data_9MDM
# 
_entry.id   9MDM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9MDM         pdb_00009mdm 10.2210/pdb9mdm/pdb 
WWPDB D_1000290783 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-12 
# 
_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             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9MDM 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'E64 inhibited' 9MDK unspecified 
PDB wild-type       9ARC unspecified 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 mgm22@buffalo.edu Michael           Malkowski G 'principal investigator/group leader' 0000-0002-1203-7463 
3 cli5@vcu.edu      'Chunhao (Chris)' Li        ? 'principal investigator/group leader' 0000-0002-1872-4870 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Clark, N.D.'     1 0000-0002-5939-736X 
'Malkowski, M.G.' 2 0000-0002-1203-7463 
# 
loop_
_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 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? US ? ? primary 'Acta Crystallogr.,Sect.F'       ACSFEN ?    2053-230X ? ? 81 ? 53 61 
;Structural insights into the role of the prosegment binding loop in a papain-superfamily cysteine protease from Treponema denticola.
;
2025 ? 10.1107/S2053230X25000378 39846228 ? ? 
? ? ? ? ? ? ? ?  ? ? 1       'Acta Crystallogr D Struct Biol' ?      0353 ?         ? ? ?  ? ?  ?  
'Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix' 2019 ? 
10.1107/S2059798319011471 31588918 ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Clark, N.D.'       1  ?                   
primary 'Li, C.'            2  0000-0002-1872-4870 
primary 'Malkowski, M.G.'   3  ?                   
1       'Liebschner, D.'    4  0000-0003-3921-3209 
1       'Afonine, P.V.'     5  0000-0002-5052-991X 
1       'Baker, M.L.'       6  ?                   
1       'Bunkoczi, G.'      7  ?                   
1       'Chen, V.B.'        8  0000-0003-2492-979X 
1       'Croll, T.I.'       9  ?                   
1       'Hintze, B.'        10 0000-0002-4871-2096 
1       'Hung, L.W.'        11 0000-0001-6690-8458 
1       'Jain, S.'          12 ?                   
1       'McCoy, A.J.'       13 ?                   
1       'Moriarty, N.W.'    14 0000-0001-8857-9464 
1       'Oeffner, R.D.'     15 0000-0003-3107-2202 
1       'Poon, B.K.'        16 0000-0001-9633-6067 
1       'Prisant, M.G.'     17 ?                   
1       'Read, R.J.'        18 0000-0001-8273-0047 
1       'Richardson, J.S.'  19 0000-0002-3311-2944 
1       'Richardson, D.C.'  20 ?                   
1       'Sammito, M.D.'     21 0000-0002-8346-9247 
1       'Sobolev, O.V.'     22 0000-0002-0623-3214 
1       'Stockwell, D.H.'   23 ?                   
1       'Terwilliger, T.C.' 24 0000-0001-6384-0320 
1       'Urzhumtsev, A.G.'  25 ?                   
1       'Videau, L.L.'      26 ?                   
1       'Williams, C.J.'    27 ?                   
1       'Adams, P.D.'       28 0000-0001-9333-8219 
# 
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 'Bacterial Ig-like domain protein C0362' 55489.352 1   ? C412S ? ? 
2 non-polymer syn 1,2-ETHANEDIOL                           62.068    8   ? ?     ? ? 
3 non-polymer syn 'PHOSPHATE ION'                          94.971    1   ? ?     ? ? 
4 non-polymer syn 'SODIUM ION'                             22.990    2   ? ?     ? ? 
5 water       nat water                                    18.015    320 ? ?     ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MTVTIEIKKKPQIKYEEKQAVMPESAAGTYTFEVQTIDGKLDYEPYFTSSTLPWITGAPTISSRTDPNKDVISFTCLKNK
TVWNRRAYIKFKDKKTGQYIKGADGKADLTVNIIQKKNENPVVHYKWVDGIGAPTENQKIKMKIKNNGIETEDYFTDPFV
FKWKETADTKFYNVRKLDKLYVQGQFPSNYFVINGIRNEQIQGRDISQSWAKTASNMLHWWFEQNKDYIEQYKQKAAIEE
WKRPLYKHDYIRGLQDEDEGKKSNIANIFRAYSHNNARGGYIEDGLTWYLYKRDGQKNLGSIYPGLFNDVFAHDTSPINI
ERCETKKEFEQLMNKTLDNKRAIGIFWQGSKGNRPYQHAVTCWGAAYDEDNNIICLYIAESNLPEAVLYPFGVRYKGNIY
EEAEKNRTYMFNYALSKPENIYIDGLTTLDKGEDQWKKWLEAHQKGELNSKLEGKPIPNPLLGLDSTRTGHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTVTIEIKKKPQIKYEEKQAVMPESAAGTYTFEVQTIDGKLDYEPYFTSSTLPWITGAPTISSRTDPNKDVISFTCLKNK
TVWNRRAYIKFKDKKTGQYIKGADGKADLTVNIIQKKNENPVVHYKWVDGIGAPTENQKIKMKIKNNGIETEDYFTDPFV
FKWKETADTKFYNVRKLDKLYVQGQFPSNYFVINGIRNEQIQGRDISQSWAKTASNMLHWWFEQNKDYIEQYKQKAAIEE
WKRPLYKHDYIRGLQDEDEGKKSNIANIFRAYSHNNARGGYIEDGLTWYLYKRDGQKNLGSIYPGLFNDVFAHDTSPINI
ERCETKKEFEQLMNKTLDNKRAIGIFWQGSKGNRPYQHAVTCWGAAYDEDNNIICLYIAESNLPEAVLYPFGVRYKGNIY
EEAEKNRTYMFNYALSKPENIYIDGLTTLDKGEDQWKKWLEAHQKGELNSKLEGKPIPNPLLGLDSTRTGHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 1,2-ETHANEDIOL  EDO 
3 'PHOSPHATE ION' PO4 
4 'SODIUM ION'    NA  
5 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   THR n 
1 3   VAL n 
1 4   THR n 
1 5   ILE n 
1 6   GLU n 
1 7   ILE n 
1 8   LYS n 
1 9   LYS n 
1 10  LYS n 
1 11  PRO n 
1 12  GLN n 
1 13  ILE n 
1 14  LYS n 
1 15  TYR n 
1 16  GLU n 
1 17  GLU n 
1 18  LYS n 
1 19  GLN n 
1 20  ALA n 
1 21  VAL n 
1 22  MET n 
1 23  PRO n 
1 24  GLU n 
1 25  SER n 
1 26  ALA n 
1 27  ALA n 
1 28  GLY n 
1 29  THR n 
1 30  TYR n 
1 31  THR n 
1 32  PHE n 
1 33  GLU n 
1 34  VAL n 
1 35  GLN n 
1 36  THR n 
1 37  ILE n 
1 38  ASP n 
1 39  GLY n 
1 40  LYS n 
1 41  LEU n 
1 42  ASP n 
1 43  TYR n 
1 44  GLU n 
1 45  PRO n 
1 46  TYR n 
1 47  PHE n 
1 48  THR n 
1 49  SER n 
1 50  SER n 
1 51  THR n 
1 52  LEU n 
1 53  PRO n 
1 54  TRP n 
1 55  ILE n 
1 56  THR n 
1 57  GLY n 
1 58  ALA n 
1 59  PRO n 
1 60  THR n 
1 61  ILE n 
1 62  SER n 
1 63  SER n 
1 64  ARG n 
1 65  THR n 
1 66  ASP n 
1 67  PRO n 
1 68  ASN n 
1 69  LYS n 
1 70  ASP n 
1 71  VAL n 
1 72  ILE n 
1 73  SER n 
1 74  PHE n 
1 75  THR n 
1 76  CYS n 
1 77  LEU n 
1 78  LYS n 
1 79  ASN n 
1 80  LYS n 
1 81  THR n 
1 82  VAL n 
1 83  TRP n 
1 84  ASN n 
1 85  ARG n 
1 86  ARG n 
1 87  ALA n 
1 88  TYR n 
1 89  ILE n 
1 90  LYS n 
1 91  PHE n 
1 92  LYS n 
1 93  ASP n 
1 94  LYS n 
1 95  LYS n 
1 96  THR n 
1 97  GLY n 
1 98  GLN n 
1 99  TYR n 
1 100 ILE n 
1 101 LYS n 
1 102 GLY n 
1 103 ALA n 
1 104 ASP n 
1 105 GLY n 
1 106 LYS n 
1 107 ALA n 
1 108 ASP n 
1 109 LEU n 
1 110 THR n 
1 111 VAL n 
1 112 ASN n 
1 113 ILE n 
1 114 ILE n 
1 115 GLN n 
1 116 LYS n 
1 117 LYS n 
1 118 ASN n 
1 119 GLU n 
1 120 ASN n 
1 121 PRO n 
1 122 VAL n 
1 123 VAL n 
1 124 HIS n 
1 125 TYR n 
1 126 LYS n 
1 127 TRP n 
1 128 VAL n 
1 129 ASP n 
1 130 GLY n 
1 131 ILE n 
1 132 GLY n 
1 133 ALA n 
1 134 PRO n 
1 135 THR n 
1 136 GLU n 
1 137 ASN n 
1 138 GLN n 
1 139 LYS n 
1 140 ILE n 
1 141 LYS n 
1 142 MET n 
1 143 LYS n 
1 144 ILE n 
1 145 LYS n 
1 146 ASN n 
1 147 ASN n 
1 148 GLY n 
1 149 ILE n 
1 150 GLU n 
1 151 THR n 
1 152 GLU n 
1 153 ASP n 
1 154 TYR n 
1 155 PHE n 
1 156 THR n 
1 157 ASP n 
1 158 PRO n 
1 159 PHE n 
1 160 VAL n 
1 161 PHE n 
1 162 LYS n 
1 163 TRP n 
1 164 LYS n 
1 165 GLU n 
1 166 THR n 
1 167 ALA n 
1 168 ASP n 
1 169 THR n 
1 170 LYS n 
1 171 PHE n 
1 172 TYR n 
1 173 ASN n 
1 174 VAL n 
1 175 ARG n 
1 176 LYS n 
1 177 LEU n 
1 178 ASP n 
1 179 LYS n 
1 180 LEU n 
1 181 TYR n 
1 182 VAL n 
1 183 GLN n 
1 184 GLY n 
1 185 GLN n 
1 186 PHE n 
1 187 PRO n 
1 188 SER n 
1 189 ASN n 
1 190 TYR n 
1 191 PHE n 
1 192 VAL n 
1 193 ILE n 
1 194 ASN n 
1 195 GLY n 
1 196 ILE n 
1 197 ARG n 
1 198 ASN n 
1 199 GLU n 
1 200 GLN n 
1 201 ILE n 
1 202 GLN n 
1 203 GLY n 
1 204 ARG n 
1 205 ASP n 
1 206 ILE n 
1 207 SER n 
1 208 GLN n 
1 209 SER n 
1 210 TRP n 
1 211 ALA n 
1 212 LYS n 
1 213 THR n 
1 214 ALA n 
1 215 SER n 
1 216 ASN n 
1 217 MET n 
1 218 LEU n 
1 219 HIS n 
1 220 TRP n 
1 221 TRP n 
1 222 PHE n 
1 223 GLU n 
1 224 GLN n 
1 225 ASN n 
1 226 LYS n 
1 227 ASP n 
1 228 TYR n 
1 229 ILE n 
1 230 GLU n 
1 231 GLN n 
1 232 TYR n 
1 233 LYS n 
1 234 GLN n 
1 235 LYS n 
1 236 ALA n 
1 237 ALA n 
1 238 ILE n 
1 239 GLU n 
1 240 GLU n 
1 241 TRP n 
1 242 LYS n 
1 243 ARG n 
1 244 PRO n 
1 245 LEU n 
1 246 TYR n 
1 247 LYS n 
1 248 HIS n 
1 249 ASP n 
1 250 TYR n 
1 251 ILE n 
1 252 ARG n 
1 253 GLY n 
1 254 LEU n 
1 255 GLN n 
1 256 ASP n 
1 257 GLU n 
1 258 ASP n 
1 259 GLU n 
1 260 GLY n 
1 261 LYS n 
1 262 LYS n 
1 263 SER n 
1 264 ASN n 
1 265 ILE n 
1 266 ALA n 
1 267 ASN n 
1 268 ILE n 
1 269 PHE n 
1 270 ARG n 
1 271 ALA n 
1 272 TYR n 
1 273 SER n 
1 274 HIS n 
1 275 ASN n 
1 276 ASN n 
1 277 ALA n 
1 278 ARG n 
1 279 GLY n 
1 280 GLY n 
1 281 TYR n 
1 282 ILE n 
1 283 GLU n 
1 284 ASP n 
1 285 GLY n 
1 286 LEU n 
1 287 THR n 
1 288 TRP n 
1 289 TYR n 
1 290 LEU n 
1 291 TYR n 
1 292 LYS n 
1 293 ARG n 
1 294 ASP n 
1 295 GLY n 
1 296 GLN n 
1 297 LYS n 
1 298 ASN n 
1 299 LEU n 
1 300 GLY n 
1 301 SER n 
1 302 ILE n 
1 303 TYR n 
1 304 PRO n 
1 305 GLY n 
1 306 LEU n 
1 307 PHE n 
1 308 ASN n 
1 309 ASP n 
1 310 VAL n 
1 311 PHE n 
1 312 ALA n 
1 313 HIS n 
1 314 ASP n 
1 315 THR n 
1 316 SER n 
1 317 PRO n 
1 318 ILE n 
1 319 ASN n 
1 320 ILE n 
1 321 GLU n 
1 322 ARG n 
1 323 CYS n 
1 324 GLU n 
1 325 THR n 
1 326 LYS n 
1 327 LYS n 
1 328 GLU n 
1 329 PHE n 
1 330 GLU n 
1 331 GLN n 
1 332 LEU n 
1 333 MET n 
1 334 ASN n 
1 335 LYS n 
1 336 THR n 
1 337 LEU n 
1 338 ASP n 
1 339 ASN n 
1 340 LYS n 
1 341 ARG n 
1 342 ALA n 
1 343 ILE n 
1 344 GLY n 
1 345 ILE n 
1 346 PHE n 
1 347 TRP n 
1 348 GLN n 
1 349 GLY n 
1 350 SER n 
1 351 LYS n 
1 352 GLY n 
1 353 ASN n 
1 354 ARG n 
1 355 PRO n 
1 356 TYR n 
1 357 GLN n 
1 358 HIS n 
1 359 ALA n 
1 360 VAL n 
1 361 THR n 
1 362 CYS n 
1 363 TRP n 
1 364 GLY n 
1 365 ALA n 
1 366 ALA n 
1 367 TYR n 
1 368 ASP n 
1 369 GLU n 
1 370 ASP n 
1 371 ASN n 
1 372 ASN n 
1 373 ILE n 
1 374 ILE n 
1 375 CYS n 
1 376 LEU n 
1 377 TYR n 
1 378 ILE n 
1 379 ALA n 
1 380 GLU n 
1 381 SER n 
1 382 ASN n 
1 383 LEU n 
1 384 PRO n 
1 385 GLU n 
1 386 ALA n 
1 387 VAL n 
1 388 LEU n 
1 389 TYR n 
1 390 PRO n 
1 391 PHE n 
1 392 GLY n 
1 393 VAL n 
1 394 ARG n 
1 395 TYR n 
1 396 LYS n 
1 397 GLY n 
1 398 ASN n 
1 399 ILE n 
1 400 TYR n 
1 401 GLU n 
1 402 GLU n 
1 403 ALA n 
1 404 GLU n 
1 405 LYS n 
1 406 ASN n 
1 407 ARG n 
1 408 THR n 
1 409 TYR n 
1 410 MET n 
1 411 PHE n 
1 412 ASN n 
1 413 TYR n 
1 414 ALA n 
1 415 LEU n 
1 416 SER n 
1 417 LYS n 
1 418 PRO n 
1 419 GLU n 
1 420 ASN n 
1 421 ILE n 
1 422 TYR n 
1 423 ILE n 
1 424 ASP n 
1 425 GLY n 
1 426 LEU n 
1 427 THR n 
1 428 THR n 
1 429 LEU n 
1 430 ASP n 
1 431 LYS n 
1 432 GLY n 
1 433 GLU n 
1 434 ASP n 
1 435 GLN n 
1 436 TRP n 
1 437 LYS n 
1 438 LYS n 
1 439 TRP n 
1 440 LEU n 
1 441 GLU n 
1 442 ALA n 
1 443 HIS n 
1 444 GLN n 
1 445 LYS n 
1 446 GLY n 
1 447 GLU n 
1 448 LEU n 
1 449 ASN n 
1 450 SER n 
1 451 LYS n 
1 452 LEU n 
1 453 GLU n 
1 454 GLY n 
1 455 LYS n 
1 456 PRO n 
1 457 ILE n 
1 458 PRO n 
1 459 ASN n 
1 460 PRO n 
1 461 LEU n 
1 462 LEU n 
1 463 GLY n 
1 464 LEU n 
1 465 ASP n 
1 466 SER n 
1 467 THR n 
1 468 ARG n 
1 469 THR n 
1 470 GLY n 
1 471 HIS n 
1 472 HIS n 
1 473 HIS n 
1 474 HIS n 
1 475 HIS n 
1 476 HIS 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                   476 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 TDE_0362 
_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      'Treponema denticola' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     158 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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               'BL21-CodonPlus (DE3)-RIL' 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET101/D 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ?                 'C3 H7 N O2 S'   121.158 
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 
NA  non-polymer         . 'SODIUM ION'    ?                 'Na 1'           22.990  
PHE 'L-peptide linking' y PHENYLALANINE   ?                 'C9 H11 N O2'    165.189 
PO4 non-polymer         . 'PHOSPHATE ION' ?                 'O4 P -3'        94.971  
PRO 'L-peptide linking' y PROLINE         ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   204 ?   ?   ?   A . n 
A 1 2   THR 2   205 ?   ?   ?   A . n 
A 1 3   VAL 3   206 ?   ?   ?   A . n 
A 1 4   THR 4   207 ?   ?   ?   A . n 
A 1 5   ILE 5   208 ?   ?   ?   A . n 
A 1 6   GLU 6   209 ?   ?   ?   A . n 
A 1 7   ILE 7   210 ?   ?   ?   A . n 
A 1 8   LYS 8   211 211 LYS LYS A . n 
A 1 9   LYS 9   212 212 LYS LYS A . n 
A 1 10  LYS 10  213 213 LYS LYS A . n 
A 1 11  PRO 11  214 214 PRO PRO A . n 
A 1 12  GLN 12  215 215 GLN GLN A . n 
A 1 13  ILE 13  216 216 ILE ILE A . n 
A 1 14  LYS 14  217 217 LYS LYS A . n 
A 1 15  TYR 15  218 218 TYR TYR A . n 
A 1 16  GLU 16  219 219 GLU GLU A . n 
A 1 17  GLU 17  220 220 GLU GLU A . n 
A 1 18  LYS 18  221 221 LYS LYS A . n 
A 1 19  GLN 19  222 222 GLN GLN A . n 
A 1 20  ALA 20  223 223 ALA ALA A . n 
A 1 21  VAL 21  224 224 VAL VAL A . n 
A 1 22  MET 22  225 225 MET MET A . n 
A 1 23  PRO 23  226 226 PRO PRO A . n 
A 1 24  GLU 24  227 227 GLU GLU A . n 
A 1 25  SER 25  228 228 SER SER A . n 
A 1 26  ALA 26  229 229 ALA ALA A . n 
A 1 27  ALA 27  230 230 ALA ALA A . n 
A 1 28  GLY 28  231 231 GLY GLY A . n 
A 1 29  THR 29  232 232 THR THR A . n 
A 1 30  TYR 30  233 233 TYR TYR A . n 
A 1 31  THR 31  234 234 THR THR A . n 
A 1 32  PHE 32  235 235 PHE PHE A . n 
A 1 33  GLU 33  236 236 GLU GLU A . n 
A 1 34  VAL 34  237 237 VAL VAL A . n 
A 1 35  GLN 35  238 238 GLN GLN A . n 
A 1 36  THR 36  239 239 THR THR A . n 
A 1 37  ILE 37  240 240 ILE ILE A . n 
A 1 38  ASP 38  241 241 ASP ASP A . n 
A 1 39  GLY 39  242 242 GLY GLY A . n 
A 1 40  LYS 40  243 243 LYS LYS A . n 
A 1 41  LEU 41  244 244 LEU LEU A . n 
A 1 42  ASP 42  245 245 ASP ASP A . n 
A 1 43  TYR 43  246 246 TYR TYR A . n 
A 1 44  GLU 44  247 247 GLU GLU A . n 
A 1 45  PRO 45  248 248 PRO PRO A . n 
A 1 46  TYR 46  249 249 TYR TYR A . n 
A 1 47  PHE 47  250 250 PHE PHE A . n 
A 1 48  THR 48  251 251 THR THR A . n 
A 1 49  SER 49  252 252 SER SER A . n 
A 1 50  SER 50  253 253 SER SER A . n 
A 1 51  THR 51  254 254 THR THR A . n 
A 1 52  LEU 52  255 255 LEU LEU A . n 
A 1 53  PRO 53  256 256 PRO PRO A . n 
A 1 54  TRP 54  257 257 TRP TRP A . n 
A 1 55  ILE 55  258 258 ILE ILE A . n 
A 1 56  THR 56  259 259 THR THR A . n 
A 1 57  GLY 57  260 260 GLY GLY A . n 
A 1 58  ALA 58  261 261 ALA ALA A . n 
A 1 59  PRO 59  262 262 PRO PRO A . n 
A 1 60  THR 60  263 263 THR THR A . n 
A 1 61  ILE 61  264 264 ILE ILE A . n 
A 1 62  SER 62  265 265 SER SER A . n 
A 1 63  SER 63  266 266 SER SER A . n 
A 1 64  ARG 64  267 267 ARG ARG A . n 
A 1 65  THR 65  268 268 THR THR A . n 
A 1 66  ASP 66  269 269 ASP ASP A . n 
A 1 67  PRO 67  270 270 PRO PRO A . n 
A 1 68  ASN 68  271 271 ASN ASN A . n 
A 1 69  LYS 69  272 272 LYS LYS A . n 
A 1 70  ASP 70  273 273 ASP ASP A . n 
A 1 71  VAL 71  274 274 VAL VAL A . n 
A 1 72  ILE 72  275 275 ILE ILE A . n 
A 1 73  SER 73  276 276 SER SER A . n 
A 1 74  PHE 74  277 277 PHE PHE A . n 
A 1 75  THR 75  278 278 THR THR A . n 
A 1 76  CYS 76  279 279 CYS CYS A . n 
A 1 77  LEU 77  280 280 LEU LEU A . n 
A 1 78  LYS 78  281 281 LYS LYS A . n 
A 1 79  ASN 79  282 282 ASN ASN A . n 
A 1 80  LYS 80  283 283 LYS LYS A . n 
A 1 81  THR 81  284 284 THR THR A . n 
A 1 82  VAL 82  285 285 VAL VAL A . n 
A 1 83  TRP 83  286 286 TRP TRP A . n 
A 1 84  ASN 84  287 287 ASN ASN A . n 
A 1 85  ARG 85  288 288 ARG ARG A . n 
A 1 86  ARG 86  289 289 ARG ARG A . n 
A 1 87  ALA 87  290 290 ALA ALA A . n 
A 1 88  TYR 88  291 291 TYR TYR A . n 
A 1 89  ILE 89  292 292 ILE ILE A . n 
A 1 90  LYS 90  293 293 LYS LYS A . n 
A 1 91  PHE 91  294 294 PHE PHE A . n 
A 1 92  LYS 92  295 295 LYS LYS A . n 
A 1 93  ASP 93  296 296 ASP ASP A . n 
A 1 94  LYS 94  297 297 LYS LYS A . n 
A 1 95  LYS 95  298 298 LYS LYS A . n 
A 1 96  THR 96  299 299 THR THR A . n 
A 1 97  GLY 97  300 300 GLY GLY A . n 
A 1 98  GLN 98  301 301 GLN GLN A . n 
A 1 99  TYR 99  302 302 TYR TYR A . n 
A 1 100 ILE 100 303 303 ILE ILE A . n 
A 1 101 LYS 101 304 304 LYS LYS A . n 
A 1 102 GLY 102 305 305 GLY GLY A . n 
A 1 103 ALA 103 306 306 ALA ALA A . n 
A 1 104 ASP 104 307 307 ASP ASP A . n 
A 1 105 GLY 105 308 308 GLY GLY A . n 
A 1 106 LYS 106 309 309 LYS LYS A . n 
A 1 107 ALA 107 310 310 ALA ALA A . n 
A 1 108 ASP 108 311 311 ASP ASP A . n 
A 1 109 LEU 109 312 312 LEU LEU A . n 
A 1 110 THR 110 313 313 THR THR A . n 
A 1 111 VAL 111 314 314 VAL VAL A . n 
A 1 112 ASN 112 315 315 ASN ASN A . n 
A 1 113 ILE 113 316 316 ILE ILE A . n 
A 1 114 ILE 114 317 317 ILE ILE A . n 
A 1 115 GLN 115 318 318 GLN GLN A . n 
A 1 116 LYS 116 319 319 LYS LYS A . n 
A 1 117 LYS 117 320 320 LYS LYS A . n 
A 1 118 ASN 118 321 321 ASN ASN A . n 
A 1 119 GLU 119 322 322 GLU GLU A . n 
A 1 120 ASN 120 323 323 ASN ASN A . n 
A 1 121 PRO 121 324 324 PRO PRO A . n 
A 1 122 VAL 122 325 325 VAL VAL A . n 
A 1 123 VAL 123 326 326 VAL VAL A . n 
A 1 124 HIS 124 327 327 HIS HIS A . n 
A 1 125 TYR 125 328 328 TYR TYR A . n 
A 1 126 LYS 126 329 329 LYS LYS A . n 
A 1 127 TRP 127 330 330 TRP TRP A . n 
A 1 128 VAL 128 331 331 VAL VAL A . n 
A 1 129 ASP 129 332 332 ASP ASP A . n 
A 1 130 GLY 130 333 333 GLY GLY A . n 
A 1 131 ILE 131 334 334 ILE ILE A . n 
A 1 132 GLY 132 335 335 GLY GLY A . n 
A 1 133 ALA 133 336 336 ALA ALA A . n 
A 1 134 PRO 134 337 337 PRO PRO A . n 
A 1 135 THR 135 338 338 THR THR A . n 
A 1 136 GLU 136 339 339 GLU GLU A . n 
A 1 137 ASN 137 340 340 ASN ASN A . n 
A 1 138 GLN 138 341 341 GLN GLN A . n 
A 1 139 LYS 139 342 342 LYS LYS A . n 
A 1 140 ILE 140 343 343 ILE ILE A . n 
A 1 141 LYS 141 344 344 LYS LYS A . n 
A 1 142 MET 142 345 345 MET MET A . n 
A 1 143 LYS 143 346 346 LYS LYS A . n 
A 1 144 ILE 144 347 347 ILE ILE A . n 
A 1 145 LYS 145 348 348 LYS LYS A . n 
A 1 146 ASN 146 349 349 ASN ASN A . n 
A 1 147 ASN 147 350 350 ASN ASN A . n 
A 1 148 GLY 148 351 351 GLY GLY A . n 
A 1 149 ILE 149 352 352 ILE ILE A . n 
A 1 150 GLU 150 353 353 GLU GLU A . n 
A 1 151 THR 151 354 354 THR THR A . n 
A 1 152 GLU 152 355 355 GLU GLU A . n 
A 1 153 ASP 153 356 356 ASP ASP A . n 
A 1 154 TYR 154 357 357 TYR TYR A . n 
A 1 155 PHE 155 358 358 PHE PHE A . n 
A 1 156 THR 156 359 359 THR THR A . n 
A 1 157 ASP 157 360 360 ASP ASP A . n 
A 1 158 PRO 158 361 361 PRO PRO A . n 
A 1 159 PHE 159 362 362 PHE PHE A . n 
A 1 160 VAL 160 363 363 VAL VAL A . n 
A 1 161 PHE 161 364 364 PHE PHE A . n 
A 1 162 LYS 162 365 365 LYS LYS A . n 
A 1 163 TRP 163 366 366 TRP TRP A . n 
A 1 164 LYS 164 367 367 LYS LYS A . n 
A 1 165 GLU 165 368 368 GLU GLU A . n 
A 1 166 THR 166 369 369 THR THR A . n 
A 1 167 ALA 167 370 370 ALA ALA A . n 
A 1 168 ASP 168 371 371 ASP ASP A . n 
A 1 169 THR 169 372 372 THR THR A . n 
A 1 170 LYS 170 373 373 LYS LYS A . n 
A 1 171 PHE 171 374 374 PHE PHE A . n 
A 1 172 TYR 172 375 375 TYR TYR A . n 
A 1 173 ASN 173 376 376 ASN ASN A . n 
A 1 174 VAL 174 377 377 VAL VAL A . n 
A 1 175 ARG 175 378 378 ARG ARG A . n 
A 1 176 LYS 176 379 379 LYS LYS A . n 
A 1 177 LEU 177 380 380 LEU LEU A . n 
A 1 178 ASP 178 381 381 ASP ASP A . n 
A 1 179 LYS 179 382 382 LYS LYS A . n 
A 1 180 LEU 180 383 383 LEU LEU A . n 
A 1 181 TYR 181 384 384 TYR TYR A . n 
A 1 182 VAL 182 385 385 VAL VAL A . n 
A 1 183 GLN 183 386 386 GLN GLN A . n 
A 1 184 GLY 184 387 387 GLY GLY A . n 
A 1 185 GLN 185 388 388 GLN GLN A . n 
A 1 186 PHE 186 389 389 PHE PHE A . n 
A 1 187 PRO 187 390 390 PRO PRO A . n 
A 1 188 SER 188 391 391 SER SER A . n 
A 1 189 ASN 189 392 392 ASN ASN A . n 
A 1 190 TYR 190 393 393 TYR TYR A . n 
A 1 191 PHE 191 394 394 PHE PHE A . n 
A 1 192 VAL 192 395 395 VAL VAL A . n 
A 1 193 ILE 193 396 396 ILE ILE A . n 
A 1 194 ASN 194 397 397 ASN ASN A . n 
A 1 195 GLY 195 398 398 GLY GLY A . n 
A 1 196 ILE 196 399 399 ILE ILE A . n 
A 1 197 ARG 197 400 400 ARG ARG A . n 
A 1 198 ASN 198 401 401 ASN ASN A . n 
A 1 199 GLU 199 402 402 GLU GLU A . n 
A 1 200 GLN 200 403 403 GLN GLN A . n 
A 1 201 ILE 201 404 404 ILE ILE A . n 
A 1 202 GLN 202 405 405 GLN GLN A . n 
A 1 203 GLY 203 406 406 GLY GLY A . n 
A 1 204 ARG 204 407 407 ARG ARG A . n 
A 1 205 ASP 205 408 408 ASP ASP A . n 
A 1 206 ILE 206 409 409 ILE ILE A . n 
A 1 207 SER 207 410 410 SER SER A . n 
A 1 208 GLN 208 411 411 GLN GLN A . n 
A 1 209 SER 209 412 412 SER SER A . n 
A 1 210 TRP 210 413 413 TRP TRP A . n 
A 1 211 ALA 211 414 414 ALA ALA A . n 
A 1 212 LYS 212 415 415 LYS LYS A . n 
A 1 213 THR 213 416 416 THR THR A . n 
A 1 214 ALA 214 417 417 ALA ALA A . n 
A 1 215 SER 215 418 418 SER SER A . n 
A 1 216 ASN 216 419 419 ASN ASN A . n 
A 1 217 MET 217 420 420 MET MET A . n 
A 1 218 LEU 218 421 421 LEU LEU A . n 
A 1 219 HIS 219 422 422 HIS HIS A . n 
A 1 220 TRP 220 423 423 TRP TRP A . n 
A 1 221 TRP 221 424 424 TRP TRP A . n 
A 1 222 PHE 222 425 425 PHE PHE A . n 
A 1 223 GLU 223 426 426 GLU GLU A . n 
A 1 224 GLN 224 427 427 GLN GLN A . n 
A 1 225 ASN 225 428 428 ASN ASN A . n 
A 1 226 LYS 226 429 429 LYS LYS A . n 
A 1 227 ASP 227 430 430 ASP ASP A . n 
A 1 228 TYR 228 431 431 TYR TYR A . n 
A 1 229 ILE 229 432 432 ILE ILE A . n 
A 1 230 GLU 230 433 433 GLU GLU A . n 
A 1 231 GLN 231 434 434 GLN GLN A . n 
A 1 232 TYR 232 435 435 TYR TYR A . n 
A 1 233 LYS 233 436 436 LYS LYS A . n 
A 1 234 GLN 234 437 437 GLN GLN A . n 
A 1 235 LYS 235 438 438 LYS LYS A . n 
A 1 236 ALA 236 439 439 ALA ALA A . n 
A 1 237 ALA 237 440 440 ALA ALA A . n 
A 1 238 ILE 238 441 441 ILE ILE A . n 
A 1 239 GLU 239 442 442 GLU GLU A . n 
A 1 240 GLU 240 443 443 GLU GLU A . n 
A 1 241 TRP 241 444 444 TRP TRP A . n 
A 1 242 LYS 242 445 445 LYS LYS A . n 
A 1 243 ARG 243 446 446 ARG ARG A . n 
A 1 244 PRO 244 447 447 PRO PRO A . n 
A 1 245 LEU 245 448 448 LEU LEU A . n 
A 1 246 TYR 246 449 449 TYR TYR A . n 
A 1 247 LYS 247 450 450 LYS LYS A . n 
A 1 248 HIS 248 451 451 HIS HIS A . n 
A 1 249 ASP 249 452 452 ASP ASP A . n 
A 1 250 TYR 250 453 453 TYR TYR A . n 
A 1 251 ILE 251 454 454 ILE ILE A . n 
A 1 252 ARG 252 455 455 ARG ARG A . n 
A 1 253 GLY 253 456 456 GLY GLY A . n 
A 1 254 LEU 254 457 457 LEU LEU A . n 
A 1 255 GLN 255 458 458 GLN GLN A . n 
A 1 256 ASP 256 459 459 ASP ASP A . n 
A 1 257 GLU 257 460 460 GLU GLU A . n 
A 1 258 ASP 258 461 461 ASP ASP A . n 
A 1 259 GLU 259 462 462 GLU GLU A . n 
A 1 260 GLY 260 463 463 GLY GLY A . n 
A 1 261 LYS 261 464 464 LYS LYS A . n 
A 1 262 LYS 262 465 465 LYS LYS A . n 
A 1 263 SER 263 466 466 SER SER A . n 
A 1 264 ASN 264 467 467 ASN ASN A . n 
A 1 265 ILE 265 468 468 ILE ILE A . n 
A 1 266 ALA 266 469 469 ALA ALA A . n 
A 1 267 ASN 267 470 470 ASN ASN A . n 
A 1 268 ILE 268 471 471 ILE ILE A . n 
A 1 269 PHE 269 472 472 PHE PHE A . n 
A 1 270 ARG 270 473 473 ARG ARG A . n 
A 1 271 ALA 271 474 474 ALA ALA A . n 
A 1 272 TYR 272 475 475 TYR TYR A . n 
A 1 273 SER 273 476 476 SER SER A . n 
A 1 274 HIS 274 477 477 HIS HIS A . n 
A 1 275 ASN 275 478 478 ASN ASN A . n 
A 1 276 ASN 276 479 479 ASN ASN A . n 
A 1 277 ALA 277 480 480 ALA ALA A . n 
A 1 278 ARG 278 481 481 ARG ARG A . n 
A 1 279 GLY 279 482 482 GLY GLY A . n 
A 1 280 GLY 280 483 483 GLY GLY A . n 
A 1 281 TYR 281 484 484 TYR TYR A . n 
A 1 282 ILE 282 485 485 ILE ILE A . n 
A 1 283 GLU 283 486 486 GLU GLU A . n 
A 1 284 ASP 284 487 487 ASP ASP A . n 
A 1 285 GLY 285 488 488 GLY GLY A . n 
A 1 286 LEU 286 489 489 LEU LEU A . n 
A 1 287 THR 287 490 490 THR THR A . n 
A 1 288 TRP 288 491 491 TRP TRP A . n 
A 1 289 TYR 289 492 492 TYR TYR A . n 
A 1 290 LEU 290 493 493 LEU LEU A . n 
A 1 291 TYR 291 494 494 TYR TYR A . n 
A 1 292 LYS 292 495 495 LYS LYS A . n 
A 1 293 ARG 293 496 496 ARG ARG A . n 
A 1 294 ASP 294 497 497 ASP ASP A . n 
A 1 295 GLY 295 498 498 GLY GLY A . n 
A 1 296 GLN 296 499 499 GLN GLN A . n 
A 1 297 LYS 297 500 500 LYS LYS A . n 
A 1 298 ASN 298 501 501 ASN ASN A . n 
A 1 299 LEU 299 502 502 LEU LEU A . n 
A 1 300 GLY 300 503 503 GLY GLY A . n 
A 1 301 SER 301 504 504 SER SER A . n 
A 1 302 ILE 302 505 505 ILE ILE A . n 
A 1 303 TYR 303 506 506 TYR TYR A . n 
A 1 304 PRO 304 507 507 PRO PRO A . n 
A 1 305 GLY 305 508 508 GLY GLY A . n 
A 1 306 LEU 306 509 509 LEU LEU A . n 
A 1 307 PHE 307 510 510 PHE PHE A . n 
A 1 308 ASN 308 511 511 ASN ASN A . n 
A 1 309 ASP 309 512 512 ASP ASP A . n 
A 1 310 VAL 310 513 513 VAL VAL A . n 
A 1 311 PHE 311 514 514 PHE PHE A . n 
A 1 312 ALA 312 515 515 ALA ALA A . n 
A 1 313 HIS 313 516 516 HIS HIS A . n 
A 1 314 ASP 314 517 517 ASP ASP A . n 
A 1 315 THR 315 518 518 THR THR A . n 
A 1 316 SER 316 519 519 SER SER A . n 
A 1 317 PRO 317 520 520 PRO PRO A . n 
A 1 318 ILE 318 521 521 ILE ILE A . n 
A 1 319 ASN 319 522 522 ASN ASN A . n 
A 1 320 ILE 320 523 523 ILE ILE A . n 
A 1 321 GLU 321 524 524 GLU GLU A . n 
A 1 322 ARG 322 525 525 ARG ARG A . n 
A 1 323 CYS 323 526 526 CYS CYS A . n 
A 1 324 GLU 324 527 527 GLU GLU A . n 
A 1 325 THR 325 528 528 THR THR A . n 
A 1 326 LYS 326 529 529 LYS LYS A . n 
A 1 327 LYS 327 530 530 LYS LYS A . n 
A 1 328 GLU 328 531 531 GLU GLU A . n 
A 1 329 PHE 329 532 532 PHE PHE A . n 
A 1 330 GLU 330 533 533 GLU GLU A . n 
A 1 331 GLN 331 534 534 GLN GLN A . n 
A 1 332 LEU 332 535 535 LEU LEU A . n 
A 1 333 MET 333 536 536 MET MET A . n 
A 1 334 ASN 334 537 537 ASN ASN A . n 
A 1 335 LYS 335 538 538 LYS LYS A . n 
A 1 336 THR 336 539 539 THR THR A . n 
A 1 337 LEU 337 540 540 LEU LEU A . n 
A 1 338 ASP 338 541 541 ASP ASP A . n 
A 1 339 ASN 339 542 542 ASN ASN A . n 
A 1 340 LYS 340 543 543 LYS LYS A . n 
A 1 341 ARG 341 544 544 ARG ARG A . n 
A 1 342 ALA 342 545 545 ALA ALA A . n 
A 1 343 ILE 343 546 546 ILE ILE A . n 
A 1 344 GLY 344 547 547 GLY GLY A . n 
A 1 345 ILE 345 548 548 ILE ILE A . n 
A 1 346 PHE 346 549 549 PHE PHE A . n 
A 1 347 TRP 347 550 550 TRP TRP A . n 
A 1 348 GLN 348 551 551 GLN GLN A . n 
A 1 349 GLY 349 552 552 GLY GLY A . n 
A 1 350 SER 350 553 553 SER SER A . n 
A 1 351 LYS 351 554 554 LYS LYS A . n 
A 1 352 GLY 352 555 555 GLY GLY A . n 
A 1 353 ASN 353 556 556 ASN ASN A . n 
A 1 354 ARG 354 557 557 ARG ARG A . n 
A 1 355 PRO 355 558 558 PRO PRO A . n 
A 1 356 TYR 356 559 559 TYR TYR A . n 
A 1 357 GLN 357 560 560 GLN GLN A . n 
A 1 358 HIS 358 561 561 HIS HIS A . n 
A 1 359 ALA 359 562 562 ALA ALA A . n 
A 1 360 VAL 360 563 563 VAL VAL A . n 
A 1 361 THR 361 564 564 THR THR A . n 
A 1 362 CYS 362 565 565 CYS CYS A . n 
A 1 363 TRP 363 566 566 TRP TRP A . n 
A 1 364 GLY 364 567 567 GLY GLY A . n 
A 1 365 ALA 365 568 568 ALA ALA A . n 
A 1 366 ALA 366 569 569 ALA ALA A . n 
A 1 367 TYR 367 570 570 TYR TYR A . n 
A 1 368 ASP 368 571 571 ASP ASP A . n 
A 1 369 GLU 369 572 572 GLU GLU A . n 
A 1 370 ASP 370 573 573 ASP ASP A . n 
A 1 371 ASN 371 574 574 ASN ASN A . n 
A 1 372 ASN 372 575 575 ASN ASN A . n 
A 1 373 ILE 373 576 576 ILE ILE A . n 
A 1 374 ILE 374 577 577 ILE ILE A . n 
A 1 375 CYS 375 578 578 CYS CYS A . n 
A 1 376 LEU 376 579 579 LEU LEU A . n 
A 1 377 TYR 377 580 580 TYR TYR A . n 
A 1 378 ILE 378 581 581 ILE ILE A . n 
A 1 379 ALA 379 582 582 ALA ALA A . n 
A 1 380 GLU 380 583 583 GLU GLU A . n 
A 1 381 SER 381 584 584 SER SER A . n 
A 1 382 ASN 382 585 585 ASN ASN A . n 
A 1 383 LEU 383 586 586 LEU LEU A . n 
A 1 384 PRO 384 587 587 PRO PRO A . n 
A 1 385 GLU 385 588 588 GLU GLU A . n 
A 1 386 ALA 386 589 589 ALA ALA A . n 
A 1 387 VAL 387 590 590 VAL VAL A . n 
A 1 388 LEU 388 591 591 LEU LEU A . n 
A 1 389 TYR 389 592 592 TYR TYR A . n 
A 1 390 PRO 390 593 593 PRO PRO A . n 
A 1 391 PHE 391 594 594 PHE PHE A . n 
A 1 392 GLY 392 595 595 GLY GLY A . n 
A 1 393 VAL 393 596 596 VAL VAL A . n 
A 1 394 ARG 394 597 597 ARG ARG A . n 
A 1 395 TYR 395 598 598 TYR TYR A . n 
A 1 396 LYS 396 599 599 LYS LYS A . n 
A 1 397 GLY 397 600 600 GLY GLY A . n 
A 1 398 ASN 398 601 601 ASN ASN A . n 
A 1 399 ILE 399 602 602 ILE ILE A . n 
A 1 400 TYR 400 603 603 TYR TYR A . n 
A 1 401 GLU 401 604 604 GLU GLU A . n 
A 1 402 GLU 402 605 605 GLU GLU A . n 
A 1 403 ALA 403 606 606 ALA ALA A . n 
A 1 404 GLU 404 607 607 GLU GLU A . n 
A 1 405 LYS 405 608 608 LYS LYS A . n 
A 1 406 ASN 406 609 609 ASN ASN A . n 
A 1 407 ARG 407 610 610 ARG ARG A . n 
A 1 408 THR 408 611 611 THR THR A . n 
A 1 409 TYR 409 612 612 TYR TYR A . n 
A 1 410 MET 410 613 613 MET MET A . n 
A 1 411 PHE 411 614 614 PHE PHE A . n 
A 1 412 ASN 412 615 615 ASN ASN A . n 
A 1 413 TYR 413 616 616 TYR TYR A . n 
A 1 414 ALA 414 617 617 ALA ALA A . n 
A 1 415 LEU 415 618 618 LEU LEU A . n 
A 1 416 SER 416 619 619 SER SER A . n 
A 1 417 LYS 417 620 620 LYS LYS A . n 
A 1 418 PRO 418 621 621 PRO PRO A . n 
A 1 419 GLU 419 622 622 GLU GLU A . n 
A 1 420 ASN 420 623 623 ASN ASN A . n 
A 1 421 ILE 421 624 624 ILE ILE A . n 
A 1 422 TYR 422 625 625 TYR TYR A . n 
A 1 423 ILE 423 626 626 ILE ILE A . n 
A 1 424 ASP 424 627 627 ASP ASP A . n 
A 1 425 GLY 425 628 628 GLY GLY A . n 
A 1 426 LEU 426 629 629 LEU LEU A . n 
A 1 427 THR 427 630 630 THR THR A . n 
A 1 428 THR 428 631 631 THR THR A . n 
A 1 429 LEU 429 632 632 LEU LEU A . n 
A 1 430 ASP 430 633 633 ASP ASP A . n 
A 1 431 LYS 431 634 634 LYS LYS A . n 
A 1 432 GLY 432 635 635 GLY GLY A . n 
A 1 433 GLU 433 636 636 GLU GLU A . n 
A 1 434 ASP 434 637 637 ASP ASP A . n 
A 1 435 GLN 435 638 638 GLN GLN A . n 
A 1 436 TRP 436 639 639 TRP TRP A . n 
A 1 437 LYS 437 640 640 LYS LYS A . n 
A 1 438 LYS 438 641 641 LYS LYS A . n 
A 1 439 TRP 439 642 642 TRP TRP A . n 
A 1 440 LEU 440 643 643 LEU LEU A . n 
A 1 441 GLU 441 644 644 GLU GLU A . n 
A 1 442 ALA 442 645 645 ALA ALA A . n 
A 1 443 HIS 443 646 646 HIS HIS A . n 
A 1 444 GLN 444 647 647 GLN GLN A . n 
A 1 445 LYS 445 648 ?   ?   ?   A . n 
A 1 446 GLY 446 649 ?   ?   ?   A . n 
A 1 447 GLU 447 650 ?   ?   ?   A . n 
A 1 448 LEU 448 651 ?   ?   ?   A . n 
A 1 449 ASN 449 652 ?   ?   ?   A . n 
A 1 450 SER 450 653 ?   ?   ?   A . n 
A 1 451 LYS 451 654 ?   ?   ?   A . n 
A 1 452 LEU 452 655 ?   ?   ?   A . n 
A 1 453 GLU 453 656 ?   ?   ?   A . n 
A 1 454 GLY 454 657 ?   ?   ?   A . n 
A 1 455 LYS 455 658 ?   ?   ?   A . n 
A 1 456 PRO 456 659 ?   ?   ?   A . n 
A 1 457 ILE 457 660 ?   ?   ?   A . n 
A 1 458 PRO 458 661 ?   ?   ?   A . n 
A 1 459 ASN 459 662 ?   ?   ?   A . n 
A 1 460 PRO 460 663 ?   ?   ?   A . n 
A 1 461 LEU 461 664 ?   ?   ?   A . n 
A 1 462 LEU 462 665 ?   ?   ?   A . n 
A 1 463 GLY 463 666 ?   ?   ?   A . n 
A 1 464 LEU 464 667 ?   ?   ?   A . n 
A 1 465 ASP 465 668 ?   ?   ?   A . n 
A 1 466 SER 466 669 ?   ?   ?   A . n 
A 1 467 THR 467 670 ?   ?   ?   A . n 
A 1 468 ARG 468 671 ?   ?   ?   A . n 
A 1 469 THR 469 672 ?   ?   ?   A . n 
A 1 470 GLY 470 673 ?   ?   ?   A . n 
A 1 471 HIS 471 674 ?   ?   ?   A . n 
A 1 472 HIS 472 675 ?   ?   ?   A . n 
A 1 473 HIS 473 676 ?   ?   ?   A . n 
A 1 474 HIS 474 677 ?   ?   ?   A . n 
A 1 475 HIS 475 678 ?   ?   ?   A . n 
A 1 476 HIS 476 679 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        PO4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   PO4 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 EDO 1   701  702 EDO EDO A . 
C 2 EDO 1   702  705 EDO EDO A . 
D 3 PO4 1   703  706 PO4 PO4 A . 
E 2 EDO 1   704  707 EDO EDO A . 
F 4 NA  1   705  709 NA  NA  A . 
G 4 NA  1   706  710 NA  NA  A . 
H 2 EDO 1   707  716 EDO EDO A . 
I 2 EDO 1   708  720 EDO EDO A . 
J 2 EDO 1   709  721 EDO EDO A . 
K 2 EDO 1   710  722 EDO EDO A . 
L 2 EDO 1   711  723 EDO EDO A . 
M 5 HOH 1   801  387 HOH HOH A . 
M 5 HOH 2   802  190 HOH HOH A . 
M 5 HOH 3   803  86  HOH HOH A . 
M 5 HOH 4   804  167 HOH HOH A . 
M 5 HOH 5   805  208 HOH HOH A . 
M 5 HOH 6   806  48  HOH HOH A . 
M 5 HOH 7   807  268 HOH HOH A . 
M 5 HOH 8   808  244 HOH HOH A . 
M 5 HOH 9   809  136 HOH HOH A . 
M 5 HOH 10  810  388 HOH HOH A . 
M 5 HOH 11  811  34  HOH HOH A . 
M 5 HOH 12  812  243 HOH HOH A . 
M 5 HOH 13  813  124 HOH HOH A . 
M 5 HOH 14  814  133 HOH HOH A . 
M 5 HOH 15  815  298 HOH HOH A . 
M 5 HOH 16  816  128 HOH HOH A . 
M 5 HOH 17  817  211 HOH HOH A . 
M 5 HOH 18  818  112 HOH HOH A . 
M 5 HOH 19  819  371 HOH HOH A . 
M 5 HOH 20  820  143 HOH HOH A . 
M 5 HOH 21  821  182 HOH HOH A . 
M 5 HOH 22  822  283 HOH HOH A . 
M 5 HOH 23  823  187 HOH HOH A . 
M 5 HOH 24  824  196 HOH HOH A . 
M 5 HOH 25  825  333 HOH HOH A . 
M 5 HOH 26  826  107 HOH HOH A . 
M 5 HOH 27  827  226 HOH HOH A . 
M 5 HOH 28  828  184 HOH HOH A . 
M 5 HOH 29  829  355 HOH HOH A . 
M 5 HOH 30  830  92  HOH HOH A . 
M 5 HOH 31  831  304 HOH HOH A . 
M 5 HOH 32  832  145 HOH HOH A . 
M 5 HOH 33  833  369 HOH HOH A . 
M 5 HOH 34  834  2   HOH HOH A . 
M 5 HOH 35  835  302 HOH HOH A . 
M 5 HOH 36  836  316 HOH HOH A . 
M 5 HOH 37  837  102 HOH HOH A . 
M 5 HOH 38  838  346 HOH HOH A . 
M 5 HOH 39  839  363 HOH HOH A . 
M 5 HOH 40  840  40  HOH HOH A . 
M 5 HOH 41  841  135 HOH HOH A . 
M 5 HOH 42  842  131 HOH HOH A . 
M 5 HOH 43  843  1   HOH HOH A . 
M 5 HOH 44  844  183 HOH HOH A . 
M 5 HOH 45  845  15  HOH HOH A . 
M 5 HOH 46  846  340 HOH HOH A . 
M 5 HOH 47  847  217 HOH HOH A . 
M 5 HOH 48  848  29  HOH HOH A . 
M 5 HOH 49  849  391 HOH HOH A . 
M 5 HOH 50  850  291 HOH HOH A . 
M 5 HOH 51  851  272 HOH HOH A . 
M 5 HOH 52  852  109 HOH HOH A . 
M 5 HOH 53  853  66  HOH HOH A . 
M 5 HOH 54  854  252 HOH HOH A . 
M 5 HOH 55  855  21  HOH HOH A . 
M 5 HOH 56  856  75  HOH HOH A . 
M 5 HOH 57  857  26  HOH HOH A . 
M 5 HOH 58  858  161 HOH HOH A . 
M 5 HOH 59  859  157 HOH HOH A . 
M 5 HOH 60  860  238 HOH HOH A . 
M 5 HOH 61  861  93  HOH HOH A . 
M 5 HOH 62  862  313 HOH HOH A . 
M 5 HOH 63  863  292 HOH HOH A . 
M 5 HOH 64  864  42  HOH HOH A . 
M 5 HOH 65  865  134 HOH HOH A . 
M 5 HOH 66  866  239 HOH HOH A . 
M 5 HOH 67  867  33  HOH HOH A . 
M 5 HOH 68  868  41  HOH HOH A . 
M 5 HOH 69  869  153 HOH HOH A . 
M 5 HOH 70  870  214 HOH HOH A . 
M 5 HOH 71  871  329 HOH HOH A . 
M 5 HOH 72  872  99  HOH HOH A . 
M 5 HOH 73  873  17  HOH HOH A . 
M 5 HOH 74  874  142 HOH HOH A . 
M 5 HOH 75  875  5   HOH HOH A . 
M 5 HOH 76  876  179 HOH HOH A . 
M 5 HOH 77  877  123 HOH HOH A . 
M 5 HOH 78  878  237 HOH HOH A . 
M 5 HOH 79  879  192 HOH HOH A . 
M 5 HOH 80  880  365 HOH HOH A . 
M 5 HOH 81  881  246 HOH HOH A . 
M 5 HOH 82  882  7   HOH HOH A . 
M 5 HOH 83  883  276 HOH HOH A . 
M 5 HOH 84  884  293 HOH HOH A . 
M 5 HOH 85  885  16  HOH HOH A . 
M 5 HOH 86  886  71  HOH HOH A . 
M 5 HOH 87  887  3   HOH HOH A . 
M 5 HOH 88  888  84  HOH HOH A . 
M 5 HOH 89  889  6   HOH HOH A . 
M 5 HOH 90  890  19  HOH HOH A . 
M 5 HOH 91  891  10  HOH HOH A . 
M 5 HOH 92  892  13  HOH HOH A . 
M 5 HOH 93  893  70  HOH HOH A . 
M 5 HOH 94  894  218 HOH HOH A . 
M 5 HOH 95  895  168 HOH HOH A . 
M 5 HOH 96  896  224 HOH HOH A . 
M 5 HOH 97  897  60  HOH HOH A . 
M 5 HOH 98  898  256 HOH HOH A . 
M 5 HOH 99  899  47  HOH HOH A . 
M 5 HOH 100 900  171 HOH HOH A . 
M 5 HOH 101 901  203 HOH HOH A . 
M 5 HOH 102 902  32  HOH HOH A . 
M 5 HOH 103 903  11  HOH HOH A . 
M 5 HOH 104 904  350 HOH HOH A . 
M 5 HOH 105 905  144 HOH HOH A . 
M 5 HOH 106 906  87  HOH HOH A . 
M 5 HOH 107 907  147 HOH HOH A . 
M 5 HOH 108 908  149 HOH HOH A . 
M 5 HOH 109 909  14  HOH HOH A . 
M 5 HOH 110 910  58  HOH HOH A . 
M 5 HOH 111 911  280 HOH HOH A . 
M 5 HOH 112 912  366 HOH HOH A . 
M 5 HOH 113 913  180 HOH HOH A . 
M 5 HOH 114 914  222 HOH HOH A . 
M 5 HOH 115 915  91  HOH HOH A . 
M 5 HOH 116 916  57  HOH HOH A . 
M 5 HOH 117 917  204 HOH HOH A . 
M 5 HOH 118 918  207 HOH HOH A . 
M 5 HOH 119 919  310 HOH HOH A . 
M 5 HOH 120 920  9   HOH HOH A . 
M 5 HOH 121 921  236 HOH HOH A . 
M 5 HOH 122 922  393 HOH HOH A . 
M 5 HOH 123 923  400 HOH HOH A . 
M 5 HOH 124 924  52  HOH HOH A . 
M 5 HOH 125 925  337 HOH HOH A . 
M 5 HOH 126 926  223 HOH HOH A . 
M 5 HOH 127 927  53  HOH HOH A . 
M 5 HOH 128 928  248 HOH HOH A . 
M 5 HOH 129 929  8   HOH HOH A . 
M 5 HOH 130 930  39  HOH HOH A . 
M 5 HOH 131 931  286 HOH HOH A . 
M 5 HOH 132 932  83  HOH HOH A . 
M 5 HOH 133 933  137 HOH HOH A . 
M 5 HOH 134 934  225 HOH HOH A . 
M 5 HOH 135 935  101 HOH HOH A . 
M 5 HOH 136 936  50  HOH HOH A . 
M 5 HOH 137 937  212 HOH HOH A . 
M 5 HOH 138 938  113 HOH HOH A . 
M 5 HOH 139 939  36  HOH HOH A . 
M 5 HOH 140 940  206 HOH HOH A . 
M 5 HOH 141 941  68  HOH HOH A . 
M 5 HOH 142 942  140 HOH HOH A . 
M 5 HOH 143 943  155 HOH HOH A . 
M 5 HOH 144 944  151 HOH HOH A . 
M 5 HOH 145 945  63  HOH HOH A . 
M 5 HOH 146 946  269 HOH HOH A . 
M 5 HOH 147 947  72  HOH HOH A . 
M 5 HOH 148 948  117 HOH HOH A . 
M 5 HOH 149 949  118 HOH HOH A . 
M 5 HOH 150 950  12  HOH HOH A . 
M 5 HOH 151 951  27  HOH HOH A . 
M 5 HOH 152 952  4   HOH HOH A . 
M 5 HOH 153 953  130 HOH HOH A . 
M 5 HOH 154 954  176 HOH HOH A . 
M 5 HOH 155 955  25  HOH HOH A . 
M 5 HOH 156 956  328 HOH HOH A . 
M 5 HOH 157 957  285 HOH HOH A . 
M 5 HOH 158 958  325 HOH HOH A . 
M 5 HOH 159 959  100 HOH HOH A . 
M 5 HOH 160 960  221 HOH HOH A . 
M 5 HOH 161 961  361 HOH HOH A . 
M 5 HOH 162 962  35  HOH HOH A . 
M 5 HOH 163 963  45  HOH HOH A . 
M 5 HOH 164 964  172 HOH HOH A . 
M 5 HOH 165 965  317 HOH HOH A . 
M 5 HOH 166 966  104 HOH HOH A . 
M 5 HOH 167 967  79  HOH HOH A . 
M 5 HOH 168 968  76  HOH HOH A . 
M 5 HOH 169 969  379 HOH HOH A . 
M 5 HOH 170 970  386 HOH HOH A . 
M 5 HOH 171 971  174 HOH HOH A . 
M 5 HOH 172 972  55  HOH HOH A . 
M 5 HOH 173 973  370 HOH HOH A . 
M 5 HOH 174 974  305 HOH HOH A . 
M 5 HOH 175 975  80  HOH HOH A . 
M 5 HOH 176 976  399 HOH HOH A . 
M 5 HOH 177 977  127 HOH HOH A . 
M 5 HOH 178 978  23  HOH HOH A . 
M 5 HOH 179 979  202 HOH HOH A . 
M 5 HOH 180 980  28  HOH HOH A . 
M 5 HOH 181 981  132 HOH HOH A . 
M 5 HOH 182 982  162 HOH HOH A . 
M 5 HOH 183 983  312 HOH HOH A . 
M 5 HOH 184 984  264 HOH HOH A . 
M 5 HOH 185 985  170 HOH HOH A . 
M 5 HOH 186 986  106 HOH HOH A . 
M 5 HOH 187 987  74  HOH HOH A . 
M 5 HOH 188 988  65  HOH HOH A . 
M 5 HOH 189 989  210 HOH HOH A . 
M 5 HOH 190 990  213 HOH HOH A . 
M 5 HOH 191 991  367 HOH HOH A . 
M 5 HOH 192 992  209 HOH HOH A . 
M 5 HOH 193 993  200 HOH HOH A . 
M 5 HOH 194 994  67  HOH HOH A . 
M 5 HOH 195 995  141 HOH HOH A . 
M 5 HOH 196 996  81  HOH HOH A . 
M 5 HOH 197 997  94  HOH HOH A . 
M 5 HOH 198 998  89  HOH HOH A . 
M 5 HOH 199 999  232 HOH HOH A . 
M 5 HOH 200 1000 175 HOH HOH A . 
M 5 HOH 201 1001 231 HOH HOH A . 
M 5 HOH 202 1002 358 HOH HOH A . 
M 5 HOH 203 1003 120 HOH HOH A . 
M 5 HOH 204 1004 85  HOH HOH A . 
M 5 HOH 205 1005 38  HOH HOH A . 
M 5 HOH 206 1006 233 HOH HOH A . 
M 5 HOH 207 1007 273 HOH HOH A . 
M 5 HOH 208 1008 277 HOH HOH A . 
M 5 HOH 209 1009 77  HOH HOH A . 
M 5 HOH 210 1010 219 HOH HOH A . 
M 5 HOH 211 1011 78  HOH HOH A . 
M 5 HOH 212 1012 115 HOH HOH A . 
M 5 HOH 213 1013 56  HOH HOH A . 
M 5 HOH 214 1014 122 HOH HOH A . 
M 5 HOH 215 1015 195 HOH HOH A . 
M 5 HOH 216 1016 281 HOH HOH A . 
M 5 HOH 217 1017 332 HOH HOH A . 
M 5 HOH 218 1018 228 HOH HOH A . 
M 5 HOH 219 1019 339 HOH HOH A . 
M 5 HOH 220 1020 154 HOH HOH A . 
M 5 HOH 221 1021 138 HOH HOH A . 
M 5 HOH 222 1022 240 HOH HOH A . 
M 5 HOH 223 1023 324 HOH HOH A . 
M 5 HOH 224 1024 108 HOH HOH A . 
M 5 HOH 225 1025 378 HOH HOH A . 
M 5 HOH 226 1026 96  HOH HOH A . 
M 5 HOH 227 1027 368 HOH HOH A . 
M 5 HOH 228 1028 290 HOH HOH A . 
M 5 HOH 229 1029 282 HOH HOH A . 
M 5 HOH 230 1030 189 HOH HOH A . 
M 5 HOH 231 1031 148 HOH HOH A . 
M 5 HOH 232 1032 216 HOH HOH A . 
M 5 HOH 233 1033 116 HOH HOH A . 
M 5 HOH 234 1034 186 HOH HOH A . 
M 5 HOH 235 1035 64  HOH HOH A . 
M 5 HOH 236 1036 164 HOH HOH A . 
M 5 HOH 237 1037 306 HOH HOH A . 
M 5 HOH 238 1038 177 HOH HOH A . 
M 5 HOH 239 1039 303 HOH HOH A . 
M 5 HOH 240 1040 311 HOH HOH A . 
M 5 HOH 241 1041 59  HOH HOH A . 
M 5 HOH 242 1042 158 HOH HOH A . 
M 5 HOH 243 1043 220 HOH HOH A . 
M 5 HOH 244 1044 62  HOH HOH A . 
M 5 HOH 245 1045 43  HOH HOH A . 
M 5 HOH 246 1046 188 HOH HOH A . 
M 5 HOH 247 1047 24  HOH HOH A . 
