5.891   1.00 105.34 ? 756 ARG A CA    1 
ATOM   6206 C  C     . ARG A 1 756 ? -24.632 -11.430 7.279   1.00 106.21 ? 756 ARG A C     1 
ATOM   6207 O  O     . ARG A 1 756 ? -23.759 -11.748 8.087   1.00 105.81 ? 756 ARG A O     1 
ATOM   6208 C  CB    . ARG A 1 756 ? -24.708 -11.889 4.794   1.00 100.57 ? 756 ARG A CB    1 
ATOM   6209 C  CG    . ARG A 1 756 ? -26.006 -12.656 5.064   1.00 108.94 ? 756 ARG A CG    1 
ATOM   6210 C  CD    . ARG A 1 756 ? -25.761 -14.002 5.746   1.00 111.92 ? 756 ARG A CD    1 
ATOM   6211 N  NE    . ARG A 1 756 ? -26.998 -14.592 6.243   1.00 115.40 ? 756 ARG A NE    1 
ATOM   6212 C  CZ    . ARG A 1 756 ? -27.334 -14.653 7.524   1.00 113.08 ? 756 ARG A CZ    1 
ATOM   6213 N  NH1   . ARG A 1 756 ? -26.553 -14.155 8.468   1.00 109.04 ? 756 ARG A NH1   1 
ATOM   6214 N  NH2   . ARG A 1 756 ? -28.480 -15.235 7.867   1.00 99.44  ? 756 ARG A NH2   1 
ATOM   6215 O  "O5'" . DG  B 2 1   ? -29.806 -23.487 -13.427 1.00 136.95 ? 1   DG  P "O5'" 1 
ATOM   6216 C  "C5'" . DG  B 2 1   ? -29.247 -23.800 -14.696 1.00 134.32 ? 1   DG  P "C5'" 1 
ATOM   6217 C  "C4'" . DG  B 2 1   ? -27.743 -23.597 -14.689 1.00 135.11 ? 1   DG  P "C4'" 1 
ATOM   6218 O  "O4'" . DG  B 2 1   ? -27.254 -23.622 -16.053 1.00 132.82 ? 1   DG  P "O4'" 1 
ATOM   6219 C  "C3'" . DG  B 2 1   ? -27.283 -22.256 -14.145 1.00 136.76 ? 1   DG  P "C3'" 1 
ATOM   6220 O  "O3'" . DG  B 2 1   ? -25.921 -22.342 -13.746 1.00 139.85 ? 1   DG  P "O3'" 1 
ATOM   6221 C  "C2'" . DG  B 2 1   ? -27.441 -21.369 -15.369 1.00 130.77 ? 1   DG  P "C2'" 1 
ATOM   6222 C  "C1'" . DG  B 2 1   ? -26.961 -22.301 -16.478 1.00 130.24 ? 1   DG  P "C1'" 1 
ATOM   6223 N  N9    . DG  B 2 1   ? -27.636 -22.067 -17.744 1.00 127.16 ? 1   DG  P N9    1 
ATOM   6224 C  C8    . DG  B 2 1   ? -28.987 -21.920 -17.936 1.00 128.16 ? 1   DG  P C8    1 
ATOM   6225 N  N7    . DG  B 2 1   ? -29.315 -21.718 -19.178 1.00 129.47 ? 1   DG  P N7    1 
ATOM   6226 C  C5    . DG  B 2 1   ? -28.105 -21.731 -19.854 1.00 124.14 ? 1   DG  P C5    1 
ATOM   6227 C  C6    . DG  B 2 1   ? -27.838 -21.565 -21.226 1.00 117.68 ? 1   DG  P C6    1 
ATOM   6228 O  O6    . DG  B 2 1   ? -28.647 -21.364 -22.140 1.00 108.96 ? 1   DG  P O6    1 
ATOM   6229 N  N1    . DG  B 2 1   ? -26.477 -21.647 -21.499 1.00 111.50 ? 1   DG  P N1    1 
ATOM   6230 C  C2    . DG  B 2 1   ? -25.493 -21.867 -20.563 1.00 106.72 ? 1   DG  P C2    1 
ATOM   6231 N  N2    . DG  B 2 1   ? -24.233 -21.913 -21.023 1.00 94.95  ? 1   DG  P N2    1 
ATOM   6232 N  N3    . DG  B 2 1   ? -25.731 -22.025 -19.266 1.00 113.49 ? 1   DG  P N3    1 
ATOM   6233 C  C4    . DG  B 2 1   ? -27.058 -21.945 -18.987 1.00 120.81 ? 1   DG  P C4    1 
ATOM   6234 P  P     . DA  B 2 2   ? -25.254 -21.192 -12.839 1.00 157.15 ? 2   DA  P P     1 
ATOM   6235 O  OP1   . DA  B 2 2   ? -25.461 -21.574 -11.425 1.00 145.96 ? 2   DA  P OP1   1 
ATOM   6236 O  OP2   . DA  B 2 2   ? -25.721 -19.869 -13.312 1.00 133.36 ? 2   DA  P OP2   1 
ATOM   6237 O  "O5'" . DA  B 2 2   ? -23.694 -21.319 -13.169 1.00 130.28 ? 2   DA  P "O5'" 1 
ATOM   6238 C  "C5'" . DA  B 2 2   ? -23.270 -22.123 -14.266 1.00 126.50 ? 2   DA  P "C5'" 1 
ATOM   6239 C  "C4'" . DA  B 2 2   ? -22.081 -21.501 -14.981 1.00 126.35 ? 2   DA  P "C4'" 1 
ATOM   6240 O  "O4'" . DA  B 2 2   ? -22.438 -21.190 -16.354 1.00 128.50 ? 2   DA  P "O4'" 1 
ATOM   6241 C  "C3'" . DA  B 2 2   ? -21.569 -20.198 -14.392 1.00 120.83 ? 2   DA  P "C3'" 1 
ATOM   6242 O  "O3'" . DA  B 2 2   ? -20.169 -20.093 -14.638 1.00 120.11 ? 2   DA  P "O3'" 1 
ATOM   6243 C  "C2'" . DA  B 2 2   ? -22.369 -19.149 -15.168 1.00 116.44 ? 2   DA  P "C2'" 1 
ATOM   6244 C  "C1'" . DA  B 2 2   ? -22.465 -19.783 -16.553 1.00 115.47 ? 2   DA  P "C1'" 1 
ATOM   6245 N  N9    . DA  B 2 2   ? -23.700 -19.464 -17.262 1.00 109.75 ? 2   DA  P N9    1 
ATOM   6246 C  C8    . DA  B 2 2   ? -24.957 -19.438 -16.731 1.00 112.11 ? 2   DA  P C8    1 
ATOM   6247 N  N7    . DA  B 2 2   ? -25.894 -19.149 -17.597 1.00 106.79 ? 2   DA  P N7    1 
ATOM   6248 C  C5    . DA  B 2 2   ? -25.209 -18.983 -18.788 1.00 104.09 ? 2   DA  P C5    1 
ATOM   6249 C  C6    . DA  B 2 2   ? -25.646 -18.662 -20.082 1.00 102.43 ? 2   DA  P C6    1 
ATOM   6250 N  N6    . DA  B 2 2   ? -26.926 -18.451 -20.375 1.00 98.82  ? 2   DA  P N6    1 
ATOM   6251 N  N1    . DA  B 2 2   ? -24.718 -18.567 -21.062 1.00 100.12 ? 2   DA  P N1    1 
ATOM   6252 C  C2    . DA  B 2 2   ? -23.430 -18.784 -20.750 1.00 102.39 ? 2   DA  P C2    1 
ATOM   6253 N  N3    . DA  B 2 2   ? -22.897 -19.091 -19.557 1.00 104.21 ? 2   DA  P N3    1 
ATOM   6254 C  C4    . DA  B 2 2   ? -23.854 -19.177 -18.609 1.00 104.31 ? 2   DA  P C4    1 
ATOM   6255 P  P     . DC  B 2 3   ? -19.378 -18.724 -14.355 1.00 147.18 ? 3   DC  P P     1 
ATOM   6256 O  OP1   . DC  B 2 3   ? -17.965 -19.086 -14.105 1.00 115.87 ? 3   DC  P OP1   1 
ATOM   6257 O  OP2   . DC  B 2 3   ? -20.124 -17.948 -13.339 1.00 131.44 ? 3   DC  P OP2   1 
ATOM   6258 O  "O5'" . DC  B 2 3   ? -19.463 -17.945 -15.748 1.00 118.65 ? 3   DC  P "O5'" 1 
ATOM   6259 C  "C5'" . DC  B 2 3   ? -19.152 -18.628 -16.958 1.00 117.41 ? 3   DC  P "C5'" 1 
ATOM   6260 C  "C4'" . DC  B 2 3   ? -19.130 -17.672 -18.137 1.00 114.11 ? 3   DC  P "C4'" 1 
ATOM   6261 O  "O4'" . DC  B 2 3   ? -20.467 -17.510 -18.680 1.00 107.96 ? 3   DC  P "O4'" 1 
ATOM   6262 C  "C3'" . DC  B 2 3   ? -18.632 -16.267 -17.823 1.00 112.39 ? 3   DC  P "C3'" 1 
ATOM   6263 O  "O3'" . DC  B 2 3   ? -17.866 -15.799 -18.910 1.00 110.73 ? 3   DC  P "O3'" 1 
ATOM   6264 C  "C2'" . DC  B 2 3   ? -19.930 -15.473 -17.666 1.00 108.97 ? 3   DC  P "C2'" 1 
ATOM   6265 C  "C1'" . DC  B 2 3   ? -20.809 -16.138 -18.712 1.00 106.70 ? 3   DC  P "C1'" 1 
ATOM   6266 N  N1    . DC  B 2 3   ? -22.272 -16.032 -18.442 1.00 104.11 ? 3   DC  P N1    1 
ATOM   6267 C  C2    . DC  B 2 3   ? -23.152 -15.774 -19.500 1.00 98.67  ? 3   DC  P C2    1 
ATOM   6268 O  O2    . DC  B 2 3   ? -22.694 -15.618 -20.640 1.00 99.10  ? 3   DC  P O2    1 
ATOM   6269 N  N3    . DC  B 2 3   ? -24.483 -15.705 -19.244 1.00 92.91  ? 3   DC  P N3    1 
ATOM   6270 C  C4    . DC  B 2 3   ? -24.934 -15.882 -18.000 1.00 95.71  ? 3   DC  P C4    1 
ATOM   6271 N  N4    . DC  B 2 3   ? -26.252 -15.804 -17.792 1.00 95.35  ? 3   DC  P N4    1 
ATOM   6272 C  C5    . DC  B 2 3   ? -24.052 -16.152 -16.912 1.00 100.18 ? 3   DC  P C5    1 
ATOM   6273 C  C6    . DC  B 2 3   ? -22.743 -16.220 -17.176 1.00 104.06 ? 3   DC  P C6    1 
ATOM   6274 P  P     . DC  B 2 4   ? -16.755 -14.662 -18.694 1.00 126.02 ? 4   DC  P P     1 
ATOM   6275 O  OP1   . DC  B 2 4   ? -15.428 -15.292 -18.874 1.00 113.98 ? 4   DC  P OP1   1 
ATOM   6276 O  OP2   . DC  B 2 4   ? -17.072 -13.948 -17.438 1.00 124.23 ? 4   DC  P OP2   1 
ATOM   6277 O  "O5'" . DC  B 2 4   ? -17.024 -13.662 -19.908 1.00 116.19 ? 4   DC  P "O5'" 1 
ATOM   6278 C  "C5'" . DC  B 2 4   ? -17.549 -14.168 -21.128 1.00 112.30 ? 4   DC  P "C5'" 1 
ATOM   6279 C  "C4'" . DC  B 2 4   ? -18.392 -13.119 -21.824 1.00 103.99 ? 4   DC  P "C4'" 1 
ATOM   6280 O  "O4'" . DC  B 2 4   ? -19.779 -13.244 -21.410 1.00 100.94 ? 4   DC  P "O4'" 1 
ATOM   6281 C  "C3'" . DC  B 2 4   ? -17.994 -11.674 -21.523 1.00 104.99 ? 4   DC  P "C3'" 1 
ATOM   6282 O  "O3'" . DC  B 2 4   ? -18.077 -10.910 -22.708 1.00 106.31 ? 4   DC  P "O3'" 1 
ATOM   6283 C  "C2'" . DC  B 2 4   ? -19.048 -11.236 -20.508 1.00 104.86 ? 4   DC  P "C2'" 1 
ATOM   6284 C  "C1'" . DC  B 2 4   ? -20.258 -11.970 -21.047 1.00 98.65  ? 4   DC  P "C1'" 1 
ATOM   6285 N  N1    . DC  B 2 4   ? -21.375 -12.131 -20.073 1.00 92.09  ? 4   DC  P N1    1 
ATOM   6286 C  C2    . DC  B 2 4   ? -22.684 -11.990 -20.524 1.00 87.11  ? 4   DC  P C2    1 
ATOM   6287 O  O2    . DC  B 2 4   ? -22.869 -11.737 -21.718 1.00 85.50  ? 4   DC  P O2    1 
ATOM   6288 N  N3    . DC  B 2 4   ? -23.706 -12.141 -19.647 1.00 85.17  ? 4   DC  P N3    1 
ATOM   6289 C  C4    . DC  B 2 4   ? -23.450 -12.419 -18.368 1.00 87.99  ? 4   DC  P C4    1 
ATOM   6290 N  N4    . DC  B 2 4   ? -24.491 -12.559 -17.537 1.00 81.27  ? 4   DC  P N4    1 
ATOM   6291 C  C5    . DC  B 2 4   ? -22.115 -12.567 -17.885 1.00 93.61  ? 4   DC  P C5    1 
ATOM   6292 C  C6    . DC  B 2 4   ? -21.116 -12.415 -18.765 1.00 96.75  ? 4   DC  P C6    1 
ATOM   6293 P  P     . DA  B 2 5   ? -17.069 -9.685  -22.952 1.00 115.32 ? 5   DA  P P     1 
ATOM   6294 O  OP1   . DA  B 2 5   ? -15.852 -10.230 -23.594 1.00 117.24 ? 5   DA  P OP1   1 
ATOM   6295 O  OP2   . DA  B 2 5   ? -16.965 -8.934  -21.681 1.00 106.03 ? 5   DA  P OP2   1 
ATOM   6296 O  "O5'" . DA  B 2 5   ? -17.844 -8.769  -24.005 1.00 102.61 ? 5   DA  P "O5'" 1 
ATOM   6297 C  "C5'" . DA  B 2 5   ? -18.306 -9.333  -25.222 1.00 95.42  ? 5   DA  P "C5'" 1 
ATOM   6298 C  "C4'" . DA  B 2 5   ? -19.604 -8.682  -25.674 1.00 98.44  ? 5   DA  P "C4'" 1 
ATOM   6299 O  "O4'" . DA  B 2 5   ? -20.666 -8.978  -24.731 1.00 93.92  ? 5   DA  P "O4'" 1 
ATOM   6300 C  "C3'" . DA  B 2 5   ? -19.573 -7.165  -25.797 1.00 97.93  ? 5   DA  P "C3'" 1 
ATOM   6301 O  "O3'" . DA  B 2 5   ? -20.423 -6.777  -26.862 1.00 99.20  ? 5   DA  P "O3'" 1 
ATOM   6302 C  "C2'" . DA  B 2 5   ? -20.118 -6.707  -24.442 1.00 92.10  ? 5   DA  P "C2'" 1 
ATOM   6303 C  "C1'" . DA  B 2 5   ? -21.163 -7.779  -24.160 1.00 93.69  ? 5   DA  P "C1'" 1 
ATOM   6304 N  N9    . DA  B 2 5   ? -21.401 -8.037  -22.741 1.00 88.62  ? 5   DA  P N9    1 
ATOM   6305 C  C8    . DA  B 2 5   ? -20.464 -8.338  -21.791 1.00 93.22  ? 5   DA  P C8    1 
ATOM   6306 N  N7    . DA  B 2 5   ? -20.969 -8.557  -20.599 1.00 88.36  ? 5   DA  P N7    1 
ATOM   6307 C  C5    . DA  B 2 5   ? -22.333 -8.404  -20.782 1.00 84.97  ? 5   DA  P C5    1 
ATOM   6308 C  C6    . DA  B 2 5   ? -23.427 -8.507  -19.898 1.00 80.03  ? 5   DA  P C6    1 
ATOM   6309 N  N6    . DA  B 2 5   ? -23.297 -8.802  -18.601 1.00 78.92  ? 5   DA  P N6    1 
ATOM   6310 N  N1    . DA  B 2 5   ? -24.662 -8.294  -20.401 1.00 78.18  ? 5   DA  P N1    1 
ATOM   6311 C  C2    . DA  B 2 5   ? -24.785 -7.997  -21.702 1.00 79.84  ? 5   DA  P C2    1 
ATOM   6312 N  N3    . DA  B 2 5   ? -23.833 -7.873  -22.629 1.00 80.16  ? 5   DA  P N3    1 
ATOM   6313 C  C4    . DA  B 2 5   ? -22.619 -8.091  -22.098 1.00 84.08  ? 5   DA  P C4    1 
ATOM   6314 P  P     . DC  B 2 6   ? -20.274 -5.336  -27.554 1.00 117.77 ? 6   DC  P P     1 
ATOM   6315 O  OP1   . DC  B 2 6   ? -20.048 -5.556  -28.999 1.00 108.91 ? 6   DC  P OP1   1 
ATOM   6316 O  OP2   . DC  B 2 6   ? -19.309 -4.540  -26.763 1.00 110.09 ? 6   DC  P OP2   1 
ATOM   6317 O  "O5'" . DC  B 2 6   ? -21.719 -4.690  -27.358 1.00 105.70 ? 6   DC  P "O5'" 1 
ATOM   6318 C  "C5'" . DC  B 2 6   ? -22.769 -5.472  -26.802 1.00 98.37  ? 6   DC  P "C5'" 1 
ATOM   6319 C  "C4'" . DC  B 2 6   ? -23.777 -4.586  -26.101 1.00 95.39  ? 6   DC  P "C4'" 1 
ATOM   6320 O  "O4'" . DC  B 2 6   ? -23.931 -5.016  -24.719 1.00 93.09  ? 6   DC  P "O4'" 1 
ATOM   6321 C  "C3'" . DC  B 2 6   ? -23.389 -3.107  -26.030 1.00 94.47  ? 6   DC  P "C3'" 1 
ATOM   6322 O  "O3'" . DC  B 2 6   ? -24.553 -2.311  -26.150 1.00 93.96  ? 6   DC  P "O3'" 1 
ATOM   6323 C  "C2'" . DC  B 2 6   ? -22.797 -2.999  -24.631 1.00 90.02  ? 6   DC  P "C2'" 1 
ATOM   6324 C  "C1'" . DC  B 2 6   ? -23.765 -3.892  -23.885 1.00 85.42  ? 6   DC  P "C1'" 1 
ATOM   6325 N  N1    . DC  B 2 6   ? -23.300 -4.333  -22.539 1.00 81.70  ? 6   DC  P N1    1 
ATOM   6326 C  C2    . DC  B 2 6   ? -24.248 -4.554  -21.540 1.00 77.93  ? 6   DC  P C2    1 
ATOM   6327 O  O2    . DC  B 2 6   ? -25.442 -4.388  -21.812 1.00 73.54  ? 6   DC  P O2    1 
ATOM   6328 N  N3    . DC  B 2 6   ? -23.832 -4.950  -20.312 1.00 79.84  ? 6   DC  P N3    1 
ATOM   6329 C  C4    . DC  B 2 6   ? -22.530 -5.118  -20.072 1.00 74.03  ? 6   DC  P C4    1 
ATOM   6330 N  N4    . DC  B 2 6   ? -22.165 -5.509  -18.846 1.00 73.01  ? 6   DC  P N4    1 
ATOM   6331 C  C5    . DC  B 2 6   ? -21.544 -4.891  -21.080 1.00 78.38  ? 6   DC  P C5    1 
ATOM   6332 C  C6    . DC  B 2 6   ? -21.971 -4.501  -22.288 1.00 80.35  ? 6   DC  P C6    1 
ATOM   6333 P  P     . DG  B 2 7   ? -24.773 -1.383  -27.439 1.00 92.74  ? 7   DG  P P     1 
ATOM   6334 O  OP1   . DG  B 2 7   ? -24.376 -2.160  -28.634 1.00 111.51 ? 7   DG  P OP1   1 
ATOM   6335 O  OP2   . DG  B 2 7   ? -24.120 -0.086  -27.154 1.00 90.65  ? 7   DG  P OP2   1 
ATOM   6336 O  "O5'" . DG  B 2 7   ? -26.358 -1.164  -27.483 1.00 99.36  ? 7   DG  P "O5'" 1 
ATOM   6337 C  "C5'" . DG  B 2 7   ? -26.919 0.027   -26.950 1.00 101.80 ? 7   DG  P "C5'" 1 
ATOM   6338 C  "C4'" . DG  B 2 7   ? -28.082 -0.273  -26.021 1.00 94.35  ? 7   DG  P "C4'" 1 
ATOM   6339 O  "O4'" . DG  B 2 7   ? -27.630 -1.089  -24.908 1.00 86.17  ? 7   DG  P "O4'" 1 
ATOM   6340 C  "C3'" . DG  B 2 7   ? -28.699 0.955   -25.380 1.00 91.13  ? 7   DG  P "C3'" 1 
ATOM   6341 O  "O3'" . DG  B 2 7   ? -30.047 0.701   -25.065 1.00 85.33  ? 7   DG  P "O3'" 1 
ATOM   6342 C  "C2'" . DG  B 2 7   ? -27.854 1.120   -24.122 1.00 88.22  ? 7   DG  P "C2'" 1 
ATOM   6343 C  "C1'" . DG  B 2 7   ? -27.662 -0.332  -23.706 1.00 84.52  ? 7   DG  P "C1'" 1 
ATOM   6344 N  N9    . DG  B 2 7   ? -26.420 -0.587  -22.982 1.00 81.09  ? 7   DG  P N9    1 
ATOM   6345 C  C8    . DG  B 2 7   ? -25.156 -0.638  -23.516 1.00 82.36  ? 7   DG  P C8    1 
ATOM   6346 N  N7    . DG  B 2 7   ? -24.231 -0.904  -22.640 1.00 74.90  ? 7   DG  P N7    1 
ATOM   6347 C  C5    . DG  B 2 7   ? -24.921 -1.051  -21.447 1.00 73.13  ? 7   DG  P C5    1 
ATOM   6348 C  C6    . DG  B 2 7   ? -24.437 -1.349  -20.154 1.00 72.46  ? 7   DG  P C6    1 
ATOM   6349 O  O6    . DG  B 2 7   ? -23.266 -1.544  -19.804 1.00 66.81  ? 7   DG  P O6    1 
ATOM   6350 N  N1    . DG  B 2 7   ? -25.465 -1.404  -19.218 1.00 70.47  ? 7   DG  P N1    1 
ATOM   6351 C  C2    . DG  B 2 7   ? -26.797 -1.202  -19.498 1.00 73.87  ? 7   DG  P C2    1 
ATOM   6352 N  N2    . DG  B 2 7   ? -27.644 -1.298  -18.462 1.00 68.61  ? 7   DG  P N2    1 
ATOM   6353 N  N3    . DG  B 2 7   ? -27.267 -0.921  -20.712 1.00 76.75  ? 7   DG  P N3    1 
ATOM   6354 C  C4    . DG  B 2 7   ? -26.273 -0.862  -21.635 1.00 75.13  ? 7   DG  P C4    1 
ATOM   6355 P  P     . DG  B 2 8   ? -31.053 1.933   -24.879 1.00 88.05  ? 8   DG  P P     1 
ATOM   6356 O  OP1   . DG  B 2 8   ? -32.436 1.411   -24.971 1.00 89.00  ? 8   DG  P OP1   1 
ATOM   6357 O  OP2   . DG  B 2 8   ? -30.588 2.992   -25.800 1.00 90.39  ? 8   DG  P OP2   1 
ATOM   6358 O  "O5'" . DG  B 2 8   ? -30.772 2.428   -23.386 1.00 81.13  ? 8   DG  P "O5'" 1 
ATOM   6359 C  "C5'" . DG  B 2 8   ? -30.987 1.540   -22.302 1.00 79.74  ? 8   DG  P "C5'" 1 
ATOM   6360 C  "C4'" . DG  B 2 8   ? -30.526 2.159   -20.996 1.00 78.66  ? 8   DG  P "C4'" 1 
ATOM   6361 O  "O4'" . DG  B 2 8   ? -29.182 1.724   -20.694 1.00 74.98  ? 8   DG  P "O4'" 1 
ATOM   6362 C  "C3'" . DG  B 2 8   ? -30.503 3.691   -20.971 1.00 77.83  ? 8   DG  P "C3'" 1 
ATOM   6363 O  "O3'" . DG  B 2 8   ? -31.304 4.154   -19.891 1.00 78.26  ? 8   DG  P "O3'" 1 
ATOM   6364 C  "C2'" . DG  B 2 8   ? -29.017 4.039   -20.777 1.00 72.61  ? 8   DG  P "C2'" 1 
ATOM   6365 C  "C1'" . DG  B 2 8   ? -28.487 2.787   -20.099 1.00 69.66  ? 8   DG  P "C1'" 1 
ATOM   6366 N  N9    . DG  B 2 8   ? -27.058 2.554   -20.289 1.00 71.91  ? 8   DG  P N9    1 
ATOM   6367 C  C8    . DG  B 2 8   ? -26.351 2.609   -21.467 1.00 73.29  ? 8   DG  P C8    1 
ATOM   6368 N  N7    . DG  B 2 8   ? -25.082 2.333   -21.324 1.00 72.41  ? 8   DG  P N7    1 
ATOM   6369 C  C5    . DG  B 2 8   ? -24.942 2.071   -19.967 1.00 70.63  ? 8   DG  P C5    1 
ATOM   6370 C  C6    . DG  B 2 8   ? -23.795 1.715   -19.216 1.00 66.01  ? 8   DG  P C6    1 
ATOM   6371 O  O6    . DG  B 2 8   ? -22.634 1.553   -19.615 1.00 63.57  ? 8   DG  P O6    1 
ATOM   6372 N  N1    . DG  B 2 8   ? -24.098 1.541   -17.867 1.00 61.99  ? 8   DG  P N1    1 
ATOM   6373 C  C2    . DG  B 2 8   ? -25.349 1.693   -17.317 1.00 63.71  ? 8   DG  P C2    1 
ATOM   6374 N  N2    . DG  B 2 8   ? -25.457 1.490   -15.999 1.00 62.28  ? 8   DG  P N2    1 
ATOM   6375 N  N3    . DG  B 2 8   ? -26.426 2.027   -18.009 1.00 67.32  ? 8   DG  P N3    1 
ATOM   6376 C  C4    . DG  B 2 8   ? -26.151 2.199   -19.320 1.00 72.08  ? 8   DG  P C4    1 
ATOM   6377 P  P     . DC  B 2 9   ? -31.677 5.710   -19.745 1.00 75.82  ? 9   DC  P P     1 
ATOM   6378 O  OP1   . DC  B 2 9   ? -33.130 5.782   -19.467 1.00 81.18  ? 9   DC  P OP1   1 
ATOM   6379 O  OP2   . DC  B 2 9   ? -31.109 6.451   -20.894 1.00 71.81  ? 9   DC  P OP2   1 
ATOM   6380 O  "O5'" . DC  B 2 9   ? -30.916 6.144   -18.409 1.00 64.41  ? 9   DC  P "O5'" 1 
ATOM   6381 C  "C5'" . DC  B 2 9   ? -31.111 5.390   -17.220 1.00 64.89  ? 9   DC  P "C5'" 1 
ATOM   6382 C  "C4'" . DC  B 2 9   ? -30.088 5.764   -16.166 1.00 67.64  ? 9   DC  P "C4'" 1 
ATOM   6383 O  "O4'" . DC  B 2 9   ? -28.803 5.210   -16.515 1.00 63.17  ? 9   DC  P "O4'" 1 
ATOM   6384 C  "C3'" . DC  B 2 9   ? -29.876 7.267   -15.979 1.00 63.39  ? 9   DC  P "C3'" 1 
ATOM   6385 O  "O3'" . DC  B 2 9   ? -30.302 7.646   -14.680 1.00 63.05  ? 9   DC  P "O3'" 1 
ATOM   6386 C  "C2'" . DC  B 2 9   ? -28.365 7.479   -16.175 1.00 61.85  ? 9   DC  P "C2'" 1 
ATOM   6387 C  "C1'" . DC  B 2 9   ? -27.794 6.070   -16.057 1.00 68.11  ? 9   DC  P "C1'" 1 
ATOM   6388 N  N1    . DC  B 2 9   ? -26.578 5.836   -16.901 1.00 68.73  ? 9   DC  P N1    1 
ATOM   6389 C  C2    . DC  B 2 9   ? -25.375 5.428   -16.303 1.00 65.61  ? 9   DC  P C2    1 
ATOM   6390 O  O2    . DC  B 2 9   ? -25.332 5.282   -15.076 1.00 66.07  ? 9   DC  P O2    1 
ATOM   6391 N  N3    . DC  B 2 9   ? -24.290 5.212   -17.092 1.00 56.12  ? 9   DC  P N3    1 
ATOM   6392 C  C4    . DC  B 2 9   ? -24.381 5.382   -18.414 1.00 63.31  ? 9   DC  P C4    1 
ATOM   6393 N  N4    . DC  B 2 9   ? -23.291 5.159   -19.156 1.00 56.88  ? 9   DC  P N4    1 
ATOM   6394 C  C5    . DC  B 2 9   ? -25.597 5.791   -19.037 1.00 60.63  ? 9   DC  P C5    1 
ATOM   6395 C  C6    . DC  B 2 9   ? -26.658 6.002   -18.252 1.00 65.01  ? 9   DC  P C6    1 
ATOM   6396 P  P     . DC  B 2 10  ? -30.475 9.195   -14.295 1.00 69.34  ? 10  DC  P P     1 
ATOM   6397 O  OP1   . DC  B 2 10  ? -31.577 9.283   -13.311 1.00 66.55  ? 10  DC  P OP1   1 
ATOM   6398 O  OP2   . DC  B 2 10  ? -30.503 9.991   -15.542 1.00 67.42  ? 10  DC  P OP2   1 
ATOM   6399 O  "O5'" . DC  B 2 10  ? -29.124 9.533   -13.528 1.00 62.61  ? 10  DC  P "O5'" 1 
ATOM   6400 C  "C5'" . DC  B 2 10  ? -28.708 8.695   -12.473 1.00 62.38  ? 10  DC  P "C5'" 1 
ATOM   6401 C  "C4'" . DC  B 2 10  ? -27.222 8.826   -12.248 1.00 62.11  ? 10  DC  P "C4'" 1 
ATOM   6402 O  "O4'" . DC  B 2 10  ? -26.513 8.360   -13.415 1.00 61.20  ? 10  DC  P "O4'" 1 
ATOM   6403 C  "C3'" . DC  B 2 10  ? -26.736 10.259  -12.004 1.00 59.52  ? 10  DC  P "C3'" 1 
ATOM   6404 O  "O3'" . DC  B 2 10  ? -26.216 10.366  -10.693 1.00 56.24  ? 10  DC  P "O3'" 1 
ATOM   6405 C  "C2'" . DC  B 2 10  ? -25.649 10.482  -13.068 1.00 54.67  ? 10  DC  P "C2'" 1 
ATOM   6406 C  "C1'" . DC  B 2 10  ? -25.306 9.060   -13.484 1.00 64.99  ? 10  DC  P "C1'" 1 
ATOM   6407 N  N1    . DC  B 2 10  ? -24.759 8.955   -14.863 1.00 62.98  ? 10  DC  P N1    1 
ATOM   6408 C  C2    . DC  B 2 10  ? -23.442 8.535   -15.041 1.00 63.00  ? 10  DC  P C2    1 
ATOM   6409 O  O2    . DC  B 2 10  ? -22.765 8.263   -14.042 1.00 60.93  ? 10  DC  P O2    1 
ATOM   6410 N  N3    . DC  B 2 10  ? -22.940 8.453   -16.298 1.00 58.80  ? 10  DC  P N3    1 
ATOM   6411 C  C4    . DC  B 2 10  ? -23.709 8.765   -17.343 1.00 59.97  ? 10  DC  P C4    1 
ATOM   6412 N  N4    . DC  B 2 10  ? -23.176 8.665   -18.566 1.00 48.50  ? 10  DC  P N4    1 
ATOM   6413 C  C5    . DC  B 2 10  ? -25.059 9.194   -17.180 1.00 61.79  ? 10  DC  P C5    1 
ATOM   6414 C  C6    . DC  B 2 10  ? -25.536 9.278   -15.934 1.00 61.94  ? 10  DC  P C6    1 
ATOM   6415 P  P     . DA  B 2 11  ? -25.928 11.806  -10.045 1.00 59.53  ? 11  DA  P P     1 
ATOM   6416 O  OP1   . DA  B 2 11  ? -26.515 11.802  -8.686  1.00 66.49  ? 11  DA  P OP1   1 
ATOM   6417 O  OP2   . DA  B 2 11  ? -26.327 12.840  -11.026 1.00 75.33  ? 11  DA  P OP2   1 
ATOM   6418 O  "O5'" . DA  B 2 11  ? -24.336 11.845  -9.916  1.00 63.71  ? 11  DA  P "O5'" 1 
ATOM   6419 C  "C5'" . DA  B 2 11  ? -23.653 10.747  -9.332  1.00 63.85  ? 11  DA  P "C5'" 1 
ATOM   6420 C  "C4'" . DA  B 2 11  ? -22.220 10.681  -9.820  1.00 65.13  ? 11  DA  P "C4'" 1 
ATOM   6421 O  "O4'" . DA  B 2 11  ? -22.197 10.336  -11.221 1.00 64.05  ? 11  DA  P "O4'" 1 
ATOM   6422 C  "C3'" . DA  B 2 11  ? -21.436 11.989  -9.694  1.00 58.91  ? 11  DA  P "C3'" 1 
ATOM   6423 O  "O3'" . DA  B 2 11  ? -20.393 11.832  -8.749  1.00 63.66  ? 11  DA  P "O3'" 1 
ATOM   6424 C  "C2'" . DA  B 2 11  ? -20.888 12.258  -11.106 1.00 56.76  ? 11  DA  P "C2'" 1 
ATOM   6425 C  "C1'" . DA  B 2 11  ? -21.059 10.914  -11.799 1.00 59.02  ? 11  DA  P "C1'" 1 
ATOM   6426 N  N9    . DA  B 2 11  ? -21.274 11.018  -13.241 1.00 63.09  ? 11  DA  P N9    1 
ATOM   6427 C  C8    . DA  B 2 11  ? -22.446 11.310  -13.881 1.00 56.73  ? 11  DA  P C8    1 
ATOM   6428 N  N7    . DA  B 2 11  ? -22.344 11.331  -15.190 1.00 55.50  ? 11  DA  P N7    1 
ATOM   6429 C  C5    . DA  B 2 11  ? -21.012 11.031  -15.424 1.00 56.44  ? 11  DA  P C5    1 
ATOM   6430 C  C6    . DA  B 2 11  ? -20.262 10.899  -16.610 1.00 56.36  ? 11  DA  P C6    1 
ATOM   6431 N  N6    . DA  B 2 11  ? -20.780 11.059  -17.832 1.00 58.06  ? 11  DA  P N6    1 
ATOM   6432 N  N1    . DA  B 2 11  ? -18.953 10.595  -16.490 1.00 60.39  ? 11  DA  P N1    1 
ATOM   6433 C  C2    . DA  B 2 11  ? -18.437 10.435  -15.265 1.00 57.95  ? 11  DA  P C2    1 
ATOM   6434 N  N3    . DA  B 2 11  ? -19.041 10.532  -14.081 1.00 56.62  ? 11  DA  P N3    1 
ATOM   6435 C  C4    . DA  B 2 11  ? -20.339 10.835  -14.233 1.00 59.77  ? 11  DA  P C4    1 
ATOM   6436 P  P     . DC  B 2 12  ? -19.574 13.112  -8.234  1.00 63.17  ? 12  DC  P P     1 
ATOM   6437 O  OP1   . DC  B 2 12  ? -19.112 12.828  -6.856  1.00 55.75  ? 12  DC  P OP1   1 
ATOM   6438 O  OP2   . DC  B 2 12  ? -20.405 14.307  -8.502  1.00 68.15  ? 12  DC  P OP2   1 
ATOM   6439 O  "O5'" . DC  B 2 12  ? -18.311 13.174  -9.212  1.00 61.70  ? 12  DC  P "O5'" 1 
ATOM   6440 C  "C5'" . DC  B 2 12  ? -17.424 12.068  -9.296  1.00 57.18  ? 12  DC  P "C5'" 1 
ATOM   6441 C  "C4'" . DC  B 2 12  ? -16.150 12.454  -10.026 1.00 61.33  ? 12  DC  P "C4'" 1 
ATOM   6442 O  "O4'" . DC  B 2 12  ? -16.355 12.350  -11.457 1.00 58.33  ? 12  DC  P "O4'" 1 
ATOM   6443 C  "C3'" . DC  B 2 12  ? -15.663 13.876  -9.765  1.00 70.07  ? 12  DC  P "C3'" 1 
ATOM   6444 O  "O3'" . DC  B 2 12  ? -14.249 13.887  -9.673  1.00 70.84  ? 12  DC  P "O3'" 1 
ATOM   6445 C  "C2'" . DC  B 2 12  ? -16.160 14.650  -10.987 1.00 64.16  ? 12  DC  P "C2'" 1 
ATOM   6446 C  "C1'" . DC  B 2 12  ? -16.098 13.592  -12.081 1.00 64.73  ? 12  DC  P "C1'" 1 
ATOM   6447 N  N1    . DC  B 2 12  ? -17.114 13.777  -13.155 1.00 59.93  ? 12  DC  P N1    1 
ATOM   6448 C  C2    . DC  B 2 12  ? -16.721 13.733  -14.495 1.00 57.50  ? 12  DC  P C2    1 
ATOM   6449 O  O2    . DC  B 2 12  ? -15.528 13.556  -14.767 1.00 57.30  ? 12  DC  P O2    1 
ATOM   6450 N  N3    . DC  B 2 12  ? -17.661 13.889  -15.460 1.00 59.46  ? 12  DC  P N3    1 
ATOM   6451 C  C4    . DC  B 2 12  ? -18.938 14.078  -15.125 1.00 55.40  ? 12  DC  P C4    1 
ATOM   6452 N  N4    . DC  B 2 12  ? -19.829 14.227  -16.111 1.00 48.38  ? 12  DC  P N4    1 
ATOM   6453 C  C5    . DC  B 2 12  ? -19.359 14.121  -13.763 1.00 54.57  ? 12  DC  P C5    1 
ATOM   6454 C  C6    . DC  B 2 12  ? -18.422 13.966  -12.821 1.00 58.58  ? 12  DC  P C6    1 
ATOM   6455 P  P     . DA  B 2 13  ? -13.498 15.051  -8.859  1.00 71.25  ? 13  DA  P P     1 
ATOM   6456 O  OP1   . DA  B 2 13  ? -12.474 14.401  -8.008  1.00 70.40  ? 13  DA  P OP1   1 
ATOM   6457 O  OP2   . DA  B 2 13  ? -14.522 15.932  -8.253  1.00 69.38  ? 13  DA  P OP2   1 
ATOM   6458 O  "O5'" . DA  B 2 13  ? -12.765 15.885  -10.004 1.00 62.02  ? 13  DA  P "O5'" 1 
ATOM   6459 C  "C5'" . DA  B 2 13  ? -12.150 15.196  -11.070 1.00 57.71  ? 13  DA  P "C5'" 1 
ATOM   6460 C  "C4'" . DA  B 2 13  ? -11.765 16.144  -12.185 1.00 62.36  ? 13  DA  P "C4'" 1 
ATOM   6461 O  "O4'" . DA  B 2 13  ? -12.443 15.754  -13.402 1.00 65.48  ? 13  DA  P "O4'" 1 
ATOM   6462 C  "C3'" . DA  B 2 13  ? -12.178 17.587  -11.974 1.00 64.49  ? 13  DA  P "C3'" 1 
ATOM   6463 O  "O3'" . DA  B 2 13  ? -11.231 18.257  -11.156 1.00 58.73  ? 13  DA  P "O3'" 1 
ATOM   6464 C  "C2'" . DA  B 2 13  ? -12.161 18.113  -13.404 1.00 54.48  ? 13  DA  P "C2'" 1 
ATOM   6465 C  "C1'" . DA  B 2 13  ? -12.690 16.905  -14.190 1.00 57.15  ? 13  DA  P "C1'" 1 
ATOM   6466 N  N9    . DA  B 2 13  ? -14.118 16.993  -14.485 1.00 58.70  ? 13  DA  P N9    1 
ATOM   6467 C  C8    . DA  B 2 13  ? -15.143 17.116  -13.587 1.00 53.85  ? 13  DA  P C8    1 
ATOM   6468 N  N7    . DA  B 2 13  ? -16.329 17.195  -14.146 1.00 57.80  ? 13  DA  P N7    1 
ATOM   6469 C  C5    . DA  B 2 13  ? -16.062 17.126  -15.503 1.00 53.74  ? 13  DA  P C5    1 
ATOM   6470 C  C6    . DA  B 2 13  ? -16.896 17.154  -16.638 1.00 52.00  ? 13  DA  P C6    1 
ATOM   6471 N  N6    . DA  B 2 13  ? -18.226 17.267  -16.571 1.00 58.30  ? 13  DA  P N6    1 
ATOM   6472 N  N1    . DA  B 2 13  ? -16.307 17.063  -17.849 1.00 55.09  ? 13  DA  P N1    1 
ATOM   6473 C  C2    . DA  B 2 13  ? -14.974 16.953  -17.913 1.00 51.77  ? 13  DA  P C2    1 
ATOM   6474 N  N3    . DA  B 2 13  ? -14.089 16.915  -16.919 1.00 52.00  ? 13  DA  P N3    1 
ATOM   6475 C  C4    . DA  B 2 13  ? -14.703 17.006  -15.729 1.00 55.55  ? 13  DA  P C4    1 
HETATM 6476 O  "O5'" . 6HA C 3 1   ? -29.748 19.467  -17.708 1.00 107.47 ? 1   6HA T "O5'" 1 
HETATM 6477 C  "C5'" . 6HA C 3 1   ? -30.952 19.737  -18.376 1.00 103.33 ? 1   6HA T "C5'" 1 
HETATM 6478 C  "C4'" . 6HA C 3 1   ? -31.437 18.476  -19.059 1.00 104.78 ? 1   6HA T "C4'" 1 
HETATM 6479 O  "O4'" . 6HA C 3 1   ? -32.876 18.559  -19.260 1.00 102.38 ? 1   6HA T "O4'" 1 
HETATM 6480 C  "C3'" . 6HA C 3 1   ? -30.726 18.318  -20.413 1.00 103.31 ? 1   6HA T "C3'" 1 
HETATM 6481 O  "O3'" . 6HA C 3 1   ? -29.307 18.125  -20.209 1.00 114.44 ? 1   6HA T "O3'" 1 
HETATM 6482 C  "C2'" . 6HA C 3 1   ? -31.287 17.146  -21.152 1.00 94.71  ? 1   6HA T "C2'" 1 
HETATM 6483 C  "C1'" . 6HA C 3 1   ? -32.746 16.964  -21.252 1.00 101.98 ? 1   6HA T "C1'" 1 
HETATM 6484 C  "C6'" . 6HA C 3 1   ? -33.478 17.375  -19.965 1.00 103.59 ? 1   6HA T "C6'" 1 
HETATM 6485 N  N9    . 6HA C 3 1   ? -33.210 17.615  -22.569 1.00 106.69 ? 1   6HA T N9    1 
HETATM 6486 C  C8    . 6HA C 3 1   ? -33.098 17.257  -23.842 1.00 99.13  ? 1   6HA T C8    1 
HETATM 6487 N  N7    . 6HA C 3 1   ? -33.666 18.190  -24.620 1.00 96.86  ? 1   6HA T N7    1 
HETATM 6488 C  C5    . 6HA C 3 1   ? -34.140 19.141  -23.817 1.00 86.93  ? 1   6HA T C5    1 
HETATM 6489 C  C6    . 6HA C 3 1   ? -34.804 20.300  -24.106 1.00 80.93  ? 1   6HA T C6    1 
HETATM 6490 N  N6    . 6HA C 3 1   ? -35.186 20.829  -25.398 1.00 79.84  ? 1   6HA T N6    1 
HETATM 6491 N  N1    . 6HA C 3 1   ? -35.200 21.131  -23.141 1.00 77.45  ? 1   6HA T N1    1 
HETATM 6492 C  C2    . 6HA C 3 1   ? -34.932 20.816  -21.865 1.00 81.60  ? 1   6HA T C2    1 
HETATM 6493 N  N3    . 6HA C 3 1   ? -34.277 19.674  -21.577 1.00 81.17  ? 1   6HA T N3    1 
HETATM 6494 C  C4    . 6HA C 3 1   ? -33.868 18.811  -22.546 1.00 88.12  ? 1   6HA T C4    1 
HETATM 6495 P  P     . 6HA C 3 2   ? -28.189 19.107  -20.673 1.00 111.49 ? 2   6HA T P     1 
HETATM 6496 O  OP1   . 6HA C 3 2   ? -27.182 19.242  -19.541 1.00 97.31  ? 2   6HA T OP1   1 
HETATM 6497 O  OP2   . 6HA C 3 2   ? -28.646 20.479  -21.099 1.00 94.09  ? 2   6HA T OP2   1 
HETATM 6498 O  "O5'" . 6HA C 3 2   ? -27.495 18.349  -21.944 1.00 84.09  ? 2   6HA T "O5'" 1 
HETATM 6499 C  "C5'" . 6HA C 3 2   ? -27.063 19.122  -23.033 1.00 79.66  ? 2   6HA T "C5'" 1 
HETATM 6500 C  "C4'" . 6HA C 3 2   ? -27.930 18.847  -24.244 1.00 72.36  ? 2   6HA T "C4'" 1 
HETATM 6501 O  "O4'" . 6HA C 3 2   ? -29.181 18.250  -23.802 1.00 83.85  ? 2   6HA T "O4'" 1 
HETATM 6502 C  "C3'" . 6HA C 3 2   ? -28.121 20.160  -25.029 1.00 70.34  ? 2   6HA T "C3'" 1 
HETATM 6503 O  "O3'" . 6HA C 3 2   ? -26.903 20.434  -25.757 1.00 74.75  ? 2   6HA T "O3'" 1 
HETATM 6504 C  "C2'" . 6HA C 3 2   ? -29.259 20.159  -26.003 1.00 71.26  ? 2   6HA T "C2'" 1 
HETATM 6505 C  "C1'" . 6HA C 3 2   ? -30.508 19.574  -25.506 1.00 73.74  ? 2   6HA T "C1'" 1 
HETATM 6506 C  "C6'" . 6HA C 3 2   ? -30.153 18.197  -24.948 1.00 79.03  ? 2   6HA T "C6'" 1 
HETATM 6507 N  N9    . 6HA C 3 2   ? -31.078 20.452  -24.400 1.00 75.72  ? 2   6HA T N9    1 
HETATM 6508 C  C8    . 6HA C 3 2   ? -31.107 20.499  -23.076 1.00 80.30  ? 2   6HA T C8    1 
HETATM 6509 N  N7    . 6HA C 3 2   ? -31.809 21.586  -22.707 1.00 76.44  ? 2   6HA T N7    1 
HETATM 6510 C  C5    . 6HA C 3 2   ? -32.212 22.209  -23.819 1.00 70.47  ? 2   6HA T C5    1 
HETATM 6511 C  C6    . 6HA C 3 2   ? -32.948 23.350  -24.019 1.00 71.84  ? 2   6HA T C6    1 
HETATM 6512 N  N6    . 6HA C 3 2   ? -33.537 24.261  -23.047 1.00 56.03  ? 2   6HA T N6    1 
HETATM 6513 N  N1    . 6HA C 3 2   ? -33.217 23.766  -25.262 1.00 72.93  ? 2   6HA T N1    1 
HETATM 6514 C  C2    . 6HA C 3 2   ? -32.762 23.062  -26.317 1.00 68.89  ? 2   6HA T C2    1 
HETATM 6515 N  N3    . 6HA C 3 2   ? -32.037 21.939  -26.125 1.00 60.68  ? 2   6HA T N3    1 
HETATM 6516 C  C4    . 6HA C 3 2   ? -31.762 21.513  -24.869 1.00 65.67  ? 2   6HA T C4    1 
HETATM 6517 P  P     . 6HC C 3 3   ? -26.218 21.804  -25.469 1.00 67.41  ? 3   6HC T P     1 
HETATM 6518 O  OP1   . 6HC C 3 3   ? -25.706 21.897  -24.050 1.00 48.35  ? 3   6HC T OP1   1 
HETATM 6519 O  OP2   . 6HC C 3 3   ? -27.008 23.043  -25.811 1.00 49.50  ? 3   6HC T OP2   1 
HETATM 6520 O  "O5'" . 6HC C 3 3   ? -24.954 21.678  -26.517 1.00 65.52  ? 3   6HC T "O5'" 1 
HETATM 6521 C  "C5'" . 6HC C 3 3   ? -23.900 20.827  -26.182 1.00 54.32  ? 3   6HC T "C5'" 1 
HETATM 6522 C  "C4'" . 6HC C 3 3   ? -22.648 21.630  -26.159 1.00 49.90  ? 3   6HC T "C4'" 1 
HETATM 6523 O  "O4'" . 6HC C 3 3   ? -22.907 22.837  -25.383 1.00 49.64  ? 3   6HC T "O4'" 1 
HETATM 6524 C  "C3'" . 6HC C 3 3   ? -21.525 20.749  -25.560 1.00 56.61  ? 3   6HC T "C3'" 1 
HETATM 6525 O  "O3'" . 6HC C 3 3   ? -21.211 19.703  -26.497 1.00 59.70  ? 3   6HC T "O3'" 1 
HETATM 6526 C  "C2'" . 6HC C 3 3   ? -20.317 21.516  -25.322 1.00 51.85  ? 3   6HC T "C2'" 1 
HETATM 6527 C  "C1'" . 6HC C 3 3   ? -20.526 22.751  -24.559 1.00 48.99  ? 3   6HC T "C1'" 1 
HETATM 6528 C  "C6'" . 6HC C 3 3   ? -21.715 23.611  -25.058 1.00 53.80  ? 3   6HC T "C6'" 1 
HETATM 6529 N  N1    . 6HC C 3 3   ? -20.742 22.391  -23.128 1.00 52.24  ? 3   6HC T N1    1 
HETATM 6530 C  C2    . 6HC C 3 3   ? -19.590 21.989  -22.292 1.00 46.88  ? 3   6HC T C2    1 
HETATM 6531 O  O2    . 6HC C 3 3   ? -18.504 21.946  -22.752 1.00 53.59  ? 3   6HC T O2    1 
HETATM 6532 N  N3    . 6HC C 3 3   ? -19.802 21.639  -20.872 1.00 46.75  ? 3   6HC T N3    1 
HETATM 6533 C  C4    . 6HC C 3 3   ? -21.109 21.674  -20.259 1.00 48.21  ? 3   6HC T C4    1 
HETATM 6534 N  N4    . 6HC C 3 3   ? -21.278 21.323  -18.859 1.00 51.99  ? 3   6HC T N4    1 
HETATM 6535 C  C5    . 6HC C 3 3   ? -22.274 22.075  -21.090 1.00 51.94  ? 3   6HC T C5    1 
HETATM 6536 C  C6    . 6HC C 3 3   ? -22.064 22.432  -22.525 1.00 53.56  ? 3   6HC T C6    1 
HETATM 6537 P  P     . 6HT C 3 4   ? -21.011 18.163  -26.384 1.00 52.44  ? 4   6HT T P     1 
HETATM 6538 O  OP1   . 6HT C 3 4   ? -22.039 17.227  -26.962 1.00 71.14  ? 4   6HT T OP1   1 
HETATM 6539 O  OP2   . 6HT C 3 4   ? -20.935 17.965  -24.897 1.00 54.94  ? 4   6HT T OP2   1 
HETATM 6540 O  "O5'" . 6HT C 3 4   ? -19.539 17.883  -27.079 1.00 68.08  ? 4   6HT T "O5'" 1 
HETATM 6541 C  "C5'" . 6HT C 3 4   ? -18.475 18.739  -26.771 1.00 53.05  ? 4   6HT T "C5'" 1 
HETATM 6542 C  "C4'" . 6HT C 3 4   ? -17.208 17.965  -26.707 1.00 57.10  ? 4   6HT T "C4'" 1 
HETATM 6543 O  "O4'" . 6HT C 3 4   ? -16.268 18.658  -25.828 1.00 62.61  ? 4   6HT T "O4'" 1 
HETATM 6544 C  "C3'" . 6HT C 3 4   ? -17.493 16.541  -26.163 1.00 61.53  ? 4   6HT T "C3'" 1 
HETATM 6545 O  "O3'" . 6HT C 3 4   ? -16.293 15.748  -26.320 1.00 60.11  ? 4   6HT T "O3'" 1 
HETATM 6546 C  "C2'" . 6HT C 3 4   ? -17.862 16.528  -24.742 1.00 59.88  ? 4   6HT T "C2'" 1 
HETATM 6547 C  "C1'" . 6HT C 3 4   ? -16.968 17.302  -23.867 1.00 59.10  ? 4   6HT T "C1'" 1 
HETATM 6548 C  "C6'" . 6HT C 3 4   ? -16.703 18.718  -24.425 1.00 54.31  ? 4   6HT T "C6'" 1 
HETATM 6549 N  N1    . 6HT C 3 4   ? -17.603 17.433  -22.521 1.00 53.50  ? 4   6HT T N1    1 
HETATM 6550 C  C2    . 6HT C 3 4   ? -16.772 17.314  -21.291 1.00 52.63  ? 4   6HT T C2    1 
HETATM 6551 O  O2    . 6HT C 3 4   ? -15.620 17.115  -21.383 1.00 59.68  ? 4   6HT T O2    1 
HETATM 6552 N  N3    . 6HT C 3 4   ? -17.437 17.449  -19.941 1.00 52.06  ? 4   6HT T N3    1 
HETATM 6553 C  C4    . 6HT C 3 4   ? -18.882 17.697  -19.824 1.00 53.20  ? 4   6HT T C4    1 
HETATM 6554 O  O4    . 6HT C 3 4   ? -19.395 17.801  -18.762 1.00 51.63  ? 4   6HT T O4    1 
HETATM 6555 C  C5    . 6HT C 3 4   ? -19.711 17.817  -21.070 1.00 52.34  ? 4   6HT T C5    1 
HETATM 6556 C  C5M   . 6HT C 3 4   ? -21.236 18.079  -20.967 1.00 45.16  ? 4   6HT T C5M   1 
HETATM 6557 C  C6    . 6HT C 3 4   ? -19.045 17.682  -22.412 1.00 50.97  ? 4   6HT T C6    1 
HETATM 6558 P  P     . 6HG C 3 5   ? -16.420 14.307  -26.900 1.00 68.38  ? 5   6HG T P     1 
HETATM 6559 O  OP1   . 6HG C 3 5   ? -16.414 14.359  -28.408 1.00 68.08  ? 5   6HG T OP1   1 
HETATM 6560 O  OP2   . 6HG C 3 5   ? -17.659 13.572  -26.450 1.00 70.71  ? 5   6HG T OP2   1 
HETATM 6561 O  "O5'" . 6HG C 3 5   ? -15.060 13.541  -26.362 1.00 69.54  ? 5   6HG T "O5'" 1 
HETATM 6562 C  "C5'" . 6HG C 3 5   ? -13.914 14.321  -26.170 1.00 66.51  ? 5   6HG T "C5'" 1 
HETATM 6563 C  "C4'" . 6HG C 3 5   ? -12.972 13.754  -25.154 1.00 66.11  ? 5   6HG T "C4'" 1 
HETATM 6564 O  "O4'" . 6HG C 3 5   ? -12.829 14.704  -24.056 1.00 63.89  ? 5   6HG T "O4'" 1 
HETATM 6565 C  "C3'" . 6HG C 3 5   ? -13.437 12.379  -24.594 1.00 75.74  ? 5   6HG T "C3'" 1 
HETATM 6566 O  "O3'" . 6HG C 3 5   ? -12.284 11.797  -23.951 1.00 92.17  ? 5   6HG T "O3'" 1 
HETATM 6567 C  "C2'" . 6HG C 3 5   ? -14.509 12.354  -23.609 1.00 70.77  ? 5   6HG T "C2'" 1 
HETATM 6568 C  "C1'" . 6HG C 3 5   ? -14.444 13.432  -22.613 1.00 70.20  ? 5   6HG T "C1'" 1 
HETATM 6569 C  "C6'" . 6HG C 3 5   ? -14.013 14.790  -23.214 1.00 59.43  ? 5   6HG T "C6'" 1 
HETATM 6570 N  N9    . 6HG C 3 5   ? -15.793 13.607  -22.011 1.00 64.44  ? 5   6HG T N9    1 
HETATM 6571 C  C8    . 6HG C 3 5   ? -17.015 13.767  -22.555 1.00 61.37  ? 5   6HG T C8    1 
HETATM 6572 N  N7    . 6HG C 3 5   ? -17.897 13.884  -21.544 1.00 62.97  ? 5   6HG T N7    1 
HETATM 6573 C  C5    . 6HG C 3 5   ? -17.226 13.798  -20.399 1.00 54.16  ? 5   6HG T C5    1 
HETATM 6574 C  C6    . 6HG C 3 5   ? -17.674 13.860  -18.940 1.00 54.89  ? 5   6HG T C6    1 
HETATM 6575 O  O6    . 6HG C 3 5   ? -18.820 14.010  -18.706 1.00 57.44  ? 5   6HG T O6    1 
HETATM 6576 N  N1    . 6HG C 3 5   ? -16.723 13.738  -17.875 1.00 58.77  ? 5   6HG T N1    1 
HETATM 6577 C  C2    . 6HG C 3 5   ? -15.325 13.555  -18.183 1.00 56.88  ? 5   6HG T C2    1 
HETATM 6578 N  N2    . 6HG C 3 5   ? -14.343 13.430  -17.115 1.00 60.91  ? 5   6HG T N2    1 
HETATM 6579 N  N3    . 6HG C 3 5   ? -14.905 13.498  -19.586 1.00 52.80  ? 5   6HG T N3    1 
HETATM 6580 C  C4    . 6HG C 3 5   ? -15.910 13.626  -20.686 1.00 59.73  ? 5   6HG T C4    1 
HETATM 6581 P  P     . 6HT C 3 6   ? -11.786 10.322  -23.978 1.00 90.08  ? 6   6HT T P     1 
HETATM 6582 O  OP1   . 6HT C 3 6   ? -10.456 10.179  -24.668 1.00 85.30  ? 6   6HT T OP1   1 
HETATM 6583 O  OP2   . 6HT C 3 6   ? -12.820 9.522   -24.720 1.00 86.86  ? 6   6HT T OP2   1 
HETATM 6584 O  "O5'" . 6HT C 3 6   ? -11.653 9.793   -22.421 1.00 79.04  ? 6   6HT T "O5'" 1 
HETATM 6585 C  "C5'" . 6HT C 3 6   ? -11.368 10.737  -21.427 1.00 83.57  ? 6   6HT T "C5'" 1 
HETATM 6586 C  "C4'" . 6HT C 3 6   ? -10.958 10.060  -20.167 1.00 84.53  ? 6   6HT T "C4'" 1 
HETATM 6587 O  "O4'" . 6HT C 3 6   ? -11.404 10.858  -19.026 1.00 84.57  ? 6   6HT T "O4'" 1 
HETATM 6588 C  "C3'" . 6HT C 3 6   ? -11.582 8.639   -20.089 1.00 81.82  ? 6   6HT T "C3'" 1 
HETATM 6589 O  "O3'" . 6HT C 3 6   ? -10.960 7.944   -18.980 1.00 84.81  ? 6   6HT T "O3'" 1 
HETATM 6590 C  "C2'" . 6HT C 3 6   ? -13.037 8.607   -19.885 1.00 78.86  ? 6   6HT T "C2'" 1 
HETATM 6591 C  "C1'" . 6HT C 3 6   ? -13.590 9.554   -18.903 1.00 73.31  ? 6   6HT T "C1'" 1 
HETATM 6592 C  "C6'" . 6HT C 3 6   ? -12.868 10.922  -18.907 1.00 74.17  ? 6   6HT T "C6'" 1 
HETATM 6593 N  N1    . 6HT C 3 6   ? -15.037 9.791   -19.205 1.00 69.84  ? 6   6HT T N1    1 
HETATM 6594 C  C2    . 6HT C 3 6   ? -16.008 9.929   -18.084 1.00 67.93  ? 6   6HT T C2    1 
HETATM 6595 O  O2    . 6HT C 3 6   ? -15.634 9.845   -16.976 1.00 72.22  ? 6   6HT T O2    1 
HETATM 6596 N  N3    . 6HT C 3 6   ? -17.467 10.172  -18.398 1.00 59.33  ? 6   6HT T N3    1 
HETATM 6597 C  C4    . 6HT C 3 6   ? -17.941 10.277  -19.785 1.00 61.45  ? 6   6HT T C4    1 
HETATM 6598 O  O4    . 6HT C 3 6   ? -19.086 10.468  -20.020 1.00 65.04  ? 6   6HT T O4    1 
HETATM 6599 C  C5    . 6HT C 3 6   ? -16.955 10.139  -20.911 1.00 63.20  ? 6   6HT T C5    1 
HETATM 6600 C  C5M   . 6HT C 3 6   ? -17.438 10.248  -22.382 1.00 59.36  ? 6   6HT T C5M   1 
HETATM 6601 C  C6    . 6HT C 3 6   ? -15.503 9.897   -20.594 1.00 70.18  ? 6   6HT T C6    1 
ATOM   6602 P  P     . DG  C 3 7   ? -10.952 6.344   -18.927 1.00 96.97  ? 7   DG  T P     1 
ATOM   6603 O  OP1   . DG  C 3 7   ? -9.651  5.913   -18.369 1.00 86.37  ? 7   DG  T OP1   1 
ATOM   6604 O  OP2   . DG  C 3 7   ? -11.400 5.832   -20.242 1.00 94.54  ? 7   DG  T OP2   1 
ATOM   6605 O  "O5'" . DG  C 3 7   ? -12.101 6.013   -17.869 1.00 84.40  ? 7   DG  T "O5'" 1 
ATOM   6606 C  "C5'" . DG  C 3 7   ? -12.005 6.502   -16.541 1.00 80.44  ? 7   DG  T "C5'" 1 
ATOM   6607 C  "C4'" . DG  C 3 7   ? -13.207 6.064   -15.730 1.00 71.19  ? 7   DG  T "C4'" 1 
ATOM   6608 O  "O4'" . DG  C 3 7   ? -14.370 6.768   -16.188 1.00 63.64  ? 7   DG  T "O4'" 1 
ATOM   6609 C  "C3'" . DG  C 3 7   ? -13.552 4.584   -15.864 1.00 60.66  ? 7   DG  T "C3'" 1 
ATOM   6610 O  "O3'" . DG  C 3 7   ? -13.059 3.871   -14.740 1.00 58.43  ? 7   DG  T "O3'" 1 
ATOM   6611 C  "C2'" . DG  C 3 7   ? -15.087 4.545   -15.930 1.00 66.13  ? 7   DG  T "C2'" 1 
ATOM   6612 C  "C1'" . DG  C 3 7   ? -15.506 6.009   -15.876 1.00 60.93  ? 7   DG  T "C1'" 1 
ATOM   6613 N  N9    . DG  C 3 7   ? -16.551 6.342   -16.833 1.00 64.34  ? 7   DG  T N9    1 
ATOM   6614 C  C8    . DG  C 3 7   ? -16.421 6.452   -18.196 1.00 65.30  ? 7   DG  T C8    1 
ATOM   6615 N  N7    . DG  C 3 7   ? -17.534 6.766   -18.798 1.00 58.28  ? 7   DG  T N7    1 
ATOM   6616 C  C5    . DG  C 3 7   ? -18.458 6.869   -17.767 1.00 59.33  ? 7   DG  T C5    1 
ATOM   6617 C  C6    . DG  C 3 7   ? -19.835 7.184   -17.806 1.00 58.25  ? 7   DG  T C6    1 
ATOM   6618 O  O6    . DG  C 3 7   ? -20.534 7.445   -18.794 1.00 59.33  ? 7   DG  T O6    1 
ATOM   6619 N  N1    . DG  C 3 7   ? -20.399 7.180   -16.534 1.00 49.82  ? 7   DG  T N1    1 
ATOM   6620 C  C2    . DG  C 3 7   ? -19.717 6.908   -15.371 1.00 57.98  ? 7   DG  T C2    1 
ATOM   6621 N  N2    . DG  C 3 7   ? -20.428 6.950   -14.238 1.00 54.49  ? 7   DG  T N2    1 
ATOM   6622 N  N3    . DG  C 3 7   ? -18.429 6.610   -15.322 1.00 62.57  ? 7   DG  T N3    1 
ATOM   6623 C  C4    . DG  C 3 7   ? -17.866 6.610   -16.552 1.00 59.16  ? 7   DG  T C4    1 
ATOM   6624 P  P     . DG  C 3 8   ? -13.425 2.320   -14.540 1.00 58.09  ? 8   DG  T P     1 
ATOM   6625 O  OP1   . DG  C 3 8   ? -12.363 1.710   -13.706 1.00 67.85  ? 8   DG  T OP1   1 
ATOM   6626 O  OP2   . DG  C 3 8   ? -13.741 1.750   -15.870 1.00 56.50  ? 8   DG  T OP2   1 
ATOM   6627 O  "O5'" . DG  C 3 8   ? -14.754 2.360   -13.657 1.00 61.01  ? 8   DG  T "O5'" 1 
ATOM   6628 C  "C5'" . DG  C 3 8   ? -14.822 3.220   -12.531 1.00 58.44  ? 8   DG  T "C5'" 1 
ATOM   6629 C  "C4'" . DG  C 3 8   ? -16.083 2.969   -11.724 1.00 63.70  ? 8   DG  T "C4'" 1 
ATOM   6630 O  "O4'" . DG  C 3 8   ? -17.220 3.571   -12.387 1.00 68.39  ? 8   DG  T "O4'" 1 
ATOM   6631 C  "C3'" . DG  C 3 8   ? -16.440 1.503   -11.514 1.00 61.92  ? 8   DG  T "C3'" 1 
ATOM   6632 O  "O3'" . DG  C 3 8   ? -17.017 1.334   -10.229 1.00 57.68  ? 8   DG  T "O3'" 1 
ATOM   6633 C  "C2'" . DG  C 3 8   ? -17.448 1.231   -12.629 1.00 61.50  ? 8   DG  T "C2'" 1 
ATOM   6634 C  "C1'" . DG  C 3 8   ? -18.152 2.578   -12.771 1.00 63.11  ? 8   DG  T "C1'" 1 
ATOM   6635 N  N9    . DG  C 3 8   ? -18.569 2.878   -14.135 1.00 60.26  ? 8   DG  T N9    1 
ATOM   6636 C  C8    . DG  C 3 8   ? -17.786 2.832   -15.259 1.00 60.59  ? 8   DG  T C8    1 
ATOM   6637 N  N7    . DG  C 3 8   ? -18.416 3.170   -16.347 1.00 62.78  ? 8   DG  T N7    1 
ATOM   6638 C  C5    . DG  C 3 8   ? -19.702 3.463   -15.917 1.00 57.07  ? 8   DG  T C5    1 
ATOM   6639 C  C6    . DG  C 3 8   ? -20.830 3.883   -16.654 1.00 59.91  ? 8   DG  T C6    1 
ATOM   6640 O  O6    . DG  C 3 8   ? -20.914 4.085   -17.872 1.00 60.05  ? 8   DG  T O6    1 
ATOM   6641 N  N1    . DG  C 3 8   ? -21.942 4.069   -15.835 1.00 64.08  ? 8   DG  T N1    1 
ATOM   6642 C  C2    . DG  C 3 8   ? -21.958 3.874   -14.472 1.00 64.89  ? 8   DG  T C2    1 
ATOM   6643 N  N2    . DG  C 3 8   ? -23.123 4.102   -13.846 1.00 55.44  ? 8   DG  T N2    1 
ATOM   6644 N  N3    . DG  C 3 8   ? -20.901 3.477   -13.769 1.00 60.48  ? 8   DG  T N3    1 
ATOM   6645 C  C4    . DG  C 3 8   ? -19.813 3.292   -14.555 1.00 55.72  ? 8   DG  T C4    1 
ATOM   6646 P  P     . DC  C 3 9   ? -17.160 -0.131  -9.589  1.00 62.34  ? 9   DC  T P     1 
ATOM   6647 O  OP1   . DC  C 3 9   ? -16.934 -0.013  -8.130  1.00 65.27  ? 9   DC  T OP1   1 
ATOM   6648 O  OP2   . DC  C 3 9   ? -16.337 -1.062  -10.392 1.00 59.42  ? 9   DC  T OP2   1 
ATOM   6649 O  "O5'" . DC  C 3 9   ? -18.691 -0.503  -9.848  1.00 69.76  ? 9   DC  T "O5'" 1 
ATOM   6650 C  "C5'" . DC  C 3 9   ? -19.699 0.461   -9.606  1.00 65.80  ? 9   DC  T "C5'" 1 
ATOM   6651 C  "C4'" . DC  C 3 9   ? -20.963 0.114   -10.367 1.00 67.94  ? 9   DC  T "C4'" 1 
ATOM   6652 O  "O4'" . DC  C 3 9   ? -20.883 0.623   -11.711 1.00 65.69  ? 9   DC  T "O4'" 1 
ATOM   6653 C  "C3'" . DC  C 3 9   ? -21.242 -1.387  -10.510 1.00 68.95  ? 9   DC  T "C3'" 1 
ATOM   6654 O  "O3'" . DC  C 3 9   ? -22.367 -1.734  -9.720  1.00 64.11  ? 9   DC  T "O3'" 1 
ATOM   6655 C  "C2'" . DC  C 3 9   ? -21.512 -1.589  -12.014 1.00 66.19  ? 9   DC  T "C2'" 1 
ATOM   6656 C  "C1'" . DC  C 3 9   ? -21.714 -0.169  -12.512 1.00 65.87  ? 9   DC  T "C1'" 1 
ATOM   6657 N  N1    . DC  C 3 9   ? -21.345 0.036   -13.940 1.00 61.68  ? 9   DC  T N1    1 
ATOM   6658 C  C2    . DC  C 3 9   ? -22.326 0.449   -14.840 1.00 59.75  ? 9   DC  T C2    1 
ATOM   6659 O  O2    . DC  C 3 9   ? -23.473 0.629   -14.421 1.00 67.79  ? 9   DC  T O2    1 
ATOM   6660 N  N3    . DC  C 3 9   ? -21.990 0.639   -16.140 1.00 61.79  ? 9   DC  T N3    1 
ATOM   6661 C  C4    . DC  C 3 9   ? -20.733 0.429   -16.541 1.00 64.01  ? 9   DC  T C4    1 
ATOM   6662 N  N4    . DC  C 3 9   ? -20.444 0.629   -17.833 1.00 63.79  ? 9   DC  T N4    1 
ATOM   6663 C  C5    . DC  C 3 9   ? -19.716 0.005   -15.633 1.00 58.29  ? 9   DC  T C5    1 
ATOM   6664 C  C6    . DC  C 3 9   ? -20.065 -0.178  -14.355 1.00 59.16  ? 9   DC  T C6    1 
ATOM   6665 P  P     . DC  C 3 10  ? -22.865 -3.259  -9.621  1.00 63.43  ? 10  DC  T P     1 
ATOM   6666 O  OP1   . DC  C 3 10  ? -23.141 -3.509  -8.188  1.00 58.49  ? 10  DC  T OP1   1 
ATOM   6667 O  OP2   . DC  C 3 10  ? -21.915 -4.141  -10.337 1.00 69.66  ? 10  DC  T OP2   1 
ATOM   6668 O  "O5'" . DC  C 3 10  ? -24.248 -3.247  -10.418 1.00 73.43  ? 10  DC  T "O5'" 1 
ATOM   6669 C  "C5'" . DC  C 3 10  ? -25.241 -2.288  -10.084 1.00 64.65  ? 10  DC  T "C5'" 1 
ATOM   6670 C  "C4'" . DC  C 3 10  ? -26.427 -2.374  -11.028 1.00 74.80  ? 10  DC  T "C4'" 1 
ATOM   6671 O  "O4'" . DC  C 3 10  ? -26.041 -1.921  -12.354 1.00 68.60  ? 10  DC  T "O4'" 1 
ATOM   6672 C  "C3'" . DC  C 3 10  ? -27.006 -3.771  -11.219 1.00 86.64  ? 10  DC  T "C3'" 1 
ATOM   6673 O  "O3'" . DC  C 3 10  ? -28.406 -3.670  -11.382 1.00 104.85 ? 10  DC  T "O3'" 1 
ATOM   6674 C  "C2'" . DC  C 3 10  ? -26.332 -4.229  -12.510 1.00 80.18  ? 10  DC  T "C2'" 1 
ATOM   6675 C  "C1'" . DC  C 3 10  ? -26.329 -2.933  -13.300 1.00 75.92  ? 10  DC  T "C1'" 1 
ATOM   6676 N  N1    . DC  C 3 10  ? -25.293 -2.871  -14.365 1.00 73.99  ? 10  DC  T N1    1 
ATOM   6677 C  C2    . DC  C 3 10  ? -25.643 -2.455  -15.659 1.00 73.88  ? 10  DC  T C2    1 
ATOM   6678 O  O2    . DC  C 3 10  ? -26.824 -2.163  -15.900 1.00 73.82  ? 10  DC  T O2    1 
ATOM   6679 N  N3    . DC  C 3 10  ? -24.675 -2.390  -16.609 1.00 72.32  ? 10  DC  T N3    1 
ATOM   6680 C  C4    . DC  C 3 10  ? -23.414 -2.714  -16.300 1.00 75.32  ? 10  DC  T C4    1 
ATOM   6681 N  N4    . DC  C 3 10  ? -22.492 -2.638  -17.263 1.00 68.27  ? 10  DC  T N4    1 
ATOM   6682 C  C5    . DC  C 3 10  ? -23.044 -3.132  -14.989 1.00 72.70  ? 10  DC  T C5    1 
ATOM   6683 C  C6    . DC  C 3 10  ? -24.004 -3.193  -14.064 1.00 73.10  ? 10  DC  T C6    1 
ATOM   6684 P  P     . DG  C 3 11  ? -29.367 -4.884  -10.965 1.00 85.62  ? 11  DG  T P     1 
ATOM   6685 O  OP1   . DG  C 3 11  ? -29.810 -4.639  -9.574  1.00 82.30  ? 11  DG  T OP1   1 
ATOM   6686 O  OP2   . DG  C 3 11  ? -28.686 -6.150  -11.315 1.00 77.24  ? 11  DG  T OP2   1 
ATOM   6687 O  "O5'" . DG  C 3 11  ? -30.612 -4.718  -11.947 1.00 82.85  ? 11  DG  T "O5'" 1 
ATOM   6688 C  "C5'" . DG  C 3 11  ? -30.547 -3.767  -12.995 1.00 84.67  ? 11  DG  T "C5'" 1 
ATOM   6689 C  "C4'" . DG  C 3 11  ? -31.333 -4.241  -14.197 1.00 85.23  ? 11  DG  T "C4'" 1 
ATOM   6690 O  "O4'" . DG  C 3 11  ? -30.454 -4.350  -15.340 1.00 85.52  ? 11  DG  T "O4'" 1 
ATOM   6691 C  "C3'" . DG  C 3 11  ? -31.979 -5.607  -14.045 1.00 78.04  ? 11  DG  T "C3'" 1 
ATOM   6692 O  "O3'" . DG  C 3 11  ? -33.173 -5.651  -14.821 1.00 78.27  ? 11  DG  T "O3'" 1 
ATOM   6693 C  "C2'" . DG  C 3 11  ? -30.899 -6.555  -14.573 1.00 75.44  ? 11  DG  T "C2'" 1 
ATOM   6694 C  "C1'" . DG  C 3 11  ? -30.183 -5.709  -15.626 1.00 80.62  ? 11  DG  T "C1'" 1 
ATOM   6695 N  N9    . DG  C 3 11  ? -28.733 -5.888  -15.636 1.00 78.13  ? 11  DG  T N9    1 
ATOM   6696 C  C8    . DG  C 3 11  ? -27.942 -6.327  -14.601 1.00 79.00  ? 11  DG  T C8    1 
ATOM   6697 N  N7    . DG  C 3 11  ? -26.673 -6.380  -14.904 1.00 78.60  ? 11  DG  T N7    1 
ATOM   6698 C  C5    . DG  C 3 11  ? -26.619 -5.942  -16.221 1.00 79.55  ? 11  DG  T C5    1 
ATOM   6699 C  C6    . DG  C 3 11  ? -25.510 -5.782  -17.088 1.00 77.37  ? 11  DG  T C6    1 
ATOM   6700 O  O6    . DG  C 3 11  ? -24.312 -6.004  -16.856 1.00 76.44  ? 11  DG  T O6    1 
ATOM   6701 N  N1    . DG  C 3 11  ? -25.900 -5.314  -18.340 1.00 73.73  ? 11  DG  T N1    1 
ATOM   6702 C  C2    . DG  C 3 11  ? -27.198 -5.036  -18.706 1.00 75.72  ? 11  DG  T C2    1 
ATOM   6703 N  N2    . DG  C 3 11  ? -27.389 -4.592  -19.954 1.00 77.31  ? 11  DG  T N2    1 
ATOM   6704 N  N3    . DG  C 3 11  ? -28.241 -5.181  -17.904 1.00 70.85  ? 11  DG  T N3    1 
ATOM   6705 C  C4    . DG  C 3 11  ? -27.880 -5.635  -16.683 1.00 74.34  ? 11  DG  T C4    1 
ATOM   6706 P  P     . DT  C 3 12  ? -33.921 -7.038  -15.134 1.00 69.90  ? 12  DT  T P     1 
ATOM   6707 O  OP1   . DT  C 3 12  ? -35.354 -6.703  -15.283 1.00 78.01  ? 12  DT  T OP1   1 
ATOM   6708 O  OP2   . DT  C 3 12  ? -33.528 -8.063  -14.140 1.00 77.29  ? 12  DT  T OP2   1 
ATOM   6709 O  "O5'" . DT  C 3 12  ? -33.341 -7.445  -16.567 1.00 81.31  ? 12  DT  T "O5'" 1 
ATOM   6710 C  "C5'" . DT  C 3 12  ? -33.180 -6.440  -17.567 1.00 76.57  ? 12  DT  T "C5'" 1 
ATOM   6711 C  "C4'" . DT  C 3 12  ? -32.644 -7.028  -18.860 1.00 76.44  ? 12  DT  T "C4'" 1 
ATOM   6712 O  "O4'" . DT  C 3 12  ? -31.194 -7.041  -18.836 1.00 74.12  ? 12  DT  T "O4'" 1 
ATOM   6713 C  "C3'" . DT  C 3 12  ? -33.084 -8.464  -19.152 1.00 83.10  ? 12  DT  T "C3'" 1 
ATOM   6714 O  "O3'" . DT  C 3 12  ? -33.570 -8.553  -20.479 1.00 84.23  ? 12  DT  T "O3'" 1 
ATOM   6715 C  "C2'" . DT  C 3 12  ? -31.802 -9.281  -18.964 1.00 76.22  ? 12  DT  T "C2'" 1 
ATOM   6716 C  "C1'" . DT  C 3 12  ? -30.737 -8.269  -19.348 1.00 79.63  ? 12  DT  T "C1'" 1 
ATOM   6717 N  N1    . DT  C 3 12  ? -29.396 -8.550  -18.758 1.00 76.23  ? 12  DT  T N1    1 
ATOM   6718 C  C2    . DT  C 3 12  ? -28.269 -8.364  -19.526 1.00 76.51  ? 12  DT  T C2    1 
ATOM   6719 O  O2    . DT  C 3 12  ? -28.305 -7.983  -20.683 1.00 75.59  ? 12  DT  T O2    1 
ATOM   6720 N  N3    . DT  C 3 12  ? -27.088 -8.642  -18.887 1.00 81.08  ? 12  DT  T N3    1 
ATOM   6721 C  C4    . DT  C 3 12  ? -26.927 -9.078  -17.583 1.00 79.15  ? 12  DT  T C4    1 
ATOM   6722 O  O4    . DT  C 3 12  ? -25.823 -9.302  -17.096 1.00 72.18  ? 12  DT  T O4    1 
ATOM   6723 C  C5    . DT  C 3 12  ? -28.149 -9.251  -16.834 1.00 74.19  ? 12  DT  T C5    1 
ATOM   6724 C  C7    . DT  C 3 12  ? -28.100 -9.720  -15.410 1.00 71.08  ? 12  DT  T C7    1 
ATOM   6725 C  C6    . DT  C 3 12  ? -29.310 -8.981  -17.450 1.00 76.26  ? 12  DT  T C6    1 
ATOM   6726 P  P     . DG  C 3 13  ? -34.604 -9.711  -20.888 1.00 90.40  ? 13  DG  T P     1 
ATOM   6727 O  OP1   . DG  C 3 13  ? -35.883 -9.060  -21.252 1.00 91.50  ? 13  DG  T OP1   1 
ATOM   6728 O  OP2   . DG  C 3 13  ? -34.566 -10.758 -19.842 1.00 82.89  ? 13  DG  T OP2   1 
ATOM   6729 O  "O5'" . DG  C 3 13  ? -33.962 -10.330 -22.210 1.00 90.27  ? 13  DG  T "O5'" 1 
ATOM   6730 C  "C5'" . DG  C 3 13  ? -33.687 -9.491  -23.321 1.00 85.04  ? 13  DG  T "C5'" 1 
ATOM   6731 C  "C4'" . DG  C 3 13  ? -32.532 -10.043 -24.128 1.00 87.05  ? 13  DG  T "C4'" 1 
ATOM   6732 O  "O4'" . DG  C 3 13  ? -31.301 -9.768  -23.431 1.00 84.65  ? 13  DG  T "O4'" 1 
ATOM   6733 C  "C3'" . DG  C 3 13  ? -32.565 -11.551 -24.329 1.00 89.16  ? 13  DG  T "C3'" 1 
ATOM   6734 O  "O3'" . DG  C 3 13  ? -33.266 -11.901 -25.560 1.00 98.42  ? 13  DG  T "O3'" 1 
ATOM   6735 C  "C2'" . DG  C 3 13  ? -31.095 -11.950 -24.363 1.00 91.22  ? 13  DG  T "C2'" 1 
ATOM   6736 C  "C1'" . DG  C 3 13  ? -30.395 -10.841 -23.587 1.00 86.94  ? 13  DG  T "C1'" 1 
ATOM   6737 N  N9    . DG  C 3 13  ? -29.916 -11.240 -22.267 1.00 85.20  ? 13  DG  T N9    1 
ATOM   6738 C  C8    . DG  C 3 13  ? -30.669 -11.561 -21.162 1.00 80.41  ? 13  DG  T C8    1 
ATOM   6739 N  N7    . DG  C 3 13  ? -29.948 -11.860 -20.113 1.00 80.50  ? 13  DG  T N7    1 
ATOM   6740 C  C5    . DG  C 3 13  ? -28.636 -11.722 -20.555 1.00 87.56  ? 13  DG  T C5    1 
ATOM   6741 C  C6    . DG  C 3 13  ? -27.410 -11.913 -19.869 1.00 86.81  ? 13  DG  T C6    1 
ATOM   6742 O  O6    . DG  C 3 13  ? -27.227 -12.254 -18.691 1.00 82.78  ? 13  DG  T O6    1 
ATOM   6743 N  N1    . DG  C 3 13  ? -26.317 -11.665 -20.698 1.00 80.77  ? 13  DG  T N1    1 
ATOM   6744 C  C2    . DG  C 3 13  ? -26.401 -11.283 -22.017 1.00 81.48  ? 13  DG  T C2    1 
ATOM   6745 N  N2    . DG  C 3 13  ? -25.247 -11.085 -22.664 1.00 81.74  ? 13  DG  T N2    1 
ATOM   6746 N  N3    . DG  C 3 13  ? -27.537 -11.102 -22.663 1.00 84.81  ? 13  DG  T N3    1 
ATOM   6747 C  C4    . DG  C 3 13  ? -28.608 -11.339 -21.876 1.00 86.40  ? 13  DG  T C4    1 
ATOM   6748 P  P     . DG  C 3 14  ? -32.697 -11.530 -27.027 1.00 100.72 ? 14  DG  T P     1 
ATOM   6749 O  OP1   . DG  C 3 14  ? -32.241 -10.124 -27.094 1.00 78.94  ? 14  DG  T OP1   1 
ATOM   6750 O  OP2   . DG  C 3 14  ? -33.735 -11.980 -27.978 1.00 92.99  ? 14  DG  T OP2   1 
ATOM   6751 O  "O5'" . DG  C 3 14  ? -31.435 -12.490 -27.242 1.00 98.73  ? 14  DG  T "O5'" 1 
ATOM   6752 C  "C5'" . DG  C 3 14  ? -30.241 -11.958 -27.815 1.00 104.87 ? 14  DG  T "C5'" 1 
ATOM   6753 C  "C4'" . DG  C 3 14  ? -29.072 -12.920 -27.668 1.00 100.37 ? 14  DG  T "C4'" 1 
ATOM   6754 O  "O4'" . DG  C 3 14  ? -28.688 -13.047 -26.270 1.00 92.87  ? 14  DG  T "O4'" 1 
ATOM   6755 C  "C3'" . DG  C 3 14  ? -29.328 -14.345 -28.169 1.00 103.49 ? 14  DG  T "C3'" 1 
ATOM   6756 O  "O3'" . DG  C 3 14  ? -28.226 -14.768 -28.948 1.00 112.40 ? 14  DG  T "O3'" 1 
ATOM   6757 C  "C2'" . DG  C 3 14  ? -29.431 -15.151 -26.876 1.00 99.91  ? 14  DG  T "C2'" 1 
ATOM   6758 C  "C1'" . DG  C 3 14  ? -28.447 -14.407 -25.994 1.00 101.30 ? 14  DG  T "C1'" 1 
ATOM   6759 N  N9    . DG  C 3 14  ? -28.630 -14.640 -24.562 1.00 101.10 ? 14  DG  T N9    1 
ATOM   6760 C  C8    . DG  C 3 14  ? -29.819 -14.831 -23.899 1.00 93.21  ? 14  DG  T C8    1 
ATOM   6761 N  N7    . DG  C 3 14  ? -29.679 -15.011 -22.616 1.00 89.91  ? 14  DG  T N7    1 
ATOM   6762 C  C5    . DG  C 3 14  ? -28.307 -14.945 -22.411 1.00 94.13  ? 14  DG  T C5    1 
ATOM   6763 C  C6    . DG  C 3 14  ? -27.560 -15.074 -21.217 1.00 90.66  ? 14  DG  T C6    1 
ATOM   6764 O  O6    . DG  C 3 14  ? -27.980 -15.277 -20.070 1.00 89.07  ? 14  DG  T O6    1 
ATOM   6765 N  N1    . DG  C 3 14  ? -26.194 -14.942 -21.447 1.00 91.58  ? 14  DG  T N1    1 
ATOM   6766 C  C2    . DG  C 3 14  ? -25.620 -14.716 -22.677 1.00 90.43  ? 14  DG  T C2    1 
ATOM   6767 N  N2    . DG  C 3 14  ? -24.284 -14.618 -22.700 1.00 92.16  ? 14  DG  T N2    1 
ATOM   6768 N  N3    . DG  C 3 14  ? -26.310 -14.592 -23.806 1.00 88.72  ? 14  DG  T N3    1 
ATOM   6769 C  C4    . DG  C 3 14  ? -27.645 -14.718 -23.598 1.00 96.99  ? 14  DG  T C4    1 
ATOM   6770 P  P     . DT  C 3 15  ? -28.391 -15.930 -30.044 1.00 116.82 ? 15  DT  T P     1 
ATOM   6771 O  OP1   . DT  C 3 15  ? -29.393 -15.471 -31.033 1.00 107.86 ? 15  DT  T OP1   1 
ATOM   6772 O  OP2   . DT  C 3 15  ? -28.597 -17.212 -29.331 1.00 103.09 ? 15  DT  T OP2   1 
ATOM   6773 O  "O5'" . DT  C 3 15  ? -26.953 -15.975 -30.745 1.00 117.41 ? 15  DT  T "O5'" 1 
ATOM   6774 C  "C5'" . DT  C 3 15  ? -25.827 -15.362 -30.103 1.00 111.50 ? 15  DT  T "C5'" 1 
ATOM   6775 C  "C4'" . DT  C 3 15  ? -24.934 -16.408 -29.454 1.00 113.83 ? 15  DT  T "C4'" 1 
ATOM   6776 O  "O4'" . DT  C 3 15  ? -25.081 -16.355 -28.019 1.00 114.84 ? 15  DT  T "O4'" 1 
ATOM   6777 C  "C3'" . DT  C 3 15  ? -25.264 -17.844 -29.842 1.00 117.91 ? 15  DT  T "C3'" 1 
ATOM   6778 O  "O3'" . DT  C 3 15  ? -24.387 -18.305 -30.902 1.00 127.06 ? 15  DT  T "O3'" 1 
ATOM   6779 C  "C2'" . DT  C 3 15  ? -25.107 -18.650 -28.542 1.00 113.59 ? 15  DT  T "C2'" 1 
ATOM   6780 C  "C1'" . DT  C 3 15  ? -24.748 -17.614 -27.475 1.00 111.22 ? 15  DT  T "C1'" 1 
ATOM   6781 N  N1    . DT  C 3 15  ? -25.523 -17.793 -26.197 1.00 101.05 ? 15  DT  T N1    1 
ATOM   6782 C  C2    . DT  C 3 15  ? -24.869 -17.831 -24.967 1.00 97.74  ? 15  DT  T C2    1 
ATOM   6783 O  O2    . DT  C 3 15  ? -23.661 -17.722 -24.841 1.00 96.57  ? 15  DT  T O2    1 
ATOM   6784 N  N3    . DT  C 3 15  ? -25.712 -17.993 -23.885 1.00 91.56  ? 15  DT  T N3    1 
ATOM   6785 C  C4    . DT  C 3 15  ? -27.092 -18.123 -23.917 1.00 98.63  ? 15  DT  T C4    1 
ATOM   6786 O  O4    . DT  C 3 15  ? -27.773 -18.266 -22.911 1.00 98.89  ? 15  DT  T O4    1 
ATOM   6787 C  C5    . DT  C 3 15  ? -27.689 -18.080 -25.221 1.00 102.82 ? 15  DT  T C5    1 
ATOM   6788 C  C7    . DT  C 3 15  ? -29.175 -18.217 -25.364 1.00 103.16 ? 15  DT  T C7    1 
ATOM   6789 C  C6    . DT  C 3 15  ? -26.891 -17.920 -26.280 1.00 101.29 ? 15  DT  T C6    1 
ATOM   6790 P  P     . DC  C 3 16  ? -22.885 -18.823 -30.616 1.00 145.79 ? 16  DC  T P     1 
ATOM   6791 O  OP1   . DC  C 3 16  ? -22.216 -17.930 -29.643 1.00 128.81 ? 16  DC  T OP1   1 
ATOM   6792 O  OP2   . DC  C 3 16  ? -22.268 -19.018 -31.945 1.00 113.08 ? 16  DC  T OP2   1 
ATOM   6793 O  "O5'" . DC  C 3 16  ? -23.079 -20.278 -29.974 1.00 112.96 ? 16  DC  T "O5'" 1 
ATOM   6794 C  "C5'" . DC  C 3 16  ? -21.948 -21.095 -29.687 1.00 110.55 ? 16  DC  T "C5'" 1 
ATOM   6795 C  "C4'" . DC  C 3 16  ? -21.462 -20.890 -28.259 1.00 116.01 ? 16  DC  T "C4'" 1 
ATOM   6796 O  "O4'" . DC  C 3 16  ? -22.553 -20.428 -27.417 1.00 117.15 ? 16  DC  T "O4'" 1 
ATOM   6797 C  "C3'" . DC  C 3 16  ? -20.911 -22.146 -27.583 1.00 111.55 ? 16  DC  T "C3'" 1 
ATOM   6798 O  "O3'" . DC  C 3 16  ? -19.759 -21.820 -26.821 1.00 113.33 ? 16  DC  T "O3'" 1 
ATOM   6799 C  "C2'" . DC  C 3 16  ? -22.066 -22.593 -26.688 1.00 103.80 ? 16  DC  T "C2'" 1 
ATOM   6800 C  "C1'" . DC  C 3 16  ? -22.658 -21.257 -26.274 1.00 110.09 ? 16  DC  T "C1'" 1 
ATOM   6801 N  N1    . DC  C 3 16  ? -24.097 -21.331 -25.893 1.00 103.30 ? 16  DC  T N1    1 
ATOM   6802 C  C2    . DC  C 3 16  ? -24.479 -21.323 -24.542 1.00 101.39 ? 16  DC  T C2    1 
ATOM   6803 O  O2    . DC  C 3 16  ? -23.610 -21.265 -23.660 1.00 101.08 ? 16  DC  T O2    1 
ATOM   6804 N  N3    . DC  C 3 16  ? -25.801 -21.383 -24.240 1.00 104.79 ? 16  DC  T N3    1 
ATOM   6805 C  C4    . DC  C 3 16  ? -26.711 -21.445 -25.217 1.00 105.47 ? 16  DC  T C4    1 
ATOM   6806 N  N4    . DC  C 3 16  ? -28.001 -21.503 -24.875 1.00 102.69 ? 16  DC  T N4    1 
ATOM   6807 C  C5    . DC  C 3 16  ? -26.337 -21.451 -26.587 1.00 99.01  ? 16  DC  T C5    1 
ATOM   6808 C  C6    . DC  C 3 16  ? -25.037 -21.402 -26.873 1.00 101.57 ? 16  DC  T C6    1 
HETATM 6809 C  C1    . EDO D 4 .   ? -11.770 16.819  -3.233  1.00 70.29  ? 801 EDO A C1    1 
HETATM 6810 O  O1    . EDO D 4 .   ? -12.292 18.080  -2.879  1.00 76.36  ? 801 EDO A O1    1 
HETATM 6811 C  C2    . EDO D 4 .   ? -11.005 16.925  -4.529  1.00 80.13  ? 801 EDO A C2    1 
HETATM 6812 O  O2    . EDO D 4 .   ? -11.843 17.434  -5.543  1.00 88.39  ? 801 EDO A O2    1 
HETATM 6813 MG MG    . MG  E 5 .   ? -8.725  24.452  -9.047  1.00 66.69  ? 802 MG  A MG    1 
HETATM 6814 N  N1    . XG4 F 6 .   ? -17.851 20.855  -19.248 1.00 51.64  ? 803 XG4 A N1    1 
HETATM 6815 C  C2    . XG4 F 6 .   ? -16.737 20.687  -20.152 1.00 48.03  ? 803 XG4 A C2    1 
HETATM 6816 N  N2    . XG4 F 6 .   ? -16.888 20.655  -21.600 1.00 54.70  ? 803 XG4 A N2    1 
HETATM 6817 N  N3    . XG4 F 6 .   ? -15.406 20.539  -19.592 1.00 46.71  ? 803 XG4 A N3    1 
HETATM 6818 C  C4    . XG4 F 6 .   ? -15.215 20.566  -18.118 1.00 48.56  ? 803 XG4 A C4    1 
HETATM 6819 C  C5    . XG4 F 6 .   ? -16.252 20.727  -17.252 1.00 47.69  ? 803 XG4 A C5    1 
HETATM 6820 C  C6    . XG4 F 6 .   ? -17.663 20.884  -17.830 1.00 50.30  ? 803 XG4 A C6    1 
HETATM 6821 O  O6    . XG4 F 6 .   ? -18.594 21.026  -17.111 1.00 52.45  ? 803 XG4 A O6    1 
HETATM 6822 N  N7    . XG4 F 6 .   ? -15.760 20.708  -16.011 1.00 47.54  ? 803 XG4 A N7    1 
HETATM 6823 C  C8    . XG4 F 6 .   ? -14.418 20.535  -16.093 1.00 58.63  ? 803 XG4 A C8    1 
HETATM 6824 N  N9    . XG4 F 6 .   ? -14.116 20.448  -17.405 1.00 57.58  ? 803 XG4 A N9    1 
HETATM 6825 P  PA    . XG4 F 6 .   ? -12.529 22.286  -12.842 1.00 60.50  ? 803 XG4 A PA    1 
HETATM 6826 P  PB    . XG4 F 6 .   ? -11.499 24.905  -12.012 1.00 62.15  ? 803 XG4 A PB    1 
HETATM 6827 P  PG    . XG4 F 6 .   ? -12.436 25.741  -9.401  1.00 61.86  ? 803 XG4 A PG    1 
HETATM 6828 C  "C1'" . XG4 F 6 .   ? -12.676 20.275  -17.387 1.00 56.33  ? 803 XG4 A "C1'" 1 
HETATM 6829 O  O1A   . XG4 F 6 .   ? -13.803 23.074  -12.970 1.00 55.63  ? 803 XG4 A O1A   1 
HETATM 6830 O  O1B   . XG4 F 6 .   ? -12.157 25.794  -13.040 1.00 58.58  ? 803 XG4 A O1B   1 
HETATM 6831 O  O1G   . XG4 F 6 .   ? -11.355 25.280  -8.453  1.00 82.08  ? 803 XG4 A O1G   1 
HETATM 6832 C  "C2'" . XG4 F 6 .   ? -12.014 21.646  -17.941 1.00 53.23  ? 803 XG4 A "C2'" 1 
HETATM 6833 O  O2A   . XG4 F 6 .   ? -12.597 21.334  -11.670 1.00 65.97  ? 803 XG4 A O2A   1 
HETATM 6834 O  O2B   . XG4 F 6 .   ? -10.186 25.511  -11.574 1.00 68.09  ? 803 XG4 A O2B   1 
HETATM 6835 O  O2G   . XG4 F 6 .   ? -12.138 27.149  -9.853  1.00 74.59  ? 803 XG4 A O2G   1 
HETATM 6836 C  "C3'" . XG4 F 6 .   ? -11.495 22.223  -16.917 1.00 57.73  ? 803 XG4 A "C3'" 1 
HETATM 6837 O  "O3'" . XG4 F 6 .   ? -10.336 23.086  -17.335 1.00 59.20  ? 803 XG4 A "O3'" 1 
HETATM 6838 N  N3A   . XG4 F 6 .   ? -11.220 23.356  -12.656 1.00 86.11  ? 803 XG4 A N3A   1 
HETATM 6839 O  O3B   . XG4 F 6 .   ? -12.486 24.741  -10.706 1.00 65.27  ? 803 XG4 A O3B   1 
HETATM 6840 O  O3G   . XG4 F 6 .   ? -13.774 25.724  -8.701  1.00 76.14  ? 803 XG4 A O3G   1 
HETATM 6841 C  "C4'" . XG4 F 6 .   ? -11.038 21.036  -16.057 1.00 61.94  ? 803 XG4 A "C4'" 1 
HETATM 6842 O  "O4'" . XG4 F 6 .   ? -12.190 20.044  -16.207 1.00 55.77  ? 803 XG4 A "O4'" 1 
HETATM 6843 C  "C5'" . XG4 F 6 .   ? -10.969 21.444  -14.719 1.00 66.23  ? 803 XG4 A "C5'" 1 
HETATM 6844 O  "O5'" . XG4 F 6 .   ? -12.273 21.451  -14.226 1.00 64.29  ? 803 XG4 A "O5'" 1 
HETATM 6845 C  C1    . EDO G 4 .   ? -21.020 0.657   -22.329 1.00 82.16  ? 101 EDO P C1    1 
HETATM 6846 O  O1    . EDO G 4 .   ? -21.061 -0.649  -21.800 1.00 86.98  ? 101 EDO P O1    1 
HETATM 6847 C  C2    . EDO G 4 .   ? -19.973 1.463   -21.602 1.00 84.70  ? 101 EDO P C2    1 
HETATM 6848 O  O2    . EDO G 4 .   ? -20.496 2.726   -21.252 1.00 78.66  ? 101 EDO P O2    1 
HETATM 6849 MG MG    . MG  H 5 .   ? -11.578 20.251  -10.070 1.00 69.55  ? 102 MG  P MG    1 
HETATM 6850 C  C1    . EDO I 4 .   ? -20.842 13.332  -26.884 1.00 79.23  ? 101 EDO T C1    1 
HETATM 6851 O  O1    . EDO I 4 .   ? -20.710 14.230  -25.805 1.00 76.30  ? 101 EDO T O1    1 
HETATM 6852 C  C2    . EDO I 4 .   ? -20.691 14.069  -28.192 1.00 79.03  ? 101 EDO T C2    1 
HETATM 6853 O  O2    . EDO I 4 .   ? -20.749 13.157  -29.266 1.00 80.97  ? 101 EDO T O2    1 
HETATM 6854 O  O     . HOH J 7 .   ? -14.053 39.880  -23.550 1.00 62.19  ? 901 HOH A O     1 
HETATM 6855 O  O     . HOH J 7 .   ? -53.807 41.730  -18.720 1.00 63.04  ? 902 HOH A O     1 
HETATM 6856 O  O     . HOH J 7 .   ? -58.814 36.781  -4.255  1.00 62.87  ? 903 HOH A O     1 
HETATM 6857 O  O     . HOH J 7 .   ? -10.075 23.507  -7.369  1.00 71.47  ? 904 HOH A O     1 
HETATM 6858 O  O     . HOH J 7 .   ? -8.986  26.619  -7.851  1.00 73.72  ? 905 HOH A O     1 
HETATM 6859 O  O     . HOH J 7 .   ? -3.662  34.686  -26.081 1.00 52.08  ? 906 HOH A O     1 
HETATM 6860 O  O     . HOH J 7 .   ? -11.745 25.286  -15.433 1.00 54.41  ? 907 HOH A O     1 
HETATM 6861 O  O     . HOH J 7 .   ? -1.620  10.426  -25.391 1.00 71.16  ? 908 HOH A O     1 
HETATM 6862 O  O     . HOH J 7 .   ? -23.597 32.839  -39.189 1.00 49.77  ? 909 HOH A O     1 
HETATM 6863 O  O     . HOH J 7 .   ? -38.908 14.745  -9.673  1.00 61.34  ? 910 HOH A O     1 
HETATM 6864 O  O     . HOH J 7 .   ? -6.421  36.852  -33.466 1.00 66.23  ? 911 HOH A O     1 
HETATM 6865 O  O     . HOH J 7 .   ? -33.305 37.649  -24.966 1.00 53.19  ? 912 HOH A O     1 
HETATM 6866 O  O     . HOH J 7 .   ? -34.923 31.413  -51.150 1.00 74.22  ? 913 HOH A O     1 
HETATM 6867 O  O     . HOH J 7 .   ? -12.464 22.026  -9.105  1.00 71.44  ? 914 HOH A O     1 
HETATM 6868 O  O     . HOH J 7 .   ? -38.540 54.632  -34.180 1.00 55.66  ? 915 HOH A O     1 
HETATM 6869 O  O     . HOH J 7 .   ? -64.466 9.454   -9.091  1.00 92.21  ? 916 HOH A O     1 
HETATM 6870 O  O     . HOH J 7 .   ? -47.992 24.803  -20.222 1.00 53.20  ? 917 HOH A O     1 
HETATM 6871 O  O     . HOH J 7 .   ? -20.969 41.545  -36.782 1.00 45.77  ? 918 HOH A O     1 
HETATM 6872 O  O     . HOH J 7 .   ? -22.500 25.920  -28.222 1.00 41.89  ? 919 HOH A O     1 
HETATM 6873 O  O     . HOH J 7 .   ? -19.861 43.952  -35.785 1.00 51.54  ? 920 HOH A O     1 
HETATM 6874 O  O     . HOH J 7 .   ? -37.394 38.161  -32.811 1.00 41.93  ? 921 HOH A O     1 
HETATM 6875 O  O     . HOH J 7 .   ? -39.389 24.882  -20.108 1.00 52.73  ? 922 HOH A O     1 
HETATM 6876 O  O     . HOH J 7 .   ? -1.520  27.226  -3.462  1.00 67.13  ? 923 HOH A O     1 
HETATM 6877 O  O     . HOH J 7 .   ? -18.429 44.606  1.950   1.00 89.40  ? 924 HOH A O     1 
HETATM 6878 O  O     . HOH J 7 .   ? -63.595 39.254  -10.904 1.00 68.77  ? 925 HOH A O     1 
HETATM 6879 O  O     . HOH J 7 .   ? -11.723 19.160  -8.144  1.00 74.41  ? 926 HOH A O     1 
HETATM 6880 O  O     . HOH J 7 .   ? -14.377 -2.034  -6.759  1.00 76.04  ? 927 HOH A O     1 
HETATM 6881 O  O     . HOH J 7 .   ? -31.127 35.607  -2.842  1.00 71.29  ? 928 HOH A O     1 
HETATM 6882 O  O     . HOH J 7 .   ? -50.755 48.223  -45.435 1.00 57.93  ? 929 HOH A O     1 
HETATM 6883 O  O     . HOH J 7 .   ? -58.474 -5.638  1.384   1.00 85.81  ? 930 HOH A O     1 
HETATM 6884 O  O     . HOH K 7 .   ? -13.733 5.437   -20.635 1.00 73.59  ? 201 HOH T O     1 
HETATM 6885 O  O     . HOH K 7 .   ? -18.181 5.902   -20.983 1.00 61.77  ? 202 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   ? 1.0648 1.0491 1.1909 0.0071  0.0247  -0.0830 1   MET A N     
2    C  CA    . MET A 1   ? 0.8461 0.8412 0.9639 0.0022  0.0204  -0.0803 1   MET A CA    
3    C  C     . MET A 1   ? 0.7865 0.7979 0.9124 0.0042  0.0213  -0.0711 1   MET A C     
4    O  O     . MET A 1   ? 0.8047 0.8224 0.9336 0.0085  0.0266  -0.0700 1   MET A O     
5    C  CB    . MET A 1   ? 0.8786 0.8720 0.9796 0.0006  0.0220  -0.0880 1   MET A CB    
6    C  CG    . MET A 1   ? 0.8070 0.8110 0.9004 -0.0039 0.0182  -0.0849 1   MET A CG    
7    S  SD    . MET A 1   ? 0.8477 0.8555 0.9262 -0.0034 0.0228  -0.0898 1   MET A SD    
8    C  CE    . MET A 1   ? 0.8029 0.8008 0.8649 -0.0097 0.0169  -0.0969 1   MET A CE    
9    N  N     . ILE A 2   ? 0.7326 0.7508 0.8620 0.0010  0.0162  -0.0646 2   ILE A N     
10   C  CA    . ILE A 2   ? 0.6668 0.6994 0.8022 0.0022  0.0160  -0.0565 2   ILE A CA    
11   C  C     . ILE A 2   ? 0.6990 0.7395 0.8251 0.0003  0.0165  -0.0582 2   ILE A C     
12   O  O     . ILE A 2   ? 0.7309 0.7702 0.8469 -0.0040 0.0135  -0.0611 2   ILE A O     
13   C  CB    . ILE A 2   ? 0.6396 0.6764 0.7791 -0.0005 0.0110  -0.0499 2   ILE A CB    
14   C  CG1   . ILE A 2   ? 0.6609 0.6953 0.8140 0.0026  0.0115  -0.0441 2   ILE A CG1   
15   C  CG2   . ILE A 2   ? 0.5865 0.6369 0.7243 -0.0015 0.0094  -0.0447 2   ILE A CG2   
16   C  CD1   . ILE A 2   ? 0.6158 0.6469 0.7719 -0.0005 0.0074  -0.0405 2   ILE A CD1   
17   N  N     . LEU A 3   ? 0.7274 0.7764 0.8583 0.0036  0.0203  -0.0557 3   LEU A N     
18   C  CA    . LEU A 3   ? 0.6365 0.6942 0.7612 0.0015  0.0206  -0.0558 3   LEU A CA    
19   C  C     . LEU A 3   ? 0.6437 0.7113 0.7699 -0.0015 0.0158  -0.0500 3   LEU A C     
20   O  O     . LEU A 3   ? 0.7538 0.8224 0.8716 -0.0057 0.0129  -0.0514 3   LEU A O     
21   C  CB    . LEU A 3   ? 0.6151 0.6786 0.7455 0.0060  0.0267  -0.0551 3   LEU A CB    
22   C  CG    . LEU A 3   ? 0.7076 0.7617 0.8336 0.0096  0.0331  -0.0620 3   LEU A CG    
23   C  CD1   . LEU A 3   ? 0.6527 0.7157 0.7832 0.0133  0.0397  -0.0604 3   LEU A CD1   
24   C  CD2   . LEU A 3   ? 0.6657 0.7106 0.7756 0.0054  0.0314  -0.0694 3   LEU A CD2   
25   N  N     . ASP A 4   ? 0.6056 0.6803 0.7420 0.0006  0.0147  -0.0434 4   ASP A N     
26   C  CA    . ASP A 4   ? 0.5799 0.6640 0.7158 -0.0023 0.0102  -0.0386 4   ASP A CA    
27   C  C     . ASP A 4   ? 0.5623 0.6516 0.7082 0.0004  0.0086  -0.0314 4   ASP A C     
28   O  O     . ASP A 4   ? 0.4837 0.5693 0.6382 0.0043  0.0112  -0.0296 4   ASP A O     
29   C  CB    . ASP A 4   ? 0.7138 0.8074 0.8494 -0.0039 0.0102  -0.0379 4   ASP A CB    
30   C  CG    . ASP A 4   ? 0.8845 0.9821 1.0131 -0.0087 0.0053  -0.0374 4   ASP A CG    
31   O  OD1   . ASP A 4   ? 0.7253 0.8248 0.8536 -0.0092 0.0019  -0.0343 4   ASP A OD1   
32   O  OD2   . ASP A 4   ? 0.8919 0.9904 1.0152 -0.0116 0.0053  -0.0400 4   ASP A OD2   
33   N  N     . THR A 5   ? 0.5256 0.6233 0.6697 -0.0019 0.0044  -0.0271 5   THR A N     
34   C  CA    . THR A 5   ? 0.5038 0.6089 0.6553 0.0001  0.0022  -0.0193 5   THR A CA    
35   C  C     . THR A 5   ? 0.4802 0.5975 0.6300 -0.0024 -0.0018 -0.0160 5   THR A C     
36   O  O     . THR A 5   ? 0.4272 0.5449 0.5680 -0.0064 -0.0038 -0.0201 5   THR A O     
37   C  CB    . THR A 5   ? 0.5273 0.6282 0.6759 -0.0005 0.0004  -0.0171 5   THR A CB    
38   O  OG1   . THR A 5   ? 0.5160 0.6169 0.6528 -0.0045 -0.0022 -0.0201 5   THR A OG1   
39   C  CG2   . THR A 5   ? 0.5203 0.6088 0.6716 0.0008  0.0031  -0.0201 5   THR A CG2   
40   N  N     . ASP A 6   ? 0.4087 0.5357 0.5677 -0.0001 -0.0034 -0.0083 6   ASP A N     
41   C  CA    . ASP A 6   ? 0.4316 0.5704 0.5880 -0.0029 -0.0089 -0.0043 6   ASP A CA    
42   C  C     . ASP A 6   ? 0.4359 0.5827 0.6001 0.0001  -0.0110 0.0052  6   ASP A C     
43   O  O     . ASP A 6   ? 0.4267 0.5683 0.5968 0.0038  -0.0082 0.0084  6   ASP A O     
44   C  CB    . ASP A 6   ? 0.5522 0.6988 0.7130 -0.0048 -0.0097 -0.0050 6   ASP A CB    
45   C  CG    . ASP A 6   ? 0.5863 0.7392 0.7638 -0.0001 -0.0065 0.0007  6   ASP A CG    
46   O  OD1   . ASP A 6   ? 0.6077 0.7584 0.7936 0.0048  -0.0038 0.0049  6   ASP A OD1   
47   O  OD2   . ASP A 6   ? 0.5534 0.7138 0.7367 -0.0012 -0.0064 0.0013  6   ASP A OD2   
48   N  N     . TYR A 7   ? 0.4375 0.5969 0.6018 -0.0019 -0.0164 0.0103  7   TYR A N     
49   C  CA    . TYR A 7   ? 0.5007 0.6697 0.6728 0.0009  -0.0189 0.0207  7   TYR A CA    
50   C  C     . TYR A 7   ? 0.4928 0.6768 0.6721 -0.0005 -0.0238 0.0264  7   TYR A C     
51   O  O     . TYR A 7   ? 0.4756 0.6633 0.6488 -0.0054 -0.0275 0.0220  7   TYR A O     
52   C  CB    . TYR A 7   ? 0.4394 0.6089 0.5994 -0.0003 -0.0218 0.0230  7   TYR A CB    
53   C  CG    . TYR A 7   ? 0.4864 0.6640 0.6331 -0.0053 -0.0285 0.0220  7   TYR A CG    
54   C  CD1   . TYR A 7   ? 0.4896 0.6603 0.6212 -0.0095 -0.0292 0.0125  7   TYR A CD1   
55   C  CD2   . TYR A 7   ? 0.5120 0.7038 0.6610 -0.0057 -0.0343 0.0305  7   TYR A CD2   
56   C  CE1   . TYR A 7   ? 0.4574 0.6334 0.5761 -0.0140 -0.0351 0.0104  7   TYR A CE1   
57   C  CE2   . TYR A 7   ? 0.5203 0.7186 0.6554 -0.0107 -0.0411 0.0285  7   TYR A CE2   
58   C  CZ    . TYR A 7   ? 0.5830 0.7725 0.7026 -0.0148 -0.0412 0.0179  7   TYR A CZ    
59   O  OH    . TYR A 7   ? 0.6136 0.8076 0.7188 -0.0198 -0.0478 0.0148  7   TYR A OH    
60   N  N     . ILE A 8   ? 0.4999 0.6928 0.6939 0.0037  -0.0241 0.0367  8   ILE A N     
61   C  CA    . ILE A 8   ? 0.4998 0.7096 0.7026 0.0026  -0.0300 0.0448  8   ILE A CA    
62   C  C     . ILE A 8   ? 0.5200 0.7392 0.7200 0.0029  -0.0355 0.0543  8   ILE A C     
63   O  O     . ILE A 8   ? 0.4888 0.7015 0.6830 0.0050  -0.0334 0.0556  8   ILE A O     
64   C  CB    . ILE A 8   ? 0.4525 0.6674 0.6773 0.0078  -0.0256 0.0504  8   ILE A CB    
65   C  CG1   . ILE A 8   ? 0.5461 0.7552 0.7826 0.0150  -0.0199 0.0563  8   ILE A CG1   
66   C  CG2   . ILE A 8   ? 0.4482 0.6559 0.6740 0.0072  -0.0202 0.0414  8   ILE A CG2   
67   C  CD1   . ILE A 8   ? 0.5025 0.7141 0.7605 0.0214  -0.0141 0.0609  8   ILE A CD1   
68   N  N     . THR A 9   ? 0.4015 0.6369 0.6057 0.0005  -0.0429 0.0616  9   THR A N     
69   C  CA    . THR A 9   ? 0.4142 0.6611 0.6149 0.0004  -0.0493 0.0717  9   THR A CA    
70   C  C     . THR A 9   ? 0.5482 0.8079 0.7721 0.0055  -0.0497 0.0856  9   THR A C     
71   O  O     . THR A 9   ? 0.5764 0.8480 0.8123 0.0042  -0.0534 0.0896  9   THR A O     
72   C  CB    . THR A 9   ? 0.5102 0.7660 0.6949 -0.0072 -0.0591 0.0690  9   THR A CB    
73   O  OG1   . THR A 9   ? 0.5568 0.7995 0.7209 -0.0111 -0.0577 0.0562  9   THR A OG1   
74   C  CG2   . THR A 9   ? 0.5132 0.7818 0.6924 -0.0073 -0.0659 0.0797  9   THR A CG2   
75   N  N     . GLU A 10  ? 0.5388 0.7960 0.7703 0.0113  -0.0458 0.0936  10  GLU A N     
76   C  CA    . GLU A 10  ? 0.5398 0.8074 0.7945 0.0173  -0.0452 0.1078  10  GLU A CA    
77   C  C     . GLU A 10  ? 0.5822 0.8627 0.8325 0.0169  -0.0521 0.1203  10  GLU A C     
78   O  O     . GLU A 10  ? 0.5313 0.8052 0.7729 0.0184  -0.0499 0.1219  10  GLU A O     
79   C  CB    . GLU A 10  ? 0.4574 0.7106 0.7264 0.0246  -0.0349 0.1075  10  GLU A CB    
80   C  CG    . GLU A 10  ? 0.6212 0.8821 0.9170 0.0317  -0.0322 0.1200  10  GLU A CG    
81   C  CD    . GLU A 10  ? 0.8162 1.0601 1.1246 0.0381  -0.0213 0.1148  10  GLU A CD    
82   O  OE1   . GLU A 10  ? 0.8701 1.1095 1.1820 0.0386  -0.0169 0.1065  10  GLU A OE1   
83   O  OE2   . GLU A 10  ? 0.7897 1.0244 1.1040 0.0424  -0.0173 0.1190  10  GLU A OE2   
84   N  N     . ASP A 11  ? 0.6129 0.9126 0.8690 0.0147  -0.0607 0.1296  11  ASP A N     
85   C  CA    . ASP A 11  ? 0.5900 0.9048 0.8410 0.0138  -0.0687 0.1424  11  ASP A CA    
86   C  C     . ASP A 11  ? 0.6185 0.9280 0.8400 0.0091  -0.0714 0.1354  11  ASP A C     
87   O  O     . ASP A 11  ? 0.6327 0.9446 0.8480 0.0112  -0.0715 0.1435  11  ASP A O     
88   C  CB    . ASP A 11  ? 0.6348 0.9521 0.9057 0.0219  -0.0645 0.1575  11  ASP A CB    
89   C  CG    . ASP A 11  ? 0.6944 1.0242 0.9941 0.0264  -0.0649 0.1690  11  ASP A CG    
90   O  OD1   . ASP A 11  ? 0.5665 0.9158 0.8694 0.0231  -0.0746 0.1774  11  ASP A OD1   
91   O  OD2   . ASP A 11  ? 0.8692 1.1891 1.1885 0.0333  -0.0556 0.1695  11  ASP A OD2   
92   N  N     . GLY A 12  ? 0.6825 0.9845 0.8863 0.0030  -0.0729 0.1205  12  GLY A N     
93   C  CA    . GLY A 12  ? 0.5879 0.8839 0.7638 -0.0011 -0.0746 0.1123  12  GLY A CA    
94   C  C     . GLY A 12  ? 0.5486 0.8272 0.7179 0.0022  -0.0650 0.1061  12  GLY A C     
95   O  O     . GLY A 12  ? 0.5215 0.7952 0.6687 -0.0003 -0.0651 0.1000  12  GLY A O     
96   N  N     . LYS A 13  ? 0.5049 0.7738 0.6927 0.0077  -0.0567 0.1072  13  LYS A N     
97   C  CA    . LYS A 13  ? 0.5059 0.7587 0.6894 0.0103  -0.0485 0.1021  13  LYS A CA    
98   C  C     . LYS A 13  ? 0.5233 0.7606 0.7089 0.0096  -0.0427 0.0884  13  LYS A C     
99   O  O     . LYS A 13  ? 0.4728 0.7107 0.6719 0.0103  -0.0419 0.0867  13  LYS A O     
100  C  CB    . LYS A 13  ? 0.4571 0.7095 0.6588 0.0168  -0.0438 0.1148  13  LYS A CB    
101  C  CG    . LYS A 13  ? 0.5014 0.7706 0.7043 0.0182  -0.0494 0.1309  13  LYS A CG    
102  C  CD    . LYS A 13  ? 0.6273 0.8925 0.8387 0.0232  -0.0440 0.1412  13  LYS A CD    
103  C  CE    . LYS A 13  ? 0.7843 1.0604 0.9787 0.0220  -0.0478 0.1497  13  LYS A CE    
104  N  NZ    . LYS A 13  ? 0.6465 0.9405 0.8307 0.0183  -0.0577 0.1540  13  LYS A NZ    
105  N  N     . PRO A 14  ? 0.4555 0.6792 0.6282 0.0085  -0.0383 0.0790  14  PRO A N     
106  C  CA    . PRO A 14  ? 0.4055 0.6150 0.5789 0.0076  -0.0333 0.0665  14  PRO A CA    
107  C  C     . PRO A 14  ? 0.4097 0.6100 0.6019 0.0128  -0.0265 0.0685  14  PRO A C     
108  O  O     . PRO A 14  ? 0.4836 0.6815 0.6834 0.0165  -0.0238 0.0761  14  PRO A O     
109  C  CB    . PRO A 14  ? 0.4877 0.6875 0.6424 0.0051  -0.0313 0.0583  14  PRO A CB    
110  C  CG    . PRO A 14  ? 0.5784 0.7881 0.7212 0.0047  -0.0350 0.0659  14  PRO A CG    
111  C  CD    . PRO A 14  ? 0.5313 0.7531 0.6890 0.0082  -0.0374 0.0803  14  PRO A CD    
112  N  N     . VAL A 15  ? 0.4073 0.6022 0.6071 0.0131  -0.0237 0.0616  15  VAL A N     
113  C  CA    . VAL A 15  ? 0.4336 0.6174 0.6482 0.0178  -0.0168 0.0604  15  VAL A CA    
114  C  C     . VAL A 15  ? 0.5526 0.7232 0.7584 0.0153  -0.0133 0.0465  15  VAL A C     
115  O  O     . VAL A 15  ? 0.5650 0.7383 0.7684 0.0129  -0.0141 0.0409  15  VAL A O     
116  C  CB    . VAL A 15  ? 0.5421 0.7336 0.7765 0.0222  -0.0158 0.0673  15  VAL A CB    
117  C  CG1   . VAL A 15  ? 0.4878 0.6653 0.7355 0.0274  -0.0078 0.0644  15  VAL A CG1   
118  C  CG2   . VAL A 15  ? 0.4572 0.6637 0.7007 0.0244  -0.0203 0.0823  15  VAL A CG2   
119  N  N     . ILE A 16  ? 0.4728 0.6300 0.6742 0.0154  -0.0097 0.0418  16  ILE A N     
120  C  CA    . ILE A 16  ? 0.4652 0.6098 0.6586 0.0131  -0.0067 0.0296  16  ILE A CA    
121  C  C     . ILE A 16  ? 0.4876 0.6256 0.6928 0.0167  -0.0015 0.0262  16  ILE A C     
122  O  O     . ILE A 16  ? 0.5282 0.6624 0.7472 0.0214  0.0017  0.0311  16  ILE A O     
123  C  CB    . ILE A 16  ? 0.4807 0.6145 0.6675 0.0120  -0.0051 0.0268  16  ILE A CB    
124  C  CG1   . ILE A 16  ? 0.4747 0.6134 0.6458 0.0081  -0.0087 0.0263  16  ILE A CG1   
125  C  CG2   . ILE A 16  ? 0.4532 0.5727 0.6375 0.0110  -0.0014 0.0162  16  ILE A CG2   
126  C  CD1   . ILE A 16  ? 0.4694 0.6053 0.6272 0.0039  -0.0097 0.0160  16  ILE A CD1   
127  N  N     . ARG A 17  ? 0.4265 0.5626 0.6262 0.0146  -0.0003 0.0179  17  ARG A N     
128  C  CA    . ARG A 17  ? 0.5092 0.6375 0.7156 0.0177  0.0055  0.0125  17  ARG A CA    
129  C  C     . ARG A 17  ? 0.4847 0.5993 0.6788 0.0149  0.0076  0.0016  17  ARG A C     
130  O  O     . ARG A 17  ? 0.5171 0.6327 0.6985 0.0101  0.0048  -0.0031 17  ARG A O     
131  C  CB    . ARG A 17  ? 0.4378 0.5767 0.6490 0.0179  0.0059  0.0131  17  ARG A CB    
132  C  CG    . ARG A 17  ? 0.5741 0.7279 0.7999 0.0209  0.0036  0.0245  17  ARG A CG    
133  C  CD    . ARG A 17  ? 0.5924 0.7603 0.8173 0.0171  -0.0006 0.0259  17  ARG A CD    
134  N  NE    . ARG A 17  ? 0.6222 0.7904 0.8538 0.0190  0.0048  0.0224  17  ARG A NE    
135  C  CZ    . ARG A 17  ? 0.6429 0.8177 0.8708 0.0147  0.0030  0.0196  17  ARG A CZ    
136  N  NH1   . ARG A 17  ? 0.5290 0.7090 0.7460 0.0081  -0.0043 0.0187  17  ARG A NH1   
137  N  NH2   . ARG A 17  ? 0.6621 0.8378 0.8974 0.0173  0.0091  0.0177  17  ARG A NH2   
138  N  N     . ILE A 18  ? 0.4550 0.5565 0.6530 0.0177  0.0120  -0.0024 18  ILE A N     
139  C  CA    . ILE A 18  ? 0.5463 0.6345 0.7335 0.0152  0.0137  -0.0126 18  ILE A CA    
140  C  C     . ILE A 18  ? 0.6004 0.6836 0.7895 0.0183  0.0195  -0.0186 18  ILE A C     
141  O  O     . ILE A 18  ? 0.5850 0.6615 0.7840 0.0233  0.0239  -0.0184 18  ILE A O     
142  C  CB    . ILE A 18  ? 0.5281 0.6044 0.7168 0.0150  0.0133  -0.0129 18  ILE A CB    
143  C  CG1   . ILE A 18  ? 0.5521 0.6352 0.7404 0.0130  0.0089  -0.0052 18  ILE A CG1   
144  C  CG2   . ILE A 18  ? 0.5262 0.5902 0.7033 0.0115  0.0136  -0.0230 18  ILE A CG2   
145  C  CD1   . ILE A 18  ? 0.6246 0.7088 0.8272 0.0168  0.0093  0.0044  18  ILE A CD1   
146  N  N     . PHE A 19  ? 0.5884 0.6748 0.7684 0.0156  0.0199  -0.0237 19  PHE A N     
147  C  CA    . PHE A 19  ? 0.5794 0.6620 0.7586 0.0183  0.0260  -0.0295 19  PHE A CA    
148  C  C     . PHE A 19  ? 0.6334 0.7004 0.8012 0.0167  0.0275  -0.0392 19  PHE A C     
149  O  O     . PHE A 19  ? 0.6557 0.7201 0.8118 0.0115  0.0235  -0.0426 19  PHE A O     
150  C  CB    . PHE A 19  ? 0.5237 0.6173 0.6988 0.0157  0.0256  -0.0295 19  PHE A CB    
151  C  CG    . PHE A 19  ? 0.5829 0.6923 0.7668 0.0150  0.0217  -0.0206 19  PHE A CG    
152  C  CD1   . PHE A 19  ? 0.5734 0.6925 0.7720 0.0196  0.0249  -0.0145 19  PHE A CD1   
153  C  CD2   . PHE A 19  ? 0.5942 0.7088 0.7716 0.0099  0.0149  -0.0184 19  PHE A CD2   
154  C  CE1   . PHE A 19  ? 0.5565 0.6911 0.7632 0.0182  0.0200  -0.0060 19  PHE A CE1   
155  C  CE2   . PHE A 19  ? 0.6156 0.7442 0.7991 0.0086  0.0104  -0.0111 19  PHE A CE2   
156  C  CZ    . PHE A 19  ? 0.6037 0.7426 0.8019 0.0124  0.0124  -0.0047 19  PHE A CZ    
157  N  N     . LYS A 20  ? 0.6494 0.7058 0.8204 0.0213  0.0331  -0.0437 20  LYS A N     
158  C  CA    . LYS A 20  ? 0.7298 0.7701 0.8902 0.0197  0.0337  -0.0531 20  LYS A CA    
159  C  C     . LYS A 20  ? 0.7492 0.7821 0.9073 0.0246  0.0416  -0.0602 20  LYS A C     
160  O  O     . LYS A 20  ? 0.7184 0.7579 0.8866 0.0302  0.0473  -0.0567 20  LYS A O     
161  C  CB    . LYS A 20  ? 0.7297 0.7598 0.8965 0.0195  0.0309  -0.0518 20  LYS A CB    
162  C  CG    . LYS A 20  ? 0.7861 0.8216 0.9708 0.0244  0.0321  -0.0423 20  LYS A CG    
163  C  CD    . LYS A 20  ? 0.7210 0.7543 0.9113 0.0220  0.0269  -0.0365 20  LYS A CD    
164  C  CE    . LYS A 20  ? 0.8191 0.8348 1.0140 0.0232  0.0283  -0.0408 20  LYS A CE    
165  N  NZ    . LYS A 20  ? 0.8286 0.8450 1.0404 0.0260  0.0276  -0.0309 20  LYS A NZ    
166  N  N     . LYS A 21  ? 0.8306 0.8501 0.9752 0.0224  0.0419  -0.0700 21  LYS A N     
167  C  CA    . LYS A 21  ? 0.9191 0.9287 1.0574 0.0268  0.0495  -0.0786 21  LYS A CA    
168  C  C     . LYS A 21  ? 0.9599 0.9501 1.0945 0.0262  0.0482  -0.0864 21  LYS A C     
169  O  O     . LYS A 21  ? 0.9690 0.9520 1.0913 0.0200  0.0425  -0.0916 21  LYS A O     
170  C  CB    . LYS A 21  ? 0.9223 0.9352 1.0440 0.0241  0.0510  -0.0839 21  LYS A CB    
171  C  CG    . LYS A 21  ? 0.9731 0.9849 1.0919 0.0304  0.0611  -0.0884 21  LYS A CG    
172  C  CD    . LYS A 21  ? 1.0018 1.0081 1.0993 0.0275  0.0622  -0.0972 21  LYS A CD    
173  C  CE    . LYS A 21  ? 1.0088 1.0157 1.1026 0.0343  0.0734  -0.1010 21  LYS A CE    
174  N  NZ    . LYS A 21  ? 0.9134 0.9362 1.0252 0.0394  0.0788  -0.0913 21  LYS A NZ    
175  N  N     . GLU A 22  ? 1.0222 1.0038 1.1685 0.0323  0.0532  -0.0869 22  GLU A N     
176  C  CA    . GLU A 22  ? 1.1410 1.1028 1.2864 0.0318  0.0521  -0.0942 22  GLU A CA    
177  C  C     . GLU A 22  ? 1.1549 1.1036 1.2965 0.0387  0.0615  -0.1038 22  GLU A C     
178  O  O     . GLU A 22  ? 1.1118 1.0663 1.2649 0.0464  0.0695  -0.0998 22  GLU A O     
179  C  CB    . GLU A 22  ? 1.1533 1.1139 1.3178 0.0327  0.0489  -0.0855 22  GLU A CB    
180  C  CG    . GLU A 22  ? 1.3223 1.2678 1.4850 0.0270  0.0423  -0.0895 22  GLU A CG    
181  C  CD    . GLU A 22  ? 1.4420 1.3949 1.6188 0.0242  0.0361  -0.0776 22  GLU A CD    
182  O  OE1   . GLU A 22  ? 1.2842 1.2495 1.4748 0.0285  0.0381  -0.0671 22  GLU A OE1   
183  O  OE2   . GLU A 22  ? 1.5126 1.4597 1.6866 0.0178  0.0293  -0.0785 22  GLU A OE2   
184  N  N     . ASN A 23  ? 1.1749 1.1065 1.3001 0.0357  0.0605  -0.1163 23  ASN A N     
185  C  CA    . ASN A 23  ? 1.2053 1.1213 1.3229 0.0417  0.0693  -0.1278 23  ASN A CA    
186  C  C     . ASN A 23  ? 1.1555 1.0830 1.2688 0.0482  0.0793  -0.1276 23  ASN A C     
187  O  O     . ASN A 23  ? 1.2130 1.1357 1.3325 0.0570  0.0895  -0.1301 23  ASN A O     
188  C  CB    . ASN A 23  ? 1.2686 1.1710 1.4039 0.0476  0.0730  -0.1276 23  ASN A CB    
189  C  CG    . ASN A 23  ? 1.4298 1.3149 1.5653 0.0413  0.0646  -0.1321 23  ASN A CG    
190  O  OD1   . ASN A 23  ? 1.6172 1.4929 1.7346 0.0343  0.0589  -0.1415 23  ASN A OD1   
191  N  ND2   . ASN A 23  ? 1.4406 1.3220 1.5975 0.0433  0.0636  -0.1246 23  ASN A ND2   
192  N  N     . GLY A 24  ? 1.1109 1.0539 1.2148 0.0438  0.0765  -0.1239 24  GLY A N     
193  C  CA    . GLY A 24  ? 1.0654 1.0210 1.1659 0.0487  0.0852  -0.1223 24  GLY A CA    
194  C  C     . GLY A 24  ? 1.0888 1.0603 1.2118 0.0550  0.0904  -0.1104 24  GLY A C     
195  O  O     . GLY A 24  ? 1.0245 1.0056 1.1485 0.0605  0.0992  -0.1088 24  GLY A O     
196  N  N     . GLU A 25  ? 1.0926 1.0683 1.2341 0.0545  0.0852  -0.1012 25  GLU A N     
197  C  CA    . GLU A 25  ? 1.0100 1.0018 1.1735 0.0598  0.0884  -0.0888 25  GLU A CA    
198  C  C     . GLU A 25  ? 0.9344 0.9416 1.1044 0.0532  0.0784  -0.0781 25  GLU A C     
199  O  O     . GLU A 25  ? 0.9165 0.9180 1.0837 0.0473  0.0699  -0.0781 25  GLU A O     
200  C  CB    . GLU A 25  ? 1.0544 1.0365 1.2361 0.0673  0.0930  -0.0870 25  GLU A CB    
201  C  CG    . GLU A 25  ? 1.1318 1.1307 1.3379 0.0706  0.0921  -0.0718 25  GLU A CG    
202  C  CD    . GLU A 25  ? 1.3603 1.3533 1.5854 0.0810  0.1010  -0.0694 25  GLU A CD    
203  O  OE1   . GLU A 25  ? 1.2545 1.2343 1.4881 0.0820  0.0989  -0.0692 25  GLU A OE1   
204  O  OE2   . GLU A 25  ? 1.7086 1.7103 1.9414 0.0883  0.1103  -0.0670 25  GLU A OE2   
205  N  N     . PHE A 26  ? 0.7938 0.8205 0.9723 0.0541  0.0794  -0.0690 26  PHE A N     
206  C  CA    . PHE A 26  ? 0.7688 0.8103 0.9529 0.0482  0.0704  -0.0593 26  PHE A CA    
207  C  C     . PHE A 26  ? 0.7540 0.7990 0.9577 0.0512  0.0680  -0.0497 26  PHE A C     
208  O  O     . PHE A 26  ? 0.8190 0.8690 1.0391 0.0585  0.0741  -0.0443 26  PHE A O     
209  C  CB    . PHE A 26  ? 0.7080 0.7681 0.8941 0.0474  0.0718  -0.0536 26  PHE A CB    
210  C  CG    . PHE A 26  ? 0.7078 0.7836 0.9022 0.0427  0.0634  -0.0433 26  PHE A CG    
211  C  CD1   . PHE A 26  ? 0.7143 0.7904 0.8969 0.0346  0.0548  -0.0443 26  PHE A CD1   
212  C  CD2   . PHE A 26  ? 0.7025 0.7926 0.9163 0.0464  0.0640  -0.0326 26  PHE A CD2   
213  C  CE1   . PHE A 26  ? 0.6739 0.7630 0.8621 0.0305  0.0475  -0.0361 26  PHE A CE1   
214  C  CE2   . PHE A 26  ? 0.6837 0.7876 0.9029 0.0416  0.0556  -0.0239 26  PHE A CE2   
215  C  CZ    . PHE A 26  ? 0.6620 0.7648 0.8676 0.0337  0.0476  -0.0263 26  PHE A CZ    
216  N  N     . LYS A 27  ? 0.7092 0.7523 0.9120 0.0459  0.0595  -0.0469 27  LYS A N     
217  C  CA    . LYS A 27  ? 0.7487 0.7956 0.9683 0.0480  0.0564  -0.0369 27  LYS A CA    
218  C  C     . LYS A 27  ? 0.7408 0.8026 0.9599 0.0420  0.0477  -0.0286 27  LYS A C     
219  O  O     . LYS A 27  ? 0.7566 0.8203 0.9613 0.0355  0.0431  -0.0323 27  LYS A O     
220  C  CB    . LYS A 27  ? 0.7909 0.8194 1.0114 0.0481  0.0553  -0.0408 27  LYS A CB    
221  C  CG    . LYS A 27  ? 0.8929 0.9020 1.1048 0.0507  0.0616  -0.0537 27  LYS A CG    
222  C  CD    . LYS A 27  ? 1.0041 0.9953 1.2220 0.0513  0.0604  -0.0559 27  LYS A CD    
223  C  CE    . LYS A 27  ? 1.0837 1.0574 1.3027 0.0581  0.0692  -0.0653 27  LYS A CE    
224  N  NZ    . LYS A 27  ? 1.1259 1.0836 1.3234 0.0540  0.0691  -0.0802 27  LYS A NZ    
225  N  N     . ILE A 28  ? 0.7109 0.7828 0.9457 0.0445  0.0455  -0.0172 28  ILE A N     
226  C  CA    . ILE A 28  ? 0.6360 0.7219 0.8706 0.0396  0.0374  -0.0088 28  ILE A CA    
227  C  C     . ILE A 28  ? 0.7641 0.8466 1.0079 0.0407  0.0344  -0.0017 28  ILE A C     
228  O  O     . ILE A 28  ? 0.7746 0.8609 1.0356 0.0464  0.0367  0.0066  28  ILE A O     
229  C  CB    . ILE A 28  ? 0.6219 0.7274 0.8662 0.0408  0.0366  -0.0003 28  ILE A CB    
230  C  CG1   . ILE A 28  ? 0.6561 0.7655 0.8923 0.0392  0.0397  -0.0064 28  ILE A CG1   
231  C  CG2   . ILE A 28  ? 0.5894 0.7076 0.8319 0.0358  0.0278  0.0077  28  ILE A CG2   
232  C  CD1   . ILE A 28  ? 0.5774 0.7067 0.8208 0.0375  0.0365  0.0015  28  ILE A CD1   
233  N  N     . GLU A 29  ? 0.6469 0.7231 0.8807 0.0355  0.0296  -0.0039 29  GLU A N     
234  C  CA    . GLU A 29  ? 0.6051 0.6799 0.8471 0.0357  0.0265  0.0041  29  GLU A CA    
235  C  C     . GLU A 29  ? 0.5588 0.6516 0.8018 0.0337  0.0206  0.0148  29  GLU A C     
236  O  O     . GLU A 29  ? 0.5986 0.6992 0.8291 0.0289  0.0168  0.0126  29  GLU A O     
237  C  CB    . GLU A 29  ? 0.6036 0.6648 0.8358 0.0311  0.0241  -0.0021 29  GLU A CB    
238  C  CG    . GLU A 29  ? 0.6760 0.7308 0.9197 0.0323  0.0231  0.0048  29  GLU A CG    
239  C  CD    . GLU A 29  ? 0.8980 0.9470 1.1329 0.0263  0.0188  0.0030  29  GLU A CD    