M 5 HOH 248 1048 97  HOH HOH A . 
M 5 HOH 249 1049 88  HOH HOH A . 
M 5 HOH 250 1050 242 HOH HOH A . 
M 5 HOH 251 1051 320 HOH HOH A . 
M 5 HOH 252 1052 191 HOH HOH A . 
M 5 HOH 253 1053 279 HOH HOH A . 
M 5 HOH 254 1054 382 HOH HOH A . 
M 5 HOH 255 1055 199 HOH HOH A . 
M 5 HOH 256 1056 198 HOH HOH A . 
M 5 HOH 257 1057 331 HOH HOH A . 
M 5 HOH 258 1058 31  HOH HOH A . 
M 5 HOH 259 1059 73  HOH HOH A . 
M 5 HOH 260 1060 194 HOH HOH A . 
M 5 HOH 261 1061 44  HOH HOH A . 
M 5 HOH 262 1062 259 HOH HOH A . 
M 5 HOH 263 1063 90  HOH HOH A . 
M 5 HOH 264 1064 258 HOH HOH A . 
M 5 HOH 265 1065 263 HOH HOH A . 
M 5 HOH 266 1066 166 HOH HOH A . 
M 5 HOH 267 1067 335 HOH HOH A . 
M 5 HOH 268 1068 229 HOH HOH A . 
M 5 HOH 269 1069 338 HOH HOH A . 
M 5 HOH 270 1070 257 HOH HOH A . 
M 5 HOH 271 1071 398 HOH HOH A . 
M 5 HOH 272 1072 384 HOH HOH A . 
M 5 HOH 273 1073 185 HOH HOH A . 
M 5 HOH 274 1074 270 HOH HOH A . 
M 5 HOH 275 1075 227 HOH HOH A . 
M 5 HOH 276 1076 95  HOH HOH A . 
M 5 HOH 277 1077 373 HOH HOH A . 
M 5 HOH 278 1078 22  HOH HOH A . 
M 5 HOH 279 1079 30  HOH HOH A . 
M 5 HOH 280 1080 295 HOH HOH A . 
M 5 HOH 281 1081 150 HOH HOH A . 
M 5 HOH 282 1082 20  HOH HOH A . 
M 5 HOH 283 1083 390 HOH HOH A . 
M 5 HOH 284 1084 392 HOH HOH A . 
M 5 HOH 285 1085 126 HOH HOH A . 
M 5 HOH 286 1086 289 HOH HOH A . 
M 5 HOH 287 1087 309 HOH HOH A . 
M 5 HOH 288 1088 129 HOH HOH A . 
M 5 HOH 289 1089 274 HOH HOH A . 
M 5 HOH 290 1090 205 HOH HOH A . 
M 5 HOH 291 1091 394 HOH HOH A . 
M 5 HOH 292 1092 169 HOH HOH A . 
M 5 HOH 293 1093 241 HOH HOH A . 
M 5 HOH 294 1094 197 HOH HOH A . 
M 5 HOH 295 1095 261 HOH HOH A . 
M 5 HOH 296 1096 201 HOH HOH A . 
M 5 HOH 297 1097 247 HOH HOH A . 
M 5 HOH 298 1098 351 HOH HOH A . 
M 5 HOH 299 1099 308 HOH HOH A . 
M 5 HOH 300 1100 278 HOH HOH A . 
M 5 HOH 301 1101 173 HOH HOH A . 
M 5 HOH 302 1102 300 HOH HOH A . 
M 5 HOH 303 1103 156 HOH HOH A . 
M 5 HOH 304 1104 380 HOH HOH A . 
M 5 HOH 305 1105 181 HOH HOH A . 
M 5 HOH 306 1106 287 HOH HOH A . 
M 5 HOH 307 1107 163 HOH HOH A . 
M 5 HOH 308 1108 235 HOH HOH A . 
M 5 HOH 309 1109 215 HOH HOH A . 
M 5 HOH 310 1110 294 HOH HOH A . 
M 5 HOH 311 1111 265 HOH HOH A . 
M 5 HOH 312 1112 385 HOH HOH A . 
M 5 HOH 313 1113 362 HOH HOH A . 
M 5 HOH 314 1114 193 HOH HOH A . 
M 5 HOH 315 1115 318 HOH HOH A . 
M 5 HOH 316 1116 341 HOH HOH A . 
M 5 HOH 317 1117 322 HOH HOH A . 
M 5 HOH 318 1118 105 HOH HOH A . 
M 5 HOH 319 1119 326 HOH HOH A . 
M 5 HOH 320 1120 297 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 211 ? CG  ? A LYS 8   CG  
2  1 Y 1 A LYS 211 ? CD  ? A LYS 8   CD  
3  1 Y 1 A LYS 211 ? CE  ? A LYS 8   CE  
4  1 Y 1 A LYS 211 ? NZ  ? A LYS 8   NZ  
5  1 Y 1 A LYS 221 ? CD  ? A LYS 18  CD  
6  1 Y 1 A LYS 221 ? CE  ? A LYS 18  CE  
7  1 Y 1 A LYS 221 ? NZ  ? A LYS 18  NZ  
8  1 Y 1 A SER 253 ? OG  ? A SER 50  OG  
9  1 Y 1 A LEU 255 ? CG  ? A LEU 52  CG  
10 1 Y 1 A LEU 255 ? CD1 ? A LEU 52  CD1 
11 1 Y 1 A LEU 255 ? CD2 ? A LEU 52  CD2 
12 1 Y 1 A LYS 298 ? CG  ? A LYS 95  CG  
13 1 Y 1 A LYS 298 ? CD  ? A LYS 95  CD  
14 1 Y 1 A LYS 298 ? CE  ? A LYS 95  CE  
15 1 Y 1 A LYS 298 ? NZ  ? A LYS 95  NZ  
16 1 Y 1 A LYS 320 ? CE  ? A LYS 117 CE  
17 1 Y 1 A LYS 320 ? NZ  ? A LYS 117 NZ  
18 1 Y 1 A ILE 352 ? CG1 ? A ILE 149 CG1 
19 1 Y 1 A ILE 352 ? CG2 ? A ILE 149 CG2 
20 1 Y 1 A ILE 352 ? CD1 ? A ILE 149 CD1 
21 1 Y 1 A LYS 367 ? NZ  ? A LYS 164 NZ  
22 1 Y 1 A ARG 400 ? CD  ? A ARG 197 CD  
23 1 Y 1 A ARG 400 ? NE  ? A ARG 197 NE  
24 1 Y 1 A ARG 400 ? CZ  ? A ARG 197 CZ  
25 1 Y 1 A ARG 400 ? NH1 ? A ARG 197 NH1 
26 1 Y 1 A ARG 400 ? NH2 ? A ARG 197 NH2 
27 1 Y 1 A ASN 478 ? CG  ? A ASN 275 CG  
28 1 Y 1 A ASN 478 ? OD1 ? A ASN 275 OD1 
29 1 Y 1 A ASN 478 ? ND2 ? A ASN 275 ND2 
30 1 Y 1 A ARG 481 ? CG  ? A ARG 278 CG  
31 1 Y 1 A ARG 481 ? CD  ? A ARG 278 CD  
32 1 Y 1 A ARG 481 ? NE  ? A ARG 278 NE  
33 1 Y 1 A ARG 481 ? CZ  ? A ARG 278 CZ  
34 1 Y 1 A ARG 481 ? NH1 ? A ARG 278 NH1 
35 1 Y 1 A ARG 481 ? NH2 ? A ARG 278 NH2 
36 1 Y 1 A LYS 500 ? CG  ? A LYS 297 CG  
37 1 Y 1 A LYS 500 ? CD  ? A LYS 297 CD  
38 1 Y 1 A LYS 500 ? CE  ? A LYS 297 CE  
39 1 Y 1 A LYS 500 ? NZ  ? A LYS 297 NZ  
40 1 Y 1 A ASN 501 ? CG  ? A ASN 298 CG  
41 1 Y 1 A ASN 501 ? OD1 ? A ASN 298 OD1 
42 1 Y 1 A ASN 501 ? ND2 ? A ASN 298 ND2 
43 1 Y 1 A LYS 530 ? CG  ? A LYS 327 CG  
44 1 Y 1 A LYS 530 ? CD  ? A LYS 327 CD  
45 1 Y 1 A LYS 530 ? CE  ? A LYS 327 CE  
46 1 Y 1 A LYS 530 ? NZ  ? A LYS 327 NZ  
47 1 Y 1 A SER 553 ? OG  ? A SER 350 OG  
48 1 Y 1 A LYS 554 ? CG  ? A LYS 351 CG  
49 1 Y 1 A LYS 554 ? CD  ? A LYS 351 CD  
50 1 Y 1 A LYS 554 ? CE  ? A LYS 351 CE  
51 1 Y 1 A LYS 554 ? NZ  ? A LYS 351 NZ  
52 1 Y 1 A ASN 556 ? CG  ? A ASN 353 CG  
53 1 Y 1 A ASN 556 ? OD1 ? A ASN 353 OD1 
54 1 Y 1 A ASN 556 ? ND2 ? A ASN 353 ND2 
55 1 Y 1 A ARG 557 ? CG  ? A ARG 354 CG  
56 1 Y 1 A ARG 557 ? CD  ? A ARG 354 CD  
57 1 Y 1 A ARG 557 ? NE  ? A ARG 354 NE  
58 1 Y 1 A ARG 557 ? CZ  ? A ARG 354 CZ  
59 1 Y 1 A ARG 557 ? NH1 ? A ARG 354 NH1 
60 1 Y 1 A ARG 557 ? NH2 ? A ARG 354 NH2 
61 1 Y 1 A GLN 560 ? CG  ? A GLN 357 CG  
62 1 Y 1 A GLN 560 ? CD  ? A GLN 357 CD  
63 1 Y 1 A GLN 560 ? OE1 ? A GLN 357 OE1 
64 1 Y 1 A GLN 560 ? NE2 ? A GLN 357 NE2 
65 1 Y 1 A LYS 599 ? CG  ? A LYS 396 CG  
66 1 Y 1 A LYS 599 ? CD  ? A LYS 396 CD  
67 1 Y 1 A LYS 599 ? CE  ? A LYS 396 CE  
68 1 Y 1 A LYS 599 ? NZ  ? A LYS 396 NZ  
69 1 Y 1 A GLU 604 ? CG  ? A GLU 401 CG  
70 1 Y 1 A GLU 604 ? CD  ? A GLU 401 CD  
71 1 Y 1 A GLU 604 ? OE1 ? A GLU 401 OE1 
72 1 Y 1 A GLU 604 ? OE2 ? A GLU 401 OE2 
73 1 Y 1 A GLU 607 ? CG  ? A GLU 404 CG  
74 1 Y 1 A GLU 607 ? CD  ? A GLU 404 CD  
75 1 Y 1 A GLU 607 ? OE1 ? A GLU 404 OE1 
76 1 Y 1 A GLU 607 ? OE2 ? A GLU 404 OE2 
77 1 Y 1 A LYS 608 ? CG  ? A LYS 405 CG  
78 1 Y 1 A LYS 608 ? CD  ? A LYS 405 CD  
79 1 Y 1 A LYS 608 ? CE  ? A LYS 405 CE  
80 1 Y 1 A LYS 608 ? NZ  ? A LYS 405 NZ  
81 1 Y 1 A LYS 640 ? CD  ? A LYS 437 CD  
82 1 Y 1 A LYS 640 ? CE  ? A LYS 437 CE  
83 1 Y 1 A LYS 640 ? NZ  ? A LYS 437 NZ  
84 1 Y 1 A LYS 641 ? CD  ? A LYS 438 CD  
85 1 Y 1 A LYS 641 ? CE  ? A LYS 438 CE  
86 1 Y 1 A LYS 641 ? NZ  ? A LYS 438 NZ  
# 
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 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS     ? ? ? 2.2.10    1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2      ? ? ? 0.6.475   2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless   ? ? ? .         3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? pointless ? ? ? .         4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? .         5 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? 1.19.2    6 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot      ? ? ? .         7 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? 1.21_5207 8 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MDM 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.402 
_cell.length_a_esd                 ? 
_cell.length_b                     99.327 
_cell.length_b_esd                 ? 
_cell.length_c                     120.006 
_cell.length_c_esd                 ? 
_cell.volume                       493503.658 
_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                         9MDM 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab (z,x,y)' 
_symmetry.space_group_name_H-M             'P 2 21 21' 
_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                   9MDM 
_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             2.22 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.68 
_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          MICROBATCH 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.0 
_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    '0.1 M HEPES, pH 7.0, 0.1 M Sodium phosphate dibasic, 20% PEG 4,000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296 
# 
_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         2021-11-22 
_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   1.033 
_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                        'APS BEAMLINE 23-ID-B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.033 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-B 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          24.67 
_reflns.entry_id                                       9MDM 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.63 
_reflns.d_resolution_low                               51.36 
_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                                     396707 
_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                           98.51 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.41 
_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                                   0.997 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.054 
_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                                    1.63 
_reflns_shell.d_res_low                                     1.65 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.43 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             8000 
_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                               4.5 
_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                                  0.826 
_reflns_shell.pdbx_CC_star                                  0.951 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          82.2 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.569 
_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                               37.56 
_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                                 9MDM 
_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                            1.63 
_refine.ls_d_res_low                             51.36 
_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                     118162 
_refine.ls_number_reflns_R_free                  5983 
_refine.ls_number_reflns_R_work                  112179 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.51 
_refine.ls_percent_reflns_R_free                 5.06 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1881 
_refine.ls_R_factor_R_free                       0.2130 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1868 
_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                          1.34 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 23.2908 
_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                            0.2004 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.63 
_refine_hist.d_res_low                        51.36 
_refine_hist.number_atoms_solvent             320 
_refine_hist.number_atoms_total               3888 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3529 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0062  ? 3866 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8316  ? 5257 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0559  ? 527  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0063  ? 695  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.4920 ? 1413 ? f_dihedral_angle_d ? ? 
# 
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' 1.63 1.65  . . 125 3176 82.20  . . . . 0.3306 . . . . . . . . . . . 0.3806 
'X-RAY DIFFRACTION' 1.65 1.67  . . 219 3598 95.59  . . . . 0.3114 . . . . . . . . . . . 0.3364 
'X-RAY DIFFRACTION' 1.67 1.69  . . 200 3749 98.85  . . . . 0.2683 . . . . . . . . . . . 0.2997 
'X-RAY DIFFRACTION' 1.69 1.71  . . 211 3741 99.65  . . . . 0.2448 . . . . . . . . . . . 0.2528 
'X-RAY DIFFRACTION' 1.71 1.73  . . 202 3811 99.21  . . . . 0.2442 . . . . . . . . . . . 0.2539 
'X-RAY DIFFRACTION' 1.73 1.75  . . 183 3734 99.47  . . . . 0.2377 . . . . . . . . . . . 0.3057 
'X-RAY DIFFRACTION' 1.75 1.78  . . 183 3786 98.78  . . . . 0.2266 . . . . . . . . . . . 0.2649 
'X-RAY DIFFRACTION' 1.78 1.80  . . 235 3776 99.13  . . . . 0.2176 . . . . . . . . . . . 0.2325 
'X-RAY DIFFRACTION' 1.80 1.83  . . 213 3671 98.53  . . . . 0.2198 . . . . . . . . . . . 0.2759 
'X-RAY DIFFRACTION' 1.83 1.86  . . 196 3771 99.27  . . . . 0.2256 . . . . . . . . . . . 0.2892 
'X-RAY DIFFRACTION' 1.86 1.89  . . 192 3803 98.86  . . . . 0.2294 . . . . . . . . . . . 0.2070 
'X-RAY DIFFRACTION' 1.89 1.93  . . 185 3734 98.99  . . . . 0.2230 . . . . . . . . . . . 0.2583 
'X-RAY DIFFRACTION' 1.93 1.97  . . 224 3786 98.77  . . . . 0.2035 . . . . . . . . . . . 0.2682 
'X-RAY DIFFRACTION' 1.97 2.01  . . 196 3669 98.62  . . . . 0.2084 . . . . . . . . . . . 0.2568 
'X-RAY DIFFRACTION' 2.01 2.05  . . 206 3785 98.62  . . . . 0.2033 . . . . . . . . . . . 0.2354 
'X-RAY DIFFRACTION' 2.05 2.10  . . 195 3719 98.71  . . . . 0.1906 . . . . . . . . . . . 0.2289 
'X-RAY DIFFRACTION' 2.10 2.15  . . 197 3824 99.60  . . . . 0.1894 . . . . . . . . . . . 0.2192 
'X-RAY DIFFRACTION' 2.15 2.21  . . 204 3778 99.72  . . . . 0.1906 . . . . . . . . . . . 0.2115 
'X-RAY DIFFRACTION' 2.21 2.27  . . 179 3801 99.95  . . . . 0.1943 . . . . . . . . . . . 0.2495 
'X-RAY DIFFRACTION' 2.27 2.35  . . 243 3744 99.65  . . . . 0.1941 . . . . . . . . . . . 0.2356 
'X-RAY DIFFRACTION' 2.35 2.43  . . 250 3751 99.40  . . . . 0.1961 . . . . . . . . . . . 0.2067 
'X-RAY DIFFRACTION' 2.43 2.53  . . 219 3730 99.47  . . . . 0.1992 . . . . . . . . . . . 0.2439 
'X-RAY DIFFRACTION' 2.53 2.64  . . 193 3789 99.23  . . . . 0.1943 . . . . . . . . . . . 0.2110 
'X-RAY DIFFRACTION' 2.64 2.78  . . 180 3754 98.82  . . . . 0.1884 . . . . . . . . . . . 0.2137 
'X-RAY DIFFRACTION' 2.78 2.96  . . 176 3768 98.40  . . . . 0.1912 . . . . . . . . . . . 0.2136 
'X-RAY DIFFRACTION' 2.96 3.18  . . 196 3808 99.88  . . . . 0.1823 . . . . . . . . . . . 0.2379 
'X-RAY DIFFRACTION' 3.19 3.51  . . 189 3786 100.00 . . . . 0.1687 . . . . . . . . . . . 0.1823 
'X-RAY DIFFRACTION' 3.51 4.01  . . 200 3800 100.00 . . . . 0.1608 . . . . . . . . . . . 0.1682 
'X-RAY DIFFRACTION' 4.01 5.05  . . 201 3792 99.55  . . . . 0.1434 . . . . . . . . . . . 0.1674 
'X-RAY DIFFRACTION' 5.06 51.36 . . 191 3745 98.55  . . . . 0.1873 . . . . . . . . . . . 0.1975 
# 
_struct.entry_id                     9MDM 
_struct.title                        'Crystal Structure of C412S Mutant of C0362 (TDE_0362 [TDE0362] resi 205-647)' 
_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        9MDM 
_struct_keywords.text            
'Papain-superfamily cysteine protease, virulence factor, TDE_0362, alpha/beta hydrolase, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 4 ? 
G N N 4 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 2 ? 
L N N 2 ? 
M N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q73QT1_TREDE 
_struct_ref.pdbx_db_accession          Q73QT1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TVTIEIKKKPQIKYEEKQAVMPESAAGTYTFEVQTIDGKLDYEPYFTSSTLPWITGAPTISSRTDPNKDVISFTCLKNKT
VWNRRAYIKFKDKKTGQYIKGADGKADLTVNIIQKKNENPVVHYKWVDGIGAPTENQKIKMKIKNNGIETEDYFTDPFVF
KWKETADTKFYNVRKLDKLYVQGQFPSNYFVINGIRNEQIQGRDISQCWAKTASNMLHWWFEQNKDYIEQYKQKAAIEEW
KRPLYKHDYIRGLQDEDEGKKSNIANIFRAYSHNNARGGYIEDGLTWYLYKRDGQKNLGSIYPGLFNDVFAHDTSPINIE
RCETKKEFEQLMNKTLDNKRAIGIFWQGSKGNRPYQHAVTCWGAAYDEDNNIICLYIAESNLPEAVLYPFGVRYKGNIYE
EAEKNRTYMFNYALSKPENIYIDGLTTLDKGEDQWKKWLEAHQ
;
_struct_ref.pdbx_align_begin           205 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9MDM 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 444 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q73QT1 
_struct_ref_seq.db_align_beg                  205 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  647 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       205 
_struct_ref_seq.pdbx_auth_seq_align_end       647 
# 
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 9MDM MET A 1   ? UNP Q73QT1 ?   ?   'initiating methionine' 204 1  
1 9MDM SER A 209 ? UNP Q73QT1 CYS 412 'engineered mutation'   412 2  
1 9MDM LYS A 445 ? UNP Q73QT1 ?   ?   'expression tag'        648 3  
1 9MDM GLY A 446 ? UNP Q73QT1 ?   ?   'expression tag'        649 4  
1 9MDM GLU A 447 ? UNP Q73QT1 ?   ?   'expression tag'        650 5  
1 9MDM LEU A 448 ? UNP Q73QT1 ?   ?   'expression tag'        651 6  
1 9MDM ASN A 449 ? UNP Q73QT1 ?   ?   'expression tag'        652 7  
1 9MDM SER A 450 ? UNP Q73QT1 ?   ?   'expression tag'        653 8  
1 9MDM LYS A 451 ? UNP Q73QT1 ?   ?   'expression tag'        654 9  
1 9MDM LEU A 452 ? UNP Q73QT1 ?   ?   'expression tag'        655 10 
1 9MDM GLU A 453 ? UNP Q73QT1 ?   ?   'expression tag'        656 11 
1 9MDM GLY A 454 ? UNP Q73QT1 ?   ?   'expression tag'        657 12 
1 9MDM LYS A 455 ? UNP Q73QT1 ?   ?   'expression tag'        658 13 
1 9MDM PRO A 456 ? UNP Q73QT1 ?   ?   'expression tag'        659 14 
1 9MDM ILE A 457 ? UNP Q73QT1 ?   ?   'expression tag'        660 15 
1 9MDM PRO A 458 ? UNP Q73QT1 ?   ?   'expression tag'        661 16 
1 9MDM ASN A 459 ? UNP Q73QT1 ?   ?   'expression tag'        662 17 
1 9MDM PRO A 460 ? UNP Q73QT1 ?   ?   'expression tag'        663 18 
1 9MDM LEU A 461 ? UNP Q73QT1 ?   ?   'expression tag'        664 19 
1 9MDM LEU A 462 ? UNP Q73QT1 ?   ?   'expression tag'        665 20 
1 9MDM GLY A 463 ? UNP Q73QT1 ?   ?   'expression tag'        666 21 
1 9MDM LEU A 464 ? UNP Q73QT1 ?   ?   'expression tag'        667 22 
1 9MDM ASP A 465 ? UNP Q73QT1 ?   ?   'expression tag'        668 23 
1 9MDM SER A 466 ? UNP Q73QT1 ?   ?   'expression tag'        669 24 
1 9MDM THR A 467 ? UNP Q73QT1 ?   ?   'expression tag'        670 25 
1 9MDM ARG A 468 ? UNP Q73QT1 ?   ?   'expression tag'        671 26 
1 9MDM THR A 469 ? UNP Q73QT1 ?   ?   'expression tag'        672 27 
1 9MDM GLY A 470 ? UNP Q73QT1 ?   ?   'expression tag'        673 28 
1 9MDM HIS A 471 ? UNP Q73QT1 ?   ?   'expression tag'        674 29 
1 9MDM HIS A 472 ? UNP Q73QT1 ?   ?   'expression tag'        675 30 
1 9MDM HIS A 473 ? UNP Q73QT1 ?   ?   'expression tag'        676 31 
1 9MDM HIS A 474 ? UNP Q73QT1 ?   ?   'expression tag'        677 32 
1 9MDM HIS A 475 ? UNP Q73QT1 ?   ?   'expression tag'        678 33 
1 9MDM HIS A 476 ? UNP Q73QT1 ?   ?   'expression tag'        679 34 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_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 THR A 135 ? ASN A 137 ? THR A 338 ASN A 340 5 ? 3  
HELX_P HELX_P2  AA2 LYS A 176 ? TYR A 181 ? LYS A 379 TYR A 384 1 ? 6  
HELX_P HELX_P3  AA3 GLN A 208 ? ASN A 225 ? GLN A 411 ASN A 428 1 ? 18 
HELX_P HELX_P4  AA4 ASN A 225 ? ALA A 236 ? ASN A 428 ALA A 439 1 ? 12 
HELX_P HELX_P5  AA5 GLU A 239 ? TYR A 246 ? GLU A 442 TYR A 449 5 ? 8  
HELX_P HELX_P6  AA6 GLN A 255 ? LYS A 262 ? GLN A 458 LYS A 465 5 ? 8  
HELX_P HELX_P7  AA7 SER A 263 ? SER A 273 ? SER A 466 SER A 476 1 ? 11 
HELX_P HELX_P8  AA8 TYR A 281 ? TYR A 291 ? TYR A 484 TYR A 494 1 ? 11 
HELX_P HELX_P9  AA9 ARG A 293 ? LYS A 297 ? ARG A 496 LYS A 500 5 ? 5  
HELX_P HELX_P10 AB1 PHE A 307 ? ALA A 312 ? PHE A 510 ALA A 515 1 ? 6  
HELX_P HELX_P11 AB2 THR A 325 ? ASN A 339 ? THR A 528 ASN A 542 1 ? 15 
HELX_P HELX_P12 AB3 GLY A 432 ? ALA A 442 ? GLY A 635 ALA A 645 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A LEU 52 O  ? ? ? 1_555 G NA  . NA ? ? A LEU 255 A NA  706  1_555 ? ? ? ? ? ? ? 2.381 ? ? 
metalc2 metalc ? ? A ILE 55 O  ? ? ? 1_555 G NA  . NA ? ? A ILE 258 A NA  706  1_555 ? ? ? ? ? ? ? 2.269 ? ? 
metalc3 metalc ? ? D PO4 .  O1 ? ? ? 1_555 F NA  . NA ? ? A PO4 703 A NA  705  1_555 ? ? ? ? ? ? ? 2.224 ? ? 
metalc4 metalc ? ? G NA  .  NA ? ? ? 1_555 M HOH . O  ? ? A NA  706 A HOH 1008 1_555 ? ? ? ? ? ? ? 2.408 ? ? 
metalc5 metalc ? ? G NA  .  NA ? ? ? 1_555 M HOH . O  ? ? A NA  706 A HOH 1028 1_555 ? ? ? ? ? ? ? 2.329 ? ? 
metalc6 metalc ? ? G NA  .  NA ? ? ? 1_555 M HOH . O  ? ? A NA  706 A HOH 1077 1_555 ? ? ? ? ? ? ? 2.272 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O ? A LEU 52 ? A LEU 255  ? 1_555 NA ? G NA . ? A NA 706 ? 1_555 O ? A ILE 55 ? A ILE 258  ? 1_555 84.2  ? 
2  O ? A LEU 52 ? A LEU 255  ? 1_555 NA ? G NA . ? A NA 706 ? 1_555 O ? M HOH .  ? A HOH 1008 ? 1_555 105.6 ? 
3  O ? A ILE 55 ? A ILE 258  ? 1_555 NA ? G NA . ? A NA 706 ? 1_555 O ? M HOH .  ? A HOH 1008 ? 1_555 95.3  ? 
4  O ? A LEU 52 ? A LEU 255  ? 1_555 NA ? G NA . ? A NA 706 ? 1_555 O ? M HOH .  ? A HOH 1028 ? 1_555 159.5 ? 
5  O ? A ILE 55 ? A ILE 258  ? 1_555 NA ? G NA . ? A NA 706 ? 1_555 O ? M HOH .  ? A HOH 1028 ? 1_555 93.3  ? 
6  O ? M HOH .  ? A HOH 1008 ? 1_555 NA ? G NA . ? A NA 706 ? 1_555 O ? M HOH .  ? A HOH 1028 ? 1_555 94.9  ? 
7  O ? A LEU 52 ? A LEU 255  ? 1_555 NA ? G NA . ? A NA 706 ? 1_555 O ? M HOH .  ? A HOH 1077 ? 1_555 92.2  ? 
8  O ? A ILE 55 ? A ILE 258  ? 1_555 NA ? G NA . ? A NA 706 ? 1_555 O ? M HOH .  ? A HOH 1077 ? 1_555 106.2 ? 
9  O ? M HOH .  ? A HOH 1008 ? 1_555 NA ? G NA . ? A NA 706 ? 1_555 O ? M HOH .  ? A HOH 1077 ? 1_555 153.4 ? 
10 O ? M HOH .  ? A HOH 1028 ? 1_555 NA ? G NA . ? A NA 706 ? 1_555 O ? M HOH .  ? A HOH 1077 ? 1_555 68.9  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4  ? 
AA2 ? 3  ? 
AA3 ? 10 ? 
AA4 ? 2  ? 
AA5 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? anti-parallel 
AA1 2 3  ? anti-parallel 
AA1 3 4  ? anti-parallel 
AA2 1 2  ? anti-parallel 
AA2 2 3  ? anti-parallel 
AA3 1 6  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 8  ? anti-parallel 
AA3 4 10 ? anti-parallel 
AA3 5 6  ? anti-parallel 
AA3 5 10 ? anti-parallel 
AA3 6 7  ? anti-parallel 
AA3 7 8  ? anti-parallel 
AA3 8 9  ? anti-parallel 
AA3 9 10 ? anti-parallel 
AA4 1 2  ? anti-parallel 
AA5 1 2  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  GLN A 12  ? LYS A 14  ? GLN A 215 LYS A 217 
AA1 2  GLY A 28  ? ILE A 37  ? GLY A 231 ILE A 240 
AA1 3  LYS A 69  ? CYS A 76  ? LYS A 272 CYS A 279 
AA1 4  THR A 60  ? SER A 63  ? THR A 263 SER A 266 
AA2 1  TYR A 43  ? PHE A 47  ? TYR A 246 PHE A 250 
AA2 2  ARG A 85  ? ASP A 93  ? ARG A 288 ASP A 296 
AA2 3  VAL A 111 ? GLN A 115 ? VAL A 314 GLN A 318 
AA3 1  HIS A 124 ? TRP A 127 ? HIS A 327 TRP A 330 
AA3 2  LYS A 139 ? ILE A 140 ? LYS A 342 ILE A 343 
AA3 3  LYS A 162 ? LYS A 164 ? LYS A 365 LYS A 367 
AA3 4  ILE A 318 ? ARG A 322 ? ILE A 521 ARG A 525 
AA3 5  ALA A 342 ? SER A 350 ? ALA A 545 SER A 553 
AA3 6  PRO A 355 ? TYR A 367 ? PRO A 558 TYR A 570 
AA3 7  ILE A 373 ? ALA A 379 ? ILE A 576 ALA A 582 
AA3 8  VAL A 387 ? TYR A 395 ? VAL A 590 TYR A 598 
AA3 9  THR A 408 ? ASN A 412 ? THR A 611 ASN A 615 
AA3 10 LYS A 417 ? LEU A 429 ? LYS A 620 LEU A 632 
AA4 1  LYS A 143 ? ASN A 146 ? LYS A 346 ASN A 349 
AA4 2  ILE A 149 ? TYR A 154 ? ILE A 352 TYR A 357 
AA5 1  VAL A 192 ? ASN A 194 ? VAL A 395 ASN A 397 
AA5 2  GLN A 200 ? GLN A 202 ? GLN A 403 GLN A 405 
# 
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 GLN A 12  ? N GLN A 215 O ILE A 37  ? O ILE A 240 
AA1 2 3  N PHE A 32  ? N PHE A 235 O ILE A 72  ? O ILE A 275 
AA1 3 4  O SER A 73  ? O SER A 276 N THR A 60  ? N THR A 263 
AA2 1 2  N GLU A 44  ? N GLU A 247 O LYS A 92  ? O LYS A 295 
AA2 2 3  N ALA A 87  ? N ALA A 290 O ILE A 113 ? O ILE A 316 
AA3 1 6  N HIS A 124 ? N HIS A 327 O TYR A 367 ? O TYR A 570 
AA3 2 3  N ILE A 140 ? N ILE A 343 O LYS A 162 ? O LYS A 365 
AA3 3 8  N TRP A 163 ? N TRP A 366 O LEU A 388 ? O LEU A 591 
AA3 4 10 N GLU A 321 ? N GLU A 524 O LEU A 426 ? O LEU A 629 
AA3 5 6  N TRP A 347 ? N TRP A 550 O HIS A 358 ? O HIS A 561 
AA3 5 10 N GLN A 348 ? N GLN A 551 O TYR A 422 ? O TYR A 625 
AA3 6 7  N ALA A 366 ? N ALA A 569 O CYS A 375 ? O CYS A 578 
AA3 7 8  N ILE A 378 ? N ILE A 581 O TYR A 389 ? O TYR A 592 
AA3 8 9  N GLY A 392 ? N GLY A 595 O PHE A 411 ? O PHE A 614 
AA3 9 10 N ASN A 412 ? N ASN A 615 O LYS A 417 ? O LYS A 620 
AA4 1 2  N ILE A 144 ? N ILE A 347 O THR A 151 ? O THR A 354 
AA5 1 2  N ILE A 193 ? N ILE A 396 O ILE A 201 ? O ILE A 404 
# 
_pdbx_entry_details.entry_id                   9MDM 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 THR A 254 ? ? -106.10 71.69  
2 1 ASN A 401 ? ? 58.51   19.69  
3 1 ASP A 408 ? ? -142.90 26.17  
4 1 LYS A 450 ? ? -174.86 131.11 
5 1 LYS A 450 ? ? -174.86 148.22 
6 1 ASN A 556 ? ? -78.14  37.44  
7 1 GLU A 604 ? ? -115.22 73.01  
8 1 GLU A 604 ? ? -115.22 73.39  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     920 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   M 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x,-y,-z         
3 -x,y+1/2,-z+1/2 
4 -x,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -0.761771844494 40.9558569246 18.4731782458  0.315896478521 ? -0.00127938652895 ? 
-0.00323916167494 ? 0.216610358565 ? 0.0322477953644   ? 0.172209197189 ? 0.375057141579 ? -0.777340389685 ? -0.430504508457 ? 
2.55470626234 ? 1.99485877216  ? 1.18465756043 ? 0.0570859560865   ? 0.00996780819109 ? 0.00681860799932 ? -0.119356026896 ? 
-0.121661911101  ? 0.0432742272274  ? -0.200402502958 ? -0.0979351024376 ? 0.0645892375967 ? 
2 'X-RAY DIFFRACTION' ? refined 15.1985382874   8.40629707799 -11.3981819848 0.13895605694  ? -0.0383632266703  ? 0.0127701065562 
? 0.249502122129 ? -0.00311447955216 ? 0.223442855289 ? 0.376720208702 ? -0.171495266998 ? -0.163378501614 ? 1.17747915582 ? 
0.572013507546 ? 4.15075870927 ? -0.0799574390563  ? 0.120486180424   ? -0.0813548936927 ? -0.183622521032 ? 0.0221703880166  ? 
-0.204883623582  ? 0.0126852193351 ? 0.482033917633   ? 0.0470692330089 ? 
3 'X-RAY DIFFRACTION' ? refined 5.53198209116   25.5834109231 -7.00823292068 0.529293541326 ? -0.0059941957095  ? -0.0666536156865 
? 0.216037723664 ? 0.0514532764949   ? 0.250328659512 ? 1.49274803594  ? -0.1926142926   ? -0.918922114106 ? 1.82253203474 ? 
1.0863107643   ? 3.06778049512 ? -0.00691642165063 ? 0.257152152347   ? 0.224674803927   ? -0.493945347771 ? -0.0493898976132 ? 
-0.0285222969124 ? -1.22592083205  ? -0.0584863909236 ? 0.0348486016971 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_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 
1 'X-RAY DIFFRACTION' 1 A 1   A 211 ? A 173 A 383 ? ? 
;chain 'A' and (resid 211 through 383 )
;
2 'X-RAY DIFFRACTION' 2 A 174 A 384 ? A 265 A 475 ? ? 
;chain 'A' and (resid 384 through 475 )
;
3 'X-RAY DIFFRACTION' 3 A 266 A 476 ? A 437 A 647 ? ? 
;chain 'A' and (resid 476 through 647 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       1120 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.15 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 204 ? A MET 1   
2  1 Y 1 A THR 205 ? A THR 2   
3  1 Y 1 A VAL 206 ? A VAL 3   
4  1 Y 1 A THR 207 ? A THR 4   
5  1 Y 1 A ILE 208 ? A ILE 5   
6  1 Y 1 A GLU 209 ? A GLU 6   
7  1 Y 1 A ILE 210 ? A ILE 7   
8  1 Y 1 A LYS 648 ? A LYS 445 
9  1 Y 1 A GLY 649 ? A GLY 446 
10 1 Y 1 A GLU 650 ? A GLU 447 
11 1 Y 1 A LEU 651 ? A LEU 448 
12 1 Y 1 A ASN 652 ? A ASN 449 
13 1 Y 1 A SER 653 ? A SER 450 
14 1 Y 1 A LYS 654 ? A LYS 451 
15 1 Y 1 A LEU 655 ? A LEU 452 
16 1 Y 1 A GLU 656 ? A GLU 453 
17 1 Y 1 A GLY 657 ? A GLY 454 
18 1 Y 1 A LYS 658 ? A LYS 455 
19 1 Y 1 A PRO 659 ? A PRO 456 
20 1 Y 1 A ILE 660 ? A ILE 457 
21 1 Y 1 A PRO 661 ? A PRO 458 
22 1 Y 1 A ASN 662 ? A ASN 459 
23 1 Y 1 A PRO 663 ? A PRO 460 
24 1 Y 1 A LEU 664 ? A LEU 461 
25 1 Y 1 A LEU 665 ? A LEU 462 
26 1 Y 1 A GLY 666 ? A GLY 463 
27 1 Y 1 A LEU 667 ? A LEU 464 
28 1 Y 1 A ASP 668 ? A ASP 465 
29 1 Y 1 A SER 669 ? A SER 466 
30 1 Y 1 A THR 670 ? A THR 467 
31 1 Y 1 A ARG 671 ? A ARG 468 
32 1 Y 1 A THR 672 ? A THR 469 
33 1 Y 1 A GLY 673 ? A GLY 470 
34 1 Y 1 A HIS 674 ? A HIS 471 
35 1 Y 1 A HIS 675 ? A HIS 472 
36 1 Y 1 A HIS 676 ? A HIS 473 
37 1 Y 1 A HIS 677 ? A HIS 474 
38 1 Y 1 A HIS 678 ? A HIS 475 
39 1 Y 1 A HIS 679 ? A HIS 476 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
EDO C1   C  N N 88  
EDO O1   O  N N 89  
EDO C2   C  N N 90  
EDO O2   O  N N 91  
EDO H11  H  N N 92  
EDO H12  H  N N 93  
EDO HO1  H  N N 94  
EDO H21  H  N N 95  
EDO H22  H  N N 96  
EDO HO2  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
NA  NA   NA N N 260 
PHE N    N  N N 261 
PHE CA   C  N S 262 
PHE C    C  N N 263 
PHE O    O  N N 264 
PHE CB   C  N N 265 
PHE CG   C  Y N 266 
PHE CD1  C  Y N 267 
PHE CD2  C  Y N 268 
PHE CE1  C  Y N 269 
PHE CE2  C  Y N 270 
PHE CZ   C  Y N 271 
PHE OXT  O  N N 272 
PHE H    H  N N 273 
PHE H2   H  N N 274 
PHE HA   H  N N 275 
PHE HB2  H  N N 276 
PHE HB3  H  N N 277 
PHE HD1  H  N N 278 
PHE HD2  H  N N 279 
PHE HE1  H  N N 280 
PHE HE2  H  N N 281 
PHE HZ   H  N N 282 
PHE HXT  H  N N 283 
PO4 P    P  N N 284 
PO4 O1   O  N N 285 
PO4 O2   O  N N 286 
PO4 O3   O  N N 287 
PO4 O4   O  N N 288 
PRO N    N  N N 289 
PRO CA   C  N S 290 
PRO C    C  N N 291 
PRO O    O  N N 292 
PRO CB   C  N N 293 
PRO CG   C  N N 294 
PRO CD   C  N N 295 
PRO OXT  O  N N 296 
PRO H    H  N N 297 
PRO HA   H  N N 298 
PRO HB2  H  N N 299 
PRO HB3  H  N N 300 
PRO HG2  H  N N 301 
PRO HG3  H  N N 302 
PRO HD2  H  N N 303 
PRO HD3  H  N N 304 
PRO HXT  H  N N 305 
SER N    N  N N 306 
SER CA   C  N S 307 
SER C    C  N N 308 
SER O    O  N N 309 
SER CB   C  N N 310 
SER OG   O  N N 311 
SER OXT  O  N N 312 
SER H    H  N N 313 
SER H2   H  N N 314 
SER HA   H  N N 315 
SER HB2  H  N N 316 
SER HB3  H  N N 317 
SER HG   H  N N 318 
SER HXT  H  N N 319 
THR N    N  N N 320 
THR CA   C  N S 321 
THR C    C  N N 322 
THR O    O  N N 323 
THR CB   C  N R 324 
THR OG1  O  N N 325 
THR CG2  C  N N 326 
THR OXT  O  N N 327 
THR H    H  N N 328 
THR H2   H  N N 329 
THR HA   H  N N 330 
THR HB   H  N N 331 
THR HG1  H  N N 332 
THR HG21 H  N N 333 
THR HG22 H  N N 334 
THR HG23 H  N N 335 
THR HXT  H  N N 336 
TRP N    N  N N 337 
TRP CA   C  N S 338 
TRP C    C  N N 339 
TRP O    O  N N 340 
TRP CB   C  N N 341 
TRP CG   C  Y N 342 
TRP CD1  C  Y N 343 
TRP CD2  C  Y N 344 
TRP NE1  N  Y N 345 
TRP CE2  C  Y N 346 
TRP CE3  C  Y N 347 
TRP CZ2  C  Y N 348 
TRP CZ3  C  Y N 349 
TRP CH2  C  Y N 350 
TRP OXT  O  N N 351 
TRP H    H  N N 352 
TRP H2   H  N N 353 
TRP HA   H  N N 354 
TRP HB2  H  N N 355 
TRP HB3  H  N N 356 
TRP HD1  H  N N 357 
TRP HE1  H  N N 358 
TRP HE3  H  N N 359 
TRP HZ2  H  N N 360 
TRP HZ3  H  N N 361 
TRP HH2  H  N N 362 
TRP HXT  H  N N 363 
TYR N    N  N N 364 
TYR CA   C  N S 365 
TYR C    C  N N 366 
TYR O    O  N N 367 
TYR CB   C  N N 368 
TYR CG   C  Y N 369 
TYR CD1  C  Y N 370 
TYR CD2  C  Y N 371 
TYR CE1  C  Y N 372 
TYR CE2  C  Y N 373 
TYR CZ   C  Y N 374 
TYR OH   O  N N 375 
TYR OXT  O  N N 376 
TYR H    H  N N 377 
TYR H2   H  N N 378 
TYR HA   H  N N 379 
TYR HB2  H  N N 380 
TYR HB3  H  N N 381 
TYR HD1  H  N N 382 
TYR HD2  H  N N 383 
TYR HE1  H  N N 384 
TYR HE2  H  N N 385 
TYR HH   H  N N 386 
TYR HXT  H  N N 387 
VAL N    N  N N 388 
VAL CA   C  N S 389 
VAL C    C  N N 390 
VAL O    O  N N 391 
VAL CB   C  N N 392 
VAL CG1  C  N N 393 
VAL CG2  C  N N 394 
VAL OXT  O  N N 395 
VAL H    H  N N 396 
VAL H2   H  N N 397 
VAL HA   H  N N 398 
VAL HB   H  N N 399 
VAL HG11 H  N N 400 
VAL HG12 H  N N 401 
VAL HG13 H  N N 402 
VAL HG21 H  N N 403 
VAL HG22 H  N N 404 
VAL HG23 H  N N 405 
VAL HXT  H  N N 406 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PO4 P   O1   doub N N 269 
PO4 P   O2   sing N N 270 
PO4 P   O3   sing N N 271 
PO4 P   O4   sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of Dental and Craniofacial Research (NIH/NIDCR)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           DE030667 
_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   9ARC 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 2 21 21' 
_space_group.name_Hall        'P 2 2ab (z,x,y)' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9MDM 
_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]   0.024153 
_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]   0.010068 
_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]   0.008333 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
NA ? ? 9.38062 1.54875 ? ? 3.38349  72.32734 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P  ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . LYS A 1 8   ? -6.68609  80.64956 33.13991  1.000 46.88508  ? 211  LYS A N   1 
ATOM   2    C  CA  . LYS A 1 8   ? -6.66835  79.23397 33.48258  1.000 46.81802  ? 211  LYS A CA  1 
ATOM   3    C  C   . LYS A 1 8   ? -5.71460  78.47257 32.56849  1.000 44.46331  ? 211  LYS A C   1 
ATOM   4    O  O   . LYS A 1 8   ? -5.57550  78.80308 31.39128  1.000 48.10421  ? 211  LYS A O   1 
ATOM   5    C  CB  . LYS A 1 8   ? -8.07753  78.64293 33.39330  1.000 44.95350  ? 211  LYS A CB  1 
ATOM   6    N  N   . LYS A 1 9   ? -5.05320  77.45974 33.12187  1.000 39.65619  ? 212  LYS A N   1 
ATOM   7    C  CA  . LYS A 1 9   ? -4.16690  76.61534 32.33386  1.000 42.26904  ? 212  LYS A CA  1 
ATOM   8    C  C   . LYS A 1 9   ? -4.96840  75.68862 31.42843  1.000 40.59806  ? 212  LYS A C   1 
ATOM   9    O  O   . LYS A 1 9   ? -6.04972  75.21449 31.78540  1.000 41.20832  ? 212  LYS A O   1 
ATOM   10   C  CB  . LYS A 1 9   ? -3.27357  75.76980 33.24078  1.000 41.19675  ? 212  LYS A CB  1 
ATOM   11   C  CG  . LYS A 1 9   ? -2.31372  76.55314 34.10592  1.000 42.42071  ? 212  LYS A CG  1 
ATOM   12   C  CD  . LYS A 1 9   ? -1.35378  75.60202 34.80586  1.000 43.96440  ? 212  LYS A CD  1 
ATOM   13   C  CE  . LYS A 1 9   ? -0.27700  76.36364 35.56114  1.000 48.42519  ? 212  LYS A CE  1 
ATOM   14   N  NZ  . LYS A 1 9   ? 0.73557   75.44625 36.15212  1.000 49.00834  ? 212  LYS A NZ  1 
ATOM   15   N  N   . LYS A 1 10  ? -4.42191  75.41870 30.25021  1.000 33.39307  ? 213  LYS A N   1 
ATOM   16   C  CA  . LYS A 1 10  ? -5.06797  74.44787 29.38822  1.000 31.88263  ? 213  LYS A CA  1 
ATOM   17   C  C   . LYS A 1 10  ? -4.74350  73.03697 29.86777  1.000 32.90156  ? 213  LYS A C   1 
ATOM   18   O  O   . LYS A 1 10  ? -3.57542  72.73051 30.12147  1.000 32.26449  ? 213  LYS A O   1 
ATOM   19   C  CB  . LYS A 1 10  ? -4.61897  74.62363 27.94724  1.000 31.21811  ? 213  LYS A CB  1 
ATOM   20   C  CG  . LYS A 1 10  ? -5.24737  73.59975 27.02053  1.000 42.54620  ? 213  LYS A CG  1 
ATOM   21   C  CD  . LYS A 1 10  ? -5.10794  73.96756 25.56199  1.000 40.29030  ? 213  LYS A CD  1 
ATOM   22   C  CE  . LYS A 1 10  ? -5.67355  72.85179 24.69591  1.000 40.89728  ? 213  LYS A CE  1 
ATOM   23   N  NZ  . LYS A 1 10  ? -5.72078  73.21553 23.24896  1.000 49.12955  ? 213  LYS A NZ  1 
ATOM   24   N  N   . PRO A 1 11  ? -5.73310  72.15661 29.99782  1.000 31.70264  ? 214  PRO A N   1 
ATOM   25   C  CA  . PRO A 1 11  ? -5.43457  70.78044 30.40628  1.000 30.50531  ? 214  PRO A CA  1 
ATOM   26   C  C   . PRO A 1 11  ? -4.60635  70.07148 29.35171  1.000 31.92202  ? 214  PRO A C   1 
ATOM   27   O  O   . PRO A 1 11  ? -4.58112  70.45034 28.18059  1.000 32.20980  ? 214  PRO A O   1 
ATOM   28   C  CB  . PRO A 1 11  ? -6.81809  70.13448 30.54825  1.000 31.05801  ? 214  PRO A CB  1 
ATOM   29   C  CG  . PRO A 1 11  ? -7.75587  71.27413 30.74045  1.000 36.42385  ? 214  PRO A CG  1 
ATOM   30   C  CD  . PRO A 1 11  ? -7.18181  72.40803 29.93408  1.000 37.98596  ? 214  PRO A CD  1 
ATOM   31   N  N   . GLN A 1 12  ? -3.92239  69.01822 29.79076  1.000 29.65572  ? 215  GLN A N   1 
ATOM   32   C  CA  . GLN A 1 12  ? -3.08661  68.21757 28.91601  1.000 32.14849  ? 215  GLN A CA  1 
ATOM   33   C  C   . GLN A 1 12  ? -3.39254  66.75235 29.15243  1.000 31.61956  ? 215  GLN A C   1 
ATOM   34   O  O   . GLN A 1 12  ? -3.98492  66.37895 30.17089  1.000 27.92890  ? 215  GLN A O   1 
ATOM   35   C  CB  . GLN A 1 12  ? -1.59604  68.45795 29.15893  1.000 32.72811  ? 215  GLN A CB  1 
ATOM   36   C  CG  . GLN A 1 12  ? -1.14971  69.90050 29.04505  1.000 39.77546  ? 215  GLN A CG  1 
ATOM   37   C  CD  . GLN A 1 12  ? 0.33010   70.04403 29.30488  1.000 48.13169  ? 215  GLN A CD  1 
ATOM   38   O  OE1 . GLN A 1 12  ? 1.15416   69.42171 28.63259  1.000 50.97468  ? 215  GLN A OE1 1 
ATOM   39   N  NE2 . GLN A 1 12  ? 0.67734   70.84888 30.29551  1.000 48.02795  ? 215  GLN A NE2 1 
ATOM   40   N  N   . ILE A 1 13  ? -2.96993  65.91530 28.20591  1.000 29.39553  ? 216  ILE A N   1 
ATOM   41   C  CA  . ILE A 1 13  ? -2.96793  64.47466 28.42939  1.000 28.80454  ? 216  ILE A CA  1 
ATOM   42   C  C   . ILE A 1 13  ? -1.57923  63.92749 28.14269  1.000 28.33937  ? 216  ILE A C   1 
ATOM   43   O  O   . ILE A 1 13  ? -0.83697  64.44751 27.30347  1.000 34.12976  ? 216  ILE A O   1 
ATOM   44   C  CB  . ILE A 1 13  ? -4.03335  63.71037 27.60717  1.000 31.21594  ? 216  ILE A CB  1 
ATOM   45   C  CG1 . ILE A 1 13  ? -3.81698  63.88131 26.09557  1.000 30.01870  ? 216  ILE A CG1 1 
ATOM   46   C  CG2 . ILE A 1 13  ? -5.43444  64.11107 28.05684  1.000 29.92005  ? 216  ILE A CG2 1 
ATOM   47   C  CD1 . ILE A 1 13  ? -4.74323  63.01200 25.25101  1.000 31.61622  ? 216  ILE A CD1 1 
ATOM   48   N  N   . LYS A 1 14  ? -1.21993  62.88195 28.87766  1.000 27.01486  ? 217  LYS A N   1 
ATOM   49   C  CA  . LYS A 1 14  ? 0.05965   62.21442 28.70016  1.000 27.64873  ? 217  LYS A CA  1 
ATOM   50   C  C   . LYS A 1 14  ? -0.15697  60.71513 28.73744  1.000 27.21691  ? 217  LYS A C   1 
ATOM   51   O  O   . LYS A 1 14  ? -1.07701  60.22140 29.39689  1.000 27.54878  ? 217  LYS A O   1 
ATOM   52   C  CB  . LYS A 1 14  ? 1.06635   62.61878 29.79257  1.000 32.61896  ? 217  LYS A CB  1 
ATOM   53   C  CG  . LYS A 1 14  ? 1.39657   64.10686 29.77597  1.000 35.03003  ? 217  LYS A CG  1 
ATOM   54   C  CD  . LYS A 1 14  ? 2.49811   64.46647 30.75745  1.000 43.05068  ? 217  LYS A CD  1 
ATOM   55   C  CE  . LYS A 1 14  ? 2.79646   65.96822 30.67514  1.000 52.52788  ? 217  LYS A CE  1 
ATOM   56   N  NZ  . LYS A 1 14  ? 3.93966   66.39851 31.53362  1.000 60.10926  ? 217  LYS A NZ  1 
ATOM   57   N  N   . TYR A 1 15  ? 0.72301   60.00199 28.04025  1.000 28.75869  ? 218  TYR A N   1 
ATOM   58   C  CA  . TYR A 1 15  ? 0.76828   58.55183 28.03323  1.000 27.38597  ? 218  TYR A CA  1 
ATOM   59   C  C   . TYR A 1 15  ? 2.21523   58.14218 27.79380  1.000 32.88924  ? 218  TYR A C   1 
ATOM   60   O  O   . TYR A 1 15  ? 2.90366   58.75767 26.97719  1.000 34.07761  ? 218  TYR A O   1 
ATOM   61   C  CB  . TYR A 1 15  ? -0.14453  57.96162 26.94402  1.000 28.89158  ? 218  TYR A CB  1 
ATOM   62   C  CG  . TYR A 1 15  ? -0.13178  56.45960 26.93756  1.000 24.87726  ? 218  TYR A CG  1 
ATOM   63   C  CD1 . TYR A 1 15  ? -0.95180  55.74307 27.80422  1.000 28.73509  ? 218  TYR A CD1 1 
ATOM   64   C  CD2 . TYR A 1 15  ? 0.72354   55.75403 26.10090  1.000 29.89936  ? 218  TYR A CD2 1 
ATOM   65   C  CE1 . TYR A 1 15  ? -0.93023  54.36808 27.83144  1.000 28.60665  ? 218  TYR A CE1 1 
ATOM   66   C  CE2 . TYR A 1 15  ? 0.74620   54.37450 26.11382  1.000 28.25213  ? 218  TYR A CE2 1 
ATOM   67   C  CZ  . TYR A 1 15  ? -0.07921  53.68846 26.99354  1.000 29.13581  ? 218  TYR A CZ  1 
ATOM   68   O  OH  . TYR A 1 15  ? -0.07194  52.30496 27.03988  1.000 29.42603  ? 218  TYR A OH  1 
ATOM   69   N  N   . GLU A 1 16  ? 2.67642   57.10070 28.49241  1.000 35.05619  ? 219  GLU A N   1 
ATOM   70   C  CA  . GLU A 1 16  ? 4.02617   56.58162 28.25102  1.000 35.70703  ? 219  GLU A CA  1 
ATOM   71   C  C   . GLU A 1 16  ? 3.97936   55.66297 27.03562  1.000 36.16503  ? 219  GLU A C   1 
ATOM   72   O  O   . GLU A 1 16  ? 3.60482   54.49086 27.14258  1.000 33.91991  ? 219  GLU A O   1 
ATOM   73   C  CB  . GLU A 1 16  ? 4.55935   55.85710 29.48294  1.000 36.11540  ? 219  GLU A CB  1 
ATOM   74   C  CG  . GLU A 1 16  ? 5.89022   55.13532 29.26726  1.000 38.90305  ? 219  GLU A CG  1 
ATOM   75   C  CD  . GLU A 1 16  ? 6.93008   55.99954 28.56344  1.000 48.59472  ? 219  GLU A CD  1 
ATOM   76   O  OE1 . GLU A 1 16  ? 7.07618   55.87095 27.32532  1.000 42.48947  ? 219  GLU A OE1 1 
ATOM   77   O  OE2 . GLU A 1 16  ? 7.59755   56.80933 29.24816  1.000 53.57797  ? 219  GLU A OE2 1 
ATOM   78   N  N   . GLU A 1 17  ? 4.38047   56.18841 25.86845  1.000 33.36213  ? 220  GLU A N   1 
ATOM   79   C  CA  . GLU A 1 17  ? 4.20365   55.46284 24.61390  1.000 36.49081  ? 220  GLU A CA  1 
ATOM   80   C  C   . GLU A 1 17  ? 5.05375   54.20033 24.52681  1.000 36.48617  ? 220  GLU A C   1 
ATOM   81   O  O   . GLU A 1 17  ? 4.73367   53.31623 23.72962  1.000 38.38821  ? 220  GLU A O   1 
ATOM   82   C  CB  . GLU A 1 17  ? 4.51046   56.37107 23.41505  1.000 38.05576  ? 220  GLU A CB  1 
ATOM   83   C  CG  . GLU A 1 17  ? 3.50497   57.49851 23.22569  1.000 39.51828  ? 220  GLU A CG  1 
ATOM   84   C  CD  . GLU A 1 17  ? 3.71219   58.27722 21.92394  1.000 42.47096  ? 220  GLU A CD  1 
ATOM   85   O  OE1 . GLU A 1 17  ? 4.41463   57.78299 21.01742  1.000 44.48160  ? 220  GLU A OE1 1 
ATOM   86   O  OE2 . GLU A 1 17  ? 3.16334   59.38509 21.80967  1.000 44.48005  ? 220  GLU A OE2 1 
ATOM   87   N  N   . LYS A 1 18  ? 6.10917   54.08115 25.33714  1.000 38.95360  ? 221  LYS A N   1 
ATOM   88   C  CA  . LYS A 1 18  ? 6.86526   52.83165 25.37414  1.000 37.53905  ? 221  LYS A CA  1 
ATOM   89   C  C   . LYS A 1 18  ? 6.03606   51.65995 25.89483  1.000 34.81537  ? 221  LYS A C   1 
ATOM   90   O  O   . LYS A 1 18  ? 6.40393   50.50298 25.66114  1.000 38.23219  ? 221  LYS A O   1 
ATOM   91   C  CB  . LYS A 1 18  ? 8.12396   53.00737 26.22386  1.000 43.50304  ? 221  LYS A CB  1 
ATOM   92   C  CG  . LYS A 1 18  ? 9.19798   53.87553 25.56969  1.000 48.00946  ? 221  LYS A CG  1 
ATOM   93   N  N   A GLN A 1 19  ? 4.95429   51.91807 26.62944  0.599 32.75012  ? 222  GLN A N   1 
ATOM   94   N  N   B GLN A 1 19  ? 4.89913   51.93662 26.52729  0.401 32.92901  ? 222  GLN A N   1 
ATOM   95   C  CA  A GLN A 1 19  ? 4.09519   50.84398 27.12362  0.599 33.86501  ? 222  GLN A CA  1 
ATOM   96   C  CA  B GLN A 1 19  ? 4.03304   50.91686 27.11687  0.401 33.81204  ? 222  GLN A CA  1 
ATOM   97   C  C   A GLN A 1 19  ? 3.05238   50.51747 26.05897  0.599 30.03047  ? 222  GLN A C   1 
ATOM   98   C  C   B GLN A 1 19  ? 2.97913   50.49888 26.09283  0.401 30.08189  ? 222  GLN A C   1 
ATOM   99   O  O   A GLN A 1 19  ? 2.18230   51.33973 25.74741  0.599 30.78840  ? 222  GLN A O   1 
ATOM   100  O  O   B GLN A 1 19  ? 2.01123   51.22505 25.84811  0.401 30.61206  ? 222  GLN A O   1 
ATOM   101  C  CB  A GLN A 1 19  ? 3.43393   51.21902 28.44880  0.599 34.14937  ? 222  GLN A CB  1 
ATOM   102  C  CB  B GLN A 1 19  ? 3.39983   51.47443 28.38585  0.401 34.41565  ? 222  GLN A CB  1 
ATOM   103  C  CG  A GLN A 1 19  ? 4.38739   51.28205 29.64298  0.599 34.90040  ? 222  GLN A CG  1 
ATOM   104  C  CG  B GLN A 1 19  ? 2.59007   50.51904 29.21937  0.401 30.69016  ? 222  GLN A CG  1 
ATOM   105  C  CD  A GLN A 1 19  ? 4.84828   49.90864 30.12919  0.599 38.65377  ? 222  GLN A CD  1 
ATOM   106  C  CD  B GLN A 1 19  ? 2.18840   51.15702 30.53741  0.401 34.81322  ? 222  GLN A CD  1 
ATOM   107  O  OE1 A GLN A 1 19  ? 4.27515   48.87711 29.77249  0.599 41.71715  ? 222  GLN A OE1 1 
ATOM   108  O  OE1 B GLN A 1 19  ? 3.02097   51.73844 31.23473  0.401 39.33184  ? 222  GLN A OE1 1 
ATOM   109  N  NE2 A GLN A 1 19  ? 5.89503   49.89769 30.94561  0.599 44.68850  ? 222  GLN A NE2 1 
ATOM   110  N  NE2 B GLN A 1 19  ? 0.90818   51.07573 30.87147  0.401 35.26942  ? 222  GLN A NE2 1 
ATOM   111  N  N   . ALA A 1 20  ? 3.15429   49.32677 25.48409  1.000 26.98453  ? 223  ALA A N   1 
ATOM   112  C  CA  . ALA A 1 20  ? 2.13280   48.84734 24.56980  1.000 30.85913  ? 223  ALA A CA  1 
ATOM   113  C  C   . ALA A 1 20  ? 0.91981   48.36491 25.35776  1.000 26.88352  ? 223  ALA A C   1 
ATOM   114  O  O   . ALA A 1 20  ? 1.03561   47.90846 26.49499  1.000 30.12080  ? 223  ALA A O   1 
ATOM   115  C  CB  . ALA A 1 20  ? 2.66655   47.71464 23.69047  1.000 34.10483  ? 223  ALA A CB  1 
ATOM   116  N  N   . VAL A 1 21  ? -0.24956  48.48010 24.74178  1.000 26.63802  ? 224  VAL A N   1 
ATOM   117  C  CA  . VAL A 1 21  ? -1.50466  47.97916 25.29455  1.000 27.07136  ? 224  VAL A CA  1 
ATOM   118  C  C   . VAL A 1 21  ? -1.77878  46.63803 24.63272  1.000 26.38792  ? 224  VAL A C   1 
ATOM   119  O  O   . VAL A 1 21  ? -1.96937  46.58079 23.41315  1.000 29.19175  ? 224  VAL A O   1 
ATOM   120  C  CB  . VAL A 1 21  ? -2.65665  48.96592 25.03652  1.000 25.77241  ? 224  VAL A CB  1 
ATOM   121  C  CG1 . VAL A 1 21  ? -3.97732  48.38589 25.54314  1.000 27.51526  ? 224  VAL A CG1 1 
ATOM   122  C  CG2 . VAL A 1 21  ? -2.35675  50.32668 25.68268  1.000 25.20676  ? 224  VAL A CG2 1 
ATOM   123  N  N   . MET A 1 22  ? -1.80623  45.55400 25.42303  1.000 26.80759  ? 225  MET A N   1 
ATOM   124  C  CA  . MET A 1 22  ? -1.75915  44.19773 24.87394  1.000 26.69991  ? 225  MET A CA  1 
ATOM   125  C  C   . MET A 1 22  ? -2.93895  43.35818 25.34856  1.000 24.96869  ? 225  MET A C   1 
ATOM   126  O  O   . MET A 1 22  ? -2.80930  42.54554 26.27794  1.000 28.64077  ? 225  MET A O   1 
ATOM   127  C  CB  . MET A 1 22  ? -0.42006  43.54852 25.20656  1.000 27.06690  ? 225  MET A CB  1 
ATOM   128  C  CG  . MET A 1 22  ? 0.74563   44.36289 24.62563  1.000 32.16389  ? 225  MET A CG  1 
ATOM   129  S  SD  . MET A 1 22  ? 2.37795   43.61552 24.75374  1.000 43.49179  ? 225  MET A SD  1 
ATOM   130  C  CE  . MET A 1 22  ? 2.88128   44.11347 26.39722  1.000 46.05627  ? 225  MET A CE  1 
ATOM   131  N  N   . PRO A 1 23  ? -4.09743  43.50021 24.70820  1.000 25.22839  ? 226  PRO A N   1 
ATOM   132  C  CA  . PRO A 1 23  ? -5.24117  42.65572 25.07087  1.000 29.73516  ? 226  PRO A CA  1 
ATOM   133  C  C   . PRO A 1 23  ? -4.94622  41.19216 24.78528  1.000 29.30218  ? 226  PRO A C   1 
ATOM   134  O  O   . PRO A 1 23  ? -4.21427  40.86211 23.85208  1.000 28.26654  ? 226  PRO A O   1 
ATOM   135  C  CB  . PRO A 1 23  ? -6.37556  43.16822 24.17289  1.000 30.52957  ? 226  PRO A CB  1 
ATOM   136  C  CG  . PRO A 1 23  ? -5.86365  44.38766 23.48976  1.000 32.58647  ? 226  PRO A CG  1 
ATOM   137  C  CD  . PRO A 1 23  ? -4.37714  44.36622 23.54777  1.000 26.59622  ? 226  PRO A CD  1 
ATOM   138  N  N   A GLU A 1 24  ? -5.50812  40.31247 25.62158  0.729 28.47726  ? 227  GLU A N   1 
ATOM   139  N  N   B GLU A 1 24  ? -5.53419  40.31751 25.59807  0.271 28.65397  ? 227  GLU A N   1 
ATOM   140  C  CA  A GLU A 1 24  ? -5.44579  38.87588 25.36849  0.729 32.15327  ? 227  GLU A CA  1 
ATOM   141  C  CA  B GLU A 1 24  ? -5.44793  38.88986 25.34110  0.271 32.19658  ? 227  GLU A CA  1 
ATOM   142  C  C   A GLU A 1 24  ? -6.17769  38.54157 24.06453  0.729 30.89939  ? 227  GLU A C   1 
ATOM   143  C  C   B GLU A 1 24  ? -6.16768  38.54652 24.03909  0.271 30.87879  ? 227  GLU A C   1 
ATOM   144  O  O   A GLU A 1 24  ? -6.86920  39.37318 23.47362  0.729 29.94593  ? 227  GLU A O   1 
ATOM   145  O  O   B GLU A 1 24  ? -6.84119  39.37950 23.42566  0.271 29.90438  ? 227  GLU A O   1 
ATOM   146  C  CB  A GLU A 1 24  ? -6.04818  38.07908 26.53804  0.729 33.26681  ? 227  GLU A CB  1 
ATOM   147  C  CB  B GLU A 1 24  ? -6.04124  38.09554 26.50430  0.271 33.26752  ? 227  GLU A CB  1 
ATOM   148  C  CG  A GLU A 1 24  ? -5.35448  38.28174 27.90746  0.729 35.40354  ? 227  GLU A CG  1 
ATOM   149  C  CG  B GLU A 1 24  ? -5.47547  38.49170 27.85369  0.271 36.00687  ? 227  GLU A CG  1 
ATOM   150  C  CD  A GLU A 1 24  ? -5.91016  37.38997 29.03115  0.729 45.60597  ? 227  GLU A CD  1 
ATOM   151  C  CD  B GLU A 1 24  ? -3.96301  38.58966 27.83405  0.271 37.51035  ? 227  GLU A CD  1 
ATOM   152  O  OE1 A GLU A 1 24  ? -6.13746  36.18264 28.79101  0.729 48.11238  ? 227  GLU A OE1 1 
ATOM   153  O  OE1 B GLU A 1 24  ? -3.30979  37.59730 27.45096  0.271 41.70831  ? 227  GLU A OE1 1 
ATOM   154  O  OE2 A GLU A 1 24  ? -6.11143  37.89884 30.16371  0.729 44.31264  ? 227  GLU A OE2 1 
ATOM   155  O  OE2 B GLU A 1 24  ? -3.42654  39.66232 28.18856  0.271 40.53757  ? 227  GLU A OE2 1 
ATOM   156  N  N   . SER A 1 25  ? -6.02281  37.29075 23.61277  1.000 30.96608  ? 228  SER A N   1 
ATOM   157  C  CA  . SER A 1 25  ? -6.64290  36.88969 22.35347  1.000 27.78575  ? 228  SER A CA  1 
ATOM   158  C  C   . SER A 1 25  ? -8.16352  36.82319 22.44453  1.000 28.12926  ? 228  SER A C   1 
ATOM   159  O  O   . SER A 1 25  ? -8.83364  36.89016 21.41010  1.000 30.19796  ? 228  SER A O   1 
ATOM   160  C  CB  . SER A 1 25  ? -6.09401  35.53687 21.88241  1.000 28.53189  ? 228  SER A CB  1 
ATOM   161  O  OG  . SER A 1 25  ? -6.38807  34.50797 22.80738  1.000 34.86329  ? 228  SER A OG  1 
ATOM   162  N  N   . ALA A 1 26  ? -8.72637  36.69043 23.64408  1.000 27.34576  ? 229  ALA A N   1 
ATOM   163  C  CA  . ALA A 1 26  ? -10.17415 36.58349 23.76576  1.000 30.68819  ? 229  ALA A CA  1 
ATOM   164  C  C   . ALA A 1 26  ? -10.86590 37.87426 23.31672  1.000 30.85653  ? 229  ALA A C   1 
ATOM   165  O  O   . ALA A 1 26  ? -10.32348 38.97660 23.44081  1.000 29.41712  ? 229  ALA A O   1 
ATOM   166  C  CB  . ALA A 1 26  ? -10.56205 36.25103 25.20676  1.000 30.56821  ? 229  ALA A CB  1 
ATOM   167  N  N   . ALA A 1 27  ? -12.06700 37.71764 22.75847  1.000 30.29674  ? 230  ALA A N   1 
ATOM   168  C  CA  . ALA A 1 27  ? -12.93007 38.85977 22.49477  1.000 33.25999  ? 230  ALA A CA  1 
ATOM   169  C  C   . ALA A 1 27  ? -13.23274 39.59820 23.78960  1.000 32.46273  ? 230  ALA A C   1 
ATOM   170  O  O   . ALA A 1 27  ? -13.33957 38.99381 24.85919  1.000 32.83810  ? 230  ALA A O   1 
ATOM   171  C  CB  . ALA A 1 27  ? -14.24065 38.40411 21.85759  1.000 33.37009  ? 230  ALA A CB  1 
ATOM   172  N  N   . GLY A 1 28  ? -13.38499 40.91416 23.69366  1.000 27.63942  ? 231  GLY A N   1 
ATOM   173  C  CA  . GLY A 1 28  ? -13.76283 41.67618 24.87207  1.000 30.52802  ? 231  GLY A CA  1 
ATOM   174  C  C   . GLY A 1 28  ? -13.54224 43.15500 24.66826  1.000 32.26375  ? 231  GLY A C   1 
ATOM   175  O  O   . GLY A 1 28  ? -12.93699 43.59750 23.68583  1.000 28.48467  ? 231  GLY A O   1 
ATOM   176  N  N   . THR A 1 29  ? -14.06188 43.92836 25.61876  1.000 28.71095  ? 232  THR A N   1 
ATOM   177  C  CA  . THR A 1 29  ? -13.80752 45.36247 25.67453  1.000 25.97381  ? 232  THR A CA  1 
ATOM   178  C  C   . THR A 1 29  ? -12.64812 45.56389 26.63635  1.000 27.88213  ? 232  THR A C   1 
ATOM   179  O  O   . THR A 1 29  ? -12.76961 45.26969 27.83108  1.000 30.15015  ? 232  THR A O   1 
ATOM   180  C  CB  . THR A 1 29  ? -15.04445 46.13831 26.11240  1.000 28.66197  ? 232  THR A CB  1 
ATOM   181  O  OG1 . THR A 1 29  ? -16.09033 45.92801 25.15762  1.000 33.74382  ? 232  THR A OG1 1 
ATOM   182  C  CG2 . THR A 1 29  ? -14.72945 47.64151 26.20954  1.000 30.05380  ? 232  THR A CG2 1 
ATOM   183  N  N   . TYR A 1 30  ? -11.51875 46.02387 26.10751  1.000 25.22204  ? 233  TYR A N   1 
ATOM   184  C  CA  . TYR A 1 30  ? -10.30071 46.22298 26.87585  1.000 25.49338  ? 233  TYR A CA  1 
ATOM   185  C  C   . TYR A 1 30  ? -10.05727 47.70880 27.11382  1.000 26.00644  ? 233  TYR A C   1 
ATOM   186  O  O   . TYR A 1 30  ? -10.61427 48.57208 26.42510  1.000 25.16496  ? 233  TYR A O   1 
ATOM   187  C  CB  . TYR A 1 30  ? -9.10964  45.59219 26.16021  1.000 25.01516  ? 233  TYR A CB  1 
ATOM   188  C  CG  . TYR A 1 30  ? -9.25081  44.09143 26.03505  1.000 26.65833  ? 233  TYR A CG  1 
ATOM   189  C  CD1 . TYR A 1 30  ? -8.85110  43.26379 27.06770  1.000 27.50472  ? 233  TYR A CD1 1 
ATOM   190  C  CD2 . TYR A 1 30  ? -9.79381  43.50606 24.89563  1.000 28.19777  ? 233  TYR A CD2 1 
ATOM   191  C  CE1 . TYR A 1 30  ? -8.96670  41.88746 26.97392  1.000 29.25004  ? 233  TYR A CE1 1 
ATOM   192  C  CE2 . TYR A 1 30  ? -9.91595  42.10608 24.78999  1.000 28.94541  ? 233  TYR A CE2 1 
ATOM   193  C  CZ  . TYR A 1 30  ? -9.49306  41.31124 25.84663  1.000 28.66292  ? 233  TYR A CZ  1 
ATOM   194  O  OH  . TYR A 1 30  ? -9.58923  39.92130 25.81281  1.000 30.63463  ? 233  TYR A OH  1 
ATOM   195  N  N   . THR A 1 31  ? -9.23242  48.00638 28.11897  1.000 24.17074  ? 234  THR A N   1 
ATOM   196  C  CA  . THR A 1 31  ? -9.04696  49.38946 28.53617  1.000 24.02997  ? 234  THR A CA  1 
ATOM   197  C  C   . THR A 1 31  ? -7.57917  49.70610 28.78019  1.000 24.41775  ? 234  THR A C   1 
ATOM   198  O  O   . THR A 1 31  ? -6.75751  48.82208 29.04052  1.000 25.31121  ? 234  THR A O   1 
ATOM   199  C  CB  . THR A 1 31  ? -9.83210  49.72448 29.80960  1.000 27.50056  ? 234  THR A CB  1 
ATOM   200  O  OG1 . THR A 1 31  ? -9.28480  48.99320 30.91725  1.000 25.46118  ? 234  THR A OG1 1 
ATOM   201  C  CG2 . THR A 1 31  ? -11.29737 49.38618 29.63115  1.000 26.68487  ? 234  THR A CG2 1 
ATOM   202  N  N   . PHE A 1 32  ? -7.27281  51.00186 28.70288  1.000 23.09642  ? 235  PHE A N   1 
ATOM   203  C  CA  . PHE A 1 32  ? -6.01539  51.55200 29.18401  1.000 24.16183  ? 235  PHE A CA  1 
ATOM   204  C  C   . PHE A 1 32  ? -6.29343  52.93096 29.76084  1.000 24.86349  ? 235  PHE A C   1 
ATOM   205  O  O   . PHE A 1 32  ? -7.39596  53.47753 29.62987  1.000 24.71015  ? 235  PHE A O   1 
ATOM   206  C  CB  . PHE A 1 32  ? -4.94255  51.60324 28.07908  1.000 22.88957  ? 235  PHE A CB  1 
ATOM   207  C  CG  . PHE A 1 32  ? -5.29143  52.48614 26.90784  1.000 24.20174  ? 235  PHE A CG  1 
ATOM   208  C  CD1 . PHE A 1 32  ? -6.01563  51.98284 25.82900  1.000 24.34177  ? 235  PHE A CD1 1 
ATOM   209  C  CD2 . PHE A 1 32  ? -4.85822  53.79841 26.86613  1.000 25.52566  ? 235  PHE A CD2 1 
ATOM   210  C  CE1 . PHE A 1 32  ? -6.31655  52.79894 24.73499  1.000 24.92755  ? 235  PHE A CE1 1 
ATOM   211  C  CE2 . PHE A 1 32  ? -5.15643  54.61467 25.77255  1.000 24.68954  ? 235  PHE A CE2 1 
ATOM   212  C  CZ  . PHE A 1 32  ? -5.88603  54.11821 24.72167  1.000 25.75479  ? 235  PHE A CZ  1 
ATOM   213  N  N   . GLU A 1 33  ? -5.28068  53.49091 30.40900  1.000 23.11517  ? 236  GLU A N   1 
ATOM   214  C  CA  . GLU A 1 33  ? -5.41007  54.76215 31.09846  1.000 23.67461  ? 236  GLU A CA  1 
ATOM   215  C  C   . GLU A 1 33  ? -4.55301  55.83698 30.44064  1.000 26.29837  ? 236  GLU A C   1 
ATOM   216  O  O   . GLU A 1 33  ? -3.43322  55.57089 29.99248  1.000 26.42165  ? 236  GLU A O   1 
ATOM   217  C  CB  . GLU A 1 33  ? -5.01362  54.59507 32.56534  1.000 25.91320  ? 236  GLU A CB  1 
ATOM   218  C  CG  . GLU A 1 33  ? -5.90759  53.61328 33.27525  1.000 29.08994  ? 236  GLU A CG  1 
ATOM   219  C  CD  . GLU A 1 33  ? -5.49961  53.36994 34.71646  1.000 34.65983  ? 236  GLU A CD  1 
ATOM   220  O  OE1 . GLU A 1 33  ? -4.31472  53.57691 35.05837  1.000 33.43236  ? 236  GLU A OE1 1 
ATOM   221  O  OE2 . GLU A 1 33  ? -6.37801  52.96468 35.49597  1.000 32.73031  ? 236  GLU A OE2 1 
ATOM   222  N  N   . VAL A 1 34  ? -5.08493  57.05788 30.40435  1.000 25.08476  ? 237  VAL A N   1 
ATOM   223  C  CA  . VAL A 1 34  ? -4.37627  58.24203 29.92453  1.000 24.72754  ? 237  VAL A CA  1 
ATOM   224  C  C   . VAL A 1 34  ? -4.33648  59.23839 31.07602  1.000 27.73116  ? 237  VAL A C   1 
ATOM   225  O  O   . VAL A 1 34  ? -5.36852  59.51493 31.69514  1.000 26.26437  ? 237  VAL A O   1 
ATOM   226  C  CB  . VAL A 1 34  ? -5.06176  58.85824 28.68535  1.000 24.37440  ? 237  VAL A CB  1 
ATOM   227  C  CG1 . VAL A 1 34  ? -4.50090  60.20960 28.38415  1.000 31.90515  ? 237  VAL A CG1 1 
ATOM   228  C  CG2 . VAL A 1 34  ? -4.87013  57.94641 27.45601  1.000 25.32310  ? 237  VAL A CG2 1 
ATOM   229  N  N   A GLN A 1 35  ? -3.15663  59.77719 31.36116  0.520 25.27286  ? 238  GLN A N   1 
ATOM   230  N  N   B GLN A 1 35  ? -3.14802  59.75903 31.36957  0.480 25.28027  ? 238  GLN A N   1 
ATOM   231  C  CA  A GLN A 1 35  ? -3.01838  60.73569 32.45025  0.520 26.01709  ? 238  GLN A CA  1 
ATOM   232  C  CA  B GLN A 1 35  ? -3.01781  60.75884 32.41977  0.480 26.02790  ? 238  GLN A CA  1 
ATOM   233  C  C   A GLN A 1 35  ? -3.59398  62.09188 32.03913  0.520 27.78567  ? 238  GLN A C   1 
ATOM   234  C  C   B GLN A 1 35  ? -3.67827  62.06395 31.98912  0.480 27.75869  ? 238  GLN A C   1 
ATOM   235  O  O   A GLN A 1 35  ? -3.29923  62.59498 30.95082  0.520 25.60663  ? 238  GLN A O   1 
ATOM   236  O  O   B GLN A 1 35  ? -3.52788  62.50735 30.84714  0.480 25.74498  ? 238  GLN A O   1 
ATOM   237  C  CB  A GLN A 1 35  ? -1.54717  60.86640 32.84571  0.520 29.29538  ? 238  GLN A CB  1 
ATOM   238  C  CB  B GLN A 1 35  ? -1.54400  60.99932 32.74808  0.480 29.11253  ? 238  GLN A CB  1 
ATOM   239  C  CG  A GLN A 1 35  ? -0.83925  59.51990 33.05913  0.520 26.34850  ? 238  GLN A CG  1 
ATOM   240  C  CG  B GLN A 1 35  ? -1.31854  61.86507 33.98268  0.480 28.15596  ? 238  GLN A CG  1 
ATOM   241  C  CD  A GLN A 1 35  ? -1.53588  58.62820 34.07948  0.520 33.08567  ? 238  GLN A CD  1 
ATOM   242  C  CD  B GLN A 1 35  ? 0.15059   61.98515 34.35665  0.480 35.44932  ? 238  GLN A CD  1 
ATOM   243  O  OE1 A GLN A 1 35  ? -1.75148  57.43263 33.83869  0.520 32.57604  ? 238  GLN A OE1 1 
ATOM   244  O  OE1 B GLN A 1 35  ? 1.03282   61.81347 33.51593  0.480 35.62630  ? 238  GLN A OE1 1 
ATOM   245  N  NE2 A GLN A 1 35  ? -1.88059  59.20120 35.22914  0.520 34.42548  ? 238  GLN A NE2 1 
ATOM   246  N  NE2 B GLN A 1 35  ? 0.41866   62.27595 35.62577  0.480 35.26350  ? 238  GLN A NE2 1 
ATOM   247  N  N   . THR A 1 36  ? -4.41867  62.67989 32.90930  1.000 25.10817  ? 239  THR A N   1 
ATOM   248  C  CA  . THR A 1 36  ? -5.05323  63.97128 32.66410  1.000 26.76408  ? 239  THR A CA  1 
ATOM   249  C  C   . THR A 1 36  ? -4.45538  64.98827 33.62696  1.000 26.86296  ? 239  THR A C   1 
ATOM   250  O  O   . THR A 1 36  ? -4.56869  64.83411 34.85317  1.000 28.55554  ? 239  THR A O   1 
ATOM   251  C  CB  . THR A 1 36  ? -6.57767  63.89635 32.81018  1.000 25.06731  ? 239  THR A CB  1 
ATOM   252  O  OG1 . THR A 1 36  ? -6.92685  63.24560 34.04095  1.000 27.94404  ? 239  THR A OG1 1 
ATOM   253  C  CG2 . THR A 1 36  ? -7.18098  63.10030 31.64344  1.000 27.14526  ? 239  THR A CG2 1 
ATOM   254  N  N   . ILE A 1 37  ? -3.81168  66.01128 33.06166  1.000 26.90578  ? 240  ILE A N   1 
ATOM   255  C  CA  . ILE A 1 37  ? -3.03673  67.00880 33.79233  1.000 29.03046  ? 240  ILE A CA  1 
ATOM   256  C  C   . ILE A 1 37  ? -3.78946  68.32906 33.75889  1.000 31.99769  ? 240  ILE A C   1 
ATOM   257  O  O   . ILE A 1 37  ? -4.28425  68.74266 32.70431  1.000 29.45251  ? 240  ILE A O   1 
ATOM   258  C  CB  . ILE A 1 37  ? -1.63256  67.17101 33.18043  1.000 32.05894  ? 240  ILE A CB  1 
ATOM   259  C  CG1 . ILE A 1 37  ? -0.87413  65.83667 33.21418  1.000 40.30189  ? 240  ILE A CG1 1 
ATOM   260  C  CG2 . ILE A 1 37  ? -0.84107  68.26219 33.88565  1.000 36.05698  ? 240  ILE A CG2 1 
ATOM   261  C  CD1 . ILE A 1 37  ? -0.29939  65.49740 34.56466  1.000 43.22580  ? 240  ILE A CD1 1 
ATOM   262  N  N   . ASP A 1 38  ? -3.86125  68.99631 34.91131  1.000 28.52096  ? 241  ASP A N   1 
ATOM   263  C  CA  . ASP A 1 38  ? -4.44598  70.32894 35.01978  1.000 28.07832  ? 241  ASP A CA  1 
ATOM   264  C  C   . ASP A 1 38  ? -5.89813  70.36558 34.54932  1.000 30.42875  ? 241  ASP A C   1 
ATOM   265  O  O   . ASP A 1 38  ? -6.34376  71.36561 33.97820  1.000 39.05793  ? 241  ASP A O   1 
ATOM   266  C  CB  . ASP A 1 38  ? -3.61462  71.36474 34.24467  1.000 34.82482  ? 241  ASP A CB  1 
ATOM   267  C  CG  . ASP A 1 38  ? -2.28321  71.66595 34.91035  1.000 37.15700  ? 241  ASP A CG  1 
ATOM   268  O  OD1 . ASP A 1 38  ? -2.19264  71.56653 36.15444  1.000 35.62127  ? 241  ASP A OD1 1 
ATOM   269  O  OD2 . ASP A 1 38  ? -1.32320  72.00386 34.19034  1.000 40.96241  ? 241  ASP A OD2 1 
ATOM   270  N  N   . GLY A 1 39  ? -6.64634  69.29131 34.77601  1.000 29.86049  ? 242  GLY A N   1 
ATOM   271  C  CA  . GLY A 1 39  ? -8.04709  69.23754 34.39574  1.000 27.90061  ? 242  GLY A CA  1 
ATOM   272  C  C   . GLY A 1 39  ? -8.31248  68.16817 33.35812  1.000 27.34366  ? 242  GLY A C   1 
ATOM   273  O  O   . GLY A 1 39  ? -7.49978  67.26920 33.13021  1.000 29.80413  ? 242  GLY A O   1 
ATOM   274  N  N   . LYS A 1 40  ? -9.47819  68.27247 32.71774  1.000 29.56989  ? 243  LYS A N   1 
ATOM   275  C  CA  . LYS A 1 40  ? -9.95840  67.26422 31.76426  1.000 27.51305  ? 243  LYS A CA  1 
ATOM   276  C  C   . LYS A 1 40  ? -10.02545 67.89697 30.37856  1.000 31.02457  ? 243  LYS A C   1 
ATOM   277  O  O   . LYS A 1 40  ? -10.94971 68.65791 30.06832  1.000 32.55848  ? 243  LYS A O   1 
ATOM   278  C  CB  . LYS A 1 40  ? -11.31416 66.70818 32.19611  1.000 31.91473  ? 243  LYS A CB  1 
ATOM   279  C  CG  . LYS A 1 40  ? -11.27980 65.88058 33.48212  1.000 27.62720  ? 243  LYS A CG  1 
ATOM   280  C  CD  . LYS A 1 40  ? -10.42793 64.62469 33.30219  1.000 26.68033  ? 243  LYS A CD  1 
ATOM   281  C  CE  . LYS A 1 40  ? -10.50399 63.68812 34.52291  1.000 28.12386  ? 243  LYS A CE  1 
ATOM   282  N  NZ  . LYS A 1 40  ? -9.60727  62.49318 34.35679  1.000 24.88230  ? 243  LYS A NZ  1 
ATOM   283  N  N   . LEU A 1 41  ? -9.03599  67.58453 29.55441  1.000 27.13081  ? 244  LEU A N   1 
ATOM   284  C  CA  . LEU A 1 41  ? -9.02240  68.07852 28.18272  1.000 30.92307  ? 244  LEU A CA  1 
ATOM   285  C  C   . LEU A 1 41  ? -10.18674 67.49554 27.38771  1.000 30.71876  ? 244  LEU A C   1 
ATOM   286  O  O   . LEU A 1 41  ? -10.51470 66.31374 27.51314  1.000 32.23237  ? 244  LEU A O   1 
ATOM   287  C  CB  . LEU A 1 41  ? -7.69751  67.71584 27.51534  1.000 28.06251  ? 244  LEU A CB  1 
ATOM   288  C  CG  . LEU A 1 41  ? -7.51509  68.08697 26.04250  1.000 33.38731  ? 244  LEU A CG  1 
ATOM   289  C  CD1 . LEU A 1 41  ? -7.51064  69.59777 25.90288  1.000 35.25023  ? 244  LEU A CD1 1 
ATOM   290  C  CD2 . LEU A 1 41  ? -6.21081  67.48479 25.57136  1.000 32.08746  ? 244  LEU A CD2 1 
ATOM   291  N  N   . ASP A 1 42  ? -10.81496 68.33428 26.55602  1.000 30.56603  ? 245  ASP A N   1 
ATOM   292  C  CA  . ASP A 1 42  ? -11.88096 67.87343 25.66456  1.000 32.87411  ? 245  ASP A CA  1 
ATOM   293  C  C   . ASP A 1 42  ? -11.23697 67.30489 24.40160  1.000 35.68541  ? 245  ASP A C   1 
ATOM   294  O  O   . ASP A 1 42  ? -10.93318 68.03054 23.45330  1.000 38.07664  ? 245  ASP A O   1 
ATOM   295  C  CB  . ASP A 1 42  ? -12.84208 69.01263 25.34090  1.000 34.86719  ? 245  ASP A CB  1 
ATOM   296  C  CG  . ASP A 1 42  ? -14.09312 68.53969 24.63297  1.000 40.27688  ? 245  ASP A CG  1 
ATOM   297  O  OD1 . ASP A 1 42  ? -14.32742 67.31781 24.56412  1.000 46.14319  ? 245  ASP A OD1 1 
ATOM   298  O  OD2 . ASP A 1 42  ? -14.84743 69.39947 24.13385  1.000 47.79868  ? 245  ASP A OD2 1 
ATOM   299  N  N   . TYR A 1 43  ? -11.01076 65.99061 24.39151  1.000 33.93909  ? 246  TYR A N   1 
ATOM   300  C  CA  . TYR A 1 43  ? -10.39847 65.29786 23.26092  1.000 33.82479  ? 246  TYR A CA  1 
ATOM   301  C  C   . TYR A 1 43  ? -11.24644 64.10033 22.85709  1.000 36.75533  ? 246  TYR A C   1 
ATOM   302  O  O   . TYR A 1 43  ? -12.14027 63.65959 23.58686  1.000 34.34027  ? 246  TYR A O   1 
ATOM   303  C  CB  . TYR A 1 43  ? -8.97440  64.82024 23.58726  1.000 32.69197  ? 246  TYR A CB  1 
ATOM   304  C  CG  . TYR A 1 43  ? -8.92573  63.73027 24.63307  1.000 27.97566  ? 246  TYR A CG  1 
ATOM   305  C  CD1 . TYR A 1 43  ? -8.88195  64.04059 25.98529  1.000 30.10175  ? 246  TYR A CD1 1 
ATOM   306  C  CD2 . TYR A 1 43  ? -8.94174  62.38866 24.26605  1.000 28.45669  ? 246  TYR A CD2 1 
ATOM   307  C  CE1 . TYR A 1 43  ? -8.85036  63.05156 26.93577  1.000 30.29126  ? 246  TYR A CE1 1 
ATOM   308  C  CE2 . TYR A 1 43  ? -8.91165  61.38634 25.21314  1.000 28.73378  ? 246  TYR A CE2 1 
ATOM   309  C  CZ  . TYR A 1 43  ? -8.85803  61.72825 26.54888  1.000 29.01113  ? 246  TYR A CZ  1 
ATOM   310  O  OH  . TYR A 1 43  ? -8.83690  60.72786 27.49711  1.000 27.63401  ? 246  TYR A OH  1 
ATOM   311  N  N   . GLU A 1 44  ? -10.94075 63.55842 21.67745  1.000 32.44368  ? 247  GLU A N   1 
ATOM   312  C  CA  . GLU A 1 44  ? -11.60969 62.35493 21.20311  1.000 35.40964  ? 247  GLU A CA  1 
ATOM   313  C  C   . GLU A 1 44  ? -10.56840 61.36578 20.68862  1.000 34.67309  ? 247  GLU A C   1 
ATOM   314  O  O   . GLU A 1 44  ? -9.70110  61.73882 19.87963  1.000 35.11912  ? 247  GLU A O   1 
ATOM   315  C  CB  . GLU A 1 44  ? -12.64133 62.68006 20.10776  1.000 43.66756  ? 247  GLU A CB  1 
ATOM   316  C  CG  . GLU A 1 44  ? -13.59545 61.51129 19.79291  1.000 51.83998  ? 247  GLU A CG  1 
ATOM   317  C  CD  . GLU A 1 44  ? -14.63650 61.84596 18.72614  1.000 58.40825  ? 247  GLU A CD  1 
ATOM   318  O  OE1 . GLU A 1 44  ? -14.71779 61.11281 17.72038  1.000 55.88407  ? 247  GLU A OE1 1 
ATOM   319  O  OE2 . GLU A 1 44  ? -15.37800 62.83822 18.89246  1.000 58.95937  ? 247  GLU A OE2 1 
ATOM   320  N  N   . PRO A 1 45  ? -10.60077 60.11841 21.14197  1.000 33.34108  ? 248  PRO A N   1 
ATOM   321  C  CA  . PRO A 1 45  ? -9.65877  59.11817 20.62529  1.000 30.01148  ? 248  PRO A CA  1 
ATOM   322  C  C   . PRO A 1 45  ? -10.13850 58.53293 19.31376  1.000 33.48715  ? 248  PRO A C   1 
ATOM   323  O  O   . PRO A 1 45  ? -11.33968 58.44134 19.05647  1.000 36.60498  ? 248  PRO A O   1 
ATOM   324  C  CB  . PRO A 1 45  ? -9.64688  58.04588 21.72034  1.000 30.46829  ? 248  PRO A CB  1 
ATOM   325  C  CG  . PRO A 1 45  ? -11.02019 58.11940 22.31717  1.000 34.79286  ? 248  PRO A CG  1 
ATOM   326  C  CD  . PRO A 1 45  ? -11.47037 59.57584 22.20303  1.000 34.77246  ? 248  PRO A CD  1 
ATOM   327  N  N   . TYR A 1 46  ? -9.17262  58.11574 18.49090  1.000 30.40439  ? 249  TYR A N   1 
ATOM   328  C  CA  . TYR A 1 46  ? -9.45468  57.56779 17.16581  1.000 30.85982  ? 249  TYR A CA  1 
ATOM   329  C  C   . TYR A 1 46  ? -8.42174  56.51004 16.83475  1.000 32.52264  ? 249  TYR A C   1 
ATOM   330  O  O   . TYR A 1 46  ? -7.24398  56.67454 17.15226  1.000 30.16946  ? 249  TYR A O   1 
ATOM   331  C  CB  . TYR A 1 46  ? -9.38772  58.61589 16.04652  1.000 32.09016  ? 249  TYR A CB  1 
ATOM   332  C  CG  . TYR A 1 46  ? -10.45353 59.68164 16.04559  1.000 42.04513  ? 249  TYR A CG  1 
ATOM   333  C  CD1 . TYR A 1 46  ? -11.59483 59.54588 15.26461  1.000 49.14264  ? 249  TYR A CD1 1 
ATOM   334  C  CD2 . TYR A 1 46  ? -10.29942 60.84654 16.78929  1.000 47.50190  ? 249  TYR A CD2 1 
ATOM   335  C  CE1 . TYR A 1 46  ? -12.56965 60.53262 15.24630  1.000 54.22359  ? 249  TYR A CE1 1 
ATOM   336  C  CE2 . TYR A 1 46  ? -11.26952 61.83802 16.77568  1.000 47.42357  ? 249  TYR A CE2 1 
ATOM   337  C  CZ  . TYR A 1 46  ? -12.39541 61.67333 16.00063  1.000 51.38525  ? 249  TYR A CZ  1 
ATOM   338  O  OH  . TYR A 1 46  ? -13.36868 62.64442 15.98178  1.000 62.92002  ? 249  TYR A OH  1 
ATOM   339  N  N   . PHE A 1 47  ? -8.84948  55.46403 16.13579  1.000 31.87628  ? 250  PHE A N   1 
ATOM   340  C  CA  . PHE A 1 47  ? -7.88641  54.58540 15.49961  1.000 31.56303  ? 250  PHE A CA  1 
ATOM   341  C  C   . PHE A 1 47  ? -7.32253  55.24720 14.24762  1.000 31.94849  ? 250  PHE A C   1 
ATOM   342  O  O   . PHE A 1 47  ? -8.00256  56.01962 13.56250  1.000 37.97837  ? 250  PHE A O   1 
ATOM   343  C  CB  . PHE A 1 47  ? -8.52546  53.24223 15.15405  1.000 31.83704  ? 250  PHE A CB  1 
ATOM   344  C  CG  . PHE A 1 47  ? -8.77074  52.38527 16.36475  1.000 31.52901  ? 250  PHE A CG  1 
ATOM   345  C  CD1 . PHE A 1 47  ? -7.70740  51.81321 17.04651  1.000 29.84641  ? 250  PHE A CD1 1 
ATOM   346  C  CD2 . PHE A 1 47  ? -10.05725 52.18129 16.83932  1.000 32.30496  ? 250  PHE A CD2 1 
ATOM   347  C  CE1 . PHE A 1 47  ? -7.92326  51.03348 18.18736  1.000 31.56700  ? 250  PHE A CE1 1 
ATOM   348  C  CE2 . PHE A 1 47  ? -10.28321 51.41772 17.97442  1.000 29.68336  ? 250  PHE A CE2 1 
ATOM   349  C  CZ  . PHE A 1 47  ? -9.21578  50.84066 18.64836  1.000 31.41781  ? 250  PHE A CZ  1 
ATOM   350  N  N   . THR A 1 48  ? -6.05452  54.94693 13.95535  1.000 36.24312  ? 251  THR A N   1 
ATOM   351  C  CA  . THR A 1 48  ? -5.43169  55.53074 12.77342  1.000 34.65655  ? 251  THR A CA  1 
ATOM   352  C  C   . THR A 1 48  ? -5.90885  54.88061 11.48556  1.000 38.83369  ? 251  THR A C   1 
ATOM   353  O  O   . THR A 1 48  ? -5.73675  55.46828 10.40822  1.000 39.82718  ? 251  THR A O   1 
ATOM   354  C  CB  . THR A 1 48  ? -3.90859  55.42967 12.85565  1.000 35.25633  ? 251  THR A CB  1 
ATOM   355  O  OG1 . THR A 1 48  ? -3.51797  54.05624 12.88497  1.000 36.37363  ? 251  THR A OG1 1 
ATOM   356  C  CG2 . THR A 1 48  ? -3.38907  56.13028 14.11328  1.000 35.73431  ? 251  THR A CG2 1 
ATOM   357  N  N   . SER A 1 49  ? -6.51627  53.70157 11.57419  1.000 38.11547  ? 252  SER A N   1 
ATOM   358  C  CA  . SER A 1 49  ? -7.01751  52.97433 10.42034  1.000 40.94369  ? 252  SER A CA  1 
ATOM   359  C  C   . SER A 1 49  ? -8.52839  52.81815 10.51424  1.000 44.35868  ? 252  SER A C   1 
ATOM   360  O  O   . SER A 1 49  ? -9.07422  52.58915 11.59879  1.000 50.43064  ? 252  SER A O   1 
ATOM   361  C  CB  . SER A 1 49  ? -6.36342  51.59817 10.32259  1.000 45.99311  ? 252  SER A CB  1 
ATOM   362  O  OG  . SER A 1 49  ? -6.88531  50.87159 9.22232   1.000 58.11442  ? 252  SER A OG  1 
ATOM   363  N  N   . SER A 1 50  ? -9.19743  52.94183 9.36617   1.000 59.82637  ? 253  SER A N   1 
ATOM   364  C  CA  . SER A 1 50  ? -10.60443 52.58687 9.23759   1.000 62.29740  ? 253  SER A CA  1 
ATOM   365  C  C   . SER A 1 50  ? -10.80462 51.15513 8.75238   1.000 63.59785  ? 253  SER A C   1 
ATOM   366  O  O   . SER A 1 50  ? -11.94966 50.69205 8.68773   1.000 64.71524  ? 253  SER A O   1 
ATOM   367  C  CB  . SER A 1 50  ? -11.31340 53.55682 8.28378   1.000 71.17498  ? 253  SER A CB  1 
ATOM   368  N  N   . THR A 1 51  ? -9.72753  50.45466 8.40251   1.000 65.25984  ? 254  THR A N   1 
ATOM   369  C  CA  . THR A 1 51  ? -9.77580  49.03870 8.03362   1.000 60.48552  ? 254  THR A CA  1 
ATOM   370  C  C   . THR A 1 51  ? -9.19314  48.22049 9.18079   1.000 56.58777  ? 254  THR A C   1 
ATOM   371  O  O   . THR A 1 51  ? -8.08375  47.68279 9.11247   1.000 50.62992  ? 254  THR A O   1 
ATOM   372  C  CB  . THR A 1 51  ? -9.01928  48.78256 6.73343   1.000 62.23252  ? 254  THR A CB  1 
ATOM   373  O  OG1 . THR A 1 51  ? -7.61613  48.70283 7.01033   1.000 60.19509  ? 254  THR A OG1 1 
ATOM   374  C  CG2 . THR A 1 51  ? -9.26520  49.90425 5.75201   1.000 51.92232  ? 254  THR A CG2 1 
ATOM   375  N  N   . LEU A 1 52  ? -9.95930  48.15276 10.26390  1.000 46.03300  ? 255  LEU A N   1 
ATOM   376  C  CA  . LEU A 1 52  ? -9.64896  47.32553 11.42132  1.000 38.69243  ? 255  LEU A CA  1 
ATOM   377  C  C   . LEU A 1 52  ? -10.86789 46.43147 11.60540  1.000 42.63421  ? 255  LEU A C   1 
ATOM   378  O  O   . LEU A 1 52  ? -11.74486 46.71937 12.43439  1.000 44.79558  ? 255  LEU A O   1 
ATOM   379  C  CB  . LEU A 1 52  ? -9.35836  48.18043 12.65458  1.000 38.50815  ? 255  LEU A CB  1 
ATOM   380  N  N   . PRO A 1 53  ? -10.98564 45.36105 10.81186  1.000 37.14208  ? 256  PRO A N   1 
ATOM   381  C  CA  . PRO A 1 53  ? -12.17082 44.50395 10.93086  1.000 33.32447  ? 256  PRO A CA  1 
ATOM   382  C  C   . PRO A 1 53  ? -12.26184 43.79335 12.27035  1.000 38.73567  ? 256  PRO A C   1 
ATOM   383  O  O   . PRO A 1 53  ? -13.35712 43.35848 12.64610  1.000 40.13631  ? 256  PRO A O   1 
ATOM   384  C  CB  . PRO A 1 53  ? -12.00264 43.50487 9.77508   1.000 36.01361  ? 256  PRO A CB  1 
ATOM   385  C  CG  . PRO A 1 53  ? -10.52132 43.44366 9.53980   1.000 42.02074  ? 256  PRO A CG  1 
ATOM   386  C  CD  . PRO A 1 53  ? -10.01246 44.84188 9.83384   1.000 43.49424  ? 256  PRO A CD  1 
ATOM   387  N  N   . TRP A 1 54  ? -11.15900 43.66828 13.00437  1.000 35.75334  ? 257  TRP A N   1 
ATOM   388  C  CA  . TRP A 1 54  ? -11.15115 42.92107 14.25501  1.000 31.24272  ? 257  TRP A CA  1 
ATOM   389  C  C   . TRP A 1 54  ? -11.40666 43.80804 15.46349  1.000 34.17416  ? 257  TRP A C   1 
ATOM   390  O  O   . TRP A 1 54  ? -11.33749 43.33221 16.60423  1.000 30.95062  ? 257  TRP A O   1 
ATOM   391  C  CB  . TRP A 1 54  ? -9.83102  42.15490 14.41725  1.000 27.75835  ? 257  TRP A CB  1 
ATOM   392  C  CG  . TRP A 1 54  ? -8.56412  42.96243 14.28734  1.000 29.79517  ? 257  TRP A CG  1 
ATOM   393  C  CD1 . TRP A 1 54  ? -7.90257  43.25950 13.13857  1.000 30.99911  ? 257  TRP A CD1 1 
ATOM   394  C  CD2 . TRP A 1 54  ? -7.79546  43.54233 15.35207  1.000 29.77174  ? 257  TRP A CD2 1 
ATOM   395  N  NE1 . TRP A 1 54  ? -6.76951  43.98528 13.41195  1.000 28.60220  ? 257  TRP A NE1 1 
ATOM   396  C  CE2 . TRP A 1 54  ? -6.68570  44.18715 14.76377  1.000 30.79001  ? 257  TRP A CE2 1 
ATOM   397  C  CE3 . TRP A 1 54  ? -7.93933  43.57824 16.74020  1.000 28.20104  ? 257  TRP A CE3 1 
ATOM   398  C  CZ2 . TRP A 1 54  ? -5.71648  44.85859 15.51997  1.000 30.15514  ? 257  TRP A CZ2 1 
ATOM   399  C  CZ3 . TRP A 1 54  ? -6.97909  44.24675 17.49359  1.000 27.49100  ? 257  TRP A CZ3 1 
ATOM   400  C  CH2 . TRP A 1 54  ? -5.88632  44.88206 16.88138  1.000 29.09597  ? 257  TRP A CH2 1 
ATOM   401  N  N   . ILE A 1 55  ? -11.71338 45.07708 15.23722  1.000 29.36142  ? 258  ILE A N   1 
ATOM   402  C  CA  . ILE A 1 55  ? -12.11479 45.99709 16.29370  1.000 31.23125  ? 258  ILE A CA  1 
ATOM   403  C  C   . ILE A 1 55  ? -13.50668 46.50127 15.95175  1.000 37.49289  ? 258  ILE A C   1 
ATOM   404  O  O   . ILE A 1 55  ? -13.77543 46.85170 14.79788  1.000 38.21519  ? 258  ILE A O   1 
ATOM   405  C  CB  . ILE A 1 55  ? -11.11568 47.15653 16.44187  1.000 35.35157  ? 258  ILE A CB  1 
ATOM   406  C  CG1 . ILE A 1 55  ? -9.78925  46.62622 16.98373  1.000 33.25398  ? 258  ILE A CG1 1 
ATOM   407  C  CG2 . ILE A 1 55  ? -11.67608 48.23058 17.36617  1.000 39.10648  ? 258  ILE A CG2 1 
ATOM   408  C  CD1 . ILE A 1 55  ? -8.73617  47.68099 17.19212  1.000 41.29761  ? 258  ILE A CD1 1 
ATOM   409  N  N   . THR A 1 56  ? -14.39313 46.53224 16.94710  1.000 34.92458  ? 259  THR A N   1 
ATOM   410  C  CA  . THR A 1 56  ? -15.78786 46.91123 16.72821  1.000 36.03999  ? 259  THR A CA  1 
ATOM   411  C  C   . THR A 1 56  ? -15.95065 48.36659 17.14663  1.000 41.29825  ? 259  THR A C   1 
ATOM   412  O  O   . THR A 1 56  ? -16.04952 48.66980 18.33503  1.000 39.79410  ? 259  THR A O   1 
ATOM   413  C  CB  . THR A 1 56  ? -16.72984 46.00208 17.51052  1.000 38.40321  ? 259  THR A CB  1 
ATOM   414  O  OG1 . THR A 1 56  ? -16.46957 44.63761 17.17001  1.000 41.75956  ? 259  THR A OG1 1 
ATOM   415  C  CG2 . THR A 1 56  ? -18.17936 46.33445 17.19351  1.000 48.03619  ? 259  THR A CG2 1 
ATOM   416  N  N   . GLY A 1 57  ? -15.96696 49.26706 16.17578  1.000 42.07702  ? 260  GLY A N   1 
ATOM   417  C  CA  . GLY A 1 57  ? -16.17434 50.66941 16.47713  1.000 39.66713  ? 260  GLY A CA  1 
ATOM   418  C  C   . GLY A 1 57  ? -14.90290 51.41297 16.83417  1.000 40.42917  ? 260  GLY A C   1 
ATOM   419  O  O   . GLY A 1 57  ? -13.77628 50.92777 16.69310  1.000 44.65550  ? 260  GLY A O   1 
ATOM   420  N  N   . ALA A 1 58  ? -15.10644 52.63100 17.30411  1.000 35.39813  ? 261  ALA A N   1 
ATOM   421  C  CA  . ALA A 1 58  ? -14.08049 53.57739 17.71188  1.000 38.57218  ? 261  ALA A CA  1 
ATOM   422  C  C   . ALA A 1 58  ? -13.73187 53.37829 19.18071  1.000 35.28844  ? 261  ALA A C   1 
ATOM   423  O  O   . ALA A 1 58  ? -14.51185 52.79053 19.92759  1.000 33.42221  ? 261  ALA A O   1 
ATOM   424  C  CB  . ALA A 1 58  ? -14.58303 55.00316 17.48408  1.000 39.86655  ? 261  ALA A CB  1 
ATOM   425  N  N   . PRO A 1 59  ? -12.58088 53.86350 19.64416  1.000 32.00197  ? 262  PRO A N   1 
ATOM   426  C  CA  . PRO A 1 59  ? -12.34210 53.87194 21.08799  1.000 29.14126  ? 262  PRO A CA  1 
ATOM   427  C  C   . PRO A 1 59  ? -13.19110 54.95410 21.72447  1.000 33.49565  ? 262  PRO A C   1 
ATOM   428  O  O   . PRO A 1 59  ? -13.61626 55.91412 21.07555  1.000 34.12447  ? 262  PRO A O   1 
ATOM   429  C  CB  . PRO A 1 59  ? -10.84522 54.18265 21.21734  1.000 30.77927  ? 262  PRO A CB  1 
ATOM   430  C  CG  . PRO A 1 59  ? -10.35393 54.45263 19.76760  1.000 35.40547  ? 262  PRO A CG  1 
ATOM   431  C  CD  . PRO A 1 59  ? -11.56430 54.66462 18.94243  1.000 33.58074  ? 262  PRO A CD  1 
ATOM   432  N  N   . THR A 1 60  ? -13.45985 54.78583 23.01017  1.000 30.07228  ? 263  THR A N   1 
ATOM   433  C  CA  . THR A 1 60  ? -14.22679 55.78075 23.73742  1.000 29.16463  ? 263  THR A CA  1 
ATOM   434  C  C   . THR A 1 60  ? -13.55726 56.07205 25.06787  1.000 29.95475  ? 263  THR A C   1 
ATOM   435  O  O   . THR A 1 60  ? -12.78799 55.26619 25.59510  1.000 29.71492  ? 263  THR A O   1 
ATOM   436  C  CB  . THR A 1 60  ? -15.67600 55.34086 23.99172  1.000 34.44926  ? 263  THR A CB  1 
ATOM   437  O  OG1 . THR A 1 60  ? -15.68074 54.08701 24.68293  1.000 40.46283  ? 263  THR A OG1 1 
ATOM   438  C  CG2 . THR A 1 60  ? -16.44944 55.20931 22.67643  1.000 37.68451  ? 263  THR A CG2 1 
ATOM   439  N  N   . ILE A 1 61  ? -13.86462 57.25067 25.60070  1.000 31.64861  ? 264  ILE A N   1 
ATOM   440  C  CA  . ILE A 1 61  ? -13.52616 57.59326 26.97886  1.000 27.47689  ? 264  ILE A CA  1 
ATOM   441  C  C   . ILE A 1 61  ? -14.64359 57.02306 27.84355  1.000 33.15215  ? 264  ILE A C   1 
ATOM   442  O  O   . ILE A 1 61  ? -15.73781 57.58364 27.89608  1.000 33.36962  ? 264  ILE A O   1 
ATOM   443  C  CB  . ILE A 1 61  ? -13.38184 59.10071 27.17862  1.000 25.58088  ? 264  ILE A CB  1 
ATOM   444  C  CG1 . ILE A 1 61  ? -12.41249 59.72121 26.16964  1.000 30.67692  ? 264  ILE A CG1 1 
ATOM   445  C  CG2 . ILE A 1 61  ? -12.93505 59.39908 28.61710  1.000 28.98201  ? 264  ILE A CG2 1 
ATOM   446  C  CD1 . ILE A 1 61  ? -12.33071 61.25012 26.30714  1.000 28.45595  ? 264  ILE A CD1 1 
ATOM   447  N  N   . SER A 1 62  ? -14.38315 55.89916 28.51113  1.000 28.37961  ? 265  SER A N   1 
ATOM   448  C  CA  . SER A 1 62  ? -15.40691 55.23634 29.30780  1.000 30.04923  ? 265  SER A CA  1 
ATOM   449  C  C   . SER A 1 62  ? -15.43879 55.69178 30.76406  1.000 30.74218  ? 265  SER A C   1 
ATOM   450  O  O   . SER A 1 62  ? -16.41604 55.39751 31.45942  1.000 32.09327  ? 265  SER A O   1 
ATOM   451  C  CB  . SER A 1 62  ? -15.22071 53.70995 29.25428  1.000 28.63264  ? 265  SER A CB  1 
ATOM   452  O  OG  . SER A 1 62  ? -13.92142 53.33394 29.68577  1.000 29.86696  ? 265  SER A OG  1 
ATOM   453  N  N   . SER A 1 63  ? -14.41183 56.38923 31.25276  1.000 25.84128  ? 266  SER A N   1 
ATOM   454  C  CA  . SER A 1 63  ? -14.47298 56.94231 32.60197  1.000 26.18794  ? 266  SER A CA  1 
ATOM   455  C  C   . SER A 1 63  ? -13.57717 58.16342 32.72807  1.000 25.83579  ? 266  SER A C   1 
ATOM   456  O  O   . SER A 1 63  ? -12.43153 58.15977 32.26867  1.000 29.43497  ? 266  SER A O   1 
ATOM   457  C  CB  . SER A 1 63  ? -14.06203 55.91432 33.66391  1.000 27.89747  ? 266  SER A CB  1 
ATOM   458  O  OG  . SER A 1 63  ? -14.09303 56.51599 34.95108  1.000 30.71304  ? 266  SER A OG  1 
ATOM   459  N  N   . ARG A 1 64  ? -14.10163 59.20425 33.38504  1.000 26.00720  ? 267  ARG A N   1 
ATOM   460  C  CA  . ARG A 1 64  ? -13.31782 60.38526 33.73744  1.000 28.91728  ? 267  ARG A CA  1 
ATOM   461  C  C   . ARG A 1 64  ? -13.46818 60.71691 35.21563  1.000 27.61704  ? 267  ARG A C   1 
ATOM   462  O  O   . ARG A 1 64  ? -13.13960 61.83252 35.64355  1.000 31.02539  ? 267  ARG A O   1 
ATOM   463  C  CB  . ARG A 1 64  ? -13.72295 61.59361 32.88439  1.000 30.13245  ? 267  ARG A CB  1 
ATOM   464  C  CG  . ARG A 1 64  ? -13.87176 61.28427 31.39383  1.000 26.28240  ? 267  ARG A CG  1 
ATOM   465  C  CD  . ARG A 1 64  ? -13.80247 62.55711 30.57661  1.000 28.42003  ? 267  ARG A CD  1 
ATOM   466  N  NE  . ARG A 1 64  ? -12.43475 63.03560 30.42132  1.000 31.11716  ? 267  ARG A NE  1 
ATOM   467  C  CZ  . ARG A 1 64  ? -12.09996 64.06013 29.64477  1.000 35.36274  ? 267  ARG A CZ  1 
ATOM   468  N  NH1 . ARG A 1 64  ? -13.01592 64.76746 29.00109  1.000 34.67214  ? 267  ARG A NH1 1 
ATOM   469  N  NH2 . ARG A 1 64  ? -10.81694 64.38199 29.50954  1.000 31.54437  ? 267  ARG A NH2 1 
ATOM   470  N  N   . THR A 1 65  ? -13.95910 59.76468 36.00346  1.000 29.18085  ? 268  THR A N   1 
ATOM   471  C  CA  . THR A 1 65  ? -14.27444 60.04298 37.40323  1.000 28.51951  ? 268  THR A CA  1 
ATOM   472  C  C   . THR A 1 65  ? -13.02798 60.33549 38.22958  1.000 32.18485  ? 268  THR A C   1 
ATOM   473  O  O   . THR A 1 65  ? -13.09763 61.10186 39.20093  1.000 30.11744  ? 268  THR A O   1 
ATOM   474  C  CB  . THR A 1 65  ? -15.05011 58.85773 37.97748  1.000 28.95030  ? 268  THR A CB  1 
ATOM   475  O  OG1 . THR A 1 65  ? -14.21586 57.69712 37.96079  1.000 40.31030  ? 268  THR A OG1 1 
ATOM   476  C  CG2 . THR A 1 65  ? -16.27882 58.57411 37.12183  1.000 33.25214  ? 268  THR A CG2 1 
ATOM   477  N  N   . ASP A 1 66  ? -11.89576 59.73649 37.88425  1.000 27.90477  ? 269  ASP A N   1 
ATOM   478  C  CA  . ASP A 1 66  ? -10.64189 60.02456 38.57865  1.000 27.66718  ? 269  ASP A CA  1 
ATOM   479  C  C   . ASP A 1 66  ? -10.02640 61.29138 37.99439  1.000 26.07003  ? 269  ASP A C   1 
ATOM   480  O  O   . ASP A 1 66  ? -9.71485  61.31592 36.80086  1.000 25.18141  ? 269  ASP A O   1 
ATOM   481  C  CB  . ASP A 1 66  ? -9.68560  58.84322 38.42270  1.000 29.07598  ? 269  ASP A CB  1 
ATOM   482  C  CG  . ASP A 1 66  ? -8.39349  58.98439 39.23822  1.000 30.73355  ? 269  ASP A CG  1 
ATOM   483  O  OD1 . ASP A 1 66  ? -7.95147  60.10754 39.58382  1.000 28.82119  ? 269  ASP A OD1 1 
ATOM   484  O  OD2 . ASP A 1 66  ? -7.79821  57.92913 39.52058  1.000 32.66489  ? 269  ASP A OD2 1 
ATOM   485  N  N   . PRO A 1 67  ? -9.84760  62.35788 38.77787  1.000 23.85804  ? 270  PRO A N   1 
ATOM   486  C  CA  . PRO A 1 67  ? -9.27838  63.59081 38.20537  1.000 24.06801  ? 270  PRO A CA  1 
ATOM   487  C  C   . PRO A 1 67  ? -7.93812  63.37987 37.52354  1.000 25.32172  ? 270  PRO A C   1 
ATOM   488  O  O   . PRO A 1 67  ? -7.61161  64.12360 36.59163  1.000 26.90936  ? 270  PRO A O   1 
ATOM   489  C  CB  . PRO A 1 67  ? -9.14855  64.51896 39.42729  1.000 25.90123  ? 270  PRO A CB  1 
ATOM   490  C  CG  . PRO A 1 67  ? -10.16002 63.97961 40.39647  1.000 27.58999  ? 270  PRO A CG  1 
ATOM   491  C  CD  . PRO A 1 67  ? -10.12562 62.50219 40.22309  1.000 27.73881  ? 270  PRO A CD  1 
ATOM   492  N  N   . ASN A 1 68  ? -7.16945  62.36285 37.92764  1.000 27.24253  ? 271  ASN A N   1 
ATOM   493  C  CA  . ASN A 1 68  ? -5.82685  62.18853 37.39552  1.000 28.08350  ? 271  ASN A CA  1 
ATOM   494  C  C   . ASN A 1 68  ? -5.74898  61.34192 36.12816  1.000 26.73681  ? 271  ASN A C   1 
ATOM   495  O  O   . ASN A 1 68  ? -4.69014  61.33816 35.49531  1.000 25.35376  ? 271  ASN A O   1 
ATOM   496  C  CB  . ASN A 1 68  ? -4.90577  61.54818 38.43235  1.000 27.39399  ? 271  ASN A CB  1 
ATOM   497  C  CG  . ASN A 1 68  ? -4.70930  62.42197 39.64595  1.000 31.65840  ? 271  ASN A CG  1 
ATOM   498  O  OD1 . ASN A 1 68  ? -4.90498  63.62682 39.58022  1.000 37.06195  ? 271  ASN A OD1 1 
ATOM   499  N  ND2 . ASN A 1 68  ? -4.30387  61.82069 40.74780  1.000 39.65600  ? 271  ASN A ND2 1 
ATOM   500  N  N   A LYS A 1 69  ? -6.80280  60.60839 35.76552  0.735 23.42731  ? 272  LYS A N   1 
ATOM   501  N  N   B LYS A 1 69  ? -6.80806  60.62741 35.74847  0.265 23.70085  ? 272  LYS A N   1 
ATOM   502  C  CA  A LYS A 1 69  ? -6.70966  59.74423 34.59195  0.735 26.20350  ? 272  LYS A CA  1 
ATOM   503  C  CA  B LYS A 1 69  ? -6.69709  59.75094 34.58720  0.265 26.20740  ? 272  LYS A CA  1 
ATOM   504  C  C   A LYS A 1 69  ? -8.07308  59.53336 33.94817  0.735 28.01312  ? 272  LYS A C   1 