240  O  OE1   . GLU A 29  ? 0.8518 0.8918 1.0745 0.0225  0.0184  -0.0075 29  GLU A OE1   
241  O  OE2   . GLU A 29  ? 0.9554 1.0100 1.1960 0.0256  0.0159  0.0127  29  GLU A OE2   
242  N  N     . TYR A 30  ? 0.5823 0.6810 0.8398 0.0373  0.0198  0.0263  30  TYR A N     
243  C  CA    . TYR A 30  ? 0.5112 0.6272 0.7692 0.0356  0.0140  0.0372  30  TYR A CA    
244  C  C     . TYR A 30  ? 0.5001 0.6136 0.7567 0.0338  0.0110  0.0431  30  TYR A C     
245  O  O     . TYR A 30  ? 0.6013 0.7028 0.8668 0.0360  0.0137  0.0441  30  TYR A O     
246  C  CB    . TYR A 30  ? 0.5780 0.7066 0.8537 0.0410  0.0147  0.0483  30  TYR A CB    
247  C  CG    . TYR A 30  ? 0.6538 0.7889 0.9321 0.0426  0.0174  0.0447  30  TYR A CG    
248  C  CD1   . TYR A 30  ? 0.5954 0.7206 0.8823 0.0480  0.0252  0.0393  30  TYR A CD1   
249  C  CD2   . TYR A 30  ? 0.5379 0.6888 0.8102 0.0386  0.0122  0.0467  30  TYR A CD2   
250  C  CE1   . TYR A 30  ? 0.5483 0.6807 0.8384 0.0498  0.0286  0.0370  30  TYR A CE1   
251  C  CE2   . TYR A 30  ? 0.5594 0.7173 0.8361 0.0396  0.0146  0.0446  30  TYR A CE2   
252  C  CZ    . TYR A 30  ? 0.6443 0.7936 0.9302 0.0454  0.0231  0.0403  30  TYR A CZ    
253  O  OH    . TYR A 30  ? 0.5868 0.7441 0.8777 0.0468  0.0264  0.0391  30  TYR A OH    
254  N  N     . ASP A 31  ? 0.5170 0.6416 0.7626 0.0296  0.0056  0.0468  31  ASP A N     
255  C  CA    . ASP A 31  ? 0.5165 0.6413 0.7595 0.0280  0.0033  0.0531  31  ASP A CA    
256  C  C     . ASP A 31  ? 0.4729 0.6157 0.7113 0.0269  -0.0019 0.0629  31  ASP A C     
257  O  O     . ASP A 31  ? 0.4887 0.6386 0.7126 0.0230  -0.0053 0.0583  31  ASP A O     
258  C  CB    . ASP A 31  ? 0.5381 0.6532 0.7665 0.0231  0.0031  0.0436  31  ASP A CB    
259  C  CG    . ASP A 31  ? 0.5681 0.6793 0.7990 0.0224  0.0029  0.0498  31  ASP A CG    
260  O  OD1   . ASP A 31  ? 0.5312 0.6504 0.7710 0.0249  0.0020  0.0622  31  ASP A OD1   
261  O  OD2   . ASP A 31  ? 0.5832 0.6841 0.8079 0.0193  0.0035  0.0430  31  ASP A OD2   
262  N  N     . ARG A 32  ? 0.5240 0.6740 0.7742 0.0302  -0.0027 0.0763  32  ARG A N     
263  C  CA    . ARG A 32  ? 0.5226 0.6902 0.7678 0.0294  -0.0081 0.0866  32  ARG A CA    
264  C  C     . ARG A 32  ? 0.5192 0.6885 0.7580 0.0282  -0.0090 0.0934  32  ARG A C     
265  O  O     . ARG A 32  ? 0.5696 0.7529 0.8056 0.0285  -0.0127 0.1043  32  ARG A O     
266  C  CB    . ARG A 32  ? 0.6359 0.8146 0.8992 0.0342  -0.0091 0.0990  32  ARG A CB    
267  C  CG    . ARG A 32  ? 0.5957 0.7692 0.8728 0.0378  -0.0051 0.0942  32  ARG A CG    
268  C  CD    . ARG A 32  ? 0.5087 0.6933 0.8065 0.0434  -0.0055 0.1081  32  ARG A CD    
269  N  NE    . ARG A 32  ? 0.6573 0.8499 0.9613 0.0445  -0.0056 0.1060  32  ARG A NE    
270  C  CZ    . ARG A 32  ? 0.7036 0.8861 1.0165 0.0480  0.0009  0.0985  32  ARG A CZ    
271  N  NH1   . ARG A 32  ? 0.5378 0.7010 0.8537 0.0504  0.0073  0.0913  32  ARG A NH1   
272  N  NH2   . ARG A 32  ? 0.8461 1.0386 1.1652 0.0490  0.0008  0.0982  32  ARG A NH2   
273  N  N     . THR A 33  ? 0.5895 0.7453 0.8255 0.0267  -0.0057 0.0877  33  THR A N     
274  C  CA    . THR A 33  ? 0.5881 0.7451 0.8209 0.0260  -0.0053 0.0949  33  THR A CA    
275  C  C     . THR A 33  ? 0.5914 0.7484 0.8037 0.0216  -0.0060 0.0872  33  THR A C     
276  O  O     . THR A 33  ? 0.5940 0.7539 0.8020 0.0212  -0.0052 0.0934  33  THR A O     
277  C  CB    . THR A 33  ? 0.6241 0.7667 0.8726 0.0275  -0.0012 0.0968  33  THR A CB    
278  O  OG1   . THR A 33  ? 0.6276 0.7555 0.8707 0.0245  0.0007  0.0827  33  THR A OG1   
279  C  CG2   . THR A 33  ? 0.6415 0.7811 0.9109 0.0324  0.0005  0.1028  33  THR A CG2   
280  N  N     . PHE A 34  ? 0.5578 0.7117 0.7581 0.0187  -0.0070 0.0745  34  PHE A N     
281  C  CA    . PHE A 34  ? 0.5418 0.6948 0.7238 0.0150  -0.0073 0.0669  34  PHE A CA    
282  C  C     . PHE A 34  ? 0.5845 0.7517 0.7516 0.0140  -0.0111 0.0706  34  PHE A C     
283  O  O     . PHE A 34  ? 0.5837 0.7589 0.7487 0.0135  -0.0151 0.0702  34  PHE A O     
284  C  CB    . PHE A 34  ? 0.5377 0.6814 0.7135 0.0123  -0.0070 0.0526  34  PHE A CB    
285  C  CG    . PHE A 34  ? 0.6358 0.7740 0.7985 0.0092  -0.0058 0.0451  34  PHE A CG    
286  C  CD1   . PHE A 34  ? 0.6210 0.7528 0.7877 0.0092  -0.0030 0.0474  34  PHE A CD1   
287  C  CD2   . PHE A 34  ? 0.5404 0.6798 0.6880 0.0063  -0.0077 0.0363  34  PHE A CD2   
288  C  CE1   . PHE A 34  ? 0.5812 0.7090 0.7376 0.0069  -0.0018 0.0415  34  PHE A CE1   
289  C  CE2   . PHE A 34  ? 0.6392 0.7734 0.7761 0.0041  -0.0062 0.0300  34  PHE A CE2   
290  C  CZ    . PHE A 34  ? 0.5876 0.7165 0.7291 0.0047  -0.0031 0.0328  34  PHE A CZ    
291  N  N     . GLU A 35  ? 0.5364 0.7069 0.6930 0.0137  -0.0100 0.0741  35  GLU A N     
292  C  CA    . GLU A 35  ? 0.5582 0.7414 0.6985 0.0130  -0.0131 0.0776  35  GLU A CA    
293  C  C     . GLU A 35  ? 0.5774 0.7567 0.6980 0.0100  -0.0127 0.0659  35  GLU A C     
294  O  O     . GLU A 35  ? 0.6437 0.8147 0.7630 0.0098  -0.0084 0.0620  35  GLU A O     
295  C  CB    . GLU A 35  ? 0.6235 0.8147 0.7651 0.0158  -0.0112 0.0915  35  GLU A CB    
296  C  CG    . GLU A 35  ? 0.7482 0.9366 0.9129 0.0189  -0.0089 0.1022  35  GLU A CG    
297  C  CD    . GLU A 35  ? 0.8105 1.0054 0.9775 0.0211  -0.0061 0.1160  35  GLU A CD    
298  O  OE1   . GLU A 35  ? 0.7913 1.0001 0.9493 0.0222  -0.0084 0.1251  35  GLU A OE1   
299  O  OE2   . GLU A 35  ? 0.7651 0.9516 0.9428 0.0215  -0.0017 0.1180  35  GLU A OE2   
300  N  N     . PRO A 36  ? 0.5755 0.7605 0.6817 0.0075  -0.0173 0.0605  36  PRO A N     
301  C  CA    . PRO A 36  ? 0.5990 0.7793 0.6866 0.0049  -0.0167 0.0495  36  PRO A CA    
302  C  C     . PRO A 36  ? 0.5645 0.7488 0.6386 0.0067  -0.0134 0.0536  36  PRO A C     
303  O  O     . PRO A 36  ? 0.5738 0.7683 0.6471 0.0089  -0.0138 0.0649  36  PRO A O     
304  C  CB    . PRO A 36  ? 0.5718 0.7579 0.6496 0.0015  -0.0234 0.0444  36  PRO A CB    
305  C  CG    . PRO A 36  ? 0.5683 0.7671 0.6547 0.0029  -0.0277 0.0563  36  PRO A CG    
306  C  CD    . PRO A 36  ? 0.5665 0.7619 0.6745 0.0066  -0.0235 0.0641  36  PRO A CD    
307  N  N     . TYR A 37  ? 0.5568 0.7333 0.6203 0.0060  -0.0096 0.0450  37  TYR A N     
308  C  CA    . TYR A 37  ? 0.5654 0.7447 0.6170 0.0085  -0.0047 0.0484  37  TYR A CA    
309  C  C     . TYR A 37  ? 0.5553 0.7261 0.5927 0.0075  -0.0019 0.0362  37  TYR A C     
310  O  O     . TYR A 37  ? 0.5169 0.6787 0.5573 0.0049  -0.0032 0.0265  37  TYR A O     
311  C  CB    . TYR A 37  ? 0.6006 0.7793 0.6681 0.0116  0.0009  0.0585  37  TYR A CB    
312  C  CG    . TYR A 37  ? 0.5757 0.7421 0.6551 0.0106  0.0040  0.0524  37  TYR A CG    
313  C  CD1   . TYR A 37  ? 0.5252 0.6854 0.6217 0.0092  0.0018  0.0514  37  TYR A CD1   
314  C  CD2   . TYR A 37  ? 0.5471 0.7086 0.6205 0.0112  0.0090  0.0479  37  TYR A CD2   
315  C  CE1   . TYR A 37  ? 0.4882 0.6374 0.5935 0.0079  0.0038  0.0456  37  TYR A CE1   
316  C  CE2   . TYR A 37  ? 0.4742 0.6258 0.5586 0.0099  0.0108  0.0432  37  TYR A CE2   
317  C  CZ    . TYR A 37  ? 0.5545 0.7000 0.6540 0.0080  0.0078  0.0419  37  TYR A CZ    
318  O  OH    . TYR A 37  ? 0.5495 0.6854 0.6580 0.0063  0.0088  0.0370  37  TYR A OH    
319  N  N     . PHE A 38  ? 0.5879 0.7620 0.6100 0.0099  0.0024  0.0373  38  PHE A N     
320  C  CA    . PHE A 38  ? 0.6381 0.8038 0.6513 0.0107  0.0078  0.0285  38  PHE A CA    
321  C  C     . PHE A 38  ? 0.5997 0.7711 0.6055 0.0154  0.0153  0.0359  38  PHE A C     
322  O  O     . PHE A 38  ? 0.6083 0.7905 0.6121 0.0174  0.0155  0.0467  38  PHE A O     
323  C  CB    . PHE A 38  ? 0.5714 0.7315 0.5668 0.0077  0.0042  0.0150  38  PHE A CB    
324  C  CG    . PHE A 38  ? 0.6660 0.8335 0.6399 0.0075  0.0009  0.0144  38  PHE A CG    
325  C  CD1   . PHE A 38  ? 0.6469 0.8177 0.6038 0.0113  0.0067  0.0159  38  PHE A CD1   
326  C  CD2   . PHE A 38  ? 0.6667 0.8379 0.6367 0.0031  -0.0081 0.0117  38  PHE A CD2   
327  C  CE1   . PHE A 38  ? 0.6997 0.8768 0.6342 0.0107  0.0033  0.0143  38  PHE A CE1   
328  C  CE2   . PHE A 38  ? 0.5781 0.7562 0.5275 0.0020  -0.0124 0.0107  38  PHE A CE2   
329  C  CZ    . PHE A 38  ? 0.6479 0.8285 0.5784 0.0057  -0.0069 0.0116  38  PHE A CZ    
330  N  N     . TYR A 39  ? 0.6116 0.7765 0.6146 0.0174  0.0219  0.0310  39  TYR A N     
331  C  CA    . TYR A 39  ? 0.6489 0.8194 0.6491 0.0224  0.0305  0.0389  39  TYR A CA    
332  C  C     . TYR A 39  ? 0.6474 0.8192 0.6210 0.0250  0.0340  0.0328  39  TYR A C     
333  O  O     . TYR A 39  ? 0.6759 0.8397 0.6359 0.0230  0.0314  0.0198  39  TYR A O     
334  C  CB    . TYR A 39  ? 0.5818 0.7459 0.5976 0.0236  0.0362  0.0391  39  TYR A CB    
335  C  CG    . TYR A 39  ? 0.5238 0.6849 0.5641 0.0207  0.0327  0.0436  39  TYR A CG    
336  C  CD1   . TYR A 39  ? 0.4828 0.6508 0.5385 0.0216  0.0336  0.0571  39  TYR A CD1   
337  C  CD2   . TYR A 39  ? 0.5214 0.6723 0.5690 0.0170  0.0286  0.0344  39  TYR A CD2   
338  C  CE1   . TYR A 39  ? 0.4749 0.6383 0.5519 0.0189  0.0303  0.0600  39  TYR A CE1   
339  C  CE2   . TYR A 39  ? 0.4829 0.6303 0.5504 0.0145  0.0256  0.0374  39  TYR A CE2   
340  C  CZ    . TYR A 39  ? 0.4761 0.6291 0.5581 0.0154  0.0263  0.0496  39  TYR A CZ    
341  O  OH    . TYR A 39  ? 0.5655 0.7131 0.6664 0.0128  0.0233  0.0514  39  TYR A OH    
342  N  N     . ALA A 40  ? 0.6700 0.8515 0.6360 0.0295  0.0403  0.0424  40  ALA A N     
343  C  CA    . ALA A 40  ? 0.7244 0.9073 0.6636 0.0330  0.0453  0.0371  40  ALA A CA    
344  C  C     . ALA A 40  ? 0.7985 0.9867 0.7399 0.0394  0.0573  0.0458  40  ALA A C     
345  O  O     . ALA A 40  ? 0.7647 0.9614 0.7235 0.0409  0.0600  0.0603  40  ALA A O     
346  C  CB    . ALA A 40  ? 0.6234 0.8160 0.5437 0.0320  0.0396  0.0399  40  ALA A CB    
347  N  N     . LEU A 41  ? 0.8327 1.0158 0.7572 0.0434  0.0648  0.0373  41  LEU A N     
348  C  CA    . LEU A 41  ? 0.7780 0.9663 0.7041 0.0503  0.0775  0.0449  41  LEU A CA    
349  C  C     . LEU A 41  ? 0.8736 1.0687 0.7701 0.0550  0.0831  0.0449  41  LEU A C     
350  O  O     . LEU A 41  ? 0.9300 1.1175 0.8018 0.0550  0.0821  0.0308  41  LEU A O     
351  C  CB    . LEU A 41  ? 0.7794 0.9565 0.7120 0.0524  0.0836  0.0362  41  LEU A CB    
352  C  CG    . LEU A 41  ? 0.7920 0.9744 0.7319 0.0596  0.0970  0.0445  41  LEU A CG    
353  C  CD1   . LEU A 41  ? 0.8179 1.0144 0.7765 0.0605  0.0995  0.0636  41  LEU A CD1   
354  C  CD2   . LEU A 41  ? 0.7003 0.8729 0.6574 0.0597  0.0996  0.0391  41  LEU A CD2   
355  N  N     . LEU A 42  ? 0.8899 1.0993 0.7887 0.0588  0.0890  0.0606  42  LEU A N     
356  C  CA    . LEU A 42  ? 0.9795 1.1976 0.8503 0.0639  0.0953  0.0630  42  LEU A CA    
357  C  C     . LEU A 42  ? 1.0458 1.2681 0.9178 0.0721  0.1110  0.0690  42  LEU A C     
358  O  O     . LEU A 42  ? 1.1372 1.3610 1.0366 0.0733  0.1159  0.0776  42  LEU A O     
359  C  CB    . LEU A 42  ? 1.0062 1.2396 0.8767 0.0625  0.0905  0.0782  42  LEU A CB    
360  C  CG    . LEU A 42  ? 0.9995 1.2326 0.8820 0.0551  0.0761  0.0793  42  LEU A CG    
361  C  CD1   . LEU A 42  ? 1.0369 1.2863 0.9202 0.0553  0.0735  0.0967  42  LEU A CD1   
362  C  CD2   . LEU A 42  ? 1.0470 1.2703 0.9090 0.0504  0.0665  0.0617  42  LEU A CD2   
363  N  N     . LYS A 43  ? 1.0389 1.2634 0.8805 0.0777  0.1189  0.0644  43  LYS A N     
364  C  CA    . LYS A 43  ? 1.1178 1.3483 0.9582 0.0866  0.1353  0.0713  43  LYS A CA    
365  C  C     . LYS A 43  ? 1.2038 1.4536 1.0508 0.0897  0.1408  0.0928  43  LYS A C     
366  O  O     . LYS A 43  ? 1.2294 1.4868 1.0897 0.0958  0.1534  0.1039  43  LYS A O     
367  C  CB    . LYS A 43  ? 1.1639 1.3877 0.9679 0.0922  0.1430  0.0566  43  LYS A CB    
368  C  CG    . LYS A 43  ? 1.1245 1.3445 0.8961 0.0877  0.1324  0.0448  43  LYS A CG    
369  C  CD    . LYS A 43  ? 1.1635 1.3751 0.8988 0.0935  0.1409  0.0296  43  LYS A CD    
370  C  CE    . LYS A 43  ? 1.2264 1.4330 0.9294 0.0879  0.1290  0.0165  43  LYS A CE    
371  N  NZ    . LYS A 43  ? 1.3006 1.5007 0.9644 0.0938  0.1375  0.0030  43  LYS A NZ    
372  N  N     . ASP A 44  ? 1.2608 1.5193 1.1003 0.0858  0.1317  0.0998  44  ASP A N     
373  C  CA    . ASP A 44  ? 1.3110 1.5879 1.1587 0.0879  0.1354  0.1215  44  ASP A CA    
374  C  C     . ASP A 44  ? 1.3148 1.5945 1.1837 0.0804  0.1216  0.1300  44  ASP A C     
375  O  O     . ASP A 44  ? 1.2158 1.4877 1.0776 0.0744  0.1091  0.1189  44  ASP A O     
376  C  CB    . ASP A 44  ? 1.3303 1.6176 1.1407 0.0927  0.1405  0.1234  44  ASP A CB    
377  C  CG    . ASP A 44  ? 1.3776 1.6844 1.1943 0.0936  0.1412  0.1464  44  ASP A CG    
378  O  OD1   . ASP A 44  ? 1.4488 1.7593 1.2741 0.0875  0.1287  0.1526  44  ASP A OD1   
379  O  OD2   . ASP A 44  ? 1.3248 1.6436 1.1391 0.1006  0.1548  0.1591  44  ASP A OD2   
380  N  N     . ASP A 45  ? 1.5385 1.8292 1.4346 0.0807  0.1243  0.1499  45  ASP A N     
381  C  CA    . ASP A 45  ? 1.4093 1.7015 1.3285 0.0743  0.1126  0.1586  45  ASP A CA    
382  C  C     . ASP A 45  ? 1.3336 1.6349 1.2328 0.0726  0.1044  0.1629  45  ASP A C     
383  O  O     . ASP A 45  ? 1.4903 1.7861 1.3908 0.0668  0.0917  0.1563  45  ASP A O     
384  C  CB    . ASP A 45  ? 1.4326 1.7333 1.3857 0.0752  0.1179  0.1788  45  ASP A CB    
385  C  CG    . ASP A 45  ? 1.5452 1.8430 1.5125 0.0790  0.1293  0.1787  45  ASP A CG    
386  O  OD1   . ASP A 45  ? 1.6222 1.9062 1.5972 0.0766  0.1266  0.1647  45  ASP A OD1   
387  O  OD2   . ASP A 45  ? 1.3176 1.6280 1.2889 0.0844  0.1409  0.1934  45  ASP A OD2   
388  N  N     . SER A 46  ? 1.2816 1.5977 1.1620 0.0777  0.1117  0.1744  46  SER A N     
389  C  CA    . SER A 46  ? 1.2759 1.6031 1.1377 0.0762  0.1039  0.1813  46  SER A CA    
390  C  C     . SER A 46  ? 1.2243 1.5432 1.0578 0.0722  0.0934  0.1617  46  SER A C     
391  O  O     . SER A 46  ? 1.2283 1.5539 1.0537 0.0686  0.0826  0.1656  46  SER A O     
392  C  CB    . SER A 46  ? 1.2705 1.6146 1.1121 0.0830  0.1150  0.1952  46  SER A CB    
393  O  OG    . SER A 46  ? 1.3055 1.6453 1.1235 0.0888  0.1268  0.1837  46  SER A OG    
394  N  N     . ALA A 47  ? 1.2135 1.5177 1.0331 0.0726  0.0959  0.1415  47  ALA A N     
395  C  CA    . ALA A 47  ? 1.1438 1.4382 0.9396 0.0679  0.0853  0.1223  47  ALA A CA    
396  C  C     . ALA A 47  ? 1.1711 1.4619 0.9864 0.0601  0.0702  0.1213  47  ALA A C     
397  O  O     . ALA A 47  ? 1.1740 1.4627 0.9713 0.0554  0.0592  0.1114  47  ALA A O     
398  C  CB    . ALA A 47  ? 1.1178 1.3949 0.9043 0.0693  0.0909  0.1020  47  ALA A CB    
399  N  N     . ILE A 48  ? 1.1240 1.4142 0.9758 0.0586  0.0695  0.1315  48  ILE A N     
400  C  CA    . ILE A 48  ? 1.1341 1.4210 1.0057 0.0523  0.0566  0.1314  48  ILE A CA    
401  C  C     . ILE A 48  ? 1.1317 1.4322 0.9922 0.0502  0.0472  0.1409  48  ILE A C     
402  O  O     . ILE A 48  ? 1.1105 1.4086 0.9752 0.0448  0.0352  0.1361  48  ILE A O     
403  C  CB    . ILE A 48  ? 1.0186 1.3034 0.9294 0.0519  0.0587  0.1426  48  ILE A CB    
404  C  CG1   . ILE A 48  ? 0.9726 1.2505 0.9031 0.0459  0.0469  0.1386  48  ILE A CG1   
405  C  CG2   . ILE A 48  ? 0.9545 1.2548 0.8770 0.0554  0.0638  0.1656  48  ILE A CG2   
406  C  CD1   . ILE A 48  ? 0.9433 1.2043 0.8754 0.0425  0.0441  0.1192  48  ILE A CD1   
407  N  N     . GLU A 49  ? 1.1920 1.5078 1.0382 0.0545  0.0525  0.1550  49  GLU A N     
408  C  CA    . GLU A 49  ? 1.2066 1.5370 1.0414 0.0527  0.0434  0.1655  49  GLU A CA    
409  C  C     . GLU A 49  ? 1.2415 1.5680 1.0488 0.0478  0.0322  0.1490  49  GLU A C     
410  O  O     . GLU A 49  ? 1.2210 1.5553 1.0296 0.0436  0.0202  0.1540  49  GLU A O     
411  C  CB    . GLU A 49  ? 1.3095 1.6565 1.1274 0.0585  0.0520  0.1816  49  GLU A CB    
412  C  CG    . GLU A 49  ? 1.4894 1.8364 1.2651 0.0615  0.0576  0.1695  49  GLU A CG    
413  C  CD    . GLU A 49  ? 1.6022 1.9686 1.3538 0.0651  0.0600  0.1846  49  GLU A CD    
414  O  OE1   . GLU A 49  ? 1.6503 2.0306 1.4213 0.0664  0.0602  0.2068  49  GLU A OE1   
415  O  OE2   . GLU A 49  ? 1.5901 1.9574 1.3029 0.0666  0.0616  0.1742  49  GLU A OE2   
416  N  N     . GLU A 50  ? 1.2560 1.5705 1.0400 0.0480  0.0357  0.1295  50  GLU A N     
417  C  CA    . GLU A 50  ? 1.3129 1.6211 1.0728 0.0425  0.0248  0.1121  50  GLU A CA    
418  C  C     . GLU A 50  ? 1.2427 1.5354 1.0223 0.0370  0.0179  0.0984  50  GLU A C     
419  O  O     . GLU A 50  ? 1.1687 1.4594 0.9402 0.0308  0.0055  0.0895  50  GLU A O     
420  C  CB    . GLU A 50  ? 1.4110 1.7131 1.1329 0.0455  0.0318  0.0974  50  GLU A CB    
421  C  CG    . GLU A 50  ? 1.4962 1.8134 1.1841 0.0471  0.0305  0.1040  50  GLU A CG    
422  C  CD    . GLU A 50  ? 1.6085 1.9172 1.2571 0.0440  0.0252  0.0833  50  GLU A CD    
423  O  OE1   . GLU A 50  ? 1.5152 1.8071 1.1541 0.0458  0.0323  0.0658  50  GLU A OE1   
424  O  OE2   . GLU A 50  ? 1.7493 2.0679 1.3771 0.0396  0.0137  0.0847  50  GLU A OE2   
425  N  N     . VAL A 51  ? 1.1993 1.4818 1.0047 0.0389  0.0253  0.0974  51  VAL A N     
426  C  CA    . VAL A 51  ? 1.1828 1.4509 1.0064 0.0340  0.0195  0.0850  51  VAL A CA    
427  C  C     . VAL A 51  ? 1.2037 1.4779 1.0481 0.0292  0.0077  0.0930  51  VAL A C     
428  O  O     . VAL A 51  ? 1.1122 1.3793 0.9598 0.0236  -0.0015 0.0821  51  VAL A O     
429  C  CB    . VAL A 51  ? 1.1221 1.3799 0.9688 0.0372  0.0298  0.0842  51  VAL A CB    
430  C  CG1   . VAL A 51  ? 1.0361 1.2803 0.9020 0.0323  0.0238  0.0730  51  VAL A CG1   
431  C  CG2   . VAL A 51  ? 1.1722 1.4240 0.9989 0.0424  0.0416  0.0756  51  VAL A CG2   
432  N  N     . LYS A 52  ? 1.1071 1.3949 0.9666 0.0314  0.0080  0.1126  52  LYS A N     
433  C  CA    . LYS A 52  ? 1.1149 1.4096 0.9944 0.0279  -0.0024 0.1218  52  LYS A CA    
434  C  C     . LYS A 52  ? 1.0739 1.3773 0.9326 0.0234  -0.0147 0.1191  52  LYS A C     
435  O  O     . LYS A 52  ? 1.0089 1.3176 0.8839 0.0200  -0.0243 0.1246  52  LYS A O     
436  C  CB    . LYS A 52  ? 1.0646 1.3715 0.9644 0.0318  0.0015  0.1443  52  LYS A CB    
437  C  CG    . LYS A 52  ? 1.0320 1.3322 0.9522 0.0359  0.0132  0.1492  52  LYS A CG    
438  C  CD    . LYS A 52  ? 1.0722 1.3809 1.0211 0.0379  0.0141  0.1700  52  LYS A CD    
439  C  CE    . LYS A 52  ? 1.0408 1.3613 0.9839 0.0431  0.0235  0.1860  52  LYS A CE    
440  N  NZ    . LYS A 52  ? 1.0797 1.4161 0.9949 0.0440  0.0199  0.1929  52  LYS A NZ    
441  N  N     . LYS A 53  ? 1.1094 1.4145 0.9332 0.0232  -0.0147 0.1108  53  LYS A N     
442  C  CA    . LYS A 53  ? 1.0513 1.3671 0.8532 0.0188  -0.0269 0.1105  53  LYS A CA    
443  C  C     . LYS A 53  ? 1.1024 1.4071 0.8909 0.0120  -0.0360 0.0902  53  LYS A C     
444  O  O     . LYS A 53  ? 1.1168 1.4300 0.8970 0.0065  -0.0489 0.0905  53  LYS A O     
445  C  CB    . LYS A 53  ? 1.1620 1.4884 0.9306 0.0224  -0.0226 0.1153  53  LYS A CB    
446  C  CG    . LYS A 53  ? 1.1453 1.4917 0.9216 0.0257  -0.0225 0.1397  53  LYS A CG    
447  C  CD    . LYS A 53  ? 1.2097 1.5662 0.9521 0.0300  -0.0162 0.1444  53  LYS A CD    
448  C  CE    . LYS A 53  ? 1.2293 1.5882 0.9334 0.0251  -0.0266 0.1320  53  LYS A CE    
449  N  NZ    . LYS A 53  ? 1.2357 1.6139 0.9141 0.0273  -0.0277 0.1460  53  LYS A NZ    
450  N  N     . ILE A 54  ? 1.0904 1.3770 0.8775 0.0119  -0.0301 0.0734  54  ILE A N     
451  C  CA    . ILE A 54  ? 1.1061 1.3814 0.8819 0.0052  -0.0387 0.0546  54  ILE A CA    
452  C  C     . ILE A 54  ? 1.0233 1.3005 0.8265 -0.0002 -0.0491 0.0573  54  ILE A C     
453  O  O     . ILE A 54  ? 1.0136 1.2878 0.8473 0.0018  -0.0452 0.0634  54  ILE A O     
454  C  CB    . ILE A 54  ? 1.1354 1.3908 0.9062 0.0069  -0.0295 0.0375  54  ILE A CB    
455  C  CG1   . ILE A 54  ? 1.1012 1.3553 0.8507 0.0141  -0.0163 0.0371  54  ILE A CG1   
456  C  CG2   . ILE A 54  ? 1.3197 1.5635 1.0743 -0.0001 -0.0382 0.0183  54  ILE A CG2   
457  C  CD1   . ILE A 54  ? 1.1217 1.3737 0.8944 0.0206  -0.0033 0.0459  54  ILE A CD1   
458  N  N     . THR A 55  ? 1.0479 1.3303 0.8404 -0.0071 -0.0626 0.0529  55  THR A N     
459  C  CA    . THR A 55  ? 1.0219 1.3067 0.8382 -0.0126 -0.0729 0.0542  55  THR A CA    
460  C  C     . THR A 55  ? 1.0217 1.2934 0.8269 -0.0197 -0.0795 0.0346  55  THR A C     
461  O  O     . THR A 55  ? 1.0161 1.2778 0.7937 -0.0205 -0.0774 0.0206  55  THR A O     
462  C  CB    . THR A 55  ? 1.0652 1.3708 0.8838 -0.0151 -0.0844 0.0695  55  THR A CB    
463  O  OG1   . THR A 55  ? 1.1552 1.4681 0.9384 -0.0171 -0.0897 0.0671  55  THR A OG1   
464  C  CG2   . THR A 55  ? 1.0130 1.3299 0.8538 -0.0085 -0.0784 0.0903  55  THR A CG2   
465  N  N     . ALA A 56  ? 1.0810 1.3526 0.9091 -0.0246 -0.0871 0.0340  56  ALA A N     
466  C  CA    . ALA A 56  ? 1.1538 1.4154 0.9753 -0.0324 -0.0951 0.0179  56  ALA A CA    
467  C  C     . ALA A 56  ? 1.1244 1.3978 0.9677 -0.0381 -0.1074 0.0252  56  ALA A C     
468  O  O     . ALA A 56  ? 1.0793 1.3689 0.9373 -0.0360 -0.1103 0.0419  56  ALA A O     
469  C  CB    . ALA A 56  ? 1.0657 1.3070 0.8949 -0.0310 -0.0859 0.0046  56  ALA A CB    
470  N  N     . GLU A 57  ? 1.2348 1.4998 1.0824 -0.0450 -0.1138 0.0134  57  GLU A N     
471  C  CA    . GLU A 57  ? 1.2891 1.5648 1.1586 -0.0507 -0.1249 0.0194  57  GLU A CA    
472  C  C     . GLU A 57  ? 1.2976 1.5604 1.1884 -0.0525 -0.1216 0.0111  57  GLU A C     
473  O  O     . GLU A 57  ? 1.3124 1.5575 1.1934 -0.0531 -0.1160 -0.0034 57  GLU A O     
474  C  CB    . GLU A 57  ? 1.3518 1.6362 1.2013 -0.0598 -0.1406 0.0154  57  GLU A CB    
475  C  CG    . GLU A 57  ? 1.5664 1.8364 1.4049 -0.0683 -0.1467 -0.0031 57  GLU A CG    
476  C  CD    . GLU A 57  ? 1.6423 1.9123 1.5104 -0.0732 -0.1513 -0.0030 57  GLU A CD    
477  O  OE1   . GLU A 57  ? 1.7431 1.9980 1.6088 -0.0782 -0.1520 -0.0174 57  GLU A OE1   
478  O  OE2   . GLU A 57  ? 1.4510 1.7366 1.3450 -0.0720 -0.1543 0.0119  57  GLU A OE2   
479  N  N     . ARG A 58  ? 1.2769 1.5490 1.1974 -0.0529 -0.1244 0.0210  58  ARG A N     
480  C  CA    . ARG A 58  ? 1.2944 1.5570 1.2361 -0.0548 -0.1220 0.0150  58  ARG A CA    
481  C  C     . ARG A 58  ? 1.3304 1.6011 1.2804 -0.0638 -0.1351 0.0139  58  ARG A C     
482  O  O     . ARG A 58  ? 1.4219 1.6828 1.3599 -0.0707 -0.1401 0.0006  58  ARG A O     
483  C  CB    . ARG A 58  ? 1.1832 1.4482 1.1537 -0.0477 -0.1132 0.0260  58  ARG A CB    
484  C  CG    . ARG A 58  ? 1.0752 1.3236 1.0572 -0.0460 -0.1040 0.0169  58  ARG A CG    
485  C  CD    . ARG A 58  ? 0.9806 1.2279 0.9821 -0.0379 -0.0936 0.0257  58  ARG A CD    
486  N  NE    . ARG A 58  ? 1.2008 1.4607 1.2282 -0.0369 -0.0966 0.0376  58  ARG A NE    
487  C  CZ    . ARG A 58  ? 0.9555 1.2203 0.9999 -0.0303 -0.0910 0.0495  58  ARG A CZ    
488  N  NH1   . ARG A 58  ? 0.9331 1.1918 0.9726 -0.0246 -0.0826 0.0517  58  ARG A NH1   
489  N  NH2   . ARG A 58  ? 0.9953 1.2710 1.0634 -0.0293 -0.0937 0.0595  58  ARG A NH2   
490  N  N     . HIS A 59  ? 1.3246 1.6131 1.2964 -0.0637 -0.1408 0.0284  59  HIS A N     
491  C  CA    . HIS A 59  ? 1.2653 1.5655 1.2487 -0.0720 -0.1538 0.0307  59  HIS A CA    
492  C  C     . HIS A 59  ? 1.2176 1.5398 1.1996 -0.0732 -0.1644 0.0450  59  HIS A C     
493  O  O     . HIS A 59  ? 1.1522 1.4904 1.1596 -0.0722 -0.1682 0.0590  59  HIS A O     
494  C  CB    . HIS A 59  ? 1.1940 1.4954 1.2106 -0.0706 -0.1498 0.0351  59  HIS A CB    
495  C  CG    . HIS A 59  ? 1.3576 1.6412 1.3752 -0.0736 -0.1451 0.0208  59  HIS A CG    
496  N  ND1   . HIS A 59  ? 1.4789 1.7442 1.4725 -0.0746 -0.1410 0.0060  59  HIS A ND1   
497  C  CD2   . HIS A 59  ? 1.3942 1.6759 1.4340 -0.0755 -0.1435 0.0198  59  HIS A CD2   
498  C  CE1   . HIS A 59  ? 1.4428 1.6956 1.4444 -0.0772 -0.1376 -0.0031 59  HIS A CE1   
499  N  NE2   . HIS A 59  ? 1.4543 1.7169 1.4832 -0.0779 -0.1390 0.0050  59  HIS A NE2   
500  N  N     . GLY A 60  ? 1.2716 1.5946 1.2231 -0.0750 -0.1690 0.0416  60  GLY A N     
501  C  CA    . GLY A 60  ? 1.2928 1.6357 1.2371 -0.0750 -0.1777 0.0554  60  GLY A CA    
502  C  C     . GLY A 60  ? 1.3318 1.6795 1.2799 -0.0645 -0.1674 0.0685  60  GLY A C     
503  O  O     . GLY A 60  ? 1.3126 1.6702 1.2421 -0.0633 -0.1708 0.0755  60  GLY A O     
504  N  N     . THR A 61  ? 1.4296 1.7704 1.4017 -0.0572 -0.1552 0.0722  61  THR A N     
505  C  CA    . THR A 61  ? 1.3502 1.6929 1.3281 -0.0477 -0.1449 0.0838  61  THR A CA    
506  C  C     . THR A 61  ? 1.3198 1.6499 1.2687 -0.0447 -0.1368 0.0750  61  THR A C     
507  O  O     . THR A 61  ? 1.3191 1.6329 1.2515 -0.0475 -0.1340 0.0582  61  THR A O     
508  C  CB    . THR A 61  ? 1.3035 1.6388 1.3123 -0.0415 -0.1340 0.0869  61  THR A CB    
509  O  OG1   . THR A 61  ? 1.2665 1.5861 1.2775 -0.0450 -0.1311 0.0714  61  THR A OG1   
510  C  CG2   . THR A 61  ? 1.2109 1.5632 1.2504 -0.0402 -0.1388 0.1029  61  THR A CG2   
511  N  N     . VAL A 62  ? 1.2576 1.5956 1.2015 -0.0386 -0.1326 0.0873  62  VAL A N     
512  C  CA    . VAL A 62  ? 1.1575 1.4860 1.0772 -0.0344 -0.1232 0.0821  62  VAL A CA    
513  C  C     . VAL A 62  ? 1.1874 1.5034 1.1258 -0.0270 -0.1087 0.0828  62  VAL A C     
514  O  O     . VAL A 62  ? 1.1537 1.4739 1.1210 -0.0232 -0.1059 0.0940  62  VAL A O     
515  C  CB    . VAL A 62  ? 1.0798 1.4247 0.9828 -0.0321 -0.1264 0.0957  62  VAL A CB    
516  C  CG1   . VAL A 62  ? 0.9763 1.3295 0.9026 -0.0240 -0.1191 0.1149  62  VAL A CG1   
517  C  CG2   . VAL A 62  ? 1.1712 1.5079 1.0374 -0.0314 -0.1218 0.0851  62  VAL A CG2   
518  N  N     . VAL A 63  ? 1.1157 1.4157 1.0383 -0.0253 -0.0996 0.0703  63  VAL A N     
519  C  CA    . VAL A 63  ? 1.0021 1.2897 0.9398 -0.0192 -0.0865 0.0698  63  VAL A CA    
520  C  C     . VAL A 63  ? 0.9741 1.2617 0.8953 -0.0136 -0.0779 0.0741  63  VAL A C     
521  O  O     . VAL A 63  ? 0.9404 1.2250 0.8325 -0.0148 -0.0778 0.0655  63  VAL A O     
522  C  CB    . VAL A 63  ? 0.9930 1.2619 0.9313 -0.0216 -0.0826 0.0524  63  VAL A CB    
523  C  CG1   . VAL A 63  ? 0.9503 1.2197 0.9125 -0.0252 -0.0879 0.0516  63  VAL A CG1   
524  C  CG2   . VAL A 63  ? 1.0598 1.3212 0.9679 -0.0262 -0.0858 0.0372  63  VAL A CG2   
525  N  N     . THR A 64  ? 0.9387 1.2295 0.8787 -0.0074 -0.0706 0.0876  64  THR A N     
526  C  CA    . THR A 64  ? 0.9503 1.2440 0.8805 -0.0018 -0.0622 0.0959  64  THR A CA    
527  C  C     . THR A 64  ? 0.8661 1.1472 0.8143 0.0029  -0.0503 0.0953  64  THR A C     
528  O  O     . THR A 64  ? 0.8673 1.1410 0.8391 0.0025  -0.0495 0.0933  64  THR A O     
529  C  CB    . THR A 64  ? 0.8852 1.1977 0.8225 0.0008  -0.0657 0.1165  64  THR A CB    
530  O  OG1   . THR A 64  ? 0.8529 1.1648 0.8232 0.0047  -0.0614 0.1278  64  THR A OG1   
531  C  CG2   . THR A 64  ? 0.9088 1.2350 0.8409 -0.0046 -0.0797 0.1193  64  THR A CG2   
532  N  N     . VAL A 65  ? 0.8581 1.1373 0.7948 0.0072  -0.0412 0.0973  65  VAL A N     
533  C  CA    . VAL A 65  ? 0.8903 1.1602 0.8451 0.0115  -0.0305 0.0998  65  VAL A CA    
534  C  C     . VAL A 65  ? 0.8728 1.1515 0.8535 0.0146  -0.0301 0.1182  65  VAL A C     
535  O  O     . VAL A 65  ? 0.9762 1.2681 0.9524 0.0172  -0.0300 0.1327  65  VAL A O     
536  C  CB    . VAL A 65  ? 0.8852 1.1524 0.8217 0.0154  -0.0206 0.0980  65  VAL A CB    
537  C  CG1   . VAL A 65  ? 0.8974 1.1554 0.8546 0.0189  -0.0107 0.1005  65  VAL A CG1   
538  C  CG2   . VAL A 65  ? 0.8906 1.1488 0.8004 0.0128  -0.0213 0.0797  65  VAL A CG2   
539  N  N     . LYS A 66  ? 0.7508 1.0217 0.7580 0.0144  -0.0298 0.1179  66  LYS A N     
540  C  CA    . LYS A 66  ? 0.7067 0.9834 0.7403 0.0173  -0.0296 0.1339  66  LYS A CA    
541  C  C     . LYS A 66  ? 0.8029 1.0807 0.8426 0.0219  -0.0207 0.1457  66  LYS A C     
542  O  O     . LYS A 66  ? 0.8139 1.1049 0.8532 0.0244  -0.0211 0.1615  66  LYS A O     
543  C  CB    . LYS A 66  ? 0.7218 0.9874 0.7802 0.0164  -0.0298 0.1284  66  LYS A CB    
544  C  CG    . LYS A 66  ? 0.8170 1.0841 0.9039 0.0200  -0.0278 0.1429  66  LYS A CG    
545  C  CD    . LYS A 66  ? 0.7981 1.0562 0.9060 0.0192  -0.0294 0.1369  66  LYS A CD    
546  C  CE    . LYS A 66  ? 0.9036 1.1508 1.0353 0.0222  -0.0227 0.1412  66  LYS A CE    
547  N  NZ    . LYS A 66  ? 0.9102 1.1439 1.0547 0.0210  -0.0221 0.1295  66  LYS A NZ    
548  N  N     . ARG A 67  ? 0.7976 1.0624 0.8438 0.0228  -0.0130 0.1391  67  ARG A N     
549  C  CA    . ARG A 67  ? 0.7814 1.0469 0.8352 0.0266  -0.0045 0.1499  67  ARG A CA    
550  C  C     . ARG A 67  ? 0.8054 1.0602 0.8499 0.0266  0.0027  0.1382  67  ARG A C     
551  O  O     . ARG A 67  ? 0.7909 1.0343 0.8328 0.0239  0.0015  0.1227  67  ARG A O     
552  C  CB    . ARG A 67  ? 0.7512 1.0125 0.8372 0.0281  -0.0030 0.1603  67  ARG A CB    
553  C  CG    . ARG A 67  ? 0.7919 1.0369 0.8935 0.0259  -0.0031 0.1478  67  ARG A CG    
554  C  CD    . ARG A 67  ? 0.8501 1.0910 0.9813 0.0273  -0.0032 0.1571  67  ARG A CD    
555  N  NE    . ARG A 67  ? 0.8290 1.0536 0.9746 0.0261  0.0004  0.1483  67  ARG A NE    
556  C  CZ    . ARG A 67  ? 0.8932 1.1122 1.0461 0.0266  0.0064  0.1511  67  ARG A CZ    
557  N  NH1   . ARG A 67  ? 0.8691 1.0975 1.0172 0.0287  0.0107  0.1629  67  ARG A NH1   
558  N  NH2   . ARG A 67  ? 0.8256 1.0300 0.9909 0.0248  0.0081  0.1424  67  ARG A NH2   
559  N  N     . VAL A 68  ? 0.7905 1.0499 0.8309 0.0300  0.0105  0.1467  68  VAL A N     
560  C  CA    . VAL A 68  ? 0.8120 1.0633 0.8460 0.0310  0.0184  0.1383  68  VAL A CA    
561  C  C     . VAL A 68  ? 0.8384 1.0866 0.8978 0.0327  0.0247  0.1487  68  VAL A C     
562  O  O     . VAL A 68  ? 0.7988 1.0528 0.8759 0.0338  0.0243  0.1638  68  VAL A O     
563  C  CB    . VAL A 68  ? 0.8440 1.1034 0.8491 0.0337  0.0232  0.1378  68  VAL A CB    
564  C  CG1   . VAL A 68  ? 0.8225 1.0850 0.8022 0.0312  0.0154  0.1281  68  VAL A CG1   
565  C  CG2   . VAL A 68  ? 0.8893 1.1629 0.8965 0.0377  0.0281  0.1574  68  VAL A CG2   
566  N  N     . GLU A 69  ? 0.7769 1.0156 0.8390 0.0326  0.0303  0.1406  69  GLU A N     
567  C  CA    . GLU A 69  ? 0.7547 0.9897 0.8414 0.0332  0.0355  0.1490  69  GLU A CA    
568  C  C     . GLU A 69  ? 0.8233 1.0544 0.9042 0.0345  0.0432  0.1430  69  GLU A C     
569  O  O     . GLU A 69  ? 0.8533 1.0752 0.9247 0.0330  0.0423  0.1276  69  GLU A O     
570  C  CB    . GLU A 69  ? 0.7102 0.9330 0.8200 0.0297  0.0303  0.1446  69  GLU A CB    
571  C  CG    . GLU A 69  ? 0.8710 1.0862 1.0040 0.0287  0.0342  0.1484  69  GLU A CG    
572  C  CD    . GLU A 69  ? 0.9063 1.1103 1.0612 0.0257  0.0289  0.1461  69  GLU A CD    
573  O  OE1   . GLU A 69  ? 0.9900 1.1972 1.1560 0.0264  0.0260  0.1556  69  GLU A OE1   
574  O  OE2   . GLU A 69  ? 0.8650 1.0570 1.0256 0.0229  0.0279  0.1347  69  GLU A OE2   
575  N  N     . LYS A 70  ? 0.7669 1.0054 0.8551 0.0375  0.0509  0.1561  70  LYS A N     
576  C  CA    . LYS A 70  ? 0.7229 0.9596 0.8092 0.0394  0.0591  0.1528  70  LYS A CA    
577  C  C     . LYS A 70  ? 0.7395 0.9645 0.8505 0.0359  0.0580  0.1492  70  LYS A C     
578  O  O     . LYS A 70  ? 0.8040 1.0275 0.9388 0.0338  0.0557  0.1586  70  LYS A O     
579  C  CB    . LYS A 70  ? 0.8435 1.0940 0.9297 0.0440  0.0683  0.1694  70  LYS A CB    
580  C  CG    . LYS A 70  ? 0.8845 1.1359 0.9652 0.0475  0.0782  0.1669  70  LYS A CG    
581  C  CD    . LYS A 70  ? 0.9068 1.1667 1.0097 0.0493  0.0858  0.1850  70  LYS A CD    
582  C  CE    . LYS A 70  ? 0.9444 1.2209 1.0332 0.0547  0.0933  0.1993  70  LYS A CE    
583  N  NZ    . LYS A 70  ? 1.0244 1.3101 1.1390 0.0549  0.0970  0.2207  70  LYS A NZ    
584  N  N     . VAL A 71  ? 0.6468 0.8634 0.7521 0.0353  0.0593  0.1358  71  VAL A N     
585  C  CA    . VAL A 71  ? 0.6978 0.9032 0.8233 0.0315  0.0569  0.1306  71  VAL A CA    
586  C  C     . VAL A 71  ? 0.7542 0.9594 0.8785 0.0336  0.0642  0.1277  71  VAL A C     
587  O  O     . VAL A 71  ? 0.8109 1.0196 0.9143 0.0376  0.0696  0.1229  71  VAL A O     
588  C  CB    . VAL A 71  ? 0.7219 0.9155 0.8439 0.0274  0.0483  0.1157  71  VAL A CB    
589  C  CG1   . VAL A 71  ? 0.8090 0.9914 0.9396 0.0245  0.0472  0.1055  71  VAL A CG1   
590  C  CG2   . VAL A 71  ? 0.7472 0.9390 0.8831 0.0249  0.0418  0.1210  71  VAL A CG2   
591  N  N     . GLN A 72  ? 0.6061 0.8074 0.7534 0.0310  0.0644  0.1311  72  GLN A N     
592  C  CA    . GLN A 72  ? 0.5924 0.7935 0.7436 0.0325  0.0704  0.1294  72  GLN A CA    
593  C  C     . GLN A 72  ? 0.6043 0.7923 0.7587 0.0283  0.0643  0.1152  72  GLN A C     
594  O  O     . GLN A 72  ? 0.5616 0.7421 0.7317 0.0231  0.0572  0.1141  72  GLN A O     
595  C  CB    . GLN A 72  ? 0.6409 0.8493 0.8171 0.0323  0.0748  0.1454  72  GLN A CB    
596  C  CG    . GLN A 72  ? 0.8326 1.0486 1.0093 0.0369  0.0848  0.1495  72  GLN A CG    
597  C  CD    . GLN A 72  ? 0.8549 1.0769 1.0609 0.0351  0.0874  0.1645  72  GLN A CD    
598  O  OE1   . GLN A 72  ? 0.9508 1.1712 1.1757 0.0304  0.0819  0.1722  72  GLN A OE1   
599  N  NE2   . GLN A 72  ? 0.9300 1.1587 1.1412 0.0386  0.0957  0.1686  72  GLN A NE2   
600  N  N     . LYS A 73  ? 0.5621 0.7470 0.7012 0.0307  0.0673  0.1045  73  LYS A N     
601  C  CA    . LYS A 73  ? 0.6375 0.8109 0.7782 0.0272  0.0622  0.0917  73  LYS A CA    
602  C  C     . LYS A 73  ? 0.7049 0.8795 0.8483 0.0302  0.0689  0.0911  73  LYS A C     
603  O  O     . LYS A 73  ? 0.7790 0.9634 0.9244 0.0350  0.0777  0.1006  73  LYS A O     
604  C  CB    . LYS A 73  ? 0.6178 0.7840 0.7372 0.0264  0.0574  0.0777  73  LYS A CB    
605  C  CG    . LYS A 73  ? 0.6127 0.7790 0.7300 0.0240  0.0510  0.0789  73  LYS A CG    
606  C  CD    . LYS A 73  ? 0.5166 0.6760 0.6169 0.0222  0.0454  0.0654  73  LYS A CD    
607  C  CE    . LYS A 73  ? 0.4089 0.5572 0.5183 0.0175  0.0392  0.0564  73  LYS A CE    
608  N  NZ    . LYS A 73  ? 0.5554 0.7014 0.6818 0.0141  0.0339  0.0611  73  LYS A NZ    
609  N  N     . LYS A 74  ? 0.6656 0.8310 0.8102 0.0276  0.0650  0.0808  74  LYS A N     
610  C  CA    . LYS A 74  ? 0.6657 0.8315 0.8149 0.0303  0.0705  0.0799  74  LYS A CA    
611  C  C     . LYS A 74  ? 0.7504 0.9084 0.8788 0.0325  0.0713  0.0658  74  LYS A C     
612  O  O     . LYS A 74  ? 0.7996 0.9480 0.9247 0.0283  0.0639  0.0557  74  LYS A O     
613  C  CB    . LYS A 74  ? 0.7225 0.8850 0.8944 0.0250  0.0649  0.0820  74  LYS A CB    
614  C  CG    . LYS A 74  ? 0.7782 0.9460 0.9721 0.0214  0.0624  0.0947  74  LYS A CG    
615  C  CD    . LYS A 74  ? 0.8511 1.0100 1.0586 0.0138  0.0520  0.0908  74  LYS A CD    
616  C  CE    . LYS A 74  ? 0.9141 1.0729 1.1353 0.0121  0.0511  0.0914  74  LYS A CE    
617  N  NZ    . LYS A 74  ? 0.7779 0.9272 1.0076 0.0045  0.0405  0.0856  74  LYS A NZ    
618  N  N     . PHE A 75  ? 0.7750 0.9367 0.8894 0.0391  0.0806  0.0652  75  PHE A N     
619  C  CA    . PHE A 75  ? 0.7272 0.8807 0.8233 0.0418  0.0827  0.0522  75  PHE A CA    
620  C  C     . PHE A 75  ? 0.8822 1.0365 0.9875 0.0463  0.0905  0.0542  75  PHE A C     
621  O  O     . PHE A 75  ? 1.0182 1.1825 1.1323 0.0510  0.0990  0.0651  75  PHE A O     
622  C  CB    . PHE A 75  ? 0.7241 0.8790 0.7943 0.0459  0.0870  0.0479  75  PHE A CB    
623  C  CG    . PHE A 75  ? 0.8070 0.9504 0.8571 0.0452  0.0840  0.0322  75  PHE A CG    
624  C  CD1   . PHE A 75  ? 0.7165 0.8512 0.7691 0.0388  0.0739  0.0242  75  PHE A CD1   
625  C  CD2   . PHE A 75  ? 0.7883 0.9294 0.8174 0.0509  0.0914  0.0255  75  PHE A CD2   
626  C  CE1   . PHE A 75  ? 0.7110 0.8355 0.7471 0.0377  0.0710  0.0108  75  PHE A CE1   
627  C  CE2   . PHE A 75  ? 0.7930 0.9225 0.8047 0.0495  0.0880  0.0109  75  PHE A CE2   
628  C  CZ    . PHE A 75  ? 0.7173 0.8389 0.7334 0.0427  0.0777  0.0041  75  PHE A CZ    
629  N  N     . LEU A 76  ? 0.8052 0.9496 0.9095 0.0452  0.0879  0.0445  76  LEU A N     
630  C  CA    . LEU A 76  ? 0.9370 1.0814 1.0534 0.0489  0.0936  0.0464  76  LEU A CA    
631  C  C     . LEU A 76  ? 0.9559 1.1112 1.0988 0.0482  0.0950  0.0612  76  LEU A C     
632  O  O     . LEU A 76  ? 0.9574 1.1195 1.1098 0.0541  0.1043  0.0684  76  LEU A O     
633  C  CB    . LEU A 76  ? 0.9876 1.1310 1.0880 0.0576  0.1054  0.0423  76  LEU A CB    
634  C  CG    . LEU A 76  ? 1.2492 1.4015 1.3370 0.0642  0.1156  0.0476  76  LEU A CG    
635  C  CD1   . LEU A 76  ? 1.0195 1.1826 1.1236 0.0710  0.1272  0.0600  76  LEU A CD1   
636  C  CD2   . LEU A 76  ? 1.0908 1.2344 1.1489 0.0682  0.1196  0.0344  76  LEU A CD2   
637  N  N     . GLY A 77  ? 1.0173 1.1740 1.1731 0.0411  0.0859  0.0659  77  GLY A N     
638  C  CA    . GLY A 77  ? 0.9975 1.1632 1.1794 0.0387  0.0850  0.0792  77  GLY A CA    
639  C  C     . GLY A 77  ? 0.9769 1.1548 1.1648 0.0417  0.0918  0.0924  77  GLY A C     
640  O  O     . GLY A 77  ? 1.0570 1.2414 1.2666 0.0378  0.0887  0.1035  77  GLY A O     
641  N  N     . ARG A 78  ? 0.9293 1.1107 1.0986 0.0484  0.1007  0.0917  78  ARG A N     
642  C  CA    . ARG A 78  ? 0.9267 1.1207 1.0978 0.0527  0.1092  0.1043  78  ARG A CA    
643  C  C     . ARG A 78  ? 0.9404 1.1347 1.1023 0.0493  0.1037  0.1054  78  ARG A C     
644  O  O     . ARG A 78  ? 0.8582 1.0436 1.0011 0.0473  0.0980  0.0937  78  ARG A O     
645  C  CB    . ARG A 78  ? 0.9786 1.1758 1.1314 0.0624  0.1224  0.1021  78  ARG A CB    
646  C  CG    . ARG A 78  ? 1.0324 1.2357 1.2008 0.0681  0.1320  0.1086  78  ARG A CG    
647  C  CD    . ARG A 78  ? 1.0282 1.2479 1.2180 0.0700  0.1387  0.1276  78  ARG A CD    
648  N  NE    . ARG A 78  ? 1.1604 1.3864 1.3789 0.0700  0.1405  0.1368  78  ARG A NE    
649  C  CZ    . ARG A 78  ? 1.0634 1.2900 1.2848 0.0766  0.1490  0.1354  78  ARG A CZ    
650  N  NH1   . ARG A 78  ? 1.0690 1.2888 1.2655 0.0841  0.1572  0.1242  78  ARG A NH1   
651  N  NH2   . ARG A 78  ? 0.9761 1.2103 1.2266 0.0756  0.1492  0.1457  78  ARG A NH2   
652  N  N     . PRO A 79  ? 0.9516 1.1564 1.1282 0.0485  0.1054  0.1201  79  PRO A N     
653  C  CA    . PRO A 79  ? 0.8606 1.0668 1.0296 0.0463  0.1013  0.1230  79  PRO A CA    
654  C  C     . PRO A 79  ? 0.8072 1.0163 0.9474 0.0524  0.1079  0.1192  79  PRO A C     
655  O  O     . PRO A 79  ? 0.8541 1.0696 0.9855 0.0597  0.1192  0.1216  79  PRO A O     
656  C  CB    . PRO A 79  ? 0.8783 1.0959 1.0722 0.0450  0.1036  0.1415  79  PRO A CB    
657  C  CG    . PRO A 79  ? 0.8770 1.0961 1.0947 0.0434  0.1041  0.1458  79  PRO A CG    
658  C  CD    . PRO A 79  ? 0.9005 1.1162 1.1043 0.0490  0.1101  0.1356  79  PRO A CD    
659  N  N     . VAL A 80  ? 0.7478 0.9525 0.8732 0.0496  0.1008  0.1133  80  VAL A N     
660  C  CA    . VAL A 80  ? 0.7795 0.9864 0.8761 0.0540  0.1045  0.1087  80  VAL A CA    
661  C  C     . VAL A 80  ? 0.7866 0.9957 0.8801 0.0503  0.0970  0.1127  80  VAL A C     
662  O  O     . VAL A 80  ? 0.6950 0.8989 0.8036 0.0442  0.0878  0.1128  80  VAL A O     
663  C  CB    . VAL A 80  ? 0.7869 0.9821 0.8616 0.0548  0.1030  0.0904  80  VAL A CB    
664  C  CG1   . VAL A 80  ? 0.6390 0.8238 0.7113 0.0479  0.0904  0.0800  80  VAL A CG1   
665  C  CG2   . VAL A 80  ? 0.7959 0.9943 0.8411 0.0610  0.1104  0.0863  80  VAL A CG2   
666  N  N     . GLU A 81  ? 0.8016 1.0189 0.8754 0.0544  0.1013  0.1165  81  GLU A N     
667  C  CA    . GLU A 81  ? 0.7647 0.9861 0.8338 0.0519  0.0949  0.1217  81  GLU A CA    
668  C  C     . GLU A 81  ? 0.7460 0.9606 0.7893 0.0506  0.0885  0.1069  81  GLU A C     
669  O  O     . GLU A 81  ? 0.7611 0.9759 0.7795 0.0546  0.0935  0.0995  81  GLU A O     
670  C  CB    . GLU A 81  ? 0.8344 1.0712 0.8993 0.0568  0.1030  0.1377  81  GLU A CB    
671  C  CG    . GLU A 81  ? 0.9076 1.1509 0.9893 0.0537  0.0980  0.1522  81  GLU A CG    
672  C  CD    . GLU A 81  ? 1.0866 1.3460 1.1677 0.0586  0.1070  0.1703  81  GLU A CD    
673  O  OE1   . GLU A 81  ? 1.0094 1.2759 1.0640 0.0627  0.1104  0.1700  81  GLU A OE1   
674  O  OE2   . GLU A 81  ? 1.2063 1.4716 1.3134 0.0581  0.1103  0.1850  81  GLU A OE2   
675  N  N     . VAL A 82  ? 0.7312 0.9394 0.7806 0.0448  0.0778  0.1024  82  VAL A N     
676  C  CA    . VAL A 82  ? 0.7873 0.9896 0.8168 0.0424  0.0704  0.0895  82  VAL A CA    
677  C  C     . VAL A 82  ? 0.7775 0.9866 0.8080 0.0403  0.0636  0.0976  82  VAL A C     
678  O  O     . VAL A 82  ? 0.7286 0.9435 0.7785 0.0399  0.0636  0.1114  82  VAL A O     
679  C  CB    . VAL A 82  ? 0.6900 0.8783 0.7262 0.0378  0.0639  0.0759  82  VAL A CB    
680  C  CG1   . VAL A 82  ? 0.8558 1.0412 0.9117 0.0326  0.0553  0.0791  82  VAL A CG1   
681  C  CG2   . VAL A 82  ? 0.7973 0.9789 0.8094 0.0370  0.0605  0.0606  82  VAL A CG2   
682  N  N     . TRP A 83  ? 0.7114 0.9198 0.7218 0.0388  0.0576  0.0894  83  TRP A N     
683  C  CA    . TRP A 83  ? 0.7812 0.9967 0.7914 0.0369  0.0505  0.0966  83  TRP A CA    
684  C  C     . TRP A 83  ? 0.7365 0.9431 0.7519 0.0316  0.0405  0.0865  83  TRP A C     
685  O  O     . TRP A 83  ? 0.6862 0.8869 0.6850 0.0297  0.0369  0.0729  83  TRP A O     
686  C  CB    . TRP A 83  ? 0.7880 1.0134 0.7705 0.0395  0.0514  0.0979  83  TRP A CB    
687  C  CG    . TRP A 83  ? 0.8623 1.1003 0.8429 0.0447  0.0603  0.1131  83  TRP A CG    
688  C  CD1   . TRP A 83  ? 0.9214 1.1622 0.8877 0.0499  0.0708  0.1126  83  TRP A CD1   
689  C  CD2   . TRP A 83  ? 0.8768 1.1266 0.8710 0.0456  0.0602  0.1317  83  TRP A CD2   
690  N  NE1   . TRP A 83  ? 0.9331 1.1876 0.9028 0.0538  0.0774  0.1301  83  TRP A NE1   
691  C  CE2   . TRP A 83  ? 0.8936 1.1538 0.8807 0.0511  0.0708  0.1423  83  TRP A CE2   
692  C  CE3   . TRP A 83  ? 0.8630 1.1155 0.8755 0.0426  0.0527  0.1408  83  TRP A CE3   
693  C  CZ2   . TRP A 83  ? 0.9006 1.1740 0.8984 0.0531  0.0736  0.1623  83  TRP A CZ2   
694  C  CZ3   . TRP A 83  ? 0.8698 1.1343 0.8932 0.0448  0.0553  0.1601  83  TRP A CZ3   
695  C  CH2   . TRP A 83  ? 0.8790 1.1541 0.8952 0.0498  0.0655  0.1710  83  TRP A CH2   
696  N  N     . LYS A 84  ? 0.6888 0.8938 0.7279 0.0292  0.0366  0.0929  84  LYS A N     
697  C  CA    . LYS A 84  ? 0.7189 0.9179 0.7644 0.0250  0.0278  0.0861  84  LYS A CA    
698  C  C     . LYS A 84  ? 0.6936 0.9020 0.7269 0.0246  0.0219  0.0897  84  LYS A C     
699  O  O     . LYS A 84  ? 0.6610 0.8799 0.6993 0.0266  0.0222  0.1039  84  LYS A O     
700  C  CB    . LYS A 84  ? 0.6870 0.8816 0.7603 0.0235  0.0264  0.0928  84  LYS A CB    
701  C  CG    . LYS A 84  ? 0.6770 0.8601 0.7594 0.0196  0.0209  0.0819  84  LYS A CG    
702  C  CD    . LYS A 84  ? 0.5763 0.7535 0.6843 0.0185  0.0210  0.0875  84  LYS A CD    
703  C  CE    . LYS A 84  ? 0.6228 0.7891 0.7384 0.0151  0.0159  0.0771  84  LYS A CE    
704  N  NZ    . LYS A 84  ? 0.5642 0.7233 0.7025 0.0139  0.0157  0.0812  84  LYS A NZ    
705  N  N     . LEU A 85  ? 0.6853 0.8906 0.7035 0.0219  0.0161  0.0777  85  LEU A N     
706  C  CA    . LEU A 85  ? 0.6767 0.8911 0.6839 0.0204  0.0088  0.0799  85  LEU A CA    
707  C  C     . LEU A 85  ? 0.6487 0.8591 0.6715 0.0168  0.0014  0.0770  85  LEU A C     
708  O  O     . LEU A 85  ? 0.6335 0.8338 0.6564 0.0139  -0.0007 0.0643  85  LEU A O     
709  C  CB    . LEU A 85  ? 0.6652 0.8793 0.6434 0.0193  0.0071  0.0685  85  LEU A CB    
710  C  CG    . LEU A 85  ? 0.7580 0.9734 0.7169 0.0233  0.0156  0.0675  85  LEU A CG    
711  C  CD1   . LEU A 85  ? 0.7372 0.9547 0.6659 0.0220  0.0119  0.0585  85  LEU A CD1   
712  C  CD2   . LEU A 85  ? 0.7551 0.9819 0.7202 0.0279  0.0217  0.0847  85  LEU A CD2   
713  N  N     . TYR A 86  ? 0.6904 0.9089 0.7271 0.0175  -0.0020 0.0893  86  TYR A N     
714  C  CA    . TYR A 86  ? 0.6651 0.8818 0.7178 0.0153  -0.0081 0.0885  86  TYR A CA    
715  C  C     . TYR A 86  ? 0.6295 0.8554 0.6698 0.0128  -0.0165 0.0873  86  TYR A C     
716  O  O     . TYR A 86  ? 0.6432 0.8795 0.6659 0.0133  -0.0183 0.0919  86  TYR A O     
717  C  CB    . TYR A 86  ? 0.6594 0.8789 0.7363 0.0178  -0.0069 0.1028  86  TYR A CB    
718  C  CG    . TYR A 86  ? 0.6648 0.8742 0.7581 0.0190  -0.0004 0.1038  86  TYR A CG    
719  C  CD1   . TYR A 86  ? 0.6541 0.8510 0.7621 0.0173  -0.0007 0.0958  86  TYR A CD1   
720  C  CD2   . TYR A 86  ? 0.7078 0.9206 0.8018 0.0216  0.0058  0.1131  86  TYR A CD2   
721  C  CE1   . TYR A 86  ? 0.6679 0.8556 0.7901 0.0176  0.0040  0.0965  86  TYR A CE1   
722  C  CE2   . TYR A 86  ? 0.7021 0.9063 0.8125 0.0219  0.0108  0.1146  86  TYR A CE2   
723  C  CZ    . TYR A 86  ? 0.6854 0.8768 0.8096 0.0196  0.0093  0.1059  86  TYR A CZ    
724  O  OH    . TYR A 86  ? 0.6526 0.8354 0.7923 0.0192  0.0131  0.1070  86  TYR A OH    
725  N  N     . PHE A 87  ? 0.5862 0.8087 0.6358 0.0099  -0.0218 0.0813  87  PHE A N     
726  C  CA    . PHE A 87  ? 0.6674 0.8988 0.7091 0.0067  -0.0306 0.0802  87  PHE A CA    
727  C  C     . PHE A 87  ? 0.6563 0.8906 0.7216 0.0068  -0.0343 0.0861  87  PHE A C     
728  O  O     . PHE A 87  ? 0.6847 0.9113 0.7697 0.0091  -0.0299 0.0880  87  PHE A O     
729  C  CB    . PHE A 87  ? 0.6173 0.8416 0.6420 0.0022  -0.0336 0.0639  87  PHE A CB    
730  C  CG    . PHE A 87  ? 0.6876 0.9078 0.6892 0.0027  -0.0292 0.0571  87  PHE A CG    
731  C  CD1   . PHE A 87  ? 0.7110 0.9399 0.6895 0.0020  -0.0327 0.0578  87  PHE A CD1   
732  C  CD2   . PHE A 87  ? 0.6436 0.8514 0.6465 0.0043  -0.0215 0.0502  87  PHE A CD2   
733  C  CE1   . PHE A 87  ? 0.7500 0.9743 0.7066 0.0033  -0.0275 0.0510  87  PHE A CE1   
734  C  CE2   . PHE A 87  ? 0.6168 0.8210 0.6001 0.0057  -0.0164 0.0444  87  PHE A CE2   
735  C  CZ    . PHE A 87  ? 0.6897 0.9016 0.6494 0.0055  -0.0189 0.0445  87  PHE A CZ    
736  N  N     . THR A 88  ? 0.7095 0.9548 0.7725 0.0044  -0.0426 0.0889  88  THR A N     
737  C  CA    . THR A 88  ? 0.5705 0.8203 0.6564 0.0050  -0.0460 0.0952  88  THR A CA    
738  C  C     . THR A 88  ? 0.5969 0.8363 0.6907 0.0025  -0.0458 0.0829  88  THR A C     
739  O  O     . THR A 88  ? 0.5332 0.7664 0.6472 0.0049  -0.0421 0.0841  88  THR A O     
740  C  CB    . THR A 88  ? 0.6275 0.8948 0.7100 0.0033  -0.0553 0.1041  88  THR A CB    
741  O  OG1   . THR A 88  ? 0.6650 0.9425 0.7378 0.0057  -0.0553 0.1160  88  THR A OG1   
742  C  CG2   . THR A 88  ? 0.6237 0.8970 0.7326 0.0051  -0.0578 0.1129  88  THR A CG2   
743  N  N     . HIS A 89  ? 0.6215 0.8583 0.6991 -0.0025 -0.0496 0.0708  89  HIS A N     
744  C  CA    . HIS A 89  ? 0.6149 0.8437 0.6986 -0.0055 -0.0502 0.0600  89  HIS A CA    
745  C  C     . HIS A 89  ? 0.6141 0.8300 0.6808 -0.0081 -0.0471 0.0459  89  HIS A C     
746  O  O     . HIS A 89  ? 0.6381 0.8546 0.6844 -0.0092 -0.0479 0.0429  89  HIS A O     
747  C  CB    . HIS A 89  ? 0.6050 0.8452 0.6899 -0.0099 -0.0595 0.0608  89  HIS A CB    
748  C  CG    . HIS A 89  ? 0.5792 0.8155 0.6801 -0.0113 -0.0593 0.0559  89  HIS A CG    
749  N  ND1   . HIS A 89  ? 0.5804 0.8082 0.6740 -0.0159 -0.0599 0.0431  89  HIS A ND1   
750  C  CD2   . HIS A 89  ? 0.5601 0.8000 0.6842 -0.0083 -0.0578 0.0626  89  HIS A CD2   
751  C  CE1   . HIS A 89  ? 0.6381 0.8654 0.7492 -0.0158 -0.0589 0.0425  89  HIS A CE1   
752  N  NE2   . HIS A 89  ? 0.6221 0.8565 0.7515 -0.0111 -0.0573 0.0537  89  HIS A NE2   
753  N  N     . PRO A 90  ? 0.5610 0.7652 0.6354 -0.0088 -0.0433 0.0373  90  PRO A N     
754  C  CA    . PRO A 90  ? 0.6157 0.8080 0.6757 -0.0110 -0.0405 0.0248  90  PRO A CA    
755  C  C     . PRO A 90  ? 0.6757 0.8698 0.7178 -0.0163 -0.0469 0.0171  90  PRO A C     
756  O  O     . PRO A 90  ? 0.7217 0.9091 0.7462 -0.0170 -0.0450 0.0098  90  PRO A O     
757  C  CB    . PRO A 90  ? 0.6227 0.8050 0.6963 -0.0113 -0.0370 0.0189  90  PRO A CB    
758  C  CG    . PRO A 90  ? 0.5691 0.7553 0.6630 -0.0075 -0.0353 0.0282  90  PRO A CG    
759  C  CD    . PRO A 90  ? 0.5366 0.7378 0.6325 -0.0070 -0.0408 0.0389  90  PRO A CD    
760  N  N     . GLN A 91  ? 0.6479 0.8510 0.6946 -0.0200 -0.0546 0.0188  91  GLN A N     
761  C  CA    . GLN A 91  ? 0.6958 0.9007 0.7264 -0.0260 -0.0621 0.0115  91  GLN A CA    
762  C  C     . GLN A 91  ? 0.7166 0.9270 0.7257 -0.0260 -0.0650 0.0132  91  GLN A C     
763  O  O     . GLN A 91  ? 0.8090 1.0176 0.8002 -0.0309 -0.0703 0.0049  91  GLN A O     
764  C  CB    . GLN A 91  ? 0.7286 0.9442 0.7719 -0.0302 -0.0703 0.0152  91  GLN A CB    
765  C  CG    . GLN A 91  ? 0.6723 0.8837 0.7364 -0.0296 -0.0667 0.0141  91  GLN A CG    
766  C  CD    . GLN A 91  ? 0.7921 1.0137 0.8679 -0.0344 -0.0743 0.0164  91  GLN A CD    
767  O  OE1   . GLN A 91  ? 0.8383 1.0686 0.9055 -0.0395 -0.0834 0.0168  91  GLN A OE1   
768  N  NE2   . GLN A 91  ? 0.6439 0.8649 0.7393 -0.0328 -0.0706 0.0181  91  GLN A NE2   
769  N  N     . ASP A 92  ? 0.7019 0.9185 0.7120 -0.0208 -0.0613 0.0236  92  ASP A N     
770  C  CA    . ASP A 92  ? 0.8057 1.0270 0.7936 -0.0200 -0.0621 0.0253  92  ASP A CA    
771  C  C     . ASP A 92  ? 0.7881 0.9958 0.7583 -0.0189 -0.0553 0.0141  92  ASP A C     
772  O  O     . ASP A 92  ? 0.8411 1.0490 0.7877 -0.0202 -0.0572 0.0092  92  ASP A O     
773  C  CB    . ASP A 92  ? 0.8610 1.0922 0.8566 -0.0143 -0.0588 0.0405  92  ASP A CB    
774  C  CG    . ASP A 92  ? 0.9253 1.1700 0.9402 -0.0143 -0.0647 0.0528  92  ASP A CG    
775  O  OD1   . ASP A 92  ? 0.8759 1.1234 0.9081 -0.0093 -0.0602 0.0639  92  ASP A OD1   
776  O  OD2   . ASP A 92  ? 0.8360 1.0882 0.8499 -0.0193 -0.0739 0.0516  92  ASP A OD2   
777  N  N     . GLN A 93  ? 0.7008 0.8968 0.6816 -0.0165 -0.0475 0.0101  93  GLN A N     
778  C  CA    . GLN A 93  ? 0.7904 0.9746 0.7576 -0.0144 -0.0401 0.0017  93  GLN A CA    
779  C  C     . GLN A 93  ? 0.8186 0.9942 0.7677 -0.0190 -0.0436 -0.0125 93  GLN A C     
780  O  O     . GLN A 93  ? 0.7418 0.9138 0.6700 -0.0176 -0.0407 -0.0176 93  GLN A O     
781  C  CB    . GLN A 93  ? 0.6872 0.8619 0.6716 -0.0114 -0.0324 0.0013  93  GLN A CB    
782  C  CG    . GLN A 93  ? 0.6586 0.8392 0.6610 -0.0071 -0.0289 0.0141  93  GLN A CG    
783  C  CD    . GLN A 93  ? 0.7089 0.8793 0.7261 -0.0050 -0.0222 0.0126  93  GLN A CD    
784  O  OE1   . GLN A 93  ? 0.6409 0.8128 0.6759 -0.0029 -0.0205 0.0202  93  GLN A OE1   
785  N  NE2   . GLN A 93  ? 0.7579 0.9174 0.7677 -0.0056 -0.0186 0.0026  93  GLN A NE2   
786  N  N     . PRO A 94  ? 0.7976 0.9690 0.7534 -0.0244 -0.0491 -0.0192 94  PRO A N     
787  C  CA    . PRO A 94  ? 0.8251 0.9872 0.7640 -0.0292 -0.0526 -0.0326 94  PRO A CA    
788  C  C     . PRO A 94  ? 0.8719 1.0406 0.7888 -0.0323 -0.0600 -0.0344 94  PRO A C     
789  O  O     . PRO A 94  ? 1.0113 1.1703 0.9086 -0.0347 -0.0608 -0.0460 94  PRO A O     
790  C  CB    . PRO A 94  ? 0.7395 0.8993 0.6943 -0.0346 -0.0579 -0.0358 94  PRO A CB    
791  C  CG    . PRO A 94  ? 0.8116 0.9830 0.7879 -0.0329 -0.0589 -0.0237 94  PRO A CG    
792  C  CD    . PRO A 94  ? 0.7398 0.9129 0.7192 -0.0259 -0.0509 -0.0157 94  PRO A CD    
793  N  N     . ALA A 95  ? 0.8308 1.0152 0.7497 -0.0323 -0.0654 -0.0233 95  ALA A N     
794  C  CA    . ALA A 95  ? 0.8680 1.0604 0.7657 -0.0360 -0.0740 -0.0242 95  ALA A CA    
795  C  C     . ALA A 95  ? 0.8648 1.0599 0.7412 -0.0307 -0.0684 -0.0215 95  ALA A C     
796  O  O     . ALA A 95  ? 0.8888 1.0855 0.7403 -0.0334 -0.0736 -0.0267 95  ALA A O     
797  C  CB    . ALA A 95  ? 0.8743 1.0842 0.7851 -0.0392 -0.0839 -0.0125 95  ALA A CB    
798  N  N     . ILE A 96  ? 0.7926 0.9882 0.6778 -0.0234 -0.0581 -0.0135 96  ILE A N     
799  C  CA    . ILE A 96  ? 0.8705 1.0710 0.7384 -0.0180 -0.0521 -0.0083 96  ILE A CA    
800  C  C     . ILE A 96  ? 0.9379 1.1250 0.7983 -0.0128 -0.0399 -0.0155 96  ILE A C     
801  O  O     . ILE A 96  ? 0.9038 1.0922 0.7434 -0.0088 -0.0346 -0.0157 96  ILE A O     
802  C  CB    . ILE A 96  ? 0.8158 1.0310 0.6998 -0.0136 -0.0504 0.0101  96  ILE A CB    
803  C  CG1   . ILE A 96  ? 0.8554 1.0800 0.7188 -0.0095 -0.0472 0.0173  96  ILE A CG1   
804  C  CG2   . ILE A 96  ? 0.8162 1.0253 0.7247 -0.0091 -0.0412 0.0146  96  ILE A CG2   
805  C  CD1   . ILE A 96  ? 0.7917 1.0290 0.6719 -0.0045 -0.0437 0.0360  96  ILE A CD1   
806  N  N     . ARG A 97  ? 0.8901 1.0651 0.7664 -0.0125 -0.0352 -0.0212 97  ARG A N     
807  C  CA    . ARG A 97  ? 0.8751 1.0394 0.7494 -0.0070 -0.0235 -0.0254 97  ARG A CA    
808  C  C     . ARG A 97  ? 0.9382 1.0950 0.7834 -0.0058 -0.0204 -0.0365 97  ARG A C     
809  O  O     . ARG A 97  ? 0.9769 1.1348 0.8117 0.0004  -0.0111 -0.0337 97  ARG A O     
810  C  CB    . ARG A 97  ? 0.8934 1.0457 0.7866 -0.0084 -0.0215 -0.0314 97  ARG A CB    
811  C  CG    . ARG A 97  ? 0.9689 1.1126 0.8592 -0.0153 -0.0292 -0.0434 97  ARG A CG    
812  C  CD    . ARG A 97  ? 0.9739 1.1052 0.8798 -0.0155 -0.0252 -0.0490 97  ARG A CD    
813  N  NE    . ARG A 97  ? 1.0530 1.1746 0.9542 -0.0217 -0.0312 -0.0609 97  ARG A NE    
814  C  CZ    . ARG A 97  ? 1.1636 1.2814 1.0817 -0.0256 -0.0344 -0.0625 97  ARG A CZ    
815  N  NH1   . ARG A 97  ? 1.0113 1.1334 0.9507 -0.0239 -0.0323 -0.0543 97  ARG A NH1   
816  N  NH2   . ARG A 97  ? 1.1757 1.2849 1.0890 -0.0314 -0.0397 -0.0726 97  ARG A NH2   
817  N  N     . ASP A 98  ? 0.9437 1.0929 0.7754 -0.0118 -0.0279 -0.0492 98  ASP A N     
818  C  CA    . ASP A 98  ? 1.0502 1.1899 0.8530 -0.0110 -0.0252 -0.0617 98  ASP A CA    
819  C  C     . ASP A 98  ? 1.0626 1.2139 0.8428 -0.0077 -0.0241 -0.0558 98  ASP A C     
820  O  O     . ASP A 98  ? 1.0719 1.2189 0.8344 -0.0017 -0.0144 -0.0593 98  ASP A O     
821  C  CB    . ASP A 98  ? 1.0781 1.2085 0.8713 -0.0193 -0.0357 -0.0754 98  ASP A CB    
822  C  CG    . ASP A 98  ? 1.1943 1.3110 1.0058 -0.0217 -0.0347 -0.0826 98  ASP A CG    
823  O  OD1   . ASP A 98  ? 1.1404 1.2501 0.9624 -0.0161 -0.0243 -0.0819 98  ASP A OD1   
824  O  OD2   . ASP A 98  ? 1.3628 1.4765 1.1787 -0.0294 -0.0446 -0.0883 98  ASP A OD2   
825  N  N     . LYS A 99  ? 0.9905 1.1575 0.7718 -0.0111 -0.0335 -0.0459 99  LYS A N     
826  C  CA    . LYS A 99  ? 1.0134 1.1932 0.7734 -0.0082 -0.0331 -0.0386 99  LYS A CA    
827  C  C     . LYS A 99  ? 1.0231 1.2083 0.7890 0.0009  -0.0197 -0.0270 99  LYS A C     
828  O  O     . LYS A 99  ? 1.0389 1.2289 0.7822 0.0055  -0.0139 -0.0251 99  LYS A O     
829  C  CB    . LYS A 99  ? 0.9826 1.1797 0.7483 -0.0131 -0.0457 -0.0274 99  LYS A CB    
830  C  CG    . LYS A 99  ? 1.0281 1.2326 0.7619 -0.0163 -0.0537 -0.0301 99  LYS A CG    
831  C  CD    . LYS A 99  ? 1.1174 1.3332 0.8579 -0.0247 -0.0699 -0.0259 99  LYS A CD    
832  C  CE    . LYS A 99  ? 1.1283 1.3572 0.8403 -0.0269 -0.0780 -0.0227 99  LYS A CE    
833  N  NZ    . LYS A 99  ? 1.2229 1.4394 0.8978 -0.0273 -0.0759 -0.0396 99  LYS A NZ    
834  N  N     . ILE A 100 ? 0.9896 1.1741 0.7852 0.0034  -0.0145 -0.0192 100 ILE A N     
835  C  CA    . ILE A 100 ? 0.9959 1.1842 0.7995 0.0113  -0.0019 -0.0089 100 ILE A CA    
836  C  C     . ILE A 100 ? 1.0598 1.2348 0.8505 0.0162  0.0094  -0.0199 100 ILE A C     
837  O  O     . ILE A 100 ? 1.0575 1.2367 0.8364 0.0228  0.0194  -0.0152 100 ILE A O     
838  C  CB    . ILE A 100 ? 0.9606 1.1509 0.7994 0.0117  -0.0008 0.0014  100 ILE A CB    
839  C  CG1   . ILE A 100 ? 0.9613 1.1678 0.8120 0.0108  -0.0070 0.0175  100 ILE A CG1   
840  C  CG2   . ILE A 100 ? 0.9901 1.1776 0.8394 0.0185  0.0123  0.0066  100 ILE A CG2   
841  C  CD1   . ILE A 100 ? 1.1412 1.3611 0.9785 0.0157  -0.0022 0.0297  100 ILE A CD1   
842  N  N     . ARG A 101 ? 1.0778 1.2370 0.8708 0.0133  0.0082  -0.0341 101 ARG A N     
843  C  CA    . ARG A 101 ? 1.0621 1.2077 0.8465 0.0182  0.0191  -0.0442 101 ARG A CA    
844  C  C     . ARG A 101 ? 1.1208 1.2627 0.8695 0.0204  0.0218  -0.0542 101 ARG A C     
845  O  O     . ARG A 101 ? 1.0778 1.2149 0.8167 0.0276  0.0342  -0.0568 101 ARG A O     
846  C  CB    . ARG A 101 ? 1.0378 1.1676 0.8349 0.0142  0.0163  -0.0558 101 ARG A CB    
847  C  CG    . ARG A 101 ? 0.9931 1.1115 0.7970 0.0201  0.0284  -0.0601 101 ARG A CG    
848  C  CD    . ARG A 101 ? 0.8929 1.0022 0.7215 0.0166  0.0256  -0.0629 101 ARG A CD    
849  N  NE    . ARG A 101 ? 1.1863 1.2926 1.0159 0.0080  0.0130  -0.0693 101 ARG A NE    
850  C  CZ    . ARG A 101 ? 1.2758 1.3736 1.1222 0.0039  0.0092  -0.0737 101 ARG A CZ    
851  N  NH1   . ARG A 101 ? 1.1363 1.2275 0.9993 0.0071  0.0163  -0.0728 101 ARG A NH1   
852  N  NH2   . ARG A 101 ? 1.0780 1.1748 0.9250 -0.0038 -0.0020 -0.0784 101 ARG A NH2   
853  N  N     . GLU A 102 ? 1.1579 1.3023 0.8870 0.0142  0.0105  -0.0598 102 GLU A N     
854  C  CA    . GLU A 102 ? 1.1748 1.3152 0.8672 0.0157  0.0121  -0.0702 102 GLU A CA    
855  C  C     . GLU A 102 ? 1.1403 1.2943 0.8187 0.0234  0.0216  -0.0587 102 GLU A C     
856  O  O     . GLU A 102 ? 1.2092 1.3583 0.8584 0.0278  0.0286  -0.0670 102 GLU A O     
857  C  CB    . GLU A 102 ? 1.2477 1.3900 0.9227 0.0065  -0.0038 -0.0770 102 GLU A CB    
858  C  CG    . GLU A 102 ? 1.2230 1.3553 0.9132 -0.0023 -0.0148 -0.0859 102 GLU A CG    
859  C  CD    . GLU A 102 ? 1.3989 1.5088 1.0845 -0.0019 -0.0098 -0.1032 102 GLU A CD    
860  O  OE1   . GLU A 102 ? 1.5448 1.6454 1.2067 0.0035  -0.0007 -0.1124 102 GLU A OE1   
861  O  OE2   . GLU A 102 ? 1.3783 1.4799 1.0845 -0.0068 -0.0145 -0.1072 102 GLU A OE2   
862  N  N     . HIS A 103 ? 1.1266 1.2971 0.8250 0.0252  0.0222  -0.0400 103 HIS A N     
863  C  CA    . HIS A 103 ? 1.1796 1.3647 0.8666 0.0319  0.0305  -0.0269 103 HIS A CA    
864  C  C     . HIS A 103 ? 1.2206 1.3990 0.9037 0.0413  0.0479  -0.0290 103 HIS A C     
865  O  O     . HIS A 103 ? 1.1707 1.3408 0.8777 0.0433  0.0540  -0.0297 103 HIS A O     
866  C  CB    . HIS A 103 ? 1.1618 1.3636 0.8766 0.0319  0.0283  -0.0060 103 HIS A CB    
867  C  CG    . HIS A 103 ? 1.1335 1.3535 0.8338 0.0354  0.0303  0.0086  103 HIS A CG    
868  N  ND1   . HIS A 103 ? 1.0969 1.3248 0.7989 0.0437  0.0441  0.0204  103 HIS A ND1   
869  C  CD2   . HIS A 103 ? 1.1370 1.3699 0.8217 0.0316  0.0199  0.0143  103 HIS A CD2   
870  C  CE1   . HIS A 103 ? 1.1571 1.4016 0.8445 0.0450  0.0427  0.0328  103 HIS A CE1   
871  N  NE2   . HIS A 103 ? 1.2054 1.4534 0.8818 0.0378  0.0279  0.0294  103 HIS A NE2   
872  N  N     . PRO A 104 ? 1.2802 1.4627 0.9339 0.0472  0.0564  -0.0298 104 PRO A N     
873  C  CA    . PRO A 104 ? 1.2324 1.4094 0.8836 0.0569  0.0740  -0.0312 104 PRO A CA    
874  C  C     . PRO A 104 ? 1.1900 1.3788 0.8723 0.0622  0.0833  -0.0119 104 PRO A C     
875  O  O     . PRO A 104 ? 1.1838 1.3661 0.8791 0.0680  0.0952  -0.0127 104 PRO A O     
876  C  CB    . PRO A 104 ? 1.2660 1.4473 0.8764 0.0616  0.0797  -0.0350 104 PRO A CB    
877  C  CG    . PRO A 104 ? 1.2232 1.4204 0.8240 0.0558  0.0668  -0.0255 104 PRO A CG    
878  C  CD    . PRO A 104 ? 1.2240 1.4167 0.8452 0.0456  0.0504  -0.0289 104 PRO A CD    
879  N  N     . ALA A 105 ? 1.1913 1.3970 0.8869 0.0600  0.0778  0.0057  105 ALA A N     
880  C  CA    . ALA A 105 ? 1.1872 1.4042 0.9118 0.0645  0.0862  0.0246  105 ALA A CA    
881  C  C     . ALA A 105 ? 1.1351 1.3436 0.8960 0.0619  0.0846  0.0247  105 ALA A C     
882  O  O     . ALA A 105 ? 1.0605 1.2744 0.8458 0.0657  0.0927  0.0372  105 ALA A O     
883  C  CB    . ALA A 105 ? 1.1465 1.3824 0.8761 0.0627  0.0802  0.0432  105 ALA A CB    
884  N  N     . VAL A 106 ? 1.1283 1.3240 0.8932 0.0551  0.0741  0.0115  106 VAL A N     
885  C  CA    . VAL A 106 ? 1.1410 1.3283 0.9374 0.0523  0.0721  0.0105  106 VAL A CA    
886  C  C     . VAL A 106 ? 1.0468 1.2181 0.8396 0.0556  0.0799  -0.0036 106 VAL A C     
887  O  O     . VAL A 106 ? 1.1437 1.3055 0.9096 0.0563  0.0809  -0.0181 106 VAL A O     
888  C  CB    . VAL A 106 ? 1.0697 1.2540 0.8759 0.0434  0.0566  0.0066  106 VAL A CB    
889  C  CG1   . VAL A 106 ? 1.0703 1.2701 0.8730 0.0406  0.0485  0.0185  106 VAL A CG1   
890  C  CG2   . VAL A 106 ? 1.1712 1.3408 0.9591 0.0390  0.0504  -0.0130 106 VAL A CG2   
891  N  N     . ILE A 107 ? 0.9660 1.1342 0.7860 0.0575  0.0854  0.0009  107 ILE A N     
892  C  CA    . ILE A 107 ? 0.9287 1.0820 0.7508 0.0601  0.0917  -0.0110 107 ILE A CA    
893  C  C     . ILE A 107 ? 0.9196 1.0604 0.7527 0.0527  0.0809  -0.0216 107 ILE A C     
894  O  O     . ILE A 107 ? 1.0217 1.1481 0.8422 0.0519  0.0803  -0.0367 107 ILE A O     
895  C  CB    . ILE A 107 ? 0.8868 1.0446 0.7327 0.0662  0.1034  0.0001  107 ILE A CB    
896  C  CG1   . ILE A 107 ? 0.8805 1.0490 0.7128 0.0748  0.1167  0.0084  107 ILE A CG1   
897  C  CG2   . ILE A 107 ? 0.8495 0.9926 0.7048 0.0677  0.1074  -0.0102 107 ILE A CG2   
898  C  CD1   . ILE A 107 ? 0.9337 1.1199 0.7813 0.0754  0.1177  0.0283  107 ILE A CD1   
899  N  N     . ASP A 108 ? 0.8681 1.0137 0.7243 0.0474  0.0725  -0.0136 108 ASP A N     
900  C  CA    . ASP A 108 ? 0.8131 0.9485 0.6819 0.0406  0.0630  -0.0216 108 ASP A CA    
901  C  C     . ASP A 108 ? 0.7591 0.9035 0.6472 0.0355  0.0541  -0.0112 108 ASP A C     
902  O  O     . ASP A 108 ? 0.7274 0.8845 0.6222 0.0375  0.0559  0.0026  108 ASP A O     
903  C  CB    . ASP A 108 ? 0.8513 0.9767 0.7372 0.0427  0.0688  -0.0251 108 ASP A CB    
904  C  CG    . ASP A 108 ? 0.9808 1.0919 0.8672 0.0373  0.0615  -0.0385 108 ASP A CG    
905  O  OD1   . ASP A 108 ? 0.9484 1.0570 0.8210 0.0320  0.0526  -0.0460 108 ASP A OD1   
906  O  OD2   . ASP A 108 ? 0.9406 1.0438 0.8421 0.0381  0.0646  -0.0408 108 ASP A OD2   
907  N  N     . ILE A 109 ? 0.7719 0.9093 0.6690 0.0292  0.0448  -0.0176 109 ILE A N     
908  C  CA    . ILE A 109 ? 0.7433 0.8865 0.6601 0.0247  0.0369  -0.0098 109 ILE A CA    
909  C  C     . ILE A 109 ? 0.7417 0.8755 0.6789 0.0221  0.0355  -0.0136 109 ILE A C     
910  O  O     . ILE A 109 ? 0.7367 0.8592 0.6699 0.0219  0.0372  -0.0241 109 ILE A O     
911  C  CB    . ILE A 109 ? 0.7704 0.9173 0.6767 0.0192  0.0260  -0.0126 109 ILE A CB    
912  C  CG1   . ILE A 109 ? 0.8104 0.9459 0.6998 0.0156  0.0216  -0.0285 109 ILE A CG1   
913  C  CG2   . ILE A 109 ? 0.7080 0.8680 0.5996 0.0215  0.0263  -0.0041 109 ILE A CG2   
914  C  CD1   . ILE A 109 ? 0.8551 0.9922 0.7450 0.0084  0.0094  -0.0316 109 ILE A CD1   
915  N  N     . TYR A 110 ? 0.6743 0.8125 0.6331 0.0203  0.0327  -0.0047 110 TYR A N     
916  C  CA    . TYR A 110 ? 0.6406 0.7715 0.6190 0.0184  0.0323  -0.0063 110 TYR A CA    
917  C  C     . TYR A 110 ? 0.6612 0.7937 0.6539 0.0137  0.0242  -0.0034 110 TYR A C     
918  O  O     . TYR A 110 ? 0.6690 0.8105 0.6647 0.0134  0.0212  0.0048  110 TYR A O     
919  C  CB    . TYR A 110 ? 0.6434 0.7767 0.6363 0.0226  0.0402  0.0025  110 TYR A CB    
920  C  CG    . TYR A 110 ? 0.6449 0.7787 0.6258 0.0285  0.0499  0.0018  110 TYR A CG    
921  C  CD1   . TYR A 110 ? 0.6691 0.7932 0.6479 0.0303  0.0543  -0.0065 110 TYR A CD1   
922  C  CD2   . TYR A 110 ? 0.6324 0.7764 0.6043 0.0329  0.0553  0.0101  110 TYR A CD2   
923  C  CE1   . TYR A 110 ? 0.7619 0.8860 0.7303 0.0367  0.0642  -0.0073 110 TYR A CE1   
924  C  CE2   . TYR A 110 ? 0.7337 0.8783 0.6938 0.0390  0.0653  0.0095  110 TYR A CE2   
925  C  CZ    . TYR A 110 ? 0.7648 0.8992 0.7235 0.0411  0.0700  0.0005  110 TYR A CZ    
926  O  OH    . TYR A 110 ? 0.7690 0.9036 0.7167 0.0481  0.0810  -0.0003 110 TYR A OH    
927  N  N     . GLU A 111 ? 0.6071 0.7310 0.6088 0.0104  0.0211  -0.0100 111 GLU A N     
928  C  CA    . GLU A 111 ? 0.6332 0.7569 0.6493 0.0064  0.0149  -0.0085 111 GLU A CA    
929  C  C     . GLU A 111 ? 0.6330 0.7629 0.6427 0.0039  0.0081  -0.0082 111 GLU A C     
930  O  O     . GLU A 111 ? 0.6415 0.7776 0.6618 0.0034  0.0053  -0.0005 111 GLU A O     
931  C  CB    . GLU A 111 ? 0.5857 0.7127 0.6205 0.0077  0.0170  0.0016  111 GLU A CB    
932  C  CG    . GLU A 111 ? 0.6632 0.7863 0.7056 0.0100  0.0230  0.0029  111 GLU A CG    
933  C  CD    . GLU A 111 ? 0.6698 0.7938 0.7325 0.0094  0.0230  0.0108  111 GLU A CD    
934  O  OE1   . GLU A 111 ? 0.6029 0.7275 0.6739 0.0071  0.0183  0.0130  111 GLU A OE1   
935  O  OE2   . GLU A 111 ? 0.6001 0.7239 0.6709 0.0111  0.0276  0.0148  111 GLU A OE2   
936  N  N     . TYR A 112 ? 0.7218 0.8495 0.7146 0.0020  0.0053  -0.0165 112 TYR A N     
937  C  CA    . TYR A 112 ? 0.7177 0.8520 0.7029 -0.0010 -0.0019 -0.0164 112 TYR A CA    
938  C  C     . TYR A 112 ? 0.7028 0.8326 0.6919 -0.0063 -0.0085 -0.0236 112 TYR A C     
939  O  O     . TYR A 112 ? 0.7274 0.8641 0.7158 -0.0092 -0.0152 -0.0220 112 TYR A O     
940  C  CB    . TYR A 112 ? 0.7004 0.8367 0.6620 0.0000  -0.0015 -0.0202 112 TYR A CB    
941  C  CG    . TYR A 112 ? 0.8514 0.9758 0.8005 0.0001  0.0018  -0.0321 112 TYR A CG    
942  C  CD1   . TYR A 112 ? 0.8616 0.9831 0.8034 0.0055  0.0108  -0.0324 112 TYR A CD1   
943  C  CD2   . TYR A 112 ? 0.8575 0.9738 0.8031 -0.0048 -0.0036 -0.0426 112 TYR A CD2   
944  C  CE1   . TYR A 112 ? 1.0859 1.1959 1.0172 0.0063  0.0145  -0.0431 112 TYR A CE1   
945  C  CE2   . TYR A 112 ? 1.0639 1.1682 0.9991 -0.0046 -0.0004 -0.0532 112 TYR A CE2   
946  C  CZ    . TYR A 112 ? 0.9799 1.0807 0.9079 0.0013  0.0088  -0.0536 112 TYR A CZ    
947  O  OH    . TYR A 112 ? 0.9795 1.0677 0.8983 0.0022  0.0126  -0.0640 112 TYR A OH    
948  N  N     . ASP A 113 ? 0.7258 0.8454 0.7202 -0.0076 -0.0068 -0.0305 113 ASP A N     
949  C  CA    . ASP A 113 ? 0.7612 0.8762 0.7586 -0.0126 -0.0122 -0.0373 113 ASP A CA    
950  C  C     . ASP A 113 ? 0.6702 0.7837 0.6863 -0.0134 -0.0122 -0.0347 113 ASP A C     
951  O  O     . ASP A 113 ? 0.6999 0.8093 0.7199 -0.0171 -0.0152 -0.0396 113 ASP A O     
952  C  CB    . ASP A 113 ? 0.8248 0.9287 0.8116 -0.0139 -0.0108 -0.0478 113 ASP A CB    
953  C  CG    . ASP A 113 ? 1.0055 1.1021 0.9960 -0.0099 -0.0031 -0.0482 113 ASP A CG    
954  O  OD1   . ASP A 113 ? 0.8497 0.9506 0.8487 -0.0063 0.0010  -0.0404 113 ASP A OD1   
955  O  OD2   . ASP A 113 ? 1.0220 1.1087 1.0083 -0.0106 -0.0014 -0.0558 113 ASP A OD2   
956  N  N     . THR A 114 ? 0.6195 0.7358 0.6467 -0.0102 -0.0089 -0.0271 114 THR A N     
957  C  CA    . THR A 114 ? 0.6224 0.7357 0.6651 -0.0109 -0.0087 -0.0258 114 THR A CA    
958  C  C     . THR A 114 ? 0.6038 0.7240 0.6548 -0.0124 -0.0132 -0.0220 114 THR A C     
959  O  O     . THR A 114 ? 0.5903 0.7189 0.6420 -0.0108 -0.0145 -0.0151 114 THR A O     
960  C  CB    . THR A 114 ? 0.6185 0.7309 0.6705 -0.0076 -0.0039 -0.0198 114 THR A CB    
961  O  OG1   . THR A 114 ? 0.7988 0.9196 0.8521 -0.0050 -0.0034 -0.0111 114 THR A OG1   
962  C  CG2   . THR A 114 ? 0.6401 0.7469 0.6867 -0.0059 0.0009  -0.0226 114 THR A CG2   
963  N  N     . PRO A 115 ? 0.6210 0.7386 0.6790 -0.0150 -0.0152 -0.0256 115 PRO A N     
964  C  CA    . PRO A 115 ? 0.5312 0.6559 0.5980 -0.0159 -0.0188 -0.0218 115 PRO A CA    
965  C  C     . PRO A 115 ? 0.5210 0.6490 0.6000 -0.0123 -0.0167 -0.0138 115 PRO A C     
966  O  O     . PRO A 115 ? 0.5353 0.6578 0.6187 -0.0102 -0.0127 -0.0126 115 PRO A O     
967  C  CB    . PRO A 115 ? 0.4382 0.5581 0.5103 -0.0187 -0.0192 -0.0273 115 PRO A CB    
968  C  CG    . PRO A 115 ? 0.6289 0.7401 0.6914 -0.0205 -0.0179 -0.0345 115 PRO A CG    
969  C  CD    . PRO A 115 ? 0.5655 0.6741 0.6234 -0.0172 -0.0140 -0.0327 115 PRO A CD    
970  N  N     . PHE A 116 ? 0.5237 0.6607 0.6093 -0.0117 -0.0197 -0.0080 116 PHE A N     
971  C  CA    . PHE A 116 ? 0.4923 0.6330 0.5893 -0.0080 -0.0180 0.0009  116 PHE A CA    
972  C  C     . PHE A 116 ? 0.5231 0.6558 0.6325 -0.0064 -0.0143 -0.0003 116 PHE A C     
973  O  O     . PHE A 116 ? 0.4820 0.6106 0.5972 -0.0041 -0.0113 0.0033  116 PHE A O     
974  C  CB    . PHE A 116 ? 0.4964 0.6490 0.5987 -0.0076 -0.0224 0.0078  116 PHE A CB    
975  C  CG    . PHE A 116 ? 0.6212 0.7787 0.7347 -0.0035 -0.0210 0.0184  116 PHE A CG    
976  C  CD1   . PHE A 116 ? 0.6112 0.7708 0.7197 -0.0015 -0.0196 0.0242  116 PHE A CD1   
977  C  CD2   . PHE A 116 ? 0.4689 0.6288 0.5986 -0.0012 -0.0207 0.0231  116 PHE A CD2   
978  C  CE1   . PHE A 116 ? 0.5917 0.7556 0.7118 0.0021  -0.0184 0.0350  116 PHE A CE1   
979  C  CE2   . PHE A 116 ? 0.5098 0.6733 0.6512 0.0028  -0.0193 0.0332  116 PHE A CE2   
980  C  CZ    . PHE A 116 ? 0.5608 0.7261 0.6976 0.0042  -0.0185 0.0395  116 PHE A CZ    
981  N  N     . ALA A 117 ? 0.5165 0.6467 0.6299 -0.0080 -0.0145 -0.0053 117 ALA A N     
982  C  CA    . ALA A 117 ? 0.5181 0.6408 0.6414 -0.0063 -0.0110 -0.0071 117 ALA A CA    
983  C  C     . ALA A 117 ? 0.4702 0.5823 0.5890 -0.0072 -0.0084 -0.0120 117 ALA A C     
984  O  O     . ALA A 117 ? 0.5234 0.6291 0.6492 -0.0056 -0.0060 -0.0113 117 ALA A O     
985  C  CB    . ALA A 117 ? 0.3622 0.4859 0.4893 -0.0075 -0.0111 -0.0109 117 ALA A CB    
986  N  N     . LYS A 118 ? 0.4897 0.5997 0.5975 -0.0098 -0.0092 -0.0170 118 LYS A N     
987  C  CA    . LYS A 118 ? 0.5396 0.6411 0.6444 -0.0105 -0.0070 -0.0205 118 LYS A CA    
988  C  C     . LYS A 118 ? 0.4985 0.6004 0.6048 -0.0085 -0.0056 -0.0149 118 LYS A C     
989  O  O     . LYS A 118 ? 0.5241 0.6199 0.6352 -0.0084 -0.0039 -0.0147 118 LYS A O     
990  C  CB    . LYS A 118 ? 0.5135 0.6127 0.6079 -0.0133 -0.0078 -0.0265 118 LYS A CB    
991  C  CG    . LYS A 118 ? 0.5260 0.6234 0.6206 -0.0157 -0.0086 -0.0316 118 LYS A CG    
992  C  CD    . LYS A 118 ? 0.6368 0.7348 0.7226 -0.0187 -0.0106 -0.0357 118 LYS A CD    
993  C  CE    . LYS A 118 ? 0.7865 0.8831 0.8741 -0.0213 -0.0110 -0.0394 118 LYS A CE    
994  N  NZ    . LYS A 118 ? 0.9419 1.0361 1.0221 -0.0246 -0.0126 -0.0438 118 LYS A NZ    
995  N  N     . ARG A 119 ? 0.5102 0.6198 0.6126 -0.0072 -0.0064 -0.0098 119 ARG A N     
996  C  CA    . ARG A 119 ? 0.4737 0.5854 0.5789 -0.0049 -0.0043 -0.0026 119 ARG A CA    
997  C  C     . ARG A 119 ? 0.5572 0.6673 0.6769 -0.0031 -0.0036 0.0030  119 ARG A C     
998  O  O     . ARG A 119 ? 0.5550 0.6621 0.6809 -0.0024 -0.0016 0.0071  119 ARG A O     
999  C  CB    . ARG A 119 ? 0.4997 0.6208 0.5963 -0.0037 -0.0053 0.0021  119 ARG A CB    
1000 C  CG    . ARG A 119 ? 0.5656 0.6912 0.6661 -0.0008 -0.0029 0.0116  119 ARG A CG    
1001 C  CD    . ARG A 119 ? 0.5810 0.7105 0.6677 0.0002  -0.0008 0.0122  119 ARG A CD    
1002 N  NE    . ARG A 119 ? 0.8771 0.9993 0.9586 -0.0008 0.0017  0.0052  119 ARG A NE    
1003 C  CZ    . ARG A 119 ? 0.8624 0.9805 0.9513 0.0000  0.0051  0.0072  119 ARG A CZ    
1004 N  NH1   . ARG A 119 ? 0.6624 0.7816 0.7643 0.0011  0.0062  0.0152  119 ARG A NH1   
1005 N  NH2   . ARG A 119 ? 0.7040 0.8166 0.7883 -0.0007 0.0070  0.0014  119 ARG A NH2   
1006 N  N     . TYR A 120 ? 0.4977 0.6094 0.6238 -0.0024 -0.0049 0.0035  120 TYR A N     
1007 C  CA    . TYR A 120 ? 0.5087 0.6165 0.6490 -0.0004 -0.0036 0.0075  120 TYR A CA    
1008 C  C     . TYR A 120 ? 0.4735 0.5695 0.6170 -0.0020 -0.0023 0.0012  120 TYR A C     
1009 O  O     . TYR A 120 ? 0.4672 0.5576 0.6198 -0.0014 -0.0013 0.0042  120 TYR A O     
1010 C  CB    . TYR A 120 ? 0.4803 0.5924 0.6271 0.0013  -0.0046 0.0089  120 TYR A CB    
1011 C  CG    . TYR A 120 ? 0.4346 0.5414 0.5965 0.0042  -0.0026 0.0125  120 TYR A CG    
1012 C  CD1   . TYR A 120 ? 0.3952 0.5070 0.5670 0.0072  -0.0024 0.0230  120 TYR A CD1   
1013 C  CD2   . TYR A 120 ? 0.4098 0.5063 0.5756 0.0041  -0.0006 0.0054  120 TYR A CD2   
1014 C  CE1   . TYR A 120 ? 0.4374 0.5429 0.6241 0.0100  -0.0004 0.0262  120 TYR A CE1   
1015 C  CE2   . TYR A 120 ? 0.4536 0.5433 0.6324 0.0070  0.0015  0.0075  120 TYR A CE2   
1016 C  CZ    . TYR A 120 ? 0.4638 0.5576 0.6537 0.0100  0.0017  0.0178  120 TYR A CZ    
1017 O  OH    . TYR A 120 ? 0.5532 0.6389 0.7572 0.0130  0.0041  0.0197  120 TYR A OH    
1018 N  N     . LEU A 121 ? 0.4120 0.5041 0.5482 -0.0042 -0.0027 -0.0073 121 LEU A N     
1019 C  CA    . LEU A 121 ? 0.4732 0.5550 0.6099 -0.0062 -0.0021 -0.0133 121 LEU A CA    
1020 C  C     . LEU A 121 ? 0.5907 0.6698 0.7281 -0.0075 -0.0021 -0.0110 121 LEU A C     
1021 O  O     . LEU A 121 ? 0.5375 0.6091 0.6814 -0.0086 -0.0023 -0.0116 121 LEU A O     
1022 C  CB    . LEU A 121 ? 0.4467 0.5267 0.5742 -0.0085 -0.0026 -0.0212 121 LEU A CB    
1023 C  CG    . LEU A 121 ? 0.5655 0.6444 0.6945 -0.0078 -0.0017 -0.0253 121 LEU A CG    
1024 C  CD1   . LEU A 121 ? 0.5390 0.6164 0.6591 -0.0105 -0.0020 -0.0318 121 LEU A CD1   
1025 C  CD2   . LEU A 121 ? 0.5603 0.6306 0.6970 -0.0064 0.0000  -0.0267 121 LEU A CD2   
1026 N  N     . ILE A 122 ? 0.4972 0.5824 0.6280 -0.0075 -0.0019 -0.0084 122 ILE A N     
1027 C  CA    . ILE A 122 ? 0.5648 0.6487 0.6969 -0.0083 -0.0010 -0.0057 122 ILE A CA    
1028 C  C     . ILE A 122 ? 0.5998 0.6858 0.7430 -0.0066 0.0000  0.0035  122 ILE A C     
1029 O  O     . ILE A 122 ? 0.5480 0.6290 0.6998 -0.0081 -0.0003 0.0054  122 ILE A O     
1030 C  CB    . ILE A 122 ? 0.5817 0.6708 0.7030 -0.0079 0.0001  -0.0063 122 ILE A CB    
1031 C  CG1   . ILE A 122 ? 0.4872 0.5717 0.6012 -0.0103 -0.0008 -0.0145 122 ILE A CG1   
1032 C  CG2   . ILE A 122 ? 0.5018 0.5934 0.6265 -0.0070 0.0024  -0.0001 122 ILE A CG2   
1033 C  CD1   . ILE A 122 ? 0.5178 0.6059 0.6202 -0.0099 -0.0002 -0.0172 122 ILE A CD1   
1034 N  N     . ASP A 123 ? 0.5593 0.6529 0.7030 -0.0039 0.0007  0.0098  123 ASP A N     
1035 C  CA    . ASP A 123 ? 0.5473 0.6442 0.7014 -0.0022 0.0020  0.0202  123 ASP A CA    
1036 C  C     . ASP A 123 ? 0.5360 0.6245 0.7045 -0.0027 0.0012  0.0213  123 ASP A C     
1037 O  O     . ASP A 123 ? 0.6211 0.7072 0.8005 -0.0033 0.0017  0.0272  123 ASP A O     
1038 C  CB    . ASP A 123 ? 0.5122 0.6197 0.6627 0.0008  0.0023  0.0270  123 ASP A CB    
1039 C  CG    . ASP A 123 ? 0.5543 0.6695 0.6908 0.0015  0.0037  0.0275  123 ASP A CG    
1040 O  OD1   . ASP A 123 ? 0.5576 0.6693 0.6866 -0.0001 0.0044  0.0209  123 ASP A OD1   
1041 O  OD2   . ASP A 123 ? 0.5476 0.6720 0.6803 0.0037  0.0042  0.0346  123 ASP A OD2   
1042 N  N     . LYS A 124 ? 0.5243 0.6080 0.6935 -0.0023 0.0002  0.0156  124 LYS A N     
1043 C  CA    . LYS A 124 ? 0.5350 0.6088 0.7163 -0.0023 -0.0001 0.0147  124 LYS A CA    
1044 C  C     . LYS A 124 ? 0.5418 0.6044 0.7230 -0.0061 -0.0016 0.0070  124 LYS A C     
1045 O  O     . LYS A 124 ? 0.6005 0.6527 0.7899 -0.0067 -0.0021 0.0045  124 LYS A O     
1046 C  CB    . LYS A 124 ? 0.5750 0.6482 0.7570 0.0002  0.0004  0.0115  124 LYS A CB    
1047 C  CG    . LYS A 124 ? 0.6301 0.7051 0.8256 0.0039  0.0015  0.0203  124 LYS A CG    
1048 C  CD    . LYS A 124 ? 0.6129 0.7018 0.8074 0.0059  0.0014  0.0310  124 LYS A CD    
1049 C  CE    . LYS A 124 ? 0.6519 0.7427 0.8616 0.0094  0.0023  0.0418  124 LYS A CE    
1050 N  NZ    . LYS A 124 ? 0.7099 0.8142 0.9181 0.0110  0.0020  0.0536  124 LYS A NZ    
1051 N  N     . GLY A 125 ? 0.5598 0.6237 0.7319 -0.0087 -0.0024 0.0032  125 GLY A N     
1052 C  CA    . GLY A 125 ? 0.5483 0.6032 0.7199 -0.0126 -0.0047 -0.0034 125 GLY A CA    
1053 C  C     . GLY A 125 ? 0.5612 0.6072 0.7282 -0.0133 -0.0055 -0.0132 125 GLY A C     
1054 O  O     . GLY A 125 ? 0.5892 0.6251 0.7585 -0.0162 -0.0076 -0.0179 125 GLY A O     
1055 N  N     . LEU A 126 ? 0.6097 0.6595 0.7698 -0.0109 -0.0038 -0.0163 126 LEU A N     
1056 C  CA    . LEU A 126 ? 0.5622 0.6051 0.7179 -0.0107 -0.0032 -0.0248 126 LEU A CA    
1057 C  C     . LEU A 126 ? 0.5035 0.5467 0.6467 -0.0134 -0.0043 -0.0315 126 LEU A C     
1058 O  O     . LEU A 126 ? 0.5190 0.5699 0.6565 -0.0139 -0.0044 -0.0297 126 LEU A O     
1059 C  CB    . LEU A 126 ? 0.5975 0.6455 0.7554 -0.0064 -0.0004 -0.0231 126 LEU A CB    
1060 C  CG    . LEU A 126 ? 0.6633 0.7121 0.8346 -0.0031 0.0008  -0.0152 126 LEU A CG    
1061 C  CD1   . LEU A 126 ? 0.4856 0.5422 0.6594 0.0010  0.0028  -0.0122 126 LEU A CD1   
1062 C  CD2   . LEU A 126 ? 0.5995 0.6345 0.7792 -0.0034 0.0010  -0.0181 126 LEU A CD2   
1063 N  N     . VAL A 127 ? 0.5945 0.6288 0.7333 -0.0151 -0.0049 -0.0391 127 VAL A N     
1064 C  CA    . VAL A 127 ? 0.5374 0.5714 0.6648 -0.0178 -0.0060 -0.0450 127 VAL A CA    
1065 C  C     . VAL A 127 ? 0.6045 0.6356 0.7262 -0.0160 -0.0031 -0.0512 127 VAL A C     
1066 O  O     . VAL A 127 ? 0.6251 0.6472 0.7481 -0.0152 -0.0022 -0.0557 127 VAL A O     
1067 C  CB    . VAL A 127 ? 0.5834 0.6106 0.7091 -0.0223 -0.0100 -0.0476 127 VAL A CB    
1068 C  CG1   . VAL A 127 ? 0.5919 0.6196 0.7058 -0.0247 -0.0112 -0.0525 127 VAL A CG1   
1069 C  CG2   . VAL A 127 ? 0.5343 0.5656 0.6678 -0.0237 -0.0120 -0.0402 127 VAL A CG2   
1070 N  N     . PRO A 128 ? 0.5473 0.5855 0.6631 -0.0152 -0.0014 -0.0519 128 PRO A N     
1071 C  CA    . PRO A 128 ? 0.6354 0.6724 0.7469 -0.0133 0.0020  -0.0568 128 PRO A CA    
1072 C  C     . PRO A 128 ? 0.6259 0.6561 0.7267 -0.0161 0.0011  -0.0637 128 PRO A C     
1073 O  O     . PRO A 128 ? 0.6808 0.7086 0.7777 -0.0199 -0.0028 -0.0642 128 PRO A O     
1074 C  CB    . PRO A 128 ? 0.6182 0.6661 0.7282 -0.0126 0.0030  -0.0538 128 PRO A CB    
1075 C  CG    . PRO A 128 ? 0.6105 0.6620 0.7180 -0.0155 -0.0003 -0.0508 128 PRO A CG    
1076 C  CD    . PRO A 128 ? 0.5554 0.6029 0.6688 -0.0159 -0.0023 -0.0479 128 PRO A CD    
1077 N  N     . MET A 129 ? 0.6987 0.7264 0.7950 -0.0139 0.0051  -0.0685 129 MET A N     
1078 C  CA    . MET A 129 ? 0.7385 0.7609 0.8224 -0.0160 0.0052  -0.0751 129 MET A CA    
1079 C  C     . MET A 129 ? 0.7729 0.7837 0.8534 -0.0189 0.0014  -0.0798 129 MET A C     
1080 O  O     . MET A 129 ? 0.8552 0.8629 0.9251 -0.0226 -0.0016 -0.0834 129 MET A O     
1081 C  CB    . MET A 129 ? 0.6504 0.6796 0.7271 -0.0193 0.0031  -0.0733 129 MET A CB    
1082 C  CG    . MET A 129 ? 0.6418 0.6808 0.7198 -0.0175 0.0067  -0.0703 129 MET A CG    
1083 S  SD    . MET A 129 ? 0.6725 0.7136 0.7571 -0.0117 0.0134  -0.0708 129 MET A SD    
1084 C  CE    . MET A 129 ? 0.5387 0.5735 0.6104 -0.0111 0.0177  -0.0783 129 MET A CE    
1085 N  N     . GLU A 130 ? 0.7881 0.7927 0.8781 -0.0177 0.0009  -0.0792 130 GLU A N     
1086 C  CA    . GLU A 130 ? 0.8565 0.8496 0.9458 -0.0211 -0.0035 -0.0832 130 GLU A CA    
1087 C  C     . GLU A 130 ? 0.8948 0.8757 0.9809 -0.0184 0.0001  -0.0913 130 GLU A C     
1088 O  O     . GLU A 130 ? 1.0318 1.0122 1.1259 -0.0130 0.0055  -0.0902 130 GLU A O     
1089 C  CB    . GLU A 130 ? 0.8149 0.8085 0.9181 -0.0221 -0.0067 -0.0764 130 GLU A CB    
1090 C  CG    . GLU A 130 ? 0.9835 0.9716 1.0869 -0.0280 -0.0136 -0.0769 130 GLU A CG    
1091 C  CD    . GLU A 130 ? 1.1687 1.1638 1.2845 -0.0293 -0.0162 -0.0674 130 GLU A CD    
1092 O  OE1   . GLU A 130 ? 0.9148 0.9114 1.0419 -0.0261 -0.0137 -0.0621 130 GLU A OE1   
1093 O  OE2   . GLU A 130 ? 1.2146 1.2141 1.3290 -0.0331 -0.0204 -0.0647 130 GLU A OE2   
1094 N  N     . GLY A 131 ? 0.8937 0.8645 0.9680 -0.0219 -0.0029 -0.0993 131 GLY A N     
1095 C  CA    . GLY A 131 ? 0.9369 0.8936 1.0058 -0.0198 0.0002  -0.1088 131 GLY A CA    
1096 C  C     . GLY A 131 ? 1.1042 1.0586 1.1536 -0.0200 0.0024  -0.1169 131 GLY A C     
1097 O  O     . GLY A 131 ? 1.0485 1.0125 1.0894 -0.0221 0.0012  -0.1145 131 GLY A O     
1098 N  N     . ASP A 132 ? 1.1858 1.1265 1.2277 -0.0176 0.0060  -0.1267 132 ASP A N     
1099 C  CA    . ASP A 132 ? 1.1759 1.1130 1.1976 -0.0168 0.0096  -0.1354 132 ASP A CA    
1100 C  C     . ASP A 132 ? 1.1664 1.1090 1.1884 -0.0087 0.0207  -0.1353 132 ASP A C     
1101 O  O     . ASP A 132 ? 1.1266 1.0672 1.1323 -0.0068 0.0256  -0.1419 132 ASP A O     
1102 C  CB    . ASP A 132 ? 1.3020 1.2199 1.3125 -0.0190 0.0071  -0.1476 132 ASP A CB    
1103 C  CG    . ASP A 132 ? 1.5371 1.4490 1.5514 -0.0272 -0.0044 -0.1472 132 ASP A CG    
1104 O  OD1   . ASP A 132 ? 1.5729 1.4949 1.5858 -0.0327 -0.0111 -0.1412 132 ASP A OD1   
1105 O  OD2   . ASP A 132 ? 1.4933 1.3902 1.5131 -0.0282 -0.0065 -0.1525 132 ASP A OD2   
1106 N  N     . GLU A 133 ? 1.1461 1.0964 1.1862 -0.0040 0.0248  -0.1274 133 GLU A N     
1107 C  CA    . GLU A 133 ? 1.0852 1.0415 1.1289 0.0037  0.0351  -0.1262 133 GLU A CA    
1108 C  C     . GLU A 133 ? 1.0304 1.0001 1.0642 0.0032  0.0376  -0.1234 133 GLU A C     
1109 O  O     . GLU A 133 ? 1.0859 1.0668 1.1219 -0.0010 0.0325  -0.1163 133 GLU A O     
1110 C  CB    . GLU A 133 ? 1.0447 1.0091 1.1106 0.0075  0.0368  -0.1165 133 GLU A CB    
1111 C  CG    . GLU A 133 ? 1.1040 1.0560 1.1812 0.0124  0.0402  -0.1192 133 GLU A CG    
1112 C  CD    . GLU A 133 ? 1.2050 1.1578 1.2863 0.0212  0.0513  -0.1206 133 GLU A CD    
1113 O  OE1   . GLU A 133 ? 1.2642 1.2206 1.3328 0.0231  0.0569  -0.1245 133 GLU A OE1   
1114 O  OE2   . GLU A 133 ? 1.2189 1.1694 1.3169 0.0265  0.0549  -0.1169 133 GLU A OE2   
1115 N  N     . GLU A 134 ? 1.0039 0.9721 1.0272 0.0078  0.0461  -0.1289 134 GLU A N     
1116 C  CA    . GLU A 134 ? 1.1066 1.0874 1.1213 0.0080  0.0498  -0.1258 134 GLU A CA    
1117 C  C     . GLU A 134 ? 1.0343 1.0283 1.0648 0.0139  0.0574  -0.1179 134 GLU A C     
1118 O  O     . GLU A 134 ? 0.9907 0.9810 1.0296 0.0208  0.0648  -0.1196 134 GLU A O     
1119 C  CB    . GLU A 134 ? 1.1435 1.1165 1.1361 0.0093  0.0549  -0.1356 134 GLU A CB    
1120 C  CG    . GLU A 134 ? 1.3471 1.3336 1.3314 0.0102  0.0603  -0.1315 134 GLU A CG    
1121 C  CD    . GLU A 134 ? 1.4439 1.4373 1.4194 0.0024  0.0518  -0.1273 134 GLU A CD    
1122 O  OE1   . GLU A 134 ? 1.2341 1.2317 1.2207 -0.0021 0.0437  -0.1210 134 GLU A OE1   
1123 O  OE2   . GLU A 134 ? 1.3592 1.3539 1.3167 0.0012  0.0536  -0.1298 134 GLU A OE2   
1124 N  N     . LEU A 135 ? 0.9727 0.9816 1.0080 0.0111  0.0552  -0.1092 135 LEU A N     
1125 C  CA    . LEU A 135 ? 0.8856 0.9087 0.9364 0.0152  0.0606  -0.1009 135 LEU A CA    
1126 C  C     . LEU A 135 ? 0.8290 0.8593 0.8721 0.0183  0.0693  -0.1009 135 LEU A C     
1127 O  O     . LEU A 135 ? 0.8635 0.8920 0.8892 0.0153  0.0690  -0.1046 135 LEU A O     
1128 C  CB    . LEU A 135 ? 0.7759 0.8105 0.8365 0.0102  0.0533  -0.0918 135 LEU A CB    
1129 C  CG    . LEU A 135 ? 0.8399 0.8686 0.9013 0.0050  0.0436  -0.0917 135 LEU A CG    
1130 C  CD1   . LEU A 135 ? 0.6948 0.7344 0.7605 0.0000  0.0377  -0.0842 135 LEU A CD1   
1131 C  CD2   . LEU A 135 ? 0.8896 0.9129 0.9644 0.0082  0.0433  -0.0909 135 LEU A CD2   
1132 N  N     . LYS A 136 ? 0.6995 0.7391 0.7566 0.0243  0.0771  -0.0960 136 LYS A N     
1133 C  CA    . LYS A 136 ? 0.7282 0.7783 0.7827 0.0272  0.0858  -0.0932 136 LYS A CA    
1134 C  C     . LYS A 136 ? 0.6831 0.7493 0.7466 0.0222  0.0814  -0.0829 136 LYS A C     
1135 O  O     . LYS A 136 ? 0.6504 0.7232 0.7300 0.0206  0.0763  -0.0764 136 LYS A O     
1136 C  CB    . LYS A 136 ? 0.7478 0.8007 0.8147 0.0365  0.0969  -0.0923 136 LYS A CB    
1137 C  CG    . LYS A 136 ? 0.7988 0.8633 0.8642 0.0403  0.1073  -0.0888 136 LYS A CG    
1138 C  CD    . LYS A 136 ? 1.0029 1.0609 1.0661 0.0501  0.1203  -0.0949 136 LYS A CD    
1139 C  CE    . LYS A 136 ? 0.8840 0.9518 0.9730 0.0571  0.1263  -0.0871 136 LYS A CE    
1140 N  NZ    . LYS A 136 ? 0.8539 0.9332 0.9475 0.0642  0.1398  -0.0833 136 LYS A NZ    
1141 N  N     . MET A 137 ? 0.6376 0.7094 0.6902 0.0195  0.0831  -0.0814 137 MET A N     
1142 C  CA    . MET A 137 ? 0.6526 0.7375 0.7124 0.0140  0.0788  -0.0724 137 MET A CA    
1143 C  C     . MET A 137 ? 0.6031 0.7015 0.6686 0.0171  0.0880  -0.0662 137 MET A C     
1144 O  O     . MET A 137 ? 0.5049 0.6017 0.5608 0.0222  0.0976  -0.0699 137 MET A O     
1145 C  CB    . MET A 137 ? 0.5682 0.6489 0.6129 0.0070  0.0713  -0.0739 137 MET A CB    
1146 C  CG    . MET A 137 ? 0.7120 0.7804 0.7515 0.0037  0.0624  -0.0793 137 MET A CG    
1147 S  SD    . MET A 137 ? 0.8004 0.8653 0.8243 -0.0039 0.0541  -0.0798 137 MET A SD    
1148 C  CE    . MET A 137 ? 0.7133 0.7650 0.7149 -0.0020 0.0570  -0.0906 137 MET A CE    
1149 N  N     . LEU A 138 ? 0.5250 0.6367 0.6062 0.0138  0.0851  -0.0569 138 LEU A N     
1150 C  CA    . LEU A 138 ? 0.5633 0.6898 0.6535 0.0152  0.0925  -0.0490 138 LEU A CA    
1151 C  C     . LEU A 138 ? 0.5097 0.6443 0.6048 0.0071  0.0852  -0.0417 138 LEU A C     
1152 O  O     . LEU A 138 ? 0.4588 0.5957 0.5653 0.0031  0.0769  -0.0386 138 LEU A O     
1153 C  CB    . LEU A 138 ? 0.5195 0.6558 0.6311 0.0209  0.0979  -0.0438 138 LEU A CB    
1154 C  CG    . LEU A 138 ? 0.5362 0.6892 0.6600 0.0230  0.1064  -0.0347 138 LEU A CG    
1155 C  CD1   . LEU A 138 ? 0.5927 0.7433 0.7015 0.0288  0.1186  -0.0387 138 LEU A CD1   
1156 C  CD2   . LEU A 138 ? 0.6051 0.7692 0.7533 0.0275  0.1091  -0.0281 138 LEU A CD2   
1157 N  N     . ALA A 139 ? 0.4775 0.6158 0.5635 0.0048  0.0882  -0.0390 139 ALA A N     
1158 C  CA    . ALA A 139 ? 0.5645 0.7097 0.6563 -0.0027 0.0821  -0.0317 139 ALA A CA    
1159 C  C     . ALA A 139 ? 0.6062 0.7679 0.7162 -0.0023 0.0878  -0.0216 139 ALA A C     
1160 O  O     . ALA A 139 ? 0.5068 0.6751 0.6188 0.0038  0.0986  -0.0199 139 ALA A O     
1161 C  CB    . ALA A 139 ? 0.5514 0.6916 0.6247 -0.0061 0.0812  -0.0328 139 ALA A CB    
1162 N  N     . PHE A 140 ? 0.5593 0.7277 0.6828 -0.0089 0.0806  -0.0150 140 PHE A N     
1163 C  CA    . PHE A 140 ? 0.5563 0.7408 0.6986 -0.0099 0.0847  -0.0047 140 PHE A CA    
1164 C  C     . PHE A 140 ? 0.5278 0.7156 0.6766 -0.0189 0.0771  0.0015  140 PHE A C     
1165 O  O     . PHE A 140 ? 0.4906 0.6692 0.6346 -0.0240 0.0674  -0.0021 140 PHE A O     
1166 C  CB    . PHE A 140 ? 0.5270 0.7200 0.6891 -0.0068 0.0849  -0.0018 140 PHE A CB    
1167 C  CG    . PHE A 140 ? 0.5302 0.7225 0.7022 -0.0128 0.0728  -0.0013 140 PHE A CG    
1168 C  CD1   . PHE A 140 ? 0.5324 0.7351 0.7205 -0.0196 0.0673  0.0067  140 PHE A CD1   
1169 C  CD2   . PHE A 140 ? 0.5209 0.7021 0.6858 -0.0117 0.0669  -0.0087 140 PHE A CD2   
1170 C  CE1   . PHE A 140 ? 0.5139 0.7151 0.7086 -0.0251 0.0561  0.0061  140 PHE A CE1   
1171 C  CE2   . PHE A 140 ? 0.5440 0.7249 0.7162 -0.0167 0.0564  -0.0083 140 PHE A CE2   
1172 C  CZ    . PHE A 140 ? 0.4988 0.6895 0.6848 -0.0234 0.0509  -0.0013 140 PHE A CZ    
1173 N  N     . ALA A 141 ? 0.5826 0.7835 0.7433 -0.0206 0.0821  0.0111  141 ALA A N     
1174 C  CA    . ALA A 141 ? 0.5167 0.7218 0.6874 -0.0292 0.0759  0.0184  141 ALA A CA    
1175 C  C     . ALA A 141 ? 0.6444 0.8672 0.8391 -0.0304 0.0795  0.0291  141 ALA A C     
1176 O  O     . ALA A 141 ? 0.5530 0.7856 0.7549 -0.0237 0.0887  0.0319  141 ALA A O     
1177 C  CB    . ALA A 141 ? 0.4205 0.6215 0.5772 -0.0315 0.0782  0.0203  141 ALA A CB    
1178 N  N     . ILE A 142 ? 0.5703 0.7971 0.7786 -0.0390 0.0721  0.0354  142 ILE A N     
1179 C  CA    . ILE A 142 ? 0.5775 0.8215 0.8107 -0.0421 0.0735  0.0465  142 ILE A CA    
1180 C  C     . ILE A 142 ? 0.5888 0.8362 0.8282 -0.0494 0.0728  0.0551  142 ILE A C     
1181 O  O     . ILE A 142 ? 0.6085 0.8440 0.8360 -0.0536 0.0679  0.0520  142 ILE A O     
1182 C  CB    . ILE A 142 ? 0.5874 0.8346 0.8367 -0.0465 0.0629  0.0462  142 ILE A CB    
1183 C  CG1   . ILE A 142 ? 0.5314 0.7684 0.7792 -0.0563 0.0503  0.0436  142 ILE A CG1   
1184 C  CG2   . ILE A 142 ? 0.5403 0.7822 0.7825 -0.0398 0.0624  0.0379  142 ILE A CG2   
1185 C  CD1   . ILE A 142 ? 0.5963 0.8331 0.8528 -0.0604 0.0391  0.0405  142 ILE A CD1   
1186 N  N     . ALA A 143 ? 0.6224 0.8870 0.8825 -0.0506 0.0781  0.0668  143 ALA A N     
1187 C  CA    . ALA A 143 ? 0.6443 0.9149 0.9164 -0.0583 0.0773  0.0772  143 ALA A CA    
1188 C  C     . ALA A 143 ? 0.7122 0.9932 1.0115 -0.0662 0.0690  0.0841  143 ALA A C     
1189 O  O     . ALA A 143 ? 0.6718 0.9656 0.9863 -0.0633 0.0710  0.0874  143 ALA A O     
1190 C  CB    . ALA A 143 ? 0.6704 0.9534 0.9433 -0.0533 0.0918  0.0868  143 ALA A CB    
1191 N  N     . THR A 144 ? 0.8328 1.1081 1.1386 -0.0763 0.0596  0.0863  144 THR A N     
1192 C  CA    . THR A 144 ? 0.7838 1.0651 1.1123 -0.0854 0.0488  0.0902  144 THR A CA    
1193 C  C     . THR A 144 ? 0.7352 1.0248 1.0836 -0.0941 0.0484  0.1029  144 THR A C     
1194 O  O     . THR A 144 ? 0.7176 1.0024 1.0591 -0.0950 0.0529  0.1066  144 THR A O     
1195 C  CB    . THR A 144 ? 0.8242 1.0880 1.1426 -0.0908 0.0350  0.0786  144 THR A CB    
1196 O  OG1   . THR A 144 ? 1.0608 1.3321 1.3988 -0.0980 0.0248  0.0809  144 THR A OG1   
1197 C  CG2   . THR A 144 ? 0.8447 1.0932 1.1544 -0.0969 0.0307  0.0768  144 THR A CG2   
1198 N  N     . LEU A 145 ? 0.7683 1.0707 1.1423 -0.1008 0.0423  0.1100  145 LEU A N     
1199 C  CA    . LEU A 145 ? 0.7798 1.0911 1.1771 -0.1104 0.0403  0.1227  145 LEU A CA    
1200 C  C     . LEU A 145 ? 0.7739 1.0687 1.1712 -0.1217 0.0251  0.1165  145 LEU A C     
1201 O  O     . LEU A 145 ? 0.7668 1.0602 1.1707 -0.1271 0.0134  0.1113  145 LEU A O     
1202 C  CB    . LEU A 145 ? 0.6678 1.0028 1.0946 -0.1120 0.0416  0.1345  145 LEU A CB    
1203 C  CG    . LEU A 145 ? 0.7919 1.1407 1.2478 -0.1216 0.0408  0.1502  145 LEU A CG    
1204 C  CD1   . LEU A 145 ? 0.7423 1.0867 1.2143 -0.1355 0.0232  0.1489  145 LEU A CD1   
1205 C  CD2   . LEU A 145 ? 0.8239 1.1671 1.2727 -0.1220 0.0486  0.1560  145 LEU A CD2   
1206 N  N     . TYR A 146 ? 0.7820 1.0642 1.1717 -0.1251 0.0254  0.1170  146 TYR A N     
1207 C  CA    . TYR A 146 ? 0.8104 1.0733 1.1966 -0.1341 0.0127  0.1096  146 TYR A CA    
1208 C  C     . TYR A 146 ? 0.8806 1.1463 1.2893 -0.1448 0.0099  0.1213  146 TYR A C     
1209 O  O     . TYR A 146 ? 0.8853 1.1546 1.2960 -0.1433 0.0190  0.1312  146 TYR A O     
1210 C  CB    . TYR A 146 ? 0.8958 1.1385 1.2540 -0.1290 0.0143  0.0992  146 TYR A CB    
1211 C  CG    . TYR A 146 ? 0.8932 1.1156 1.2487 -0.1373 0.0035  0.0927  146 TYR A CG    
1212 C  CD1   . TYR A 146 ? 0.9280 1.1387 1.2776 -0.1408 -0.0080 0.0804  146 TYR A CD1   
1213 C  CD2   . TYR A 146 ? 0.8528 1.0677 1.2115 -0.1413 0.0052  0.0992  146 TYR A CD2   
1214 C  CE1   . TYR A 146 ? 0.9728 1.1639 1.3191 -0.1478 -0.0170 0.0736  146 TYR A CE1   
1215 C  CE2   . TYR A 146 ? 0.8734 1.0685 1.2306 -0.1483 -0.0040 0.0931  146 TYR A CE2   
1216 C  CZ    . TYR A 146 ? 0.9681 1.1510 1.3188 -0.1513 -0.0148 0.0798  146 TYR A CZ    
1217 O  OH    . TYR A 146 ? 0.9816 1.1439 1.3299 -0.1576 -0.0231 0.0730  146 TYR A OH    
1218 N  N     . HIS A 147 ? 1.0003 1.2643 1.4256 -0.1556 -0.0029 0.1204  147 HIS A N     
1219 C  CA    . HIS A 147 ? 1.0533 1.3114 1.4963 -0.1675 -0.0094 0.1268  147 HIS A CA    
1220 C  C     . HIS A 147 ? 1.1068 1.3393 1.5362 -0.1731 -0.0217 0.1122  147 HIS A C     
1221 O  O     . HIS A 147 ? 1.0892 1.3154 1.5073 -0.1724 -0.0294 0.0998  147 HIS A O     
1222 C  CB    . HIS A 147 ? 0.9696 1.2458 1.4448 -0.1771 -0.0151 0.1379  147 HIS A CB    
1223 C  CG    . HIS A 147 ? 0.9577 1.2599 1.4503 -0.1723 -0.0023 0.1544  147 HIS A CG    
1224 N  ND1   . HIS A 147 ? 0.9332 1.2557 1.4358 -0.1677 0.0005  0.1580  147 HIS A ND1   
1225 C  CD2   . HIS A 147 ? 0.9780 1.2895 1.4799 -0.1708 0.0091  0.1687  147 HIS A CD2   
1226 C  CE1   . HIS A 147 ? 1.0056 1.3484 1.5229 -0.1634 0.0136  0.1732  147 HIS A CE1   
1227 N  NE2   . HIS A 147 ? 1.0402 1.3770 1.5567 -0.1653 0.0191  0.1800  147 HIS A NE2   
1228 N  N     . GLU A 148 ? 1.1668 1.3843 1.5971 -0.1780 -0.0228 0.1139  148 GLU A N     
1229 C  CA    . GLU A 148 ? 1.1271 1.3191 1.5455 -0.1828 -0.0332 0.1003  148 GLU A CA    
1230 C  C     . GLU A 148 ? 1.1945 1.3842 1.6288 -0.1951 -0.0477 0.0966  148 GLU A C     
1231 O  O     . GLU A 148 ? 1.1128 1.3126 1.5735 -0.2044 -0.0507 0.1080  148 GLU A O     
1232 C  CB    . GLU A 148 ? 1.2112 1.3886 1.6296 -0.1847 -0.0301 0.1047  148 GLU A CB    
1233 C  CG    . GLU A 148 ? 1.1934 1.3433 1.5944 -0.1854 -0.0368 0.0902  148 GLU A CG    
1234 C  CD    . GLU A 148 ? 1.3572 1.4920 1.7735 -0.1954 -0.0420 0.0941  148 GLU A CD    
1235 O  OE1   . GLU A 148 ? 1.3959 1.5120 1.8105 -0.2020 -0.0527 0.0826  148 GLU A OE1   
1236 O  OE2   . GLU A 148 ? 1.4048 1.5460 1.8345 -0.1964 -0.0351 0.1088  148 GLU A OE2   
1237 N  N     . GLY A 149 ? 1.1604 1.3375 1.5784 -0.1953 -0.0568 0.0809  149 GLY A N     
1238 C  CA    . GLY A 149 ? 1.0914 1.2642 1.5188 -0.2067 -0.0716 0.0747  149 GLY A CA    
1239 C  C     . GLY A 149 ? 1.1634 1.3503 1.5878 -0.2048 -0.0766 0.0704  149 GLY A C     
1240 O  O     . GLY A 149 ? 1.1414 1.3200 1.5616 -0.2115 -0.0893 0.0600  149 GLY A O     
1241 N  N     . GLU A 150 ? 1.3347 1.5423 1.7609 -0.1956 -0.0668 0.0782  150 GLU A N     
1242 C  CA    . GLU A 150 ? 1.2195 1.4412 1.6447 -0.1930 -0.0708 0.0756  150 GLU A CA    
1243 C  C     . GLU A 150 ? 1.1287 1.3348 1.5243 -0.1868 -0.0738 0.0591  150 GLU A C     
1244 O  O     . GLU A 150 ? 1.1911 1.3780 1.5670 -0.1824 -0.0704 0.0506  150 GLU A O     
1245 C  CB    . GLU A 150 ? 1.2533 1.4990 1.6870 -0.1834 -0.0581 0.0874  150 GLU A CB    
1246 C  CG    . GLU A 150 ? 1.2982 1.5576 1.7533 -0.1844 -0.0483 0.1040  150 GLU A CG    
1247 C  CD    . GLU A 150 ? 1.3607 1.6414 1.8190 -0.1729 -0.0344 0.1130  150 GLU A CD    
1248 O  OE1   . GLU A 150 ? 1.3425 1.6215 1.7894 -0.1643 -0.0215 0.1156  150 GLU A OE1   
1249 O  OE2   . GLU A 150 ? 1.3880 1.6870 1.8603 -0.1727 -0.0366 0.1176  150 GLU A OE2   
1250 N  N     . GLU A 151 ? 1.0646 1.2805 1.4585 -0.1862 -0.0802 0.0556  151 GLU A N     
1251 C  CA    . GLU A 151 ? 1.0502 1.2560 1.4178 -0.1787 -0.0813 0.0425  151 GLU A CA    
1252 C  C     . GLU A 151 ? 1.0169 1.2310 1.3749 -0.1648 -0.0673 0.0453  151 GLU A C     
1253 O  O     . GLU A 151 ? 0.9607 1.1880 1.3310 -0.1607 -0.0569 0.0567  151 GLU A O     
1254 C  CB    . GLU A 151 ? 1.0593 1.2724 1.4283 -0.1838 -0.0940 0.0384  151 GLU A CB    
1255 C  CG    . GLU A 151 ? 1.1419 1.3570 1.5300 -0.1988 -0.1077 0.0409  151 GLU A CG    
1256 C  CD    . GLU A 151 ? 1.1652 1.3929 1.5572 -0.2035 -0.1199 0.0398  151 GLU A CD    
1257 O  OE1   . GLU A 151 ? 1.2306 1.4472 1.6166 -0.2133 -0.1339 0.0306  151 GLU A OE1   
1258 O  OE2   . GLU A 151 ? 1.1766 1.4254 1.5775 -0.1971 -0.1155 0.0482  151 GLU A OE2   
1259 N  N     . PHE A 152 ? 1.0201 1.2260 1.3556 -0.1573 -0.0670 0.0349  152 PHE A N     
1260 C  CA    . PHE A 152 ? 0.9193 1.1292 1.2434 -0.1445 -0.0547 0.0355  152 PHE A CA    
1261 C  C     . PHE A 152 ? 0.8461 1.0792 1.1848 -0.1401 -0.0510 0.0446  152 PHE A C     
1262 O  O     . PHE A 152 ? 0.8725 1.1152 1.2192 -0.1440 -0.0599 0.0451  152 PHE A O     
1263 C  CB    . PHE A 152 ? 0.8766 1.0710 1.1744 -0.1387 -0.0561 0.0222  152 PHE A CB    
1264 C  CG    . PHE A 152 ? 0.8737 1.0708 1.1596 -0.1264 -0.0450 0.0219  152 PHE A CG    
1265 C  CD1   . PHE A 152 ? 0.9126 1.1032 1.1908 -0.1209 -0.0349 0.0230  152 PHE A CD1   
1266 C  CD2   . PHE A 152 ? 0.8478 1.0535 1.1301 -0.1205 -0.0451 0.0205  152 PHE A CD2   
1267 C  CE1   . PHE A 152 ? 0.7793 0.9714 1.0458 -0.1104 -0.0255 0.0218  152 PHE A CE1   
1268 C  CE2   . PHE A 152 ? 0.7970 1.0036 1.0689 -0.1096 -0.0351 0.0197  152 PHE A CE2   
1269 C  CZ    . PHE A 152 ? 0.7570 0.9564 1.0205 -0.1048 -0.0256 0.0198  152 PHE A CZ    
1270 N  N     . ALA A 153 ? 0.8359 1.0783 1.1781 -0.1320 -0.0378 0.0521  153 ALA A N     
1271 C  CA    . ALA A 153 ? 0.8100 1.0725 1.1640 -0.1250 -0.0310 0.0601  153 ALA A CA    
1272 C  C     . ALA A 153 ? 0.8801 1.1629 1.2635 -0.1324 -0.0359 0.0720  153 ALA A C     
1273 O  O     . ALA A 153 ? 0.8122 1.1117 1.2074 -0.1288 -0.0354 0.0775  153 ALA A O     
1274 C  CB    . ALA A 153 ? 0.7980 1.0591 1.1383 -0.1180 -0.0329 0.0524  153 ALA A CB    
1275 N  N     . GLU A 154 ? 0.8268 1.1086 1.2239 -0.1429 -0.0409 0.0768  154 GLU A N     
1276 C  CA    . GLU A 154 ? 1.0524 1.3551 1.4802 -0.1499 -0.0442 0.0902  154 GLU A CA    
1277 C  C     . GLU A 154 ? 0.9640 1.2850 1.4061 -0.1420 -0.0287 0.1032  154 GLU A C     
1278 O  O     . GLU A 154 ? 0.7853 1.1271 1.2459 -0.1391 -0.0263 0.1123  154 GLU A O     
1279 C  CB    . GLU A 154 ? 1.1522 1.4480 1.5918 -0.1637 -0.0535 0.0922  154 GLU A CB    
1280 C  CG    . GLU A 154 ? 1.2276 1.5249 1.6764 -0.1754 -0.0711 0.0892  154 GLU A CG    
1281 C  CD    . GLU A 154 ? 1.2785 1.5612 1.7318 -0.1887 -0.0813 0.0864  154 GLU A CD    
1282 O  OE1   . GLU A 154 ? 1.2832 1.5673 1.7503 -0.1918 -0.0754 0.0953  154 GLU A OE1   
1283 O  OE2   . GLU A 154 ? 1.3912 1.6613 1.8348 -0.1962 -0.0950 0.0755  154 GLU A OE2   
1284 N  N     . GLY A 155 ? 0.8563 1.1702 1.2903 -0.1382 -0.0179 0.1048  155 GLY A N     
1285 C  CA    . GLY A 155 ? 0.7250 1.0541 1.1674 -0.1297 -0.0020 0.1156  155 GLY A CA    
1286 C  C     . GLY A 155 ? 0.7827 1.1151 1.2120 -0.1162 0.0072  0.1112  155 GLY A C     
1287 O  O     . GLY A 155 ? 0.7340 1.0519 1.1411 -0.1122 0.0037  0.0986  155 GLY A O     
1288 N  N     . PRO A 156 ? 0.7838 1.1352 1.2270 -0.1088 0.0196  0.1218  156 PRO A N     
1289 C  CA    . PRO A 156 ? 0.6482 1.0025 1.0809 -0.0955 0.0291  0.1179  156 PRO A CA    
1290 C  C     . PRO A 156 ? 0.6940 1.0337 1.0994 -0.0867 0.0405  0.1104  156 PRO A C     
1291 O  O     . PRO A 156 ? 0.6732 1.0045 1.0703 -0.0898 0.0429  0.1108  156 PRO A O     
1292 C  CB    . PRO A 156 ? 0.6103 0.9905 1.0707 -0.0915 0.0387  0.1330  156 PRO A CB    
1293 C  CG    . PRO A 156 ? 0.5953 0.9825 1.0708 -0.0989 0.0412  0.1441  156 PRO A CG    
1294 C  CD    . PRO A 156 ? 0.5959 0.9675 1.0672 -0.1121 0.0255  0.1382  156 PRO A CD    
1295 N  N     . ILE A 157 ? 0.6929 1.0297 1.0847 -0.0758 0.0470  0.1037  157 ILE A N     
1296 C  CA    . ILE A 157 ? 0.6099 0.9356 0.9773 -0.0665 0.0586  0.0972  157 ILE A CA    
1297 C  C     . ILE A 157 ? 0.6265 0.9681 1.0039 -0.0595 0.0747  0.1078  157 ILE A C     
1298 O  O     . ILE A 157 ? 0.6452 1.0045 1.0429 -0.0553 0.0799  0.1159  157 ILE A O     
1299 C  CB    . ILE A 157 ? 0.5901 0.9050 0.9392 -0.0582 0.0587  0.0854  157 ILE A CB    
1300 C  CG1   . ILE A 157 ? 0.6017 0.9011 0.9395 -0.0647 0.0438  0.0753  157 ILE A CG1   
1301 C  CG2   . ILE A 157 ? 0.5931 0.8972 0.9180 -0.0491 0.0704  0.0788  157 ILE A CG2   
1302 C  CD1   . ILE A 157 ? 0.5706 0.8694 0.9068 -0.0600 0.0397  0.0699  157 ILE A CD1   
1303 N  N     . LEU A 158 ? 0.6068 0.9429 0.9703 -0.0580 0.0829  0.1085  158 LEU A N     
1304 C  CA    . LEU A 158 ? 0.5961 0.9468 0.9662 -0.0516 0.0989  0.1187  158 LEU A CA    
1305 C  C     . LEU A 158 ? 0.6457 0.9913 0.9947 -0.0383 0.1120  0.1111  158 LEU A C     
1306 O  O     . LEU A 158 ? 0.5759 0.9355 0.9353 -0.0298 0.1240  0.1168  158 LEU A O     
1307 C  CB    . LEU A 158 ? 0.6552 1.0045 1.0224 -0.0575 0.1011  0.1254  158 LEU A CB    
1308 C  CG    . LEU A 158 ? 0.7103 1.0648 1.0998 -0.0708 0.0908  0.1349  158 LEU A CG    
1309 C  CD1   . LEU A 158 ? 0.7105 1.0489 1.0953 -0.0794 0.0735  0.1250  158 LEU A CD1   
1310 C  CD2   . LEU A 158 ? 0.6908 1.0440 1.0754 -0.0738 0.0965  0.1422  158 LEU A CD2   
1311 N  N     . MET A 159 ? 0.6069 0.9325 0.9269 -0.0364 0.1098  0.0985  159 MET A N     
1312 C  CA    . MET A 159 ? 0.5897 0.9074 0.8873 -0.0250 0.1204  0.0895  159 MET A CA    
1313 C  C     . MET A 159 ? 0.5723 0.8710 0.8519 -0.0245 0.1108  0.0750  159 MET A C     
1314 O  O     . MET A 159 ? 0.6306 0.9181 0.9046 -0.0326 0.0984  0.0706  159 MET A O     
1315 C  CB    . MET A 159 ? 0.5913 0.9050 0.8686 -0.0224 0.1301  0.0899  159 MET A CB    
1316 C  CG    . MET A 159 ? 0.5483 0.8766 0.8410 -0.0276 0.1344  0.1048  159 MET A CG    
1317 S  SD    . MET A 159 ? 0.6250 0.9468 0.8905 -0.0257 0.1432  0.1052  159 MET A SD    
1318 C  CE    . MET A 159 ? 0.5597 0.9068 0.8478 -0.0249 0.1570  0.1246  159 MET A CE    
1319 N  N     . ILE A 160 ? 0.5610 0.8559 0.8325 -0.0148 0.1170  0.0678  160 ILE A N     
1320 C  CA    . ILE A 160 ? 0.5745 0.8511 0.8269 -0.0128 0.1106  0.0542  160 ILE A CA    
1321 C  C     . ILE A 160 ? 0.5785 0.8455 0.8066 -0.0039 0.1217  0.0463  160 ILE A C     
1322 O  O     . ILE A 160 ? 0.5930 0.8670 0.8241 0.0053  0.1342  0.0476  160 ILE A O     
1323 C  CB    . ILE A 160 ? 0.5744 0.8540 0.8408 -0.0102 0.1059  0.0527  160 ILE A CB    
1324 C  CG1   . ILE A 160 ? 0.5460 0.8336 0.8329 -0.0203 0.0927  0.0592  160 ILE A CG1   
1325 C  CG2   . ILE A 160 ? 0.5557 0.8168 0.8020 -0.0068 0.1016  0.0394  160 ILE A CG2   
1326 C  CD1   . ILE A 160 ? 0.4985 0.7928 0.8015 -0.0182 0.0878  0.0603  160 ILE A CD1   
1327 N  N     . SER A 161 ? 0.5485 0.8000 0.7529 -0.0065 0.1174  0.0383  161 SER A N     
1328 C  CA    . SER A 161 ? 0.5278 0.7692 0.7067 0.0003  0.1260  0.0303  161 SER A CA    
1329 C  C     . SER A 161 ? 0.5963 0.8201 0.7598 0.0025  0.1198  0.0171  161 SER A C     
1330 O  O     . SER A 161 ? 0.5711 0.7876 0.7360 -0.0036 0.1075  0.0141  161 SER A O     
1331 C  CB    . SER A 161 ? 0.5540 0.7926 0.7174 -0.0042 0.1263  0.0326  161 SER A CB    
1332 O  OG    . SER A 161 ? 0.5976 0.8267 0.7581 -0.0130 0.1128  0.0306  161 SER A OG    
1333 N  N     . TYR A 162 ? 0.5748 0.7916 0.7237 0.0111  0.1287  0.0092  162 TYR A N     
1334 C  CA    . TYR A 162 ? 0.5421 0.7416 0.6758 0.0133  0.1237  -0.0032 162 TYR A CA    
1335 C  C     . TYR A 162 ? 0.6123 0.8010 0.7187 0.0177  0.1307  -0.0117 162 TYR A C     
1336 O  O     . TYR A 162 ? 0.5714 0.7670 0.6714 0.0213  0.1415  -0.0082 162 TYR A O     
1337 C  CB    . TYR A 162 ? 0.5902 0.7902 0.7377 0.0195  0.1254  -0.0054 162 TYR A CB    
1338 C  CG    . TYR A 162 ? 0.6412 0.8492 0.7949 0.0295  0.1405  -0.0034 162 TYR A CG    
1339 C  CD1   . TYR A 162 ? 0.6663 0.8937 0.8442 0.0309  0.1463  0.0088  162 TYR A CD1   
1340 C  CD2   . TYR A 162 ? 0.6313 0.8273 0.7672 0.0378  0.1492  -0.0136 162 TYR A CD2   
1341 C  CE1   . TYR A 162 ? 0.6751 0.9106 0.8600 0.0409  0.1612  0.0113  162 TYR A CE1   
1342 C  CE2   . TYR A 162 ? 0.6488 0.8511 0.7899 0.0478  0.1641  -0.0123 162 TYR A CE2   
1343 C  CZ    . TYR A 162 ? 0.7112 0.9337 0.8772 0.0497  0.1705  0.0005  162 TYR A CZ    
1344 O  OH    . TYR A 162 ? 0.6862 0.9158 0.8588 0.0605  0.1863  0.0023  162 TYR A OH    
1345 N  N     . ALA A 163 ? 0.6041 0.7760 0.6940 0.0171  0.1241  -0.0225 163 ALA A N     
1346 C  CA    . ALA A 163 ? 0.6272 0.7873 0.6897 0.0196  0.1277  -0.0316 163 ALA A CA    
1347 C  C     . ALA A 163 ? 0.6864 0.8294 0.7392 0.0211  0.1221  -0.0435 163 ALA A C     
1348 O  O     . ALA A 163 ? 0.6570 0.7960 0.7190 0.0170  0.1118  -0.0440 163 ALA A O     
1349 C  CB    . ALA A 163 ? 0.5200 0.6794 0.5688 0.0123  0.1221  -0.0287 163 ALA A CB    
1350 N  N     . ASP A 164 ? 0.7482 0.8810 0.7822 0.0270  0.1292  -0.0531 164 ASP A N     
1351 C  CA    . ASP A 164 ? 0.6882 0.8032 0.7107 0.0278  0.1239  -0.0649 164 ASP A CA    
1352 C  C     . ASP A 164 ? 0.8369 0.9407 0.8311 0.0305  0.1289  -0.0750 164 ASP A C     
1353 O  O     . ASP A 164 ? 0.8358 0.9446 0.8157 0.0286  0.1316  -0.0722 164 ASP A O     
1354 C  CB    . ASP A 164 ? 0.6921 0.8049 0.7315 0.0342  0.1273  -0.0671 164 ASP A CB    
1355 C  CG    . ASP A 164 ? 0.8090 0.9274 0.8521 0.0441  0.1428  -0.0667 164 ASP A CG    
1356 O  OD1   . ASP A 164 ? 0.8741 0.9970 0.9040 0.0463  0.1516  -0.0661 164 ASP A OD1   
1357 O  OD2   . ASP A 164 ? 0.8092 0.9277 0.8687 0.0500  0.1466  -0.0666 164 ASP A OD2   
1358 N  N     . GLU A 165 ? 0.8923 0.9807 0.8779 0.0347  0.1299  -0.0865 165 GLU A N     
1359 C  CA    . GLU A 165 ? 0.9795 1.0557 0.9368 0.0370  0.1341  -0.0975 165 GLU A CA    
1360 C  C     . GLU A 165 ? 1.0192 1.1017 0.9694 0.0454  0.1503  -0.0974 165 GLU A C     
1361 O  O     . GLU A 165 ? 1.0524 1.1293 0.9764 0.0464  0.1545  -0.1041 165 GLU A O     
1362 C  CB    . GLU A 165 ? 1.0154 1.0722 0.9670 0.0388  0.1305  -0.1102 165 GLU A CB    
1363 C  CG    . GLU A 165 ? 1.1695 1.2113 1.0926 0.0345  0.1242  -0.1212 165 GLU A CG    
1364 C  CD    . GLU A 165 ? 1.2325 1.2786 1.1503 0.0246  0.1116  -0.1157 165 GLU A CD    
1365 O  OE1   . GLU A 165 ? 1.3957 1.4512 1.3024 0.0225  0.1138  -0.1103 165 GLU A OE1   
1366 O  OE2   . GLU A 165 ? 1.3688 1.4092 1.2943 0.0192  0.1000  -0.1160 165 GLU A OE2   
1367 N  N     . GLU A 166 ? 0.9464 1.0414 0.9192 0.0514  0.1595  -0.0897 166 GLU A N     
1368 C  CA    . GLU A 166 ? 0.9971 1.0993 0.9664 0.0604  0.1764  -0.0887 166 GLU A CA    
1369 C  C     . GLU A 166 ? 0.9225 1.0428 0.8909 0.0579  0.1809  -0.0768 166 GLU A C     
1370 O  O     . GLU A 166 ? 0.9185 1.0449 0.8783 0.0648  0.1951  -0.0760 166 GLU A O     
1371 C  CB    . GLU A 166 ? 0.9812 1.0896 0.9775 0.0687  0.1849  -0.0846 166 GLU A CB    
1372 C  CG    . GLU A 166 ? 1.1479 1.2412 1.1527 0.0707  0.1795  -0.0927 166 GLU A CG    
1373 C  CD    . GLU A 166 ? 1.4183 1.4881 1.3965 0.0723  0.1790  -0.1095 166 GLU A CD    
1374 O  OE1   . GLU A 166 ? 1.5218 1.5865 1.4749 0.0754  0.1871  -0.1167 166 GLU A OE1   
1375 O  OE2   . GLU A 166 ? 1.4692 1.5257 1.4515 0.0702  0.1701  -0.1155 166 GLU A OE2   
1376 N  N     . GLY A 167 ? 0.8737 1.0023 0.8510 0.0486  0.1698  -0.0675 167 GLY A N     
1377 C  CA    . GLY A 167 ? 0.8335 0.9786 0.8127 0.0452  0.1726  -0.0552 167 GLY A CA    
1378 C  C     . GLY A 167 ? 0.7884 0.9475 0.7978 0.0398  0.1663  -0.0422 167 GLY A C     
1379 O  O     . GLY A 167 ? 0.7571 0.9125 0.7826 0.0375  0.1576  -0.0431 167 GLY A O     
1380 N  N     . ALA A 168 ? 0.6977 0.8731 0.7147 0.0376  0.1706  -0.0297 168 ALA A N     
1381 C  CA    . ALA A 168 ? 0.7181 0.9071 0.7628 0.0314  0.1644  -0.0170 168 ALA A CA    
1382 C  C     . ALA A 168 ? 0.6963 0.9038 0.7623 0.0369  0.1769  -0.0061 168 ALA A C     
1383 O  O     . ALA A 168 ? 0.7053 0.9191 0.7616 0.0430  0.1905  -0.0043 168 ALA A O     
1384 C  CB    . ALA A 168 ? 0.6633 0.8551 0.7022 0.0221  0.1562  -0.0100 168 ALA A CB    
1385 N  N     . ARG A 169 ? 0.6235 0.8403 0.7186 0.0345  0.1723  0.0013  169 ARG A N     
1386 C  CA    . ARG A 169 ? 0.6911 0.9272 0.8113 0.0388  0.1824  0.0129  169 ARG A CA    
1387 C  C     . ARG A 169 ? 0.6009 0.8492 0.7478 0.0296  0.1721  0.0248  169 ARG A C     
1388 O  O     . ARG A 169 ? 0.5994 0.8400 0.7503 0.0230  0.1581  0.0217  169 ARG A O     
1389 C  CB    . ARG A 169 ? 0.7248 0.9600 0.8557 0.0487  0.1900  0.0085  169 ARG A CB    
1390 C  CG    . ARG A 169 ? 0.7089 0.9328 0.8159 0.0589  0.2027  -0.0029 169 ARG A CG    
1391 C  CD    . ARG A 169 ? 0.7841 1.0138 0.9081 0.0702  0.2152  -0.0022 169 ARG A CD    
1392 N  NE    . ARG A 169 ? 0.6419 0.8935 0.7842 0.0742  0.2280  0.0115  169 ARG A NE    
1393 C  CZ    . ARG A 169 ? 0.7182 0.9750 0.8458 0.0796  0.2423  0.0130  169 ARG A CZ    
1394 N  NH1   . ARG A 169 ? 0.7000 0.9415 0.7929 0.0814  0.2453  0.0011  169 ARG A NH1   
1395 N  NH2   . ARG A 169 ? 0.7250 1.0035 0.8733 0.0831  0.2538  0.0271  169 ARG A NH2   
1396 N  N     . VAL A 170 ? 0.6045 0.8718 0.7695 0.0293  0.1794  0.0384  170 VAL A N     
1397 C  CA    . VAL A 170 ? 0.6003 0.8809 0.7930 0.0206  0.1709  0.0505  170 VAL A CA    
1398 C  C     . VAL A 170 ? 0.6714 0.9684 0.8931 0.0258  0.1774  0.0587  170 VAL A C     
1399 O  O     . VAL A 170 ? 0.5917 0.8958 0.8140 0.0358  0.1927  0.0601  170 VAL A O     
1400 C  CB    . VAL A 170 ? 0.6378 0.9279 0.8309 0.0144  0.1726  0.0615  170 VAL A CB    
1401 C  CG1   . VAL A 170 ? 0.5742 0.8764 0.7965 0.0046  0.1631  0.0735  170 VAL A CG1   
1402 C  CG2   . VAL A 170 ? 0.6218 0.8962 0.7863 0.0101  0.1666  0.0543  170 VAL A CG2   
1403 N  N     . ILE A 171 ? 0.6446 0.9478 0.8900 0.0193  0.1659  0.0638  171 ILE A N     
1404 C  CA    . ILE A 171 ? 0.5456 0.8672 0.8225 0.0221  0.1694  0.0740  171 ILE A CA    
1405 C  C     . ILE A 171 ? 0.6780 1.0146 0.9784 0.0113  0.1618  0.0876  171 ILE A C     
1406 O  O     . ILE A 171 ? 0.7038 1.0329 1.0031 0.0010  0.1468  0.0856  171 ILE A O     
1407 C  CB    . ILE A 171 ? 0.5711 0.8868 0.8559 0.0242  0.1616  0.0679  171 ILE A CB    
1408 C  CG1   . ILE A 171 ? 0.5940 0.8920 0.8554 0.0338  0.1678  0.0538  171 ILE A CG1   
1409 C  CG2   . ILE A 171 ? 0.6141 0.9505 0.9325 0.0274  0.1651  0.0798  171 ILE A CG2   
1410 C  CD1   . ILE A 171 ? 0.5526 0.8394 0.8149 0.0333  0.1568  0.0461  171 ILE A CD1   
1411 N  N     . THR A 172 ? 0.6391 0.9966 0.9613 0.0136  0.1721  0.1013  172 THR A N     
1412 C  CA    . THR A 172 ? 0.6404 1.0127 0.9867 0.0027  0.1650  0.1150  172 THR A CA    
1413 C  C     . THR A 172 ? 0.6598 1.0569 1.0399 0.0063  0.1729  0.1295  172 THR A C     
1414 O  O     . THR A 172 ? 0.6384 1.0424 1.0207 0.0183  0.1879  0.1305  172 THR A O     
1415 C  CB    . THR A 172 ? 0.6002 0.9718 0.9343 -0.0018 0.1687  0.1195  172 THR A CB    
1416 O  OG1   . THR A 172 ? 0.6926 1.0775 1.0522 -0.0129 0.1614  0.1330  172 THR A OG1   
1417 C  CG2   . THR A 172 ? 0.6245 1.0046 0.9505 0.0089  0.1888  0.1235  172 THR A CG2   
1418 N  N     . TRP A 173 ? 0.6040 1.0144 1.0115 -0.0044 0.1624  0.1408  173 TRP A N     
1419 C  CA    . TRP A 173 ? 0.6974 1.1333 1.1410 -0.0031 0.1673  0.1563  173 TRP A CA    
1420 C  C     . TRP A 173 ? 0.7288 1.1822 1.1885 -0.0072 0.1750  0.1720  173 TRP A C     
1421 O  O     . TRP A 173 ? 0.6039 1.0784 1.0974 -0.0120 0.1730  0.1867  173 TRP A O     
1422 C  CB    . TRP A 173 ? 0.6765 1.1178 1.1432 -0.0119 0.1499  0.1591  173 TRP A CB    
1423 C  CG    . TRP A 173 ? 0.6974 1.1292 1.1616 -0.0271 0.1316  0.1569  173 TRP A CG    
1424 C  CD1   . TRP A 173 ? 0.6732 1.0813 1.1094 -0.0314 0.1219  0.1428  173 TRP A CD1   
1425 C  CD2   . TRP A 173 ? 0.7175 1.1629 1.2093 -0.0399 0.1208  0.1689  173 TRP A CD2   
1426 N  NE1   . TRP A 173 ? 0.6828 1.0882 1.1267 -0.0453 0.1066  0.1449  173 TRP A NE1   
1427 C  CE2   . TRP A 173 ? 0.7190 1.1463 1.1963 -0.0511 0.1052  0.1603  173 TRP A CE2   
1428 C  CE3   . TRP A 173 ? 0.6366 1.1077 1.1647 -0.0431 0.1227  0.1861  173 TRP A CE3   
1429 C  CZ2   . TRP A 173 ? 0.7380 1.1703 1.2344 -0.0653 0.0916  0.1674  173 TRP A CZ2   
1430 C  CZ3   . TRP A 173 ? 0.6116 1.0886 1.1595 -0.0580 0.1083  0.1938  173 TRP A CZ3   
1431 C  CH2   . TRP A 173 ? 0.7080 1.1649 1.2394 -0.0690 0.0930  0.1838  173 TRP A CH2   
1432 N  N     . LYS A 174 ? 0.7189 1.1645 1.1554 -0.0056 0.1835  0.1699  174 LYS A N     
1433 C  CA    . LYS A 174 ? 0.7435 1.2062 1.1909 -0.0053 0.1962  0.1848  174 LYS A CA    
1434 C  C     . LYS A 174 ? 0.7274 1.1847 1.1463 0.0074  0.2148  0.1792  174 LYS A C     
1435 O  O     . LYS A 174 ? 0.8127 1.2486 1.1988 0.0114  0.2137  0.1631  174 LYS A O     
1436 C  CB    . LYS A 174 ? 0.7418 1.2019 1.1915 -0.0193 0.1859  0.1910  174 LYS A CB    
1437 C  CG    . LYS A 174 ? 0.7623 1.2349 1.2473 -0.0321 0.1717  0.2021  174 LYS A CG    
1438 C  CD    . LYS A 174 ? 0.8643 1.3554 1.3727 -0.0387 0.1766  0.2209  174 LYS A CD    
1439 C  CE    . LYS A 174 ? 0.9739 1.4850 1.5242 -0.0473 0.1676  0.2342  174 LYS A CE    
1440 N  NZ    . LYS A 174 ? 0.9579 1.4845 1.5325 -0.0565 0.1691  0.2523  174 LYS A NZ    
1441 N  N     . ASN A 175 ? 0.6899 1.1670 1.1213 0.0136  0.2320  0.1926  175 ASN A N     
1442 C  CA    . ASN A 175 ? 0.7609 1.2354 1.1669 0.0271  0.2516  0.1878  175 ASN A CA    
1443 C  C     . ASN A 175 ? 0.7744 1.2350 1.1477 0.0235  0.2515  0.1830  175 ASN A C     
1444 O  O     . ASN A 175 ? 0.7785 1.2474 1.1606 0.0148  0.2493  0.1952  175 ASN A O     
1445 C  CB    . ASN A 175 ? 0.7654 1.2669 1.1961 0.0349  0.2706  0.2048  175 ASN A CB    
1446 C  CG    . ASN A 175 ? 0.8531 1.3533 1.2560 0.0479  0.2919  0.2014  175 ASN A CG    
1447 O  OD1   . ASN A 175 ? 0.9871 1.4664 1.3550 0.0546  0.2942  0.1841  175 ASN A OD1   
1448 N  ND2   . ASN A 175 ? 0.9458 1.4684 1.3638 0.0513  0.3077  0.2182  175 ASN A ND2   
1449 N  N     . VAL A 176 ? 0.7686 1.2080 1.1051 0.0299  0.2532  0.1656  176 VAL A N     
1450 C  CA    . VAL A 176 ? 0.7351 1.1621 1.0372 0.0291  0.2554  0.1603  176 VAL A CA    
1451 C  C     . VAL A 176 ? 0.7921 1.2135 1.0658 0.0436  0.2728  0.1503  176 VAL A C     
1452 O  O     . VAL A 176 ? 0.8514 1.2626 1.1186 0.0514  0.2741  0.1377  176 VAL A O     
1453 C  CB    . VAL A 176 ? 0.7147 1.1182 0.9973 0.0200  0.2363  0.1474  176 VAL A CB    
1454 C  CG1   . VAL A 176 ? 0.7577 1.1501 1.0061 0.0194  0.2386  0.1433  176 VAL A CG1   
1455 C  CG2   . VAL A 176 ? 0.6384 1.0457 0.9481 0.0060  0.2193  0.1556  176 VAL A CG2   
1456 N  N     . ASP A 177 ? 0.8287 1.2563 1.0852 0.0474  0.2862  0.1561  177 ASP A N     
1457 C  CA    . ASP A 177 ? 0.9386 1.3617 1.1663 0.0613  0.3041  0.1470  177 ASP A CA    
1458 C  C     . ASP A 177 ? 0.8607 1.2592 1.0457 0.0599  0.2970  0.1302  177 ASP A C     
1459 O  O     . ASP A 177 ? 0.8684 1.2662 1.0320 0.0570  0.2989  0.1334  177 ASP A O     
1460 C  CB    . ASP A 177 ? 0.8776 1.3221 1.1088 0.0668  0.3236  0.1625  177 ASP A CB    
1461 C  CG    . ASP A 177 ? 1.0179 1.4611 1.2264 0.0830  0.3446  0.1541  177 ASP A CG    
1462 O  OD1   . ASP A 177 ? 1.1812 1.6156 1.3905 0.0911  0.3469  0.1422  177 ASP A OD1   
1463 O  OD2   . ASP A 177 ? 1.1127 1.5634 1.3024 0.0877  0.3590  0.1595  177 ASP A OD2   
1464 N  N     . LEU A 178 ? 0.8951 1.2740 1.0686 0.0618  0.2885  0.1129  178 LEU A N     
1465 C  CA    . LEU A 178 ? 0.9137 1.2688 1.0488 0.0607  0.2810  0.0961  178 LEU A CA    
1466 C  C     . LEU A 178 ? 1.0282 1.3678 1.1511 0.0704  0.2844  0.0787  178 LEU A C     
1467 O  O     . LEU A 178 ? 0.9394 1.2843 1.0880 0.0744  0.2858  0.0798  178 LEU A O     
1468 C  CB    . LEU A 178 ? 0.8354 1.1795 0.9725 0.0472  0.2592  0.0945  178 LEU A CB    
1469 C  CG    . LEU A 178 ? 0.8133 1.1643 0.9489 0.0377  0.2547  0.1070  178 LEU A CG    
1470 C  CD1   . LEU A 178 ? 0.7578 1.0962 0.8969 0.0255  0.2338  0.1040  178 LEU A CD1   
1471 C  CD2   . LEU A 178 ? 0.7537 1.1009 0.8527 0.0421  0.2643  0.1040  178 LEU A CD2   
1472 N  N     . PRO A 179 ? 0.9099 1.2307 0.9949 0.0742  0.2855  0.0630  179 PRO A N     
1473 C  CA    . PRO A 179 ? 0.8936 1.1984 0.9668 0.0836  0.2897  0.0461  179 PRO A CA    
1474 C  C     . PRO A 179 ? 0.8758 1.1658 0.9585 0.0783  0.2724  0.0370  179 PRO A C     
1475 O  O     . PRO A 179 ? 0.9956 1.2743 1.0764 0.0859  0.2755  0.0256  179 PRO A O     
1476 C  CB    . PRO A 179 ? 0.9040 1.1935 0.9324 0.0872  0.2947  0.0330  179 PRO A CB    
1477 C  CG    . PRO A 179 ? 0.9254 1.2171 0.9426 0.0761  0.2844  0.0401  179 PRO A CG    
1478 C  CD    . PRO A 179 ? 0.8127 1.1275 0.8642 0.0707  0.2849  0.0610  179 PRO A CD    
1479 N  N     . TYR A 180 ? 0.7477 1.0370 0.8405 0.0660  0.2550  0.0417  180 TYR A N     
1480 C  CA    . TYR A 180 ? 0.7371 1.0126 0.8367 0.0608  0.2388  0.0333  180 TYR A CA    
1481 C  C     . TYR A 180 ? 0.7450 1.0338 0.8823 0.0545  0.2300  0.0451  180 TYR A C     
1482 O  O     . TYR A 180 ? 0.6897 0.9689 0.8329 0.0481  0.2148  0.0404  180 TYR A O     
1483 C  CB    . TYR A 180 ? 0.7189 0.9778 0.7937 0.0521  0.2243  0.0252  180 TYR A CB    
1484 C  CG    . TYR A 180 ? 0.7330 1.0009 0.8075 0.0430  0.2196  0.0370  180 TYR A CG    
1485 C  CD1   . TYR A 180 ? 0.7020 0.9771 0.8016 0.0332  0.2077  0.0471  180 TYR A CD1   
1486 C  CD2   . TYR A 180 ? 0.7644 1.0330 0.8129 0.0442  0.2269  0.0379  180 TYR A CD2   
1487 C  CE1   . TYR A 180 ? 0.7366 1.0185 0.8372 0.0250  0.2035  0.0579  180 TYR A CE1   
1488 C  CE2   . TYR A 180 ? 0.8052 1.0820 0.8546 0.0361  0.2227  0.0498  180 TYR A CE2   
1489 C  CZ    . TYR A 180 ? 0.7855 1.0684 0.8617 0.0266  0.2111  0.0598  180 TYR A CZ    
1490 O  OH    . TYR A 180 ? 0.7706 1.0605 0.8491 0.0187  0.2070  0.0717  180 TYR A OH    
1491 N  N     . VAL A 181 ? 0.7370 1.0477 0.8997 0.0559  0.2389  0.0604  181 VAL A N     
1492 C  CA    . VAL A 181 ? 0.7154 1.0400 0.9145 0.0493  0.2303  0.0722  181 VAL A CA    
1493 C  C     . VAL A 181 ? 0.7423 1.0774 0.9650 0.0588  0.2399  0.0752  181 VAL A C     
1494 O  O     . VAL A 181 ? 0.7304 1.0731 0.9511 0.0697  0.2577  0.0770  181 VAL A O     
1495 C  CB    . VAL A 181 ? 0.7733 1.1162 0.9885 0.0417  0.2308  0.0894  181 VAL A CB    
1496 C  CG1   . VAL A 181 ? 0.7936 1.1494 1.0026 0.0500  0.2505  0.0967  181 VAL A CG1   
1497 C  CG2   . VAL A 181 ? 0.7115 1.0705 0.9661 0.0359  0.2238  0.1018  181 VAL A CG2   
1498 N  N     . ASP A 182 ? 0.6935 1.0291 0.9380 0.0551  0.2282  0.0757  182 ASP A N     
1499 C  CA    . ASP A 182 ? 0.6836 1.0313 0.9560 0.0624  0.2341  0.0812  182 ASP A CA    
1500 C  C     . ASP A 182 ? 0.6336 1.0021 0.9417 0.0535  0.2260  0.0976  182 ASP A C     
1501 O  O     . ASP A 182 ? 0.5767 0.9408 0.8899 0.0422  0.2085  0.0974  182 ASP A O     
1502 C  CB    . ASP A 182 ? 0.6967 1.0278 0.9645 0.0658  0.2269  0.0684  182 ASP A CB    
1503 C  CG    . ASP A 182 ? 0.7890 1.0985 1.0226 0.0738  0.2341  0.0516  182 ASP A CG    
1504 O  OD1   . ASP A 182 ? 0.7423 1.0529 0.9595 0.0805  0.2489  0.0505  182 ASP A OD1   
1505 O  OD2   . ASP A 182 ? 0.8464 1.1378 1.0690 0.0731  0.2247  0.0397  182 ASP A OD2   
1506 N  N     . VAL A 183 ? 0.6992 1.0901 1.0319 0.0586  0.2386  0.1116  183 VAL A N     
1507 C  CA    . VAL A 183 ? 0.6268 1.0398 0.9953 0.0501  0.2323  0.1288  183 VAL A CA    
1508 C  C     . VAL A 183 ? 0.6122 1.0347 1.0097 0.0532  0.2285  0.1327  183 VAL A C     
1509 O  O     . VAL A 183 ? 0.6357 1.0613 1.0382 0.0660  0.2417  0.1316  183 VAL A O     
1510 C  CB    . VAL A 183 ? 0.6660 1.1004 1.0472 0.0530  0.2480  0.1440  183 VAL A CB    
1511 C  CG1   . VAL A 183 ? 0.6266 1.0811 1.0418 0.0410  0.2385  0.1612  183 VAL A CG1   
1512 C  CG2   . VAL A 183 ? 0.6422 1.0663 0.9898 0.0537  0.2554  0.1387  183 VAL A CG2   
1513 N  N     . VAL A 184 ? 0.6004 1.0269 1.0163 0.0416  0.2105  0.1373  184 VAL A N     
1514 C  CA    . VAL A 184 ? 0.6435 1.0824 1.0896 0.0425  0.2047  0.1438  184 VAL A CA    
1515 C  C     . VAL A 184 ? 0.6552 1.1187 1.1363 0.0329  0.1989  0.1621  184 VAL A C     
1516 O  O     . VAL A 184 ? 0.6877 1.1576 1.1693 0.0267  0.2010  0.1693  184 VAL A O     
1517 C  CB    . VAL A 184 ? 0.6001 1.0215 1.0362 0.0375  0.1872  0.1322  184 VAL A CB    
1518 C  CG1   . VAL A 184 ? 0.5867 0.9840 0.9901 0.0465  0.1929  0.1148  184 VAL A CG1   
1519 C  CG2   . VAL A 184 ? 0.6105 1.0251 1.0403 0.0219  0.1693  0.1308  184 VAL A CG2   
1520 N  N     . SER A 185 ? 0.6139 1.0914 1.1248 0.0311  0.1910  0.1701  185 SER A N     
1521 C  CA    . SER A 185 ? 0.8397 1.3427 1.3872 0.0225  0.1857  0.1883  185 SER A CA    
1522 C  C     . SER A 185 ? 0.6987 1.1965 1.2473 0.0050  0.1637  0.1877  185 SER A C     
1523 O  O     . SER A 185 ? 0.6256 1.1330 1.1858 -0.0047 0.1608  0.1973  185 SER A O     
1524 C  CB    . SER A 185 ? 0.7656 1.2884 1.3466 0.0288  0.1876  0.1987  185 SER A CB    
1525 O  OG    . SER A 185 ? 0.9446 1.4614 1.5288 0.0227  0.1692  0.1940  185 SER A OG    
1526 N  N     . THR A 186 ? 0.6358 1.1185 1.1729 0.0008  0.1484  0.1767  186 THR A N     
1527 C  CA    . THR A 186 ? 0.6113 1.0886 1.1493 -0.0150 0.1274  0.1750  186 THR A CA    
1528 C  C     . THR A 186 ? 0.7092 1.1575 1.2103 -0.0168 0.1194  0.1565  186 THR A C     
1529 O  O     . THR A 186 ? 0.6836 1.1172 1.1606 -0.0066 0.1289  0.1456  186 THR A O     
1530 C  CB    . THR A 186 ? 0.7243 1.2164 1.2903 -0.0201 0.1139  0.1826  186 THR A CB    
1531 O  OG1   . THR A 186 ? 0.5448 1.0253 1.0983 -0.0132 0.1106  0.1723  186 THR A OG1   
1532 C  CG2   . THR A 186 ? 0.5862 1.1082 1.1904 -0.0157 0.1233  0.2012  186 THR A CG2   
1533 N  N     . GLU A 187 ? 0.6797 1.1200 1.1774 -0.0303 0.1018  0.1532  187 GLU A N     
1534 C  CA    . GLU A 187 ? 0.6204 1.0349 1.0867 -0.0328 0.0926  0.1368  187 GLU A CA    
1535 C  C     . GLU A 187 ? 0.6737 1.0823 1.1349 -0.0265 0.0887  0.1293  187 GLU A C     
1536 O  O     . GLU A 187 ? 0.6843 1.0731 1.1185 -0.0213 0.0901  0.1161  187 GLU A O     
1537 C  CB    . GLU A 187 ? 0.5990 1.0077 1.0658 -0.0482 0.0753  0.1358  187 GLU A CB    
1538 C  CG    . GLU A 187 ? 0.8063 1.1947 1.2514 -0.0521 0.0616  0.1217  187 GLU A CG    
1539 C  CD    . GLU A 187 ? 0.8896 1.2708 1.3340 -0.0667 0.0460  0.1199  187 GLU A CD    
1540 O  OE1   . GLU A 187 ? 0.7260 1.1211 1.1942 -0.0756 0.0361  0.1285  187 GLU A OE1   
1541 O  OE2   . GLU A 187 ? 0.7691 1.1304 1.1894 -0.0693 0.0434  0.1097  187 GLU A OE2   
1542 N  N     . ARG A 188 ? 0.6729 1.0990 1.1606 -0.0270 0.0833  0.1386  188 ARG A N     
1543 C  CA    . ARG A 188 ? 0.7483 1.1716 1.2349 -0.0203 0.0804  0.1342  188 ARG A CA    
1544 C  C     . ARG A 188 ? 0.6578 1.0737 1.1320 -0.0049 0.0976  0.1286  188 ARG A C     
1545 O  O     . ARG A 188 ? 0.6452 1.0437 1.0991 0.0000  0.0965  0.1170  188 ARG A O     
1546 C  CB    . ARG A 188 ? 0.7954 1.2431 1.3167 -0.0224 0.0742  0.1483  188 ARG A CB    
1547 C  CG    . ARG A 188 ? 0.8228 1.2677 1.3436 -0.0277 0.0571  0.1450  188 ARG A CG    
1548 C  CD    . ARG A 188 ? 0.7527 1.2232 1.3081 -0.0276 0.0529  0.1600  188 ARG A CD    
1549 N  NE    . ARG A 188 ? 0.7869 1.2545 1.3393 -0.0261 0.0428  0.1569  188 ARG A NE    
1550 C  CZ    . ARG A 188 ? 0.7072 1.1760 1.2635 -0.0134 0.0513  0.1578  188 ARG A CZ    
1551 N  NH1   . ARG A 188 ? 0.6298 1.1015 1.1918 -0.0006 0.0703  0.1604  188 ARG A NH1   
1552 N  NH2   . ARG A 188 ? 0.5965 1.0631 1.1505 -0.0134 0.0407  0.1561  188 ARG A NH2   
1553 N  N     . GLU A 189 ? 0.6294 1.0580 1.1158 0.0029  0.1140  0.1368  189 GLU A N     
1554 C  CA    . GLU A 189 ? 0.6757 1.0967 1.1499 0.0178  0.1314  0.1310  189 GLU A CA    
1555 C  C     . GLU A 189 ? 0.6182 1.0139 1.0547 0.0188  0.1341  0.1154  189 GLU A C     
1556 O  O     . GLU A 189 ? 0.5959 0.9766 1.0147 0.0280  0.1405  0.1048  189 GLU A O     
1557 C  CB    . GLU A 189 ? 0.6741 1.1147 1.1682 0.0255  0.1489  0.1431  189 GLU A CB    
1558 C  CG    . GLU A 189 ? 0.7944 1.2419 1.3016 0.0406  0.1624  0.1460  189 GLU A CG    
1559 C  CD    . GLU A 189 ? 0.9803 1.4393 1.5126 0.0396  0.1515  0.1531  189 GLU A CD    
1560 O  OE1   . GLU A 189 ? 1.0750 1.5487 1.6274 0.0281  0.1375  0.1628  189 GLU A OE1   
1561 O  OE2   . GLU A 189 ? 0.9737 1.4271 1.5058 0.0503  0.1568  0.1492  189 GLU A OE2   
1562 N  N     . MET A 190 ? 0.5818 0.9724 1.0068 0.0091  0.1289  0.1140  190 MET A N     
1563 C  CA    . MET A 190 ? 0.6303 0.9981 1.0208 0.0092  0.1302  0.1004  190 MET A CA    
1564 C  C     . MET A 190 ? 0.5698 0.9184 0.9425 0.0070  0.1180  0.0878  190 MET A C     
1565 O  O     . MET A 190 ? 0.5590 0.8902 0.9081 0.0135  0.1227  0.0761  190 MET A O     
1566 C  CB    . MET A 190 ? 0.5835 0.9513 0.9692 -0.0012 0.1261  0.1037  190 MET A CB    
1567 C  CG    . MET A 190 ? 0.5823 0.9271 0.9348 -0.0037 0.1229  0.0906  190 MET A CG    
1568 S  SD    . MET A 190 ? 0.4710 0.8150 0.8215 -0.0168 0.1154  0.0953  190 MET A SD    
1569 C  CE    . MET A 190 ? 0.5119 0.8600 0.8822 -0.0291 0.0956  0.0984  190 MET A CE    
1570 N  N     . ILE A 191 ? 0.5483 0.9000 0.9317 -0.0023 0.1021  0.0901  191 ILE A N     
1571 C  CA    . ILE A 191 ? 0.5875 0.9227 0.9550 -0.0044 0.0908  0.0794  191 ILE A CA    
1572 C  C     . ILE A 191 ? 0.5963 0.9293 0.9655 0.0067  0.0964  0.0765  191 ILE A C     
1573 O  O     . ILE A 191 ? 0.5544 0.8692 0.9027 0.0103  0.0959  0.0651  191 ILE A O     
1574 C  CB    . ILE A 191 ? 0.5728 0.9133 0.9517 -0.0164 0.0733  0.0830  191 ILE A CB    
1575 C  CG1   . ILE A 191 ? 0.6002 0.9377 0.9743 -0.0273 0.0675  0.0836  191 ILE A CG1   
1576 C  CG2   . ILE A 191 ? 0.6120 0.9380 0.9761 -0.0173 0.0628  0.0733  191 ILE A CG2   
1577 C  CD1   . ILE A 191 ? 0.6294 0.9720 1.0154 -0.0397 0.0508  0.0870  191 ILE A CD1   
1578 N  N     . LYS A 192 ? 0.5644 0.9161 0.9601 0.0122  0.1021  0.0874  192 LYS A N     
1579 C  CA    . LYS A 192 ? 0.5881 0.9380 0.9881 0.0235  0.1085  0.0858  192 LYS A CA    
1580 C  C     . LYS A 192 ? 0.5765 0.9115 0.9562 0.0343  0.1238  0.0761  192 LYS A C     
1581 O  O     . LYS A 192 ? 0.5323 0.8529 0.9007 0.0409  0.1254  0.0675  192 LYS A O     
1582 C  CB    . LYS A 192 ? 0.6530 1.0274 1.0876 0.0279  0.1127  0.1008  192 LYS A CB    
1583 C  CG    . LYS A 192 ? 0.6286 1.0157 1.0825 0.0195  0.0962  0.1089  192 LYS A CG    
1584 C  CD    . LYS A 192 ? 0.7355 1.1500 1.2260 0.0220  0.0996  0.1258  192 LYS A CD    
1585 C  CE    . LYS A 192 ? 0.7710 1.1910 1.2701 0.0362  0.1204  0.1292  192 LYS A CE    
1586 N  NZ    . LYS A 192 ? 0.7287 1.1698 1.2614 0.0433  0.1239  0.1430  192 LYS A NZ    
1587 N  N     . ARG A 193 ? 0.5234 0.8613 0.8978 0.0359  0.1349  0.0774  193 ARG A N     
1588 C  CA    . ARG A 193 ? 0.5653 0.8888 0.9176 0.0456  0.1491  0.0675  193 ARG A CA    
1589 C  C     . ARG A 193 ? 0.5785 0.8779 0.8989 0.0416  0.1419  0.0528  193 ARG A C     
1590 O  O     . ARG A 193 ? 0.6157 0.8990 0.9190 0.0490  0.1478  0.0422  193 ARG A O     
1591 C  CB    . ARG A 193 ? 0.5540 0.8877 0.9068 0.0477  0.1622  0.0732  193 ARG A CB    
1592 C  CG    . ARG A 193 ? 0.6201 0.9427 0.9537 0.0597  0.1792  0.0645  193 ARG A CG    
1593 C  CD    . ARG A 193 ? 0.7581 1.0819 1.0762 0.0584  0.1877  0.0650  193 ARG A CD    
1594 N  NE    . ARG A 193 ? 0.8108 1.1253 1.1099 0.0702  0.2045  0.0567  193 ARG A NE    
1595 C  CZ    . ARG A 193 ? 0.7780 1.1029 1.0904 0.0819  0.2208  0.0616  193 ARG A CZ    
1596 N  NH1   . ARG A 193 ? 0.6608 1.0075 1.0077 0.0836  0.2228  0.0759  193 ARG A NH1   
1597 N  NH2   . ARG A 193 ? 0.8457 1.1589 1.1364 0.0922  0.2354  0.0518  193 ARG A NH2   
1598 N  N     . PHE A 194 ? 0.5201 0.8164 0.8330 0.0299  0.1293  0.0521  194 PHE A N     
1599 C  CA    . PHE A 194 ? 0.6247 0.8995 0.9102 0.0260  0.1218  0.0394  194 PHE A CA    
1600 C  C     . PHE A 194 ? 0.6179 0.8827 0.9022 0.0283  0.1148  0.0334  194 PHE A C     
1601 O  O     . PHE A 194 ? 0.6036 0.8502 0.8674 0.0315  0.1156  0.0222  194 PHE A O     
1602 C  CB    . PHE A 194 ? 0.5673 0.8414 0.8483 0.0135  0.1097  0.0408  194 PHE A CB    
1603 C  CG    . PHE A 194 ? 0.5988 0.8525 0.8548 0.0094  0.1013  0.0290  194 PHE A CG    
1604 C  CD1   . PHE A 194 ? 0.6184 0.8576 0.8501 0.0135  0.1080  0.0198  194 PHE A CD1   
1605 C  CD2   . PHE A 194 ? 0.5966 0.8460 0.8531 0.0017  0.0870  0.0274  194 PHE A CD2   
1606 C  CE1   . PHE A 194 ? 0.6290 0.8510 0.8399 0.0097  0.1001  0.0101  194 PHE A CE1   
1607 C  CE2   . PHE A 194 ? 0.5916 0.8234 0.8267 -0.0015 0.0802  0.0175  194 PHE A CE2   
1608 C  CZ    . PHE A 194 ? 0.6219 0.8404 0.8354 0.0024  0.0866  0.0093  194 PHE A CZ    
1609 N  N     . LEU A 195 ? 0.6061 0.8831 0.9126 0.0264  0.1075  0.0415  195 LEU A N     
1610 C  CA    . LEU A 195 ? 0.5581 0.8281 0.8659 0.0293  0.1017  0.0380  195 LEU A CA    
1611 C  C     . LEU A 195 ? 0.6465 0.9090 0.9525 0.0419  0.1144  0.0336  195 LEU A C     
1612 O  O     . LEU A 195 ? 0.6522 0.8985 0.9454 0.0447  0.1124  0.0248  195 LEU A O     
1613 C  CB    . LEU A 195 ? 0.6013 0.8888 0.9348 0.0257  0.0926  0.0492  195 LEU A CB    
1614 C  CG    . LEU A 195 ? 0.8213 1.1076 1.1509 0.0140  0.0757  0.0487  195 LEU A CG    
1615 C  CD1   . LEU A 195 ? 0.7779 1.0561 1.0902 0.0061  0.0731  0.0436  195 LEU A CD1   
1616 C  CD2   . LEU A 195 ? 0.7501 1.0574 1.1058 0.0089  0.0677  0.0613  195 LEU A CD2   
1617 N  N     . ARG A 196 ? 0.6265 0.9006 0.9461 0.0496  0.1278  0.0397  196 ARG A N     
1618 C  CA    . ARG A 196 ? 0.6883 0.9545 1.0063 0.0624  0.1413  0.0349  196 ARG A CA    
1619 C  C     . ARG A 196 ? 0.6388 0.8831 0.9255 0.0645  0.1467  0.0203  196 ARG A C     
1620 O  O     . ARG A 196 ? 0.6487 0.8772 0.9261 0.0712  0.1505  0.0115  196 ARG A O     
1621 C  CB    . ARG A 196 ? 0.6406 0.9249 0.9798 0.0704  0.1554  0.0450  196 ARG A CB    
1622 C  CG    . ARG A 196 ? 0.7302 1.0187 1.0898 0.0817  0.1628  0.0493  196 ARG A CG    
1623 C  CD    . ARG A 196 ? 0.8126 1.1186 1.1921 0.0906  0.1787  0.0588  196 ARG A CD    
1624 N  NE    . ARG A 196 ? 1.0201 1.3124 1.3819 0.1013  0.1956  0.0488  196 ARG A NE    
1625 C  CZ    . ARG A 196 ? 1.0861 1.3819 1.4377 0.1029  0.2068  0.0482  196 ARG A CZ    
1626 N  NH1   . ARG A 196 ? 0.9144 1.2270 1.2733 0.0946  0.2033  0.0577  196 ARG A NH1   
1627 N  NH2   . ARG A 196 ? 1.1342 1.4161 1.4673 0.1130  0.2218  0.0378  196 ARG A NH2   
1628 N  N     . VAL A 197 ? 0.6442 0.8873 0.9149 0.0587  0.1468  0.0181  197 VAL A N     
1629 C  CA    . VAL A 197 ? 0.7036 0.9270 0.9436 0.0593  0.1500  0.0049  197 VAL A CA    
1630 C  C     . VAL A 197 ? 0.6513 0.8569 0.8772 0.0548  0.1379  -0.0043 197 VAL A C     
1631 O  O     . VAL A 197 ? 0.6462 0.8341 0.8556 0.0593  0.1411  -0.0153 197 VAL A O     
1632 C  CB    . VAL A 197 ? 0.6762 0.9037 0.9038 0.0529  0.1505  0.0064  197 VAL A CB    
1633 C  CG1   . VAL A 197 ? 0.6389 0.8473 0.8347 0.0537  0.1534  -0.0065 197 VAL A CG1   
1634 C  CG2   . VAL A 197 ? 0.6312 0.8771 0.8735 0.0577  0.1634  0.0165  197 VAL A CG2   
1635 N  N     . VAL A 198 ? 0.5942 0.8042 0.8267 0.0456  0.1239  0.0000  198 VAL A N     
1636 C  CA    . VAL A 198 ? 0.6933 0.8880 0.9135 0.0414  0.1129  -0.0077 198 VAL A CA    
1637 C  C     . VAL A 198 ? 0.7172 0.9057 0.9458 0.0487  0.1145  -0.0095 198 VAL A C     
1638 O  O     . VAL A 198 ? 0.6576 0.8284 0.8715 0.0503  0.1133  -0.0192 198 VAL A O     
1639 C  CB    . VAL A 198 ? 0.6495 0.8509 0.8751 0.0308  0.0987  -0.0025 198 VAL A CB    
1640 C  CG1   . VAL A 198 ? 0.6145 0.8015 0.8286 0.0274  0.0886  -0.0095 198 VAL A CG1   
1641 C  CG2   . VAL A 198 ? 0.6166 0.8214 0.8335 0.0236  0.0972  -0.0012 198 VAL A CG2   
1642 N  N     . LYS A 199 ? 0.6759 0.8791 0.9294 0.0532  0.1171  0.0003  199 LYS A N     
1643 C  CA    . LYS A 199 ? 0.6603 0.8589 0.9247 0.0603  0.1185  0.0005  199 LYS A CA    
1644 C  C     . LYS A 199 ? 0.6636 0.8473 0.9183 0.0705  0.1315  -0.0088 199 LYS A C     
1645 O  O     . LYS A 199 ? 0.7171 0.8860 0.9681 0.0741  0.1307  -0.0148 199 LYS A O     
1646 C  CB    . LYS A 199 ? 0.6993 0.9190 0.9940 0.0632  0.1189  0.0144  199 LYS A CB    
1647 C  CG    . LYS A 199 ? 0.7269 0.9465 1.0350 0.0652  0.1123  0.0185  199 LYS A CG    
1648 C  CD    . LYS A 199 ? 0.8936 1.1359 1.2323 0.0680  0.1126  0.0333  199 LYS A CD    
1649 C  CE    . LYS A 199 ? 0.8407 1.0855 1.1942 0.0811  0.1284  0.0359  199 LYS A CE    
1650 N  NZ    . LYS A 199 ? 1.0659 1.2873 1.4046 0.0887  0.1359  0.0239  199 LYS A NZ    
1651 N  N     . GLU A 200 ? 0.7242 0.9109 0.9740 0.0750  0.1437  -0.0101 200 GLU A N     
1652 C  CA    . GLU A 200 ? 0.7676 0.9393 1.0056 0.0848  0.1568  -0.0200 200 GLU A CA    
1653 C  C     . GLU A 200 ? 0.7317 0.8814 0.9394 0.0808  0.1529  -0.0343 200 GLU A C     
1654 O  O     . GLU A 200 ? 0.7276 0.8592 0.9267 0.0858  0.1557  -0.0439 200 GLU A O     
1655 C  CB    . GLU A 200 ? 0.8094 0.9924 1.0503 0.0910  0.1715  -0.0165 200 GLU A CB    
1656 C  CG    . GLU A 200 ? 1.0696 1.2368 1.2943 0.1011  0.1860  -0.0281 200 GLU A CG    
1657 C  CD    . GLU A 200 ? 1.4009 1.5820 1.6376 0.1107  0.2028  -0.0219 200 GLU A CD    
1658 O  OE1   . GLU A 200 ? 1.2628 1.4664 1.5257 0.1105  0.2030  -0.0074 200 GLU A OE1   
1659 O  OE2   . GLU A 200 ? 1.4761 1.6459 1.6958 0.1185  0.2159  -0.0314 200 GLU A OE2   
1660 N  N     . LYS A 201 ? 0.7078 0.8587 0.9000 0.0717  0.1462  -0.0355 201 LYS A N     
1661 C  CA    . LYS A 201 ? 0.7922 0.9242 0.9567 0.0674  0.1418  -0.0478 201 LYS A CA    
1662 C  C     . LYS A 201 ? 0.6998 0.8208 0.8634 0.0624  0.1291  -0.0510 201 LYS A C     
1663 O  O     . LYS A 201 ? 0.6461 0.7484 0.7930 0.0625  0.1276  -0.0617 201 LYS A O     
1664 C  CB    . LYS A 201 ? 0.7553 0.8930 0.9058 0.0595  0.1385  -0.0466 201 LYS A CB    
1665 C  CG    . LYS A 201 ? 0.7049 0.8529 0.8537 0.0643  0.1516  -0.0434 201 LYS A CG    
1666 C  CD    . LYS A 201 ? 0.6501 0.7969 0.7773 0.0578  0.1499  -0.0458 201 LYS A CD    
1667 C  CE    . LYS A 201 ? 0.5522 0.7028 0.6696 0.0646  0.1651  -0.0468 201 LYS A CE    
1668 N  NZ    . LYS A 201 ? 0.7534 0.9016 0.8472 0.0590  0.1637  -0.0494 201 LYS A NZ    
1669 N  N     . ASP A 202 ? 0.6549 0.7873 0.8359 0.0580  0.1201  -0.0417 202 ASP A N     
1670 C  CA    . ASP A 202 ? 0.7141 0.8386 0.8957 0.0536  0.1086  -0.0428 202 ASP A CA    
1671 C  C     . ASP A 202 ? 0.7512 0.8613 0.9094 0.0466  0.1013  -0.0520 202 ASP A C     
1672 O  O     . ASP A 202 ? 0.6785 0.7722 0.8277 0.0478  0.1000  -0.0600 202 ASP A O     
1673 C  CB    . ASP A 202 ? 0.7418 0.8575 0.9336 0.0614  0.1124  -0.0445 202 ASP A CB    
1674 C  CG    . ASP A 202 ? 0.8222 0.9358 1.0214 0.0575  0.1012  -0.0413 202 ASP A CG    
1675 O  OD1   . ASP A 202 ? 0.9052 1.0283 1.1061 0.0498  0.0914  -0.0358 202 ASP A OD1   
1676 O  OD2   . ASP A 202 ? 0.8345 0.9365 1.0376 0.0622  0.1024  -0.0442 202 ASP A OD2   
1677 N  N     . PRO A 203 ? 0.7635 0.8793 0.9130 0.0392  0.0964  -0.0504 203 PRO A N     
1678 C  CA    . PRO A 203 ? 0.6654 0.7688 0.7944 0.0329  0.0895  -0.0578 203 PRO A CA    
1679 C  C     . PRO A 203 ? 0.6407 0.7403 0.7732 0.0280  0.0781  -0.0568 203 PRO A C     
1680 O  O     . PRO A 203 ? 0.6058 0.7154 0.7540 0.0269  0.0738  -0.0491 203 PRO A O     
1681 C  CB    . PRO A 203 ? 0.6098 0.7228 0.7329 0.0274  0.0885  -0.0541 203 PRO A CB    
1682 C  CG    . PRO A 203 ? 0.6634 0.7942 0.8077 0.0271  0.0884  -0.0432 203 PRO A CG    
1683 C  CD    . PRO A 203 ? 0.7358 0.8696 0.8954 0.0359  0.0963  -0.0410 203 PRO A CD    
1684 N  N     . ASP A 204 ? 0.6417 0.7270 0.7590 0.0248  0.0734  -0.0644 204 ASP A N     
1685 C  CA    . ASP A 204 ? 0.5989 0.6810 0.7176 0.0197  0.0631  -0.0632 204 ASP A CA    
1686 C  C     . ASP A 204 ? 0.6005 0.6896 0.7150 0.0122  0.0561  -0.0597 204 ASP A C     
1687 O  O     . ASP A 204 ? 0.5397 0.6320 0.6598 0.0085  0.0487  -0.0558 204 ASP A O     
1688 C  CB    . ASP A 204 ? 0.6575 0.7225 0.7643 0.0192  0.0605  -0.0717 204 ASP A CB    
1689 C  CG    . ASP A 204 ? 0.7345 0.7897 0.8442 0.0264  0.0677  -0.0766 204 ASP A CG    
1690 O  OD1   . ASP A 204 ? 0.6933 0.7519 0.8196 0.0308  0.0692  -0.0717 204 ASP A OD1   
1691 O  OD2   . ASP A 204 ? 0.7013 0.7450 0.7964 0.0278  0.0717  -0.0854 204 ASP A OD2   
1692 N  N     . VAL A 205 ? 0.5324 0.6236 0.6368 0.0101  0.0588  -0.0608 205 VAL A N     
1693 C  CA    . VAL A 205 ? 0.5615 0.6575 0.6616 0.0033  0.0530  -0.0578 205 VAL A CA    
1694 C  C     . VAL A 205 ? 0.4979 0.6066 0.6036 0.0032  0.0580  -0.0520 205 VAL A C     
1695 O  O     . VAL A 205 ? 0.5223 0.6320 0.6238 0.0073  0.0666  -0.0535 205 VAL A O     
1696 C  CB    . VAL A 205 ? 0.5497 0.6352 0.6315 -0.0003 0.0499  -0.0637 205 VAL A CB    
1697 C  CG1   . VAL A 205 ? 0.5099 0.6004 0.5890 -0.0067 0.0448  -0.0597 205 VAL A CG1   
1698 C  CG2   . VAL A 205 ? 0.5702 0.6440 0.6486 -0.0008 0.0446  -0.0685 205 VAL A CG2   
1699 N  N     . LEU A 206 ? 0.4104 0.5286 0.5255 -0.0015 0.0529  -0.0456 206 LEU A N     
1700 C  CA    . LEU A 206 ? 0.5426 0.6728 0.6641 -0.0035 0.0559  -0.0393 206 LEU A CA    
1701 C  C     . LEU A 206 ? 0.4819 0.6096 0.5940 -0.0102 0.0507  -0.0391 206 LEU A C     
1702 O  O     . LEU A 206 ? 0.4727 0.5982 0.5860 -0.0150 0.0426  -0.0387 206 LEU A O     
1703 C  CB    . LEU A 206 ? 0.4819 0.6250 0.6230 -0.0043 0.0536  -0.0317 206 LEU A CB    
1704 C  CG    . LEU A 206 ? 0.4916 0.6424 0.6464 0.0028  0.0609  -0.0285 206 LEU A CG    
1705 C  CD1   . LEU A 206 ? 0.5800 0.7409 0.7524 0.0015  0.0550  -0.0220 206 LEU A CD1   
1706 C  CD2   . LEU A 206 ? 0.5350 0.6951 0.6937 0.0055  0.0704  -0.0245 206 LEU A CD2   
1707 N  N     . ILE A 207 ? 0.4750 0.6030 0.5779 -0.0103 0.0558  -0.0390 207 ILE A N     
1708 C  CA    . ILE A 207 ? 0.4916 0.6163 0.5847 -0.0159 0.0517  -0.0385 207 ILE A CA    
1709 C  C     . ILE A 207 ? 0.5413 0.6771 0.6453 -0.0200 0.0519  -0.0302 207 ILE A C     
1710 O  O     . ILE A 207 ? 0.5246 0.6703 0.6354 -0.0176 0.0592  -0.0254 207 ILE A O     
1711 C  CB    . ILE A 207 ? 0.5006 0.6186 0.5755 -0.0141 0.0561  -0.0429 207 ILE A CB    
1712 C  CG1   . ILE A 207 ? 0.5476 0.6548 0.6137 -0.0097 0.0568  -0.0513 207 ILE A CG1   
1713 C  CG2   . ILE A 207 ? 0.5244 0.6381 0.5897 -0.0197 0.0503  -0.0420 207 ILE A CG2   
1714 C  CD1   . ILE A 207 ? 0.5626 0.6627 0.6094 -0.0080 0.0607  -0.0569 207 ILE A CD1   
1715 N  N     . THR A 208 ? 0.5459 0.6800 0.6523 -0.0261 0.0441  -0.0284 208 THR A N     
1716 C  CA    . THR A 208 ? 0.4769 0.6188 0.5930 -0.0313 0.0429  -0.0211 208 THR A CA    
1717 C  C     . THR A 208 ? 0.5389 0.6733 0.6466 -0.0362 0.0380  -0.0212 208 THR A C     
1718 O  O     . THR A 208 ? 0.5315 0.6559 0.6284 -0.0361 0.0341  -0.0265 208 THR A O     
1719 C  CB    . THR A 208 ? 0.5680 0.7162 0.7005 -0.0344 0.0374  -0.0181 208 THR A CB    
1720 O  OG1   . THR A 208 ? 0.4755 0.6149 0.6042 -0.0381 0.0288  -0.0220 208 THR A OG1   
1721 C  CG2   . THR A 208 ? 0.5062 0.6602 0.6471 -0.0292 0.0403  -0.0184 208 THR A CG2   
1722 N  N     . TYR A 209 ? 0.5428 0.6828 0.6573 -0.0406 0.0383  -0.0144 209 TYR A N     
1723 C  CA    . TYR A 209 ? 0.5567 0.6903 0.6680 -0.0457 0.0332  -0.0129 209 TYR A CA    
1724 C  C     . TYR A 209 ? 0.6102 0.7460 0.7362 -0.0514 0.0275  -0.0098 209 TYR A C     
1725 O  O     . TYR A 209 ? 0.6348 0.7800 0.7732 -0.0540 0.0296  -0.0030 209 TYR A O     
1726 C  CB    . TYR A 209 ? 0.6043 0.7409 0.7100 -0.0463 0.0382  -0.0071 209 TYR A CB    
1727 C  CG    . TYR A 209 ? 0.6319 0.7604 0.7322 -0.0502 0.0333  -0.0058 209 TYR A CG    
1728 C  CD1   . TYR A 209 ? 0.6091 0.7274 0.6975 -0.0491 0.0292  -0.0118 209 TYR A CD1   
1729 C  CD2   . TYR A 209 ? 0.6981 0.8294 0.8069 -0.0551 0.0328  0.0020  209 TYR A CD2   
1730 C  CE1   . TYR A 209 ? 0.7222 0.8340 0.8076 -0.0521 0.0251  -0.0097 209 TYR A CE1   
1731 C  CE2   . TYR A 209 ? 0.6463 0.7698 0.7517 -0.0581 0.0287  0.0038  209 TYR A CE2   
1732 C  CZ    . TYR A 209 ? 0.7346 0.8487 0.8284 -0.0563 0.0250  -0.0020 209 TYR A CZ    
1733 O  OH    . TYR A 209 ? 0.6183 0.7254 0.7103 -0.0587 0.0212  0.0006  209 TYR A OH    
1734 N  N     . ASN A 210 ? 0.5862 0.7135 0.7106 -0.0533 0.0204  -0.0148 210 ASN A N     
1735 C  CA    . ASN A 210 ? 0.6062 0.7335 0.7416 -0.0586 0.0140  -0.0142 210 ASN A CA    
1736 C  C     . ASN A 210 ? 0.6202 0.7582 0.7677 -0.0585 0.0139  -0.0123 210 ASN A C     
1737 O  O     . ASN A 210 ? 0.6651 0.8073 0.8245 -0.0638 0.0096  -0.0093 210 ASN A O     
1738 C  CB    . ASN A 210 ? 0.6922 0.8187 0.8342 -0.0644 0.0128  -0.0084 210 ASN A CB    
1739 C  CG    . ASN A 210 ? 0.7628 0.8831 0.9111 -0.0701 0.0050  -0.0108 210 ASN A CG    
1740 O  OD1   . ASN A 210 ? 0.7747 0.8873 0.9165 -0.0692 0.0007  -0.0175 210 ASN A OD1   
1741 N  ND2   . ASN A 210 ? 0.8222 0.9455 0.9827 -0.0760 0.0034  -0.0052 210 ASN A ND2   
1742 N  N     . GLY A 211 ? 0.5962 0.7385 0.7416 -0.0526 0.0181  -0.0140 211 GLY A N     
1743 C  CA    . GLY A 211 ? 0.5318 0.6842 0.6893 -0.0517 0.0175  -0.0120 211 GLY A CA    
1744 C  C     . GLY A 211 ? 0.6205 0.7696 0.7794 -0.0543 0.0090  -0.0158 211 GLY A C     
1745 O  O     . GLY A 211 ? 0.6297 0.7881 0.8003 -0.0557 0.0061  -0.0129 211 GLY A O     
1746 N  N     . ASP A 212 ? 0.5876 0.7245 0.7347 -0.0549 0.0050  -0.0217 212 ASP A N     
1747 C  CA    . ASP A 212 ? 0.5797 0.7129 0.7256 -0.0571 -0.0025 -0.0256 212 ASP A CA    
1748 C  C     . ASP A 212 ? 0.5777 0.7131 0.7325 -0.0646 -0.0087 -0.0237 212 ASP A C     
1749 O  O     . ASP A 212 ? 0.6067 0.7445 0.7643 -0.0670 -0.0149 -0.0251 212 ASP A O     
1750 C  CB    . ASP A 212 ? 0.5357 0.6557 0.6678 -0.0558 -0.0041 -0.0317 212 ASP A CB    
1751 C  CG    . ASP A 212 ? 0.6163 0.7344 0.7417 -0.0499 -0.0025 -0.0350 212 ASP A CG    
1752 O  OD1   . ASP A 212 ? 0.5329 0.6589 0.6643 -0.0471 -0.0012 -0.0331 212 ASP A OD1   
1753 O  OD2   . ASP A 212 ? 0.6646 0.7733 0.7799 -0.0482 -0.0026 -0.0388 212 ASP A OD2   
1754 N  N     . ASN A 213 ? 0.5245 0.6588 0.6835 -0.0686 -0.0075 -0.0203 213 ASN A N     
1755 C  CA    . ASN A 213 ? 0.6847 0.8177 0.8515 -0.0765 -0.0139 -0.0194 213 ASN A CA    
1756 C  C     . ASN A 213 ? 0.6684 0.8129 0.8514 -0.0804 -0.0120 -0.0108 213 ASN A C     
1757 O  O     . ASN A 213 ? 0.6999 0.8426 0.8909 -0.0877 -0.0169 -0.0092 213 ASN A O     
1758 C  CB    . ASN A 213 ? 0.6588 0.7770 0.8172 -0.0788 -0.0156 -0.0233 213 ASN A CB    
1759 C  CG    . ASN A 213 ? 0.7783 0.8859 0.9225 -0.0753 -0.0175 -0.0311 213 ASN A CG    
1760 O  OD1   . ASN A 213 ? 0.8256 0.9298 0.9671 -0.0774 -0.0234 -0.0358 213 ASN A OD1   
1761 N  ND2   . ASN A 213 ? 0.7786 0.8815 0.9136 -0.0700 -0.0127 -0.0322 213 ASN A ND2   
1762 N  N     . PHE A 214 ? 0.6473 0.8033 0.8359 -0.0758 -0.0048 -0.0053 214 PHE A N     
1763 C  CA    . PHE A 214 ? 0.6802 0.8488 0.8855 -0.0791 -0.0021 0.0039  214 PHE A CA    
1764 C  C     . PHE A 214 ? 0.6468 0.8306 0.8614 -0.0738 0.0036  0.0088  214 PHE A C     
1765 O  O     . PHE A 214 ? 0.6891 0.8838 0.9180 -0.0766 -0.0005 0.0127  214 PHE A O     
1766 C  CB    . PHE A 214 ? 0.6949 0.8607 0.8980 -0.0793 0.0041  0.0081  214 PHE A CB    
1767 C  CG    . PHE A 214 ? 0.7482 0.9274 0.9689 -0.0827 0.0077  0.0187  214 PHE A CG    
1768 C  CD1   . PHE A 214 ? 0.7433 0.9243 0.9786 -0.0916 0.0010  0.0227  214 PHE A CD1   
1769 C  CD2   . PHE A 214 ? 0.7025 0.8926 0.9254 -0.0769 0.0180  0.0246  214 PHE A CD2   
1770 C  CE1   . PHE A 214 ? 0.8133 1.0077 1.0669 -0.0951 0.0043  0.0335  214 PHE A CE1   
1771 C  CE2   . PHE A 214 ? 0.7738 0.9775 1.0136 -0.0796 0.0222  0.0353  214 PHE A CE2   
1772 C  CZ    . PHE A 214 ? 0.8101 1.0165 1.0663 -0.0889 0.0153  0.0403  214 PHE A CZ    
1773 N  N     . ASP A 215 ? 0.6241 0.8084 0.8308 -0.0662 0.0129  0.0087  215 ASP A N     
1774 C  CA    . ASP A 215 ? 0.6385 0.8366 0.8546 -0.0605 0.0207  0.0141  215 ASP A CA    
1775 C  C     . ASP A 215 ? 0.6769 0.8819 0.9013 -0.0588 0.0165  0.0137  215 ASP A C     
1776 O  O     . ASP A 215 ? 0.6573 0.8774 0.8995 -0.0588 0.0179  0.0212  215 ASP A O     
1777 C  CB    . ASP A 215 ? 0.6391 0.8324 0.8406 -0.0523 0.0303  0.0109  215 ASP A CB    
1778 C  CG    . ASP A 215 ? 0.6484 0.8346 0.8392 -0.0539 0.0334  0.0113  215 ASP A CG    
1779 O  OD1   . ASP A 215 ? 0.7175 0.8917 0.8995 -0.0578 0.0272  0.0069  215 ASP A OD1   
1780 O  OD2   . ASP A 215 ? 0.6167 0.8094 0.8078 -0.0509 0.0423  0.0163  215 ASP A OD2   
1781 N  N     . PHE A 216 ? 0.6278 0.8229 0.8404 -0.0573 0.0114  0.0060  216 PHE A N     
1782 C  CA    . PHE A 216 ? 0.6174 0.8190 0.8365 -0.0549 0.0079  0.0063  216 PHE A CA    
1783 C  C     . PHE A 216 ? 0.6169 0.8267 0.8493 -0.0628 -0.0022 0.0100  216 PHE A C     
1784 O  O     . PHE A 216 ? 0.5881 0.8119 0.8357 -0.0621 -0.0034 0.0161  216 PHE A O     
1785 C  CB    . PHE A 216 ? 0.6273 0.8165 0.8302 -0.0512 0.0055  -0.0020 216 PHE A CB    
1786 C  CG    . PHE A 216 ? 0.6010 0.7878 0.7978 -0.0422 0.0143  -0.0041 216 PHE A CG    
1787 C  CD1   . PHE A 216 ? 0.6019 0.7985 0.8097 -0.0365 0.0181  -0.0002 216 PHE A CD1   
1788 C  CD2   . PHE A 216 ? 0.5207 0.6950 0.7013 -0.0396 0.0184  -0.0099 216 PHE A CD2   
1789 C  CE1   . PHE A 216 ? 0.6188 0.8111 0.8209 -0.0283 0.0263  -0.0030 216 PHE A CE1   
1790 C  CE2   . PHE A 216 ? 0.5502 0.7209 0.7245 -0.0320 0.0256  -0.0128 216 PHE A CE2   
1791 C  CZ    . PHE A 216 ? 0.5507 0.7296 0.7354 -0.0263 0.0298  -0.0098 216 PHE A CZ    
1792 N  N     . ALA A 217 ? 0.6344 0.8356 0.8617 -0.0705 -0.0097 0.0066  217 ALA A N     
1793 C  CA    . ALA A 217 ? 0.6576 0.8648 0.8959 -0.0791 -0.0201 0.0089  217 ALA A CA    
1794 C  C     . ALA A 217 ? 0.7011 0.9239 0.9613 -0.0829 -0.0185 0.0193  217 ALA A C     
1795 O  O     . ALA A 217 ? 0.6712 0.9069 0.9468 -0.0870 -0.0248 0.0246  217 ALA A O     
1796 C  CB    . ALA A 217 ? 0.5524 0.7445 0.7795 -0.0859 -0.0274 0.0019  217 ALA A CB    
1797 N  N     . TYR A 218 ? 0.6381 0.8610 0.9004 -0.0818 -0.0101 0.0230  218 TYR A N     
1798 C  CA    . TYR A 218 ? 0.6939 0.9328 0.9776 -0.0843 -0.0064 0.0341  218 TYR A CA    
1799 C  C     . TYR A 218 ? 0.6660 0.9217 0.9632 -0.0776 -0.0010 0.0407  218 TYR A C     
1800 O  O     . TYR A 218 ? 0.6684 0.9401 0.9868 -0.0815 -0.0047 0.0492  218 TYR A O     
1801 C  CB    . TYR A 218 ? 0.6516 0.8870 0.9316 -0.0827 0.0031  0.0369  218 TYR A CB    
1802 C  CG    . TYR A 218 ? 0.7653 1.0129 1.0660 -0.0891 0.0039  0.0478  218 TYR A CG    
1803 C  CD1   . TYR A 218 ? 0.8232 1.0625 1.1242 -0.0969 0.0002  0.0484  218 TYR A CD1   
1804 C  CD2   . TYR A 218 ? 0.7931 1.0608 1.1148 -0.0872 0.0086  0.0581  218 TYR A CD2   
1805 C  CE1   . TYR A 218 ? 0.8159 1.0664 1.1375 -0.1033 0.0007  0.0592  218 TYR A CE1   
1806 C  CE2   . TYR A 218 ? 0.7766 1.0566 1.1190 -0.0933 0.0094  0.0691  218 TYR A CE2   
1807 C  CZ    . TYR A 218 ? 0.8285 1.0998 1.1709 -0.1017 0.0052  0.0697  218 TYR A CZ    
1808 O  OH    . TYR A 218 ? 0.8737 1.1574 1.2382 -0.1082 0.0062  0.0816  218 TYR A OH    
1809 N  N     . LEU A 219 ? 0.6271 0.8794 0.9134 -0.0675 0.0078  0.0372  219 LEU A N     
1810 C  CA    . LEU A 219 ? 0.5823 0.8483 0.8809 -0.0599 0.0138  0.0427  219 LEU A CA    
1811 C  C     . LEU A 219 ? 0.6764 0.9498 0.9843 -0.0624 0.0035  0.0441  219 LEU A C     
1812 O  O     . LEU A 219 ? 0.7258 1.0163 1.0537 -0.0604 0.0048  0.0530  219 LEU A O     
1813 C  CB    . LEU A 219 ? 0.6113 0.8682 0.8940 -0.0492 0.0238  0.0366  219 LEU A CB    
1814 C  CG    . LEU A 219 ? 0.5699 0.8308 0.8531 -0.0428 0.0379  0.0402  219 LEU A CG    
1815 C  CD1   . LEU A 219 ? 0.6906 0.9357 0.9504 -0.0359 0.0444  0.0306  219 LEU A CD1   
1816 C  CD2   . LEU A 219 ? 0.5872 0.8661 0.8911 -0.0366 0.0454  0.0491  219 LEU A CD2   
1817 N  N     . LYS A 220 ? 0.6958 0.9573 0.9897 -0.0668 -0.0067 0.0361  220 LYS A N     
1818 C  CA    . LYS A 220 ? 0.7499 1.0183 1.0500 -0.0698 -0.0174 0.0374  220 LYS A CA    
1819 C  C     . LYS A 220 ? 0.7086 0.9912 1.0289 -0.0795 -0.0261 0.0454  220 LYS A C     
1820 O  O     . LYS A 220 ? 0.6283 0.9276 0.9662 -0.0795 -0.0298 0.0533  220 LYS A O     
1821 C  CB    . LYS A 220 ? 0.5447 0.7965 0.8230 -0.0723 -0.0253 0.0267  220 LYS A CB    
1822 C  CG    . LYS A 220 ? 0.5774 0.8350 0.8572 -0.0743 -0.0357 0.0272  220 LYS A CG    
1823 C  CD    . LYS A 220 ? 0.6530 0.8953 0.9126 -0.0794 -0.0446 0.0172  220 LYS A CD    
1824 C  CE    . LYS A 220 ? 0.7623 1.0091 1.0183 -0.0791 -0.0528 0.0170  220 LYS A CE    
1825 N  NZ    . LYS A 220 ? 0.8373 1.0735 1.0777 -0.0867 -0.0635 0.0090  220 LYS A NZ    
1826 N  N     . LYS A 221 ? 0.6867 0.9629 1.0057 -0.0881 -0.0301 0.0437  221 LYS A N     
1827 C  CA    . LYS A 221 ? 0.7885 1.0770 1.1276 -0.0985 -0.0388 0.0511  221 LYS A CA    
1828 C  C     . LYS A 221 ? 0.8296 1.1398 1.1950 -0.0955 -0.0314 0.0647  221 LYS A C     
1829 O  O     . LYS A 221 ? 0.8339 1.1613 1.2199 -0.1000 -0.0385 0.0731  221 LYS A O     
1830 C  CB    . LYS A 221 ? 0.8208 1.0969 1.1549 -0.1071 -0.0421 0.0474  221 LYS A CB    
1831 C  CG    . LYS A 221 ? 0.8986 1.1736 1.2374 -0.1198 -0.0576 0.0456  221 LYS A CG    
1832 C  CD    . LYS A 221 ? 0.9988 1.2522 1.3122 -0.1221 -0.0643 0.0319  221 LYS A CD    
1833 C  CE    . LYS A 221 ? 0.9564 1.2054 1.2722 -0.1351 -0.0788 0.0285  221 LYS A CE    
1834 N  NZ    . LYS A 221 ? 0.9551 1.1808 1.2464 -0.1369 -0.0828 0.0150  221 LYS A NZ    
1835 N  N     . ARG A 222 ? 0.7502 1.0606 1.1152 -0.0878 -0.0170 0.0672  222 ARG A N     
1836 C  CA    . ARG A 222 ? 0.6971 1.0282 1.0866 -0.0839 -0.0081 0.0801  222 ARG A CA    
1837 C  C     . ARG A 222 ? 0.7422 1.0859 1.1416 -0.0756 -0.0056 0.0845  222 ARG A C     
1838 O  O     . ARG A 222 ? 0.8390 1.2035 1.2644 -0.0761 -0.0057 0.0964  222 ARG A O     
1839 C  CB    . ARG A 222 ? 0.6930 1.0204 1.0767 -0.0774 0.0072  0.0810  222 ARG A CB    
1840 C  CG    . ARG A 222 ? 0.6780 0.9919 1.0508 -0.0846 0.0053  0.0771  222 ARG A CG    
1841 C  CD    . ARG A 222 ? 0.6073 0.9305 1.0009 -0.0969 -0.0037 0.0852  222 ARG A CD    
1842 N  NE    . ARG A 222 ? 0.7281 1.0747 1.1497 -0.0958 0.0027  0.0997  222 ARG A NE    
1843 C  CZ    . ARG A 222 ? 0.7069 1.0662 1.1523 -0.1058 -0.0036 0.1097  222 ARG A CZ    
1844 N  NH1   . ARG A 222 ? 0.6624 1.0122 1.1066 -0.1180 -0.0168 0.1059  222 ARG A NH1   
1845 N  NH2   . ARG A 222 ? 0.6589 1.0408 1.1305 -0.1034 0.0037  0.1237  222 ARG A NH2   
1846 N  N     . CYS A 223 ? 0.7458 1.0777 1.1265 -0.0680 -0.0037 0.0759  223 CYS A N     
1847 C  CA    . CYS A 223 ? 0.7767 1.1187 1.1666 -0.0595 -0.0009 0.0801  223 CYS A CA    
1848 C  C     . CYS A 223 ? 0.8117 1.1668 1.2162 -0.0664 -0.0153 0.0858  223 CYS A C     
1849 O  O     . CYS A 223 ? 0.8129 1.1861 1.2386 -0.0622 -0.0140 0.0960  223 CYS A O     
1850 C  CB    . CYS A 223 ? 0.7504 1.0750 1.1166 -0.0512 0.0033  0.0693  223 CYS A CB    
1851 S  SG    . CYS A 223 ? 0.7359 1.0523 1.0922 -0.0385 0.0226  0.0659  223 CYS A SG    
1852 N  N     . GLU A 224 ? 0.8630 1.2092 1.2560 -0.0768 -0.0292 0.0795  224 GLU A N     
1853 C  CA    . GLU A 224 ? 0.9590 1.3178 1.3641 -0.0845 -0.0440 0.0846  224 GLU A CA    
1854 C  C     . GLU A 224 ? 0.9425 1.3197 1.3747 -0.0933 -0.0489 0.0959  224 GLU A C     
1855 O  O     . GLU A 224 ? 0.9033 1.2989 1.3551 -0.0968 -0.0575 0.1052  224 GLU A O     
1856 C  CB    . GLU A 224 ? 1.1985 1.5412 1.5805 -0.0922 -0.0572 0.0731  224 GLU A CB    
1857 C  CG    . GLU A 224 ? 1.2179 1.5454 1.5883 -0.1008 -0.0601 0.0655  224 GLU A CG    
1858 C  CD    . GLU A 224 ? 1.4806 1.8031 1.8437 -0.1129 -0.0769 0.0600  224 GLU A CD    
1859 O  OE1   . GLU A 224 ? 1.7405 2.0741 2.1091 -0.1155 -0.0870 0.0635  224 GLU A OE1   
1860 O  OE2   . GLU A 224 ? 1.2437 1.5509 1.5954 -0.1197 -0.0801 0.0523  224 GLU A OE2   
1861 N  N     . LYS A 225 ? 0.9240 1.2975 1.3589 -0.0972 -0.0437 0.0964  225 LYS A N     
1862 C  CA    . LYS A 225 ? 0.8215 1.2131 1.2843 -0.1057 -0.0476 0.1083  225 LYS A CA    
1863 C  C     . LYS A 225 ? 0.8069 1.2217 1.2971 -0.0973 -0.0366 0.1228  225 LYS A C     
1864 O  O     . LYS A 225 ? 0.8744 1.3100 1.3928 -0.1035 -0.0420 0.1353  225 LYS A O     
1865 C  CB    . LYS A 225 ? 0.8264 1.2074 1.2852 -0.1119 -0.0447 0.1058  225 LYS A CB    
1866 C  CG    . LYS A 225 ? 0.9464 1.3140 1.3949 -0.1256 -0.0603 0.0978  225 LYS A CG    
1867 C  CD    . LYS A 225 ? 0.9312 1.3033 1.3976 -0.1359 -0.0623 0.1046  225 LYS A CD    
1868 C  CE    . LYS A 225 ? 0.9563 1.3040 1.4017 -0.1417 -0.0649 0.0932  225 LYS A CE    
1869 N  NZ    . LYS A 225 ? 0.9595 1.3081 1.4159 -0.1434 -0.0559 0.1001  225 LYS A NZ    
1870 N  N     . LEU A 226 ? 0.8175 1.2290 1.3006 -0.0835 -0.0211 0.1214  226 LEU A N     
1871 C  CA    . LEU A 226 ? 0.7581 1.1897 1.2655 -0.0738 -0.0087 0.1340  226 LEU A CA    
1872 C  C     . LEU A 226 ? 0.7658 1.2021 1.2751 -0.0639 -0.0074 0.1351  226 LEU A C     
1873 O  O     . LEU A 226 ? 0.7030 1.1542 1.2316 -0.0541 0.0039  0.1447  226 LEU A O     
1874 C  CB    . LEU A 226 ? 0.7793 1.2050 1.2799 -0.0648 0.0101  0.1328  226 LEU A CB    
1875 C  CG    . LEU A 226 ? 0.7841 1.1969 1.2717 -0.0722 0.0105  0.1277  226 LEU A CG    
1876 C  CD1   . LEU A 226 ? 0.7208 1.1235 1.1924 -0.0618 0.0282  0.1233  226 LEU A CD1   
1877 C  CD2   . LEU A 226 ? 0.7313 1.1613 1.2459 -0.0827 0.0059  0.1402  226 LEU A CD2   
1878 N  N     . GLY A 227 ? 0.7410 1.1651 1.2314 -0.0659 -0.0180 0.1260  227 GLY A N     
1879 C  CA    . GLY A 227 ? 0.7463 1.1751 1.2393 -0.0575 -0.0182 0.1282  227 GLY A CA    
1880 C  C     . GLY A 227 ? 0.8034 1.2223 1.2867 -0.0426 -0.0013 0.1238  227 GLY A C     
1881 O  O     . GLY A 227 ? 0.7694 1.2013 1.2713 -0.0328 0.0073  0.1326  227 GLY A O     
1882 N  N     . ILE A 228 ? 0.7830 1.1786 1.2375 -0.0407 0.0034  0.1102  228 ILE A N     
1883 C  CA    . ILE A 228 ? 0.7821 1.1649 1.2233 -0.0279 0.0177  0.1037  228 ILE A CA    
1884 C  C     . ILE A 228 ? 0.8382 1.2028 1.2553 -0.0272 0.0113  0.0927  228 ILE A C     
1885 O  O     . ILE A 228 ? 0.8360 1.1892 1.2355 -0.0360 0.0007  0.0850  228 ILE A O     
1886 C  CB    . ILE A 228 ? 0.8271 1.1989 1.2553 -0.0258 0.0299  0.0979  228 ILE A CB    
1887 C  CG1   . ILE A 228 ? 0.7994 1.1890 1.2498 -0.0297 0.0339  0.1091  228 ILE A CG1   
1888 C  CG2   . ILE A 228 ? 0.8513 1.2136 1.2701 -0.0120 0.0456  0.0929  228 ILE A CG2   
1889 C  CD1   . ILE A 228 ? 0.7971 1.1817 1.2403 -0.0233 0.0502  0.1072  228 ILE A CD1   
1890 N  N     . ASN A 229 ? 0.8222 1.1839 1.2392 -0.0164 0.0180  0.0924  229 ASN A N     
1891 C  CA    . ASN A 229 ? 0.8585 1.2025 1.2534 -0.0142 0.0144  0.0826  229 ASN A CA    
1892 C  C     . ASN A 229 ? 0.8342 1.1573 1.2059 -0.0099 0.0246  0.0705  229 ASN A C     
1893 O  O     . ASN A 229 ? 0.8007 1.1208 1.1740 0.0000  0.0381  0.0698  229 ASN A O     
1894 C  CB    . ASN A 229 ? 0.9201 1.2702 1.3271 -0.0051 0.0166  0.0885  229 ASN A CB    
1895 C  CG    . ASN A 229 ? 0.9280 1.2691 1.3203 -0.0075 0.0060  0.0840  229 ASN A CG    
1896 O  OD1   . ASN A 229 ? 1.0323 1.3618 1.4160 0.0003  0.0111  0.0797  229 ASN A OD1   
1897 N  ND2   . ASN A 229 ? 1.0029 1.3488 1.3918 -0.0183 -0.0087 0.0848  229 ASN A ND2   
1898 N  N     . PHE A 230 ? 0.8420 1.1504 1.1918 -0.0173 0.0179  0.0610  230 PHE A N     
1899 C  CA    . PHE A 230 ? 0.7701 1.0598 1.0978 -0.0150 0.0255  0.0503  230 PHE A CA    
1900 C  C     . PHE A 230 ? 0.7457 1.0200 1.0585 -0.0078 0.0285  0.0426  230 PHE A C     
1901 O  O     . PHE A 230 ? 0.7409 0.9993 1.0329 -0.0105 0.0247  0.0334  230 PHE A O     
1902 C  CB    . PHE A 230 ? 0.8055 1.0865 1.1186 -0.0255 0.0171  0.0444  230 PHE A CB    
1903 C  CG    . PHE A 230 ? 0.9165 1.1859 1.2153 -0.0249 0.0252  0.0382  230 PHE A CG    
1904 C  CD1   . PHE A 230 ? 0.8795 1.1323 1.1568 -0.0295 0.0207  0.0288  230 PHE A CD1   
1905 C  CD2   . PHE A 230 ? 0.8527 1.1286 1.1596 -0.0196 0.0375  0.0424  230 PHE A CD2   
1906 C  CE1   . PHE A 230 ? 1.0229 1.2661 1.2876 -0.0292 0.0274  0.0242  230 PHE A CE1   
1907 C  CE2   . PHE A 230 ? 0.8300 1.0961 1.1223 -0.0193 0.0445  0.0373  230 PHE A CE2   
1908 C  CZ    . PHE A 230 ? 0.7635 1.0135 1.0351 -0.0242 0.0390  0.0285  230 PHE A CZ    
1909 N  N     . ALA A 231 ? 0.7012 0.9806 1.0264 0.0016  0.0359  0.0471  231 ALA A N     
1910 C  CA    . ALA A 231 ? 0.7257 0.9921 1.0417 0.0085  0.0382  0.0417  231 ALA A CA    
1911 C  C     . ALA A 231 ? 0.7516 0.9998 1.0486 0.0131  0.0481  0.0310  231 ALA A C     
1912 O  O     . ALA A 231 ? 0.9488 1.1934 1.2487 0.0222  0.0593  0.0298  231 ALA A O     
1913 C  CB    . ALA A 231 ? 0.7359 1.0134 1.0733 0.0171  0.0427  0.0506  231 ALA A CB    
1914 N  N     . LEU A 232 ? 0.6827 0.9191 0.9597 0.0065  0.0434  0.0230  232 LEU A N     
1915 C  CA    . LEU A 232 ? 0.6493 0.8683 0.9067 0.0096  0.0503  0.0129  232 LEU A CA    
1916 C  C     . LEU A 232 ? 0.5893 0.7936 0.8356 0.0128  0.0485  0.0064  232 LEU A C     
1917 O  O     . LEU A 232 ? 0.7058 0.8971 0.9415 0.0180  0.0558  -0.0007 232 LEU A O     
1918 C  CB    . LEU A 232 ? 0.6436 0.8567 0.8860 0.0015  0.0464  0.0081  232 LEU A CB    
1919 C  CG    . LEU A 232 ? 0.7008 0.9231 0.9488 -0.0006 0.0517  0.0123  232 LEU A CG    
1920 C  CD1   . LEU A 232 ? 0.6913 0.9059 0.9245 -0.0088 0.0463  0.0079  232 LEU A CD1   
1921 C  CD2   . LEU A 232 ? 0.5607 0.7812 0.8071 0.0080  0.0657  0.0108  232 LEU A CD2   
1922 N  N     . GLY A 233 ? 0.5757 0.7818 0.8239 0.0094  0.0387  0.0088  233 GLY A N     
1923 C  CA    . GLY A 233 ? 0.7608 0.9541 1.0000 0.0121  0.0369  0.0041  233 GLY A CA    
1924 C  C     . GLY A 233 ? 0.7538 0.9448 1.0031 0.0218  0.0451  0.0056  233 GLY A C     
1925 O  O     . GLY A 233 ? 0.7166 0.9202 0.9846 0.0264  0.0493  0.0135  233 GLY A O     
1926 N  N     . ARG A 234 ? 0.7321 0.9066 0.9698 0.0249  0.0474  -0.0018 234 ARG A N     
1927 C  CA    . ARG A 234 ? 0.7253 0.8940 0.9713 0.0340  0.0553  -0.0018 234 ARG A CA    
1928 C  C     . ARG A 234 ? 0.7934 0.9720 1.0578 0.0370  0.0516  0.0082  234 ARG A C     
1929 O  O     . ARG A 234 ? 0.8453 1.0241 1.1234 0.0453  0.0587  0.0115  234 ARG A O     
1930 C  CB    . ARG A 234 ? 0.7130 0.8612 0.9427 0.0351  0.0567  -0.0119 234 ARG A CB    
1931 C  CG    . ARG A 234 ? 0.7481 0.8855 0.9636 0.0366  0.0646  -0.0214 234 ARG A CG    
1932 C  CD    . ARG A 234 ? 0.6490 0.7673 0.8558 0.0408  0.0685  -0.0299 234 ARG A CD    
1933 N  NE    . ARG A 234 ? 0.6788 0.7847 0.8657 0.0347  0.0634  -0.0381 234 ARG A NE    
1934 C  CZ    . ARG A 234 ? 0.6571 0.7512 0.8281 0.0349  0.0678  -0.0475 234 ARG A CZ    
1935 N  NH1   . ARG A 234 ? 0.5153 0.6073 0.6858 0.0410  0.0780  -0.0509 234 ARG A NH1   
1936 N  NH2   . ARG A 234 ? 0.7446 0.8295 0.8997 0.0289  0.0618  -0.0533 234 ARG A NH2   
1937 N  N     . ASP A 235 ? 0.8026 0.9893 1.0673 0.0307  0.0408  0.0132  235 ASP A N     
1938 C  CA    . ASP A 235 ? 0.8525 1.0510 1.1335 0.0325  0.0358  0.0239  235 ASP A CA    
1939 C  C     . ASP A 235 ? 0.7891 1.0089 1.0870 0.0307  0.0330  0.0339  235 ASP A C     
1940 O  O     . ASP A 235 ? 0.8237 1.0561 1.1337 0.0301  0.0263  0.0436  235 ASP A O     
1941 C  CB    . ASP A 235 ? 0.8513 1.0468 1.1216 0.0269  0.0256  0.0239  235 ASP A CB    
1942 C  CG    . ASP A 235 ? 0.8832 1.0844 1.1425 0.0174  0.0169  0.0223  235 ASP A CG    
1943 O  OD1   . ASP A 235 ? 0.8682 1.0692 1.1225 0.0144  0.0193  0.0179  235 ASP A OD1   
1944 O  OD2   . ASP A 235 ? 0.8409 1.0465 1.0963 0.0131  0.0079  0.0255  235 ASP A OD2   
1945 N  N     . GLY A 236 ? 0.7756 1.0003 1.0749 0.0294  0.0376  0.0325  236 GLY A N     
1946 C  CA    . GLY A 236 ? 0.7696 1.0149 1.0865 0.0270  0.0351  0.0423  236 GLY A CA    
1947 C  C     . GLY A 236 ? 0.8237 1.0762 1.1339 0.0159  0.0235  0.0428  236 GLY A C     
1948 O  O     . GLY A 236 ? 0.8219 1.0914 1.1467 0.0124  0.0202  0.0506  236 GLY A O     
1949 N  N     . SER A 237 ? 0.7027 0.9429 0.9922 0.0102  0.0172  0.0349  237 SER A N     
1950 C  CA    . SER A 237 ? 0.7064 0.9509 0.9880 0.0000  0.0065  0.0340  237 SER A CA    
1951 C  C     . SER A 237 ? 0.6257 0.8679 0.9018 -0.0044 0.0096  0.0293  237 SER A C     
1952 O  O     . SER A 237 ? 0.7094 0.9452 0.9835 0.0003  0.0198  0.0256  237 SER A O     
1953 C  CB    . SER A 237 ? 0.7629 0.9952 1.0251 -0.0034 -0.0002 0.0277  237 SER A CB    
1954 O  OG    . SER A 237 ? 0.6548 0.8693 0.9004 -0.0022 0.0054  0.0176  237 SER A OG    
1955 N  N     . GLU A 238 ? 0.5886 0.8355 0.8615 -0.0136 0.0005  0.0294  238 GLU A N     
1956 C  CA    . GLU A 238 ? 0.6873 0.9317 0.9552 -0.0190 0.0018  0.0258  238 GLU A CA    
1957 C  C     . GLU A 238 ? 0.6949 0.9233 0.9403 -0.0242 -0.0026 0.0159  238 GLU A C     
1958 O  O     . GLU A 238 ? 0.6678 0.8903 0.9031 -0.0252 -0.0086 0.0130  238 GLU A O     
1959 C  CB    . GLU A 238 ? 0.6778 0.9392 0.9616 -0.0260 -0.0049 0.0336  238 GLU A CB    
1960 C  CG    . GLU A 238 ? 0.8094 1.0805 1.0980 -0.0310 -0.0173 0.0384  238 GLU A CG    
1961 C  CD    . GLU A 238 ? 0.9730 1.2629 1.2816 -0.0371 -0.0233 0.0477  238 GLU A CD    
1962 O  OE1   . GLU A 238 ? 0.9212 1.2173 1.2415 -0.0369 -0.0167 0.0511  238 GLU A OE1   
1963 O  OE2   . GLU A 238 ? 1.0444 1.3437 1.3572 -0.0423 -0.0347 0.0519  238 GLU A OE2   
1964 N  N     . PRO A 239 ? 0.6607 0.8823 0.8984 -0.0271 0.0008  0.0113  239 PRO A N     
1965 C  CA    . PRO A 239 ? 0.6513 0.8574 0.8691 -0.0312 -0.0025 0.0025  239 PRO A CA    
1966 C  C     . PRO A 239 ? 0.7003 0.9061 0.9122 -0.0380 -0.0139 0.0011  239 PRO A C     
1967 O  O     . PRO A 239 ? 0.7435 0.9593 0.9643 -0.0441 -0.0208 0.0052  239 PRO A O     
1968 C  CB    . PRO A 239 ? 0.6285 0.8333 0.8456 -0.0346 0.0013  0.0016  239 PRO A CB    
1969 C  CG    . PRO A 239 ? 0.6664 0.8799 0.8962 -0.0285 0.0111  0.0069  239 PRO A CG    
1970 C  CD    . PRO A 239 ? 0.7026 0.9291 0.9488 -0.0250 0.0098  0.0141  239 PRO A CD    
1971 N  N     . LYS A 240 ? 0.7132 0.9074 0.9099 -0.0369 -0.0158 -0.0049 240 LYS A N     
1972 C  CA    . LYS A 240 ? 0.7850 0.9768 0.9724 -0.0420 -0.0252 -0.0074 240 LYS A CA    
1973 C  C     . LYS A 240 ? 0.8121 0.9916 0.9861 -0.0472 -0.0268 -0.0148 240 LYS A C     
1974 O  O     . LYS A 240 ? 0.8621 1.0302 1.0267 -0.0444 -0.0214 -0.0196 240 LYS A O     
1975 C  CB    . LYS A 240 ? 0.8823 1.0697 1.0620 -0.0372 -0.0256 -0.0084 240 LYS A CB    
1976 C  CG    . LYS A 240 ? 1.1474 1.3421 1.3258 -0.0403 -0.0347 -0.0056 240 LYS A CG    
1977 C  CD    . LYS A 240 ? 1.1791 1.3663 1.3454 -0.0366 -0.0348 -0.0079 240 LYS A CD    
1978 C  CE    . LYS A 240 ? 1.3723 1.5675 1.5354 -0.0393 -0.0436 -0.0045 240 LYS A CE    
1979 N  NZ    . LYS A 240 ? 1.3906 1.5995 1.5688 -0.0353 -0.0442 0.0054  240 LYS A NZ    
1980 N  N     . ILE A 241 ? 0.7918 0.9734 0.9656 -0.0547 -0.0345 -0.0155 241 ILE A N     
1981 C  CA    . ILE A 241 ? 0.8261 0.9957 0.9892 -0.0597 -0.0363 -0.0221 241 ILE A CA    
1982 C  C     . ILE A 241 ? 0.9243 1.0843 1.0710 -0.0601 -0.0405 -0.0283 241 ILE A C     
1983 O  O     . ILE A 241 ? 0.9964 1.1621 1.1413 -0.0611 -0.0466 -0.0271 241 ILE A O     
1984 C  CB    . ILE A 241 ? 0.8504 1.0253 1.0224 -0.0681 -0.0421 -0.0202 241 ILE A CB    
1985 C  CG1   . ILE A 241 ? 0.8300 1.0140 1.0181 -0.0674 -0.0362 -0.0136 241 ILE A CG1   
1986 C  CG2   . ILE A 241 ? 0.8518 1.0127 1.0124 -0.0733 -0.0449 -0.0275 241 ILE A CG2   
1987 C  CD1   . ILE A 241 ? 0.7995 1.0013 1.0053 -0.0658 -0.0368 -0.0048 241 ILE A CD1   
1988 N  N     . GLN A 242 ? 0.9865 1.1328 1.1213 -0.0589 -0.0371 -0.0343 242 GLN A N     
1989 C  CA    . GLN A 242 ? 1.0450 1.1819 1.1646 -0.0583 -0.0393 -0.0400 242 GLN A CA    
1990 C  C     . GLN A 242 ? 1.0728 1.1970 1.1843 -0.0620 -0.0396 -0.0462 242 GLN A C     
1991 O  O     . GLN A 242 ? 0.9980 1.1195 1.1148 -0.0636 -0.0367 -0.0456 242 GLN A O     
1992 C  CB    . GLN A 242 ? 1.0352 1.1684 1.1499 -0.0510 -0.0336 -0.0399 242 GLN A CB    
1993 C  CG    . GLN A 242 ? 1.1114 1.2551 1.2334 -0.0468 -0.0334 -0.0340 242 GLN A CG    
1994 C  CD    . GLN A 242 ? 1.2208 1.3592 1.3377 -0.0406 -0.0287 -0.0342 242 GLN A CD    
1995 O  OE1   . GLN A 242 ? 1.2123 1.3403 1.3216 -0.0392 -0.0252 -0.0384 242 GLN A OE1   
1996 N  NE2   . GLN A 242 ? 1.3731 1.5191 1.4955 -0.0369 -0.0290 -0.0290 242 GLN A NE2   
1997 N  N     . ARG A 243 ? 1.1873 1.3037 1.2860 -0.0629 -0.0428 -0.0517 243 ARG A N     
1998 C  CA    . ARG A 243 ? 1.2536 1.3567 1.3443 -0.0655 -0.0427 -0.0580 243 ARG A CA    
1999 C  C     . ARG A 243 ? 1.2067 1.3011 1.2924 -0.0600 -0.0357 -0.0593 243 ARG A C     
2000 O  O     . ARG A 243 ? 1.2340 1.3298 1.3161 -0.0547 -0.0328 -0.0581 243 ARG A O     
2001 C  CB    . ARG A 243 ? 1.3883 1.4864 1.4665 -0.0680 -0.0483 -0.0640 243 ARG A CB    
2002 C  CG    . ARG A 243 ? 1.4605 1.5461 1.5336 -0.0732 -0.0509 -0.0706 243 ARG A CG    
2003 C  CD    . ARG A 243 ? 1.6282 1.7080 1.6859 -0.0745 -0.0554 -0.0776 243 ARG A CD    
2004 N  NE    . ARG A 243 ? 1.7878 1.8651 1.8342 -0.0675 -0.0506 -0.0788 243 ARG A NE    
2005 C  CZ    . ARG A 243 ? 1.6644 1.7328 1.7077 -0.0625 -0.0437 -0.0802 243 ARG A CZ    
2006 N  NH1   . ARG A 243 ? 1.5780 1.6380 1.6266 -0.0636 -0.0408 -0.0812 243 ARG A NH1   
2007 N  NH2   . ARG A 243 ? 1.5816 1.6501 1.6169 -0.0566 -0.0397 -0.0798 243 ARG A NH2   
2008 N  N     . MET A 244 ? 1.1436 1.2294 1.2300 -0.0616 -0.0334 -0.0611 244 MET A N     
2009 C  CA    . MET A 244 ? 1.1273 1.2051 1.2096 -0.0572 -0.0278 -0.0618 244 MET A CA    
2010 C  C     . MET A 244 ? 1.1167 1.1820 1.1939 -0.0593 -0.0280 -0.0665 244 MET A C     
2011 O  O     . MET A 244 ? 1.1185 1.1786 1.1991 -0.0598 -0.0254 -0.0653 244 MET A O     
2012 C  CB    . MET A 244 ? 1.0251 1.1067 1.1152 -0.0559 -0.0234 -0.0570 244 MET A CB    
2013 C  CG    . MET A 244 ? 0.9479 1.0260 1.0340 -0.0506 -0.0186 -0.0566 244 MET A CG    
2014 S  SD    . MET A 244 ? 1.0261 1.1109 1.1115 -0.0455 -0.0175 -0.0549 244 MET A SD    
2015 C  CE    . MET A 244 ? 0.7872 0.8634 0.8635 -0.0419 -0.0160 -0.0576 244 MET A CE    
2016 N  N     . GLY A 245 ? 1.1963 1.2564 1.2646 -0.0602 -0.0311 -0.0719 245 GLY A N     
2017 C  CA    . GLY A 245 ? 1.2179 1.2651 1.2813 -0.0622 -0.0315 -0.0775 245 GLY A CA    
2018 C  C     . GLY A 245 ? 1.2417 1.2872 1.3110 -0.0697 -0.0367 -0.0788 245 GLY A C     
2019 O  O     . GLY A 245 ? 1.2761 1.3261 1.3439 -0.0738 -0.0426 -0.0807 245 GLY A O     
2020 N  N     . ASP A 246 ? 1.1929 1.2325 1.2695 -0.0718 -0.0349 -0.0770 246 ASP A N     
2021 C  CA    . ASP A 246 ? 1.2248 1.2630 1.3099 -0.0792 -0.0394 -0.0768 246 ASP A CA    
2022 C  C     . ASP A 246 ? 1.2797 1.3318 1.3778 -0.0817 -0.0398 -0.0688 246 ASP A C     
2023 O  O     . ASP A 246 ? 1.3400 1.3960 1.4462 -0.0882 -0.0448 -0.0676 246 ASP A O     
2024 C  CB    . ASP A 246 ? 1.2231 1.2477 1.3110 -0.0802 -0.0370 -0.0779 246 ASP A CB    
2025 C  CG    . ASP A 246 ? 1.1503 1.1765 1.2424 -0.0755 -0.0305 -0.0716 246 ASP A CG    
2026 O  OD1   . ASP A 246 ? 1.2494 1.2854 1.3406 -0.0714 -0.0278 -0.0679 246 ASP A OD1   
2027 O  OD2   . ASP A 246 ? 1.0366 1.0538 1.1328 -0.0761 -0.0284 -0.0703 246 ASP A OD2   
2028 N  N     . ARG A 247 ? 1.1808 1.2405 1.2812 -0.0766 -0.0345 -0.0635 247 ARG A N     
2029 C  CA    . ARG A 247 ? 1.0978 1.1704 1.2094 -0.0775 -0.0332 -0.0563 247 ARG A CA    
2030 C  C     . ARG A 247 ? 1.0452 1.1296 1.1567 -0.0749 -0.0344 -0.0549 247 ARG A C     
2031 O  O     . ARG A 247 ? 1.0475 1.1308 1.1504 -0.0733 -0.0369 -0.0590 247 ARG A O     
2032 C  CB    . ARG A 247 ? 1.0448 1.1177 1.1583 -0.0736 -0.0265 -0.0517 247 ARG A CB    
2033 C  CG    . ARG A 247 ? 1.0937 1.1547 1.2055 -0.0741 -0.0245 -0.0523 247 ARG A CG    
2034 C  CD    . ARG A 247 ? 1.0866 1.1467 1.1933 -0.0681 -0.0191 -0.0503 247 ARG A CD    
2035 N  NE    . ARG A 247 ? 1.2504 1.3063 1.3605 -0.0690 -0.0164 -0.0461 247 ARG A NE    
2036 C  CZ    . ARG A 247 ? 1.1722 1.2168 1.2822 -0.0701 -0.0169 -0.0474 247 ARG A CZ    
2037 N  NH1   . ARG A 247 ? 1.1291 1.1643 1.2346 -0.0705 -0.0196 -0.0540 247 ARG A NH1   
2038 N  NH2   . ARG A 247 ? 1.0998 1.1424 1.2139 -0.0706 -0.0144 -0.0419 247 ARG A NH2   
2039 N  N     . PHE A 248 ? 0.9674 1.0635 1.0887 -0.0741 -0.0318 -0.0485 248 PHE A N     
2040 C  CA    . PHE A 248 ? 0.9487 1.0565 1.0730 -0.0711 -0.0320 -0.0458 248 PHE A CA    
2041 C  C     . PHE A 248 ? 0.7956 0.9060 0.9195 -0.0645 -0.0247 -0.0430 248 PHE A C     
2042 O  O     . PHE A 248 ? 0.7435 0.8495 0.8662 -0.0632 -0.0201 -0.0422 248 PHE A O     
2043 C  CB    . PHE A 248 ? 0.9539 1.0742 1.0921 -0.0759 -0.0356 -0.0405 248 PHE A CB    
2044 C  CG    . PHE A 248 ? 1.1237 1.2412 1.2632 -0.0838 -0.0439 -0.0434 248 PHE A CG    
2045 C  CD1   . PHE A 248 ? 1.1677 1.2835 1.3164 -0.0900 -0.0453 -0.0413 248 PHE A CD1   
2046 C  CD2   . PHE A 248 ? 1.1609 1.2769 1.2919 -0.0852 -0.0504 -0.0482 248 PHE A CD2   
2047 C  CE1   . PHE A 248 ? 1.1732 1.2848 1.3234 -0.0980 -0.0535 -0.0447 248 PHE A CE1   
2048 C  CE2   . PHE A 248 ? 1.2582 1.3703 1.3885 -0.0929 -0.0585 -0.0520 248 PHE A CE2   
2049 C  CZ    . PHE A 248 ? 1.1583 1.2677 1.2985 -0.0995 -0.0604 -0.0507 248 PHE A CZ    
2050 N  N     . ALA A 249 ? 0.7578 0.8753 0.8824 -0.0603 -0.0240 -0.0416 249 ALA A N     
2051 C  CA    . ALA A 249 ? 0.7173 0.8373 0.8425 -0.0542 -0.0175 -0.0395 249 ALA A CA    
2052 C  C     . ALA A 249 ? 0.6788 0.8115 0.8143 -0.0521 -0.0172 -0.0347 249 ALA A C     
2053 O  O     . ALA A 249 ? 0.7820 0.9212 0.9217 -0.0546 -0.0228 -0.0333 249 ALA A O     
2054 C  CB    . ALA A 249 ? 0.7421 0.8537 0.8562 -0.0496 -0.0161 -0.0434 249 ALA A CB    
2055 N  N     . VAL A 250 ? 0.6320 0.7683 0.7717 -0.0474 -0.0106 -0.0321 250 VAL A N     
2056 C  CA    . VAL A 250 ? 0.5838 0.7323 0.7357 -0.0446 -0.0085 -0.0267 250 VAL A CA    
2057 C  C     . VAL A 250 ? 0.5823 0.7281 0.7312 -0.0374 -0.0035 -0.0277 250 VAL A C     
2058 O  O     . VAL A 250 ? 0.5557 0.6946 0.6981 -0.0344 0.0020  -0.0304 250 VAL A O     
2059 C  CB    . VAL A 250 ? 0.5138 0.6703 0.6763 -0.0457 -0.0040 -0.0218 250 VAL A CB    
2060 C  CG1   . VAL A 250 ? 0.5235 0.6927 0.6996 -0.0414 -0.0006 -0.0160 250 VAL A CG1   
2061 C  CG2   . VAL A 250 ? 0.5037 0.6628 0.6716 -0.0536 -0.0097 -0.0201 250 VAL A CG2   
2062 N  N     . GLU A 251 ? 0.5969 0.7481 0.7505 -0.0349 -0.0058 -0.0254 251 GLU A N     
2063 C  CA    . GLU A 251 ? 0.5927 0.7421 0.7469 -0.0281 -0.0013 -0.0253 251 GLU A CA    
2064 C  C     . GLU A 251 ? 0.6294 0.7895 0.7982 -0.0240 0.0036  -0.0197 251 GLU A C     
2065 O  O     . GLU A 251 ? 0.6371 0.8092 0.8177 -0.0265 0.0010  -0.0142 251 GLU A O     
2066 C  CB    . GLU A 251 ? 0.7116 0.8601 0.8628 -0.0272 -0.0062 -0.0250 251 GLU A CB    
2067 C  CG    . GLU A 251 ? 0.8666 1.0035 1.0036 -0.0285 -0.0083 -0.0305 251 GLU A CG    
2068 C  CD    . GLU A 251 ? 1.1633 1.2979 1.2980 -0.0249 -0.0091 -0.0298 251 GLU A CD    
2069 O  OE1   . GLU A 251 ? 1.0408 1.1840 1.1811 -0.0245 -0.0128 -0.0252 251 GLU A OE1   
2070 O  OE2   . GLU A 251 ? 1.3297 1.4548 1.4577 -0.0227 -0.0065 -0.0330 251 GLU A OE2   
2071 N  N     . VAL A 252 ? 0.5615 0.7169 0.7299 -0.0177 0.0106  -0.0212 252 VAL A N     
2072 C  CA    . VAL A 252 ? 0.5640 0.7274 0.7458 -0.0119 0.0168  -0.0165 252 VAL A CA    
2073 C  C     . VAL A 252 ? 0.5686 0.7255 0.7500 -0.0060 0.0188  -0.0178 252 VAL A C     
2074 O  O     . VAL A 252 ? 0.5807 0.7257 0.7528 -0.0031 0.0231  -0.0236 252 VAL A O     
2075 C  CB    . VAL A 252 ? 0.6141 0.7771 0.7956 -0.0096 0.0254  -0.0177 252 VAL A CB    
2076 C  CG1   . VAL A 252 ? 0.5874 0.7574 0.7824 -0.0023 0.0331  -0.0136 252 VAL A CG1   
2077 C  CG2   . VAL A 252 ? 0.5952 0.7654 0.7793 -0.0158 0.0234  -0.0150 252 VAL A CG2   
2078 N  N     . LYS A 253 ? 0.5547 0.7193 0.7463 -0.0045 0.0151  -0.0120 253 LYS A N     
2079 C  CA    . LYS A 253 ? 0.5750 0.7336 0.7673 0.0004  0.0158  -0.0118 253 LYS A CA    
2080 C  C     . LYS A 253 ? 0.6474 0.7991 0.8430 0.0076  0.0252  -0.0142 253 LYS A C     
2081 O  O     . LYS A 253 ? 0.6498 0.8068 0.8529 0.0106  0.0316  -0.0128 253 LYS A O     
2082 C  CB    . LYS A 253 ? 0.5876 0.7584 0.7925 0.0011  0.0107  -0.0031 253 LYS A CB    
2083 C  CG    . LYS A 253 ? 0.6407 0.8158 0.8388 -0.0056 0.0009  -0.0021 253 LYS A CG    
2084 C  CD    . LYS A 253 ? 0.6305 0.7937 0.8145 -0.0063 -0.0014 -0.0067 253 LYS A CD    
2085 C  CE    . LYS A 253 ? 0.7811 0.9469 0.9555 -0.0128 -0.0096 -0.0074 253 LYS A CE    
2086 N  NZ    . LYS A 253 ? 0.8376 1.0073 1.0117 -0.0117 -0.0143 -0.0025 253 LYS A NZ    
2087 N  N     . GLY A 254 ? 0.6002 0.7397 0.7902 0.0103  0.0261  -0.0180 254 GLY A N     
2088 C  CA    . GLY A 254 ? 0.6553 0.7842 0.8448 0.0163  0.0341  -0.0227 254 GLY A CA    
2089 C  C     . GLY A 254 ? 0.6427 0.7626 0.8182 0.0149  0.0383  -0.0310 254 GLY A C     
2090 O  O     . GLY A 254 ? 0.6247 0.7327 0.7949 0.0186  0.0435  -0.0370 254 GLY A O     
2091 N  N     . ARG A 255 ? 0.6764 0.8011 0.8454 0.0095  0.0359  -0.0315 255 ARG A N     
2092 C  CA    . ARG A 255 ? 0.6007 0.7184 0.7562 0.0077  0.0392  -0.0379 255 ARG A CA    
2093 C  C     . ARG A 255 ? 0.6084 0.7219 0.7519 0.0009  0.0321  -0.0405 255 ARG A C     
2094 O  O     . ARG A 255 ? 0.5742 0.6902 0.7194 -0.0023 0.0254  -0.0378 255 ARG A O     
2095 C  CB    . ARG A 255 ? 0.6180 0.7462 0.7788 0.0083  0.0446  -0.0348 255 ARG A CB    
2096 C  CG    . ARG A 255 ? 0.6427 0.7737 0.8134 0.0162  0.0541  -0.0335 255 ARG A CG    
2097 C  CD    . ARG A 255 ? 0.7421 0.8854 0.9195 0.0167  0.0597  -0.0290 255 ARG A CD    
2098 N  NE    . ARG A 255 ? 0.7587 0.9035 0.9438 0.0252  0.0705  -0.0286 255 ARG A NE    
2099 C  CZ    . ARG A 255 ? 0.6960 0.8508 0.9003 0.0303  0.0734  -0.0215 255 ARG A CZ    
2100 N  NH1   . ARG A 255 ? 0.6711 0.8363 0.8887 0.0273  0.0656  -0.0139 255 ARG A NH1   
2101 N  NH2   . ARG A 255 ? 0.7592 0.9136 0.9695 0.0388  0.0846  -0.0221 255 ARG A NH2   
2102 N  N     . ILE A 256 ? 0.4984 0.6054 0.6293 -0.0012 0.0339  -0.0455 256 ILE A N     
2103 C  CA    . ILE A 256 ? 0.5331 0.6364 0.6537 -0.0072 0.0282  -0.0473 256 ILE A CA    
2104 C  C     . ILE A 256 ? 0.4593 0.5690 0.5785 -0.0102 0.0298  -0.0454 256 ILE A C     
2105 O  O     . ILE A 256 ? 0.5102 0.6185 0.6240 -0.0085 0.0357  -0.0474 256 ILE A O     
2106 C  CB    . ILE A 256 ? 0.5871 0.6773 0.6949 -0.0075 0.0275  -0.0537 256 ILE A CB    
2107 C  CG1   . ILE A 256 ? 0.5580 0.6420 0.6691 -0.0054 0.0252  -0.0545 256 ILE A CG1   
2108 C  CG2   . ILE A 256 ? 0.5552 0.6429 0.6539 -0.0131 0.0226  -0.0546 256 ILE A CG2   
2109 C  CD1   . ILE A 256 ? 0.7200 0.8080 0.8353 -0.0081 0.0188  -0.0504 256 ILE A CD1   
2110 N  N     . HIS A 257 ? 0.4541 0.5708 0.5782 -0.0148 0.0249  -0.0414 257 HIS A N     
2111 C  CA    . HIS A 257 ? 0.4989 0.6207 0.6228 -0.0187 0.0255  -0.0391 257 HIS A CA    
2112 C  C     . HIS A 257 ? 0.5297 0.6425 0.6406 -0.0223 0.0228  -0.0427 257 HIS A C     
2113 O  O     . HIS A 257 ? 0.4094 0.5185 0.5178 -0.0257 0.0169  -0.0435 257 HIS A O     
2114 C  CB    . HIS A 257 ? 0.4672 0.5989 0.6020 -0.0228 0.0207  -0.0339 257 HIS A CB    
2115 C  CG    . HIS A 257 ? 0.4001 0.5350 0.5353 -0.0280 0.0199  -0.0315 257 HIS A CG    
2116 N  ND1   . HIS A 257 ? 0.4474 0.5845 0.5862 -0.0339 0.0131  -0.0298 257 HIS A ND1   
2117 C  CD2   . HIS A 257 ? 0.3858 0.5215 0.5180 -0.0283 0.0250  -0.0304 257 HIS A CD2   
2118 C  CE1   . HIS A 257 ? 0.4956 0.6341 0.6351 -0.0377 0.0140  -0.0275 257 HIS A CE1   
2119 N  NE2   . HIS A 257 ? 0.4102 0.5487 0.5460 -0.0344 0.0213  -0.0273 257 HIS A NE2   
2120 N  N     . PHE A 258 ? 0.5002 0.6098 0.6027 -0.0214 0.0275  -0.0445 258 PHE A N     
2121 C  CA    . PHE A 258 ? 0.4834 0.5857 0.5741 -0.0245 0.0252  -0.0467 258 PHE A CA    
2122 C  C     . PHE A 258 ? 0.4906 0.5986 0.5836 -0.0285 0.0255  -0.0420 258 PHE A C     
2123 O  O     . PHE A 258 ? 0.5374 0.6503 0.6299 -0.0274 0.0313  -0.0397 258 PHE A O     
2124 C  CB    . PHE A 258 ? 0.5244 0.6197 0.6032 -0.0215 0.0291  -0.0514 258 PHE A CB    
2125 C  CG    . PHE A 258 ? 0.5997 0.6872 0.6669 -0.0246 0.0250  -0.0537 258 PHE A CG    
2126 C  CD1   . PHE A 258 ? 0.5777 0.6595 0.6447 -0.0263 0.0190  -0.0552 258 PHE A CD1   
2127 C  CD2   . PHE A 258 ? 0.5759 0.6626 0.6329 -0.0255 0.0275  -0.0537 258 PHE A CD2   
2128 C  CE1   . PHE A 258 ? 0.6942 0.7701 0.7528 -0.0288 0.0153  -0.0563 258 PHE A CE1   
2129 C  CE2   . PHE A 258 ? 0.6428 0.7235 0.6903 -0.0283 0.0231  -0.0548 258 PHE A CE2   
2130 C  CZ    . PHE A 258 ? 0.6820 0.7574 0.7312 -0.0300 0.0170  -0.0559 258 PHE A CZ    
2131 N  N     . ASP A 259 ? 0.5038 0.6109 0.5997 -0.0331 0.0197  -0.0405 259 ASP A N     
2132 C  CA    . ASP A 259 ? 0.5158 0.6257 0.6140 -0.0376 0.0191  -0.0363 259 ASP A CA    
2133 C  C     . ASP A 259 ? 0.5692 0.6712 0.6562 -0.0389 0.0179  -0.0374 259 ASP A C     
2134 O  O     . ASP A 259 ? 0.5371 0.6319 0.6202 -0.0397 0.0134  -0.0402 259 ASP A O     
2135 C  CB    . ASP A 259 ? 0.4673 0.5787 0.5743 -0.0419 0.0134  -0.0347 259 ASP A CB    
2136 C  CG    . ASP A 259 ? 0.5797 0.6936 0.6918 -0.0469 0.0128  -0.0299 259 ASP A CG    
2137 O  OD1   . ASP A 259 ? 0.5027 0.6185 0.6120 -0.0467 0.0172  -0.0268 259 ASP A OD1   
2138 O  OD2   . ASP A 259 ? 0.6286 0.7423 0.7471 -0.0511 0.0078  -0.0293 259 ASP A OD2   