ATOM   505  C  C   B LYS A 1 69  ? -8.06073  59.50073 33.95674  0.265 27.88182  ? 272  LYS A C   1 
ATOM   506  O  O   A LYS A 1 69  ? -9.11459  59.58628 34.60621  0.735 27.13454  ? 272  LYS A O   1 
ATOM   507  O  O   B LYS A 1 69  ? -9.08901  59.49965 34.63817  0.265 27.21417  ? 272  LYS A O   1 
ATOM   508  C  CB  A LYS A 1 69  ? -6.08690  58.38637 34.94801  0.735 26.49832  ? 272  LYS A CB  1 
ATOM   509  C  CB  B LYS A 1 69  ? -6.03836  58.41619 34.96233  0.265 26.55789  ? 272  LYS A CB  1 
ATOM   510  C  CG  A LYS A 1 69  ? -6.94488  57.51605 35.86015  0.735 31.02489  ? 272  LYS A CG  1 
ATOM   511  C  CG  B LYS A 1 69  ? -6.64496  57.72206 36.17898  0.265 30.62481  ? 272  LYS A CG  1 
ATOM   512  C  CD  A LYS A 1 69  ? -6.14753  56.33910 36.43027  0.735 31.84984  ? 272  LYS A CD  1 
ATOM   513  C  CD  B LYS A 1 69  ? -5.98208  56.36609 36.41583  0.265 31.91086  ? 272  LYS A CD  1 
ATOM   514  C  CE  A LYS A 1 69  ? -6.99343  55.49078 37.38067  0.735 39.45669  ? 272  LYS A CE  1 
ATOM   515  C  CE  B LYS A 1 69  ? -6.34447  55.76733 37.77231  0.265 35.83018  ? 272  LYS A CE  1 
ATOM   516  N  NZ  A LYS A 1 69  ? -6.23686  54.33204 37.94085  0.735 32.20841  ? 272  LYS A NZ  1 
ATOM   517  N  NZ  B LYS A 1 69  ? -7.80499  55.49907 37.93572  0.265 37.07416  ? 272  LYS A NZ  1 
ATOM   518  N  N   . ASP A 1 70  ? -8.04821  59.28292 32.64057  1.000 22.55587  ? 273  ASP A N   1 
ATOM   519  C  CA  . ASP A 1 70  ? -9.20855  58.81762 31.90524  1.000 24.01934  ? 273  ASP A CA  1 
ATOM   520  C  C   . ASP A 1 70  ? -9.00335  57.34022 31.59185  1.000 27.00845  ? 273  ASP A C   1 
ATOM   521  O  O   . ASP A 1 70  ? -7.87099  56.87935 31.44232  1.000 28.45808  ? 273  ASP A O   1 
ATOM   522  C  CB  . ASP A 1 70  ? -9.38920  59.57319 30.57583  1.000 22.22679  ? 273  ASP A CB  1 
ATOM   523  C  CG  . ASP A 1 70  ? -9.83860  61.00700 30.75138  1.000 28.59464  ? 273  ASP A CG  1 
ATOM   524  O  OD1 . ASP A 1 70  ? -10.44277 61.34165 31.77966  1.000 26.36693  ? 273  ASP A OD1 1 
ATOM   525  O  OD2 . ASP A 1 70  ? -9.60558  61.81246 29.81994  1.000 30.37284  ? 273  ASP A OD2 1 
ATOM   526  N  N   . VAL A 1 71  ? -10.09806 56.59976 31.49686  1.000 21.67023  ? 274  VAL A N   1 
ATOM   527  C  CA  . VAL A 1 71  ? -10.06121 55.23170 30.99095  1.000 22.49022  ? 274  VAL A CA  1 
ATOM   528  C  C   . VAL A 1 71  ? -10.54707 55.25289 29.55037  1.000 25.25956  ? 274  VAL A C   1 
ATOM   529  O  O   . VAL A 1 71  ? -11.60573 55.82314 29.25443  1.000 25.96659  ? 274  VAL A O   1 
ATOM   530  C  CB  . VAL A 1 71  ? -10.91579 54.28892 31.84932  1.000 25.32905  ? 274  VAL A CB  1 
ATOM   531  C  CG1 . VAL A 1 71  ? -10.81842 52.84971 31.33698  1.000 27.49689  ? 274  VAL A CG1 1 
ATOM   532  C  CG2 . VAL A 1 71  ? -10.47965 54.36567 33.31043  1.000 23.91287  ? 274  VAL A CG2 1 
ATOM   533  N  N   . ILE A 1 72  ? -9.76274  54.66046 28.64788  1.000 23.13963  ? 275  ILE A N   1 
ATOM   534  C  CA  . ILE A 1 72  ? -10.13668 54.49996 27.24208  1.000 26.19168  ? 275  ILE A CA  1 
ATOM   535  C  C   . ILE A 1 72  ? -10.52198 53.04240 27.02053  1.000 26.79641  ? 275  ILE A C   1 
ATOM   536  O  O   . ILE A 1 72  ? -9.78470  52.14242 27.43387  1.000 27.02765  ? 275  ILE A O   1 
ATOM   537  C  CB  . ILE A 1 72  ? -8.97961  54.88731 26.30347  1.000 24.99221  ? 275  ILE A CB  1 
ATOM   538  C  CG1 . ILE A 1 72  ? -8.46018  56.29613 26.60120  1.000 29.59894  ? 275  ILE A CG1 1 
ATOM   539  C  CG2 . ILE A 1 72  ? -9.41498  54.74821 24.84039  1.000 27.85858  ? 275  ILE A CG2 1 
ATOM   540  C  CD1 . ILE A 1 72  ? -9.52338  57.36489 26.47546  1.000 30.54188  ? 275  ILE A CD1 1 
ATOM   541  N  N   . SER A 1 73  ? -11.66685 52.80647 26.37206  1.000 26.07673  ? 276  SER A N   1 
ATOM   542  C  CA  . SER A 1 73  ? -12.15657 51.46474 26.06924  1.000 25.34480  ? 276  SER A CA  1 
ATOM   543  C  C   . SER A 1 73  ? -12.18606 51.21870 24.56482  1.000 26.89104  ? 276  SER A C   1 
ATOM   544  O  O   . SER A 1 73  ? -12.46408 52.12611 23.77420  1.000 28.40638  ? 276  SER A O   1 
ATOM   545  C  CB  . SER A 1 73  ? -13.56887 51.24444 26.61788  1.000 26.23857  ? 276  SER A CB  1 
ATOM   546  O  OG  . SER A 1 73  ? -13.57515 51.23481 28.03689  1.000 26.85149  ? 276  SER A OG  1 
ATOM   547  N  N   . PHE A 1 74  ? -11.93239 49.97204 24.17806  1.000 24.60644  ? 277  PHE A N   1 
ATOM   548  C  CA  . PHE A 1 74  ? -12.09371 49.57297 22.78822  1.000 26.53585  ? 277  PHE A CA  1 
ATOM   549  C  C   . PHE A 1 74  ? -12.42652 48.09082 22.77672  1.000 26.41016  ? 277  PHE A C   1 
ATOM   550  O  O   . PHE A 1 74  ? -12.05955 47.35456 23.69755  1.000 27.64996  ? 277  PHE A O   1 
ATOM   551  C  CB  . PHE A 1 74  ? -10.84171 49.88604 21.94833  1.000 28.01616  ? 277  PHE A CB  1 
ATOM   552  C  CG  . PHE A 1 74  ? -9.60971  49.17287 22.41073  1.000 25.45464  ? 277  PHE A CG  1 
ATOM   553  C  CD1 . PHE A 1 74  ? -8.88247  49.64261 23.49311  1.000 31.56639  ? 277  PHE A CD1 1 
ATOM   554  C  CD2 . PHE A 1 74  ? -9.17938  48.01993 21.76620  1.000 26.08498  ? 277  PHE A CD2 1 
ATOM   555  C  CE1 . PHE A 1 74  ? -7.75088  48.97486 23.93728  1.000 30.45113  ? 277  PHE A CE1 1 
ATOM   556  C  CE2 . PHE A 1 74  ? -8.04245  47.34072 22.20581  1.000 27.24024  ? 277  PHE A CE2 1 
ATOM   557  C  CZ  . PHE A 1 74  ? -7.33220  47.81019 23.29374  1.000 29.07028  ? 277  PHE A CZ  1 
ATOM   558  N  N   . THR A 1 75  ? -13.13141 47.65201 21.73011  1.000 28.04454  ? 278  THR A N   1 
ATOM   559  C  CA  . THR A 1 75  ? -13.68935 46.30204 21.70141  1.000 25.66486  ? 278  THR A CA  1 
ATOM   560  C  C   . THR A 1 75  ? -13.05168 45.48319 20.58378  1.000 28.66169  ? 278  THR A C   1 
ATOM   561  O  O   . THR A 1 75  ? -13.12880 45.86169 19.41046  1.000 32.16319  ? 278  THR A O   1 
ATOM   562  C  CB  . THR A 1 75  ? -15.21097 46.35575 21.54246  1.000 30.05447  ? 278  THR A CB  1 
ATOM   563  O  OG1 . THR A 1 75  ? -15.77088 47.09396 22.64313  1.000 31.11841  ? 278  THR A OG1 1 
ATOM   564  C  CG2 . THR A 1 75  ? -15.80071 44.94470 21.52943  1.000 32.06873  ? 278  THR A CG2 1 
ATOM   565  N  N   . CYS A 1 76  ? -12.44690 44.35319 20.95338  1.000 27.16185  ? 279  CYS A N   1 
ATOM   566  C  CA  . CYS A 1 76  ? -11.78671 43.43485 20.02774  1.000 26.71104  ? 279  CYS A CA  1 
ATOM   567  C  C   . CYS A 1 76  ? -12.62174 42.17862 19.79996  1.000 29.30924  ? 279  CYS A C   1 
ATOM   568  O  O   . CYS A 1 76  ? -13.21580 41.63270 20.73823  1.000 28.98749  ? 279  CYS A O   1 
ATOM   569  C  CB  . CYS A 1 76  ? -10.42258 43.00537 20.57527  1.000 28.71635  ? 279  CYS A CB  1 
ATOM   570  S  SG  . CYS A 1 76  ? -9.18945  44.28506 20.78032  1.000 29.88552  ? 279  CYS A SG  1 
ATOM   571  N  N   . LEU A 1 77  ? -12.64975 41.70785 18.55165  1.000 29.39365  ? 280  LEU A N   1 
ATOM   572  C  CA  . LEU A 1 77  ? -13.05850 40.33908 18.28908  1.000 31.94861  ? 280  LEU A CA  1 
ATOM   573  C  C   . LEU A 1 77  ? -11.99462 39.37678 18.81754  1.000 29.11933  ? 280  LEU A C   1 
ATOM   574  O  O   . LEU A 1 77  ? -10.86531 39.76291 19.12444  1.000 27.94984  ? 280  LEU A O   1 
ATOM   575  C  CB  . LEU A 1 77  ? -13.26188 40.10814 16.78888  1.000 32.24938  ? 280  LEU A CB  1 
ATOM   576  C  CG  . LEU A 1 77  ? -14.30219 40.99388 16.11259  1.000 35.84603  ? 280  LEU A CG  1 
ATOM   577  C  CD1 . LEU A 1 77  ? -14.41279 40.67130 14.61727  1.000 30.02025  ? 280  LEU A CD1 1 
ATOM   578  C  CD2 . LEU A 1 77  ? -15.64675 40.84855 16.80355  1.000 37.77337  ? 280  LEU A CD2 1 
ATOM   579  N  N   . LYS A 1 78  ? -12.35399 38.10168 18.90603  1.000 31.19136  ? 281  LYS A N   1 
ATOM   580  C  CA  . LYS A 1 78  ? -11.36147 37.09915 19.26805  1.000 31.91406  ? 281  LYS A CA  1 
ATOM   581  C  C   . LYS A 1 78  ? -10.26591 37.05701 18.21394  1.000 30.27490  ? 281  LYS A C   1 
ATOM   582  O  O   . LYS A 1 78  ? -10.54528 37.07687 17.01071  1.000 30.03773  ? 281  LYS A O   1 
ATOM   583  C  CB  . LYS A 1 78  ? -12.01305 35.72139 19.40371  1.000 33.88961  ? 281  LYS A CB  1 
ATOM   584  C  CG  . LYS A 1 78  ? -11.01327 34.60539 19.71493  1.000 35.06019  ? 281  LYS A CG  1 
ATOM   585  C  CD  . LYS A 1 78  ? -11.67723 33.24585 19.86198  1.000 33.99952  ? 281  LYS A CD  1 
ATOM   586  C  CE  . LYS A 1 78  ? -10.61973 32.16746 20.06890  1.000 38.70305  ? 281  LYS A CE  1 
ATOM   587  N  NZ  . LYS A 1 78  ? -11.24265 30.82318 20.11650  1.000 39.94093  ? 281  LYS A NZ  1 
ATOM   588  N  N   . ASN A 1 79  ? -9.01152  37.01103 18.65590  1.000 28.21026  ? 282  ASN A N   1 
ATOM   589  C  CA  . ASN A 1 79  ? -7.90939  36.76909 17.72493  1.000 28.18258  ? 282  ASN A CA  1 
ATOM   590  C  C   . ASN A 1 79  ? -7.77058  35.25691 17.58258  1.000 29.43546  ? 282  ASN A C   1 
ATOM   591  O  O   . ASN A 1 79  ? -7.24140  34.57705 18.46760  1.000 29.63170  ? 282  ASN A O   1 
ATOM   592  C  CB  . ASN A 1 79  ? -6.61319  37.41924 18.19006  1.000 26.50659  ? 282  ASN A CB  1 
ATOM   593  C  CG  . ASN A 1 79  ? -5.49244  37.32470 17.14420  1.000 27.14399  ? 282  ASN A CG  1 
ATOM   594  O  OD1 . ASN A 1 79  ? -5.69793  36.83519 16.02028  1.000 28.01407  ? 282  ASN A OD1 1 
ATOM   595  N  ND2 . ASN A 1 79  ? -4.30591  37.80439 17.50759  1.000 25.06344  ? 282  ASN A ND2 1 
ATOM   596  N  N   . LYS A 1 80  ? -8.27802  34.73035 16.47071  1.000 29.46642  ? 283  LYS A N   1 
ATOM   597  C  CA  . LYS A 1 80  ? -8.17181  33.30597 16.17888  1.000 32.38767  ? 283  LYS A CA  1 
ATOM   598  C  C   . LYS A 1 80  ? -6.82230  32.92715 15.57730  1.000 29.24248  ? 283  LYS A C   1 
ATOM   599  O  O   . LYS A 1 80  ? -6.45596  31.74652 15.60883  1.000 30.37212  ? 283  LYS A O   1 
ATOM   600  C  CB  . LYS A 1 80  ? -9.29323  32.88223 15.22488  1.000 31.02391  ? 283  LYS A CB  1 
ATOM   601  C  CG  . LYS A 1 80  ? -10.68836 33.22012 15.70819  1.000 30.79421  ? 283  LYS A CG  1 
ATOM   602  C  CD  . LYS A 1 80  ? -11.75555 32.67469 14.77635  1.000 37.16542  ? 283  LYS A CD  1 
ATOM   603  C  CE  . LYS A 1 80  ? -13.14381 32.98520 15.30733  1.000 36.78274  ? 283  LYS A CE  1 
ATOM   604  N  NZ  . LYS A 1 80  ? -14.20190 32.47927 14.39507  1.000 42.12480  ? 283  LYS A NZ  1 
ATOM   605  N  N   . THR A 1 81  ? -6.07773  33.89624 15.05145  1.000 29.51547  ? 284  THR A N   1 
ATOM   606  C  CA  . THR A 1 81  ? -4.81310  33.66519 14.37121  1.000 25.07819  ? 284  THR A CA  1 
ATOM   607  C  C   . THR A 1 81  ? -3.68619  33.42821 15.37118  1.000 29.63628  ? 284  THR A C   1 
ATOM   608  O  O   . THR A 1 81  ? -3.78507  33.75815 16.55615  1.000 29.89820  ? 284  THR A O   1 
ATOM   609  C  CB  . THR A 1 81  ? -4.44300  34.85429 13.49117  1.000 27.04768  ? 284  THR A CB  1 
ATOM   610  O  OG1 . THR A 1 81  ? -3.77470  35.83382 14.29921  1.000 28.09540  ? 284  THR A OG1 1 
ATOM   611  C  CG2 . THR A 1 81  ? -5.68715  35.46009 12.85592  1.000 29.77241  ? 284  THR A CG2 1 
ATOM   612  N  N   . VAL A 1 82  ? -2.59345  32.85012 14.88214  1.000 25.87056  ? 285  VAL A N   1 
ATOM   613  C  CA  . VAL A 1 82  ? -1.43056  32.62496 15.71886  1.000 23.69456  ? 285  VAL A CA  1 
ATOM   614  C  C   . VAL A 1 82  ? -0.45688  33.79727 15.63113  1.000 26.95375  ? 285  VAL A C   1 
ATOM   615  O  O   . VAL A 1 82  ? 0.72649   33.64637 15.92532  1.000 29.03500  ? 285  VAL A O   1 
ATOM   616  C  CB  . VAL A 1 82  ? -0.73529  31.29539 15.38764  1.000 30.35233  ? 285  VAL A CB  1 
ATOM   617  C  CG1 . VAL A 1 82  ? -1.69237  30.13645 15.60963  1.000 30.43203  ? 285  VAL A CG1 1 
ATOM   618  C  CG2 . VAL A 1 82  ? -0.21114  31.29878 13.96061  1.000 29.65151  ? 285  VAL A CG2 1 
ATOM   619  N  N   . TRP A 1 83  ? -0.94256  34.97647 15.24576  1.000 26.86415  ? 286  TRP A N   1 
ATOM   620  C  CA  . TRP A 1 83  ? -0.10616  36.16115 15.13555  1.000 28.13729  ? 286  TRP A CA  1 
ATOM   621  C  C   . TRP A 1 83  ? -0.66841  37.27814 16.00577  1.000 25.47860  ? 286  TRP A C   1 
ATOM   622  O  O   . TRP A 1 83  ? -1.88767  37.46332 16.07523  1.000 31.62366  ? 286  TRP A O   1 
ATOM   623  C  CB  . TRP A 1 83  ? -0.02693  36.64855 13.69265  1.000 28.89212  ? 286  TRP A CB  1 
ATOM   624  C  CG  . TRP A 1 83  ? 0.44019   35.60614 12.69769  1.000 29.16085  ? 286  TRP A CG  1 
ATOM   625  C  CD1 . TRP A 1 83  ? 1.57884   34.85211 12.77252  1.000 30.99868  ? 286  TRP A CD1 1 
ATOM   626  C  CD2 . TRP A 1 83  ? -0.19575  35.25268 11.45886  1.000 29.93327  ? 286  TRP A CD2 1 
ATOM   627  N  NE1 . TRP A 1 83  ? 1.67691   34.02998 11.66088  1.000 30.28877  ? 286  TRP A NE1 1 
ATOM   628  C  CE2 . TRP A 1 83  ? 0.60227   34.26341 10.84396  1.000 29.28420  ? 286  TRP A CE2 1 
ATOM   629  C  CE3 . TRP A 1 83  ? -1.37026  35.66521 10.81726  1.000 30.08296  ? 286  TRP A CE3 1 
ATOM   630  C  CZ2 . TRP A 1 83  ? 0.26310   33.68584 9.61662   1.000 30.91950  ? 286  TRP A CZ2 1 
ATOM   631  C  CZ3 . TRP A 1 83  ? -1.70005  35.09973 9.59495   1.000 30.21178  ? 286  TRP A CZ3 1 
ATOM   632  C  CH2 . TRP A 1 83  ? -0.88808  34.10985 9.01300   1.000 30.80494  ? 286  TRP A CH2 1 
ATOM   633  N  N   . ASN A 1 84  ? 0.22848   38.03873 16.62595  1.000 27.11721  ? 287  ASN A N   1 
ATOM   634  C  CA  . ASN A 1 84  ? -0.14960  39.34143 17.16776  1.000 28.27861  ? 287  ASN A CA  1 
ATOM   635  C  C   . ASN A 1 84  ? -0.65251  40.25795 16.05202  1.000 28.96722  ? 287  ASN A C   1 
ATOM   636  O  O   . ASN A 1 84  ? -0.20673  40.18029 14.90306  1.000 28.86078  ? 287  ASN A O   1 
ATOM   637  C  CB  . ASN A 1 84  ? 1.04210   40.00781 17.85801  1.000 30.80352  ? 287  ASN A CB  1 
ATOM   638  C  CG  . ASN A 1 84  ? 1.68469   39.13521 18.90744  1.000 36.95307  ? 287  ASN A CG  1 
ATOM   639  O  OD1 . ASN A 1 84  ? 1.02622   38.32181 19.56142  1.000 36.91902  ? 287  ASN A OD1 1 
ATOM   640  N  ND2 . ASN A 1 84  ? 2.99068   39.30584 19.08076  1.000 43.10866  ? 287  ASN A ND2 1 
ATOM   641  N  N   . ARG A 1 85  ? -1.58132  41.15851 16.39223  1.000 26.18018  ? 288  ARG A N   1 
ATOM   642  C  CA  . ARG A 1 85  ? -2.08632  42.11784 15.41315  1.000 25.11342  ? 288  ARG A CA  1 
ATOM   643  C  C   . ARG A 1 85  ? -2.13536  43.50998 16.03399  1.000 25.52767  ? 288  ARG A C   1 
ATOM   644  O  O   . ARG A 1 85  ? -2.38593  43.65766 17.23013  1.000 27.10418  ? 288  ARG A O   1 
ATOM   645  C  CB  . ARG A 1 85  ? -3.46268  41.71107 14.87088  1.000 29.34405  ? 288  ARG A CB  1 
ATOM   646  C  CG  . ARG A 1 85  ? -4.45045  41.20779 15.90782  1.000 29.80631  ? 288  ARG A CG  1 
ATOM   647  C  CD  . ARG A 1 85  ? -5.67398  40.63534 15.19892  1.000 30.43463  ? 288  ARG A CD  1 
ATOM   648  N  NE  . ARG A 1 85  ? -6.79741  40.38283 16.09270  1.000 29.29360  ? 288  ARG A NE  1 
ATOM   649  C  CZ  . ARG A 1 85  ? -7.90242  39.73972 15.73537  1.000 28.68081  ? 288  ARG A CZ  1 
ATOM   650  N  NH1 . ARG A 1 85  ? -8.03241  39.19968 14.53262  1.000 28.39131  ? 288  ARG A NH1 1 
ATOM   651  N  NH2 . ARG A 1 85  ? -8.90775  39.64560 16.60070  1.000 31.55890  ? 288  ARG A NH2 1 
ATOM   652  N  N   A ARG A 1 86  ? -1.90254  44.52404 15.19990  0.516 30.36595  ? 289  ARG A N   1 
ATOM   653  N  N   B ARG A 1 86  ? -1.92132  44.53181 15.20863  0.484 30.37447  ? 289  ARG A N   1 
ATOM   654  C  CA  A ARG A 1 86  ? -1.60447  45.87584 15.66206  0.516 30.09576  ? 289  ARG A CA  1 
ATOM   655  C  CA  B ARG A 1 86  ? -1.59664  45.86303 15.70991  0.484 30.08791  ? 289  ARG A CA  1 
ATOM   656  C  C   A ARG A 1 86  ? -2.66812  46.88297 15.24477  0.516 30.42018  ? 289  ARG A C   1 
ATOM   657  C  C   B ARG A 1 86  ? -2.57104  46.93241 15.22588  0.484 30.40797  ? 289  ARG A C   1 
ATOM   658  O  O   A ARG A 1 86  ? -3.20947  46.82569 14.13469  0.516 31.10227  ? 289  ARG A O   1 
ATOM   659  O  O   B ARG A 1 86  ? -2.97312  46.95579 14.05762  0.484 31.34086  ? 289  ARG A O   1 
ATOM   660  C  CB  A ARG A 1 86  ? -0.24417  46.34992 15.13736  0.516 32.02116  ? 289  ARG A CB  1 
ATOM   661  C  CB  B ARG A 1 86  ? -0.16330  46.23239 15.31853  0.484 32.31338  ? 289  ARG A CB  1 
ATOM   662  C  CG  A ARG A 1 86  ? 0.94529   45.68977 15.81842  0.516 32.82512  ? 289  ARG A CG  1 
ATOM   663  C  CG  B ARG A 1 86  ? 0.86811   45.39395 16.06627  0.484 32.67695  ? 289  ARG A CG  1 
ATOM   664  C  CD  A ARG A 1 86  ? 2.25474   46.35009 15.40684  0.516 36.63523  ? 289  ARG A CD  1 
ATOM   665  C  CD  B ARG A 1 86  ? 2.25176   45.45157 15.43964  0.484 35.87845  ? 289  ARG A CD  1 
ATOM   666  N  NE  A ARG A 1 86  ? 3.36694   45.93758 16.25734  0.516 41.53444  ? 289  ARG A NE  1 
ATOM   667  N  NE  B ARG A 1 86  ? 3.27396   44.98311 16.37044  0.484 39.17089  ? 289  ARG A NE  1 
ATOM   668  C  CZ  A ARG A 1 86  ? 3.82779   46.63162 17.29015  0.516 41.38692  ? 289  ARG A CZ  1 
ATOM   669  C  CZ  B ARG A 1 86  ? 3.68383   43.72546 16.47386  0.484 40.62574  ? 289  ARG A CZ  1 
ATOM   670  N  NH1 A ARG A 1 86  ? 3.29468   47.79217 17.64082  0.516 32.85447  ? 289  ARG A NH1 1 
ATOM   671  N  NH1 B ARG A 1 86  ? 3.18868   42.77008 15.70512  0.484 44.25356  ? 289  ARG A NH1 1 
ATOM   672  N  NH2 A ARG A 1 86  ? 4.85112   46.14822 17.99061  0.516 47.74000  ? 289  ARG A NH2 1 
ATOM   673  N  NH2 B ARG A 1 86  ? 4.61334   43.41860 17.37402  0.484 45.61782  ? 289  ARG A NH2 1 
ATOM   674  N  N   . ALA A 1 87  ? -2.94284  47.82158 16.14782  1.000 30.22175  ? 290  ALA A N   1 
ATOM   675  C  CA  . ALA A 1 87  ? -3.74429  48.99835 15.84991  1.000 31.10732  ? 290  ALA A CA  1 
ATOM   676  C  C   . ALA A 1 87  ? -3.10380  50.15878 16.60411  1.000 27.44735  ? 290  ALA A C   1 
ATOM   677  O  O   . ALA A 1 87  ? -2.25118  49.95019 17.46986  1.000 28.53836  ? 290  ALA A O   1 
ATOM   678  C  CB  . ALA A 1 87  ? -5.21420  48.78414 16.23535  1.000 32.25826  ? 290  ALA A CB  1 
ATOM   679  N  N   . TYR A 1 88  ? -3.49571  51.39066 16.26279  1.000 28.08975  ? 291  TYR A N   1 
ATOM   680  C  CA  . TYR A 1 88  ? -2.87832  52.58097 16.83697  1.000 31.71412  ? 291  TYR A CA  1 
ATOM   681  C  C   . TYR A 1 88  ? -3.95224  53.60982 17.14983  1.000 31.98917  ? 291  TYR A C   1 
ATOM   682  O  O   . TYR A 1 88  ? -4.82862  53.85977 16.32130  1.000 30.13482  ? 291  TYR A O   1 
ATOM   683  C  CB  . TYR A 1 88  ? -1.84466  53.18178 15.87002  1.000 30.96171  ? 291  TYR A CB  1 
ATOM   684  C  CG  . TYR A 1 88  ? -0.80058  52.18730 15.44711  1.000 33.84782  ? 291  TYR A CG  1 
ATOM   685  C  CD1 . TYR A 1 88  ? -0.98777  51.39579 14.31896  1.000 35.34746  ? 291  TYR A CD1 1 
ATOM   686  C  CD2 . TYR A 1 88  ? 0.36558   52.02298 16.18213  1.000 34.93286  ? 291  TYR A CD2 1 
ATOM   687  C  CE1 . TYR A 1 88  ? -0.04288  50.46500 13.93677  1.000 35.15070  ? 291  TYR A CE1 1 
ATOM   688  C  CE2 . TYR A 1 88  ? 1.31809   51.09581 15.80519  1.000 39.43783  ? 291  TYR A CE2 1 
ATOM   689  C  CZ  . TYR A 1 88  ? 1.10900   50.32473 14.67768  1.000 37.26246  ? 291  TYR A CZ  1 
ATOM   690  O  OH  . TYR A 1 88  ? 2.05469   49.40135 14.29695  1.000 39.19728  ? 291  TYR A OH  1 
ATOM   691  N  N   . ILE A 1 89  ? -3.88819  54.21513 18.33598  1.000 30.58222  ? 292  ILE A N   1 
ATOM   692  C  CA  . ILE A 1 89  ? -4.85931  55.22855 18.73417  1.000 29.91278  ? 292  ILE A CA  1 
ATOM   693  C  C   . ILE A 1 89  ? -4.15921  56.57211 18.84357  1.000 29.70603  ? 292  ILE A C   1 
ATOM   694  O  O   . ILE A 1 89  ? -3.12082  56.68674 19.50911  1.000 30.71219  ? 292  ILE A O   1 
ATOM   695  C  CB  . ILE A 1 89  ? -5.54532  54.86802 20.06093  1.000 27.44869  ? 292  ILE A CB  1 
ATOM   696  C  CG1 . ILE A 1 89  ? -6.35909  53.58650 19.90466  1.000 27.92024  ? 292  ILE A CG1 1 
ATOM   697  C  CG2 . ILE A 1 89  ? -6.44051  56.02533 20.53172  1.000 29.16389  ? 292  ILE A CG2 1 
ATOM   698  C  CD1 . ILE A 1 89  ? -6.97435  53.11283 21.23621  1.000 28.92452  ? 292  ILE A CD1 1 
ATOM   699  N  N   . LYS A 1 90  ? -4.73005  57.58218 18.19885  1.000 28.27776  ? 293  LYS A N   1 
ATOM   700  C  CA  . LYS A 1 90  ? -4.33536  58.97102 18.38343  1.000 30.28919  ? 293  LYS A CA  1 
ATOM   701  C  C   . LYS A 1 90  ? -5.49680  59.73183 19.01048  1.000 32.82579  ? 293  LYS A C   1 
ATOM   702  O  O   . LYS A 1 90  ? -6.57415  59.17757 19.24401  1.000 31.39247  ? 293  LYS A O   1 
ATOM   703  C  CB  . LYS A 1 90  ? -3.89584  59.60253 17.06120  1.000 32.33780  ? 293  LYS A CB  1 
ATOM   704  C  CG  . LYS A 1 90  ? -2.58751  59.03730 16.55014  1.000 36.45479  ? 293  LYS A CG  1 
ATOM   705  C  CD  . LYS A 1 90  ? -2.11709  59.77206 15.29825  1.000 38.65482  ? 293  LYS A CD  1 
ATOM   706  C  CE  . LYS A 1 90  ? -0.80226  59.19285 14.78269  1.000 40.80648  ? 293  LYS A CE  1 
ATOM   707  N  NZ  . LYS A 1 90  ? -0.25470  60.01386 13.65148  1.000 50.19780  ? 293  LYS A NZ  1 
ATOM   708  N  N   . PHE A 1 91  ? -5.26735  61.01609 19.28745  1.000 33.48551  ? 294  PHE A N   1 
ATOM   709  C  CA  . PHE A 1 91  ? -6.18488  61.79927 20.09882  1.000 31.42706  ? 294  PHE A CA  1 
ATOM   710  C  C   . PHE A 1 91  ? -6.31696  63.18820 19.49835  1.000 34.01014  ? 294  PHE A C   1 
ATOM   711  O  O   . PHE A 1 91  ? -5.31214  63.88262 19.31193  1.000 40.23156  ? 294  PHE A O   1 
ATOM   712  C  CB  . PHE A 1 91  ? -5.68458  61.91713 21.54060  1.000 30.50320  ? 294  PHE A CB  1 
ATOM   713  C  CG  . PHE A 1 91  ? -5.41312  60.59350 22.19613  1.000 30.48772  ? 294  PHE A CG  1 
ATOM   714  C  CD1 . PHE A 1 91  ? -4.20778  59.93189 21.99411  1.000 33.39394  ? 294  PHE A CD1 1 
ATOM   715  C  CD2 . PHE A 1 91  ? -6.36841  60.00986 23.00207  1.000 26.08885  ? 294  PHE A CD2 1 
ATOM   716  C  CE1 . PHE A 1 91  ? -3.96131  58.70172 22.59547  1.000 33.88020  ? 294  PHE A CE1 1 
ATOM   717  C  CE2 . PHE A 1 91  ? -6.12516  58.78995 23.61238  1.000 29.95690  ? 294  PHE A CE2 1 
ATOM   718  C  CZ  . PHE A 1 91  ? -4.92133  58.13769 23.40724  1.000 33.49005  ? 294  PHE A CZ  1 
ATOM   719  N  N   . LYS A 1 92  ? -7.54795  63.59508 19.21405  1.000 35.79892  ? 295  LYS A N   1 
ATOM   720  C  CA  . LYS A 1 92  ? -7.81462  64.87909 18.57671  1.000 34.83922  ? 295  LYS A CA  1 
ATOM   721  C  C   . LYS A 1 92  ? -8.36041  65.86829 19.59720  1.000 39.39450  ? 295  LYS A C   1 
ATOM   722  O  O   . LYS A 1 92  ? -9.34824  65.57897 20.28127  1.000 36.82367  ? 295  LYS A O   1 
ATOM   723  C  CB  . LYS A 1 92  ? -8.79825  64.71040 17.41895  1.000 38.59906  ? 295  LYS A CB  1 
ATOM   724  C  CG  . LYS A 1 92  ? -8.97628  65.97001 16.58429  1.000 45.78724  ? 295  LYS A CG  1 
ATOM   725  C  CD  . LYS A 1 92  ? -9.85280  65.70494 15.35903  1.000 56.07134  ? 295  LYS A CD  1 
ATOM   726  C  CE  . LYS A 1 92  ? -11.27413 66.22853 15.55340  1.000 62.97850  ? 295  LYS A CE  1 
ATOM   727  N  NZ  . LYS A 1 92  ? -12.16470 65.85139 14.41003  1.000 60.11405  ? 295  LYS A NZ  1 
ATOM   728  N  N   . ASP A 1 93  ? -7.69741  67.02391 19.70892  1.000 38.62353  ? 296  ASP A N   1 
ATOM   729  C  CA  . ASP A 1 93  ? -8.17010  68.13761 20.52717  1.000 40.67680  ? 296  ASP A CA  1 
ATOM   730  C  C   . ASP A 1 93  ? -9.40949  68.72063 19.85780  1.000 41.36828  ? 296  ASP A C   1 
ATOM   731  O  O   . ASP A 1 93  ? -9.32792  69.24499 18.74338  1.000 43.19451  ? 296  ASP A O   1 
ATOM   732  C  CB  . ASP A 1 93  ? -7.04803  69.16972 20.66160  1.000 38.59072  ? 296  ASP A CB  1 
ATOM   733  C  CG  . ASP A 1 93  ? -7.38843  70.32424 21.60067  1.000 45.49180  ? 296  ASP A CG  1 
ATOM   734  O  OD1 . ASP A 1 93  ? -8.55336  70.77300 21.63040  1.000 48.05614  ? 296  ASP A OD1 1 
ATOM   735  O  OD2 . ASP A 1 93  ? -6.46723  70.79428 22.30778  1.000 45.05526  ? 296  ASP A OD2 1 
ATOM   736  N  N   . LYS A 1 94  ? -10.56631 68.61218 20.51680  1.000 41.76240  ? 297  LYS A N   1 
ATOM   737  C  CA  . LYS A 1 94  ? -11.81457 68.98752 19.85317  1.000 46.84726  ? 297  LYS A CA  1 
ATOM   738  C  C   . LYS A 1 94  ? -11.94549 70.49936 19.68950  1.000 49.04401  ? 297  LYS A C   1 
ATOM   739  O  O   . LYS A 1 94  ? -12.65237 70.96133 18.78591  1.000 57.32526  ? 297  LYS A O   1 
ATOM   740  C  CB  . LYS A 1 94  ? -13.00764 68.41246 20.62566  1.000 44.64389  ? 297  LYS A CB  1 
ATOM   741  C  CG  . LYS A 1 94  ? -13.03335 66.89167 20.63132  1.000 54.68313  ? 297  LYS A CG  1 
ATOM   742  C  CD  . LYS A 1 94  ? -14.04132 66.30223 21.61421  1.000 49.58869  ? 297  LYS A CD  1 
ATOM   743  C  CE  . LYS A 1 94  ? -15.47738 66.43938 21.12609  1.000 59.35844  ? 297  LYS A CE  1 
ATOM   744  N  NZ  . LYS A 1 94  ? -16.43477 65.83421 22.09446  1.000 66.46920  ? 297  LYS A NZ  1 
ATOM   745  N  N   . LYS A 1 95  ? -11.27149 71.28773 20.52820  1.000 43.79088  ? 298  LYS A N   1 
ATOM   746  C  CA  . LYS A 1 95  ? -11.36032 72.73908 20.37419  1.000 48.56561  ? 298  LYS A CA  1 
ATOM   747  C  C   . LYS A 1 95  ? -10.49145 73.23810 19.22047  1.000 54.69638  ? 298  LYS A C   1 
ATOM   748  O  O   . LYS A 1 95  ? -10.90855 74.12013 18.45825  1.000 53.79706  ? 298  LYS A O   1 
ATOM   749  C  CB  . LYS A 1 95  ? -10.97123 73.43246 21.68056  1.000 48.92430  ? 298  LYS A CB  1 
ATOM   750  N  N   . THR A 1 96  ? -9.28644  72.68783 19.07259  1.000 46.44736  ? 299  THR A N   1 
ATOM   751  C  CA  . THR A 1 96  ? -8.34823  73.13636 18.05256  1.000 45.73755  ? 299  THR A CA  1 
ATOM   752  C  C   . THR A 1 96  ? -8.40775  72.30980 16.78028  1.000 48.75607  ? 299  THR A C   1 
ATOM   753  O  O   . THR A 1 96  ? -7.92532  72.76751 15.73720  1.000 52.76604  ? 299  THR A O   1 
ATOM   754  C  CB  . THR A 1 96  ? -6.91318  73.09892 18.59278  1.000 52.15044  ? 299  THR A CB  1 
ATOM   755  O  OG1 . THR A 1 96  ? -6.52422  71.73596 18.82097  1.000 46.60810  ? 299  THR A OG1 1 
ATOM   756  C  CG2 . THR A 1 96  ? -6.80943  73.87139 19.90636  1.000 48.19592  ? 299  THR A CG2 1 
ATOM   757  N  N   . GLY A 1 97  ? -8.97663  71.11075 16.83833  1.000 53.43807  ? 300  GLY A N   1 
ATOM   758  C  CA  . GLY A 1 97  ? -9.00499  70.22635 15.69857  1.000 45.54267  ? 300  GLY A CA  1 
ATOM   759  C  C   . GLY A 1 97  ? -7.69525  69.53218 15.38975  1.000 52.11757  ? 300  GLY A C   1 
ATOM   760  O  O   . GLY A 1 97  ? -7.63396  68.77380 14.41586  1.000 55.95097  ? 300  GLY A O   1 
ATOM   761  N  N   . GLN A 1 98  ? -6.65015  69.76604 16.17804  1.000 48.11777  ? 301  GLN A N   1 
ATOM   762  C  CA  . GLN A 1 98  ? -5.33494  69.19877 15.92683  1.000 40.75129  ? 301  GLN A CA  1 
ATOM   763  C  C   . GLN A 1 98  ? -5.14088  67.92064 16.73075  1.000 42.22746  ? 301  GLN A C   1 
ATOM   764  O  O   . GLN A 1 98  ? -5.73314  67.73372 17.79800  1.000 43.02455  ? 301  GLN A O   1 
ATOM   765  C  CB  . GLN A 1 98  ? -4.22938  70.19447 16.28950  1.000 51.33779  ? 301  GLN A CB  1 
ATOM   766  C  CG  . GLN A 1 98  ? -4.30208  71.55518 15.58594  1.000 50.58573  ? 301  GLN A CG  1 
ATOM   767  C  CD  . GLN A 1 98  ? -3.69164  71.53043 14.19525  1.000 53.15491  ? 301  GLN A CD  1 
ATOM   768  O  OE1 . GLN A 1 98  ? -3.94727  70.62005 13.40913  1.000 60.59251  ? 301  GLN A OE1 1 
ATOM   769  N  NE2 . GLN A 1 98  ? -2.86456  72.52247 13.89409  1.000 52.74945  ? 301  GLN A NE2 1 
ATOM   770  N  N   . TYR A 1 99  ? -4.30853  67.02909 16.20399  1.000 42.31846  ? 302  TYR A N   1 
ATOM   771  C  CA  . TYR A 1 99  ? -3.89625  65.87776 16.98675  1.000 36.84035  ? 302  TYR A CA  1 
ATOM   772  C  C   . TYR A 1 99  ? -3.01332  66.32639 18.13937  1.000 35.24990  ? 302  TYR A C   1 
ATOM   773  O  O   . TYR A 1 99  ? -2.18440  67.23223 18.00205  1.000 38.76188  ? 302  TYR A O   1 
ATOM   774  C  CB  . TYR A 1 99  ? -3.17347  64.86470 16.10802  1.000 44.90024  ? 302  TYR A CB  1 
ATOM   775  C  CG  . TYR A 1 99  ? -4.14005  63.98334 15.36168  1.000 47.78600  ? 302  TYR A CG  1 
ATOM   776  C  CD1 . TYR A 1 99  ? -5.01325  63.15501 16.05117  1.000 43.35621  ? 302  TYR A CD1 1 
ATOM   777  C  CD2 . TYR A 1 99  ? -4.19412  63.98416 13.97240  1.000 60.37707  ? 302  TYR A CD2 1 
ATOM   778  C  CE1 . TYR A 1 99  ? -5.91070  62.34132 15.38533  1.000 53.90151  ? 302  TYR A CE1 1 
ATOM   779  C  CE2 . TYR A 1 99  ? -5.09083  63.17036 13.29305  1.000 62.10107  ? 302  TYR A CE2 1 
ATOM   780  C  CZ  . TYR A 1 99  ? -5.94615  62.34981 14.00764  1.000 69.12394  ? 302  TYR A CZ  1 
ATOM   781  O  OH  . TYR A 1 99  ? -6.84308  61.53386 13.35157  1.000 77.35132  ? 302  TYR A OH  1 
ATOM   782  N  N   . ILE A 1 100 ? -3.21324  65.69014 19.28429  1.000 33.66605  ? 303  ILE A N   1 
ATOM   783  C  CA  . ILE A 1 100 ? -2.54074  66.06004 20.51949  1.000 35.85216  ? 303  ILE A CA  1 
ATOM   784  C  C   . ILE A 1 100 ? -1.10289  65.55931 20.48084  1.000 31.73059  ? 303  ILE A C   1 
ATOM   785  O  O   . ILE A 1 100 ? -0.81686  64.47650 19.96120  1.000 34.95513  ? 303  ILE A O   1 
ATOM   786  C  CB  . ILE A 1 100 ? -3.34215  65.50254 21.70898  1.000 37.04713  ? 303  ILE A CB  1 
ATOM   787  C  CG1 . ILE A 1 100 ? -4.62397  66.32567 21.86899  1.000 38.11748  ? 303  ILE A CG1 1 
ATOM   788  C  CG2 . ILE A 1 100 ? -2.53073  65.49587 22.99096  1.000 35.60187  ? 303  ILE A CG2 1 
ATOM   789  C  CD1 . ILE A 1 100 ? -5.72624  65.57372 22.54994  1.000 41.44788  ? 303  ILE A CD1 1 
ATOM   790  N  N   . LYS A 1 101 ? -0.18236  66.37262 20.98637  1.000 36.74727  ? 304  LYS A N   1 
ATOM   791  C  CA  . LYS A 1 101 ? 1.23041   66.04891 20.89033  1.000 34.60470  ? 304  LYS A CA  1 
ATOM   792  C  C   . LYS A 1 101 ? 1.65007   65.10859 22.01063  1.000 36.86699  ? 304  LYS A C   1 
ATOM   793  O  O   . LYS A 1 101 ? 1.13345   65.15983 23.13601  1.000 36.28115  ? 304  LYS A O   1 
ATOM   794  C  CB  . LYS A 1 101 ? 2.08995   67.31422 20.94628  1.000 37.90999  ? 304  LYS A CB  1 
ATOM   795  C  CG  . LYS A 1 101 ? 1.75292   68.39944 19.91082  1.000 43.70903  ? 304  LYS A CG  1 
ATOM   796  C  CD  . LYS A 1 101 ? 2.37735   68.10392 18.56596  1.000 46.68354  ? 304  LYS A CD  1 
ATOM   797  C  CE  . LYS A 1 101 ? 1.47191   67.27018 17.69388  1.000 48.61404  ? 304  LYS A CE  1 
ATOM   798  N  NZ  . LYS A 1 101 ? 1.93861   67.32811 16.28322  1.000 43.81265  ? 304  LYS A NZ  1 
ATOM   799  N  N   . GLY A 1 102 ? 2.62034   64.27116 21.70026  1.000 34.56820  ? 305  GLY A N   1 
ATOM   800  C  CA  . GLY A 1 102 ? 3.23703   63.40492 22.67915  1.000 38.68339  ? 305  GLY A CA  1 
ATOM   801  C  C   . GLY A 1 102 ? 4.36867   64.09780 23.40146  1.000 38.00393  ? 305  GLY A C   1 
ATOM   802  O  O   . GLY A 1 102 ? 4.54829   65.31817 23.32188  1.000 37.13302  ? 305  GLY A O   1 
ATOM   803  N  N   . ALA A 1 103 ? 5.17764   63.27905 24.07602  1.000 43.30747  ? 306  ALA A N   1 
ATOM   804  C  CA  . ALA A 1 103 ? 6.14373   63.79088 25.04285  1.000 40.12617  ? 306  ALA A CA  1 
ATOM   805  C  C   . ALA A 1 103 ? 7.12670   64.77574 24.41666  1.000 40.47521  ? 306  ALA A C   1 
ATOM   806  O  O   . ALA A 1 103 ? 7.48732   65.77188 25.05010  1.000 44.44145  ? 306  ALA A O   1 
ATOM   807  C  CB  . ALA A 1 103 ? 6.89144   62.62384 25.69011  1.000 42.38369  ? 306  ALA A CB  1 
ATOM   808  N  N   . ASP A 1 104 ? 7.58331   64.51777 23.18212  1.000 44.06574  ? 307  ASP A N   1 
ATOM   809  C  CA  . ASP A 1 104 ? 8.59502   65.39030 22.57982  1.000 43.06161  ? 307  ASP A CA  1 
ATOM   810  C  C   . ASP A 1 104 ? 8.01229   66.65194 21.95331  1.000 52.34238  ? 307  ASP A C   1 
ATOM   811  O  O   . ASP A 1 104 ? 8.76080   67.41197 21.32687  1.000 50.65401  ? 307  ASP A O   1 
ATOM   812  C  CB  . ASP A 1 104 ? 9.43814   64.63276 21.53964  1.000 42.63579  ? 307  ASP A CB  1 
ATOM   813  C  CG  . ASP A 1 104 ? 8.66909   64.28566 20.25438  1.000 48.53229  ? 307  ASP A CG  1 
ATOM   814  O  OD1 . ASP A 1 104 ? 7.48036   64.64009 20.10887  1.000 47.52983  ? 307  ASP A OD1 1 
ATOM   815  O  OD2 . ASP A 1 104 ? 9.27202   63.63305 19.37298  1.000 57.30408  ? 307  ASP A OD2 1 
ATOM   816  N  N   . GLY A 1 105 ? 6.71262   66.89925 22.10322  1.000 48.68033  ? 308  GLY A N   1 
ATOM   817  C  CA  . GLY A 1 105 ? 6.12097   68.11962 21.58781  1.000 46.01722  ? 308  GLY A CA  1 
ATOM   818  C  C   . GLY A 1 105 ? 5.99410   68.19320 20.08303  1.000 44.02036  ? 308  GLY A C   1 
ATOM   819  O  O   . GLY A 1 105 ? 5.48957   69.19914 19.57073  1.000 52.40479  ? 308  GLY A O   1 
ATOM   820  N  N   . LYS A 1 106 ? 6.42402   67.16597 19.35629  1.000 44.53077  ? 309  LYS A N   1 
ATOM   821  C  CA  . LYS A 1 106 ? 6.40212   67.18920 17.90037  1.000 51.03979  ? 309  LYS A CA  1 
ATOM   822  C  C   . LYS A 1 106 ? 5.59326   66.04717 17.31105  1.000 50.51215  ? 309  LYS A C   1 
ATOM   823  O  O   . LYS A 1 106 ? 4.72487   66.28610 16.46388  1.000 42.07953  ? 309  LYS A O   1 
ATOM   824  C  CB  . LYS A 1 106 ? 7.84288   67.17498 17.36014  1.000 44.68569  ? 309  LYS A CB  1 
ATOM   825  C  CG  . LYS A 1 106 ? 8.64503   68.36095 17.86837  1.000 50.68388  ? 309  LYS A CG  1 
ATOM   826  C  CD  . LYS A 1 106 ? 10.01934  68.47029 17.24605  1.000 52.91434  ? 309  LYS A CD  1 
ATOM   827  C  CE  . LYS A 1 106 ? 10.73350  69.68610 17.81658  1.000 51.55735  ? 309  LYS A CE  1 
ATOM   828  N  NZ  . LYS A 1 106 ? 12.02711  69.97318 17.14354  1.000 58.27280  ? 309  LYS A NZ  1 
ATOM   829  N  N   . ALA A 1 107 ? 5.83601   64.81067 17.74254  1.000 42.08026  ? 310  ALA A N   1 
ATOM   830  C  CA  . ALA A 1 107 ? 5.06272   63.69067 17.23689  1.000 34.22996  ? 310  ALA A CA  1 
ATOM   831  C  C   . ALA A 1 107 ? 3.66202   63.68701 17.83923  1.000 40.97770  ? 310  ALA A C   1 
ATOM   832  O  O   . ALA A 1 107 ? 3.43384   64.17561 18.94994  1.000 44.51216  ? 310  ALA A O   1 
ATOM   833  C  CB  . ALA A 1 107 ? 5.76028   62.36456 17.55633  1.000 43.38282  ? 310  ALA A CB  1 
ATOM   834  N  N   . ASP A 1 108 ? 2.72178   63.11404 17.09485  1.000 38.47064  ? 311  ASP A N   1 
ATOM   835  C  CA  . ASP A 1 108 ? 1.38760   62.87041 17.62620  1.000 33.88232  ? 311  ASP A CA  1 
ATOM   836  C  C   . ASP A 1 108 ? 1.43347   61.82180 18.72797  1.000 32.70575  ? 311  ASP A C   1 
ATOM   837  O  O   . ASP A 1 108 ? 2.11126   60.80288 18.60821  1.000 34.01062  ? 311  ASP A O   1 
ATOM   838  C  CB  . ASP A 1 108 ? 0.45008   62.38485 16.52158  1.000 37.66636  ? 311  ASP A CB  1 
ATOM   839  C  CG  . ASP A 1 108 ? 0.31057   63.38214 15.40348  1.000 44.54886  ? 311  ASP A CG  1 
ATOM   840  O  OD1 . ASP A 1 108 ? 0.64535   64.56509 15.62508  1.000 46.21964  ? 311  ASP A OD1 1 
ATOM   841  O  OD2 . ASP A 1 108 ? -0.12143  62.96473 14.30847  1.000 48.99324  ? 311  ASP A OD2 1 
ATOM   842  N  N   . LEU A 1 109 ? 0.72027   62.08845 19.81663  1.000 34.21767  ? 312  LEU A N   1 
ATOM   843  C  CA  . LEU A 1 109 ? 0.56485   61.08191 20.85637  1.000 33.20067  ? 312  LEU A CA  1 
ATOM   844  C  C   . LEU A 1 109 ? -0.11745  59.84893 20.27494  1.000 31.80926  ? 312  LEU A C   1 
ATOM   845  O  O   . LEU A 1 109 ? -1.22913  59.93699 19.74399  1.000 34.34745  ? 312  LEU A O   1 
ATOM   846  C  CB  . LEU A 1 109 ? -0.24473  61.66876 22.00818  1.000 30.05401  ? 312  LEU A CB  1 
ATOM   847  C  CG  . LEU A 1 109 ? -0.53443  60.78153 23.21970  1.000 34.43741  ? 312  LEU A CG  1 
ATOM   848  C  CD1 . LEU A 1 109 ? 0.75947   60.35501 23.89395  1.000 36.60894  ? 312  LEU A CD1 1 
ATOM   849  C  CD2 . LEU A 1 109 ? -1.42260  61.54498 24.18788  1.000 34.02772  ? 312  LEU A CD2 1 
ATOM   850  N  N   . THR A 1 110 ? 0.55134   58.69959 20.36743  1.000 31.15228  ? 313  THR A N   1 
ATOM   851  C  CA  . THR A 1 110 ? 0.08687   57.47516 19.72163  1.000 28.30071  ? 313  THR A CA  1 
ATOM   852  C  C   . THR A 1 110 ? 0.21371   56.31666 20.69818  1.000 33.24090  ? 313  THR A C   1 
ATOM   853  O  O   . THR A 1 110 ? 1.30598   56.05303 21.20663  1.000 33.12951  ? 313  THR A O   1 
ATOM   854  C  CB  . THR A 1 110 ? 0.89871   57.18017 18.45538  1.000 37.14972  ? 313  THR A CB  1 
ATOM   855  O  OG1 . THR A 1 110 ? 0.91390   58.33571 17.61658  1.000 37.05536  ? 313  THR A OG1 1 
ATOM   856  C  CG2 . THR A 1 110 ? 0.30738   56.01148 17.69070  1.000 36.10757  ? 313  THR A CG2 1 
ATOM   857  N  N   . VAL A 1 111 ? -0.88970  55.62302 20.94797  1.000 27.15512  ? 314  VAL A N   1 
ATOM   858  C  CA  . VAL A 1 111 ? -0.89095  54.42429 21.78038  1.000 27.92689  ? 314  VAL A CA  1 
ATOM   859  C  C   . VAL A 1 111 ? -0.85942  53.19787 20.87948  1.000 26.99698  ? 314  VAL A C   1 
ATOM   860  O  O   . VAL A 1 111 ? -1.69183  53.05874 19.97436  1.000 30.12119  ? 314  VAL A O   1 
ATOM   861  C  CB  . VAL A 1 111 ? -2.11001  54.38020 22.71502  1.000 30.96046  ? 314  VAL A CB  1 
ATOM   862  C  CG1 . VAL A 1 111 ? -2.07292  53.10552 23.55233  1.000 25.19688  ? 314  VAL A CG1 1 
ATOM   863  C  CG2 . VAL A 1 111 ? -2.11148  55.60065 23.62466  1.000 27.40411  ? 314  VAL A CG2 1 
ATOM   864  N  N   . ASN A 1 112 ? 0.09360   52.30725 21.13183  1.000 26.55558  ? 315  ASN A N   1 
ATOM   865  C  CA  . ASN A 1 112 ? 0.23715   51.08575 20.34783  1.000 25.62787  ? 315  ASN A CA  1 
ATOM   866  C  C   . ASN A 1 112 ? -0.60369  49.96773 20.96128  1.000 30.81396  ? 315  ASN A C   1 
ATOM   867  O  O   . ASN A 1 112 ? -0.41428  49.61079 22.12853  1.000 28.87768  ? 315  ASN A O   1 
ATOM   868  C  CB  . ASN A 1 112 ? 1.70845   50.68622 20.26730  1.000 29.00812  ? 315  ASN A CB  1 
ATOM   869  C  CG  . ASN A 1 112 ? 2.57216   51.75983 19.60409  1.000 37.03903  ? 315  ASN A CG  1 
ATOM   870  O  OD1 . ASN A 1 112 ? 2.08611   52.56968 18.81218  1.000 38.84930  ? 315  ASN A OD1 1 
ATOM   871  N  ND2 . ASN A 1 112 ? 3.85748   51.76617 19.92836  1.000 44.84883  ? 315  ASN A ND2 1 
ATOM   872  N  N   . ILE A 1 113 ? -1.52872  49.42010 20.17108  1.000 27.60928  ? 316  ILE A N   1 
ATOM   873  C  CA  . ILE A 1 113 ? -2.34937  48.27875 20.55962  1.000 26.22284  ? 316  ILE A CA  1 
ATOM   874  C  C   . ILE A 1 113 ? -1.76955  47.03937 19.89240  1.000 29.62446  ? 316  ILE A C   1 
ATOM   875  O  O   . ILE A 1 113 ? -1.51515  47.04957 18.68370  1.000 29.48414  ? 316  ILE A O   1 
ATOM   876  C  CB  . ILE A 1 113 ? -3.81491  48.46643 20.13007  1.000 28.63347  ? 316  ILE A CB  1 
ATOM   877  C  CG1 . ILE A 1 113 ? -4.38229  49.80798 20.60009  1.000 31.77734  ? 316  ILE A CG1 1 
ATOM   878  C  CG2 . ILE A 1 113 ? -4.66655  47.29881 20.64000  1.000 27.36801  ? 316  ILE A CG2 1 
ATOM   879  C  CD1 . ILE A 1 113 ? -4.26167  50.03073 22.05691  1.000 33.11928  ? 316  ILE A CD1 1 
ATOM   880  N  N   . ILE A 1 114 ? -1.56156  45.96921 20.65659  1.000 26.45181  ? 317  ILE A N   1 
ATOM   881  C  CA  . ILE A 1 114 ? -1.11444  44.69152 20.08431  1.000 24.74123  ? 317  ILE A CA  1 
ATOM   882  C  C   . ILE A 1 114 ? -1.99074  43.62412 20.71599  1.000 25.18246  ? 317  ILE A C   1 
ATOM   883  O  O   . ILE A 1 114 ? -1.76962  43.25231 21.86736  1.000 27.83440  ? 317  ILE A O   1 
ATOM   884  C  CB  . ILE A 1 114 ? 0.36624   44.40438 20.36087  1.000 28.39612  ? 317  ILE A CB  1 
ATOM   885  C  CG1 . ILE A 1 114 ? 1.24508   45.61316 20.02485  1.000 29.91810  ? 317  ILE A CG1 1 
ATOM   886  C  CG2 . ILE A 1 114 ? 0.82252   43.15248 19.60448  1.000 32.97565  ? 317  ILE A CG2 1 
ATOM   887  C  CD1 . ILE A 1 114 ? 2.67368   45.43999 20.46044  1.000 33.22898  ? 317  ILE A CD1 1 
ATOM   888  N  N   . GLN A 1 115 ? -2.98970  43.13577 19.99039  1.000 26.59648  ? 318  GLN A N   1 
ATOM   889  C  CA  . GLN A 1 115 ? -3.75020  42.01782 20.52900  1.000 27.25791  ? 318  GLN A CA  1 
ATOM   890  C  C   . GLN A 1 115 ? -2.94646  40.73455 20.34503  1.000 27.99222  ? 318  GLN A C   1 
ATOM   891  O  O   . GLN A 1 115 ? -2.45182  40.45307 19.24540  1.000 27.41099  ? 318  GLN A O   1 
ATOM   892  C  CB  . GLN A 1 115 ? -5.12375  41.88551 19.87412  1.000 24.55614  ? 318  GLN A CB  1 
ATOM   893  C  CG  . GLN A 1 115 ? -5.90806  40.70697 20.48024  1.000 26.71752  ? 318  GLN A CG  1 
ATOM   894  C  CD  . GLN A 1 115 ? -7.31166  40.56527 19.92700  1.000 24.63915  ? 318  GLN A CD  1 
ATOM   895  O  OE1 . GLN A 1 115 ? -7.57079  40.91581 18.77325  1.000 26.66633  ? 318  GLN A OE1 1 
ATOM   896  N  NE2 . GLN A 1 115 ? -8.23198  40.03719 20.75057  1.000 25.93813  ? 318  GLN A NE2 1 
ATOM   897  N  N   . LYS A 1 116 ? -2.81952  39.96948 21.42488  1.000 26.60588  ? 319  LYS A N   1 
ATOM   898  C  CA  . LYS A 1 116 ? -1.95888  38.79423 21.43924  1.000 26.18958  ? 319  LYS A CA  1 
ATOM   899  C  C   . LYS A 1 116 ? -2.53631  37.67003 20.59615  1.000 26.26385  ? 319  LYS A C   1 
ATOM   900  O  O   . LYS A 1 116 ? -3.75258  37.53662 20.43998  1.000 25.48046  ? 319  LYS A O   1 
ATOM   901  C  CB  . LYS A 1 116 ? -1.76546  38.26415 22.85604  1.000 27.93807  ? 319  LYS A CB  1 
ATOM   902  C  CG  . LYS A 1 116 ? -1.08734  39.20932 23.81892  1.000 34.09544  ? 319  LYS A CG  1 
ATOM   903  C  CD  . LYS A 1 116 ? -0.94821  38.50057 25.14989  1.000 41.95234  ? 319  LYS A CD  1 
ATOM   904  C  CE  . LYS A 1 116 ? -0.62369  39.44077 26.28622  1.000 50.04109  ? 319  LYS A CE  1 
ATOM   905  N  NZ  . LYS A 1 116 ? -0.35540  38.62576 27.50815  1.000 46.24380  ? 319  LYS A NZ  1 
ATOM   906  N  N   . LYS A 1 117 ? -1.62945  36.82300 20.11737  1.000 27.90379  ? 320  LYS A N   1 
ATOM   907  C  CA  . LYS A 1 117 ? -1.94372  35.64681 19.32281  1.000 32.73269  ? 320  LYS A CA  1 
ATOM   908  C  C   . LYS A 1 117 ? -2.76807  34.63066 20.11141  1.000 26.71040  ? 320  LYS A C   1 
ATOM   909  O  O   . LYS A 1 117 ? -2.74300  34.57097 21.34713  1.000 28.74031  ? 320  LYS A O   1 
ATOM   910  C  CB  . LYS A 1 117 ? -0.65190  34.98591 18.84850  1.000 32.78283  ? 320  LYS A CB  1 
ATOM   911  C  CG  . LYS A 1 117 ? 0.14428   34.33168 19.97928  1.000 34.11034  ? 320  LYS A CG  1 
ATOM   912  C  CD  . LYS A 1 117 ? 1.47281   33.75386 19.49573  1.000 37.16056  ? 320  LYS A CD  1 
ATOM   913  N  N   . ASN A 1 118 ? -3.48591  33.79925 19.36372  1.000 28.67676  ? 321  ASN A N   1 
ATOM   914  C  CA  . ASN A 1 118 ? -4.23693  32.68602 19.92563  1.000 27.25669  ? 321  ASN A CA  1 
ATOM   915  C  C   . ASN A 1 118 ? -3.26734  31.58578 20.35656  1.000 34.33292  ? 321  ASN A C   1 