2139 N  N     . LEU A 260 ? 0.5390 0.6434 0.6215 -0.0390 0.0221  -0.0346 260 LEU A N     
2140 C  CA    . LEU A 260 ? 0.5605 0.6589 0.6321 -0.0401 0.0208  -0.0348 260 LEU A CA    
2141 C  C     . LEU A 260 ? 0.5903 0.6854 0.6657 -0.0445 0.0160  -0.0318 260 LEU A C     
2142 O  O     . LEU A 260 ? 0.6779 0.7665 0.7470 -0.0451 0.0128  -0.0327 260 LEU A O     
2143 C  CB    . LEU A 260 ? 0.5836 0.6865 0.6482 -0.0391 0.0267  -0.0319 260 LEU A CB    
2144 C  CG    . LEU A 260 ? 0.6178 0.7198 0.6727 -0.0343 0.0315  -0.0368 260 LEU A CG    
2145 C  CD1   . LEU A 260 ? 0.5594 0.6693 0.6118 -0.0324 0.0395  -0.0332 260 LEU A CD1   
2146 C  CD2   . LEU A 260 ? 0.6298 0.7232 0.6709 -0.0342 0.0281  -0.0414 260 LEU A CD2   
2147 N  N     . TYR A 261 ? 0.6160 0.7149 0.7024 -0.0476 0.0151  -0.0282 261 TYR A N     
2148 C  CA    . TYR A 261 ? 0.6597 0.7546 0.7501 -0.0519 0.0117  -0.0250 261 TYR A CA    
2149 C  C     . TYR A 261 ? 0.6962 0.7816 0.7832 -0.0519 0.0068  -0.0289 261 TYR A C     
2150 O  O     . TYR A 261 ? 0.7388 0.8195 0.8225 -0.0528 0.0056  -0.0266 261 TYR A O     
2151 C  CB    . TYR A 261 ? 0.6351 0.7346 0.7385 -0.0557 0.0106  -0.0220 261 TYR A CB    
2152 C  CG    . TYR A 261 ? 0.7254 0.8191 0.8339 -0.0603 0.0072  -0.0192 261 TYR A CG    
2153 C  CD1   . TYR A 261 ? 0.7987 0.8935 0.9086 -0.0624 0.0093  -0.0124 261 TYR A CD1   
2154 C  CD2   . TYR A 261 ? 0.7715 0.8582 0.8833 -0.0624 0.0021  -0.0233 261 TYR A CD2   
2155 C  CE1   . TYR A 261 ? 0.8575 0.9459 0.9736 -0.0664 0.0064  -0.0095 261 TYR A CE1   
2156 C  CE2   . TYR A 261 ? 0.8607 0.9403 0.9772 -0.0663 -0.0006 -0.0216 261 TYR A CE2   
2157 C  CZ    . TYR A 261 ? 0.9326 1.0126 1.0521 -0.0683 0.0015  -0.0146 261 TYR A CZ    
2158 O  OH    . TYR A 261 ? 1.1111 1.1830 1.2367 -0.0719 -0.0010 -0.0126 261 TYR A OH    
2159 N  N     . PRO A 262 ? 0.6967 0.7794 0.7846 -0.0506 0.0041  -0.0339 262 PRO A N     
2160 C  CA    . PRO A 262 ? 0.6462 0.7206 0.7309 -0.0501 0.0007  -0.0369 262 PRO A CA    
2161 C  C     . PRO A 262 ? 0.6797 0.7513 0.7560 -0.0476 0.0010  -0.0374 262 PRO A C     
2162 O  O     . PRO A 262 ? 0.8270 0.8932 0.9020 -0.0478 -0.0011 -0.0365 262 PRO A O     
2163 C  CB    . PRO A 262 ? 0.6350 0.7096 0.7216 -0.0489 -0.0013 -0.0413 262 PRO A CB    
2164 C  CG    . PRO A 262 ? 0.6256 0.7082 0.7144 -0.0473 0.0013  -0.0410 262 PRO A CG    
2165 C  CD    . PRO A 262 ? 0.5976 0.6856 0.6901 -0.0495 0.0043  -0.0361 262 PRO A CD    
2166 N  N     . VAL A 263 ? 0.6559 0.7308 0.7270 -0.0452 0.0033  -0.0389 263 VAL A N     
2167 C  CA    . VAL A 263 ? 0.7300 0.8019 0.7926 -0.0437 0.0027  -0.0401 263 VAL A CA    
2168 C  C     . VAL A 263 ? 0.7787 0.8504 0.8376 -0.0456 0.0024  -0.0353 263 VAL A C     
2169 O  O     . VAL A 263 ? 0.8277 0.8956 0.8840 -0.0459 -0.0007 -0.0342 263 VAL A O     
2170 C  CB    . VAL A 263 ? 0.6548 0.7291 0.7122 -0.0410 0.0057  -0.0434 263 VAL A CB    
2171 C  CG1   . VAL A 263 ? 0.7624 0.8331 0.8096 -0.0405 0.0043  -0.0450 263 VAL A CG1   
2172 C  CG2   . VAL A 263 ? 0.6566 0.7307 0.7186 -0.0387 0.0054  -0.0471 263 VAL A CG2   
2173 N  N     . ILE A 264 ? 0.7014 0.7781 0.7611 -0.0470 0.0055  -0.0312 264 ILE A N     
2174 C  CA    . ILE A 264 ? 0.7939 0.8715 0.8500 -0.0489 0.0055  -0.0252 264 ILE A CA    
2175 C  C     . ILE A 264 ? 0.8236 0.8965 0.8872 -0.0509 0.0023  -0.0215 264 ILE A C     
2176 O  O     . ILE A 264 ? 0.7510 0.8216 0.8121 -0.0513 0.0000  -0.0180 264 ILE A O     
2177 C  CB    . ILE A 264 ? 0.7980 0.8829 0.8543 -0.0497 0.0105  -0.0207 264 ILE A CB    
2178 C  CG1   . ILE A 264 ? 0.7301 0.8192 0.7808 -0.0467 0.0149  -0.0250 264 ILE A CG1   
2179 C  CG2   . ILE A 264 ? 0.7122 0.7990 0.7624 -0.0512 0.0107  -0.0140 264 ILE A CG2   
2180 C  CD1   . ILE A 264 ? 0.7020 0.7882 0.7389 -0.0446 0.0144  -0.0293 264 ILE A CD1   
2181 N  N     . ARG A 265 ? 0.7484 0.8196 0.8216 -0.0522 0.0021  -0.0223 265 ARG A N     
2182 C  CA    . ARG A 265 ? 0.8273 0.8922 0.9075 -0.0539 -0.0003 -0.0200 265 ARG A CA    
2183 C  C     . ARG A 265 ? 0.8800 0.9390 0.9582 -0.0516 -0.0031 -0.0226 265 ARG A C     
2184 O  O     . ARG A 265 ? 0.9423 0.9969 1.0238 -0.0518 -0.0044 -0.0188 265 ARG A O     
2185 C  CB    . ARG A 265 ? 0.8081 0.8712 0.8969 -0.0560 -0.0007 -0.0224 265 ARG A CB    
2186 C  CG    . ARG A 265 ? 1.0220 1.0758 1.1157 -0.0565 -0.0032 -0.0242 265 ARG A CG    
2187 C  CD    . ARG A 265 ? 1.1170 1.1672 1.2180 -0.0595 -0.0031 -0.0180 265 ARG A CD    
2188 N  NE    . ARG A 265 ? 1.1509 1.2049 1.2588 -0.0635 -0.0024 -0.0157 265 ARG A NE    
2189 C  CZ    . ARG A 265 ? 1.1641 1.2121 1.2810 -0.0671 -0.0038 -0.0151 265 ARG A CZ    
2190 N  NH1   . ARG A 265 ? 1.1237 1.1606 1.2429 -0.0667 -0.0055 -0.0171 265 ARG A NH1   
2191 N  NH2   . ARG A 265 ? 1.0451 1.0981 1.1694 -0.0713 -0.0036 -0.0123 265 ARG A NH2   
2192 N  N     . ARG A 266 ? 0.8944 0.9535 0.9684 -0.0492 -0.0037 -0.0281 266 ARG A N     
2193 C  CA    . ARG A 266 ? 0.8082 0.8631 0.8816 -0.0470 -0.0059 -0.0299 266 ARG A CA    
2194 C  C     . ARG A 266 ? 0.8044 0.8610 0.8720 -0.0465 -0.0077 -0.0272 266 ARG A C     
2195 O  O     . ARG A 266 ? 0.8623 0.9163 0.9320 -0.0454 -0.0099 -0.0260 266 ARG A O     
2196 C  CB    . ARG A 266 ? 0.8080 0.8627 0.8806 -0.0451 -0.0059 -0.0360 266 ARG A CB    
2197 C  CG    . ARG A 266 ? 0.9383 0.9890 1.0124 -0.0427 -0.0073 -0.0376 266 ARG A CG    
2198 C  CD    . ARG A 266 ? 0.9209 0.9734 0.9928 -0.0408 -0.0073 -0.0419 266 ARG A CD    
2199 N  NE    . ARG A 266 ? 1.1675 1.2228 1.2344 -0.0407 -0.0077 -0.0422 266 ARG A NE    
2200 C  CZ    . ARG A 266 ? 1.0712 1.1286 1.1361 -0.0396 -0.0067 -0.0455 266 ARG A CZ    
2201 N  NH1   . ARG A 266 ? 0.8004 0.8590 0.8683 -0.0387 -0.0056 -0.0478 266 ARG A NH1   
2202 N  NH2   . ARG A 266 ? 0.8888 0.9469 0.9485 -0.0395 -0.0069 -0.0466 266 ARG A NH2   
2203 N  N     . THR A 267 ? 0.8599 0.9210 0.9203 -0.0474 -0.0068 -0.0263 267 THR A N     
2204 C  CA    . THR A 267 ? 0.7724 0.8351 0.8250 -0.0476 -0.0093 -0.0247 267 THR A CA    
2205 C  C     . THR A 267 ? 0.7842 0.8491 0.8356 -0.0495 -0.0104 -0.0169 267 THR A C     
2206 O  O     . THR A 267 ? 0.8865 0.9512 0.9375 -0.0498 -0.0142 -0.0133 267 THR A O     
2207 C  CB    . THR A 267 ? 0.8560 0.9212 0.8989 -0.0471 -0.0076 -0.0294 267 THR A CB    
2208 O  OG1   . THR A 267 ? 1.0302 1.0933 1.0755 -0.0452 -0.0071 -0.0356 267 THR A OG1   
2209 C  CG2   . THR A 267 ? 0.9366 1.0025 0.9694 -0.0481 -0.0109 -0.0289 267 THR A CG2   
2210 N  N     . ILE A 268 ? 0.8432 0.9111 0.8950 -0.0509 -0.0073 -0.0133 268 ILE A N     
2211 C  CA    . ILE A 268 ? 0.8841 0.9550 0.9346 -0.0527 -0.0078 -0.0046 268 ILE A CA    
2212 C  C     . ILE A 268 ? 0.9160 0.9839 0.9790 -0.0537 -0.0065 0.0003  268 ILE A C     
2213 O  O     . ILE A 268 ? 0.8943 0.9603 0.9636 -0.0540 -0.0041 -0.0029 268 ILE A O     
2214 C  CB    . ILE A 268 ? 0.8169 0.8942 0.8567 -0.0535 -0.0045 -0.0032 268 ILE A CB    
2215 C  CG1   . ILE A 268 ? 0.8547 0.9325 0.8821 -0.0521 -0.0048 -0.0108 268 ILE A CG1   
2216 C  CG2   . ILE A 268 ? 0.8614 0.9429 0.8974 -0.0552 -0.0057 0.0064  268 ILE A CG2   
2217 C  CD1   . ILE A 268 ? 0.8469 0.9301 0.8601 -0.0524 -0.0021 -0.0097 268 ILE A CD1   
2218 N  N     . ASN A 269 ? 0.9622 1.0294 1.0295 -0.0544 -0.0086 0.0084  269 ASN A N     
2219 C  CA    . ASN A 269 ? 1.1887 1.2517 1.2683 -0.0554 -0.0075 0.0138  269 ASN A CA    
2220 C  C     . ASN A 269 ? 0.9419 1.0106 1.0207 -0.0579 -0.0055 0.0229  269 ASN A C     
2221 O  O     . ASN A 269 ? 0.8166 0.8902 0.8894 -0.0582 -0.0073 0.0299  269 ASN A O     
2222 C  CB    . ASN A 269 ? 1.1772 1.2349 1.2649 -0.0538 -0.0103 0.0175  269 ASN A CB    
2223 C  CG    . ASN A 269 ? 1.1755 1.2259 1.2767 -0.0543 -0.0086 0.0210  269 ASN A CG    
2224 O  OD1   . ASN A 269 ? 1.1663 1.2099 1.2724 -0.0540 -0.0072 0.0144  269 ASN A OD1   
2225 N  ND2   . ASN A 269 ? 1.1075 1.1586 1.2141 -0.0551 -0.0091 0.0315  269 ASN A ND2   
2226 N  N     . LEU A 270 ? 0.9225 0.9913 1.0074 -0.0598 -0.0022 0.0234  270 LEU A N     
2227 C  CA    . LEU A 270 ? 0.8416 0.9164 0.9279 -0.0622 0.0006  0.0325  270 LEU A CA    
2228 C  C     . LEU A 270 ? 0.7778 0.8465 0.8801 -0.0647 0.0014  0.0366  270 LEU A C     
2229 O  O     . LEU A 270 ? 0.8138 0.8746 0.9234 -0.0648 0.0005  0.0297  270 LEU A O     
2230 C  CB    . LEU A 270 ? 0.8981 0.9809 0.9766 -0.0625 0.0048  0.0295  270 LEU A CB    
2231 C  CG    . LEU A 270 ? 0.8291 0.9182 0.8902 -0.0605 0.0054  0.0265  270 LEU A CG    
2232 C  CD1   . LEU A 270 ? 0.8554 0.9532 0.9113 -0.0607 0.0114  0.0281  270 LEU A CD1   
2233 C  CD2   . LEU A 270 ? 0.7109 0.8019 0.7643 -0.0605 0.0019  0.0333  270 LEU A CD2   
2234 N  N     . PRO A 271 ? 0.7652 0.8370 0.8729 -0.0670 0.0028  0.0479  271 PRO A N     
2235 C  CA    . PRO A 271 ? 0.7757 0.8412 0.8999 -0.0701 0.0036  0.0517  271 PRO A CA    
2236 C  C     . PRO A 271 ? 0.8646 0.9312 0.9933 -0.0727 0.0055  0.0459  271 PRO A C     
2237 O  O     . PRO A 271 ? 0.7832 0.8407 0.9223 -0.0746 0.0040  0.0414  271 PRO A O     
2238 C  CB    . PRO A 271 ? 0.7305 0.8020 0.8579 -0.0720 0.0052  0.0664  271 PRO A CB    
2239 C  CG    . PRO A 271 ? 0.7673 0.8507 0.8774 -0.0703 0.0065  0.0685  271 PRO A CG    
2240 C  CD    . PRO A 271 ? 0.7086 0.7894 0.8080 -0.0670 0.0034  0.0580  271 PRO A CD    
2241 N  N     . THR A 272 ? 0.8642 0.9419 0.9852 -0.0727 0.0089  0.0460  272 THR A N     
2242 C  CA    . THR A 272 ? 0.7864 0.8675 0.9119 -0.0745 0.0107  0.0410  272 THR A CA    
2243 C  C     . THR A 272 ? 0.7937 0.8810 0.9057 -0.0708 0.0123  0.0330  272 THR A C     
2244 O  O     . THR A 272 ? 0.8135 0.9048 0.9120 -0.0680 0.0132  0.0336  272 THR A O     
2245 C  CB    . THR A 272 ? 0.8135 0.9033 0.9478 -0.0781 0.0147  0.0511  272 THR A CB    
2246 O  OG1   . THR A 272 ? 0.9643 1.0641 1.0878 -0.0762 0.0186  0.0590  272 THR A OG1   
2247 C  CG2   . THR A 272 ? 0.7404 0.8224 0.8912 -0.0825 0.0128  0.0582  272 THR A CG2   
2248 N  N     . TYR A 273 ? 0.7840 0.8716 0.8997 -0.0712 0.0122  0.0256  273 TYR A N     
2249 C  CA    . TYR A 273 ? 0.7323 0.8243 0.8379 -0.0676 0.0137  0.0178  273 TYR A CA    
2250 C  C     . TYR A 273 ? 0.7490 0.8518 0.8587 -0.0682 0.0185  0.0198  273 TYR A C     
2251 O  O     . TYR A 273 ? 0.7383 0.8432 0.8490 -0.0669 0.0187  0.0134  273 TYR A O     
2252 C  CB    . TYR A 273 ? 0.7469 0.8310 0.8529 -0.0664 0.0095  0.0077  273 TYR A CB    
2253 C  CG    . TYR A 273 ? 0.8919 0.9677 0.9915 -0.0642 0.0061  0.0051  273 TYR A CG    
2254 C  CD1   . TYR A 273 ? 0.8604 0.9383 0.9474 -0.0608 0.0063  0.0033  273 TYR A CD1   
2255 C  CD2   . TYR A 273 ? 0.9078 0.9737 1.0148 -0.0654 0.0029  0.0047  273 TYR A CD2   
2256 C  CE1   . TYR A 273 ? 0.8600 0.9318 0.9434 -0.0592 0.0029  0.0020  273 TYR A CE1   
2257 C  CE2   . TYR A 273 ? 0.9215 0.9812 1.0247 -0.0628 0.0006  0.0033  273 TYR A CE2   
2258 C  CZ    . TYR A 273 ? 0.9432 1.0066 1.0354 -0.0599 0.0004  0.0025  273 TYR A CZ    
2259 O  OH    . TYR A 273 ? 0.9477 1.0061 1.0381 -0.0577 -0.0023 0.0022  273 TYR A OH    
2260 N  N     . THR A 274 ? 0.6650 0.7755 0.7779 -0.0699 0.0227  0.0296  274 THR A N     
2261 C  CA    . THR A 274 ? 0.6512 0.7737 0.7675 -0.0694 0.0287  0.0328  274 THR A CA    
2262 C  C     . THR A 274 ? 0.6703 0.7980 0.7699 -0.0639 0.0335  0.0289  274 THR A C     
2263 O  O     . THR A 274 ? 0.6675 0.7915 0.7526 -0.0617 0.0325  0.0272  274 THR A O     
2264 C  CB    . THR A 274 ? 0.6419 0.7716 0.7676 -0.0730 0.0324  0.0456  274 THR A CB    
2265 O  OG1   . THR A 274 ? 0.6921 0.8246 0.8044 -0.0708 0.0355  0.0514  274 THR A OG1   
2266 C  CG2   . THR A 274 ? 0.6405 0.7618 0.7815 -0.0786 0.0271  0.0493  274 THR A CG2   
2267 N  N     . LEU A 275 ? 0.7053 0.8415 0.8075 -0.0617 0.0387  0.0274  275 LEU A N     
2268 C  CA    . LEU A 275 ? 0.6793 0.8192 0.7661 -0.0560 0.0441  0.0228  275 LEU A CA    
2269 C  C     . LEU A 275 ? 0.6574 0.8012 0.7301 -0.0548 0.0484  0.0287  275 LEU A C     
2270 O  O     . LEU A 275 ? 0.6172 0.7577 0.6719 -0.0515 0.0487  0.0232  275 LEU A O     
2271 C  CB    . LEU A 275 ? 0.6420 0.7919 0.7372 -0.0536 0.0503  0.0228  275 LEU A CB    
2272 C  CG    . LEU A 275 ? 0.6453 0.7975 0.7267 -0.0470 0.0566  0.0164  275 LEU A CG    
2273 C  CD1   . LEU A 275 ? 0.6195 0.7600 0.6882 -0.0448 0.0512  0.0056  275 LEU A CD1   
2274 C  CD2   . LEU A 275 ? 0.6121 0.7732 0.7063 -0.0445 0.0617  0.0164  275 LEU A CD2   
2275 N  N     . GLU A 276 ? 0.5837 0.7344 0.6642 -0.0578 0.0514  0.0402  276 GLU A N     
2276 C  CA    . GLU A 276 ? 0.7061 0.8616 0.7731 -0.0570 0.0554  0.0475  276 GLU A CA    
2277 C  C     . GLU A 276 ? 0.7584 0.9047 0.8140 -0.0579 0.0483  0.0459  276 GLU A C     
2278 O  O     . GLU A 276 ? 0.7319 0.8784 0.7679 -0.0553 0.0491  0.0438  276 GLU A O     
2279 C  CB    . GLU A 276 ? 0.6649 0.8294 0.7458 -0.0607 0.0592  0.0616  276 GLU A CB    
2280 C  CG    . GLU A 276 ? 0.7318 0.9088 0.8234 -0.0595 0.0677  0.0657  276 GLU A CG    
2281 C  CD    . GLU A 276 ? 0.7787 0.9543 0.8899 -0.0617 0.0642  0.0615  276 GLU A CD    
2282 O  OE1   . GLU A 276 ? 0.7699 0.9370 0.8923 -0.0666 0.0561  0.0608  276 GLU A OE1   
2283 O  OE2   . GLU A 276 ? 0.6980 0.8812 0.8133 -0.0585 0.0696  0.0590  276 GLU A OE2   
2284 N  N     . ALA A 277 ? 0.6990 0.8371 0.7666 -0.0616 0.0411  0.0469  277 ALA A N     
2285 C  CA    . ALA A 277 ? 0.6790 0.8092 0.7391 -0.0622 0.0346  0.0468  277 ALA A CA    
2286 C  C     . ALA A 277 ? 0.7243 0.8482 0.7707 -0.0589 0.0311  0.0349  277 ALA A C     
2287 O  O     . ALA A 277 ? 0.7382 0.8607 0.7704 -0.0581 0.0284  0.0347  277 ALA A O     
2288 C  CB    . ALA A 277 ? 0.5746 0.6965 0.6520 -0.0660 0.0289  0.0497  277 ALA A CB    
2289 N  N     . VAL A 278 ? 0.6874 0.8080 0.7386 -0.0575 0.0307  0.0255  278 VAL A N     
2290 C  CA    . VAL A 278 ? 0.6508 0.7653 0.6910 -0.0546 0.0277  0.0147  278 VAL A CA    
2291 C  C     . VAL A 278 ? 0.7206 0.8391 0.7417 -0.0514 0.0319  0.0118  278 VAL A C     
2292 O  O     . VAL A 278 ? 0.7533 0.8673 0.7609 -0.0505 0.0280  0.0072  278 VAL A O     
2293 C  CB    . VAL A 278 ? 0.6428 0.7543 0.6928 -0.0535 0.0271  0.0068  278 VAL A CB    
2294 C  CG1   . VAL A 278 ? 0.7014 0.8082 0.7403 -0.0501 0.0257  -0.0034 278 VAL A CG1   
2295 C  CG2   . VAL A 278 ? 0.6924 0.7973 0.7565 -0.0566 0.0216  0.0074  278 VAL A CG2   
2296 N  N     . TYR A 279 ? 0.7317 0.8587 0.7516 -0.0495 0.0400  0.0142  279 TYR A N     
2297 C  CA    . TYR A 279 ? 0.7652 0.8953 0.7655 -0.0460 0.0452  0.0108  279 TYR A CA    
2298 C  C     . TYR A 279 ? 0.7784 0.9103 0.7635 -0.0475 0.0433  0.0168  279 TYR A C     
2299 O  O     . TYR A 279 ? 0.7437 0.8723 0.7099 -0.0462 0.0414  0.0108  279 TYR A O     
2300 C  CB    . TYR A 279 ? 0.6664 0.8064 0.6704 -0.0432 0.0555  0.0137  279 TYR A CB    
2301 C  CG    . TYR A 279 ? 0.6668 0.8098 0.6497 -0.0387 0.0626  0.0099  279 TYR A CG    
2302 C  CD1   . TYR A 279 ? 0.6427 0.7792 0.6151 -0.0347 0.0636  -0.0023 279 TYR A CD1   
2303 C  CD2   . TYR A 279 ? 0.7575 0.9095 0.7306 -0.0385 0.0687  0.0185  279 TYR A CD2   
2304 C  CE1   . TYR A 279 ? 0.5961 0.7335 0.5480 -0.0304 0.0703  -0.0071 279 TYR A CE1   
2305 C  CE2   . TYR A 279 ? 0.7705 0.9246 0.7219 -0.0341 0.0757  0.0142  279 TYR A CE2   
2306 C  CZ    . TYR A 279 ? 0.7094 0.8556 0.6500 -0.0301 0.0764  0.0007  279 TYR A CZ    
2307 O  OH    . TYR A 279 ? 0.8539 1.0005 0.7718 -0.0256 0.0836  -0.0049 279 TYR A OH    
2308 N  N     . GLU A 280 ? 0.7306 0.8677 0.7241 -0.0507 0.0432  0.0290  280 GLU A N     
2309 C  CA    . GLU A 280 ? 0.9036 1.0436 0.8839 -0.0523 0.0411  0.0367  280 GLU A CA    
2310 C  C     . GLU A 280 ? 0.8557 0.9875 0.8316 -0.0540 0.0310  0.0335  280 GLU A C     
2311 O  O     . GLU A 280 ? 0.8830 1.0164 0.8426 -0.0547 0.0279  0.0359  280 GLU A O     
2312 C  CB    . GLU A 280 ? 1.0170 1.1639 1.0107 -0.0554 0.0432  0.0515  280 GLU A CB    
2313 C  CG    . GLU A 280 ? 1.0607 1.2144 1.0398 -0.0562 0.0437  0.0619  280 GLU A CG    
2314 C  CD    . GLU A 280 ? 1.1870 1.3464 1.1822 -0.0596 0.0451  0.0776  280 GLU A CD    
2315 O  OE1   . GLU A 280 ? 1.2603 1.4134 1.2754 -0.0623 0.0404  0.0800  280 GLU A OE1   
2316 O  OE2   . GLU A 280 ? 1.2166 1.3864 1.2043 -0.0593 0.0511  0.0876  280 GLU A OE2   
2317 N  N     . ALA A 281 ? 0.8082 0.9319 0.7981 -0.0548 0.0258  0.0286  281 ALA A N     
2318 C  CA    . ALA A 281 ? 0.7854 0.9021 0.7731 -0.0560 0.0170  0.0259  281 ALA A CA    
2319 C  C     . ALA A 281 ? 0.8622 0.9745 0.8345 -0.0540 0.0147  0.0141  281 ALA A C     
2320 O  O     . ALA A 281 ? 0.8422 0.9529 0.8031 -0.0552 0.0086  0.0136  281 ALA A O     
2321 C  CB    . ALA A 281 ? 0.7124 0.8221 0.7201 -0.0570 0.0131  0.0252  281 ALA A CB    
2322 N  N     . VAL A 282 ? 0.8922 1.0024 0.8649 -0.0513 0.0192  0.0050  282 VAL A N     
2323 C  CA    . VAL A 282 ? 0.7840 0.8881 0.7445 -0.0495 0.0171  -0.0066 282 VAL A CA    
2324 C  C     . VAL A 282 ? 0.7834 0.8903 0.7208 -0.0483 0.0201  -0.0091 282 VAL A C     
2325 O  O     . VAL A 282 ? 0.8376 0.9396 0.7609 -0.0489 0.0150  -0.0156 282 VAL A O     
2326 C  CB    . VAL A 282 ? 0.7445 0.8453 0.7148 -0.0466 0.0208  -0.0147 282 VAL A CB    
2327 C  CG1   . VAL A 282 ? 0.7401 0.8339 0.6988 -0.0446 0.0191  -0.0261 282 VAL A CG1   
2328 C  CG2   . VAL A 282 ? 0.7171 0.8145 0.7070 -0.0481 0.0168  -0.0131 282 VAL A CG2   
2329 N  N     . PHE A 283 ? 0.8198 0.9347 0.7525 -0.0468 0.0284  -0.0040 283 PHE A N     
2330 C  CA    . PHE A 283 ? 0.8475 0.9648 0.7568 -0.0446 0.0333  -0.0076 283 PHE A CA    
2331 C  C     . PHE A 283 ? 0.9568 1.0829 0.8545 -0.0465 0.0342  0.0034  283 PHE A C     
2332 O  O     . PHE A 283 ? 0.9658 1.0937 0.8404 -0.0452 0.0371  0.0004  283 PHE A O     
2333 C  CB    . PHE A 283 ? 0.7638 0.8837 0.6740 -0.0397 0.0445  -0.0123 283 PHE A CB    
2334 C  CG    . PHE A 283 ? 0.7754 0.8868 0.6923 -0.0371 0.0442  -0.0238 283 PHE A CG    
2335 C  CD1   . PHE A 283 ? 0.8392 0.9420 0.7396 -0.0353 0.0429  -0.0357 283 PHE A CD1   
2336 C  CD2   . PHE A 283 ? 0.7527 0.8644 0.6925 -0.0367 0.0447  -0.0226 283 PHE A CD2   
2337 C  CE1   . PHE A 283 ? 0.8715 0.9664 0.7794 -0.0328 0.0427  -0.0452 283 PHE A CE1   
2338 C  CE2   . PHE A 283 ? 0.7445 0.8493 0.6905 -0.0343 0.0443  -0.0319 283 PHE A CE2   
2339 C  CZ    . PHE A 283 ? 0.8211 0.9176 0.7520 -0.0322 0.0436  -0.0428 283 PHE A CZ    
2340 N  N     . GLY A 284 ? 0.9901 1.1212 0.9024 -0.0494 0.0320  0.0160  284 GLY A N     
2341 C  CA    . GLY A 284 ? 1.0600 1.1999 0.9634 -0.0513 0.0323  0.0282  284 GLY A CA    
2342 C  C     . GLY A 284 ? 1.0856 1.2358 0.9866 -0.0491 0.0437  0.0354  284 GLY A C     
2343 O  O     . GLY A 284 ? 1.1650 1.3235 1.0659 -0.0510 0.0447  0.0487  284 GLY A O     
2344 N  N     . GLN A 285 ? 1.0534 1.2040 0.9536 -0.0449 0.0526  0.0279  285 GLN A N     
2345 C  CA    . GLN A 285 ? 1.1132 1.2754 1.0125 -0.0427 0.0640  0.0365  285 GLN A CA    
2346 C  C     . GLN A 285 ? 1.1289 1.2955 1.0575 -0.0439 0.0672  0.0446  285 GLN A C     
2347 O  O     . GLN A 285 ? 1.1695 1.3299 1.1145 -0.0439 0.0648  0.0381  285 GLN A O     
2348 C  CB    . GLN A 285 ? 1.1071 1.2697 0.9901 -0.0369 0.0737  0.0261  285 GLN A CB    
2349 C  CG    . GLN A 285 ? 1.1931 1.3541 1.0430 -0.0357 0.0734  0.0204  285 GLN A CG    
2350 C  CD    . GLN A 285 ? 1.2875 1.4572 1.1259 -0.0390 0.0711  0.0337  285 GLN A CD    
2351 O  OE1   . GLN A 285 ? 1.2959 1.4767 1.1271 -0.0370 0.0806  0.0424  285 GLN A OE1   
2352 N  NE2   . GLN A 285 ? 1.3242 1.4897 1.1609 -0.0438 0.0586  0.0359  285 GLN A NE2   
2353 N  N     . PRO A 286 ? 1.0749 1.2523 1.0105 -0.0454 0.0723  0.0591  286 PRO A N     
2354 C  CA    . PRO A 286 ? 1.0055 1.1864 0.9697 -0.0477 0.0742  0.0674  286 PRO A CA    
2355 C  C     . PRO A 286 ? 0.9588 1.1441 0.9325 -0.0440 0.0832  0.0628  286 PRO A C     
2356 O  O     . PRO A 286 ? 0.9162 1.1040 0.8742 -0.0388 0.0908  0.0559  286 PRO A O     
2357 C  CB    . PRO A 286 ? 0.9592 1.1510 0.9254 -0.0501 0.0778  0.0847  286 PRO A CB    
2358 C  CG    . PRO A 286 ? 1.0646 1.2625 1.0015 -0.0466 0.0834  0.0842  286 PRO A CG    
2359 C  CD    . PRO A 286 ? 1.0822 1.2689 0.9993 -0.0452 0.0763  0.0690  286 PRO A CD    
2360 N  N     . LYS A 287 ? 0.8672 1.0532 0.8673 -0.0468 0.0821  0.0666  287 LYS A N     
2361 C  CA    . LYS A 287 ? 0.7993 0.9909 0.8134 -0.0442 0.0893  0.0644  287 LYS A CA    
2362 C  C     . LYS A 287 ? 0.7875 0.9877 0.8271 -0.0486 0.0911  0.0781  287 LYS A C     
2363 O  O     . LYS A 287 ? 0.7716 0.9656 0.8266 -0.0540 0.0829  0.0811  287 LYS A O     
2364 C  CB    . LYS A 287 ? 0.7509 0.9324 0.7717 -0.0433 0.0836  0.0512  287 LYS A CB    
2365 C  CG    . LYS A 287 ? 0.7550 0.9429 0.7905 -0.0403 0.0903  0.0492  287 LYS A CG    
2366 C  CD    . LYS A 287 ? 0.7109 0.8913 0.7637 -0.0428 0.0823  0.0429  287 LYS A CD    
2367 C  CE    . LYS A 287 ? 0.6989 0.8859 0.7645 -0.0393 0.0882  0.0403  287 LYS A CE    
2368 N  NZ    . LYS A 287 ? 0.7686 0.9640 0.8604 -0.0440 0.0877  0.0500  287 LYS A NZ    
2369 N  N     . GLU A 288 ? 0.7938 1.0076 0.8380 -0.0464 0.1021  0.0862  288 GLU A N     
2370 C  CA    . GLU A 288 ? 0.7655 0.9887 0.8349 -0.0511 0.1042  0.1004  288 GLU A CA    
2371 C  C     . GLU A 288 ? 0.7409 0.9608 0.8350 -0.0542 0.0989  0.0963  288 GLU A C     
2372 O  O     . GLU A 288 ? 0.7518 0.9705 0.8463 -0.0505 0.1002  0.0862  288 GLU A O     
2373 C  CB    . GLU A 288 ? 0.8252 1.0653 0.8944 -0.0474 0.1180  0.1102  288 GLU A CB    
2374 C  CG    . GLU A 288 ? 0.9164 1.1677 1.0119 -0.0528 0.1206  0.1270  288 GLU A CG    
2375 C  CD    . GLU A 288 ? 1.0514 1.3206 1.1451 -0.0489 0.1350  0.1387  288 GLU A CD    
2376 O  OE1   . GLU A 288 ? 1.1501 1.4259 1.2396 -0.0424 0.1442  0.1333  288 GLU A OE1   
2377 O  OE2   . GLU A 288 ? 1.0936 1.3705 1.1907 -0.0521 0.1377  0.1538  288 GLU A OE2   
2378 N  N     . LYS A 289 ? 0.7545 0.9724 0.8691 -0.0613 0.0927  0.1043  289 LYS A N     
2379 C  CA    . LYS A 289 ? 0.7690 0.9839 0.9070 -0.0656 0.0868  0.1016  289 LYS A CA    
2380 C  C     . LYS A 289 ? 0.7375 0.9670 0.8990 -0.0688 0.0927  0.1147  289 LYS A C     
2381 O  O     . LYS A 289 ? 0.7663 1.0026 0.9332 -0.0717 0.0962  0.1284  289 LYS A O     
2382 C  CB    . LYS A 289 ? 0.7038 0.9042 0.8485 -0.0716 0.0750  0.0996  289 LYS A CB    
2383 C  CG    . LYS A 289 ? 0.7058 0.9039 0.8761 -0.0779 0.0690  0.1003  289 LYS A CG    
2384 C  CD    . LYS A 289 ? 0.6967 0.8935 0.8696 -0.0757 0.0667  0.0885  289 LYS A CD    
2385 C  CE    . LYS A 289 ? 0.7649 0.9493 0.9492 -0.0812 0.0556  0.0819  289 LYS A CE    
2386 N  NZ    . LYS A 289 ? 0.5314 0.7201 0.7275 -0.0816 0.0537  0.0764  289 LYS A NZ    
2387 N  N     . VAL A 290 ? 0.7068 0.9419 0.8832 -0.0685 0.0935  0.1115  290 VAL A N     
2388 C  CA    . VAL A 290 ? 0.7520 1.0010 0.9548 -0.0725 0.0972  0.1235  290 VAL A CA    
2389 C  C     . VAL A 290 ? 0.7342 0.9758 0.9574 -0.0798 0.0857  0.1196  290 VAL A C     
2390 O  O     . VAL A 290 ? 0.7071 0.9423 0.9275 -0.0780 0.0806  0.1074  290 VAL A O     
2391 C  CB    . VAL A 290 ? 0.7081 0.9728 0.9129 -0.0657 0.1088  0.1249  290 VAL A CB    
2392 C  CG1   . VAL A 290 ? 0.7633 1.0439 0.9983 -0.0705 0.1120  0.1385  290 VAL A CG1   
2393 C  CG2   . VAL A 290 ? 0.7332 1.0037 0.9143 -0.0582 0.1205  0.1270  290 VAL A CG2   
2394 N  N     . TYR A 291 ? 0.7473 0.9892 0.9903 -0.0881 0.0815  0.1298  291 TYR A N     
2395 C  CA    . TYR A 291 ? 0.7669 0.9991 1.0269 -0.0959 0.0696  0.1255  291 TYR A CA    
2396 C  C     . TYR A 291 ? 0.7167 0.9617 1.0000 -0.0989 0.0695  0.1287  291 TYR A C     
2397 O  O     . TYR A 291 ? 0.7566 1.0194 1.0484 -0.0960 0.0792  0.1380  291 TYR A O     
2398 C  CB    . TYR A 291 ? 0.7567 0.9811 1.0276 -0.1038 0.0646  0.1343  291 TYR A CB    
2399 C  CG    . TYR A 291 ? 0.7363 0.9497 0.9867 -0.1009 0.0645  0.1331  291 TYR A CG    
2400 C  CD1   . TYR A 291 ? 0.7460 0.9683 0.9872 -0.0976 0.0734  0.1442  291 TYR A CD1   
2401 C  CD2   . TYR A 291 ? 0.7309 0.9259 0.9709 -0.1012 0.0556  0.1214  291 TYR A CD2   
2402 C  CE1   . TYR A 291 ? 0.7873 1.0007 1.0101 -0.0953 0.0724  0.1440  291 TYR A CE1   
2403 C  CE2   . TYR A 291 ? 0.7436 0.9298 0.9668 -0.0985 0.0551  0.1213  291 TYR A CE2   
2404 C  CZ    . TYR A 291 ? 0.7693 0.9650 0.9842 -0.0958 0.0630  0.1327  291 TYR A CZ    
2405 O  OH    . TYR A 291 ? 0.7830 0.9711 0.9816 -0.0936 0.0617  0.1334  291 TYR A OH    
2406 N  N     . ALA A 292 ? 0.7185 0.9547 1.0120 -0.1047 0.0582  0.1211  292 ALA A N     
2407 C  CA    . ALA A 292 ? 0.7482 0.9957 1.0618 -0.1075 0.0559  0.1222  292 ALA A CA    
2408 C  C     . ALA A 292 ? 0.8487 1.1117 1.1895 -0.1139 0.0590  0.1387  292 ALA A C     
2409 O  O     . ALA A 292 ? 0.8523 1.1324 1.2092 -0.1132 0.0628  0.1443  292 ALA A O     
2410 C  CB    . ALA A 292 ? 0.7063 0.9402 1.0232 -0.1133 0.0421  0.1108  292 ALA A CB    
2411 N  N     . GLU A 293 ? 0.8313 1.0893 1.1794 -0.1203 0.0575  0.1474  293 GLU A N     
2412 C  CA    . GLU A 293 ? 0.7827 1.0553 1.1579 -0.1269 0.0605  0.1644  293 GLU A CA    
2413 C  C     . GLU A 293 ? 0.6923 0.9861 1.0674 -0.1194 0.0760  0.1758  293 GLU A C     
2414 O  O     . GLU A 293 ? 0.7102 1.0226 1.1083 -0.1213 0.0802  0.1864  293 GLU A O     
2415 C  CB    . GLU A 293 ? 0.9152 1.1766 1.2965 -0.1342 0.0568  0.1718  293 GLU A CB    
2416 C  CG    . GLU A 293 ? 0.9344 1.1747 1.3208 -0.1430 0.0421  0.1624  293 GLU A CG    
2417 C  CD    . GLU A 293 ? 1.0877 1.3111 1.4506 -0.1384 0.0356  0.1433  293 GLU A CD    
2418 O  OE1   . GLU A 293 ? 1.1551 1.3648 1.5228 -0.1447 0.0241  0.1340  293 GLU A OE1   
2419 O  OE2   . GLU A 293 ? 1.1825 1.4059 1.5220 -0.1287 0.0420  0.1376  293 GLU A OE2   
2420 N  N     . GLU A 294 ? 0.7185 1.0101 1.0678 -0.1106 0.0847  0.1737  294 GLU A N     
2421 C  CA    . GLU A 294 ? 0.7579 1.0679 1.1022 -0.1024 0.1002  0.1828  294 GLU A CA    
2422 C  C     . GLU A 294 ? 0.7529 1.0758 1.1029 -0.0966 0.1050  0.1789  294 GLU A C     
2423 O  O     . GLU A 294 ? 0.7051 1.0481 1.0723 -0.0950 0.1146  0.1911  294 GLU A O     
2424 C  CB    . GLU A 294 ? 0.7557 1.0581 1.0670 -0.0943 0.1064  0.1776  294 GLU A CB    
2425 C  CG    . GLU A 294 ? 0.8209 1.1095 1.1248 -0.0991 0.1008  0.1805  294 GLU A CG    
2426 C  CD    . GLU A 294 ? 0.9295 1.2132 1.2014 -0.0912 0.1066  0.1766  294 GLU A CD    
2427 O  OE1   . GLU A 294 ? 0.9760 1.2727 1.2411 -0.0870 0.1182  0.1874  294 GLU A OE1   
2428 O  OE2   . GLU A 294 ? 0.8642 1.1314 1.1175 -0.0894 0.0993  0.1629  294 GLU A OE2   
2429 N  N     . ILE A 295 ? 0.7204 1.0324 1.0573 -0.0931 0.0988  0.1627  295 ILE A N     
2430 C  CA    . ILE A 295 ? 0.7185 1.0418 1.0597 -0.0865 0.1037  0.1590  295 ILE A CA    
2431 C  C     . ILE A 295 ? 0.7121 1.0477 1.0867 -0.0940 0.0977  0.1663  295 ILE A C     
2432 O  O     . ILE A 295 ? 0.6830 1.0367 1.0721 -0.0897 0.1055  0.1726  295 ILE A O     
2433 C  CB    . ILE A 295 ? 0.7478 1.0558 1.0661 -0.0807 0.0987  0.1405  295 ILE A CB    
2434 C  CG1   . ILE A 295 ? 0.7934 1.0887 1.1191 -0.0887 0.0826  0.1319  295 ILE A CG1   
2435 C  CG2   . ILE A 295 ? 0.7217 1.0158 1.0090 -0.0759 0.1014  0.1335  295 ILE A CG2   
2436 C  CD1   . ILE A 295 ? 0.7958 1.0886 1.1159 -0.0836 0.0794  0.1200  295 ILE A CD1   
2437 N  N     . THR A 296 ? 0.7490 1.0753 1.1370 -0.1053 0.0841  0.1662  296 THR A N     
2438 C  CA    . THR A 296 ? 0.7198 1.0576 1.1398 -0.1141 0.0769  0.1737  296 THR A CA    
2439 C  C     . THR A 296 ? 0.6834 1.0429 1.1279 -0.1161 0.0868  0.1935  296 THR A C     
2440 O  O     . THR A 296 ? 0.6741 1.0531 1.1414 -0.1158 0.0899  0.2015  296 THR A O     
2441 C  CB    . THR A 296 ? 0.7562 1.0770 1.1826 -0.1261 0.0605  0.1684  296 THR A CB    
2442 O  OG1   . THR A 296 ? 0.7910 1.0953 1.1984 -0.1241 0.0515  0.1508  296 THR A OG1   
2443 C  CG2   . THR A 296 ? 0.7696 1.1026 1.2303 -0.1370 0.0526  0.1781  296 THR A CG2   
2444 N  N     . THR A 297 ? 0.6050 0.9627 1.0464 -0.1180 0.0920  0.2026  297 THR A N     
2445 C  CA    . THR A 297 ? 0.7254 1.1045 1.1892 -0.1194 0.1026  0.2226  297 THR A CA    
2446 C  C     . THR A 297 ? 0.7286 1.1259 1.1854 -0.1065 0.1200  0.2266  297 THR A C     
2447 O  O     . THR A 297 ? 0.6267 1.0464 1.1083 -0.1061 0.1280  0.2408  297 THR A O     
2448 C  CB    . THR A 297 ? 0.6320 1.0046 1.0923 -0.1237 0.1046  0.2319  297 THR A CB    
2449 O  OG1   . THR A 297 ? 0.8540 1.2189 1.2805 -0.1138 0.1132  0.2258  297 THR A OG1   
2450 C  CG2   . THR A 297 ? 0.6231 0.9753 1.0896 -0.1356 0.0879  0.2266  297 THR A CG2   
2451 N  N     . ALA A 298 ? 0.7280 1.1156 1.1518 -0.0958 0.1261  0.2142  298 ALA A N     
2452 C  CA    . ALA A 298 ? 0.7175 1.1191 1.1313 -0.0829 0.1428  0.2158  298 ALA A CA    
2453 C  C     . ALA A 298 ? 0.6295 1.0434 1.0609 -0.0794 0.1433  0.2139  298 ALA A C     
2454 O  O     . ALA A 298 ? 0.6534 1.0865 1.0939 -0.0716 0.1576  0.2225  298 ALA A O     
2455 C  CB    . ALA A 298 ? 0.6443 1.0299 1.0184 -0.0736 0.1467  0.2010  298 ALA A CB    
2456 N  N     . TRP A 299 ? 0.6115 1.0151 1.0480 -0.0847 0.1284  0.2033  299 TRP A N     
2457 C  CA    . TRP A 299 ? 0.6563 1.0720 1.1110 -0.0821 0.1271  0.2026  299 TRP A CA    
2458 C  C     . TRP A 299 ? 0.6796 1.1159 1.1745 -0.0911 0.1244  0.2196  299 TRP A C     
2459 O  O     . TRP A 299 ? 0.7831 1.2405 1.2978 -0.0859 0.1331  0.2286  299 TRP A O     
2460 C  CB    . TRP A 299 ? 0.6875 1.0854 1.1319 -0.0848 0.1118  0.1859  299 TRP A CB    
2461 C  CG    . TRP A 299 ? 0.6724 1.0812 1.1315 -0.0811 0.1102  0.1842  299 TRP A CG    
2462 C  CD1   . TRP A 299 ? 0.6822 1.0997 1.1686 -0.0899 0.0983  0.1886  299 TRP A CD1   
2463 C  CD2   . TRP A 299 ? 0.7368 1.1484 1.1841 -0.0679 0.1202  0.1775  299 TRP A CD2   
2464 N  NE1   . TRP A 299 ? 0.6394 1.0664 1.1325 -0.0826 0.1004  0.1863  299 TRP A NE1   
2465 C  CE2   . TRP A 299 ? 0.6861 1.1091 1.1560 -0.0689 0.1141  0.1794  299 TRP A CE2   
2466 C  CE3   . TRP A 299 ? 0.7635 1.1686 1.1832 -0.0556 0.1334  0.1701  299 TRP A CE3   
2467 C  CZ2   . TRP A 299 ? 0.7184 1.1464 1.1857 -0.0574 0.1214  0.1749  299 TRP A CZ2   
2468 C  CZ3   . TRP A 299 ? 0.7809 1.1895 1.1972 -0.0445 0.1406  0.1643  299 TRP A CZ3   
2469 C  CH2   . TRP A 299 ? 0.7226 1.1424 1.1632 -0.0453 0.1348  0.1670  299 TRP A CH2   
2470 N  N     . GLU A 300 ? 0.7755 1.2057 1.2839 -0.1045 0.1120  0.2241  300 GLU A N     
2471 C  CA    . GLU A 300 ? 0.7407 1.1890 1.2883 -0.1148 0.1072  0.2397  300 GLU A CA    
2472 C  C     . GLU A 300 ? 0.6726 1.1440 1.2375 -0.1115 0.1238  0.2595  300 GLU A C     
2473 O  O     . GLU A 300 ? 0.7826 1.2766 1.3808 -0.1144 0.1258  0.2735  300 GLU A O     
2474 C  CB    . GLU A 300 ? 0.8222 1.2556 1.3783 -0.1301 0.0901  0.2386  300 GLU A CB    
2475 C  CG    . GLU A 300 ? 0.9422 1.3552 1.4855 -0.1345 0.0730  0.2204  300 GLU A CG    
2476 C  CD    . GLU A 300 ? 0.9886 1.3865 1.5411 -0.1495 0.0569  0.2189  300 GLU A CD    
2477 O  OE1   . GLU A 300 ? 0.9274 1.3177 1.4775 -0.1532 0.0593  0.2246  300 GLU A OE1   
2478 O  OE2   . GLU A 300 ? 1.0022 1.3954 1.5637 -0.1574 0.0418  0.2121  300 GLU A OE2   
2479 N  N     . THR A 301 ? 0.6753 1.1423 1.2184 -0.1054 0.1359  0.2616  301 THR A N     
2480 C  CA    . THR A 301 ? 0.6399 1.1284 1.1956 -0.1015 0.1529  0.2804  301 THR A CA    
2481 C  C     . THR A 301 ? 0.7366 1.2364 1.2765 -0.0849 0.1722  0.2791  301 THR A C     
2482 O  O     . THR A 301 ? 0.7212 1.2436 1.2768 -0.0803 0.1875  0.2952  301 THR A O     
2483 C  CB    . THR A 301 ? 0.6988 1.1779 1.2421 -0.1056 0.1549  0.2862  301 THR A CB    
2484 O  OG1   . THR A 301 ? 0.7288 1.1855 1.2317 -0.0993 0.1542  0.2695  301 THR A OG1   
2485 C  CG2   . THR A 301 ? 0.7443 1.2156 1.3104 -0.1221 0.1383  0.2915  301 THR A CG2   
2486 N  N     . GLY A 302 ? 0.7588 1.2434 1.2687 -0.0759 0.1721  0.2605  302 GLY A N     
2487 C  CA    . GLY A 302 ? 0.7242 1.2165 1.2183 -0.0603 0.1896  0.2572  302 GLY A CA    
2488 C  C     . GLY A 302 ? 0.6798 1.1694 1.1443 -0.0521 0.2046  0.2580  302 GLY A C     
2489 O  O     . GLY A 302 ? 0.8020 1.3010 1.2559 -0.0392 0.2215  0.2579  302 GLY A O     
2490 N  N     . GLU A 303 ? 0.6473 1.1242 1.0978 -0.0588 0.1989  0.2586  303 GLU A N     
2491 C  CA    . GLU A 303 ? 0.6992 1.1738 1.1208 -0.0523 0.2114  0.2604  303 GLU A CA    
2492 C  C     . GLU A 303 ? 0.7644 1.2122 1.1491 -0.0515 0.2025  0.2419  303 GLU A C     
2493 O  O     . GLU A 303 ? 0.7673 1.1984 1.1528 -0.0590 0.1857  0.2317  303 GLU A O     
2494 C  CB    . GLU A 303 ? 0.7556 1.2410 1.1935 -0.0604 0.2140  0.2804  303 GLU A CB    
2495 C  CG    . GLU A 303 ? 0.7954 1.2731 1.2579 -0.0762 0.1953  0.2843  303 GLU A CG    
2496 C  CD    . GLU A 303 ? 0.9855 1.4744 1.4682 -0.0844 0.1981  0.3054  303 GLU A CD    
2497 O  OE1   . GLU A 303 ? 0.8209 1.3331 1.3178 -0.0801 0.2137  0.3220  303 GLU A OE1   
2498 O  OE2   . GLU A 303 ? 1.0608 1.5351 1.5458 -0.0950 0.1852  0.3057  303 GLU A OE2   
2499 N  N     . ASN A 304 ? 0.8044 1.2486 1.1562 -0.0423 0.2142  0.2378  304 ASN A N     
2500 C  CA    . ASN A 304 ? 0.8936 1.3146 1.2094 -0.0411 0.2071  0.2221  304 ASN A CA    
2501 C  C     . ASN A 304 ? 0.8934 1.2980 1.1992 -0.0386 0.1973  0.2021  304 ASN A C     
2502 O  O     . ASN A 304 ? 0.8655 1.2498 1.1530 -0.0420 0.1854  0.1899  304 ASN A O     
2503 C  CB    . ASN A 304 ? 1.0005 1.4107 1.3181 -0.0526 0.1946  0.2272  304 ASN A CB    
2504 C  CG    . ASN A 304 ? 1.1991 1.6075 1.4901 -0.0499 0.2019  0.2322  304 ASN A CG    
2505 O  OD1   . ASN A 304 ? 1.1358 1.5393 1.3947 -0.0406 0.2094  0.2224  304 ASN A OD1   
2506 N  ND2   . ASN A 304 ? 1.2340 1.6464 1.5385 -0.0583 0.1993  0.2476  304 ASN A ND2   
2507 N  N     . LEU A 305 ? 0.7748 1.1887 1.0936 -0.0324 0.2027  0.1995  305 LEU A N     
2508 C  CA    . LEU A 305 ? 0.7275 1.1275 1.0394 -0.0299 0.1939  0.1823  305 LEU A CA    
2509 C  C     . LEU A 305 ? 0.7062 1.0907 0.9797 -0.0204 0.1986  0.1660  305 LEU A C     
2510 O  O     . LEU A 305 ? 0.6893 1.0569 0.9511 -0.0203 0.1884  0.1508  305 LEU A O     
2511 C  CB    . LEU A 305 ? 0.7165 1.1321 1.0553 -0.0258 0.1985  0.1859  305 LEU A CB    
2512 C  CG    . LEU A 305 ? 0.7215 1.1450 1.0968 -0.0369 0.1856  0.1942  305 LEU A CG    
2513 C  CD1   . LEU A 305 ? 0.7298 1.1706 1.1306 -0.0316 0.1911  0.1987  305 LEU A CD1   
2514 C  CD2   . LEU A 305 ? 0.5607 0.9630 0.9288 -0.0452 0.1660  0.1812  305 LEU A CD2   
2515 N  N     . GLU A 306 ? 0.7071 1.0969 0.9603 -0.0125 0.2136  0.1689  306 GLU A N     
2516 C  CA    . GLU A 306 ? 0.7418 1.1164 0.9571 -0.0043 0.2175  0.1532  306 GLU A CA    
2517 C  C     . GLU A 306 ? 0.8444 1.1987 1.0387 -0.0112 0.2030  0.1444  306 GLU A C     
2518 O  O     . GLU A 306 ? 0.7929 1.1304 0.9635 -0.0076 0.1986  0.1282  306 GLU A O     
2519 C  CB    . GLU A 306 ? 0.8625 1.2477 1.0595 0.0045  0.2362  0.1591  306 GLU A CB    
2520 C  CG    . GLU A 306 ? 1.0252 1.4359 1.2504 0.0073  0.2502  0.1768  306 GLU A CG    
2521 C  CD    . GLU A 306 ? 1.1479 1.5679 1.3538 0.0200  0.2713  0.1778  306 GLU A CD    
2522 O  OE1   . GLU A 306 ? 1.2756 1.6848 1.4451 0.0238  0.2747  0.1696  306 GLU A OE1   
2523 O  OE2   . GLU A 306 ? 1.0155 1.4539 1.2426 0.0263  0.2846  0.1869  306 GLU A OE2   
2524 N  N     . ARG A 307 ? 0.9025 1.2581 1.1070 -0.0211 0.1954  0.1552  307 ARG A N     
2525 C  CA    . ARG A 307 ? 0.7659 1.1030 0.9549 -0.0277 0.1814  0.1482  307 ARG A CA    
2526 C  C     . ARG A 307 ? 0.7364 1.0591 0.9323 -0.0315 0.1668  0.1354  307 ARG A C     
2527 O  O     . ARG A 307 ? 0.6699 0.9751 0.8442 -0.0311 0.1589  0.1221  307 ARG A O     
2528 C  CB    . ARG A 307 ? 0.7706 1.1128 0.9737 -0.0372 0.1773  0.1639  307 ARG A CB    
2529 C  CG    . ARG A 307 ? 0.8948 1.2190 1.0890 -0.0448 0.1624  0.1590  307 ARG A CG    
2530 C  CD    . ARG A 307 ? 0.8359 1.1659 1.0474 -0.0535 0.1599  0.1760  307 ARG A CD    
2531 N  NE    . ARG A 307 ? 0.8912 1.2039 1.0967 -0.0603 0.1463  0.1722  307 ARG A NE    
2532 C  CZ    . ARG A 307 ? 0.9690 1.2727 1.1482 -0.0586 0.1450  0.1693  307 ARG A CZ    
2533 N  NH1   . ARG A 307 ? 1.0602 1.3696 1.2141 -0.0509 0.1558  0.1689  307 ARG A NH1   
2534 N  NH2   . ARG A 307 ? 0.9827 1.2714 1.1609 -0.0647 0.1326  0.1666  307 ARG A NH2   
2535 N  N     . VAL A 308 ? 0.6934 1.0240 0.9192 -0.0351 0.1630  0.1395  308 VAL A N     
2536 C  CA    . VAL A 308 ? 0.6769 0.9955 0.9091 -0.0385 0.1496  0.1281  308 VAL A CA    
2537 C  C     . VAL A 308 ? 0.6635 0.9752 0.8789 -0.0288 0.1534  0.1136  308 VAL A C     
2538 O  O     . VAL A 308 ? 0.6448 0.9405 0.8492 -0.0296 0.1434  0.1006  308 VAL A O     
2539 C  CB    . VAL A 308 ? 0.5969 0.9273 0.8649 -0.0451 0.1443  0.1370  308 VAL A CB    
2540 C  CG1   . VAL A 308 ? 0.4628 0.7804 0.7355 -0.0497 0.1294  0.1258  308 VAL A CG1   
2541 C  CG2   . VAL A 308 ? 0.6241 0.9617 0.9098 -0.0545 0.1421  0.1523  308 VAL A CG2   
2542 N  N     . ALA A 309 ? 0.6390 0.9624 0.8529 -0.0194 0.1683  0.1159  309 ALA A N     
2543 C  CA    . ALA A 309 ? 0.6591 0.9745 0.8562 -0.0097 0.1732  0.1020  309 ALA A CA    
2544 C  C     . ALA A 309 ? 0.6198 0.9172 0.7816 -0.0076 0.1708  0.0896  309 ALA A C     
2545 O  O     . ALA A 309 ? 0.6193 0.9020 0.7687 -0.0053 0.1648  0.0757  309 ALA A O     
2546 C  CB    . ALA A 309 ? 0.6640 0.9950 0.8655 0.0006  0.1912  0.1073  309 ALA A CB    
2547 N  N     . ARG A 310 ? 0.6196 0.9184 0.7654 -0.0087 0.1752  0.0953  310 ARG A N     
2548 C  CA    . ARG A 310 ? 0.6615 0.9444 0.7751 -0.0083 0.1711  0.0852  310 ARG A CA    
2549 C  C     . ARG A 310 ? 0.6827 0.9502 0.7968 -0.0162 0.1538  0.0785  310 ARG A C     
2550 O  O     . ARG A 310 ? 0.6557 0.9080 0.7499 -0.0143 0.1483  0.0652  310 ARG A O     
2551 C  CB    . ARG A 310 ? 0.7474 1.0371 0.8477 -0.0096 0.1772  0.0956  310 ARG A CB    
2552 C  CG    . ARG A 310 ? 0.7819 1.0717 0.8521 -0.0005 0.1900  0.0904  310 ARG A CG    
2553 C  CD    . ARG A 310 ? 0.9305 1.2193 0.9786 -0.0035 0.1894  0.0959  310 ARG A CD    
2554 N  NE    . ARG A 310 ? 1.0200 1.3176 1.0887 -0.0121 0.1849  0.1123  310 ARG A NE    
2555 C  CZ    . ARG A 310 ? 1.0112 1.3271 1.0997 -0.0125 0.1943  0.1284  310 ARG A CZ    
2556 N  NH1   . ARG A 310 ? 0.8639 1.1929 0.9551 -0.0043 0.2096  0.1310  310 ARG A NH1   
2557 N  NH2   . ARG A 310 ? 1.0243 1.3455 1.1316 -0.0213 0.1885  0.1424  310 ARG A NH2   
2558 N  N     . TYR A 311 ? 0.7012 0.9721 0.8380 -0.0249 0.1454  0.0875  311 TYR A N     
2559 C  CA    . TYR A 311 ? 0.6359 0.8920 0.7735 -0.0320 0.1300  0.0812  311 TYR A CA    
2560 C  C     . TYR A 311 ? 0.6184 0.8656 0.7576 -0.0295 0.1241  0.0683  311 TYR A C     
2561 O  O     . TYR A 311 ? 0.6207 0.8527 0.7453 -0.0302 0.1158  0.0576  311 TYR A O     
2562 C  CB    . TYR A 311 ? 0.6438 0.9050 0.8069 -0.0415 0.1229  0.0926  311 TYR A CB    
2563 C  CG    . TYR A 311 ? 0.6676 0.9137 0.8335 -0.0483 0.1079  0.0858  311 TYR A CG    
2564 C  CD1   . TYR A 311 ? 0.6727 0.9065 0.8229 -0.0511 0.1016  0.0836  311 TYR A CD1   
2565 C  CD2   . TYR A 311 ? 0.7256 0.9702 0.9096 -0.0515 0.1001  0.0821  311 TYR A CD2   
2566 C  CE1   . TYR A 311 ? 0.7040 0.9242 0.8571 -0.0565 0.0891  0.0775  311 TYR A CE1   
2567 C  CE2   . TYR A 311 ? 0.6612 0.8918 0.8460 -0.0572 0.0873  0.0755  311 TYR A CE2   
2568 C  CZ    . TYR A 311 ? 0.6891 0.9074 0.8587 -0.0593 0.0824  0.0731  311 TYR A CZ    
2569 O  OH    . TYR A 311 ? 0.9724 1.1770 1.1431 -0.0641 0.0709  0.0666  311 TYR A OH    
2570 N  N     . SER A 312 ? 0.5755 0.8328 0.7332 -0.0264 0.1286  0.0701  312 SER A N     
2571 C  CA    . SER A 312 ? 0.5827 0.8330 0.7434 -0.0238 0.1235  0.0594  312 SER A CA    
2572 C  C     . SER A 312 ? 0.6100 0.8496 0.7455 -0.0155 0.1283  0.0468  312 SER A C     
2573 O  O     . SER A 312 ? 0.5755 0.8014 0.7025 -0.0155 0.1201  0.0358  312 SER A O     
2574 C  CB    . SER A 312 ? 0.6275 0.8930 0.8147 -0.0219 0.1278  0.0660  312 SER A CB    
2575 O  OG    . SER A 312 ? 0.6852 0.9451 0.8813 -0.0229 0.1187  0.0591  312 SER A OG    
2576 N  N     . MET A 313 ? 0.5739 0.8194 0.6972 -0.0084 0.1416  0.0481  313 MET A N     
2577 C  CA    . MET A 313 ? 0.5993 0.8336 0.6973 -0.0008 0.1464  0.0354  313 MET A CA    
2578 C  C     . MET A 313 ? 0.6667 0.8851 0.7414 -0.0048 0.1369  0.0275  313 MET A C     
2579 O  O     . MET A 313 ? 0.5919 0.7966 0.6544 -0.0028 0.1319  0.0153  313 MET A O     
2580 C  CB    . MET A 313 ? 0.5658 0.8096 0.6535 0.0071  0.1629  0.0387  313 MET A CB    
2581 C  CG    . MET A 313 ? 0.5938 0.8256 0.6510 0.0148  0.1693  0.0257  313 MET A CG    
2582 S  SD    . MET A 313 ? 0.8666 1.0833 0.8897 0.0106  0.1614  0.0181  313 MET A SD    
2583 C  CE    . MET A 313 ? 0.6598 0.8914 0.6749 0.0101  0.1715  0.0320  313 MET A CE    
2584 N  N     . GLU A 314 ? 0.6244 0.8451 0.6946 -0.0106 0.1340  0.0353  314 GLU A N     
2585 C  CA    . GLU A 314 ? 0.6387 0.8461 0.6889 -0.0145 0.1249  0.0298  314 GLU A CA    
2586 C  C     . GLU A 314 ? 0.6724 0.8690 0.7317 -0.0198 0.1112  0.0243  314 GLU A C     
2587 O  O     . GLU A 314 ? 0.6653 0.8487 0.7088 -0.0201 0.1044  0.0149  314 GLU A O     
2588 C  CB    . GLU A 314 ? 0.6601 0.8739 0.7072 -0.0193 0.1252  0.0415  314 GLU A CB    
2589 C  CG    . GLU A 314 ? 0.6583 0.8806 0.6880 -0.0140 0.1381  0.0456  314 GLU A CG    
2590 C  CD    . GLU A 314 ? 0.8045 1.0297 0.8243 -0.0187 0.1363  0.0553  314 GLU A CD    
2591 O  OE1   . GLU A 314 ? 0.8726 1.0914 0.8984 -0.0257 0.1249  0.0578  314 GLU A OE1   
2592 O  OE2   . GLU A 314 ? 1.0432 1.2770 1.0492 -0.0151 0.1467  0.0608  314 GLU A OE2   
2593 N  N     . ASP A 315 ? 0.5766 0.7787 0.6609 -0.0240 0.1069  0.0301  315 ASP A N     
2594 C  CA    . ASP A 315 ? 0.6007 0.7931 0.6930 -0.0281 0.0950  0.0242  315 ASP A CA    
2595 C  C     . ASP A 315 ? 0.6305 0.8141 0.7145 -0.0226 0.0944  0.0120  315 ASP A C     
2596 O  O     . ASP A 315 ? 0.6342 0.8050 0.7070 -0.0238 0.0867  0.0038  315 ASP A O     
2597 C  CB    . ASP A 315 ? 0.5880 0.7890 0.7075 -0.0328 0.0916  0.0317  315 ASP A CB    
2598 C  CG    . ASP A 315 ? 0.7159 0.9151 0.8436 -0.0413 0.0837  0.0384  315 ASP A CG    
2599 O  OD1   . ASP A 315 ? 0.7626 0.9596 0.8789 -0.0428 0.0846  0.0422  315 ASP A OD1   
2600 O  OD2   . ASP A 315 ? 0.7049 0.9044 0.8504 -0.0465 0.0766  0.0400  315 ASP A OD2   
2601 N  N     . ALA A 316 ? 0.5809 0.7716 0.6720 -0.0164 0.1029  0.0113  316 ALA A N     
2602 C  CA    . ALA A 316 ? 0.6024 0.7846 0.6878 -0.0108 0.1031  0.0005  316 ALA A CA    
2603 C  C     . ALA A 316 ? 0.5697 0.7391 0.6280 -0.0080 0.1036  -0.0093 316 ALA A C     
2604 O  O     . ALA A 316 ? 0.5884 0.7455 0.6397 -0.0080 0.0969  -0.0184 316 ALA A O     
2605 C  CB    . ALA A 316 ? 0.5613 0.7538 0.6586 -0.0036 0.1139  0.0026  316 ALA A CB    
2606 N  N     . LYS A 317 ? 0.5681 0.7407 0.6109 -0.0060 0.1112  -0.0072 317 LYS A N     
2607 C  CA    . LYS A 317 ? 0.6666 0.8278 0.6821 -0.0037 0.1116  -0.0165 317 LYS A CA    
2608 C  C     . LYS A 317 ? 0.6346 0.7851 0.6415 -0.0102 0.0988  -0.0195 317 LYS A C     
2609 O  O     . LYS A 317 ? 0.6494 0.7874 0.6439 -0.0095 0.0939  -0.0297 317 LYS A O     
2610 C  CB    . LYS A 317 ? 0.6509 0.8195 0.6513 -0.0010 0.1219  -0.0120 317 LYS A CB    
2611 C  CG    . LYS A 317 ? 0.8787 1.0368 0.8491 0.0024  0.1243  -0.0225 317 LYS A CG    
2612 C  CD    . LYS A 317 ? 0.9302 1.0966 0.8882 0.0088  0.1390  -0.0202 317 LYS A CD    
2613 C  CE    . LYS A 317 ? 1.1069 1.2658 1.0321 0.0090  0.1390  -0.0266 317 LYS A CE    
2614 N  NZ    . LYS A 317 ? 0.9912 1.1431 0.9093 0.0008  0.1247  -0.0262 317 LYS A NZ    
2615 N  N     . VAL A 318 ? 0.6195 0.7747 0.6344 -0.0166 0.0933  -0.0104 318 VAL A N     
2616 C  CA    . VAL A 318 ? 0.6164 0.7622 0.6240 -0.0221 0.0822  -0.0121 318 VAL A CA    
2617 C  C     . VAL A 318 ? 0.6418 0.7794 0.6602 -0.0238 0.0735  -0.0180 318 VAL A C     
2618 O  O     . VAL A 318 ? 0.6438 0.7711 0.6526 -0.0255 0.0660  -0.0240 318 VAL A O     
2619 C  CB    . VAL A 318 ? 0.5775 0.7297 0.5914 -0.0279 0.0795  -0.0004 318 VAL A CB    
2620 C  CG1   . VAL A 318 ? 0.5844 0.7452 0.5857 -0.0262 0.0882  0.0062  318 VAL A CG1   
2621 C  CG2   . VAL A 318 ? 0.6339 0.7927 0.6736 -0.0313 0.0779  0.0068  318 VAL A CG2   
2622 N  N     . THR A 319 ? 0.5705 0.7131 0.6088 -0.0234 0.0741  -0.0159 319 THR A N     
2623 C  CA    . THR A 319 ? 0.6108 0.7460 0.6570 -0.0244 0.0664  -0.0217 319 THR A CA    
2624 C  C     . THR A 319 ? 0.6008 0.7272 0.6361 -0.0192 0.0677  -0.0321 319 THR A C     
2625 O  O     . THR A 319 ? 0.6267 0.7434 0.6591 -0.0206 0.0604  -0.0380 319 THR A O     
2626 C  CB    . THR A 319 ? 0.4554 0.5984 0.5240 -0.0254 0.0659  -0.0171 319 THR A CB    
2627 O  OG1   . THR A 319 ? 0.7505 0.9004 0.8249 -0.0195 0.0746  -0.0174 319 THR A OG1   
2628 C  CG2   . THR A 319 ? 0.4690 0.6199 0.5494 -0.0310 0.0645  -0.0070 319 THR A CG2   
2629 N  N     . TYR A 320 ? 0.5997 0.7288 0.6289 -0.0133 0.0774  -0.0346 320 TYR A N     
2630 C  CA    . TYR A 320 ? 0.6103 0.7289 0.6284 -0.0085 0.0789  -0.0452 320 TYR A CA    
2631 C  C     . TYR A 320 ? 0.6726 0.7803 0.6695 -0.0109 0.0734  -0.0514 320 TYR A C     
2632 O  O     . TYR A 320 ? 0.6609 0.7578 0.6536 -0.0111 0.0678  -0.0590 320 TYR A O     
2633 C  CB    . TYR A 320 ? 0.5870 0.7098 0.6021 -0.0010 0.0914  -0.0470 320 TYR A CB    
2634 C  CG    . TYR A 320 ? 0.6728 0.7830 0.6765 0.0040  0.0933  -0.0586 320 TYR A CG    
2635 C  CD1   . TYR A 320 ? 0.6307 0.7355 0.6466 0.0059  0.0902  -0.0624 320 TYR A CD1   
2636 C  CD2   . TYR A 320 ? 0.7437 0.8467 0.7240 0.0066  0.0979  -0.0658 320 TYR A CD2   
2637 C  CE1   . TYR A 320 ? 0.6517 0.7440 0.6588 0.0103  0.0919  -0.0726 320 TYR A CE1   
2638 C  CE2   . TYR A 320 ? 0.7881 0.8778 0.7581 0.0107  0.0992  -0.0772 320 TYR A CE2   
2639 C  CZ    . TYR A 320 ? 0.7432 0.8272 0.7275 0.0126  0.0963  -0.0805 320 TYR A CZ    
2640 O  OH    . TYR A 320 ? 0.8629 0.9327 0.8385 0.0164  0.0975  -0.0915 320 TYR A OH    
2641 N  N     . GLU A 321 ? 0.6523 0.7634 0.6363 -0.0131 0.0747  -0.0475 321 GLU A N     
2642 C  CA    . GLU A 321 ? 0.7094 0.8117 0.6734 -0.0159 0.0686  -0.0522 321 GLU A CA    
2643 C  C     . GLU A 321 ? 0.7314 0.8286 0.7024 -0.0215 0.0568  -0.0512 321 GLU A C     
2644 O  O     . GLU A 321 ? 0.7405 0.8278 0.7026 -0.0228 0.0504  -0.0580 321 GLU A O     
2645 C  CB    . GLU A 321 ? 0.7365 0.8456 0.6866 -0.0172 0.0723  -0.0463 321 GLU A CB    
2646 C  CG    . GLU A 321 ? 0.8641 0.9775 0.8029 -0.0111 0.0848  -0.0481 321 GLU A CG    
2647 C  CD    . GLU A 321 ? 1.2460 1.3489 1.1587 -0.0088 0.0854  -0.0593 321 GLU A CD    
2648 O  OE1   . GLU A 321 ? 1.2671 1.3667 1.1637 -0.0132 0.0786  -0.0595 321 GLU A OE1   
2649 O  OE2   . GLU A 321 ? 1.2115 1.3091 1.1200 -0.0028 0.0926  -0.0678 321 GLU A OE2   
2650 N  N     . LEU A 322 ? 0.6913 0.7948 0.6786 -0.0249 0.0540  -0.0429 322 LEU A N     
2651 C  CA    . LEU A 322 ? 0.6796 0.7781 0.6741 -0.0294 0.0441  -0.0421 322 LEU A CA    
2652 C  C     . LEU A 322 ? 0.7119 0.8033 0.7130 -0.0277 0.0407  -0.0491 322 LEU A C     
2653 O  O     . LEU A 322 ? 0.7079 0.7920 0.7068 -0.0300 0.0333  -0.0521 322 LEU A O     
2654 C  CB    . LEU A 322 ? 0.6004 0.7059 0.6109 -0.0328 0.0427  -0.0329 322 LEU A CB    
2655 C  CG    . LEU A 322 ? 0.6369 0.7480 0.6431 -0.0358 0.0436  -0.0242 322 LEU A CG    
2656 C  CD1   . LEU A 322 ? 0.5748 0.6937 0.5989 -0.0383 0.0453  -0.0155 322 LEU A CD1   
2657 C  CD2   . LEU A 322 ? 0.7202 0.8255 0.7194 -0.0394 0.0355  -0.0232 322 LEU A CD2   
2658 N  N     . GLY A 323 ? 0.6531 0.7472 0.6635 -0.0237 0.0461  -0.0508 323 GLY A N     
2659 C  CA    . GLY A 323 ? 0.6380 0.7257 0.6545 -0.0217 0.0434  -0.0567 323 GLY A CA    
2660 C  C     . GLY A 323 ? 0.7119 0.7890 0.7138 -0.0201 0.0423  -0.0654 323 GLY A C     
2661 O  O     . GLY A 323 ? 0.7006 0.7703 0.7038 -0.0215 0.0359  -0.0690 323 GLY A O     
2662 N  N     . LYS A 324 ? 0.7359 0.8120 0.7237 -0.0172 0.0486  -0.0690 324 LYS A N     
2663 C  CA    . LYS A 324 ? 0.7685 0.8332 0.7402 -0.0165 0.0469  -0.0783 324 LYS A CA    
2664 C  C     . LYS A 324 ? 0.7908 0.8508 0.7547 -0.0223 0.0369  -0.0782 324 LYS A C     
2665 O  O     . LYS A 324 ? 0.8899 0.9402 0.8499 -0.0235 0.0314  -0.0845 324 LYS A O     
2666 C  CB    . LYS A 324 ? 0.7882 0.8530 0.7430 -0.0128 0.0555  -0.0820 324 LYS A CB    
2667 C  CG    . LYS A 324 ? 1.0059 1.0575 0.9452 -0.0106 0.0558  -0.0938 324 LYS A CG    
2668 C  CD    . LYS A 324 ? 1.3129 1.3557 1.2644 -0.0097 0.0519  -0.0985 324 LYS A CD    
2669 C  CE    . LYS A 324 ? 1.0485 1.0767 0.9858 -0.0115 0.0464  -0.1086 324 LYS A CE    
2670 N  NZ    . LYS A 324 ? 1.2081 1.2285 1.1285 -0.0067 0.0543  -0.1181 324 LYS A NZ    
2671 N  N     . GLU A 325 ? 0.7437 0.8104 0.7070 -0.0261 0.0342  -0.0705 325 GLU A N     
2672 C  CA    . GLU A 325 ? 0.7964 0.8598 0.7539 -0.0312 0.0249  -0.0693 325 GLU A CA    
2673 C  C     . GLU A 325 ? 0.8181 0.8791 0.7909 -0.0333 0.0181  -0.0677 325 GLU A C     
2674 O  O     . GLU A 325 ? 0.8493 0.9042 0.8190 -0.0359 0.0109  -0.0701 325 GLU A O     
2675 C  CB    . GLU A 325 ? 0.8541 0.9254 0.8070 -0.0340 0.0247  -0.0607 325 GLU A CB    
2676 C  CG    . GLU A 325 ? 0.9789 1.0486 0.9294 -0.0390 0.0151  -0.0571 325 GLU A CG    
2677 C  CD    . GLU A 325 ? 1.1055 1.1718 1.0350 -0.0409 0.0116  -0.0609 325 GLU A CD    
2678 O  OE1   . GLU A 325 ? 1.2543 1.3128 1.1739 -0.0395 0.0120  -0.0705 325 GLU A OE1   
2679 O  OE2   . GLU A 325 ? 1.1763 1.2473 1.0992 -0.0440 0.0082  -0.0542 325 GLU A OE2   
2680 N  N     . PHE A 326 ? 0.7542 0.8199 0.7430 -0.0323 0.0201  -0.0635 326 PHE A N     
2681 C  CA    . PHE A 326 ? 0.6326 0.6972 0.6341 -0.0344 0.0141  -0.0609 326 PHE A CA    
2682 C  C     . PHE A 326 ? 0.6763 0.7365 0.6865 -0.0320 0.0136  -0.0653 326 PHE A C     
2683 O  O     . PHE A 326 ? 0.7778 0.8356 0.7950 -0.0336 0.0084  -0.0643 326 PHE A O     
2684 C  CB    . PHE A 326 ? 0.6218 0.6935 0.6345 -0.0357 0.0152  -0.0535 326 PHE A CB    
2685 C  CG    . PHE A 326 ? 0.6960 0.7705 0.7048 -0.0391 0.0128  -0.0473 326 PHE A CG    
2686 C  CD1   . PHE A 326 ? 0.8030 0.8829 0.8042 -0.0391 0.0173  -0.0437 326 PHE A CD1   
2687 C  CD2   . PHE A 326 ? 0.7246 0.7966 0.7378 -0.0418 0.0065  -0.0442 326 PHE A CD2   
2688 C  CE1   . PHE A 326 ? 0.8472 0.9299 0.8455 -0.0422 0.0151  -0.0367 326 PHE A CE1   
2689 C  CE2   . PHE A 326 ? 0.7594 0.8338 0.7705 -0.0444 0.0044  -0.0376 326 PHE A CE2   
2690 C  CZ    . PHE A 326 ? 0.8448 0.9245 0.8485 -0.0448 0.0084  -0.0336 326 PHE A CZ    
2691 N  N     . LEU A 327 ? 0.7233 0.7827 0.7339 -0.0280 0.0193  -0.0695 327 LEU A N     
2692 C  CA    . LEU A 327 ? 0.7255 0.7816 0.7462 -0.0256 0.0188  -0.0720 327 LEU A CA    
2693 C  C     . LEU A 327 ? 0.7032 0.7498 0.7200 -0.0267 0.0136  -0.0770 327 LEU A C     
2694 O  O     . LEU A 327 ? 0.6883 0.7337 0.7147 -0.0273 0.0097  -0.0755 327 LEU A O     
2695 C  CB    . LEU A 327 ? 0.6352 0.6935 0.6596 -0.0205 0.0265  -0.0740 327 LEU A CB    
2696 C  CG    . LEU A 327 ? 0.6574 0.7131 0.6931 -0.0176 0.0264  -0.0756 327 LEU A CG    
2697 C  CD1   . LEU A 327 ? 0.8021 0.8668 0.8503 -0.0144 0.0315  -0.0713 327 LEU A CD1   
2698 C  CD2   . LEU A 327 ? 0.7238 0.7691 0.7529 -0.0147 0.0282  -0.0832 327 LEU A CD2   
2699 N  N     . PRO A 328 ? 0.7205 0.7603 0.7239 -0.0271 0.0131  -0.0827 328 PRO A N     
2700 C  CA    . PRO A 328 ? 0.8800 0.9107 0.8816 -0.0293 0.0070  -0.0869 328 PRO A CA    
2701 C  C     . PRO A 328 ? 0.7685 0.8012 0.7746 -0.0337 -0.0006 -0.0819 328 PRO A C     
2702 O  O     . PRO A 328 ? 0.7783 0.8062 0.7898 -0.0352 -0.0055 -0.0827 328 PRO A O     
2703 C  CB    . PRO A 328 ? 0.8274 0.8515 0.8110 -0.0300 0.0073  -0.0938 328 PRO A CB    
2704 C  CG    . PRO A 328 ? 0.8227 0.8511 0.8009 -0.0258 0.0163  -0.0946 328 PRO A CG    
2705 C  CD    . PRO A 328 ? 0.7335 0.7733 0.7221 -0.0260 0.0180  -0.0858 328 PRO A CD    
2706 N  N     . MET A 329 ? 0.7576 0.7972 0.7628 -0.0356 -0.0013 -0.0761 329 MET A N     
2707 C  CA    . MET A 329 ? 0.8073 0.8489 0.8178 -0.0389 -0.0074 -0.0708 329 MET A CA    
2708 C  C     . MET A 329 ? 0.8156 0.8596 0.8407 -0.0375 -0.0072 -0.0674 329 MET A C     
2709 O  O     . MET A 329 ? 0.8036 0.8460 0.8352 -0.0388 -0.0115 -0.0657 329 MET A O     
2710 C  CB    . MET A 329 ? 0.8058 0.8531 0.8110 -0.0409 -0.0076 -0.0655 329 MET A CB    
2711 C  CG    . MET A 329 ? 0.9181 0.9646 0.9068 -0.0421 -0.0071 -0.0681 329 MET A CG    
2712 S  SD    . MET A 329 ? 1.4711 1.5158 1.4513 -0.0472 -0.0165 -0.0665 329 MET A SD    
2713 C  CE    . MET A 329 ? 1.0237 1.0601 0.9863 -0.0476 -0.0170 -0.0768 329 MET A CE    
2714 N  N     . GLU A 330 ? 0.7052 0.7537 0.7357 -0.0351 -0.0022 -0.0660 330 GLU A N     
2715 C  CA    . GLU A 330 ? 0.6206 0.6716 0.6629 -0.0338 -0.0022 -0.0634 330 GLU A CA    
2716 C  C     . GLU A 330 ? 0.6453 0.6925 0.6929 -0.0317 -0.0024 -0.0662 330 GLU A C     
2717 O  O     . GLU A 330 ? 0.5951 0.6433 0.6509 -0.0311 -0.0038 -0.0638 330 GLU A O     
2718 C  CB    . GLU A 330 ? 0.7293 0.7865 0.7758 -0.0326 0.0021  -0.0612 330 GLU A CB    
2719 C  CG    . GLU A 330 ? 0.7246 0.7855 0.7713 -0.0351 0.0014  -0.0567 330 GLU A CG    
2720 C  CD    . GLU A 330 ? 0.7736 0.8335 0.8262 -0.0364 -0.0023 -0.0541 330 GLU A CD    
2721 O  OE1   . GLU A 330 ? 0.7330 0.7944 0.7923 -0.0354 -0.0020 -0.0537 330 GLU A OE1   
2722 O  OE2   . GLU A 330 ? 0.8283 0.8860 0.8785 -0.0381 -0.0055 -0.0522 330 GLU A OE2   
2723 N  N     . ALA A 331 ? 0.6512 0.6934 0.6939 -0.0302 -0.0006 -0.0711 331 ALA A N     
2724 C  CA    . ALA A 331 ? 0.6736 0.7107 0.7222 -0.0285 -0.0012 -0.0734 331 ALA A CA    
2725 C  C     . ALA A 331 ? 0.7076 0.7410 0.7587 -0.0315 -0.0072 -0.0721 331 ALA A C     
2726 O  O     . ALA A 331 ? 0.6552 0.6875 0.7153 -0.0305 -0.0082 -0.0705 331 ALA A O     
2727 C  CB    . ALA A 331 ? 0.6509 0.6814 0.6932 -0.0265 0.0021  -0.0798 331 ALA A CB    
2728 N  N     . GLN A 332 ? 0.7183 0.7511 0.7627 -0.0351 -0.0112 -0.0717 332 GLN A N     
2729 C  CA    . GLN A 332 ? 0.6898 0.7213 0.7389 -0.0380 -0.0171 -0.0689 332 GLN A CA    
2730 C  C     . GLN A 332 ? 0.6020 0.6392 0.6609 -0.0370 -0.0168 -0.0629 332 GLN A C     
2731 O  O     . GLN A 332 ? 0.5991 0.6359 0.6662 -0.0372 -0.0189 -0.0602 332 GLN A O     
2732 C  CB    . GLN A 332 ? 0.6675 0.6986 0.7078 -0.0420 -0.0217 -0.0688 332 GLN A CB    
2733 C  CG    . GLN A 332 ? 0.7609 0.7854 0.7888 -0.0435 -0.0228 -0.0757 332 GLN A CG    
2734 C  CD    . GLN A 332 ? 1.1803 1.2041 1.2011 -0.0484 -0.0299 -0.0750 332 GLN A CD    
2735 O  OE1   . GLN A 332 ? 1.2160 1.2344 1.2373 -0.0516 -0.0355 -0.0774 332 GLN A OE1   
2736 N  NE2   . GLN A 332 ? 1.1937 1.2232 1.2086 -0.0495 -0.0302 -0.0712 332 GLN A NE2   
2737 N  N     . LEU A 333 ? 0.5958 0.6381 0.6539 -0.0360 -0.0141 -0.0606 333 LEU A N     
2738 C  CA    . LEU A 333 ? 0.5593 0.6057 0.6250 -0.0347 -0.0133 -0.0565 333 LEU A CA    
2739 C  C     . LEU A 333 ? 0.5509 0.5979 0.6230 -0.0319 -0.0111 -0.0566 333 LEU A C     
2740 O  O     . LEU A 333 ? 0.5491 0.5976 0.6274 -0.0311 -0.0117 -0.0534 333 LEU A O     
2741 C  CB    . LEU A 333 ? 0.5314 0.5816 0.5948 -0.0347 -0.0110 -0.0551 333 LEU A CB    
2742 C  CG    . LEU A 333 ? 0.5337 0.5864 0.6024 -0.0338 -0.0104 -0.0521 333 LEU A CG    
2743 C  CD1   . LEU A 333 ? 0.5437 0.5956 0.6163 -0.0343 -0.0129 -0.0488 333 LEU A CD1   
2744 C  CD2   . LEU A 333 ? 0.4972 0.5520 0.5639 -0.0347 -0.0089 -0.0513 333 LEU A CD2   
2745 N  N     . SER A 334 ? 0.5948 0.6412 0.6657 -0.0301 -0.0083 -0.0596 334 SER A N     
2746 C  CA    . SER A 334 ? 0.5663 0.6138 0.6440 -0.0273 -0.0065 -0.0587 334 SER A CA    
2747 C  C     . SER A 334 ? 0.4994 0.5427 0.5826 -0.0274 -0.0087 -0.0577 334 SER A C     
2748 O  O     . SER A 334 ? 0.5050 0.5509 0.5951 -0.0259 -0.0085 -0.0539 334 SER A O     
2749 C  CB    . SER A 334 ? 0.5856 0.6330 0.6625 -0.0250 -0.0027 -0.0617 334 SER A CB    
2750 O  OG    . SER A 334 ? 0.5326 0.5827 0.6175 -0.0220 -0.0011 -0.0595 334 SER A OG    
2751 N  N     . ARG A 335 ? 0.5273 0.5643 0.6073 -0.0296 -0.0112 -0.0608 335 ARG A N     
2752 C  CA    . ARG A 335 ? 0.6702 0.7028 0.7568 -0.0307 -0.0142 -0.0597 335 ARG A CA    
2753 C  C     . ARG A 335 ? 0.5132 0.5499 0.6053 -0.0322 -0.0168 -0.0540 335 ARG A C     
2754 O  O     . ARG A 335 ? 0.5269 0.5643 0.6279 -0.0316 -0.0172 -0.0499 335 ARG A O     
2755 C  CB    . ARG A 335 ? 0.6518 0.6761 0.7326 -0.0336 -0.0172 -0.0651 335 ARG A CB    
2756 C  CG    . ARG A 335 ? 0.6890 0.7075 0.7652 -0.0313 -0.0137 -0.0713 335 ARG A CG    
2757 C  CD    . ARG A 335 ? 0.7861 0.7941 0.8572 -0.0342 -0.0172 -0.0773 335 ARG A CD    
2758 N  NE    . ARG A 335 ? 0.8685 0.8756 0.9259 -0.0371 -0.0192 -0.0812 335 ARG A NE    
2759 C  CZ    . ARG A 335 ? 1.0454 1.0516 1.0919 -0.0352 -0.0151 -0.0861 335 ARG A CZ    
2760 N  NH1   . ARG A 335 ? 0.8443 0.8502 0.8929 -0.0304 -0.0086 -0.0879 335 ARG A NH1   
2761 N  NH2   . ARG A 335 ? 1.1006 1.1069 1.1343 -0.0381 -0.0173 -0.0884 335 ARG A NH2   
2762 N  N     . LEU A 336 ? 0.4604 0.5000 0.5479 -0.0339 -0.0180 -0.0530 336 LEU A N     
2763 C  CA    . LEU A 336 ? 0.5134 0.5568 0.6068 -0.0346 -0.0198 -0.0474 336 LEU A CA    
2764 C  C     . LEU A 336 ? 0.5611 0.6095 0.6592 -0.0312 -0.0161 -0.0436 336 LEU A C     
2765 O  O     . LEU A 336 ? 0.5190 0.5697 0.6246 -0.0305 -0.0162 -0.0388 336 LEU A O     
2766 C  CB    . LEU A 336 ? 0.5869 0.6319 0.6750 -0.0365 -0.0215 -0.0469 336 LEU A CB    
2767 C  CG    . LEU A 336 ? 0.6118 0.6601 0.7070 -0.0374 -0.0237 -0.0410 336 LEU A CG    
2768 C  CD1   . LEU A 336 ? 0.5032 0.5498 0.6055 -0.0401 -0.0280 -0.0391 336 LEU A CD1   
2769 C  CD2   . LEU A 336 ? 0.6100 0.6597 0.7008 -0.0390 -0.0254 -0.0399 336 LEU A CD2   
2770 N  N     . ILE A 337 ? 0.5433 0.5938 0.6367 -0.0292 -0.0131 -0.0454 337 ILE A N     
2771 C  CA    . ILE A 337 ? 0.4756 0.5307 0.5710 -0.0265 -0.0103 -0.0427 337 ILE A CA    
2772 C  C     . ILE A 337 ? 0.4430 0.4994 0.5428 -0.0243 -0.0090 -0.0412 337 ILE A C     
2773 O  O     . ILE A 337 ? 0.4766 0.5371 0.5787 -0.0222 -0.0074 -0.0375 337 ILE A O     
2774 C  CB    . ILE A 337 ? 0.5385 0.5954 0.6276 -0.0262 -0.0088 -0.0450 337 ILE A CB    
2775 C  CG1   . ILE A 337 ? 0.5216 0.5767 0.6071 -0.0285 -0.0101 -0.0459 337 ILE A CG1   
2776 C  CG2   . ILE A 337 ? 0.5035 0.5640 0.5924 -0.0241 -0.0068 -0.0431 337 ILE A CG2   
2777 C  CD1   . ILE A 337 ? 0.5172 0.5727 0.6060 -0.0283 -0.0105 -0.0423 337 ILE A CD1   
2778 N  N     . GLY A 338 ? 0.4898 0.5427 0.5906 -0.0244 -0.0093 -0.0437 338 GLY A N     
2779 C  CA    . GLY A 338 ? 0.5008 0.5548 0.6074 -0.0220 -0.0079 -0.0416 338 GLY A CA    
2780 C  C     . GLY A 338 ? 0.5019 0.5611 0.6064 -0.0198 -0.0058 -0.0415 338 GLY A C     
2781 O  O     . GLY A 338 ? 0.5000 0.5631 0.6092 -0.0175 -0.0049 -0.0376 338 GLY A O     
2782 N  N     . GLN A 339 ? 0.4974 0.5576 0.5958 -0.0207 -0.0054 -0.0451 339 GLN A N     
2783 C  CA    . GLN A 339 ? 0.5159 0.5817 0.6136 -0.0194 -0.0042 -0.0450 339 GLN A CA    
2784 C  C     . GLN A 339 ? 0.5648 0.6293 0.6609 -0.0197 -0.0027 -0.0488 339 GLN A C     
2785 O  O     . GLN A 339 ? 0.5189 0.5780 0.6115 -0.0210 -0.0027 -0.0521 339 GLN A O     
2786 C  CB    . GLN A 339 ? 0.5573 0.6268 0.6500 -0.0206 -0.0048 -0.0448 339 GLN A CB    
2787 C  CG    . GLN A 339 ? 0.5172 0.5887 0.6101 -0.0194 -0.0050 -0.0412 339 GLN A CG    
2788 C  CD    . GLN A 339 ? 0.5719 0.6481 0.6692 -0.0170 -0.0047 -0.0369 339 GLN A CD    
2789 O  OE1   . GLN A 339 ? 0.6232 0.7039 0.7217 -0.0163 -0.0050 -0.0365 339 GLN A OE1   
2790 N  NE2   . GLN A 339 ? 0.5437 0.6198 0.6449 -0.0156 -0.0041 -0.0328 339 GLN A NE2   
2791 N  N     . SER A 340 ? 0.5891 0.6593 0.6875 -0.0184 -0.0015 -0.0478 340 SER A N     
2792 C  CA    . SER A 340 ? 0.5690 0.6394 0.6679 -0.0176 0.0011  -0.0502 340 SER A CA    
2793 C  C     . SER A 340 ? 0.5402 0.6092 0.6320 -0.0203 0.0013  -0.0533 340 SER A C     
2794 O  O     . SER A 340 ? 0.4573 0.5273 0.5455 -0.0228 -0.0007 -0.0528 340 SER A O     
2795 C  CB    . SER A 340 ? 0.5599 0.6389 0.6649 -0.0159 0.0019  -0.0471 340 SER A CB    
2796 O  OG    . SER A 340 ? 0.5807 0.6648 0.6828 -0.0187 0.0003  -0.0468 340 SER A OG    
2797 N  N     . LEU A 341 ? 0.4220 0.4885 0.5116 -0.0196 0.0041  -0.0562 341 LEU A N     
2798 C  CA    . LEU A 341 ? 0.4937 0.5601 0.5765 -0.0219 0.0049  -0.0580 341 LEU A CA    
2799 C  C     . LEU A 341 ? 0.6063 0.6800 0.6913 -0.0236 0.0048  -0.0553 341 LEU A C     
2800 O  O     . LEU A 341 ? 0.6117 0.6851 0.6928 -0.0265 0.0034  -0.0551 341 LEU A O     
2801 C  CB    . LEU A 341 ? 0.4974 0.5611 0.5769 -0.0200 0.0091  -0.0613 341 LEU A CB    
2802 C  CG    . LEU A 341 ? 0.6330 0.6985 0.7057 -0.0216 0.0113  -0.0621 341 LEU A CG    
2803 C  CD1   . LEU A 341 ? 0.6855 0.7473 0.7507 -0.0253 0.0075  -0.0624 341 LEU A CD1   
2804 C  CD2   . LEU A 341 ? 0.7261 0.7887 0.7943 -0.0187 0.0164  -0.0659 341 LEU A CD2   
2805 N  N     . TRP A 342 ? 0.5523 0.6327 0.6449 -0.0219 0.0058  -0.0529 342 TRP A N     
2806 C  CA    . TRP A 342 ? 0.5485 0.6361 0.6444 -0.0242 0.0045  -0.0504 342 TRP A CA    
2807 C  C     . TRP A 342 ? 0.5376 0.6235 0.6302 -0.0272 0.0002  -0.0503 342 TRP A C     
2808 O  O     . TRP A 342 ? 0.5058 0.5926 0.5972 -0.0305 -0.0010 -0.0501 342 TRP A O     
2809 C  CB    . TRP A 342 ? 0.5784 0.6742 0.6838 -0.0221 0.0049  -0.0471 342 TRP A CB    
2810 C  CG    . TRP A 342 ? 0.5641 0.6682 0.6744 -0.0250 0.0034  -0.0443 342 TRP A CG    
2811 C  CD1   . TRP A 342 ? 0.5616 0.6724 0.6780 -0.0250 0.0066  -0.0422 342 TRP A CD1   
2812 C  CD2   . TRP A 342 ? 0.6327 0.7394 0.7427 -0.0287 -0.0018 -0.0434 342 TRP A CD2   
2813 N  NE1   . TRP A 342 ? 0.6124 0.7300 0.7337 -0.0290 0.0030  -0.0395 342 TRP A NE1   
2814 C  CE2   . TRP A 342 ? 0.6542 0.7687 0.7708 -0.0315 -0.0024 -0.0408 342 TRP A CE2   
2815 C  CE3   . TRP A 342 ? 0.6082 0.7112 0.7126 -0.0298 -0.0056 -0.0447 342 TRP A CE3   
2816 C  CZ2   . TRP A 342 ? 0.6475 0.7651 0.7649 -0.0360 -0.0078 -0.0403 342 TRP A CZ2   
2817 C  CZ3   . TRP A 342 ? 0.6322 0.7380 0.7359 -0.0336 -0.0101 -0.0446 342 TRP A CZ3   
2818 C  CH2   . TRP A 342 ? 0.6812 0.7937 0.7911 -0.0370 -0.0116 -0.0428 342 TRP A CH2   
2819 N  N     . ASP A 343 ? 0.5697 0.6526 0.6611 -0.0260 -0.0016 -0.0504 343 ASP A N     
2820 C  CA    . ASP A 343 ? 0.5581 0.6391 0.6458 -0.0278 -0.0045 -0.0505 343 ASP A CA    
2821 C  C     . ASP A 343 ? 0.5440 0.6187 0.6265 -0.0295 -0.0045 -0.0522 343 ASP A C     
2822 O  O     . ASP A 343 ? 0.5563 0.6297 0.6366 -0.0319 -0.0056 -0.0527 343 ASP A O     
2823 C  CB    . ASP A 343 ? 0.6376 0.7187 0.7261 -0.0255 -0.0054 -0.0489 343 ASP A CB    
2824 C  CG    . ASP A 343 ? 0.8564 0.9450 0.9489 -0.0246 -0.0068 -0.0462 343 ASP A CG    
2825 O  OD1   . ASP A 343 ? 0.7574 0.8489 0.8472 -0.0268 -0.0094 -0.0465 343 ASP A OD1   
2826 O  OD2   . ASP A 343 ? 0.9854 1.0768 1.0838 -0.0219 -0.0056 -0.0438 343 ASP A OD2   
2827 N  N     . VAL A 344 ? 0.5495 0.6198 0.6304 -0.0284 -0.0036 -0.0528 344 VAL A N     
2828 C  CA    . VAL A 344 ? 0.5853 0.6507 0.6622 -0.0299 -0.0045 -0.0532 344 VAL A CA    
2829 C  C     . VAL A 344 ? 0.5592 0.6248 0.6336 -0.0323 -0.0037 -0.0534 344 VAL A C     
2830 O  O     . VAL A 344 ? 0.6486 0.7112 0.7208 -0.0338 -0.0047 -0.0526 344 VAL A O     
2831 C  CB    . VAL A 344 ? 0.5093 0.5707 0.5856 -0.0290 -0.0049 -0.0536 344 VAL A CB    
2832 C  CG1   . VAL A 344 ? 0.4557 0.5175 0.5363 -0.0268 -0.0052 -0.0523 344 VAL A CG1   
2833 C  CG2   . VAL A 344 ? 0.5021 0.5624 0.5759 -0.0289 -0.0033 -0.0558 344 VAL A CG2   
2834 N  N     . SER A 345 ? 0.5614 0.6309 0.6370 -0.0323 -0.0017 -0.0535 345 SER A N     
2835 C  CA    . SER A 345 ? 0.5616 0.6322 0.6354 -0.0345 -0.0004 -0.0525 345 SER A CA    
2836 C  C     . SER A 345 ? 0.5619 0.6337 0.6386 -0.0372 -0.0019 -0.0510 345 SER A C     
2837 O  O     . SER A 345 ? 0.6317 0.7024 0.7073 -0.0395 -0.0017 -0.0493 345 SER A O     
2838 C  CB    . SER A 345 ? 0.5635 0.6389 0.6386 -0.0332 0.0033  -0.0525 345 SER A CB    
2839 O  OG    . SER A 345 ? 0.4915 0.5723 0.5737 -0.0321 0.0036  -0.0516 345 SER A OG    
2840 N  N     . ARG A 346 ? 0.5173 0.5909 0.5972 -0.0372 -0.0036 -0.0515 346 ARG A N     
2841 C  CA    . ARG A 346 ? 0.5511 0.6245 0.6330 -0.0403 -0.0056 -0.0514 346 ARG A CA    
2842 C  C     . ARG A 346 ? 0.6055 0.6735 0.6844 -0.0401 -0.0076 -0.0533 346 ARG A C     
2843 O  O     . ARG A 346 ? 0.6847 0.7495 0.7638 -0.0426 -0.0091 -0.0542 346 ARG A O     
2844 C  CB    . ARG A 346 ? 0.6147 0.6955 0.7023 -0.0414 -0.0065 -0.0506 346 ARG A CB    
2845 C  CG    . ARG A 346 ? 0.6070 0.6943 0.6986 -0.0396 -0.0033 -0.0486 346 ARG A CG    
2846 C  CD    . ARG A 346 ? 0.6085 0.7042 0.7075 -0.0400 -0.0046 -0.0468 346 ARG A CD    
2847 N  NE    . ARG A 346 ? 0.5661 0.6690 0.6718 -0.0401 -0.0014 -0.0437 346 ARG A NE    
2848 C  CZ    . ARG A 346 ? 0.5128 0.6180 0.6193 -0.0362 0.0034  -0.0431 346 ARG A CZ    
2849 N  NH1   . ARG A 346 ? 0.5093 0.6093 0.6108 -0.0325 0.0047  -0.0457 346 ARG A NH1   
2850 N  NH2   . ARG A 346 ? 0.5141 0.6266 0.6269 -0.0360 0.0072  -0.0399 346 ARG A NH2   
2851 N  N     . SER A 347 ? 0.6877 0.7542 0.7644 -0.0371 -0.0074 -0.0539 347 SER A N     
2852 C  CA    . SER A 347 ? 0.7140 0.7766 0.7877 -0.0360 -0.0082 -0.0553 347 SER A CA    
2853 C  C     . SER A 347 ? 0.6789 0.7350 0.7516 -0.0361 -0.0075 -0.0550 347 SER A C     
2854 O  O     . SER A 347 ? 0.6258 0.6811 0.6993 -0.0363 -0.0069 -0.0530 347 SER A O     
2855 C  CB    . SER A 347 ? 0.6798 0.7441 0.7530 -0.0327 -0.0077 -0.0546 347 SER A CB    
2856 O  OG    . SER A 347 ? 0.9562 1.0190 1.0260 -0.0314 -0.0080 -0.0557 347 SER A OG    
2857 N  N     . SER A 348 ? 0.6455 0.6969 0.7160 -0.0359 -0.0076 -0.0569 348 SER A N     
2858 C  CA    . SER A 348 ? 0.6673 0.7124 0.7384 -0.0352 -0.0064 -0.0561 348 SER A CA    
2859 C  C     . SER A 348 ? 0.6369 0.6823 0.7090 -0.0319 -0.0050 -0.0536 348 SER A C     
2860 O  O     . SER A 348 ? 0.6116 0.6610 0.6835 -0.0302 -0.0050 -0.0531 348 SER A O     
2861 C  CB    . SER A 348 ? 0.6726 0.7115 0.7410 -0.0352 -0.0061 -0.0598 348 SER A CB    
2862 O  OG    . SER A 348 ? 0.6503 0.6895 0.7144 -0.0319 -0.0048 -0.0614 348 SER A OG    
2863 N  N     . THR A 349 ? 0.5529 0.5945 0.6277 -0.0312 -0.0042 -0.0513 349 THR A N     
2864 C  CA    . THR A 349 ? 0.6012 0.6440 0.6790 -0.0286 -0.0035 -0.0479 349 THR A CA    
2865 C  C     . THR A 349 ? 0.4877 0.5306 0.5645 -0.0251 -0.0012 -0.0487 349 THR A C     
2866 O  O     . THR A 349 ? 0.5239 0.5707 0.6029 -0.0236 -0.0011 -0.0463 349 THR A O     
2867 C  CB    . THR A 349 ? 0.5969 0.6363 0.6790 -0.0284 -0.0032 -0.0443 349 THR A CB    
2868 O  OG1   . THR A 349 ? 0.6549 0.6949 0.7370 -0.0317 -0.0051 -0.0427 349 THR A OG1   
2869 C  CG2   . THR A 349 ? 0.5526 0.5948 0.6396 -0.0264 -0.0034 -0.0398 349 THR A CG2   
2870 N  N     . GLY A 350 ? 0.5472 0.5859 0.6204 -0.0239 0.0007  -0.0522 350 GLY A N     
2871 C  CA    . GLY A 350 ? 0.4735 0.5127 0.5438 -0.0201 0.0036  -0.0531 350 GLY A CA    
2872 C  C     . GLY A 350 ? 0.5553 0.6008 0.6227 -0.0201 0.0025  -0.0531 350 GLY A C     
2873 O  O     . GLY A 350 ? 0.5990 0.6480 0.6676 -0.0172 0.0044  -0.0503 350 GLY A O     
2874 N  N     . ASN A 351 ? 0.5725 0.6199 0.6374 -0.0233 -0.0005 -0.0553 351 ASN A N     
2875 C  CA    . ASN A 351 ? 0.5681 0.6218 0.6319 -0.0230 -0.0016 -0.0545 351 ASN A CA    
2876 C  C     . ASN A 351 ? 0.4832 0.5404 0.5533 -0.0225 -0.0020 -0.0504 351 ASN A C     
2877 O  O     . ASN A 351 ? 0.5846 0.6458 0.6561 -0.0207 -0.0016 -0.0479 351 ASN A O     
2878 C  CB    . ASN A 351 ? 0.6797 0.7355 0.7414 -0.0263 -0.0046 -0.0571 351 ASN A CB    
2879 C  CG    . ASN A 351 ? 0.8215 0.8745 0.8761 -0.0273 -0.0054 -0.0616 351 ASN A CG    
2880 O  OD1   . ASN A 351 ? 0.8492 0.8981 0.8988 -0.0249 -0.0030 -0.0634 351 ASN A OD1   
2881 N  ND2   . ASN A 351 ? 0.7970 0.8523 0.8512 -0.0309 -0.0088 -0.0634 351 ASN A ND2   
2882 N  N     . LEU A 352 ? 0.4315 0.4870 0.5051 -0.0244 -0.0031 -0.0496 352 LEU A N     
2883 C  CA    . LEU A 352 ? 0.5442 0.6012 0.6225 -0.0244 -0.0040 -0.0467 352 LEU A CA    
2884 C  C     . LEU A 352 ? 0.5780 0.6358 0.6604 -0.0219 -0.0025 -0.0430 352 LEU A C     
2885 O  O     . LEU A 352 ? 0.5713 0.6317 0.6575 -0.0211 -0.0028 -0.0404 352 LEU A O     
2886 C  CB    . LEU A 352 ? 0.4975 0.5523 0.5766 -0.0269 -0.0057 -0.0465 352 LEU A CB    
2887 C  CG    . LEU A 352 ? 0.5134 0.5692 0.5906 -0.0291 -0.0069 -0.0484 352 LEU A CG    
2888 C  CD1   . LEU A 352 ? 0.6984 0.7559 0.7734 -0.0298 -0.0064 -0.0508 352 LEU A CD1   
2889 C  CD2   . LEU A 352 ? 0.5401 0.5940 0.6163 -0.0313 -0.0081 -0.0475 352 LEU A CD2   
2890 N  N     . VAL A 353 ? 0.5055 0.5610 0.5885 -0.0204 -0.0006 -0.0421 353 VAL A N     
2891 C  CA    . VAL A 353 ? 0.4802 0.5376 0.5687 -0.0175 0.0017  -0.0376 353 VAL A CA    
2892 C  C     . VAL A 353 ? 0.5655 0.6263 0.6517 -0.0147 0.0043  -0.0368 353 VAL A C     
2893 O  O     . VAL A 353 ? 0.5451 0.6097 0.6373 -0.0133 0.0052  -0.0321 353 VAL A O     
2894 C  CB    . VAL A 353 ? 0.4841 0.5382 0.5741 -0.0155 0.0043  -0.0369 353 VAL A CB    
2895 C  CG1   . VAL A 353 ? 0.5344 0.5913 0.6296 -0.0114 0.0084  -0.0323 353 VAL A CG1   
2896 C  CG2   . VAL A 353 ? 0.5021 0.5548 0.5966 -0.0181 0.0013  -0.0349 353 VAL A CG2   
2897 N  N     . GLU A 354 ? 0.4820 0.5420 0.5599 -0.0142 0.0052  -0.0410 354 GLU A N     
2898 C  CA    . GLU A 354 ? 0.5739 0.6378 0.6477 -0.0115 0.0074  -0.0398 354 GLU A CA    
2899 C  C     . GLU A 354 ? 0.6369 0.7057 0.7147 -0.0124 0.0053  -0.0367 354 GLU A C     
2900 O  O     . GLU A 354 ? 0.5368 0.6100 0.6172 -0.0100 0.0072  -0.0320 354 GLU A O     
2901 C  CB    . GLU A 354 ? 0.6037 0.6655 0.6665 -0.0117 0.0075  -0.0454 354 GLU A CB    
2902 C  CG    . GLU A 354 ? 0.6903 0.7472 0.7479 -0.0088 0.0117  -0.0481 354 GLU A CG    
2903 C  CD    . GLU A 354 ? 0.8027 0.8610 0.8492 -0.0063 0.0141  -0.0503 354 GLU A CD    
2904 O  OE1   . GLU A 354 ? 0.9837 1.0478 1.0273 -0.0070 0.0119  -0.0489 354 GLU A OE1   
2905 O  OE2   . GLU A 354 ? 0.6423 0.6958 0.6828 -0.0032 0.0183  -0.0533 354 GLU A OE2   
2906 N  N     A TRP A 355 ? 0.6420 0.7100 0.7210 -0.0154 0.0018  -0.0387 355 TRP A N     
2907 N  N     B TRP A 355 ? 0.6519 0.7198 0.7309 -0.0154 0.0018  -0.0387 355 TRP A N     
2908 C  CA    A TRP A 355 ? 0.6145 0.6855 0.6984 -0.0158 0.0002  -0.0361 355 TRP A CA    
2909 C  CA    B TRP A 355 ? 0.6052 0.6763 0.6891 -0.0157 0.0002  -0.0360 355 TRP A CA    
2910 C  C     A TRP A 355 ? 0.6492 0.7199 0.7422 -0.0158 0.0001  -0.0317 355 TRP A C     
2911 C  C     B TRP A 355 ? 0.6571 0.7278 0.7501 -0.0158 0.0001  -0.0317 355 TRP A C     
2912 O  O     A TRP A 355 ? 0.7293 0.8028 0.8275 -0.0146 0.0005  -0.0273 355 TRP A O     
2913 O  O     B TRP A 355 ? 0.6823 0.7559 0.7807 -0.0146 0.0005  -0.0273 355 TRP A O     
2914 C  CB    A TRP A 355 ? 0.6403 0.7102 0.7236 -0.0184 -0.0025 -0.0396 355 TRP A CB    
2915 C  CB    B TRP A 355 ? 0.6138 0.6839 0.6971 -0.0183 -0.0024 -0.0396 355 TRP A CB    
2916 C  CG    A TRP A 355 ? 0.6620 0.7346 0.7397 -0.0188 -0.0033 -0.0421 355 TRP A CG    
2917 C  CG    B TRP A 355 ? 0.7099 0.7828 0.7875 -0.0186 -0.0032 -0.0418 355 TRP A CG    
2918 C  CD1   A TRP A 355 ? 0.6848 0.7617 0.7581 -0.0172 -0.0029 -0.0408 355 TRP A CD1   
2919 C  CD1   B TRP A 355 ? 0.6693 0.7408 0.7427 -0.0209 -0.0045 -0.0460 355 TRP A CD1   
2920 C  CD2   A TRP A 355 ? 0.6750 0.7472 0.7509 -0.0213 -0.0050 -0.0456 355 TRP A CD2   
2921 C  CD2   B TRP A 355 ? 0.6694 0.7480 0.7457 -0.0170 -0.0034 -0.0393 355 TRP A CD2   
2922 N  NE1   A TRP A 355 ? 0.6513 0.7302 0.7205 -0.0190 -0.0052 -0.0437 355 TRP A NE1   
2923 N  NE1   B TRP A 355 ? 0.6524 0.7282 0.7222 -0.0212 -0.0059 -0.0466 355 TRP A NE1   
2924 C  CE2   A TRP A 355 ? 0.6552 0.7315 0.7270 -0.0215 -0.0063 -0.0464 355 TRP A CE2   
2925 C  CE2   B TRP A 355 ? 0.6543 0.7348 0.7254 -0.0187 -0.0054 -0.0425 355 TRP A CE2   
2926 C  CE3   A TRP A 355 ? 0.6671 0.7365 0.7445 -0.0235 -0.0057 -0.0478 355 TRP A CE3   
2927 C  CE3   B TRP A 355 ? 0.5655 0.6482 0.6453 -0.0145 -0.0023 -0.0339 355 TRP A CE3   
2928 C  CZ2   A TRP A 355 ? 0.6598 0.7378 0.7310 -0.0242 -0.0084 -0.0488 355 TRP A CZ2   
2929 C  CZ2   B TRP A 355 ? 0.5927 0.6795 0.6610 -0.0182 -0.0070 -0.0406 355 TRP A CZ2   
2930 C  CZ3   A TRP A 355 ? 0.6411 0.7122 0.7174 -0.0256 -0.0068 -0.0499 355 TRP A CZ3   
2931 C  CZ3   B TRP A 355 ? 0.5841 0.6730 0.6610 -0.0135 -0.0033 -0.0316 355 TRP A CZ3   
2932 C  CH2   A TRP A 355 ? 0.6060 0.6815 0.6802 -0.0261 -0.0083 -0.0503 355 TRP A CH2   
2933 C  CH2   B TRP A 355 ? 0.5985 0.6897 0.6693 -0.0153 -0.0058 -0.0351 355 TRP A CH2   
2934 N  N     . PHE A 356 ? 0.5373 0.6046 0.6328 -0.0174 -0.0010 -0.0323 356 PHE A N     
2935 C  CA    . PHE A 356 ? 0.6042 0.6715 0.7088 -0.0183 -0.0022 -0.0281 356 PHE A CA    
2936 C  C     . PHE A 356 ? 0.5291 0.6009 0.6390 -0.0153 0.0011  -0.0220 356 PHE A C     
2937 O  O     . PHE A 356 ? 0.5702 0.6441 0.6883 -0.0155 0.0006  -0.0171 356 PHE A O     
2938 C  CB    . PHE A 356 ? 0.5462 0.6106 0.6517 -0.0206 -0.0044 -0.0292 356 PHE A CB    
2939 C  CG    . PHE A 356 ? 0.6019 0.6669 0.7168 -0.0223 -0.0068 -0.0247 356 PHE A CG    
2940 C  CD1   . PHE A 356 ? 0.5824 0.6447 0.7000 -0.0255 -0.0109 -0.0257 356 PHE A CD1   
2941 C  CD2   . PHE A 356 ? 0.5756 0.6437 0.6972 -0.0208 -0.0052 -0.0195 356 PHE A CD2   
2942 C  CE1   . PHE A 356 ? 0.5312 0.5937 0.6574 -0.0280 -0.0143 -0.0219 356 PHE A CE1   
2943 C  CE2   . PHE A 356 ? 0.5177 0.5875 0.6496 -0.0230 -0.0082 -0.0146 356 PHE A CE2   
2944 C  CZ    . PHE A 356 ? 0.4893 0.5563 0.6235 -0.0271 -0.0134 -0.0159 356 PHE A CZ    
2945 N  N     . LEU A 357 ? 0.5490 0.6219 0.6543 -0.0124 0.0049  -0.0221 357 LEU A N     
2946 C  CA    . LEU A 357 ? 0.5493 0.6270 0.6585 -0.0087 0.0094  -0.0163 357 LEU A CA    
2947 C  C     . LEU A 357 ? 0.5712 0.6533 0.6784 -0.0069 0.0111  -0.0135 357 LEU A C     
2948 O  O     . LEU A 357 ? 0.4723 0.5593 0.5870 -0.0052 0.0134  -0.0064 357 LEU A O     
2949 C  CB    . LEU A 357 ? 0.4992 0.5755 0.6021 -0.0055 0.0139  -0.0185 357 LEU A CB    
2950 C  CG    . LEU A 357 ? 0.5114 0.5847 0.6193 -0.0060 0.0135  -0.0185 357 LEU A CG    
2951 C  CD1   . LEU A 357 ? 0.5028 0.5731 0.6042 -0.0022 0.0185  -0.0215 357 LEU A CD1   
2952 C  CD2   . LEU A 357 ? 0.4663 0.5441 0.5884 -0.0061 0.0133  -0.0106 357 LEU A CD2   
2953 N  N     . LEU A 358 ? 0.5293 0.6107 0.6275 -0.0074 0.0097  -0.0179 358 LEU A N     
2954 C  CA    . LEU A 358 ? 0.5158 0.6024 0.6124 -0.0057 0.0105  -0.0144 358 LEU A CA    
2955 C  C     . LEU A 358 ? 0.4736 0.5610 0.5819 -0.0072 0.0082  -0.0094 358 LEU A C     
2956 O  O     . LEU A 358 ? 0.3851 0.4775 0.4986 -0.0054 0.0102  -0.0023 358 LEU A O     
2957 C  CB    . LEU A 358 ? 0.5437 0.6300 0.6298 -0.0065 0.0085  -0.0198 358 LEU A CB    
2958 C  CG    . LEU A 358 ? 0.6465 0.7349 0.7198 -0.0041 0.0110  -0.0220 358 LEU A CG    
2959 C  CD1   . LEU A 358 ? 0.7455 0.8329 0.8103 -0.0065 0.0073  -0.0280 358 LEU A CD1   
2960 C  CD2   . LEU A 358 ? 0.8063 0.9021 0.8788 -0.0009 0.0140  -0.0150 358 LEU A CD2   
2961 N  N     . ARG A 359 ? 0.4194 0.5015 0.5315 -0.0106 0.0043  -0.0130 359 ARG A N     
2962 C  CA    . ARG A 359 ? 0.4452 0.5257 0.5679 -0.0122 0.0020  -0.0097 359 ARG A CA    
2963 C  C     . ARG A 359 ? 0.5630 0.6451 0.6968 -0.0125 0.0028  -0.0030 359 ARG A C     
2964 O  O     . ARG A 359 ? 0.4944 0.5789 0.6373 -0.0120 0.0033  0.0036  359 ARG A O     
2965 C  CB    . ARG A 359 ? 0.4041 0.4778 0.5263 -0.0155 -0.0018 -0.0161 359 ARG A CB    
2966 C  CG    . ARG A 359 ? 0.6190 0.6881 0.7511 -0.0182 -0.0047 -0.0148 359 ARG A CG    
2967 C  CD    . ARG A 359 ? 0.5298 0.5958 0.6657 -0.0181 -0.0056 -0.0153 359 ARG A CD    
2968 N  NE    . ARG A 359 ? 0.5499 0.6144 0.6778 -0.0176 -0.0056 -0.0214 359 ARG A NE    
2969 C  CZ    . ARG A 359 ? 0.5668 0.6289 0.6973 -0.0167 -0.0057 -0.0226 359 ARG A CZ    
2970 N  NH1   . ARG A 359 ? 0.5301 0.5896 0.6706 -0.0163 -0.0059 -0.0187 359 ARG A NH1   
2971 N  NH2   . ARG A 359 ? 0.4984 0.5609 0.6228 -0.0160 -0.0052 -0.0273 359 ARG A NH2   
2972 N  N     . LYS A 360 ? 0.5632 0.6449 0.6978 -0.0132 0.0030  -0.0036 360 LYS A N     
2973 C  CA    . LYS A 360 ? 0.5099 0.5946 0.6567 -0.0136 0.0036  0.0036  360 LYS A CA    
2974 C  C     . LYS A 360 ? 0.5260 0.6185 0.6755 -0.0094 0.0093  0.0115  360 LYS A C     
2975 O  O     . LYS A 360 ? 0.4861 0.5821 0.6482 -0.0098 0.0097  0.0196  360 LYS A O     
2976 C  CB    . LYS A 360 ? 0.4690 0.5529 0.6163 -0.0144 0.0031  0.0022  360 LYS A CB    
2977 C  CG    . LYS A 360 ? 0.5148 0.5924 0.6618 -0.0191 -0.0030 -0.0032 360 LYS A CG    
2978 C  CD    . LYS A 360 ? 0.4888 0.5641 0.6466 -0.0232 -0.0078 -0.0006 360 LYS A CD    
2979 C  CE    . LYS A 360 ? 0.5352 0.6041 0.6901 -0.0279 -0.0139 -0.0066 360 LYS A CE    
2980 N  NZ    . LYS A 360 ? 0.8225 0.8865 0.9847 -0.0321 -0.0188 -0.0066 360 LYS A NZ    
2981 N  N     . ALA A 361 ? 0.4406 0.5358 0.5780 -0.0055 0.0136  0.0094  361 ALA A N     
2982 C  CA    . ALA A 361 ? 0.5397 0.6425 0.6763 -0.0011 0.0195  0.0164  361 ALA A CA    
2983 C  C     . ALA A 361 ? 0.5602 0.6663 0.7010 -0.0011 0.0188  0.0221  361 ALA A C     
2984 O  O     . ALA A 361 ? 0.5413 0.6538 0.6902 0.0008  0.0223  0.0315  361 ALA A O     
2985 C  CB    . ALA A 361 ? 0.4175 0.5207 0.5373 0.0024  0.0234  0.0110  361 ALA A CB    
2986 N  N     . TYR A 362 ? 0.4417 0.5439 0.5782 -0.0029 0.0148  0.0173  362 TYR A N     
2987 C  CA    . TYR A 362 ? 0.5177 0.6222 0.6606 -0.0028 0.0139  0.0233  362 TYR A CA    
2988 C  C     . TYR A 362 ? 0.4874 0.5896 0.6480 -0.0056 0.0119  0.0292  362 TYR A C     
2989 O  O     . TYR A 362 ? 0.3703 0.4769 0.5404 -0.0046 0.0135  0.0384  362 TYR A O     
2990 C  CB    . TYR A 362 ? 0.4422 0.5428 0.5793 -0.0040 0.0101  0.0171  362 TYR A CB    
2991 C  CG    . TYR A 362 ? 0.4759 0.5795 0.6199 -0.0029 0.0096  0.0239  362 TYR A CG    
2992 C  CD1   . TYR A 362 ? 0.5276 0.6395 0.6645 0.0003  0.0118  0.0289  362 TYR A CD1   
2993 C  CD2   . TYR A 362 ? 0.4370 0.5348 0.5942 -0.0051 0.0069  0.0255  362 TYR A CD2   
2994 C  CE1   . TYR A 362 ? 0.5220 0.6373 0.6662 0.0015  0.0113  0.0365  362 TYR A CE1   
2995 C  CE2   . TYR A 362 ? 0.4842 0.5840 0.6492 -0.0037 0.0068  0.0323  362 TYR A CE2   
2996 C  CZ    . TYR A 362 ? 0.5583 0.6674 0.7175 -0.0003 0.0090  0.0384  362 TYR A CZ    
2997 O  OH    . TYR A 362 ? 0.6865 0.7983 0.8545 0.0012  0.0087  0.0465  362 TYR A OH    
2998 N  N     . GLU A 363 ? 0.5018 0.5974 0.6672 -0.0094 0.0081  0.0242  363 GLU A N     
2999 C  CA    . GLU A 363 ? 0.4900 0.5824 0.6716 -0.0130 0.0049  0.0288  363 GLU A CA    
3000 C  C     . GLU A 363 ? 0.4698 0.5701 0.6631 -0.0119 0.0085  0.0398  363 GLU A C     
3001 O  O     . GLU A 363 ? 0.4520 0.5525 0.6603 -0.0140 0.0073  0.0472  363 GLU A O     
3002 C  CB    . GLU A 363 ? 0.5352 0.6198 0.7171 -0.0175 -0.0003 0.0212  363 GLU A CB    
3003 C  CG    . GLU A 363 ? 0.5524 0.6288 0.7252 -0.0189 -0.0036 0.0113  363 GLU A CG    
3004 C  CD    . GLU A 363 ? 0.6683 0.7378 0.8393 -0.0232 -0.0084 0.0043  363 GLU A CD    
3005 O  OE1   . GLU A 363 ? 0.7267 0.7981 0.9040 -0.0254 -0.0100 0.0072  363 GLU A OE1   
3006 O  OE2   . GLU A 363 ? 0.5555 0.6185 0.7190 -0.0243 -0.0106 -0.0037 363 GLU A OE2   
3007 N  N     . ARG A 364 ? 0.5090 0.6158 0.6966 -0.0086 0.0134  0.0412  364 ARG A N     
3008 C  CA    . ARG A 364 ? 0.5344 0.6499 0.7333 -0.0067 0.0181  0.0519  364 ARG A CA    
3009 C  C     . ARG A 364 ? 0.5651 0.6897 0.7582 -0.0011 0.0254  0.0589  364 ARG A C     
3010 O  O     . ARG A 364 ? 0.6477 0.7807 0.8466 0.0019  0.0313  0.0672  364 ARG A O     
3011 C  CB    . ARG A 364 ? 0.4805 0.5976 0.6793 -0.0061 0.0196  0.0501  364 ARG A CB    
3012 C  CG    . ARG A 364 ? 0.5928 0.7014 0.7889 -0.0105 0.0130  0.0407  364 ARG A CG    
3013 C  CD    . ARG A 364 ? 0.7824 0.8873 0.9940 -0.0168 0.0059  0.0430  364 ARG A CD    
3014 N  NE    . ARG A 364 ? 1.0045 1.1011 1.2104 -0.0210 -0.0006 0.0336  364 ARG A NE    
3015 C  CZ    . ARG A 364 ? 0.9937 1.0912 1.2009 -0.0222 -0.0025 0.0324  364 ARG A CZ    
3016 N  NH1   . ARG A 364 ? 0.7536 0.8594 0.9686 -0.0194 0.0020  0.0398  364 ARG A NH1   
3017 N  NH2   . ARG A 364 ? 0.7997 0.8899 1.0003 -0.0261 -0.0085 0.0243  364 ARG A NH2   
3018 N  N     . ASN A 365 ? 0.5481 0.6718 0.7299 0.0005  0.0252  0.0562  365 ASN A N     
3019 C  CA    . ASN A 365 ? 0.5831 0.7157 0.7565 0.0055  0.0312  0.0624  365 ASN A CA    
3020 C  C     . ASN A 365 ? 0.5886 0.7257 0.7491 0.0102  0.0378  0.0602  365 ASN A C     
3021 O  O     . ASN A 365 ? 0.5254 0.6715 0.6836 0.0146  0.0447  0.0680  365 ASN A O     
3022 C  CB    . ASN A 365 ? 0.5813 0.7211 0.7708 0.0059  0.0337  0.0767  365 ASN A CB    
3023 C  CG    . ASN A 365 ? 0.7345 0.8807 0.9165 0.0092  0.0361  0.0826  365 ASN A CG    
3024 O  OD1   . ASN A 365 ? 0.7365 0.8906 0.9054 0.0139  0.0421  0.0850  365 ASN A OD1   
3025 N  ND2   . ASN A 365 ? 0.9034 1.0460 1.0934 0.0068  0.0315  0.0849  365 ASN A ND2   
3026 N  N     . GLU A 366 ? 0.5837 0.7143 0.7354 0.0094  0.0360  0.0495  366 GLU A N     
3027 C  CA    . GLU A 366 ? 0.5715 0.7035 0.7109 0.0138  0.0420  0.0456  366 GLU A CA    
3028 C  C     . GLU A 366 ? 0.5852 0.7152 0.7032 0.0154  0.0418  0.0373  366 GLU A C     
3029 O  O     . GLU A 366 ? 0.5564 0.6796 0.6690 0.0120  0.0357  0.0291  366 GLU A O     
3030 C  CB    . GLU A 366 ? 0.5579 0.6839 0.7017 0.0119  0.0401  0.0397  366 GLU A CB    
3031 C  CG    . GLU A 366 ? 0.6936 0.8224 0.8588 0.0097  0.0392  0.0479  366 GLU A CG    
3032 C  CD    . GLU A 366 ? 0.7987 0.9348 0.9694 0.0146  0.0474  0.0544  366 GLU A CD    
3033 O  OE1   . GLU A 366 ? 0.8071 0.9466 0.9647 0.0205  0.0550  0.0538  366 GLU A OE1   
3034 O  OE2   . GLU A 366 ? 0.9623 1.1009 1.1504 0.0127  0.0463  0.0601  366 GLU A OE2   
3035 N  N     . LEU A 367 ? 0.5990 0.7349 0.7045 0.0204  0.0483  0.0395  367 LEU A N     
3036 C  CA    . LEU A 367 ? 0.5363 0.6706 0.6204 0.0215  0.0476  0.0316  367 LEU A CA    
3037 C  C     . LEU A 367 ? 0.5867 0.7115 0.6615 0.0207  0.0464  0.0192  367 LEU A C     
3038 O  O     . LEU A 367 ? 0.5300 0.6530 0.6054 0.0237  0.0517  0.0179  367 LEU A O     
3039 C  CB    . LEU A 367 ? 0.6161 0.7586 0.6874 0.0272  0.0553  0.0364  367 LEU A CB    
3040 C  CG    . LEU A 367 ? 0.6661 0.8087 0.7145 0.0277  0.0535  0.0299  367 LEU A CG    
3041 C  CD1   . LEU A 367 ? 0.5851 0.7309 0.6367 0.0242  0.0462  0.0335  367 LEU A CD1   
3042 C  CD2   . LEU A 367 ? 0.6893 0.8393 0.7229 0.0338  0.0621  0.0338  367 LEU A CD2   
3043 N  N     . ALA A 368 ? 0.6194 0.7385 0.6872 0.0169  0.0396  0.0110  368 ALA A N     
3044 C  CA    . ALA A 368 ? 0.5510 0.6609 0.6122 0.0153  0.0378  0.0002  368 ALA A CA    
3045 C  C     . ALA A 368 ? 0.5531 0.6609 0.5954 0.0190  0.0425  -0.0062 368 ALA A C     
3046 O  O     . ALA A 368 ? 0.6163 0.7279 0.6446 0.0199  0.0424  -0.0068 368 ALA A O     
3047 C  CB    . ALA A 368 ? 0.6137 0.7192 0.6735 0.0102  0.0297  -0.0058 368 ALA A CB    
3048 N  N     . PRO A 369 ? 0.5712 0.6729 0.6123 0.0212  0.0467  -0.0109 369 PRO A N     
3049 C  CA    . PRO A 369 ? 0.6096 0.7064 0.6319 0.0245  0.0510  -0.0191 369 PRO A CA    
3050 C  C     . PRO A 369 ? 0.6222 0.7124 0.6318 0.0199  0.0439  -0.0292 369 PRO A C     
3051 O  O     . PRO A 369 ? 0.5927 0.6809 0.6097 0.0147  0.0367  -0.0307 369 PRO A O     
3052 C  CB    . PRO A 369 ? 0.5916 0.6822 0.6207 0.0276  0.0564  -0.0210 369 PRO A CB    
3053 C  CG    . PRO A 369 ? 0.6350 0.7307 0.6864 0.0265  0.0557  -0.0115 369 PRO A CG    
3054 C  CD    . PRO A 369 ? 0.5860 0.6848 0.6433 0.0209  0.0475  -0.0089 369 PRO A CD    
3055 N  N     . ASN A 370 ? 0.6327 0.7197 0.6227 0.0218  0.0460  -0.0363 370 ASN A N     
3056 C  CA    . ASN A 370 ? 0.6432 0.7248 0.6207 0.0170  0.0388  -0.0457 370 ASN A CA    
3057 C  C     . ASN A 370 ? 0.6716 0.7402 0.6482 0.0155  0.0383  -0.0554 370 ASN A C     
3058 O  O     . ASN A 370 ? 0.6461 0.7092 0.6263 0.0196  0.0449  -0.0563 370 ASN A O     
3059 C  CB    . ASN A 370 ? 0.6211 0.7053 0.5765 0.0187  0.0397  -0.0490 370 ASN A CB    
3060 C  CG    . ASN A 370 ? 0.6943 0.7918 0.6500 0.0193  0.0386  -0.0388 370 ASN A CG    
3061 O  OD1   . ASN A 370 ? 0.7202 0.8233 0.6896 0.0159  0.0332  -0.0326 370 ASN A OD1   
3062 N  ND2   . ASN A 370 ? 0.7576 0.8602 0.6981 0.0238  0.0442  -0.0369 370 ASN A ND2   
3063 N  N     . LYS A 371 ? 0.7672 0.8315 0.7405 0.0095  0.0303  -0.0617 371 LYS A N     
3064 C  CA    . LYS A 371 ? 0.7057 0.7574 0.6770 0.0074  0.0292  -0.0710 371 LYS A CA    
3065 C  C     . LYS A 371 ? 0.6683 0.7118 0.6206 0.0107  0.0339  -0.0798 371 LYS A C     
3066 O  O     . LYS A 371 ? 0.7015 0.7494 0.6382 0.0121  0.0345  -0.0808 371 LYS A O     
3067 C  CB    . LYS A 371 ? 0.6380 0.6885 0.6107 0.0000  0.0197  -0.0747 371 LYS A CB    
3068 C  CG    . LYS A 371 ? 0.7095 0.7654 0.7002 -0.0029 0.0159  -0.0679 371 LYS A CG    
3069 C  CD    . LYS A 371 ? 0.7435 0.7915 0.7411 -0.0074 0.0122  -0.0724 371 LYS A CD    
3070 C  CE    . LYS A 371 ? 0.8087 0.8621 0.8212 -0.0101 0.0088  -0.0664 371 LYS A CE    
3071 N  NZ    . LYS A 371 ? 0.8286 0.8751 0.8503 -0.0117 0.0087  -0.0675 371 LYS A NZ    
3072 N  N     . PRO A 372 ? 0.6985 0.7296 0.6513 0.0121  0.0373  -0.0863 372 PRO A N     
3073 C  CA    . PRO A 372 ? 0.8178 0.8391 0.7528 0.0163  0.0432  -0.0954 372 PRO A CA    
3074 C  C     . PRO A 372 ? 0.9336 0.9490 0.8502 0.0108  0.0360  -0.1058 372 PRO A C     
3075 O  O     . PRO A 372 ? 0.8661 0.8806 0.7874 0.0035  0.0270  -0.1078 372 PRO A O     
3076 C  CB    . PRO A 372 ? 0.8508 0.8600 0.7958 0.0187  0.0479  -0.0984 372 PRO A CB    
3077 C  CG    . PRO A 372 ? 0.7815 0.7917 0.7434 0.0124  0.0403  -0.0950 372 PRO A CG    
3078 C  CD    . PRO A 372 ? 0.7408 0.7661 0.7106 0.0106  0.0367  -0.0852 372 PRO A CD    
3079 N  N     . ASP A 373 ? 1.0248 1.0366 0.9200 0.0143  0.0402  -0.1124 373 ASP A N     
3080 C  CA    . ASP A 373 ? 1.0697 1.0731 0.9456 0.0091  0.0335  -0.1242 373 ASP A CA    
3081 C  C     . ASP A 373 ? 1.1392 1.1233 1.0136 0.0089  0.0356  -0.1354 373 ASP A C     
3082 O  O     . ASP A 373 ? 1.0792 1.0577 0.9690 0.0126  0.0415  -0.1329 373 ASP A O     
3083 C  CB    . ASP A 373 ? 1.0662 1.0741 0.9175 0.0124  0.0362  -0.1269 373 ASP A CB    
3084 C  CG    . ASP A 373 ? 1.1943 1.1951 1.0351 0.0220  0.0495  -0.1305 373 ASP A CG    
3085 O  OD1   . ASP A 373 ? 1.2549 1.2390 1.0920 0.0239  0.0536  -0.1406 373 ASP A OD1   
3086 O  OD2   . ASP A 373 ? 1.2568 1.2690 1.0936 0.0281  0.0564  -0.1226 373 ASP A OD2   
3087 N  N     . GLU A 374 ? 1.2105 1.1838 1.0667 0.0044  0.0302  -0.1478 374 GLU A N     
3088 C  CA    . GLU A 374 ? 1.2096 1.1632 1.0658 0.0027  0.0305  -0.1587 374 GLU A CA    
3089 C  C     . GLU A 374 ? 1.1519 1.0940 1.0037 0.0126  0.0439  -0.1629 374 GLU A C     
3090 O  O     . GLU A 374 ? 1.1799 1.1114 1.0461 0.0147  0.0481  -0.1634 374 GLU A O     
3091 C  CB    . GLU A 374 ? 1.2497 1.1943 1.0868 -0.0052 0.0209  -0.1713 374 GLU A CB    
3092 C  CG    . GLU A 374 ? 1.2899 1.2481 1.1301 -0.0144 0.0079  -0.1666 374 GLU A CG    
3093 C  CD    . GLU A 374 ? 1.3111 1.2798 1.1785 -0.0170 0.0049  -0.1545 374 GLU A CD    
3094 O  OE1   . GLU A 374 ? 1.2808 1.2647 1.1567 -0.0134 0.0076  -0.1431 374 GLU A OE1   
3095 O  OE2   . GLU A 374 ? 1.2923 1.2537 1.1723 -0.0227 0.0000  -0.1565 374 GLU A OE2   
3096 N  N     . LYS A 375 ? 1.1733 1.1179 1.0057 0.0191  0.0513  -0.1652 375 LYS A N     
3097 C  CA    . LYS A 375 ? 1.2329 1.1678 1.0612 0.0297  0.0654  -0.1685 375 LYS A CA    
3098 C  C     . LYS A 375 ? 1.2112 1.1551 1.0655 0.0358  0.0732  -0.1547 375 LYS A C     
3099 O  O     . LYS A 375 ? 1.2149 1.1483 1.0791 0.0417  0.0815  -0.1559 375 LYS A O     
3100 C  CB    . LYS A 375 ? 1.2738 1.2125 1.0757 0.0356  0.0721  -0.1721 375 LYS A CB    
3101 C  CG    . LYS A 375 ? 1.3177 1.2520 1.0925 0.0286  0.0625  -0.1838 375 LYS A CG    
3102 C  CD    . LYS A 375 ? 1.3636 1.2866 1.1086 0.0354  0.0717  -0.1961 375 LYS A CD    
3103 C  CE    . LYS A 375 ? 1.4952 1.4351 1.2209 0.0382  0.0733  -0.1907 375 LYS A CE    
3104 N  NZ    . LYS A 375 ? 1.5273 1.4757 1.2419 0.0275  0.0578  -0.1915 375 LYS A NZ    
3105 N  N     . GLU A 376 ? 1.1894 1.1524 1.0555 0.0345  0.0702  -0.1414 376 GLU A N     
3106 C  CA    . GLU A 376 ? 1.1465 1.1185 1.0372 0.0392  0.0761  -0.1284 376 GLU A CA    
3107 C  C     . GLU A 376 ? 1.0667 1.0322 0.9785 0.0347  0.0710  -0.1268 376 GLU A C     
3108 O  O     . GLU A 376 ? 1.1418 1.1057 1.0705 0.0397  0.0776  -0.1213 376 GLU A O     
3109 C  CB    . GLU A 376 ? 1.1461 1.1386 1.0437 0.0381  0.0734  -0.1154 376 GLU A CB    
3110 C  CG    . GLU A 376 ? 1.2379 1.2392 1.1144 0.0410  0.0762  -0.1150 376 GLU A CG    
3111 C  CD    . GLU A 376 ? 1.4437 1.4356 1.2992 0.0491  0.0874  -0.1239 376 GLU A CD    
3112 O  OE1   . GLU A 376 ? 1.5394 1.5249 1.4032 0.0566  0.0980  -0.1235 376 GLU A OE1   
3113 O  OE2   . GLU A 376 ? 1.3445 1.3355 1.1748 0.0480  0.0854  -0.1312 376 GLU A OE2   
3114 N  N     . LEU A 377 ? 1.0777 1.0405 0.9894 0.0253  0.0595  -0.1308 377 LEU A N     
3115 C  CA    . LEU A 377 ? 1.0626 1.0177 0.9914 0.0209  0.0551  -0.1306 377 LEU A CA    
3116 C  C     . LEU A 377 ? 1.1755 1.1116 1.1029 0.0253  0.0619  -0.1391 377 LEU A C     
3117 O  O     . LEU A 377 ? 1.1441 1.0758 1.0898 0.0267  0.0641  -0.1347 377 LEU A O     
3118 C  CB    . LEU A 377 ? 1.0700 1.0247 0.9965 0.0103  0.0425  -0.1345 377 LEU A CB    
3119 C  CG    . LEU A 377 ? 1.0092 0.9790 0.9509 0.0050  0.0351  -0.1239 377 LEU A CG    
3120 C  CD1   . LEU A 377 ? 1.0060 0.9751 0.9446 -0.0046 0.0238  -0.1284 377 LEU A CD1   
3121 C  CD2   . LEU A 377 ? 0.9634 0.9339 0.9270 0.0065  0.0374  -0.1158 377 LEU A CD2   
3122 N  N     . ALA A 378 ? 1.1410 1.0654 1.0465 0.0276  0.0653  -0.1514 378 ALA A N     
3123 C  CA    . ALA A 378 ? 1.1637 1.0681 1.0666 0.0325  0.0727  -0.1606 378 ALA A CA    
3124 C  C     . ALA A 378 ? 1.2061 1.1127 1.1208 0.0438  0.0860  -0.1532 378 ALA A C     
3125 O  O     . ALA A 378 ? 1.3848 1.2809 1.3139 0.0471  0.0906  -0.1528 378 ALA A O     
3126 C  CB    . ALA A 378 ? 1.1604 1.0517 1.0346 0.0326  0.0734  -0.1762 378 ALA A CB    
3127 N  N     . ARG A 379 ? 1.1824 1.1035 1.0929 0.0497  0.0925  -0.1463 379 ARG A N     
3128 C  CA    . ARG A 379 ? 1.0972 1.0228 1.0215 0.0602  0.1050  -0.1377 379 ARG A CA    
3129 C  C     . ARG A 379 ? 1.0899 1.0228 1.0436 0.0585  0.1021  -0.1250 379 ARG A C     
3130 O  O     . ARG A 379 ? 1.1834 1.1121 1.1524 0.0651  0.1099  -0.1208 379 ARG A O     
3131 C  CB    . ARG A 379 ? 1.1279 1.0700 1.0443 0.0657  0.1114  -0.1307 379 ARG A CB    
3132 C  CG    . ARG A 379 ? 1.0904 1.0455 1.0299 0.0729  0.1199  -0.1158 379 ARG A CG    
3133 C  CD    . ARG A 379 ? 1.1705 1.1448 1.1072 0.0755  0.1231  -0.1059 379 ARG A CD    
3134 N  NE    . ARG A 379 ? 1.3215 1.3102 1.2707 0.0674  0.1121  -0.0961 379 ARG A NE    
3135 C  CZ    . ARG A 379 ? 1.2330 1.2280 1.1695 0.0609  0.1036  -0.0975 379 ARG A CZ    
3136 N  NH1   . ARG A 379 ? 1.2574 1.2473 1.1678 0.0608  0.1037  -0.1076 379 ARG A NH1   
3137 N  NH2   . ARG A 379 ? 1.0801 1.0867 1.0304 0.0543  0.0946  -0.0886 379 ARG A NH2   
3138 N  N     . ARG A 380 ? 1.0266 0.9704 0.9882 0.0498  0.0909  -0.1188 380 ARG A N     
3139 C  CA    . ARG A 380 ? 1.0110 0.9628 0.9976 0.0475  0.0872  -0.1070 380 ARG A CA    
3140 C  C     . ARG A 380 ? 1.0471 0.9855 1.0441 0.0440  0.0835  -0.1102 380 ARG A C     
3141 O  O     . ARG A 380 ? 1.0430 0.9875 1.0590 0.0413  0.0794  -0.1009 380 ARG A O     
3142 C  CB    . ARG A 380 ? 0.9316 0.8986 0.9214 0.0399  0.0772  -0.1003 380 ARG A CB    
3143 C  CG    . ARG A 380 ? 0.8772 0.8584 0.8593 0.0427  0.0802  -0.0954 380 ARG A CG    
3144 C  CD    . ARG A 380 ? 0.8212 0.8153 0.8075 0.0353  0.0703  -0.0891 380 ARG A CD    
3145 N  NE    . ARG A 380 ? 0.7762 0.7844 0.7592 0.0382  0.0733  -0.0822 380 ARG A NE    
3146 C  CZ    . ARG A 380 ? 0.7294 0.7497 0.7175 0.0335  0.0669  -0.0752 380 ARG A CZ    
3147 N  NH1   . ARG A 380 ? 0.6836 0.7045 0.6794 0.0262  0.0574  -0.0746 380 ARG A NH1   
3148 N  NH2   . ARG A 380 ? 0.7226 0.7547 0.7083 0.0367  0.0705  -0.0684 380 ARG A NH2   
3149 N  N     . ARG A 381 ? 1.1191 1.0391 1.1039 0.0439  0.0845  -0.1228 381 ARG A N     
3150 C  CA    . ARG A 381 ? 1.1365 1.0427 1.1326 0.0412  0.0821  -0.1250 381 ARG A CA    
3151 C  C     . ARG A 381 ? 1.2340 1.1344 1.2447 0.0509  0.0929  -0.1205 381 ARG A C     
3152 O  O     . ARG A 381 ? 1.2607 1.1426 1.2692 0.0542  0.0978  -0.1287 381 ARG A O     
3153 C  CB    . ARG A 381 ? 1.1344 1.0223 1.1135 0.0365  0.0782  -0.1402 381 ARG A CB    
3154 C  CG    . ARG A 381 ? 1.1775 1.0717 1.1418 0.0273  0.0676  -0.1447 381 ARG A CG    
3155 C  CD    . ARG A 381 ? 1.2350 1.1332 1.2124 0.0175  0.0565  -0.1399 381 ARG A CD    
3156 N  NE    . ARG A 381 ? 1.4086 1.3171 1.3764 0.0096  0.0469  -0.1410 381 ARG A NE    
3157 C  CZ    . ARG A 381 ? 1.3551 1.2583 1.3033 0.0056  0.0426  -0.1516 381 ARG A CZ    
3158 N  NH1   . ARG A 381 ? 1.2915 1.1772 1.2252 0.0080  0.0464  -0.1640 381 ARG A NH1   
3159 N  NH2   . ARG A 381 ? 1.1797 1.0953 1.1229 -0.0011 0.0339  -0.1498 381 ARG A NH2   
3160 N  N     . GLN A 382 ? 1.4352 1.3510 1.4616 0.0554  0.0967  -0.1073 382 GLN A N     
3161 C  CA    . GLN A 382 ? 1.3694 1.2837 1.4123 0.0649  0.1069  -0.1004 382 GLN A CA    
3162 C  C     . GLN A 382 ? 1.3206 1.2362 1.3866 0.0617  0.1016  -0.0907 382 GLN A C     
3163 O  O     . GLN A 382 ? 1.3479 1.2640 1.4155 0.0525  0.0910  -0.0904 382 GLN A O     
3164 C  CB    . GLN A 382 ? 1.3151 1.2466 1.3627 0.0717  0.1140  -0.0908 382 GLN A CB    
3165 C  CG    . GLN A 382 ? 1.4092 1.3380 1.4359 0.0782  0.1233  -0.0990 382 GLN A CG    
3166 C  CD    . GLN A 382 ? 1.6406 1.5538 1.6658 0.0887  0.1364  -0.1054 382 GLN A CD    
3167 O  OE1   . GLN A 382 ? 1.6731 1.5696 1.6776 0.0898  0.1391  -0.1201 382 GLN A OE1   
3168 N  NE2   . GLN A 382 ? 1.5724 1.4909 1.6197 0.0966  0.1445  -0.0944 382 GLN A NE2   
3169 N  N     . LYS A 383 ? 1.2287 1.1459 1.3132 0.0696  0.1094  -0.0820 383 LYS A N     
3170 C  CA    . LYS A 383 ? 1.1379 1.0569 1.2448 0.0677  0.1052  -0.0715 383 LYS A CA    
3171 C  C     . LYS A 383 ? 1.0889 1.0229 1.2160 0.0746  0.1108  -0.0570 383 LYS A C     
3172 O  O     . LYS A 383 ? 1.2346 1.1670 1.3640 0.0847  0.1226  -0.0567 383 LYS A O     
3173 C  CB    . LYS A 383 ? 1.1996 1.0975 1.3102 0.0700  0.1085  -0.0776 383 LYS A CB    
3174 C  CG    . LYS A 383 ? 1.2503 1.1324 1.3492 0.0793  0.1207  -0.0890 383 LYS A CG    
3175 C  CD    . LYS A 383 ? 1.2739 1.1316 1.3707 0.0787  0.1213  -0.0991 383 LYS A CD    
3176 C  CE    . LYS A 383 ? 1.2954 1.1516 1.4181 0.0791  0.1196  -0.0876 383 LYS A CE    
3177 N  NZ    . LYS A 383 ? 1.2736 1.1350 1.4154 0.0908  0.1307  -0.0771 383 LYS A NZ    
3178 N  N     . TYR A 384 ? 1.0081 0.9568 1.1497 0.0692  0.1025  -0.0449 384 TYR A N     
3179 C  CA    . TYR A 384 ? 0.8824 0.8463 1.0452 0.0740  0.1054  -0.0301 384 TYR A CA    
3180 C  C     . TYR A 384 ? 0.8555 0.8223 1.0371 0.0700  0.0981  -0.0198 384 TYR A C     
3181 O  O     . TYR A 384 ? 0.8306 0.7928 1.0075 0.0618  0.0890  -0.0225 384 TYR A O     
3182 C  CB    . TYR A 384 ? 0.8422 0.8247 1.0033 0.0712  0.1022  -0.0244 384 TYR A CB    
3183 C  CG    . TYR A 384 ? 0.7595 0.7492 0.9153 0.0599  0.0890  -0.0239 384 TYR A CG    
3184 C  CD1   . TYR A 384 ? 0.7136 0.6975 0.8487 0.0540  0.0845  -0.0351 384 TYR A CD1   
3185 C  CD2   . TYR A 384 ? 0.7356 0.7383 0.9070 0.0553  0.0813  -0.0120 384 TYR A CD2   
3186 C  CE1   . TYR A 384 ? 0.7087 0.6993 0.8400 0.0447  0.0736  -0.0343 384 TYR A CE1   
3187 C  CE2   . TYR A 384 ? 0.7268 0.7352 0.8924 0.0457  0.0703  -0.0122 384 TYR A CE2   
3188 C  CZ    . TYR A 384 ? 0.7721 0.7744 0.9182 0.0408  0.0670  -0.0233 384 TYR A CZ    
3189 O  OH    . TYR A 384 ? 0.6077 0.6158 0.7492 0.0322  0.0571  -0.0232 384 TYR A OH    
3190 N  N     . GLU A 385 ? 0.9484 0.9237 1.1518 0.0762  0.1023  -0.0070 385 GLU A N     
3191 C  CA    . GLU A 385 ? 1.0156 0.9946 1.2378 0.0734  0.0959  0.0042  385 GLU A CA    
3192 C  C     . GLU A 385 ? 0.9777 0.9712 1.1998 0.0630  0.0829  0.0104  385 GLU A C     
3193 O  O     . GLU A 385 ? 0.8676 0.8703 1.0804 0.0594  0.0799  0.0085  385 GLU A O     
3194 C  CB    . GLU A 385 ? 0.9211 0.9076 1.1676 0.0826  0.1033  0.0173  385 GLU A CB    
3195 C  CG    . GLU A 385 ? 0.9479 0.9254 1.2104 0.0856  0.1041  0.0231  385 GLU A CG    
3196 C  CD    . GLU A 385 ? 0.9855 0.9774 1.2758 0.0910  0.1058  0.0408  385 GLU A CD    
3197 O  OE1   . GLU A 385 ? 1.0279 1.0249 1.3275 0.1003  0.1162  0.0444  385 GLU A OE1   
3198 O  OE2   . GLU A 385 ? 0.9414 0.9403 1.2444 0.0859  0.0967  0.0515  385 GLU A OE2   
3199 N  N     . GLY A 386 ? 0.9516 0.9465 1.1839 0.0584  0.0753  0.0178  386 GLY A N     
3200 C  CA    . GLY A 386 ? 0.7935 0.8004 1.0243 0.0488  0.0631  0.0229  386 GLY A CA    
3201 C  C     . GLY A 386 ? 0.8051 0.8267 1.0567 0.0486  0.0584  0.0390  386 GLY A C     
3202 O  O     . GLY A 386 ? 0.7410 0.7695 1.0088 0.0557  0.0644  0.0473  386 GLY A O     
3203 N  N     . GLY A 387 ? 0.6870 0.7141 0.9382 0.0404  0.0475  0.0437  387 GLY A N     
3204 C  CA    . GLY A 387 ? 0.6634 0.7048 0.9322 0.0389  0.0412  0.0587  387 GLY A CA    
3205 C  C     . GLY A 387 ? 0.7906 0.8283 1.0774 0.0444  0.0444  0.0682  387 GLY A C     
3206 O  O     . GLY A 387 ? 0.8453 0.8680 1.1292 0.0467  0.0487  0.0630  387 GLY A O     
3207 N  N     . TYR A 388 ? 0.7319 0.7837 1.0389 0.0463  0.0419  0.0829  388 TYR A N     
3208 C  CA    . TYR A 388 ? 0.7419 0.7932 1.0691 0.0515  0.0439  0.0947  388 TYR A CA    
3209 C  C     . TYR A 388 ? 0.6847 0.7360 1.0091 0.0441  0.0339  0.0996  388 TYR A C     
3210 O  O     . TYR A 388 ? 0.7044 0.7642 1.0182 0.0351  0.0234  0.0998  388 TYR A O     
3211 C  CB    . TYR A 388 ? 0.7192 0.7879 1.0702 0.0556  0.0436  0.1101  388 TYR A CB    
3212 C  CG    . TYR A 388 ? 0.8360 0.9093 1.2095 0.0588  0.0418  0.1259  388 TYR A CG    
3213 C  CD1   . TYR A 388 ? 0.7349 0.8241 1.1167 0.0519  0.0291  0.1391  388 TYR A CD1   
3214 C  CD2   . TYR A 388 ? 0.8115 0.8730 1.1978 0.0688  0.0527  0.1276  388 TYR A CD2   
3215 C  CE1   . TYR A 388 ? 0.6958 0.7903 1.0984 0.0547  0.0269  0.1547  388 TYR A CE1   
3216 C  CE2   . TYR A 388 ? 0.7812 0.8471 1.1898 0.0722  0.0512  0.1430  388 TYR A CE2   
3217 C  CZ    . TYR A 388 ? 0.7529 0.8360 1.1698 0.0651  0.0381  0.1571  388 TYR A CZ    
3218 O  OH    . TYR A 388 ? 0.8341 0.9228 1.2734 0.0683  0.0361  0.1737  388 TYR A OH    
3219 N  N     . VAL A 389 ? 0.7473 0.7883 1.0807 0.0481  0.0376  0.1034  389 VAL A N     
3220 C  CA    . VAL A 389 ? 0.8708 0.9123 1.2042 0.0421  0.0292  0.1104  389 VAL A CA    
3221 C  C     . VAL A 389 ? 0.8451 0.8828 1.2014 0.0495  0.0338  0.1226  389 VAL A C     
3222 O  O     . VAL A 389 ? 0.9622 0.9857 1.3250 0.0580  0.0450  0.1178  389 VAL A O     
3223 C  CB    . VAL A 389 ? 0.7798 0.8076 1.0914 0.0360  0.0278  0.0971  389 VAL A CB    
3224 C  CG1   . VAL A 389 ? 0.8190 0.8263 1.1281 0.0422  0.0388  0.0857  389 VAL A CG1   
3225 C  CG2   . VAL A 389 ? 0.6317 0.6621 0.9434 0.0296  0.0195  0.1058  389 VAL A CG2   
3226 N  N     . LYS A 390 ? 0.8831 0.9336 1.2516 0.0464  0.0252  0.1385  390 LYS A N     
3227 C  CA    . LYS A 390 ? 0.9223 0.9726 1.3156 0.0533  0.0283  0.1533  390 LYS A CA    
3228 C  C     . LYS A 390 ? 0.8978 0.9407 1.2887 0.0491  0.0240  0.1576  390 LYS A C     
3229 O  O     . LYS A 390 ? 0.8778 0.9245 1.2515 0.0395  0.0151  0.1553  390 LYS A O     
3230 C  CB    . LYS A 390 ? 0.9923 1.0650 1.4052 0.0537  0.0215  0.1713  390 LYS A CB    
3231 C  CG    . LYS A 390 ? 0.9469 1.0354 1.3496 0.0423  0.0062  0.1777  390 LYS A CG    
3232 C  CD    . LYS A 390 ? 0.8572 0.9665 1.2821 0.0426  -0.0014 0.1978  390 LYS A CD    
3233 C  CE    . LYS A 390 ? 1.0066 1.1134 1.4569 0.0508  0.0033  0.2126  390 LYS A CE    
3234 N  NZ    . LYS A 390 ? 0.9602 1.0869 1.4253 0.0471  -0.0087 0.2332  390 LYS A NZ    
3235 N  N     . GLU A 391 ? 0.8091 0.8413 1.2180 0.0565  0.0310  0.1643  391 GLU A N     
3236 C  CA    . GLU A 391 ? 0.7517 0.7783 1.1637 0.0533  0.0272  0.1721  391 GLU A CA    
3237 C  C     . GLU A 391 ? 0.7433 0.7916 1.1617 0.0476  0.0146  0.1902  391 GLU A C     
3238 O  O     . GLU A 391 ? 0.7332 0.7955 1.1721 0.0521  0.0132  0.2046  391 GLU A O     
3239 C  CB    . GLU A 391 ? 0.7094 0.7203 1.1429 0.0633  0.0374  0.1770  391 GLU A CB    
3240 C  CG    . GLU A 391 ? 0.7921 0.7771 1.2142 0.0644  0.0457  0.1599  391 GLU A CG    
3241 C  CD    . GLU A 391 ? 0.8472 0.8268 1.2557 0.0547  0.0389  0.1581  391 GLU A CD    
3242 O  OE1   . GLU A 391 ? 0.8444 0.8363 1.2591 0.0502  0.0305  0.1737  391 GLU A OE1   
3243 O  OE2   . GLU A 391 ? 0.9654 0.9293 1.3569 0.0515  0.0419  0.1416  391 GLU A OE2   
3244 N  N     . PRO A 392 ? 0.7446 0.7972 1.1461 0.0377  0.0054  0.1905  392 PRO A N     
3245 C  CA    . PRO A 392 ? 0.7068 0.7805 1.1097 0.0316  -0.0072 0.2061  392 PRO A CA    
3246 C  C     . PRO A 392 ? 0.7977 0.8760 1.2256 0.0361  -0.0083 0.2269  392 PRO A C     
3247 O  O     . PRO A 392 ? 0.8308 0.8940 1.2691 0.0408  -0.0012 0.2289  392 PRO A O     
3248 C  CB    . PRO A 392 ? 0.7039 0.7768 1.0811 0.0213  -0.0139 0.1992  392 PRO A CB    
3249 C  CG    . PRO A 392 ? 0.8007 0.8541 1.1635 0.0217  -0.0054 0.1794  392 PRO A CG    
3250 C  CD    . PRO A 392 ? 0.7602 0.7985 1.1411 0.0320  0.0063  0.1773  392 PRO A CD    
3251 N  N     . GLU A 393 ? 0.7497 0.8493 1.1882 0.0344  -0.0176 0.2428  393 GLU A N     
3252 C  CA    . GLU A 393 ? 0.7299 0.8380 1.1891 0.0364  -0.0218 0.2648  393 GLU A CA    
3253 C  C     . GLU A 393 ? 0.7897 0.8956 1.2330 0.0287  -0.0276 0.2674  393 GLU A C     
3254 O  O     . GLU A 393 ? 0.7593 0.8810 1.1886 0.0201  -0.0394 0.2733  393 GLU A O     
3255 C  CB    . GLU A 393 ? 0.7029 0.8359 1.1739 0.0346  -0.0325 0.2807  393 GLU A CB    
3256 C  CG    . GLU A 393 ? 0.7746 0.9125 1.2619 0.0415  -0.0272 0.2792  393 GLU A CG    
3257 C  CD    . GLU A 393 ? 0.7968 0.9240 1.3127 0.0547  -0.0140 0.2851  393 GLU A CD    
3258 O  OE1   . GLU A 393 ? 0.9384 1.0646 1.4718 0.0583  -0.0138 0.3005  393 GLU A OE1   
3259 O  OE2   . GLU A 393 ? 0.8769 0.9963 1.3975 0.0617  -0.0034 0.2746  393 GLU A OE2   
3260 N  N     . ARG A 394 ? 0.8040 0.8902 1.2490 0.0315  -0.0192 0.2629  394 ARG A N     
3261 C  CA    . ARG A 394 ? 0.8682 0.9499 1.2961 0.0240  -0.0226 0.2618  394 ARG A CA    
3262 C  C     . ARG A 394 ? 0.7651 0.8647 1.1972 0.0196  -0.0332 0.2834  394 ARG A C     
3263 O  O     . ARG A 394 ? 0.8875 0.9963 1.3436 0.0246  -0.0352 0.3019  394 ARG A O     
3264 C  CB    . ARG A 394 ? 0.9533 1.0112 1.3889 0.0282  -0.0121 0.2567  394 ARG A CB    
3265 C  CG    . ARG A 394 ? 0.9822 1.0208 1.4204 0.0350  -0.0003 0.2390  394 ARG A CG    
3266 C  CD    . ARG A 394 ? 1.2326 1.2459 1.6749 0.0375  0.0087  0.2316  394 ARG A CD    
3267 N  NE    . ARG A 394 ? 1.4040 1.4116 1.8271 0.0285  0.0057  0.2252  394 ARG A NE    
3268 C  CZ    . ARG A 394 ? 1.2706 1.2866 1.6922 0.0225  -0.0009 0.2388  394 ARG A CZ    
3269 N  NH1   . ARG A 394 ? 1.3089 1.3368 1.7484 0.0246  -0.0051 0.2607  394 ARG A NH1   
3270 N  NH2   . ARG A 394 ? 0.9177 0.9301 1.3200 0.0144  -0.0028 0.2309  394 ARG A NH2   
3271 N  N     . GLY A 395 ? 0.8160 0.9211 1.2243 0.0103  -0.0400 0.2814  395 GLY A N     
3272 C  CA    . GLY A 395 ? 0.7516 0.8729 1.1596 0.0056  -0.0498 0.3010  395 GLY A CA    
3273 C  C     . GLY A 395 ? 0.7901 0.9300 1.1734 -0.0034 -0.0617 0.2994  395 GLY A C     
3274 O  O     . GLY A 395 ? 0.8137 0.9511 1.1764 -0.0072 -0.0616 0.2812  395 GLY A O     
3275 N  N     . LEU A 396 ? 0.7660 0.9244 1.1510 -0.0068 -0.0722 0.3185  396 LEU A N     
3276 C  CA    . LEU A 396 ? 0.8468 1.0226 1.2066 -0.0159 -0.0844 0.3183  396 LEU A CA    
3277 C  C     . LEU A 396 ? 0.8358 1.0290 1.2068 -0.0158 -0.0938 0.3268  396 LEU A C     
3278 O  O     . LEU A 396 ? 0.8286 1.0289 1.2270 -0.0103 -0.0950 0.3448  396 LEU A O     
3279 C  CB    . LEU A 396 ? 0.8770 1.0620 1.2264 -0.0211 -0.0905 0.3333  396 LEU A CB    
3280 C  CG    . LEU A 396 ? 0.9860 1.1902 1.3092 -0.0303 -0.1039 0.3361  396 LEU A CG    
3281 C  CD1   . LEU A 396 ? 0.8612 1.0588 1.1517 -0.0363 -0.1021 0.3148  396 LEU A CD1   
3282 C  CD2   . LEU A 396 ? 0.9588 1.1758 1.2818 -0.0329 -0.1104 0.3582  396 LEU A CD2   
3283 N  N     . TRP A 397 ? 0.8618 1.0616 1.2128 -0.0217 -0.1002 0.3143  397 TRP A N     
3284 C  CA    . TRP A 397 ? 0.9028 1.1192 1.2617 -0.0235 -0.1103 0.3204  397 TRP A CA    
3285 C  C     . TRP A 397 ? 0.9301 1.1598 1.2594 -0.0343 -0.1237 0.3173  397 TRP A C     
3286 O  O     . TRP A 397 ? 0.8962 1.1199 1.1977 -0.0394 -0.1228 0.3059  397 TRP A O     
3287 C  CB    . TRP A 397 ? 0.7731 0.9821 1.1415 -0.0190 -0.1037 0.3062  397 TRP A CB    
3288 C  CG    . TRP A 397 ? 0.7855 0.9811 1.1812 -0.0080 -0.0902 0.3076  397 TRP A CG    
3289 C  CD1   . TRP A 397 ? 0.7658 0.9408 1.1606 -0.0033 -0.0775 0.2979  397 TRP A CD1   
3290 C  CD2   . TRP A 397 ? 0.6962 0.8976 1.1240 0.0000  -0.0878 0.3191  397 TRP A CD2   
3291 N  NE1   . TRP A 397 ? 0.7758 0.9421 1.1987 0.0071  -0.0674 0.3017  397 TRP A NE1   
3292 C  CE2   . TRP A 397 ? 0.7047 0.8871 1.1484 0.0097  -0.0728 0.3149  397 TRP A CE2   
3293 C  CE3   . TRP A 397 ? 0.7474 0.9684 1.1926 -0.0003 -0.0969 0.3328  397 TRP A CE3   
3294 C  CZ2   . TRP A 397 ? 0.8058 0.9879 1.2813 0.0200  -0.0656 0.3234  397 TRP A CZ2   
3295 C  CZ3   . TRP A 397 ? 0.7203 0.9424 1.1990 0.0097  -0.0899 0.3424  397 TRP A CZ3   
3296 C  CH2   . TRP A 397 ? 0.7367 0.9392 1.2298 0.0202  -0.0738 0.3375  397 TRP A CH2   
3297 N  N     . GLU A 398 ? 0.9241 1.1720 1.2601 -0.0378 -0.1362 0.3275  398 GLU A N     
3298 C  CA    . GLU A 398 ? 0.9315 1.1925 1.2406 -0.0484 -0.1505 0.3255  398 GLU A CA    
3299 C  C     . GLU A 398 ? 0.9250 1.1933 1.2385 -0.0514 -0.1576 0.3191  398 GLU A C     
3300 O  O     . GLU A 398 ? 0.9259 1.1964 1.2685 -0.0453 -0.1544 0.3247  398 GLU A O     
3301 C  CB    . GLU A 398 ? 0.9838 1.2632 1.2938 -0.0522 -0.1627 0.3481  398 GLU A CB    
3302 C  CG    . GLU A 398 ? 1.1178 1.3935 1.4417 -0.0462 -0.1555 0.3635  398 GLU A CG    
3303 C  CD    . GLU A 398 ? 1.3072 1.5840 1.6724 -0.0365 -0.1504 0.3793  398 GLU A CD    
3304 O  OE1   . GLU A 398 ? 1.2049 1.4727 1.5869 -0.0306 -0.1422 0.3699  398 GLU A OE1   
3305 O  OE2   . GLU A 398 ? 1.4439 1.7307 1.8249 -0.0345 -0.1542 0.4014  398 GLU A OE2   
3306 N  N     . ASN A 399 ? 0.8750 1.1468 1.1595 -0.0607 -0.1669 0.3073  399 ASN A N     
3307 C  CA    . ASN A 399 ? 0.8407 1.1193 1.1259 -0.0656 -0.1755 0.3006  399 ASN A CA    
3308 C  C     . ASN A 399 ? 0.8263 1.0925 1.1273 -0.0591 -0.1634 0.2880  399 ASN A C     
3309 O  O     . ASN A 399 ? 0.8443 1.1172 1.1732 -0.0551 -0.1635 0.2958  399 ASN A O     
3310 C  CB    . ASN A 399 ? 0.8730 1.1733 1.1787 -0.0683 -0.1898 0.3215  399 ASN A CB    
3311 C  CG    . ASN A 399 ? 0.9858 1.2999 1.2725 -0.0760 -0.2035 0.3334  399 ASN A CG    
3312 O  OD1   . ASN A 399 ? 1.1025 1.4131 1.3545 -0.0830 -0.2075 0.3216  399 ASN A OD1   
3313 N  ND2   . ASN A 399 ? 0.9381 1.2683 1.2472 -0.0743 -0.2106 0.3571  399 ASN A ND2   
3314 N  N     . ILE A 400 ? 0.7817 1.0304 1.0642 -0.0579 -0.1529 0.2689  400 ILE A N     
3315 C  CA    . ILE A 400 ? 0.7345 0.9696 1.0278 -0.0514 -0.1402 0.2558  400 ILE A CA    
3316 C  C     . ILE A 400 ? 0.7160 0.9485 0.9916 -0.0576 -0.1440 0.2385  400 ILE A C     
3317 O  O     . ILE A 400 ? 0.6998 0.9314 0.9466 -0.0652 -0.1503 0.2293  400 ILE A O     
3318 C  CB    . ILE A 400 ? 0.8139 1.0309 1.1017 -0.0454 -0.1254 0.2472  400 ILE A CB    
3319 C  CG1   . ILE A 400 ? 0.7976 1.0168 1.0962 -0.0418 -0.1239 0.2642  400 ILE A CG1   
3320 C  CG2   . ILE A 400 ? 0.7887 0.9933 1.0931 -0.0371 -0.1123 0.2382  400 ILE A CG2   
3321 C  CD1   . ILE A 400 ? 0.8839 1.0850 1.1856 -0.0350 -0.1092 0.2581  400 ILE A CD1   
3322 N  N     . VAL A 401 ? 0.6199 0.8509 0.9129 -0.0539 -0.1396 0.2344  401 VAL A N     
3323 C  CA    . VAL A 401 ? 0.6678 0.8941 0.9483 -0.0583 -0.1408 0.2180  401 VAL A CA    
3324 C  C     . VAL A 401 ? 0.6340 0.8443 0.9187 -0.0505 -0.1249 0.2051  401 VAL A C     
3325 O  O     . VAL A 401 ? 0.6398 0.8480 0.9481 -0.0418 -0.1156 0.2115  401 VAL A O     
3326 C  CB    . VAL A 401 ? 0.5820 0.8228 0.8791 -0.0624 -0.1515 0.2252  401 VAL A CB    
3327 C  CG1   . VAL A 401 ? 0.7196 0.9735 1.0024 -0.0731 -0.1693 0.2313  401 VAL A CG1   
3328 C  CG2   . VAL A 401 ? 0.6568 0.9064 0.9905 -0.0543 -0.1474 0.2421  401 VAL A CG2   
3329 N  N     . TYR A 402 ? 0.5128 0.7119 0.7742 -0.0536 -0.1218 0.1870  402 TYR A N     
3330 C  CA    . TYR A 402 ? 0.6203 0.8051 0.8825 -0.0476 -0.1084 0.1737  402 TYR A CA    
3331 C  C     . TYR A 402 ? 0.6069 0.7937 0.8717 -0.0501 -0.1107 0.1662  402 TYR A C     
3332 O  O     . TYR A 402 ? 0.5920 0.7802 0.8392 -0.0582 -0.1194 0.1586  402 TYR A O     
3333 C  CB    . TYR A 402 ? 0.6081 0.7793 0.8449 -0.0486 -0.1025 0.1598  402 TYR A CB    
3334 C  CG    . TYR A 402 ? 0.6202 0.7772 0.8567 -0.0429 -0.0896 0.1462  402 TYR A CG    
3335 C  CD1   . TYR A 402 ? 0.6086 0.7595 0.8637 -0.0341 -0.0788 0.1494  402 TYR A CD1   
3336 C  CD2   . TYR A 402 ? 0.6713 0.8210 0.8887 -0.0463 -0.0884 0.1302  402 TYR A CD2   
3337 C  CE1   . TYR A 402 ? 0.6193 0.7576 0.8723 -0.0293 -0.0677 0.1368  402 TYR A CE1   
3338 C  CE2   . TYR A 402 ? 0.7746 0.9125 0.9914 -0.0414 -0.0775 0.1187  402 TYR A CE2   
3339 C  CZ    . TYR A 402 ? 0.7423 0.8748 0.9761 -0.0332 -0.0675 0.1219  402 TYR A CZ    
3340 O  OH    . TYR A 402 ? 0.7602 0.8812 0.9915 -0.0287 -0.0573 0.1102  402 TYR A OH    
3341 N  N     . LEU A 403 ? 0.5826 0.7691 0.8693 -0.0432 -0.1028 0.1684  403 LEU A N     
3342 C  CA    . LEU A 403 ? 0.5463 0.7350 0.8388 -0.0446 -0.1033 0.1629  403 LEU A CA    
3343 C  C     . LEU A 403 ? 0.5950 0.7699 0.8855 -0.0376 -0.0888 0.1506  403 LEU A C     
3344 O  O     . LEU A 403 ? 0.5803 0.7497 0.8823 -0.0291 -0.0781 0.1534  403 LEU A O     
3345 C  CB    . LEU A 403 ? 0.4635 0.6674 0.7858 -0.0429 -0.1073 0.1786  403 LEU A CB    
3346 C  CG    . LEU A 403 ? 0.5400 0.7598 0.8707 -0.0481 -0.1211 0.1949  403 LEU A CG    
3347 C  CD1   . LEU A 403 ? 0.4764 0.7117 0.8395 -0.0458 -0.1239 0.2101  403 LEU A CD1   
3348 C  CD2   . LEU A 403 ? 0.5007 0.7232 0.8074 -0.0600 -0.1356 0.1889  403 LEU A CD2   
3349 N  N     . ASP A 404 ? 0.5245 0.6935 0.8007 -0.0413 -0.0886 0.1372  404 ASP A N     
3350 C  CA    . ASP A 404 ? 0.6013 0.7581 0.8740 -0.0352 -0.0757 0.1257  404 ASP A CA    
3351 C  C     . ASP A 404 ? 0.5628 0.7207 0.8357 -0.0378 -0.0766 0.1190  404 ASP A C     
3352 O  O     . ASP A 404 ? 0.5440 0.7085 0.8137 -0.0456 -0.0876 0.1196  404 ASP A O     
3353 C  CB    . ASP A 404 ? 0.5861 0.7294 0.8354 -0.0355 -0.0711 0.1135  404 ASP A CB    
3354 C  CG    . ASP A 404 ? 0.7118 0.8525 0.9381 -0.0436 -0.0781 0.1028  404 ASP A CG    
3355 O  OD1   . ASP A 404 ? 0.8220 0.9712 1.0479 -0.0502 -0.0889 0.1059  404 ASP A OD1   
3356 O  OD2   . ASP A 404 ? 0.8145 0.9446 1.0235 -0.0434 -0.0729 0.0912  404 ASP A OD2   
3357 N  N     . PHE A 405 ? 0.5137 0.6648 0.7904 -0.0312 -0.0651 0.1130  405 PHE A N     
3358 C  CA    . PHE A 405 ? 0.5512 0.7032 0.8295 -0.0327 -0.0644 0.1078  405 PHE A CA    
3359 C  C     . PHE A 405 ? 0.6266 0.7691 0.8803 -0.0382 -0.0666 0.0932  405 PHE A C     
3360 O  O     . PHE A 405 ? 0.6571 0.7907 0.8932 -0.0384 -0.0646 0.0856  405 PHE A O     
3361 C  CB    . PHE A 405 ? 0.5669 0.7158 0.8568 -0.0233 -0.0508 0.1072  405 PHE A CB    
3362 C  CG    . PHE A 405 ? 0.5523 0.7112 0.8687 -0.0170 -0.0472 0.1216  405 PHE A CG    
3363 C  CD1   . PHE A 405 ? 0.5879 0.7602 0.9244 -0.0184 -0.0511 0.1314  405 PHE A CD1   
3364 C  CD2   . PHE A 405 ? 0.4801 0.6348 0.8027 -0.0095 -0.0397 0.1256  405 PHE A CD2   
3365 C  CE1   . PHE A 405 ? 0.5940 0.7766 0.9567 -0.0120 -0.0471 0.1456  405 PHE A CE1   
3366 C  CE2   . PHE A 405 ? 0.5678 0.7313 0.9159 -0.0028 -0.0355 0.1390  405 PHE A CE2   
3367 C  CZ    . PHE A 405 ? 0.5279 0.7060 0.8962 -0.0038 -0.0390 0.1493  405 PHE A CZ    
3368 N  N     . ARG A 406 ? 0.5914 0.7362 0.8456 -0.0426 -0.0706 0.0899  406 ARG A N     
3369 C  CA    . ARG A 406 ? 0.5853 0.7208 0.8192 -0.0468 -0.0716 0.0764  406 ARG A CA    
3370 C  C     . ARG A 406 ? 0.6076 0.7357 0.8403 -0.0402 -0.0595 0.0693  406 ARG A C     
3371 O  O     . ARG A 406 ? 0.5509 0.6835 0.7978 -0.0375 -0.0557 0.0730  406 ARG A O     
3372 C  CB    . ARG A 406 ? 0.6643 0.8043 0.8994 -0.0550 -0.0822 0.0762  406 ARG A CB    
3373 C  CG    . ARG A 406 ? 0.6165 0.7467 0.8361 -0.0575 -0.0808 0.0631  406 ARG A CG    
3374 C  CD    . ARG A 406 ? 0.7013 0.8344 0.9246 -0.0654 -0.0907 0.0629  406 ARG A CD    
3375 N  NE    . ARG A 406 ? 0.7610 0.8974 0.9769 -0.0733 -0.1036 0.0644  406 ARG A NE    
3376 C  CZ    . ARG A 406 ? 0.9705 1.1137 1.1957 -0.0807 -0.1150 0.0694  406 ARG A CZ    
3377 N  NH1   . ARG A 406 ? 0.9583 1.1063 1.2025 -0.0813 -0.1151 0.0742  406 ARG A NH1   
3378 N  NH2   . ARG A 406 ? 1.0951 1.2407 1.3101 -0.0880 -0.1269 0.0699  406 ARG A NH2   
3379 N  N     . SER A 407 ? 0.5254 0.6430 0.7412 -0.0380 -0.0537 0.0596  407 SER A N     
3380 C  CA    . SER A 407 ? 0.4993 0.6095 0.7105 -0.0326 -0.0433 0.0518  407 SER A CA    
3381 C  C     . SER A 407 ? 0.5508 0.6650 0.7796 -0.0250 -0.0348 0.0585  407 SER A C     
3382 O  O     . SER A 407 ? 0.5448 0.6619 0.7806 -0.0236 -0.0318 0.0591  407 SER A O     
3383 C  CB    . SER A 407 ? 0.5693 0.6768 0.7725 -0.0365 -0.0454 0.0441  407 SER A CB    
3384 O  OG    . SER A 407 ? 0.6193 0.7233 0.8072 -0.0432 -0.0533 0.0382  407 SER A OG    
3385 N  N     . LEU A 408 ? 0.5454 0.6595 0.7815 -0.0199 -0.0305 0.0639  408 LEU A N     
3386 C  CA    . LEU A 408 ? 0.4982 0.6169 0.7529 -0.0123 -0.0226 0.0719  408 LEU A CA    
3387 C  C     . LEU A 408 ? 0.5195 0.6338 0.7712 -0.0069 -0.0124 0.0655  408 LEU A C     
3388 O  O     . LEU A 408 ? 0.4588 0.5806 0.7235 -0.0047 -0.0097 0.0710  408 LEU A O     
3389 C  CB    . LEU A 408 ? 0.5250 0.6401 0.7843 -0.0070 -0.0181 0.0757  408 LEU A CB    
3390 C  CG    . LEU A 408 ? 0.4681 0.5865 0.7468 0.0021  -0.0088 0.0838  408 LEU A CG    
3391 C  CD1   . LEU A 408 ? 0.4643 0.5979 0.7641 0.0013  -0.0127 0.0961  408 LEU A CD1   
3392 C  CD2   . LEU A 408 ? 0.4920 0.6062 0.7763 0.0063  -0.0062 0.0884  408 LEU A CD2   
3393 N  N     . TYR A 409 ? 0.5143 0.6173 0.7492 -0.0049 -0.0070 0.0545  409 TYR A N     
3394 C  CA    . TYR A 409 ? 0.5132 0.6121 0.7441 0.0007  0.0029  0.0489  409 TYR A CA    
3395 C  C     . TYR A 409 ? 0.5140 0.6167 0.7420 -0.0028 0.0005  0.0467  409 TYR A C     
3396 O  O     . TYR A 409 ? 0.4486 0.5557 0.6845 0.0017  0.0070  0.0498  409 TYR A O     
3397 C  CB    . TYR A 409 ? 0.5240 0.6100 0.7381 0.0029  0.0079  0.0381  409 TYR A CB    
3398 C  CG    . TYR A 409 ? 0.6294 0.7097 0.8487 0.0088  0.0138  0.0400  409 TYR A CG    
3399 C  CD1   . TYR A 409 ? 0.4965 0.5835 0.7342 0.0113  0.0132  0.0515  409 TYR A CD1   
3400 C  CD2   . TYR A 409 ? 0.5118 0.5798 0.7186 0.0114  0.0193  0.0306  409 TYR A CD2   
3401 C  CE1   . TYR A 409 ? 0.5007 0.5815 0.7445 0.0170  0.0189  0.0535  409 TYR A CE1   
3402 C  CE2   . TYR A 409 ? 0.4460 0.5070 0.6580 0.0165  0.0246  0.0318  409 TYR A CE2   
3403 C  CZ    . TYR A 409 ? 0.5259 0.5929 0.7565 0.0196  0.0247  0.0433  409 TYR A CZ    
3404 O  OH    . TYR A 409 ? 0.5075 0.5665 0.7445 0.0251  0.0304  0.0448  409 TYR A OH    
3405 N  N     . PRO A 410 ? 0.5482 0.6493 0.7657 -0.0102 -0.0077 0.0417  410 PRO A N     
3406 C  CA    . PRO A 410 ? 0.4680 0.5725 0.6859 -0.0134 -0.0099 0.0408  410 PRO A CA    
3407 C  C     . PRO A 410 ? 0.4362 0.5521 0.6742 -0.0148 -0.0133 0.0521  410 PRO A C     
3408 O  O     . PRO A 410 ? 0.4382 0.5584 0.6830 -0.0136 -0.0101 0.0546  410 PRO A O     
3409 C  CB    . PRO A 410 ? 0.4161 0.5154 0.6195 -0.0207 -0.0183 0.0334  410 PRO A CB    
3410 C  CG    . PRO A 410 ? 0.4659 0.5577 0.6571 -0.0197 -0.0168 0.0278  410 PRO A CG    
3411 C  CD    . PRO A 410 ? 0.5158 0.6107 0.7191 -0.0153 -0.0138 0.0356  410 PRO A CD    
3412 N  N     . SER A 411 ? 0.4020 0.5238 0.6505 -0.0177 -0.0201 0.0597  411 SER A N     
3413 C  CA    . SER A 411 ? 0.4902 0.6242 0.7600 -0.0195 -0.0242 0.0715  411 SER A CA    
3414 C  C     . SER A 411 ? 0.4234 0.5637 0.7091 -0.0108 -0.0131 0.0791  411 SER A C     
3415 O  O     . SER A 411 ? 0.4311 0.5804 0.7321 -0.0109 -0.0124 0.0867  411 SER A O     
3416 C  CB    . SER A 411 ? 0.5341 0.6738 0.8113 -0.0242 -0.0340 0.0786  411 SER A CB    
3417 O  OG    . SER A 411 ? 0.4702 0.6048 0.7316 -0.0324 -0.0441 0.0715  411 SER A OG    
3418 N  N     . ILE A 412 ? 0.3789 0.5140 0.6612 -0.0030 -0.0039 0.0772  412 ILE A N     
3419 C  CA    . ILE A 412 ? 0.4089 0.5480 0.7030 0.0064  0.0083  0.0826  412 ILE A CA    
3420 C  C     . ILE A 412 ? 0.4500 0.5875 0.7365 0.0086  0.0151  0.0776  412 ILE A C     
3421 O  O     . ILE A 412 ? 0.5016 0.6484 0.8025 0.0120  0.0204  0.0856  412 ILE A O     
3422 C  CB    . ILE A 412 ? 0.4703 0.6011 0.7594 0.0139  0.0165  0.0792  412 ILE A CB    
3423 C  CG1   . ILE A 412 ? 0.4449 0.5806 0.7483 0.0134  0.0114  0.0886  412 ILE A CG1   
3424 C  CG2   . ILE A 412 ? 0.4254 0.5560 0.7186 0.0242  0.0309  0.0799  412 ILE A CG2   
3425 C  CD1   . ILE A 412 ? 0.4273 0.5533 0.7266 0.0198  0.0182  0.0854  412 ILE A CD1   
3426 N  N     . ILE A 413 ? 0.4137 0.5404 0.6784 0.0068  0.0151  0.0653  413 ILE A N     
3427 C  CA    . ILE A 413 ? 0.4241 0.5492 0.6800 0.0086  0.0207  0.0607  413 ILE A CA    
3428 C  C     . ILE A 413 ? 0.4076 0.5421 0.6761 0.0037  0.0158  0.0678  413 ILE A C     
3429 O  O     . ILE A 413 ? 0.3645 0.5047 0.6392 0.0075  0.0227  0.0723  413 ILE A O     
3430 C  CB    . ILE A 413 ? 0.4150 0.5283 0.6474 0.0059  0.0189  0.0474  413 ILE A CB    
3431 C  CG1   . ILE A 413 ? 0.4468 0.5507 0.6675 0.0118  0.0261  0.0403  413 ILE A CG1   
3432 C  CG2   . ILE A 413 ? 0.3880 0.5015 0.6132 0.0054  0.0210  0.0443  413 ILE A CG2   
3433 C  CD1   . ILE A 413 ? 0.4738 0.5675 0.6771 0.0073  0.0209  0.0300  413 ILE A CD1   
3434 N  N     . ILE A 414 ? 0.3604 0.4964 0.6325 -0.0050 0.0037  0.0691  414 ILE A N     
3435 C  CA    . ILE A 414 ? 0.3955 0.5385 0.6795 -0.0109 -0.0025 0.0750  414 ILE A CA    
3436 C  C     . ILE A 414 ? 0.4648 0.6217 0.7747 -0.0086 -0.0003 0.0895  414 ILE A C     
3437 O  O     . ILE A 414 ? 0.3696 0.5336 0.6911 -0.0081 0.0029  0.0961  414 ILE A O     
3438 C  CB    . ILE A 414 ? 0.3971 0.5363 0.6759 -0.0209 -0.0162 0.0710  414 ILE A CB    
3439 C  CG1   . ILE A 414 ? 0.4174 0.5441 0.6725 -0.0227 -0.0171 0.0575  414 ILE A CG1   
3440 C  CG2   . ILE A 414 ? 0.4177 0.5637 0.7118 -0.0277 -0.0237 0.0778  414 ILE A CG2   
3441 C  CD1   . ILE A 414 ? 0.4162 0.5377 0.6619 -0.0303 -0.0281 0.0521  414 ILE A CD1   
3442 N  N     . THR A 415 ? 0.4078 0.5695 0.7284 -0.0070 -0.0016 0.0957  415 THR A N     
3443 C  CA    . THR A 415 ? 0.4204 0.5968 0.7682 -0.0056 -0.0011 0.1108  415 THR A CA    
3444 C  C     . THR A 415 ? 0.4593 0.6413 0.8156 0.0047  0.0140  0.1163  415 THR A C     
3445 O  O     . THR A 415 ? 0.4903 0.6847 0.8672 0.0050  0.0159  0.1278  415 THR A O     
3446 C  CB    . THR A 415 ? 0.4439 0.6240 0.8006 -0.0054 -0.0056 0.1163  415 THR A CB    
3447 O  OG1   . THR A 415 ? 0.4257 0.6010 0.7721 -0.0150 -0.0195 0.1112  415 THR A OG1   
3448 C  CG2   . THR A 415 ? 0.4657 0.6626 0.8530 -0.0044 -0.0061 0.1332  415 THR A CG2   
3449 N  N     . HIS A 416 ? 0.4896 0.6629 0.8303 0.0129  0.0249  0.1083  416 HIS A N     
3450 C  CA    . HIS A 416 ? 0.4474 0.6248 0.7931 0.0235  0.0401  0.1123  416 HIS A CA    
3451 C  C     . HIS A 416 ? 0.5270 0.6984 0.8543 0.0256  0.0467  0.1042  416 HIS A C     
3452 O  O     . HIS A 416 ? 0.4401 0.6125 0.7646 0.0347  0.0599  0.1045  416 HIS A O     
3453 C  CB    . HIS A 416 ? 0.5045 0.6767 0.8478 0.0323  0.0486  0.1103  416 HIS A CB    
3454 C  CG    . HIS A 416 ? 0.5771 0.7566 0.9406 0.0314  0.0432  0.1203  416 HIS A CG    
3455 N  ND1   . HIS A 416 ? 0.6277 0.8235 1.0183 0.0289  0.0390  0.1354  416 HIS A ND1   
3456 C  CD2   . HIS A 416 ? 0.6005 0.7741 0.9620 0.0323  0.0405  0.1184  416 HIS A CD2   
3457 C  CE1   . HIS A 416 ? 0.5075 0.7075 0.9116 0.0285  0.0339  0.1423  416 HIS A CE1   
3458 N  NE2   . HIS A 416 ? 0.6207 0.8073 1.0074 0.0308  0.0350  0.1324  416 HIS A NE2   
3459 N  N     . ASN A 417 ? 0.5238 0.6895 0.8387 0.0176  0.0380  0.0971  417 ASN A N     
3460 C  CA    . ASN A 417 ? 0.4654 0.6269 0.7649 0.0187  0.0428  0.0910  417 ASN A CA    
3461 C  C     . ASN A 417 ? 0.4453 0.5970 0.7235 0.0265  0.0528  0.0808  417 ASN A C     
3462 O  O     . ASN A 417 ? 0.4044 0.5573 0.6754 0.0323  0.0624  0.0803  417 ASN A O     
3463 C  CB    . ASN A 417 ? 0.4700 0.6440 0.7857 0.0208  0.0485  0.1027  417 ASN A CB    
3464 C  CG    . ASN A 417 ? 0.4486 0.6204 0.7562 0.0160  0.0452  0.0999  417 ASN A CG    
3465 O  OD1   . ASN A 417 ? 0.4670 0.6314 0.7668 0.0081  0.0346  0.0931  417 ASN A OD1   
3466 N  ND2   . ASN A 417 ? 0.4845 0.6629 0.7941 0.0211  0.0548  0.1056  417 ASN A ND2   
3467 N  N     . VAL A 418 ? 0.4070 0.5490 0.6750 0.0264  0.0502  0.0727  418 VAL A N     
3468 C  CA    . VAL A 418 ? 0.4698 0.6011 0.7183 0.0328  0.0583  0.0623  418 VAL A CA    
3469 C  C     . VAL A 418 ? 0.5045 0.6284 0.7316 0.0294  0.0560  0.0520  418 VAL A C     
3470 O  O     . VAL A 418 ? 0.4629 0.5818 0.6831 0.0220  0.0461  0.0466  418 VAL A O     
3471 C  CB    . VAL A 418 ? 0.5337 0.6568 0.7799 0.0328  0.0556  0.0578  418 VAL A CB    
3472 C  CG1   . VAL A 418 ? 0.4543 0.5647 0.6804 0.0382  0.0629  0.0462  418 VAL A CG1   
3473 C  CG2   . VAL A 418 ? 0.4992 0.6307 0.7683 0.0368  0.0582  0.0694  418 VAL A CG2   
3474 N  N     . SER A 419 ? 0.4369 0.5606 0.6533 0.0352  0.0653  0.0495  419 SER A N     
3475 C  CA    . SER A 419 ? 0.4709 0.5894 0.6681 0.0328  0.0637  0.0413  419 SER A CA    
3476 C  C     . SER A 419 ? 0.5116 0.6290 0.6950 0.0409  0.0753  0.0380  419 SER A C     
3477 O  O     . SER A 419 ? 0.5115 0.6360 0.7039 0.0478  0.0850  0.0453  419 SER A O     
3478 C  CB    . SER A 419 ? 0.4828 0.6086 0.6881 0.0269  0.0576  0.0475  419 SER A CB    
3479 O  OG    . SER A 419 ? 0.6048 0.7249 0.7933 0.0236  0.0538  0.0397  419 SER A OG    
3480 N  N     . PRO A 420 ? 0.5742 0.6832 0.7357 0.0403  0.0748  0.0272  420 PRO A N     
3481 C  CA    . PRO A 420 ? 0.5354 0.6433 0.6811 0.0474  0.0851  0.0235  420 PRO A CA    
3482 C  C     . PRO A 420 ? 0.5252 0.6455 0.6765 0.0504  0.0910  0.0335  420 PRO A C     
3483 O  O     . PRO A 420 ? 0.5309 0.6536 0.6754 0.0583  0.1022  0.0345  420 PRO A O     
3484 C  CB    . PRO A 420 ? 0.5025 0.6010 0.6261 0.0435  0.0797  0.0115  420 PRO A CB    
3485 C  CG    . PRO A 420 ? 0.5746 0.6666 0.7023 0.0366  0.0696  0.0074  420 PRO A CG    
3486 C  CD    . PRO A 420 ? 0.4910 0.5914 0.6408 0.0333  0.0651  0.0180  420 PRO A CD    
3487 N  N     . ASP A 421 ? 0.5238 0.6514 0.6870 0.0446  0.0842  0.0411  421 ASP A N     
3488 C  CA    . ASP A 421 ? 0.5773 0.7169 0.7482 0.0466  0.0892  0.0520  421 ASP A CA    
3489 C  C     . ASP A 421 ? 0.5103 0.6609 0.7050 0.0503  0.0951  0.0651  421 ASP A C     
3490 O  O     . ASP A 421 ? 0.6538 0.8155 0.8569 0.0528  0.1008  0.0756  421 ASP A O     
3491 C  CB    . ASP A 421 ? 0.4559 0.5976 0.6311 0.0387  0.0794  0.0548  421 ASP A CB    
3492 C  CG    . ASP A 421 ? 0.5006 0.6380 0.6876 0.0309  0.0680  0.0535  421 ASP A CG    
3493 O  OD1   . ASP A 421 ? 0.4925 0.6200 0.6690 0.0287  0.0632  0.0432  421 ASP A OD1   
3494 O  OD2   . ASP A 421 ? 0.5661 0.7102 0.7725 0.0267  0.0636  0.0627  421 ASP A OD2   
3495 N  N     . THR A 422 ? 0.5075 0.6563 0.7144 0.0506  0.0939  0.0657  422 THR A N     
3496 C  CA    . THR A 422 ? 0.5479 0.7082 0.7794 0.0541  0.0991  0.0788  422 THR A CA    
3497 C  C     . THR A 422 ? 0.6049 0.7633 0.8350 0.0640  0.1109  0.0773  422 THR A C     
3498 O  O     . THR A 422 ? 0.5313 0.6999 0.7824 0.0684  0.1170  0.0886  422 THR A O     
3499 C  CB    . THR A 422 ? 0.4817 0.6441 0.7335 0.0461  0.0873  0.0838  422 THR A CB    
3500 O  OG1   . THR A 422 ? 0.5055 0.6574 0.7511 0.0452  0.0830  0.0750  422 THR A OG1   
3501 C  CG2   . THR A 422 ? 0.4740 0.6357 0.7259 0.0365  0.0758  0.0834  422 THR A CG2   
3502 N  N     . LEU A 423 ? 0.6134 0.7588 0.8205 0.0674  0.1141  0.0639  423 LEU A N     
3503 C  CA    . LEU A 423 ? 0.5813 0.7217 0.7862 0.0767  0.1249  0.0607  423 LEU A CA    
3504 C  C     . LEU A 423 ? 0.6293 0.7769 0.8299 0.0866  0.1403  0.0652  423 LEU A C     
3505 O  O     . LEU A 423 ? 0.6936 0.8397 0.8735 0.0877  0.1433  0.0600  423 LEU A O     
3506 C  CB    . LEU A 423 ? 0.5799 0.7027 0.7616 0.0761  0.1225  0.0443  423 LEU A CB    
3507 C  CG    . LEU A 423 ? 0.6719 0.7859 0.8453 0.0861  0.1347  0.0379  423 LEU A CG    
3508 C  CD1   . LEU A 423 ? 0.6559 0.7704 0.8517 0.0888  0.1357  0.0441  423 LEU A CD1   
3509 C  CD2   . LEU A 423 ? 0.6092 0.7061 0.7555 0.0845  0.1321  0.0210  423 LEU A CD2   
3510 N  N     . ASN A 424 ? 0.5779 0.7339 0.7980 0.0941  0.1500  0.0753  424 ASN A N     
3511 C  CA    . ASN A 424 ? 0.5977 0.7611 0.8151 0.1051  0.1667  0.0802  424 ASN A CA    
3512 C  C     . ASN A 424 ? 0.6660 0.8410 0.8802 0.1032  0.1679  0.0876  424 ASN A C     
3513 O  O     . ASN A 424 ? 0.7316 0.9074 0.9271 0.1098  0.1785  0.0849  424 ASN A O     
3514 C  CB    . ASN A 424 ? 0.6431 0.7914 0.8332 0.1130  0.1763  0.0651  424 ASN A CB    
3515 C  CG    . ASN A 424 ? 0.8317 0.9664 1.0245 0.1143  0.1745  0.0573  424 ASN A CG    
3516 O  OD1   . ASN A 424 ? 1.0724 1.1904 1.2426 0.1136  0.1724  0.0420  424 ASN A OD1   
3517 N  ND2   . ASN A 424 ? 0.7312 0.8734 0.9526 0.1159  0.1749  0.0684  424 ASN A ND2   
3518 N  N     . ARG A 425 ? 0.6536 0.8375 0.8859 0.0941  0.1569  0.0971  425 ARG A N     
3519 C  CA    . ARG A 425 ? 0.7474 0.9417 0.9797 0.0911  0.1563  0.1051  425 ARG A CA    
3520 C  C     . ARG A 425 ? 0.7651 0.9767 1.0168 0.0986  0.1694  0.1215  425 ARG A C     
3521 O  O     . ARG A 425 ? 0.8215 1.0438 1.1032 0.0970  0.1678  0.1342  425 ARG A O     
3522 C  CB    . ARG A 425 ? 0.7610 0.9565 1.0063 0.0787  0.1399  0.1084  425 ARG A CB    
3523 C  CG    . ARG A 425 ? 0.8862 1.0920 1.1364 0.0750  0.1385  0.1182  425 ARG A CG    
3524 C  CD    . ARG A 425 ? 0.8417 1.0471 1.1071 0.0631  0.1226  0.1211  425 ARG A CD    
3525 N  NE    . ARG A 425 ? 1.0674 1.2720 1.3228 0.0582  0.1176  0.1206  425 ARG A NE    
3526 C  CZ    . ARG A 425 ? 1.0534 1.2690 1.3248 0.0554  0.1174  0.1338  425 ARG A CZ    
3527 N  NH1   . ARG A 425 ? 0.9494 1.1784 1.2478 0.0566  0.1216  0.1488  425 ARG A NH1   
3528 N  NH2   . ARG A 425 ? 1.0443 1.2577 1.3057 0.0514  0.1128  0.1326  425 ARG A NH2   
3529 N  N     . GLU A 426 ? 0.8208 1.0360 1.0554 0.1065  0.1822  0.1216  426 GLU A N     
3530 C  CA    . GLU A 426 ? 0.8561 1.0882 1.1067 0.1149  0.1968  0.1372  426 GLU A CA    
3531 C  C     . GLU A 426 ? 0.8407 1.0887 1.1183 0.1077  0.1908  0.1546  426 GLU A C     
3532 O  O     . GLU A 426 ? 0.7748 1.0216 1.0465 0.0996  0.1809  0.1540  426 GLU A O     
3533 C  CB    . GLU A 426 ? 0.8727 1.1049 1.0950 0.1240  0.2109  0.1329  426 GLU A CB    
3534 C  CG    . GLU A 426 ? 0.9914 1.2107 1.1913 0.1340  0.2217  0.1186  426 GLU A CG    
3535 C  CD    . GLU A 426 ? 1.3039 1.5219 1.4713 0.1415  0.2334  0.1125  426 GLU A CD    
3536 O  OE1   . GLU A 426 ? 1.3566 1.5852 1.5201 0.1391  0.2331  0.1208  426 GLU A OE1   
3537 O  OE2   . GLU A 426 ? 1.2241 1.4302 1.3696 0.1496  0.2426  0.0996  426 GLU A OE2   
3538 N  N     . GLY A 427 ? 0.7918 1.0548 1.1007 0.1108  0.1967  0.1705  427 GLY A N     
3539 C  CA    . GLY A 427 ? 0.7435 1.0235 1.0792 0.1058  0.1944  0.1890  427 GLY A CA    
3540 C  C     . GLY A 427 ? 0.7212 1.0041 1.0862 0.0941  0.1783  0.1958  427 GLY A C     
3541 O  O     . GLY A 427 ? 0.6527 0.9490 1.0418 0.0890  0.1755  0.2112  427 GLY A O     
3542 N  N     . CYS A 428 ? 0.8976 1.1683 1.2610 0.0894  0.1674  0.1851  428 CYS A N     
3543 C  CA    . CYS A 428 ? 0.7473 1.0212 1.1371 0.0783  0.1520  0.1916  428 CYS A CA    
3544 C  C     . CYS A 428 ? 0.7371 1.0253 1.1592 0.0823  0.1571  0.2059  428 CYS A C     
3545 O  O     . CYS A 428 ? 0.6646 0.9569 1.0867 0.0940  0.1720  0.2080  428 CYS A O     
3546 C  CB    . CYS A 428 ? 0.8694 1.1258 1.2447 0.0711  0.1377  0.1756  428 CYS A CB    
3547 S  SG    . CYS A 428 ? 1.2394 1.4802 1.5853 0.0630  0.1267  0.1606  428 CYS A SG    
3548 N  N     . GLY A 429 ? 0.6727 0.9684 1.1227 0.0722  0.1441  0.2158  429 GLY A N     
3549 C  CA    . GLY A 429 ? 0.6514 0.9633 1.1362 0.0741  0.1466  0.2318  429 GLY A CA    
3550 C  C     . GLY A 429 ? 0.5725 0.8793 1.0658 0.0705  0.1361  0.2277  429 GLY A C     
3551 O  O     . GLY A 429 ? 0.5626 0.8816 1.0815 0.0748  0.1403  0.2394  429 GLY A O     
3552 N  N     . GLU A 430 ? 0.5294 0.8191 1.0023 0.0629  0.1228  0.2123  430 GLU A N     
3553 C  CA    . GLU A 430 ? 0.4632 0.7473 0.9412 0.0588  0.1120  0.2079  430 GLU A CA    
3554 C  C     . GLU A 430 ? 0.6281 0.8927 1.0734 0.0627  0.1135  0.1888  430 GLU A C     
3555 O  O     . GLU A 430 ? 0.6828 0.9343 1.1034 0.0576  0.1073  0.1759  430 GLU A O     
3556 C  CB    . GLU A 430 ? 0.4788 0.7625 0.9679 0.0436  0.0917  0.2093  430 GLU A CB    
3557 C  CG    . GLU A 430 ? 0.5932 0.8737 1.0890 0.0389  0.0800  0.2071  430 GLU A CG    
3558 C  CD    . GLU A 430 ? 0.6731 0.9568 1.1845 0.0243  0.0609  0.2117  430 GLU A CD    
3559 O  OE1   . GLU A 430 ? 0.8944 1.1819 1.4129 0.0178  0.0569  0.2163  430 GLU A OE1   
3560 O  OE2   . GLU A 430 ? 0.7852 1.0675 1.3016 0.0193  0.0498  0.2106  430 GLU A OE2   
3561 N  N     . TYR A 431 ? 0.5598 0.8227 1.0064 0.0716  0.1216  0.1876  431 TYR A N     
3562 C  CA    . TYR A 431 ? 0.5795 0.8241 0.9981 0.0760  0.1242  0.1706  431 TYR A CA    
3563 C  C     . TYR A 431 ? 0.5761 0.8163 1.0031 0.0726  0.1143  0.1692  431 TYR A C     
3564 O  O     . TYR A 431 ? 0.5748 0.8282 1.0307 0.0714  0.1108  0.1830  431 TYR A O     
3565 C  CB    . TYR A 431 ? 0.7053 0.9483 1.1142 0.0909  0.1442  0.1682  431 TYR A CB    
3566 C  CG    . TYR A 431 ? 0.9196 1.1617 1.3083 0.0950  0.1541  0.1644  431 TYR A CG    
3567 C  CD1   . TYR A 431 ? 0.8526 1.0977 1.2379 0.0863  0.1461  0.1660  431 TYR A CD1   
3568 C  CD2   . TYR A 431 ? 1.0893 1.3276 1.4624 0.1078  0.1717  0.1594  431 TYR A CD2   
3569 C  CE1   . TYR A 431 ? 0.7918 1.0372 1.1594 0.0901  0.1548  0.1638  431 TYR A CE1   
3570 C  CE2   . TYR A 431 ? 1.1090 1.3475 1.4621 0.1114  0.1803  0.1563  431 TYR A CE2   
3571 C  CZ    . TYR A 431 ? 0.8764 1.1192 1.2274 0.1024  0.1716  0.1592  431 TYR A CZ    
3572 O  OH    . TYR A 431 ? 0.6606 0.9046 0.9925 0.1057  0.1795  0.1576  431 TYR A OH    
3573 N  N     . ASP A 432 ? 0.6212 0.8438 1.0233 0.0710  0.1097  0.1534  432 ASP A N     
3574 C  CA    . ASP A 432 ? 0.5683 0.7847 0.9739 0.0699  0.1033  0.1509  432 ASP A CA    
3575 C  C     . ASP A 432 ? 0.5606 0.7622 0.9462 0.0798  0.1147  0.1389  432 ASP A C     
3576 O  O     . ASP A 432 ? 0.6398 0.8288 0.9978 0.0805  0.1176  0.1252  432 ASP A O     
3577 C  CB    . ASP A 432 ? 0.6015 0.8102 0.9975 0.0569  0.0850  0.1437  432 ASP A CB    
3578 C  CG    . ASP A 432 ? 0.5969 0.8192 1.0187 0.0476  0.0718  0.1566  432 ASP A CG    
3579 O  OD1   . ASP A 432 ? 0.6246 0.8632 1.0722 0.0500  0.0760  0.1716  432 ASP A OD1   
3580 O  OD2   . ASP A 432 ? 0.5586 0.7755 0.9748 0.0378  0.0571  0.1519  432 ASP A OD2   
3581 N  N     . VAL A 433 ? 0.5763 0.7794 0.9767 0.0874  0.1209  0.1443  433 VAL A N     
3582 C  CA    . VAL A 433 ? 0.5840 0.7730 0.9695 0.0980  0.1333  0.1342  433 VAL A CA    
3583 C  C     . VAL A 433 ? 0.6139 0.7908 0.9952 0.0942  0.1240  0.1279  433 VAL A C     
3584 O  O     . VAL A 433 ? 0.5580 0.7432 0.9614 0.0909  0.1160  0.1384  433 VAL A O     
3585 C  CB    . VAL A 433 ? 0.5794 0.7778 0.9852 0.1114  0.1500  0.1450  433 VAL A CB    
3586 C  CG1   . VAL A 433 ? 0.6363 0.8182 1.0206 0.1229  0.1651  0.1319  433 VAL A CG1   
3587 C  CG2   . VAL A 433 ? 0.5898 0.8062 1.0095 0.1130  0.1562  0.1573  433 VAL A CG2   
3588 N  N     . ALA A 434 ? 0.5884 0.7464 0.9419 0.0946  0.1250  0.1113  434 ALA A N     
3589 C  CA    . ALA A 434 ? 0.5183 0.6638 0.8656 0.0908  0.1168  0.1046  434 ALA A CA    
3590 C  C     . ALA A 434 ? 0.5542 0.6961 0.9156 0.1011  0.1264  0.1087  434 ALA A C     
3591 O  O     . ALA A 434 ? 0.5732 0.7125 0.9341 0.1125  0.1420  0.1075  434 ALA A O     
3592 C  CB    . ALA A 434 ? 0.5128 0.6400 0.8276 0.0877  0.1151  0.0863  434 ALA A CB    
3593 N  N     . PRO A 435 ? 0.5616 0.7030 0.9353 0.0976  0.1176  0.1137  435 PRO A N     
3594 C  CA    . PRO A 435 ? 0.5421 0.6788 0.9302 0.1075  0.1263  0.1180  435 PRO A CA    
3595 C  C     . PRO A 435 ? 0.7069 0.8213 1.0719 0.1141  0.1361  0.1016  435 PRO A C     
3596 O  O     . PRO A 435 ? 0.6055 0.7070 0.9441 0.1080  0.1312  0.0873  435 PRO A O     
3597 C  CB    . PRO A 435 ? 0.5396 0.6796 0.9405 0.0997  0.1117  0.1255  435 PRO A CB    
3598 C  CG    . PRO A 435 ? 0.5338 0.6733 0.9175 0.0860  0.0966  0.1190  435 PRO A CG    
3599 C  CD    . PRO A 435 ? 0.5185 0.6651 0.8954 0.0848  0.0995  0.1173  435 PRO A CD    
3600 N  N     . GLN A 436 ? 0.5618 0.6715 0.9376 0.1266  0.1502  0.1039  436 GLN A N     
3601 C  CA    . GLN A 436 ? 0.6195 0.7066 0.9765 0.1340  0.1606  0.0888  436 GLN A CA    
3602 C  C     . GLN A 436 ? 0.7016 0.7801 1.0293 0.1355  0.1678  0.0740  436 GLN A C     
3603 O  O     . GLN A 436 ? 0.6762 0.7500 0.9996 0.1469  0.1836  0.0702  436 GLN A O     
3604 C  CB    . GLN A 436 ? 0.6600 0.7319 1.0077 0.1269  0.1498  0.0813  436 GLN A CB    
3605 C  CG    . GLN A 436 ? 0.7770 0.8585 1.1497 0.1227  0.1394  0.0960  436 GLN A CG    
3606 C  CD    . GLN A 436 ? 1.0085 1.0753 1.3708 0.1159  0.1298  0.0890  436 GLN A CD    
3607 O  OE1   . GLN A 436 ? 0.8776 0.9522 1.2454 0.1063  0.1156  0.0956  436 GLN A OE1   
3608 N  NE2   . GLN A 436 ? 0.9520 0.9972 1.2991 0.1209  0.1375  0.0755  436 GLN A NE2   
3609 N  N     . VAL A 437 ? 0.6234 0.7000 0.9306 0.1244  0.1564  0.0657  437 VAL A N     
3610 C  CA    . VAL A 437 ? 0.6286 0.6960 0.9064 0.1250  0.1614  0.0511  437 VAL A CA    
3611 C  C     . VAL A 437 ? 0.6810 0.7638 0.9618 0.1297  0.1702  0.0579  437 VAL A C     
3612 O  O     . VAL A 437 ? 0.7358 0.8122 0.9958 0.1350  0.1801  0.0483  437 VAL A O     
3613 C  CB    . VAL A 437 ? 0.6573 0.7191 0.9148 0.1119  0.1466  0.0416  437 VAL A CB    
3614 C  CG1   . VAL A 437 ? 0.6221 0.6649 0.8702 0.1093  0.1421  0.0313  437 VAL A CG1   
3615 C  CG2   . VAL A 437 ? 0.5992 0.6777 0.8715 0.1019  0.1329  0.0533  437 VAL A CG2   
3616 N  N     . GLY A 438 ? 0.6194 0.7225 0.9253 0.1276  0.1664  0.0746  438 GLY A N     
3617 C  CA    . GLY A 438 ? 0.5320 0.6513 0.8468 0.1330  0.1759  0.0840  438 GLY A CA    
3618 C  C     . GLY A 438 ? 0.6673 0.7916 0.9643 0.1266  0.1719  0.0802  438 GLY A C     
3619 O  O     . GLY A 438 ? 0.6601 0.7960 0.9607 0.1319  0.1816  0.0868  438 GLY A O     
3620 N  N     . HIS A 439 ? 0.5724 0.6888 0.8513 0.1157  0.1586  0.0706  439 HIS A N     
3621 C  CA    . HIS A 439 ? 0.6342 0.7553 0.8977 0.1096  0.1544  0.0678  439 HIS A CA    
3622 C  C     . HIS A 439 ? 0.6007 0.7418 0.8874 0.1038  0.1477  0.0836  439 HIS A C     
3623 O  O     . HIS A 439 ? 0.5659 0.7132 0.8727 0.0981  0.1377  0.0921  439 HIS A O     
3624 C  CB    . HIS A 439 ? 0.6396 0.7475 0.8804 0.0997  0.1420  0.0542  439 HIS A CB    
3625 C  CG    . HIS A 439 ? 0.6158 0.7037 0.8354 0.1035  0.1463  0.0387  439 HIS A CG    
3626 N  ND1   . HIS A 439 ? 0.6210 0.7007 0.8203 0.1113  0.1584  0.0293  439 HIS A ND1   
3627 C  CD2   . HIS A 439 ? 0.5443 0.6185 0.7599 0.1001  0.1399  0.0312  439 HIS A CD2   
3628 C  CE1   . HIS A 439 ? 0.6449 0.7059 0.8289 0.1122  0.1588  0.0159  439 HIS A CE1   
3629 N  NE2   . HIS A 439 ? 0.6285 0.6860 0.8230 0.1055  0.1478  0.0173  439 HIS A NE2   
3630 N  N     . ARG A 440 ? 0.5555 0.7063 0.8391 0.1051  0.1530  0.0877  440 ARG A N     
3631 C  CA    . ARG A 440 ? 0.6312 0.8005 0.9369 0.0998  0.1476  0.1028  440 ARG A CA    
3632 C  C     . ARG A 440 ? 0.5368 0.7051 0.8285 0.0892  0.1362  0.0981  440 ARG A C     
3633 O  O     . ARG A 440 ? 0.6736 0.8325 0.9391 0.0895  0.1382  0.0865  440 ARG A O     
3634 C  CB    . ARG A 440 ? 0.5859 0.7696 0.9039 0.1093  0.1628  0.1143  440 ARG A CB    
3635 C  CG    . ARG A 440 ? 0.7102 0.8876 1.0224 0.1233  0.1803  0.1104  440 ARG A CG    
3636 C  CD    . ARG A 440 ? 0.8966 1.0903 1.2226 0.1328  0.1957  0.1233  440 ARG A CD    
3637 N  NE    . ARG A 440 ? 0.9498 1.1576 1.3114 0.1368  0.1987  0.1397  440 ARG A NE    
3638 C  CZ    . ARG A 440 ? 1.0306 1.2516 1.4090 0.1477  0.2146  0.1515  440 ARG A CZ    
3639 N  NH1   . ARG A 440 ? 1.1584 1.3801 1.5198 0.1562  0.2296  0.1487  440 ARG A NH1   
3640 N  NH2   . ARG A 440 ? 1.0874 1.3219 1.5004 0.1503  0.2156  0.1670  440 ARG A NH2   
3641 N  N     . PHE A 441 ? 0.5747 0.7526 0.8846 0.0798  0.1240  0.1073  441 PHE A N     
3642 C  CA    . PHE A 441 ? 0.5769 0.7536 0.8773 0.0696  0.1125  0.1038  441 PHE A CA    
3643 C  C     . PHE A 441 ? 0.5678 0.7612 0.8914 0.0656  0.1100  0.1190  441 PHE A C     
3644 O  O     . PHE A 441 ? 0.5870 0.7910 0.9369 0.0639  0.1065  0.1309  441 PHE A O     
3645 C  CB    . PHE A 441 ? 0.4562 0.6233 0.7517 0.0601  0.0975  0.0963  441 PHE A CB    
3646 C  CG    . PHE A 441 ? 0.5785 0.7295 0.8542 0.0630  0.0991  0.0826  441 PHE A CG    
3647 C  CD1   . PHE A 441 ? 0.5644 0.7128 0.8500 0.0676  0.1019  0.0843  441 PHE A CD1   
3648 C  CD2   . PHE A 441 ? 0.6213 0.7603 0.8702 0.0611  0.0977  0.0689  441 PHE A CD2   
3649 C  CE1   . PHE A 441 ? 0.5791 0.7120 0.8481 0.0700  0.1033  0.0722  441 PHE A CE1   
3650 C  CE2   . PHE A 441 ? 0.6149 0.7392 0.8472 0.0630  0.0986  0.0568  441 PHE A CE2   
3651 C  CZ    . PHE A 441 ? 0.6430 0.7636 0.8853 0.0674  0.1015  0.0583  441 PHE A CZ    
3652 N  N     . CYS A 442 ? 0.5412 0.7372 0.8559 0.0641  0.1115  0.1193  442 CYS A N     
3653 C  CA    . CYS A 442 ? 0.5557 0.7664 0.8918 0.0597  0.1089  0.1335  442 CYS A CA    
3654 C  C     . CYS A 442 ? 0.5875 0.7967 0.9331 0.0469  0.0913  0.1339  442 CYS A C     
3655 O  O     . CYS A 442 ? 0.5379 0.7343 0.8654 0.0411  0.0822  0.1216  442 CYS A O     
3656 C  CB    . CYS A 442 ? 0.6632 0.8762 0.9859 0.0618  0.1155  0.1336  442 CYS A CB    
3657 S  SG    . CYS A 442 ? 1.0205 1.2452 1.3633 0.0526  0.1075  0.1469  442 CYS A SG    
3658 N  N     . LYS A 443 ? 0.5363 0.7587 0.9104 0.0425  0.0866  0.1482  443 LYS A N     
3659 C  CA    . LYS A 443 ? 0.5279 0.7494 0.9122 0.0301  0.0698  0.1491  443 LYS A CA    
3660 C  C     . LYS A 443 ? 0.5197 0.7483 0.9162 0.0237  0.0656  0.1575  443 LYS A C     
3661 O  O     . LYS A 443 ? 0.5925 0.8206 0.9997 0.0132  0.0518  0.1591  443 LYS A O     
3662 C  CB    . LYS A 443 ? 0.5952 0.8248 1.0034 0.0280  0.0640  0.1580  443 LYS A CB    
3663 C  CG    . LYS A 443 ? 0.5541 0.7796 0.9568 0.0363  0.0708  0.1538  443 LYS A CG    
3664 C  CD    . LYS A 443 ? 0.5981 0.8257 1.0152 0.0305  0.0591  0.1574  443 LYS A CD    
3665 C  CE    . LYS A 443 ? 0.4768 0.6921 0.8778 0.0198  0.0438  0.1460  443 LYS A CE    
3666 N  NZ    . LYS A 443 ? 0.6277 0.8501 1.0478 0.0106  0.0294  0.1536  443 LYS A NZ    
3667 N  N     . ASP A 444 ? 0.5486 0.7832 0.9435 0.0295  0.0769  0.1628  444 ASP A N     
3668 C  CA    . ASP A 444 ? 0.6239 0.8652 1.0318 0.0236  0.0735  0.1720  444 ASP A CA    
3669 C  C     . ASP A 444 ? 0.6435 0.8711 1.0344 0.0152  0.0624  0.1606  444 ASP A C     
3670 O  O     . ASP A 444 ? 0.7242 0.9515 1.1285 0.0053  0.0507  0.1639  444 ASP A O     
3671 C  CB    . ASP A 444 ? 0.7066 0.9577 1.1142 0.0325  0.0892  0.1805  444 ASP A CB    
3672 C  CG    . ASP A 444 ? 0.6929 0.9591 1.1203 0.0412  0.1013  0.1934  444 ASP A CG    
3673 O  OD1   . ASP A 444 ? 0.6215 0.8901 1.0625 0.0407  0.0976  0.1954  444 ASP A OD1   
3674 O  OD2   . ASP A 444 ? 0.7467 1.0230 1.1764 0.0487  0.1148  0.2022  444 ASP A OD2   
3675 N  N     . LEU A 445 ? 0.6913 0.9072 1.0533 0.0190  0.0657  0.1472  445 LEU A N     
3676 C  CA    . LEU A 445 ? 0.6889 0.8920 1.0343 0.0123  0.0564  0.1361  445 LEU A CA    
3677 C  C     . LEU A 445 ? 0.5710 0.7612 0.8991 0.0105  0.0498  0.1216  445 LEU A C     
3678 O  O     . LEU A 445 ? 0.5553 0.7428 0.8711 0.0175  0.0569  0.1160  445 LEU A O     
3679 C  CB    . LEU A 445 ? 0.7645 0.9656 1.0914 0.0173  0.0644  0.1333  445 LEU A CB    
3680 C  CG    . LEU A 445 ? 0.9340 1.1458 1.2756 0.0170  0.0685  0.1470  445 LEU A CG    
3681 C  CD1   . LEU A 445 ? 0.7747 0.9878 1.1400 0.0065  0.0566  0.1542  445 LEU A CD1   
3682 C  CD2   . LEU A 445 ? 0.8659 1.0925 1.2182 0.0260  0.0827  0.1595  445 LEU A CD2   
3683 N  N     . PRO A 446 ? 0.6145 0.7961 0.9409 0.0014  0.0367  0.1152  446 PRO A N     
3684 C  CA    . PRO A 446 ? 0.5978 0.7679 0.9075 -0.0004 0.0308  0.1022  446 PRO A CA    
3685 C  C     . PRO A 446 ? 0.4903 0.6510 0.7733 0.0044  0.0362  0.0904  446 PRO A C     
3686 O  O     . PRO A 446 ? 0.5733 0.7325 0.8481 0.0048  0.0383  0.0892  446 PRO A O     
3687 C  CB    . PRO A 446 ? 0.5153 0.6792 0.8289 -0.0111 0.0167  0.0989  446 PRO A CB    
3688 C  CG    . PRO A 446 ? 0.5265 0.6940 0.8508 -0.0140 0.0164  0.1061  446 PRO A CG    
3689 C  CD    . PRO A 446 ? 0.5912 0.7729 0.9311 -0.0076 0.0271  0.1197  446 PRO A CD    
3690 N  N     . GLY A 447 ? 0.4659 0.6206 0.7363 0.0077  0.0380  0.0822  447 GLY A N     
3691 C  CA    . GLY A 447 ? 0.5906 0.7366 0.8367 0.0119  0.0426  0.0711  447 GLY A CA    
3692 C  C     . GLY A 447 ? 0.3988 0.5342 0.6306 0.0057  0.0337  0.0605  447 GLY A C     
3693 O  O     . GLY A 447 ? 0.4075 0.5400 0.6453 -0.0014 0.0239  0.0595  447 GLY A O     
3694 N  N     . PHE A 448 ? 0.4778 0.6077 0.6902 0.0087  0.0375  0.0525  448 PHE A N     
3695 C  CA    . PHE A 448 ? 0.4608 0.5815 0.6594 0.0041  0.0306  0.0427  448 PHE A CA    
3696 C  C     . PHE A 448 ? 0.4996 0.6131 0.6948 0.0002  0.0238  0.0358  448 PHE A C     
3697 O  O     . PHE A 448 ? 0.4521 0.5625 0.6510 -0.0063 0.0151  0.0342  448 PHE A O     
3698 C  CB    . PHE A 448 ? 0.5169 0.6345 0.6960 0.0086  0.0363  0.0361  448 PHE A CB    
3699 C  CG    . PHE A 448 ? 0.6269 0.7370 0.7930 0.0047  0.0303  0.0274  448 PHE A CG    
3700 C  CD1   . PHE A 448 ? 0.6785 0.7878 0.8506 -0.0004 0.0241  0.0290  448 PHE A CD1   
3701 C  CD2   . PHE A 448 ? 0.5238 0.6274 0.6726 0.0062  0.0313  0.0177  448 PHE A CD2   
3702 C  CE1   . PHE A 448 ? 0.6541 0.7571 0.8155 -0.0031 0.0196  0.0214  448 PHE A CE1   
3703 C  CE2   . PHE A 448 ? 0.5602 0.6583 0.6989 0.0028  0.0262  0.0107  448 PHE A CE2   
3704 C  CZ    . PHE A 448 ? 0.5416 0.6399 0.6868 -0.0014 0.0207  0.0127  448 PHE A CZ    
3705 N  N     . ILE A 449 ? 0.4496 0.5602 0.6379 0.0043  0.0280  0.0318  449 ILE A N     
3706 C  CA    . ILE A 449 ? 0.4683 0.5726 0.6534 0.0011  0.0222  0.0263  449 ILE A CA    
3707 C  C     . ILE A 449 ? 0.5135 0.6222 0.7151 -0.0036 0.0155  0.0330  449 ILE A C     
3708 O  O     . ILE A 449 ? 0.4733 0.5773 0.6716 -0.0094 0.0072  0.0288  449 ILE A O     
3709 C  CB    . ILE A 449 ? 0.4756 0.5760 0.6529 0.0068  0.0287  0.0222  449 ILE A CB    
3710 C  CG1   . ILE A 449 ? 0.5117 0.6075 0.6713 0.0104  0.0342  0.0149  449 ILE A CG1   
3711 C  CG2   . ILE A 449 ? 0.3678 0.4618 0.5422 0.0034  0.0230  0.0176  449 ILE A CG2   
3712 C  CD1   . ILE A 449 ? 0.5173 0.6066 0.6637 0.0056  0.0281  0.0064  449 ILE A CD1   
3713 N  N     . PRO A 450 ? 0.4731 0.5909 0.6924 -0.0015 0.0182  0.0435  450 PRO A N     
3714 C  CA    . PRO A 450 ? 0.4444 0.5669 0.6797 -0.0073 0.0098  0.0501  450 PRO A CA    
3715 C  C     . PRO A 450 ? 0.3734 0.4937 0.6098 -0.0152 0.0007  0.0486  450 PRO A C     
3716 O  O     . PRO A 450 ? 0.4162 0.5343 0.6542 -0.0214 -0.0085 0.0472  450 PRO A O     
3717 C  CB    . PRO A 450 ? 0.3914 0.5257 0.6468 -0.0032 0.0156  0.0627  450 PRO A CB    
3718 C  CG    . PRO A 450 ? 0.4142 0.5488 0.6622 0.0058  0.0280  0.0616  450 PRO A CG    
3719 C  CD    . PRO A 450 ? 0.4815 0.6057 0.7062 0.0065  0.0292  0.0495  450 PRO A CD    
3720 N  N     . SER A 451 ? 0.3559 0.4762 0.5908 -0.0149 0.0030  0.0489  451 SER A N     
3721 C  CA    . SER A 451 ? 0.4150 0.5316 0.6519 -0.0220 -0.0051 0.0472  451 SER A CA    
3722 C  C     . SER A 451 ? 0.5113 0.6172 0.7310 -0.0255 -0.0106 0.0355  451 SER A C     
3723 O  O     . SER A 451 ? 0.5175 0.6196 0.7383 -0.0320 -0.0195 0.0330  451 SER A O     
3724 C  CB    . SER A 451 ? 0.4709 0.5895 0.7100 -0.0201 -0.0004 0.0506  451 SER A CB    
3725 O  OG    . SER A 451 ? 0.6578 0.7864 0.9069 -0.0143 0.0083  0.0601  451 SER A OG    
3726 N  N     . LEU A 452 ? 0.4949 0.5960 0.6984 -0.0213 -0.0055 0.0282  452 LEU A N     
3727 C  CA    . LEU A 452 ? 0.4853 0.5775 0.6736 -0.0241 -0.0098 0.0180  452 LEU A CA    
3728 C  C     . LEU A 452 ? 0.4935 0.5842 0.6808 -0.0272 -0.0153 0.0164  452 LEU A C     
3729 O  O     . LEU A 452 ? 0.5253 0.6108 0.7071 -0.0324 -0.0222 0.0114  452 LEU A O     
3730 C  CB    . LEU A 452 ? 0.4465 0.5354 0.6198 -0.0194 -0.0037 0.0116  452 LEU A CB    
3731 C  CG    . LEU A 452 ? 0.5280 0.6210 0.7012 -0.0144 0.0036  0.0150  452 LEU A CG    
3732 C  CD1   . LEU A 452 ? 0.5199 0.6103 0.6782 -0.0098 0.0091  0.0090  452 LEU A CD1   
3733 C  CD2   . LEU A 452 ? 0.6333 0.7254 0.8085 -0.0168 0.0013  0.0156  452 LEU A CD2   
3734 N  N     . LEU A 453 ? 0.4344 0.5297 0.6272 -0.0239 -0.0120 0.0210  453 LEU A N     
3735 C  CA    . LEU A 453 ? 0.4386 0.5333 0.6312 -0.0263 -0.0170 0.0210  453 LEU A CA    
3736 C  C     . LEU A 453 ? 0.4797 0.5779 0.6832 -0.0330 -0.0263 0.0257  453 LEU A C     
3737 O  O     . LEU A 453 ? 0.4691 0.5644 0.6668 -0.0376 -0.0334 0.0226  453 LEU A O     
3738 C  CB    . LEU A 453 ? 0.4203 0.5191 0.6187 -0.0205 -0.0108 0.0259  453 LEU A CB    
3739 C  CG    . LEU A 453 ? 0.4936 0.5863 0.6784 -0.0154 -0.0039 0.0191  453 LEU A CG    
3740 C  CD1   . LEU A 453 ? 0.4368 0.5311 0.6279 -0.0112 -0.0002 0.0233  453 LEU A CD1   
3741 C  CD2   . LEU A 453 ? 0.5008 0.5856 0.6700 -0.0192 -0.0081 0.0099  453 LEU A CD2   
3742 N  N     . GLY A 454 ? 0.4625 0.5672 0.6818 -0.0338 -0.0267 0.0336  454 GLY A N     
3743 C  CA    . GLY A 454 ? 0.3801 0.4877 0.6105 -0.0412 -0.0365 0.0379  454 GLY A CA    
3744 C  C     . GLY A 454 ? 0.4883 0.5867 0.7077 -0.0474 -0.0437 0.0291  454 GLY A C     
3745 O  O     . GLY A 454 ? 0.5025 0.5986 0.7186 -0.0535 -0.0526 0.0268  454 GLY A O     
3746 N  N     . ASP A 455 ? 0.5365 0.6295 0.7496 -0.0457 -0.0395 0.0242  455 ASP A N     
3747 C  CA    . ASP A 455 ? 0.5716 0.6547 0.7736 -0.0502 -0.0447 0.0152  455 ASP A CA    
3748 C  C     . ASP A 455 ? 0.5376 0.6150 0.7222 -0.0511 -0.0469 0.0068  455 ASP A C     
3749 O  O     . ASP A 455 ? 0.6249 0.6968 0.8027 -0.0568 -0.0544 0.0016  455 ASP A O     
3750 C  CB    . ASP A 455 ? 0.6647 0.7438 0.8631 -0.0468 -0.0386 0.0122  455 ASP A CB    
3751 C  CG    . ASP A 455 ? 0.7209 0.8047 0.9362 -0.0470 -0.0374 0.0207  455 ASP A CG    
3752 O  OD1   . ASP A 455 ? 1.0126 1.0991 1.2416 -0.0524 -0.0439 0.0261  455 ASP A OD1   
3753 O  OD2   . ASP A 455 ? 0.7954 0.8808 1.0108 -0.0422 -0.0302 0.0225  455 ASP A OD2   
3754 N  N     . LEU A 456 ? 0.5047 0.5832 0.6816 -0.0458 -0.0406 0.0055  456 LEU A N     
3755 C  CA    . LEU A 456 ? 0.5382 0.6119 0.6996 -0.0464 -0.0418 -0.0014 456 LEU A CA    
3756 C  C     . LEU A 456 ? 0.5433 0.6197 0.7058 -0.0509 -0.0493 0.0015  456 LEU A C     
3757 O  O     . LEU A 456 ? 0.5614 0.6331 0.7121 -0.0548 -0.0545 -0.0043 456 LEU A O     
3758 C  CB    . LEU A 456 ? 0.5191 0.5934 0.6746 -0.0402 -0.0337 -0.0025 456 LEU A CB    
3759 C  CG    . LEU A 456 ? 0.5606 0.6291 0.7038 -0.0379 -0.0293 -0.0102 456 LEU A CG    
3760 C  CD1   . LEU A 456 ? 0.6570 0.7245 0.8046 -0.0376 -0.0281 -0.0104 456 LEU A CD1   
3761 C  CD2   . LEU A 456 ? 0.5472 0.6166 0.6865 -0.0325 -0.0222 -0.0106 456 LEU A CD2   
3762 N  N     . LEU A 457 ? 0.5069 0.5916 0.6836 -0.0501 -0.0499 0.0108  457 LEU A N     
3763 C  CA    . LEU A 457 ? 0.5403 0.6292 0.7197 -0.0543 -0.0577 0.0152  457 LEU A CA    
3764 C  C     . LEU A 457 ? 0.5469 0.6343 0.7274 -0.0624 -0.0682 0.0139  457 LEU A C     
3765 O  O     . LEU A 457 ? 0.5374 0.6238 0.7094 -0.0673 -0.0758 0.0119  457 LEU A O     
3766 C  CB    . LEU A 457 ? 0.4994 0.5984 0.6965 -0.0510 -0.0555 0.0265  457 LEU A CB    
3767 C  CG    . LEU A 457 ? 0.5414 0.6408 0.7375 -0.0432 -0.0457 0.0277  457 LEU A CG    
3768 C  CD1   . LEU A 457 ? 0.4846 0.5936 0.6984 -0.0404 -0.0447 0.0391  457 LEU A CD1   
3769 C  CD2   . LEU A 457 ? 0.5222 0.6152 0.7012 -0.0431 -0.0454 0.0209  457 LEU A CD2   
3770 N  N     . GLU A 458 ? 0.5273 0.6141 0.7176 -0.0641 -0.0688 0.0150  458 GLU A N     
3771 C  CA    . GLU A 458 ? 0.6171 0.7000 0.8080 -0.0721 -0.0788 0.0123  458 GLU A CA    
3772 C  C     . GLU A 458 ? 0.6704 0.7417 0.8399 -0.0745 -0.0809 -0.0002 458 GLU A C     
3773 O  O     . GLU A 458 ? 0.6870 0.7551 0.8482 -0.0808 -0.0899 -0.0040 458 GLU A O     
3774 C  CB    . GLU A 458 ? 0.6552 0.7385 0.8615 -0.0729 -0.0778 0.0160  458 GLU A CB    
3775 C  CG    . GLU A 458 ? 0.8778 0.9574 1.0896 -0.0819 -0.0888 0.0150  458 GLU A CG    
3776 C  CD    . GLU A 458 ? 1.1349 1.2161 1.3653 -0.0826 -0.0874 0.0209  458 GLU A CD    
3777 O  OE1   . GLU A 458 ? 1.1150 1.2006 1.3521 -0.0756 -0.0774 0.0256  458 GLU A OE1   
3778 O  OE2   . GLU A 458 ? 1.1925 1.2705 1.4307 -0.0903 -0.0964 0.0209  458 GLU A OE2   
3779 N  N     . GLU A 459 ? 0.7128 0.7781 0.8729 -0.0693 -0.0725 -0.0066 459 GLU A N     
3780 C  CA    . GLU A 459 ? 0.7078 0.7630 0.8488 -0.0703 -0.0729 -0.0179 459 GLU A CA    
3781 C  C     . GLU A 459 ? 0.6474 0.7036 0.7742 -0.0712 -0.0752 -0.0200 459 GLU A C     
3782 O  O     . GLU A 459 ? 0.6579 0.7081 0.7707 -0.0754 -0.0802 -0.0271 459 GLU A O     
3783 C  CB    . GLU A 459 ? 0.7654 0.8165 0.9019 -0.0641 -0.0633 -0.0223 459 GLU A CB    
3784 C  CG    . GLU A 459 ? 0.8306 0.8723 0.9498 -0.0641 -0.0621 -0.0330 459 GLU A CG    
3785 C  CD    . GLU A 459 ? 1.1054 1.1377 1.2245 -0.0678 -0.0660 -0.0389 459 GLU A CD    
3786 O  OE1   . GLU A 459 ? 1.1176 1.1507 1.2512 -0.0706 -0.0695 -0.0341 459 GLU A OE1   
3787 O  OE2   . GLU A 459 ? 1.1618 1.1857 1.2670 -0.0678 -0.0651 -0.0480 459 GLU A OE2   
3788 N  N     . ARG A 460 ? 0.5648 0.6283 0.6949 -0.0673 -0.0712 -0.0139 460 ARG A N     
3789 C  CA    . ARG A 460 ? 0.6043 0.6695 0.7228 -0.0680 -0.0731 -0.0141 460 ARG A CA    
3790 C  C     . ARG A 460 ? 0.7517 0.8202 0.8700 -0.0750 -0.0843 -0.0111 460 ARG A C     
3791 O  O     . ARG A 460 ? 0.7871 0.8531 0.8896 -0.0781 -0.0884 -0.0154 460 ARG A O     
3792 C  CB    . ARG A 460 ? 0.6723 0.7439 0.7975 -0.0624 -0.0668 -0.0073 460 ARG A CB    
3793 C  CG    . ARG A 460 ? 0.7043 0.7793 0.8226 -0.0634 -0.0696 -0.0043 460 ARG A CG    
3794 C  CD    . ARG A 460 ? 0.6884 0.7625 0.8029 -0.0577 -0.0611 -0.0045 460 ARG A CD    
3795 N  NE    . ARG A 460 ? 0.7611 0.8371 0.8671 -0.0590 -0.0634 -0.0023 460 ARG A NE    
3796 C  CZ    . ARG A 460 ? 0.7719 0.8538 0.8865 -0.0576 -0.0639 0.0066  460 ARG A CZ    
3797 N  NH1   . ARG A 460 ? 0.8280 0.9145 0.9599 -0.0545 -0.0618 0.0137  460 ARG A NH1   
3798 N  NH2   . ARG A 460 ? 0.7511 0.8346 0.8573 -0.0591 -0.0662 0.0089  460 ARG A NH2   
3799 N  N     . GLN A 461 ? 0.7552 0.8301 0.8911 -0.0776 -0.0894 -0.0030 461 GLN A N     
3800 C  CA    . GLN A 461 ? 0.7479 0.8267 0.8848 -0.0852 -0.1014 0.0004  461 GLN A CA    
3801 C  C     . GLN A 461 ? 0.7255 0.7943 0.8488 -0.0916 -0.1084 -0.0100 461 GLN A C     
3802 O  O     . GLN A 461 ? 0.8460 0.9141 0.9562 -0.0971 -0.1167 -0.0127 461 GLN A O     
3803 C  CB    . GLN A 461 ? 0.8459 0.9346 1.0073 -0.0867 -0.1051 0.0120  461 GLN A CB    
3804 C  CG    . GLN A 461 ? 0.9156 1.0155 1.0890 -0.0822 -0.1022 0.0234  461 GLN A CG    
3805 C  CD    . GLN A 461 ? 0.9589 1.0620 1.1211 -0.0847 -0.1080 0.0252  461 GLN A CD    
3806 O  OE1   . GLN A 461 ? 1.0375 1.1413 1.1933 -0.0922 -0.1192 0.0244  461 GLN A OE1   
3807 N  NE2   . GLN A 461 ? 0.8535 0.9581 1.0128 -0.0785 -0.1006 0.0277  461 GLN A NE2   
3808 N  N     . LYS A 462 ? 0.7371 0.7977 0.8625 -0.0909 -0.1050 -0.0161 462 LYS A N     
3809 C  CA    . LYS A 462 ? 0.8020 0.8507 0.9141 -0.0961 -0.1102 -0.0273 462 LYS A CA    
3810 C  C     . LYS A 462 ? 0.8622 0.9044 0.9494 -0.0945 -0.1073 -0.0368 462 LYS A C     
3811 O  O     . LYS A 462 ? 0.9305 0.9663 1.0020 -0.0999 -0.1142 -0.0443 462 LYS A O     
3812 C  CB    . LYS A 462 ? 0.8103 0.8513 0.9306 -0.0941 -0.1052 -0.0310 462 LYS A CB    
3813 C  CG    . LYS A 462 ? 0.8783 0.9215 1.0192 -0.0992 -0.1117 -0.0247 462 LYS A CG    
3814 C  CD    . LYS A 462 ? 0.9484 0.9928 1.1051 -0.0938 -0.1029 -0.0203 462 LYS A CD    
3815 C  CE    . LYS A 462 ? 1.1654 1.1966 1.3206 -0.0953 -0.1026 -0.0285 462 LYS A CE    
3816 N  NZ    . LYS A 462 ? 1.0777 1.1113 1.2499 -0.0908 -0.0953 -0.0223 462 LYS A NZ    
3817 N  N     . ILE A 463 ? 0.8734 0.9173 0.9565 -0.0872 -0.0970 -0.0367 463 ILE A N     
3818 C  CA    . ILE A 463 ? 0.8376 0.8769 0.8995 -0.0852 -0.0930 -0.0443 463 ILE A CA    
3819 C  C     . ILE A 463 ? 0.9102 0.9553 0.9614 -0.0889 -0.0997 -0.0411 463 ILE A C     
3820 O  O     . ILE A 463 ? 0.9936 1.0335 1.0250 -0.0918 -0.1026 -0.0485 463 ILE A O     
3821 C  CB    . ILE A 463 ? 0.8294 0.8703 0.8926 -0.0773 -0.0813 -0.0435 463 ILE A CB    
3822 C  CG1   . ILE A 463 ? 0.8424 0.8755 0.9077 -0.0740 -0.0749 -0.0499 463 ILE A CG1   
3823 C  CG2   . ILE A 463 ? 0.7408 0.7823 0.7868 -0.0756 -0.0780 -0.0462 463 ILE A CG2   
3824 C  CD1   . ILE A 463 ? 0.8529 0.8891 0.9234 -0.0670 -0.0649 -0.0476 463 ILE A CD1   
3825 N  N     . LYS A 464 ? 0.8624 0.9185 0.9262 -0.0886 -0.1017 -0.0297 464 LYS A N     
3826 C  CA    . LYS A 464 ? 0.9071 0.9701 0.9630 -0.0921 -0.1086 -0.0245 464 LYS A CA    
3827 C  C     . LYS A 464 ? 1.0044 1.0656 1.0536 -0.1009 -0.1216 -0.0272 464 LYS A C     
3828 O  O     . LYS A 464 ? 1.1372 1.1997 1.1694 -0.1046 -0.1273 -0.0286 464 LYS A O     
3829 C  CB    . LYS A 464 ? 0.8046 0.8793 0.8788 -0.0896 -0.1082 -0.0109 464 LYS A CB    
3830 C  CG    . LYS A 464 ? 0.8243 0.8996 0.9054 -0.0815 -0.0961 -0.0087 464 LYS A CG    
3831 C  CD    . LYS A 464 ? 0.7500 0.8355 0.8486 -0.0787 -0.0953 0.0039  464 LYS A CD    
3832 C  CE    . LYS A 464 ? 0.8909 0.9802 0.9813 -0.0774 -0.0945 0.0084  464 LYS A CE    
3833 N  NZ    . LYS A 464 ? 0.8755 0.9749 0.9827 -0.0764 -0.0972 0.0217  464 LYS A NZ    
3834 N  N     . LYS A 465 ? 0.9451 1.0036 1.0072 -0.1046 -0.1266 -0.0279 465 LYS A N     
3835 C  CA    . LYS A 465 ? 1.0547 1.1098 1.1106 -0.1138 -0.1396 -0.0318 465 LYS A CA    
3836 C  C     . LYS A 465 ? 1.1389 1.1802 1.1690 -0.1155 -0.1393 -0.0470 465 LYS A C     
3837 O  O     . LYS A 465 ? 1.1999 1.2398 1.2114 -0.1211 -0.1476 -0.0511 465 LYS A O     
3838 C  CB    . LYS A 465 ? 1.0257 1.0804 1.1037 -0.1174 -0.1441 -0.0287 465 LYS A CB    
3839 C  CG    . LYS A 465 ? 0.9652 1.0170 1.0405 -0.1280 -0.1591 -0.0315 465 LYS A CG    
3840 C  CD    . LYS A 465 ? 1.0172 1.0785 1.1210 -0.1321 -0.1660 -0.0198 465 LYS A CD    
3841 C  CE    . LYS A 465 ? 0.9685 1.0245 1.0714 -0.1435 -0.1810 -0.0241 465 LYS A CE    
3842 N  NZ    . LYS A 465 ? 0.9291 0.9879 1.0127 -0.1502 -0.1927 -0.0258 465 LYS A NZ    
3843 N  N     . LYS A 466 ? 1.1802 1.2112 1.2085 -0.1105 -0.1296 -0.0553 466 LYS A N     
3844 C  CA    . LYS A 466 ? 1.2151 1.2325 1.2205 -0.1107 -0.1276 -0.0698 466 LYS A CA    
3845 C  C     . LYS A 466 ? 1.3157 1.3353 1.2987 -0.1078 -0.1232 -0.0722 466 LYS A C     
3846 O  O     . LYS A 466 ? 1.4233 1.4337 1.3837 -0.1094 -0.1238 -0.0832 466 LYS A O     
3847 C  CB    . LYS A 466 ? 1.1367 1.1445 1.1481 -0.1050 -0.1174 -0.0761 466 LYS A CB    
3848 C  CG    . LYS A 466 ? 1.1639 1.1667 1.1941 -0.1084 -0.1217 -0.0756 466 LYS A CG    
3849 C  CD    . LYS A 466 ? 1.2828 1.2724 1.3120 -0.1041 -0.1136 -0.0849 466 LYS A CD    
3850 C  CE    . LYS A 466 ? 1.2361 1.2115 1.2408 -0.1059 -0.1147 -0.0996 466 LYS A CE    
3851 N  NZ    . LYS A 466 ? 1.1326 1.0933 1.1403 -0.1036 -0.1097 -0.1085 466 LYS A NZ    
3852 N  N     . MET A 467 ? 1.2936 1.3248 1.2825 -0.1034 -0.1182 -0.0621 467 MET A N     
3853 C  CA    . MET A 467 ? 1.5268 1.5611 1.4966 -0.1009 -0.1141 -0.0626 467 MET A CA    
3854 C  C     . MET A 467 ? 1.4912 1.5281 1.4431 -0.1079 -0.1252 -0.0629 467 MET A C     
3855 O  O     . MET A 467 ? 1.5433 1.5782 1.4722 -0.1072 -0.1227 -0.0682 467 MET A O     
3856 C  CB    . MET A 467 ? 1.3468 1.3923 1.3293 -0.0956 -0.1077 -0.0509 467 MET A CB    
3857 C  CG    . MET A 467 ? 1.1849 1.2277 1.1660 -0.0879 -0.0943 -0.0540 467 MET A CG    
3858 S  SD    . MET A 467 ? 1.3130 1.3664 1.3120 -0.0824 -0.0878 -0.0412 467 MET A SD    
3859 C  CE    . MET A 467 ? 1.2176 1.2816 1.2121 -0.0868 -0.0967 -0.0308 467 MET A CE    
3860 N  N     . LYS A 468 ? 1.4400 1.4821 1.4021 -0.1148 -0.1375 -0.0568 468 LYS A N     
3861 C  CA    . LYS A 468 ? 1.3917 1.4378 1.3373 -0.1221 -0.1497 -0.0559 468 LYS A CA    
3862 C  C     . LYS A 468 ? 1.4202 1.4522 1.3417 -0.1270 -0.1542 -0.0717 468 LYS A C     
3863 O  O     . LYS A 468 ? 1.4160 1.4479 1.3124 -0.1301 -0.1586 -0.0756 468 LYS A O     
3864 C  CB    . LYS A 468 ? 1.3351 1.3918 1.3009 -0.1283 -0.1620 -0.0442 468 LYS A CB    
3865 C  CG    . LYS A 468 ? 1.3690 1.4407 1.3540 -0.1241 -0.1591 -0.0278 468 LYS A CG    
3866 C  CD    . LYS A 468 ? 1.4185 1.4928 1.3911 -0.1174 -0.1488 -0.0261 468 LYS A CD    
3867 C  CE    . LYS A 468 ? 1.4185 1.5074 1.4064 -0.1152 -0.1493 -0.0097 468 LYS A CE    
3868 N  NZ    . LYS A 468 ? 1.3185 1.4106 1.3350 -0.1101 -0.1432 -0.0023 468 LYS A NZ    
3869 N  N     . ALA A 469 ? 1.4510 1.4706 1.3793 -0.1275 -0.1531 -0.0808 469 ALA A N     
3870 C  CA    . ALA A 469 ? 1.5002 1.5037 1.4075 -0.1315 -0.1565 -0.0968 469 ALA A CA    
3871 C  C     . ALA A 469 ? 1.6396 1.6322 1.5314 -0.1236 -0.1423 -0.1082 469 ALA A C     
3872 O  O     . ALA A 469 ? 1.6395 1.6172 1.5132 -0.1253 -0.1428 -0.1225 469 ALA A O     
3873 C  CB    . ALA A 469 ? 1.3203 1.3151 1.2446 -0.1369 -0.1638 -0.1003 469 ALA A CB    
3874 N  N     . THR A 470 ? 1.8471 1.8466 1.7458 -0.1151 -0.1297 -0.1021 470 THR A N     
3875 C  CA    . THR A 470 ? 1.8303 1.8215 1.7180 -0.1074 -0.1160 -0.1111 470 THR A CA    
3876 C  C     . THR A 470 ? 1.8293 1.8183 1.6855 -0.1074 -0.1145 -0.1184 470 THR A C     
3877 O  O     . THR A 470 ? 1.8887 1.8893 1.7362 -0.1084 -0.1168 -0.1104 470 THR A O     
3878 C  CB    . THR A 470 ? 1.7612 1.7617 1.6656 -0.0994 -0.1045 -0.1018 470 THR A CB    
3879 O  OG1   . THR A 470 ? 1.8995 1.9008 1.8307 -0.0986 -0.1047 -0.0964 470 THR A OG1   
3880 C  CG2   . THR A 470 ? 1.6833 1.6775 1.5771 -0.0917 -0.0909 -0.1096 470 THR A CG2   
3881 N  N     . ILE A 471 ? 1.6903 1.6643 1.5294 -0.1058 -0.1101 -0.1332 471 ILE A N     
3882 C  CA    . ILE A 471 ? 1.7065 1.6766 1.5134 -0.1052 -0.1074 -0.1419 471 ILE A CA    
3883 C  C     . ILE A 471 ? 1.7214 1.6957 1.5249 -0.0955 -0.0912 -0.1406 471 ILE A C     
3884 O  O     . ILE A 471 ? 1.6842 1.6701 1.4778 -0.0940 -0.0884 -0.1333 471 ILE A O     
3885 C  CB    . ILE A 471 ? 1.6616 1.6122 1.4504 -0.1083 -0.1106 -0.1596 471 ILE A CB    
3886 C  CG1   . ILE A 471 ? 1.5925 1.5394 1.3863 -0.1191 -0.1279 -0.1604 471 ILE A CG1   
3887 C  CG2   . ILE A 471 ? 1.6468 1.5934 1.4003 -0.1069 -0.1065 -0.1691 471 ILE A CG2   
3888 C  CD1   . ILE A 471 ? 1.4986 1.4240 1.2834 -0.1224 -0.1313 -0.1772 471 ILE A CD1   
3889 N  N     . ASP A 472 ? 1.6234 1.5888 1.4362 -0.0891 -0.0808 -0.1468 472 ASP A N     
3890 C  CA    . ASP A 472 ? 1.5477 1.5170 1.3612 -0.0799 -0.0655 -0.1455 472 ASP A CA    
3891 C  C     . ASP A 472 ? 1.5669 1.5533 1.3970 -0.0781 -0.0633 -0.1296 472 ASP A C     
3892 O  O     . ASP A 472 ? 1.5429 1.5334 1.3977 -0.0782 -0.0654 -0.1221 472 ASP A O     
3893 C  CB    . ASP A 472 ? 1.4397 1.3980 1.2673 -0.0743 -0.0573 -0.1523 472 ASP A CB    
3894 C  CG    . ASP A 472 ? 1.5521 1.5140 1.3803 -0.0650 -0.0418 -0.1517 472 ASP A CG    
3895 O  OD1   . ASP A 472 ? 1.6060 1.5777 1.4220 -0.0629 -0.0369 -0.1473 472 ASP A OD1   
3896 O  OD2   . ASP A 472 ? 1.5543 1.5101 1.3966 -0.0599 -0.0348 -0.1548 472 ASP A OD2   
3897 N  N     . PRO A 473 ? 1.6177 1.6141 1.4348 -0.0763 -0.0590 -0.1242 473 PRO A N     
3898 C  CA    . PRO A 473 ? 1.5968 1.6081 1.4297 -0.0753 -0.0580 -0.1090 473 PRO A CA    
3899 C  C     . PRO A 473 ? 1.5161 1.5300 1.3705 -0.0688 -0.0477 -0.1052 473 PRO A C     
3900 O  O     . PRO A 473 ? 1.5023 1.5250 1.3753 -0.0687 -0.0487 -0.0943 473 PRO A O     
3901 C  CB    . PRO A 473 ? 1.5825 1.6020 1.3941 -0.0748 -0.0549 -0.1055 473 PRO A CB    
3902 C  CG    . PRO A 473 ? 1.6032 1.6124 1.3922 -0.0715 -0.0475 -0.1190 473 PRO A CG    
3903 C  CD    . PRO A 473 ? 1.5773 1.5715 1.3649 -0.0748 -0.0542 -0.1313 473 PRO A CD    
3904 N  N     . ILE A 474 ? 1.5329 1.5392 1.3849 -0.0632 -0.0378 -0.1138 474 ILE A N     
3905 C  CA    . ILE A 474 ? 1.6096 1.6180 1.4830 -0.0577 -0.0297 -0.1105 474 ILE A CA    
3906 C  C     . ILE A 474 ? 1.5002 1.5062 1.3948 -0.0601 -0.0365 -0.1079 474 ILE A C     
3907 O  O     . ILE A 474 ? 1.5461 1.5590 1.4598 -0.0584 -0.0347 -0.0996 474 ILE A O     
3908 C  CB    . ILE A 474 ? 1.6595 1.6600 1.5273 -0.0513 -0.0188 -0.1201 474 ILE A CB    
3909 C  CG1   . ILE A 474 ? 1.5023 1.5120 1.3647 -0.0462 -0.0078 -0.1159 474 ILE A CG1   
3910 C  CG2   . ILE A 474 ? 1.5288 1.5246 1.4181 -0.0482 -0.0161 -0.1213 474 ILE A CG2   
3911 C  CD1   . ILE A 474 ? 1.4051 1.4207 1.2459 -0.0487 -0.0091 -0.1134 474 ILE A CD1   
3912 N  N     . GLU A 475 ? 1.4573 1.4535 1.3486 -0.0645 -0.0444 -0.1148 475 GLU A N     
3913 C  CA    . GLU A 475 ? 1.3702 1.3655 1.2817 -0.0675 -0.0514 -0.1109 475 GLU A CA    
3914 C  C     . GLU A 475 ? 1.2861 1.2933 1.2069 -0.0712 -0.0584 -0.0988 475 GLU A C     
3915 O  O     . GLU A 475 ? 1.1660 1.1776 1.1072 -0.0706 -0.0590 -0.0917 475 GLU A O     
3916 C  CB    . GLU A 475 ? 1.3555 1.3382 1.2617 -0.0724 -0.0594 -0.1202 475 GLU A CB    
3917 C  CG    . GLU A 475 ? 1.4716 1.4405 1.3664 -0.0687 -0.0527 -0.1332 475 GLU A CG    
3918 C  CD    . GLU A 475 ? 1.4830 1.4438 1.3966 -0.0662 -0.0503 -0.1357 475 GLU A CD    
3919 O  OE1   . GLU A 475 ? 1.4813 1.4498 1.4155 -0.0640 -0.0482 -0.1267 475 GLU A OE1   
3920 O  OE2   . GLU A 475 ? 1.4139 1.3603 1.3211 -0.0665 -0.0504 -0.1465 475 GLU A OE2   
3921 N  N     . ARG A 476 ? 1.3207 1.3330 1.2265 -0.0750 -0.0636 -0.0962 476 ARG A N     
3922 C  CA    . ARG A 476 ? 1.3432 1.3670 1.2588 -0.0778 -0.0697 -0.0837 476 ARG A CA    
3923 C  C     . ARG A 476 ? 1.2557 1.2874 1.1862 -0.0726 -0.0614 -0.0752 476 ARG A C     
3924 O  O     . ARG A 476 ? 1.3582 1.3950 1.3075 -0.0726 -0.0636 -0.0672 476 ARG A O     
3925 C  CB    . ARG A 476 ? 1.4255 1.4544 1.3213 -0.0819 -0.0753 -0.0814 476 ARG A CB    
3926 C  CG    . ARG A 476 ? 1.4690 1.5111 1.3726 -0.0816 -0.0759 -0.0675 476 ARG A CG    
3927 C  CD    . ARG A 476 ? 1.4829 1.5313 1.3841 -0.0883 -0.0885 -0.0607 476 ARG A CD    
3928 N  NE    . ARG A 476 ? 1.5792 1.6388 1.4969 -0.0874 -0.0893 -0.0464 476 ARG A NE    
3929 C  CZ    . ARG A 476 ? 1.5530 1.6208 1.4740 -0.0919 -0.0991 -0.0369 476 ARG A CZ    
3930 N  NH1   . ARG A 476 ? 1.5530 1.6201 1.4613 -0.0985 -0.1102 -0.0398 476 ARG A NH1   
3931 N  NH2   . ARG A 476 ? 1.4159 1.4927 1.3537 -0.0899 -0.0980 -0.0242 476 ARG A NH2   
3932 N  N     . LYS A 477 ? 1.2227 1.2553 1.1453 -0.0679 -0.0517 -0.0771 477 LYS A N     
3933 C  CA    . LYS A 477 ? 1.1708 1.2098 1.1075 -0.0634 -0.0441 -0.0702 477 LYS A CA    
3934 C  C     . LYS A 477 ? 1.0792 1.1148 1.0347 -0.0608 -0.0419 -0.0713 477 LYS A C     
3935 O  O     . LYS A 477 ? 1.1609 1.2016 1.1321 -0.0596 -0.0410 -0.0640 477 LYS A O     
3936 C  CB    . LYS A 477 ? 1.2646 1.3049 1.1905 -0.0593 -0.0342 -0.0727 477 LYS A CB    
3937 C  CG    . LYS A 477 ? 1.2109 1.2603 1.1293 -0.0600 -0.0331 -0.0645 477 LYS A CG    
3938 C  CD    . LYS A 477 ? 1.2297 1.2829 1.1487 -0.0552 -0.0221 -0.0633 477 LYS A CD    
3939 C  CE    . LYS A 477 ? 1.1774 1.2280 1.0756 -0.0532 -0.0164 -0.0708 477 LYS A CE    
3940 N  NZ    . LYS A 477 ? 1.1610 1.2204 1.0536 -0.0514 -0.0092 -0.0641 477 LYS A NZ    
3941 N  N     . LEU A 478 ? 1.0748 1.1014 1.0286 -0.0599 -0.0408 -0.0803 478 LEU A N     
3942 C  CA    . LEU A 478 ? 1.0744 1.0981 1.0453 -0.0573 -0.0385 -0.0808 478 LEU A CA    
3943 C  C     . LEU A 478 ? 1.0422 1.0688 1.0281 -0.0603 -0.0455 -0.0742 478 LEU A C     
3944 O  O     . LEU A 478 ? 1.0065 1.0375 1.0071 -0.0579 -0.0429 -0.0685 478 LEU A O     
3945 C  CB    . LEU A 478 ? 1.0471 1.0599 1.0135 -0.0563 -0.0370 -0.0910 478 LEU A CB    
3946 C  CG    . LEU A 478 ? 1.1331 1.1435 1.0970 -0.0503 -0.0267 -0.0959 478 LEU A CG    
3947 C  CD1   . LEU A 478 ? 0.9984 0.9966 0.9595 -0.0492 -0.0257 -0.1057 478 LEU A CD1   
3948 C  CD2   . LEU A 478 ? 0.9573 0.9744 0.9379 -0.0465 -0.0214 -0.0896 478 LEU A CD2   
3949 N  N     . LEU A 479 ? 1.0540 1.0784 1.0364 -0.0657 -0.0546 -0.0749 479 LEU A N     
3950 C  CA    . LEU A 479 ? 0.9681 0.9964 0.9667 -0.0683 -0.0609 -0.0677 479 LEU A CA    
3951 C  C     . LEU A 479 ? 0.9628 1.0013 0.9680 -0.0679 -0.0614 -0.0572 479 LEU A C     
3952 O  O     . LEU A 479 ? 0.9423 0.9849 0.9640 -0.0670 -0.0619 -0.0506 479 LEU A O     
3953 C  CB    . LEU A 479 ? 0.9311 0.9555 0.9268 -0.0748 -0.0715 -0.0699 479 LEU A CB    
3954 C  CG    . LEU A 479 ? 0.9157 0.9282 0.9063 -0.0774 -0.0745 -0.0801 479 LEU A CG    
3955 C  CD1   . LEU A 479 ? 0.8917 0.8994 0.8964 -0.0732 -0.0684 -0.0819 479 LEU A CD1   
3956 C  CD2   . LEU A 479 ? 1.1083 1.1125 1.0754 -0.0785 -0.0743 -0.0908 479 LEU A CD2   
3957 N  N     . ASP A 480 ? 0.9376 0.9802 0.9307 -0.0682 -0.0607 -0.0552 480 ASP A N     
3958 C  CA    . ASP A 480 ? 0.9813 1.0324 0.9823 -0.0672 -0.0602 -0.0450 480 ASP A CA    
3959 C  C     . ASP A 480 ? 1.0345 1.0865 1.0475 -0.0620 -0.0518 -0.0431 480 ASP A C     
3960 O  O     . ASP A 480 ? 0.9885 1.0442 1.0158 -0.0607 -0.0518 -0.0363 480 ASP A O     
3961 C  CB    . ASP A 480 ? 0.9761 1.0312 0.9618 -0.0684 -0.0603 -0.0427 480 ASP A CB    
3962 C  CG    . ASP A 480 ? 1.0656 1.1288 1.0603 -0.0680 -0.0609 -0.0312 480 ASP A CG    
3963 O  OD1   . ASP A 480 ? 1.0464 1.1109 1.0480 -0.0641 -0.0538 -0.0285 480 ASP A OD1   
3964 O  OD2   . ASP A 480 ? 1.0916 1.1597 1.0872 -0.0716 -0.0688 -0.0248 480 ASP A OD2   
3965 N  N     . TYR A 481 ? 1.1826 1.2312 1.1898 -0.0589 -0.0447 -0.0491 481 TYR A N     
3966 C  CA    . TYR A 481 ? 1.1973 1.2468 1.2150 -0.0546 -0.0378 -0.0479 481 TYR A CA    
3967 C  C     . TYR A 481 ? 1.0789 1.1265 1.1103 -0.0535 -0.0385 -0.0479 481 TYR A C     
3968 O  O     . TYR A 481 ? 1.0660 1.1162 1.1084 -0.0512 -0.0361 -0.0435 481 TYR A O     
3969 C  CB    . TYR A 481 ? 1.0932 1.1406 1.1028 -0.0519 -0.0308 -0.0538 481 TYR A CB    
3970 C  CG    . TYR A 481 ? 1.0941 1.1440 1.1123 -0.0484 -0.0243 -0.0520 481 TYR A CG    
3971 C  CD1   . TYR A 481 ? 1.1084 1.1615 1.1217 -0.0473 -0.0192 -0.0511 481 TYR A CD1   
3972 C  CD2   . TYR A 481 ? 1.1839 1.2330 1.2145 -0.0464 -0.0232 -0.0515 481 TYR A CD2   
3973 C  CE1   . TYR A 481 ? 1.0228 1.0782 1.0444 -0.0450 -0.0143 -0.0495 481 TYR A CE1   
3974 C  CE2   . TYR A 481 ? 0.9780 1.0293 1.0149 -0.0439 -0.0183 -0.0505 481 TYR A CE2   
3975 C  CZ    . TYR A 481 ? 1.0183 1.0725 1.0511 -0.0435 -0.0143 -0.0497 481 TYR A CZ    
3976 O  OH    . TYR A 481 ? 1.1878 1.2440 1.2275 -0.0418 -0.0105 -0.0487 481 TYR A OH    
3977 N  N     . ARG A 482 ? 0.9531 0.9959 0.9837 -0.0552 -0.0421 -0.0525 482 ARG A N     
3978 C  CA    . ARG A 482 ? 0.9228 0.9645 0.9670 -0.0542 -0.0425 -0.0514 482 ARG A CA    
3979 C  C     . ARG A 482 ? 0.8791 0.9261 0.9352 -0.0554 -0.0464 -0.0431 482 ARG A C     
3980 O  O     . ARG A 482 ? 0.7790 0.8282 0.8468 -0.0524 -0.0432 -0.0395 482 ARG A O     
3981 C  CB    . ARG A 482 ? 0.8538 0.8886 0.8959 -0.0564 -0.0458 -0.0575 482 ARG A CB    
3982 C  CG    . ARG A 482 ? 0.8236 0.8562 0.8778 -0.0538 -0.0430 -0.0577 482 ARG A CG    
3983 C  CD    . ARG A 482 ? 0.8619 0.8862 0.9151 -0.0560 -0.0460 -0.0636 482 ARG A CD    
3984 N  NE    . ARG A 482 ? 1.0993 1.1239 1.1676 -0.0571 -0.0487 -0.0593 482 ARG A NE    
3985 C  CZ    . ARG A 482 ? 1.1162 1.1428 1.1955 -0.0533 -0.0440 -0.0561 482 ARG A CZ    
3986 N  NH1   . ARG A 482 ? 1.0279 1.0561 1.1051 -0.0486 -0.0371 -0.0571 482 ARG A NH1   
3987 N  NH2   . ARG A 482 ? 1.0242 1.0520 1.1171 -0.0545 -0.0465 -0.0513 482 ARG A NH2   
3988 N  N     . GLN A 483 ? 0.7602 0.8100 0.8137 -0.0594 -0.0531 -0.0396 483 GLN A N     
3989 C  CA    . GLN A 483 ? 0.7843 0.8402 0.8510 -0.0599 -0.0565 -0.0307 483 GLN A CA    
3990 C  C     . GLN A 483 ? 0.7333 0.7932 0.8049 -0.0560 -0.0511 -0.0253 483 GLN A C     
3991 O  O     . GLN A 483 ? 0.7195 0.7824 0.8043 -0.0535 -0.0494 -0.0198 483 GLN A O     
3992 C  CB    . GLN A 483 ? 0.7745 0.8335 0.8378 -0.0655 -0.0658 -0.0273 483 GLN A CB    
3993 C  CG    . GLN A 483 ? 0.8701 0.9311 0.9194 -0.0669 -0.0671 -0.0266 483 GLN A CG    
3994 C  CD    . GLN A 483 ? 0.8351 0.9032 0.8928 -0.0652 -0.0665 -0.0165 483 GLN A CD    
3995 O  OE1   . GLN A 483 ? 0.8103 0.8825 0.8842 -0.0638 -0.0670 -0.0098 483 GLN A OE1   
3996 N  NE2   . GLN A 483 ? 0.8107 0.8804 0.8583 -0.0650 -0.0650 -0.0150 483 GLN A NE2   
3997 N  N     . ARG A 484 ? 0.7461 0.8054 0.8074 -0.0552 -0.0479 -0.0270 484 ARG A N     
3998 C  CA    . ARG A 484 ? 0.7404 0.8015 0.8067 -0.0518 -0.0426 -0.0230 484 ARG A CA    
3999 C  C     . ARG A 484 ? 0.7234 0.7820 0.7964 -0.0477 -0.0364 -0.0259 484 ARG A C     
4000 O  O     . ARG A 484 ? 0.6853 0.7449 0.7672 -0.0449 -0.0334 -0.0220 484 ARG A O     
4001 C  CB    . ARG A 484 ? 0.8247 0.8858 0.8796 -0.0523 -0.0404 -0.0240 484 ARG A CB    
4002 C  CG    . ARG A 484 ? 0.9360 1.0011 0.9941 -0.0525 -0.0414 -0.0157 484 ARG A CG    
4003 C  CD    . ARG A 484 ? 1.0154 1.0802 1.0664 -0.0519 -0.0367 -0.0160 484 ARG A CD    
4004 N  NE    . ARG A 484 ? 1.2818 1.3435 1.3379 -0.0488 -0.0304 -0.0194 484 ARG A NE    
4005 C  CZ    . ARG A 484 ? 1.1825 1.2429 1.2322 -0.0483 -0.0261 -0.0245 484 ARG A CZ    
4006 N  NH1   . ARG A 484 ? 1.1479 1.2094 1.1856 -0.0499 -0.0262 -0.0272 484 ARG A NH1   
4007 N  NH2   . ARG A 484 ? 1.0202 1.0785 1.0756 -0.0461 -0.0216 -0.0268 484 ARG A NH2   
4008 N  N     . LEU A 485 ? 0.7107 0.7659 0.7791 -0.0473 -0.0345 -0.0326 485 LEU A N     
4009 C  CA    . LEU A 485 ? 0.6400 0.6939 0.7142 -0.0439 -0.0296 -0.0347 485 LEU A CA    
4010 C  C     . LEU A 485 ? 0.6544 0.7101 0.7405 -0.0426 -0.0304 -0.0304 485 LEU A C     
4011 O  O     . LEU A 485 ? 0.5700 0.6264 0.6619 -0.0392 -0.0262 -0.0287 485 LEU A O     
4012 C  CB    . LEU A 485 ? 0.6507 0.7011 0.7195 -0.0437 -0.0282 -0.0413 485 LEU A CB    
4013 C  CG    . LEU A 485 ? 0.7839 0.8333 0.8426 -0.0435 -0.0253 -0.0454 485 LEU A CG    
4014 C  CD1   . LEU A 485 ? 0.7159 0.7625 0.7725 -0.0420 -0.0226 -0.0512 485 LEU A CD1   
4015 C  CD2   . LEU A 485 ? 0.6263 0.6780 0.6875 -0.0418 -0.0215 -0.0430 485 LEU A CD2   
4016 N  N     . ILE A 486 ? 0.6322 0.6887 0.7219 -0.0453 -0.0356 -0.0288 486 ILE A N     
4017 C  CA    . ILE A 486 ? 0.5328 0.5924 0.6355 -0.0443 -0.0361 -0.0235 486 ILE A CA    
4018 C  C     . ILE A 486 ? 0.5491 0.6129 0.6597 -0.0421 -0.0348 -0.0166 486 ILE A C     
4019 O  O     . ILE A 486 ? 0.5437 0.6094 0.6633 -0.0384 -0.0306 -0.0133 486 ILE A O     
4020 C  CB    . ILE A 486 ? 0.6320 0.6918 0.7383 -0.0487 -0.0431 -0.0226 486 ILE A CB    
4021 C  CG1   . ILE A 486 ? 0.6095 0.6630 0.7067 -0.0507 -0.0442 -0.0305 486 ILE A CG1   
4022 C  CG2   . ILE A 486 ? 0.5346 0.5983 0.6562 -0.0475 -0.0427 -0.0166 486 ILE A CG2   
4023 C  CD1   . ILE A 486 ? 0.6750 0.7265 0.7791 -0.0489 -0.0414 -0.0317 486 ILE A CD1   
4024 N  N     . LYS A 487 ? 0.5373 0.6025 0.6445 -0.0441 -0.0379 -0.0140 487 LYS A N     
4025 C  CA    . LYS A 487 ? 0.4926 0.5611 0.6084 -0.0417 -0.0365 -0.0068 487 LYS A CA    
4026 C  C     . LYS A 487 ? 0.5418 0.6070 0.6574 -0.0369 -0.0289 -0.0088 487 LYS A C     
4027 O  O     . LYS A 487 ? 0.5377 0.6039 0.6626 -0.0329 -0.0249 -0.0052 487 LYS A O     
4028 C  CB    . LYS A 487 ? 0.6382 0.7089 0.7496 -0.0450 -0.0416 -0.0031 487 LYS A CB    
4029 C  CG    . LYS A 487 ? 0.7026 0.7729 0.8154 -0.0423 -0.0380 0.0005  487 LYS A CG    
4030 C  CD    . LYS A 487 ? 0.7325 0.8072 0.8448 -0.0454 -0.0438 0.0074  487 LYS A CD    
4031 C  CE    . LYS A 487 ? 0.7353 0.8102 0.8555 -0.0420 -0.0404 0.0140  487 LYS A CE    
4032 N  NZ    . LYS A 487 ? 0.7560 0.8377 0.8830 -0.0439 -0.0465 0.0241  487 LYS A NZ    
4033 N  N     . ILE A 488 ? 0.5347 0.5960 0.6397 -0.0374 -0.0267 -0.0147 488 ILE A N     
4034 C  CA    . ILE A 488 ? 0.5336 0.5912 0.6377 -0.0340 -0.0207 -0.0173 488 ILE A CA    
4035 C  C     . ILE A 488 ? 0.4916 0.5486 0.5987 -0.0307 -0.0167 -0.0198 488 ILE A C     
4036 O  O     . ILE A 488 ? 0.5052 0.5604 0.6157 -0.0270 -0.0121 -0.0195 488 ILE A O     
4037 C  CB    . ILE A 488 ? 0.5922 0.6471 0.6858 -0.0358 -0.0199 -0.0224 488 ILE A CB    