ATOM   916  O  O   . ASN A 1 118 ? -2.50819  31.06603 19.53308  1.000 31.82451  ? 321  ASN A O   1 
ATOM   917  C  CB  . ASN A 1 118 ? -5.21942  32.17094 18.87353  1.000 28.07977  ? 321  ASN A CB  1 
ATOM   918  C  CG  . ASN A 1 118 ? -6.16707  31.08978 19.38932  1.000 39.12790  ? 321  ASN A CG  1 
ATOM   919  O  OD1 . ASN A 1 118 ? -6.16131  30.71087 20.57206  1.000 34.23647  ? 321  ASN A OD1 1 
ATOM   920  N  ND2 . ASN A 1 118 ? -6.99881  30.57972 18.47764  1.000 38.52255  ? 321  ASN A ND2 1 
ATOM   921  N  N   . GLU A 1 119 ? -3.27121  31.24939 21.64532  1.000 33.61613  ? 322  GLU A N   1 
ATOM   922  C  CA  . GLU A 1 119 ? -2.40293  30.18872 22.15649  1.000 34.28622  ? 322  GLU A CA  1 
ATOM   923  C  C   . GLU A 1 119 ? -2.97046  28.79325 21.95172  1.000 37.61878  ? 322  GLU A C   1 
ATOM   924  O  O   . GLU A 1 119 ? -2.24342  27.81201 22.15096  1.000 41.62511  ? 322  GLU A O   1 
ATOM   925  C  CB  . GLU A 1 119 ? -2.13420  30.39226 23.65319  1.000 39.79157  ? 322  GLU A CB  1 
ATOM   926  C  CG  . GLU A 1 119 ? -1.43061  31.68833 23.99625  1.000 52.12167  ? 322  GLU A CG  1 
ATOM   927  C  CD  . GLU A 1 119 ? 0.02234   31.68573 23.58003  1.000 60.84574  ? 322  GLU A CD  1 
ATOM   928  O  OE1 . GLU A 1 119 ? 0.55324   30.59403 23.27968  1.000 66.99282  ? 322  GLU A OE1 1 
ATOM   929  O  OE2 . GLU A 1 119 ? 0.63498   32.77585 23.55359  1.000 66.33828  ? 322  GLU A OE2 1 
ATOM   930  N  N   . ASN A 1 120 ? -4.24288  28.66999 21.59017  1.000 34.58801  ? 323  ASN A N   1 
ATOM   931  C  CA  . ASN A 1 120 ? -4.87662  27.36639 21.38675  1.000 39.99908  ? 323  ASN A CA  1 
ATOM   932  C  C   . ASN A 1 120 ? -5.67104  27.36495 20.08372  1.000 35.03738  ? 323  ASN A C   1 
ATOM   933  O  O   . ASN A 1 120 ? -6.89841  27.21435 20.08108  1.000 32.96725  ? 323  ASN A O   1 
ATOM   934  C  CB  . ASN A 1 120 ? -5.75723  27.02001 22.58270  1.000 43.05795  ? 323  ASN A CB  1 
ATOM   935  C  CG  . ASN A 1 120 ? -4.97870  27.00863 23.87973  1.000 52.01724  ? 323  ASN A CG  1 
ATOM   936  O  OD1 . ASN A 1 120 ? -5.26641  27.77581 24.80016  1.000 59.17908  ? 323  ASN A OD1 1 
ATOM   937  N  ND2 . ASN A 1 120 ? -3.97028  26.14515 23.95380  1.000 59.32397  ? 323  ASN A ND2 1 
ATOM   938  N  N   . PRO A 1 121 ? -4.99161  27.51933 18.95010  1.000 33.15734  ? 324  PRO A N   1 
ATOM   939  C  CA  . PRO A 1 121 ? -5.69891  27.56070 17.66862  1.000 31.92740  ? 324  PRO A CA  1 
ATOM   940  C  C   . PRO A 1 121 ? -6.19904  26.18635 17.25693  1.000 36.64579  ? 324  PRO A C   1 
ATOM   941  O  O   . PRO A 1 121 ? -5.59301  25.15870 17.56882  1.000 35.49823  ? 324  PRO A O   1 
ATOM   942  C  CB  . PRO A 1 121 ? -4.62442  28.05781 16.70044  1.000 33.97506  ? 324  PRO A CB  1 
ATOM   943  C  CG  . PRO A 1 121 ? -3.36054  27.47853 17.27816  1.000 30.62637  ? 324  PRO A CG  1 
ATOM   944  C  CD  . PRO A 1 121 ? -3.53208  27.63151 18.76522  1.000 30.69976  ? 324  PRO A CD  1 
ATOM   945  N  N   . VAL A 1 122 ? -7.32331  26.17300 16.54821  1.000 32.08591  ? 325  VAL A N   1 
ATOM   946  C  CA  . VAL A 1 122 ? -7.78835  24.97799 15.85003  1.000 34.51446  ? 325  VAL A CA  1 
ATOM   947  C  C   . VAL A 1 122 ? -7.28756  25.08441 14.41778  1.000 33.32598  ? 325  VAL A C   1 
ATOM   948  O  O   . VAL A 1 122 ? -7.60479  26.05089 13.71368  1.000 28.87416  ? 325  VAL A O   1 
ATOM   949  C  CB  . VAL A 1 122 ? -9.31864  24.83818 15.90070  1.000 35.80000  ? 325  VAL A CB  1 
ATOM   950  C  CG1 . VAL A 1 122 ? -9.76864  23.60656 15.11978  1.000 41.04888  ? 325  VAL A CG1 1 
ATOM   951  C  CG2 . VAL A 1 122 ? -9.79897  24.76163 17.35104  1.000 39.67807  ? 325  VAL A CG2 1 
ATOM   952  N  N   . VAL A 1 123 ? -6.48798  24.10806 13.99472  1.000 32.82846  ? 326  VAL A N   1 
ATOM   953  C  CA  . VAL A 1 123 ? -5.80897  24.15240 12.70568  1.000 30.34255  ? 326  VAL A CA  1 
ATOM   954  C  C   . VAL A 1 123 ? -6.43432  23.10503 11.79785  1.000 29.20528  ? 326  VAL A C   1 
ATOM   955  O  O   . VAL A 1 123 ? -6.87527  22.05015 12.26039  1.000 31.15742  ? 326  VAL A O   1 
ATOM   956  C  CB  . VAL A 1 123 ? -4.29048  23.91085 12.87778  1.000 27.20062  ? 326  VAL A CB  1 
ATOM   957  C  CG1 . VAL A 1 123 ? -3.56757  23.87836 11.53301  1.000 29.79322  ? 326  VAL A CG1 1 
ATOM   958  C  CG2 . VAL A 1 123 ? -3.67116  24.98362 13.79537  1.000 30.16521  ? 326  VAL A CG2 1 
ATOM   959  N  N   . HIS A 1 124 ? -6.48450  23.39669 10.49911  1.000 27.43689  ? 327  HIS A N   1 
ATOM   960  C  CA  . HIS A 1 124 ? -6.84603  22.37523 9.52248   1.000 27.68844  ? 327  HIS A CA  1 
ATOM   961  C  C   . HIS A 1 124 ? -5.80993  22.36234 8.40744   1.000 27.14984  ? 327  HIS A C   1 
ATOM   962  O  O   . HIS A 1 124 ? -4.99603  23.27836 8.28104   1.000 25.38816  ? 327  HIS A O   1 
ATOM   963  C  CB  . HIS A 1 124 ? -8.27714  22.56584 8.97735   1.000 28.19291  ? 327  HIS A CB  1 
ATOM   964  C  CG  . HIS A 1 124 ? -8.51898  23.86951 8.27987   1.000 32.30924  ? 327  HIS A CG  1 
ATOM   965  N  ND1 . HIS A 1 124 ? -8.71461  25.05677 8.95550   1.000 32.53211  ? 327  HIS A ND1 1 
ATOM   966  C  CD2 . HIS A 1 124 ? -8.66300  24.15920 6.96408   1.000 35.87939  ? 327  HIS A CD2 1 
ATOM   967  C  CE1 . HIS A 1 124 ? -8.94237  26.02543 8.08585   1.000 32.31270  ? 327  HIS A CE1 1 
ATOM   968  N  NE2 . HIS A 1 124 ? -8.91359  25.50770 6.86900   1.000 32.93294  ? 327  HIS A NE2 1 
ATOM   969  N  N   . TYR A 1 125 ? -5.81846  21.28232 7.61312   1.000 23.50021  ? 328  TYR A N   1 
ATOM   970  C  CA  . TYR A 1 125 ? -4.73418  20.99757 6.68584   1.000 25.71089  ? 328  TYR A CA  1 
ATOM   971  C  C   . TYR A 1 125 ? -5.28463  20.64949 5.31172   1.000 22.87541  ? 328  TYR A C   1 
ATOM   972  O  O   . TYR A 1 125 ? -6.35971  20.06030 5.18720   1.000 27.95685  ? 328  TYR A O   1 
ATOM   973  C  CB  . TYR A 1 125 ? -3.85045  19.81919 7.19103   1.000 21.82866  ? 328  TYR A CB  1 
ATOM   974  C  CG  . TYR A 1 125 ? -3.23590  20.10265 8.53965   1.000 23.27062  ? 328  TYR A CG  1 
ATOM   975  C  CD1 . TYR A 1 125 ? -3.95554  19.89043 9.70334   1.000 27.92805  ? 328  TYR A CD1 1 
ATOM   976  C  CD2 . TYR A 1 125 ? -1.93706  20.58405 8.63583   1.000 22.33110  ? 328  TYR A CD2 1 
ATOM   977  C  CE1 . TYR A 1 125 ? -3.39802  20.16705 10.94788  1.000 27.71349  ? 328  TYR A CE1 1 
ATOM   978  C  CE2 . TYR A 1 125 ? -1.36614  20.85590 9.86704   1.000 23.19264  ? 328  TYR A CE2 1 
ATOM   979  C  CZ  . TYR A 1 125 ? -2.10257  20.64683 11.01264  1.000 26.05889  ? 328  TYR A CZ  1 
ATOM   980  O  OH  . TYR A 1 125 ? -1.53776  20.91882 12.24281  1.000 25.58390  ? 328  TYR A OH  1 
ATOM   981  N  N   . LYS A 1 126 ? -4.53490  21.04217 4.28637   1.000 23.16636  ? 329  LYS A N   1 
ATOM   982  C  CA  . LYS A 1 126 ? -4.79370  20.64087 2.90655   1.000 24.83231  ? 329  LYS A CA  1 
ATOM   983  C  C   . LYS A 1 126 ? -3.51208  20.05765 2.34433   1.000 23.50759  ? 329  LYS A C   1 
ATOM   984  O  O   . LYS A 1 126 ? -2.47526  20.73095 2.34418   1.000 24.46951  ? 329  LYS A O   1 
ATOM   985  C  CB  . LYS A 1 126 ? -5.23296  21.82659 2.03941   1.000 24.51033  ? 329  LYS A CB  1 
ATOM   986  C  CG  . LYS A 1 126 ? -6.57882  22.41071 2.33999   1.000 32.38668  ? 329  LYS A CG  1 
ATOM   987  C  CD  . LYS A 1 126 ? -6.93599  23.39122 1.23882   1.000 35.84105  ? 329  LYS A CD  1 
ATOM   988  C  CE  . LYS A 1 126 ? -8.23747  24.11255 1.50288   1.000 50.96395  ? 329  LYS A CE  1 
ATOM   989  N  NZ  . LYS A 1 126 ? -8.49857  25.09071 0.40414   1.000 50.41117  ? 329  LYS A NZ  1 
ATOM   990  N  N   . TRP A 1 127 ? -3.58329  18.82630 1.84267   1.000 22.87946  ? 330  TRP A N   1 
ATOM   991  C  CA  . TRP A 1 127 ? -2.43336  18.14160 1.27528   1.000 23.36619  ? 330  TRP A CA  1 
ATOM   992  C  C   . TRP A 1 127 ? -2.60546  18.05119 -0.23468  1.000 19.46706  ? 330  TRP A C   1 
ATOM   993  O  O   . TRP A 1 127 ? -3.72954  18.03221 -0.74257  1.000 23.79055  ? 330  TRP A O   1 
ATOM   994  C  CB  . TRP A 1 127 ? -2.25661  16.73338 1.89116   1.000 21.75126  ? 330  TRP A CB  1 
ATOM   995  C  CG  . TRP A 1 127 ? -2.16750  16.81955 3.40270   1.000 20.26412  ? 330  TRP A CG  1 
ATOM   996  C  CD1 . TRP A 1 127 ? -3.16870  16.59743 4.29554   1.000 23.03268  ? 330  TRP A CD1 1 
ATOM   997  C  CD2 . TRP A 1 127 ? -1.04243  17.27829 4.16139   1.000 21.43909  ? 330  TRP A CD2 1 
ATOM   998  N  NE1 . TRP A 1 127 ? -2.72248  16.84689 5.58520   1.000 22.69225  ? 330  TRP A NE1 1 
ATOM   999  C  CE2 . TRP A 1 127 ? -1.42188  17.27361 5.52313   1.000 20.73545  ? 330  TRP A CE2 1 
ATOM   1000 C  CE3 . TRP A 1 127 ? 0.25776   17.67121 3.82137   1.000 20.77577  ? 330  TRP A CE3 1 
ATOM   1001 C  CZ2 . TRP A 1 127 ? -0.54072  17.64596 6.55379   1.000 22.06281  ? 330  TRP A CZ2 1 
ATOM   1002 C  CZ3 . TRP A 1 127 ? 1.13582   18.04636 4.84584   1.000 22.83218  ? 330  TRP A CZ3 1 
ATOM   1003 C  CH2 . TRP A 1 127 ? 0.72525   18.03104 6.19504   1.000 22.16357  ? 330  TRP A CH2 1 
ATOM   1004 N  N   . VAL A 1 128 ? -1.47945  18.02556 -0.94971  1.000 20.59017  ? 331  VAL A N   1 
ATOM   1005 C  CA  . VAL A 1 128 ? -1.52438  17.73588 -2.38358  1.000 23.07911  ? 331  VAL A CA  1 
ATOM   1006 C  C   . VAL A 1 128 ? -2.30773  16.44242 -2.63001  1.000 23.65060  ? 331  VAL A C   1 
ATOM   1007 O  O   . VAL A 1 128 ? -2.19247  15.46431 -1.88244  1.000 22.44057  ? 331  VAL A O   1 
ATOM   1008 C  CB  . VAL A 1 128 ? -0.09300  17.66355 -2.94795  1.000 20.04143  ? 331  VAL A CB  1 
ATOM   1009 C  CG1 . VAL A 1 128 ? -0.07062  17.05641 -4.35555  1.000 19.24130  ? 331  VAL A CG1 1 
ATOM   1010 C  CG2 . VAL A 1 128 ? 0.53011   19.07875 -2.96221  1.000 23.94304  ? 331  VAL A CG2 1 
ATOM   1011 N  N   . ASP A 1 129 ? -3.10887  16.44114 -3.68794  1.000 21.60211  ? 332  ASP A N   1 
ATOM   1012 C  CA  . ASP A 1 129 ? -4.00488  15.32146 -3.94592  1.000 24.73347  ? 332  ASP A CA  1 
ATOM   1013 C  C   . ASP A 1 129 ? -3.23626  14.01828 -4.13639  1.000 27.85349  ? 332  ASP A C   1 
ATOM   1014 O  O   . ASP A 1 129 ? -2.21229  13.96543 -4.82450  1.000 24.81456  ? 332  ASP A O   1 
ATOM   1015 C  CB  . ASP A 1 129 ? -4.85534  15.61635 -5.17926  1.000 27.74400  ? 332  ASP A CB  1 
ATOM   1016 C  CG  . ASP A 1 129 ? -5.90396  14.54870 -5.42757  1.000 35.87619  ? 332  ASP A CG  1 
ATOM   1017 O  OD1 . ASP A 1 129 ? -6.87644  14.46436 -4.64978  1.000 39.95162  ? 332  ASP A OD1 1 
ATOM   1018 O  OD2 . ASP A 1 129 ? -5.74815  13.79249 -6.39418  1.000 34.69220  ? 332  ASP A OD2 1 
ATOM   1019 N  N   . GLY A 1 130 ? -3.72376  12.95546 -3.50079  1.000 24.29381  ? 333  GLY A N   1 
ATOM   1020 C  CA  . GLY A 1 130 ? -3.19615  11.62842 -3.74554  1.000 25.08830  ? 333  GLY A CA  1 
ATOM   1021 C  C   . GLY A 1 130 ? -2.02253  11.19383 -2.89787  1.000 25.65861  ? 333  GLY A C   1 
ATOM   1022 O  O   . GLY A 1 130 ? -1.52950  10.07381 -3.08507  1.000 26.30082  ? 333  GLY A O   1 
ATOM   1023 N  N   . ILE A 1 131 ? -1.53967  12.02557 -1.97441  1.000 21.42819  ? 334  ILE A N   1 
ATOM   1024 C  CA  . ILE A 1 131 ? -0.40802  11.63328 -1.14590  1.000 20.19677  ? 334  ILE A CA  1 
ATOM   1025 C  C   . ILE A 1 131 ? -0.84137  11.23798 0.26019   1.000 19.45196  ? 334  ILE A C   1 
ATOM   1026 O  O   . ILE A 1 131 ? 0.01174   11.07263 1.13757   1.000 24.17399  ? 334  ILE A O   1 
ATOM   1027 C  CB  . ILE A 1 131 ? 0.68194   12.72300 -1.08106  1.000 23.06693  ? 334  ILE A CB  1 
ATOM   1028 C  CG1 . ILE A 1 131 ? 0.20529   13.95040 -0.27903  1.000 21.37651  ? 334  ILE A CG1 1 
ATOM   1029 C  CG2 . ILE A 1 131 ? 1.19318   13.06016 -2.49232  1.000 21.87776  ? 334  ILE A CG2 1 
ATOM   1030 C  CD1 . ILE A 1 131 ? 1.35656   14.81122 0.19824   1.000 20.63433  ? 334  ILE A CD1 1 
ATOM   1031 N  N   . GLY A 1 132 ? -2.14136  11.08159 0.49126   1.000 23.17656  ? 335  GLY A N   1 
ATOM   1032 C  CA  . GLY A 1 132 ? -2.59722  10.76085 1.82798   1.000 25.33170  ? 335  GLY A CA  1 
ATOM   1033 C  C   . GLY A 1 132 ? -2.42911  11.94860 2.76300   1.000 23.34314  ? 335  GLY A C   1 
ATOM   1034 O  O   . GLY A 1 132 ? -2.47270  13.11510 2.35411   1.000 24.40066  ? 335  GLY A O   1 
ATOM   1035 N  N   . ALA A 1 133 ? -2.23743  11.63861 4.04383   1.000 22.47513  ? 336  ALA A N   1 
ATOM   1036 C  CA  . ALA A 1 133 ? -2.08188  12.64956 5.08759   1.000 20.75107  ? 336  ALA A CA  1 
ATOM   1037 C  C   . ALA A 1 133 ? -1.27098  12.02769 6.21169   1.000 21.30070  ? 336  ALA A C   1 
ATOM   1038 O  O   . ALA A 1 133 ? -1.33815  10.81196 6.41533   1.000 23.00241  ? 336  ALA A O   1 
ATOM   1039 C  CB  . ALA A 1 133 ? -3.44704  13.13281 5.61400   1.000 21.11452  ? 336  ALA A CB  1 
ATOM   1040 N  N   . PRO A 1 134 ? -0.50989  12.82009 6.95934   1.000 19.55290  ? 337  PRO A N   1 
ATOM   1041 C  CA  . PRO A 1 134 ? 0.31108   12.23425 8.02765   1.000 21.37956  ? 337  PRO A CA  1 
ATOM   1042 C  C   . PRO A 1 134 ? -0.53734  11.61579 9.12801   1.000 23.83870  ? 337  PRO A C   1 
ATOM   1043 O  O   . PRO A 1 134 ? -1.53685  12.18670 9.57571   1.000 27.91424  ? 337  PRO A O   1 
ATOM   1044 C  CB  . PRO A 1 134 ? 1.12463   13.42861 8.55245   1.000 21.98793  ? 337  PRO A CB  1 
ATOM   1045 C  CG  . PRO A 1 134 ? 0.32577   14.64391 8.16829   1.000 21.76949  ? 337  PRO A CG  1 
ATOM   1046 C  CD  . PRO A 1 134 ? -0.27228  14.26634 6.81114   1.000 19.75464  ? 337  PRO A CD  1 
ATOM   1047 N  N   . THR A 1 135 ? -0.11246  10.44292 9.58087   1.000 21.48928  ? 338  THR A N   1 
ATOM   1048 C  CA  . THR A 1 135 ? -0.65323  9.87683  10.80403  1.000 24.75597  ? 338  THR A CA  1 
ATOM   1049 C  C   . THR A 1 135 ? 0.01194   10.53437 12.00264  1.000 23.92449  ? 338  THR A C   1 
ATOM   1050 O  O   . THR A 1 135 ? 1.05553   11.17205 11.88368  1.000 25.05641  ? 338  THR A O   1 
ATOM   1051 C  CB  . THR A 1 135 ? -0.41182  8.37286  10.85393  1.000 27.88464  ? 338  THR A CB  1 
ATOM   1052 O  OG1 . THR A 1 135 ? 0.99943   8.14358  10.84892  1.000 26.51963  ? 338  THR A OG1 1 
ATOM   1053 C  CG2 . THR A 1 135 ? -1.02554  7.69200  9.63599   1.000 29.70882  ? 338  THR A CG2 1 
ATOM   1054 N  N   . GLU A 1 136 ? -0.59519  10.36481 13.17753  1.000 28.67061  ? 339  GLU A N   1 
ATOM   1055 C  CA  . GLU A 1 136 ? 0.02577   10.92705 14.37266  1.000 31.74941  ? 339  GLU A CA  1 
ATOM   1056 C  C   . GLU A 1 136 ? 1.42429   10.35418 14.59130  1.000 29.75572  ? 339  GLU A C   1 
ATOM   1057 O  O   . GLU A 1 136 ? 2.35220   11.09471 14.95011  1.000 29.25321  ? 339  GLU A O   1 
ATOM   1058 C  CB  . GLU A 1 136 ? -0.86837  10.69788 15.59055  1.000 38.75879  ? 339  GLU A CB  1 
ATOM   1059 C  CG  . GLU A 1 136 ? -2.14268  11.54406 15.55421  1.000 44.36105  ? 339  GLU A CG  1 
ATOM   1060 C  CD  . GLU A 1 136 ? -1.86390  13.03899 15.44302  1.000 51.90091  ? 339  GLU A CD  1 
ATOM   1061 O  OE1 . GLU A 1 136 ? -1.26743  13.60801 16.38292  1.000 51.00056  ? 339  GLU A OE1 1 
ATOM   1062 O  OE2 . GLU A 1 136 ? -2.23313  13.64802 14.41018  1.000 49.96058  ? 339  GLU A OE2 1 
ATOM   1063 N  N   . ASN A 1 137 ? 1.60343   9.05245  14.34153  1.000 26.74112  ? 340  ASN A N   1 
ATOM   1064 C  CA  . ASN A 1 137 ? 2.92033   8.43525  14.47348  1.000 32.44193  ? 340  ASN A CA  1 
ATOM   1065 C  C   . ASN A 1 137 ? 3.93982   8.99678  13.49233  1.000 33.79423  ? 340  ASN A C   1 
ATOM   1066 O  O   . ASN A 1 137 ? 5.14302   8.86849  13.73560  1.000 31.53655  ? 340  ASN A O   1 
ATOM   1067 C  CB  . ASN A 1 137 ? 2.83562   6.91991  14.28253  1.000 31.53948  ? 340  ASN A CB  1 
ATOM   1068 C  CG  . ASN A 1 137 ? 2.20227   6.22500  15.45635  1.000 45.05561  ? 340  ASN A CG  1 
ATOM   1069 O  OD1 . ASN A 1 137 ? 2.05466   6.81167  16.53160  1.000 48.00336  ? 340  ASN A OD1 1 
ATOM   1070 N  ND2 . ASN A 1 137 ? 1.83221   4.96105  15.26816  1.000 46.54482  ? 340  ASN A ND2 1 
ATOM   1071 N  N   . GLN A 1 138 ? 3.50047   9.60102  12.38980  1.000 24.36885  ? 341  GLN A N   1 
ATOM   1072 C  CA  . GLN A 1 138 ? 4.42667   10.14834 11.40498  1.000 23.64876  ? 341  GLN A CA  1 
ATOM   1073 C  C   . GLN A 1 138 ? 4.78690   11.60845 11.65257  1.000 26.01019  ? 341  GLN A C   1 
ATOM   1074 O  O   . GLN A 1 138 ? 5.59313   12.15654 10.89379  1.000 22.85732  ? 341  GLN A O   1 
ATOM   1075 C  CB  . GLN A 1 138 ? 3.85015   10.01010 9.98082   1.000 20.23865  ? 341  GLN A CB  1 
ATOM   1076 C  CG  . GLN A 1 138 ? 3.82829   8.55748  9.47873   1.000 24.37293  ? 341  GLN A CG  1 
ATOM   1077 C  CD  . GLN A 1 138 ? 2.81761   8.32422  8.36555   1.000 26.85643  ? 341  GLN A CD  1 
ATOM   1078 O  OE1 . GLN A 1 138 ? 2.25015   9.27306  7.81934   1.000 22.30142  ? 341  GLN A OE1 1 
ATOM   1079 N  NE2 . GLN A 1 138 ? 2.58093   7.04705  8.02887   1.000 21.06457  ? 341  GLN A NE2 1 
ATOM   1080 N  N   . LYS A 1 139 ? 4.21981   12.25074 12.67849  1.000 23.17717  ? 342  LYS A N   1 
ATOM   1081 C  CA  . LYS A 1 139 ? 4.46952   13.66173 12.95249  1.000 22.74194  ? 342  LYS A CA  1 
ATOM   1082 C  C   . LYS A 1 139 ? 5.52214   13.76270 14.04745  1.000 25.44322  ? 342  LYS A C   1 
ATOM   1083 O  O   . LYS A 1 139 ? 5.34309   13.20196 15.13158  1.000 30.76052  ? 342  LYS A O   1 
ATOM   1084 C  CB  . LYS A 1 139 ? 3.19697   14.37868 13.38980  1.000 23.78111  ? 342  LYS A CB  1 
ATOM   1085 C  CG  . LYS A 1 139 ? 2.08052   14.42261 12.36183  1.000 24.52373  ? 342  LYS A CG  1 
ATOM   1086 C  CD  . LYS A 1 139 ? 0.91031   15.17311 12.97865  1.000 30.25968  ? 342  LYS A CD  1 
ATOM   1087 C  CE  . LYS A 1 139 ? -0.20822  15.40815 11.99132  1.000 37.61750  ? 342  LYS A CE  1 
ATOM   1088 N  NZ  . LYS A 1 139 ? -1.30700  16.14032 12.68735  1.000 37.22859  ? 342  LYS A NZ  1 
ATOM   1089 N  N   . ILE A 1 140 ? 6.61832   14.45343 13.76412  1.000 22.19684  ? 343  ILE A N   1 
ATOM   1090 C  CA  . ILE A 1 140 ? 7.74778   14.53182 14.68913  1.000 23.15383  ? 343  ILE A CA  1 
ATOM   1091 C  C   . ILE A 1 140 ? 7.87987   15.97479 15.16113  1.000 20.88489  ? 343  ILE A C   1 
ATOM   1092 O  O   . ILE A 1 140 ? 8.14313   16.87247 14.35639  1.000 22.57133  ? 343  ILE A O   1 
ATOM   1093 C  CB  . ILE A 1 140 ? 9.05557   14.05217 14.03418  1.000 23.07066  ? 343  ILE A CB  1 
ATOM   1094 C  CG1 . ILE A 1 140 ? 8.86859   12.69335 13.33067  1.000 22.94069  ? 343  ILE A CG1 1 
ATOM   1095 C  CG2 . ILE A 1 140 ? 10.17034  14.00313 15.07477  1.000 29.21721  ? 343  ILE A CG2 1 
ATOM   1096 C  CD1 . ILE A 1 140 ? 8.36354   11.57408 14.21223  1.000 30.57592  ? 343  ILE A CD1 1 
ATOM   1097 N  N   . LYS A 1 141 ? 7.74893   16.18944 16.47473  1.000 22.67019  ? 344  LYS A N   1 
ATOM   1098 C  CA  . LYS A 1 141 ? 7.92353   17.53945 17.00644  1.000 25.60611  ? 344  LYS A CA  1 
ATOM   1099 C  C   . LYS A 1 141 ? 9.39646   17.94264 16.96996  1.000 26.61999  ? 344  LYS A C   1 
ATOM   1100 O  O   . LYS A 1 141 ? 10.29436  17.09694 16.86079  1.000 27.99023  ? 344  LYS A O   1 
ATOM   1101 C  CB  . LYS A 1 141 ? 7.38349   17.61385 18.43379  1.000 28.35295  ? 344  LYS A CB  1 
ATOM   1102 C  CG  . LYS A 1 141 ? 5.94279   17.15406 18.54669  1.000 33.34667  ? 344  LYS A CG  1 
ATOM   1103 C  CD  . LYS A 1 141 ? 5.26304   17.77566 19.76109  1.000 47.54267  ? 344  LYS A CD  1 
ATOM   1104 C  CE  . LYS A 1 141 ? 4.11331   16.92448 20.27240  1.000 44.74474  ? 344  LYS A CE  1 
ATOM   1105 N  NZ  . LYS A 1 141 ? 3.21891   16.43195 19.18719  1.000 57.74024  ? 344  LYS A NZ  1 
ATOM   1106 N  N   . MET A 1 142 ? 9.64500   19.25577 17.09622  1.000 24.35735  ? 345  MET A N   1 
ATOM   1107 C  CA  . MET A 1 142 ? 10.95888  19.83107 16.84447  1.000 26.98945  ? 345  MET A CA  1 
ATOM   1108 C  C   . MET A 1 142 ? 11.45733  20.63420 18.03211  1.000 27.12393  ? 345  MET A C   1 
ATOM   1109 O  O   . MET A 1 142 ? 10.71155  21.42199 18.62583  1.000 25.78351  ? 345  MET A O   1 
ATOM   1110 C  CB  . MET A 1 142 ? 10.93578  20.74061 15.60719  1.000 23.85796  ? 345  MET A CB  1 
ATOM   1111 C  CG  . MET A 1 142 ? 10.76922  19.94641 14.34327  1.000 22.54641  ? 345  MET A CG  1 
ATOM   1112 S  SD  . MET A 1 142 ? 10.44235  21.01120 12.93375  1.000 27.02865  ? 345  MET A SD  1 
ATOM   1113 C  CE  . MET A 1 142 ? 12.11381  21.51875 12.52068  1.000 33.48102  ? 345  MET A CE  1 
ATOM   1114 N  N   . LYS A 1 143 ? 12.72903  20.43403 18.34885  1.000 28.42463  ? 346  LYS A N   1 
ATOM   1115 C  CA  . LYS A 1 143 ? 13.38088  21.21044 19.38679  1.000 33.13253  ? 346  LYS A CA  1 
ATOM   1116 C  C   . LYS A 1 143 ? 13.77553  22.58820 18.86819  1.000 34.54653  ? 346  LYS A C   1 
ATOM   1117 O  O   . LYS A 1 143 ? 14.13619  22.76877 17.70098  1.000 33.23151  ? 346  LYS A O   1 
ATOM   1118 C  CB  . LYS A 1 143 ? 14.61230  20.47198 19.91398  1.000 35.57196  ? 346  LYS A CB  1 
ATOM   1119 C  CG  . LYS A 1 143 ? 14.28057  19.41214 20.96359  1.000 41.14294  ? 346  LYS A CG  1 
ATOM   1120 C  CD  . LYS A 1 143 ? 15.49717  18.60968 21.36812  1.000 53.69177  ? 346  LYS A CD  1 
ATOM   1121 C  CE  . LYS A 1 143 ? 15.20982  17.78199 22.61375  1.000 54.43214  ? 346  LYS A CE  1 
ATOM   1122 N  NZ  . LYS A 1 143 ? 16.17508  16.65419 22.76300  1.000 62.96336  ? 346  LYS A NZ  1 
ATOM   1123 N  N   . ILE A 1 144 ? 13.70592  23.55983 19.75833  1.000 35.92361  ? 347  ILE A N   1 
ATOM   1124 C  CA  . ILE A 1 144 ? 14.14429  24.91389 19.45393  1.000 38.22096  ? 347  ILE A CA  1 
ATOM   1125 C  C   . ILE A 1 144 ? 15.66105  24.96841 19.55881  1.000 48.50170  ? 347  ILE A C   1 
ATOM   1126 O  O   . ILE A 1 144 ? 16.25128  24.42222 20.49858  1.000 45.66586  ? 347  ILE A O   1 
ATOM   1127 C  CB  . ILE A 1 144 ? 13.47275  25.91284 20.40088  1.000 34.28600  ? 347  ILE A CB  1 
ATOM   1128 C  CG1 . ILE A 1 144 ? 11.95868  25.83131 20.21588  1.000 32.23990  ? 347  ILE A CG1 1 
ATOM   1129 C  CG2 . ILE A 1 144 ? 14.01340  27.32054 20.18213  1.000 38.16765  ? 347  ILE A CG2 1 
ATOM   1130 C  CD1 . ILE A 1 144 ? 11.16520  26.60496 21.20767  1.000 34.07405  ? 347  ILE A CD1 1 
ATOM   1131 N  N   . LYS A 1 145 ? 16.29801  25.58588 18.57092  1.000 50.36626  ? 348  LYS A N   1 
ATOM   1132 C  CA  . LYS A 1 145 ? 17.74107  25.75061 18.55734  1.000 51.15516  ? 348  LYS A CA  1 
ATOM   1133 C  C   . LYS A 1 145 ? 18.11051  27.14789 19.02899  1.000 63.62054  ? 348  LYS A C   1 
ATOM   1134 O  O   . LYS A 1 145 ? 17.34341  28.10342 18.87567  1.000 54.93886  ? 348  LYS A O   1 
ATOM   1135 C  CB  . LYS A 1 145 ? 18.32300  25.51974 17.15940  1.000 51.78749  ? 348  LYS A CB  1 
ATOM   1136 C  CG  . LYS A 1 145 ? 18.39068  24.06949 16.72712  1.000 57.29306  ? 348  LYS A CG  1 
ATOM   1137 C  CD  . LYS A 1 145 ? 19.08606  23.92947 15.38319  1.000 49.64188  ? 348  LYS A CD  1 
ATOM   1138 C  CE  . LYS A 1 145 ? 19.00726  22.50348 14.88248  1.000 57.74343  ? 348  LYS A CE  1 
ATOM   1139 N  NZ  . LYS A 1 145 ? 17.59288  22.05085 14.81941  1.000 60.44056  ? 348  LYS A NZ  1 
ATOM   1140 N  N   A ASN A 1 146 ? 19.30469  27.25545 19.60435  0.537 66.08547  ? 349  ASN A N   1 
ATOM   1141 N  N   B ASN A 1 146 ? 19.29285  27.25264 19.63052  0.463 66.08599  ? 349  ASN A N   1 
ATOM   1142 C  CA  A ASN A 1 146 ? 19.87171  28.53933 19.99417  0.537 69.86442  ? 349  ASN A CA  1 
ATOM   1143 C  CA  B ASN A 1 146 ? 19.87601  28.53798 19.99693  0.463 69.85678  ? 349  ASN A CA  1 
ATOM   1144 C  C   A ASN A 1 146 ? 21.36011  28.49468 19.69321  0.537 73.24798  ? 349  ASN A C   1 
ATOM   1145 C  C   B ASN A 1 146 ? 21.35923  28.48227 19.67711  0.463 73.23649  ? 349  ASN A C   1 
ATOM   1146 O  O   A ASN A 1 146 ? 22.06584  27.61109 20.19022  0.537 72.66906  ? 349  ASN A O   1 
ATOM   1147 O  O   B ASN A 1 146 ? 22.06129  27.58416 20.15252  0.463 72.65738  ? 349  ASN A O   1 
ATOM   1148 C  CB  A ASN A 1 146 ? 19.61693  28.83680 21.47461  0.537 67.63369  ? 349  ASN A CB  1 
ATOM   1149 C  CB  B ASN A 1 146 ? 19.65146  28.86614 21.47685  0.463 67.64633  ? 349  ASN A CB  1 
ATOM   1150 C  CG  A ASN A 1 146 ? 19.66792  30.31705 21.78616  0.537 67.86513  ? 349  ASN A CG  1 
ATOM   1151 C  CG  B ASN A 1 146 ? 18.29272  29.48722 21.73705  0.463 67.90646  ? 349  ASN A CG  1 
ATOM   1152 O  OD1 A ASN A 1 146 ? 20.06996  30.72164 22.87744  0.537 67.00360  ? 349  ASN A OD1 1 
ATOM   1153 O  OD1 B ASN A 1 146 ? 17.70957  29.30983 22.80790  0.463 63.88229  ? 349  ASN A OD1 1 
ATOM   1154 N  ND2 A ASN A 1 146 ? 19.26292  31.13713 20.82186  0.537 67.15259  ? 349  ASN A ND2 1 
ATOM   1155 N  ND2 B ASN A 1 146 ? 17.77906  30.21916 20.75322  0.463 64.46431  ? 349  ASN A ND2 1 
ATOM   1156 N  N   . ASN A 1 147 ? 21.82448  29.43099 18.86376  1.000 79.28902  ? 350  ASN A N   1 
ATOM   1157 C  CA  . ASN A 1 147 ? 23.21983  29.47652 18.42375  1.000 79.14714  ? 350  ASN A CA  1 
ATOM   1158 C  C   . ASN A 1 147 ? 23.64020  28.15069 17.79249  1.000 83.89989  ? 350  ASN A C   1 
ATOM   1159 O  O   . ASN A 1 147 ? 24.75162  27.65899 18.00146  1.000 85.57250  ? 350  ASN A O   1 
ATOM   1160 C  CB  . ASN A 1 147 ? 24.14662  29.86109 19.57854  1.000 82.67343  ? 350  ASN A CB  1 
ATOM   1161 C  CG  . ASN A 1 147 ? 23.71819  31.14739 20.26160  1.000 87.14045  ? 350  ASN A CG  1 
ATOM   1162 O  OD1 . ASN A 1 147 ? 22.74790  31.16622 21.02093  1.000 84.92598  ? 350  ASN A OD1 1 
ATOM   1163 N  ND2 . ASN A 1 147 ? 24.44276  32.23145 19.99582  1.000 91.08887  ? 350  ASN A ND2 1 
ATOM   1164 N  N   . GLY A 1 148 ? 22.72972  27.56049 17.01850  1.000 79.83022  ? 351  GLY A N   1 
ATOM   1165 C  CA  . GLY A 1 148 ? 22.99092  26.30380 16.34709  1.000 77.82273  ? 351  GLY A CA  1 
ATOM   1166 C  C   . GLY A 1 148 ? 22.95200  25.07672 17.22800  1.000 73.56837  ? 351  GLY A C   1 
ATOM   1167 O  O   . GLY A 1 148 ? 23.25756  23.98081 16.74524  1.000 75.43972  ? 351  GLY A O   1 
ATOM   1168 N  N   . ILE A 1 149 ? 22.58766  25.21941 18.49998  1.000 76.00423  ? 352  ILE A N   1 
ATOM   1169 C  CA  . ILE A 1 149 ? 22.54076  24.10977 19.44487  1.000 74.65579  ? 352  ILE A CA  1 
ATOM   1170 C  C   . ILE A 1 149 ? 21.09415  23.89458 19.86037  1.000 66.18008  ? 352  ILE A C   1 
ATOM   1171 O  O   . ILE A 1 149 ? 20.40251  24.84908 20.23867  1.000 60.75586  ? 352  ILE A O   1 
ATOM   1172 C  CB  . ILE A 1 149 ? 23.42848  24.37536 20.67288  1.000 69.24448  ? 352  ILE A CB  1 
ATOM   1173 N  N   . GLU A 1 150 ? 20.63482  22.64602 19.77927  1.000 67.28234  ? 353  GLU A N   1 
ATOM   1174 C  CA  . GLU A 1 150 ? 19.30304  22.31383 20.26684  1.000 61.58019  ? 353  GLU A CA  1 
ATOM   1175 C  C   . GLU A 1 150 ? 19.20148  22.60897 21.75796  1.000 58.81114  ? 353  GLU A C   1 
ATOM   1176 O  O   . GLU A 1 150 ? 20.04288  22.17402 22.54910  1.000 65.39671  ? 353  GLU A O   1 
ATOM   1177 C  CB  . GLU A 1 150 ? 18.98651  20.84025 20.00299  1.000 65.99309  ? 353  GLU A CB  1 
ATOM   1178 C  CG  . GLU A 1 150 ? 18.51632  20.51810 18.58891  1.000 60.18533  ? 353  GLU A CG  1 
ATOM   1179 C  CD  . GLU A 1 150 ? 18.13460  19.05602 18.42733  1.000 72.60035  ? 353  GLU A CD  1 
ATOM   1180 O  OE1 . GLU A 1 150 ? 18.38123  18.27213 19.37096  1.000 76.28751  ? 353  GLU A OE1 1 
ATOM   1181 O  OE2 . GLU A 1 150 ? 17.58711  18.68996 17.36237  1.000 63.52300  ? 353  GLU A OE2 1 
ATOM   1182 N  N   . THR A 1 151 ? 18.18219  23.36979 22.13938  1.000 55.75754  ? 354  THR A N   1 
ATOM   1183 C  CA  . THR A 1 151 ? 17.86367  23.51820 23.54839  1.000 54.81761  ? 354  THR A CA  1 
ATOM   1184 C  C   . THR A 1 151 ? 17.00907  22.33515 23.99701  1.000 58.88777  ? 354  THR A C   1 
ATOM   1185 O  O   . THR A 1 151 ? 16.73240  21.40436 23.23300  1.000 52.88456  ? 354  THR A O   1 
ATOM   1186 C  CB  . THR A 1 151 ? 17.14399  24.83993 23.80808  1.000 52.69001  ? 354  THR A CB  1 
ATOM   1187 O  OG1 . THR A 1 151 ? 15.74687  24.69799 23.51985  1.000 55.30221  ? 354  THR A OG1 1 
ATOM   1188 C  CG2 . THR A 1 151 ? 17.72180  25.94340 22.93428  1.000 59.90080  ? 354  THR A CG2 1 
ATOM   1189 N  N   . GLU A 1 152 ? 16.58093  22.36291 25.25296  1.000 58.52351  ? 355  GLU A N   1 
ATOM   1190 C  CA  . GLU A 1 152 ? 15.65803  21.35544 25.75399  1.000 56.99299  ? 355  GLU A CA  1 
ATOM   1191 C  C   . GLU A 1 152 ? 14.20387  21.71245 25.47589  1.000 47.59647  ? 355  GLU A C   1 
ATOM   1192 O  O   . GLU A 1 152 ? 13.31180  20.92032 25.79473  1.000 42.13642  ? 355  GLU A O   1 
ATOM   1193 C  CB  . GLU A 1 152 ? 15.87940  21.14273 27.25565  1.000 55.79355  ? 355  GLU A CB  1 
ATOM   1194 C  CG  . GLU A 1 152 ? 17.23844  20.54251 27.58135  1.000 64.49691  ? 355  GLU A CG  1 
ATOM   1195 C  CD  . GLU A 1 152 ? 17.57225  20.60534 29.06120  1.000 79.68161  ? 355  GLU A CD  1 
ATOM   1196 O  OE1 . GLU A 1 152 ? 17.17627  21.59033 29.72327  1.000 83.76899  ? 355  GLU A OE1 1 
ATOM   1197 O  OE2 . GLU A 1 152 ? 18.22844  19.66556 29.56154  1.000 81.06035  ? 355  GLU A OE2 1 
ATOM   1198 N  N   . ASP A 1 153 ? 13.95104  22.86351 24.86279  1.000 42.87391  ? 356  ASP A N   1 
ATOM   1199 C  CA  . ASP A 1 153 ? 12.60162  23.31356 24.56662  1.000 33.22441  ? 356  ASP A CA  1 
ATOM   1200 C  C   . ASP A 1 153 ? 12.15989  22.84727 23.18030  1.000 36.86111  ? 356  ASP A C   1 
ATOM   1201 O  O   . ASP A 1 153 ? 12.98150  22.62391 22.28802  1.000 38.73306  ? 356  ASP A O   1 
ATOM   1202 C  CB  . ASP A 1 153 ? 12.52328  24.83707 24.64366  1.000 34.78958  ? 356  ASP A CB  1 
ATOM   1203 C  CG  . ASP A 1 153 ? 12.82297  25.34941 26.03612  1.000 48.66062  ? 356  ASP A CG  1 
ATOM   1204 O  OD1 . ASP A 1 153 ? 12.27572  24.76509 27.00301  1.000 44.81952  ? 356  ASP A OD1 1 
ATOM   1205 O  OD2 . ASP A 1 153 ? 13.62175  26.30317 26.16372  1.000 48.04283  ? 356  ASP A OD2 1 
ATOM   1206 N  N   . TYR A 1 154 ? 10.84618  22.71060 23.01357  1.000 32.73935  ? 357  TYR A N   1 
ATOM   1207 C  CA  . TYR A 1 154 ? 10.23715  22.27490 21.75957  1.000 33.41643  ? 357  TYR A CA  1 
ATOM   1208 C  C   . TYR A 1 154 ? 9.26906   23.34059 21.26277  1.000 31.31813  ? 357  TYR A C   1 
ATOM   1209 O  O   . TYR A 1 154 ? 8.68745   24.09108 22.05455  1.000 33.02274  ? 357  TYR A O   1 
ATOM   1210 C  CB  . TYR A 1 154 ? 9.46573   20.94284 21.93255  1.000 32.81072  ? 357  TYR A CB  1 
ATOM   1211 C  CG  . TYR A 1 154 ? 10.28228  19.66580 21.94440  1.000 33.54935  ? 357  TYR A CG  1 
ATOM   1212 C  CD1 . TYR A 1 154 ? 10.87259  19.19504 23.11342  1.000 39.32881  ? 357  TYR A CD1 1 
ATOM   1213 C  CD2 . TYR A 1 154 ? 10.42639  18.90637 20.78792  1.000 33.96053  ? 357  TYR A CD2 1 
ATOM   1214 C  CE1 . TYR A 1 154 ? 11.60307  18.00547 23.11128  1.000 40.09076  ? 357  TYR A CE1 1 
ATOM   1215 C  CE2 . TYR A 1 154 ? 11.15047  17.72975 20.77692  1.000 35.35257  ? 357  TYR A CE2 1 
ATOM   1216 C  CZ  . TYR A 1 154 ? 11.73768  17.28438 21.93777  1.000 38.73166  ? 357  TYR A CZ  1 
ATOM   1217 O  OH  . TYR A 1 154 ? 12.45897  16.10307 21.92093  1.000 44.51411  ? 357  TYR A OH  1 
ATOM   1218 N  N   . PHE A 1 155 ? 9.09162   23.42073 19.94060  1.000 26.44240  ? 358  PHE A N   1 
ATOM   1219 C  CA  . PHE A 1 155 ? 8.02799   24.26174 19.40981  1.000 26.53995  ? 358  PHE A CA  1 
ATOM   1220 C  C   . PHE A 1 155 ? 6.68870   23.63534 19.75941  1.000 31.50541  ? 358  PHE A C   1 
ATOM   1221 O  O   . PHE A 1 155 ? 6.48508   22.43425 19.54428  1.000 33.15713  ? 358  PHE A O   1 
ATOM   1222 C  CB  . PHE A 1 155 ? 8.15729   24.42812 17.88817  1.000 29.42183  ? 358  PHE A CB  1 
ATOM   1223 C  CG  . PHE A 1 155 ? 9.32254   25.27623 17.46850  1.000 25.17618  ? 358  PHE A CG  1 
ATOM   1224 C  CD1 . PHE A 1 155 ? 9.26270   26.66020 17.57604  1.000 25.87066  ? 358  PHE A CD1 1 
ATOM   1225 C  CD2 . PHE A 1 155 ? 10.48787  24.68770 17.00199  1.000 28.70594  ? 358  PHE A CD2 1 
ATOM   1226 C  CE1 . PHE A 1 155 ? 10.34176  27.44151 17.18907  1.000 24.15829  ? 358  PHE A CE1 1 
ATOM   1227 C  CE2 . PHE A 1 155 ? 11.57090  25.45865 16.62414  1.000 26.80636  ? 358  PHE A CE2 1 
ATOM   1228 C  CZ  . PHE A 1 155 ? 11.50555  26.83923 16.74026  1.000 23.55407  ? 358  PHE A CZ  1 
ATOM   1229 N  N   . THR A 1 156 ? 5.77025   24.44360 20.28901  1.000 32.97534  ? 359  THR A N   1 
ATOM   1230 C  CA  . THR A 1 156 ? 4.52580   23.91491 20.83482  1.000 35.24215  ? 359  THR A CA  1 
ATOM   1231 C  C   . THR A 1 156 ? 3.31406   24.13840 19.93461  1.000 32.93133  ? 359  THR A C   1 
ATOM   1232 O  O   . THR A 1 156 ? 2.26201   23.54098 20.19431  1.000 38.89024  ? 359  THR A O   1 
ATOM   1233 C  CB  . THR A 1 156 ? 4.25302   24.51614 22.23303  1.000 35.01502  ? 359  THR A CB  1 
ATOM   1234 O  OG1 . THR A 1 156 ? 3.99825   25.92016 22.11487  1.000 38.21483  ? 359  THR A OG1 1 
ATOM   1235 C  CG2 . THR A 1 156 ? 5.44925   24.29383 23.13645  1.000 39.99339  ? 359  THR A CG2 1 
ATOM   1236 N  N   . ASP A 1 157 ? 3.43382   24.93673 18.87355  1.000 33.50502  ? 360  ASP A N   1 
ATOM   1237 C  CA  . ASP A 1 157 ? 2.29582   25.13080 17.98387  1.000 35.67892  ? 360  ASP A CA  1 
ATOM   1238 C  C   . ASP A 1 157 ? 1.95916   23.79689 17.31372  1.000 32.13809  ? 360  ASP A C   1 
ATOM   1239 O  O   . ASP A 1 157 ? 2.86886   23.04842 16.93318  1.000 29.78548  ? 360  ASP A O   1 
ATOM   1240 C  CB  . ASP A 1 157 ? 2.58726   26.20282 16.92789  1.000 34.42440  ? 360  ASP A CB  1 
ATOM   1241 C  CG  . ASP A 1 157 ? 2.39392   27.63006 17.45363  1.000 42.25860  ? 360  ASP A CG  1 
ATOM   1242 O  OD1 . ASP A 1 157 ? 1.92687   27.78930 18.60353  1.000 52.37670  ? 360  ASP A OD1 1 
ATOM   1243 O  OD2 . ASP A 1 157 ? 2.70754   28.58949 16.71301  1.000 41.60661  ? 360  ASP A OD2 1 
ATOM   1244 N  N   . PRO A 1 158 ? 0.67426   23.44686 17.19288  1.000 34.64110  ? 361  PRO A N   1 
ATOM   1245 C  CA  . PRO A 1 158 ? 0.33121   22.07658 16.77456  1.000 29.35122  ? 361  PRO A CA  1 
ATOM   1246 C  C   . PRO A 1 158 ? 0.70187   21.76263 15.33734  1.000 27.61546  ? 361  PRO A C   1 
ATOM   1247 O  O   . PRO A 1 158 ? 0.83395   20.57837 15.00039  1.000 27.77744  ? 361  PRO A O   1 
ATOM   1248 C  CB  . PRO A 1 158 ? -1.18934  22.00081 16.98496  1.000 33.83337  ? 361  PRO A CB  1 
ATOM   1249 C  CG  . PRO A 1 158 ? -1.65776  23.40524 17.01428  1.000 31.97516  ? 361  PRO A CG  1 
ATOM   1250 C  CD  . PRO A 1 158 ? -0.51660  24.24516 17.53421  1.000 34.33284  ? 361  PRO A CD  1 
ATOM   1251 N  N   . PHE A 1 159 ? 0.87173   22.76841 14.49356  1.000 26.64542  ? 362  PHE A N   1 
ATOM   1252 C  CA  . PHE A 1 159 ? 1.25536   22.56436 13.10393  1.000 23.25850  ? 362  PHE A CA  1 
ATOM   1253 C  C   . PHE A 1 159 ? 2.75907   22.44012 12.92540  1.000 23.36847  ? 362  PHE A C   1 
ATOM   1254 O  O   . PHE A 1 159 ? 3.22731   22.20574 11.80500  1.000 22.43395  ? 362  PHE A O   1 
ATOM   1255 C  CB  . PHE A 1 159 ? 0.73290   23.72461 12.23530  1.000 21.82353  ? 362  PHE A CB  1 
ATOM   1256 C  CG  . PHE A 1 159 ? 1.17661   25.09128 12.71771  1.000 27.02806  ? 362  PHE A CG  1 
ATOM   1257 C  CD1 . PHE A 1 159 ? 2.38194   25.62672 12.30367  1.000 25.89819  ? 362  PHE A CD1 1 
ATOM   1258 C  CD2 . PHE A 1 159 ? 0.39381   25.81612 13.61454  1.000 30.38619  ? 362  PHE A CD2 1 
ATOM   1259 C  CE1 . PHE A 1 159 ? 2.79694   26.88054 12.75458  1.000 32.73111  ? 362  PHE A CE1 1 
ATOM   1260 C  CE2 . PHE A 1 159 ? 0.80323   27.07233 14.06737  1.000 31.11786  ? 362  PHE A CE2 1 
ATOM   1261 C  CZ  . PHE A 1 159 ? 2.00540   27.59815 13.63824  1.000 30.47200  ? 362  PHE A CZ  1 
ATOM   1262 N  N   . VAL A 1 160 ? 3.54665   22.61275 13.98319  1.000 23.99366  ? 363  VAL A N   1 
ATOM   1263 C  CA  . VAL A 1 160 ? 4.99797   22.56174 13.83932  1.000 22.21358  ? 363  VAL A CA  1 
ATOM   1264 C  C   . VAL A 1 160 ? 5.39661   21.10234 14.03595  1.000 21.97334  ? 363  VAL A C   1 
ATOM   1265 O  O   . VAL A 1 160 ? 5.58537   20.62367 15.15961  1.000 22.43720  ? 363  VAL A O   1 
ATOM   1266 C  CB  . VAL A 1 160 ? 5.71281   23.49899 14.80415  1.000 24.53095  ? 363  VAL A CB  1 
ATOM   1267 C  CG1 . VAL A 1 160 ? 7.19534   23.49505 14.47123  1.000 23.72472  ? 363  VAL A CG1 1 
ATOM   1268 C  CG2 . VAL A 1 160 ? 5.12938   24.91800 14.68977  1.000 22.84372  ? 363  VAL A CG2 1 
ATOM   1269 N  N   . PHE A 1 161 ? 5.48039   20.37093 12.92354  1.000 20.12518  ? 364  PHE A N   1 
ATOM   1270 C  CA  . PHE A 1 161 ? 5.96791   19.00005 12.94386  1.000 20.36677  ? 364  PHE A CA  1 
ATOM   1271 C  C   . PHE A 1 161 ? 6.67208   18.70570 11.62880  1.000 19.07053  ? 364  PHE A C   1 
ATOM   1272 O  O   . PHE A 1 161 ? 6.34394   19.28397 10.58270  1.000 20.74197  ? 364  PHE A O   1 
ATOM   1273 C  CB  . PHE A 1 161 ? 4.83709   17.96976 13.14856  1.000 20.33205  ? 364  PHE A CB  1 
ATOM   1274 C  CG  . PHE A 1 161 ? 3.71013   18.08292 12.13158  1.000 20.77585  ? 364  PHE A CG  1 
ATOM   1275 C  CD1 . PHE A 1 161 ? 3.77444   17.41021 10.91699  1.000 20.51110  ? 364  PHE A CD1 1 
ATOM   1276 C  CD2 . PHE A 1 161 ? 2.57855   18.84565 12.40531  1.000 21.57018  ? 364  PHE A CD2 1 
ATOM   1277 C  CE1 . PHE A 1 161 ? 2.73247   17.49241 10.00160  1.000 21.32061  ? 364  PHE A CE1 1 
ATOM   1278 C  CE2 . PHE A 1 161 ? 1.53547   18.95540 11.48471  1.000 21.88938  ? 364  PHE A CE2 1 
ATOM   1279 C  CZ  . PHE A 1 161 ? 1.61672   18.27548 10.27068  1.000 21.59711  ? 364  PHE A CZ  1 
ATOM   1280 N  N   . LYS A 1 162 ? 7.64273   17.79648 11.69565  1.000 19.85401  ? 365  LYS A N   1 
ATOM   1281 C  CA  . LYS A 1 162 ? 8.17016   17.16238 10.49817  1.000 22.08031  ? 365  LYS A CA  1 
ATOM   1282 C  C   . LYS A 1 162 ? 7.26643   15.99777 10.13820  1.000 20.57345  ? 365  LYS A C   1 
ATOM   1283 O  O   . LYS A 1 162 ? 6.74543   15.31966 11.02355  1.000 20.63015  ? 365  LYS A O   1 
ATOM   1284 C  CB  . LYS A 1 162 ? 9.59145   16.66364 10.74035  1.000 21.69575  ? 365  LYS A CB  1 
ATOM   1285 C  CG  . LYS A 1 162 ? 10.52629  17.78990 11.15142  1.000 23.82812  ? 365  LYS A CG  1 
ATOM   1286 C  CD  . LYS A 1 162 ? 11.92754  17.31388 11.49505  1.000 23.63194  ? 365  LYS A CD  1 
ATOM   1287 C  CE  . LYS A 1 162 ? 11.99847  16.63181 12.83800  1.000 34.19710  ? 365  LYS A CE  1 
ATOM   1288 N  NZ  . LYS A 1 162 ? 13.43625  16.48874 13.24721  1.000 37.26790  ? 365  LYS A NZ  1 
ATOM   1289 N  N   . TRP A 1 163 ? 7.03525   15.79984 8.83742   1.000 18.61722  ? 366  TRP A N   1 
ATOM   1290 C  CA  . TRP A 1 163 ? 6.31050   14.61984 8.36875   1.000 18.27028  ? 366  TRP A CA  1 
ATOM   1291 C  C   . TRP A 1 163 ? 7.36764   13.58614 7.98824   1.000 18.93692  ? 366  TRP A C   1 
ATOM   1292 O  O   . TRP A 1 163 ? 8.03405   13.72184 6.95872   1.000 18.79874  ? 366  TRP A O   1 
ATOM   1293 C  CB  . TRP A 1 163 ? 5.38481   14.95904 7.19401   1.000 20.12803  ? 366  TRP A CB  1 
ATOM   1294 C  CG  . TRP A 1 163 ? 4.48342   13.80325 6.77413   1.000 16.39666  ? 366  TRP A CG  1 
ATOM   1295 C  CD1 . TRP A 1 163 ? 4.45853   12.52832 7.30766   1.000 17.55086  ? 366  TRP A CD1 1 
ATOM   1296 C  CD2 . TRP A 1 163 ? 3.50552   13.80689 5.71719   1.000 17.80783  ? 366  TRP A CD2 1 
ATOM   1297 N  NE1 . TRP A 1 163 ? 3.52818   11.75579 6.64310   1.000 18.37923  ? 366  TRP A NE1 1 
ATOM   1298 C  CE2 . TRP A 1 163 ? 2.92473   12.51743 5.67295   1.000 18.00636  ? 366  TRP A CE2 1 
ATOM   1299 C  CE3 . TRP A 1 163 ? 3.05197   14.77850 4.82168   1.000 18.46871  ? 366  TRP A CE3 1 
ATOM   1300 C  CZ2 . TRP A 1 163 ? 1.92323   12.17006 4.75080   1.000 20.15081  ? 366  TRP A CZ2 1 
ATOM   1301 C  CZ3 . TRP A 1 163 ? 2.05134   14.43622 3.90761   1.000 21.86909  ? 366  TRP A CZ3 1 
ATOM   1302 C  CH2 . TRP A 1 163 ? 1.50160   13.14200 3.87244   1.000 19.79545  ? 366  TRP A CH2 1 
ATOM   1303 N  N   A LYS A 1 164 ? 7.51768   12.55936 8.82469   0.447 19.10386  ? 367  LYS A N   1 
ATOM   1304 N  N   B LYS A 1 164 ? 7.51854   12.56500 8.83143   0.553 19.09127  ? 367  LYS A N   1 
ATOM   1305 C  CA  A LYS A 1 164 ? 8.55993   11.56021 8.62898   0.447 19.06410  ? 367  LYS A CA  1 
ATOM   1306 C  CA  B LYS A 1 164 ? 8.53838   11.54680 8.62762   0.553 19.07384  ? 367  LYS A CA  1 
ATOM   1307 C  C   A LYS A 1 164 ? 8.19879   10.62273 7.48407   0.447 19.00192  ? 367  LYS A C   1 
ATOM   1308 C  C   B LYS A 1 164 ? 8.17265   10.66333 7.44317   0.553 18.98249  ? 367  LYS A C   1 
ATOM   1309 O  O   A LYS A 1 164 ? 7.08624   10.09307 7.43043   0.447 18.72026  ? 367  LYS A O   1 
ATOM   1310 O  O   B LYS A 1 164 ? 7.02777   10.22231 7.31619   0.553 18.80416  ? 367  LYS A O   1 
ATOM   1311 C  CB  A LYS A 1 164 ? 8.75535   10.76114 9.92050   0.447 21.45024  ? 367  LYS A CB  1 
ATOM   1312 C  CB  B LYS A 1 164 ? 8.67863   10.69739 9.89606   0.553 21.36843  ? 367  LYS A CB  1 
ATOM   1313 C  CG  A LYS A 1 164 ? 9.58547   9.50802  9.77613   0.447 27.77281  ? 367  LYS A CG  1 
ATOM   1314 C  CG  B LYS A 1 164 ? 9.67003   9.56479  9.79474   0.553 27.81849  ? 367  LYS A CG  1 
ATOM   1315 C  CD  A LYS A 1 164 ? 9.68932   8.78905  11.12190  0.447 27.46719  ? 367  LYS A CD  1 
ATOM   1316 C  CD  B LYS A 1 164 ? 9.81373   8.86437  11.14936  0.553 27.47187  ? 367  LYS A CD  1 
ATOM   1317 C  CE  A LYS A 1 164 ? 8.31391   8.40159  11.64989  0.447 25.80058  ? 367  LYS A CE  1 
ATOM   1318 C  CE  B LYS A 1 164 ? 10.76077  7.67632  11.06902  0.553 29.53899  ? 367  LYS A CE  1 
ATOM   1319 N  N   . GLU A 1 165 ? 9.14324   10.40969 6.57449   1.000 17.26581  ? 368  GLU A N   1 
ATOM   1320 C  CA  . GLU A 1 165 ? 8.96068   9.38745  5.55000   1.000 18.12626  ? 368  GLU A CA  1 
ATOM   1321 C  C   . GLU A 1 165 ? 9.05026   8.00034  6.18058   1.000 18.65089  ? 368  GLU A C   1 
ATOM   1322 O  O   . GLU A 1 165 ? 9.94152   7.72699  6.99994   1.000 19.11033  ? 368  GLU A O   1 
ATOM   1323 C  CB  . GLU A 1 165 ? 10.01577  9.52669  4.46267   1.000 18.12361  ? 368  GLU A CB  1 
ATOM   1324 C  CG  . GLU A 1 165 ? 9.86443   8.51037  3.34968   1.000 18.66811  ? 368  GLU A CG  1 
ATOM   1325 C  CD  . GLU A 1 165 ? 10.70483  8.90143  2.13250   1.000 18.47088  ? 368  GLU A CD  1 
ATOM   1326 O  OE1 . GLU A 1 165 ? 11.91849  8.60036  2.11314   1.000 23.11250  ? 368  GLU A OE1 1 