4038 C  CG1   . ILE A 488 ? 0.6736 0.7300 0.7636 -0.0388 -0.0232 -0.0188 488 ILE A CG1   
4039 C  CG2   . ILE A 488 ? 0.5506 0.6017 0.6440 -0.0334 -0.0149 -0.0252 488 ILE A CG2   
4040 C  CD1   . ILE A 488 ? 0.8976 0.9524 0.9790 -0.0402 -0.0213 -0.0221 488 ILE A CD1   
4041 N  N     . LEU A 489 ? 0.5006 0.5587 0.6064 -0.0319 -0.0184 -0.0221 489 LEU A N     
4042 C  CA    . LEU A 489 ? 0.5341 0.5926 0.6425 -0.0290 -0.0147 -0.0234 489 LEU A CA    
4043 C  C     . LEU A 489 ? 0.5182 0.5800 0.6375 -0.0260 -0.0128 -0.0173 489 LEU A C     
4044 O  O     . LEU A 489 ? 0.5000 0.5616 0.6205 -0.0220 -0.0075 -0.0176 489 LEU A O     
4045 C  CB    . LEU A 489 ? 0.5213 0.5799 0.6274 -0.0310 -0.0170 -0.0263 489 LEU A CB    
4046 C  CG    . LEU A 489 ? 0.5607 0.6207 0.6705 -0.0284 -0.0140 -0.0260 489 LEU A CG    
4047 C  CD1   . LEU A 489 ? 0.4641 0.5227 0.5682 -0.0253 -0.0092 -0.0294 489 LEU A CD1   
4048 C  CD2   . LEU A 489 ? 0.5257 0.5846 0.6349 -0.0307 -0.0168 -0.0281 489 LEU A CD2   
4049 N  N     . ALA A 490 ? 0.5269 0.5926 0.6544 -0.0279 -0.0169 -0.0115 490 ALA A N     
4050 C  CA    . ALA A 490 ? 0.4755 0.5458 0.6158 -0.0248 -0.0147 -0.0044 490 ALA A CA    
4051 C  C     . ALA A 490 ? 0.4809 0.5495 0.6236 -0.0203 -0.0095 -0.0026 490 ALA A C     
4052 O  O     . ALA A 490 ? 0.4541 0.5235 0.6018 -0.0153 -0.0034 -0.0009 490 ALA A O     
4053 C  CB    . ALA A 490 ? 0.4275 0.5031 0.5771 -0.0286 -0.0214 0.0021  490 ALA A CB    
4054 N  N     . ASN A 491 ? 0.4392 0.5050 0.5783 -0.0218 -0.0114 -0.0030 491 ASN A N     
4055 C  CA    . ASN A 491 ? 0.4834 0.5455 0.6252 -0.0176 -0.0064 -0.0017 491 ASN A CA    
4056 C  C     . ASN A 491 ? 0.5159 0.5720 0.6497 -0.0144 -0.0002 -0.0090 491 ASN A C     
4057 O  O     . ASN A 491 ? 0.4712 0.5245 0.6083 -0.0093 0.0058  -0.0087 491 ASN A O     
4058 C  CB    . ASN A 491 ? 0.4834 0.5435 0.6228 -0.0204 -0.0100 -0.0003 491 ASN A CB    
4059 C  CG    . ASN A 491 ? 0.6090 0.6758 0.7572 -0.0229 -0.0160 0.0083  491 ASN A CG    
4060 O  OD1   . ASN A 491 ? 0.5747 0.6476 0.7334 -0.0222 -0.0171 0.0138  491 ASN A OD1   
4061 N  ND2   . ASN A 491 ? 0.6409 0.7075 0.7851 -0.0262 -0.0201 0.0101  491 ASN A ND2   
4062 N  N     . SER A 492 ? 0.5069 0.5609 0.6300 -0.0171 -0.0016 -0.0156 492 SER A N     
4063 C  CA    . SER A 492 ? 0.5578 0.6070 0.6728 -0.0149 0.0028  -0.0222 492 SER A CA    
4064 C  C     . SER A 492 ? 0.5673 0.6195 0.6837 -0.0112 0.0069  -0.0218 492 SER A C     
4065 O  O     . SER A 492 ? 0.4971 0.5458 0.6083 -0.0078 0.0118  -0.0257 492 SER A O     
4066 C  CB    . SER A 492 ? 0.5097 0.5575 0.6150 -0.0189 -0.0002 -0.0279 492 SER A CB    
4067 O  OG    . SER A 492 ? 0.6332 0.6796 0.7373 -0.0223 -0.0035 -0.0271 492 SER A OG    
4068 N  N     . VAL A 493 ? 0.5190 0.5776 0.6421 -0.0120 0.0048  -0.0171 493 VAL A N     
4069 C  CA    . VAL A 493 ? 0.4942 0.5568 0.6209 -0.0082 0.0092  -0.0145 493 VAL A CA    
4070 C  C     . VAL A 493 ? 0.4879 0.5509 0.6220 -0.0027 0.0153  -0.0104 493 VAL A C     
4071 O  O     . VAL A 493 ? 0.4602 0.5229 0.5913 0.0021  0.0218  -0.0116 493 VAL A O     
4072 C  CB    . VAL A 493 ? 0.5108 0.5796 0.6451 -0.0111 0.0051  -0.0096 493 VAL A CB    
4073 C  CG1   . VAL A 493 ? 0.5105 0.5852 0.6534 -0.0069 0.0100  -0.0037 493 VAL A CG1   
4074 C  CG2   . VAL A 493 ? 0.4592 0.5266 0.5855 -0.0145 0.0018  -0.0146 493 VAL A CG2   
4075 N  N     . TYR A 494 ? 0.4046 0.4685 0.5482 -0.0029 0.0136  -0.0052 494 TYR A N     
4076 C  CA    . TYR A 494 ? 0.4289 0.4921 0.5802 0.0032  0.0201  -0.0016 494 TYR A CA    
4077 C  C     . TYR A 494 ? 0.5291 0.5824 0.6693 0.0064  0.0254  -0.0096 494 TYR A C     
4078 O  O     . TYR A 494 ? 0.4904 0.5417 0.6287 0.0122  0.0330  -0.0111 494 TYR A O     
4079 C  CB    . TYR A 494 ? 0.4630 0.5287 0.6267 0.0024  0.0168  0.0058  494 TYR A CB    
4080 C  CG    . TYR A 494 ? 0.4627 0.5229 0.6306 0.0084  0.0235  0.0065  494 TYR A CG    
4081 C  CD1   . TYR A 494 ? 0.4857 0.5482 0.6615 0.0156  0.0319  0.0101  494 TYR A CD1   
4082 C  CD2   . TYR A 494 ? 0.4709 0.5233 0.6352 0.0072  0.0222  0.0036  494 TYR A CD2   
4083 C  CE1   . TYR A 494 ? 0.4752 0.5312 0.6547 0.0218  0.0389  0.0100  494 TYR A CE1   
4084 C  CE2   . TYR A 494 ? 0.5499 0.5956 0.7187 0.0128  0.0285  0.0039  494 TYR A CE2   
4085 C  CZ    . TYR A 494 ? 0.4701 0.5170 0.6462 0.0203  0.0369  0.0067  494 TYR A CZ    
4086 O  OH    . TYR A 494 ? 0.5368 0.5757 0.7175 0.0265  0.0438  0.0064  494 TYR A OH    
4087 N  N     . GLY A 495 ? 0.5412 0.5881 0.6739 0.0025  0.0215  -0.0147 495 GLY A N     
4088 C  CA    . GLY A 495 ? 0.5013 0.5380 0.6248 0.0043  0.0253  -0.0223 495 GLY A CA    
4089 C  C     . GLY A 495 ? 0.5072 0.5419 0.6182 0.0058  0.0285  -0.0294 495 GLY A C     
4090 O  O     . GLY A 495 ? 0.5031 0.5299 0.6069 0.0091  0.0333  -0.0353 495 GLY A O     
4091 N  N     . HIS A 496 ? 0.4407 0.4822 0.5486 0.0033  0.0256  -0.0290 496 HIS A N     
4092 C  CA    . HIS A 496 ? 0.5124 0.5540 0.6090 0.0046  0.0280  -0.0341 496 HIS A CA    
4093 C  C     . HIS A 496 ? 0.5499 0.5913 0.6457 0.0115  0.0364  -0.0334 496 HIS A C     
4094 O  O     . HIS A 496 ? 0.5718 0.6085 0.6550 0.0137  0.0398  -0.0400 496 HIS A O     
4095 C  CB    . HIS A 496 ? 0.4980 0.5476 0.5954 0.0014  0.0238  -0.0312 496 HIS A CB    
4096 C  CG    . HIS A 496 ? 0.5536 0.6057 0.6417 0.0029  0.0260  -0.0337 496 HIS A CG    
4097 N  ND1   . HIS A 496 ? 0.6223 0.6730 0.7001 -0.0002 0.0226  -0.0394 496 HIS A ND1   
4098 C  CD2   . HIS A 496 ? 0.6431 0.7003 0.7314 0.0074  0.0313  -0.0303 496 HIS A CD2   
4099 C  CE1   . HIS A 496 ? 0.6228 0.6774 0.6942 0.0020  0.0251  -0.0394 496 HIS A CE1   
4100 N  NE2   . HIS A 496 ? 0.5491 0.6075 0.6260 0.0067  0.0306  -0.0339 496 HIS A NE2   
4101 N  N     . MET A 497 ? 0.5659 0.6127 0.6747 0.0152  0.0398  -0.0254 497 MET A N     
4102 C  CA    . MET A 497 ? 0.5152 0.5631 0.6246 0.0227  0.0491  -0.0236 497 MET A CA    
4103 C  C     . MET A 497 ? 0.5523 0.5887 0.6552 0.0272  0.0550  -0.0303 497 MET A C     
4104 O  O     . MET A 497 ? 0.5105 0.5453 0.6076 0.0335  0.0633  -0.0324 497 MET A O     
4105 C  CB    . MET A 497 ? 0.5875 0.6447 0.7154 0.0253  0.0511  -0.0123 497 MET A CB    
4106 C  CG    . MET A 497 ? 0.5897 0.6574 0.7241 0.0213  0.0462  -0.0060 497 MET A CG    
4107 S  SD    . MET A 497 ? 0.6340 0.7139 0.7893 0.0252  0.0504  0.0074  497 MET A SD    
4108 C  CE    . MET A 497 ? 0.4578 0.5396 0.6285 0.0199  0.0417  0.0132  497 MET A CE    
4109 N  N     . GLY A 498 ? 0.5640 0.5922 0.6676 0.0241  0.0512  -0.0337 498 GLY A N     
4110 C  CA    . GLY A 498 ? 0.5399 0.5553 0.6384 0.0278  0.0562  -0.0404 498 GLY A CA    
4111 C  C     . GLY A 498 ? 0.6508 0.6563 0.7346 0.0229  0.0519  -0.0509 498 GLY A C     
4112 O  O     . GLY A 498 ? 0.7093 0.7028 0.7912 0.0235  0.0533  -0.0563 498 GLY A O     
4113 N  N     . PHE A 499 ? 0.6222 0.6328 0.6970 0.0179  0.0464  -0.0534 499 PHE A N     
4114 C  CA    . PHE A 499 ? 0.6888 0.6926 0.7514 0.0125  0.0413  -0.0621 499 PHE A CA    
4115 C  C     . PHE A 499 ? 0.7260 0.7271 0.7718 0.0146  0.0444  -0.0698 499 PHE A C     
4116 O  O     . PHE A 499 ? 0.6679 0.6778 0.7102 0.0170  0.0466  -0.0668 499 PHE A O     
4117 C  CB    . PHE A 499 ? 0.6028 0.6143 0.6674 0.0056  0.0330  -0.0594 499 PHE A CB    
4118 C  CG    . PHE A 499 ? 0.7762 0.7836 0.8303 0.0001  0.0278  -0.0669 499 PHE A CG    
4119 C  CD1   . PHE A 499 ? 0.8136 0.8110 0.8675 -0.0029 0.0257  -0.0714 499 PHE A CD1   
4120 C  CD2   . PHE A 499 ? 0.7980 0.8121 0.8441 -0.0023 0.0245  -0.0683 499 PHE A CD2   
4121 C  CE1   . PHE A 499 ? 0.7998 0.7944 0.8460 -0.0086 0.0205  -0.0774 499 PHE A CE1   
4122 C  CE2   . PHE A 499 ? 0.8622 0.8740 0.9005 -0.0075 0.0193  -0.0741 499 PHE A CE2   
4123 C  CZ    . PHE A 499 ? 0.7943 0.7967 0.8329 -0.0109 0.0172  -0.0787 499 PHE A CZ    
4124 N  N     . GLU A 500 ? 0.7803 0.7692 0.8155 0.0132  0.0440  -0.0794 500 GLU A N     
4125 C  CA    . GLU A 500 ? 0.7824 0.7667 0.7998 0.0157  0.0473  -0.0878 500 GLU A CA    
4126 C  C     . GLU A 500 ? 0.7679 0.7627 0.7758 0.0123  0.0425  -0.0874 500 GLU A C     
4127 O  O     . GLU A 500 ? 0.6983 0.6979 0.6966 0.0164  0.0469  -0.0874 500 GLU A O     
4128 C  CB    . GLU A 500 ? 0.9105 0.8789 0.9189 0.0130  0.0457  -0.0987 500 GLU A CB    
4129 C  CG    . GLU A 500 ? 1.1318 1.0877 1.1484 0.0175  0.0517  -0.0999 500 GLU A CG    
4130 C  CD    . GLU A 500 ? 1.4152 1.3682 1.4464 0.0125  0.0463  -0.0960 500 GLU A CD    
4131 O  OE1   . GLU A 500 ? 1.3387 1.2970 1.3857 0.0149  0.0481  -0.0866 500 GLU A OE1   
4132 O  OE2   . GLU A 500 ? 1.3276 1.2737 1.3548 0.0059  0.0401  -0.1018 500 GLU A OE2   
4133 N  N     . ASN A 501 ? 0.7410 0.7400 0.7520 0.0051  0.0340  -0.0865 501 ASN A N     
4134 C  CA    . ASN A 501 ? 0.7469 0.7555 0.7508 0.0018  0.0291  -0.0857 501 ASN A CA    
4135 C  C     . ASN A 501 ? 0.7128 0.7344 0.7277 0.0025  0.0286  -0.0755 501 ASN A C     
4136 O  O     . ASN A 501 ? 0.7216 0.7510 0.7357 -0.0011 0.0234  -0.0734 501 ASN A O     
4137 C  CB    . ASN A 501 ? 0.6649 0.6713 0.6666 -0.0059 0.0205  -0.0902 501 ASN A CB    
4138 C  CG    . ASN A 501 ? 0.7224 0.7354 0.7122 -0.0087 0.0159  -0.0924 501 ASN A CG    
4139 O  OD1   . ASN A 501 ? 0.6922 0.7051 0.6684 -0.0056 0.0188  -0.0957 501 ASN A OD1   
4140 N  ND2   . ASN A 501 ? 0.7333 0.7529 0.7285 -0.0143 0.0090  -0.0899 501 ASN A ND2   
4141 N  N     . ALA A 502 ? 0.7404 0.7643 0.7662 0.0069  0.0337  -0.0690 502 ALA A N     
4142 C  CA    . ALA A 502 ? 0.6400 0.6750 0.6772 0.0069  0.0328  -0.0597 502 ALA A CA    
4143 C  C     . ALA A 502 ? 0.5913 0.6341 0.6238 0.0113  0.0374  -0.0558 502 ALA A C     
4144 O  O     . ALA A 502 ? 0.6468 0.6870 0.6717 0.0167  0.0443  -0.0579 502 ALA A O     
4145 C  CB    . ALA A 502 ? 0.6200 0.6549 0.6726 0.0086  0.0348  -0.0537 502 ALA A CB    
4146 N  N     . ARG A 503 ? 0.5421 0.5943 0.5794 0.0092  0.0340  -0.0499 503 ARG A N     
4147 C  CA    . ARG A 503 ? 0.6368 0.6976 0.6716 0.0129  0.0379  -0.0444 503 ARG A CA    
4148 C  C     . ARG A 503 ? 0.6087 0.6728 0.6538 0.0183  0.0452  -0.0374 503 ARG A C     
4149 O  O     . ARG A 503 ? 0.6111 0.6769 0.6495 0.0239  0.0526  -0.0367 503 ARG A O     
4150 C  CB    . ARG A 503 ? 0.5698 0.6387 0.6103 0.0092  0.0324  -0.0391 503 ARG A CB    
4151 C  CG    . ARG A 503 ? 0.7141 0.7846 0.7423 0.0065  0.0278  -0.0431 503 ARG A CG    
4152 C  CD    . ARG A 503 ? 0.6921 0.7699 0.7285 0.0036  0.0231  -0.0372 503 ARG A CD    
4153 N  NE    . ARG A 503 ? 0.7609 0.8375 0.7942 -0.0012 0.0164  -0.0418 503 ARG A NE    
4154 C  CZ    . ARG A 503 ? 0.8895 0.9705 0.9142 -0.0024 0.0133  -0.0426 503 ARG A CZ    
4155 N  NH1   . ARG A 503 ? 0.7859 0.8726 0.8024 0.0008  0.0161  -0.0394 503 ARG A NH1   
4156 N  NH2   . ARG A 503 ? 0.9691 1.0496 0.9936 -0.0068 0.0073  -0.0460 503 ARG A NH2   
4157 N  N     . TRP A 504 ? 0.5041 0.5700 0.5657 0.0167  0.0432  -0.0318 504 TRP A N     
4158 C  CA    . TRP A 504 ? 0.6236 0.6939 0.6984 0.0210  0.0490  -0.0239 504 TRP A CA    
4159 C  C     . TRP A 504 ? 0.6399 0.7027 0.7168 0.0244  0.0533  -0.0269 504 TRP A C     
4160 O  O     . TRP A 504 ? 0.5875 0.6513 0.6791 0.0243  0.0528  -0.0218 504 TRP A O     
4161 C  CB    . TRP A 504 ? 0.5205 0.5969 0.6121 0.0170  0.0437  -0.0161 504 TRP A CB    
4162 C  CG    . TRP A 504 ? 0.5640 0.6484 0.6576 0.0159  0.0422  -0.0105 504 TRP A CG    
4163 C  CD1   . TRP A 504 ? 0.5477 0.6407 0.6495 0.0192  0.0471  -0.0015 504 TRP A CD1   
4164 C  CD2   . TRP A 504 ? 0.6023 0.6871 0.6912 0.0114  0.0360  -0.0127 504 TRP A CD2   
4165 N  NE1   . TRP A 504 ? 0.5446 0.6425 0.6469 0.0167  0.0439  0.0021  504 TRP A NE1   
4166 C  CE2   . TRP A 504 ? 0.5796 0.6725 0.6742 0.0122  0.0371  -0.0048 504 TRP A CE2   
4167 C  CE3   . TRP A 504 ? 0.5558 0.6353 0.6376 0.0069  0.0298  -0.0198 504 TRP A CE3   
4168 C  CZ2   . TRP A 504 ? 0.5441 0.6391 0.6376 0.0090  0.0324  -0.0041 504 TRP A CZ2   
4169 C  CZ3   . TRP A 504 ? 0.5188 0.6012 0.5995 0.0041  0.0255  -0.0191 504 TRP A CZ3   
4170 C  CH2   . TRP A 504 ? 0.5738 0.6636 0.6603 0.0053  0.0267  -0.0114 504 TRP A CH2   
4171 N  N     . TYR A 505 ? 0.6126 0.6674 0.6746 0.0273  0.0573  -0.0353 505 TYR A N     
4172 C  CA    . TYR A 505 ? 0.6109 0.6565 0.6741 0.0311  0.0622  -0.0391 505 TYR A CA    
4173 C  C     . TYR A 505 ? 0.6013 0.6517 0.6735 0.0389  0.0720  -0.0322 505 TYR A C     
4174 O  O     . TYR A 505 ? 0.5571 0.6146 0.6251 0.0430  0.0777  -0.0287 505 TYR A O     
4175 C  CB    . TYR A 505 ? 0.5725 0.6068 0.6162 0.0315  0.0633  -0.0512 505 TYR A CB    
4176 C  CG    . TYR A 505 ? 0.6150 0.6377 0.6578 0.0366  0.0699  -0.0562 505 TYR A CG    
4177 C  CD1   . TYR A 505 ? 0.6535 0.6677 0.7042 0.0339  0.0665  -0.0583 505 TYR A CD1   
4178 C  CD2   . TYR A 505 ? 0.6160 0.6360 0.6498 0.0444  0.0802  -0.0589 505 TYR A CD2   
4179 C  CE1   . TYR A 505 ? 0.6761 0.6787 0.7273 0.0388  0.0727  -0.0625 505 TYR A CE1   
4180 C  CE2   . TYR A 505 ? 0.6613 0.6694 0.6946 0.0497  0.0870  -0.0641 505 TYR A CE2   
4181 C  CZ    . TYR A 505 ? 0.6440 0.6430 0.6867 0.0469  0.0831  -0.0658 505 TYR A CZ    
4182 O  OH    . TYR A 505 ? 0.7059 0.6921 0.7496 0.0524  0.0900  -0.0706 505 TYR A OH    
4183 N  N     . CYS A 506 ? 0.5558 0.6031 0.6415 0.0413  0.0743  -0.0291 506 CYS A N     
4184 C  CA    . CYS A 506 ? 0.5351 0.5873 0.6322 0.0493  0.0842  -0.0217 506 CYS A CA    
4185 C  C     . CYS A 506 ? 0.5141 0.5582 0.6216 0.0516  0.0858  -0.0221 506 CYS A C     
4186 O  O     . CYS A 506 ? 0.5484 0.5969 0.6728 0.0485  0.0807  -0.0147 506 CYS A O     
4187 C  CB    . CYS A 506 ? 0.6336 0.7007 0.7480 0.0484  0.0830  -0.0088 506 CYS A CB    
4188 S  SG    . CYS A 506 ? 0.7891 0.8650 0.9226 0.0576  0.0945  0.0027  506 CYS A SG    
4189 N  N     . LYS A 507 ? 0.5479 0.5798 0.6446 0.0568  0.0928  -0.0307 507 LYS A N     
4190 C  CA    . LYS A 507 ? 0.6780 0.7009 0.7850 0.0598  0.0953  -0.0310 507 LYS A CA    
4191 C  C     . LYS A 507 ? 0.6607 0.6932 0.7899 0.0661  0.1017  -0.0183 507 LYS A C     
4192 O  O     . LYS A 507 ? 0.6169 0.6494 0.7628 0.0655  0.0989  -0.0123 507 LYS A O     
4193 C  CB    . LYS A 507 ? 0.6094 0.6159 0.6998 0.0647  0.1023  -0.0435 507 LYS A CB    
4194 C  CG    . LYS A 507 ? 0.7040 0.7009 0.8061 0.0711  0.1091  -0.0429 507 LYS A CG    
4195 C  CD    . LYS A 507 ? 0.8736 0.8571 0.9601 0.0793  0.1204  -0.0536 507 LYS A CD    
4196 C  CE    . LYS A 507 ? 0.9781 0.9662 1.0775 0.0907  0.1338  -0.0461 507 LYS A CE    
4197 N  NZ    . LYS A 507 ? 0.9591 0.9461 1.0828 0.0933  0.1345  -0.0377 507 LYS A NZ    
4198 N  N     . GLU A 508 ? 0.5146 0.5566 0.6451 0.0722  0.1102  -0.0132 508 GLU A N     
4199 C  CA    . GLU A 508 ? 0.6773 0.7308 0.8310 0.0779  0.1163  0.0002  508 GLU A CA    
4200 C  C     . GLU A 508 ? 0.6093 0.6744 0.7823 0.0704  0.1053  0.0112  508 GLU A C     
4201 O  O     . GLU A 508 ? 0.5446 0.6140 0.7380 0.0720  0.1050  0.0201  508 GLU A O     
4202 C  CB    . GLU A 508 ? 0.6633 0.7267 0.8143 0.0846  0.1266  0.0046  508 GLU A CB    
4203 C  CG    . GLU A 508 ? 0.7239 0.7763 0.8536 0.0926  0.1381  -0.0065 508 GLU A CG    
4204 C  CD    . GLU A 508 ? 0.9025 0.9507 1.0057 0.0879  0.1340  -0.0169 508 GLU A CD    
4205 O  OE1   . GLU A 508 ? 0.8560 0.9041 0.9559 0.0783  0.1216  -0.0190 508 GLU A OE1   
4206 O  OE2   . GLU A 508 ? 1.0051 1.0506 1.0907 0.0941  0.1433  -0.0226 508 GLU A OE2   
4207 N  N     . CYS A 509 ? 0.4723 0.5423 0.6389 0.0623  0.0961  0.0106  509 CYS A N     
4208 C  CA    . CYS A 509 ? 0.4578 0.5370 0.6398 0.0546  0.0853  0.0191  509 CYS A CA    
4209 C  C     . CYS A 509 ? 0.5062 0.5785 0.6931 0.0505  0.0779  0.0178  509 CYS A C     
4210 O  O     . CYS A 509 ? 0.5108 0.5904 0.7165 0.0489  0.0738  0.0276  509 CYS A O     
4211 C  CB    . CYS A 509 ? 0.4551 0.5374 0.6266 0.0471  0.0774  0.0164  509 CYS A CB    
4212 S  SG    . CYS A 509 ? 0.5924 0.6828 0.7561 0.0511  0.0850  0.0184  509 CYS A SG    
4213 N  N     . ALA A 510 ? 0.4790 0.5379 0.6495 0.0485  0.0760  0.0064  510 ALA A N     
4214 C  CA    . ALA A 510 ? 0.5221 0.5747 0.6963 0.0440  0.0689  0.0055  510 ALA A CA    
4215 C  C     . ALA A 510 ? 0.5383 0.5888 0.7283 0.0504  0.0745  0.0115  510 ALA A C     
4216 O  O     . ALA A 510 ? 0.5578 0.6126 0.7622 0.0476  0.0685  0.0194  510 ALA A O     
4217 C  CB    . ALA A 510 ? 0.6319 0.6710 0.7865 0.0406  0.0663  -0.0074 510 ALA A CB    
4218 N  N     . GLU A 511 ? 0.5540 0.5980 0.7411 0.0594  0.0862  0.0080  511 GLU A N     
4219 C  CA    . GLU A 511 ? 0.6110 0.6524 0.8144 0.0666  0.0928  0.0139  511 GLU A CA    
4220 C  C     . GLU A 511 ? 0.5242 0.5825 0.7518 0.0693  0.0938  0.0295  511 GLU A C     
4221 O  O     . GLU A 511 ? 0.6016 0.6625 0.8477 0.0711  0.0930  0.0383  511 GLU A O     
4222 C  CB    . GLU A 511 ? 0.5415 0.5704 0.7349 0.0761  0.1058  0.0052  511 GLU A CB    
4223 C  CG    . GLU A 511 ? 0.7079 0.7441 0.8992 0.0836  0.1166  0.0069  511 GLU A CG    
4224 C  CD    . GLU A 511 ? 0.8060 0.8282 0.9857 0.0933  0.1298  -0.0027 511 GLU A CD    
4225 O  OE1   . GLU A 511 ? 0.8395 0.8465 1.0178 0.0948  0.1308  -0.0090 511 GLU A OE1   
4226 O  OE2   . GLU A 511 ? 0.8506 0.8766 1.0224 0.0995  0.1394  -0.0040 511 GLU A OE2   
4227 N  N     . SER A 512 ? 0.5722 0.6426 0.8011 0.0689  0.0949  0.0339  512 SER A N     
4228 C  CA    . SER A 512 ? 0.5814 0.6689 0.8344 0.0692  0.0935  0.0492  512 SER A CA    
4229 C  C     . SER A 512 ? 0.5489 0.6420 0.8116 0.0596  0.0792  0.0553  512 SER A C     
4230 O  O     . SER A 512 ? 0.5143 0.6156 0.7982 0.0604  0.0770  0.0669  512 SER A O     
4231 C  CB    . SER A 512 ? 0.4632 0.5616 0.7147 0.0692  0.0963  0.0523  512 SER A CB    
4232 O  OG    . SER A 512 ? 0.5352 0.6296 0.7767 0.0785  0.1101  0.0474  512 SER A OG    
4233 N  N     . VAL A 513 ? 0.5413 0.6303 0.7883 0.0507  0.0695  0.0477  513 VAL A N     
4234 C  CA    . VAL A 513 ? 0.5144 0.6077 0.7667 0.0415  0.0561  0.0519  513 VAL A CA    
4235 C  C     . VAL A 513 ? 0.5462 0.6344 0.8061 0.0426  0.0543  0.0548  513 VAL A C     
4236 O  O     . VAL A 513 ? 0.5433 0.6405 0.8193 0.0396  0.0475  0.0654  513 VAL A O     
4237 C  CB    . VAL A 513 ? 0.4699 0.5573 0.7019 0.0334  0.0483  0.0416  513 VAL A CB    
4238 C  CG1   . VAL A 513 ? 0.4686 0.5572 0.7020 0.0249  0.0360  0.0436  513 VAL A CG1   
4239 C  CG2   . VAL A 513 ? 0.4746 0.5693 0.7037 0.0314  0.0481  0.0420  513 VAL A CG2   
4240 N  N     . THR A 514 ? 0.5818 0.6556 0.8305 0.0465  0.0600  0.0458  514 THR A N     
4241 C  CA    . THR A 514 ? 0.5604 0.6282 0.8164 0.0471  0.0582  0.0487  514 THR A CA    
4242 C  C     . THR A 514 ? 0.5526 0.6267 0.8323 0.0553  0.0648  0.0608  514 THR A C     
4243 O  O     . THR A 514 ? 0.5980 0.6758 0.8918 0.0540  0.0596  0.0699  514 THR A O     
4244 C  CB    . THR A 514 ? 0.6094 0.6592 0.8484 0.0485  0.0621  0.0358  514 THR A CB    
4245 O  OG1   . THR A 514 ? 0.9028 0.9472 1.1481 0.0469  0.0580  0.0392  514 THR A OG1   
4246 C  CG2   . THR A 514 ? 0.5457 0.5870 0.7822 0.0586  0.0757  0.0305  514 THR A CG2   
4247 N  N     . ALA A 515 ? 0.5649 0.6416 0.8499 0.0639  0.0763  0.0620  515 ALA A N     
4248 C  CA    . ALA A 515 ? 0.5431 0.6281 0.8530 0.0722  0.0832  0.0748  515 ALA A CA    
4249 C  C     . ALA A 515 ? 0.4958 0.6002 0.8262 0.0670  0.0739  0.0899  515 ALA A C     
4250 O  O     . ALA A 515 ? 0.5611 0.6726 0.9127 0.0689  0.0720  0.1021  515 ALA A O     
4251 C  CB    . ALA A 515 ? 0.5723 0.6566 0.8819 0.0827  0.0984  0.0726  515 ALA A CB    
4252 N  N     . TRP A 516 ? 0.5271 0.6401 0.8521 0.0601  0.0677  0.0895  516 TRP A N     
4253 C  CA    . TRP A 516 ? 0.5102 0.6398 0.8521 0.0531  0.0566  0.1019  516 TRP A CA    
4254 C  C     . TRP A 516 ? 0.5113 0.6402 0.8544 0.0459  0.0442  0.1049  516 TRP A C     
4255 O  O     . TRP A 516 ? 0.5262 0.6669 0.8899 0.0448  0.0385  0.1184  516 TRP A O     
4256 C  CB    . TRP A 516 ? 0.6034 0.7378 0.9352 0.0457  0.0508  0.0981  516 TRP A CB    
4257 C  CG    . TRP A 516 ? 0.7192 0.8605 1.0556 0.0510  0.0604  0.1004  516 TRP A CG    
4258 C  CD1   . TRP A 516 ? 0.7807 0.9150 1.0982 0.0530  0.0672  0.0901  516 TRP A CD1   
4259 C  CD2   . TRP A 516 ? 0.6518 0.8095 1.0136 0.0544  0.0639  0.1150  516 TRP A CD2   
4260 N  NE1   . TRP A 516 ? 0.6679 0.8129 0.9964 0.0579  0.0752  0.0973  516 TRP A NE1   
4261 C  CE2   . TRP A 516 ? 0.6067 0.7664 0.9632 0.0589  0.0737  0.1127  516 TRP A CE2   
4262 C  CE3   . TRP A 516 ? 0.5357 0.7077 0.9250 0.0541  0.0596  0.1306  516 TRP A CE3   
4263 C  CZ2   . TRP A 516 ? 0.5964 0.7715 0.9744 0.0631  0.0799  0.1255  516 TRP A CZ2   
4264 C  CZ3   . TRP A 516 ? 0.9768 1.1643 1.3885 0.0581  0.0653  0.1433  516 TRP A CZ3   
4265 C  CH2   . TRP A 516 ? 0.9828 1.1718 1.3889 0.0627  0.0757  0.1407  516 TRP A CH2   
4266 N  N     . GLY A 517 ? 0.5274 0.6436 0.8486 0.0409  0.0397  0.0932  517 GLY A N     
4267 C  CA    . GLY A 517 ? 0.4395 0.5552 0.7595 0.0341  0.0285  0.0959  517 GLY A CA    
4268 C  C     . GLY A 517 ? 0.4608 0.5761 0.7975 0.0399  0.0315  0.1052  517 GLY A C     
4269 O  O     . GLY A 517 ? 0.4662 0.5913 0.8159 0.0360  0.0224  0.1166  517 GLY A O     
4270 N  N     . ARG A 518 ? 0.4277 0.5315 0.7640 0.0493  0.0439  0.1006  518 ARG A N     
4271 C  CA    . ARG A 518 ? 0.5222 0.6244 0.8766 0.0563  0.0485  0.1096  518 ARG A CA    
4272 C  C     . ARG A 518 ? 0.5492 0.6697 0.9320 0.0596  0.0480  0.1270  518 ARG A C     
4273 O  O     . ARG A 518 ? 0.4491 0.5771 0.8483 0.0585  0.0416  0.1394  518 ARG A O     
4274 C  CB    . ARG A 518 ? 0.5687 0.6548 0.9180 0.0667  0.0634  0.1006  518 ARG A CB    
4275 C  CG    . ARG A 518 ? 0.6334 0.7005 0.9609 0.0639  0.0632  0.0866  518 ARG A CG    
4276 C  CD    . ARG A 518 ? 0.6087 0.6594 0.9316 0.0739  0.0775  0.0773  518 ARG A CD    
4277 N  NE    . ARG A 518 ? 0.7229 0.7667 1.0235 0.0734  0.0818  0.0628  518 ARG A NE    
4278 C  CZ    . ARG A 518 ? 0.7302 0.7712 1.0286 0.0819  0.0940  0.0583  518 ARG A CZ    
4279 N  NH1   . ARG A 518 ? 0.7033 0.7475 1.0210 0.0923  0.1043  0.0667  518 ARG A NH1   
4280 N  NH2   . ARG A 518 ? 0.7925 0.8279 1.0689 0.0803  0.0964  0.0456  518 ARG A NH2   
4281 N  N     . GLU A 519 ? 0.4460 0.5748 0.8359 0.0635  0.0545  0.1290  519 GLU A N     
4282 C  CA    . GLU A 519 ? 0.5121 0.6596 0.9314 0.0669  0.0549  0.1461  519 GLU A CA    
4283 C  C     . GLU A 519 ? 0.5334 0.6957 0.9613 0.0559  0.0377  0.1566  519 GLU A C     
4284 O  O     . GLU A 519 ? 0.4627 0.6365 0.9134 0.0568  0.0334  0.1716  519 GLU A O     
4285 C  CB    . GLU A 519 ? 0.5653 0.7198 0.9885 0.0715  0.0640  0.1461  519 GLU A CB    
4286 C  CG    . GLU A 519 ? 0.7774 0.9525 1.2332 0.0752  0.0652  0.1647  519 GLU A CG    
4287 C  CD    . GLU A 519 ? 1.0059 1.1930 1.4652 0.0728  0.0660  0.1671  519 GLU A CD    
4288 O  OE1   . GLU A 519 ? 0.9523 1.1349 1.4045 0.0804  0.0795  0.1608  519 GLU A OE1   
4289 O  OE2   . GLU A 519 ? 0.9355 1.1364 1.4044 0.0632  0.0529  0.1753  519 GLU A OE2   
4290 N  N     . TYR A 520 ? 0.5194 0.6816 0.9292 0.0454  0.0277  0.1488  520 TYR A N     
4291 C  CA    . TYR A 520 ? 0.4652 0.6405 0.8806 0.0344  0.0113  0.1570  520 TYR A CA    
4292 C  C     . TYR A 520 ? 0.5430 0.7168 0.9577 0.0308  0.0024  0.1615  520 TYR A C     
4293 O  O     . TYR A 520 ? 0.5656 0.7536 0.9975 0.0269  -0.0075 0.1754  520 TYR A O     
4294 C  CB    . TYR A 520 ? 0.4402 0.6124 0.8341 0.0248  0.0038  0.1457  520 TYR A CB    
4295 C  CG    . TYR A 520 ? 0.5869 0.7667 0.9875 0.0255  0.0079  0.1466  520 TYR A CG    
4296 C  CD1   . TYR A 520 ? 0.5804 0.7782 1.0061 0.0235  0.0032  0.1612  520 TYR A CD1   
4297 C  CD2   . TYR A 520 ? 0.4961 0.6660 0.8789 0.0278  0.0162  0.1339  520 TYR A CD2   
4298 C  CE1   . TYR A 520 ? 0.5392 0.7443 0.9725 0.0239  0.0072  0.1631  520 TYR A CE1   
4299 C  CE2   . TYR A 520 ? 0.5918 0.7690 0.9808 0.0285  0.0202  0.1358  520 TYR A CE2   
4300 C  CZ    . TYR A 520 ? 0.5410 0.7357 0.9556 0.0266  0.0160  0.1505  520 TYR A CZ    
4301 O  OH    . TYR A 520 ? 0.6219 0.8243 1.0441 0.0271  0.0202  0.1535  520 TYR A OH    
4302 N  N     . LEU A 521 ? 0.4641 0.6215 0.8597 0.0317  0.0055  0.1507  521 LEU A N     
4303 C  CA    . LEU A 521 ? 0.5416 0.6975 0.9355 0.0281  -0.0026 0.1554  521 LEU A CA    
4304 C  C     . LEU A 521 ? 0.4971 0.6590 0.9176 0.0361  0.0015  0.1707  521 LEU A C     
4305 O  O     . LEU A 521 ? 0.4558 0.6288 0.8879 0.0320  -0.0088 0.1836  521 LEU A O     
4306 C  CB    . LEU A 521 ? 0.4383 0.5755 0.8076 0.0273  0.0005  0.1409  521 LEU A CB    
4307 C  CG    . LEU A 521 ? 0.4887 0.6232 0.8567 0.0247  -0.0057 0.1462  521 LEU A CG    
4308 C  CD1   . LEU A 521 ? 0.4113 0.5579 0.7747 0.0137  -0.0217 0.1521  521 LEU A CD1   
4309 C  CD2   . LEU A 521 ? 0.5843 0.7002 0.9312 0.0249  -0.0007 0.1324  521 LEU A CD2   
4310 N  N     . THR A 522 ? 0.4181 0.5727 0.8482 0.0478  0.0167  0.1696  522 THR A N     
4311 C  CA    . THR A 522 ? 0.5645 0.7244 1.0219 0.0566  0.0221  0.1844  522 THR A CA    
4312 C  C     . THR A 522 ? 0.4932 0.6761 0.9778 0.0558  0.0161  0.2021  522 THR A C     
4313 O  O     . THR A 522 ? 0.5001 0.6933 1.0064 0.0574  0.0118  0.2179  522 THR A O     
4314 C  CB    . THR A 522 ? 0.5583 0.7047 1.0194 0.0699  0.0406  0.1782  522 THR A CB    
4315 O  OG1   . THR A 522 ? 0.5470 0.6972 1.0072 0.0731  0.0483  0.1734  522 THR A OG1   
4316 C  CG2   . THR A 522 ? 0.5603 0.6838 0.9968 0.0700  0.0450  0.1619  522 THR A CG2   
4317 N  N     . MET A 523 ? 0.5304 0.7222 1.0151 0.0527  0.0153  0.2003  523 MET A N     
4318 C  CA    . MET A 523 ? 0.5544 0.7688 1.0650 0.0501  0.0080  0.2168  523 MET A CA    
4319 C  C     . MET A 523 ? 0.5180 0.7431 1.0282 0.0380  -0.0114 0.2249  523 MET A C     
4320 O  O     . MET A 523 ? 0.6254 0.8666 1.1606 0.0379  -0.0179 0.2426  523 MET A O     
4321 C  CB    . MET A 523 ? 0.4887 0.7081 0.9963 0.0479  0.0105  0.2117  523 MET A CB    
4322 C  CG    . MET A 523 ? 0.6436 0.8861 1.1797 0.0455  0.0047  0.2283  523 MET A CG    
4323 S  SD    . MET A 523 ? 0.7149 0.9724 1.2527 0.0288  -0.0200 0.2366  523 MET A SD    
4324 C  CE    . MET A 523 ? 0.6576 0.9047 1.1635 0.0184  -0.0254 0.2176  523 MET A CE    
4325 N  N     . THR A 524 ? 0.5382 0.7551 1.0200 0.0278  -0.0208 0.2123  524 THR A N     
4326 C  CA    . THR A 524 ? 0.5179 0.7437 0.9950 0.0162  -0.0389 0.2182  524 THR A CA    
4327 C  C     . THR A 524 ? 0.5295 0.7561 1.0147 0.0189  -0.0414 0.2288  524 THR A C     
4328 O  O     . THR A 524 ? 0.5541 0.7959 1.0520 0.0134  -0.0542 0.2430  524 THR A O     
4329 C  CB    . THR A 524 ? 0.5348 0.7492 0.9783 0.0066  -0.0458 0.2013  524 THR A CB    
4330 O  OG1   . THR A 524 ? 0.5905 0.7855 1.0147 0.0118  -0.0350 0.1876  524 THR A OG1   
4331 C  CG2   . THR A 524 ? 0.5773 0.7946 1.0163 0.0018  -0.0473 0.1944  524 THR A CG2   
4332 N  N     . ILE A 525 ? 0.6022 0.8125 1.0808 0.0270  -0.0297 0.2224  525 ILE A N     
4333 C  CA    . ILE A 525 ? 0.5741 0.7838 1.0624 0.0303  -0.0309 0.2332  525 ILE A CA    
4334 C  C     . ILE A 525 ? 0.5555 0.7813 1.0805 0.0377  -0.0288 0.2535  525 ILE A C     
4335 O  O     . ILE A 525 ? 0.4574 0.6962 0.9963 0.0346  -0.0394 0.2694  525 ILE A O     
4336 C  CB    . ILE A 525 ? 0.5538 0.7413 1.0293 0.0376  -0.0179 0.2215  525 ILE A CB    
4337 C  CG1   . ILE A 525 ? 0.5207 0.6961 0.9631 0.0287  -0.0239 0.2067  525 ILE A CG1   
4338 C  CG2   . ILE A 525 ? 0.4386 0.6253 0.9344 0.0453  -0.0141 0.2351  525 ILE A CG2   
4339 C  CD1   . ILE A 525 ? 0.4516 0.6048 0.8776 0.0341  -0.0113 0.1907  525 ILE A CD1   
4340 N  N     . LYS A 526 ? 0.4756 0.7012 1.0170 0.0479  -0.0148 0.2539  526 LYS A N     
4341 C  CA    . LYS A 526 ? 0.5975 0.8389 1.1758 0.0561  -0.0110 0.2734  526 LYS A CA    
4342 C  C     . LYS A 526 ? 0.5941 0.8602 1.1886 0.0467  -0.0276 0.2888  526 LYS A C     
4343 O  O     . LYS A 526 ? 0.5674 0.8485 1.1876 0.0483  -0.0333 0.3080  526 LYS A O     
4344 C  CB    . LYS A 526 ? 0.6544 0.8924 1.2442 0.0678  0.0071  0.2696  526 LYS A CB    
4345 C  CG    . LYS A 526 ? 0.7295 0.9857 1.3590 0.0767  0.0122  0.2900  526 LYS A CG    
4346 C  CD    . LYS A 526 ? 0.8664 1.1126 1.5053 0.0924  0.0344  0.2857  526 LYS A CD    
4347 C  CE    . LYS A 526 ? 0.8817 1.1481 1.5498 0.0975  0.0398  0.2987  526 LYS A CE    
4348 N  NZ    . LYS A 526 ? 0.9308 1.2038 1.5860 0.0882  0.0340  0.2913  526 LYS A NZ    
4349 N  N     . GLU A 527 ? 0.5871 0.8575 1.1672 0.0364  -0.0363 0.2809  527 GLU A N     
4350 C  CA    . GLU A 527 ? 0.5886 0.8814 1.1837 0.0266  -0.0527 0.2943  527 GLU A CA    
4351 C  C     . GLU A 527 ? 0.6136 0.9120 1.1995 0.0163  -0.0707 0.3005  527 GLU A C     
4352 O  O     . GLU A 527 ? 0.6577 0.9759 1.2660 0.0129  -0.0821 0.3189  527 GLU A O     
4353 C  CB    . GLU A 527 ? 0.6222 0.9158 1.2042 0.0184  -0.0567 0.2833  527 GLU A CB    
4354 C  CG    . GLU A 527 ? 0.6333 0.9270 1.2288 0.0277  -0.0408 0.2815  527 GLU A CG    
4355 C  CD    . GLU A 527 ? 0.7436 1.0613 1.3763 0.0287  -0.0434 0.3010  527 GLU A CD    
4356 O  OE1   . GLU A 527 ? 0.7394 1.0734 1.3819 0.0181  -0.0611 0.3122  527 GLU A OE1   
4357 O  OE2   . GLU A 527 ? 0.8341 1.1547 1.4860 0.0400  -0.0277 0.3053  527 GLU A OE2   
4358 N  N     . ILE A 528 ? 0.5821 0.8644 1.1352 0.0113  -0.0734 0.2860  528 ILE A N     
4359 C  CA    . ILE A 528 ? 0.5268 0.8144 1.0685 0.0019  -0.0896 0.2916  528 ILE A CA    
4360 C  C     . ILE A 528 ? 0.5652 0.8585 1.1281 0.0090  -0.0881 0.3090  528 ILE A C     
4361 O  O     . ILE A 528 ? 0.5710 0.8774 1.1376 0.0024  -0.1027 0.3221  528 ILE A O     
4362 C  CB    . ILE A 528 ? 0.5512 0.8206 1.0536 -0.0044 -0.0913 0.2723  528 ILE A CB    
4363 C  CG1   . ILE A 528 ? 0.5169 0.7944 1.0041 -0.0163 -0.1098 0.2768  528 ILE A CG1   
4364 C  CG2   . ILE A 528 ? 0.5578 0.8084 1.0526 0.0051  -0.0769 0.2655  528 ILE A CG2   
4365 C  CD1   . ILE A 528 ? 0.6008 0.8637 1.0497 -0.0240 -0.1130 0.2580  528 ILE A CD1   
4366 N  N     . GLU A 529 ? 0.5816 0.8649 1.1586 0.0227  -0.0706 0.3098  529 GLU A N     
4367 C  CA    . GLU A 529 ? 0.6629 0.9502 1.2619 0.0302  -0.0684 0.3267  529 GLU A CA    
4368 C  C     . GLU A 529 ? 0.6254 0.9353 1.2647 0.0350  -0.0700 0.3487  529 GLU A C     
4369 O  O     . GLU A 529 ? 0.6107 0.9365 1.2662 0.0322  -0.0816 0.3674  529 GLU A O     
4370 C  CB    . GLU A 529 ? 0.6618 0.9268 1.2582 0.0426  -0.0495 0.3177  529 GLU A CB    
4371 C  CG    . GLU A 529 ? 0.6548 0.8998 1.2167 0.0378  -0.0497 0.3013  529 GLU A CG    
4372 C  CD    . GLU A 529 ? 0.6728 0.8974 1.2365 0.0489  -0.0340 0.2965  529 GLU A CD    
4373 O  OE1   . GLU A 529 ? 0.7620 0.9795 1.3397 0.0601  -0.0186 0.2935  529 GLU A OE1   
4374 O  OE2   . GLU A 529 ? 0.6242 0.8397 1.1753 0.0464  -0.0369 0.2958  529 GLU A OE2   
4375 N  N     . GLU A 530 ? 0.6188 0.9313 1.2749 0.0422  -0.0587 0.3477  530 GLU A N     
4376 C  CA    . GLU A 530 ? 0.6658 0.9992 1.3635 0.0490  -0.0570 0.3692  530 GLU A CA    
4377 C  C     . GLU A 530 ? 0.7031 1.0620 1.4124 0.0365  -0.0772 0.3828  530 GLU A C     
4378 O  O     . GLU A 530 ? 0.6910 1.0702 1.4323 0.0384  -0.0834 0.4050  530 GLU A O     
4379 C  CB    . GLU A 530 ? 0.6560 0.9853 1.3671 0.0604  -0.0380 0.3640  530 GLU A CB    
4380 C  CG    . GLU A 530 ? 0.7469 1.0518 1.4500 0.0739  -0.0173 0.3518  530 GLU A CG    
4381 C  CD    . GLU A 530 ? 0.9259 1.2284 1.6419 0.0855  0.0014  0.3477  530 GLU A CD    
4382 O  OE1   . GLU A 530 ? 0.7298 1.0502 1.4615 0.0830  -0.0015 0.3549  530 GLU A OE1   
4383 O  OE2   . GLU A 530 ? 1.0499 1.3324 1.7598 0.0971  0.0190  0.3373  530 GLU A OE2   
4384 N  N     . LYS A 531 ? 0.6865 1.0447 1.3714 0.0237  -0.0880 0.3700  531 LYS A N     
4385 C  CA    . LYS A 531 ? 0.6662 1.0467 1.3624 0.0117  -0.1063 0.3805  531 LYS A CA    
4386 C  C     . LYS A 531 ? 0.6331 1.0171 1.3052 -0.0034 -0.1278 0.3793  531 LYS A C     
4387 O  O     . LYS A 531 ? 0.7448 1.1480 1.4267 -0.0142 -0.1452 0.3896  531 LYS A O     
4388 C  CB    . LYS A 531 ? 0.6843 1.0638 1.3761 0.0082  -0.1031 0.3690  531 LYS A CB    
4389 C  CG    . LYS A 531 ? 0.6879 1.0612 1.3958 0.0231  -0.0804 0.3666  531 LYS A CG    
4390 C  CD    . LYS A 531 ? 0.6636 1.0475 1.3838 0.0200  -0.0799 0.3668  531 LYS A CD    
4391 C  CE    . LYS A 531 ? 0.7436 1.1222 1.4785 0.0354  -0.0564 0.3651  531 LYS A CE    
4392 N  NZ    . LYS A 531 ? 0.7963 1.1745 1.5254 0.0320  -0.0527 0.3555  531 LYS A NZ    
4393 N  N     . TYR A 532 ? 0.6487 1.0151 1.2896 -0.0048 -0.1272 0.3671  532 TYR A N     
4394 C  CA    . TYR A 532 ? 0.6043 0.9740 1.2212 -0.0180 -0.1462 0.3666  532 TYR A CA    
4395 C  C     . TYR A 532 ? 0.5739 0.9394 1.1857 -0.0143 -0.1460 0.3739  532 TYR A C     
4396 O  O     . TYR A 532 ? 0.6696 1.0365 1.2584 -0.0243 -0.1601 0.3730  532 TYR A O     
4397 C  CB    . TYR A 532 ? 0.6018 0.9554 1.1788 -0.0273 -0.1491 0.3425  532 TYR A CB    
4398 C  CG    . TYR A 532 ? 0.5338 0.8962 1.1121 -0.0370 -0.1589 0.3387  532 TYR A CG    
4399 C  CD1   . TYR A 532 ? 0.5777 0.9392 1.1717 -0.0313 -0.1472 0.3350  532 TYR A CD1   
4400 C  CD2   . TYR A 532 ? 0.5907 0.9626 1.1551 -0.0519 -0.1798 0.3392  532 TYR A CD2   
4401 C  CE1   . TYR A 532 ? 0.6013 0.9708 1.1986 -0.0405 -0.1561 0.3326  532 TYR A CE1   
4402 C  CE2   . TYR A 532 ? 0.6798 1.0585 1.2466 -0.0613 -0.1892 0.3356  532 TYR A CE2   
4403 C  CZ    . TYR A 532 ? 0.6386 1.0163 1.2230 -0.0556 -0.1773 0.3327  532 TYR A CZ    
4404 O  OH    . TYR A 532 ? 0.6125 0.9968 1.2011 -0.0652 -0.1865 0.3300  532 TYR A OH    
4405 N  N     . GLY A 533 ? 0.5971 0.9570 1.2296 -0.0002 -0.1305 0.3813  533 GLY A N     
4406 C  CA    . GLY A 533 ? 0.6219 0.9791 1.2551 0.0036  -0.1304 0.3912  533 GLY A CA    
4407 C  C     . GLY A 533 ? 0.7146 1.0504 1.3104 0.0009  -0.1277 0.3742  533 GLY A C     
4408 O  O     . GLY A 533 ? 0.6983 1.0347 1.2890 -0.0003 -0.1329 0.3828  533 GLY A O     
4409 N  N     . PHE A 534 ? 0.6727 0.9907 1.2433 -0.0003 -0.1198 0.3513  534 PHE A N     
4410 C  CA    . PHE A 534 ? 0.6551 0.9531 1.1923 -0.0024 -0.1160 0.3353  534 PHE A CA    
4411 C  C     . PHE A 534 ? 0.7073 0.9880 1.2530 0.0106  -0.0980 0.3336  534 PHE A C     
4412 O  O     . PHE A 534 ? 0.6414 0.9215 1.2140 0.0218  -0.0858 0.3394  534 PHE A O     
4413 C  CB    . PHE A 534 ? 0.6600 0.9460 1.1681 -0.0085 -0.1147 0.3120  534 PHE A CB    
4414 C  CG    . PHE A 534 ? 0.7017 0.9961 1.1867 -0.0231 -0.1327 0.3080  534 PHE A CG    
4415 C  CD1   . PHE A 534 ? 0.7044 1.0163 1.2016 -0.0300 -0.1449 0.3150  534 PHE A CD1   
4416 C  CD2   . PHE A 534 ? 0.6510 0.9355 1.1024 -0.0298 -0.1372 0.2970  534 PHE A CD2   
4417 C  CE1   . PHE A 534 ? 0.6697 0.9876 1.1447 -0.0436 -0.1616 0.3100  534 PHE A CE1   
4418 C  CE2   . PHE A 534 ? 0.6472 0.9381 1.0758 -0.0426 -0.1530 0.2922  534 PHE A CE2   
4419 C  CZ    . PHE A 534 ? 0.6905 0.9974 1.1303 -0.0496 -0.1654 0.2981  534 PHE A CZ    
4420 N  N     . LYS A 535 ? 0.7386 1.0046 1.2609 0.0089  -0.0963 0.3254  535 LYS A N     
4421 C  CA    . LYS A 535 ? 0.6690 0.9144 1.1929 0.0191  -0.0799 0.3193  535 LYS A CA    
4422 C  C     . LYS A 535 ? 0.6968 0.9230 1.1861 0.0148  -0.0754 0.2959  535 LYS A C     
4423 O  O     . LYS A 535 ? 0.6826 0.9089 1.1466 0.0054  -0.0850 0.2915  535 LYS A O     
4424 C  CB    . LYS A 535 ? 0.6343 0.8809 1.1693 0.0221  -0.0816 0.3357  535 LYS A CB    
4425 C  CG    . LYS A 535 ? 0.7309 0.9636 1.2889 0.0361  -0.0648 0.3392  535 LYS A CG    
4426 C  CD    . LYS A 535 ? 0.6848 0.8921 1.2216 0.0378  -0.0545 0.3226  535 LYS A CD    
4427 C  CE    . LYS A 535 ? 0.6810 0.8724 1.2399 0.0514  -0.0380 0.3246  535 LYS A CE    
4428 N  NZ    . LYS A 535 ? 0.5993 0.7872 1.1717 0.0603  -0.0259 0.3174  535 LYS A NZ    
4429 N  N     . VAL A 536 ? 0.6677 0.8781 1.1555 0.0219  -0.0609 0.2813  536 VAL A N     
4430 C  CA    . VAL A 536 ? 0.6640 0.8566 1.1214 0.0185  -0.0561 0.2594  536 VAL A CA    
4431 C  C     . VAL A 536 ? 0.6460 0.8226 1.0962 0.0212  -0.0500 0.2574  536 VAL A C     
4432 O  O     . VAL A 536 ? 0.6654 0.8311 1.1325 0.0312  -0.0383 0.2600  536 VAL A O     
4433 C  CB    . VAL A 536 ? 0.6532 0.8360 1.1114 0.0247  -0.0435 0.2454  536 VAL A CB    
4434 C  CG1   . VAL A 536 ? 0.6014 0.7662 1.0293 0.0214  -0.0388 0.2239  536 VAL A CG1   
4435 C  CG2   . VAL A 536 ? 0.6265 0.8259 1.0930 0.0213  -0.0498 0.2485  536 VAL A CG2   
4436 N  N     . ILE A 537 ? 0.6371 0.8119 1.0627 0.0124  -0.0579 0.2529  537 ILE A N     
4437 C  CA    . ILE A 537 ? 0.6570 0.8174 1.0751 0.0137  -0.0528 0.2512  537 ILE A CA    
4438 C  C     . ILE A 537 ? 0.7363 0.8752 1.1406 0.0168  -0.0406 0.2308  537 ILE A C     
4439 O  O     . ILE A 537 ? 0.7415 0.8651 1.1550 0.0240  -0.0299 0.2293  537 ILE A O     
4440 C  CB    . ILE A 537 ? 0.6389 0.8063 1.0354 0.0033  -0.0649 0.2543  537 ILE A CB    
4441 C  CG1   . ILE A 537 ? 0.6690 0.8580 1.0785 0.0001  -0.0778 0.2754  537 ILE A CG1   
4442 C  CG2   . ILE A 537 ? 0.7006 0.8534 1.0895 0.0042  -0.0592 0.2525  537 ILE A CG2   
4443 C  CD1   . ILE A 537 ? 0.7065 0.9104 1.1005 -0.0097 -0.0913 0.2729  537 ILE A CD1   
4444 N  N     . TYR A 538 ? 0.6818 0.8189 1.0640 0.0112  -0.0423 0.2149  538 TYR A N     
4445 C  CA    . TYR A 538 ? 0.6514 0.7703 1.0180 0.0127  -0.0326 0.1955  538 TYR A CA    
4446 C  C     . TYR A 538 ? 0.5920 0.7142 0.9494 0.0107  -0.0328 0.1839  538 TYR A C     
4447 O  O     . TYR A 538 ? 0.5611 0.6983 0.9164 0.0050  -0.0427 0.1881  538 TYR A O     
4448 C  CB    . TYR A 538 ? 0.6261 0.7374 0.9696 0.0058  -0.0353 0.1885  538 TYR A CB    
4449 C  CG    . TYR A 538 ? 0.6476 0.7418 0.9740 0.0059  -0.0272 0.1690  538 TYR A CG    
4450 C  CD1   . TYR A 538 ? 0.6857 0.7642 1.0210 0.0139  -0.0152 0.1621  538 TYR A CD1   
4451 C  CD2   . TYR A 538 ? 0.6425 0.7364 0.9437 -0.0020 -0.0317 0.1576  538 TYR A CD2   
4452 C  CE1   . TYR A 538 ? 0.7163 0.7799 1.0354 0.0133  -0.0090 0.1446  538 TYR A CE1   
4453 C  CE2   . TYR A 538 ? 0.6540 0.7339 0.9410 -0.0021 -0.0249 0.1410  538 TYR A CE2   
4454 C  CZ    . TYR A 538 ? 0.7042 0.7693 1.0000 0.0052  -0.0142 0.1347  538 TYR A CZ    
4455 O  OH    . TYR A 538 ? 0.7035 0.7554 0.9847 0.0044  -0.0086 0.1185  538 TYR A OH    
4456 N  N     . SER A 539 ? 0.6156 0.7238 0.9678 0.0154  -0.0220 0.1693  539 SER A N     
4457 C  CA    . SER A 539 ? 0.6514 0.7619 0.9961 0.0145  -0.0208 0.1588  539 SER A CA    
4458 C  C     . SER A 539 ? 0.6474 0.7404 0.9756 0.0162  -0.0116 0.1406  539 SER A C     
4459 O  O     . SER A 539 ? 0.7172 0.7974 1.0529 0.0240  -0.0009 0.1372  539 SER A O     
4460 C  CB    . SER A 539 ? 0.6264 0.7455 0.9951 0.0218  -0.0164 0.1674  539 SER A CB    
4461 O  OG    . SER A 539 ? 0.5945 0.7146 0.9567 0.0216  -0.0136 0.1573  539 SER A OG    
4462 N  N     . ASP A 540 ? 0.6645 0.7568 0.9707 0.0091  -0.0158 0.1289  540 ASP A N     
4463 C  CA    . ASP A 540 ? 0.7278 0.8058 1.0188 0.0104  -0.0081 0.1122  540 ASP A CA    
4464 C  C     . ASP A 540 ? 0.5814 0.6626 0.8743 0.0135  -0.0039 0.1067  540 ASP A C     
4465 O  O     . ASP A 540 ? 0.9719 1.0589 1.2838 0.0197  0.0000  0.1148  540 ASP A O     
4466 C  CB    . ASP A 540 ? 0.7110 0.7860 0.9786 0.0020  -0.0136 0.1029  540 ASP A CB    
4467 C  CG    . ASP A 540 ? 0.8063 0.8646 1.0633 0.0033  -0.0063 0.0910  540 ASP A CG    
4468 O  OD1   . ASP A 540 ? 0.6068 0.6565 0.8635 0.0084  0.0018  0.0820  540 ASP A OD1   
4469 O  OD2   . ASP A 540 ? 0.7550 0.8092 1.0041 -0.0008 -0.0089 0.0910  540 ASP A OD2   
4470 N  N     . THR A 541 ? 0.5775 0.6559 0.8523 0.0094  -0.0045 0.0940  541 THR A N     
4471 C  CA    . THR A 541 ? 0.6409 0.7195 0.9165 0.0133  0.0016  0.0879  541 THR A CA    
4472 C  C     . THR A 541 ? 0.6851 0.7789 0.9656 0.0094  -0.0054 0.0933  541 THR A C     
4473 O  O     . THR A 541 ? 0.5777 0.6759 0.8680 0.0140  -0.0003 0.0946  541 THR A O     
4474 C  CB    . THR A 541 ? 0.7334 0.8005 0.9885 0.0119  0.0057  0.0718  541 THR A CB    
4475 O  OG1   . THR A 541 ? 0.8403 0.9035 1.0980 0.0188  0.0153  0.0665  541 THR A OG1   
4476 C  CG2   . THR A 541 ? 0.6623 0.7351 0.9022 0.0036  -0.0024 0.0665  541 THR A CG2   
4477 N  N     . ASP A 542 ? 0.6327 0.7345 0.9067 0.0010  -0.0169 0.0966  542 ASP A N     
4478 C  CA    . ASP A 542 ? 0.5394 0.6535 0.8158 -0.0041 -0.0247 0.0997  542 ASP A CA    
4479 C  C     . ASP A 542 ? 0.5417 0.6685 0.8264 -0.0094 -0.0363 0.1124  542 ASP A C     
4480 O  O     . ASP A 542 ? 0.4957 0.6319 0.7801 -0.0156 -0.0451 0.1143  542 ASP A O     
4481 C  CB    . ASP A 542 ? 0.6471 0.7569 0.9019 -0.0104 -0.0279 0.0868  542 ASP A CB    
4482 C  CG    . ASP A 542 ? 0.6211 0.7264 0.8580 -0.0164 -0.0337 0.0824  542 ASP A CG    
4483 O  OD1   . ASP A 542 ? 0.6114 0.7129 0.8501 -0.0146 -0.0321 0.0863  542 ASP A OD1   
4484 O  OD2   . ASP A 542 ? 0.6909 0.7966 0.9128 -0.0228 -0.0394 0.0755  542 ASP A OD2   
4485 N  N     . GLY A 543 ? 0.4732 0.6003 0.7652 -0.0076 -0.0371 0.1213  543 GLY A N     
4486 C  CA    . GLY A 543 ? 0.5190 0.6589 0.8176 -0.0128 -0.0487 0.1342  543 GLY A CA    
4487 C  C     . GLY A 543 ? 0.5701 0.7097 0.8818 -0.0080 -0.0465 0.1455  543 GLY A C     
4488 O  O     . GLY A 543 ? 0.6180 0.7463 0.9339 -0.0008 -0.0358 0.1427  543 GLY A O     
4489 N  N     . PHE A 544 ? 0.5184 0.6705 0.8364 -0.0125 -0.0572 0.1586  544 PHE A N     
4490 C  CA    . PHE A 544 ? 0.4968 0.6507 0.8291 -0.0084 -0.0565 0.1721  544 PHE A CA    
4491 C  C     . PHE A 544 ? 0.5109 0.6765 0.8371 -0.0165 -0.0703 0.1821  544 PHE A C     
4492 O  O     . PHE A 544 ? 0.5254 0.7004 0.8425 -0.0244 -0.0811 0.1813  544 PHE A O     
4493 C  CB    . PHE A 544 ? 0.5362 0.6968 0.8989 0.0002  -0.0510 0.1845  544 PHE A CB    
4494 C  CG    . PHE A 544 ? 0.5303 0.7089 0.9070 -0.0033 -0.0599 0.1939  544 PHE A CG    
4495 C  CD1   . PHE A 544 ? 0.4497 0.6442 0.8374 -0.0077 -0.0720 0.2101  544 PHE A CD1   
4496 C  CD2   . PHE A 544 ? 0.5540 0.7342 0.9335 -0.0025 -0.0564 0.1874  544 PHE A CD2   
4497 C  CE1   . PHE A 544 ? 0.5715 0.7828 0.9729 -0.0117 -0.0811 0.2190  544 PHE A CE1   
4498 C  CE2   . PHE A 544 ? 0.5219 0.7186 0.9159 -0.0063 -0.0649 0.1966  544 PHE A CE2   
4499 C  CZ    . PHE A 544 ? 0.5406 0.7528 0.9459 -0.0112 -0.0775 0.2122  544 PHE A CZ    
4500 N  N     . PHE A 545 ? 0.5297 0.6938 0.8606 -0.0143 -0.0697 0.1915  545 PHE A N     
4501 C  CA    . PHE A 545 ? 0.5374 0.7139 0.8666 -0.0202 -0.0818 0.2049  545 PHE A CA    
4502 C  C     . PHE A 545 ? 0.5953 0.7848 0.9549 -0.0154 -0.0842 0.2246  545 PHE A C     
4503 O  O     . PHE A 545 ? 0.5696 0.7531 0.9496 -0.0059 -0.0735 0.2292  545 PHE A O     
4504 C  CB    . PHE A 545 ? 0.5437 0.7116 0.8599 -0.0209 -0.0797 0.2048  545 PHE A CB    
4505 C  CG    . PHE A 545 ? 0.6359 0.7929 0.9236 -0.0257 -0.0776 0.1872  545 PHE A CG    
4506 C  CD1   . PHE A 545 ? 0.6353 0.7759 0.9189 -0.0211 -0.0657 0.1736  545 PHE A CD1   
4507 C  CD2   . PHE A 545 ? 0.6601 0.8231 0.9248 -0.0346 -0.0875 0.1845  545 PHE A CD2   
4508 C  CE1   . PHE A 545 ? 0.6430 0.7749 0.9024 -0.0253 -0.0641 0.1586  545 PHE A CE1   
4509 C  CE2   . PHE A 545 ? 0.6937 0.8472 0.9337 -0.0382 -0.0847 0.1691  545 PHE A CE2   
4510 C  CZ    . PHE A 545 ? 0.6516 0.7900 0.8901 -0.0335 -0.0731 0.1567  545 PHE A CZ    
4511 N  N     . ALA A 546 ? 0.6302 0.8374 0.9932 -0.0220 -0.0981 0.2360  546 ALA A N     
4512 C  CA    . ALA A 546 ? 0.6347 0.8572 1.0278 -0.0183 -0.1021 0.2561  546 ALA A CA    
4513 C  C     . ALA A 546 ? 0.6572 0.8955 1.0453 -0.0265 -0.1181 0.2700  546 ALA A C     
4514 O  O     . ALA A 546 ? 0.7228 0.9611 1.0832 -0.0354 -0.1265 0.2625  546 ALA A O     
4515 C  CB    . ALA A 546 ? 0.6042 0.8354 1.0151 -0.0169 -0.1022 0.2569  546 ALA A CB    
4516 N  N     . THR A 547 ? 0.6713 0.9236 1.0866 -0.0230 -0.1221 0.2906  547 THR A N     
4517 C  CA    . THR A 547 ? 0.7016 0.9713 1.1154 -0.0303 -0.1381 0.3065  547 THR A CA    
4518 C  C     . THR A 547 ? 0.7292 1.0167 1.1797 -0.0259 -0.1421 0.3283  547 THR A C     
4519 O  O     . THR A 547 ? 0.7000 0.9839 1.1770 -0.0154 -0.1300 0.3320  547 THR A O     
4520 C  CB    . THR A 547 ? 0.7731 1.0374 1.1736 -0.0305 -0.1374 0.3111  547 THR A CB    
4521 O  OG1   . THR A 547 ? 0.7100 0.9912 1.1008 -0.0394 -0.1541 0.3234  547 THR A OG1   
4522 C  CG2   . THR A 547 ? 0.7995 1.0592 1.2281 -0.0192 -0.1264 0.3243  547 THR A CG2   
4523 N  N     . ILE A 548 ? 0.7672 1.0742 1.2185 -0.0340 -0.1591 0.3424  548 ILE A N     
4524 C  CA    . ILE A 548 ? 0.6991 1.0258 1.1852 -0.0308 -0.1653 0.3665  548 ILE A CA    
4525 C  C     . ILE A 548 ? 0.7275 1.0555 1.2205 -0.0265 -0.1644 0.3826  548 ILE A C     
4526 O  O     . ILE A 548 ? 0.6673 0.9999 1.1377 -0.0344 -0.1751 0.3857  548 ILE A O     
4527 C  CB    . ILE A 548 ? 0.7130 1.0614 1.1980 -0.0425 -0.1857 0.3746  548 ILE A CB    
4528 C  CG1   . ILE A 548 ? 0.7055 1.0532 1.1882 -0.0467 -0.1868 0.3606  548 ILE A CG1   
4529 C  CG2   . ILE A 548 ? 0.7500 1.1200 1.2725 -0.0390 -0.1924 0.4011  548 ILE A CG2   
4530 C  CD1   . ILE A 548 ? 0.7352 1.0702 1.2348 -0.0356 -0.1680 0.3520  548 ILE A CD1   
4531 N  N     . PRO A 549 ? 0.7917 1.1153 1.3145 -0.0141 -0.1517 0.3930  549 PRO A N     
4532 C  CA    . PRO A 549 ? 0.7471 1.0708 1.2786 -0.0097 -0.1505 0.4091  549 PRO A CA    
4533 C  C     . PRO A 549 ? 0.7771 1.1252 1.3129 -0.0172 -0.1694 0.4309  549 PRO A C     
4534 O  O     . PRO A 549 ? 0.7144 1.0811 1.2804 -0.0151 -0.1757 0.4492  549 PRO A O     
4535 C  CB    . PRO A 549 ? 0.8543 1.1722 1.4234 0.0050  -0.1350 0.4177  549 PRO A CB    
4536 C  CG    . PRO A 549 ? 0.9269 1.2322 1.4939 0.0088  -0.1233 0.3978  549 PRO A CG    
4537 C  CD    . PRO A 549 ? 0.9975 1.3146 1.5467 -0.0031 -0.1370 0.3899  549 PRO A CD    
4538 N  N     . GLY A 550 ? 0.8205 1.1695 1.3257 -0.0260 -0.1785 0.4294  550 GLY A N     
4539 C  CA    . GLY A 550 ? 0.7631 1.1347 1.2664 -0.0340 -0.1972 0.4489  550 GLY A CA    
4540 C  C     . GLY A 550 ? 0.7641 1.1519 1.2569 -0.0455 -0.2143 0.4459  550 GLY A C     
4541 O  O     . GLY A 550 ? 1.0095 1.4161 1.5301 -0.0456 -0.2228 0.4614  550 GLY A O     
4542 N  N     . ALA A 551 ? 0.8605 1.2412 1.3143 -0.0553 -0.2195 0.4263  551 ALA A N     
4543 C  CA    . ALA A 551 ? 0.7711 1.1643 1.2117 -0.0672 -0.2362 0.4212  551 ALA A CA    
4544 C  C     . ALA A 551 ? 0.7652 1.1506 1.1586 -0.0775 -0.2425 0.4040  551 ALA A C     
4545 O  O     . ALA A 551 ? 0.9002 1.2678 1.2728 -0.0745 -0.2308 0.3913  551 ALA A O     
4546 C  CB    . ALA A 551 ? 0.7511 1.1397 1.2064 -0.0651 -0.2304 0.4090  551 ALA A CB    
4547 N  N     . ASP A 552 ? 0.7959 1.1949 1.1733 -0.0897 -0.2611 0.4037  552 ASP A N     
4548 C  CA    . ASP A 552 ? 0.8875 1.2793 1.2196 -0.0998 -0.2678 0.3859  552 ASP A CA    
4549 C  C     . ASP A 552 ? 0.8695 1.2395 1.1867 -0.0983 -0.2552 0.3591  552 ASP A C     
4550 O  O     . ASP A 552 ? 0.8243 1.1895 1.1645 -0.0931 -0.2471 0.3543  552 ASP A O     
4551 C  CB    . ASP A 552 ? 0.9226 1.3326 1.2438 -0.1132 -0.2909 0.3902  552 ASP A CB    
4552 C  CG    . ASP A 552 ? 1.0546 1.4570 1.3272 -0.1238 -0.2985 0.3713  552 ASP A CG    
4553 O  OD1   . ASP A 552 ? 1.0689 1.4529 1.3224 -0.1241 -0.2897 0.3480  552 ASP A OD1   
4554 O  OD2   . ASP A 552 ? 1.2294 1.6450 1.4829 -0.1317 -0.3135 0.3806  552 ASP A OD2   
4555 N  N     . ALA A 553 ? 0.9166 1.2742 1.1950 -0.1027 -0.2533 0.3423  553 ALA A N     
4556 C  CA    . ALA A 553 ? 0.9039 1.2418 1.1652 -0.1023 -0.2430 0.3170  553 ALA A CA    
4557 C  C     . ALA A 553 ? 0.9742 1.3153 1.2380 -0.1094 -0.2524 0.3078  553 ALA A C     
4558 O  O     . ALA A 553 ? 0.8992 1.2291 1.1728 -0.1054 -0.2425 0.2955  553 ALA A O     
4559 C  CB    . ALA A 553 ? 0.8957 1.2230 1.1149 -0.1066 -0.2415 0.3028  553 ALA A CB    
4560 N  N     . GLU A 554 ? 0.9819 1.3382 1.2368 -0.1202 -0.2719 0.3141  554 GLU A N     
4561 C  CA    . GLU A 554 ? 1.1043 1.4639 1.3621 -0.1283 -0.2826 0.3062  554 GLU A CA    
4562 C  C     . GLU A 554 ? 0.9866 1.3540 1.2886 -0.1225 -0.2790 0.3173  554 GLU A C     
4563 O  O     . GLU A 554 ? 0.9074 1.2694 1.2170 -0.1239 -0.2771 0.3063  554 GLU A O     
4564 C  CB    . GLU A 554 ? 1.0625 1.4377 1.3033 -0.1415 -0.3056 0.3124  554 GLU A CB    
4565 C  CG    . GLU A 554 ? 1.2754 1.6418 1.4870 -0.1526 -0.3148 0.2913  554 GLU A CG    
4566 C  CD    . GLU A 554 ? 1.4230 1.7660 1.6040 -0.1497 -0.3005 0.2674  554 GLU A CD    
4567 O  OE1   . GLU A 554 ? 1.4060 1.7433 1.5674 -0.1455 -0.2924 0.2666  554 GLU A OE1   
4568 O  OE2   . GLU A 554 ? 1.2291 1.5598 1.4069 -0.1516 -0.2973 0.2502  554 GLU A OE2   
4569 N  N     . THR A 555 ? 0.8575 1.2379 1.1899 -0.1154 -0.2772 0.3395  555 THR A N     
4570 C  CA    . THR A 555 ? 0.7778 1.1661 1.1535 -0.1082 -0.2718 0.3511  555 THR A CA    
4571 C  C     . THR A 555 ? 0.7801 1.1489 1.1628 -0.0977 -0.2504 0.3367  555 THR A C     
4572 O  O     . THR A 555 ? 0.7849 1.1536 1.1866 -0.0962 -0.2467 0.3328  555 THR A O     
4573 C  CB    . THR A 555 ? 0.7825 1.1870 1.1881 -0.1016 -0.2728 0.3777  555 THR A CB    
4574 O  OG1   . THR A 555 ? 0.8193 1.2395 1.2101 -0.1111 -0.2915 0.3897  555 THR A OG1   
4575 C  CG2   . THR A 555 ? 0.7364 1.1554 1.1869 -0.0972 -0.2729 0.3926  555 THR A CG2   
4576 N  N     . VAL A 556 ? 0.7765 1.1293 1.1442 -0.0907 -0.2362 0.3291  556 VAL A N     
4577 C  CA    . VAL A 556 ? 0.7602 1.0937 1.1308 -0.0814 -0.2166 0.3143  556 VAL A CA    
4578 C  C     . VAL A 556 ? 0.7612 1.0841 1.1120 -0.0876 -0.2172 0.2926  556 VAL A C     
4579 O  O     . VAL A 556 ? 0.7476 1.0646 1.1135 -0.0828 -0.2078 0.2859  556 VAL A O     
4580 C  CB    . VAL A 556 ? 0.7803 1.0989 1.1349 -0.0750 -0.2041 0.3095  556 VAL A CB    
4581 C  CG1   . VAL A 556 ? 0.6704 0.9678 1.0199 -0.0680 -0.1862 0.2906  556 VAL A CG1   
4582 C  CG2   . VAL A 556 ? 0.7499 1.0764 1.1305 -0.0669 -0.2005 0.3311  556 VAL A CG2   
4583 N  N     . LYS A 557 ? 0.7520 1.0724 1.0688 -0.0980 -0.2281 0.2818  557 LYS A N     
4584 C  CA    . LYS A 557 ? 0.7991 1.1082 1.0962 -0.1040 -0.2288 0.2609  557 LYS A CA    
4585 C  C     . LYS A 557 ? 0.7887 1.1083 1.1083 -0.1087 -0.2375 0.2646  557 LYS A C     
4586 O  O     . LYS A 557 ? 0.7730 1.0835 1.0975 -0.1070 -0.2300 0.2530  557 LYS A O     
4587 C  CB    . LYS A 557 ? 0.8572 1.1626 1.1143 -0.1141 -0.2395 0.2501  557 LYS A CB    
4588 C  CG    . LYS A 557 ? 0.8231 1.1156 1.0551 -0.1098 -0.2288 0.2426  557 LYS A CG    
4589 C  CD    . LYS A 557 ? 0.8963 1.1907 1.0921 -0.1192 -0.2407 0.2380  557 LYS A CD    
4590 C  CE    . LYS A 557 ? 0.9570 1.2517 1.1415 -0.1151 -0.2355 0.2461  557 LYS A CE    
4591 N  NZ    . LYS A 557 ? 0.9742 1.2662 1.1182 -0.1225 -0.2420 0.2369  557 LYS A NZ    
4592 N  N     . LYS A 558 ? 0.7049 1.0444 1.0391 -0.1150 -0.2537 0.2818  558 LYS A N     
4593 C  CA    . LYS A 558 ? 0.7479 1.0997 1.1053 -0.1207 -0.2639 0.2873  558 LYS A CA    
4594 C  C     . LYS A 558 ? 0.7371 1.0907 1.1321 -0.1097 -0.2495 0.2945  558 LYS A C     
4595 O  O     . LYS A 558 ? 0.7651 1.1164 1.1707 -0.1109 -0.2473 0.2877  558 LYS A O     
4596 C  CB    . LYS A 558 ? 0.8010 1.1752 1.1674 -0.1292 -0.2843 0.3063  558 LYS A CB    
4597 C  CG    . LYS A 558 ? 0.8190 1.2087 1.2091 -0.1376 -0.2986 0.3141  558 LYS A CG    
4598 C  CD    . LYS A 558 ? 0.9378 1.3472 1.3737 -0.1304 -0.2970 0.3387  558 LYS A CD    
4599 C  CE    . LYS A 558 ? 0.8991 1.3239 1.3622 -0.1379 -0.3091 0.3465  558 LYS A CE    
4600 N  NZ    . LYS A 558 ? 0.8497 1.2617 1.3174 -0.1359 -0.2982 0.3316  558 LYS A NZ    
4601 N  N     . LYS A 559 ? 0.7643 1.1218 1.1797 -0.0986 -0.2392 0.3084  559 LYS A N     
4602 C  CA    . LYS A 559 ? 0.7790 1.1374 1.2287 -0.0869 -0.2242 0.3148  559 LYS A CA    
4603 C  C     . LYS A 559 ? 0.6704 1.0072 1.1075 -0.0806 -0.2066 0.2945  559 LYS A C     
4604 O  O     . LYS A 559 ? 0.5885 0.9253 1.0464 -0.0756 -0.1979 0.2937  559 LYS A O     
4605 C  CB    . LYS A 559 ? 0.7777 1.1425 1.2499 -0.0761 -0.2167 0.3330  559 LYS A CB    
4606 C  CG    . LYS A 559 ? 0.8167 1.2062 1.3112 -0.0805 -0.2329 0.3570  559 LYS A CG    
4607 C  CD    . LYS A 559 ? 0.7473 1.1539 1.2710 -0.0848 -0.2413 0.3662  559 LYS A CD    
4608 C  CE    . LYS A 559 ? 0.8944 1.3254 1.4300 -0.0944 -0.2632 0.3860  559 LYS A CE    
4609 N  NZ    . LYS A 559 ? 0.8134 1.2630 1.3835 -0.0977 -0.2707 0.3979  559 LYS A NZ    
4610 N  N     . ALA A 560 ? 0.6931 1.0125 1.0969 -0.0809 -0.2014 0.2786  560 ALA A N     
4611 C  CA    . ALA A 560 ? 0.6901 0.9899 1.0803 -0.0762 -0.1865 0.2591  560 ALA A CA    
4612 C  C     . ALA A 560 ? 0.6850 0.9828 1.0682 -0.0843 -0.1926 0.2472  560 ALA A C     
4613 O  O     . ALA A 560 ? 0.6069 0.8969 0.9976 -0.0793 -0.1812 0.2391  560 ALA A O     
4614 C  CB    . ALA A 560 ? 0.6719 0.9555 1.0290 -0.0757 -0.1812 0.2461  560 ALA A CB    
4615 N  N     . MET A 561 ? 0.6944 0.9987 1.0630 -0.0969 -0.2104 0.2459  561 MET A N     
4616 C  CA    . MET A 561 ? 0.7097 1.0122 1.0743 -0.1055 -0.2176 0.2358  561 MET A CA    
4617 C  C     . MET A 561 ? 0.6533 0.9691 1.0560 -0.1033 -0.2170 0.2480  561 MET A C     
4618 O  O     . MET A 561 ? 0.7140 1.0235 1.1220 -0.1025 -0.2105 0.2395  561 MET A O     
4619 C  CB    . MET A 561 ? 0.6933 1.0010 1.0368 -0.1196 -0.2382 0.2337  561 MET A CB    
4620 C  CG    . MET A 561 ? 0.7643 1.0578 1.0667 -0.1227 -0.2385 0.2186  561 MET A CG    
4621 S  SD    . MET A 561 ? 0.8888 1.1576 1.1706 -0.1162 -0.2199 0.1955  561 MET A SD    
4622 C  CE    . MET A 561 ? 0.8805 1.1397 1.1241 -0.1167 -0.2188 0.1874  561 MET A CE    
4623 N  N     . GLU A 562 ? 0.5462 0.8814 0.9765 -0.1022 -0.2236 0.2691  562 GLU A N     
4624 C  CA    . GLU A 562 ? 0.6588 1.0084 1.1286 -0.0987 -0.2213 0.2831  562 GLU A CA    
4625 C  C     . GLU A 562 ? 0.6352 0.9747 1.1172 -0.0850 -0.1989 0.2785  562 GLU A C     
4626 O  O     . GLU A 562 ? 0.6027 0.9427 1.0988 -0.0842 -0.1939 0.2761  562 GLU A O     
4627 C  CB    . GLU A 562 ? 0.6785 1.0499 1.1770 -0.0971 -0.2290 0.3074  562 GLU A CB    
4628 C  CG    . GLU A 562 ? 0.7533 1.1407 1.2499 -0.1113 -0.2531 0.3164  562 GLU A CG    
4629 C  CD    . GLU A 562 ? 0.9475 1.3601 1.4842 -0.1093 -0.2598 0.3427  562 GLU A CD    
4630 O  OE1   . GLU A 562 ? 0.9364 1.3525 1.5009 -0.0960 -0.2443 0.3533  562 GLU A OE1   
4631 O  OE2   . GLU A 562 ? 1.1996 1.6285 1.7401 -0.1210 -0.2804 0.3528  562 GLU A OE2   
4632 N  N     . PHE A 563 ? 0.5958 0.9264 1.0732 -0.0742 -0.1854 0.2781  563 PHE A N     
4633 C  CA    . PHE A 563 ? 0.5264 0.8465 1.0134 -0.0611 -0.1644 0.2733  563 PHE A CA    
4634 C  C     . PHE A 563 ? 0.5515 0.8548 1.0165 -0.0628 -0.1576 0.2524  563 PHE A C     
4635 O  O     . PHE A 563 ? 0.5563 0.8565 1.0341 -0.0558 -0.1449 0.2499  563 PHE A O     
4636 C  CB    . PHE A 563 ? 0.5200 0.8306 1.0017 -0.0509 -0.1527 0.2740  563 PHE A CB    
4637 C  CG    . PHE A 563 ? 0.5524 0.8477 1.0346 -0.0389 -0.1318 0.2641  563 PHE A CG    
4638 C  CD1   . PHE A 563 ? 0.4936 0.7952 1.0065 -0.0285 -0.1199 0.2737  563 PHE A CD1   
4639 C  CD2   . PHE A 563 ? 0.5013 0.7762 0.9529 -0.0381 -0.1242 0.2450  563 PHE A CD2   
4640 C  CE1   . PHE A 563 ? 0.5263 0.8134 1.0373 -0.0177 -0.1010 0.2638  563 PHE A CE1   
4641 C  CE2   . PHE A 563 ? 0.5470 0.8082 0.9981 -0.0278 -0.1061 0.2356  563 PHE A CE2   
4642 C  CZ    . PHE A 563 ? 0.5851 0.8519 1.0647 -0.0177 -0.0947 0.2446  563 PHE A CZ    
4643 N  N     . LEU A 564 ? 0.5401 0.8326 0.9720 -0.0716 -0.1656 0.2378  564 LEU A N     
4644 C  CA    . LEU A 564 ? 0.6063 0.8831 1.0178 -0.0735 -0.1599 0.2186  564 LEU A CA    
4645 C  C     . LEU A 564 ? 0.5719 0.8564 0.9999 -0.0789 -0.1650 0.2203  564 LEU A C     
4646 O  O     . LEU A 564 ? 0.5264 0.8045 0.9596 -0.0738 -0.1533 0.2140  564 LEU A O     
4647 C  CB    . LEU A 564 ? 0.5461 0.8115 0.9208 -0.0819 -0.1682 0.2042  564 LEU A CB    
4648 C  CG    . LEU A 564 ? 0.6048 0.8567 0.9592 -0.0752 -0.1577 0.1967  564 LEU A CG    
4649 C  CD1   . LEU A 564 ? 0.6269 0.8715 0.9477 -0.0839 -0.1672 0.1858  564 LEU A CD1   
4650 C  CD2   . LEU A 564 ? 0.5214 0.7586 0.8726 -0.0663 -0.1401 0.1848  564 LEU A CD2   
4651 N  N     . LYS A 565 ? 0.5143 0.8126 0.9507 -0.0897 -0.1829 0.2291  565 LYS A N     
4652 C  CA    . LYS A 565 ? 0.6340 0.9407 1.0894 -0.0958 -0.1889 0.2324  565 LYS A CA    
4653 C  C     . LYS A 565 ? 0.5823 0.8990 1.0728 -0.0853 -0.1755 0.2450  565 LYS A C     
4654 O  O     . LYS A 565 ? 0.4625 0.7761 0.9607 -0.0836 -0.1679 0.2406  565 LYS A O     
4655 C  CB    . LYS A 565 ? 0.5559 0.8779 1.0184 -0.1090 -0.2110 0.2423  565 LYS A CB    
4656 C  CG    . LYS A 565 ? 0.7425 1.0681 1.2153 -0.1191 -0.2206 0.2406  565 LYS A CG    
4657 C  CD    . LYS A 565 ? 0.8380 1.1707 1.3024 -0.1347 -0.2442 0.2421  565 LYS A CD    
4658 C  CE    . LYS A 565 ? 0.8760 1.2267 1.3741 -0.1424 -0.2558 0.2561  565 LYS A CE    
4659 N  NZ    . LYS A 565 ? 0.9802 1.3216 1.4667 -0.1550 -0.2665 0.2431  565 LYS A NZ    
4660 N  N     . TYR A 566 ? 0.5311 0.8593 1.0427 -0.0774 -0.1715 0.2609  566 TYR A N     
4661 C  CA    . TYR A 566 ? 0.4633 0.8022 1.0096 -0.0665 -0.1584 0.2741  566 TYR A CA    
4662 C  C     . TYR A 566 ? 0.5639 0.8866 1.1015 -0.0549 -0.1371 0.2618  566 TYR A C     
4663 O  O     . TYR A 566 ? 0.4783 0.8033 1.0302 -0.0516 -0.1287 0.2623  566 TYR A O     
4664 C  CB    . TYR A 566 ? 0.5443 0.8965 1.1123 -0.0598 -0.1582 0.2925  566 TYR A CB    
4665 C  CG    . TYR A 566 ? 0.6248 0.9816 1.2211 -0.0444 -0.1394 0.3027  566 TYR A CG    
4666 C  CD1   . TYR A 566 ? 0.5738 0.9496 1.2073 -0.0422 -0.1382 0.3189  566 TYR A CD1   
4667 C  CD2   . TYR A 566 ? 0.5908 0.9330 1.1771 -0.0321 -0.1227 0.2963  566 TYR A CD2   
4668 C  CE1   . TYR A 566 ? 0.6128 0.9927 1.2715 -0.0273 -0.1199 0.3280  566 TYR A CE1   
4669 C  CE2   . TYR A 566 ? 0.6485 0.9933 1.2590 -0.0178 -0.1052 0.3043  566 TYR A CE2   
4670 C  CZ    . TYR A 566 ? 0.6954 1.0590 1.3415 -0.0150 -0.1033 0.3201  566 TYR A CZ    
4671 O  OH    . TYR A 566 ? 0.7348 1.1006 1.4040 0.0001  -0.0846 0.3277  566 TYR A OH    
4672 N  N     . ILE A 567 ? 0.5491 0.8555 1.0626 -0.0491 -0.1286 0.2508  567 ILE A N     
4673 C  CA    . ILE A 567 ? 0.4620 0.7534 0.9671 -0.0379 -0.1090 0.2398  567 ILE A CA    
4674 C  C     . ILE A 567 ? 0.4691 0.7489 0.9548 -0.0427 -0.1075 0.2234  567 ILE A C     
4675 O  O     . ILE A 567 ? 0.5148 0.7883 1.0022 -0.0348 -0.0929 0.2180  567 ILE A O     
4676 C  CB    . ILE A 567 ? 0.5093 0.7868 0.9951 -0.0317 -0.1021 0.2331  567 ILE A CB    
4677 C  CG1   . ILE A 567 ? 0.5293 0.7966 1.0190 -0.0176 -0.0812 0.2288  567 ILE A CG1   
4678 C  CG2   . ILE A 567 ? 0.5634 0.8259 1.0124 -0.0398 -0.1086 0.2158  567 ILE A CG2   
4679 C  CD1   . ILE A 567 ? 0.6014 0.8818 1.1260 -0.0073 -0.0726 0.2460  567 ILE A CD1   
4680 N  N     . ASN A 568 ? 0.4788 0.7553 0.9456 -0.0552 -0.1223 0.2154  568 ASN A N     
4681 C  CA    . ASN A 568 ? 0.4991 0.7647 0.9497 -0.0598 -0.1212 0.2008  568 ASN A CA    
4682 C  C     . ASN A 568 ? 0.5941 0.8716 1.0700 -0.0628 -0.1233 0.2092  568 ASN A C     
4683 O  O     . ASN A 568 ? 0.5645 0.8349 1.0368 -0.0612 -0.1154 0.2013  568 ASN A O     
4684 C  CB    . ASN A 568 ? 0.5664 0.8229 0.9880 -0.0714 -0.1352 0.1886  568 ASN A CB    
4685 C  CG    . ASN A 568 ? 0.5596 0.7992 0.9510 -0.0675 -0.1284 0.1748  568 ASN A CG    
4686 O  OD1   . ASN A 568 ? 0.4578 0.6880 0.8449 -0.0579 -0.1131 0.1688  568 ASN A OD1   
4687 N  ND2   . ASN A 568 ? 0.5201 0.7564 0.8903 -0.0752 -0.1398 0.1700  568 ASN A ND2   
4688 N  N     . ALA A 569 ? 0.6163 0.9127 1.1189 -0.0674 -0.1340 0.2260  569 ALA A N     
4689 C  CA    . ALA A 569 ? 0.6220 0.9324 1.1552 -0.0678 -0.1329 0.2374  569 ALA A CA    
4690 C  C     . ALA A 569 ? 0.5887 0.9006 1.1379 -0.0528 -0.1118 0.2423  569 ALA A C     
4691 O  O     . ALA A 569 ? 0.6346 0.9486 1.1948 -0.0507 -0.1041 0.2430  569 ALA A O     
4692 C  CB    . ALA A 569 ? 0.7088 1.0407 1.2696 -0.0749 -0.1482 0.2561  569 ALA A CB    
4693 N  N     . LYS A 570 ? 0.5813 0.8916 1.1313 -0.0422 -0.1021 0.2456  570 LYS A N     
4694 C  CA    . LYS A 570 ? 0.5631 0.8730 1.1258 -0.0273 -0.0815 0.2489  570 LYS A CA    
4695 C  C     . LYS A 570 ? 0.5999 0.8896 1.1351 -0.0215 -0.0678 0.2304  570 LYS A C     
4696 O  O     . LYS A 570 ? 0.5999 0.8884 1.1427 -0.0104 -0.0510 0.2310  570 LYS A O     
4697 C  CB    . LYS A 570 ? 0.5957 0.9101 1.1706 -0.0181 -0.0763 0.2591  570 LYS A CB    
4698 C  CG    . LYS A 570 ? 0.6147 0.9376 1.2174 -0.0040 -0.0588 0.2706  570 LYS A CG    
4699 C  CD    . LYS A 570 ? 0.7229 1.0610 1.3536 0.0006  -0.0611 0.2894  570 LYS A CD    
4700 C  CE    . LYS A 570 ? 0.8295 1.1895 1.4844 -0.0107 -0.0795 0.3055  570 LYS A CE    
4701 N  NZ    . LYS A 570 ? 0.7263 1.1051 1.4163 -0.0042 -0.0789 0.3271  570 LYS A NZ    
4702 N  N     . LEU A 571 ? 0.6159 0.8901 1.1193 -0.0285 -0.0743 0.2143  571 LEU A N     
4703 C  CA    . LEU A 571 ? 0.6030 0.8588 1.0810 -0.0226 -0.0617 0.1976  571 LEU A CA    
4704 C  C     . LEU A 571 ? 0.5515 0.8046 1.0253 -0.0264 -0.0603 0.1910  571 LEU A C     
4705 O  O     . LEU A 571 ? 0.6053 0.8627 1.0810 -0.0375 -0.0736 0.1917  571 LEU A O     
4706 C  CB    . LEU A 571 ? 0.6052 0.8461 1.0523 -0.0270 -0.0676 0.1841  571 LEU A CB    
4707 C  CG    . LEU A 571 ? 0.5582 0.7924 0.9998 -0.0186 -0.0600 0.1838  571 LEU A CG    
4708 C  CD1   . LEU A 571 ? 0.6023 0.8227 1.0135 -0.0241 -0.0663 0.1709  571 LEU A CD1   
4709 C  CD2   . LEU A 571 ? 0.6039 0.8305 1.0468 -0.0057 -0.0408 0.1799  571 LEU A CD2   
4710 N  N     . PRO A 572 ? 0.5347 0.7804 1.0025 -0.0175 -0.0446 0.1846  572 PRO A N     
4711 C  CA    . PRO A 572 ? 0.5164 0.7613 0.9833 -0.0200 -0.0420 0.1809  572 PRO A CA    
4712 C  C     . PRO A 572 ? 0.5221 0.7497 0.9576 -0.0244 -0.0437 0.1629  572 PRO A C     
4713 O  O     . PRO A 572 ? 0.4907 0.7051 0.9036 -0.0215 -0.0404 0.1516  572 PRO A O     
4714 C  CB    . PRO A 572 ? 0.5052 0.7532 0.9831 -0.0067 -0.0230 0.1853  572 PRO A CB    
4715 C  CG    . PRO A 572 ? 0.4751 0.7125 0.9395 0.0019  -0.0146 0.1790  572 PRO A CG    
4716 C  CD    . PRO A 572 ? 0.5042 0.7434 0.9690 -0.0043 -0.0281 0.1824  572 PRO A CD    
4717 N  N     . GLY A 573 ? 0.5241 0.7521 0.9604 -0.0315 -0.0489 0.1610  573 GLY A N     
4718 C  CA    . GLY A 573 ? 0.4645 0.6774 0.8751 -0.0344 -0.0484 0.1455  573 GLY A CA    
4719 C  C     . GLY A 573 ? 0.4927 0.6938 0.8789 -0.0409 -0.0585 0.1338  573 GLY A C     
4720 O  O     . GLY A 573 ? 0.4607 0.6662 0.8499 -0.0487 -0.0717 0.1372  573 GLY A O     
4721 N  N     . ALA A 574 ? 0.4928 0.6796 0.8542 -0.0376 -0.0520 0.1200  574 ALA A N     
4722 C  CA    . ALA A 574 ? 0.5699 0.7449 0.9067 -0.0427 -0.0592 0.1081  574 ALA A CA    
4723 C  C     . ALA A 574 ? 0.5659 0.7404 0.8980 -0.0394 -0.0589 0.1094  574 ALA A C     
4724 O  O     . ALA A 574 ? 0.5364 0.7014 0.8476 -0.0423 -0.0629 0.1001  574 ALA A O     
4725 C  CB    . ALA A 574 ? 0.3977 0.5590 0.7124 -0.0403 -0.0521 0.0941  574 ALA A CB    
4726 N  N     . LEU A 575 ? 0.5391 0.7233 0.8908 -0.0331 -0.0540 0.1213  575 LEU A N     
4727 C  CA    . LEU A 575 ? 0.5345 0.7182 0.8847 -0.0295 -0.0533 0.1241  575 LEU A CA    
4728 C  C     . LEU A 575 ? 0.4820 0.6745 0.8386 -0.0379 -0.0685 0.1320  575 LEU A C     
4729 O  O     . LEU A 575 ? 0.6836 0.8897 1.0622 -0.0414 -0.0750 0.1439  575 LEU A O     
4730 C  CB    . LEU A 575 ? 0.5563 0.7455 0.9249 -0.0183 -0.0406 0.1332  575 LEU A CB    
4731 C  CG    . LEU A 575 ? 0.6571 0.8334 1.0108 -0.0093 -0.0261 0.1226  575 LEU A CG    
4732 C  CD1   . LEU A 575 ? 0.5709 0.7487 0.9287 -0.0054 -0.0168 0.1215  575 LEU A CD1   
4733 C  CD2   . LEU A 575 ? 0.6407 0.8158 1.0020 -0.0001 -0.0173 0.1273  575 LEU A CD2   
4734 N  N     . GLU A 576 ? 0.5700 0.7556 0.9078 -0.0414 -0.0744 0.1260  576 GLU A N     
4735 C  CA    . GLU A 576 ? 0.6355 0.8280 0.9732 -0.0503 -0.0897 0.1315  576 GLU A CA    
4736 C  C     . GLU A 576 ? 0.6234 0.8121 0.9499 -0.0482 -0.0897 0.1315  576 GLU A C     
4737 O  O     . GLU A 576 ? 0.5431 0.7191 0.8495 -0.0454 -0.0834 0.1204  576 GLU A O     
4738 C  CB    . GLU A 576 ? 0.6057 0.7924 0.9258 -0.0608 -0.1003 0.1212  576 GLU A CB    
4739 C  CG    . GLU A 576 ? 0.8044 0.9991 1.1248 -0.0712 -0.1174 0.1265  576 GLU A CG    
4740 C  CD    . GLU A 576 ? 1.1095 1.2944 1.4066 -0.0805 -0.1263 0.1132  576 GLU A CD    
4741 O  OE1   . GLU A 576 ? 0.9464 1.1199 1.2318 -0.0788 -0.1194 0.1015  576 GLU A OE1   
4742 O  OE2   . GLU A 576 ? 1.2153 1.4037 1.5055 -0.0892 -0.1402 0.1144  576 GLU A OE2   
4743 N  N     . LEU A 577 ? 0.5859 0.7865 0.9269 -0.0495 -0.0971 0.1450  577 LEU A N     
4744 C  CA    . LEU A 577 ? 0.5278 0.7267 0.8598 -0.0488 -0.0994 0.1475  577 LEU A CA    
4745 C  C     . LEU A 577 ? 0.5797 0.7790 0.8923 -0.0599 -0.1143 0.1436  577 LEU A C     
4746 O  O     . LEU A 577 ? 0.6338 0.8415 0.9517 -0.0681 -0.1264 0.1471  577 LEU A O     
4747 C  CB    . LEU A 577 ? 0.4963 0.7085 0.8550 -0.0438 -0.0992 0.1653  577 LEU A CB    
4748 C  CG    . LEU A 577 ? 0.5439 0.7527 0.9006 -0.0381 -0.0948 0.1698  577 LEU A CG    
4749 C  CD1   . LEU A 577 ? 0.4356 0.6264 0.7703 -0.0338 -0.0840 0.1550  577 LEU A CD1   
4750 C  CD2   . LEU A 577 ? 0.5208 0.7384 0.9076 -0.0287 -0.0874 0.1849  577 LEU A CD2   
4751 N  N     . GLU A 578 ? 0.5345 0.7246 0.8245 -0.0602 -0.1135 0.1363  578 GLU A N     
4752 C  CA    . GLU A 578 ? 0.6237 0.8124 0.8911 -0.0697 -0.1256 0.1308  578 GLU A CA    
4753 C  C     . GLU A 578 ? 0.6408 0.8328 0.9025 -0.0694 -0.1288 0.1383  578 GLU A C     
4754 O  O     . GLU A 578 ? 0.6900 0.8773 0.9543 -0.0616 -0.1186 0.1403  578 GLU A O     
4755 C  CB    . GLU A 578 ? 0.7305 0.9040 0.9716 -0.0713 -0.1214 0.1127  578 GLU A CB    
4756 C  CG    . GLU A 578 ? 0.8225 0.9896 1.0683 -0.0683 -0.1132 0.1046  578 GLU A CG    
4757 C  CD    . GLU A 578 ? 0.9435 1.0996 1.1662 -0.0735 -0.1151 0.0891  578 GLU A CD    
4758 O  OE1   . GLU A 578 ? 1.0409 1.1991 1.2587 -0.0821 -0.1266 0.0871  578 GLU A OE1   
4759 O  OE2   . GLU A 578 ? 0.8947 1.0398 1.1045 -0.0691 -0.1053 0.0789  578 GLU A OE2   
4760 N  N     . TYR A 579 ? 0.6230 0.8228 0.8763 -0.0781 -0.1433 0.1424  579 TYR A N     
4761 C  CA    . TYR A 579 ? 0.7490 0.9524 0.9912 -0.0799 -0.1486 0.1488  579 TYR A CA    
4762 C  C     . TYR A 579 ? 0.8001 0.9904 1.0106 -0.0817 -0.1454 0.1340  579 TYR A C     
4763 O  O     . TYR A 579 ? 0.8278 1.0145 1.0183 -0.0891 -0.1527 0.1237  579 TYR A O     
4764 C  CB    . TYR A 579 ? 0.7428 0.9608 0.9877 -0.0890 -0.1661 0.1589  579 TYR A CB    
4765 C  CG    . TYR A 579 ? 0.8506 1.0729 1.0777 -0.0932 -0.1743 0.1638  579 TYR A CG    
4766 C  CD1   . TYR A 579 ? 0.8557 1.0870 1.0967 -0.0887 -0.1738 0.1800  579 TYR A CD1   
4767 C  CD2   . TYR A 579 ? 0.8667 1.0842 1.0633 -0.1015 -0.1826 0.1529  579 TYR A CD2   
4768 C  CE1   . TYR A 579 ? 0.8701 1.1065 1.0950 -0.0927 -0.1814 0.1859  579 TYR A CE1   
4769 C  CE2   . TYR A 579 ? 0.8801 1.1025 1.0590 -0.1052 -0.1898 0.1578  579 TYR A CE2   
4770 C  CZ    . TYR A 579 ? 0.8577 1.0900 1.0508 -0.1010 -0.1893 0.1748  579 TYR A CZ    
4771 O  OH    . TYR A 579 ? 1.0474 1.2854 1.2228 -0.1047 -0.1964 0.1809  579 TYR A OH    
4772 N  N     . GLU A 580 ? 0.7470 0.9300 0.9535 -0.0749 -0.1344 0.1328  580 GLU A N     
4773 C  CA    . GLU A 580 ? 0.8181 0.9893 0.9973 -0.0758 -0.1299 0.1195  580 GLU A CA    
4774 C  C     . GLU A 580 ? 0.7564 0.9299 0.9261 -0.0755 -0.1306 0.1267  580 GLU A C     
4775 O  O     . GLU A 580 ? 0.9312 1.0964 1.0962 -0.0704 -0.1204 0.1235  580 GLU A O     
4776 C  CB    . GLU A 580 ? 0.8033 0.9618 0.9835 -0.0689 -0.1156 0.1088  580 GLU A CB    
4777 C  CG    . GLU A 580 ? 0.9629 1.1198 1.1536 -0.0685 -0.1139 0.1032  580 GLU A CG    
4778 C  CD    . GLU A 580 ? 1.0514 1.1955 1.2259 -0.0680 -0.1070 0.0867  580 GLU A CD    
4779 O  OE1   . GLU A 580 ? 1.1138 1.2534 1.2660 -0.0732 -0.1111 0.0778  580 GLU A OE1   
4780 O  OE2   . GLU A 580 ? 0.7996 0.9384 0.9834 -0.0623 -0.0974 0.0829  580 GLU A OE2   
4781 N  N     . GLY A 581 ? 0.7500 0.9353 0.9173 -0.0812 -0.1429 0.1371  581 GLY A N     
4782 C  CA    . GLY A 581 ? 0.6827 0.8711 0.8376 -0.0819 -0.1446 0.1440  581 GLY A CA    
4783 C  C     . GLY A 581 ? 0.7587 0.9604 0.9340 -0.0803 -0.1498 0.1642  581 GLY A C     
4784 O  O     . GLY A 581 ? 0.7839 0.9876 0.9861 -0.0738 -0.1442 0.1728  581 GLY A O     
4785 N  N     . PHE A 582 ? 0.7560 0.9673 0.9181 -0.0862 -0.1607 0.1721  582 PHE A N     
4786 C  CA    . PHE A 582 ? 0.7257 0.9493 0.9026 -0.0846 -0.1651 0.1921  582 PHE A CA    
4787 C  C     . PHE A 582 ? 0.7386 0.9582 0.8996 -0.0829 -0.1596 0.1941  582 PHE A C     
4788 O  O     . PHE A 582 ? 0.7705 0.9842 0.9031 -0.0867 -0.1590 0.1825  582 PHE A O     
4789 C  CB    . PHE A 582 ? 0.7747 1.0146 0.9498 -0.0931 -0.1829 0.2023  582 PHE A CB    
4790 C  CG    . PHE A 582 ? 0.7774 1.0315 0.9675 -0.0917 -0.1884 0.2242  582 PHE A CG    
4791 C  CD1   . PHE A 582 ? 0.8171 1.0805 1.0420 -0.0869 -0.1887 0.2395  582 PHE A CD1   
4792 C  CD2   . PHE A 582 ? 0.8110 1.0697 0.9810 -0.0948 -0.1928 0.2304  582 PHE A CD2   
4793 C  CE1   . PHE A 582 ? 0.8352 1.1118 1.0756 -0.0852 -0.1937 0.2606  582 PHE A CE1   
4794 C  CE2   . PHE A 582 ? 0.8769 1.1490 1.0614 -0.0934 -0.1979 0.2518  582 PHE A CE2   
4795 C  CZ    . PHE A 582 ? 0.8688 1.1498 1.0891 -0.0886 -0.1986 0.2669  582 PHE A CZ    
4796 N  N     . TYR A 583 ? 0.7636 0.9864 0.9440 -0.0770 -0.1550 0.2091  583 TYR A N     
4797 C  CA    . TYR A 583 ? 0.8310 1.0500 1.0013 -0.0748 -0.1488 0.2131  583 TYR A CA    
4798 C  C     . TYR A 583 ? 0.8373 1.0706 1.0200 -0.0748 -0.1561 0.2355  583 TYR A C     
4799 O  O     . TYR A 583 ? 0.7810 1.0201 0.9932 -0.0702 -0.1563 0.2486  583 TYR A O     
4800 C  CB    . TYR A 583 ? 0.7404 0.9442 0.9224 -0.0666 -0.1328 0.2068  583 TYR A CB    
4801 C  CG    . TYR A 583 ? 0.7704 0.9614 0.9411 -0.0665 -0.1261 0.1860  583 TYR A CG    
4802 C  CD1   . TYR A 583 ? 0.7447 0.9298 0.8865 -0.0708 -0.1251 0.1724  583 TYR A CD1   
4803 C  CD2   . TYR A 583 ? 0.7364 0.9221 0.9254 -0.0620 -0.1207 0.1805  583 TYR A CD2   
4804 C  CE1   . TYR A 583 ? 0.6823 0.8564 0.8152 -0.0705 -0.1193 0.1544  583 TYR A CE1   
4805 C  CE2   . TYR A 583 ? 0.7318 0.9067 0.9106 -0.0620 -0.1151 0.1626  583 TYR A CE2   
4806 C  CZ    . TYR A 583 ? 0.6833 0.8525 0.8347 -0.0663 -0.1146 0.1498  583 TYR A CZ    
4807 O  OH    . TYR A 583 ? 0.6920 0.8509 0.8347 -0.0660 -0.1091 0.1331  583 TYR A OH    
4808 N  N     . LYS A 584 ? 0.9397 1.1791 1.1000 -0.0797 -0.1618 0.2404  584 LYS A N     
4809 C  CA    . LYS A 584 ? 0.8787 1.1325 1.0485 -0.0800 -0.1691 0.2627  584 LYS A CA    
4810 C  C     . LYS A 584 ? 0.8938 1.1429 1.0929 -0.0709 -0.1584 0.2749  584 LYS A C     
4811 O  O     . LYS A 584 ? 0.8986 1.1576 1.1242 -0.0678 -0.1624 0.2923  584 LYS A O     
4812 C  CB    . LYS A 584 ? 1.0122 1.2710 1.1508 -0.0856 -0.1735 0.2646  584 LYS A CB    
4813 C  CG    . LYS A 584 ? 1.1404 1.4163 1.2853 -0.0872 -0.1832 0.2884  584 LYS A CG    
4814 C  CD    . LYS A 584 ? 1.2227 1.5051 1.3329 -0.0935 -0.1887 0.2896  584 LYS A CD    
4815 C  CE    . LYS A 584 ? 1.1358 1.4279 1.2546 -0.0911 -0.1888 0.3126  584 LYS A CE    
4816 N  NZ    . LYS A 584 ? 1.0814 1.3771 1.1662 -0.0955 -0.1894 0.3126  584 LYS A NZ    
4817 N  N     . ARG A 585 ? 0.9193 1.1531 1.1151 -0.0665 -0.1448 0.2660  585 ARG A N     
4818 C  CA    . ARG A 585 ? 0.8968 1.1235 1.1190 -0.0582 -0.1346 0.2761  585 ARG A CA    
4819 C  C     . ARG A 585 ? 0.8491 1.0563 1.0736 -0.0532 -0.1204 0.2586  585 ARG A C     
4820 O  O     . ARG A 585 ? 0.7980 0.9980 1.0019 -0.0562 -0.1181 0.2403  585 ARG A O     
4821 C  CB    . ARG A 585 ? 0.9020 1.1332 1.1201 -0.0586 -0.1345 0.2913  585 ARG A CB    
4822 C  CG    . ARG A 585 ? 0.9913 1.2430 1.2075 -0.0633 -0.1488 0.3108  585 ARG A CG    
4823 C  CD    . ARG A 585 ? 0.9614 1.2174 1.1866 -0.0608 -0.1471 0.3309  585 ARG A CD    
4824 N  NE    . ARG A 585 ? 1.1296 1.3837 1.3265 -0.0649 -0.1444 0.3271  585 ARG A NE    
4825 C  CZ    . ARG A 585 ? 1.1753 1.4438 1.3517 -0.0707 -0.1536 0.3378  585 ARG A CZ    
4826 N  NH1   . ARG A 585 ? 1.1845 1.4708 1.3648 -0.0738 -0.1674 0.3531  585 ARG A NH1   
4827 N  NH2   . ARG A 585 ? 1.2468 1.5126 1.3982 -0.0733 -0.1490 0.3335  585 ARG A NH2   
4828 N  N     . GLY A 586 ? 0.8486 1.0470 1.0985 -0.0454 -0.1109 0.2646  586 GLY A N     
4829 C  CA    . GLY A 586 ? 0.7564 0.9361 1.0097 -0.0406 -0.0979 0.2489  586 GLY A CA    
4830 C  C     . GLY A 586 ? 0.8257 0.9946 1.1035 -0.0329 -0.0880 0.2569  586 GLY A C     
4831 O  O     . GLY A 586 ? 0.8051 0.9783 1.1085 -0.0276 -0.0884 0.2708  586 GLY A O     
4832 N  N     . PHE A 587 ? 0.8177 0.9721 1.0886 -0.0321 -0.0789 0.2481  587 PHE A N     
4833 C  CA    . PHE A 587 ? 0.7706 0.9113 1.0624 -0.0256 -0.0691 0.2528  587 PHE A CA    
4834 C  C     . PHE A 587 ? 0.7244 0.8477 1.0191 -0.0213 -0.0589 0.2341  587 PHE A C     
4835 O  O     . PHE A 587 ? 0.7250 0.8415 1.0001 -0.0248 -0.0561 0.2179  587 PHE A O     
4836 C  CB    . PHE A 587 ? 0.7321 0.8697 1.0157 -0.0286 -0.0669 0.2584  587 PHE A CB    
4837 C  CG    . PHE A 587 ? 0.7607 0.8869 1.0689 -0.0228 -0.0595 0.2687  587 PHE A CG    
4838 C  CD1   . PHE A 587 ? 0.7932 0.9283 1.1206 -0.0202 -0.0633 0.2908  587 PHE A CD1   
4839 C  CD2   . PHE A 587 ? 0.7257 0.8320 1.0381 -0.0201 -0.0491 0.2563  587 PHE A CD2   
4840 C  CE1   . PHE A 587 ? 0.7574 0.8806 1.1086 -0.0146 -0.0562 0.3003  587 PHE A CE1   
4841 C  CE2   . PHE A 587 ? 0.7825 0.8765 1.1176 -0.0150 -0.0425 0.2649  587 PHE A CE2   
4842 C  CZ    . PHE A 587 ? 0.7487 0.8506 1.1035 -0.0121 -0.0457 0.2869  587 PHE A CZ    
4843 N  N     . PHE A 588 ? 0.7691 0.8857 1.0880 -0.0135 -0.0532 0.2367  588 PHE A N     
4844 C  CA    . PHE A 588 ? 0.7470 0.8473 1.0694 -0.0085 -0.0433 0.2201  588 PHE A CA    
4845 C  C     . PHE A 588 ? 0.7542 0.8369 1.0922 -0.0032 -0.0338 0.2219  588 PHE A C     
4846 O  O     . PHE A 588 ? 0.7459 0.8283 1.1077 0.0028  -0.0319 0.2360  588 PHE A O     
4847 C  CB    . PHE A 588 ? 0.6980 0.8035 1.0348 -0.0033 -0.0431 0.2204  588 PHE A CB    
4848 C  CG    . PHE A 588 ? 0.7027 0.8244 1.0264 -0.0090 -0.0529 0.2185  588 PHE A CG    
4849 C  CD1   . PHE A 588 ? 0.7219 0.8619 1.0474 -0.0130 -0.0642 0.2342  588 PHE A CD1   
4850 C  CD2   . PHE A 588 ? 0.6480 0.7661 0.9576 -0.0106 -0.0512 0.2011  588 PHE A CD2   
4851 C  CE1   . PHE A 588 ? 0.6749 0.8284 0.9880 -0.0189 -0.0739 0.2315  588 PHE A CE1   
4852 C  CE2   . PHE A 588 ? 0.6783 0.8096 0.9768 -0.0162 -0.0603 0.1991  588 PHE A CE2   
4853 C  CZ    . PHE A 588 ? 0.6429 0.7914 0.9430 -0.0205 -0.0718 0.2138  588 PHE A CZ    
4854 N  N     . VAL A 589 ? 0.7634 0.8317 1.0892 -0.0053 -0.0281 0.2078  589 VAL A N     
4855 C  CA    . VAL A 589 ? 0.7942 0.8442 1.1337 -0.0015 -0.0198 0.2081  589 VAL A CA    
4856 C  C     . VAL A 589 ? 0.7524 0.7870 1.1037 0.0064  -0.0107 0.1971  589 VAL A C     
4857 O  O     . VAL A 589 ? 0.7565 0.7820 1.1301 0.0135  -0.0051 0.2045  589 VAL A O     
4858 C  CB    . VAL A 589 ? 0.7267 0.7687 1.0493 -0.0080 -0.0184 0.1991  589 VAL A CB    
4859 C  CG1   . VAL A 589 ? 0.7725 0.7916 1.1054 -0.0045 -0.0092 0.1907  589 VAL A CG1   
4860 C  CG2   . VAL A 589 ? 0.7585 0.8116 1.0775 -0.0134 -0.0243 0.2148  589 VAL A CG2   
4861 N  N     . THR A 590 ? 0.7140 0.7457 1.0507 0.0057  -0.0087 0.1797  590 THR A N     
4862 C  CA    . THR A 590 ? 0.7426 0.7594 1.0855 0.0126  0.0005  0.1669  590 THR A CA    
4863 C  C     . THR A 590 ? 0.7060 0.7282 1.0309 0.0104  -0.0007 0.1524  590 THR A C     
4864 O  O     . THR A 590 ? 0.6464 0.6819 0.9555 0.0037  -0.0084 0.1519  590 THR A O     
4865 C  CB    . THR A 590 ? 0.8702 0.8649 1.2137 0.0131  0.0077  0.1576  590 THR A CB    
4866 O  OG1   . THR A 590 ? 0.9358 0.9151 1.2921 0.0220  0.0171  0.1511  590 THR A OG1   
4867 C  CG2   . THR A 590 ? 0.7108 0.7015 1.0306 0.0060  0.0066  0.1414  590 THR A CG2   
4868 N  N     . LYS A 591 ? 0.6560 0.6673 0.9833 0.0163  0.0072  0.1406  591 LYS A N     
4869 C  CA    . LYS A 591 ? 0.6755 0.6906 0.9874 0.0150  0.0071  0.1272  591 LYS A CA    
4870 C  C     . LYS A 591 ? 0.7082 0.7226 0.9969 0.0064  0.0032  0.1162  591 LYS A C     
4871 O  O     . LYS A 591 ? 0.7409 0.7428 1.0251 0.0041  0.0057  0.1107  591 LYS A O     
4872 C  CB    . LYS A 591 ? 0.7031 0.7038 1.0192 0.0227  0.0175  0.1156  591 LYS A CB    
4873 C  CG    . LYS A 591 ? 0.7777 0.7772 1.1182 0.0325  0.0234  0.1259  591 LYS A CG    
4874 C  CD    . LYS A 591 ? 0.7806 0.7781 1.1222 0.0395  0.0310  0.1172  591 LYS A CD    
4875 C  CE    . LYS A 591 ? 0.8352 0.8135 1.1886 0.0491  0.0429  0.1126  591 LYS A CE    
4876 N  NZ    . LYS A 591 ? 0.9122 0.8805 1.2522 0.0524  0.0506  0.0950  591 LYS A NZ    
4877 N  N     . LYS A 592 ? 0.6883 0.7161 0.9635 0.0018  -0.0030 0.1136  592 LYS A N     
4878 C  CA    . LYS A 592 ? 0.7039 0.7335 0.9575 -0.0058 -0.0068 0.1041  592 LYS A CA    
4879 C  C     . LYS A 592 ? 0.6922 0.7256 0.9411 -0.0116 -0.0116 0.1123  592 LYS A C     
4880 O  O     . LYS A 592 ? 0.6940 0.7264 0.9273 -0.0171 -0.0127 0.1048  592 LYS A O     
4881 C  CB    . LYS A 592 ? 0.6348 0.6498 0.8789 -0.0054 -0.0004 0.0874  592 LYS A CB    
4882 C  CG    . LYS A 592 ? 0.6243 0.6337 0.8721 0.0011  0.0058  0.0791  592 LYS A CG    
4883 C  CD    . LYS A 592 ? 0.6396 0.6576 0.8736 -0.0014 0.0032  0.0708  592 LYS A CD    
4884 C  CE    . LYS A 592 ? 0.6933 0.7034 0.9268 0.0043  0.0106  0.0601  592 LYS A CE    
4885 N  NZ    . LYS A 592 ? 0.7626 0.7845 0.9983 0.0063  0.0094  0.0620  592 LYS A NZ    
4886 N  N     . LYS A 593 ? 0.6600 0.6986 0.9227 -0.0104 -0.0141 0.1284  593 LYS A N     
4887 C  CA    . LYS A 593 ? 0.7035 0.7461 0.9624 -0.0156 -0.0180 0.1377  593 LYS A CA    
4888 C  C     . LYS A 593 ? 0.6476 0.7062 0.9132 -0.0162 -0.0254 0.1553  593 LYS A C     
4889 O  O     . LYS A 593 ? 0.5857 0.6442 0.8714 -0.0112 -0.0244 0.1677  593 LYS A O     
4890 C  CB    . LYS A 593 ? 0.7449 0.7720 1.0152 -0.0138 -0.0119 0.1396  593 LYS A CB    
4891 C  CG    . LYS A 593 ? 0.7395 0.7545 0.9977 -0.0172 -0.0080 0.1245  593 LYS A CG    
4892 C  CD    . LYS A 593 ? 0.8303 0.8319 1.0995 -0.0176 -0.0041 0.1283  593 LYS A CD    
4893 C  CE    . LYS A 593 ? 0.8433 0.8282 1.1076 -0.0183 0.0013  0.1116  593 LYS A CE    
4894 N  NZ    . LYS A 593 ? 0.7890 0.7728 1.0443 -0.0255 0.0001  0.1094  593 LYS A NZ    
4895 N  N     . TYR A 594 ? 0.7058 0.7779 0.9543 -0.0224 -0.0329 0.1563  594 TYR A N     
4896 C  CA    . TYR A 594 ? 0.6839 0.7722 0.9350 -0.0243 -0.0415 0.1721  594 TYR A CA    
4897 C  C     . TYR A 594 ? 0.7111 0.8096 0.9383 -0.0320 -0.0480 0.1708  594 TYR A C     
4898 O  O     . TYR A 594 ? 0.6985 0.7918 0.9093 -0.0351 -0.0453 0.1582  594 TYR A O     
4899 C  CB    . TYR A 594 ? 0.6671 0.7636 0.9280 -0.0212 -0.0450 0.1744  594 TYR A CB    
4900 C  CG    . TYR A 594 ? 0.6314 0.7302 0.8773 -0.0238 -0.0467 0.1597  594 TYR A CG    
4901 C  CD1   . TYR A 594 ? 0.6490 0.7603 0.8781 -0.0303 -0.0559 0.1595  594 TYR A CD1   
4902 C  CD2   . TYR A 594 ? 0.6424 0.7302 0.8905 -0.0198 -0.0393 0.1462  594 TYR A CD2   
4903 C  CE1   . TYR A 594 ? 0.6285 0.7406 0.8452 -0.0327 -0.0575 0.1464  594 TYR A CE1   
4904 C  CE2   . TYR A 594 ? 0.7240 0.8141 0.9596 -0.0220 -0.0408 0.1341  594 TYR A CE2   
4905 C  CZ    . TYR A 594 ? 0.7223 0.8241 0.9431 -0.0285 -0.0499 0.1344  594 TYR A CZ    
4906 O  OH    . TYR A 594 ? 0.6971 0.8000 0.9070 -0.0307 -0.0513 0.1226  594 TYR A OH    
4907 N  N     . ALA A 595 ? 0.6846 0.7980 0.9101 -0.0347 -0.0567 0.1843  595 ALA A N     
4908 C  CA    . ALA A 595 ? 0.7346 0.8587 0.9362 -0.0417 -0.0635 0.1839  595 ALA A CA    
4909 C  C     . ALA A 595 ? 0.7718 0.9120 0.9739 -0.0439 -0.0744 0.1952  595 ALA A C     
4910 O  O     . ALA A 595 ? 0.7052 0.8506 0.9275 -0.0407 -0.0768 0.2101  595 ALA A O     
4911 C  CB    . ALA A 595 ? 0.6957 0.8197 0.8910 -0.0441 -0.0614 0.1915  595 ALA A CB    
4912 N  N     . VAL A 596 ? 0.7686 0.9163 0.9492 -0.0495 -0.0813 0.1879  596 VAL A N     
4913 C  CA    . VAL A 596 ? 0.7719 0.9346 0.9506 -0.0530 -0.0930 0.1963  596 VAL A CA    
4914 C  C     . VAL A 596 ? 0.8441 1.0153 0.9944 -0.0601 -0.1000 0.1955  596 VAL A C     
4915 O  O     . VAL A 596 ? 0.9066 1.0717 1.0373 -0.0621 -0.0953 0.1838  596 VAL A O     
4916 C  CB    . VAL A 596 ? 0.6997 0.8627 0.8833 -0.0527 -0.0957 0.1871  596 VAL A CB    
4917 C  CG1   . VAL A 596 ? 0.6374 0.7916 0.8470 -0.0449 -0.0874 0.1869  596 VAL A CG1   
4918 C  CG2   . VAL A 596 ? 0.6961 0.8530 0.8568 -0.0563 -0.0944 0.1679  596 VAL A CG2   
4919 N  N     . ILE A 597 ? 0.8229 1.0087 0.9710 -0.0638 -0.1112 0.2084  597 ILE A N     
4920 C  CA    . ILE A 597 ? 0.8286 1.0238 0.9483 -0.0708 -0.1195 0.2081  597 ILE A CA    
4921 C  C     . ILE A 597 ? 0.9537 1.1594 1.0704 -0.0755 -0.1325 0.2087  597 ILE A C     
4922 O  O     . ILE A 597 ? 0.9697 1.1844 1.1078 -0.0743 -0.1387 0.2223  597 ILE A O     
4923 C  CB    . ILE A 597 ? 0.9007 1.1047 1.0171 -0.0717 -0.1213 0.2256  597 ILE A CB    
4924 C  CG1   . ILE A 597 ? 0.9903 1.2036 1.0737 -0.0787 -0.1289 0.2237  597 ILE A CG1   
4925 C  CG2   . ILE A 597 ? 0.9154 1.1294 1.0575 -0.0693 -0.1271 0.2464  597 ILE A CG2   
4926 C  CD1   . ILE A 597 ? 1.0156 1.2294 1.0849 -0.0789 -0.1228 0.2290  597 ILE A CD1   
4927 N  N     . ASP A 598 ? 0.9231 1.1276 1.0147 -0.0808 -0.1365 0.1940  598 ASP A N     
4928 C  CA    . ASP A 598 ? 0.9854 1.1975 1.0715 -0.0865 -0.1491 0.1913  598 ASP A CA    
4929 C  C     . ASP A 598 ? 1.1098 1.3359 1.1766 -0.0931 -0.1615 0.2016  598 ASP A C     
4930 O  O     . ASP A 598 ? 1.1942 1.4272 1.2620 -0.0920 -0.1612 0.2165  598 ASP A O     
4931 C  CB    . ASP A 598 ? 0.9580 1.1595 1.0279 -0.0887 -0.1466 0.1696  598 ASP A CB    
4932 C  CG    . ASP A 598 ? 1.0998 1.2956 1.1387 -0.0908 -0.1421 0.1583  598 ASP A CG    
4933 O  OD1   . ASP A 598 ? 1.1632 1.3638 1.1922 -0.0909 -0.1406 0.1673  598 ASP A OD1   
4934 O  OD2   . ASP A 598 ? 1.0975 1.2842 1.1226 -0.0922 -0.1394 0.1409  598 ASP A OD2   
4935 N  N     . GLU A 599 ? 1.1690 1.3992 1.2175 -0.1003 -0.1727 0.1938  599 GLU A N     
4936 C  CA    . GLU A 599 ? 1.2504 1.4946 1.2804 -0.1072 -0.1863 0.2034  599 GLU A CA    
4937 C  C     . GLU A 599 ? 1.2832 1.5250 1.2776 -0.1096 -0.1832 0.1963  599 GLU A C     
4938 O  O     . GLU A 599 ? 1.3603 1.6132 1.3429 -0.1118 -0.1881 0.2094  599 GLU A O     
4939 C  CB    . GLU A 599 ? 1.2646 1.5140 1.2906 -0.1146 -0.2009 0.1982  599 GLU A CB    
4940 C  CG    . GLU A 599 ? 1.2711 1.5229 1.3323 -0.1122 -0.2030 0.2036  599 GLU A CG    
4941 C  CD    . GLU A 599 ? 1.4483 1.7182 1.5220 -0.1172 -0.2194 0.2209  599 GLU A CD    
4942 O  OE1   . GLU A 599 ? 1.5678 1.8455 1.6177 -0.1258 -0.2328 0.2204  599 GLU A OE1   
4943 O  OE2   . GLU A 599 ? 1.2754 1.5521 1.3828 -0.1126 -0.2188 0.2352  599 GLU A OE2   
4944 N  N     . GLU A 600 ? 1.3072 1.5355 1.2847 -0.1090 -0.1747 0.1766  600 GLU A N     
4945 C  CA    . GLU A 600 ? 1.3089 1.5348 1.2522 -0.1109 -0.1709 0.1686  600 GLU A CA    
4946 C  C     . GLU A 600 ? 1.2499 1.4741 1.1957 -0.1051 -0.1577 0.1756  600 GLU A C     
4947 O  O     . GLU A 600 ? 1.2651 1.4906 1.1845 -0.1063 -0.1543 0.1735  600 GLU A O     
4948 C  CB    . GLU A 600 ? 1.3322 1.5445 1.2575 -0.1121 -0.1669 0.1451  600 GLU A CB    
4949 C  CG    . GLU A 600 ? 1.3475 1.5583 1.2768 -0.1171 -0.1780 0.1368  600 GLU A CG    
4950 C  CD    . GLU A 600 ? 1.5366 1.7451 1.4311 -0.1241 -0.1861 0.1231  600 GLU A CD    
4951 O  OE1   . GLU A 600 ? 1.5494 1.7620 1.4164 -0.1259 -0.1862 0.1243  600 GLU A OE1   
4952 O  OE2   . GLU A 600 ? 1.5671 1.7693 1.4617 -0.1279 -0.1920 0.1111  600 GLU A OE2   
4953 N  N     . GLY A 601 ? 1.1833 1.4043 1.1597 -0.0991 -0.1501 0.1838  601 GLY A N     
4954 C  CA    . GLY A 601 ? 1.1397 1.3583 1.1216 -0.0944 -0.1384 0.1913  601 GLY A CA    
4955 C  C     . GLY A 601 ? 1.1705 1.3742 1.1580 -0.0897 -0.1243 0.1774  601 GLY A C     
4956 O  O     . GLY A 601 ? 1.2879 1.4894 1.2718 -0.0873 -0.1148 0.1799  601 GLY A O     
4957 N  N     . LYS A 602 ? 1.1335 1.3278 1.1301 -0.0885 -0.1229 0.1637  602 LYS A N     
4958 C  CA    . LYS A 602 ? 1.0266 1.2074 1.0300 -0.0841 -0.1105 0.1510  602 LYS A CA    
4959 C  C     . LYS A 602 ? 1.0800 1.2562 1.1159 -0.0786 -0.1052 0.1589  602 LYS A C     
4960 O  O     . LYS A 602 ? 1.0499 1.2287 1.1047 -0.0777 -0.1106 0.1642  602 LYS A O     
4961 C  CB    . LYS A 602 ? 0.9617 1.1345 0.9570 -0.0854 -0.1115 0.1322  602 LYS A CB    
4962 C  CG    . LYS A 602 ? 1.0142 1.1762 0.9988 -0.0832 -0.1003 0.1169  602 LYS A CG    
4963 C  CD    . LYS A 602 ? 1.0050 1.1570 0.9992 -0.0815 -0.0980 0.1029  602 LYS A CD    
4964 C  CE    . LYS A 602 ? 0.9290 1.0709 0.9203 -0.0781 -0.0860 0.0912  602 LYS A CE    
4965 N  NZ    . LYS A 602 ? 0.9954 1.1368 0.9980 -0.0748 -0.0778 0.1002  602 LYS A NZ    
4966 N  N     . ILE A 603 ? 1.0300 1.1995 1.0727 -0.0750 -0.0944 0.1597  603 ILE A N     
4967 C  CA    . ILE A 603 ? 1.0010 1.1642 1.0725 -0.0698 -0.0885 0.1664  603 ILE A CA    
4968 C  C     . ILE A 603 ? 1.0142 1.1641 1.0921 -0.0668 -0.0809 0.1500  603 ILE A C     
4969 O  O     . ILE A 603 ? 0.9544 1.0985 1.0188 -0.0673 -0.0747 0.1384  603 ILE A O     
4970 C  CB    . ILE A 603 ? 1.0314 1.1946 1.1086 -0.0683 -0.0822 0.1784  603 ILE A CB    
4971 C  CG1   . ILE A 603 ? 0.9807 1.1579 1.0545 -0.0707 -0.0895 0.1975  603 ILE A CG1   
4972 C  CG2   . ILE A 603 ? 0.9188 1.0715 1.0243 -0.0630 -0.0751 0.1812  603 ILE A CG2   
4973 C  CD1   . ILE A 603 ? 1.0935 1.2807 1.1359 -0.0760 -0.0952 0.1958  603 ILE A CD1   
4974 N  N     . THR A 604 ? 0.9257 1.0716 1.0243 -0.0635 -0.0811 0.1497  604 THR A N     
4975 C  CA    . THR A 604 ? 0.8299 0.9637 0.9366 -0.0601 -0.0738 0.1361  604 THR A CA    
4976 C  C     . THR A 604 ? 0.8502 0.9759 0.9799 -0.0548 -0.0665 0.1422  604 THR A C     
4977 O  O     . THR A 604 ? 0.8487 0.9775 0.9970 -0.0521 -0.0689 0.1543  604 THR A O     
4978 C  CB    . THR A 604 ? 0.7844 0.9192 0.8958 -0.0600 -0.0788 0.1300  604 THR A CB    
4979 O  OG1   . THR A 604 ? 0.8396 0.9835 0.9331 -0.0656 -0.0885 0.1291  604 THR A OG1   
4980 C  CG2   . THR A 604 ? 0.7853 0.9091 0.8954 -0.0580 -0.0719 0.1135  604 THR A CG2   
4981 N  N     . THR A 605 ? 0.8163 0.9316 0.9453 -0.0535 -0.0579 0.1339  605 THR A N     
4982 C  CA    . THR A 605 ? 0.8361 0.9415 0.9846 -0.0492 -0.0509 0.1376  605 THR A CA    
4983 C  C     . THR A 605 ? 0.8045 0.8980 0.9584 -0.0461 -0.0449 0.1230  605 THR A C     
4984 O  O     . THR A 605 ? 0.7353 0.8260 0.8753 -0.0479 -0.0429 0.1099  605 THR A O     
4985 C  CB    . THR A 605 ? 0.8206 0.9241 0.9654 -0.0511 -0.0465 0.1421  605 THR A CB    
4986 O  OG1   . THR A 605 ? 1.0371 1.1374 1.1655 -0.0535 -0.0427 0.1287  605 THR A OG1   