ATOM   1327 O  OE2 . GLU A 1 165 ? 10.12860  9.53259  1.22218   1.000 20.44871  ? 368  GLU A OE2 1 
ATOM   1328 N  N   . THR A 1 166 ? 8.11532   7.12961  5.80036   1.000 18.92560  ? 369  THR A N   1 
ATOM   1329 C  CA  . THR A 1 166 ? 8.11052   5.73506  6.22509   1.000 19.11111  ? 369  THR A CA  1 
ATOM   1330 C  C   . THR A 1 166 ? 7.79208   4.86547  5.01512   1.000 18.88291  ? 369  THR A C   1 
ATOM   1331 O  O   . THR A 1 166 ? 7.55742   5.35484  3.91130   1.000 19.32393  ? 369  THR A O   1 
ATOM   1332 C  CB  . THR A 1 166 ? 7.08102   5.46142  7.32302   1.000 22.19631  ? 369  THR A CB  1 
ATOM   1333 O  OG1 . THR A 1 166 ? 5.76813   5.44121  6.74577   1.000 22.44085  ? 369  THR A OG1 1 
ATOM   1334 C  CG2 . THR A 1 166 ? 7.15354   6.51295  8.42402   1.000 21.97033  ? 369  THR A CG2 1 
ATOM   1335 N  N   . ALA A 1 167 ? 7.76282   3.54582  5.23649   1.000 21.53235  ? 370  ALA A N   1 
ATOM   1336 C  CA  . ALA A 1 167 ? 7.35828   2.64348  4.17344   1.000 21.44115  ? 370  ALA A CA  1 
ATOM   1337 C  C   . ALA A 1 167 ? 5.97995   2.97990  3.62737   1.000 23.90328  ? 370  ALA A C   1 
ATOM   1338 O  O   . ALA A 1 167 ? 5.68178   2.65083  2.47471   1.000 24.03055  ? 370  ALA A O   1 
ATOM   1339 C  CB  . ALA A 1 167 ? 7.35672   1.19378  4.69059   1.000 20.45643  ? 370  ALA A CB  1 
ATOM   1340 N  N   . ASP A 1 168 ? 5.14584   3.63836  4.42309   1.000 21.83639  ? 371  ASP A N   1 
ATOM   1341 C  CA  . ASP A 1 168 ? 3.74074   3.83965  4.11673   1.000 20.97172  ? 371  ASP A CA  1 
ATOM   1342 C  C   . ASP A 1 168 ? 3.40834   5.23655  3.59788   1.000 22.20457  ? 371  ASP A C   1 
ATOM   1343 O  O   . ASP A 1 168 ? 2.24778   5.48454  3.26014   1.000 24.35590  ? 371  ASP A O   1 
ATOM   1344 C  CB  . ASP A 1 168 ? 2.90961   3.56324  5.37235   1.000 22.48497  ? 371  ASP A CB  1 
ATOM   1345 C  CG  . ASP A 1 168 ? 3.13956   2.15949  5.92218   1.000 27.57648  ? 371  ASP A CG  1 
ATOM   1346 O  OD1 . ASP A 1 168 ? 3.14451   1.22776  5.10206   1.000 30.84888  ? 371  ASP A OD1 1 
ATOM   1347 O  OD2 . ASP A 1 168 ? 3.34524   2.01979  7.14581   1.000 39.97748  ? 371  ASP A OD2 1 
ATOM   1348 N  N   . THR A 1 169 ? 4.36257   6.15993  3.55314   1.000 21.19394  ? 372  THR A N   1 
ATOM   1349 C  CA  . THR A 1 169 ? 4.01120   7.51838  3.14742   1.000 18.21729  ? 372  THR A CA  1 
ATOM   1350 C  C   . THR A 1 169 ? 4.10347   7.68006  1.63424   1.000 19.47888  ? 372  THR A C   1 
ATOM   1351 O  O   . THR A 1 169 ? 4.76553   6.90530  0.93827   1.000 21.26003  ? 372  THR A O   1 
ATOM   1352 C  CB  . THR A 1 169 ? 4.90727   8.55086  3.84141   1.000 17.61253  ? 372  THR A CB  1 
ATOM   1353 O  OG1 . THR A 1 169 ? 6.28768   8.24682  3.62387   1.000 16.14239  ? 372  THR A OG1 1 
ATOM   1354 C  CG2 . THR A 1 169 ? 4.63737   8.58624  5.35127   1.000 19.46989  ? 372  THR A CG2 1 
ATOM   1355 N  N   . LYS A 1 170 ? 3.42242   8.70471  1.11582   1.000 18.44091  ? 373  LYS A N   1 
ATOM   1356 C  CA  . LYS A 1 170 ? 3.23770   8.79706  -0.33247  1.000 16.38462  ? 373  LYS A CA  1 
ATOM   1357 C  C   . LYS A 1 170 ? 3.73266   10.10534 -0.93934  1.000 17.40103  ? 373  LYS A C   1 
ATOM   1358 O  O   . LYS A 1 170 ? 3.52742   10.32884 -2.14483  1.000 19.41852  ? 373  LYS A O   1 
ATOM   1359 C  CB  . LYS A 1 170 ? 1.76861   8.57818  -0.68164  1.000 20.34840  ? 373  LYS A CB  1 
ATOM   1360 C  CG  . LYS A 1 170 ? 1.30334   7.12466  -0.41540  1.000 23.40157  ? 373  LYS A CG  1 
ATOM   1361 C  CD  . LYS A 1 170 ? -0.21216  7.03503  -0.59629  1.000 30.50059  ? 373  LYS A CD  1 
ATOM   1362 C  CE  . LYS A 1 170 ? -0.71952  5.60205  -0.59805  1.000 46.63109  ? 373  LYS A CE  1 
ATOM   1363 N  NZ  . LYS A 1 170 ? -2.20252  5.55922  -0.37564  1.000 55.09498  ? 373  LYS A NZ  1 
ATOM   1364 N  N   . PHE A 1 171 ? 4.36763   10.97583 -0.14534  1.000 17.78297  ? 374  PHE A N   1 
ATOM   1365 C  CA  . PHE A 1 171 ? 5.06144   12.11586 -0.72666  1.000 17.86109  ? 374  PHE A CA  1 
ATOM   1366 C  C   . PHE A 1 171 ? 6.43269   11.68144 -1.24774  1.000 16.83455  ? 374  PHE A C   1 
ATOM   1367 O  O   . PHE A 1 171 ? 6.87377   10.54515 -1.03954  1.000 16.96740  ? 374  PHE A O   1 
ATOM   1368 C  CB  . PHE A 1 171 ? 5.20136   13.24712 0.31281   1.000 18.39425  ? 374  PHE A CB  1 
ATOM   1369 C  CG  . PHE A 1 171 ? 5.98110   12.86292 1.55082   1.000 15.91007  ? 374  PHE A CG  1 
ATOM   1370 C  CD1 . PHE A 1 171 ? 7.37990   12.87527 1.54757   1.000 16.72714  ? 374  PHE A CD1 1 
ATOM   1371 C  CD2 . PHE A 1 171 ? 5.32416   12.52893 2.72367   1.000 17.08120  ? 374  PHE A CD2 1 
ATOM   1372 C  CE1 . PHE A 1 171 ? 8.11354   12.55008 2.68926   1.000 18.66226  ? 374  PHE A CE1 1 
ATOM   1373 C  CE2 . PHE A 1 171 ? 6.03910   12.18968 3.85926   1.000 18.02601  ? 374  PHE A CE2 1 
ATOM   1374 C  CZ  . PHE A 1 171 ? 7.44103   12.18282 3.84229   1.000 19.70060  ? 374  PHE A CZ  1 
ATOM   1375 N  N   . TYR A 1 172 ? 7.13790   12.60178 -1.91887  1.000 17.35731  ? 375  TYR A N   1 
ATOM   1376 C  CA  . TYR A 1 172 ? 8.48012   12.33484 -2.43122  1.000 15.68702  ? 375  TYR A CA  1 
ATOM   1377 C  C   . TYR A 1 172 ? 9.42262   13.44314 -1.99151  1.000 17.10984  ? 375  TYR A C   1 
ATOM   1378 O  O   . TYR A 1 172 ? 9.05958   14.61766 -2.03893  1.000 18.91613  ? 375  TYR A O   1 
ATOM   1379 C  CB  . TYR A 1 172 ? 8.47077   12.24859 -3.98029  1.000 15.91799  ? 375  TYR A CB  1 
ATOM   1380 C  CG  . TYR A 1 172 ? 7.47419   11.22121 -4.44508  1.000 17.77734  ? 375  TYR A CG  1 
ATOM   1381 C  CD1 . TYR A 1 172 ? 7.83589   9.88137  -4.54249  1.000 17.90148  ? 375  TYR A CD1 1 
ATOM   1382 C  CD2 . TYR A 1 172 ? 6.16140   11.58107 -4.72201  1.000 16.50823  ? 375  TYR A CD2 1 
ATOM   1383 C  CE1 . TYR A 1 172 ? 6.89796   8.93381  -4.94914  1.000 16.23125  ? 375  TYR A CE1 1 
ATOM   1384 C  CE2 . TYR A 1 172 ? 5.22577   10.64111 -5.11342  1.000 18.80079  ? 375  TYR A CE2 1 
ATOM   1385 C  CZ  . TYR A 1 172 ? 5.61903   9.31667  -5.21927  1.000 17.94590  ? 375  TYR A CZ  1 
ATOM   1386 O  OH  . TYR A 1 172 ? 4.67252   8.38652  -5.60254  1.000 22.67498  ? 375  TYR A OH  1 
ATOM   1387 N  N   . ASN A 1 173 ? 10.63216  13.05619 -1.56421  1.000 15.54402  ? 376  ASN A N   1 
ATOM   1388 C  CA  . ASN A 1 173 ? 11.66279  14.02553 -1.15354  1.000 16.64558  ? 376  ASN A CA  1 
ATOM   1389 C  C   . ASN A 1 173 ? 13.03860  13.45693 -1.52319  1.000 18.79613  ? 376  ASN A C   1 
ATOM   1390 O  O   . ASN A 1 173 ? 13.77032  12.92279 -0.69140  1.000 20.54017  ? 376  ASN A O   1 
ATOM   1391 C  CB  . ASN A 1 173 ? 11.57368  14.33768 0.34151   1.000 17.59678  ? 376  ASN A CB  1 
ATOM   1392 C  CG  . ASN A 1 173 ? 12.74938  15.16943 0.82705   1.000 18.89389  ? 376  ASN A CG  1 
ATOM   1393 O  OD1 . ASN A 1 173 ? 13.20575  16.06719 0.12754   1.000 20.70993  ? 376  ASN A OD1 1 
ATOM   1394 N  ND2 . ASN A 1 173 ? 13.25407  14.86541 2.03686   1.000 19.58036  ? 376  ASN A ND2 1 
ATOM   1395 N  N   . VAL A 1 174 ? 13.41066  13.59274 -2.80377  1.000 17.20950  ? 377  VAL A N   1 
ATOM   1396 C  CA  . VAL A 1 174 ? 14.74711  13.19359 -3.23565  1.000 18.94958  ? 377  VAL A CA  1 
ATOM   1397 C  C   . VAL A 1 174 ? 15.77198  14.20951 -2.72881  1.000 20.26795  ? 377  VAL A C   1 
ATOM   1398 O  O   . VAL A 1 174 ? 15.58333  15.43380 -2.83628  1.000 22.48478  ? 377  VAL A O   1 
ATOM   1399 C  CB  . VAL A 1 174 ? 14.79882  13.02355 -4.77112  1.000 18.07379  ? 377  VAL A CB  1 
ATOM   1400 C  CG1 . VAL A 1 174 ? 13.87656  11.84910 -5.23990  1.000 17.08987  ? 377  VAL A CG1 1 
ATOM   1401 C  CG2 . VAL A 1 174 ? 14.43838  14.32596 -5.51935  1.000 18.16588  ? 377  VAL A CG2 1 
ATOM   1402 N  N   . ARG A 1 175 ? 16.85638  13.71220 -2.12850  1.000 19.15667  ? 378  ARG A N   1 
ATOM   1403 C  CA  . ARG A 1 175 ? 17.81749  14.59225 -1.47177  1.000 20.18837  ? 378  ARG A CA  1 
ATOM   1404 C  C   . ARG A 1 175 ? 19.10862  14.70968 -2.28151  1.000 21.60469  ? 378  ARG A C   1 
ATOM   1405 O  O   . ARG A 1 175 ? 19.47639  13.80403 -3.03673  1.000 25.05646  ? 378  ARG A O   1 
ATOM   1406 C  CB  . ARG A 1 175 ? 18.11267  14.08864 -0.04505  1.000 24.85119  ? 378  ARG A CB  1 
ATOM   1407 C  CG  . ARG A 1 175 ? 16.95902  14.35258 0.94310   1.000 21.22513  ? 378  ARG A CG  1 
ATOM   1408 C  CD  . ARG A 1 175 ? 17.16993  13.57599 2.27552   1.000 22.87217  ? 378  ARG A CD  1 
ATOM   1409 N  NE  . ARG A 1 175 ? 17.11503  12.13644 2.04300   1.000 21.63709  ? 378  ARG A NE  1 
ATOM   1410 C  CZ  . ARG A 1 175 ? 17.58381  11.22042 2.88608   1.000 23.37126  ? 378  ARG A CZ  1 
ATOM   1411 N  NH1 . ARG A 1 175 ? 18.12335  11.56211 4.05458   1.000 22.20854  ? 378  ARG A NH1 1 
ATOM   1412 N  NH2 . ARG A 1 175 ? 17.51391  9.93914  2.54737   1.000 22.08652  ? 378  ARG A NH2 1 
ATOM   1413 N  N   . LYS A 1 176 ? 19.79381  15.84791 -2.13521  1.000 23.54042  ? 379  LYS A N   1 
ATOM   1414 C  CA  . LYS A 1 176 ? 21.05661  16.03077 -2.84813  1.000 25.45668  ? 379  LYS A CA  1 
ATOM   1415 C  C   . LYS A 1 176 ? 22.13282  15.12660 -2.25818  1.000 27.57860  ? 379  LYS A C   1 
ATOM   1416 O  O   . LYS A 1 176 ? 22.44197  15.21831 -1.06335  1.000 27.79429  ? 379  LYS A O   1 
ATOM   1417 C  CB  . LYS A 1 176 ? 21.50914  17.48442 -2.79097  1.000 27.76799  ? 379  LYS A CB  1 
ATOM   1418 C  CG  . LYS A 1 176 ? 20.58364  18.50388 -3.44709  1.000 25.06331  ? 379  LYS A CG  1 
ATOM   1419 C  CD  . LYS A 1 176 ? 21.18719  19.91050 -3.28055  1.000 29.85910  ? 379  LYS A CD  1 
ATOM   1420 C  CE  . LYS A 1 176 ? 20.45547  20.98996 -4.07790  1.000 33.37582  ? 379  LYS A CE  1 
ATOM   1421 N  NZ  . LYS A 1 176 ? 20.99526  22.36654 -3.79124  1.000 29.05977  ? 379  LYS A NZ  1 
ATOM   1422 N  N   . LEU A 1 177 ? 22.71430  14.26394 -3.09692  1.000 24.52889  ? 380  LEU A N   1 
ATOM   1423 C  CA  . LEU A 1 177 ? 23.84923  13.46053 -2.65496  1.000 26.75493  ? 380  LEU A CA  1 
ATOM   1424 C  C   . LEU A 1 177 ? 25.00446  14.34752 -2.20948  1.000 31.32855  ? 380  LEU A C   1 
ATOM   1425 O  O   . LEU A 1 177 ? 25.71710  14.01685 -1.25524  1.000 31.01299  ? 380  LEU A O   1 
ATOM   1426 C  CB  . LEU A 1 177 ? 24.30986  12.52163 -3.76519  1.000 28.89747  ? 380  LEU A CB  1 
ATOM   1427 C  CG  . LEU A 1 177 ? 23.52008  11.22361 -3.93752  1.000 30.68618  ? 380  LEU A CG  1 
ATOM   1428 C  CD1 . LEU A 1 177 ? 22.16693  11.47763 -4.59736  1.000 27.31523  ? 380  LEU A CD1 1 
ATOM   1429 C  CD2 . LEU A 1 177 ? 24.33190  10.20268 -4.71887  1.000 28.67328  ? 380  LEU A CD2 1 
ATOM   1430 N  N   . ASP A 1 178 ? 25.19916  15.48749 -2.88452  1.000 31.19193  ? 381  ASP A N   1 
ATOM   1431 C  CA  . ASP A 1 178 ? 26.28961  16.39717 -2.53891  1.000 34.61074  ? 381  ASP A CA  1 
ATOM   1432 C  C   . ASP A 1 178 ? 26.11391  17.03111 -1.16506  1.000 37.18462  ? 381  ASP A C   1 
ATOM   1433 O  O   . ASP A 1 178 ? 27.10001  17.51242 -0.59101  1.000 36.10662  ? 381  ASP A O   1 
ATOM   1434 C  CB  . ASP A 1 178 ? 26.42769  17.49725 -3.60021  1.000 34.29637  ? 381  ASP A CB  1 
ATOM   1435 C  CG  . ASP A 1 178 ? 27.32492  17.08223 -4.76214  1.000 47.56278  ? 381  ASP A CG  1 
ATOM   1436 O  OD1 . ASP A 1 178 ? 28.16822  16.18653 -4.56885  1.000 55.58637  ? 381  ASP A OD1 1 
ATOM   1437 O  OD2 . ASP A 1 178 ? 27.19518  17.65298 -5.86533  1.000 47.97752  ? 381  ASP A OD2 1 
ATOM   1438 N  N   . LYS A 1 179 ? 24.88876  17.06457 -0.63471  1.000 30.53143  ? 382  LYS A N   1 
ATOM   1439 C  CA  . LYS A 1 179 ? 24.65401  17.55998 0.71812   1.000 29.31900  ? 382  LYS A CA  1 
ATOM   1440 C  C   . LYS A 1 179 ? 24.72821  16.45146 1.77055   1.000 35.03520  ? 382  LYS A C   1 
ATOM   1441 O  O   . LYS A 1 179 ? 25.22470  16.69917 2.87761   1.000 34.81373  ? 382  LYS A O   1 
ATOM   1442 C  CB  . LYS A 1 179 ? 23.29556  18.26335 0.80116   1.000 34.91451  ? 382  LYS A CB  1 
ATOM   1443 C  CG  . LYS A 1 179 ? 23.25054  19.63954 0.14754   1.000 33.02342  ? 382  LYS A CG  1 
ATOM   1444 C  CD  . LYS A 1 179 ? 24.12911  20.63443 0.90624   1.000 37.88463  ? 382  LYS A CD  1 
ATOM   1445 C  CE  . LYS A 1 179 ? 23.70702  22.06529 0.63861   1.000 49.70047  ? 382  LYS A CE  1 
ATOM   1446 N  NZ  . LYS A 1 179 ? 23.86200  22.42920 -0.79131  1.000 55.65304  ? 382  LYS A NZ  1 
ATOM   1447 N  N   . LEU A 1 180 ? 24.23213  15.24538 1.45915   1.000 29.86063  ? 383  LEU A N   1 
ATOM   1448 C  CA  . LEU A 1 180 ? 24.30910  14.13164 2.40992   1.000 29.78487  ? 383  LEU A CA  1 
ATOM   1449 C  C   . LEU A 1 180 ? 25.74170  13.64721 2.58597   1.000 37.71019  ? 383  LEU A C   1 
ATOM   1450 O  O   . LEU A 1 180 ? 26.14771  13.27262 3.69476   1.000 35.53132  ? 383  LEU A O   1 
ATOM   1451 C  CB  . LEU A 1 180 ? 23.42587  12.96976 1.95119   1.000 31.24365  ? 383  LEU A CB  1 
ATOM   1452 C  CG  . LEU A 1 180 ? 21.92406  13.22831 1.94677   1.000 31.47612  ? 383  LEU A CG  1 
ATOM   1453 C  CD1 . LEU A 1 180 ? 21.17050  12.02175 1.43532   1.000 24.30199  ? 383  LEU A CD1 1 
ATOM   1454 C  CD2 . LEU A 1 180 ? 21.47472  13.59720 3.35240   1.000 30.59800  ? 383  LEU A CD2 1 
ATOM   1455 N  N   . TYR A 1 181 ? 26.51731  13.67747 1.50539   1.000 27.66597  ? 384  TYR A N   1 
ATOM   1456 C  CA  . TYR A 1 181 ? 27.85398  13.09636 1.45142   1.000 31.56946  ? 384  TYR A CA  1 
ATOM   1457 C  C   . TYR A 1 181 ? 28.75699  13.60737 2.56882   1.000 38.94396  ? 384  TYR A C   1 
ATOM   1458 O  O   . TYR A 1 181 ? 28.88046  14.81619 2.78644   1.000 37.52267  ? 384  TYR A O   1 
ATOM   1459 C  CB  . TYR A 1 181 ? 28.46206  13.42310 0.08570   1.000 33.41193  ? 384  TYR A CB  1 
ATOM   1460 C  CG  . TYR A 1 181 ? 29.85775  12.90241 -0.15880  1.000 36.56466  ? 384  TYR A CG  1 
ATOM   1461 C  CD1 . TYR A 1 181 ? 30.12493  11.53579 -0.16083  1.000 36.05255  ? 384  TYR A CD1 1 
ATOM   1462 C  CD2 . TYR A 1 181 ? 30.89961  13.77913 -0.44686  1.000 35.70524  ? 384  TYR A CD2 1 
ATOM   1463 C  CE1 . TYR A 1 181 ? 31.40243  11.06266 -0.40222  1.000 37.31171  ? 384  TYR A CE1 1 
ATOM   1464 C  CE2 . TYR A 1 181 ? 32.16858  13.31436 -0.69892  1.000 40.33166  ? 384  TYR A CE2 1 
ATOM   1465 C  CZ  . TYR A 1 181 ? 32.41700  11.95782 -0.67340  1.000 38.52593  ? 384  TYR A CZ  1 
ATOM   1466 O  OH  . TYR A 1 181 ? 33.69090  11.50526 -0.92124  1.000 46.66133  ? 384  TYR A OH  1 
ATOM   1467 N  N   . VAL A 1 182 ? 29.39757  12.67580 3.26944   1.000 35.42732  ? 385  VAL A N   1 
ATOM   1468 C  CA  . VAL A 1 182 ? 30.41903  12.99234 4.26211   1.000 34.81145  ? 385  VAL A CA  1 
ATOM   1469 C  C   . VAL A 1 182 ? 31.73547  12.41977 3.76171   1.000 37.37003  ? 385  VAL A C   1 
ATOM   1470 O  O   . VAL A 1 182 ? 31.87906  11.19626 3.64828   1.000 37.57620  ? 385  VAL A O   1 
ATOM   1471 C  CB  . VAL A 1 182 ? 30.07757  12.43815 5.65098   1.000 35.95525  ? 385  VAL A CB  1 
ATOM   1472 C  CG1 . VAL A 1 182 ? 31.24954  12.66891 6.59293   1.000 38.92112  ? 385  VAL A CG1 1 
ATOM   1473 C  CG2 . VAL A 1 182 ? 28.80075  13.09446 6.19105   1.000 40.12568  ? 385  VAL A CG2 1 
ATOM   1474 N  N   . GLN A 1 183 ? 32.69689  13.29790 3.47255   1.000 39.52380  ? 386  GLN A N   1 
ATOM   1475 C  CA  . GLN A 1 183 ? 33.99057  12.85770 2.96619   1.000 42.29231  ? 386  GLN A CA  1 
ATOM   1476 C  C   . GLN A 1 183 ? 34.66591  11.92708 3.96552   1.000 43.84948  ? 386  GLN A C   1 
ATOM   1477 O  O   . GLN A 1 183 ? 34.70246  12.20879 5.16197   1.000 44.12225  ? 386  GLN A O   1 
ATOM   1478 C  CB  . GLN A 1 183 ? 34.88502  14.06879 2.67895   1.000 44.59614  ? 386  GLN A CB  1 
ATOM   1479 C  CG  . GLN A 1 183 ? 34.29774  15.02296 1.64025   1.000 43.44178  ? 386  GLN A CG  1 
ATOM   1480 C  CD  . GLN A 1 183 ? 35.23120  16.15857 1.27517   1.000 46.05287  ? 386  GLN A CD  1 
ATOM   1481 O  OE1 . GLN A 1 183 ? 35.63367  16.95648 2.13003   1.000 47.39883  ? 386  GLN A OE1 1 
ATOM   1482 N  NE2 . GLN A 1 183 ? 35.58533  16.23853 -0.00502  1.000 46.93799  ? 386  GLN A NE2 1 
ATOM   1483 N  N   . GLY A 1 184 ? 35.18559  10.80697 3.46885   1.000 44.96816  ? 387  GLY A N   1 
ATOM   1484 C  CA  . GLY A 1 184 ? 35.86643  9.83938  4.29617   1.000 46.75495  ? 387  GLY A CA  1 
ATOM   1485 C  C   . GLY A 1 184 ? 34.96961  8.82818  4.97503   1.000 44.82335  ? 387  GLY A C   1 
ATOM   1486 O  O   . GLY A 1 184 ? 35.47960  7.86205  5.55305   1.000 51.00807  ? 387  GLY A O   1 
ATOM   1487 N  N   . GLN A 1 185 ? 33.65377  9.01056  4.93157   1.000 41.75180  ? 388  GLN A N   1 
ATOM   1488 C  CA  . GLN A 1 185 ? 32.74813  8.08506  5.58928   1.000 40.18862  ? 388  GLN A CA  1 
ATOM   1489 C  C   . GLN A 1 185 ? 31.73513  7.44040  4.66001   1.000 46.29062  ? 388  GLN A C   1 
ATOM   1490 O  O   . GLN A 1 185 ? 31.20524  6.38002  5.00274   1.000 54.54698  ? 388  GLN A O   1 
ATOM   1491 C  CB  . GLN A 1 185 ? 32.01550  8.79304  6.73962   1.000 43.62798  ? 388  GLN A CB  1 
ATOM   1492 C  CG  . GLN A 1 185 ? 32.95301  9.09791  7.90764   1.000 57.35509  ? 388  GLN A CG  1 
ATOM   1493 C  CD  . GLN A 1 185 ? 32.39769  10.12349 8.87550   1.000 59.64777  ? 388  GLN A CD  1 
ATOM   1494 O  OE1 . GLN A 1 185 ? 33.12006  11.01329 9.33364   1.000 61.61969  ? 388  GLN A OE1 1 
ATOM   1495 N  NE2 . GLN A 1 185 ? 31.11286  10.00267 9.19851   1.000 57.42635  ? 388  GLN A NE2 1 
ATOM   1496 N  N   . PHE A 1 186 ? 31.46929  8.01950  3.50949   1.000 41.40109  ? 389  PHE A N   1 
ATOM   1497 C  CA  . PHE A 1 186 ? 30.53048  7.43892  2.56528   1.000 39.76903  ? 389  PHE A CA  1 
ATOM   1498 C  C   . PHE A 1 186 ? 31.25098  6.50711  1.59997   1.000 41.80222  ? 389  PHE A C   1 
ATOM   1499 O  O   . PHE A 1 186 ? 32.48021  6.54348  1.48701   1.000 45.61648  ? 389  PHE A O   1 
ATOM   1500 C  CB  . PHE A 1 186 ? 29.80255  8.55252  1.80711   1.000 37.95642  ? 389  PHE A CB  1 
ATOM   1501 C  CG  . PHE A 1 186 ? 28.56199  9.05930  2.51193   1.000 37.08846  ? 389  PHE A CG  1 
ATOM   1502 C  CD1 . PHE A 1 186 ? 28.60113  9.42383  3.84935   1.000 40.96944  ? 389  PHE A CD1 1 
ATOM   1503 C  CD2 . PHE A 1 186 ? 27.35986  9.17464  1.83331   1.000 35.25663  ? 389  PHE A CD2 1 
ATOM   1504 C  CE1 . PHE A 1 186 ? 27.45496  9.88638  4.49750   1.000 37.73280  ? 389  PHE A CE1 1 
ATOM   1505 C  CE2 . PHE A 1 186 ? 26.21990  9.63603  2.46758   1.000 34.48143  ? 389  PHE A CE2 1 
ATOM   1506 C  CZ  . PHE A 1 186 ? 26.26610  9.99733  3.80666   1.000 33.44955  ? 389  PHE A CZ  1 
ATOM   1507 N  N   . PRO A 1 187 ? 30.51772  5.63222  0.90672   1.000 43.15077  ? 390  PRO A N   1 
ATOM   1508 C  CA  . PRO A 1 187 ? 31.15854  4.78019  -0.10387  1.000 45.11803  ? 390  PRO A CA  1 
ATOM   1509 C  C   . PRO A 1 187 ? 31.81510  5.61904  -1.19351  1.000 46.54194  ? 390  PRO A C   1 
ATOM   1510 O  O   . PRO A 1 187 ? 31.30252  6.66720  -1.58931  1.000 43.25813  ? 390  PRO A O   1 
ATOM   1511 C  CB  . PRO A 1 187 ? 29.99558  3.94944  -0.66146  1.000 48.48342  ? 390  PRO A CB  1 
ATOM   1512 C  CG  . PRO A 1 187 ? 28.93643  4.00266  0.37817   1.000 48.67047  ? 390  PRO A CG  1 
ATOM   1513 C  CD  . PRO A 1 187 ? 29.07910  5.33845  1.04404   1.000 42.01396  ? 390  PRO A CD  1 
ATOM   1514 N  N   . SER A 1 188 ? 32.96912  5.14801  -1.67538  1.000 52.13093  ? 391  SER A N   1 
ATOM   1515 C  CA  . SER A 1 188 ? 33.70444  5.88534  -2.69662  1.000 45.31739  ? 391  SER A CA  1 
ATOM   1516 C  C   . SER A 1 188 ? 32.95759  5.94071  -4.02398  1.000 48.07257  ? 391  SER A C   1 
ATOM   1517 O  O   . SER A 1 188 ? 33.23423  6.82758  -4.83861  1.000 47.09554  ? 391  SER A O   1 
ATOM   1518 C  CB  . SER A 1 188 ? 35.09304  5.27181  -2.89906  1.000 50.87310  ? 391  SER A CB  1 
ATOM   1519 O  OG  . SER A 1 188 ? 35.01122  3.88080  -3.15186  1.000 60.69725  ? 391  SER A OG  1 
ATOM   1520 N  N   . ASN A 1 189 ? 32.02195  5.02084  -4.25954  1.000 50.43981  ? 392  ASN A N   1 
ATOM   1521 C  CA  . ASN A 1 189 ? 31.19910  5.02700  -5.46214  1.000 48.54234  ? 392  ASN A CA  1 
ATOM   1522 C  C   . ASN A 1 189 ? 29.83576  5.67445  -5.23025  1.000 42.47818  ? 392  ASN A C   1 
ATOM   1523 O  O   . ASN A 1 189 ? 28.90758  5.43918  -6.01099  1.000 43.69047  ? 392  ASN A O   1 
ATOM   1524 C  CB  . ASN A 1 189 ? 31.01869  3.60129  -5.98902  1.000 51.82677  ? 392  ASN A CB  1 
ATOM   1525 C  CG  . ASN A 1 189 ? 30.32216  2.68866  -4.98737  1.000 54.57323  ? 392  ASN A CG  1 
ATOM   1526 O  OD1 . ASN A 1 189 ? 29.90789  3.12363  -3.91257  1.000 53.64672  ? 392  ASN A OD1 1 
ATOM   1527 N  ND2 . ASN A 1 189 ? 30.18607  1.41543  -5.34251  1.000 53.84927  ? 392  ASN A ND2 1 
ATOM   1528 N  N   . TYR A 1 190 ? 29.70544  6.48575  -4.17424  1.000 41.71179  ? 393  TYR A N   1 
ATOM   1529 C  CA  . TYR A 1 190 ? 28.41213  7.04654  -3.78323  1.000 40.27767  ? 393  TYR A CA  1 
ATOM   1530 C  C   . TYR A 1 190 ? 27.69271  7.71426  -4.94760  1.000 39.99714  ? 393  TYR A C   1 
ATOM   1531 O  O   . TYR A 1 190 ? 26.46918  7.58662  -5.08810  1.000 36.97496  ? 393  TYR A O   1 
ATOM   1532 C  CB  . TYR A 1 190 ? 28.62013  8.05350  -2.65493  1.000 36.22102  ? 393  TYR A CB  1 
ATOM   1533 C  CG  . TYR A 1 190 ? 27.36687  8.63831  -2.04318  1.000 34.94799  ? 393  TYR A CG  1 
ATOM   1534 C  CD1 . TYR A 1 190 ? 26.37358  7.81928  -1.51874  1.000 36.41128  ? 393  TYR A CD1 1 
ATOM   1535 C  CD2 . TYR A 1 190 ? 27.20570  10.01434 -1.93489  1.000 33.32441  ? 393  TYR A CD2 1 
ATOM   1536 C  CE1 . TYR A 1 190 ? 25.24864  8.35450  -0.93542  1.000 30.86963  ? 393  TYR A CE1 1 
ATOM   1537 C  CE2 . TYR A 1 190 ? 26.08613  10.55724 -1.34723  1.000 29.64786  ? 393  TYR A CE2 1 
ATOM   1538 C  CZ  . TYR A 1 190 ? 25.11447  9.72132  -0.84986  1.000 28.52979  ? 393  TYR A CZ  1 
ATOM   1539 O  OH  . TYR A 1 190 ? 23.99889  10.25280 -0.25820  1.000 29.03059  ? 393  TYR A OH  1 
ATOM   1540 N  N   . PHE A 1 191 ? 28.43028  8.42721  -5.79264  1.000 37.59645  ? 394  PHE A N   1 
ATOM   1541 C  CA  . PHE A 1 191 ? 27.81207  9.23293  -6.83423  1.000 35.08175  ? 394  PHE A CA  1 
ATOM   1542 C  C   . PHE A 1 191 ? 27.66300  8.50134  -8.16059  1.000 39.40517  ? 394  PHE A C   1 
ATOM   1543 O  O   . PHE A 1 191 ? 27.22645  9.12008  -9.13386  1.000 38.08181  ? 394  PHE A O   1 
ATOM   1544 C  CB  . PHE A 1 191 ? 28.61714  10.51774 -7.05887  1.000 41.03548  ? 394  PHE A CB  1 
ATOM   1545 C  CG  . PHE A 1 191 ? 28.73532  11.38605 -5.83631  1.000 38.57079  ? 394  PHE A CG  1 
ATOM   1546 C  CD1 . PHE A 1 191 ? 27.73435  12.29478 -5.51057  1.000 35.66461  ? 394  PHE A CD1 1 
ATOM   1547 C  CD2 . PHE A 1 191 ? 29.84873  11.29757 -5.01585  1.000 43.47538  ? 394  PHE A CD2 1 
ATOM   1548 C  CE1 . PHE A 1 191 ? 27.84582  13.09853 -4.37924  1.000 36.71647  ? 394  PHE A CE1 1 
ATOM   1549 C  CE2 . PHE A 1 191 ? 29.96560  12.09327 -3.89411  1.000 37.61327  ? 394  PHE A CE2 1 
ATOM   1550 C  CZ  . PHE A 1 191 ? 28.96114  12.99337 -3.57378  1.000 37.23801  ? 394  PHE A CZ  1 
ATOM   1551 N  N   . VAL A 1 192 ? 27.99754  7.21561  -8.23299  1.000 39.26784  ? 395  VAL A N   1 
ATOM   1552 C  CA  . VAL A 1 192 ? 28.01103  6.52075  -9.51863  1.000 42.85170  ? 395  VAL A CA  1 
ATOM   1553 C  C   . VAL A 1 192 ? 26.58656  6.18122  -9.93429  1.000 38.64829  ? 395  VAL A C   1 
ATOM   1554 O  O   . VAL A 1 192 ? 25.80317  5.63874  -9.14509  1.000 35.47185  ? 395  VAL A O   1 
ATOM   1555 C  CB  . VAL A 1 192 ? 28.88213  5.25654  -9.45958  1.000 45.49966  ? 395  VAL A CB  1 
ATOM   1556 C  CG1 . VAL A 1 192 ? 28.82243  4.52812  -10.79638 1.000 47.92924  ? 395  VAL A CG1 1 
ATOM   1557 C  CG2 . VAL A 1 192 ? 30.31675  5.61338  -9.12769  1.000 44.56383  ? 395  VAL A CG2 1 
ATOM   1558 N  N   . ILE A 1 193 ? 26.25867  6.48281  -11.18766 1.000 38.56244  ? 396  ILE A N   1 
ATOM   1559 C  CA  . ILE A 1 193 ? 24.96709  6.17005  -11.78020 1.000 37.52843  ? 396  ILE A CA  1 
ATOM   1560 C  C   . ILE A 1 193 ? 25.19306  5.21294  -12.93990 1.000 39.19079  ? 396  ILE A C   1 
ATOM   1561 O  O   . ILE A 1 193 ? 26.11633  5.40159  -13.73733 1.000 44.41904  ? 396  ILE A O   1 
ATOM   1562 C  CB  . ILE A 1 193 ? 24.25014  7.43803  -12.27942 1.000 35.54362  ? 396  ILE A CB  1 
ATOM   1563 C  CG1 . ILE A 1 193 ? 24.04024  8.42986  -11.13708 1.000 34.46933  ? 396  ILE A CG1 1 
ATOM   1564 C  CG2 . ILE A 1 193 ? 22.92337  7.08637  -12.93638 1.000 35.17889  ? 396  ILE A CG2 1 
ATOM   1565 C  CD1 . ILE A 1 193 ? 23.48644  9.74887  -11.61655 1.000 31.64624  ? 396  ILE A CD1 1 
ATOM   1566 N  N   . ASN A 1 194 ? 24.34676  4.19544  -13.03681 1.000 41.23458  ? 397  ASN A N   1 
ATOM   1567 C  CA  . ASN A 1 194 ? 24.33715  3.31743  -14.19902 1.000 47.22814  ? 397  ASN A CA  1 
ATOM   1568 C  C   . ASN A 1 194 ? 23.39003  3.92176  -15.23099 1.000 40.34778  ? 397  ASN A C   1 
ATOM   1569 O  O   . ASN A 1 194 ? 22.16815  3.88144  -15.06055 1.000 44.62985  ? 397  ASN A O   1 
ATOM   1570 C  CB  . ASN A 1 194 ? 23.91969  1.90250  -13.81098 1.000 45.61832  ? 397  ASN A CB  1 
ATOM   1571 C  CG  . ASN A 1 194 ? 24.12961  0.91086  -14.93980 1.000 53.42330  ? 397  ASN A CG  1 
ATOM   1572 O  OD1 . ASN A 1 194 ? 23.17272  0.44031  -15.55430 1.000 57.97183  ? 397  ASN A OD1 1 
ATOM   1573 N  ND2 . ASN A 1 194 ? 25.39068  0.60707  -15.23436 1.000 62.11651  ? 397  ASN A ND2 1 
ATOM   1574 N  N   . GLY A 1 195 ? 23.95749  4.48247  -16.29548 1.000 43.30789  ? 398  GLY A N   1 
ATOM   1575 C  CA  . GLY A 1 195 ? 23.19518  5.21343  -17.28469 1.000 47.39678  ? 398  GLY A CA  1 
ATOM   1576 C  C   . GLY A 1 195 ? 22.32695  4.32213  -18.15748 1.000 47.58133  ? 398  GLY A C   1 
ATOM   1577 O  O   . GLY A 1 195 ? 22.23533  3.10651  -17.98601 1.000 50.88619  ? 398  GLY A O   1 
ATOM   1578 N  N   . ILE A 1 196 ? 21.68181  4.96190  -19.13734 1.000 41.26536  ? 399  ILE A N   1 
ATOM   1579 C  CA  . ILE A 1 196 ? 20.65829  4.27848  -19.92313 1.000 48.12511  ? 399  ILE A CA  1 
ATOM   1580 C  C   . ILE A 1 196 ? 21.25105  3.24175  -20.86903 1.000 56.32444  ? 399  ILE A C   1 
ATOM   1581 O  O   . ILE A 1 196 ? 20.54594  2.31179  -21.27681 1.000 61.58958  ? 399  ILE A O   1 
ATOM   1582 C  CB  . ILE A 1 196 ? 19.80458  5.29457  -20.70440 1.000 50.04240  ? 399  ILE A CB  1 
ATOM   1583 C  CG1 . ILE A 1 196 ? 20.68481  6.14911  -21.61252 1.000 49.63124  ? 399  ILE A CG1 1 
ATOM   1584 C  CG2 . ILE A 1 196 ? 19.00677  6.17046  -19.74917 1.000 50.16500  ? 399  ILE A CG2 1 
ATOM   1585 C  CD1 . ILE A 1 196 ? 19.89672  6.99714  -22.59055 1.000 55.73613  ? 399  ILE A CD1 1 
ATOM   1586 N  N   . ARG A 1 197 ? 22.52194  3.38469  -21.24732 1.000 47.64077  ? 400  ARG A N   1 
ATOM   1587 C  CA  . ARG A 1 197 ? 23.25521  2.34704  -21.96217 1.000 52.79863  ? 400  ARG A CA  1 
ATOM   1588 C  C   . ARG A 1 197 ? 24.19032  1.57188  -21.03828 1.000 54.26748  ? 400  ARG A C   1 
ATOM   1589 O  O   . ARG A 1 197 ? 25.23654  1.08635  -21.47905 1.000 58.30811  ? 400  ARG A O   1 
ATOM   1590 C  CB  . ARG A 1 197 ? 24.04218  2.95103  -23.12543 1.000 53.44238  ? 400  ARG A CB  1 
ATOM   1591 C  CG  . ARG A 1 197 ? 23.18351  3.43449  -24.28664 1.000 56.90908  ? 400  ARG A CG  1 
ATOM   1592 N  N   . ASN A 1 198 ? 23.83641  1.46473  -19.75587 1.000 55.02810  ? 401  ASN A N   1 
ATOM   1593 C  CA  . ASN A 1 198 ? 24.64605  0.80313  -18.73282 1.000 59.82309  ? 401  ASN A CA  1 
ATOM   1594 C  C   . ASN A 1 198 ? 26.03232  1.42671  -18.59112 1.000 57.05869  ? 401  ASN A C   1 
ATOM   1595 O  O   . ASN A 1 198 ? 26.95074  0.78938  -18.06374 1.000 61.52340  ? 401  ASN A O   1 
ATOM   1596 C  CB  . ASN A 1 198 ? 24.77261  -0.70130 -19.00507 1.000 65.63906  ? 401  ASN A CB  1 
ATOM   1597 C  CG  . ASN A 1 198 ? 23.42586  -1.37923 -19.18265 1.000 73.30967  ? 401  ASN A CG  1 
ATOM   1598 O  OD1 . ASN A 1 198 ? 22.51877  -1.21771 -18.36262 1.000 61.44702  ? 401  ASN A OD1 1 
ATOM   1599 N  ND2 . ASN A 1 198 ? 23.28716  -2.13841 -20.26598 1.000 69.14299  ? 401  ASN A ND2 1 
ATOM   1600 N  N   . GLU A 1 199 ? 26.20951  2.66129  -19.05627 1.000 50.17387  ? 402  GLU A N   1 
ATOM   1601 C  CA  . GLU A 1 199 ? 27.46954  3.36523  -18.86984 1.000 53.03941  ? 402  GLU A CA  1 
ATOM   1602 C  C   . GLU A 1 199 ? 27.54425  3.93695  -17.45597 1.000 53.64343  ? 402  GLU A C   1 
ATOM   1603 O  O   . GLU A 1 199 ? 26.52276  4.24671  -16.83705 1.000 51.75693  ? 402  GLU A O   1 
ATOM   1604 C  CB  . GLU A 1 199 ? 27.62449  4.48285  -19.90620 1.000 53.96658  ? 402  GLU A CB  1 
ATOM   1605 C  CG  . GLU A 1 199 ? 26.89032  5.78387  -19.58160 1.000 53.19611  ? 402  GLU A CG  1 
ATOM   1606 C  CD  . GLU A 1 199 ? 25.49378  5.85479  -20.17367 1.000 54.15772  ? 402  GLU A CD  1 
ATOM   1607 O  OE1 . GLU A 1 199 ? 24.83598  4.80011  -20.29195 1.000 56.16243  ? 402  GLU A OE1 1 
ATOM   1608 O  OE2 . GLU A 1 199 ? 25.05283  6.97236  -20.52297 1.000 50.02336  ? 402  GLU A OE2 1 
ATOM   1609 N  N   . GLN A 1 200 ? 28.76699  4.06797  -16.94308 1.000 51.47408  ? 403  GLN A N   1 
ATOM   1610 C  CA  . GLN A 1 200 ? 28.99812  4.49526  -15.56528 1.000 61.20928  ? 403  GLN A CA  1 
ATOM   1611 C  C   . GLN A 1 200 ? 29.26297  5.99753  -15.52872 1.000 57.75043  ? 403  GLN A C   1 
ATOM   1612 O  O   . GLN A 1 200 ? 30.16939  6.48827  -16.20952 1.000 55.08056  ? 403  GLN A O   1 
ATOM   1613 C  CB  . GLN A 1 200 ? 30.16516  3.72618  -14.94590 1.000 57.49392  ? 403  GLN A CB  1 
ATOM   1614 C  CG  . GLN A 1 200 ? 30.00763  2.21195  -15.00477 1.000 63.41043  ? 403  GLN A CG  1 
ATOM   1615 C  CD  . GLN A 1 200 ? 28.75488  1.71770  -14.29867 1.000 62.43773  ? 403  GLN A CD  1 
ATOM   1616 O  OE1 . GLN A 1 200 ? 27.81923  1.23064  -14.93679 1.000 63.30337  ? 403  GLN A OE1 1 
ATOM   1617 N  NE2 . GLN A 1 200 ? 28.73539  1.83216  -12.97463 1.000 59.19971  ? 403  GLN A NE2 1 
ATOM   1618 N  N   . ILE A 1 201 ? 28.48084  6.71805  -14.72338 1.000 53.99314  ? 404  ILE A N   1 
ATOM   1619 C  CA  . ILE A 1 201 ? 28.49881  8.17680  -14.67640 1.000 48.48169  ? 404  ILE A CA  1 
ATOM   1620 C  C   . ILE A 1 201 ? 28.62823  8.62773  -13.22769 1.000 49.67569  ? 404  ILE A C   1 
ATOM   1621 O  O   . ILE A 1 201 ? 27.89470  8.14651  -12.35823 1.000 50.25710  ? 404  ILE A O   1 
ATOM   1622 C  CB  . ILE A 1 201 ? 27.22340  8.78054  -15.29685 1.000 44.45880  ? 404  ILE A CB  1 
ATOM   1623 C  CG1 . ILE A 1 201 ? 27.04925  8.31721  -16.74183 1.000 50.50413  ? 404  ILE A CG1 1 
ATOM   1624 C  CG2 . ILE A 1 201 ? 27.24886  10.29656 -15.21369 1.000 46.81224  ? 404  ILE A CG2 1 
ATOM   1625 C  CD1 . ILE A 1 201 ? 25.74477  8.77515  -17.35443 1.000 45.39537  ? 404  ILE A CD1 1 
ATOM   1626 N  N   . GLN A 1 202 ? 29.54774  9.55880  -12.97543 1.000 51.50370  ? 405  GLN A N   1 
ATOM   1627 C  CA  . GLN A 1 202 ? 29.65257  10.24740 -11.68726 1.000 52.91697  ? 405  GLN A CA  1 
ATOM   1628 C  C   . GLN A 1 202 ? 28.81231  11.51755 -11.76933 1.000 54.61114  ? 405  GLN A C   1 
ATOM   1629 O  O   . GLN A 1 202 ? 29.25825  12.52942 -12.31428 1.000 60.85784  ? 405  GLN A O   1 
ATOM   1630 C  CB  . GLN A 1 202 ? 31.10587  10.57842 -11.36472 1.000 55.27178  ? 405  GLN A CB  1 
ATOM   1631 C  CG  . GLN A 1 202 ? 32.00710  9.37964  -11.13555 1.000 63.06781  ? 405  GLN A CG  1 
ATOM   1632 C  CD  . GLN A 1 202 ? 32.03015  8.93564  -9.68422  1.000 66.90121  ? 405  GLN A CD  1 
ATOM   1633 O  OE1 . GLN A 1 202 ? 31.43931  9.57747  -8.81424  1.000 62.55265  ? 405  GLN A OE1 1 
ATOM   1634 N  NE2 . GLN A 1 202 ? 32.72294  7.83451  -9.41548  1.000 68.49898  ? 405  GLN A NE2 1 
ATOM   1635 N  N   . GLY A 1 203 ? 27.59779  11.47535 -11.23320 1.000 43.36721  ? 406  GLY A N   1 
ATOM   1636 C  CA  . GLY A 1 203 ? 26.70631  12.62328 -11.25795 1.000 39.24178  ? 406  GLY A CA  1 
ATOM   1637 C  C   . GLY A 1 203 ? 26.68320  13.32967 -9.91159  1.000 38.21951  ? 406  GLY A C   1 
ATOM   1638 O  O   . GLY A 1 203 ? 26.49141  12.69676 -8.87152  1.000 37.07282  ? 406  GLY A O   1 
ATOM   1639 N  N   . ARG A 1 204 ? 26.88169  14.64359 -9.95151  1.000 35.93281  ? 407  ARG A N   1 
ATOM   1640 C  CA  . ARG A 1 204 ? 26.82930  15.48749 -8.76391  1.000 37.80326  ? 407  ARG A CA  1 
ATOM   1641 C  C   . ARG A 1 204 ? 25.62793  16.42064 -8.87637  1.000 32.99625  ? 407  ARG A C   1 
ATOM   1642 O  O   . ARG A 1 204 ? 25.11899  16.67274 -9.97282  1.000 33.97700  ? 407  ARG A O   1 
ATOM   1643 C  CB  . ARG A 1 204 ? 28.13607  16.28141 -8.58735  1.000 39.70645  ? 407  ARG A CB  1 
ATOM   1644 C  CG  . ARG A 1 204 ? 29.42080  15.46666 -8.78567  1.000 43.64795  ? 407  ARG A CG  1 
ATOM   1645 C  CD  . ARG A 1 204 ? 29.52596  14.25676 -7.85084  1.000 48.79558  ? 407  ARG A CD  1 
ATOM   1646 N  NE  . ARG A 1 204 ? 29.92582  14.61788 -6.49447  1.000 45.28230  ? 407  ARG A NE  1 
ATOM   1647 C  CZ  . ARG A 1 204 ? 31.15945  14.50368 -6.01127  1.000 50.79270  ? 407  ARG A CZ  1 
ATOM   1648 N  NH1 . ARG A 1 204 ? 32.15254  14.02299 -6.74407  1.000 47.71774  ? 407  ARG A NH1 1 
ATOM   1649 N  NH2 . ARG A 1 204 ? 31.40484  14.88687 -4.76111  1.000 52.74391  ? 407  ARG A NH2 1 
ATOM   1650 N  N   . ASP A 1 205 ? 25.14716  16.91536 -7.72645  1.000 33.68185  ? 408  ASP A N   1 
ATOM   1651 C  CA  . ASP A 1 205 ? 23.84906  17.58834 -7.71163  1.000 26.32843  ? 408  ASP A CA  1 
ATOM   1652 C  C   . ASP A 1 205 ? 23.80920  18.78477 -6.76229  1.000 26.60055  ? 408  ASP A C   1 
ATOM   1653 O  O   . ASP A 1 205 ? 22.72781  19.18213 -6.30878  1.000 30.76185  ? 408  ASP A O   1 
ATOM   1654 C  CB  . ASP A 1 205 ? 22.72355  16.60138 -7.35996  1.000 29.12326  ? 408  ASP A CB  1 
ATOM   1655 C  CG  . ASP A 1 205 ? 22.95927  15.86957 -6.04041  1.000 27.39884  ? 408  ASP A CG  1 
ATOM   1656 O  OD1 . ASP A 1 205 ? 23.87261  16.25960 -5.27382  1.000 29.55390  ? 408  ASP A OD1 1 
ATOM   1657 O  OD2 . ASP A 1 205 ? 22.21558  14.88469 -5.78453  1.000 27.89065  ? 408  ASP A OD2 1 
ATOM   1658 N  N   . ILE A 1 206 ? 24.95992  19.40483 -6.49537  1.000 30.72205  ? 409  ILE A N   1 
ATOM   1659 C  CA  . ILE A 1 206 ? 25.02015  20.45283 -5.47630  1.000 34.09416  ? 409  ILE A CA  1 
ATOM   1660 C  C   . ILE A 1 206 ? 24.14884  21.65666 -5.83815  1.000 32.48682  ? 409  ILE A C   1 
ATOM   1661 O  O   . ILE A 1 206 ? 23.63798  22.34906 -4.94862  1.000 35.95128  ? 409  ILE A O   1 
ATOM   1662 C  CB  . ILE A 1 206 ? 26.48671  20.86565 -5.23124  1.000 34.41612  ? 409  ILE A CB  1 
ATOM   1663 C  CG1 . ILE A 1 206 ? 26.58253  21.72754 -3.98205  1.000 39.68782  ? 409  ILE A CG1 1 
ATOM   1664 C  CG2 . ILE A 1 206 ? 27.05451  21.61781 -6.43224  1.000 39.22866  ? 409  ILE A CG2 1 
ATOM   1665 C  CD1 . ILE A 1 206 ? 26.07200  21.03937 -2.74255  1.000 46.15270  ? 409  ILE A CD1 1 
ATOM   1666 N  N   . SER A 1 207 ? 23.95117  21.92884 -7.13197  1.000 35.35909  ? 410  SER A N   1 
ATOM   1667 C  CA  . SER A 1 207 ? 23.17073  23.08504 -7.55330  1.000 35.96824  ? 410  SER A CA  1 
ATOM   1668 C  C   . SER A 1 207 ? 21.85919  22.68856 -8.22205  1.000 34.83475  ? 410  SER A C   1 
ATOM   1669 O  O   . SER A 1 207 ? 21.30235  23.45366 -9.01566  1.000 34.73952  ? 410  SER A O   1 
ATOM   1670 C  CB  . SER A 1 207 ? 24.00076  23.96362 -8.49035  1.000 49.52493  ? 410  SER A CB  1 
ATOM   1671 O  OG  . SER A 1 207 ? 24.32882  23.25993 -9.67890  1.000 56.45147  ? 410  SER A OG  1 
ATOM   1672 N  N   . GLN A 1 208 ? 21.33824  21.50311 -7.90711  1.000 28.14425  ? 411  GLN A N   1 
ATOM   1673 C  CA  . GLN A 1 208 ? 20.20713  20.94779 -8.63780  1.000 28.51147  ? 411  GLN A CA  1 
ATOM   1674 C  C   . GLN A 1 208 ? 18.89363  21.00851 -7.86284  1.000 28.53275  ? 411  GLN A C   1 
ATOM   1675 O  O   . GLN A 1 208 ? 18.04950  20.14073 -8.05168  1.000 26.62999  ? 411  GLN A O   1 
ATOM   1676 C  CB  . GLN A 1 208 ? 20.47158  19.49223 -9.04808  1.000 31.83220  ? 411  GLN A CB  1 
ATOM   1677 C  CG  . GLN A 1 208 ? 21.27833  19.35275 -10.32389 1.000 32.23289  ? 411  GLN A CG  1 
ATOM   1678 C  CD  . GLN A 1 208 ? 21.15155  17.98884 -10.99850 1.000 36.58740  ? 411  GLN A CD  1 
ATOM   1679 O  OE1 . GLN A 1 208 ? 20.68035  17.01750 -10.40594 1.000 32.34168  ? 411  GLN A OE1 1 
ATOM   1680 N  NE2 . GLN A 1 208 ? 21.58085  17.91890 -12.25040 1.000 37.41613  ? 411  GLN A NE2 1 
ATOM   1681 N  N   . SER A 1 209 ? 18.66135  22.03098 -7.02531  1.000 29.55754  ? 412  SER A N   1 
ATOM   1682 C  CA  . SER A 1 209 ? 17.38494  22.01989 -6.30612  1.000 27.78314  ? 412  SER A CA  1 
ATOM   1683 C  C   . SER A 1 209 ? 16.19955  22.08811 -7.26497  1.000 27.09931  ? 412  SER A C   1 
ATOM   1684 O  O   . SER A 1 209 ? 15.16740  21.44967 -7.02014  1.000 26.93255  ? 412  SER A O   1 
ATOM   1685 C  CB  . SER A 1 209 ? 17.32386  23.15254 -5.27402  1.000 29.90744  ? 412  SER A CB  1 
ATOM   1686 O  OG  . SER A 1 209 ? 17.17735  24.41661 -5.89157  1.000 35.68413  ? 412  SER A OG  1 
ATOM   1687 N  N   . TRP A 1 210 ? 16.34460  22.80995 -8.38294  1.000 30.50503  ? 413  TRP A N   1 
ATOM   1688 C  CA  . TRP A 1 210 ? 15.30451  22.81786 -9.40607  1.000 26.80499  ? 413  TRP A CA  1 
ATOM   1689 C  C   . TRP A 1 210 ? 14.98282  21.40680 -9.89415  1.000 25.82677  ? 413  TRP A C   1 
ATOM   1690 O  O   . TRP A 1 210 ? 13.81924  21.08737 -10.16346 1.000 25.81199  ? 413  TRP A O   1 
ATOM   1691 C  CB  . TRP A 1 210 ? 15.74780  23.69634 -10.58049 1.000 28.69075  ? 413  TRP A CB  1 
ATOM   1692 C  CG  . TRP A 1 210 ? 16.98003  23.18174 -11.25705 1.000 30.44643  ? 413  TRP A CG  1 
ATOM   1693 C  CD1 . TRP A 1 210 ? 18.27779  23.41000 -10.89638 1.000 33.91326  ? 413  TRP A CD1 1 
ATOM   1694 C  CD2 . TRP A 1 210 ? 17.03028  22.34229 -12.41765 1.000 31.05359  ? 413  TRP A CD2 1 
ATOM   1695 N  NE1 . TRP A 1 210 ? 19.13278  22.77075 -11.76057 1.000 30.79251  ? 413  TRP A NE1 1 
ATOM   1696 C  CE2 . TRP A 1 210 ? 18.39002  22.09434 -12.69566 1.000 33.03073  ? 413  TRP A CE2 1 
ATOM   1697 C  CE3 . TRP A 1 210 ? 16.05642  21.76048 -13.23672 1.000 29.84619  ? 413  TRP A CE3 1 
ATOM   1698 C  CZ2 . TRP A 1 210 ? 18.79996  21.30675 -13.76852 1.000 35.86144  ? 413  TRP A CZ2 1 
ATOM   1699 C  CZ3 . TRP A 1 210 ? 16.46774  20.97430 -14.31150 1.000 32.64639  ? 413  TRP A CZ3 1 
ATOM   1700 C  CH2 . TRP A 1 210 ? 17.82519  20.75740 -14.56448 1.000 32.82762  ? 413  TRP A CH2 1 
ATOM   1701 N  N   . ALA A 1 211 ? 16.00406  20.55310 -10.03412 1.000 26.31664  ? 414  ALA A N   1 
ATOM   1702 C  CA  . ALA A 1 211 ? 15.79601  19.21351 -10.57660 1.000 24.55959  ? 414  ALA A CA  1 
ATOM   1703 C  C   . ALA A 1 211 ? 15.28530  18.24401 -9.51244  1.000 21.05834  ? 414  ALA A C   1 
ATOM   1704 O  O   . ALA A 1 211 ? 14.54251  17.31335 -9.82973  1.000 22.30205  ? 414  ALA A O   1 
ATOM   1705 C  CB  . ALA A 1 211 ? 17.09354  18.68683 -11.18858 1.000 24.56148  ? 414  ALA A CB  1 
ATOM   1706 N  N   . LYS A 1 212 ? 15.67737  18.43353 -8.25464  1.000 23.33076  ? 415  LYS A N   1 
ATOM   1707 C  CA  . LYS A 1 212 ? 15.08138  17.62595 -7.19845  1.000 22.60275  ? 415  LYS A CA  1 
ATOM   1708 C  C   . LYS A 1 212 ? 13.59886  17.93641 -7.05798  1.000 21.05945  ? 415  LYS A C   1 
ATOM   1709 O  O   . LYS A 1 212 ? 12.77820  17.02695 -6.86467  1.000 19.20893  ? 415  LYS A O   1 
ATOM   1710 C  CB  . LYS A 1 212 ? 15.80875  17.87757 -5.87431  1.000 22.67790  ? 415  LYS A CB  1 
ATOM   1711 C  CG  . LYS A 1 212 ? 17.29370  17.63490 -5.92305  1.000 23.09767  ? 415  LYS A CG  1 
ATOM   1712 C  CD  . LYS A 1 212 ? 17.64851  16.20279 -6.34138  1.000 22.97504  ? 415  LYS A CD  1 
ATOM   1713 C  CE  . LYS A 1 212 ? 19.17279  16.04609 -6.30315  1.000 23.87871  ? 415  LYS A CE  1 
ATOM   1714 N  NZ  . LYS A 1 212 ? 19.65953  14.71434 -6.78117  1.000 25.78692  ? 415  LYS A NZ  1 
ATOM   1715 N  N   . THR A 1 213 ? 13.24860  19.22732 -7.13561  1.000 22.67854  ? 416  THR A N   1 
ATOM   1716 C  CA  . THR A 1 213 ? 11.85350  19.63973 -7.07338  1.000 21.29717  ? 416  THR A CA  1 
ATOM   1717 C  C   . THR A 1 213 ? 11.07660  19.09060 -8.26389  1.000 23.95800  ? 416  THR A C   1 
ATOM   1718 O  O   . THR A 1 213 ? 10.00560  18.49311 -8.09926  1.000 20.31954  ? 416  THR A O   1 
ATOM   1719 C  CB  . THR A 1 213 ? 11.75827  21.16872 -7.01972  1.000 23.95299  ? 416  THR A CB  1 
ATOM   1720 O  OG1 . THR A 1 213 ? 12.44181  21.65299 -5.84998  1.000 26.17168  ? 416  THR A OG1 1 
ATOM   1721 C  CG2 . THR A 1 213 ? 10.29302  21.60363 -6.97937  1.000 23.52097  ? 416  THR A CG2 1 
ATOM   1722 N  N   . ALA A 1 214 ? 11.62063  19.24498 -9.47425  1.000 22.33804  ? 417  ALA A N   1 
ATOM   1723 C  CA  . ALA A 1 214 ? 10.97441  18.62655 -10.63041 1.000 23.36781  ? 417  ALA A CA  1 
ATOM   1724 C  C   . ALA A 1 214 ? 10.80852  17.11767 -10.44731 1.000 19.18577  ? 417  ALA A C   1 
ATOM   1725 O  O   . ALA A 1 214 ? 9.75032   16.56418 -10.77466 1.000 20.27788  ? 417  ALA A O   1 
ATOM   1726 C  CB  . ALA A 1 214 ? 11.76004  18.92990 -11.91013 1.000 21.84541  ? 417  ALA A CB  1 
ATOM   1727 N  N   . SER A 1 215 ? 11.84228  16.43651 -9.93729  1.000 21.74788  ? 418  SER A N   1 
ATOM   1728 C  CA  . SER A 1 215 ? 11.77312  14.98138 -9.77701  1.000 19.53797  ? 418  SER A CA  1 
ATOM   1729 C  C   . SER A 1 215 ? 10.67579  14.57637 -8.79559  1.000 20.35206  ? 418  SER A C   1 
ATOM   1730 O  O   . SER A 1 215 ? 9.92776   13.62783 -9.05535  1.000 20.88342  ? 418  SER A O   1 
ATOM   1731 C  CB  . SER A 1 215 ? 13.11846  14.41387 -9.30628  1.000 22.22262  ? 418  SER A CB  1 
ATOM   1732 O  OG  . SER A 1 215 ? 14.13998  14.59672 -10.27228 1.000 22.96056  ? 418  SER A OG  1 
ATOM   1733 N  N   . ASN A 1 216 ? 10.55586  15.28231 -7.66571  1.000 19.23398  ? 419  ASN A N   1 
ATOM   1734 C  CA  . ASN A 1 216 ? 9.48984   14.95397 -6.72188  1.000 21.64432  ? 419  ASN A CA  1 
ATOM   1735 C  C   . ASN A 1 216 ? 8.12905   15.09038 -7.37325  1.000 17.81643  ? 419  ASN A C   1 
ATOM   1736 O  O   . ASN A 1 216 ? 7.24919   14.24017 -7.18446  1.000 17.81189  ? 419  ASN A O   1 
ATOM   1737 C  CB  . ASN A 1 216 ? 9.54298   15.86914 -5.48837  1.000 17.89976  ? 419  ASN A CB  1 
ATOM   1738 C  CG  . ASN A 1 216 ? 10.75362  15.62384 -4.62788  1.000 19.98433  ? 419  ASN A CG  1 
ATOM   1739 O  OD1 . ASN A 1 216 ? 11.24770  14.50846 -4.52440  1.000 18.66268  ? 419  ASN A OD1 1 
ATOM   1740 N  ND2 . ASN A 1 216 ? 11.23128  16.68481 -3.97787  1.000 19.38519  ? 419  ASN A ND2 1 
ATOM   1741 N  N   . MET A 1 217 ? 7.93002   16.18170 -8.12069  1.000 19.56298  ? 420  MET A N   1 
ATOM   1742 C  CA  . MET A 1 217 ? 6.64865   16.42366 -8.76798  1.000 18.70764  ? 420  MET A CA  1 
ATOM   1743 C  C   . MET A 1 217 ? 6.38080   15.38819 -9.84702  1.000 20.10072  ? 420  MET A C   1 
ATOM   1744 O  O   . MET A 1 217 ? 5.24218   14.94405 -9.99965  1.000 19.45934  ? 420  MET A O   1 
ATOM   1745 C  CB  . MET A 1 217 ? 6.60561   17.83943 -9.34326  1.000 22.00345  ? 420  MET A CB  1 
ATOM   1746 C  CG  . MET A 1 217 ? 6.73271   18.91754 -8.25348  1.000 21.86908  ? 420  MET A CG  1 
ATOM   1747 S  SD  . MET A 1 217 ? 7.13855   20.55747 -8.93768  1.000 25.73356  ? 420  MET A SD  1 
ATOM   1748 C  CE  . MET A 1 217 ? 5.54934   20.98128 -9.63379  1.000 26.26062  ? 420  MET A CE  1 
ATOM   1749 N  N   . LEU A 1 218 ? 7.42729   14.98562 -10.58209 1.000 18.77388  ? 421  LEU A N   1 
ATOM   1750 C  CA  . LEU A 1 218 ? 7.29667   13.96081 -11.61399 1.000 21.71601  ? 421  LEU A CA  1 
ATOM   1751 C  C   . LEU A 1 218 ? 6.99307   12.58567 -11.01608 1.000 19.88646  ? 421  LEU A C   1 
ATOM   1752 O  O   . LEU A 1 218 ? 6.21588   11.82466 -11.58713 1.000 18.31695  ? 421  LEU A O   1 
ATOM   1753 C  CB  . LEU A 1 218 ? 8.56395   13.90868 -12.46844 1.000 19.09215  ? 421  LEU A CB  1 
ATOM   1754 C  CG  . LEU A 1 218 ? 8.73441   15.10471 -13.41345 1.000 22.08296  ? 421  LEU A CG  1 
ATOM   1755 C  CD1 . LEU A 1 218 ? 10.16105  15.18381 -13.91669 1.000 25.89766  ? 421  LEU A CD1 1 
ATOM   1756 C  CD2 . LEU A 1 218 ? 7.75682   14.99784 -14.59461 1.000 26.69570  ? 421  LEU A CD2 1 
ATOM   1757 N  N   . HIS A 1 219 ? 7.58978   12.24305 -9.87400  1.000 17.62600  ? 422  HIS A N   1 
ATOM   1758 C  CA  . HIS A 1 219 ? 7.22004   10.98635 -9.21599  1.000 19.04916  ? 422  HIS A CA  1 
ATOM   1759 C  C   . HIS A 1 219 ? 5.73079   10.96141 -8.90082  1.000 18.70546  ? 422  HIS A C   1 
ATOM   1760 O  O   . HIS A 1 219 ? 5.03851   9.96788  -9.15407  1.000 19.01508  ? 422  HIS A O   1 
ATOM   1761 C  CB  . HIS A 1 219 ? 8.03690   10.78435 -7.92361  1.000 19.20456  ? 422  HIS A CB  1 
ATOM   1762 C  CG  . HIS A 1 219 ? 9.35892   10.10322 -8.12768  1.000 19.29961  ? 422  HIS A CG  1 
ATOM   1763 N  ND1 . HIS A 1 219 ? 9.47004   8.78790  -8.54415  1.000 21.12776  ? 422  HIS A ND1 1 
ATOM   1764 C  CD2 . HIS A 1 219 ? 10.62502  10.54638 -7.95263  1.000 20.08498  ? 422  HIS A CD2 1 
ATOM   1765 C  CE1 . HIS A 1 219 ? 10.75007  8.46016  -8.61927  1.000 20.77144  ? 422  HIS A CE1 1 
ATOM   1766 N  NE2 . HIS A 1 219 ? 11.47053  9.50956  -8.26799  1.000 19.73760  ? 422  HIS A NE2 1 
ATOM   1767 N  N   . TRP A 1 220 ? 5.22011   12.05977 -8.33864  1.000 18.71693  ? 423  TRP A N   1 
ATOM   1768 C  CA  . TRP A 1 220 ? 3.79144   12.16163 -8.07048  1.000 20.39581  ? 423  TRP A CA  1 
ATOM   1769 C  C   . TRP A 1 220 ? 2.96805   12.02113 -9.34559  1.000 18.60736  ? 423  TRP A C   1 
ATOM   1770 O  O   . TRP A 1 220 ? 1.94855   11.32491 -9.36009  1.000 20.93378  ? 423  TRP A O   1 
ATOM   1771 C  CB  . TRP A 1 220 ? 3.50971   13.49541 -7.37778  1.000 19.57822  ? 423  TRP A CB  1 
ATOM   1772 C  CG  . TRP A 1 220 ? 2.06393   13.89264 -7.30703  1.000 20.39614  ? 423  TRP A CG  1 
ATOM   1773 C  CD1 . TRP A 1 220 ? 1.17609   13.59285 -6.30894  1.000 20.84822  ? 423  TRP A CD1 1 
ATOM   1774 C  CD2 . TRP A 1 220 ? 1.34966   14.71405 -8.24555  1.000 19.38027  ? 423  TRP A CD2 1 
ATOM   1775 N  NE1 . TRP A 1 220 ? -0.03858  14.16225 -6.57781  1.000 20.96698  ? 423  TRP A NE1 1 
ATOM   1776 C  CE2 . TRP A 1 220 ? 0.03527   14.84194 -7.76709  1.000 22.48442  ? 423  TRP A CE2 1 
ATOM   1777 C  CE3 . TRP A 1 220 ? 1.69665   15.33883 -9.44986  1.000 22.69074  ? 423  TRP A CE3 1 
ATOM   1778 C  CZ2 . TRP A 1 220 ? -0.93958  15.58212 -8.43803  1.000 24.84071  ? 423  TRP A CZ2 1 
ATOM   1779 C  CZ3 . TRP A 1 220 ? 0.71800   16.06788 -10.13431 1.000 24.91687  ? 423  TRP A CZ3 1 
ATOM   1780 C  CH2 . TRP A 1 220 ? -0.58378  16.18371 -9.62193  1.000 26.86047  ? 423  TRP A CH2 1 
ATOM   1781 N  N   . TRP A 1 221 ? 3.39277   12.68068 -10.41729 1.000 19.90423  ? 424  TRP A N   1 
ATOM   1782 C  CA  . TRP A 1 221 ? 2.65108   12.64921 -11.67278 1.000 19.50051  ? 424  TRP A CA  1 
ATOM   1783 C  C   . TRP A 1 221 ? 2.61885   11.24793 -12.29007 1.000 18.32798  ? 424  TRP A C   1 
ATOM   1784 O  O   . TRP A 1 221 ? 1.56775   10.79548 -12.76305 1.000 20.88401  ? 424  TRP A O   1 
ATOM   1785 C  CB  . TRP A 1 221 ? 3.29384   13.66562 -12.61475 1.000 19.35316  ? 424  TRP A CB  1 
ATOM   1786 C  CG  . TRP A 1 221 ? 2.53539   14.05073 -13.84657 1.000 20.59590  ? 424  TRP A CG  1 
ATOM   1787 C  CD1 . TRP A 1 221 ? 1.69352   15.11582 -13.98925 1.000 24.39055  ? 424  TRP A CD1 1 
ATOM   1788 C  CD2 . TRP A 1 221 ? 2.63592   13.43832 -15.14019 1.000 24.45753  ? 424  TRP A CD2 1 
ATOM   1789 N  NE1 . TRP A 1 221 ? 1.24227   15.19208 -15.29014 1.000 25.18159  ? 424  TRP A NE1 1 
ATOM   1790 C  CE2 . TRP A 1 221 ? 1.79965   14.17262 -16.01587 1.000 24.69424  ? 424  TRP A CE2 1 
ATOM   1791 C  CE3 . TRP A 1 221 ? 3.32925   12.33087 -15.63310 1.000 21.08698  ? 424  TRP A CE3 1 
ATOM   1792 C  CZ2 . TRP A 1 221 ? 1.64793   13.84081 -17.37061 1.000 25.10833  ? 424  TRP A CZ2 1 
ATOM   1793 C  CZ3 . TRP A 1 221 ? 3.17267   11.99224 -16.99174 1.000 24.02589  ? 424  TRP A CZ3 1 
ATOM   1794 C  CH2 . TRP A 1 221 ? 2.33566   12.75189 -17.83480 1.000 23.48270  ? 424  TRP A CH2 1 
ATOM   1795 N  N   . PHE A 1 222 ? 3.75760   10.54978 -12.30555 1.000 20.50032  ? 425  PHE A N   1 
ATOM   1796 C  CA  . PHE A 1 222 ? 3.77854   9.16633  -12.79066 1.000 19.98124  ? 425  PHE A CA  1 
ATOM   1797 C  C   . PHE A 1 222 ? 2.86884   8.27538  -11.95292 1.000 22.04484  ? 425  PHE A C   1 
ATOM   1798 O  O   . PHE A 1 222 ? 2.19153   7.38246  -12.48177 1.000 22.03794  ? 425  PHE A O   1 
ATOM   1799 C  CB  . PHE A 1 222 ? 5.21549   8.62157  -12.78270 1.000 18.46112  ? 425  PHE A CB  1 
ATOM   1800 C  CG  . PHE A 1 222 ? 5.99136   8.88105  -14.05770 1.000 19.08948  ? 425  PHE A CG  1 
ATOM   1801 C  CD1 . PHE A 1 222 ? 6.45313   10.15591 -14.37136 1.000 23.25073  ? 425  PHE A CD1 1 
ATOM   1802 C  CD2 . PHE A 1 222 ? 6.31042   7.82526  -14.90650 1.000 24.87052  ? 425  PHE A CD2 1 
ATOM   1803 C  CE1 . PHE A 1 222 ? 7.17680   10.38481 -15.54101 1.000 22.89871  ? 425  PHE A CE1 1 
ATOM   1804 C  CE2 . PHE A 1 222 ? 7.04287   8.04616  -16.08341 1.000 25.98430  ? 425  PHE A CE2 1 
ATOM   1805 C  CZ  . PHE A 1 222 ? 7.47174   9.31342  -16.39919 1.000 24.90946  ? 425  PHE A CZ  1 
ATOM   1806 N  N   . GLU A 1 223 ? 2.82593   8.50739  -10.64009 1.000 19.86000  ? 426  GLU A N   1 
ATOM   1807 C  CA  . GLU A 1 223 ? 1.95567   7.70646  -9.79029  1.000 22.34926  ? 426  GLU A CA  1 
ATOM   1808 C  C   . GLU A 1 223 ? 0.48475   8.02242  -10.05130 1.000 21.74952  ? 426  GLU A C   1 
ATOM   1809 O  O   . GLU A 1 223 ? -0.33731  7.10638  -10.19852 1.000 24.15554  ? 426  GLU A O   1 
ATOM   1810 C  CB  . GLU A 1 223 ? 2.32995   7.92194  -8.31468  1.000 20.04609  ? 426  GLU A CB  1 
ATOM   1811 C  CG  . GLU A 1 223 ? 1.51978   7.04742  -7.33810  1.000 24.69451  ? 426  GLU A CG  1 
ATOM   1812 C  CD  . GLU A 1 223 ? 1.83347   5.55596  -7.47277  1.000 33.91840  ? 426  GLU A CD  1 
ATOM   1813 O  OE1 . GLU A 1 223 ? 2.87106   5.20419  -8.07516  1.000 28.71484  ? 426  GLU A OE1 1 
ATOM   1814 O  OE2 . GLU A 1 223 ? 1.04345   4.73037  -6.96627  1.000 33.53461  ? 426  GLU A OE2 1 
ATOM   1815 N  N   . GLN A 1 224 ? 0.12524   9.31170  -10.12877 1.000 23.65027  ? 427  GLN A N   1 
ATOM   1816 C  CA  . GLN A 1 224 ? -1.28151  9.65267  -10.32603 1.000 22.93940  ? 427  GLN A CA  1 
ATOM   1817 C  C   . GLN A 1 224 ? -1.76643  9.18475  -11.68809 1.000 27.11314  ? 427  GLN A C   1 
ATOM   1818 O  O   . GLN A 1 224 ? -2.91832  8.77461  -11.83474 1.000 28.56603  ? 427  GLN A O   1 
ATOM   1819 C  CB  . GLN A 1 224 ? -1.51511  11.15953 -10.20096 1.000 29.59204  ? 427  GLN A CB  1 
ATOM   1820 C  CG  . GLN A 1 224 ? -1.12914  11.78104 -8.86110  1.000 26.91818  ? 427  GLN A CG  1 
ATOM   1821 C  CD  . GLN A 1 224 ? -1.45552  10.90711 -7.66614  1.000 34.97304  ? 427  GLN A CD  1 
ATOM   1822 O  OE1 . GLN A 1 224 ? -2.62207  10.65941 -7.35995  1.000 37.01082  ? 427  GLN A OE1 1 
ATOM   1823 N  NE2 . GLN A 1 224 ? -0.41837  10.43427 -6.98121  1.000 36.49317  ? 427  GLN A NE2 1 
ATOM   1824 N  N   . ASN A 1 225 ? -0.89689  9.23998  -12.69048 1.000 24.25931  ? 428  ASN A N   1 
ATOM   1825 C  CA  . ASN A 1 225 ? -1.25464  8.89041  -14.05666 1.000 25.53758  ? 428  ASN A CA  1 
ATOM   1826 C  C   . ASN A 1 225 ? -0.84184  7.47418  -14.41842 1.000 25.16523  ? 428  ASN A C   1 
ATOM   1827 O  O   . ASN A 1 225 ? -0.75905  7.15720  -15.60573 1.000 26.72852  ? 428  ASN A O   1 
ATOM   1828 C  CB  . ASN A 1 225 ? -0.61658  9.87722  -15.04054 1.000 24.41974  ? 428  ASN A CB  1 
ATOM   1829 C  CG  . ASN A 1 225 ? -1.37017  11.17719 -15.14033 1.000 31.43326  ? 428  ASN A CG  1 
ATOM   1830 O  OD1 . ASN A 1 225 ? -2.59347  11.19143 -15.09155 1.000 34.05582  ? 428  ASN A OD1 1 
ATOM   1831 N  ND2 . ASN A 1 225 ? -0.64148  12.28267 -15.29582 1.000 27.26263  ? 428  ASN A ND2 1 
ATOM   1832 N  N   . LYS A 1 226 ? -0.59108  6.60741  -13.42852 1.000 25.61715  ? 429  LYS A N   1 
ATOM   1833 C  CA  . LYS A 1 226 ? 0.04054   5.33107  -13.75131 1.000 25.06304  ? 429  LYS A CA  1 
ATOM   1834 C  C   . LYS A 1 226 ? -0.80258  4.50004  -14.71757 1.000 26.70722  ? 429  LYS A C   1 
ATOM   1835 O  O   . LYS A 1 226 ? -0.24359  3.79095  -15.55750 1.000 30.96388  ? 429  LYS A O   1 
ATOM   1836 C  CB  . LYS A 1 226 ? 0.36471   4.53360  -12.48458 1.000 29.98010  ? 429  LYS A CB  1 
ATOM   1837 C  CG  . LYS A 1 226 ? -0.80057  4.02900  -11.67733 1.000 34.77001  ? 429  LYS A CG  1 
ATOM   1838 C  CD  . LYS A 1 226 ? -0.24967  3.39896  -10.39050 1.000 37.69643  ? 429  LYS A CD  1 
ATOM   1839 C  CE  . LYS A 1 226 ? -1.33118  3.13592  -9.35829  1.000 50.42456  ? 429  LYS A CE  1 
ATOM   1840 N  NZ  . LYS A 1 226 ? -0.72826  2.57048  -8.11363  1.000 54.69866  ? 429  LYS A NZ  1 
ATOM   1841 N  N   . ASP A 1 227 ? -2.13404  4.59521  -14.65092 1.000 27.94725  ? 430  ASP A N   1 
ATOM   1842 C  CA  . ASP A 1 227 ? -2.95496  3.80492  -15.56723 1.000 32.69261  ? 430  ASP A CA  1 
ATOM   1843 C  C   . ASP A 1 227 ? -2.90449  4.36314  -16.98635 1.000 31.28883  ? 430  ASP A C   1 
ATOM   1844 O  O   . ASP A 1 227 ? -2.89572  3.59514  -17.96080 1.000 31.73930  ? 430  ASP A O   1 
ATOM   1845 C  CB  . ASP A 1 227 ? -4.39839  3.72566  -15.06190 1.000 33.03511  ? 430  ASP A CB  1 
ATOM   1846 C  CG  . ASP A 1 227 ? -4.52868  2.89442  -13.78861 1.000 46.89042  ? 430  ASP A CG  1 
ATOM   1847 O  OD1 . ASP A 1 227 ? -3.61110  2.09723  -13.48555 1.000 41.98495  ? 430  ASP A OD1 1 
ATOM   1848 O  OD2 . ASP A 1 227 ? -5.55190  3.03891  -13.08827 1.000 50.14754  ? 430  ASP A OD2 1 
ATOM   1849 N  N   . TYR A 1 228 ? -2.88003  5.69306  -17.13101 1.000 31.03464  ? 431  TYR A N   1 
ATOM   1850 C  CA  . TYR A 1 228 ? -2.71772  6.27841  -18.46013 1.000 28.85059  ? 431  TYR A CA  1 
ATOM   1851 C  C   . TYR A 1 228 ? -1.36245  5.92470  -19.04804 1.000 29.22393  ? 431  TYR A C   1 
ATOM   1852 O  O   . TYR A 1 228 ? -1.25409  5.61823  -20.24574 1.000 28.55575  ? 431  TYR A O   1 
ATOM   1853 C  CB  . TYR A 1 228 ? -2.87460  7.79952  -18.41089 1.000 29.56628  ? 431  TYR A CB  1 
ATOM   1854 C  CG  . TYR A 1 228 ? -4.30222  8.26363  -18.28848 1.000 33.80357  ? 431  TYR A CG  1 
ATOM   1855 C  CD1 . TYR A 1 228 ? -4.69534  9.06116  -17.22685 1.000 37.75448  ? 431  TYR A CD1 1 
ATOM   1856 C  CD2 . TYR A 1 228 ? -5.25778  7.90583  -19.23422 1.000 46.65617  ? 431  TYR A CD2 1 
ATOM   1857 C  CE1 . TYR A 1 228 ? -5.99994  9.49222  -17.09937 1.000 44.63380  ? 431  TYR A CE1 1 
ATOM   1858 C  CE2 . TYR A 1 228 ? -6.57040  8.33474  -19.11761 1.000 52.14579  ? 431  TYR A CE2 1 
ATOM   1859 C  CZ  . TYR A 1 228 ? -6.93278  9.12783  -18.04236 1.000 52.43355  ? 431  TYR A CZ  1 
ATOM   1860 O  OH  . TYR A 1 228 ? -8.22917  9.56647  -17.90543 1.000 59.77153  ? 431  TYR A OH  1 
ATOM   1861 N  N   . ILE A 1 229 ? -0.32045  5.96123  -18.21897 1.000 25.78962  ? 432  ILE A N   1 
ATOM   1862 C  CA  . ILE A 1 229 ? 1.03323   5.67087  -18.67317 1.000 28.62910  ? 432  ILE A CA  1 
ATOM   1863 C  C   . ILE A 1 229 ? 1.16304   4.20691  -19.08042 1.000 31.00457  ? 432  ILE A C   1 
ATOM   1864 O  O   . ILE A 1 229 ? 1.88349   3.87852  -20.02966 1.000 29.55774  ? 432  ILE A O   1 
ATOM   1865 C  CB  . ILE A 1 229 ? 2.04548   6.07624  -17.58407 1.000 26.90673  ? 432  ILE A CB  1 
ATOM   1866 C  CG1 . ILE A 1 229 ? 2.07643   7.60260  -17.47544 1.000 23.94906  ? 432  ILE A CG1 1 
ATOM   1867 C  CG2 . ILE A 1 229 ? 3.42646   5.53621  -17.90381 1.000 25.09709  ? 432  ILE A CG2 1 
ATOM   1868 C  CD1 . ILE A 1 229 ? 2.69834   8.11864  -16.15502 1.000 23.30241  ? 432  ILE A CD1 1 
ATOM   1869 N  N   A GLU A 1 230 ? 0.47297   3.30546  -18.37423 0.511 31.04400  ? 433  GLU A N   1 
ATOM   1870 N  N   B GLU A 1 230 ? 0.46329   3.30505  -18.38500 0.489 31.04207  ? 433  GLU A N   1 
ATOM   1871 C  CA  A GLU A 1 230 ? 0.45560   1.91043  -18.79972 0.511 30.48914  ? 433  GLU A CA  1 
ATOM   1872 C  CA  B GLU A 1 230 ? 0.47025   1.90837  -18.80707 0.489 30.49680  ? 433  GLU A CA  1 
ATOM   1873 C  C   A GLU A 1 230 ? -0.17606  1.77103  -20.17870 0.511 33.89199  ? 433  GLU A C   1 
ATOM   1874 C  C   B GLU A 1 230 ? -0.19761  1.74296  -20.16794 0.489 33.88467  ? 433  GLU A C   1 
ATOM   1875 O  O   A GLU A 1 230 ? 0.31814   1.01471  -21.02246 0.511 32.21578  ? 433  GLU A O   1 
ATOM   1876 O  O   B GLU A 1 230 ? 0.25207   0.93722  -20.98958 0.489 32.28598  ? 433  GLU A O   1 
ATOM   1877 C  CB  A GLU A 1 230 ? -0.28931  1.04578  -17.78025 0.511 32.80662  ? 433  GLU A CB  1 
ATOM   1878 C  CB  B GLU A 1 230 ? -0.20884  1.02581  -17.75729 0.489 32.81861  ? 433  GLU A CB  1 
ATOM   1879 C  CG  A GLU A 1 230 ? -0.44029  -0.40768 -18.20084 0.511 32.53934  ? 433  GLU A CG  1 
ATOM   1880 C  CG  B GLU A 1 230 ? 0.59198   0.88156  -16.46912 0.489 33.54823  ? 433  GLU A CG  1 
ATOM   1881 C  CD  A GLU A 1 230 ? 0.89013   -1.06491 -18.51476 0.511 37.04637  ? 433  GLU A CD  1 
ATOM   1882 C  CD  B GLU A 1 230 ? 2.00194   0.36629  -16.71248 0.489 36.29402  ? 433  GLU A CD  1 
ATOM   1883 O  OE1 A GLU A 1 230 ? 1.88361   -0.77037 -17.81948 0.511 41.53673  ? 433  GLU A OE1 1 
ATOM   1884 O  OE1 B GLU A 1 230 ? 2.17364   -0.52151 -17.57469 0.489 42.12909  ? 433  GLU A OE1 1 
ATOM   1885 O  OE2 A GLU A 1 230 ? 0.94634   -1.86682 -19.46899 0.511 44.03799  ? 433  GLU A OE2 1 
ATOM   1886 O  OE2 B GLU A 1 230 ? 2.94105   0.86144  -16.05827 0.489 35.75675  ? 433  GLU A OE2 1 
ATOM   1887 N  N   . GLN A 1 231 ? -1.26173  2.50708  -20.43183 1.000 32.37723  ? 434  GLN A N   1 
ATOM   1888 C  CA  . GLN A 1 231 ? -1.87544  2.48582  -21.75851 1.000 31.61561  ? 434  GLN A CA  1 
ATOM   1889 C  C   . GLN A 1 231 ? -0.93247  3.06352  -22.80757 1.000 31.07053  ? 434  GLN A C   1 
ATOM   1890 O  O   . GLN A 1 231 ? -0.85260  2.55762  -23.93541 1.000 30.71225  ? 434  GLN A O   1 
ATOM   1891 C  CB  . GLN A 1 231 ? -3.19161  3.26526  -21.73761 1.000 36.84687  ? 434  GLN A CB  1 
ATOM   1892 C  CG  . GLN A 1 231 ? -4.28662  2.58339  -20.94341 1.000 36.93033  ? 434  GLN A CG  1 
ATOM   1893 C  CD  . GLN A 1 231 ? -4.59525  1.21440  -21.49985 1.000 51.63241  ? 434  GLN A CD  1 
ATOM   1894 O  OE1 . GLN A 1 231 ? -4.99567  1.08277  -22.65660 1.000 53.96497  ? 434  GLN A OE1 1 
ATOM   1895 N  NE2 . GLN A 1 231 ? -4.38127  0.18146  -20.69136 1.000 53.89080  ? 434  GLN A NE2 1 
ATOM   1896 N  N   . TYR A 1 232 ? -0.20840  4.12364  -22.44753 1.000 28.21210  ? 435  TYR A N   1 
ATOM   1897 C  CA  . TYR A 1 232 ? 0.78596   4.69311  -23.34714 1.000 29.10936  ? 435  TYR A CA  1 
ATOM   1898 C  C   . TYR A 1 232 ? 1.84425   3.66326  -23.72323 1.000 29.85779  ? 435  TYR A C   1 
ATOM   1899 O  O   . TYR A 1 232 ? 2.17201   3.49075  -24.90471 1.000 28.35758  ? 435  TYR A O   1 
ATOM   1900 C  CB  . TYR A 1 232 ? 1.42288   5.91297  -22.67867 1.000 29.51035  ? 435  TYR A CB  1 
ATOM   1901 C  CG  . TYR A 1 232 ? 2.24560   6.74450  -23.62222 1.000 25.89490  ? 435  TYR A CG  1 
ATOM   1902 C  CD1 . TYR A 1 232 ? 1.64685   7.68876  -24.44557 1.000 28.73072  ? 435  TYR A CD1 1 
ATOM   1903 C  CD2 . TYR A 1 232 ? 3.62109   6.57365  -23.70252 1.000 26.86982  ? 435  TYR A CD2 1 
ATOM   1904 C  CE1 . TYR A 1 232 ? 2.39891   8.44579  -25.33156 1.000 30.52308  ? 435  TYR A CE1 1 
ATOM   1905 C  CE2 . TYR A 1 232 ? 4.37795   7.32904  -24.57005 1.000 29.40538  ? 435  TYR A CE2 1 
ATOM   1906 C  CZ  . TYR A 1 232 ? 3.76567   8.26151  -25.37847 1.000 31.49328  ? 435  TYR A CZ  1 
ATOM   1907 O  OH  . TYR A 1 232 ? 4.52526   9.00890  -26.24335 1.000 34.01379  ? 435  TYR A OH  1 
ATOM   1908 N  N   . LYS A 1 233 ? 2.39453   2.96815  -22.72765 1.000 30.20710  ? 436  LYS A N   1 
ATOM   1909 C  CA  . LYS A 1 233 ? 3.38908   1.93374  -23.00036 1.000 30.77894  ? 436  LYS A CA  1 
ATOM   1910 C  C   . LYS A 1 233 ? 2.83155   0.84060  -23.90262 1.000 30.15057  ? 436  LYS A C   1 
ATOM   1911 O  O   . LYS A 1 233 ? 3.57794   0.23757  -24.68189 1.000 32.61916  ? 436  LYS A O   1 
ATOM   1912 C  CB  . LYS A 1 233 ? 3.89059   1.32946  -21.68715 1.000 33.76779  ? 436  LYS A CB  1 
ATOM   1913 C  CG  . LYS A 1 233 ? 4.73161   2.28801  -20.85346 1.000 34.81952  ? 436  LYS A CG  1 
ATOM   1914 C  CD  . LYS A 1 233 ? 4.75930   1.91269  -19.36965 1.000 40.21216  ? 436  LYS A CD  1 
ATOM   1915 C  CE  . LYS A 1 233 ? 5.48338   0.59906  -19.13194 1.000 42.27713  ? 436  LYS A CE  1 
ATOM   1916 N  NZ  . LYS A 1 233 ? 5.73691   0.41729  -17.66939 1.000 58.01555  ? 436  LYS A NZ  1 
ATOM   1917 N  N   . GLN A 1 234 ? 1.52734   0.57092  -23.82112 1.000 30.17583  ? 437  GLN A N   1 
ATOM   1918 C  CA  . GLN A 1 234 ? 0.95775   -0.48317 -24.64807 1.000 33.93347  ? 437  GLN A CA  1 
ATOM   1919 C  C   . GLN A 1 234 ? 0.63311   -0.01283 -26.05544 1.000 34.51292  ? 437  GLN A C   1 
ATOM   1920 O  O   . GLN A 1 234 ? 0.70424   -0.81345 -26.99457 1.000 33.90051  ? 437  GLN A O   1 
ATOM   1921 C  CB  . GLN A 1 234 ? -0.30706  -1.04282 -24.00080 1.000 36.57107  ? 437  GLN A CB  1 
ATOM   1922 C  CG  . GLN A 1 234 ? -0.03761  -1.88697 -22.76843 1.000 45.55917  ? 437  GLN A CG  1 
ATOM   1923 C  CD  . GLN A 1 234 ? -1.30796  -2.24239 -22.01072 1.000 53.89074  ? 437  GLN A CD  1 
ATOM   1924 O  OE1 . GLN A 1 234 ? -2.41855  -1.98036 -22.47395 1.000 58.99159  ? 437  GLN A OE1 1 
ATOM   1925 N  NE2 . GLN A 1 234 ? -1.14596  -2.83062 -20.83222 1.000 51.47673  ? 437  GLN A NE2 1 
ATOM   1926 N  N   . LYS A 1 235 ? 0.26803   1.25785  -26.22286 1.000 32.95939  ? 438  LYS A N   1 
ATOM   1927 C  CA  . LYS A 1 235 ? -0.33075  1.71587  -27.46853 1.000 30.86719  ? 438  LYS A CA  1 
ATOM   1928 C  C   . LYS A 1 235 ? 0.53397   2.68487  -28.26179 1.000 30.91065  ? 438  LYS A C   1 
ATOM   1929 O  O   . LYS A 1 235 ? 0.37566   2.75994  -29.48755 1.000 32.60996  ? 438  LYS A O   1 
ATOM   1930 C  CB  . LYS A 1 235 ? -1.69062  2.37713  -27.18759 1.000 34.17449  ? 438  LYS A CB  1 
ATOM   1931 C  CG  . LYS A 1 235 ? -2.74394  1.39856  -26.66013 1.000 42.94040  ? 438  LYS A CG  1 
ATOM   1932 C  CD  . LYS A 1 235 ? -3.95212  2.12224  -26.07318 1.000 46.88085  ? 438  LYS A CD  1 
ATOM   1933 C  CE  . LYS A 1 235 ? -5.20632  1.24531  -26.09627 1.000 52.60136  ? 438  LYS A CE  1 
ATOM   1934 N  NZ  . LYS A 1 235 ? -5.01469  -0.06258 -25.40596 1.000 58.26548  ? 438  LYS A NZ  1 
ATOM   1935 N  N   . ALA A 1 236 ? 1.44900   3.39567  -27.61760 1.000 28.96773  ? 439  ALA A N   1 
ATOM   1936 C  CA  . ALA A 1 236 ? 2.28159   4.36530  -28.31550 1.000 26.09958  ? 439  ALA A CA  1 
ATOM   1937 C  C   . ALA A 1 236 ? 3.42246   3.67282  -29.04974 1.000 30.38759  ? 439  ALA A C   1 
ATOM   1938 O  O   . ALA A 1 236 ? 3.82618   2.55517  -28.72142 1.000 30.28704  ? 439  ALA A O   1 
ATOM   1939 C  CB  . ALA A 1 236 ? 2.85892   5.38954  -27.33964 1.000 25.72227  ? 439  ALA A CB  1 
ATOM   1940 N  N   . ALA A 1 237 ? 3.93866   4.35275  -30.07154 1.000 25.39595  ? 440  ALA A N   1 
ATOM   1941 C  CA  . ALA A 1 237 ? 5.10533   3.86232  -30.80485 1.000 25.72441  ? 440  ALA A CA  1 
ATOM   1942 C  C   . ALA A 1 237 ? 6.32072   4.48652  -30.13386 1.000 29.87212  ? 440  ALA A C   1 
ATOM   1943 O  O   . ALA A 1 237 ? 6.74993   5.58836  -30.46714 1.000 32.59672  ? 440  ALA A O   1 
ATOM   1944 C  CB  . ALA A 1 237 ? 5.00987   4.21899  -32.28256 1.000 28.92041  ? 440  ALA A CB  1 
ATOM   1945 N  N   . ILE A 1 238 ? 6.86259   3.79846  -29.13644 1.000 26.90305  ? 441  ILE A N   1 
ATOM   1946 C  CA  . ILE A 1 238 ? 7.86356   4.41384  -28.27085 1.000 24.78288  ? 441  ILE A CA  1 
ATOM   1947 C  C   . ILE A 1 238 ? 9.22879   4.35687  -28.93856 1.000 26.24619  ? 441  ILE A C   1 
ATOM   1948 O  O   . ILE A 1 238 ? 9.62542   3.31841  -29.48366 1.000 27.93009  ? 441  ILE A O   1 
ATOM   1949 C  CB  . ILE A 1 238 ? 7.87732   3.72773  -26.89655 1.000 27.52438  ? 441  ILE A CB  1 
ATOM   1950 C  CG1 . ILE A 1 238 ? 6.53741   3.98607  -26.19906 1.000 36.63550  ? 441  ILE A CG1 1 
ATOM   1951 C  CG2 . ILE A 1 238 ? 9.03796   4.25059  -26.04712 1.000 27.82560  ? 441  ILE A CG2 1 
ATOM   1952 C  CD1 . ILE A 1 238 ? 6.49856   3.59460  -24.74327 1.000 36.48904  ? 441  ILE A CD1 1 
ATOM   1953 N  N   . GLU A 1 239 ? 9.94774   5.48338  -28.91270 1.000 26.52208  ? 442  GLU A N   1 
ATOM   1954 C  CA  . GLU A 1 239 ? 11.28861  5.50573  -29.47814 1.000 27.42546  ? 442  GLU A CA  1 
ATOM   1955 C  C   . GLU A 1 239 ? 12.17116  4.52342  -28.71737 1.000 28.89926  ? 442  GLU A C   1 
ATOM   1956 O  O   . GLU A 1 239 ? 12.12006  4.46453  -27.48492 1.000 30.42453  ? 442  GLU A O   1 
ATOM   1957 C  CB  . GLU A 1 239 ? 11.85967  6.92198  -29.41611 1.000 31.07086  ? 442  GLU A CB  1 
ATOM   1958 C  CG  . GLU A 1 239 ? 13.03000  7.15523  -30.33516 1.000 34.21800  ? 442  GLU A CG  1 
ATOM   1959 C  CD  . GLU A 1 239 ? 13.39433  8.63323  -30.46391 1.000 35.40517  ? 442  GLU A CD  1 
ATOM   1960 O  OE1 . GLU A 1 239 ? 12.60983  9.50048  -30.01418 1.000 35.75991  ? 442  GLU A OE1 1 
ATOM   1961 O  OE2 . GLU A 1 239 ? 14.47645  8.91698  -31.01433 1.000 39.39097  ? 442  GLU A OE2 1 
ATOM   1962 N  N   . GLU A 1 240 ? 12.95106  3.72808  -29.46043 1.000 30.27612  ? 443  GLU A N   1 
ATOM   1963 C  CA  . GLU A 1 240 ? 13.65142  2.59018  -28.85702 1.000 31.56797  ? 443  GLU A CA  1 
ATOM   1964 C  C   . GLU A 1 240 ? 14.45665  2.99955  -27.62671 1.000 34.69323  ? 443  GLU A C   1 
ATOM   1965 O  O   . GLU A 1 240 ? 14.34965  2.37291  -26.56356 1.000 33.17124  ? 443  GLU A O   1 
ATOM   1966 C  CB  . GLU A 1 240 ? 14.56541  1.92859  -29.87718 1.000 30.87786  ? 443  GLU A CB  1 
ATOM   1967 C  CG  . GLU A 1 240 ? 15.20795  0.62880  -29.36189 1.000 37.35284  ? 443  GLU A CG  1 
ATOM   1968 C  CD  . GLU A 1 240 ? 16.27152  0.08040  -30.30252 1.000 34.96764  ? 443  GLU A CD  1 
ATOM   1969 O  OE1 . GLU A 1 240 ? 15.93866  -0.48175 -31.37378 1.000 33.63790  ? 443  GLU A OE1 1 
ATOM   1970 O  OE2 . GLU A 1 240 ? 17.46684  0.22546  -29.97282 1.000 47.16141  ? 443  GLU A OE2 1 
ATOM   1971 N  N   . TRP A 1 241 ? 15.26636  4.05683  -27.74483 1.000 31.05952  ? 444  TRP A N   1 
ATOM   1972 C  CA  . TRP A 1 241 ? 16.15185  4.39960  -26.63482 1.000 33.61974  ? 444  TRP A CA  1 
ATOM   1973 C  C   . TRP A 1 241 ? 15.39473  4.85849  -25.39311 1.000 35.96071  ? 444  TRP A C   1 
ATOM   1974 O  O   . TRP A 1 241 ? 15.92768  4.73834  -24.28428 1.000 32.70933  ? 444  TRP A O   1 
ATOM   1975 C  CB  . TRP A 1 241 ? 17.18516  5.45477  -27.07724 1.000 33.13519  ? 444  TRP A CB  1 
ATOM   1976 C  CG  . TRP A 1 241 ? 16.71106  6.89945  -27.13790 1.000 33.33812  ? 444  TRP A CG  1 
ATOM   1977 C  CD1 . TRP A 1 241 ? 16.32155  7.58738  -28.25282 1.000 37.35135  ? 444  TRP A CD1 1 
ATOM   1978 C  CD2 . TRP A 1 241 ? 16.62483  7.82639  -26.04631 1.000 32.05499  ? 444  TRP A CD2 1 
ATOM   1979 N  NE1 . TRP A 1 241 ? 15.98239  8.87646  -27.92081 1.000 35.99216  ? 444  TRP A NE1 1 
ATOM   1980 C  CE2 . TRP A 1 241 ? 16.15956  9.05064  -26.57210 1.000 37.76935  ? 444  TRP A CE2 1 
ATOM   1981 C  CE3 . TRP A 1 241 ? 16.89014  7.73989  -24.67717 1.000 34.94131  ? 444  TRP A CE3 1 
ATOM   1982 C  CZ2 . TRP A 1 241 ? 15.95054  10.17707 -25.77318 1.000 36.18006  ? 444  TRP A CZ2 1 
ATOM   1983 C  CZ3 . TRP A 1 241 ? 16.67538  8.86776  -23.87835 1.000 36.68133  ? 444  TRP A CZ3 1 
ATOM   1984 C  CH2 . TRP A 1 241 ? 16.21266  10.06519 -24.43368 1.000 38.76721  ? 444  TRP A CH2 1 
ATOM   1985 N  N   . LYS A 1 242 ? 14.15460  5.33287  -25.53273 1.000 29.21637  ? 445  LYS A N   1 
ATOM   1986 C  CA  . LYS A 1 242 ? 13.42394  5.85330  -24.38499 1.000 29.47349  ? 445  LYS A CA  1 
ATOM   1987 C  C   . LYS A 1 242 ? 12.67690  4.79023  -23.59520 1.000 31.33658  ? 445  LYS A C   1 
ATOM   1988 O  O   . LYS A 1 242 ? 12.14995  5.11126  -22.52791 1.000 30.97650  ? 445  LYS A O   1 
ATOM   1989 C  CB  . LYS A 1 242 ? 12.40564  6.91367  -24.81267 1.000 28.33702  ? 445  LYS A CB  1 
ATOM   1990 C  CG  . LYS A 1 242 ? 13.00831  8.07404  -25.57620 1.000 29.39836  ? 445  LYS A CG  1 
ATOM   1991 C  CD  . LYS A 1 242 ? 11.95871  9.11715  -25.85342 1.000 28.87472  ? 445  LYS A CD  1 
ATOM   1992 C  CE  . LYS A 1 242 ? 12.54680  10.27353 -26.63891 1.000 32.73628  ? 445  LYS A CE  1 
ATOM   1993 N  NZ  . LYS A 1 242 ? 11.51301  11.31595 -26.85608 1.000 28.23782  ? 445  LYS A NZ  1 
ATOM   1994 N  N   . ARG A 1 243 ? 12.58861  3.56155  -24.09768 1.000 32.12809  ? 446  ARG A N   1 
ATOM   1995 C  CA  . ARG A 1 243 ? 11.75777  2.55656  -23.44183 1.000 32.75316  ? 446  ARG A CA  1 
ATOM   1996 C  C   . ARG A 1 243 ? 12.09186  2.35762  -21.96631 1.000 41.40146  ? 446  ARG A C   1 
ATOM   1997 O  O   . ARG A 1 243 ? 11.14672  2.24393  -21.16779 1.000 37.83389  ? 446  ARG A O   1 
ATOM   1998 C  CB  . ARG A 1 243 ? 11.84241  1.23558  -24.21914 1.000 34.21927  ? 446  ARG A CB  1 
ATOM   1999 C  CG  . ARG A 1 243 ? 11.21279  1.32033  -25.58345 1.000 29.66487  ? 446  ARG A CG  1 
ATOM   2000 C  CD  . ARG A 1 243 ? 11.33955  0.00651  -26.33204 1.000 32.70277  ? 446  ARG A CD  1 
ATOM   2001 N  NE  . ARG A 1 243 ? 10.69373  -1.06474 -25.58319 1.000 33.11704  ? 446  ARG A NE  1 
ATOM   2002 C  CZ  . ARG A 1 243 ? 9.38851   -1.28720 -25.58358 1.000 37.57840  ? 446  ARG A CZ  1 
ATOM   2003 N  NH1 . ARG A 1 243 ? 8.56158   -0.55990 -26.32218 1.000 31.93892  ? 446  ARG A NH1 1 
ATOM   2004 N  NH2 . ARG A 1 243 ? 8.89798   -2.25690 -24.81629 1.000 39.93438  ? 446  ARG A NH2 1 
ATOM   2005 N  N   . PRO A 1 244 ? 13.36014  2.35107  -21.53266 1.000 47.82333  ? 447  PRO A N   1 
ATOM   2006 C  CA  . PRO A 1 244 ? 13.64503  2.20438  -20.09083 1.000 51.46475  ? 447  PRO A CA  1 
ATOM   2007 C  C   . PRO A 1 244 ? 13.12420  3.33079  -19.20931 1.000 54.86654  ? 447  PRO A C   1 
ATOM   2008 O  O   . PRO A 1 244 ? 13.03073  3.14223  -17.98908 1.000 53.53776  ? 447  PRO A O   1 
ATOM   2009 C  CB  . PRO A 1 244 ? 15.17844  2.14605  -20.04902 1.000 46.68735  ? 447  PRO A CB  1 
ATOM   2010 C  CG  . PRO A 1 244 ? 15.55861  1.59593  -21.36254 1.000 52.61504  ? 447  PRO A CG  1 
ATOM   2011 C  CD  . PRO A 1 244 ? 14.59090  2.20077  -22.33314 1.000 45.11014  ? 447  PRO A CD  1 
ATOM   2012 N  N   . LEU A 1 245 ? 12.79564  4.49319  -19.76231 1.000 34.49508  ? 448  LEU A N   1 
ATOM   2013 C  CA  . LEU A 1 245 ? 12.45995  5.65289  -18.94447 1.000 37.42655  ? 448  LEU A CA  1 
ATOM   2014 C  C   . LEU A 1 245 ? 10.98873  5.72848  -18.55549 1.000 35.56055  ? 448  LEU A C   1 
ATOM   2015 O  O   . LEU A 1 245 ? 10.59281  6.69430  -17.89172 1.000 42.83212  ? 448  LEU A O   1 
ATOM   2016 C  CB  . LEU A 1 245 ? 12.85784  6.94309  -19.67325 1.000 34.80988  ? 448  LEU A CB  1 
ATOM   2017 C  CG  . LEU A 1 245 ? 14.34995  7.23772  -19.83212 1.000 43.61810  ? 448  LEU A CG  1 
ATOM   2018 C  CD1 . LEU A 1 245 ? 14.96657  6.47656  -21.00558 1.000 52.93828  ? 448  LEU A CD1 1 
ATOM   2019 C  CD2 . LEU A 1 245 ? 14.56281  8.72771  -20.00043 1.000 47.07618  ? 448  LEU A CD2 1 
ATOM   2020 N  N   . TYR A 1 246 ? 10.17139  4.75101  -18.93989 1.000 33.99661  ? 449  TYR A N   1 
ATOM   2021 C  CA  . TYR A 1 246 ? 8.73337   4.79158  -18.66623 1.000 29.41564  ? 449  TYR A CA  1 
ATOM   2022 C  C   . TYR A 1 246 ? 8.44203   4.00569  -17.39073 1.000 47.40925  ? 449  TYR A C   1 
ATOM   2023 O  O   . TYR A 1 246 ? 7.83271   2.93485  -17.38487 1.000 54.68442  ? 449  TYR A O   1 
ATOM   2024 C  CB  . TYR A 1 246 ? 7.94645   4.26829  -19.86093 1.000 36.50031  ? 449  TYR A CB  1 
ATOM   2025 C  CG  . TYR A 1 246 ? 7.95493   5.24670  -20.99750 1.000 36.96245  ? 449  TYR A CG  1 
ATOM   2026 C  CD1 . TYR A 1 246 ? 6.97215   6.22084  -21.09734 1.000 31.51375  ? 449  TYR A CD1 1 
ATOM   2027 C  CD2 . TYR A 1 246 ? 8.96312   5.22163  -21.95761 1.000 30.57082  ? 449  TYR A CD2 1 
ATOM   2028 C  CE1 . TYR A 1 246 ? 6.98166   7.13233  -22.12419 1.000 27.04829  ? 449  TYR A CE1 1 
ATOM   2029 C  CE2 . TYR A 1 246 ? 8.98368   6.13196  -22.98513 1.000 29.24445  ? 449  TYR A CE2 1 
ATOM   2030 C  CZ  . TYR A 1 246 ? 7.99129   7.08598  -23.06898 1.000 27.14816  ? 449  TYR A CZ  1 
ATOM   2031 O  OH  . TYR A 1 246 ? 8.00529   8.00328  -24.08917 1.000 29.06766  ? 449  TYR A OH  1 
ATOM   2032 N  N   . LYS A 1 247 ? 8.87253   4.61297  -16.29281 1.000 25.95300  ? 450  LYS A N   1 
ATOM   2033 C  CA  . LYS A 1 247 ? 9.13762   3.95814  -15.01673 1.000 49.54065  ? 450  LYS A CA  1 
ATOM   2034 C  C   . LYS A 1 247 ? 9.49164   5.01843  -13.98016 1.000 33.64064  ? 450  LYS A C   1 
ATOM   2035 O  O   . LYS A 1 247 ? 10.20805  5.97066  -14.29432 1.000 30.51677  ? 450  LYS A O   1 
ATOM   2036 C  CB  . LYS A 1 247 ? 10.29635  2.97072  -15.16390 1.000 44.06231  ? 450  LYS A CB  1 
ATOM   2037 C  CG  . LYS A 1 247 ? 10.41538  1.95827  -14.05722 1.000 56.67725  ? 450  LYS A CG  1 
ATOM   2038 C  CD  . LYS A 1 247 ? 11.37849  0.85286  -14.44593 1.000 45.55719  ? 450  LYS A CD  1 
ATOM   2039 C  CE  . LYS A 1 247 ? 12.81962  1.25823  -14.20882 1.000 60.04413  ? 450  LYS A CE  1 
ATOM   2040 N  NZ  . LYS A 1 247 ? 13.53398  0.22272  -13.40494 1.000 65.87528  ? 450  LYS A NZ  1 
ATOM   2041 N  N   A HIS A 1 248 ? 8.85344   4.94971  -12.81924 0.544 33.05699  ? 451  HIS A N   1 
ATOM   2042 N  N   B HIS A 1 248 ? 9.13829   4.76717  -12.71392 0.456 32.03172  ? 451  HIS A N   1 
ATOM   2043 C  CA  A HIS A 1 248 ? 9.25565   5.75971  -11.68082 0.544 26.80039  ? 451  HIS A CA  1 
ATOM   2044 C  CA  B HIS A 1 248 ? 9.22421   5.81237  -11.67641 0.456 26.79447  ? 451  HIS A CA  1 
ATOM   2045 C  C   A HIS A 1 248 ? 9.44902   4.77065  -10.54614 0.544 29.91675  ? 451  HIS A C   1 
ATOM   2046 C  C   B HIS A 1 248 ? 9.53968   5.27480  -10.27175 0.456 27.01513  ? 451  HIS A C   1 
ATOM   2047 O  O   A HIS A 1 248 ? 8.52273   4.03048  -10.19457 0.544 24.67046  ? 451  HIS A O   1 
ATOM   2048 O  O   B HIS A 1 248 ? 8.79279   5.46361  -9.31110  0.456 23.88298  ? 451  HIS A O   1 
ATOM   2049 C  CB  A HIS A 1 248 ? 8.25624   6.90656  -11.38996 0.544 25.44333  ? 451  HIS A CB  1 
ATOM   2050 C  CB  B HIS A 1 248 ? 7.91599   6.59919  -11.67213 0.456 24.96847  ? 451  HIS A CB  1 
ATOM   2051 C  CG  A HIS A 1 248 ? 7.23851   6.66261  -10.30362 0.544 28.45233  ? 451  HIS A CG  1 
ATOM   2052 C  CG  B HIS A 1 248 ? 6.69655   5.73955  -11.54572 0.456 25.37375  ? 451  HIS A CG  1 
ATOM   2053 N  ND1 A HIS A 1 248 ? 7.24544   7.35829  -9.10789  0.544 18.32088  ? 451  HIS A ND1 1 
ATOM   2054 N  ND1 B HIS A 1 248 ? 5.78785   5.88552  -10.51868 0.456 28.55277  ? 451  HIS A ND1 1 
ATOM   2055 C  CD2 A HIS A 1 248 ? 6.12060   5.89731  -10.27661 0.544 27.27599  ? 451  HIS A CD2 1 
ATOM   2056 C  CD2 B HIS A 1 248 ? 6.23161   4.72920  -12.31848 0.456 29.44973  ? 451  HIS A CD2 1 
ATOM   2057 C  CE1 A HIS A 1 248 ? 6.21229   6.99304  -8.37498  0.544 23.05801  ? 451  HIS A CE1 1 
ATOM   2058 C  CE1 B HIS A 1 248 ? 4.82005   4.99709  -10.66118 0.456 27.82462  ? 451  HIS A CE1 1 
ATOM   2059 N  NE2 A HIS A 1 248 ? 5.51166   6.10479  -9.05979  0.544 25.36210  ? 451  HIS A NE2 1 
ATOM   2060 N  NE2 B HIS A 1 248 ? 5.06588   4.28358  -11.74601 0.456 30.53588  ? 451  HIS A NE2 1 
ATOM   2061 N  N   . ASP A 1 249 ? 10.69844  4.64476  -10.10923 1.000 24.12813  ? 452  ASP A N   1 
ATOM   2062 C  CA  . ASP A 1 249 ? 11.04121  3.92513  -8.89022  1.000 21.36442  ? 452  ASP A CA  1 
ATOM   2063 C  C   . ASP A 1 249 ? 11.50614  4.92316  -7.84538  1.000 18.11883  ? 452  ASP A C   1 
ATOM   2064 O  O   . ASP A 1 249 ? 12.36586  5.76361  -8.12413  1.000 21.30684  ? 452  ASP A O   1 
ATOM   2065 C  CB  . ASP A 1 249 ? 12.15165  2.90855  -9.13817  1.000 28.50135  ? 452  ASP A CB  1 
ATOM   2066 C  CG  . ASP A 1 249 ? 11.75661  1.85068  -10.14946 1.000 38.14471  ? 452  ASP A CG  1 
ATOM   2067 O  OD1 . ASP A 1 249 ? 10.63809  1.31343  -10.04142 1.000 32.34796  ? 452  ASP A OD1 1 
ATOM   2068 O  OD2 . ASP A 1 249 ? 12.56231  1.57902  -11.05820 1.000 46.54655  ? 452  ASP A OD2 1 
ATOM   2069 N  N   . TYR A 1 250 ? 10.96293  4.80474  -6.63903  1.000 19.84030  ? 453  TYR A N   1 
ATOM   2070 C  CA  . TYR A 1 250 ? 11.32702  5.66563  -5.51498  1.000 17.77982  ? 453  TYR A CA  1 
ATOM   2071 C  C   . TYR A 1 250 ? 11.33120  4.72331  -4.32278  1.000 19.04015  ? 453  TYR A C   1 
ATOM   2072 O  O   . TYR A 1 250 ? 10.25883  4.32622  -3.84787  1.000 21.10273  ? 453  TYR A O   1 
ATOM   2073 C  CB  . TYR A 1 250 ? 10.32915  6.80354  -5.33813  1.000 19.71058  ? 453  TYR A CB  1 
ATOM   2074 C  CG  . TYR A 1 250 ? 10.59036  7.71371  -4.15639  1.000 17.17824  ? 453  TYR A CG  1 
ATOM   2075 C  CD1 . TYR A 1 250 ? 11.41106  8.83505  -4.29248  1.000 17.40767  ? 453  TYR A CD1 1 
ATOM   2076 C  CD2 . TYR A 1 250 ? 9.99163   7.47674  -2.92268  1.000 18.63235  ? 453  TYR A CD2 1 
ATOM   2077 C  CE1 . TYR A 1 250 ? 11.63646  9.70569  -3.22309  1.000 19.08578  ? 453  TYR A CE1 1 
ATOM   2078 C  CE2 . TYR A 1 250 ? 10.20624  8.35294  -1.83800  1.000 18.44221  ? 453  TYR A CE2 1 
ATOM   2079 C  CZ  . TYR A 1 250 ? 11.03241  9.44770  -1.99483  1.000 18.70204  ? 453  TYR A CZ  1 
ATOM   2080 O  OH  . TYR A 1 250 ? 11.25842  10.30246 -0.94087  1.000 18.04043  ? 453  TYR A OH  1 
ATOM   2081 N  N   A ILE A 1 251 ? 12.52004  4.35951  -3.84564  0.618 20.53250  ? 454  ILE A N   1 
ATOM   2082 N  N   B ILE A 1 251 ? 12.52099  4.33080  -3.88148  0.382 20.53927  ? 454  ILE A N   1 
ATOM   2083 C  CA  A ILE A 1 251 ? 12.68921  3.23801  -2.92104  0.618 21.80137  ? 454  ILE A CA  1 
ATOM   2084 C  CA  B ILE A 1 251 ? 12.68459  3.25252  -2.91274  0.382 21.79469  ? 454  ILE A CA  1 
ATOM   2085 C  C   A ILE A 1 251 ? 12.82965  3.78620  -1.50210  0.618 20.46637  ? 454  ILE A C   1 
ATOM   2086 C  C   B ILE A 1 251 ? 12.79601  3.86554  -1.52420  0.382 20.46853  ? 454  ILE A C   1 
ATOM   2087 O  O   A ILE A 1 251 ? 13.90565  4.23821  -1.09655  0.618 21.05957  ? 454  ILE A O   1 
ATOM   2088 O  O   B ILE A 1 251 ? 13.81348  4.47578  -1.18000  0.382 21.32617  ? 454  ILE A O   1 
ATOM   2089 C  CB  A ILE A 1 251 ? 13.89103  2.36660  -3.29997  0.618 21.85040  ? 454  ILE A CB  1 
ATOM   2090 C  CB  B ILE A 1 251 ? 13.90822  2.38534  -3.23462  0.382 21.85917  ? 454  ILE A CB  1 
ATOM   2091 C  CG1 A ILE A 1 251 ? 13.86330  2.02192  -4.78739  0.618 22.25134  ? 454  ILE A CG1 1 
ATOM   2092 C  CG1 B ILE A 1 251 ? 13.73543  1.70421  -4.59266  0.382 22.15010  ? 454  ILE A CG1 1 
ATOM   2093 C  CG2 A ILE A 1 251 ? 13.88895  1.07712  -2.48503  0.618 20.51935  ? 454  ILE A CG2 1 
ATOM   2094 C  CG2 B ILE A 1 251 ? 14.13734  1.34931  -2.13164  0.382 20.58835  ? 454  ILE A CG2 1 
ATOM   2095 C  CD1 A ILE A 1 251 ? 12.56622  1.40119  -5.21751  0.618 23.17421  ? 454  ILE A CD1 1 
ATOM   2096 C  CD1 B ILE A 1 251 ? 15.00312  1.10985  -5.12002  0.382 23.09372  ? 454  ILE A CD1 1 
ATOM   2097 N  N   . ARG A 1 252 ? 11.76316  3.68390  -0.71129  1.000 19.14192  ? 455  ARG A N   1 
ATOM   2098 C  CA  . ARG A 1 252 ? 11.80215  4.17503  0.65868   1.000 18.82999  ? 455  ARG A CA  1 
ATOM   2099 C  C   . ARG A 1 252 ? 12.58232  3.23353  1.57945   1.000 19.09492  ? 455  ARG A C   1 
ATOM   2100 O  O   . ARG A 1 252 ? 12.71163  2.03158  1.31768   1.000 22.77504  ? 455  ARG A O   1 
ATOM   2101 C  CB  . ARG A 1 252 ? 10.37402  4.38071  1.16849   1.000 18.76653  ? 455  ARG A CB  1 
ATOM   2102 C  CG  . ARG A 1 252 ? 9.66907   5.52621  0.41254   1.000 19.36157  ? 455  ARG A CG  1 
ATOM   2103 C  CD  . ARG A 1 252 ? 8.18439   5.62333  0.73485   1.000 19.56430  ? 455  ARG A CD  1 
ATOM   2104 N  NE  . ARG A 1 252 ? 7.57682   6.72394  -0.01800  1.000 19.31505  ? 455  ARG A NE  1 
ATOM   2105 C  CZ  . ARG A 1 252 ? 7.02975   6.57783  -1.22008  1.000 19.37219  ? 455  ARG A CZ  1 
ATOM   2106 N  NH1 . ARG A 1 252 ? 7.02001   5.40158  -1.83592  1.000 21.75713  ? 455  ARG A NH1 1 
ATOM   2107 N  NH2 . ARG A 1 252 ? 6.49253   7.64002  -1.82361  1.000 19.46116  ? 455  ARG A NH2 1 
ATOM   2108 N  N   . GLY A 1 253 ? 13.13712  3.80510  2.65525   1.000 18.64109  ? 456  GLY A N   1 
ATOM   2109 C  CA  . GLY A 1 253 ? 13.78981  3.01864  3.69364   1.000 20.56339  ? 456  GLY A CA  1 
ATOM   2110 C  C   . GLY A 1 253 ? 15.28085  2.83360  3.52541   1.000 27.15458  ? 456  GLY A C   1 
ATOM   2111 O  O   . GLY A 1 253 ? 15.88915  2.04678  4.27056   1.000 27.91096  ? 456  GLY A O   1 
ATOM   2112 N  N   . LEU A 1 254 ? 15.88322  3.51664  2.55927   1.000 23.49415  ? 457  LEU A N   1 
ATOM   2113 C  CA  . LEU A 1 254 ? 17.31252  3.44560  2.32284   1.000 25.61258  ? 457  LEU A CA  1 
ATOM   2114 C  C   . LEU A 1 254 ? 18.06310  4.32918  3.30861   1.000 23.90684  ? 457  LEU A C   1 
ATOM   2115 O  O   . LEU A 1 254 ? 17.56652  5.37881  3.73370   1.000 25.81656  ? 457  LEU A O   1 
ATOM   2116 C  CB  . LEU A 1 254 ? 17.62941  3.89656  0.89511   1.000 24.00391  ? 457  LEU A CB  1 
ATOM   2117 C  CG  . LEU A 1 254 ? 17.02168  3.03448  -0.21576  1.000 30.49386  ? 457  LEU A CG  1 
ATOM   2118 C  CD1 . LEU A 1 254 ? 17.41891  3.49372  -1.60569  1.000 24.42885  ? 457  LEU A CD1 1 
ATOM   2119 C  CD2 . LEU A 1 254 ? 17.46302  1.65122  -0.01274  1.000 32.64879  ? 457  LEU A CD2 1 
ATOM   2120 N  N   . GLN A 1 255 ? 19.27333  3.89792  3.65590   1.000 26.51203  ? 458  GLN A N   1 
ATOM   2121 C  CA  . GLN A 1 255 ? 20.18934  4.73261  4.42010   1.000 29.76008  ? 458  GLN A CA  1 
ATOM   2122 C  C   . GLN A 1 255 ? 20.68919  5.88843  3.55679   1.000 25.95237  ? 458  GLN A C   1 
ATOM   2123 O  O   . GLN A 1 255 ? 20.62576  5.84162  2.32411   1.000 25.56442  ? 458  GLN A O   1 
ATOM   2124 C  CB  . GLN A 1 255 ? 21.37491  3.90726  4.91928   1.000 30.62010  ? 458  GLN A CB  1 
ATOM   2125 C  CG  . GLN A 1 255 ? 20.99987  2.88939  5.96865   1.000 38.93575  ? 458  GLN A CG  1 
ATOM   2126 C  CD  . GLN A 1 255 ? 22.14910  1.96950  6.31400   1.000 49.92952  ? 458  GLN A CD  1 
ATOM   2127 O  OE1 . GLN A 1 255 ? 23.25980  2.12014  5.79902   1.000 51.78773  ? 458  GLN A OE1 1 
ATOM   2128 N  NE2 . GLN A 1 255 ? 21.88844  1.00370  7.18588   1.000 43.97642  ? 458  GLN A NE2 1 
ATOM   2129 N  N   . ASP A 1 256 ? 21.19344  6.93814  4.22351   1.000 26.73175  ? 459  ASP A N   1 
ATOM   2130 C  CA  . ASP A 1 256 ? 21.71485  8.09584  3.49362   1.000 28.39350  ? 459  ASP A CA  1 
ATOM   2131 C  C   . ASP A 1 256 ? 22.78415  7.67999  2.49695   1.000 31.81921  ? 459  ASP A C   1 
ATOM   2132 O  O   . ASP A 1 256 ? 22.85346  8.21380  1.38273   1.000 28.74922  ? 459  ASP A O   1 
ATOM   2133 C  CB  . ASP A 1 256 ? 22.30900  9.12805  4.45898   1.000 29.75916  ? 459  ASP A CB  1 
ATOM   2134 C  CG  . ASP A 1 256 ? 21.25793  9.87036  5.26177   1.000 34.23416  ? 459  ASP A CG  1 
ATOM   2135 O  OD1 . ASP A 1 256 ? 20.04690  9.63753  5.05904   1.000 27.15733  ? 459  ASP A OD1 1 
ATOM   2136 O  OD2 . ASP A 1 256 ? 21.66158  10.69741 6.11364   1.000 33.80350  ? 459  ASP A OD2 1 
ATOM   2137 N  N   . GLU A 1 257 ? 23.62428  6.71763  2.88280   1.000 29.57192  ? 460  GLU A N   1 
ATOM   2138 C  CA  . GLU A 1 257 ? 24.70119  6.23644  2.02756   1.000 33.40568  ? 460  GLU A CA  1 
ATOM   2139 C  C   . GLU A 1 257 ? 24.19776  5.51568  0.78278   1.000 34.60573  ? 460  GLU A C   1 
ATOM   2140 O  O   . GLU A 1 257 ? 25.00963  5.16953  -0.07973  1.000 36.94007  ? 460  GLU A O   1 
ATOM   2141 C  CB  . GLU A 1 257 ? 25.62586  5.31518  2.83613   1.000 33.56475  ? 460  GLU A CB  1 
ATOM   2142 C  CG  . GLU A 1 257 ? 26.37449  6.00724  4.01216   1.000 38.56430  ? 460  GLU A CG  1 
ATOM   2143 C  CD  . GLU A 1 257 ? 25.53689  6.19415  5.28730   1.000 44.71155  ? 460  GLU A CD  1 
ATOM   2144 O  OE1 . GLU A 1 257 ? 24.29908  6.00388  5.26221   1.000 34.71702  ? 460  GLU A OE1 1 
ATOM   2145 O  OE2 . GLU A 1 257 ? 26.13253  6.53607  6.33427   1.000 50.86589  ? 460  GLU A OE2 1 
ATOM   2146 N  N   . ASP A 1 258 ? 22.89012  5.28221  0.66209   1.000 30.69179  ? 461  ASP A N   1 
ATOM   2147 C  CA  . ASP A 1 258 ? 22.31980  4.59407  -0.48809  1.000 32.35009  ? 461  ASP A CA  1 
ATOM   2148 C  C   . ASP A 1 258 ? 21.40582  5.50470  -1.30780  1.000 30.35115  ? 461  ASP A C   1 