4987 C  CG2   . THR A 605 ? 0.7551 0.8715 0.8923 -0.0542 -0.0522 0.1571  605 THR A CG2   
4988 N  N     . ARG A 606 ? 0.7411 0.8276 0.9149 -0.0410 -0.0417 0.1256  606 ARG A N     
4989 C  CA    . ARG A 606 ? 0.7497 0.8252 0.9286 -0.0374 -0.0359 0.1128  606 ARG A CA    
4990 C  C     . ARG A 606 ? 0.6688 0.7313 0.8631 -0.0336 -0.0289 0.1141  606 ARG A C     
4991 O  O     . ARG A 606 ? 0.6911 0.7529 0.9021 -0.0304 -0.0285 0.1260  606 ARG A O     
4992 C  CB    . ARG A 606 ? 0.7054 0.7850 0.8929 -0.0342 -0.0385 0.1129  606 ARG A CB    
4993 C  CG    . ARG A 606 ? 0.7275 0.8179 0.9007 -0.0384 -0.0459 0.1098  606 ARG A CG    
4994 C  CD    . ARG A 606 ? 0.7898 0.8750 0.9493 -0.0398 -0.0432 0.0934  606 ARG A CD    
4995 N  NE    . ARG A 606 ? 0.8903 0.9818 1.0294 -0.0454 -0.0479 0.0893  606 ARG A NE    
4996 C  CZ    . ARG A 606 ? 0.9343 1.0322 1.0646 -0.0481 -0.0540 0.0858  606 ARG A CZ    
4997 N  NH1   . ARG A 606 ? 0.9285 1.0289 1.0697 -0.0464 -0.0566 0.0869  606 ARG A NH1   
4998 N  NH2   . ARG A 606 ? 1.0317 1.1332 1.1423 -0.0528 -0.0572 0.0811  606 ARG A NH2   
4999 N  N     . GLY A 607 ? 0.6756 0.7277 0.8647 -0.0342 -0.0235 0.1020  607 GLY A N     
5000 C  CA    . GLY A 607 ? 0.6957 0.7329 0.8976 -0.0310 -0.0170 0.0994  607 GLY A CA    
5001 C  C     . GLY A 607 ? 0.7235 0.7570 0.9323 -0.0330 -0.0157 0.1088  607 GLY A C     
5002 O  O     . GLY A 607 ? 0.6818 0.7020 0.8968 -0.0327 -0.0109 0.1039  607 GLY A O     
5003 N  N     . LEU A 608 ? 0.6168 0.6619 0.8244 -0.0355 -0.0204 0.1224  608 LEU A N     
5004 C  CA    . LEU A 608 ? 0.6878 0.7308 0.9035 -0.0372 -0.0192 0.1340  608 LEU A CA    
5005 C  C     . LEU A 608 ? 0.7364 0.7755 0.9427 -0.0421 -0.0164 0.1270  608 LEU A C     
5006 O  O     . LEU A 608 ? 0.7299 0.7711 0.9211 -0.0444 -0.0163 0.1150  608 LEU A O     
5007 C  CB    . LEU A 608 ? 0.6277 0.6860 0.8413 -0.0391 -0.0252 0.1505  608 LEU A CB    
5008 C  CG    . LEU A 608 ? 0.7601 0.8245 0.9855 -0.0348 -0.0291 0.1598  608 LEU A CG    
5009 C  CD1   . LEU A 608 ? 0.6857 0.7670 0.9047 -0.0378 -0.0366 0.1746  608 LEU A CD1   
5010 C  CD2   . LEU A 608 ? 0.6661 0.7185 0.9160 -0.0291 -0.0243 0.1665  608 LEU A CD2   
5011 N  N     . GLU A 609 ? 0.6826 0.7160 0.8999 -0.0435 -0.0139 0.1356  609 GLU A N     
5012 C  CA    . GLU A 609 ? 0.6732 0.7025 0.8861 -0.0482 -0.0110 0.1307  609 GLU A CA    
5013 C  C     . GLU A 609 ? 0.7078 0.7519 0.9016 -0.0527 -0.0130 0.1314  609 GLU A C     
5014 O  O     . GLU A 609 ? 0.7268 0.7699 0.9145 -0.0563 -0.0105 0.1247  609 GLU A O     
5015 C  CB    . GLU A 609 ? 0.5585 0.5799 0.7890 -0.0493 -0.0085 0.1423  609 GLU A CB    
5016 C  CG    . GLU A 609 ? 0.6208 0.6236 0.8697 -0.0451 -0.0052 0.1389  609 GLU A CG    
5017 C  CD    . GLU A 609 ? 0.8051 0.8088 1.0656 -0.0389 -0.0063 0.1479  609 GLU A CD    
5018 O  OE1   . GLU A 609 ? 0.7151 0.7335 0.9737 -0.0390 -0.0104 0.1614  609 GLU A OE1   
5019 O  OE2   . GLU A 609 ? 0.7978 0.7880 1.0692 -0.0338 -0.0030 0.1415  609 GLU A OE2   
5020 N  N     . ILE A 610 ? 0.7010 0.7589 0.8854 -0.0526 -0.0176 0.1393  610 ILE A N     
5021 C  CA    . ILE A 610 ? 0.7280 0.7992 0.8922 -0.0563 -0.0192 0.1393  610 ILE A CA    
5022 C  C     . ILE A 610 ? 0.7460 0.8163 0.8959 -0.0569 -0.0182 0.1218  610 ILE A C     
5023 O  O     . ILE A 610 ? 0.7197 0.7957 0.8564 -0.0598 -0.0165 0.1181  610 ILE A O     
5024 C  CB    . ILE A 610 ? 0.7281 0.8127 0.8846 -0.0561 -0.0254 0.1504  610 ILE A CB    
5025 C  CG1   . ILE A 610 ? 1.0231 1.1196 1.1549 -0.0591 -0.0276 0.1455  610 ILE A CG1   
5026 C  CG2   . ILE A 610 ? 0.8288 0.9113 0.9937 -0.0522 -0.0291 0.1491  610 ILE A CG2   
5027 C  CD1   . ILE A 610 ? 1.0381 1.1482 1.1599 -0.0603 -0.0340 0.1574  610 ILE A CD1   
5028 N  N     . VAL A 611 ? 0.7241 0.7874 0.8771 -0.0538 -0.0188 0.1115  611 VAL A N     
5029 C  CA    . VAL A 611 ? 0.7376 0.8003 0.8782 -0.0540 -0.0182 0.0960  611 VAL A CA    
5030 C  C     . VAL A 611 ? 0.7425 0.7935 0.8892 -0.0540 -0.0136 0.0852  611 VAL A C     
5031 O  O     . VAL A 611 ? 0.8481 0.8982 0.9859 -0.0540 -0.0129 0.0728  611 VAL A O     
5032 C  CB    . VAL A 611 ? 0.7447 0.8089 0.8834 -0.0510 -0.0220 0.0915  611 VAL A CB    
5033 C  CG1   . VAL A 611 ? 0.6614 0.7366 0.7971 -0.0514 -0.0278 0.1034  611 VAL A CG1   
5034 C  CG2   . VAL A 611 ? 0.6994 0.7519 0.8542 -0.0467 -0.0197 0.0883  611 VAL A CG2   
5035 N  N     . ARG A 612 ? 0.6902 0.7319 0.8517 -0.0542 -0.0109 0.0897  612 ARG A N     
5036 C  CA    . ARG A 612 ? 0.7568 0.7862 0.9245 -0.0547 -0.0076 0.0793  612 ARG A CA    
5037 C  C     . ARG A 612 ? 0.7438 0.7757 0.9093 -0.0597 -0.0056 0.0795  612 ARG A C     
5038 O  O     . ARG A 612 ? 0.7768 0.8145 0.9451 -0.0622 -0.0051 0.0914  612 ARG A O     
5039 C  CB    . ARG A 612 ? 0.7371 0.7527 0.9228 -0.0522 -0.0059 0.0825  612 ARG A CB    
5040 C  CG    . ARG A 612 ? 0.7597 0.7733 0.9505 -0.0465 -0.0069 0.0837  612 ARG A CG    
5041 C  CD    . ARG A 612 ? 0.7269 0.7243 0.9344 -0.0431 -0.0036 0.0831  612 ARG A CD    
5042 N  NE    . ARG A 612 ? 0.6491 0.6339 0.8561 -0.0450 -0.0010 0.0704  612 ARG A NE    
5043 C  CZ    . ARG A 612 ? 0.7453 0.7207 0.9506 -0.0418 0.0011  0.0578  612 ARG A CZ    
5044 N  NH1   . ARG A 612 ? 0.7609 0.7381 0.9657 -0.0362 0.0015  0.0562  612 ARG A NH1   
5045 N  NH2   . ARG A 612 ? 0.7146 0.6792 0.9185 -0.0444 0.0025  0.0470  612 ARG A NH2   
5046 N  N     . ARG A 613 ? 0.7103 0.7387 0.8714 -0.0611 -0.0043 0.0671  613 ARG A N     
5047 C  CA    . ARG A 613 ? 0.7995 0.8315 0.9601 -0.0658 -0.0023 0.0670  613 ARG A CA    
5048 C  C     . ARG A 613 ? 0.7820 0.8038 0.9592 -0.0689 -0.0010 0.0715  613 ARG A C     
5049 O  O     . ARG A 613 ? 0.8223 0.8494 1.0037 -0.0731 0.0004  0.0790  613 ARG A O     
5050 C  CB    . ARG A 613 ? 0.7351 0.7678 0.8869 -0.0662 -0.0020 0.0532  613 ARG A CB    
5051 C  CG    . ARG A 613 ? 0.8042 0.8330 0.9631 -0.0706 -0.0007 0.0494  613 ARG A CG    
5052 C  CD    . ARG A 613 ? 0.8205 0.8434 0.9758 -0.0700 -0.0017 0.0350  613 ARG A CD    
5053 N  NE    . ARG A 613 ? 0.9894 1.0222 1.1309 -0.0682 -0.0016 0.0291  613 ARG A NE    
5054 C  CZ    . ARG A 613 ? 0.9284 0.9585 1.0632 -0.0652 -0.0027 0.0191  613 ARG A CZ    
5055 N  NH1   . ARG A 613 ? 0.8068 0.8254 0.9458 -0.0633 -0.0035 0.0133  613 ARG A NH1   
5056 N  NH2   . ARG A 613 ? 0.9328 0.9716 1.0564 -0.0638 -0.0025 0.0148  613 ARG A NH2   
5057 N  N     . ASP A 614 ? 0.7856 0.7927 0.9729 -0.0670 -0.0013 0.0672  614 ASP A N     
5058 C  CA    . ASP A 614 ? 0.6705 0.6646 0.8735 -0.0702 -0.0004 0.0690  614 ASP A CA    
5059 C  C     . ASP A 614 ? 0.6804 0.6739 0.8963 -0.0707 0.0002  0.0852  614 ASP A C     
5060 O  O     . ASP A 614 ? 0.7323 0.7120 0.9634 -0.0721 0.0009  0.0872  614 ASP A O     
5061 C  CB    . ASP A 614 ? 0.7556 0.7327 0.9627 -0.0673 -0.0004 0.0574  614 ASP A CB    
5062 C  CG    . ASP A 614 ? 0.8211 0.7973 1.0255 -0.0604 -0.0001 0.0571  614 ASP A CG    
5063 O  OD1   . ASP A 614 ? 0.7611 0.7492 0.9617 -0.0585 -0.0010 0.0666  614 ASP A OD1   
5064 O  OD2   . ASP A 614 ? 0.9940 0.9579 1.2000 -0.0569 0.0010  0.0477  614 ASP A OD2   
5065 N  N     . TRP A 615 ? 0.6703 0.6778 0.8805 -0.0696 -0.0001 0.0968  615 TRP A N     
5066 C  CA    . TRP A 615 ? 0.6958 0.7052 0.9174 -0.0702 0.0002  0.1140  615 TRP A CA    
5067 C  C     . TRP A 615 ? 0.7151 0.7398 0.9312 -0.0744 0.0014  0.1240  615 TRP A C     
5068 O  O     . TRP A 615 ? 0.8377 0.8738 1.0380 -0.0750 0.0017  0.1186  615 TRP A O     
5069 C  CB    . TRP A 615 ? 0.6574 0.6703 0.8780 -0.0648 -0.0016 0.1211  615 TRP A CB    
5070 C  CG    . TRP A 615 ? 0.6738 0.6706 0.9067 -0.0603 -0.0011 0.1168  615 TRP A CG    
5071 C  CD1   . TRP A 615 ? 0.6567 0.6461 0.8850 -0.0567 -0.0009 0.1024  615 TRP A CD1   
5072 C  CD2   . TRP A 615 ? 0.6798 0.6658 0.9321 -0.0585 0.0000  0.1270  615 TRP A CD2   
5073 N  NE1   . TRP A 615 ? 0.6665 0.6412 0.9091 -0.0524 0.0007  0.1026  615 TRP A NE1   
5074 C  CE2   . TRP A 615 ? 0.6694 0.6411 0.9274 -0.0533 0.0013  0.1174  615 TRP A CE2   
5075 C  CE3   . TRP A 615 ? 0.6075 0.5945 0.8734 -0.0604 0.0004  0.1440  615 TRP A CE3   
5076 C  CZ2   . TRP A 615 ? 0.6813 0.6390 0.9580 -0.0496 0.0034  0.1234  615 TRP A CZ2   
5077 C  CZ3   . TRP A 615 ? 0.5978 0.5708 0.8832 -0.0572 0.0019  0.1505  615 TRP A CZ3   
5078 C  CH2   . TRP A 615 ? 0.6455 0.6037 0.9363 -0.0516 0.0035  0.1399  615 TRP A CH2   
5079 N  N     . SER A 616 ? 0.6958 0.7203 0.9253 -0.0770 0.0026  0.1388  616 SER A N     
5080 C  CA    . SER A 616 ? 0.7115 0.7504 0.9375 -0.0810 0.0048  0.1496  616 SER A CA    
5081 C  C     . SER A 616 ? 0.6995 0.7552 0.9085 -0.0785 0.0040  0.1576  616 SER A C     
5082 O  O     . SER A 616 ? 0.7364 0.7923 0.9432 -0.0746 0.0010  0.1612  616 SER A O     
5083 C  CB    . SER A 616 ? 0.7178 0.7517 0.9643 -0.0847 0.0063  0.1643  616 SER A CB    
5084 O  OG    . SER A 616 ? 0.8275 0.8582 1.0827 -0.0814 0.0050  0.1765  616 SER A OG    
5085 N  N     . GLU A 617 ? 0.7489 0.8190 0.9459 -0.0808 0.0066  0.1604  617 GLU A N     
5086 C  CA    . GLU A 617 ? 0.7421 0.8278 0.9195 -0.0788 0.0059  0.1662  617 GLU A CA    
5087 C  C     . GLU A 617 ? 0.7094 0.8004 0.8923 -0.0785 0.0046  0.1855  617 GLU A C     
5088 O  O     . GLU A 617 ? 0.8025 0.9017 0.9725 -0.0760 0.0012  0.1895  617 GLU A O     
5089 C  CB    . GLU A 617 ? 0.8345 0.9333 0.9984 -0.0809 0.0104  0.1650  617 GLU A CB    
5090 C  CG    . GLU A 617 ? 0.8413 0.9554 0.9822 -0.0790 0.0103  0.1693  617 GLU A CG    
5091 C  CD    . GLU A 617 ? 1.0993 1.2117 1.2252 -0.0756 0.0054  0.1575  617 GLU A CD    
5092 O  OE1   . GLU A 617 ? 1.0574 1.1631 1.1812 -0.0746 0.0051  0.1418  617 GLU A OE1   
5093 O  OE2   . GLU A 617 ? 1.0336 1.1520 1.1505 -0.0741 0.0014  0.1647  617 GLU A OE2   
5094 N  N     . ILE A 618 ? 0.7015 0.7883 0.9039 -0.0812 0.0068  0.1980  618 ILE A N     
5095 C  CA    . ILE A 618 ? 0.7449 0.8364 0.9547 -0.0808 0.0056  0.2178  618 ILE A CA    
5096 C  C     . ILE A 618 ? 0.7226 0.8056 0.9391 -0.0764 0.0007  0.2179  618 ILE A C     
5097 O  O     . ILE A 618 ? 0.7722 0.8646 0.9828 -0.0744 -0.0027 0.2292  618 ILE A O     
5098 C  CB    . ILE A 618 ? 0.6912 0.7782 0.9234 -0.0849 0.0091  0.2311  618 ILE A CB    
5099 C  CG1   . ILE A 618 ? 0.7611 0.8559 0.9998 -0.0845 0.0084  0.2539  618 ILE A CG1   
5100 C  CG2   . ILE A 618 ? 0.6722 0.7377 0.9263 -0.0857 0.0087  0.2225  618 ILE A CG2   
5101 C  CD1   . ILE A 618 ? 0.7962 0.9120 1.0110 -0.0838 0.0083  0.2623  618 ILE A CD1   
5102 N  N     . ALA A 619 ? 0.7478 0.8140 0.9758 -0.0748 0.0001  0.2051  619 ALA A N     
5103 C  CA    . ALA A 619 ? 0.7296 0.7876 0.9651 -0.0699 -0.0033 0.2045  619 ALA A CA    
5104 C  C     . ALA A 619 ? 0.7643 0.8324 0.9798 -0.0669 -0.0073 0.1977  619 ALA A C     
5105 O  O     . ALA A 619 ? 0.7431 0.8162 0.9596 -0.0640 -0.0113 0.2069  619 ALA A O     
5106 C  CB    . ALA A 619 ? 0.6262 0.6636 0.8762 -0.0687 -0.0019 0.1911  619 ALA A CB    
5107 N  N     . LYS A 620 ? 0.7617 0.8328 0.9599 -0.0678 -0.0068 0.1822  620 LYS A N     
5108 C  CA    . LYS A 620 ? 0.7306 0.8107 0.9096 -0.0657 -0.0107 0.1753  620 LYS A CA    
5109 C  C     . LYS A 620 ? 0.8274 0.9242 0.9936 -0.0665 -0.0138 0.1895  620 LYS A C     
5110 O  O     . LYS A 620 ? 0.7703 0.8725 0.9320 -0.0644 -0.0192 0.1931  620 LYS A O     
5111 C  CB    . LYS A 620 ? 0.7586 0.8402 0.9215 -0.0670 -0.0088 0.1584  620 LYS A CB    
5112 C  CG    . LYS A 620 ? 0.7044 0.7717 0.8759 -0.0668 -0.0063 0.1436  620 LYS A CG    
5113 C  CD    . LYS A 620 ? 0.7795 0.8520 0.9366 -0.0690 -0.0038 0.1322  620 LYS A CD    
5114 C  CE    . LYS A 620 ? 0.7302 0.7907 0.8929 -0.0689 -0.0024 0.1169  620 LYS A CE    
5115 N  NZ    . LYS A 620 ? 0.7723 0.8347 0.9202 -0.0667 -0.0040 0.1030  620 LYS A NZ    
5116 N  N     . GLU A 621 ? 0.7930 0.8988 0.9528 -0.0698 -0.0105 0.1977  621 GLU A N     
5117 C  CA    . GLU A 621 ? 0.8520 0.9742 0.9956 -0.0708 -0.0128 0.2103  621 GLU A CA    
5118 C  C     . GLU A 621 ? 0.8462 0.9711 1.0031 -0.0695 -0.0169 0.2291  621 GLU A C     
5119 O  O     . GLU A 621 ? 0.8062 0.9420 0.9512 -0.0689 -0.0227 0.2359  621 GLU A O     
5120 C  CB    . GLU A 621 ? 0.8732 1.0042 1.0088 -0.0740 -0.0068 0.2154  621 GLU A CB    
5121 C  CG    . GLU A 621 ? 1.0504 1.1964 1.1780 -0.0752 -0.0073 0.2348  621 GLU A CG    
5122 C  CD    . GLU A 621 ? 1.1464 1.3017 1.2651 -0.0778 -0.0001 0.2390  621 GLU A CD    
5123 O  OE1   . GLU A 621 ? 1.0656 1.2150 1.1894 -0.0789 0.0051  0.2284  621 GLU A OE1   
5124 O  OE2   . GLU A 621 ? 1.2181 1.3874 1.3249 -0.0787 0.0005  0.2533  621 GLU A OE2   
5125 N  N     . THR A 622 ? 0.7978 0.9122 0.9799 -0.0693 -0.0143 0.2377  622 THR A N     
5126 C  CA    . THR A 622 ? 0.8333 0.9490 1.0312 -0.0675 -0.0176 0.2562  622 THR A CA    
5127 C  C     . THR A 622 ? 0.7782 0.8911 0.9795 -0.0633 -0.0234 0.2524  622 THR A C     
5128 O  O     . THR A 622 ? 0.7821 0.9058 0.9813 -0.0622 -0.0292 0.2653  622 THR A O     
5129 C  CB    . THR A 622 ? 0.8300 0.9320 1.0556 -0.0678 -0.0131 0.2640  622 THR A CB    
5130 O  OG1   . THR A 622 ? 0.8256 0.9306 1.0492 -0.0723 -0.0076 0.2667  622 THR A OG1   
5131 C  CG2   . THR A 622 ? 0.7303 0.8351 0.9729 -0.0659 -0.0157 0.2860  622 THR A CG2   
5132 N  N     . GLN A 623 ? 0.7523 0.8517 0.9591 -0.0610 -0.0222 0.2352  623 GLN A N     
5133 C  CA    . GLN A 623 ? 0.7419 0.8392 0.9529 -0.0568 -0.0268 0.2312  623 GLN A CA    
5134 C  C     . GLN A 623 ? 0.8376 0.9502 1.0253 -0.0578 -0.0332 0.2285  623 GLN A C     
5135 O  O     . GLN A 623 ? 0.8663 0.9854 1.0570 -0.0558 -0.0393 0.2358  623 GLN A O     
5136 C  CB    . GLN A 623 ? 0.6765 0.7573 0.8950 -0.0543 -0.0233 0.2126  623 GLN A CB    
5137 C  CG    . GLN A 623 ? 0.6260 0.7033 0.8533 -0.0491 -0.0263 0.2098  623 GLN A CG    
5138 C  CD    . GLN A 623 ? 0.6356 0.6974 0.8677 -0.0465 -0.0222 0.1913  623 GLN A CD    
5139 O  OE1   . GLN A 623 ? 0.6691 0.7318 0.8853 -0.0479 -0.0221 0.1761  623 GLN A OE1   
5140 N  NE2   . GLN A 623 ? 0.6087 0.6558 0.8623 -0.0424 -0.0186 0.1926  623 GLN A NE2   
5141 N  N     . ALA A 624 ? 0.8512 0.9696 1.0161 -0.0611 -0.0320 0.2184  624 ALA A N     
5142 C  CA    . ALA A 624 ? 0.8573 0.9883 0.9982 -0.0626 -0.0379 0.2141  624 ALA A CA    
5143 C  C     . ALA A 624 ? 0.8596 1.0061 0.9931 -0.0642 -0.0435 0.2328  624 ALA A C     
5144 O  O     . ALA A 624 ? 0.8483 1.0032 0.9753 -0.0642 -0.0515 0.2358  624 ALA A O     
5145 C  CB    . ALA A 624 ? 0.8415 0.9740 0.9609 -0.0651 -0.0341 0.1997  624 ALA A CB    
5146 N  N     . ARG A 625 ? 0.8801 1.0313 1.0147 -0.0661 -0.0398 0.2460  625 ARG A N     
5147 C  CA    . ARG A 625 ? 0.8452 1.0120 0.9719 -0.0677 -0.0449 0.2651  625 ARG A CA    
5148 C  C     . ARG A 625 ? 0.8723 1.0396 1.0211 -0.0649 -0.0505 0.2803  625 ARG A C     
5149 O  O     . ARG A 625 ? 0.9035 1.0843 1.0442 -0.0657 -0.0587 0.2914  625 ARG A O     
5150 C  CB    . ARG A 625 ? 0.9323 1.1039 1.0577 -0.0699 -0.0386 0.2770  625 ARG A CB    
5151 C  CG    . ARG A 625 ? 0.9337 1.1074 1.0373 -0.0722 -0.0325 0.2641  625 ARG A CG    
5152 C  CD    . ARG A 625 ? 0.8918 1.0659 1.0040 -0.0739 -0.0243 0.2742  625 ARG A CD    
5153 N  NE    . ARG A 625 ? 0.9642 1.1532 1.0701 -0.0753 -0.0256 0.2956  625 ARG A NE    
5154 C  CZ    . ARG A 625 ? 0.9375 1.1287 1.0563 -0.0766 -0.0200 0.3115  625 ARG A CZ    
5155 N  NH1   . ARG A 625 ? 0.9567 1.1357 1.0961 -0.0772 -0.0132 0.3081  625 ARG A NH1   
5156 N  NH2   . ARG A 625 ? 0.8083 1.0146 0.9193 -0.0778 -0.0217 0.3315  625 ARG A NH2   
5157 N  N     . VAL A 626 ? 0.8207 0.9735 0.9974 -0.0615 -0.0464 0.2809  626 VAL A N     
5158 C  CA    . VAL A 626 ? 0.8580 1.0099 1.0581 -0.0577 -0.0505 0.2945  626 VAL A CA    
5159 C  C     . VAL A 626 ? 0.8566 1.0128 1.0521 -0.0561 -0.0579 0.2874  626 VAL A C     
5160 O  O     . VAL A 626 ? 0.8330 1.0010 1.0321 -0.0555 -0.0658 0.3013  626 VAL A O     
5161 C  CB    . VAL A 626 ? 0.8018 0.9344 1.0310 -0.0540 -0.0433 0.2934  626 VAL A CB    
5162 C  CG1   . VAL A 626 ? 0.7002 0.8277 0.9508 -0.0484 -0.0462 0.2968  626 VAL A CG1   
5163 C  CG2   . VAL A 626 ? 0.8524 0.9840 1.0948 -0.0552 -0.0392 0.3108  626 VAL A CG2   
5164 N  N     . LEU A 627 ? 0.8400 0.9875 1.0287 -0.0555 -0.0559 0.2663  627 LEU A N     
5165 C  CA    . LEU A 627 ? 0.8135 0.9650 0.9985 -0.0544 -0.0625 0.2588  627 LEU A CA    
5166 C  C     . LEU A 627 ? 0.9175 1.0865 1.0776 -0.0590 -0.0718 0.2624  627 LEU A C     
5167 O  O     . LEU A 627 ? 0.9382 1.1157 1.1005 -0.0588 -0.0803 0.2672  627 LEU A O     
5168 C  CB    . LEU A 627 ? 0.7354 0.8747 0.9156 -0.0535 -0.0580 0.2359  627 LEU A CB    
5169 C  CG    . LEU A 627 ? 0.6930 0.8170 0.8978 -0.0479 -0.0529 0.2305  627 LEU A CG    
5170 C  CD1   . LEU A 627 ? 0.6620 0.7771 0.8578 -0.0476 -0.0495 0.2085  627 LEU A CD1   
5171 C  CD2   . LEU A 627 ? 0.6881 0.8175 0.9108 -0.0440 -0.0583 0.2420  627 LEU A CD2   
5172 N  N     . GLU A 628 ? 0.8564 1.0311 0.9926 -0.0631 -0.0703 0.2602  628 GLU A N     
5173 C  CA    . GLU A 628 ? 0.9318 1.1223 1.0417 -0.0675 -0.0788 0.2633  628 GLU A CA    
5174 C  C     . GLU A 628 ? 0.9920 1.1963 1.1085 -0.0680 -0.0860 0.2870  628 GLU A C     
5175 O  O     . GLU A 628 ? 1.0599 1.2759 1.1681 -0.0702 -0.0967 0.2917  628 GLU A O     
5176 C  CB    . GLU A 628 ? 0.9635 1.1564 1.0466 -0.0708 -0.0738 0.2557  628 GLU A CB    
5177 C  CG    . GLU A 628 ? 1.0122 1.2158 1.0633 -0.0749 -0.0811 0.2488  628 GLU A CG    
5178 C  CD    . GLU A 628 ? 1.1285 1.3434 1.1561 -0.0778 -0.0796 0.2572  628 GLU A CD    
5179 O  OE1   . GLU A 628 ? 1.1449 1.3659 1.1825 -0.0774 -0.0784 0.2764  628 GLU A OE1   
5180 O  OE2   . GLU A 628 ? 1.1705 1.3879 1.1696 -0.0803 -0.0793 0.2447  628 GLU A OE2   
5181 N  N     . ALA A 629 ? 0.9721 1.1753 1.1044 -0.0664 -0.0809 0.3028  629 ALA A N     
5182 C  CA    . ALA A 629 ? 1.0235 1.2396 1.1656 -0.0663 -0.0875 0.3273  629 ALA A CA    
5183 C  C     . ALA A 629 ? 1.0694 1.2861 1.2349 -0.0629 -0.0941 0.3336  629 ALA A C     
5184 O  O     . ALA A 629 ? 1.1712 1.4028 1.3378 -0.0640 -0.1038 0.3500  629 ALA A O     
5185 C  CB    . ALA A 629 ? 1.0239 1.2359 1.1834 -0.0647 -0.0797 0.3426  629 ALA A CB    
5186 N  N     . LEU A 630 ? 0.9916 1.1932 1.1761 -0.0586 -0.0890 0.3212  630 LEU A N     
5187 C  CA    . LEU A 630 ? 0.9674 1.1696 1.1753 -0.0545 -0.0938 0.3264  630 LEU A CA    
5188 C  C     . LEU A 630 ? 1.0276 1.2397 1.2202 -0.0576 -0.1038 0.3179  630 LEU A C     
5189 O  O     . LEU A 630 ? 0.9822 1.2060 1.1854 -0.0573 -0.1130 0.3306  630 LEU A O     
5190 C  CB    . LEU A 630 ? 0.9194 1.1018 1.1510 -0.0485 -0.0840 0.3157  630 LEU A CB    
5191 C  CG    . LEU A 630 ? 0.9572 1.1308 1.2208 -0.0429 -0.0781 0.3306  630 LEU A CG    
5192 C  CD1   . LEU A 630 ? 0.9684 1.1356 1.2300 -0.0446 -0.0710 0.3351  630 LEU A CD1   
5193 C  CD2   . LEU A 630 ? 0.9719 1.1283 1.2564 -0.0366 -0.0712 0.3183  630 LEU A CD2   
5194 N  N     . LEU A 631 ? 1.0075 1.2151 1.1767 -0.0608 -0.1025 0.2971  631 LEU A N     
5195 C  CA    . LEU A 631 ? 0.9956 1.2082 1.1538 -0.0634 -0.1106 0.2859  631 LEU A CA    
5196 C  C     . LEU A 631 ? 1.1005 1.3288 1.2291 -0.0704 -0.1216 0.2884  631 LEU A C     
5197 O  O     . LEU A 631 ? 1.1236 1.3593 1.2474 -0.0733 -0.1316 0.2853  631 LEU A O     
5198 C  CB    . LEU A 631 ? 0.9833 1.1815 1.1334 -0.0628 -0.1033 0.2616  631 LEU A CB    
5199 C  CG    . LEU A 631 ? 0.8858 1.0720 1.0603 -0.0571 -0.0980 0.2536  631 LEU A CG    
5200 C  CD1   . LEU A 631 ? 0.8993 1.0797 1.1045 -0.0509 -0.0924 0.2677  631 LEU A CD1   
5201 C  CD2   . LEU A 631 ? 0.8115 0.9830 0.9761 -0.0566 -0.0892 0.2317  631 LEU A CD2   
5202 N  N     . LYS A 632 ? 1.1154 1.3490 1.2241 -0.0733 -0.1201 0.2938  632 LYS A N     
5203 C  CA    . LYS A 632 ? 1.2301 1.4775 1.3070 -0.0797 -0.1298 0.2948  632 LYS A CA    
5204 C  C     . LYS A 632 ? 1.3869 1.6520 1.4686 -0.0816 -0.1410 0.3184  632 LYS A C     
5205 O  O     . LYS A 632 ? 1.4335 1.7109 1.4959 -0.0871 -0.1532 0.3193  632 LYS A O     
5206 C  CB    . LYS A 632 ? 1.2877 1.5334 1.3385 -0.0816 -0.1221 0.2891  632 LYS A CB    
5207 C  CG    . LYS A 632 ? 1.2153 1.4524 1.2422 -0.0836 -0.1185 0.2644  632 LYS A CG    
5208 C  CD    . LYS A 632 ? 1.1844 1.4299 1.1866 -0.0892 -0.1308 0.2572  632 LYS A CD    
5209 C  CE    . LYS A 632 ? 1.2092 1.4497 1.1787 -0.0918 -0.1265 0.2378  632 LYS A CE    
5210 N  NZ    . LYS A 632 ? 1.1989 1.4239 1.1764 -0.0877 -0.1131 0.2232  632 LYS A NZ    
5211 N  N     . ASP A 633 ? 1.5388 1.8052 1.6459 -0.0774 -0.1375 0.3378  633 ASP A N     
5212 C  CA    . ASP A 633 ? 1.6660 1.9498 1.7800 -0.0787 -0.1479 0.3623  633 ASP A CA    
5213 C  C     . ASP A 633 ? 1.6790 1.9605 1.8332 -0.0722 -0.1444 0.3807  633 ASP A C     
5214 O  O     . ASP A 633 ? 1.9289 2.2249 2.0925 -0.0725 -0.1522 0.4034  633 ASP A O     
5215 C  CB    . ASP A 633 ? 1.8036 2.0985 1.8904 -0.0827 -0.1488 0.3723  633 ASP A CB    
5216 C  CG    . ASP A 633 ? 1.8723 2.1573 1.9652 -0.0794 -0.1345 0.3749  633 ASP A CG    
5217 O  OD1   . ASP A 633 ? 1.7020 1.9698 1.8028 -0.0764 -0.1238 0.3585  633 ASP A OD1   
5218 O  OD2   . ASP A 633 ? 1.9831 2.2779 2.0733 -0.0801 -0.1343 0.3939  633 ASP A OD2   
5219 N  N     . GLY A 634 ? 1.3624 1.6261 1.5401 -0.0662 -0.1332 0.3720  634 GLY A N     
5220 C  CA    . GLY A 634 ? 1.2864 1.5455 1.5019 -0.0595 -0.1289 0.3881  634 GLY A CA    
5221 C  C     . GLY A 634 ? 1.2993 1.5607 1.5217 -0.0584 -0.1247 0.4076  634 GLY A C     
5222 O  O     . GLY A 634 ? 1.2175 1.4856 1.4645 -0.0551 -0.1278 0.4297  634 GLY A O     
5223 N  N     . ASP A 635 ? 1.4715 1.7277 1.6742 -0.0611 -0.1174 0.4010  635 ASP A N     
5224 C  CA    . ASP A 635 ? 1.4900 1.7490 1.6975 -0.0609 -0.1129 0.4196  635 ASP A CA    
5225 C  C     . ASP A 635 ? 1.4354 1.6734 1.6694 -0.0558 -0.0997 0.4159  635 ASP A C     
5226 O  O     . ASP A 635 ? 1.2909 1.5182 1.5151 -0.0571 -0.0907 0.4036  635 ASP A O     
5227 C  CB    . ASP A 635 ? 1.4305 1.6982 1.6011 -0.0669 -0.1127 0.4162  635 ASP A CB    
5228 C  CG    . ASP A 635 ? 1.4700 1.7560 1.6346 -0.0693 -0.1183 0.4421  635 ASP A CG    
5229 O  OD1   . ASP A 635 ? 1.4141 1.6996 1.6069 -0.0656 -0.1161 0.4626  635 ASP A OD1   
5230 O  OD2   . ASP A 635 ? 1.6025 1.9028 1.7336 -0.0746 -0.1246 0.4420  635 ASP A OD2   
5231 N  N     . VAL A 636 ? 1.2251 1.4570 1.4938 -0.0497 -0.0987 0.4269  636 VAL A N     
5232 C  CA    . VAL A 636 ? 1.1513 1.3615 1.4464 -0.0446 -0.0869 0.4233  636 VAL A CA    
5233 C  C     . VAL A 636 ? 1.0944 1.3026 1.3913 -0.0464 -0.0807 0.4360  636 VAL A C     
5234 O  O     . VAL A 636 ? 1.0956 1.2868 1.3976 -0.0461 -0.0708 0.4253  636 VAL A O     
5235 C  CB    . VAL A 636 ? 1.0366 1.2418 1.3682 -0.0372 -0.0872 0.4343  636 VAL A CB    
5236 C  CG1   . VAL A 636 ? 0.9891 1.1685 1.3423 -0.0317 -0.0753 0.4206  636 VAL A CG1   
5237 C  CG2   . VAL A 636 ? 0.9895 1.2067 1.3188 -0.0366 -0.0969 0.4317  636 VAL A CG2   
5238 N  N     . GLU A 637 ? 1.1251 1.3511 1.4181 -0.0486 -0.0869 0.4595  637 GLU A N     
5239 C  CA    . GLU A 637 ? 1.1412 1.3679 1.4354 -0.0507 -0.0813 0.4738  637 GLU A CA    
5240 C  C     . GLU A 637 ? 1.1435 1.3686 1.4082 -0.0559 -0.0757 0.4575  637 GLU A C     
5241 O  O     . GLU A 637 ? 1.0725 1.2873 1.3447 -0.0567 -0.0666 0.4579  637 GLU A O     
5242 C  CB    . GLU A 637 ? 1.2692 1.5181 1.5612 -0.0523 -0.0898 0.5024  637 GLU A CB    
5243 C  CG    . GLU A 637 ? 1.3899 1.6611 1.6437 -0.0581 -0.1002 0.5018  637 GLU A CG    
5244 C  CD    . GLU A 637 ? 1.6250 1.9036 1.8479 -0.0635 -0.0962 0.5008  637 GLU A CD    
5245 O  OE1   . GLU A 637 ? 1.6032 1.8685 1.8298 -0.0636 -0.0851 0.4931  637 GLU A OE1   
5246 O  OE2   . GLU A 637 ? 1.4994 1.7977 1.6936 -0.0678 -0.1043 0.5076  637 GLU A OE2   
5247 N  N     . LYS A 638 ? 1.1931 1.4283 1.4252 -0.0597 -0.0811 0.4432  638 LYS A N     
5248 C  CA    . LYS A 638 ? 1.1395 1.3732 1.3441 -0.0639 -0.0751 0.4273  638 LYS A CA    
5249 C  C     . LYS A 638 ? 1.0737 1.2850 1.2909 -0.0620 -0.0651 0.4072  638 LYS A C     
5250 O  O     . LYS A 638 ? 1.0712 1.2769 1.2852 -0.0640 -0.0568 0.4038  638 LYS A O     
5251 C  CB    . LYS A 638 ? 1.1895 1.4353 1.3585 -0.0676 -0.0827 0.4139  638 LYS A CB    
5252 C  CG    . LYS A 638 ? 1.1558 1.4025 1.2940 -0.0714 -0.0767 0.3992  638 LYS A CG    
5253 C  CD    . LYS A 638 ? 1.1965 1.4631 1.2986 -0.0757 -0.0841 0.4033  638 LYS A CD    
5254 C  CE    . LYS A 638 ? 1.2055 1.4833 1.2975 -0.0777 -0.0794 0.4212  638 LYS A CE    
5255 N  NZ    . LYS A 638 ? 1.1660 1.4625 1.2193 -0.0817 -0.0858 0.4235  638 LYS A NZ    
5256 N  N     . ALA A 639 ? 1.0310 1.2299 1.2641 -0.0581 -0.0658 0.3950  639 ALA A N     
5257 C  CA    . ALA A 639 ? 0.9968 1.1744 1.2416 -0.0562 -0.0570 0.3759  639 ALA A CA    
5258 C  C     . ALA A 639 ? 1.0248 1.1888 1.2978 -0.0544 -0.0492 0.3866  639 ALA A C     
5259 O  O     . ALA A 639 ? 1.0163 1.1680 1.2902 -0.0562 -0.0414 0.3756  639 ALA A O     
5260 C  CB    . ALA A 639 ? 0.9579 1.1267 1.2133 -0.0519 -0.0594 0.3626  639 ALA A CB    
5261 N  N     . VAL A 640 ? 1.0230 1.1886 1.3203 -0.0512 -0.0514 0.4081  640 VAL A N     
5262 C  CA    . VAL A 640 ? 1.0003 1.1515 1.3258 -0.0496 -0.0442 0.4186  640 VAL A CA    
5263 C  C     . VAL A 640 ? 0.9948 1.1527 1.3099 -0.0551 -0.0402 0.4278  640 VAL A C     
5264 O  O     . VAL A 640 ? 0.9783 1.1218 1.3060 -0.0565 -0.0325 0.4245  640 VAL A O     
5265 C  CB    . VAL A 640 ? 0.9953 1.1468 1.3502 -0.0444 -0.0472 0.4407  640 VAL A CB    
5266 C  CG1   . VAL A 640 ? 1.0722 1.2442 1.4240 -0.0467 -0.0522 0.4684  640 VAL A CG1   
5267 C  CG2   . VAL A 640 ? 0.9691 1.0963 1.3572 -0.0405 -0.0390 0.4409  640 VAL A CG2   
5268 N  N     . ARG A 641 ? 0.9935 1.1736 1.2840 -0.0585 -0.0452 0.4385  641 ARG A N     
5269 C  CA    . ARG A 641 ? 0.9804 1.1685 1.2578 -0.0634 -0.0404 0.4461  641 ARG A CA    
5270 C  C     . ARG A 641 ? 1.0225 1.2033 1.2828 -0.0664 -0.0342 0.4223  641 ARG A C     
5271 O  O     . ARG A 641 ? 1.0321 1.2088 1.2969 -0.0693 -0.0269 0.4244  641 ARG A O     
5272 C  CB    . ARG A 641 ? 1.0021 1.2157 1.2536 -0.0660 -0.0469 0.4615  641 ARG A CB    
5273 C  CG    . ARG A 641 ? 1.0725 1.2969 1.3403 -0.0639 -0.0530 0.4895  641 ARG A CG    
5274 C  CD    . ARG A 641 ? 1.1366 1.3855 1.3740 -0.0664 -0.0624 0.4980  641 ARG A CD    
5275 N  NE    . ARG A 641 ? 1.1556 1.4136 1.3570 -0.0709 -0.0595 0.4867  641 ARG A NE    
5276 C  CZ    . ARG A 641 ? 1.1538 1.4254 1.3214 -0.0732 -0.0663 0.4779  641 ARG A CZ    
5277 N  NH1   . ARG A 641 ? 1.1983 1.4766 1.3630 -0.0722 -0.0774 0.4785  641 ARG A NH1   
5278 N  NH2   . ARG A 641 ? 1.1436 1.4219 1.2801 -0.0765 -0.0619 0.4682  641 ARG A NH2   
5279 N  N     . ILE A 642 ? 1.0046 1.1843 1.2462 -0.0659 -0.0370 0.4005  642 ILE A N     
5280 C  CA    . ILE A 642 ? 1.0051 1.1778 1.2318 -0.0683 -0.0313 0.3780  642 ILE A CA    
5281 C  C     . ILE A 642 ? 0.9768 1.1279 1.2294 -0.0677 -0.0241 0.3703  642 ILE A C     
5282 O  O     . ILE A 642 ? 0.9263 1.0741 1.1774 -0.0711 -0.0175 0.3657  642 ILE A O     
5283 C  CB    . ILE A 642 ? 1.0154 1.1890 1.2215 -0.0673 -0.0360 0.3567  642 ILE A CB    
5284 C  CG1   . ILE A 642 ? 1.0579 1.2523 1.2352 -0.0691 -0.0436 0.3625  642 ILE A CG1   
5285 C  CG2   . ILE A 642 ? 0.9382 1.1026 1.1333 -0.0690 -0.0297 0.3337  642 ILE A CG2   
5286 C  CD1   . ILE A 642 ? 1.0655 1.2688 1.2105 -0.0726 -0.0405 0.3519  642 ILE A CD1   
5287 N  N     . VAL A 643 ? 0.9321 1.0683 1.2090 -0.0635 -0.0251 0.3688  643 VAL A N     
5288 C  CA    . VAL A 643 ? 0.9585 1.0723 1.2577 -0.0631 -0.0188 0.3591  643 VAL A CA    
5289 C  C     . VAL A 643 ? 0.9894 1.0998 1.3087 -0.0657 -0.0142 0.3774  643 VAL A C     
5290 O  O     . VAL A 643 ? 0.9247 1.0237 1.2517 -0.0690 -0.0085 0.3700  643 VAL A O     
5291 C  CB    . VAL A 643 ? 0.9495 1.0472 1.2681 -0.0573 -0.0201 0.3516  643 VAL A CB    
5292 C  CG1   . VAL A 643 ? 1.0236 1.1285 1.3563 -0.0531 -0.0251 0.3719  643 VAL A CG1   
5293 C  CG2   . VAL A 643 ? 0.9878 1.0612 1.3302 -0.0569 -0.0137 0.3439  643 VAL A CG2   
5294 N  N     . LYS A 644 ? 0.9441 1.0654 1.2722 -0.0648 -0.0168 0.4023  644 LYS A N     
5295 C  CA    . LYS A 644 ? 1.0033 1.1227 1.3503 -0.0677 -0.0124 0.4215  644 LYS A CA    
5296 C  C     . LYS A 644 ? 0.9551 1.0862 1.2840 -0.0736 -0.0080 0.4217  644 LYS A C     
5297 O  O     . LYS A 644 ? 0.9741 1.0962 1.3181 -0.0772 -0.0021 0.4236  644 LYS A O     
5298 C  CB    . LYS A 644 ? 1.0221 1.1533 1.3804 -0.0654 -0.0165 0.4496  644 LYS A CB    
5299 C  CG    . LYS A 644 ? 1.1882 1.3087 1.5691 -0.0589 -0.0200 0.4527  644 LYS A CG    
5300 C  CD    . LYS A 644 ? 1.1469 1.2826 1.5369 -0.0566 -0.0251 0.4813  644 LYS A CD    
5301 C  CE    . LYS A 644 ? 1.1202 1.2391 1.5472 -0.0507 -0.0243 0.4914  644 LYS A CE    
5302 N  NZ    . LYS A 644 ? 1.1281 1.2204 1.5781 -0.0513 -0.0164 0.4817  644 LYS A NZ    
5303 N  N     . GLU A 645 ? 0.9778 1.1288 1.2747 -0.0747 -0.0105 0.4195  645 GLU A N     
5304 C  CA    . GLU A 645 ? 1.1191 1.2822 1.3975 -0.0793 -0.0053 0.4194  645 GLU A CA    
5305 C  C     . GLU A 645 ? 0.9318 1.0819 1.2095 -0.0815 -0.0001 0.3963  645 GLU A C     
5306 O  O     . GLU A 645 ? 0.9998 1.1503 1.2829 -0.0856 0.0062  0.3992  645 GLU A O     
5307 C  CB    . GLU A 645 ? 1.1779 1.3630 1.4202 -0.0793 -0.0091 0.4196  645 GLU A CB    
5308 C  CG    . GLU A 645 ? 1.1726 1.3736 1.4120 -0.0780 -0.0152 0.4434  645 GLU A CG    
5309 C  CD    . GLU A 645 ? 1.2337 1.4557 1.4349 -0.0788 -0.0194 0.4420  645 GLU A CD    
5310 O  OE1   . GLU A 645 ? 1.2558 1.4775 1.4341 -0.0794 -0.0183 0.4204  645 GLU A OE1   
5311 O  OE2   . GLU A 645 ? 1.1729 1.4110 1.3667 -0.0788 -0.0240 0.4624  645 GLU A OE2   
5312 N  N     . VAL A 646 ? 0.9606 1.1001 1.2327 -0.0790 -0.0028 0.3740  646 VAL A N     
5313 C  CA    . VAL A 646 ? 0.9105 1.0383 1.1815 -0.0810 0.0013  0.3520  646 VAL A CA    
5314 C  C     . VAL A 646 ? 0.8996 1.0078 1.2018 -0.0830 0.0050  0.3533  646 VAL A C     
5315 O  O     . VAL A 646 ? 0.9151 1.0193 1.2209 -0.0873 0.0097  0.3466  646 VAL A O     
5316 C  CB    . VAL A 646 ? 0.8223 0.9436 1.0805 -0.0776 -0.0027 0.3295  646 VAL A CB    
5317 C  CG1   . VAL A 646 ? 0.7957 0.9016 1.0585 -0.0792 0.0009  0.3082  646 VAL A CG1   
5318 C  CG2   . VAL A 646 ? 0.8212 0.9608 1.0464 -0.0772 -0.0057 0.3250  646 VAL A CG2   
5319 N  N     . THR A 647 ? 0.8661 0.9618 1.1922 -0.0802 0.0029  0.3624  647 THR A N     
5320 C  CA    . THR A 647 ? 0.8855 0.9604 1.2411 -0.0822 0.0062  0.3629  647 THR A CA    
5321 C  C     . THR A 647 ? 0.9635 1.0449 1.3318 -0.0875 0.0104  0.3830  647 THR A C     
5322 O  O     . THR A 647 ? 0.9589 1.0279 1.3433 -0.0921 0.0139  0.3790  647 THR A O     
5323 C  CB    . THR A 647 ? 0.9331 0.9918 1.3110 -0.0769 0.0038  0.3668  647 THR A CB    
5324 O  OG1   . THR A 647 ? 0.9941 1.0277 1.3939 -0.0782 0.0065  0.3558  647 THR A OG1   
5325 C  CG2   . THR A 647 ? 0.9837 1.0500 1.3772 -0.0757 0.0028  0.3951  647 THR A CG2   
5326 N  N     . GLU A 648 ? 0.9566 1.0580 1.3169 -0.0873 0.0099  0.4046  648 GLU A N     
5327 C  CA    . GLU A 648 ? 1.0009 1.1111 1.3711 -0.0924 0.0146  0.4242  648 GLU A CA    
5328 C  C     . GLU A 648 ? 1.0764 1.1963 1.4299 -0.0969 0.0194  0.4141  648 GLU A C     
5329 O  O     . GLU A 648 ? 0.9869 1.1037 1.3566 -0.1022 0.0241  0.4197  648 GLU A O     
5330 C  CB    . GLU A 648 ? 1.1251 1.2557 1.4885 -0.0908 0.0130  0.4502  648 GLU A CB    
5331 C  CG    . GLU A 648 ? 1.2233 1.3689 1.5885 -0.0957 0.0187  0.4700  648 GLU A CG    
5332 C  CD    . GLU A 648 ? 1.4495 1.6198 1.7962 -0.0942 0.0172  0.4915  648 GLU A CD    
5333 O  OE1   . GLU A 648 ? 1.5114 1.6865 1.8475 -0.0897 0.0107  0.4929  648 GLU A OE1   
5334 O  OE2   . GLU A 648 ? 1.2369 1.4226 1.5797 -0.0976 0.0225  0.5075  648 GLU A OE2   
5335 N  N     . LYS A 649 ? 1.0186 1.1501 1.3411 -0.0950 0.0183  0.3995  649 LYS A N     
5336 C  CA    . LYS A 649 ? 0.9735 1.1133 1.2806 -0.0982 0.0232  0.3879  649 LYS A CA    
5337 C  C     . LYS A 649 ? 0.9521 1.0726 1.2769 -0.1016 0.0248  0.3710  649 LYS A C     
5338 O  O     . LYS A 649 ? 0.9277 1.0516 1.2587 -0.1065 0.0298  0.3720  649 LYS A O     
5339 C  CB    . LYS A 649 ? 0.9791 1.1302 1.2516 -0.0949 0.0211  0.3725  649 LYS A CB    
5340 C  CG    . LYS A 649 ? 1.0362 1.2118 1.2830 -0.0946 0.0234  0.3851  649 LYS A CG    
5341 C  CD    . LYS A 649 ? 1.0533 1.2370 1.2671 -0.0923 0.0227  0.3658  649 LYS A CD    
5342 C  CE    . LYS A 649 ? 1.0775 1.2832 1.2661 -0.0929 0.0281  0.3743  649 LYS A CE    
5343 N  NZ    . LYS A 649 ? 1.0420 1.2503 1.2150 -0.0932 0.0335  0.3558  649 LYS A NZ    
5344 N  N     . LEU A 650 ? 0.9406 1.0415 1.2737 -0.0990 0.0205  0.3558  650 LEU A N     
5345 C  CA    . LEU A 650 ? 0.8937 0.9751 1.2425 -0.1023 0.0211  0.3393  650 LEU A CA    
5346 C  C     . LEU A 650 ? 0.9734 1.0441 1.3537 -0.1075 0.0234  0.3533  650 LEU A C     
5347 O  O     . LEU A 650 ? 0.9065 0.9723 1.2969 -0.1133 0.0257  0.3475  650 LEU A O     
5348 C  CB    . LEU A 650 ? 0.8595 0.9224 1.2096 -0.0977 0.0166  0.3216  650 LEU A CB    
5349 C  CG    . LEU A 650 ? 0.8957 0.9636 1.2190 -0.0938 0.0143  0.3018  650 LEU A CG    
5350 C  CD1   . LEU A 650 ? 0.7828 0.8292 1.1129 -0.0919 0.0120  0.2811  650 LEU A CD1   
5351 C  CD2   . LEU A 650 ? 0.8191 0.9021 1.1231 -0.0967 0.0175  0.2947  650 LEU A CD2   
5352 N  N     . SER A 651 ? 0.9689 1.0358 1.3662 -0.1059 0.0224  0.3723  651 SER A N     
5353 C  CA    . SER A 651 ? 0.8645 0.9181 1.2940 -0.1108 0.0241  0.3855  651 SER A CA    
5354 C  C     . SER A 651 ? 0.9508 1.0202 1.3843 -0.1173 0.0292  0.4000  651 SER A C     
5355 O  O     . SER A 651 ? 0.9674 1.0259 1.4237 -0.1238 0.0307  0.4011  651 SER A O     
5356 C  CB    . SER A 651 ? 0.8397 0.8883 1.2861 -0.1069 0.0225  0.4050  651 SER A CB    
5357 O  OG    . SER A 651 ? 0.9628 1.0350 1.4006 -0.1063 0.0240  0.4285  651 SER A OG    
5358 N  N     . LYS A 652 ? 0.9879 1.0828 1.3995 -0.1159 0.0318  0.4111  652 LYS A N     
5359 C  CA    . LYS A 652 ? 0.9045 1.0172 1.3177 -0.1210 0.0379  0.4261  652 LYS A CA    
5360 C  C     . LYS A 652 ? 0.9523 1.0723 1.3511 -0.1236 0.0410  0.4088  652 LYS A C     
5361 O  O     . LYS A 652 ? 1.0003 1.1390 1.3946 -0.1264 0.0470  0.4195  652 LYS A O     
5362 C  CB    . LYS A 652 ? 0.8965 1.0336 1.2919 -0.1178 0.0401  0.4472  652 LYS A CB    
5363 C  CG    . LYS A 652 ? 0.8696 1.0027 1.2784 -0.1148 0.0366  0.4664  652 LYS A CG    
5364 C  CD    . LYS A 652 ? 0.9298 1.0883 1.3158 -0.1115 0.0373  0.4849  652 LYS A CD    
5365 C  CE    . LYS A 652 ? 0.9208 1.0949 1.3170 -0.1158 0.0438  0.5110  652 LYS A CE    
5366 N  NZ    . LYS A 652 ? 0.9816 1.1521 1.4025 -0.1156 0.0421  0.5369  652 LYS A NZ    
5367 N  N     . TYR A 653 ? 0.9930 1.0994 1.3852 -0.1225 0.0374  0.3832  653 TYR A N     
5368 C  CA    . TYR A 653 ? 1.0188 1.1308 1.3986 -0.1246 0.0397  0.3659  653 TYR A CA    
5369 C  C     . TYR A 653 ? 1.0404 1.1784 1.3907 -0.1214 0.0445  0.3694  653 TYR A C     
5370 O  O     . TYR A 653 ? 1.0763 1.2278 1.4239 -0.1243 0.0502  0.3714  653 TYR A O     
5371 C  CB    . TYR A 653 ? 0.9902 1.0971 1.3959 -0.1328 0.0420  0.3689  653 TYR A CB    
5372 C  CG    . TYR A 653 ? 1.1564 1.2359 1.5901 -0.1366 0.0371  0.3636  653 TYR A CG    
5373 C  CD1   . TYR A 653 ? 1.0717 1.1417 1.5300 -0.1385 0.0366  0.3824  653 TYR A CD1   
5374 C  CD2   . TYR A 653 ? 1.1537 1.2160 1.5882 -0.1380 0.0329  0.3395  653 TYR A CD2   
5375 C  CE1   . TYR A 653 ? 1.0830 1.1260 1.5663 -0.1416 0.0325  0.3764  653 TYR A CE1   
5376 C  CE2   . TYR A 653 ? 1.1228 1.1588 1.5803 -0.1412 0.0285  0.3332  653 TYR A CE2   
5377 C  CZ    . TYR A 653 ? 1.1487 1.1745 1.6305 -0.1430 0.0285  0.3512  653 TYR A CZ    
5378 O  OH    . TYR A 653 ? 1.2143 1.2121 1.7186 -0.1459 0.0246  0.3440  653 TYR A OH    
5379 N  N     . GLU A 654 ? 1.1518 1.2964 1.4798 -0.1153 0.0420  0.3700  654 GLU A N     
5380 C  CA    . GLU A 654 ? 1.0355 1.2031 1.3334 -0.1120 0.0458  0.3743  654 GLU A CA    
5381 C  C     . GLU A 654 ? 0.9875 1.1561 1.2574 -0.1077 0.0436  0.3509  654 GLU A C     
5382 O  O     . GLU A 654 ? 1.1306 1.3162 1.3733 -0.1049 0.0466  0.3510  654 GLU A O     
5383 C  CB    . GLU A 654 ? 1.1261 1.3031 1.4175 -0.1091 0.0440  0.3945  654 GLU A CB    
5384 C  CG    . GLU A 654 ? 1.1862 1.3874 1.4647 -0.1096 0.0509  0.4141  654 GLU A CG    
5385 C  CD    . GLU A 654 ? 1.2666 1.4762 1.5428 -0.1076 0.0483  0.4364  654 GLU A CD    
5386 O  OE1   . GLU A 654 ? 1.1957 1.3994 1.4641 -0.1038 0.0409  0.4318  654 GLU A OE1   
5387 O  OE2   . GLU A 654 ? 1.2127 1.4355 1.4955 -0.1098 0.0536  0.4593  654 GLU A OE2   
5388 N  N     . VAL A 655 ? 0.9666 1.1170 1.2419 -0.1071 0.0387  0.3311  655 VAL A N     
5389 C  CA    . VAL A 655 ? 0.9558 1.1057 1.2067 -0.1031 0.0361  0.3096  655 VAL A CA    
5390 C  C     . VAL A 655 ? 0.9467 1.0963 1.1974 -0.1054 0.0396  0.2941  655 VAL A C     
5391 O  O     . VAL A 655 ? 0.8993 1.0380 1.1734 -0.1100 0.0397  0.2922  655 VAL A O     
5392 C  CB    . VAL A 655 ? 0.9164 1.0485 1.1717 -0.1000 0.0286  0.2986  655 VAL A CB    
5393 C  CG1   . VAL A 655 ? 0.8148 0.9416 1.0541 -0.0975 0.0264  0.2740  655 VAL A CG1   
5394 C  CG2   . VAL A 655 ? 0.9265 1.0649 1.1727 -0.0962 0.0248  0.3112  655 VAL A CG2   
5395 N  N     . PRO A 656 ? 0.9599 1.1209 1.1853 -0.1025 0.0422  0.2834  656 PRO A N     
5396 C  CA    . PRO A 656 ? 0.9394 1.1014 1.1651 -0.1041 0.0457  0.2697  656 PRO A CA    
5397 C  C     . PRO A 656 ? 0.9368 1.0792 1.1745 -0.1053 0.0400  0.2517  656 PRO A C     
5398 O  O     . PRO A 656 ? 0.8848 1.0167 1.1152 -0.1019 0.0344  0.2414  656 PRO A O     
5399 C  CB    . PRO A 656 ? 0.8686 1.0436 1.0623 -0.0992 0.0484  0.2603  656 PRO A CB    
5400 C  CG    . PRO A 656 ? 0.8732 1.0594 1.0513 -0.0968 0.0487  0.2752  656 PRO A CG    
5401 C  CD    . PRO A 656 ? 0.9203 1.0946 1.1158 -0.0978 0.0422  0.2845  656 PRO A CD    
5402 N  N     . PRO A 657 ? 0.9033 1.0410 1.1595 -0.1102 0.0413  0.2479  657 PRO A N     
5403 C  CA    . PRO A 657 ? 0.8596 0.9786 1.1260 -0.1117 0.0357  0.2306  657 PRO A CA    
5404 C  C     . PRO A 657 ? 0.8291 0.9472 1.0745 -0.1072 0.0337  0.2104  657 PRO A C     
5405 O  O     . PRO A 657 ? 0.8105 0.9131 1.0597 -0.1071 0.0287  0.1960  657 PRO A O     
5406 C  CB    . PRO A 657 ? 0.8183 0.9371 1.1066 -0.1186 0.0376  0.2329  657 PRO A CB    
5407 C  CG    . PRO A 657 ? 0.8094 0.9504 1.0924 -0.1189 0.0456  0.2460  657 PRO A CG    
5408 C  CD    . PRO A 657 ? 0.8370 0.9868 1.1065 -0.1149 0.0477  0.2601  657 PRO A CD    
5409 N  N     . GLU A 658 ? 0.8523 0.9861 1.0754 -0.1035 0.0379  0.2088  658 GLU A N     
5410 C  CA    . GLU A 658 ? 0.8572 0.9896 1.0607 -0.0992 0.0361  0.1903  658 GLU A CA    
5411 C  C     . GLU A 658 ? 0.9272 1.0488 1.1223 -0.0954 0.0298  0.1842  658 GLU A C     
5412 O  O     . GLU A 658 ? 0.8774 0.9899 1.0670 -0.0933 0.0261  0.1680  658 GLU A O     
5413 C  CB    . GLU A 658 ? 0.9250 1.0752 1.1064 -0.0957 0.0422  0.1907  658 GLU A CB    
5414 C  CG    . GLU A 658 ? 1.0405 1.2026 1.2298 -0.0983 0.0494  0.1948  658 GLU A CG    
5415 C  CD    . GLU A 658 ? 1.1890 1.3616 1.3900 -0.1014 0.0546  0.2161  658 GLU A CD    
5416 O  OE1   . GLU A 658 ? 1.0089 1.1833 1.2046 -0.1004 0.0537  0.2279  658 GLU A OE1   
5417 O  OE2   . GLU A 658 ? 1.1595 1.3396 1.3759 -0.1051 0.0594  0.2220  658 GLU A OE2   
5418 N  N     . LYS A 659 ? 0.8438 0.9671 1.0388 -0.0944 0.0286  0.1979  659 LYS A N     
5419 C  CA    . LYS A 659 ? 0.8916 1.0054 1.0830 -0.0911 0.0227  0.1950  659 LYS A CA    
5420 C  C     . LYS A 659 ? 0.8355 0.9303 1.0495 -0.0926 0.0190  0.1923  659 LYS A C     
5421 O  O     . LYS A 659 ? 0.7074 0.7938 0.9230 -0.0896 0.0149  0.1923  659 LYS A O     
5422 C  CB    . LYS A 659 ? 0.8423 0.9661 1.0266 -0.0895 0.0223  0.2121  659 LYS A CB    
5423 C  CG    . LYS A 659 ? 0.8686 1.0107 1.0281 -0.0879 0.0260  0.2153  659 LYS A CG    
5424 C  CD    . LYS A 659 ? 0.8299 0.9818 0.9834 -0.0872 0.0249  0.2338  659 LYS A CD    
5425 C  CE    . LYS A 659 ? 0.9285 1.0951 1.0513 -0.0845 0.0257  0.2323  659 LYS A CE    
5426 N  NZ    . LYS A 659 ? 0.9424 1.1145 1.0565 -0.0832 0.0205  0.2445  659 LYS A NZ    
5427 N  N     . LEU A 660 ? 0.8434 0.9310 1.0749 -0.0973 0.0203  0.1900  660 LEU A N     
5428 C  CA    . LEU A 660 ? 0.7476 0.8160 1.0007 -0.0995 0.0172  0.1883  660 LEU A CA    
5429 C  C     . LEU A 660 ? 0.6700 0.7260 0.9249 -0.1005 0.0149  0.1688  660 LEU A C     
5430 O  O     . LEU A 660 ? 0.6142 0.6531 0.8854 -0.1028 0.0125  0.1648  660 LEU A O     
5431 C  CB    . LEU A 660 ? 0.6601 0.7282 0.9351 -0.1052 0.0196  0.2041  660 LEU A CB    
5432 C  CG    . LEU A 660 ? 0.7529 0.8197 1.0375 -0.1040 0.0194  0.2223  660 LEU A CG    
5433 C  CD1   . LEU A 660 ? 0.7457 0.8099 1.0546 -0.1101 0.0215  0.2373  660 LEU A CD1   
5434 C  CD2   . LEU A 660 ? 0.7663 0.8161 1.0553 -0.0999 0.0150  0.2158  660 LEU A CD2   
5435 N  N     . VAL A 661 ? 0.7084 0.7722 0.9465 -0.0988 0.0154  0.1566  661 VAL A N     
5436 C  CA    . VAL A 661 ? 0.7449 0.8002 0.9839 -0.1003 0.0133  0.1395  661 VAL A CA    
5437 C  C     . VAL A 661 ? 0.6696 0.7124 0.9014 -0.0955 0.0096  0.1267  661 VAL A C     
5438 O  O     . VAL A 661 ? 0.6640 0.7116 0.8819 -0.0904 0.0091  0.1267  661 VAL A O     
5439 C  CB    . VAL A 661 ? 0.7138 0.7839 0.9398 -0.1002 0.0162  0.1337  661 VAL A CB    
5440 C  CG1   . VAL A 661 ? 0.5916 0.6541 0.8190 -0.1018 0.0134  0.1173  661 VAL A CG1   
5441 C  CG2   . VAL A 661 ? 0.7576 0.8415 0.9917 -0.1043 0.0210  0.1476  661 VAL A CG2   
5442 N  N     . ILE A 662 ? 0.6295 0.6562 0.8707 -0.0973 0.0069  0.1158  662 ILE A N     
5443 C  CA    . ILE A 662 ? 0.6876 0.7023 0.9222 -0.0928 0.0042  0.1023  662 ILE A CA    
5444 C  C     . ILE A 662 ? 0.6897 0.7060 0.9146 -0.0934 0.0030  0.0868  662 ILE A C     
5445 O  O     . ILE A 662 ? 0.7498 0.7639 0.9827 -0.0987 0.0022  0.0830  662 ILE A O     
5446 C  CB    . ILE A 662 ? 0.7099 0.7039 0.9606 -0.0935 0.0025  0.1008  662 ILE A CB    
5447 C  CG1   . ILE A 662 ? 0.6657 0.6583 0.9266 -0.0917 0.0037  0.1170  662 ILE A CG1   
5448 C  CG2   . ILE A 662 ? 0.6836 0.6657 0.9268 -0.0887 0.0008  0.0855  662 ILE A CG2   
5449 C  CD1   . ILE A 662 ? 0.6635 0.6372 0.9454 -0.0945 0.0031  0.1199  662 ILE A CD1   
5450 N  N     . HIS A 663 ? 0.7528 0.7735 0.9613 -0.0882 0.0027  0.0787  663 HIS A N     
5451 C  CA    . HIS A 663 ? 0.7489 0.7714 0.9474 -0.0877 0.0016  0.0646  663 HIS A CA    
5452 C  C     . HIS A 663 ? 0.7456 0.7533 0.9424 -0.0846 -0.0008 0.0525  663 HIS A C     
5453 O  O     . HIS A 663 ? 0.6829 0.6879 0.8749 -0.0794 -0.0008 0.0526  663 HIS A O     
5454 C  CB    . HIS A 663 ? 0.6897 0.7274 0.8712 -0.0842 0.0033  0.0638  663 HIS A CB    
5455 C  CG    . HIS A 663 ? 0.7108 0.7628 0.8902 -0.0854 0.0067  0.0766  663 HIS A CG    
5456 N  ND1   . HIS A 663 ? 0.6747 0.7376 0.8552 -0.0885 0.0095  0.0787  663 HIS A ND1   
5457 C  CD2   . HIS A 663 ? 0.7290 0.7871 0.9049 -0.0836 0.0078  0.0883  663 HIS A CD2   
5458 C  CE1   . HIS A 663 ? 0.6404 0.7150 0.8173 -0.0883 0.0131  0.0908  663 HIS A CE1   
5459 N  NE2   . HIS A 663 ? 0.7175 0.7894 0.8908 -0.0856 0.0117  0.0967  663 HIS A NE2   
5460 N  N     . LYS A 664 ? 0.7329 0.7317 0.9337 -0.0878 -0.0029 0.0424  664 LYS A N     
5461 C  CA    . LYS A 664 ? 0.7409 0.7261 0.9381 -0.0849 -0.0046 0.0298  664 LYS A CA    
5462 C  C     . LYS A 664 ? 0.7156 0.7033 0.9055 -0.0868 -0.0067 0.0179  664 LYS A C     
5463 O  O     . LYS A 664 ? 0.7033 0.6968 0.8983 -0.0924 -0.0079 0.0189  664 LYS A O     
5464 C  CB    . LYS A 664 ? 0.8320 0.7984 1.0426 -0.0868 -0.0054 0.0293  664 LYS A CB    
5465 C  CG    . LYS A 664 ? 0.7897 0.7419 0.9960 -0.0811 -0.0051 0.0196  664 LYS A CG    
5466 C  CD    . LYS A 664 ? 0.7756 0.7116 0.9957 -0.0801 -0.0038 0.0243  664 LYS A CD    
5467 C  CE    . LYS A 664 ? 0.7676 0.7110 0.9978 -0.0808 -0.0023 0.0416  664 LYS A CE    
5468 N  NZ    . LYS A 664 ? 0.8493 0.7774 1.0934 -0.0784 -0.0007 0.0472  664 LYS A NZ    
5469 N  N     . GLN A 665 ? 0.7390 0.7233 0.9180 -0.0822 -0.0072 0.0075  665 GLN A N     
5470 C  CA    . GLN A 665 ? 0.7827 0.7712 0.9531 -0.0830 -0.0091 -0.0027 665 GLN A CA    
5471 C  C     . GLN A 665 ? 0.8400 0.8134 1.0109 -0.0847 -0.0119 -0.0140 665 GLN A C     
5472 O  O     . GLN A 665 ? 0.9010 0.8611 1.0717 -0.0812 -0.0109 -0.0177 665 GLN A O     
5473 C  CB    . GLN A 665 ? 0.8047 0.8014 0.9616 -0.0769 -0.0077 -0.0059 665 GLN A CB    
5474 C  CG    . GLN A 665 ? 0.8925 0.8894 1.0403 -0.0759 -0.0095 -0.0174 665 GLN A CG    
5475 C  CD    . GLN A 665 ? 1.0520 1.0586 1.1887 -0.0707 -0.0081 -0.0186 665 GLN A CD    
5476 O  OE1   . GLN A 665 ? 1.1357 1.1526 1.2676 -0.0712 -0.0084 -0.0203 665 GLN A OE1   
5477 N  NE2   . GLN A 665 ? 0.9254 0.9286 1.0591 -0.0657 -0.0066 -0.0173 665 GLN A NE2   
5478 N  N     . ILE A 666 ? 0.8880 0.8636 1.0596 -0.0901 -0.0154 -0.0193 666 ILE A N     
5479 C  CA    . ILE A 666 ? 0.9008 0.8639 1.0692 -0.0922 -0.0190 -0.0313 666 ILE A CA    
5480 C  C     . ILE A 666 ? 0.8716 0.8391 1.0250 -0.0872 -0.0189 -0.0399 666 ILE A C     
5481 O  O     . ILE A 666 ? 0.9206 0.9029 1.0694 -0.0864 -0.0188 -0.0382 666 ILE A O     
5482 C  CB    . ILE A 666 ? 0.9196 0.8840 1.0965 -0.1011 -0.0240 -0.0323 666 ILE A CB    
5483 C  CG1   . ILE A 666 ? 0.9365 0.9210 1.1168 -0.1031 -0.0233 -0.0239 666 ILE A CG1   
5484 C  CG2   . ILE A 666 ? 0.9519 0.9028 1.1431 -0.1065 -0.0252 -0.0286 666 ILE A CG2   
5485 C  CD1   . ILE A 666 ? 1.1807 1.1696 1.3708 -0.1115 -0.0282 -0.0236 666 ILE A CD1   
5486 N  N     . THR A 667 ? 0.9301 0.8845 1.0764 -0.0836 -0.0185 -0.0490 667 THR A N     
5487 C  CA    . THR A 667 ? 0.9718 0.9298 1.1044 -0.0780 -0.0175 -0.0558 667 THR A CA    
5488 C  C     . THR A 667 ? 0.9161 0.8694 1.0402 -0.0806 -0.0215 -0.0672 667 THR A C     
5489 O  O     . THR A 667 ? 1.0415 0.9997 1.1543 -0.0765 -0.0210 -0.0720 667 THR A O     
5490 C  CB    . THR A 667 ? 0.9156 0.8649 1.0452 -0.0705 -0.0128 -0.0565 667 THR A CB    
5491 O  OG1   . THR A 667 ? 0.9175 0.8490 1.0450 -0.0702 -0.0128 -0.0655 667 THR A OG1   
5492 C  CG2   . THR A 667 ? 0.7815 0.7317 0.9215 -0.0691 -0.0100 -0.0451 667 THR A CG2   
5493 N  N     . ARG A 668 ? 0.9936 0.9378 1.1226 -0.0875 -0.0260 -0.0712 668 ARG A N     
5494 C  CA    . ARG A 668 ? 1.0673 1.0061 1.1870 -0.0908 -0.0309 -0.0825 668 ARG A CA    
5495 C  C     . ARG A 668 ? 1.0607 1.0030 1.1898 -0.1007 -0.0377 -0.0813 668 ARG A C     
5496 O  O     . ARG A 668 ? 1.0111 0.9601 1.1539 -0.1044 -0.0376 -0.0715 668 ARG A O     
5497 C  CB    . ARG A 668 ? 1.0519 0.9698 1.1651 -0.0884 -0.0295 -0.0926 668 ARG A CB    
5498 C  CG    . ARG A 668 ? 1.1108 1.0252 1.2172 -0.0784 -0.0223 -0.0930 668 ARG A CG    
5499 C  CD    . ARG A 668 ? 1.1397 1.0370 1.2542 -0.0760 -0.0182 -0.0921 668 ARG A CD    
5500 N  NE    . ARG A 668 ? 1.2326 1.1099 1.3418 -0.0781 -0.0198 -0.1041 668 ARG A NE    
5501 C  CZ    . ARG A 668 ? 1.1871 1.0463 1.2994 -0.0741 -0.0152 -0.1072 668 ARG A CZ    
5502 N  NH1   . ARG A 668 ? 1.0806 0.9399 1.2025 -0.0680 -0.0093 -0.0980 668 ARG A NH1   
5503 N  NH2   . ARG A 668 ? 1.2755 1.1157 1.3810 -0.0762 -0.0168 -0.1197 668 ARG A NH2   
5504 N  N     . ASP A 669 ? 1.1677 1.1061 1.2891 -0.1051 -0.0437 -0.0909 669 ASP A N     
5505 C  CA    . ASP A 669 ? 1.2567 1.1960 1.3877 -0.1155 -0.0514 -0.0909 669 ASP A CA    
5506 C  C     . ASP A 669 ? 1.1507 1.0708 1.2912 -0.1202 -0.0525 -0.0926 669 ASP A C     
5507 O  O     . ASP A 669 ? 1.2231 1.1249 1.3563 -0.1166 -0.0499 -0.1006 669 ASP A O     
5508 C  CB    . ASP A 669 ? 1.4135 1.3537 1.5322 -0.1191 -0.0586 -0.1010 669 ASP A CB    
5509 C  CG    . ASP A 669 ? 1.5119 1.4738 1.6278 -0.1174 -0.0596 -0.0964 669 ASP A CG    
5510 O  OD1   . ASP A 669 ? 1.3903 1.3673 1.5192 -0.1189 -0.0587 -0.0857 669 ASP A OD1   
5511 O  OD2   . ASP A 669 ? 1.5643 1.5282 1.6651 -0.1141 -0.0608 -0.1031 669 ASP A OD2   
5512 N  N     . LEU A 670 ? 1.0388 0.9631 1.1967 -0.1281 -0.0558 -0.0846 670 LEU A N     
5513 C  CA    . LEU A 670 ? 1.0688 0.9756 1.2390 -0.1330 -0.0566 -0.0841 670 LEU A CA    
5514 C  C     . LEU A 670 ? 1.1025 0.9877 1.2641 -0.1371 -0.0620 -0.0992 670 LEU A C     
5515 O  O     . LEU A 670 ? 1.1559 1.0207 1.3223 -0.1377 -0.0605 -0.1023 670 LEU A O     
5516 C  CB    . LEU A 670 ? 1.0202 0.9370 1.2110 -0.1420 -0.0602 -0.0728 670 LEU A CB    
5517 C  CG    . LEU A 670 ? 1.0043 0.9429 1.2038 -0.1389 -0.0549 -0.0579 670 LEU A CG    
5518 C  CD1   . LEU A 670 ? 0.9308 0.8802 1.1496 -0.1485 -0.0591 -0.0483 670 LEU A CD1   
5519 C  CD2   . LEU A 670 ? 0.9657 0.8999 1.1677 -0.1318 -0.0466 -0.0504 670 LEU A CD2   
5520 N  N     . LYS A 671 ? 1.1218 1.0106 1.2703 -0.1400 -0.0684 -0.1086 671 LYS A N     
5521 C  CA    . LYS A 671 ? 1.1922 1.0604 1.3286 -0.1438 -0.0738 -0.1242 671 LYS A CA    
5522 C  C     . LYS A 671 ? 1.1779 1.0288 1.2999 -0.1337 -0.0659 -0.1329 671 LYS A C     
5523 O  O     . LYS A 671 ? 1.1722 0.9996 1.2911 -0.1352 -0.0665 -0.1429 671 LYS A O     
5524 C  CB    . LYS A 671 ? 1.1456 1.0242 1.2690 -0.1481 -0.0820 -0.1313 671 LYS A CB    
5525 C  CG    . LYS A 671 ? 1.1897 1.0934 1.3260 -0.1535 -0.0868 -0.1199 671 LYS A CG    
5526 C  CD    . LYS A 671 ? 1.2682 1.1878 1.3897 -0.1510 -0.0897 -0.1228 671 LYS A CD    
5527 C  CE    . LYS A 671 ? 1.3027 1.2488 1.4371 -0.1514 -0.0895 -0.1092 671 LYS A CE    
5528 N  NZ    . LYS A 671 ? 1.1928 1.1462 1.3343 -0.1430 -0.0789 -0.0984 671 LYS A NZ    
5529 N  N     . ASP A 672 ? 1.1765 1.0383 1.2903 -0.1234 -0.0584 -0.1290 672 ASP A N     
5530 C  CA    . ASP A 672 ? 1.2466 1.0958 1.3469 -0.1132 -0.0505 -0.1361 672 ASP A CA    
5531 C  C     . ASP A 672 ? 1.2015 1.0410 1.3144 -0.1076 -0.0425 -0.1291 672 ASP A C     
5532 O  O     . ASP A 672 ? 1.1770 1.0089 1.2822 -0.0981 -0.0350 -0.1321 672 ASP A O     
5533 C  CB    . ASP A 672 ? 1.2293 1.0955 1.3164 -0.1052 -0.0467 -0.1346 672 ASP A CB    
5534 C  CG    . ASP A 672 ? 1.2824 1.1518 1.3514 -0.1078 -0.0528 -0.1450 672 ASP A CG    
5535 O  OD1   . ASP A 672 ? 1.2271 1.1148 1.2980 -0.1123 -0.0584 -0.1403 672 ASP A OD1   
5536 O  OD2   . ASP A 672 ? 1.3664 1.2205 1.4192 -0.1050 -0.0516 -0.1575 672 ASP A OD2   
5537 N  N     . TYR A 673 ? 1.1313 0.9717 1.2639 -0.1130 -0.0439 -0.1189 673 TYR A N     
5538 C  CA    . TYR A 673 ? 1.1192 0.9509 1.2649 -0.1083 -0.0371 -0.1108 673 TYR A CA    
5539 C  C     . TYR A 673 ? 1.1151 0.9187 1.2635 -0.1104 -0.0374 -0.1203 673 TYR A C     
5540 O  O     . TYR A 673 ? 1.1883 0.9830 1.3440 -0.1204 -0.0445 -0.1236 673 TYR A O     
5541 C  CB    . TYR A 673 ? 1.0890 0.9347 1.2541 -0.1128 -0.0379 -0.0946 673 TYR A CB    
5542 C  CG    . TYR A 673 ? 1.1222 0.9891 1.2869 -0.1061 -0.0327 -0.0831 673 TYR A CG    
5543 C  CD1   . TYR A 673 ? 1.1505 1.0261 1.3303 -0.1064 -0.0300 -0.0682 673 TYR A CD1   
5544 C  CD2   . TYR A 673 ? 1.1828 1.0606 1.3318 -0.0998 -0.0307 -0.0871 673 TYR A CD2   
5545 C  CE1   . TYR A 673 ? 1.1299 1.0238 1.3077 -0.1008 -0.0259 -0.0587 673 TYR A CE1   
5546 C  CE2   . TYR A 673 ? 1.1252 1.0208 1.2740 -0.0944 -0.0266 -0.0773 673 TYR A CE2   
5547 C  CZ    . TYR A 673 ? 1.0379 0.9410 1.2004 -0.0950 -0.0244 -0.0638 673 TYR A CZ    
5548 O  OH    . TYR A 673 ? 1.0885 1.0083 1.2491 -0.0900 -0.0208 -0.0551 673 TYR A OH    
5549 N  N     . LYS A 674 ? 1.1000 0.8896 1.2434 -0.1009 -0.0296 -0.1245 674 LYS A N     
5550 C  CA    . LYS A 674 ? 1.0845 0.8458 1.2307 -0.1013 -0.0283 -0.1337 674 LYS A CA    
5551 C  C     . LYS A 674 ? 1.0876 0.8419 1.2576 -0.1025 -0.0259 -0.1213 674 LYS A C     
5552 O  O     . LYS A 674 ? 1.1713 0.9096 1.3523 -0.1106 -0.0304 -0.1236 674 LYS A O     
5553 C  CB    . LYS A 674 ? 1.1709 0.9200 1.3020 -0.0898 -0.0201 -0.1437 674 LYS A CB    
5554 C  CG    . LYS A 674 ? 1.2500 1.0107 1.3582 -0.0865 -0.0205 -0.1521 674 LYS A CG    
5555 C  CD    . LYS A 674 ? 1.2914 1.0395 1.3858 -0.0750 -0.0114 -0.1614 674 LYS A CD    
5556 C  CE    . LYS A 674 ? 1.4003 1.1633 1.4997 -0.0644 -0.0028 -0.1493 674 LYS A CE    
5557 N  NZ    . LYS A 674 ? 1.3354 1.1068 1.4154 -0.0568 0.0014  -0.1553 674 LYS A NZ    
5558 N  N     . ALA A 675 ? 1.0811 0.8472 1.2594 -0.0950 -0.0193 -0.1075 675 ALA A N     
5559 C  CA    . ALA A 675 ? 1.0709 0.8344 1.2715 -0.0956 -0.0170 -0.0930 675 ALA A CA    
5560 C  C     . ALA A 675 ? 1.1180 0.9052 1.3282 -0.1021 -0.0210 -0.0785 675 ALA A C     
5561 O  O     . ALA A 675 ? 1.0770 0.8860 1.2798 -0.0985 -0.0198 -0.0730 675 ALA A O     
5562 C  CB    . ALA A 675 ? 1.0245 0.7870 1.2286 -0.0836 -0.0077 -0.0859 675 ALA A CB    
5563 N  N     . THR A 676 ? 1.1018 0.8846 1.3289 -0.1113 -0.0254 -0.0723 676 THR A N     
5564 C  CA    . THR A 676 ? 1.1289 0.9334 1.3660 -0.1182 -0.0290 -0.0590 676 THR A CA    
5565 C  C     . THR A 676 ? 1.0621 0.8715 1.3166 -0.1155 -0.0242 -0.0408 676 THR A C     
5566 O  O     . THR A 676 ? 1.0094 0.8044 1.2809 -0.1194 -0.0244 -0.0356 676 THR A O     
5567 C  CB    . THR A 676 ? 1.0397 0.8390 1.2848 -0.1309 -0.0376 -0.0629 676 THR A CB    
5568 O  OG1   . THR A 676 ? 1.2220 1.0020 1.4858 -0.1354 -0.0379 -0.0589 676 THR A OG1   
5569 C  CG2   . THR A 676 ? 1.0136 0.8021 1.2410 -0.1333 -0.0427 -0.0824 676 THR A CG2   
5570 N  N     . GLY A 677 ? 0.9970 0.8265 1.2468 -0.1091 -0.0201 -0.0310 677 GLY A N     
5571 C  CA    . GLY A 677 ? 0.8973 0.7352 1.1606 -0.1067 -0.0161 -0.0132 677 GLY A CA    
5572 C  C     . GLY A 677 ? 0.8967 0.7505 1.1712 -0.1150 -0.0190 -0.0005 677 GLY A C     
5573 O  O     . GLY A 677 ? 1.0573 0.9146 1.3323 -0.1231 -0.0242 -0.0053 677 GLY A O     
5574 N  N     . PRO A 678 ? 0.8634 0.7280 1.1475 -0.1130 -0.0154 0.0166  678 PRO A N     
5575 C  CA    . PRO A 678 ? 0.8454 0.7261 1.1406 -0.1202 -0.0167 0.0301  678 PRO A CA    
5576 C  C     . PRO A 678 ? 0.8136 0.7157 1.0969 -0.1220 -0.0183 0.0278  678 PRO A C     
5577 O  O     . PRO A 678 ? 0.8115 0.7199 1.1021 -0.1302 -0.0220 0.0290  678 PRO A O     
5578 C  CB    . PRO A 678 ? 0.8154 0.7041 1.1177 -0.1153 -0.0118 0.0477  678 PRO A CB    
5579 C  CG    . PRO A 678 ? 0.8134 0.6830 1.1174 -0.1083 -0.0091 0.0441  678 PRO A CG    
5580 C  CD    . PRO A 678 ? 0.9482 0.8099 1.2354 -0.1045 -0.0101 0.0251  678 PRO A CD    
5581 N  N     . HIS A 679 ? 0.8499 0.7638 1.1164 -0.1144 -0.0157 0.0250  679 HIS A N     
5582 C  CA    . HIS A 679 ? 0.8155 0.7478 1.0707 -0.1153 -0.0170 0.0216  679 HIS A CA    
5583 C  C     . HIS A 679 ? 0.8273 0.7525 1.0781 -0.1202 -0.0225 0.0068  679 HIS A C     
5584 O  O     . HIS A 679 ? 0.8363 0.7745 1.0877 -0.1253 -0.0252 0.0069  679 HIS A O     
5585 C  CB    . HIS A 679 ? 0.7597 0.7025 0.9980 -0.1064 -0.0135 0.0201  679 HIS A CB    
5586 C  CG    . HIS A 679 ? 0.8411 0.7719 1.0674 -0.1008 -0.0138 0.0061  679 HIS A CG    
5587 N  ND1   . HIS A 679 ? 0.8378 0.7495 1.0679 -0.0975 -0.0125 0.0028  679 HIS A ND1   
5588 C  CD2   . HIS A 679 ? 0.8549 0.7903 1.0657 -0.0976 -0.0146 -0.0047 679 HIS A CD2   
5589 C  CE1   . HIS A 679 ? 0.8802 0.7860 1.0973 -0.0923 -0.0121 -0.0096 679 HIS A CE1   
5590 N  NE2   . HIS A 679 ? 0.8348 0.7548 1.0399 -0.0926 -0.0136 -0.0141 679 HIS A NE2   
5591 N  N     . VAL A 680 ? 0.8349 0.7397 1.0817 -0.1189 -0.0241 -0.0056 680 VAL A N     
5592 C  CA    . VAL A 680 ? 0.8917 0.7880 1.1335 -0.1243 -0.0301 -0.0199 680 VAL A CA    
5593 C  C     . VAL A 680 ? 0.8644 0.7580 1.1232 -0.1355 -0.0354 -0.0162 680 VAL A C     
5594 O  O     . VAL A 680 ? 0.9455 0.8461 1.2033 -0.1419 -0.0410 -0.0211 680 VAL A O     
5595 C  CB    . VAL A 680 ? 0.9915 0.8649 1.2247 -0.1200 -0.0297 -0.0337 680 VAL A CB    
5596 C  CG1   . VAL A 680 ? 1.0174 0.8840 1.2409 -0.1251 -0.0361 -0.0492 680 VAL A CG1   
5597 C  CG2   . VAL A 680 ? 0.9581 0.8353 1.1784 -0.1088 -0.0238 -0.0346 680 VAL A CG2   
5598 N  N     . ALA A 681 ? 0.8766 0.7600 1.1525 -0.1383 -0.0342 -0.0070 681 ALA A N     
5599 C  CA    . ALA A 681 ? 0.8961 0.7762 1.1906 -0.1496 -0.0393 -0.0024 681 ALA A CA    
5600 C  C     . ALA A 681 ? 0.9351 0.8411 1.2366 -0.1540 -0.0396 0.0095  681 ALA A C     
5601 O  O     . ALA A 681 ? 0.9676 0.8781 1.2770 -0.1630 -0.0456 0.0080  681 ALA A O     
5602 C  CB    . ALA A 681 ? 0.7604 0.6250 1.0729 -0.1509 -0.0370 0.0070  681 ALA A CB    
5603 N  N     . VAL A 682 ? 0.8655 0.7888 1.1640 -0.1476 -0.0330 0.0214  682 VAL A N     
5604 C  CA    . VAL A 682 ? 0.8683 0.8163 1.1713 -0.1501 -0.0316 0.0322  682 VAL A CA    
5605 C  C     . VAL A 682 ? 0.9213 0.8801 1.2123 -0.1506 -0.0352 0.0218  682 VAL A C     
5606 O  O     . VAL A 682 ? 0.9378 0.9094 1.2381 -0.1573 -0.0383 0.0255  682 VAL A O     
5607 C  CB    . VAL A 682 ? 0.8125 0.7751 1.1104 -0.1424 -0.0238 0.0449  682 VAL A CB    
5608 C  CG1   . VAL A 682 ? 0.7945 0.7820 1.0872 -0.1415 -0.0213 0.0498  682 VAL A CG1   
5609 C  CG2   . VAL A 682 ? 0.8007 0.7603 1.1161 -0.1448 -0.0209 0.0607  682 VAL A CG2   
5610 N  N     . ALA A 683 ? 0.8976 0.8519 1.1692 -0.1436 -0.0349 0.0094  683 ALA A N     
5611 C  CA    . ALA A 683 ? 0.9390 0.9032 1.1990 -0.1435 -0.0383 0.0000  683 ALA A CA    
5612 C  C     . ALA A 683 ? 1.0352 0.9913 1.3015 -0.1531 -0.0472 -0.0086 683 ALA A C     
5613 O  O     . ALA A 683 ? 1.1117 1.0818 1.3795 -0.1572 -0.0511 -0.0091 683 ALA A O     
5614 C  CB    . ALA A 683 ? 0.8776 0.8367 1.1166 -0.1343 -0.0362 -0.0108 683 ALA A CB    
5615 N  N     . LYS A 684 ? 1.0255 0.9587 1.2958 -0.1569 -0.0507 -0.0154 684 LYS A N     
5616 C  CA    . LYS A 684 ? 1.0294 0.9527 1.3040 -0.1667 -0.0601 -0.0249 684 LYS A CA    
5617 C  C     . LYS A 684 ? 1.1205 1.0541 1.4181 -0.1774 -0.0641 -0.0134 684 LYS A C     
5618 O  O     . LYS A 684 ? 1.0963 1.0371 1.3977 -0.1850 -0.0716 -0.0169 684 LYS A O     
5619 C  CB    . LYS A 684 ? 1.0358 0.9300 1.3079 -0.1675 -0.0622 -0.0361 684 LYS A CB    
5620 C  CG    . LYS A 684 ? 1.0615 0.9457 1.3103 -0.1584 -0.0598 -0.0501 684 LYS A CG    
5621 C  CD    . LYS A 684 ? 1.1244 0.9825 1.3669 -0.1622 -0.0652 -0.0662 684 LYS A CD    
5622 C  CE    . LYS A 684 ? 1.0528 0.8931 1.2841 -0.1520 -0.0583 -0.0730 684 LYS A CE    
5623 N  NZ    . LYS A 684 ? 1.1000 0.9183 1.3165 -0.1528 -0.0622 -0.0918 684 LYS A NZ    
5624 N  N     . ARG A 685 ? 1.0568 0.9928 1.3706 -0.1780 -0.0591 0.0013  685 ARG A N     
5625 C  CA    . ARG A 685 ? 0.9805 0.9296 1.3172 -0.1874 -0.0614 0.0146  685 ARG A CA    
5626 C  C     . ARG A 685 ? 1.0491 1.0265 1.3845 -0.1859 -0.0595 0.0210  685 ARG A C     
5627 O  O     . ARG A 685 ? 1.0034 0.9920 1.3523 -0.1944 -0.0651 0.0243  685 ARG A O     
5628 C  CB    . ARG A 685 ? 0.8809 0.8284 1.2336 -0.1872 -0.0552 0.0304  685 ARG A CB    
5629 C  CG    . ARG A 685 ? 0.9031 0.8312 1.2758 -0.1974 -0.0607 0.0317  685 ARG A CG    
5630 C  CD    . ARG A 685 ? 0.9705 0.8766 1.3426 -0.1923 -0.0565 0.0314  685 ARG A CD    
5631 N  NE    . ARG A 685 ? 1.0057 0.9240 1.3812 -0.1854 -0.0471 0.0481  685 ARG A NE    
5632 C  CZ    . ARG A 685 ? 0.9919 0.8996 1.3608 -0.1769 -0.0415 0.0494  685 ARG A CZ    
5633 N  NH1   . ARG A 685 ? 0.9109 0.7952 1.2705 -0.1735 -0.0431 0.0353  685 ARG A NH1   
5634 N  NH2   . ARG A 685 ? 0.9870 0.9084 1.3587 -0.1716 -0.0341 0.0655  685 ARG A NH2   
5635 N  N     . LEU A 686 ? 1.0110 0.9999 1.3311 -0.1751 -0.0518 0.0227  686 LEU A N     
5636 C  CA    . LEU A 686 ? 1.0251 1.0390 1.3427 -0.1724 -0.0491 0.0277  686 LEU A CA    
5637 C  C     . LEU A 686 ? 1.0438 1.0609 1.3553 -0.1757 -0.0571 0.0161  686 LEU A C     
5638 O  O     . LEU A 686 ? 1.0172 1.0525 1.3392 -0.1800 -0.0592 0.0217  686 LEU A O     
5639 C  CB    . LEU A 686 ? 0.9761 0.9975 1.2761 -0.1604 -0.0402 0.0291  686 LEU A CB    
5640 C  CG    . LEU A 686 ? 0.9593 1.0032 1.2640 -0.1568 -0.0320 0.0437  686 LEU A CG    
5641 C  CD1   . LEU A 686 ? 0.9181 0.9629 1.2420 -0.1618 -0.0291 0.0588  686 LEU A CD1   
5642 C  CD2   . LEU A 686 ? 0.8935 0.9409 1.1783 -0.1456 -0.0249 0.0422  686 LEU A CD2   
5643 N  N     . ALA A 687 ? 1.0481 1.0485 1.3427 -0.1736 -0.0613 0.0006  687 ALA A N     
5644 C  CA    . ALA A 687 ? 1.0496 1.0522 1.3369 -0.1771 -0.0696 -0.0104 687 ALA A CA    
5645 C  C     . ALA A 687 ? 1.0403 1.0401 1.3454 -0.1905 -0.0797 -0.0102 687 ALA A C     
5646 O  O     . ALA A 687 ? 1.0410 1.0536 1.3496 -0.1954 -0.0863 -0.0114 687 ALA A O     
5647 C  CB    . ALA A 687 ? 0.9436 0.9279 1.2084 -0.1718 -0.0711 -0.0266 687 ALA A CB    
5648 N  N     . ALA A 688 ? 1.0028 0.9858 1.3205 -0.1967 -0.0815 -0.0083 688 ALA A N     
5649 C  CA    . ALA A 688 ? 1.1160 1.0964 1.4536 -0.2104 -0.0912 -0.0065 688 ALA A CA    
5650 C  C     . ALA A 688 ? 1.1591 1.1657 1.5188 -0.2148 -0.0898 0.0104  688 ALA A C     
5651 O  O     . ALA A 688 ? 1.0886 1.1017 1.4638 -0.2256 -0.0989 0.0122  688 ALA A O     
5652 C  CB    . ALA A 688 ? 1.0632 1.0194 1.4111 -0.2153 -0.0921 -0.0068 688 ALA A CB    
5653 N  N     . ARG A 689 ? 1.2710 1.2931 1.6322 -0.2066 -0.0786 0.0230  689 ARG A N     
5654 C  CA    . ARG A 689 ? 1.1172 1.1657 1.4965 -0.2085 -0.0750 0.0388  689 ARG A CA    
5655 C  C     . ARG A 689 ? 1.0746 1.1435 1.4450 -0.2034 -0.0745 0.0368  689 ARG A C     
5656 O  O     . ARG A 689 ? 1.0754 1.1674 1.4585 -0.2025 -0.0695 0.0495  689 ARG A O     
5657 C  CB    . ARG A 689 ? 1.1381 1.1940 1.5222 -0.2022 -0.0628 0.0535  689 ARG A CB    
5658 C  CG    . ARG A 689 ? 1.1952 1.2420 1.6007 -0.2101 -0.0632 0.0640  689 ARG A CG    
5659 C  CD    . ARG A 689 ? 1.2353 1.2795 1.6363 -0.2020 -0.0524 0.0730  689 ARG A CD    
5660 N  NE    . ARG A 689 ? 1.2090 1.2754 1.6013 -0.1926 -0.0423 0.0810  689 ARG A NE    
5661 C  CZ    . ARG A 689 ? 1.2801 1.3577 1.6783 -0.1890 -0.0329 0.0965  689 ARG A CZ    
5662 N  NH1   . ARG A 689 ? 1.3857 1.4556 1.7998 -0.1940 -0.0319 0.1072  689 ARG A NH1   
5663 N  NH2   . ARG A 689 ? 1.2592 1.3557 1.6467 -0.1803 -0.0241 0.1013  689 ARG A NH2   
5664 N  N     . GLY A 690 ? 1.0682 1.1293 1.4177 -0.1997 -0.0788 0.0218  690 GLY A N     
5665 C  CA    . GLY A 690 ? 0.9853 1.0648 1.3271 -0.1947 -0.0786 0.0203  690 GLY A CA    
5666 C  C     . GLY A 690 ? 1.0091 1.1004 1.3397 -0.1820 -0.0662 0.0254  690 GLY A C     
5667 O  O     . GLY A 690 ? 0.9661 1.0790 1.3030 -0.1790 -0.0622 0.0331  690 GLY A O     
5668 N  N     . VAL A 691 ? 1.0476 1.1251 1.3623 -0.1745 -0.0601 0.0212  691 VAL A N     
5669 C  CA    . VAL A 691 ? 0.9398 1.0258 1.2415 -0.1629 -0.0494 0.0243  691 VAL A CA    
5670 C  C     . VAL A 691 ? 0.9671 1.0432 1.2451 -0.1559 -0.0505 0.0103  691 VAL A C     
5671 O  O     . VAL A 691 ? 0.9662 1.0229 1.2353 -0.1574 -0.0554 -0.0002 691 VAL A O     
5672 C  CB    . VAL A 691 ? 0.8975 0.9780 1.2010 -0.1600 -0.0414 0.0328  691 VAL A CB    
5673 C  CG1   . VAL A 691 ? 0.9031 0.9932 1.1925 -0.1488 -0.0314 0.0358  691 VAL A CG1   
5674 C  CG2   . VAL A 691 ? 0.9963 1.0860 1.3245 -0.1677 -0.0406 0.0474  691 VAL A CG2   
5675 N  N     . LYS A 692 ? 0.9928 1.0821 1.2611 -0.1479 -0.0457 0.0103  692 LYS A N     
5676 C  CA    . LYS A 692 ? 1.0179 1.1002 1.2652 -0.1411 -0.0463 -0.0015 692 LYS A CA    
5677 C  C     . LYS A 692 ? 1.0596 1.1261 1.2937 -0.1353 -0.0416 -0.0052 692 LYS A C     
5678 O  O     . LYS A 692 ? 1.1199 1.1905 1.3534 -0.1304 -0.0338 0.0023  692 LYS A O     
5679 C  CB    . LYS A 692 ? 1.0242 1.1238 1.2664 -0.1339 -0.0414 0.0008  692 LYS A CB    
5680 C  CG    . LYS A 692 ? 1.1226 1.2203 1.3508 -0.1308 -0.0460 -0.0098 692 LYS A CG    
5681 C  CD    . LYS A 692 ? 1.1007 1.2032 1.3150 -0.1202 -0.0385 -0.0109 692 LYS A CD    
5682 C  CE    . LYS A 692 ? 1.1189 1.2260 1.3250 -0.1176 -0.0425 -0.0174 692 LYS A CE    
5683 N  NZ    . LYS A 692 ? 0.9139 1.0323 1.1152 -0.1090 -0.0353 -0.0146 692 LYS A NZ    
5684 N  N     . ILE A 693 ? 1.0905 1.1394 1.3137 -0.1357 -0.0463 -0.0166 693 ILE A N     
5685 C  CA    . ILE A 693 ? 1.1205 1.1539 1.3326 -0.1302 -0.0424 -0.0206 693 ILE A CA    
5686 C  C     . ILE A 693 ? 1.1391 1.1651 1.3329 -0.1253 -0.0444 -0.0330 693 ILE A C     
5687 O  O     . ILE A 693 ? 1.1770 1.1963 1.3676 -0.1297 -0.0515 -0.0417 693 ILE A O     
5688 C  CB    . ILE A 693 ? 1.1016 1.1178 1.3228 -0.1360 -0.0449 -0.0205 693 ILE A CB    
5689 C  CG1   . ILE A 693 ? 0.9861 1.0080 1.2211 -0.1370 -0.0394 -0.0064 693 ILE A CG1   
5690 C  CG2   . ILE A 693 ? 1.0668 1.0635 1.2747 -0.1312 -0.0440 -0.0299 693 ILE A CG2   
5691 C  CD1   . ILE A 693 ? 0.9844 1.0098 1.2100 -0.1279 -0.0312 -0.0016 693 ILE A CD1   
5692 N  N     . ARG A 694 ? 1.1071 1.1348 1.2889 -0.1164 -0.0385 -0.0335 694 ARG A N     
5693 C  CA    . ARG A 694 ? 1.2396 1.2639 1.4051 -0.1109 -0.0391 -0.0430 694 ARG A CA    
5694 C  C     . ARG A 694 ? 1.1947 1.2102 1.3509 -0.1035 -0.0334 -0.0441 694 ARG A C     
5695 O  O     . ARG A 694 ? 1.0999 1.1167 1.2612 -0.1017 -0.0287 -0.0361 694 ARG A O     
5696 C  CB    . ARG A 694 ? 1.2572 1.2988 1.4197 -0.1078 -0.0382 -0.0413 694 ARG A CB    
5697 C  CG    . ARG A 694 ? 1.4227 1.4688 1.5847 -0.1122 -0.0456 -0.0466 694 ARG A CG    
5698 C  CD    . ARG A 694 ? 1.5351 1.5760 1.6802 -0.1073 -0.0468 -0.0560 694 ARG A CD    
5699 N  NE    . ARG A 694 ? 1.7234 1.7720 1.8670 -0.1106 -0.0535 -0.0593 694 ARG A NE    
5700 C  CZ    . ARG A 694 ? 1.6915 1.7549 1.8347 -0.1072 -0.0527 -0.0562 694 ARG A CZ    
5701 N  NH1   . ARG A 694 ? 1.5396 1.6107 1.6828 -0.1005 -0.0455 -0.0508 694 ARG A NH1   
5702 N  NH2   . ARG A 694 ? 1.5861 1.6563 1.7286 -0.1107 -0.0597 -0.0585 694 ARG A NH2   
5703 N  N     . PRO A 695 ? 1.0912 1.0981 1.2340 -0.0991 -0.0337 -0.0531 695 PRO A N     
5704 C  CA    . PRO A 695 ? 0.9804 0.9812 1.1158 -0.0916 -0.0283 -0.0532 695 PRO A CA    
5705 C  C     . PRO A 695 ? 1.0600 1.0741 1.1942 -0.0867 -0.0235 -0.0459 695 PRO A C     
5706 O  O     . PRO A 695 ? 1.1145 1.1378 1.2420 -0.0834 -0.0230 -0.0476 695 PRO A O     
5707 C  CB    . PRO A 695 ? 0.9328 0.9271 1.0545 -0.0880 -0.0295 -0.0636 695 PRO A CB    
5708 C  CG    . PRO A 695 ? 1.1251 1.1141 1.2471 -0.0948 -0.0361 -0.0703 695 PRO A CG    
5709 C  CD    . PRO A 695 ? 1.1678 1.1691 1.3026 -0.1013 -0.0393 -0.0634 695 PRO A CD    
5710 N  N     . GLY A 696 ? 1.0097 1.0243 1.1501 -0.0862 -0.0200 -0.0377 696 GLY A N     
5711 C  CA    . GLY A 696 ? 0.9470 0.9728 1.0845 -0.0819 -0.0157 -0.0312 696 GLY A CA    
5712 C  C     . GLY A 696 ? 0.9406 0.9729 1.0875 -0.0847 -0.0133 -0.0207 696 GLY A C     
5713 O  O     . GLY A 696 ? 0.9671 1.0036 1.1109 -0.0813 -0.0096 -0.0149 696 GLY A O     
5714 N  N     . THR A 697 ? 0.8962 0.9298 1.0544 -0.0912 -0.0156 -0.0179 697 THR A N     
5715 C  CA    . THR A 697 ? 0.8857 0.9267 1.0540 -0.0941 -0.0128 -0.0068 697 THR A CA    
5716 C  C     . THR A 697 ? 0.9303 0.9616 1.1020 -0.0937 -0.0112 -0.0013 697 THR A C     
5717 O  O     . THR A 697 ? 0.8449 0.8616 1.0164 -0.0933 -0.0132 -0.0063 697 THR A O     
5718 C  CB    . THR A 697 ? 0.8933 0.9379 1.0754 -0.1018 -0.0161 -0.0044 697 THR A CB    
5719 O  OG1   . THR A 697 ? 0.8360 0.8664 1.0269 -0.1068 -0.0193 -0.0048 697 THR A OG1   
5720 C  CG2   . THR A 697 ? 0.9726 1.0212 1.1518 -0.1030 -0.0203 -0.0125 697 THR A CG2   
5721 N  N     . VAL A 698 ? 0.8474 0.8872 1.0221 -0.0933 -0.0072 0.0095  698 VAL A N     
5722 C  CA    . VAL A 698 ? 0.7112 0.7449 0.8894 -0.0924 -0.0054 0.0172  698 VAL A CA    
5723 C  C     . VAL A 698 ? 0.7625 0.7973 0.9566 -0.0988 -0.0052 0.0270  698 VAL A C     
5724 O  O     . VAL A 698 ? 0.7635 0.8120 0.9617 -0.1009 -0.0026 0.0342  698 VAL A O     
5725 C  CB    . VAL A 698 ? 0.7848 0.8276 0.9523 -0.0869 -0.0015 0.0227  698 VAL A CB    
5726 C  CG1   . VAL A 698 ? 0.7859 0.8290 0.9597 -0.0879 0.0007  0.0353  698 VAL A CG1   
5727 C  CG2   . VAL A 698 ? 0.7948 0.8316 0.9504 -0.0812 -0.0024 0.0148  698 VAL A CG2   
5728 N  N     . ILE A 699 ? 0.7574 0.7776 0.9612 -0.1017 -0.0075 0.0275  699 ILE A N     
5729 C  CA    . ILE A 699 ? 0.7096 0.7283 0.9304 -0.1080 -0.0075 0.0376  699 ILE A CA    
5730 C  C     . ILE A 699 ? 0.7543 0.7765 0.9764 -0.1053 -0.0034 0.0507  699 ILE A C     
5731 O  O     . ILE A 699 ? 0.7792 0.7931 0.9965 -0.1007 -0.0030 0.0503  699 ILE A O     
5732 C  CB    . ILE A 699 ? 0.7233 0.7225 0.9539 -0.1126 -0.0122 0.0314  699 ILE A CB    
5733 C  CG1   . ILE A 699 ? 0.7754 0.7736 1.0061 -0.1172 -0.0172 0.0205  699 ILE A CG1   
5734 C  CG2   . ILE A 699 ? 0.7006 0.6952 0.9495 -0.1180 -0.0118 0.0432  699 ILE A CG2   
5735 C  CD1   . ILE A 699 ? 0.8554 0.8396 1.0746 -0.1142 -0.0202 0.0057  699 ILE A CD1   
5736 N  N     . SER A 700 ? 0.7379 0.7733 0.9669 -0.1081 -0.0001 0.0629  700 SER A N     
5737 C  CA    . SER A 700 ? 0.7556 0.7964 0.9859 -0.1064 0.0037  0.0771  700 SER A CA    
5738 C  C     . SER A 700 ? 0.7207 0.7581 0.9716 -0.1132 0.0036  0.0884  700 SER A C     
5739 O  O     . SER A 700 ? 0.8012 0.8487 1.0614 -0.1182 0.0048  0.0936  700 SER A O     
5740 C  CB    . SER A 700 ? 0.7408 0.8009 0.9589 -0.1031 0.0087  0.0824  700 SER A CB    
5741 O  OG    . SER A 700 ? 0.6569 0.7194 0.8583 -0.0980 0.0082  0.0707  700 SER A OG    
5742 N  N     . TYR A 701 ? 0.6691 0.6926 0.9287 -0.1134 0.0024  0.0927  701 TYR A N     
5743 C  CA    . TYR A 701 ? 0.7210 0.7372 1.0020 -0.1202 0.0015  0.1020  701 TYR A CA    
5744 C  C     . TYR A 701 ? 0.7375 0.7544 1.0249 -0.1186 0.0045  0.1183  701 TYR A C     
5745 O  O     . TYR A 701 ? 0.7489 0.7683 1.0245 -0.1121 0.0061  0.1207  701 TYR A O     
5746 C  CB    . TYR A 701 ? 0.7125 0.7065 1.0025 -0.1236 -0.0038 0.0903  701 TYR A CB    
5747 C  CG    . TYR A 701 ? 0.7353 0.7129 1.0196 -0.1176 -0.0045 0.0840  701 TYR A CG    
5748 C  CD1   . TYR A 701 ? 0.7117 0.6783 1.0084 -0.1169 -0.0034 0.0937  701 TYR A CD1   
5749 C  CD2   . TYR A 701 ? 0.7300 0.7036 0.9980 -0.1123 -0.0057 0.0692  701 TYR A CD2   
5750 C  CE1   . TYR A 701 ? 0.7326 0.6849 1.0259 -0.1108 -0.0034 0.0887  701 TYR A CE1   
5751 C  CE2   . TYR A 701 ? 0.7950 0.7548 1.0592 -0.1063 -0.0055 0.0642  701 TYR A CE2   
5752 C  CZ    . TYR A 701 ? 0.7654 0.7148 1.0425 -0.1054 -0.0042 0.0739  701 TYR A CZ    
5753 O  OH    . TYR A 701 ? 0.7293 0.6657 1.0043 -0.0989 -0.0034 0.0697  701 TYR A OH    
5754 N  N     . ILE A 702 ? 0.7081 0.7232 1.0155 -0.1250 0.0049  0.1302  702 ILE A N     
5755 C  CA    . ILE A 702 ? 0.7245 0.7377 1.0432 -0.1249 0.0071  0.1470  702 ILE A CA    
5756 C  C     . ILE A 702 ? 0.7409 0.7327 1.0813 -0.1304 0.0036  0.1469  702 ILE A C     
5757 O  O     . ILE A 702 ? 0.7821 0.7682 1.1336 -0.1375 0.0005  0.1410  702 ILE A O     
5758 C  CB    . ILE A 702 ? 0.7195 0.7534 1.0422 -0.1273 0.0122  0.1651  702 ILE A CB    
5759 C  CG1   . ILE A 702 ? 0.9521 1.0048 1.2515 -0.1207 0.0162  0.1662  702 ILE A CG1   
5760 C  CG2   . ILE A 702 ? 0.7249 0.7550 1.0648 -0.1293 0.0137  0.1837  702 ILE A CG2   
5761 C  CD1   . ILE A 702 ? 0.8054 0.8754 1.1052 -0.1207 0.0218  0.1862  702 ILE A CD1   
5762 N  N     . VAL A 703 ? 0.6716 0.6513 1.0184 -0.1271 0.0040  0.1532  703 VAL A N     
5763 C  CA    . VAL A 703 ? 0.7411 0.6992 1.1097 -0.1315 0.0017  0.1552  703 VAL A CA    
5764 C  C     . VAL A 703 ? 0.7344 0.6999 1.1226 -0.1370 0.0041  0.1764  703 VAL A C     
5765 O  O     . VAL A 703 ? 0.7680 0.7484 1.1530 -0.1336 0.0081  0.1924  703 VAL A O     
5766 C  CB    . VAL A 703 ? 0.7211 0.6626 1.0889 -0.1243 0.0017  0.1526  703 VAL A CB    
5767 C  CG1   . VAL A 703 ? 0.7594 0.6788 1.1514 -0.1281 0.0006  0.1578  703 VAL A CG1   
5768 C  CG2   . VAL A 703 ? 0.6935 0.6260 1.0444 -0.1194 -0.0004 0.1314  703 VAL A CG2   
5769 N  N     . LEU A 704 ? 0.7381 0.6937 1.1465 -0.1459 0.0014  0.1770  704 LEU A N     
5770 C  CA    . LEU A 704 ? 0.7584 0.7207 1.1883 -0.1525 0.0034  0.1972  704 LEU A CA    
5771 C  C     . LEU A 704 ? 0.7710 0.7102 1.2230 -0.1546 0.0020  0.2037  704 LEU A C     
5772 O  O     . LEU A 704 ? 0.8131 0.7288 1.2661 -0.1531 -0.0013 0.1894  704 LEU A O     
5773 C  CB    . LEU A 704 ? 0.7295 0.6989 1.1700 -0.1621 0.0013  0.1954  704 LEU A CB    
5774 C  CG    . LEU A 704 ? 0.7355 0.7323 1.1623 -0.1613 0.0047  0.1971  704 LEU A CG    
5775 C  CD1   . LEU A 704 ? 0.8356 0.8529 1.2528 -0.1554 0.0118  0.2143  704 LEU A CD1   
5776 C  CD2   . LEU A 704 ? 0.7799 0.7761 1.1838 -0.1566 0.0022  0.1760  704 LEU A CD2   
5777 N  N     . LYS A 705 ? 0.7936 0.7397 1.2635 -0.1577 0.0050  0.2258  705 LYS A N     
5778 C  CA    . LYS A 705 ? 0.8118 0.7367 1.3067 -0.1607 0.0040  0.2348  705 LYS A CA    
5779 C  C     . LYS A 705 ? 0.9937 0.8969 1.5046 -0.1700 -0.0018 0.2217  705 LYS A C     
5780 O  O     . LYS A 705 ? 0.9759 0.8882 1.4952 -0.1787 -0.0037 0.2230  705 LYS A O     
5781 C  CB    . LYS A 705 ? 0.7787 0.7184 1.2904 -0.1637 0.0083  0.2622  705 LYS A CB    
5782 C  CG    . LYS A 705 ? 0.8451 0.7722 1.3717 -0.1601 0.0099  0.2772  705 LYS A CG    
5783 C  CD    . LYS A 705 ? 0.8658 0.8024 1.4163 -0.1664 0.0128  0.3032  705 LYS A CD    
5784 C  CE    . LYS A 705 ? 0.8466 0.7810 1.4062 -0.1608 0.0157  0.3230  705 LYS A CE    
5785 N  NZ    . LYS A 705 ? 0.9090 0.8713 1.4683 -0.1610 0.0209  0.3483  705 LYS A NZ    
5786 N  N     . GLY A 706 ? 1.1514 1.0262 1.6667 -0.1682 -0.0047 0.2090  706 GLY A N     
5787 C  CA    . GLY A 706 ? 1.3675 1.2200 1.8951 -0.1772 -0.0109 0.1945  706 GLY A CA    
5788 C  C     . GLY A 706 ? 1.4913 1.3105 2.0218 -0.1743 -0.0132 0.1793  706 GLY A C     
5789 O  O     . GLY A 706 ? 1.4040 1.2118 1.9418 -0.1678 -0.0097 0.1873  706 GLY A O     
5790 N  N     . SER A 707 ? 1.6891 1.4929 2.2131 -0.1789 -0.0190 0.1572  707 SER A N     
5791 C  CA    . SER A 707 ? 1.4841 1.2531 2.0150 -0.1799 -0.0222 0.1417  707 SER A CA    
5792 C  C     . SER A 707 ? 1.3744 1.1345 1.8798 -0.1693 -0.0207 0.1218  707 SER A C     
5793 O  O     . SER A 707 ? 1.3331 1.0914 1.8211 -0.1709 -0.0248 0.1022  707 SER A O     
5794 C  CB    . SER A 707 ? 1.4122 1.1689 1.9533 -0.1933 -0.0303 0.1306  707 SER A CB    
5795 O  OG    . SER A 707 ? 1.3190 1.0932 1.8414 -0.1960 -0.0340 0.1189  707 SER A OG    
5796 N  N     . GLY A 708 ? 1.3307 1.0859 1.8349 -0.1585 -0.0150 0.1278  708 GLY A N     
5797 C  CA    . GLY A 708 ? 1.3258 1.0671 1.8122 -0.1484 -0.0129 0.1103  708 GLY A CA    
5798 C  C     . GLY A 708 ? 1.3622 1.1223 1.8201 -0.1443 -0.0134 0.0977  708 GLY A C     
5799 O  O     . GLY A 708 ? 1.5494 1.3358 1.9972 -0.1399 -0.0106 0.1083  708 GLY A O     
5800 N  N     . ARG A 709 ? 1.1471 0.8927 1.5915 -0.1459 -0.0172 0.0748  709 ARG A N     
5801 C  CA    . ARG A 709 ? 1.0175 0.7756 1.4349 -0.1419 -0.0180 0.0599  709 ARG A CA    
5802 C  C     . ARG A 709 ? 1.0079 0.7999 1.4166 -0.1418 -0.0172 0.0715  709 ARG A C     
5803 O  O     . ARG A 709 ? 1.0214 0.8264 1.4370 -0.1509 -0.0206 0.0776  709 ARG A O     
5804 C  CB    . ARG A 709 ? 0.9900 0.7350 1.4001 -0.1500 -0.0250 0.0395  709 ARG A CB    
5805 C  CG    . ARG A 709 ? 0.9705 0.6970 1.3614 -0.1431 -0.0242 0.0175  709 ARG A CG    
5806 C  CD    . ARG A 709 ? 1.0130 0.7096 1.4085 -0.1507 -0.0296 0.0010  709 ARG A CD    
5807 N  NE    . ARG A 709 ? 1.1134 0.8086 1.4865 -0.1528 -0.0346 -0.0198 709 ARG A NE    
5808 C  CZ    . ARG A 709 ? 1.0415 0.7517 1.4103 -0.1622 -0.0418 -0.0224 709 ARG A CZ    
5809 N  NH1   . ARG A 709 ? 1.0086 0.7365 1.3941 -0.1703 -0.0445 -0.0062 709 ARG A NH1   
5810 N  NH2   . ARG A 709 ? 1.0519 0.7600 1.3998 -0.1633 -0.0462 -0.0411 709 ARG A NH2   
5811 N  N     . ILE A 710 ? 0.9385 0.7445 1.3327 -0.1316 -0.0126 0.0747  710 ILE A N     
5812 C  CA    . ILE A 710 ? 0.9342 0.7708 1.3203 -0.1305 -0.0109 0.0869  710 ILE A CA    
5813 C  C     . ILE A 710 ? 0.8825 0.7325 1.2576 -0.1368 -0.0151 0.0777  710 ILE A C     
5814 O  O     . ILE A 710 ? 0.9201 0.7900 1.2996 -0.1418 -0.0152 0.0891  710 ILE A O     
5815 C  CB    . ILE A 710 ? 0.8892 0.7356 1.2596 -0.1189 -0.0065 0.0882  710 ILE A CB    
5816 C  CG1   . ILE A 710 ? 0.9059 0.7557 1.2893 -0.1145 -0.0025 0.1084  710 ILE A CG1   
5817 C  CG2   . ILE A 710 ? 0.7996 0.6721 1.1512 -0.1178 -0.0065 0.0877  710 ILE A CG2   
5818 C  CD1   . ILE A 710 ? 0.9089 0.7329 1.3128 -0.1143 -0.0015 0.1111  710 ILE A CD1   
5819 N  N     . GLY A 711 ? 0.8496 0.6894 1.2109 -0.1364 -0.0182 0.0576  711 GLY A N     
5820 C  CA    . GLY A 711 ? 0.8721 0.7238 1.2238 -0.1422 -0.0228 0.0486  711 GLY A CA    
5821 C  C     . GLY A 711 ? 0.8638 0.7164 1.2337 -0.1545 -0.0277 0.0540  711 GLY A C     
5822 O  O     . GLY A 711 ? 0.8754 0.7456 1.2421 -0.1594 -0.0304 0.0539  711 GLY A O     
5823 N  N     . ASP A 712 ? 0.9136 0.7475 1.3039 -0.1596 -0.0289 0.0592  712 ASP A N     
5824 C  CA    . ASP A 712 ? 0.9386 0.7736 1.3493 -0.1720 -0.0336 0.0663  712 ASP A CA    
5825 C  C     . ASP A 712 ? 0.9263 0.7861 1.3487 -0.1736 -0.0296 0.0890  712 ASP A C     
5826 O  O     . ASP A 712 ? 0.9104 0.7827 1.3442 -0.1825 -0.0326 0.0952  712 ASP A O     
5827 C  CB    . ASP A 712 ? 0.8960 0.7015 1.3258 -0.1773 -0.0363 0.0646  712 ASP A CB    
5828 C  CG    . ASP A 712 ? 0.8451 0.6255 1.2645 -0.1789 -0.0417 0.0409  712 ASP A CG    
5829 O  OD1   . ASP A 712 ? 0.8888 0.6768 1.2897 -0.1792 -0.0452 0.0272  712 ASP A OD1   
5830 O  OD2   . ASP A 712 ? 0.9589 0.7116 1.3883 -0.1799 -0.0422 0.0359  712 ASP A OD2   
5831 N  N     . ARG A 713 ? 0.8677 0.7359 1.2875 -0.1651 -0.0228 0.1018  713 ARG A N     
5832 C  CA    . ARG A 713 ? 0.8221 0.7127 1.2514 -0.1660 -0.0183 0.1239  713 ARG A CA    
5833 C  C     . ARG A 713 ? 0.8114 0.7280 1.2196 -0.1586 -0.0139 0.1265  713 ARG A C     
5834 O  O     . ARG A 713 ? 0.8329 0.7673 1.2431 -0.1565 -0.0088 0.1439  713 ARG A O     
5835 C  CB    . ARG A 713 ? 0.8912 0.7726 1.3358 -0.1632 -0.0144 0.1398  713 ARG A CB    
5836 C  CG    . ARG A 713 ? 1.0191 0.8773 1.4587 -0.1554 -0.0135 0.1302  713 ARG A CG    
5837 C  CD    . ARG A 713 ? 1.0676 0.9239 1.5207 -0.1509 -0.0088 0.1494  713 ARG A CD    
5838 N  NE    . ARG A 713 ? 1.1295 0.9630 1.5828 -0.1434 -0.0075 0.1424  713 ARG A NE    
5839 C  CZ    . ARG A 713 ? 1.1262 0.9612 1.5828 -0.1355 -0.0032 0.1554  713 ARG A CZ    
5840 N  NH1   . ARG A 713 ? 1.0086 0.8667 1.4656 -0.1340 -0.0001 0.1752  713 ARG A NH1   
5841 N  NH2   . ARG A 713 ? 1.2675 1.0808 1.7269 -0.1288 -0.0017 0.1486  713 ARG A NH2   
5842 N  N     . ALA A 714 ? 0.7524 0.6711 1.1401 -0.1549 -0.0157 0.1095  714 ALA A N     
5843 C  CA    . ALA A 714 ? 0.8281 0.7688 1.1953 -0.1480 -0.0120 0.1097  714 ALA A CA    
5844 C  C     . ALA A 714 ? 0.8598 0.8172 1.2245 -0.1532 -0.0139 0.1061  714 ALA A C     
5845 O  O     . ALA A 714 ? 0.8346 0.7832 1.2009 -0.1587 -0.0198 0.0932  714 ALA A O     
5846 C  CB    . ALA A 714 ? 0.7761 0.7085 1.1229 -0.1391 -0.0119 0.0947  714 ALA A CB    
5847 N  N     . ILE A 715 ? 0.8730 0.8543 1.2332 -0.1513 -0.0091 0.1176  715 ILE A N     
5848 C  CA    . ILE A 715 ? 0.8199 0.8191 1.1780 -0.1547 -0.0096 0.1154  715 ILE A CA    
5849 C  C     . ILE A 715 ? 0.8100 0.8271 1.1459 -0.1461 -0.0046 0.1140  715 ILE A C     
5850 O  O     . ILE A 715 ? 0.7424 0.7630 1.0689 -0.1394 -0.0002 0.1208  715 ILE A O     
5851 C  CB    . ILE A 715 ? 0.8306 0.8424 1.2104 -0.1626 -0.0079 0.1321  715 ILE A CB    
5852 C  CG1   . ILE A 715 ? 0.8236 0.8496 1.2033 -0.1584 -0.0001 0.1511  715 ILE A CG1   
5853 C  CG2   . ILE A 715 ? 0.8361 0.8292 1.2392 -0.1723 -0.0138 0.1329  715 ILE A CG2   
5854 C  CD1   . ILE A 715 ? 0.8433 0.8905 1.2367 -0.1633 0.0043  0.1672  715 ILE A CD1   
5855 N  N     . PRO A 716 ? 0.8824 0.9110 1.2100 -0.1461 -0.0055 0.1057  716 PRO A N     
5856 C  CA    . PRO A 716 ? 0.8351 0.8806 1.1431 -0.1383 -0.0003 0.1052  716 PRO A CA    
5857 C  C     . PRO A 716 ? 0.8396 0.9029 1.1502 -0.1369 0.0071  0.1230  716 PRO A C     
5858 O  O     . PRO A 716 ? 0.8582 0.9279 1.1872 -0.1431 0.0085  0.1357  716 PRO A O     
5859 C  CB    . PRO A 716 ? 0.8527 0.9072 1.1586 -0.1404 -0.0028 0.0957  716 PRO A CB    
5860 C  CG    . PRO A 716 ? 0.8567 0.8949 1.1744 -0.1479 -0.0109 0.0866  716 PRO A CG    
5861 C  CD    . PRO A 716 ? 0.8407 0.8670 1.1766 -0.1533 -0.0117 0.0965  716 PRO A CD    
5862 N  N     . PHE A 717 ? 0.8574 0.9289 1.1487 -0.1289 0.0116  0.1240  717 PHE A N     
5863 C  CA    . PHE A 717 ? 0.8824 0.9694 1.1720 -0.1269 0.0186  0.1403  717 PHE A CA    
5864 C  C     . PHE A 717 ? 0.8469 0.9540 1.1411 -0.1289 0.0238  0.1471  717 PHE A C     
5865 O  O     . PHE A 717 ? 0.8354 0.9549 1.1355 -0.1297 0.0297  0.1632  717 PHE A O     
5866 C  CB    . PHE A 717 ? 0.8001 0.8906 1.0662 -0.1184 0.0212  0.1383  717 PHE A CB    
5867 C  CG    . PHE A 717 ? 0.7842 0.8892 1.0456 -0.1162 0.0276  0.1546  717 PHE A CG    
5868 C  CD1   . PHE A 717 ? 0.7693 0.8731 1.0466 -0.1200 0.0288  0.1708  717 PHE A CD1   
5869 C  CD2   . PHE A 717 ? 0.8205 0.9398 1.0610 -0.1104 0.0326  0.1538  717 PHE A CD2   
5870 C  CE1   . PHE A 717 ? 0.8188 0.9368 1.0906 -0.1180 0.0347  0.1867  717 PHE A CE1   
5871 C  CE2   . PHE A 717 ? 0.8753 1.0078 1.1088 -0.1084 0.0384  0.1684  717 PHE A CE2   
5872 C  CZ    . PHE A 717 ? 0.8273 0.9599 1.0762 -0.1122 0.0395  0.1852  717 PHE A CZ    
5873 N  N     . ASP A 718 ? 0.9214 1.0329 1.2135 -0.1292 0.0223  0.1362  718 ASP A N     
5874 C  CA    . ASP A 718 ? 0.9847 1.1158 1.2839 -0.1307 0.0276  0.1431  718 ASP A CA    
5875 C  C     . ASP A 718 ? 0.8872 1.0211 1.2141 -0.1399 0.0268  0.1557  718 ASP A C     
5876 O  O     . ASP A 718 ? 0.9586 1.1106 1.2941 -0.1409 0.0334  0.1682  718 ASP A O     
5877 C  CB    . ASP A 718 ? 0.9914 1.1262 1.2844 -0.1290 0.0254  0.1291  718 ASP A CB    
5878 C  CG    . ASP A 718 ? 1.1751 1.2944 1.4773 -0.1348 0.0156  0.1173  718 ASP A CG    
5879 O  OD1   . ASP A 718 ? 1.2609 1.3799 1.5541 -0.1324 0.0127  0.1044  718 ASP A OD1   
5880 O  OD2   . ASP A 718 ? 1.2267 1.3336 1.5444 -0.1415 0.0108  0.1204  718 ASP A OD2   
5881 N  N     . GLU A 719 ? 0.9244 1.0403 1.2655 -0.1464 0.0191  0.1526  719 GLU A N     
5882 C  CA    . GLU A 719 ? 0.8534 0.9686 1.2221 -0.1562 0.0169  0.1636  719 GLU A CA    
5883 C  C     . GLU A 719 ? 0.8633 0.9761 1.2413 -0.1575 0.0204  0.1804  719 GLU A C     
5884 O  O     . GLU A 719 ? 0.9320 1.0414 1.3343 -0.1659 0.0182  0.1903  719 GLU A O     
5885 C  CB    . GLU A 719 ? 0.8359 0.9313 1.2151 -0.1633 0.0062  0.1509  719 GLU A CB    
5886 C  CG    . GLU A 719 ? 0.9590 1.0576 1.3326 -0.1638 0.0015  0.1363  719 GLU A CG    
5887 C  CD    . GLU A 719 ? 1.0392 1.1154 1.4131 -0.1682 -0.0088 0.1204  719 GLU A CD    
5888 O  OE1   . GLU A 719 ? 1.0496 1.1091 1.4371 -0.1743 -0.0130 0.1224  719 GLU A OE1   
5889 O  OE2   . GLU A 719 ? 1.0370 1.1117 1.3972 -0.1654 -0.0123 0.1058  719 GLU A OE2   
5890 N  N     . PHE A 720 ? 0.8990 1.0136 1.2590 -0.1497 0.0253  0.1842  720 PHE A N     
5891 C  CA    . PHE A 720 ? 0.9375 1.0505 1.3051 -0.1503 0.0283  0.2009  720 PHE A CA    
5892 C  C     . PHE A 720 ? 1.0599 1.1959 1.4350 -0.1513 0.0371  0.2199  720 PHE A C     
5893 O  O     . PHE A 720 ? 1.0783 1.2313 1.4354 -0.1448 0.0441  0.2213  720 PHE A O     
5894 C  CB    . PHE A 720 ? 0.8705 0.9778 1.2162 -0.1420 0.0292  0.1982  720 PHE A CB    
5895 C  CG    . PHE A 720 ? 0.8933 1.0000 1.2458 -0.1419 0.0320  0.2162  720 PHE A CG    
5896 C  CD1   . PHE A 720 ? 0.8903 0.9773 1.2591 -0.1456 0.0270  0.2187  720 PHE A CD1   
5897 C  CD2   . PHE A 720 ? 0.9058 1.0317 1.2481 -0.1380 0.0398  0.2308  720 PHE A CD2   
5898 C  CE1   . PHE A 720 ? 0.8772 0.9640 1.2537 -0.1453 0.0295  0.2365  720 PHE A CE1   
5899 C  CE2   . PHE A 720 ? 0.8835 1.0099 1.2317 -0.1380 0.0419  0.2485  720 PHE A CE2   
5900 C  CZ    . PHE A 720 ? 0.8451 0.9523 1.2114 -0.1417 0.0367  0.2519  720 PHE A CZ    
5901 N  N     . ASP A 721 ? 1.1900 1.3263 1.5918 -0.1594 0.0369  0.2345  721 ASP A N     
5902 C  CA    . ASP A 721 ? 1.4270 1.5847 1.8389 -0.1608 0.0458  0.2553  721 ASP A CA    
5903 C  C     . ASP A 721 ? 1.3035 1.4574 1.7207 -0.1608 0.0480  0.2724  721 ASP A C     
5904 O  O     . ASP A 721 ? 1.2792 1.4174 1.7184 -0.1676 0.0427  0.2773  721 ASP A O     
5905 C  CB    . ASP A 721 ? 1.5028 1.6667 1.9440 -0.1705 0.0443  0.2616  721 ASP A CB    
5906 C  CG    . ASP A 721 ? 1.7153 1.8894 2.1523 -0.1699 0.0438  0.2492  721 ASP A CG    
5907 O  OD1   . ASP A 721 ? 1.8062 1.9860 2.2175 -0.1612 0.0471  0.2386  721 ASP A OD1   
5908 O  OD2   . ASP A 721 ? 1.4829 1.6594 1.9434 -0.1783 0.0399  0.2506  721 ASP A OD2   
5909 N  N     . PRO A 722 ? 1.1819 1.3491 1.5799 -0.1536 0.0554  0.2819  722 PRO A N     
5910 C  CA    . PRO A 722 ? 1.1462 1.3109 1.5490 -0.1534 0.0571  0.2995  722 PRO A CA    
5911 C  C     . PRO A 722 ? 1.2229 1.3903 1.6579 -0.1622 0.0586  0.3195  722 PRO A C     
5912 O  O     . PRO A 722 ? 1.2094 1.3657 1.6572 -0.1645 0.0564  0.3309  722 PRO A O     
5913 C  CB    . PRO A 722 ? 1.0939 1.2786 1.4697 -0.1451 0.0658  0.3069  722 PRO A CB    
5914 C  CG    . PRO A 722 ? 1.1235 1.3106 1.4752 -0.1392 0.0655  0.2863  722 PRO A CG    
5915 C  CD    . PRO A 722 ? 1.1391 1.3223 1.5084 -0.1450 0.0618  0.2757  722 PRO A CD    
5916 N  N     . THR A 723 ? 1.2608 1.4427 1.7110 -0.1671 0.0623  0.3247  723 THR A N     
5917 C  CA    . THR A 723 ? 1.3020 1.4886 1.7845 -0.1759 0.0641  0.3450  723 THR A CA    
5918 C  C     . THR A 723 ? 1.3211 1.4817 1.8290 -0.1848 0.0536  0.3405  723 THR A C     
5919 O  O     . THR A 723 ? 1.3310 1.4850 1.8597 -0.1896 0.0532  0.3568  723 THR A O     
5920 C  CB    . THR A 723 ? 1.3152 1.5232 1.8096 -0.1793 0.0697  0.3497  723 THR A CB    
5921 O  OG1   . THR A 723 ? 1.3973 1.5944 1.9030 -0.1851 0.0610  0.3326  723 THR A OG1   
5922 C  CG2   . THR A 723 ? 1.2329 1.4624 1.6983 -0.1693 0.0795  0.3474  723 THR A CG2   
5923 N  N     . LYS A 724 ? 1.3765 1.5214 1.8826 -0.1868 0.0450  0.3183  724 LYS A N     
5924 C  CA    . LYS A 724 ? 1.2429 1.3623 1.7714 -0.1955 0.0349  0.3114  724 LYS A CA    
5925 C  C     . LYS A 724 ? 1.1713 1.2658 1.6830 -0.1907 0.0281  0.2919  724 LYS A C     
5926 O  O     . LYS A 724 ? 1.1303 1.2029 1.6529 -0.1965 0.0194  0.2787  724 LYS A O     
5927 C  CB    . LYS A 724 ? 1.2010 1.3224 1.7464 -0.2043 0.0297  0.3031  724 LYS A CB    
5928 C  CG    . LYS A 724 ? 1.2280 1.3710 1.7566 -0.1994 0.0340  0.2955  724 LYS A CG    
5929 C  CD    . LYS A 724 ? 1.2385 1.3878 1.7896 -0.2090 0.0295  0.2934  724 LYS A CD    
5930 C  CE    . LYS A 724 ? 1.1300 1.2971 1.7102 -0.2161 0.0351  0.3180  724 LYS A CE    
5931 N  NZ    . LYS A 724 ? 0.9294 1.1072 1.5318 -0.2249 0.0312  0.3174  724 LYS A NZ    
5932 N  N     . HIS A 725 ? 1.1468 1.2443 1.6322 -0.1804 0.0318  0.2898  725 HIS A N     
5933 C  CA    . HIS A 725 ? 1.0207 1.0968 1.4906 -0.1751 0.0261  0.2724  725 HIS A CA    
5934 C  C     . HIS A 725 ? 0.9346 1.0101 1.3941 -0.1679 0.0296  0.2835  725 HIS A C     
5935 O  O     . HIS A 725 ? 0.9604 1.0566 1.4090 -0.1636 0.0368  0.2975  725 HIS A O     
5936 C  CB    . HIS A 725 ? 1.0093 1.0893 1.4533 -0.1694 0.0249  0.2514  725 HIS A CB    