ATOM   2149 O  O   . ASP A 1 258 ? 20.61557  5.02071  -2.12608  1.000 29.23025  ? 461  ASP A O   1 
ATOM   2150 C  CB  . ASP A 1 258 ? 21.56988  3.34125  -0.02066  1.000 30.82921  ? 461  ASP A CB  1 
ATOM   2151 C  CG  . ASP A 1 258 ? 22.51327  2.24183  0.47674   1.000 35.90656  ? 461  ASP A CG  1 
ATOM   2152 O  OD1 . ASP A 1 258 ? 23.60814  2.09067  -0.10165  1.000 36.24113  ? 461  ASP A OD1 1 
ATOM   2153 O  OD2 . ASP A 1 258 ? 22.16677  1.53267  1.44833   1.000 40.31976  ? 461  ASP A OD2 1 
ATOM   2154 N  N   . GLU A 1 259 ? 21.50481  6.82360  -1.11037  1.000 27.83984  ? 462  GLU A N   1 
ATOM   2155 C  CA  . GLU A 1 259 ? 20.58134  7.75235  -1.75716  1.000 23.21707  ? 462  GLU A CA  1 
ATOM   2156 C  C   . GLU A 1 259 ? 20.68700  7.70091  -3.27231  1.000 23.74271  ? 462  GLU A C   1 
ATOM   2157 O  O   . GLU A 1 259 ? 19.69974  7.96813  -3.96358  1.000 22.25325  ? 462  GLU A O   1 
ATOM   2158 C  CB  . GLU A 1 259 ? 20.83126  9.18092  -1.25042  1.000 26.50206  ? 462  GLU A CB  1 
ATOM   2159 C  CG  . GLU A 1 259 ? 19.89108  10.24043 -1.83875  1.000 24.56597  ? 462  GLU A CG  1 
ATOM   2160 C  CD  . GLU A 1 259 ? 18.48055  10.16179 -1.29056  1.000 21.02149  ? 462  GLU A CD  1 
ATOM   2161 O  OE1 . GLU A 1 259 ? 18.27007  9.52183  -0.23220  1.000 24.46208  ? 462  GLU A OE1 1 
ATOM   2162 O  OE2 . GLU A 1 259 ? 17.55323  10.74270 -1.91374  1.000 21.55317  ? 462  GLU A OE2 1 
ATOM   2163 N  N   . GLY A 1 260 ? 21.85551  7.33571  -3.80470  1.000 25.53673  ? 463  GLY A N   1 
ATOM   2164 C  CA  . GLY A 1 260 ? 21.99183  7.23480  -5.25525  1.000 23.87799  ? 463  GLY A CA  1 
ATOM   2165 C  C   . GLY A 1 260 ? 21.24213  6.06932  -5.87017  1.000 27.12048  ? 463  GLY A C   1 
ATOM   2166 O  O   . GLY A 1 260 ? 21.11846  6.01226  -7.09997  1.000 27.17465  ? 463  GLY A O   1 
ATOM   2167 N  N   . LYS A 1 261 ? 20.74383  5.14679  -5.05231  1.000 26.85012  ? 464  LYS A N   1 
ATOM   2168 C  CA  . LYS A 1 261 ? 19.96115  4.02056  -5.53982  1.000 26.81521  ? 464  LYS A CA  1 
ATOM   2169 C  C   . LYS A 1 261 ? 18.47002  4.20749  -5.30730  1.000 27.50313  ? 464  LYS A C   1 
ATOM   2170 O  O   . LYS A 1 261 ? 17.70552  3.25564  -5.47218  1.000 27.59337  ? 464  LYS A O   1 
ATOM   2171 C  CB  . LYS A 1 261 ? 20.44491  2.72361  -4.88312  1.000 30.21316  ? 464  LYS A CB  1 
ATOM   2172 C  CG  . LYS A 1 261 ? 21.85455  2.34153  -5.29862  1.000 38.28875  ? 464  LYS A CG  1 
ATOM   2173 C  CD  . LYS A 1 261 ? 22.43388  1.18665  -4.48377  1.000 44.69442  ? 464  LYS A CD  1 
ATOM   2174 C  CE  . LYS A 1 261 ? 22.99938  1.67205  -3.16012  1.000 39.46953  ? 464  LYS A CE  1 
ATOM   2175 N  NZ  . LYS A 1 261 ? 23.84215  0.63407  -2.47854  1.000 42.40338  ? 464  LYS A NZ  1 
ATOM   2176 N  N   . LYS A 1 262 ? 18.03216  5.42136  -4.95949  1.000 23.52324  ? 465  LYS A N   1 
ATOM   2177 C  CA  . LYS A 1 262 ? 16.65897  5.61883  -4.50417  1.000 21.01011  ? 465  LYS A CA  1 
ATOM   2178 C  C   . LYS A 1 262 ? 15.67334  5.96870  -5.62100  1.000 23.79929  ? 465  LYS A C   1 
ATOM   2179 O  O   . LYS A 1 262 ? 14.54685  5.44801  -5.62710  1.000 21.89965  ? 465  LYS A O   1 
ATOM   2180 C  CB  . LYS A 1 262 ? 16.62053  6.71661  -3.43390  1.000 19.55329  ? 465  LYS A CB  1 
ATOM   2181 C  CG  . LYS A 1 262 ? 15.23101  6.87243  -2.77972  1.000 19.58238  ? 465  LYS A CG  1 
ATOM   2182 C  CD  . LYS A 1 262 ? 15.33936  7.71592  -1.52098  1.000 21.20353  ? 465  LYS A CD  1 
ATOM   2183 C  CE  . LYS A 1 262 ? 13.98085  7.88057  -0.83323  1.000 20.66975  ? 465  LYS A CE  1 
ATOM   2184 N  NZ  . LYS A 1 262 ? 14.19905  8.57480  0.48638   1.000 20.32803  ? 465  LYS A NZ  1 
ATOM   2185 N  N   . SER A 1 263 ? 16.04308  6.85037  -6.55404  1.000 20.23732  ? 466  SER A N   1 
ATOM   2186 C  CA  . SER A 1 263 ? 15.08375  7.42492  -7.49170  1.000 19.62369  ? 466  SER A CA  1 
ATOM   2187 C  C   . SER A 1 263 ? 15.63936  7.40364  -8.91070  1.000 21.55765  ? 466  SER A C   1 
ATOM   2188 O  O   . SER A 1 263 ? 16.67887  8.00756  -9.17578  1.000 21.54095  ? 466  SER A O   1 
ATOM   2189 C  CB  . SER A 1 263 ? 14.74445  8.86659  -7.09414  1.000 19.65931  ? 466  SER A CB  1 
ATOM   2190 O  OG  . SER A 1 263 ? 14.14618  9.53294  -8.19421  1.000 21.29513  ? 466  SER A OG  1 
ATOM   2191 N  N   . ASN A 1 264 ? 14.94575  6.72431  -9.83074  1.000 22.07469  ? 467  ASN A N   1 
ATOM   2192 C  CA  . ASN A 1 264 ? 15.44324  6.73837  -11.20295 1.000 23.02888  ? 467  ASN A CA  1 
ATOM   2193 C  C   . ASN A 1 264 ? 15.27837  8.11184  -11.84455 1.000 23.02767  ? 467  ASN A C   1 
ATOM   2194 O  O   . ASN A 1 264 ? 16.13978  8.52605  -12.62912 1.000 22.81204  ? 467  ASN A O   1 
ATOM   2195 C  CB  . ASN A 1 264 ? 14.77116  5.65058  -12.04965 1.000 24.09367  ? 467  ASN A CB  1 
ATOM   2196 C  CG  . ASN A 1 264 ? 13.30361  5.91443  -12.28534 1.000 26.79782  ? 467  ASN A CG  1 
ATOM   2197 O  OD1 . ASN A 1 264 ? 12.54116  6.14574  -11.35409 1.000 29.99441  ? 467  ASN A OD1 1 
ATOM   2198 N  ND2 . ASN A 1 264 ? 12.89664  5.89939  -13.55429 1.000 29.94233  ? 467  ASN A ND2 1 
ATOM   2199 N  N   . ILE A 1 265 ? 14.20122  8.83639  -11.51497 1.000 21.92081  ? 468  ILE A N   1 
ATOM   2200 C  CA  . ILE A 1 265 ? 13.98131  10.15081 -12.10539 1.000 21.70659  ? 468  ILE A CA  1 
ATOM   2201 C  C   . ILE A 1 265 ? 15.05649  11.12843 -11.64972 1.000 20.95211  ? 468  ILE A C   1 
ATOM   2202 O  O   . ILE A 1 265 ? 15.66874  11.82165 -12.46696 1.000 23.74374  ? 468  ILE A O   1 
ATOM   2203 C  CB  . ILE A 1 265 ? 12.57513  10.67492 -11.76496 1.000 22.20000  ? 468  ILE A CB  1 
ATOM   2204 C  CG1 . ILE A 1 265 ? 11.50917  9.72983  -12.32665 1.000 22.53668  ? 468  ILE A CG1 1 
ATOM   2205 C  CG2 . ILE A 1 265 ? 12.39377  12.09837 -12.32899 1.000 20.78554  ? 468  ILE A CG2 1 
ATOM   2206 C  CD1 . ILE A 1 265 ? 10.10721  10.17336 -12.00206 1.000 21.85701  ? 468  ILE A CD1 1 
ATOM   2207 N  N   . ALA A 1 266 ? 15.29607  11.21657 -10.33577 1.000 19.53581  ? 469  ALA A N   1 
ATOM   2208 C  CA  . ALA A 1 266 ? 16.34450  12.12316 -9.87900  1.000 21.81126  ? 469  ALA A CA  1 
ATOM   2209 C  C   . ALA A 1 266 ? 17.69021  11.73509 -10.46809 1.000 23.88505  ? 469  ALA A C   1 
ATOM   2210 O  O   . ALA A 1 266 ? 18.49248  12.60422 -10.82055 1.000 23.28940  ? 469  ALA A O   1 
ATOM   2211 C  CB  . ALA A 1 266 ? 16.40102  12.14666 -8.34009  1.000 20.67221  ? 469  ALA A CB  1 
ATOM   2212 N  N   . ASN A 1 267 ? 17.93301  10.43718 -10.64231 1.000 23.70979  ? 470  ASN A N   1 
ATOM   2213 C  CA  . ASN A 1 267 ? 19.19578  9.99631  -11.22071 1.000 25.98104  ? 470  ASN A CA  1 
ATOM   2214 C  C   . ASN A 1 267 ? 19.32779  10.39558 -12.69045 1.000 26.52162  ? 470  ASN A C   1 
ATOM   2215 O  O   . ASN A 1 267 ? 20.44218  10.64835 -13.15783 1.000 27.15123  ? 470  ASN A O   1 
ATOM   2216 C  CB  . ASN A 1 267 ? 19.33389  8.48498  -11.07549 1.000 21.30917  ? 470  ASN A CB  1 
ATOM   2217 C  CG  . ASN A 1 267 ? 19.75121  8.07146  -9.68420  1.000 24.82806  ? 470  ASN A CG  1 
ATOM   2218 O  OD1 . ASN A 1 267 ? 19.94027  8.91205  -8.79354  1.000 25.46274  ? 470  ASN A OD1 1 
ATOM   2219 N  ND2 . ASN A 1 267 ? 19.88002  6.77224  -9.48104  1.000 25.22824  ? 470  ASN A ND2 1 
ATOM   2220 N  N   . ILE A 1 268 ? 18.21985  10.44462 -13.43232 1.000 25.53669  ? 471  ILE A N   1 
ATOM   2221 C  CA  . ILE A 1 268 ? 18.27719  10.90492 -14.82200 1.000 25.12649  ? 471  ILE A CA  1 
ATOM   2222 C  C   . ILE A 1 268 ? 18.73798  12.35630 -14.88069 1.000 26.74516  ? 471  ILE A C   1 
ATOM   2223 O  O   . ILE A 1 268 ? 19.58868  12.72181 -15.70130 1.000 26.76410  ? 471  ILE A O   1 
ATOM   2224 C  CB  . ILE A 1 268 ? 16.91404  10.71243 -15.51141 1.000 24.65879  ? 471  ILE A CB  1 
ATOM   2225 C  CG1 . ILE A 1 268 ? 16.67491  9.22197  -15.81520 1.000 28.21940  ? 471  ILE A CG1 1 
ATOM   2226 C  CG2 . ILE A 1 268 ? 16.82671  11.53726 -16.79918 1.000 28.61798  ? 471  ILE A CG2 1 
ATOM   2227 C  CD1 . ILE A 1 268 ? 17.68756  8.61230  -16.78438 1.000 30.04939  ? 471  ILE A CD1 1 
ATOM   2228 N  N   . PHE A 1 269 ? 18.18219  13.21060 -14.01173 1.000 25.29255  ? 472  PHE A N   1 
ATOM   2229 C  CA  . PHE A 1 269 ? 18.65515  14.59379 -13.94594 1.000 25.50435  ? 472  PHE A CA  1 
ATOM   2230 C  C   . PHE A 1 269 ? 20.11579  14.66031 -13.52322 1.000 29.43314  ? 472  PHE A C   1 
ATOM   2231 O  O   . PHE A 1 269 ? 20.89346  15.44703 -14.07057 1.000 28.30308  ? 472  PHE A O   1 
ATOM   2232 C  CB  . PHE A 1 269 ? 17.80181  15.41470 -12.97153 1.000 26.09142  ? 472  PHE A CB  1 
ATOM   2233 C  CG  . PHE A 1 269 ? 16.45923  15.80858 -13.51426 1.000 21.66311  ? 472  PHE A CG  1 
ATOM   2234 C  CD1 . PHE A 1 269 ? 16.32537  16.93018 -14.32369 1.000 26.27322  ? 472  PHE A CD1 1 
ATOM   2235 C  CD2 . PHE A 1 269 ? 15.32653  15.05613 -13.21347 1.000 23.59144  ? 472  PHE A CD2 1 
ATOM   2236 C  CE1 . PHE A 1 269 ? 15.08059  17.29786 -14.82889 1.000 26.13875  ? 472  PHE A CE1 1 
ATOM   2237 C  CE2 . PHE A 1 269 ? 14.07758  15.41340 -13.72083 1.000 24.62905  ? 472  PHE A CE2 1 
ATOM   2238 C  CZ  . PHE A 1 269 ? 13.95999  16.53872 -14.53582 1.000 24.38241  ? 472  PHE A CZ  1 
ATOM   2239 N  N   . ARG A 1 270 ? 20.50197  13.85935 -12.52626 1.000 27.26006  ? 473  ARG A N   1 
ATOM   2240 C  CA  . ARG A 1 270 ? 21.86435  13.94116 -12.01129 1.000 25.37618  ? 473  ARG A CA  1 
ATOM   2241 C  C   . ARG A 1 270 ? 22.88798  13.37506 -12.99526 1.000 31.59498  ? 473  ARG A C   1 
ATOM   2242 O  O   . ARG A 1 270 ? 24.04354  13.82239 -13.01992 1.000 34.01462  ? 473  ARG A O   1 
ATOM   2243 C  CB  . ARG A 1 270 ? 21.93407  13.22113 -10.65895 1.000 28.44156  ? 473  ARG A CB  1 
ATOM   2244 C  CG  . ARG A 1 270 ? 23.26970  13.39286 -9.95516  1.000 26.27612  ? 473  ARG A CG  1 
ATOM   2245 C  CD  . ARG A 1 270 ? 23.18652  12.97252 -8.48486  1.000 29.88893  ? 473  ARG A CD  1 
ATOM   2246 N  NE  . ARG A 1 270 ? 22.65379  11.62525 -8.28146  1.000 28.85421  ? 473  ARG A NE  1 
ATOM   2247 C  CZ  . ARG A 1 270 ? 23.39596  10.52681 -8.21092  1.000 26.61974  ? 473  ARG A CZ  1 
ATOM   2248 N  NH1 . ARG A 1 270 ? 24.70916  10.56863 -8.37842  1.000 28.51273  ? 473  ARG A NH1 1 
ATOM   2249 N  NH2 . ARG A 1 270 ? 22.80300  9.35651  -7.96836  1.000 26.04720  ? 473  ARG A NH2 1 
ATOM   2250 N  N   . ALA A 1 271 ? 22.48963  12.42113 -13.83424 1.000 30.81352  ? 474  ALA A N   1 
ATOM   2251 C  CA  . ALA A 1 271 ? 23.43809  11.86313 -14.79141 1.000 30.15753  ? 474  ALA A CA  1 
ATOM   2252 C  C   . ALA A 1 271 ? 23.54212  12.70699 -16.05629 1.000 32.66731  ? 474  ALA A C   1 
ATOM   2253 O  O   . ALA A 1 271 ? 24.63411  12.85307 -16.61577 1.000 35.23436  ? 474  ALA A O   1 
ATOM   2254 C  CB  . ALA A 1 271 ? 23.03481  10.43343 -15.15957 1.000 31.24662  ? 474  ALA A CB  1 
ATOM   2255 N  N   . TYR A 1 272 ? 22.42855  13.26749 -16.52360 1.000 31.72043  ? 475  TYR A N   1 
ATOM   2256 C  CA  . TYR A 1 272 ? 22.36725  13.77446 -17.88701 1.000 34.52034  ? 475  TYR A CA  1 
ATOM   2257 C  C   . TYR A 1 272 ? 22.11720  15.27002 -18.01507 1.000 42.99894  ? 475  TYR A C   1 
ATOM   2258 O  O   . TYR A 1 272 ? 22.30968  15.81264 -19.11090 1.000 39.32403  ? 475  TYR A O   1 
ATOM   2259 C  CB  . TYR A 1 272 ? 21.28628  13.01647 -18.67546 1.000 32.46761  ? 475  TYR A CB  1 
ATOM   2260 C  CG  . TYR A 1 272 ? 21.62529  11.55631 -18.85226 1.000 34.54273  ? 475  TYR A CG  1 
ATOM   2261 C  CD1 . TYR A 1 272 ? 22.65095  11.17051 -19.70694 1.000 35.32531  ? 475  TYR A CD1 1 
ATOM   2262 C  CD2 . TYR A 1 272 ? 20.92583  10.56468 -18.17083 1.000 30.14191  ? 475  TYR A CD2 1 
ATOM   2263 C  CE1 . TYR A 1 272 ? 22.97841  9.85186  -19.87326 1.000 41.66546  ? 475  TYR A CE1 1 
ATOM   2264 C  CE2 . TYR A 1 272 ? 21.24665  9.23642  -18.33176 1.000 33.25118  ? 475  TYR A CE2 1 
ATOM   2265 C  CZ  . TYR A 1 272 ? 22.27800  8.88581  -19.18940 1.000 38.35014  ? 475  TYR A CZ  1 
ATOM   2266 O  OH  . TYR A 1 272 ? 22.61581  7.56672  -19.36667 1.000 42.87639  ? 475  TYR A OH  1 
ATOM   2267 N  N   . SER A 1 273 ? 21.71300  15.95509 -16.94945 1.000 41.62729  ? 476  SER A N   1 
ATOM   2268 C  CA  . SER A 1 273 ? 21.45822  17.38595 -17.03615 1.000 44.74229  ? 476  SER A CA  1 
ATOM   2269 C  C   . SER A 1 273 ? 22.77144  18.16073 -17.02827 1.000 55.72306  ? 476  SER A C   1 
ATOM   2270 O  O   . SER A 1 273 ? 23.70653  17.82045 -16.29729 1.000 51.97775  ? 476  SER A O   1 
ATOM   2271 C  CB  . SER A 1 273 ? 20.56299  17.83846 -15.88156 1.000 53.09543  ? 476  SER A CB  1 
ATOM   2272 O  OG  . SER A 1 273 ? 19.97803  19.09958 -16.15432 1.000 63.14857  ? 476  SER A OG  1 
ATOM   2273 N  N   . HIS A 1 274 ? 22.84986  19.19055 -17.86980 1.000 57.87817  ? 477  HIS A N   1 
ATOM   2274 C  CA  . HIS A 1 274 ? 24.03128  20.04060 -17.88148 1.000 63.03854  ? 477  HIS A CA  1 
ATOM   2275 C  C   . HIS A 1 274 ? 24.02988  20.96367 -16.66494 1.000 67.39670  ? 477  HIS A C   1 
ATOM   2276 O  O   . HIS A 1 274 ? 22.98425  21.28611 -16.09241 1.000 65.81312  ? 477  HIS A O   1 
ATOM   2277 C  CB  . HIS A 1 274 ? 24.10629  20.85787 -19.17107 1.000 65.28088  ? 477  HIS A CB  1 
ATOM   2278 C  CG  . HIS A 1 274 ? 24.42214  20.04128 -20.38762 1.000 66.31156  ? 477  HIS A CG  1 
ATOM   2279 N  ND1 . HIS A 1 274 ? 25.52338  19.21424 -20.46587 1.000 67.73239  ? 477  HIS A ND1 1 
ATOM   2280 C  CD2 . HIS A 1 274 ? 23.78124  19.92678 -21.57573 1.000 57.26631  ? 477  HIS A CD2 1 
ATOM   2281 C  CE1 . HIS A 1 274 ? 25.54433  18.62247 -21.64763 1.000 62.97147  ? 477  HIS A CE1 1 
ATOM   2282 N  NE2 . HIS A 1 274 ? 24.49725  19.03607 -22.33947 1.000 62.13583  ? 477  HIS A NE2 1 
ATOM   2283 N  N   . ASN A 1 275 ? 25.22584  21.39366 -16.27640 1.000 79.98827  ? 478  ASN A N   1 
ATOM   2284 C  CA  . ASN A 1 275 ? 25.42414  22.08631 -15.01129 1.000 83.82177  ? 478  ASN A CA  1 
ATOM   2285 C  C   . ASN A 1 275 ? 25.24635  23.59440 -15.15364 1.000 86.08445  ? 478  ASN A C   1 
ATOM   2286 O  O   . ASN A 1 275 ? 25.46656  24.17413 -16.22189 1.000 79.29872  ? 478  ASN A O   1 
ATOM   2287 C  CB  . ASN A 1 275 ? 26.81655  21.78740 -14.44936 1.000 80.70617  ? 478  ASN A CB  1 
ATOM   2288 N  N   . ASN A 1 276 ? 24.83861  24.22224 -14.05061 1.000 90.17821  ? 479  ASN A N   1 
ATOM   2289 C  CA  . ASN A 1 276 ? 24.77311  25.67943 -13.95226 1.000 92.14843  ? 479  ASN A CA  1 
ATOM   2290 C  C   . ASN A 1 276 ? 24.83779  26.04519 -12.47879 1.000 91.45575  ? 479  ASN A C   1 
ATOM   2291 O  O   . ASN A 1 276 ? 23.96307  25.64079 -11.70515 1.000 82.69846  ? 479  ASN A O   1 
ATOM   2292 C  CB  . ASN A 1 276 ? 23.49559  26.22907 -14.59517 1.000 88.63565  ? 479  ASN A CB  1 
ATOM   2293 C  CG  . ASN A 1 276 ? 23.44160  27.74937 -14.58704 1.000 96.49297  ? 479  ASN A CG  1 
ATOM   2294 O  OD1 . ASN A 1 276 ? 24.47045  28.42364 -14.48845 1.000 100.61009 ? 479  ASN A OD1 1 
ATOM   2295 N  ND2 . ASN A 1 276 ? 22.23619  28.29621 -14.69399 1.000 96.22560  ? 479  ASN A ND2 1 
ATOM   2296 N  N   . ALA A 1 277 ? 25.87544  26.79293 -12.08873 1.000 89.84303  ? 480  ALA A N   1 
ATOM   2297 C  CA  . ALA A 1 277 ? 26.02246  27.21401 -10.69917 1.000 88.57520  ? 480  ALA A CA  1 
ATOM   2298 C  C   . ALA A 1 277 ? 24.95128  28.21195 -10.28059 1.000 89.77480  ? 480  ALA A C   1 
ATOM   2299 O  O   . ALA A 1 277 ? 24.67809  28.34367 -9.08171  1.000 87.91716  ? 480  ALA A O   1 
ATOM   2300 C  CB  . ALA A 1 277 ? 27.41108  27.81639 -10.47365 1.000 87.10083  ? 480  ALA A CB  1 
ATOM   2301 N  N   . ARG A 1 278 ? 24.34832  28.92115 -11.23750 1.000 94.53734  ? 481  ARG A N   1 
ATOM   2302 C  CA  . ARG A 1 278 ? 23.21279  29.79739 -10.98086 1.000 95.00954  ? 481  ARG A CA  1 
ATOM   2303 C  C   . ARG A 1 278 ? 21.88920  29.03646 -10.90486 1.000 91.25247  ? 481  ARG A C   1 
ATOM   2304 O  O   . ARG A 1 278 ? 20.82312  29.64487 -11.06615 1.000 95.41341  ? 481  ARG A O   1 
ATOM   2305 C  CB  . ARG A 1 278 ? 23.13267  30.88523 -12.05712 1.000 87.34409  ? 481  ARG A CB  1 
ATOM   2306 N  N   . GLY A 1 279 ? 21.93934  27.72554 -10.66966 1.000 66.35284  ? 482  GLY A N   1 
ATOM   2307 C  CA  . GLY A 1 279 ? 20.74428  26.92193 -10.58125 1.000 58.82257  ? 482  GLY A CA  1 
ATOM   2308 C  C   . GLY A 1 279 ? 20.05943  26.74160 -11.92764 1.000 59.70412  ? 482  GLY A C   1 
ATOM   2309 O  O   . GLY A 1 279 ? 20.65754  26.84749 -13.00213 1.000 67.06406  ? 482  GLY A O   1 
ATOM   2310 N  N   . GLY A 1 280 ? 18.76655  26.46126 -11.84128 1.000 57.43072  ? 483  GLY A N   1 
ATOM   2311 C  CA  . GLY A 1 280 ? 17.93601  26.24633 -13.00521 1.000 50.22483  ? 483  GLY A CA  1 
ATOM   2312 C  C   . GLY A 1 280 ? 16.50310  26.56698 -12.65688 1.000 40.62352  ? 483  GLY A C   1 
ATOM   2313 O  O   . GLY A 1 280 ? 16.24329  27.21709 -11.64152 1.000 45.63082  ? 483  GLY A O   1 
ATOM   2314 N  N   . TYR A 1 281 ? 15.55662  26.10064 -13.45956 1.000 40.21979  ? 484  TYR A N   1 
ATOM   2315 C  CA  . TYR A 1 281 ? 14.15324  26.41052 -13.23420 1.000 37.65585  ? 484  TYR A CA  1 
ATOM   2316 C  C   . TYR A 1 281 ? 13.36177  25.11427 -13.14951 1.000 36.82142  ? 484  TYR A C   1 
ATOM   2317 O  O   . TYR A 1 281 ? 13.54875  24.21899 -13.98039 1.000 35.23508  ? 484  TYR A O   1 
ATOM   2318 C  CB  . TYR A 1 281 ? 13.61924  27.31809 -14.35392 1.000 36.86116  ? 484  TYR A CB  1 
ATOM   2319 C  CG  . TYR A 1 281 ? 14.36096  28.63996 -14.46798 1.000 42.48360  ? 484  TYR A CG  1 
ATOM   2320 C  CD1 . TYR A 1 281 ? 13.88271  29.78505 -13.84895 1.000 56.31624  ? 484  TYR A CD1 1 
ATOM   2321 C  CD2 . TYR A 1 281 ? 15.54448  28.73355 -15.19530 1.000 48.29718  ? 484  TYR A CD2 1 
ATOM   2322 C  CE1 . TYR A 1 281 ? 14.56544  30.99668 -13.95736 1.000 51.74175  ? 484  TYR A CE1 1 
ATOM   2323 C  CE2 . TYR A 1 281 ? 16.23086  29.93487 -15.30725 1.000 53.10735  ? 484  TYR A CE2 1 
ATOM   2324 C  CZ  . TYR A 1 281 ? 15.73561  31.05961 -14.68197 1.000 62.86247  ? 484  TYR A CZ  1 
ATOM   2325 O  OH  . TYR A 1 281 ? 16.40902  32.25837 -14.78207 1.000 71.22688  ? 484  TYR A OH  1 
ATOM   2326 N  N   . ILE A 1 282 ? 12.49279  25.01462 -12.13422 1.000 30.81344  ? 485  ILE A N   1 
ATOM   2327 C  CA  . ILE A 1 282 ? 11.62603  23.84313 -11.98155 1.000 28.74369  ? 485  ILE A CA  1 
ATOM   2328 C  C   . ILE A 1 282 ? 10.93116  23.52879 -13.29910 1.000 32.11532  ? 485  ILE A C   1 
ATOM   2329 O  O   . ILE A 1 282 ? 10.91103  22.38276 -13.75898 1.000 29.68992  ? 485  ILE A O   1 
ATOM   2330 C  CB  . ILE A 1 282 ? 10.57770  24.07519 -10.88133 1.000 31.98883  ? 485  ILE A CB  1 
ATOM   2331 C  CG1 . ILE A 1 282 ? 11.22189  24.35328 -9.52860  1.000 31.71888  ? 485  ILE A CG1 1 
ATOM   2332 C  CG2 . ILE A 1 282 ? 9.62580   22.88018 -10.79259 1.000 28.01826  ? 485  ILE A CG2 1 
ATOM   2333 C  CD1 . ILE A 1 282 ? 10.27260  25.05337 -8.58246  1.000 31.51550  ? 485  ILE A CD1 1 
ATOM   2334 N  N   . GLU A 1 283 ? 10.31777  24.54810 -13.89879 1.000 32.78111  ? 486  GLU A N   1 
ATOM   2335 C  CA  . GLU A 1 283 ? 9.51992   24.33048 -15.09997 1.000 31.76262  ? 486  GLU A CA  1 
ATOM   2336 C  C   . GLU A 1 283 ? 10.36371  23.80021 -16.24969 1.000 34.20027  ? 486  GLU A C   1 
ATOM   2337 O  O   . GLU A 1 283 ? 9.84974   23.06868 -17.10306 1.000 35.51751  ? 486  GLU A O   1 
ATOM   2338 C  CB  . GLU A 1 283 ? 8.80284   25.62336 -15.48977 1.000 33.94964  ? 486  GLU A CB  1 
ATOM   2339 C  CG  . GLU A 1 283 ? 9.72404   26.81846 -15.74241 1.000 38.69702  ? 486  GLU A CG  1 
ATOM   2340 C  CD  . GLU A 1 283 ? 10.08116  27.59940 -14.46702 1.000 38.76091  ? 486  GLU A CD  1 
ATOM   2341 O  OE1 . GLU A 1 283 ? 9.86983   27.08249 -13.33461 1.000 37.28119  ? 486  GLU A OE1 1 
ATOM   2342 O  OE2 . GLU A 1 283 ? 10.57723  28.73713 -14.61229 1.000 41.20172  ? 486  GLU A OE2 1 
ATOM   2343 N  N   . ASP A 1 284 ? 11.65121  24.15203 -16.29889 1.000 33.58610  ? 487  ASP A N   1 
ATOM   2344 C  CA  . ASP A 1 284 ? 12.50204  23.65601 -17.37543 1.000 35.62740  ? 487  ASP A CA  1 
ATOM   2345 C  C   . ASP A 1 284 ? 12.70774  22.15235 -17.25518 1.000 33.51456  ? 487  ASP A C   1 
ATOM   2346 O  O   . ASP A 1 284 ? 12.59693  21.42038 -18.24466 1.000 33.02386  ? 487  ASP A O   1 
ATOM   2347 C  CB  . ASP A 1 284 ? 13.84739  24.37259 -17.37599 1.000 36.42990  ? 487  ASP A CB  1 
ATOM   2348 C  CG  . ASP A 1 284 ? 13.74847  25.81341 -17.85320 1.000 48.77058  ? 487  ASP A CG  1 
ATOM   2349 O  OD1 . ASP A 1 284 ? 12.62639  26.28067 -18.15069 1.000 43.46656  ? 487  ASP A OD1 1 
ATOM   2350 O  OD2 . ASP A 1 284 ? 14.80386  26.47340 -17.93396 1.000 52.92852  ? 487  ASP A OD2 1 
ATOM   2351 N  N   . GLY A 1 285 ? 13.01219  21.67614 -16.04875 1.000 31.06288  ? 488  GLY A N   1 
ATOM   2352 C  CA  . GLY A 1 285 ? 13.16155  20.24049 -15.85140 1.000 29.06947  ? 488  GLY A CA  1 
ATOM   2353 C  C   . GLY A 1 285 ? 11.87896  19.47567 -16.11038 1.000 28.38085  ? 488  GLY A C   1 
ATOM   2354 O  O   . GLY A 1 285 ? 11.90331  18.36429 -16.65244 1.000 29.02984  ? 488  GLY A O   1 
ATOM   2355 N  N   . LEU A 1 286 ? 10.74064  20.04968 -15.72052 1.000 27.98398  ? 489  LEU A N   1 
ATOM   2356 C  CA  . LEU A 1 286 ? 9.46526   19.39226 -15.98458 1.000 29.61870  ? 489  LEU A CA  1 
ATOM   2357 C  C   . LEU A 1 286 ? 9.21138   19.28383 -17.48250 1.000 28.39164  ? 489  LEU A C   1 
ATOM   2358 O  O   . LEU A 1 286 ? 8.83664   18.21711 -17.98381 1.000 29.00984  ? 489  LEU A O   1 
ATOM   2359 C  CB  . LEU A 1 286 ? 8.32552   20.14523 -15.30525 1.000 26.64848  ? 489  LEU A CB  1 
ATOM   2360 C  CG  . LEU A 1 286 ? 8.28717   20.14422 -13.76400 1.000 25.17385  ? 489  LEU A CG  1 
ATOM   2361 C  CD1 . LEU A 1 286 ? 7.13184   20.99538 -13.27608 1.000 27.39932  ? 489  LEU A CD1 1 
ATOM   2362 C  CD2 . LEU A 1 286 ? 8.15083   18.71704 -13.24376 1.000 24.08174  ? 489  LEU A CD2 1 
ATOM   2363 N  N   . THR A 1 287 ? 9.40099   20.38454 -18.21168 1.000 30.09665  ? 490  THR A N   1 
ATOM   2364 C  CA  . THR A 1 287 ? 9.21413   20.35337 -19.66304 1.000 31.75512  ? 490  THR A CA  1 
ATOM   2365 C  C   . THR A 1 287 ? 10.12429  19.31258 -20.30341 1.000 36.37930  ? 490  THR A C   1 
ATOM   2366 O  O   . THR A 1 287 ? 9.68584   18.49792 -21.12893 1.000 33.73594  ? 490  THR A O   1 
ATOM   2367 C  CB  . THR A 1 287 ? 9.49327   21.74232 -20.25961 1.000 34.50112  ? 490  THR A CB  1 
ATOM   2368 O  OG1 . THR A 1 287 ? 8.60848   22.71115 -19.68097 1.000 38.40005  ? 490  THR A OG1 1 
ATOM   2369 C  CG2 . THR A 1 287 ? 9.29640   21.71633 -21.75556 1.000 36.15045  ? 490  THR A CG2 1 
ATOM   2370 N  N   . TRP A 1 288 ? 11.40325  19.33401 -19.92373 1.000 32.40571  ? 491  TRP A N   1 
ATOM   2371 C  CA  . TRP A 1 288 ? 12.40980  18.42387 -20.46355 1.000 33.99670  ? 491  TRP A CA  1 
ATOM   2372 C  C   . TRP A 1 288 ? 11.98933  16.96608 -20.33039 1.000 30.31572  ? 491  TRP A C   1 
ATOM   2373 O  O   . TRP A 1 288 ? 12.19838  16.15693 -21.24861 1.000 31.00486  ? 491  TRP A O   1 
ATOM   2374 C  CB  . TRP A 1 288 ? 13.71968  18.68194 -19.71933 1.000 35.99286  ? 491  TRP A CB  1 
ATOM   2375 C  CG  . TRP A 1 288 ? 14.92509  17.91934 -20.14347 1.000 34.30095  ? 491  TRP A CG  1 
ATOM   2376 C  CD1 . TRP A 1 288 ? 15.64273  18.07788 -21.29612 1.000 35.84222  ? 491  TRP A CD1 1 
ATOM   2377 C  CD2 . TRP A 1 288 ? 15.60197  16.91756 -19.37988 1.000 30.61216  ? 491  TRP A CD2 1 
ATOM   2378 N  NE1 . TRP A 1 288 ? 16.71896  17.22063 -21.30433 1.000 36.53358  ? 491  TRP A NE1 1 
ATOM   2379 C  CE2 . TRP A 1 288 ? 16.72269  16.50599 -20.13278 1.000 32.88133  ? 491  TRP A CE2 1 
ATOM   2380 C  CE3 . TRP A 1 288 ? 15.37869  16.34156 -18.12398 1.000 33.16785  ? 491  TRP A CE3 1 
ATOM   2381 C  CZ2 . TRP A 1 288 ? 17.60385  15.52316 -19.68039 1.000 32.10335  ? 491  TRP A CZ2 1 
ATOM   2382 C  CZ3 . TRP A 1 288 ? 16.24749  15.36841 -17.67260 1.000 33.49235  ? 491  TRP A CZ3 1 
ATOM   2383 C  CH2 . TRP A 1 288 ? 17.35572  14.97373 -18.44569 1.000 33.18336  ? 491  TRP A CH2 1 
ATOM   2384 N  N   . TYR A 1 289 ? 11.40713  16.61120 -19.18774 1.000 27.60923  ? 492  TYR A N   1 
ATOM   2385 C  CA  . TYR A 1 289 ? 11.01414  15.22644 -18.96740 1.000 26.10661  ? 492  TYR A CA  1 
ATOM   2386 C  C   . TYR A 1 289 ? 9.78084   14.85177 -19.77967 1.000 31.07157  ? 492  TYR A C   1 
ATOM   2387 O  O   . TYR A 1 289 ? 9.64384   13.68836 -20.18018 1.000 29.92319  ? 492  TYR A O   1 
ATOM   2388 C  CB  . TYR A 1 289 ? 10.76308  14.98269 -17.47466 1.000 25.36315  ? 492  TYR A CB  1 
ATOM   2389 C  CG  . TYR A 1 289 ? 11.29155  13.64689 -16.98530 1.000 24.58633  ? 492  TYR A CG  1 
ATOM   2390 C  CD1 . TYR A 1 289 ? 12.64162  13.48708 -16.66637 1.000 26.53389  ? 492  TYR A CD1 1 
ATOM   2391 C  CD2 . TYR A 1 289 ? 10.45300  12.55108 -16.86149 1.000 24.67748  ? 492  TYR A CD2 1 
ATOM   2392 C  CE1 . TYR A 1 289 ? 13.13223  12.27225 -16.23098 1.000 25.67278  ? 492  TYR A CE1 1 
ATOM   2393 C  CE2 . TYR A 1 289 ? 10.93658  11.32380 -16.40692 1.000 25.15145  ? 492  TYR A CE2 1 
ATOM   2394 C  CZ  . TYR A 1 289 ? 12.28216  11.19895 -16.11019 1.000 27.37692  ? 492  TYR A CZ  1 
ATOM   2395 O  OH  . TYR A 1 289 ? 12.76072  9.98477  -15.67459 1.000 30.01580  ? 492  TYR A OH  1 
ATOM   2396 N  N   . LEU A 1 290 ? 8.88621   15.81043 -20.04575 1.000 30.03992  ? 493  LEU A N   1 
ATOM   2397 C  CA  . LEU A 1 290 ? 7.53754   15.48811 -20.51357 1.000 27.91053  ? 493  LEU A CA  1 
ATOM   2398 C  C   . LEU A 1 290 ? 7.29914   15.72126 -22.00577 1.000 30.81213  ? 493  LEU A C   1 
ATOM   2399 O  O   . LEU A 1 290 ? 6.58052   14.93031 -22.62169 1.000 30.37433  ? 493  LEU A O   1 
ATOM   2400 C  CB  . LEU A 1 290 ? 6.49605   16.27265 -19.71052 1.000 27.76153  ? 493  LEU A CB  1 
ATOM   2401 C  CG  . LEU A 1 290 ? 6.42099   15.91587 -18.22182 1.000 25.76315  ? 493  LEU A CG  1 
ATOM   2402 C  CD1 . LEU A 1 290 ? 5.37338   16.74360 -17.50876 1.000 30.04015  ? 493  LEU A CD1 1 
ATOM   2403 C  CD2 . LEU A 1 290 ? 6.12423   14.41263 -18.04623 1.000 25.91109  ? 493  LEU A CD2 1 
ATOM   2404 N  N   . TYR A 1 291 ? 7.83828   16.78166 -22.60996 1.000 32.19211  ? 494  TYR A N   1 
ATOM   2405 C  CA  . TYR A 1 291 ? 7.56270   17.04142 -24.02601 1.000 35.80767  ? 494  TYR A CA  1 
ATOM   2406 C  C   . TYR A 1 291 ? 8.64321   17.94997 -24.60403 1.000 38.82163  ? 494  TYR A C   1 
ATOM   2407 O  O   . TYR A 1 291 ? 9.43921   18.54660 -23.87741 1.000 37.34956  ? 494  TYR A O   1 
ATOM   2408 C  CB  . TYR A 1 291 ? 6.16306   17.64575 -24.22458 1.000 38.40868  ? 494  TYR A CB  1 
ATOM   2409 C  CG  . TYR A 1 291 ? 5.90170   18.91325 -23.42203 1.000 41.47385  ? 494  TYR A CG  1 
ATOM   2410 C  CD1 . TYR A 1 291 ? 5.38935   18.84813 -22.13569 1.000 41.38776  ? 494  TYR A CD1 1 
ATOM   2411 C  CD2 . TYR A 1 291 ? 6.14863   20.17253 -23.97028 1.000 47.15255  ? 494  TYR A CD2 1 
ATOM   2412 C  CE1 . TYR A 1 291 ? 5.14233   20.00675 -21.39618 1.000 42.37643  ? 494  TYR A CE1 1 
ATOM   2413 C  CE2 . TYR A 1 291 ? 5.90818   21.32975 -23.24459 1.000 50.10452  ? 494  TYR A CE2 1 
ATOM   2414 C  CZ  . TYR A 1 291 ? 5.40474   21.24049 -21.96160 1.000 52.05130  ? 494  TYR A CZ  1 
ATOM   2415 O  OH  . TYR A 1 291 ? 5.16864   22.39180 -21.23984 1.000 48.20882  ? 494  TYR A OH  1 
ATOM   2416 N  N   . LYS A 1 292 ? 8.64581   18.06543 -25.93024 1.000 38.30203  ? 495  LYS A N   1 
ATOM   2417 C  CA  . LYS A 1 292 ? 9.72208   18.74629 -26.64096 1.000 39.78959  ? 495  LYS A CA  1 
ATOM   2418 C  C   . LYS A 1 292 ? 9.46200   20.24743 -26.71153 1.000 55.08496  ? 495  LYS A C   1 
ATOM   2419 O  O   . LYS A 1 292 ? 8.38010   20.67989 -27.12030 1.000 49.66260  ? 495  LYS A O   1 
ATOM   2420 C  CB  . LYS A 1 292 ? 9.89050   18.15962 -28.04499 1.000 42.34425  ? 495  LYS A CB  1 
ATOM   2421 C  CG  . LYS A 1 292 ? 10.27591  16.68049 -28.02649 1.000 51.14365  ? 495  LYS A CG  1 
ATOM   2422 C  CD  . LYS A 1 292 ? 10.83326  16.19094 -29.35554 1.000 53.78424  ? 495  LYS A CD  1 
ATOM   2423 C  CE  . LYS A 1 292 ? 9.73132   15.84232 -30.32746 1.000 52.87799  ? 495  LYS A CE  1 
ATOM   2424 N  NZ  . LYS A 1 292 ? 10.28621  15.38902 -31.63596 1.000 57.03754  ? 495  LYS A NZ  1 
ATOM   2425 N  N   . ARG A 1 293 ? 10.45244  21.03288 -26.27896 1.000 47.32532  ? 496  ARG A N   1 
ATOM   2426 C  CA  . ARG A 1 293 ? 10.48738  22.47643 -26.47202 1.000 49.81175  ? 496  ARG A CA  1 
ATOM   2427 C  C   . ARG A 1 293 ? 11.90803  22.88105 -26.84433 1.000 47.85613  ? 496  ARG A C   1 
ATOM   2428 O  O   . ARG A 1 293 ? 12.87389  22.39813 -26.24866 1.000 48.22542  ? 496  ARG A O   1 
ATOM   2429 C  CB  . ARG A 1 293 ? 10.02137  23.22425 -25.21141 1.000 60.71248  ? 496  ARG A CB  1 
ATOM   2430 C  CG  . ARG A 1 293 ? 8.61552   23.79671 -25.31845 1.000 68.37555  ? 496  ARG A CG  1 
ATOM   2431 C  CD  . ARG A 1 293 ? 8.14314   24.37266 -23.99155 1.000 71.18566  ? 496  ARG A CD  1 
ATOM   2432 N  NE  . ARG A 1 293 ? 8.87071   25.57361 -23.59400 1.000 77.44541  ? 496  ARG A NE  1 
ATOM   2433 C  CZ  . ARG A 1 293 ? 8.34783   26.79254 -23.56644 1.000 77.39541  ? 496  ARG A CZ  1 
ATOM   2434 N  NH1 . ARG A 1 293 ? 7.08872   27.01267 -23.90965 1.000 77.19625  ? 496  ARG A NH1 1 
ATOM   2435 N  NH2 . ARG A 1 293 ? 9.10466   27.81476 -23.17596 1.000 75.64668  ? 496  ARG A NH2 1 
ATOM   2436 N  N   . ASP A 1 294 ? 12.03216  23.75992 -27.84682 1.000 52.13167  ? 497  ASP A N   1 
ATOM   2437 C  CA  . ASP A 1 294 ? 13.35164  24.18937 -28.29745 1.000 50.33355  ? 497  ASP A CA  1 
ATOM   2438 C  C   . ASP A 1 294 ? 14.16658  24.80390 -27.16706 1.000 49.72595  ? 497  ASP A C   1 
ATOM   2439 O  O   . ASP A 1 294 ? 15.39139  24.64077 -27.12808 1.000 54.61370  ? 497  ASP A O   1 
ATOM   2440 C  CB  . ASP A 1 294 ? 13.20616  25.18933 -29.44647 1.000 55.42324  ? 497  ASP A CB  1 
ATOM   2441 C  CG  . ASP A 1 294 ? 12.37271  24.64184 -30.58851 1.000 72.04083  ? 497  ASP A CG  1 
ATOM   2442 O  OD1 . ASP A 1 294 ? 12.86890  24.63282 -31.73634 1.000 77.66559  ? 497  ASP A OD1 1 
ATOM   2443 O  OD2 . ASP A 1 294 ? 11.22854  24.20261 -30.33437 1.000 74.21073  ? 497  ASP A OD2 1 
ATOM   2444 N  N   . GLY A 1 295 ? 13.51143  25.51292 -26.24486 1.000 54.32441  ? 498  GLY A N   1 
ATOM   2445 C  CA  . GLY A 1 295 ? 14.23553  26.15719 -25.16217 1.000 53.10117  ? 498  GLY A CA  1 
ATOM   2446 C  C   . GLY A 1 295 ? 15.04305  25.19102 -24.31827 1.000 53.59273  ? 498  GLY A C   1 
ATOM   2447 O  O   . GLY A 1 295 ? 16.12623  25.53727 -23.83853 1.000 52.23501  ? 498  GLY A O   1 
ATOM   2448 N  N   . GLN A 1 296 ? 14.53770  23.97379 -24.13153 1.000 51.61742  ? 499  GLN A N   1 
ATOM   2449 C  CA  . GLN A 1 296 ? 15.19346  22.95788 -23.31718 1.000 44.85519  ? 499  GLN A CA  1 
ATOM   2450 C  C   . GLN A 1 296 ? 16.07602  22.01827 -24.13657 1.000 42.54798  ? 499  GLN A C   1 
ATOM   2451 O  O   . GLN A 1 296 ? 16.52568  20.99579 -23.60517 1.000 48.90354  ? 499  GLN A O   1 
ATOM   2452 C  CB  . GLN A 1 296 ? 14.14812  22.14374 -22.53776 1.000 44.58499  ? 499  GLN A CB  1 
ATOM   2453 C  CG  . GLN A 1 296 ? 13.62392  22.80380 -21.26233 1.000 49.22071  ? 499  GLN A CG  1 
ATOM   2454 C  CD  . GLN A 1 296 ? 12.93508  24.13891 -21.51682 1.000 59.76007  ? 499  GLN A CD  1 
ATOM   2455 O  OE1 . GLN A 1 296 ? 11.82948  24.19031 -22.05903 1.000 57.90733  ? 499  GLN A OE1 1 
ATOM   2456 N  NE2 . GLN A 1 296 ? 13.59316  25.22679 -21.13011 1.000 52.70042  ? 499  GLN A NE2 1 
ATOM   2457 N  N   . LYS A 1 297 ? 16.33027  22.34047 -25.41380 1.000 49.43753  ? 500  LYS A N   1 
ATOM   2458 C  CA  . LYS A 1 297 ? 17.15757  21.47917 -26.25781 1.000 49.24846  ? 500  LYS A CA  1 
ATOM   2459 C  C   . LYS A 1 297 ? 18.54900  21.26939 -25.66885 1.000 51.68799  ? 500  LYS A C   1 
ATOM   2460 O  O   . LYS A 1 297 ? 19.15237  20.20803 -25.87000 1.000 56.27033  ? 500  LYS A O   1 
ATOM   2461 C  CB  . LYS A 1 297 ? 17.27097  22.07025 -27.66945 1.000 47.69178  ? 500  LYS A CB  1 
ATOM   2462 N  N   . ASN A 1 298 ? 19.06880  22.25871 -24.93586 1.000 50.40308  ? 501  ASN A N   1 
ATOM   2463 C  CA  . ASN A 1 298 ? 20.41458  22.21086 -24.37815 1.000 51.53918  ? 501  ASN A CA  1 
ATOM   2464 C  C   . ASN A 1 298 ? 20.42202  21.99866 -22.86742 1.000 53.53414  ? 501  ASN A C   1 
ATOM   2465 O  O   . ASN A 1 298 ? 21.44609  22.24171 -22.21973 1.000 52.20791  ? 501  ASN A O   1 
ATOM   2466 C  CB  . ASN A 1 298 ? 21.17497  23.49022 -24.72232 1.000 55.81798  ? 501  ASN A CB  1 
ATOM   2467 N  N   . LEU A 1 299 ? 19.30006  21.56540 -22.28824 1.000 42.14872  ? 502  LEU A N   1 
ATOM   2468 C  CA  . LEU A 1 299 ? 19.26717  21.32060 -20.84767 1.000 39.44641  ? 502  LEU A CA  1 
ATOM   2469 C  C   . LEU A 1 299 ? 20.18318  20.16142 -20.46791 1.000 46.13222  ? 502  LEU A C   1 
ATOM   2470 O  O   . LEU A 1 299 ? 20.92260  20.24527 -19.47995 1.000 45.66762  ? 502  LEU A O   1 
ATOM   2471 C  CB  . LEU A 1 299 ? 17.82730  21.05793 -20.39195 1.000 41.84161  ? 502  LEU A CB  1 
ATOM   2472 C  CG  . LEU A 1 299 ? 17.55112  20.90295 -18.88567 1.000 39.07318  ? 502  LEU A CG  1 
ATOM   2473 C  CD1 . LEU A 1 299 ? 16.14828  21.39330 -18.49380 1.000 38.21060  ? 502  LEU A CD1 1 
ATOM   2474 C  CD2 . LEU A 1 299 ? 17.73173  19.45678 -18.43599 1.000 43.34773  ? 502  LEU A CD2 1 
ATOM   2475 N  N   . GLY A 1 300 ? 20.15640  19.07294 -21.24391 1.000 43.00535  ? 503  GLY A N   1 
ATOM   2476 C  CA  . GLY A 1 300 ? 20.93851  17.89360 -20.93691 1.000 43.14022  ? 503  GLY A CA  1 
ATOM   2477 C  C   . GLY A 1 300 ? 21.51468  17.26272 -22.18943 1.000 45.52538  ? 503  GLY A C   1 
ATOM   2478 O  O   . GLY A 1 300 ? 21.27039  17.72081 -23.30692 1.000 45.03658  ? 503  GLY A O   1 
ATOM   2479 N  N   . SER A 1 301 ? 22.29800  16.20216 -21.98098 1.000 42.80645  ? 504  SER A N   1 
ATOM   2480 C  CA  . SER A 1 301 ? 22.88777  15.48439 -23.10761 1.000 44.88505  ? 504  SER A CA  1 
ATOM   2481 C  C   . SER A 1 301 ? 21.90322  14.53366 -23.77682 1.000 43.10130  ? 504  SER A C   1 
ATOM   2482 O  O   . SER A 1 301 ? 22.21721  13.98349 -24.84052 1.000 47.02251  ? 504  SER A O   1 
ATOM   2483 C  CB  . SER A 1 301 ? 24.13388  14.71549 -22.65416 1.000 48.65031  ? 504  SER A CB  1 
ATOM   2484 O  OG  . SER A 1 301 ? 23.86556  13.94040 -21.49339 1.000 45.87095  ? 504  SER A OG  1 
ATOM   2485 N  N   . ILE A 1 302 ? 20.73682  14.31840 -23.16896 1.000 41.55522  ? 505  ILE A N   1 
ATOM   2486 C  CA  . ILE A 1 302 ? 19.61888  13.60827 -23.77272 1.000 36.49070  ? 505  ILE A CA  1 
ATOM   2487 C  C   . ILE A 1 302 ? 18.38631  14.48552 -23.59284 1.000 40.07364  ? 505  ILE A C   1 
ATOM   2488 O  O   . ILE A 1 302 ? 18.39154  15.44191 -22.81953 1.000 36.91845  ? 505  ILE A O   1 
ATOM   2489 C  CB  . ILE A 1 302 ? 19.39021  12.21560 -23.14292 1.000 37.11915  ? 505  ILE A CB  1 
ATOM   2490 C  CG1 . ILE A 1 302 ? 18.90857  12.35502 -21.69726 1.000 33.12629  ? 505  ILE A CG1 1 
ATOM   2491 C  CG2 . ILE A 1 302 ? 20.66167  11.38271 -23.19317 1.000 39.72621  ? 505  ILE A CG2 1 
ATOM   2492 C  CD1 . ILE A 1 302 ? 18.53371  11.03512 -21.06243 1.000 34.17980  ? 505  ILE A CD1 1 
ATOM   2493 N  N   . TYR A 1 303 ? 17.31967  14.15127 -24.31567 1.000 37.07229  ? 506  TYR A N   1 
ATOM   2494 C  CA  . TYR A 1 303 ? 16.03903  14.84426 -24.17266 1.000 38.73000  ? 506  TYR A CA  1 
ATOM   2495 C  C   . TYR A 1 303 ? 14.94338  13.79782 -24.00312 1.000 34.26394  ? 506  TYR A C   1 
ATOM   2496 O  O   . TYR A 1 303 ? 14.48771  13.21190 -25.00383 1.000 35.81902  ? 506  TYR A O   1 
ATOM   2497 C  CB  . TYR A 1 303 ? 15.74299  15.75296 -25.36778 1.000 37.53526  ? 506  TYR A CB  1 
ATOM   2498 C  CG  . TYR A 1 303 ? 14.71648  16.82429 -25.04254 1.000 39.43182  ? 506  TYR A CG  1 
ATOM   2499 C  CD1 . TYR A 1 303 ? 13.43740  16.48108 -24.62628 1.000 41.73174  ? 506  TYR A CD1 1 
ATOM   2500 C  CD2 . TYR A 1 303 ? 15.02980  18.17544 -25.13316 1.000 43.09340  ? 506  TYR A CD2 1 
ATOM   2501 C  CE1 . TYR A 1 303 ? 12.50053  17.43973 -24.31191 1.000 38.80524  ? 506  TYR A CE1 1 
ATOM   2502 C  CE2 . TYR A 1 303 ? 14.08839  19.14766 -24.81998 1.000 41.19750  ? 506  TYR A CE2 1 
ATOM   2503 C  CZ  . TYR A 1 303 ? 12.82625  18.76737 -24.40740 1.000 37.79771  ? 506  TYR A CZ  1 
ATOM   2504 O  OH  . TYR A 1 303 ? 11.87115  19.70452 -24.07897 1.000 39.80075  ? 506  TYR A OH  1 
ATOM   2505 N  N   . PRO A 1 304 ? 14.50322  13.52825 -22.76792 1.000 33.47999  ? 507  PRO A N   1 
ATOM   2506 C  CA  . PRO A 1 304 ? 13.45835  12.51373 -22.55524 1.000 28.98229  ? 507  PRO A CA  1 
ATOM   2507 C  C   . PRO A 1 304 ? 12.17408  12.79554 -23.32163 1.000 35.85670  ? 507  PRO A C   1 
ATOM   2508 O  O   . PRO A 1 304 ? 11.75010  11.95196 -24.12214 1.000 32.62507  ? 507  PRO A O   1 
ATOM   2509 C  CB  . PRO A 1 304 ? 13.23236  12.55241 -21.03361 1.000 27.83435  ? 507  PRO A CB  1 
ATOM   2510 C  CG  . PRO A 1 304 ? 14.58705  12.97395 -20.50000 1.000 29.16017  ? 507  PRO A CG  1 
ATOM   2511 C  CD  . PRO A 1 304 ? 15.07089  14.00219 -21.49131 1.000 32.79638  ? 507  PRO A CD  1 
ATOM   2512 N  N   . GLY A 1 305 ? 11.55402  13.95816 -23.08468 1.000 31.42113  ? 508  GLY A N   1 
ATOM   2513 C  CA  . GLY A 1 305 ? 10.31543  14.34333 -23.75169 1.000 33.68362  ? 508  GLY A CA  1 
ATOM   2514 C  C   . GLY A 1 305 ? 9.34302   13.19131 -23.90213 1.000 30.48614  ? 508  GLY A C   1 
ATOM   2515 O  O   . GLY A 1 305 ? 8.89672   12.88589 -25.01133 1.000 33.64619  ? 508  GLY A O   1 
ATOM   2516 N  N   . LEU A 1 306 ? 9.02033   12.54000 -22.78495 1.000 28.92727  ? 509  LEU A N   1 
ATOM   2517 C  CA  . LEU A 1 306 ? 8.47461   11.18493 -22.83041 1.000 27.81826  ? 509  LEU A CA  1 
ATOM   2518 C  C   . LEU A 1 306 ? 7.02722   11.12263 -23.28891 1.000 29.01819  ? 509  LEU A C   1 
ATOM   2519 O  O   . LEU A 1 306 ? 6.56829   10.05087 -23.70005 1.000 32.60016  ? 509  LEU A O   1 
ATOM   2520 C  CB  . LEU A 1 306 ? 8.58848   10.53035 -21.44985 1.000 25.64066  ? 509  LEU A CB  1 
ATOM   2521 C  CG  . LEU A 1 306 ? 10.02155  10.33462 -20.96278 1.000 28.19779  ? 509  LEU A CG  1 
ATOM   2522 C  CD1 . LEU A 1 306 ? 9.98343   9.86205  -19.51723 1.000 28.96189  ? 509  LEU A CD1 1 
ATOM   2523 C  CD2 . LEU A 1 306 ? 10.76085  9.33530  -21.84639 1.000 30.21327  ? 509  LEU A CD2 1 
ATOM   2524 N  N   . PHE A 1 307 ? 6.29408   12.22612 -23.22996 1.000 29.69301  ? 510  PHE A N   1 
ATOM   2525 C  CA  . PHE A 1 307 ? 4.88986   12.20864 -23.60375 1.000 30.04409  ? 510  PHE A CA  1 
ATOM   2526 C  C   . PHE A 1 307 ? 4.59303   13.35084 -24.55637 1.000 33.86310  ? 510  PHE A C   1 
ATOM   2527 O  O   . PHE A 1 307 ? 3.56029   14.01710 -24.45600 1.000 33.08195  ? 510  PHE A O   1 
ATOM   2528 C  CB  . PHE A 1 307 ? 4.00285   12.25753 -22.36090 1.000 28.77638  ? 510  PHE A CB  1 
ATOM   2529 C  CG  . PHE A 1 307 ? 4.30860   11.15912 -21.36852 1.000 28.50963  ? 510  PHE A CG  1 
ATOM   2530 C  CD1 . PHE A 1 307 ? 3.82240   9.87948  -21.57308 1.000 29.73649  ? 510  PHE A CD1 1 
ATOM   2531 C  CD2 . PHE A 1 307 ? 5.10057   11.40154 -20.25371 1.000 25.98565  ? 510  PHE A CD2 1 
ATOM   2532 C  CE1 . PHE A 1 307 ? 4.10990   8.85329  -20.68639 1.000 25.04664  ? 510  PHE A CE1 1 
ATOM   2533 C  CE2 . PHE A 1 307 ? 5.39163   10.37716 -19.34512 1.000 26.09821  ? 510  PHE A CE2 1 
ATOM   2534 C  CZ  . PHE A 1 307 ? 4.88665   9.10413  -19.55190 1.000 24.69687  ? 510  PHE A CZ  1 
ATOM   2535 N  N   . ASN A 1 308 ? 5.51606   13.58266 -25.49616 1.000 33.46048  ? 511  ASN A N   1 
ATOM   2536 C  CA  . ASN A 1 308 ? 5.37599   14.69571 -26.43040 1.000 36.98841  ? 511  ASN A CA  1 
ATOM   2537 C  C   . ASN A 1 308 ? 4.07986   14.58545 -27.21876 1.000 47.27756  ? 511  ASN A C   1 
ATOM   2538 O  O   . ASN A 1 308 ? 3.38051   15.58591 -27.42587 1.000 49.09293  ? 511  ASN A O   1 
ATOM   2539 C  CB  . ASN A 1 308 ? 6.58311   14.74051 -27.37024 1.000 39.04210  ? 511  ASN A CB  1 
ATOM   2540 C  CG  . ASN A 1 308 ? 6.59117   15.97869 -28.24541 1.000 41.03318  ? 511  ASN A CG  1 
ATOM   2541 O  OD1 . ASN A 1 308 ? 6.71728   17.09429 -27.73849 1.000 41.36954  ? 511  ASN A OD1 1 
ATOM   2542 N  ND2 . ASN A 1 308 ? 6.45680   15.79271 -29.56523 1.000 42.86035  ? 511  ASN A ND2 1 
ATOM   2543 N  N   A ASP A 1 309 ? 3.75513   13.36363 -27.65174 0.400 38.21161  ? 512  ASP A N   1 
ATOM   2544 N  N   B ASP A 1 309 ? 3.71933   13.38322 -27.65792 0.600 38.13367  ? 512  ASP A N   1 
ATOM   2545 C  CA  A ASP A 1 309 ? 2.52790   13.07531 -28.38240 0.400 43.87829  ? 512  ASP A CA  1 
ATOM   2546 C  CA  B ASP A 1 309 ? 2.50162   13.26580 -28.45204 0.600 43.97242  ? 512  ASP A CA  1 
ATOM   2547 C  C   A ASP A 1 309 ? 1.29091   13.54456 -27.63031 0.400 43.40557  ? 512  ASP A C   1 
ATOM   2548 C  C   B ASP A 1 309 ? 1.22671   13.34293 -27.62055 0.600 43.48471  ? 512  ASP A C   1 
ATOM   2549 O  O   A ASP A 1 309 ? 0.30314   13.95553 -28.25202 0.400 42.97216  ? 512  ASP A O   1 
ATOM   2550 O  O   B ASP A 1 309 ? 0.13534   13.26520 -28.19862 0.600 43.23957  ? 512  ASP A O   1 
ATOM   2551 C  CB  A ASP A 1 309 ? 2.45033   11.56811 -28.63223 0.400 43.96845  ? 512  ASP A CB  1 
ATOM   2552 C  CB  B ASP A 1 309 ? 2.50422   11.96813 -29.26739 0.600 44.66116  ? 512  ASP A CB  1 
ATOM   2553 C  CG  A ASP A 1 309 ? 1.65731   11.21654 -29.86298 0.400 44.31311  ? 512  ASP A CG  1 
ATOM   2554 C  CG  B ASP A 1 309 ? 2.49180   10.73620 -28.40110 0.600 43.77308  ? 512  ASP A CG  1 
ATOM   2555 O  OD1 A ASP A 1 309 ? 1.41634   12.11333 -30.70215 0.400 47.88008  ? 512  ASP A OD1 1 
ATOM   2556 O  OD1 B ASP A 1 309 ? 3.15350   10.75309 -27.34909 0.600 44.65900  ? 512  ASP A OD1 1 
ATOM   2557 O  OD2 A ASP A 1 309 ? 1.27502   10.03475 -30.00125 0.400 42.09267  ? 512  ASP A OD2 1 
ATOM   2558 O  OD2 B ASP A 1 309 ? 1.81794   9.75156  -28.77291 0.600 47.07922  ? 512  ASP A OD2 1 
ATOM   2559 N  N   . VAL A 1 310 ? 1.32686   13.48799 -26.29850 1.000 37.12930  