5937 C  CG    . HIS A 725 ? 0.9928 1.0679 1.4458 -0.1760 0.0189  0.2371  725 HIS A CG    
5938 N  ND1   . HIS A 725 ? 0.9832 1.0763 1.4279 -0.1752 0.0212  0.2316  725 HIS A ND1   
5939 C  CD2   . HIS A 725 ? 0.9714 1.0255 1.4405 -0.1836 0.0105  0.2271  725 HIS A CD2   
5940 C  CE1   . HIS A 725 ? 1.0318 1.1166 1.4878 -0.1822 0.0139  0.2198  725 HIS A CE1   
5941 N  NE2   . HIS A 725 ? 0.9625 1.0234 1.4323 -0.1876 0.0071  0.2164  725 HIS A NE2   
5942 N  N     . ARG A 726 ? 0.9512 1.0033 1.4141 -0.1666 0.0245  0.2772  726 ARG A N     
5943 C  CA    . ARG A 726 ? 0.8861 0.9354 1.3417 -0.1598 0.0264  0.2870  726 ARG A CA    
5944 C  C     . ARG A 726 ? 0.8206 0.8497 1.2636 -0.1541 0.0212  0.2678  726 ARG A C     
5945 O  O     . ARG A 726 ? 0.7467 0.7525 1.2033 -0.1578 0.0159  0.2572  726 ARG A O     
5946 C  CB    . ARG A 726 ? 0.9084 0.9499 1.3918 -0.1647 0.0270  0.3076  726 ARG A CB    
5947 C  CG    . ARG A 726 ? 1.0044 1.0586 1.4816 -0.1591 0.0320  0.3282  726 ARG A CG    
5948 C  CD    . ARG A 726 ? 1.1293 1.1797 1.6364 -0.1650 0.0335  0.3514  726 ARG A CD    
5949 N  NE    . ARG A 726 ? 1.1845 1.2575 1.6861 -0.1619 0.0401  0.3753  726 ARG A NE    
5950 C  CZ    . ARG A 726 ? 1.2107 1.3101 1.7004 -0.1617 0.0466  0.3835  726 ARG A CZ    
5951 N  NH1   . ARG A 726 ? 1.1261 1.2337 1.6107 -0.1644 0.0476  0.3712  726 ARG A NH1   
5952 N  NH2   . ARG A 726 ? 1.2824 1.4005 1.7651 -0.1584 0.0524  0.4049  726 ARG A NH2   
5953 N  N     . TYR A 727 ? 0.7776 0.8154 1.1948 -0.1454 0.0228  0.2631  727 TYR A N     
5954 C  CA    . TYR A 727 ? 0.7777 0.7987 1.1831 -0.1396 0.0186  0.2457  727 TYR A CA    
5955 C  C     . TYR A 727 ? 0.8118 0.8135 1.2330 -0.1381 0.0168  0.2531  727 TYR A C     
5956 O  O     . TYR A 727 ? 0.7821 0.7880 1.2172 -0.1393 0.0193  0.2738  727 TYR A O     
5957 C  CB    . TYR A 727 ? 0.7576 0.7930 1.1334 -0.1312 0.0203  0.2404  727 TYR A CB    
5958 C  CG    . TYR A 727 ? 0.7621 0.8160 1.1294 -0.1274 0.0247  0.2599  727 TYR A CG    
5959 C  CD1   . TYR A 727 ? 0.7720 0.8200 1.1454 -0.1241 0.0239  0.2724  727 TYR A CD1   
5960 C  CD2   . TYR A 727 ? 0.8021 0.8795 1.1542 -0.1268 0.0297  0.2655  727 TYR A CD2   
5961 C  CE1   . TYR A 727 ? 0.8399 0.9056 1.2040 -0.1210 0.0271  0.2904  727 TYR A CE1   
5962 C  CE2   . TYR A 727 ? 0.7656 0.8598 1.1070 -0.1235 0.0335  0.2824  727 TYR A CE2   
5963 C  CZ    . TYR A 727 ? 0.8838 0.9725 1.2309 -0.1209 0.0317  0.2949  727 TYR A CZ    
5964 O  OH    . TYR A 727 ? 0.9725 1.0787 1.3076 -0.1179 0.0348  0.3122  727 TYR A OH    
5965 N  N     . ASP A 728 ? 0.7421 0.7228 1.1616 -0.1352 0.0128  0.2362  728 ASP A N     
5966 C  CA    . ASP A 728 ? 0.7777 0.7377 1.2124 -0.1328 0.0116  0.2407  728 ASP A CA    
5967 C  C     . ASP A 728 ? 0.7365 0.7065 1.1587 -0.1239 0.0135  0.2503  728 ASP A C     
5968 O  O     . ASP A 728 ? 0.7401 0.7071 1.1462 -0.1171 0.0122  0.2379  728 ASP A O     
5969 C  CB    . ASP A 728 ? 0.7958 0.7301 1.2321 -0.1323 0.0077  0.2188  728 ASP A CB    
5970 C  CG    . ASP A 728 ? 0.8588 0.7684 1.3168 -0.1316 0.0071  0.2232  728 ASP A CG    
5971 O  OD1   . ASP A 728 ? 0.9507 0.8625 1.4131 -0.1259 0.0093  0.2379  728 ASP A OD1   
5972 O  OD2   . ASP A 728 ? 1.0713 0.9591 1.5423 -0.1369 0.0042  0.2122  728 ASP A OD2   
5973 N  N     . ALA A 729 ? 0.7801 0.7629 1.2101 -0.1244 0.0163  0.2736  729 ALA A N     
5974 C  CA    . ALA A 729 ? 0.7999 0.7936 1.2191 -0.1169 0.0171  0.2852  729 ALA A CA    
5975 C  C     . ALA A 729 ? 0.8592 0.8325 1.2872 -0.1110 0.0149  0.2811  729 ALA A C     
5976 O  O     . ALA A 729 ? 0.7629 0.7412 1.1759 -0.1038 0.0139  0.2780  729 ALA A O     
5977 C  CB    . ALA A 729 ? 0.7591 0.7684 1.1878 -0.1191 0.0203  0.3122  729 ALA A CB    
5978 N  N     . GLU A 730 ? 0.8167 0.7666 1.2693 -0.1140 0.0143  0.2807  730 GLU A N     
5979 C  CA    . GLU A 730 ? 0.8078 0.7365 1.2704 -0.1078 0.0134  0.2764  730 GLU A CA    
5980 C  C     . GLU A 730 ? 0.8245 0.7457 1.2688 -0.1027 0.0118  0.2520  730 GLU A C     
5981 O  O     . GLU A 730 ? 0.8749 0.7914 1.3162 -0.0947 0.0117  0.2502  730 GLU A O     
5982 C  CB    . GLU A 730 ? 0.9092 0.8121 1.4008 -0.1126 0.0134  0.2779  730 GLU A CB    
5983 C  CG    . GLU A 730 ? 1.1256 1.0167 1.6383 -0.1076 0.0147  0.2941  730 GLU A CG    
5984 C  CD    . GLU A 730 ? 1.3219 1.2339 1.8410 -0.1081 0.0163  0.3227  730 GLU A CD    
5985 O  OE1   . GLU A 730 ? 1.3099 1.2404 1.8238 -0.1143 0.0172  0.3310  730 GLU A OE1   
5986 O  OE2   . GLU A 730 ? 1.2767 1.1871 1.8061 -0.1020 0.0170  0.3373  730 GLU A OE2   
5987 N  N     . TYR A 731 ? 0.7945 0.7154 1.2270 -0.1070 0.0105  0.2340  731 TYR A N     
5988 C  CA    . TYR A 731 ? 0.8187 0.7338 1.2331 -0.1024 0.0091  0.2116  731 TYR A CA    
5989 C  C     . TYR A 731 ? 0.7820 0.7174 1.1744 -0.0956 0.0092  0.2134  731 TYR A C     
5990 O  O     . TYR A 731 ? 0.8103 0.7400 1.1970 -0.0883 0.0089  0.2067  731 TYR A O     
5991 C  CB    . TYR A 731 ? 0.7531 0.6670 1.1592 -0.1088 0.0072  0.1944  731 TYR A CB    
5992 C  CG    . TYR A 731 ? 0.7002 0.6141 1.0844 -0.1041 0.0060  0.1735  731 TYR A CG    
5993 C  CD1   . TYR A 731 ? 0.7207 0.6123 1.1058 -0.1009 0.0052  0.1570  731 TYR A CD1   
5994 C  CD2   . TYR A 731 ? 0.7027 0.6383 1.0649 -0.1027 0.0060  0.1706  731 TYR A CD2   
5995 C  CE1   . TYR A 731 ? 0.7676 0.6599 1.1330 -0.0965 0.0044  0.1392  731 TYR A CE1   
5996 C  CE2   . TYR A 731 ? 0.7142 0.6496 1.0578 -0.0986 0.0049  0.1526  731 TYR A CE2   
5997 C  CZ    . TYR A 731 ? 0.7392 0.6536 1.0847 -0.0956 0.0041  0.1376  731 TYR A CZ    
5998 O  OH    . TYR A 731 ? 0.8073 0.7225 1.1346 -0.0914 0.0033  0.1209  731 TYR A OH    
5999 N  N     . TYR A 732 ? 0.7247 0.6837 1.1046 -0.0980 0.0098  0.2223  732 TYR A N     
6000 C  CA    . TYR A 732 ? 0.7430 0.7209 1.1002 -0.0926 0.0093  0.2226  732 TYR A CA    
6001 C  C     . TYR A 732 ? 0.7493 0.7335 1.1107 -0.0873 0.0090  0.2404  732 TYR A C     
6002 O  O     . TYR A 732 ? 0.6173 0.6142 0.9614 -0.0825 0.0074  0.2399  732 TYR A O     
6003 C  CB    . TYR A 732 ? 0.6845 0.6844 1.0261 -0.0966 0.0106  0.2254  732 TYR A CB    
6004 C  CG    . TYR A 732 ? 0.7241 0.7214 1.0588 -0.1007 0.0104  0.2074  732 TYR A CG    
6005 C  CD1   . TYR A 732 ? 0.7107 0.7068 1.0279 -0.0972 0.0087  0.1884  732 TYR A CD1   
6006 C  CD2   . TYR A 732 ? 0.6971 0.6943 1.0442 -0.1083 0.0116  0.2104  732 TYR A CD2   
6007 C  CE1   . TYR A 732 ? 0.7347 0.7294 1.0462 -0.1008 0.0082  0.1731  732 TYR A CE1   
6008 C  CE2   . TYR A 732 ? 0.7096 0.7059 1.0516 -0.1122 0.0107  0.1950  732 TYR A CE2   
6009 C  CZ    . TYR A 732 ? 0.7224 0.7174 1.0462 -0.1083 0.0090  0.1764  732 TYR A CZ    
6010 O  OH    . TYR A 732 ? 0.7109 0.7059 1.0301 -0.1120 0.0078  0.1621  732 TYR A OH    
6011 N  N     . ILE A 733 ? 0.8137 0.7893 1.1982 -0.0883 0.0100  0.2565  733 ILE A N     
6012 C  CA    . ILE A 733 ? 0.7906 0.7704 1.1824 -0.0828 0.0093  0.2740  733 ILE A CA    
6013 C  C     . ILE A 733 ? 0.8145 0.7744 1.2163 -0.0762 0.0089  0.2647  733 ILE A C     
6014 O  O     . ILE A 733 ? 0.7450 0.7109 1.1359 -0.0700 0.0072  0.2613  733 ILE A O     
6015 C  CB    . ILE A 733 ? 0.8102 0.7908 1.2235 -0.0864 0.0110  0.2977  733 ILE A CB    
6016 C  CG1   . ILE A 733 ? 0.8608 0.8661 1.2613 -0.0910 0.0122  0.3106  733 ILE A CG1   
6017 C  CG2   . ILE A 733 ? 0.6832 0.6617 1.1104 -0.0802 0.0101  0.3143  733 ILE A CG2   
6018 C  CD1   . ILE A 733 ? 0.7833 0.7949 1.2016 -0.0933 0.0138  0.3376  733 ILE A CD1   
6019 N  N     . GLU A 734 ? 0.8304 0.7663 1.2532 -0.0777 0.0106  0.2602  734 GLU A N     
6020 C  CA    . GLU A 734 ? 0.9189 0.8340 1.3540 -0.0709 0.0116  0.2532  734 GLU A CA    
6021 C  C     . GLU A 734 ? 0.8806 0.7894 1.2989 -0.0672 0.0113  0.2288  734 GLU A C     
6022 O  O     . GLU A 734 ? 0.9908 0.8855 1.4156 -0.0602 0.0128  0.2226  734 GLU A O     
6023 C  CB    . GLU A 734 ? 0.8955 0.7849 1.3564 -0.0740 0.0137  0.2538  734 GLU A CB    
6024 C  CG    . GLU A 734 ? 1.0509 0.9405 1.5355 -0.0741 0.0147  0.2795  734 GLU A CG    
6025 C  CD    . GLU A 734 ? 1.1026 1.0025 1.5895 -0.0655 0.0144  0.2943  734 GLU A CD    
6026 O  OE1   . GLU A 734 ? 1.0178 0.9059 1.5072 -0.0578 0.0155  0.2851  734 GLU A OE1   
6027 O  OE2   . GLU A 734 ? 1.1355 1.0559 1.6219 -0.0664 0.0130  0.3155  734 GLU A OE2   
6028 N  N     . LYS A 735 ? 0.7977 0.7167 1.1950 -0.0713 0.0099  0.2157  735 LYS A N     
6029 C  CA    . LYS A 735 ? 0.8195 0.7302 1.2029 -0.0686 0.0097  0.1925  735 LYS A CA    
6030 C  C     . LYS A 735 ? 0.7581 0.6893 1.1154 -0.0691 0.0077  0.1845  735 LYS A C     
6031 O  O     . LYS A 735 ? 0.7380 0.6638 1.0830 -0.0688 0.0074  0.1654  735 LYS A O     
6032 C  CB    . LYS A 735 ? 0.8258 0.7153 1.2163 -0.0739 0.0103  0.1776  735 LYS A CB    
6033 C  CG    . LYS A 735 ? 0.9744 0.8367 1.3854 -0.0704 0.0127  0.1753  735 LYS A CG    
6034 C  CD    . LYS A 735 ? 0.9950 0.8356 1.4083 -0.0758 0.0123  0.1570  735 LYS A CD    
6035 C  CE    . LYS A 735 ? 1.0440 0.8922 1.4336 -0.0776 0.0103  0.1382  735 LYS A CE    
6036 N  NZ    . LYS A 735 ? 1.0418 0.8903 1.4183 -0.0684 0.0120  0.1279  735 LYS A NZ    
6037 N  N     . GLN A 736 ? 0.6893 0.6429 1.0371 -0.0699 0.0063  0.1982  736 GLN A N     
6038 C  CA    . GLN A 736 ? 0.7120 0.6836 1.0350 -0.0698 0.0046  0.1904  736 GLN A CA    
6039 C  C     . GLN A 736 ? 0.6623 0.6522 0.9771 -0.0660 0.0024  0.2041  736 GLN A C     
6040 O  O     . GLN A 736 ? 0.6875 0.6827 0.9901 -0.0615 0.0005  0.1970  736 GLN A O     
6041 C  CB    . GLN A 736 ? 0.7689 0.7504 1.0834 -0.0771 0.0051  0.1888  736 GLN A CB    
6042 C  CG    . GLN A 736 ? 0.6805 0.6518 0.9904 -0.0802 0.0053  0.1686  736 GLN A CG    
6043 C  CD    . GLN A 736 ? 0.6773 0.6579 0.9646 -0.0776 0.0040  0.1541  736 GLN A CD    
6044 O  OE1   . GLN A 736 ? 0.7329 0.7308 1.0056 -0.0758 0.0032  0.1593  736 GLN A OE1   
6045 N  NE2   . GLN A 736 ? 0.6845 0.6532 0.9683 -0.0776 0.0037  0.1359  736 GLN A NE2   
6046 N  N     . VAL A 737 ? 0.5765 0.5765 0.8979 -0.0681 0.0023  0.2243  737 VAL A N     
6047 C  CA    . VAL A 737 ? 0.7088 0.7272 1.0213 -0.0653 -0.0006 0.2384  737 VAL A CA    
6048 C  C     . VAL A 737 ? 0.7744 0.7858 1.1037 -0.0591 -0.0019 0.2477  737 VAL A C     
6049 O  O     . VAL A 737 ? 0.6901 0.7092 1.0115 -0.0545 -0.0050 0.2470  737 VAL A O     
6050 C  CB    . VAL A 737 ? 0.6614 0.6953 0.9720 -0.0700 0.0000  0.2568  737 VAL A CB    
6051 C  CG1   . VAL A 737 ? 0.6722 0.7233 0.9756 -0.0672 -0.0037 0.2735  737 VAL A CG1   
6052 C  CG2   . VAL A 737 ? 0.7084 0.7526 1.0001 -0.0749 0.0017  0.2477  737 VAL A CG2   
6053 N  N     . LEU A 738 ? 0.7252 0.7218 1.0790 -0.0589 0.0006  0.2569  738 LEU A N     
6054 C  CA    . LEU A 738 ? 0.7376 0.7273 1.1104 -0.0524 0.0003  0.2679  738 LEU A CA    
6055 C  C     . LEU A 738 ? 0.8358 0.8150 1.2084 -0.0458 0.0008  0.2522  738 LEU A C     
6056 O  O     . LEU A 738 ? 0.7491 0.7358 1.1243 -0.0401 -0.0016 0.2600  738 LEU A O     
6057 C  CB    . LEU A 738 ? 0.7120 0.6847 1.1120 -0.0535 0.0037  0.2787  738 LEU A CB    
6058 C  CG    . LEU A 738 ? 0.8664 0.8508 1.2782 -0.0549 0.0027  0.3057  738 LEU A CG    
6059 C  CD1   . LEU A 738 ? 0.9409 0.9284 1.3652 -0.0475 0.0007  0.3200  738 LEU A CD1   
6060 C  CD2   . LEU A 738 ? 0.8393 0.8487 1.2289 -0.0601 0.0003  0.3131  738 LEU A CD2   
6061 N  N     . PRO A 739 ? 0.7672 0.7299 1.1371 -0.0460 0.0036  0.2312  739 PRO A N     
6062 C  CA    . PRO A 739 ? 0.7707 0.7259 1.1382 -0.0393 0.0045  0.2172  739 PRO A CA    
6063 C  C     . PRO A 739 ? 0.8552 0.8298 1.2014 -0.0381 0.0005  0.2132  739 PRO A C     
6064 O  O     . PRO A 739 ? 0.8620 0.8375 1.2104 -0.0318 0.0000  0.2114  739 PRO A O     
6065 C  CB    . PRO A 739 ? 0.7472 0.6830 1.1121 -0.0416 0.0078  0.1960  739 PRO A CB    
6066 C  CG    . PRO A 739 ? 0.7657 0.6929 1.1426 -0.0480 0.0089  0.2023  739 PRO A CG    
6067 C  CD    . PRO A 739 ? 0.7586 0.7080 1.1299 -0.0522 0.0060  0.2203  739 PRO A CD    
6068 N  N     . ALA A 740 ? 0.8351 0.8252 1.1615 -0.0440 -0.0022 0.2119  740 ALA A N     
6069 C  CA    . ALA A 740 ? 0.7572 0.7642 1.0626 -0.0434 -0.0063 0.2070  740 ALA A CA    
6070 C  C     . ALA A 740 ? 0.7480 0.7710 1.0557 -0.0408 -0.0109 0.2251  740 ALA A C     
6071 O  O     . ALA A 740 ? 0.7530 0.7838 1.0541 -0.0375 -0.0142 0.2221  740 ALA A O     
6072 C  CB    . ALA A 740 ? 0.6652 0.6831 0.9495 -0.0499 -0.0072 0.2006  740 ALA A CB    
6073 N  N     . VAL A 741 ? 0.7954 0.8240 1.1127 -0.0426 -0.0117 0.2445  741 VAL A N     
6074 C  CA    . VAL A 741 ? 0.7897 0.8345 1.1089 -0.0405 -0.0170 0.2631  741 VAL A CA    
6075 C  C     . VAL A 741 ? 0.7827 0.8189 1.1280 -0.0335 -0.0161 0.2733  741 VAL A C     
6076 O  O     . VAL A 741 ? 0.7484 0.7980 1.0967 -0.0307 -0.0211 0.2862  741 VAL A O     
6077 C  CB    . VAL A 741 ? 0.7690 0.8271 1.0844 -0.0454 -0.0186 0.2814  741 VAL A CB    
6078 C  CG1   . VAL A 741 ? 0.7001 0.7714 0.9872 -0.0511 -0.0199 0.2733  741 VAL A CG1   
6079 C  CG2   . VAL A 741 ? 0.7680 0.8119 1.1043 -0.0469 -0.0134 0.2892  741 VAL A CG2   
6080 N  N     . GLU A 742 ? 0.8118 0.8260 1.1761 -0.0307 -0.0100 0.2677  742 GLU A N     
6081 C  CA    . GLU A 742 ? 0.8142 0.8187 1.2049 -0.0233 -0.0078 0.2778  742 GLU A CA    
6082 C  C     . GLU A 742 ? 0.8976 0.9031 1.2886 -0.0167 -0.0083 0.2694  742 GLU A C     
6083 O  O     . GLU A 742 ? 0.8146 0.8269 1.2205 -0.0112 -0.0103 0.2835  742 GLU A O     
6084 C  CB    . GLU A 742 ? 0.9798 0.9584 1.3889 -0.0225 -0.0009 0.2723  742 GLU A CB    
6085 C  CG    . GLU A 742 ? 1.0146 0.9777 1.4503 -0.0137 0.0034  0.2771  742 GLU A CG    
6086 C  CD    . GLU A 742 ? 1.2022 1.1445 1.6380 -0.0096 0.0093  0.2543  742 GLU A CD    
6087 O  OE1   . GLU A 742 ? 1.1777 1.1169 1.6225 -0.0014 0.0116  0.2525  742 GLU A OE1   
6088 O  OE2   . GLU A 742 ? 1.1233 1.0531 1.5500 -0.0146 0.0116  0.2386  742 GLU A OE2   
6089 N  N     . ARG A 743 ? 0.7978 0.7978 1.1735 -0.0170 -0.0065 0.2477  743 ARG A N     
6090 C  CA    . ARG A 743 ? 0.8381 0.8400 1.2136 -0.0110 -0.0065 0.2397  743 ARG A CA    
6091 C  C     . ARG A 743 ? 0.7731 0.7991 1.1416 -0.0114 -0.0146 0.2516  743 ARG A C     
6092 O  O     . ARG A 743 ? 0.7803 0.8105 1.1568 -0.0057 -0.0153 0.2526  743 ARG A O     
6093 C  CB    . ARG A 743 ? 0.8646 0.8595 1.2218 -0.0126 -0.0041 0.2156  743 ARG A CB    
6094 C  CG    . ARG A 743 ? 0.7093 0.6833 1.0675 -0.0149 0.0017  0.2025  743 ARG A CG    
6095 C  CD    . ARG A 743 ? 0.8001 0.7742 1.1353 -0.0191 0.0015  0.1823  743 ARG A CD    
6096 N  NE    . ARG A 743 ? 0.8417 0.7951 1.1787 -0.0206 0.0066  0.1681  743 ARG A NE    
6097 C  CZ    . ARG A 743 ? 0.9009 0.8528 1.2276 -0.0279 0.0059  0.1618  743 ARG A CZ    
6098 N  NH1   . ARG A 743 ? 0.9461 0.9154 1.2594 -0.0337 0.0016  0.1679  743 ARG A NH1   
6099 N  NH2   . ARG A 743 ? 0.8814 0.8140 1.2115 -0.0294 0.0097  0.1493  743 ARG A NH2   
6100 N  N     . ILE A 744 ? 0.7468 0.7888 1.1005 -0.0180 -0.0205 0.2604  744 ILE A N     
6101 C  CA    . ILE A 744 ? 0.7464 0.8111 1.0916 -0.0194 -0.0293 0.2720  744 ILE A CA    
6102 C  C     . ILE A 744 ? 0.8011 0.8741 1.1651 -0.0173 -0.0325 0.2973  744 ILE A C     
6103 O  O     . ILE A 744 ? 0.7613 0.8447 1.1361 -0.0133 -0.0369 0.3081  744 ILE A O     
6104 C  CB    . ILE A 744 ? 0.7618 0.8393 1.0773 -0.0274 -0.0339 0.2665  744 ILE A CB    
6105 C  CG1   . ILE A 744 ? 0.7038 0.7743 1.0024 -0.0288 -0.0311 0.2424  744 ILE A CG1   
6106 C  CG2   . ILE A 744 ? 0.8003 0.9004 1.1052 -0.0297 -0.0437 0.2787  744 ILE A CG2   
6107 C  CD1   . ILE A 744 ? 0.7414 0.8257 1.0114 -0.0351 -0.0361 0.2359  744 ILE A CD1   
6108 N  N     . LEU A 745 ? 0.8399 0.9091 1.2097 -0.0199 -0.0303 0.3081  745 LEU A N     
6109 C  CA    . LEU A 745 ? 0.7563 0.8357 1.1416 -0.0188 -0.0340 0.3339  745 LEU A CA    
6110 C  C     . LEU A 745 ? 0.7773 0.8438 1.1961 -0.0104 -0.0294 0.3437  745 LEU A C     
6111 O  O     . LEU A 745 ? 0.7704 0.8452 1.2057 -0.0085 -0.0324 0.3664  745 LEU A O     
6112 C  CB    . LEU A 745 ? 0.7628 0.8440 1.1422 -0.0249 -0.0332 0.3435  745 LEU A CB    
6113 C  CG    . LEU A 745 ? 0.8169 0.9188 1.1669 -0.0322 -0.0395 0.3465  745 LEU A CG    
6114 C  CD1   . LEU A 745 ? 0.9098 1.0324 1.2619 -0.0324 -0.0477 0.3708  745 LEU A CD1   
6115 C  CD2   . LEU A 745 ? 0.8451 0.9522 1.1695 -0.0345 -0.0423 0.3260  745 LEU A CD2   
6116 N  N     . ARG A 746 ? 0.7909 0.8374 1.2198 -0.0051 -0.0219 0.3275  746 ARG A N     
6117 C  CA    . ARG A 746 ? 0.7810 0.8153 1.2410 0.0040  -0.0168 0.3356  746 ARG A CA    
6118 C  C     . ARG A 746 ? 0.8530 0.9045 1.3224 0.0092  -0.0222 0.3474  746 ARG A C     
6119 O  O     . ARG A 746 ? 0.8423 0.8926 1.3391 0.0161  -0.0207 0.3641  746 ARG A O     
6120 C  CB    . ARG A 746 ? 0.7997 0.8088 1.2645 0.0086  -0.0073 0.3138  746 ARG A CB    
6121 C  CG    . ARG A 746 ? 0.8499 0.8630 1.3002 0.0104  -0.0076 0.2959  746 ARG A CG    
6122 C  CD    . ARG A 746 ? 0.9731 0.9657 1.4131 0.0100  -0.0005 0.2709  746 ARG A CD    
6123 N  NE    . ARG A 746 ? 1.0304 0.9978 1.4901 0.0144  0.0080  0.2686  746 ARG A NE    
6124 C  CZ    . ARG A 746 ? 1.0926 1.0387 1.5483 0.0157  0.0149  0.2479  746 ARG A CZ    
6125 N  NH1   . ARG A 746 ? 1.0086 0.9563 1.4421 0.0130  0.0146  0.2286  746 ARG A NH1   
6126 N  NH2   . ARG A 746 ? 1.1661 1.0886 1.6401 0.0194  0.0220  0.2467  746 ARG A NH2   
6127 N  N     . ALA A 747 ? 0.8935 0.9611 1.3422 0.0060  -0.0287 0.3395  747 ALA A N     
6128 C  CA    . ALA A 747 ? 0.8866 0.9725 1.3432 0.0093  -0.0353 0.3505  747 ALA A CA    
6129 C  C     . ALA A 747 ? 0.8641 0.9699 1.3282 0.0074  -0.0442 0.3774  747 ALA A C     
6130 O  O     . ALA A 747 ? 0.9052 1.0276 1.3786 0.0099  -0.0509 0.3893  747 ALA A O     
6131 C  CB    . ALA A 747 ? 0.7492 0.8470 1.1798 0.0046  -0.0411 0.3353  747 ALA A CB    
6132 N  N     . PHE A 748 ? 0.8109 0.9165 1.2717 0.0029  -0.0447 0.3881  748 PHE A N     
6133 C  CA    . PHE A 748 ? 0.7228 0.8471 1.1901 0.0011  -0.0527 0.4149  748 PHE A CA    
6134 C  C     . PHE A 748 ? 0.7816 0.8935 1.2767 0.0055  -0.0466 0.4315  748 PHE A C     
6135 O  O     . PHE A 748 ? 0.8591 0.9845 1.3596 0.0035  -0.0520 0.4547  748 PHE A O     
6136 C  CB    . PHE A 748 ? 0.8023 0.9425 1.2370 -0.0090 -0.0602 0.4155  748 PHE A CB    
6137 C  CG    . PHE A 748 ? 0.8941 1.0449 1.3005 -0.0137 -0.0662 0.3986  748 PHE A CG    
6138 C  CD1   . PHE A 748 ? 0.8346 1.0073 1.2355 -0.0154 -0.0775 0.4079  748 PHE A CD1   
6139 C  CD2   . PHE A 748 ? 0.8377 0.9765 1.2242 -0.0167 -0.0609 0.3736  748 PHE A CD2   
6140 C  CE1   . PHE A 748 ? 0.8070 0.9879 1.1831 -0.0201 -0.0832 0.3920  748 PHE A CE1   
6141 C  CE2   . PHE A 748 ? 0.8701 1.0175 1.2323 -0.0207 -0.0662 0.3585  748 PHE A CE2   
6142 C  CZ    . PHE A 748 ? 0.8931 1.0609 1.2500 -0.0225 -0.0772 0.3673  748 PHE A CZ    
6143 N  N     . GLY A 749 ? 0.7624 0.8484 1.2746 0.0112  -0.0355 0.4202  749 GLY A N     
6144 C  CA    . GLY A 749 ? 0.7989 0.8693 1.3403 0.0161  -0.0290 0.4340  749 GLY A CA    
6145 C  C     . GLY A 749 ? 0.8568 0.9131 1.3925 0.0104  -0.0244 0.4308  749 GLY A C     
6146 O  O     . GLY A 749 ? 0.9009 0.9424 1.4616 0.0138  -0.0189 0.4419  749 GLY A O     
6147 N  N     . TYR A 750 ? 0.8188 0.8792 1.3242 0.0018  -0.0262 0.4165  750 TYR A N     
6148 C  CA    . TYR A 750 ? 0.9290 0.9787 1.4291 -0.0043 -0.0223 0.4146  750 TYR A CA    
6149 C  C     . TYR A 750 ? 0.8969 0.9179 1.4025 -0.0026 -0.0129 0.3919  750 TYR A C     
6150 O  O     . TYR A 750 ? 0.8261 0.8423 1.3159 -0.0026 -0.0115 0.3693  750 TYR A O     
6151 C  CB    . TYR A 750 ? 0.9052 0.9726 1.3712 -0.0137 -0.0278 0.4098  750 TYR A CB    
6152 C  CG    . TYR A 750 ? 0.9533 1.0480 1.4103 -0.0167 -0.0370 0.4323  750 TYR A CG    
6153 C  CD1   . TYR A 750 ? 0.9812 1.0816 1.4464 -0.0194 -0.0375 0.4547  750 TYR A CD1   
6154 C  CD2   . TYR A 750 ? 0.9141 1.0288 1.3536 -0.0174 -0.0455 0.4312  750 TYR A CD2   
6155 C  CE1   . TYR A 750 ? 1.0044 1.1304 1.4593 -0.0223 -0.0461 0.4755  750 TYR A CE1   
6156 C  CE2   . TYR A 750 ? 0.9353 1.0747 1.3645 -0.0208 -0.0547 0.4510  750 TYR A CE2   
6157 C  CZ    . TYR A 750 ? 0.9782 1.1234 1.4143 -0.0231 -0.0549 0.4731  750 TYR A CZ    
6158 O  OH    . TYR A 750 ? 0.9870 1.1573 1.4108 -0.0265 -0.0643 0.4930  750 TYR A OH    
6159 N  N     . ARG A 751 ? 0.9426 0.9442 1.4703 -0.0016 -0.0069 0.3980  751 ARG A N     
6160 C  CA    . ARG A 751 ? 1.0610 1.0353 1.5911 -0.0023 0.0008  0.3771  751 ARG A CA    
6161 C  C     . ARG A 751 ? 1.0830 1.0596 1.5936 -0.0127 -0.0001 0.3709  751 ARG A C     
6162 O  O     . ARG A 751 ? 1.0794 1.0778 1.5749 -0.0183 -0.0055 0.3828  751 ARG A O     
6163 C  CB    . ARG A 751 ? 1.0816 1.0320 1.6455 0.0035  0.0076  0.3853  751 ARG A CB    
6164 C  CG    . ARG A 751 ? 1.0216 0.9762 1.6104 0.0135  0.0076  0.4030  751 ARG A CG    
6165 C  CD    . ARG A 751 ? 1.0770 1.0027 1.6887 0.0227  0.0168  0.3922  751 ARG A CD    
6166 N  NE    . ARG A 751 ? 1.2189 1.1338 1.8128 0.0238  0.0205  0.3633  751 ARG A NE    
6167 C  CZ    . ARG A 751 ? 1.0549 0.9409 1.6539 0.0260  0.0283  0.3440  751 ARG A CZ    
6168 N  NH1   . ARG A 751 ? 1.0714 0.9342 1.6933 0.0272  0.0335  0.3490  751 ARG A NH1   
6169 N  NH2   . ARG A 751 ? 0.9787 0.8585 1.5590 0.0267  0.0308  0.3191  751 ARG A NH2   
6170 N  N     . LYS A 752 ? 1.0922 1.0463 1.6028 -0.0152 0.0054  0.3521  752 LYS A N     
6171 C  CA    . LYS A 752 ? 1.1219 1.0778 1.6163 -0.0249 0.0050  0.3457  752 LYS A CA    
6172 C  C     . LYS A 752 ? 1.1949 1.1569 1.7019 -0.0295 0.0043  0.3695  752 LYS A C     
6173 O  O     . LYS A 752 ? 1.1324 1.1098 1.6228 -0.0368 0.0019  0.3738  752 LYS A O     
6174 C  CB    . LYS A 752 ? 1.0092 0.9390 1.5050 -0.0267 0.0103  0.3224  752 LYS A CB    
6175 C  CG    . LYS A 752 ? 1.1004 1.0262 1.5783 -0.0239 0.0111  0.2974  752 LYS A CG    
6176 C  CD    . LYS A 752 ? 0.9929 0.9218 1.4468 -0.0320 0.0100  0.2802  752 LYS A CD    
6177 C  CE    . LYS A 752 ? 0.9587 0.8703 1.4046 -0.0299 0.0132  0.2537  752 LYS A CE    
6178 N  NZ    . LYS A 752 ? 0.9740 0.8563 1.4392 -0.0292 0.0182  0.2466  752 LYS A NZ    
6179 N  N     . GLU A 753 ? 1.2190 1.1693 1.7558 -0.0249 0.0067  0.3859  753 GLU A N     
6180 C  CA    . GLU A 753 ? 1.2200 1.1732 1.7719 -0.0293 0.0068  0.4087  753 GLU A CA    
6181 C  C     . GLU A 753 ? 1.1776 1.1617 1.7194 -0.0305 0.0007  0.4321  753 GLU A C     
6182 O  O     . GLU A 753 ? 1.2437 1.2376 1.7863 -0.0363 0.0001  0.4489  753 GLU A O     
6183 C  CB    . GLU A 753 ? 1.2364 1.1664 1.8244 -0.0236 0.0114  0.4192  753 GLU A CB    
6184 C  CG    . GLU A 753 ? 1.2974 1.1937 1.8976 -0.0244 0.0176  0.3989  753 GLU A CG    
6185 C  CD    . GLU A 753 ? 1.4725 1.3584 2.0541 -0.0225 0.0192  0.3681  753 GLU A CD    
6186 O  OE1   . GLU A 753 ? 1.4098 1.3102 1.9754 -0.0180 0.0168  0.3622  753 GLU A OE1   
6187 O  OE2   . GLU A 753 ? 1.5349 1.3980 2.1178 -0.0261 0.0226  0.3500  753 GLU A OE2   
6188 N  N     . ASP A 754 ? 1.1850 1.1848 1.7176 -0.0254 -0.0039 0.4341  754 ASP A N     
6189 C  CA    . ASP A 754 ? 1.2242 1.2542 1.7422 -0.0273 -0.0111 0.4531  754 ASP A CA    
6190 C  C     . ASP A 754 ? 1.1950 1.2422 1.6766 -0.0345 -0.0141 0.4414  754 ASP A C     
6191 O  O     . ASP A 754 ? 1.1813 1.2533 1.6447 -0.0363 -0.0204 0.4526  754 ASP A O     
6192 C  CB    . ASP A 754 ? 1.1633 1.2039 1.6858 -0.0197 -0.0158 0.4593  754 ASP A CB    
6193 C  CG    . ASP A 754 ? 1.1734 1.1931 1.7302 -0.0108 -0.0110 0.4628  754 ASP A CG    
6194 O  OD1   . ASP A 754 ? 1.2584 1.2799 1.8398 -0.0076 -0.0113 0.4874  754 ASP A OD1   
6195 O  OD2   . ASP A 754 ? 1.3208 1.3223 1.8800 -0.0066 -0.0064 0.4411  754 ASP A OD2   
6196 N  N     . LEU A 755 ? 1.2719 1.3064 1.7426 -0.0388 -0.0099 0.4193  755 LEU A N     
6197 C  CA    . LEU A 755 ? 1.2504 1.2991 1.6883 -0.0447 -0.0117 0.4062  755 LEU A CA    
6198 C  C     . LEU A 755 ? 1.2759 1.3222 1.7101 -0.0523 -0.0076 0.4055  755 LEU A C     
6199 O  O     . LEU A 755 ? 1.2273 1.2908 1.6361 -0.0571 -0.0089 0.4034  755 LEU A O     
6200 C  CB    . LEU A 755 ? 1.1540 1.1941 1.5778 -0.0427 -0.0113 0.3781  755 LEU A CB    
6201 C  CG    . LEU A 755 ? 1.1443 1.1847 1.5732 -0.0351 -0.0142 0.3752  755 LEU A CG    
6202 C  CD1   . LEU A 755 ? 1.0525 1.0775 1.4749 -0.0329 -0.0112 0.3477  755 LEU A CD1   
6203 C  CD2   . LEU A 755 ? 1.0656 1.1328 1.4750 -0.0355 -0.0222 0.3846  755 LEU A CD2   
6204 N  N     . ARG A 756 ? 1.2539 1.2794 1.7127 -0.0535 -0.0025 0.4071  756 ARG A N     
6205 C  CA    . ARG A 756 ? 1.1738 1.1966 1.6320 -0.0612 0.0012  0.4063  756 ARG A CA    
6206 C  C     . ARG A 756 ? 1.1777 1.2183 1.6395 -0.0646 0.0008  0.4341  756 ARG A C     
6207 O  O     . ARG A 756 ? 1.1668 1.2188 1.6345 -0.0609 -0.0024 0.4543  756 ARG A O     
6208 C  CB    . ARG A 756 ? 1.1149 1.1079 1.5983 -0.0620 0.0058  0.3967  756 ARG A CB    
6209 C  CG    . ARG A 756 ? 1.2181 1.2064 1.7146 -0.0698 0.0092  0.4056  756 ARG A CG    
6210 C  CD    . ARG A 756 ? 1.2475 1.2315 1.7734 -0.0689 0.0103  0.4325  756 ARG A CD    
6211 N  NE    . ARG A 756 ? 1.2877 1.2736 1.8233 -0.0769 0.0131  0.4447  756 ARG A NE    
6212 C  CZ    . ARG A 756 ? 1.2522 1.2607 1.7836 -0.0799 0.0130  0.4679  756 ARG A CZ    
6213 N  NH1   . ARG A 756 ? 1.1987 1.2299 1.7144 -0.0759 0.0095  0.4811  756 ARG A NH1   
6214 N  NH2   . ARG A 756 ? 1.0755 1.0843 1.6186 -0.0872 0.0163  0.4786  756 ARG A NH2   
6215 O  "O5'" . DG  B 1   ? 1.6957 1.1681 2.3398 -0.0981 0.0255  0.1083  1   DG  P "O5'" 
6216 C  "C5'" . DG  B 1   ? 1.6765 1.1170 2.3102 -0.0915 0.0294  0.0823  1   DG  P "C5'" 
6217 C  "C4'" . DG  B 1   ? 1.6867 1.1297 2.3172 -0.0736 0.0393  0.0850  1   DG  P "C4'" 
6218 O  "O4'" . DG  B 1   ? 1.6725 1.0891 2.2849 -0.0669 0.0436  0.0565  1   DG  P "O4'" 
6219 C  "C3'" . DG  B 1   ? 1.7004 1.1838 2.3119 -0.0679 0.0398  0.0943  1   DG  P "C3'" 
6220 O  "O3'" . DG  B 1   ? 1.7352 1.2229 2.3558 -0.0527 0.0482  0.1066  1   DG  P "O3'" 
6221 C  "C2'" . DG  B 1   ? 1.6362 1.1181 2.2144 -0.0683 0.0381  0.0659  1   DG  P "C2'" 
6222 C  "C1'" . DG  B 1   ? 1.6423 1.0825 2.2237 -0.0624 0.0437  0.0456  1   DG  P "C1'" 
6223 N  N9    . DG  B 1   ? 1.6167 1.0408 2.1742 -0.0694 0.0392  0.0168  1   DG  P N9    
6224 C  C8    . DG  B 1   ? 1.6307 1.0571 2.1817 -0.0853 0.0289  0.0098  1   DG  P C8    
6225 N  N7    . DG  B 1   ? 1.6602 1.0707 2.1883 -0.0886 0.0261  -0.0172 1   DG  P N7    
6226 C  C5    . DG  B 1   ? 1.6009 0.9971 2.1187 -0.0735 0.0360  -0.0291 1   DG  P C5    
6227 C  C6    . DG  B 1   ? 1.5342 0.9107 2.0263 -0.0692 0.0386  -0.0573 1   DG  P C6    
6228 O  O6    . DG  B 1   ? 1.4334 0.8010 1.9056 -0.0786 0.0315  -0.0781 1   DG  P O6    
6229 N  N1    . DG  B 1   ? 1.4592 0.8274 1.9499 -0.0521 0.0507  -0.0598 1   DG  P N1    
6230 C  C2    . DG  B 1   ? 1.3880 0.7661 1.9007 -0.0408 0.0585  -0.0373 1   DG  P C2    
6231 N  N2    . DG  B 1   ? 1.2431 0.6119 1.7525 -0.0246 0.0701  -0.0429 1   DG  P N2    
6232 N  N3    . DG  B 1   ? 1.4597 0.8564 1.9960 -0.0451 0.0553  -0.0105 1   DG  P N3    
6233 C  C4    . DG  B 1   ? 1.5496 0.9542 2.0864 -0.0615 0.0443  -0.0083 1   DG  P C4    
6234 P  P     . DA  B 2   ? 1.9437 1.4732 2.5540 -0.0461 0.0488  0.1241  2   DA  P P     
6235 O  OP1   . DA  B 2   ? 1.7887 1.3354 2.4217 -0.0498 0.0465  0.1543  2   DA  P OP1   
6236 O  OP2   . DA  B 2   ? 1.6464 1.1962 2.2244 -0.0505 0.0441  0.1088  2   DA  P OP2   
6237 O  "O5'" . DA  B 2   ? 1.6050 1.1260 2.2190 -0.0286 0.0586  0.1228  2   DA  P "O5'" 
6238 C  "C5'" . DA  B 2   ? 1.5683 1.0518 2.1864 -0.0221 0.0652  0.1037  2   DA  P "C5'" 
6239 C  "C4'" . DA  B 2   ? 1.5708 1.0569 2.1730 -0.0078 0.0729  0.0917  2   DA  P "C4'" 
6240 O  "O4'" . DA  B 2   ? 1.6127 1.0810 2.1888 -0.0099 0.0730  0.0609  2   DA  P "O4'" 
6241 C  "C3'" . DA  B 2   ? 1.4925 1.0187 2.0798 -0.0040 0.0713  0.1027  2   DA  P "C3'" 
6242 O  "O3'" . DA  B 2   ? 1.4822 1.0090 2.0726 0.0117  0.0802  0.1038  2   DA  P "O3'" 
6243 C  "C2'" . DA  B 2   ? 1.4451 0.9797 1.9995 -0.0121 0.0656  0.0811  2   DA  P "C2'" 
6244 C  "C1'" . DA  B 2   ? 1.4477 0.9446 1.9953 -0.0106 0.0698  0.0542  2   DA  P "C1'" 
6245 N  N9    . DA  B 2   ? 1.3840 0.8751 1.9110 -0.0236 0.0621  0.0346  2   DA  P N9    
6246 C  C8    . DA  B 2   ? 1.4098 0.9103 1.9395 -0.0384 0.0526  0.0411  2   DA  P C8    
6247 N  N7    . DA  B 2   ? 1.3515 0.8442 1.8617 -0.0479 0.0467  0.0205  2   DA  P N7    
6248 C  C5    . DA  B 2   ? 1.3288 0.8053 1.8208 -0.0389 0.0528  -0.0015 2   DA  P C5    
6249 C  C6    . DA  B 2   ? 1.3210 0.7840 1.7869 -0.0424 0.0506  -0.0287 2   DA  P C6    
6250 N  N6    . DA  B 2   ? 1.2784 0.7426 1.7338 -0.0569 0.0406  -0.0380 2   DA  P N6    
6251 N  N1    . DA  B 2   ? 1.3011 0.7503 1.7526 -0.0305 0.0591  -0.0452 2   DA  P N1    
6252 C  C2    . DA  B 2   ? 1.3255 0.7749 1.7901 -0.0158 0.0693  -0.0346 2   DA  P C2    
6253 N  N3    . DA  B 2   ? 1.3356 0.7976 1.8261 -0.0112 0.0717  -0.0087 2   DA  P N3    
6254 C  C4    . DA  B 2   ? 1.3287 0.8038 1.8309 -0.0236 0.0629  0.0067  2   DA  P C4    
6255 P  P     . DC  B 3   ? 1.8186 1.3816 2.3920 0.0181  0.0801  0.1097  3   DC  P P     
6256 O  OP1   . DC  B 3   ? 1.4153 0.9789 2.0084 0.0331  0.0885  0.1232  3   DC  P OP1   
6257 O  OP2   . DC  B 3   ? 1.6113 1.2060 2.1769 0.0074  0.0704  0.1238  3   DC  P OP2   
6258 O  "O5'" . DC  B 3   ? 1.4700 1.0260 2.0121 0.0192  0.0819  0.0800  3   DC  P "O5'" 
6259 C  "C5'" . DC  B 3   ? 1.4663 0.9880 2.0069 0.0260  0.0900  0.0592  3   DC  P "C5'" 
6260 C  "C4'" . DC  B 3   ? 1.4346 0.9581 1.9431 0.0276  0.0914  0.0348  3   DC  P "C4'" 
6261 O  "O4'" . DC  B 3   ? 1.3657 0.8810 1.8553 0.0137  0.0833  0.0176  3   DC  P "O4'" 
6262 C  "C3'" . DC  B 3   ? 1.4057 0.9659 1.8987 0.0304  0.0895  0.0416  3   DC  P "C3'" 
6263 O  "O3'" . DC  B 3   ? 1.3917 0.9472 1.8683 0.0405  0.0972  0.0249  3   DC  P "O3'" 
6264 C  "C2'" . DC  B 3   ? 1.3636 0.9398 1.8369 0.0154  0.0783  0.0369  3   DC  P "C2'" 
6265 C  "C1'" . DC  B 3   ? 1.3484 0.8925 1.8132 0.0088  0.0774  0.0141  3   DC  P "C1'" 
6266 N  N1    . DC  B 3   ? 1.3160 0.8646 1.7752 -0.0075 0.0665  0.0128  3   DC  P N1    
6267 C  C2    . DC  B 3   ? 1.2585 0.7955 1.6950 -0.0154 0.0622  -0.0106 3   DC  P C2    
6268 O  O2    . DC  B 3   ? 1.2741 0.7976 1.6937 -0.0086 0.0676  -0.0301 3   DC  P O2    
6269 N  N3    . DC  B 3   ? 1.1846 0.7266 1.6187 -0.0301 0.0523  -0.0105 3   DC  P N3    
6270 C  C4    . DC  B 3   ? 1.2090 0.7663 1.6613 -0.0365 0.0476  0.0114  3   DC  P C4    
6271 N  N4    . DC  B 3   ? 1.2032 0.7660 1.6537 -0.0506 0.0386  0.0114  3   DC  P N4    
6272 C  C5    . DC  B 3   ? 1.2546 0.8234 1.7282 -0.0286 0.0520  0.0350  3   DC  P C5    
6273 C  C6    . DC  B 3   ? 1.3044 0.8683 1.7810 -0.0144 0.0609  0.0349  3   DC  P C6    
6274 P  P     . DC  B 4   ? 1.5769 1.1634 2.0477 0.0498  0.1002  0.0341  4   DC  P P     
6275 O  OP1   . DC  B 4   ? 1.4217 0.9973 1.9117 0.0655  0.1120  0.0396  4   DC  P OP1   
6276 O  OP2   . DC  B 4   ? 1.5428 1.1618 2.0156 0.0420  0.0906  0.0540  4   DC  P OP2   
6277 O  "O5'" . DC  B 4   ? 1.4631 1.0514 1.9002 0.0484  0.1003  0.0100  4   DC  P "O5'" 
6278 C  "C5'" . DC  B 4   ? 1.4286 0.9865 1.8516 0.0468  0.1031  -0.0147 4   DC  P "C5'" 
6279 C  "C4'" . DC  B 4   ? 1.3307 0.8985 1.7221 0.0380  0.0964  -0.0316 4   DC  P "C4'" 
6280 O  "O4'" . DC  B 4   ? 1.2926 0.8603 1.6822 0.0225  0.0852  -0.0314 4   DC  P "O4'" 
6281 C  "C3'" . DC  B 4   ? 1.3357 0.9390 1.7147 0.0393  0.0939  -0.0239 4   DC  P "C3'" 
6282 O  "O3'" . DC  B 4   ? 1.3618 0.9644 1.7131 0.0403  0.0956  -0.0440 4   DC  P "O3'" 
6283 C  "C2'" . DC  B 4   ? 1.3272 0.9505 1.7064 0.0257  0.0817  -0.0124 4   DC  P "C2'" 
6284 C  "C1'" . DC  B 4   ? 1.2586 0.8569 1.6326 0.0154  0.0773  -0.0273 4   DC  P "C1'" 
6285 N  N1    . DC  B 4   ? 1.1697 0.7765 1.5528 0.0023  0.0673  -0.0156 4   DC  P N1    
6286 C  C2    . DC  B 4   ? 1.1131 0.7149 1.4816 -0.0102 0.0593  -0.0287 4   DC  P C2    
6287 O  O2    . DC  B 4   ? 1.1035 0.6939 1.4512 -0.0103 0.0602  -0.0497 4   DC  P O2    
6288 N  N3    . DC  B 4   ? 1.0825 0.6929 1.4606 -0.0219 0.0511  -0.0173 4   DC  P N3    
6289 C  C4    . DC  B 4   ? 1.1070 0.7301 1.5062 -0.0212 0.0508  0.0059  4   DC  P C4    
6290 N  N4    . DC  B 4   ? 1.0162 0.6481 1.4236 -0.0325 0.0433  0.0169  4   DC  P N4    
6291 C  C5    . DC  B 4   ? 1.1718 0.8001 1.5849 -0.0087 0.0581  0.0195  4   DC  P C5    
6292 C  C6    . DC  B 4   ? 1.2170 0.8370 1.6223 0.0026  0.0661  0.0083  4   DC  P C6    
6293 P  P     . DA  B 5   ? 1.4712 1.0986 1.8117 0.0492  0.1001  -0.0416 5   DA  P P     
6294 O  OP1   . DA  B 5   ? 1.4980 1.1103 1.8463 0.0643  0.1136  -0.0453 5   DA  P OP1   
6295 O  OP2   . DA  B 5   ? 1.3400 0.9989 1.6896 0.0456  0.0933  -0.0203 5   DA  P OP2   
6296 O  "O5'" . DA  B 5   ? 1.3202 0.9501 1.6282 0.0428  0.0960  -0.0619 5   DA  P "O5'" 
6297 C  "C5'" . DA  B 5   ? 1.2438 0.8457 1.5361 0.0419  0.0988  -0.0846 5   DA  P "C5'" 
6298 C  "C4'" . DA  B 5   ? 1.2883 0.8950 1.5571 0.0288  0.0883  -0.0973 5   DA  P "C4'" 
6299 O  "O4'" . DA  B 5   ? 1.2261 0.8363 1.5063 0.0162  0.0778  -0.0878 5   DA  P "O4'" 
6300 C  "C3'" . DA  B 5   ? 1.2780 0.9139 1.5288 0.0278  0.0850  -0.0962 5   DA  P "C3'" 
6301 O  "O3'" . DA  B 5   ? 1.3049 0.9346 1.5296 0.0213  0.0808  -0.1155 5   DA  P "O3'" 
6302 C  "C2'" . DA  B 5   ? 1.1925 0.8521 1.4550 0.0190  0.0754  -0.0776 5   DA  P "C2'" 
6303 C  "C1'" . DA  B 5   ? 1.2157 0.8561 1.4880 0.0092  0.0696  -0.0794 5   DA  P "C1'" 
6304 N  N9    . DA  B 5   ? 1.1403 0.7926 1.4342 0.0043  0.0647  -0.0587 5   DA  P N9    
6305 C  C8    . DA  B 5   ? 1.1888 0.8486 1.5044 0.0115  0.0689  -0.0399 5   DA  P C8    
6306 N  N7    . DA  B 5   ? 1.1190 0.7889 1.4495 0.0045  0.0628  -0.0235 5   DA  P N7    
6307 C  C5    . DA  B 5   ? 1.0802 0.7489 1.3995 -0.0080 0.0544  -0.0321 5   DA  P C5    
6308 C  C6    . DA  B 5   ? 1.0124 0.6896 1.3389 -0.0196 0.0461  -0.0222 5   DA  P C6    
6309 N  N6    . DA  B 5   ? 0.9881 0.6767 1.3339 -0.0204 0.0448  -0.0011 5   DA  P N6    
6310 N  N1    . DA  B 5   ? 0.9943 0.6687 1.3075 -0.0304 0.0391  -0.0343 5   DA  P N1    
6311 C  C2    . DA  B 5   ? 1.0257 0.6895 1.3185 -0.0297 0.0399  -0.0549 5   DA  P C2    
6312 N  N3    . DA  B 5   ? 1.0361 0.6909 1.3185 -0.0194 0.0476  -0.0661 5   DA  P N3    
6313 C  C4    . DA  B 5   ? 1.0799 0.7377 1.3770 -0.0086 0.0550  -0.0537 5   DA  P C4    
6314 P  P     . DC  B 6   ? 1.5410 1.1920 1.7418 0.0231  0.0806  -0.1214 6   DC  P P     
6315 O  OP1   . DC  B 6   ? 1.4421 1.0736 1.6224 0.0287  0.0875  -0.1420 6   DC  P OP1   
6316 O  OP2   . DC  B 6   ? 1.4314 1.1082 1.6434 0.0298  0.0836  -0.1036 6   DC  P OP2   
6317 O  "O5'" . DC  B 6   ? 1.3876 1.0513 1.5774 0.0081  0.0672  -0.1233 6   DC  P "O5'" 
6318 C  "C5'" . DC  B 6   ? 1.2945 0.9481 1.4951 -0.0028 0.0593  -0.1213 6   DC  P "C5'" 
6319 C  "C4'" . DC  B 6   ? 1.2493 0.9269 1.4479 -0.0138 0.0485  -0.1129 6   DC  P "C4'" 
6320 O  "O4'" . DC  B 6   ? 1.2102 0.8947 1.4322 -0.0174 0.0456  -0.0945 6   DC  P "O4'" 
6321 C  "C3'" . DC  B 6   ? 1.2320 0.9378 1.4196 -0.0105 0.0485  -0.1076 6   DC  P "C3'" 
6322 O  "O3'" . DC  B 6   ? 1.2255 0.9443 1.4001 -0.0208 0.0392  -0.1114 6   DC  P "O3'" 
6323 C  "C2'" . DC  B 6   ? 1.1632 0.8856 1.3714 -0.0077 0.0494  -0.0863 6   DC  P "C2'" 
6324 C  "C1'" . DC  B 6   ? 1.1030 0.8169 1.3256 -0.0173 0.0431  -0.0807 6   DC  P "C1'" 
6325 N  N1    . DC  B 6   ? 1.0458 0.7667 1.2918 -0.0153 0.0442  -0.0607 6   DC  P N1    
6326 C  C2    . DC  B 6   ? 0.9921 0.7200 1.2489 -0.0251 0.0370  -0.0499 6   DC  P C2    
6327 O  O2    . DC  B 6   ? 0.9394 0.6674 1.1875 -0.0350 0.0302  -0.0573 6   DC  P O2    
6328 N  N3    . DC  B 6   ? 1.0072 0.7424 1.2838 -0.0233 0.0378  -0.0311 6   DC  P N3    
6329 C  C4    . DC  B 6   ? 0.9301 0.6660 1.2167 -0.0126 0.0448  -0.0230 6   DC  P C4    
6330 N  N4    . DC  B 6   ? 0.9081 0.6521 1.2140 -0.0115 0.0446  -0.0036 6   DC  P N4    
6331 C  C5    . DC  B 6   ? 0.9904 0.7196 1.2681 -0.0024 0.0523  -0.0335 6   DC  P C5    
6332 C  C6    . DC  B 6   ? 1.0248 0.7466 1.2817 -0.0040 0.0521  -0.0523 6   DC  P C6    
6333 P  P     . DG  B 7   ? 1.2177 0.9407 1.3654 -0.0208 0.0382  -0.1267 7   DG  P P     
6334 O  OP1   . DG  B 7   ? 1.4674 1.1649 1.6045 -0.0154 0.0444  -0.1433 7   DG  P OP1   
6335 O  OP2   . DG  B 7   ? 1.1841 0.9323 1.3281 -0.0154 0.0404  -0.1178 7   DG  P OP2   
6336 O  "O5'" . DG  B 7   ? 1.3021 1.0297 1.4434 -0.0347 0.0265  -0.1311 7   DG  P "O5'" 
6337 C  "C5'" . DG  B 7   ? 1.3252 1.0789 1.4637 -0.0396 0.0206  -0.1227 7   DG  P "C5'" 
6338 C  "C4'" . DG  B 7   ? 1.2248 0.9835 1.3767 -0.0506 0.0124  -0.1143 7   DG  P "C4'" 
6339 O  "O4'" . DG  B 7   ? 1.1153 0.8698 1.2889 -0.0485 0.0156  -0.1009 7   DG  P "O4'" 
6340 C  "C3'" . DG  B 7   ? 1.1756 0.9613 1.3255 -0.0551 0.0072  -0.1051 7   DG  P "C3'" 
6341 O  "O3'" . DG  B 7   ? 1.0996 0.8872 1.2553 -0.0664 -0.0009 -0.1037 7   DG  P "O3'" 
6342 C  "C2'" . DG  B 7   ? 1.1299 0.9278 1.2941 -0.0494 0.0116  -0.0884 7   DG  P "C2'" 
6343 C  "C1'" . DG  B 7   ? 1.0837 0.8621 1.2653 -0.0494 0.0139  -0.0847 7   DG  P "C1'" 
6344 N  N9    . DG  B 7   ? 1.0358 0.8155 1.2300 -0.0404 0.0207  -0.0732 7   DG  P N9    
6345 C  C8    . DG  B 7   ? 1.0549 0.8279 1.2466 -0.0296 0.0287  -0.0766 7   DG  P C8    
6346 N  N7    . DG  B 7   ? 0.9539 0.7309 1.1610 -0.0234 0.0329  -0.0630 7   DG  P N7    
6347 C  C5    . DG  B 7   ? 0.9244 0.7110 1.1434 -0.0307 0.0275  -0.0500 7   DG  P C5    
6348 C  C6    . DG  B 7   ? 0.9072 0.7022 1.1438 -0.0288 0.0283  -0.0320 7   DG  P C6    
6349 O  O6    . DG  B 7   ? 0.8320 0.6280 1.0784 -0.0204 0.0336  -0.0235 7   DG  P O6    
6350 N  N1    . DG  B 7   ? 0.8769 0.6809 1.1197 -0.0379 0.0222  -0.0229 7   DG  P N1    
6351 C  C2    . DG  B 7   ? 0.9221 0.7272 1.1572 -0.0475 0.0162  -0.0300 7   DG  P C2    
6352 N  N2    . DG  B 7   ? 0.8492 0.6645 1.0931 -0.0550 0.0118  -0.0185 7   DG  P N2    
6353 N  N3    . DG  B 7   ? 0.9662 0.7638 1.1861 -0.0497 0.0146  -0.0466 7   DG  P N3    
6354 C  C4    . DG  B 7   ? 0.9516 0.7399 1.1633 -0.0409 0.0204  -0.0560 7   DG  P C4    
6355 P  P     . DG  B 8   ? 1.1284 0.9398 1.2774 -0.0727 -0.0075 -0.1004 8   DG  P P     
6356 O  OP1   . DG  B 8   ? 1.1400 0.9472 1.2941 -0.0844 -0.0156 -0.1032 8   DG  P OP1   
6357 O  OP2   . DG  B 8   ? 1.1619 0.9807 1.2918 -0.0671 -0.0056 -0.1085 8   DG  P OP2   
6358 O  "O5'" . DG  B 8   ? 1.0302 0.8608 1.1917 -0.0705 -0.0054 -0.0824 8   DG  P "O5'" 
6359 C  "C5'" . DG  B 8   ? 1.0074 0.8349 1.1876 -0.0739 -0.0056 -0.0708 8   DG  P "C5'" 
6360 C  "C4'" . DG  B 8   ? 0.9851 0.8317 1.1719 -0.0703 -0.0031 -0.0551 8   DG  P "C4'" 
6361 O  "O4'" . DG  B 8   ? 0.9386 0.7786 1.1317 -0.0616 0.0032  -0.0500 8   DG  P "O4'" 
6362 C  "C3'" . DG  B 8   ? 0.9719 0.8396 1.1457 -0.0681 -0.0037 -0.0546 8   DG  P "C3'" 
6363 O  "O3'" . DG  B 8   ? 0.9698 0.8548 1.1491 -0.0732 -0.0066 -0.0437 8   DG  P "O3'" 
6364 C  "C2'" . DG  B 8   ? 0.9054 0.7758 1.0776 -0.0580 0.0023  -0.0507 8   DG  P "C2'" 
6365 C  "C1'" . DG  B 8   ? 0.8664 0.7250 1.0553 -0.0562 0.0052  -0.0423 8   DG  P "C1'" 
6366 N  N9    . DG  B 8   ? 0.8965 0.7481 1.0875 -0.0465 0.0115  -0.0416 8   DG  P N9    
6367 C  C8    . DG  B 8   ? 0.9206 0.7619 1.1021 -0.0403 0.0156  -0.0533 8   DG  P C8    
6368 N  N7    . DG  B 8   ? 0.9083 0.7463 1.0968 -0.0316 0.0216  -0.0484 8   DG  P N7    
6369 C  C5    . DG  B 8   ? 0.8780 0.7245 1.0811 -0.0327 0.0205  -0.0325 8   DG  P C5    
6370 C  C6    . DG  B 8   ? 0.8143 0.6630 1.0308 -0.0260 0.0245  -0.0201 8   DG  P C6    
6371 O  O6    . DG  B 8   ? 0.7840 0.6275 1.0037 -0.0172 0.0303  -0.0206 8   DG  P O6    
6372 N  N1    . DG  B 8   ? 0.7563 0.6154 0.9836 -0.0301 0.0211  -0.0051 8   DG  P N1    
6373 C  C2    . DG  B 8   ? 0.7762 0.6426 1.0017 -0.0391 0.0157  -0.0026 8   DG  P C2    
6374 N  N2    . DG  B 8   ? 0.7514 0.6279 0.9869 -0.0416 0.0138  0.0128  8   DG  P N2    
6375 N  N3    . DG  B 8   ? 0.8261 0.6908 1.0408 -0.0452 0.0124  -0.0138 8   DG  P N3    
6376 C  C4    . DG  B 8   ? 0.8934 0.7481 1.0973 -0.0417 0.0146  -0.0283 8   DG  P C4    
6377 P  P     . DC  B 9   ? 0.9354 0.8420 1.1033 -0.0731 -0.0082 -0.0430 9   DC  P P     
6378 O  OP1   . DC  B 9   ? 0.9992 0.9140 1.1713 -0.0817 -0.0129 -0.0407 9   DC  P OP1   
6379 O  OP2   . DC  B 9   ? 0.8901 0.7952 1.0433 -0.0681 -0.0070 -0.0542 9   DC  P OP2   
6380 O  "O5'" . DC  B 9   ? 0.7852 0.7049 0.9572 -0.0685 -0.0050 -0.0295 9   DC  P "O5'" 
6381 C  "C5'" . DC  B 9   ? 0.7863 0.7075 0.9717 -0.0712 -0.0048 -0.0169 9   DC  P "C5'" 
6382 C  "C4'" . DC  B 9   ? 0.8175 0.7488 1.0039 -0.0657 -0.0020 -0.0059 9   DC  P "C4'" 
6383 O  "O4'" . DC  B 9   ? 0.7635 0.6831 0.9535 -0.0590 0.0014  -0.0068 9   DC  P "O4'" 
6384 C  "C3'" . DC  B 9   ? 0.7624 0.7102 0.9359 -0.0629 -0.0022 -0.0067 9   DC  P "C3'" 
6385 O  "O3'" . DC  B 9   ? 0.7528 0.7154 0.9274 -0.0653 -0.0028 0.0042  9   DC  P "O3'" 
6386 C  "C2'" . DC  B 9   ? 0.7444 0.6898 0.9157 -0.0550 0.0006  -0.0069 9   DC  P "C2'" 
6387 C  "C1'" . DC  B 9   ? 0.8240 0.7551 1.0089 -0.0532 0.0028  -0.0021 9   DC  P "C1'" 
6388 N  N1    . DC  B 9   ? 0.8353 0.7557 1.0203 -0.0459 0.0065  -0.0075 9   DC  P N1    
6389 C  C2    . DC  B 9   ? 0.7927 0.7129 0.9872 -0.0402 0.0092  0.0022  9   DC  P C2    
6390 O  O2    . DC  B 9   ? 0.7934 0.7224 0.9947 -0.0417 0.0078  0.0151  9   DC  P O2    
6391 N  N3    . DC  B 9   ? 0.6751 0.5862 0.8711 -0.0330 0.0135  -0.0024 9   DC  P N3    
6392 C  C4    . DC  B 9   ? 0.7723 0.6744 0.9589 -0.0314 0.0153  -0.0164 9   DC  P C4    
6393 N  N4    . DC  B 9   ? 0.6932 0.5869 0.8811 -0.0237 0.0205  -0.0202 9   DC  P N4    
6394 C  C5    . DC  B 9   ? 0.7420 0.6440 0.9175 -0.0376 0.0118  -0.0264 9   DC  P C5    
6395 C  C6    . DC  B 9   ? 0.7941 0.7055 0.9703 -0.0446 0.0075  -0.0214 9   DC  P C6    
6396 P  P     . DC  B 10  ? 0.8311 0.8108 0.9929 -0.0644 -0.0035 0.0035  10  DC  P P     
6397 O  OP1   . DC  B 10  ? 0.7914 0.7821 0.9552 -0.0693 -0.0040 0.0110  10  DC  P OP1   
6398 O  OP2   . DC  B 10  ? 0.8104 0.7883 0.9627 -0.0628 -0.0042 -0.0089 10  DC  P OP2   
6399 O  "O5'" . DC  B 10  ? 0.7446 0.7298 0.9046 -0.0589 -0.0024 0.0107  10  DC  P "O5'" 
6400 C  "C5'" . DC  B 10  ? 0.7385 0.7240 0.9076 -0.0588 -0.0019 0.0230  10  DC  P "C5'" 
6401 C  "C4'" . DC  B 10  ? 0.7346 0.7209 0.9042 -0.0529 -0.0014 0.0272  10  DC  P "C4'" 
6402 O  "O4'" . DC  B 10  ? 0.7263 0.6991 0.9001 -0.0488 0.0005  0.0198  10  DC  P "O4'" 
6403 C  "C3'" . DC  B 10  ? 0.7018 0.7005 0.8591 -0.0507 -0.0028 0.0252  10  DC  P "C3'" 
6404 O  "O3'" . DC  B 10  ? 0.6571 0.6658 0.8139 -0.0505 -0.0044 0.0367  10  DC  P "O3'" 
6405 C  "C2'" . DC  B 10  ? 0.6426 0.6347 0.7998 -0.0452 -0.0016 0.0183  10  DC  P "C2'" 
6406 C  "C1'" . DC  B 10  ? 0.7738 0.7515 0.9441 -0.0434 0.0008  0.0201  10  DC  P "C1'" 
6407 N  N1    . DC  B 10  ? 0.7522 0.7186 0.9222 -0.0390 0.0036  0.0098  10  DC  P N1    
6408 C  C2    . DC  B 10  ? 0.7513 0.7131 0.9293 -0.0328 0.0063  0.0133  10  DC  P C2    
6409 O  O2    . DC  B 10  ? 0.7205 0.6881 0.9064 -0.0314 0.0054  0.0253  10  DC  P O2    
6410 N  N3    . DC  B 10  ? 0.7018 0.6537 0.8785 -0.0281 0.0099  0.0040  10  DC  P N3    
6411 C  C4    . DC  B 10  ? 0.7216 0.6684 0.8885 -0.0301 0.0101  -0.0083 10  DC  P C4    
6412 N  N4    . DC  B 10  ? 0.5804 0.5178 0.7445 -0.0252 0.0140  -0.0172 10  DC  P N4    
6413 C  C5    . DC  B 10  ? 0.7454 0.6973 0.9049 -0.0369 0.0064  -0.0116 10  DC  P C5    
6414 C  C6    . DC  B 10  ? 0.7432 0.7049 0.9052 -0.0409 0.0037  -0.0022 10  DC  P C6    
6415 P  P     . DA  B 11  ? 0.6988 0.7212 0.8420 -0.0501 -0.0068 0.0364  11  DA  P P     
6416 O  OP1   . DA  B 11  ? 0.7850 0.8173 0.9240 -0.0535 -0.0077 0.0453  11  DA  P OP1   
6417 O  OP2   . DA  B 11  ? 0.9018 0.9238 1.0364 -0.0497 -0.0064 0.0239  11  DA  P OP2   
6418 O  "O5'" . DA  B 11  ? 0.7499 0.7734 0.8973 -0.0456 -0.0085 0.0414  11  DA  P "O5'" 
6419 C  "C5'" . DA  B 11  ? 0.7484 0.7700 0.9078 -0.0442 -0.0086 0.0530  11  DA  P "C5'" 
6420 C  "C4'" . DA  B 11  ? 0.7629 0.7818 0.9301 -0.0388 -0.0086 0.0543  11  DA  P "C4'" 
6421 O  "O4'" . DA  B 11  ? 0.7519 0.7580 0.9238 -0.0357 -0.0046 0.0445  11  DA  P "O4'" 
6422 C  "C3'" . DA  B 11  ? 0.6836 0.7125 0.8423 -0.0377 -0.0120 0.0524  11  DA  P "C3'" 
6423 O  "O3'" . DA  B 11  ? 0.7393 0.7762 0.9034 -0.0367 -0.0156 0.0645  11  DA  P "O3'" 
6424 C  "C2'" . DA  B 11  ? 0.6578 0.6794 0.8194 -0.0333 -0.0089 0.0429  11  DA  P "C2'" 
6425 C  "C1'" . DA  B 11  ? 0.6872 0.6949 0.8602 -0.0310 -0.0043 0.0421  11  DA  P "C1'" 
6426 N  N9    . DA  B 11  ? 0.7430 0.7408 0.9135 -0.0288 -0.0004 0.0295  11  DA  P N9    
6427 C  C8    . DA  B 11  ? 0.6667 0.6606 0.8281 -0.0320 0.0002  0.0191  11  DA  P C8    
6428 N  N7    . DA  B 11  ? 0.6545 0.6400 0.8143 -0.0290 0.0035  0.0093  11  DA  P N7    
6429 C  C5    . DA  B 11  ? 0.6642 0.6475 0.8329 -0.0230 0.0060  0.0133  11  DA  P C5    
6430 C  C6    . DA  B 11  ? 0.6649 0.6407 0.8360 -0.0171 0.0108  0.0074  11  DA  P C6    
6431 N  N6    . DA  B 11  ? 0.6917 0.6599 0.8543 -0.0167 0.0133  -0.0047 11  DA  P N6    
6432 N  N1    . DA  B 11  ? 0.7117 0.6887 0.8942 -0.0114 0.0130  0.0149  11  DA  P N1    
6433 C  C2    . DA  B 11  ? 0.6751 0.6607 0.8659 -0.0121 0.0096  0.0276  11  DA  P C2    
6434 N  N3    . DA  B 11  ? 0.6568 0.6498 0.8446 -0.0178 0.0045  0.0340  11  DA  P N3    
6435 C  C4    . DA  B 11  ? 0.7010 0.6923 0.8775 -0.0228 0.0034  0.0260  11  DA  P C4    
6436 P  P     . DC  B 12  ? 0.7318 0.7808 0.8875 -0.0374 -0.0211 0.0654  12  DC  P P     
6437 O  OP1   . DC  B 12  ? 0.6343 0.6931 0.7908 -0.0393 -0.0262 0.0788  12  DC  P OP1   
6438 O  OP2   . DC  B 12  ? 0.7995 0.8501 0.9399 -0.0400 -0.0212 0.0538  12  DC  P OP2   
6439 O  "O5'" . DC  B 12  ? 0.7103 0.7565 0.8776 -0.0319 -0.0197 0.0642  12  DC  P "O5'" 
6440 C  "C5'" . DC  B 12  ? 0.6484 0.6911 0.8330 -0.0275 -0.0178 0.0734  12  DC  P "C5'" 
6441 C  "C4'" . DC  B 12  ? 0.6973 0.7418 0.8910 -0.0225 -0.0170 0.0733  12  DC  P "C4'" 
6442 O  "O4'" . DC  B 12  ? 0.6628 0.6959 0.8576 -0.0186 -0.0101 0.0621  12  DC  P "O4'" 
6443 C  "C3'" . DC  B 12  ? 0.8072 0.8629 0.9923 -0.0250 -0.0226 0.0714  12  DC  P "C3'" 
6444 O  "O3'" . DC  B 12  ? 0.8099 0.8729 1.0087 -0.0219 -0.0250 0.0806  12  DC  P "O3'" 
6445 C  "C2'" . DC  B 12  ? 0.7370 0.7867 0.9140 -0.0241 -0.0185 0.0572  12  DC  P "C2'" 
6446 C  "C1'" . DC  B 12  ? 0.7449 0.7823 0.9324 -0.0184 -0.0108 0.0544  12  DC  P "C1'" 
6447 N  N1    . DC  B 12  ? 0.6904 0.7182 0.8682 -0.0186 -0.0062 0.0408  12  DC  P N1    
6448 C  C2    . DC  B 12  ? 0.6609 0.6817 0.8422 -0.0133 -0.0003 0.0340  12  DC  P C2    
6449 O  O2    . DC  B 12  ? 0.6538 0.6765 0.8469 -0.0082 0.0018  0.0395  12  DC  P O2    
6450 N  N3    . DC  B 12  ? 0.6916 0.7045 0.8631 -0.0140 0.0029  0.0221  12  DC  P N3    
6451 C  C4    . DC  B 12  ? 0.6440 0.6563 0.8048 -0.0195 0.0005  0.0175  12  DC  P C4    
6452 N  N4    . DC  B 12  ? 0.5601 0.5656 0.7125 -0.0202 0.0030  0.0065  12  DC  P N4    
6453 C  C5    . DC  B 12  ? 0.6320 0.6514 0.7902 -0.0243 -0.0045 0.0245  12  DC  P C5    
6454 C  C6    . DC  B 12  ? 0.6778 0.7045 0.8436 -0.0238 -0.0077 0.0357  12  DC  P C6    
6455 P  P     . DA  B 13  ? 0.8119 0.8892 1.0062 -0.0260 -0.0340 0.0851  13  DA  P P     
6456 O  OP1   . DA  B 13  ? 0.7937 0.8796 1.0018 -0.0252 -0.0387 0.1008  13  DA  P OP1   
6457 O  OP2   . DA  B 13  ? 0.7944 0.8736 0.9681 -0.0322 -0.0378 0.0777  13  DA  P OP2   
6458 O  "O5'" . DA  B 13  ? 0.6931 0.7707 0.8926 -0.0227 -0.0315 0.0791  13  DA  P "O5'" 
6459 C  "C5'" . DA  B 13  ? 0.6355 0.7071 0.8503 -0.0154 -0.0239 0.0799  13  DA  P "C5'" 
6460 C  "C4'" . DA  B 13  ? 0.6943 0.7662 0.9090 -0.0131 -0.0208 0.0723  13  DA  P "C4'" 
6461 O  "O4'" . DA  B 13  ? 0.7394 0.7985 0.9502 -0.0091 -0.0119 0.0617  13  DA  P "O4'" 
6462 C  "C3'" . DA  B 13  ? 0.7246 0.8014 0.9243 -0.0191 -0.0263 0.0651  13  DA  P "C3'" 
6463 O  "O3'" . DA  B 13  ? 0.6459 0.7351 0.8504 -0.0225 -0.0348 0.0735  13  DA  P "O3'" 
6464 C  "C2'" . DA  B 13  ? 0.5995 0.6715 0.7990 -0.0151 -0.0196 0.0561  13  DA  P "C2'" 
6465 C  "C1'" . DA  B 13  ? 0.6369 0.6964 0.8382 -0.0100 -0.0109 0.0520  13  DA  P "C1'" 
6466 N  N9    . DA  B 13  ? 0.6647 0.7157 0.8500 -0.0128 -0.0092 0.0407  13  DA  P N9    
6467 C  C8    . DA  B 13  ? 0.6070 0.6584 0.7805 -0.0186 -0.0136 0.0389  13  DA  P C8    
6468 N  N7    . DA  B 13  ? 0.6632 0.7072 0.8256 -0.0198 -0.0107 0.0287  13  DA  P N7    
6469 C  C5    . DA  B 13  ? 0.6126 0.6508 0.7783 -0.0148 -0.0044 0.0231  13  DA  P C5    
6470 C  C6    . DA  B 13  ? 0.5962 0.6260 0.7536 -0.0137 0.0004  0.0122  13  DA  P C6    
6471 N  N6    . DA  B 13  ? 0.6809 0.7074 0.8270 -0.0179 -0.0008 0.0055  13  DA  P N6    
6472 N  N1    . DA  B 13  ? 0.6353 0.6613 0.7968 -0.0081 0.0063  0.0091  13  DA  P N1    
6473 C  C2    . DA  B 13  ? 0.5874 0.6179 0.7619 -0.0035 0.0081  0.0167  13  DA  P C2    
6474 N  N3    . DA  B 13  ? 0.5839 0.6228 0.7691 -0.0041 0.0038  0.0277  13  DA  P N3    
6475 C  C4    . DA  B 13  ? 0.6298 0.6720 0.8091 -0.0101 -0.0028 0.0302  13  DA  P C4    
6476 O  "O5'" . 6HA C 1   ? 1.3207 1.3506 1.4121 -0.0471 -0.0061 -0.0379 1   6HA T "O5'" 
6477 C  "C5'" . 6HA C 1   ? 1.2679 1.3001 1.3581 -0.0494 -0.0069 -0.0422 1   6HA T "C5'" 
6478 C  "C4'" . 6HA C 1   ? 1.2874 1.3118 1.3818 -0.0522 -0.0077 -0.0446 1   6HA T "C4'" 
6479 O  "O4'" . 6HA C 1   ? 1.2550 1.2841 1.3511 -0.0563 -0.0095 -0.0459 1   6HA T "O4'" 
6480 C  "C3'" . 6HA C 1   ? 1.2726 1.2893 1.3633 -0.0494 -0.0075 -0.0508 1   6HA T "C3'" 
6481 O  "O3'" . 6HA C 1   ? 1.4146 1.4272 1.5062 -0.0451 -0.0053 -0.0484 1   6HA T "O3'" 
6482 C  "C2'" . 6HA C 1   ? 1.1660 1.1737 1.2588 -0.0526 -0.0089 -0.0550 1   6HA T "C2'" 
6483 C  "C1'" . 6HA C 1   ? 1.2561 1.2670 1.3515 -0.0582 -0.0119 -0.0560 1   6HA T "C1'" 
6484 C  "C6'" . 6HA C 1   ? 1.2715 1.2929 1.3717 -0.0603 -0.0116 -0.0490 1   6HA T "C6'" 
6485 N  N9    . 6HA C 1   ? 1.3173 1.3304 1.4058 -0.0583 -0.0142 -0.0628 1   6HA T N9    
6486 C  C8    . 6HA C 1   ? 1.2261 1.2317 1.3086 -0.0582 -0.0156 -0.0700 1   6HA T C8    
6487 N  N7    . 6HA C 1   ? 1.1966 1.2098 1.2738 -0.0584 -0.0179 -0.0726 1   6HA T N7    
6488 C  C5    . 6HA C 1   ? 1.0657 1.0903 1.1467 -0.0583 -0.0175 -0.0672 1   6HA T C5    
6489 C  C6    . 6HA C 1   ? 0.9866 1.0219 1.0663 -0.0580 -0.0189 -0.0665 1   6HA T C6    
6490 N  N6    . 6HA C 1   ? 0.9739 1.0122 1.0476 -0.0580 -0.0218 -0.0706 1   6HA T N6    
6491 N  N1    . 6HA C 1   ? 0.9380 0.9825 1.0221 -0.0572 -0.0173 -0.0613 1   6HA T N1    
6492 C  C2    . 6HA C 1   ? 0.9894 1.0334 1.0777 -0.0572 -0.0148 -0.0568 1   6HA T C2    
6493 N  N3    . 6HA C 1   ? 0.9866 1.0213 1.0764 -0.0578 -0.0140 -0.0565 1   6HA T N3    
6494 C  C4    . 6HA C 1   ? 1.0789 1.1034 1.1659 -0.0582 -0.0152 -0.0616 1   6HA T C4    
6495 P  P     . 6HA C 2   ? 1.3777 1.3930 1.4654 -0.0402 -0.0038 -0.0493 2   6HA T P     
6496 O  OP1   . 6HA C 2   ? 1.1959 1.2141 1.2873 -0.0384 -0.0033 -0.0424 2   6HA T OP1   
6497 O  OP2   . 6HA C 2   ? 1.1566 1.1797 1.2388 -0.0399 -0.0048 -0.0518 2   6HA T OP2   
6498 O  "O5'" . 6HA C 2   ? 1.0345 1.0396 1.1208 -0.0369 -0.0014 -0.0544 2   6HA T "O5'" 
6499 C  "C5'" . 6HA C 2   ? 0.9800 0.9867 1.0602 -0.0335 -0.0001 -0.0583 2   6HA T "C5'" 
6500 C  "C4'" . 6HA C 2   ? 0.8911 0.8936 0.9645 -0.0354 -0.0013 -0.0659 2   6HA T "C4'" 
6501 O  "O4'" . 6HA C 2   ? 1.0360 1.0376 1.1122 -0.0412 -0.0046 -0.0663 2   6HA T "O4'" 
6502 C  "C3'" . 6HA C 2   ? 0.8651 0.8757 0.9319 -0.0340 -0.0019 -0.0677 2   6HA T "C3'" 
6503 O  "O3'" . 6HA C 2   ? 0.9223 0.9315 0.9864 -0.0284 0.0020  -0.0681 2   6HA T "O3'" 
6504 C  "C2'" . 6HA C 2   ? 0.8789 0.8896 0.9392 -0.0372 -0.0050 -0.0734 2   6HA T "C2'" 
6505 C  "C1'" . 6HA C 2   ? 0.9090 0.9196 0.9732 -0.0431 -0.0087 -0.0737 2   6HA T "C1'" 
6506 C  "C6'" . 6HA C 2   ? 0.9776 0.9778 1.0474 -0.0441 -0.0074 -0.0732 2   6HA T "C6'" 
6507 N  N9    . 6HA C 2   ? 0.9288 0.9499 0.9985 -0.0447 -0.0098 -0.0678 2   6HA T N9    
6508 C  C8    . 6HA C 2   ? 0.9836 1.0081 1.0594 -0.0456 -0.0093 -0.0623 2   6HA T C8    
6509 N  N7    . 6HA C 2   ? 0.9313 0.9654 1.0075 -0.0463 -0.0102 -0.0602 2   6HA T N7    
6510 C  C5    . 6HA C 2   ? 0.8562 0.8934 0.9280 -0.0458 -0.0116 -0.0636 2   6HA T C5    
6511 C  C6    . 6HA C 2   ? 0.8706 0.9168 0.9423 -0.0457 -0.0128 -0.0628 2   6HA T C6    
6512 N  N6    . 6HA C 2   ? 0.6663 0.7205 0.7422 -0.0456 -0.0121 -0.0589 2   6HA T N6    
6513 N  N1    . 6HA C 2   ? 0.8852 0.9335 0.9523 -0.0451 -0.0146 -0.0657 2   6HA T N1    
6514 C  C2    . 6HA C 2   ? 0.8385 0.8799 0.8992 -0.0447 -0.0150 -0.0703 2   6HA T C2    
6515 N  N3    . 6HA C 2   ? 0.7378 0.7693 0.7983 -0.0445 -0.0132 -0.0721 2   6HA T N3    
6516 C  C4    . 6HA C 2   ? 0.7995 0.8291 0.8666 -0.0450 -0.0117 -0.0683 2   6HA T C4    
6517 P  P     . 6HC C 3   ? 0.8255 0.8442 0.8917 -0.0257 0.0027  -0.0630 3   6HC T P     
6518 O  OP1   . 6HC C 3   ? 0.5805 0.6018 0.6547 -0.0263 0.0021  -0.0566 3   6HC T OP1   
6519 O  OP2   . 6HC C 3   ? 0.5971 0.6241 0.6596 -0.0271 0.0003  -0.0634 3   6HC T OP2   
6520 O  "O5'" . 6HC C 3   ? 0.8034 0.8187 0.8672 -0.0197 0.0078  -0.0639 3   6HC T "O5'" 
6521 C  "C5'" . 6HC C 3   ? 0.6615 0.6711 0.7313 -0.0166 0.0113  -0.0615 3   6HC T "C5'" 
6522 C  "C4'" . 6HC C 3   ? 0.6017 0.6177 0.6767 -0.0123 0.0140  -0.0557 3   6HC T "C4'" 
6523 O  "O4'" . 6HC C 3   ? 0.5944 0.6194 0.6721 -0.0152 0.0100  -0.0517 3   6HC T "O4'" 
6524 C  "C3'" . 6HC C 3   ? 0.6847 0.6967 0.7694 -0.0093 0.0170  -0.0511 3   6HC T "C3'" 
6525 O  "O3'" . 6HC C 3   ? 0.7282 0.7305 0.8096 -0.0052 0.0222  -0.0559 3   6HC T "O3'" 
6526 C  "C2'" . 6HC C 3   ? 0.6192 0.6389 0.7118 -0.0062 0.0184  -0.0440 3   6HC T "C2'" 
6527 C  "C1'" . 6HC C 3   ? 0.5795 0.6079 0.6738 -0.0099 0.0135  -0.0403 3   6HC T "C1'" 
6528 C  "C6'" . 6HC C 3   ? 0.6427 0.6737 0.7278 -0.0127 0.0110  -0.0452 3   6HC T "C6'" 
6529 N  N1    . 6HC C 3   ? 0.6192 0.6476 0.7181 -0.0137 0.0092  -0.0370 3   6HC T N1    
6530 C  C2    . 6HC C 3   ? 0.5471 0.5773 0.6567 -0.0123 0.0092  -0.0295 3   6HC T C2    
6531 O  O2    . 6HC C 3   ? 0.6295 0.6611 0.7454 -0.0080 0.0127  -0.0261 3   6HC T O2    
6532 N  N3    . 6HC C 3   ? 0.5442 0.5753 0.6568 -0.0162 0.0047  -0.0254 3   6HC T N3    
6533 C  C4    . 6HC C 3   ? 0.5653 0.5956 0.6709 -0.0210 0.0014  -0.0287 3   6HC T C4    
6534 N  N4    . 6HC C 3   ? 0.6120 0.6441 0.7195 -0.0244 -0.0021 -0.0240 3   6HC T N4    
6535 C  C5    . 6HC C 3   ? 0.6158 0.6448 0.7127 -0.0223 0.0019  -0.0360 3   6HC T C5    
6536 C  C6    . 6HC C 3   ? 0.6378 0.6659 0.7313 -0.0188 0.0053  -0.0400 3   6HC T C6    
6537 P  P     . 6HT C 4   ? 0.6391 0.6293 0.7242 -0.0036 0.0251  -0.0578 4   6HT T P     
6538 O  OP1   . 6HT C 4   ? 0.8825 0.8614 0.9590 -0.0063 0.0243  -0.0669 4   6HT T OP1   
6539 O  OP2   . 6HT C 4   ? 0.6661 0.6593 0.7620 -0.0066 0.0213  -0.0504 4   6HT T OP2   
6540 O  "O5'" . 6HT C 4   ? 0.8362 0.8245 0.9259 0.0049  0.0333  -0.0557 4   6HT T "O5'" 
6541 C  "C5'" . 6HT C 4   ? 0.6393 0.6384 0.7378 0.0077  0.0344  -0.0472 4   6HT T "C5'" 
6542 C  "C4'" . 6HT C 4   ? 0.6877 0.6840 0.7977 0.0141  0.0405  -0.0421 4   6HT T "C4'" 
6543 O  "O4'" . 6HT C 4   ? 0.7492 0.7571 0.8726 0.0142  0.0384  -0.0312 4   6HT T "O4'" 
6544 C  "C3'" . 6HT C 4   ? 0.7464 0.7307 0.8606 0.0134  0.0405  -0.0437 4   6HT T "C3'" 
6545 O  "O3'" . 6HT C 4   ? 0.7262 0.7064 0.8512 0.0209  0.0478  -0.0396 4   6HT T "O3'" 
6546 C  "C2'" . 6HT C 4   ? 0.7218 0.7101 0.8431 0.0076  0.0335  -0.0376 4   6HT T "C2'" 
6547 C  "C1'" . 6HT C 4   ? 0.7041 0.7050 0.8363 0.0076  0.0309  -0.0271 4   6HT T "C1'" 
6548 C  "C6'" . 6HT C 4   ? 0.6414 0.6525 0.7695 0.0080  0.0307  -0.0268 4   6HT T "C6'" 
6549 N  N1    . 6HT C 4   ? 0.6314 0.6363 0.7650 0.0009  0.0233  -0.0232 4   6HT T N1    
6550 C  C2    . 6HT C 4   ? 0.6139 0.6253 0.7603 0.0005  0.0202  -0.0122 4   6HT T C2    
6551 O  O2    . 6HT C 4   ? 0.6988 0.7127 0.8559 0.0054  0.0235  -0.0062 4   6HT T O2    
6552 N  N3    . 6HT C 4   ? 0.6058 0.6214 0.7509 -0.0061 0.0130  -0.0086 4   6HT T N3    
6553 C  C4    . 6HT C 4   ? 0.6248 0.6383 0.7581 -0.0116 0.0099  -0.0154 4   6HT T C4    
6554 O  O4    . 6HT C 4   ? 0.6042 0.6213 0.7361 -0.0162 0.0053  -0.0124 4   6HT T O4    
6555 C  C5    . 6HT C 4   ? 0.6195 0.6270 0.7424 -0.0113 0.0126  -0.0257 4   6HT T C5    
6556 C  C5M   . 6HT C 4   ? 0.5320 0.5389 0.6450 -0.0170 0.0091  -0.0316 4   6HT T C5M   
6557 C  C6    . 6HT C 4   ? 0.6038 0.6069 0.7261 -0.0052 0.0189  -0.0296 4   6HT T C6    
6558 P  P     . 6HG C 5   ? 0.8376 0.8004 0.9600 0.0246  0.0535  -0.0471 5   6HG T P     
6559 O  OP1   . 6HG C 5   ? 0.8404 0.7975 0.9487 0.0292  0.0601  -0.0568 5   6HG T OP1   
6560 O  OP2   . 6HG C 5   ? 0.8720 0.8249 0.9899 0.0179  0.0479  -0.0524 5   6HG T OP2   
6561 O  "O5'" . 6HG C 5   ? 0.8460 0.8083 0.9880 0.0316  0.0590  -0.0371 5   6HG T "O5'" 
6562 C  "C5'" . 6HG C 5   ? 0.7992 0.7756 0.9523 0.0352  0.0606  -0.0270 5   6HG T "C5'" 
6563 C  "C4'" . 6HG C 5   ? 0.7862 0.7661 0.9595 0.0378  0.0606  -0.0150 5   6HG T "C4'" 
6564 O  "O4'" . 6HG C 5   ? 0.7509 0.7459 0.9306 0.0319  0.0520  -0.0056 5   6HG T "O4'" 
6565 C  "C3'" . 6HG C 5   ? 0.9114 0.8774 1.0890 0.0368  0.0600  -0.0162 5   6HG T "C3'" 
6566 O  "O3'" . 6HG C 5   ? 1.1115 1.0809 1.3096 0.0420  0.0628  -0.0041 5   6HG T "O3'" 
6567 C  "C2'" . 6HG C 5   ? 0.8497 0.8157 1.0236 0.0278  0.0508  -0.0159 5   6HG T "C2'" 
6568 C  "C1'" . 6HG C 5   ? 0.8362 0.8184 1.0128 0.0223  0.0428  -0.0077 5   6HG T "C1'" 
6569 C  "C6'" . 6HG C 5   ? 0.6974 0.6913 0.8694 0.0232  0.0433  -0.0080 5   6HG T "C6'" 
6570 N  N9    . 6HG C 5   ? 0.7670 0.7482 0.9332 0.0136  0.0353  -0.0117 5   6HG T N9    
6571 C  C8    . 6HG C 5   ? 0.7349 0.7104 0.8864 0.0094  0.0337  -0.0222 5   6HG T C8    
6572 N  N7    . 6HG C 5   ? 0.7547 0.7336 0.9042 0.0023  0.0268  -0.0200 5   6HG T N7    
6573 C  C5    . 6HG C 5   ? 0.6368 0.6230 0.7979 0.0020  0.0240  -0.0088 5   6HG T C5    
6574 C  C6    . 6HG C 5   ? 0.6432 0.6362 0.8063 -0.0041 0.0169  -0.0013 5   6HG T C6    
6575 O  O6    . 6HG C 5   ? 0.6787 0.6709 0.8330 -0.0095 0.0137  -0.0057 5   6HG T O6    
6576 N  N1    . 6HG C 5   ? 0.6855 0.6866 0.8607 -0.0033 0.0143  0.0111  5   6HG T N1    
6577 C  C2    . 6HG C 5   ? 0.6565 0.6599 0.8446 0.0035  0.0184  0.0173  5   6HG T C2    
6578 N  N2    . 6HG C 5   ? 0.6998 0.7129 0.9015 0.0040  0.0148  0.0309  5   6HG T N2    
6579 N  N3    . 6HG C 5   ? 0.6073 0.6043 0.7947 0.0099  0.0262  0.0103  5   6HG T N3    
6580 C  C4    . 6HG C 5   ? 0.7032 0.6911 0.8753 0.0089  0.0288  -0.0033 5   6HG T C4    
6581 P  P     . 6HT C 6   ? 1.0854 1.0411 1.2961 0.0490  0.0699  -0.0023 6   6HT T P     
6582 O  OP1   . 6HT C 6   ? 1.0203 0.9781 1.2424 0.0598  0.0804  0.0019  6   6HT T OP1   
6583 O  OP2   . 6HT C 6   ? 1.0560 0.9922 1.2522 0.0479  0.0725  -0.0167 6   6HT T OP2   
6584 O  "O5'" . 6HT C 6   ? 0.9385 0.8989 1.1657 0.0453  0.0629  0.0111  6   6HT T "O5'" 
6585 C  "C5'" . 6HT C 6   ? 0.9882 0.9667 1.2203 0.0402  0.0545  0.0215  6   6HT T "C5'" 
6586 C  "C4'" . 6HT C 6   ? 0.9935 0.9758 1.2424 0.0394  0.0503  0.0350  6   6HT T "C4'" 
6587 O  "O4'" . 6HT C 6   ? 0.9914 0.9864 1.2356 0.0304  0.0392  0.0403  6   6HT T "O4'" 
6588 C  "C3'" . 6HT C 6   ? 0.9646 0.9288 1.2156 0.0401  0.0530  0.0317  6   6HT T "C3'" 
6589 O  "O3'" . 6HT C 6   ? 0.9946 0.9633 1.2647 0.0413  0.0505  0.0468  6   6HT T "O3'" 
6590 C  "C2'" . 6HT C 6   ? 0.9345 0.8917 1.1700 0.0316  0.0475  0.0232  6   6HT T "C2'" 
6591 C  "C1'" . 6HT C 6   ? 0.8620 0.8332 1.0903 0.0229  0.0376  0.0272  6   6HT T "C1'" 
6592 C  "C6'" . 6HT C 6   ? 0.8676 0.8557 1.0947 0.0229  0.0349  0.0307  6   6HT T "C6'" 
6593 N  N1    . 6HT C 6   ? 0.8263 0.7910 1.0365 0.0162  0.0347  0.0152  6   6HT T N1    
6594 C  C2    . 6HT C 6   ? 0.8020 0.7717 1.0074 0.0076  0.0267  0.0185  6   6HT T C2    
6595 O  O2    . 6HT C 6   ? 0.8507 0.8289 1.0647 0.0061  0.0225  0.0301  6   6HT T O2    
6596 N  N3    . 6HT C 6   ? 0.7000 0.6647 0.8897 0.0012  0.0242  0.0075  6   6HT T N3    
6597 C  C4    . 6HT C 6   ? 0.7338 0.6888 0.9122 0.0026  0.0283  -0.0064 6   6HT T C4    
6598 O  O4    . 6HT C 6   ? 0.7839 0.7361 0.9512 -0.0028 0.0256  -0.0141 6   6HT T O4    
6599 C  C5    . 6HT C 6   ? 0.7571 0.7066 0.9378 0.0110  0.0361  -0.0103 6   6HT T C5    
6600 C  C5M   . 6HT C 6   ? 0.7165 0.6562 0.8828 0.0125  0.0403  -0.0250 6   6HT T C5M   
6601 C  C6    . 6HT C 6   ? 0.8383 0.7928 1.0356 0.0180  0.0398  0.0007  6   6HT T C6    
6602 P  P     . DG  C 7   ? 1.1501 1.1015 1.4330 0.0461  0.0561  0.0489  7   DG  T P     
6603 O  OP1   . DG  C 7   ? 1.0051 0.9647 1.3119 0.0527  0.0581  0.0650  7   DG  T OP1   
6604 O  OP2   . DG  C 7   ? 1.1292 1.0612 1.4019 0.0501  0.0647  0.0330  7   DG  T OP2   
6605 O  "O5'" . DG  C 7   ? 0.9932 0.9427 1.2711 0.0366  0.0475  0.0512  7   DG  T "O5'" 
6606 C  "C5'" . DG  C 7   ? 0.9361 0.9026 1.2176 0.0308  0.0382  0.0640  7   DG  T "C5'" 
6607 C  "C4'" . DG  C 7   ? 0.8225 0.7847 1.0977 0.0228  0.0325  0.0644  7   DG  T "C4'" 
6608 O  "O4'" . DG  C 7   ? 0.7346 0.6944 0.9891 0.0165  0.0303  0.0507  7   DG  T "O4'" 
6609 C  "C3'" . DG  C 7   ? 0.6922 0.6355 0.9771 0.0252  0.0374  0.0640  7   DG  T "C3'" 
6610 O  "O3'" . DG  C 7   ? 0.6566 0.6048 0.9589 0.0260  0.0348  0.0810  7   DG  T "O3'" 
6611 C  "C2'" . DG  C 7   ? 0.7695 0.7044 1.0386 0.0169  0.0343  0.0534  7   DG  T "C2'" 
6612 C  "C1'" . DG  C 7   ? 0.7047 0.6542 0.9562 0.0113  0.0287  0.0483  7   DG  T "C1'" 
6613 N  N9    . DG  C 7   ? 0.7564 0.6972 0.9911 0.0080  0.0297  0.0321  7   DG  T N9    
6614 C  C8    . DG  C 7   ? 0.7739 0.7053 1.0017 0.0125  0.0358  0.0194  7   DG  T C8    
6615 N  N7    . DG  C 7   ? 0.6919 0.6182 0.9043 0.0074  0.0343  0.0071  7   DG  T N7    
6616 C  C5    . DG  C 7   ? 0.7039 0.6366 0.9139 -0.0006 0.0274  0.0121  7   DG  T C5    
6617 C  C6    . DG  C 7   ? 0.6944 0.6268 0.8921 -0.0082 0.0233  0.0047  7   DG  T C6    
6618 O  O6    . DG  C 7   ? 0.7141 0.6403 0.8999 -0.0100 0.0240  -0.0079 7   DG  T O6    
6619 N  N1    . DG  C 7   ? 0.5839 0.5250 0.7840 -0.0141 0.0179  0.0142  7   DG  T N1    
6620 C  C2    . DG  C 7   ? 0.6808 0.6300 0.8922 -0.0131 0.0161  0.0288  7   DG  T C2    
6621 N  N2    . DG  C 7   ? 0.6344 0.5917 0.8444 -0.0192 0.0113  0.0363  7   DG  T N2    
6622 N  N3    . DG  C 7   ? 0.7347 0.6846 0.9581 -0.0064 0.0190  0.0362  7   DG  T N3    
6623 C  C4    . DG  C 7   ? 0.6946 0.6361 0.9173 -0.0002 0.0248  0.0272  7   DG  T C4    
6624 P  P     . DG  C 8   ? 0.6537 0.5842 0.9694 0.0273  0.0382  0.0848  8   DG  T P     
6625 O  OP1   . DG  C 8   ? 0.7675 0.7051 1.1055 0.0323  0.0380  0.1036  8   DG  T OP1   
6626 O  OP2   . DG  C 8   ? 0.6422 0.5509 0.9538 0.0313  0.0464  0.0688  8   DG  T OP2   
6627 O  "O5'" . DG  C 8   ? 0.6932 0.6266 0.9984 0.0166  0.0306  0.0860  8   DG  T "O5'" 
6628 C  "C5'" . DG  C 8   ? 0.6559 0.6097 0.9546 0.0107  0.0222  0.0953  8   DG  T "C5'" 
6629 C  "C4'" . DG  C 8   ? 0.7249 0.6786 1.0166 0.0021  0.0174  0.0975  8   DG  T "C4'" 
6630 O  "O4'" . DG  C 8   ? 0.7920 0.7411 1.0653 -0.0031 0.0171  0.0815  8   DG  T "O4'" 
6631 C  "C3'" . DG  C 8   ? 0.7025 0.6411 1.0091 0.0025  0.0203  0.1034  8   DG  T "C3'" 
6632 O  "O3'" . DG  C 8   ? 0.6454 0.5938 0.9523 -0.0039 0.0146  0.1159  8   DG  T "O3'" 
6633 C  "C2'" . DG  C 8   ? 0.7062 0.6263 1.0040 0.0003  0.0242  0.0857  8   DG  T "C2'" 
6634 C  "C1'" . DG  C 8   ? 0.7301 0.6617 1.0061 -0.0055 0.0199  0.0757  8   DG  T "C1'" 
6635 N  N9    . DG  C 8   ? 0.7017 0.6219 0.9661 -0.0048 0.0235  0.0574  8   DG  T N9    
6636 C  C8    . DG  C 8   ? 0.7084 0.6196 0.9743 0.0027  0.0297  0.0490  8   DG  T C8    
6637 N  N7    . DG  C 8   ? 0.7435 0.6464 0.9954 0.0013  0.0314  0.0330  8   DG  T N7    
6638 C  C5    . DG  C 8   ? 0.6731 0.5802 0.9153 -0.0078 0.0257  0.0309  8   DG  T C5    
6639 C  C6    . DG  C 8   ? 0.7154 0.6183 0.9424 -0.0131 0.0241  0.0171  8   DG  T C6    
6640 O  O6    . DG  C 8   ? 0.7233 0.6177 0.9408 -0.0112 0.0270  0.0034  8   DG  T O6    
6641 N  N1    . DG  C 8   ? 0.7669 0.6777 0.9902 -0.0214 0.0186  0.0209  8   DG  T N1    
6642 C  C2    . DG  C 8   ? 0.7710 0.6921 1.0023 -0.0240 0.0155  0.0359  8   DG  T C2    
6643 N  N2    . DG  C 8   ? 0.6509 0.5790 0.8767 -0.0317 0.0115  0.0378  8   DG  T N2    
6644 N  N3    . DG  C 8   ? 0.7097 0.6346 0.9537 -0.0194 0.0164  0.0489  8   DG  T N3    
6645 C  C4    . DG  C 8   ? 0.6500 0.5676 0.8995 -0.0114 0.0214  0.0457  8   DG  T C4    
6646 P  P     . DC  C 9   ? 0.7011 0.6400 1.0273 -0.0038 0.0159  0.1295  9   DC  T P     
6647 O  OP1   . DC  C 9   ? 0.7312 0.6889 1.0600 -0.0067 0.0097  0.1481  9   DC  T OP1   
6648 O  OP2   . DC  C 9   ? 0.6639 0.5859 1.0078 0.0050  0.0231  0.1283  9   DC  T OP2   
6649 O  "O5'" . DC  C 9   ? 0.8017 0.7284 1.1204 -0.0112 0.0163  0.1199  9   DC  T "O5'" 
6650 C  "C5'" . DC  C 9   ? 0.7545 0.6919 1.0538 -0.0187 0.0120  0.1136  9   DC  T "C5'" 
6651 C  "C4'" . DC  C 9   ? 0.7881 0.7106 1.0826 -0.0237 0.0137  0.1002  9   DC  T "C4'" 
6652 O  "O4'" . DC  C 9   ? 0.7659 0.6796 1.0504 -0.0209 0.0166  0.0822  9   DC  T "O4'" 
6653 C  "C3'" . DC  C 9   ? 0.8015 0.7042 1.1141 -0.0236 0.0170  0.1037  9   DC  T "C3'" 
6654 O  "O3'" . DC  C 9   ? 0.7386 0.6447 1.0526 -0.0316 0.0141  0.1109  9   DC  T "O3'" 
6655 C  "C2'" . DC  C 9   ? 0.7747 0.6571 1.0831 -0.0222 0.0211  0.0839  9   DC  T "C2'" 
6656 C  "C1'" . DC  C 9   ? 0.7739 0.6682 1.0609 -0.0236 0.0190  0.0718  9   DC  T "C1'" 
6657 N  N1    . DC  C 9   ? 0.7272 0.6092 1.0073 -0.0187 0.0232  0.0551  9   DC  T N1    
6658 C  C2    . DC  C 9   ? 0.7095 0.5859 0.9750 -0.0234 0.0221  0.0391  9   DC  T C2    
6659 O  O2    . DC  C 9   ? 0.8111 0.6930 1.0715 -0.0315 0.0179  0.0396  9   DC  T O2    
6660 N  N3    . DC  C 9   ? 0.7415 0.6074 0.9989 -0.0189 0.0260  0.0243  9   DC  T N3    
6661 C  C4    . DC  C 9   ? 0.7691 0.6300 1.0331 -0.0097 0.0315  0.0250  9   DC  T C4    
6662 N  N4    . DC  C 9   ? 0.7727 0.6238 1.0273 -0.0051 0.0360  0.0103  9   DC  T N4    
6663 C  C5    . DC  C 9   ? 0.6891 0.5559 0.9699 -0.0045 0.0329  0.0415  9   DC  T C5    
6664 C  C6    . DC  C 9   ? 0.6942 0.5714 0.9822 -0.0094 0.0282  0.0561  9   DC  T C6    
6665 P  P     . DC  C 10  ? 0.7295 0.6174 1.0632 -0.0340 0.0161  0.1173  10  DC  T P     
6666 O  OP1   . DC  C 10  ? 0.6600 0.5624 1.0002 -0.0379 0.0132  0.1371  10  DC  T OP1   
6667 O  OP2   . DC  C 10  ? 0.8097 0.6786 1.1584 -0.0260 0.0213  0.1150  10  DC  T OP2   
6668 O  "O5'" . DC  C 10  ? 0.8624 0.7397 1.1877 -0.0415 0.0153  0.1017  10  DC  T "O5'" 
6669 C  "C5'" . DC  C 10  ? 0.7511 0.6445 1.0609 -0.0483 0.0116  0.0992  10  DC  T "C5'" 
6670 C  "C4'" . DC  C 10  ? 0.8853 0.7668 1.1901 -0.0546 0.0108  0.0839  10  DC  T "C4'" 
6671 O  "O4'" . DC  C 10  ? 0.8136 0.6854 1.1076 -0.0506 0.0124  0.0657  10  DC  T "O4'" 
6672 C  "C3'" . DC  C 10  ? 1.0359 0.8974 1.3585 -0.0587 0.0116  0.0855  10  DC  T "C3'" 
6673 O  "O3'" . DC  C 10  ? 1.2676 1.1301 1.5864 -0.0679 0.0085  0.0800  10  DC  T "O3'" 
6674 C  "C2'" . DC  C 10  ? 0.9612 0.8002 1.2851 -0.0530 0.0150  0.0707  10  DC  T "C2'" 
6675 C  "C1'" . DC  C 10  ? 0.9116 0.7592 1.2136 -0.0517 0.0141  0.0557  10  DC  T "C1'" 
6676 N  N1    . DC  C 10  ? 0.8928 0.7285 1.1902 -0.0432 0.0184  0.0439  10  DC  T N1    
6677 C  C2    . DC  C 10  ? 0.8992 0.7262 1.1819 -0.0440 0.0183  0.0246  10  DC  T C2    
6678 O  O2    . DC  C 10  ? 0.9002 0.7294 1.1751 -0.0520 0.0141  0.0179  10  DC  T O2    
6679 N  N3    . DC  C 10  ? 0.8842 0.7015 1.1621 -0.0357 0.0231  0.0147  10  DC  T N3    
6680 C  C4    . DC  C 10  ? 0.9190 0.7353 1.2076 -0.0269 0.0278  0.0234  10  DC  T C4    
6681 N  N4    . DC  C 10  ? 0.8341 0.6415 1.1184 -0.0185 0.0334  0.0138  10  DC  T N4    
6682 C  C5    . DC  C 10  ? 0.8773 0.7028 1.1820 -0.0263 0.0272  0.0433  10  DC  T C5    
6683 C  C6    . DC  C 10  ? 0.8784 0.7132 1.1860 -0.0345 0.0224  0.0528  10  DC  T C6    
6684 P  P     . DG  C 11  ? 1.0208 0.8736 1.3588 -0.0758 0.0074  0.0891  11  DG  T P     
6685 O  OP1   . DG  C 11  ? 0.9709 0.8453 1.3109 -0.0792 0.0063  0.1072  11  DG  T OP1   
6686 O  OP2   . DG  C 11  ? 0.9168 0.7460 1.2720 -0.0719 0.0103  0.0899  11  DG  T OP2   
6687 O  "O5'" . DG  C 11  ? 0.9903 0.8360 1.3215 -0.0838 0.0040  0.0729  11  DG  T "O5'" 
6688 C  "C5'" . DG  C 11  ? 1.0196 0.8658 1.3317 -0.0818 0.0031  0.0551  11  DG  T "C5'" 
6689 C  "C4'" . DG  C 11  ? 1.0329 0.8603 1.3450 -0.0877 0.0004  0.0390  11  DG  T "C4'" 
6690 O  "O4'" . DG  C 11  ? 1.0449 0.8548 1.3496 -0.0809 0.0029  0.0240  11  DG  T "O4'" 
6691 C  "C3'" . DG  C 11  ? 0.9405 0.7514 1.2733 -0.0946 -0.0010 0.0444  11  DG  T "C3'" 
6692 O  "O3'" . DG  C 11  ? 0.9462 0.7510 1.2766 -0.1038 -0.0061 0.0327  11  DG  T "O3'" 
6693 C  "C2'" . DG  C 11  ? 0.9131 0.6995 1.2539 -0.0875 0.0031  0.0398  11  DG  T "C2'" 
6694 C  "C1'" . DG  C 11  ? 0.9860 0.7708 1.3063 -0.0804 0.0049  0.0231  11  DG  T "C1'" 
6695 N  N9    . DG  C 11  ? 0.9558 0.7346 1.2783 -0.0691 0.0109  0.0254  11  DG  T N9    
6696 C  C8    . DG  C 11  ? 0.9603 0.7438 1.2976 -0.0640 0.0141  0.0431  11  DG  T C8    
6697 N  N7    . DG  C 11  ? 0.9572 0.7347 1.2947 -0.0538 0.0192  0.0415  11  DG  T N7    
6698 C  C5    . DG  C 11  ? 0.9778 0.7459 1.2987 -0.0518 0.0201  0.0212  11  DG  T C5    
6699 C  C6    . DG  C 11  ? 0.9556 0.7150 1.2692 -0.0418 0.0257  0.0111  11  DG  T C6    
6700 O  O6    . DG  C 11  ? 0.9412 0.6997 1.2635 -0.0324 0.0311  0.0185  11  DG  T O6    
6701 N  N1    . DG  C 11  ? 0.9180 0.6703 1.2130 -0.0434 0.0247  -0.0087 11  DG  T N1    
6702 C  C2    . DG  C 11  ? 0.9460 0.6996 1.2315 -0.0536 0.0183  -0.0174 11  DG  T C2    
6703 N  N2    . DG  C 11  ? 0.9744 0.7214 1.2416 -0.0537 0.0177  -0.0359 11  DG  T N2    
6704 N  N3    . DG  C 11  ? 0.8787 0.6408 1.1725 -0.0629 0.0130  -0.0079 11  DG  T N3    
6705 C  C4    . DG  C 11  ? 0.9149 0.6836 1.2259 -0.0613 0.0146  0.0112  11  DG  T C4    
6706 P  P     . DT  C 12  ? 0.8415 0.6235 1.1909 -0.1125 -0.0092 0.0312  12  DT  T P     
6707 O  OP1   . DT  C 12  ? 0.9412 0.7330 1.2898 -0.1234 -0.0153 0.0287  12  DT  T OP1   
6708 O  OP2   . DT  C 12  ? 0.9298 0.7062 1.3008 -0.1112 -0.0060 0.0490  12  DT  T OP2   
6709 O  "O5'" . DT  C 12  ? 0.9979 0.7528 1.3388 -0.1088 -0.0087 0.0102  12  DT  T "O5'" 
6710 C  "C5'" . DT  C 12  ? 0.9443 0.7031 1.2618 -0.1056 -0.0095 -0.0064 12  DT  T "C5'" 
6711 C  "C4'" . DT  C 12  ? 0.9542 0.6853 1.2650 -0.1022 -0.0081 -0.0251 12  DT  T "C4'" 
6712 O  "O4'" . DT  C 12  ? 0.9271 0.6534 1.2358 -0.0895 -0.0004 -0.0238 12  DT  T "O4'" 
6713 C  "C3'" . DT  C 12  ? 1.0422 0.7457 1.3695 -0.1088 -0.0104 -0.0288 12  DT  T "C3'" 
6714 O  "O3'" . DT  C 12  ? 1.0663 0.7535 1.3804 -0.1136 -0.0150 -0.0497 12  DT  T "O3'" 
6715 C  "C2'" . DT  C 12  ? 0.9574 0.6437 1.2951 -0.0985 -0.0025 -0.0246 12  DT  T "C2'" 
6716 C  "C1'" . DT  C 12  ? 1.0034 0.7002 1.3219 -0.0871 0.0027  -0.0304 12  DT  T "C1'" 
6717 N  N1    . DT  C 12  ? 0.9574 0.6533 1.2856 -0.0755 0.0106  -0.0193 12  DT  T N1    
6718 C  C2    . DT  C 12  ? 0.9674 0.6547 1.2848 -0.0646 0.0170  -0.0296 12  DT  T C2    
6719 O  O2    . DT  C 12  ? 0.9644 0.6444 1.2632 -0.0637 0.0168  -0.0478 12  DT  T O2    
6720 N  N3    . DT  C 12  ? 1.0207 0.7094 1.3505 -0.0545 0.0237  -0.0169 12  DT  T N3    
6721 C  C4    . DT  C 12  ? 0.9866 0.6842 1.3367 -0.0545 0.0241  0.0046  12  DT  T C4    
6722 O  O4    . DT  C 12  ? 0.8942 0.5934 1.2548 -0.0452 0.0297  0.0156  12  DT  T O4    
6723 C  C5    . DT  C 12  ? 0.9180 0.6241 1.2769 -0.0662 0.0176  0.0143  12  DT  T C5    
6724 C  C7    . DT  C 12  ? 0.8682 0.5850 1.2476 -0.0671 0.0178  0.0382  12  DT  T C7    
6725 C  C6    . DT  C 12  ? 0.9482 0.6530 1.2964 -0.0759 0.0115  0.0020  12  DT  T C6    
6726 P  P     . DG  C 13  ? 1.1478 0.8122 1.4750 -0.1261 -0.0220 -0.0562 13  DG  T P     
6727 O  OP1   . DG  C 13  ? 1.1596 0.8382 1.4788 -0.1370 -0.0310 -0.0613 13  DG  T OP1   
6728 O  OP2   . DG  C 13  ? 1.0458 0.7032 1.4003 -0.1277 -0.0198 -0.0389 13  DG  T OP2   
6729 O  "O5'" . DG  C 13  ? 1.1607 0.7931 1.4760 -0.1215 -0.0198 -0.0781 13  DG  T "O5'" 
6730 C  "C5'" . DG  C 13  ? 1.1030 0.7371 1.3910 -0.1172 -0.0197 -0.0955 13  DG  T "C5'" 
6731 C  "C4'" . DG  C 13  ? 1.1399 0.7481 1.4196 -0.1066 -0.0119 -0.1090 13  DG  T "C4'" 
6732 O  "O4'" . DG  C 13  ? 1.1044 0.7227 1.3891 -0.0936 -0.0023 -0.0965 13  DG  T "O4'" 
6733 C  "C3'" . DG  C 13  ? 1.1727 0.7468 1.4680 -0.1097 -0.0117 -0.1145 13  DG  T "C3'" 
6734 O  "O3'" . DG  C 13  ? 1.3017 0.8549 1.5828 -0.1181 -0.0188 -0.1363 13  DG  T "O3'" 
6735 C  "C2'" . DG  C 13  ? 1.2029 0.7629 1.5001 -0.0946 0.0003  -0.1146 13  DG  T "C2'" 
6736 C  "C1'" . DG  C 13  ? 1.1389 0.7306 1.4337 -0.0858 0.0052  -0.0993 13  DG  T "C1'" 
6737 N  N9    . DG  C 13  ? 1.1062 0.7056 1.4254 -0.0819 0.0095  -0.0769 13  DG  T N9    
6738 C  C8    . DG  C 13  ? 1.0354 0.6449 1.3749 -0.0904 0.0048  -0.0593 13  DG  T C8    
6739 N  N7    . DG  C 13  ? 1.0284 0.6443 1.3858 -0.0839 0.0103  -0.0405 13  DG  T N7    
6740 C  C5    . DG  C 13  ? 1.1225 0.7323 1.4721 -0.0703 0.0189  -0.0460 13  DG  T C5    
6741 C  C6    . DG  C 13  ? 1.1075 0.7210 1.4699 -0.0587 0.0269  -0.0318 13  DG  T C6    
6742 O  O6    . DG  C 13  ? 1.0466 0.6695 1.4291 -0.0581 0.0277  -0.0109 13  DG  T O6    
6743 N  N1    . DG  C 13  ? 1.0378 0.6437 1.3876 -0.0468 0.0345  -0.0433 13  DG  T N1    
6744 C  C2    . DG  C 13  ? 1.0579 0.6538 1.3840 -0.0461 0.0346  -0.0658 13  DG  T C2    
6745 N  N2    . DG  C 13  ? 1.0660 0.6567 1.3830 -0.0334 0.0434  -0.0734 13  DG  T N2    
6746 N  N3    . DG  C 13  ? 1.1058 0.6981 1.4184 -0.0570 0.0267  -0.0793 13  DG  T N3    
6747 C  C4    . DG  C 13  ? 1.1190 0.7188 1.4452 -0.0688 0.0189  -0.0683 13  DG  T C4    
6748 P  P     . DG  C 14  ? 1.3456 0.8859 1.5954 -0.1111 -0.0158 -0.1603 14  DG  T P     
6749 O  OP1   . DG  C 14  ? 1.0663 0.6351 1.2981 -0.1035 -0.0126 -0.1576 14  DG  T OP1   
6750 O  OP2   . DG  C 14  ? 1.2567 0.7792 1.4973 -0.1239 -0.0263 -0.1780 14  DG  T OP2   
6751 O  "O5'" . DG  C 14  ? 1.3283 0.8398 1.5833 -0.0986 -0.0042 -0.1656 14  DG  T "O5'" 
6752 C  "C5'" . DG  C 14  ? 1.4116 0.9242 1.6487 -0.0840 0.0061  -0.1728 14  DG  T "C5'" 
6753 C  "C4'" . DG  C 14  ? 1.3578 0.8472 1.6085 -0.0719 0.0179  -0.1712 14  DG  T "C4'" 
6754 O  "O4'" . DG  C 14  ? 1.2488 0.7531 1.5266 -0.0685 0.0213  -0.1463 14  DG  T "O4'" 
6755 C  "C3'" . DG  C 14  ? 1.4080 0.8578 1.6663 -0.0763 0.0170  -0.1846 14  DG  T "C3'" 
6756 O  "O3'" . DG  C 14  ? 1.5319 0.9585 1.7804 -0.0629 0.0286  -0.1980 14  DG  T "O3'" 
6757 C  "C2'" . DG  C 14  ? 1.3514 0.8000 1.6447 -0.0791 0.0169  -0.1633 14  DG  T "C2'" 
6758 C  "C1'" . DG  C 14  ? 1.3575 0.8338 1.6577 -0.0672 0.0250  -0.1438 14  DG  T "C1'" 
6759 N  N9    . DG  C 14  ? 1.3406 0.8319 1.6689 -0.0705 0.0233  -0.1186 14  DG  T N9    
6760 C  C8    . DG  C 14  ? 1.2334 0.7325 1.5755 -0.0846 0.0135  -0.1087 14  DG  T C8    
6761 N  N7    . DG  C 14  ? 1.1792 0.6923 1.5448 -0.0838 0.0150  -0.0852 14  DG  T N7    
6762 C  C5    . DG  C 14  ? 1.2312 0.7459 1.5994 -0.0686 0.0258  -0.0790 14  DG  T C5    
6763 C  C6    . DG  C 14  ? 1.1758 0.7039 1.5649 -0.0613 0.0311  -0.0556 14  DG  T C6    
6764 O  O6    . DG  C 14  ? 1.1448 0.6861 1.5533 -0.0668 0.0277  -0.0354 14  DG  T O6    
6765 N  N1    . DG  C 14  ? 1.1892 0.7153 1.5751 -0.0460 0.0414  -0.0565 14  DG  T N1    
6766 C  C2    . DG  C 14  ? 1.1861 0.6989 1.5510 -0.0383 0.0469  -0.0772 14  DG  T C2    
6767 N  N2    . DG  C 14  ? 1.2067 0.7210 1.5738 -0.0234 0.0574  -0.0734 14  DG  T N2    
6768 N  N3    . DG  C 14  ? 1.1759 0.6757 1.5192 -0.0447 0.0424  -0.0996 14  DG  T N3    
6769 C  C4    . DG  C 14  ? 1.2790 0.7806 1.6254 -0.0601 0.0313  -0.0991 14  DG  T C4    
6770 P  P     . DT  C 15  ? 1.6053 0.9883 1.8450 -0.0653 0.0287  -0.2226 15  DT  T P     
6771 O  OP1   . DT  C 15  ? 1.5007 0.8840 1.7134 -0.0769 0.0175  -0.2411 15  DT  T OP1   
6772 O  OP2   . DT  C 15  ? 1.4285 0.7892 1.6991 -0.0697 0.0280  -0.2141 15  DT  T OP2   
6773 O  "O5'" . DT  C 15  ? 1.6215 0.9912 1.8482 -0.0465 0.0446  -0.2327 15  DT  T "O5'" 
6774 C  "C5'" . DT  C 15  ? 1.5361 0.9289 1.7715 -0.0325 0.0551  -0.2155 15  DT  T "C5'" 
6775 C  "C4'" . DT  C 15  ? 1.5619 0.9369 1.8261 -0.0224 0.0655  -0.2044 15  DT  T "C4'" 
6776 O  "O4'" . DT  C 15  ? 1.5580 0.9549 1.8506 -0.0260 0.0618  -0.1776 15  DT  T "O4'" 
6777 C  "C3'" . DT  C 15  ? 1.6248 0.9574 1.8979 -0.0265 0.0653  -0.2178 15  DT  T "C3'" 
6778 O  "O3'" . DT  C 15  ? 1.7551 1.0596 2.0131 -0.0137 0.0775  -0.2375 15  DT  T "O3'" 
6779 C  "C2'" . DT  C 15  ? 1.5576 0.8884 1.8697 -0.0262 0.0667  -0.1945 15  DT  T "C2'" 
6780 C  "C1'" . DT  C 15  ? 1.5105 0.8838 1.8317 -0.0227 0.0668  -0.1695 15  DT  T "C1'" 
6781 N  N1    . DT  C 15  ? 1.3682 0.7564 1.7149 -0.0340 0.0577  -0.1476 15  DT  T N1    
6782 C  C2    . DT  C 15  ? 1.3118 0.7175 1.6841 -0.0274 0.0622  -0.1217 15  DT  T C2    
6783 O  O2    . DT  C 15  ? 1.2939 0.7042 1.6710 -0.0129 0.0729  -0.1150 15  DT  T O2    
6784 N  N3    . DT  C 15  ? 1.2227 0.6414 1.6147 -0.0390 0.0534  -0.1034 15  DT  T N3    
6785 C  C4    . DT  C 15  ? 1.3135 0.7299 1.7042 -0.0557 0.0414  -0.1078 15  DT  T C4    
6786 O  O4    . DT  C 15  ? 1.3060 0.7355 1.7157 -0.0648 0.0350  -0.0898 15  DT  T O4    
6787 C  C5    . DT  C 15  ? 1.3810 0.7793 1.7464 -0.0619 0.0367  -0.1347 15  DT  T C5    
6788 C  C7    . DT  C 15  ? 1.3868 0.7823 1.7506 -0.0803 0.0229  -0.1407 15  DT  T C7    
6789 C  C6    . DT  C 15  ? 1.3731 0.7582 1.7171 -0.0510 0.0448  -0.1532 15  DT  T C6    
6790 P  P     . DC  C 16  ? 1.9891 1.2842 2.2659 0.0060  0.0951  -0.2284 16  DC  T P     
6791 O  OP1   . DC  C 16  ? 1.7568 1.0905 2.0468 0.0130  0.0982  -0.2034 16  DC  T OP1   
6792 O  OP2   . DC  C 16  ? 1.5916 0.8619 1.8430 0.0167  0.1057  -0.2532 16  DC  T OP2   
6793 O  "O5'" . DC  C 16  ? 1.5723 0.8377 1.8821 0.0027  0.0949  -0.2217 16  DC  T "O5'" 
6794 C  "C5'" . DC  C 16  ? 1.5398 0.7881 1.8726 0.0180  0.1091  -0.2141 16  DC  T "C5'" 
6795 C  "C4'" . DC  C 16  ? 1.5889 0.8661 1.9531 0.0221  0.1103  -0.1817 16  DC  T "C4'" 
6796 O  "O4'" . DC  C 16  ? 1.5931 0.8950 1.9633 0.0058  0.0954  -0.1677 16  DC  T "O4'" 
6797 C  "C3'" . DC  C 16  ? 1.5277 0.7834 1.9274 0.0291  0.1176  -0.1683 16  DC  T "C3'" 
6798 O  "O3'" . DC  C 16  ? 1.5363 0.8146 1.9551 0.0429  0.1269  -0.1461 16  DC  T "O3'" 
6799 C  "C2'" . DC  C 16  ? 1.4224 0.6802 1.8415 0.0121  0.1039  -0.1553 16  DC  T "C2'" 
6800 C  "C1'" . DC  C 16  ? 1.4929 0.7912 1.8987 0.0029  0.0937  -0.1465 16  DC  T "C1'" 
6801 N  N1    . DC  C 16  ? 1.4046 0.7067 1.8136 -0.0166 0.0784  -0.1440 16  DC  T N1    
6802 C  C2    . DC  C 16  ? 1.3645 0.6890 1.7990 -0.0233 0.0724  -0.1171 16  DC  T C2    
6803 O  O2    . DC  C 16  ? 1.3488 0.6896 1.8022 -0.0133 0.0790  -0.0957 16  DC  T O2    
6804 N  N3    . DC  C 16  ? 1.4051 0.7336 1.8427 -0.0408 0.0593  -0.1151 16  DC  T N3    
6805 C  C4    . DC  C 16  ? 1.4261 0.7376 1.8437 -0.0517 0.0515  -0.1381 16  DC  T C4    
6806 N  N4    . DC  C 16  ? 1.3869 0.7043 1.8105 -0.0689 0.0386  -0.1341 16  DC  T N4    
6807 C  C5    . DC  C 16  ? 1.3609 0.6495 1.7514 -0.0455 0.0566  -0.1658 16  DC  T C5    
6808 C  C6    . DC  C 16  ? 1.3960 0.6803 1.7828 -0.0279 0.0704  -0.1678 16  DC  T C6    
6809 C  C1    . EDO D .   ? 0.7924 0.9207 0.9577 -0.0493 -0.0770 0.1192  801 EDO A C1    
6810 O  O1    . EDO D .   ? 0.8762 1.0048 1.0202 -0.0547 -0.0811 0.1082  801 EDO A O1    
6811 C  C2    . EDO D .   ? 0.9120 1.0371 1.0956 -0.0441 -0.0723 0.1169  801 EDO A C2    
6812 O  O2    . EDO D .   ? 1.0227 1.1371 1.1984 -0.0425 -0.0649 0.1020  801 EDO A O2    
6813 MG MG    . MG  E .   ? 0.7390 0.8642 0.9306 -0.0506 -0.0768 0.0724  802 MG  A MG    
6814 N  N1    . XG4 F .   ? 0.5979 0.6346 0.7297 -0.0147 0.0021  -0.0098 803 XG4 A N1    
6815 C  C2    . XG4 F .   ? 0.5494 0.5861 0.6893 -0.0088 0.0073  -0.0074 803 XG4 A C2    
6816 N  N2    . XG4 F .   ? 0.6372 0.6691 0.7721 -0.0047 0.0134  -0.0140 803 XG4 A N2    
6817 N  N3    . XG4 F .   ? 0.5261 0.5689 0.6797 -0.0068 0.0064  0.0025  803 XG4 A N3    
6818 C  C4    . XG4 F .   ? 0.5464 0.5949 0.7037 -0.0113 -0.0007 0.0095  803 XG4 A C4    
6819 C  C5    . XG4 F .   ? 0.5389 0.5867 0.6863 -0.0168 -0.0054 0.0068  803 XG4 A C5    
6820 C  C6    . XG4 F .   ? 0.5783 0.6200 0.7128 -0.0184 -0.0035 -0.0033 803 XG4 A C6    
6821 O  O6    . XG4 F .   ? 0.6080 0.6498 0.7349 -0.0227 -0.0067 -0.0053 803 XG4 A O6    
6822 N  N7    . XG4 F .   ? 0.5336 0.5875 0.6852 -0.0197 -0.0112 0.0145  803 XG4 A N7    
6823 C  C8    . XG4 F .   ? 0.6678 0.7267 0.8334 -0.0164 -0.0108 0.0226  803 XG4 A C8    
6824 N  N9    . XG4 F .   ? 0.6544 0.7097 0.8236 -0.0110 -0.0037 0.0193  803 XG4 A N9    
6825 P  PA    . XG4 F .   ? 0.6804 0.7658 0.8526 -0.0298 -0.0355 0.0421  803 XG4 A PA    
6826 P  PB    . XG4 F .   ? 0.6980 0.7956 0.8680 -0.0400 -0.0507 0.0423  803 XG4 A PB    
6827 P  PG    . XG4 F .   ? 0.7039 0.8029 0.8438 -0.0527 -0.0662 0.0377  803 XG4 A PG    
6828 C  "C1'" . XG4 F .   ? 0.6309 0.6928 0.8165 -0.0073 -0.0031 0.0292  803 XG4 A "C1'" 
6829 O  O1A   . XG4 F .   ? 0.6263 0.7060 0.7813 -0.0327 -0.0349 0.0306  803 XG4 A O1A   
6830 O  O1B   . XG4 F .   ? 0.6568 0.7486 0.8205 -0.0388 -0.0457 0.0323  803 XG4 A O1B   
6831 O  O1G   . XG4 F .   ? 0.9539 1.0625 1.1022 -0.0554 -0.0743 0.0495  803 XG4 A O1G   
6832 C  "C2'" . XG4 F .   ? 0.5880 0.6578 0.7766 -0.0076 -0.0040 0.0296  803 XG4 A "C2'" 
6833 O  O2A   . XG4 F .   ? 0.7491 0.8364 0.9210 -0.0316 -0.0393 0.0493  803 XG4 A O2A   
6834 O  O2B   . XG4 F .   ? 0.7658 0.8733 0.9479 -0.0435 -0.0588 0.0505  803 XG4 A O2B   
6835 O  O2G   . XG4 F .   ? 0.8649 0.9635 1.0056 -0.0552 -0.0687 0.0323  803 XG4 A O2G   
6836 C  "C3'" . XG4 F .   ? 0.6408 0.7190 0.8337 -0.0123 -0.0120 0.0359  803 XG4 A "C3'" 
6837 O  "O3'" . XG4 F .   ? 0.6522 0.7395 0.8576 -0.0113 -0.0126 0.0417  803 XG4 A "O3'" 
6838 N  N3A   . XG4 F .   ? 0.9978 1.0935 1.1803 -0.0325 -0.0424 0.0482  803 XG4 A N3A   
6839 O  O3B   . XG4 F .   ? 0.7442 0.8395 0.8962 -0.0449 -0.0554 0.0391  803 XG4 A O3B   
6840 O  O3G   . XG4 F .   ? 0.8931 0.9867 1.0131 -0.0548 -0.0653 0.0303  803 XG4 A O3G   
6841 C  "C4'" . XG4 F .   ? 0.6907 0.7701 0.8929 -0.0113 -0.0137 0.0447  803 XG4 A "C4'" 
6842 O  "O4'" . XG4 F .   ? 0.6196 0.6875 0.8118 -0.0101 -0.0092 0.0379  803 XG4 A "O4'" 
6843 C  "C5'" . XG4 F .   ? 0.7436 0.8295 0.9432 -0.0179 -0.0235 0.0492  803 XG4 A "C5'" 
6844 O  "O5'" . XG4 F .   ? 0.7267 0.8066 0.9095 -0.0218 -0.0252 0.0417  803 XG4 A "O5'" 
6845 C  C1    . EDO G .   ? 1.0346 0.8416 1.2456 0.0004  0.0466  -0.0463 101 EDO P C1    
6846 O  O1    . EDO G .   ? 1.0949 0.8868 1.3232 -0.0001 0.0477  -0.0405 101 EDO P O1    
6847 C  C2    . EDO G .   ? 1.0577 0.8853 1.2752 0.0058  0.0479  -0.0328 101 EDO P C2    
6848 O  O2    . EDO G .   ? 0.9783 0.8259 1.1847 0.0001  0.0415  -0.0310 101 EDO P O2    
6849 MG MG    . MG  H .   ? 0.7872 0.8849 0.9705 -0.0335 -0.0475 0.0673  102 MG  P MG    
6850 C  C1    . EDO I .   ? 0.9922 0.9334 1.0847 0.0020  0.0357  -0.0709 101 EDO T C1    
6851 O  O1    . EDO I .   ? 0.9478 0.9036 1.0478 -0.0005 0.0314  -0.0612 101 EDO T O1    
6852 C  C2    . EDO I .   ? 0.9932 0.9372 1.0723 0.0054  0.0389  -0.0773 101 EDO T C2    
6853 O  O2    . EDO I .   ? 1.0259 0.9548 1.0956 0.0083  0.0435  -0.0876 101 EDO T O2    
6854 O  O     . HOH J .   ? 0.6974 0.7772 0.8885 -0.0344 -0.0208 0.0122  901 HOH A O     
6855 O  O     . HOH J .   ? 0.6277 0.8494 0.9181 0.0358  0.0696  0.0204  902 HOH A O     
6856 O  O     . HOH J .   ? 0.6279 0.9021 0.8588 0.0660  0.2005  0.0306  903 HOH A O     
6857 O  O     . HOH J .   ? 0.8092 0.9308 0.9756 -0.0543 -0.0801 0.0712  904 HOH A O     
6858 O  O     . HOH J .   ? 0.8359 0.9608 1.0043 -0.0639 -0.0921 0.0614  905 HOH A O     
6859 O  O     . HOH J .   ? 0.5004 0.6637 0.8147 -0.0074 0.0118  0.0944  906 HOH A O     
6860 O  O     . HOH J .   ? 0.6001 0.6885 0.7787 -0.0277 -0.0305 0.0318  907 HOH A O     
6861 O  O     . HOH J .   ? 0.7731 0.8024 1.1281 0.1140  0.1245  0.0780  908 HOH A O     
6862 O  O     . HOH J .   ? 0.5939 0.6975 0.5997 0.0109  0.0273  -0.0244 909 HOH A O     
6863 O  O     . HOH J .   ? 0.7021 0.7849 0.8436 -0.0791 0.0090  0.0242  910 HOH A O     
6864 O  O     . HOH J .   ? 0.6981 0.8645 0.9537 0.0203  0.0603  0.0914  911 HOH A O     
6865 O  O     . HOH J .   ? 0.6120 0.6949 0.7140 -0.0171 -0.0039 -0.0410 912 HOH A O     
6866 O  O     . HOH J .   ? 0.9457 1.1213 0.7530 -0.0252 -0.0566 -0.0440 913 HOH A O     
6867 O  O     . HOH J .   ? 0.8194 0.9186 0.9764 -0.0431 -0.0566 0.0563  914 HOH A O     
6868 O  O     . HOH J .   ? 0.5672 0.6963 0.8514 0.0385  0.0053  0.0843  915 HOH A O     
6869 O  O     . HOH J .   ? 0.8554 1.2196 1.4285 -0.1802 0.0245  0.2150  916 HOH A O     
6870 O  O     . HOH J .   ? 0.5557 0.7212 0.7446 -0.0707 -0.0134 -0.0110 917 HOH A O     
6871 O  O     . HOH J .   ? 0.4974 0.6247 0.6170 0.0077  0.0244  0.0374  918 HOH A O     
6872 O  O     . HOH J .   ? 0.4942 0.5358 0.5615 -0.0089 0.0141  -0.0503 919 HOH A O     
6873 O  O     . HOH J .   ? 0.5589 0.6832 0.7164 0.0036  0.0217  0.0516  920 HOH A O     
6874 O  O     . HOH J .   ? 0.4499 0.5894 0.5538 -0.0153 -0.0223 -0.0123 921 HOH A O     
6875 O  O     . HOH J .   ? 0.6017 0.6929 0.7090 -0.0553 -0.0097 -0.0435 922 HOH A O     
6876 O  O     . HOH J .   ? 0.7002 0.9048 0.9456 -0.0978 -0.1676 0.1329  923 HOH A O     
6877 O  O     . HOH J .   ? 1.1964 1.1406 1.0598 -0.1140 -0.1216 -0.1496 924 HOH A O     
6878 O  O     . HOH J .   ? 0.6164 0.9686 1.0280 0.0735  0.1733  0.0851  925 HOH A O     
6879 O  O     . HOH J .   ? 0.8481 0.9520 1.0273 -0.0377 -0.0552 0.0800  926 HOH A O     
6880 O  O     . HOH J .   ? 0.8476 0.8109 1.2308 0.0076  0.0108  0.1922  927 HOH A O     
6881 O  O     . HOH J .   ? 0.9140 0.9512 0.8434 -0.0386 0.0047  -0.0877 928 HOH A O     
6882 O  O     . HOH J .   ? 0.5215 0.9010 0.7785 0.0062  -0.1017 0.1812  929 HOH A O     
6883 O  O     . HOH J .   ? 0.7894 1.0379 1.4331 -0.2272 0.0587  0.3757  930 HOH A O     
6884 O  O     . HOH K .   ? 0.8796 0.7909 1.1257 0.0383  0.0596  0.0127  201 HOH T O     
6885 O  O     . HOH K .   ? 0.7503 0.6472 0.9494 0.0109  0.0428  -0.0171 202 HOH T O     
# 
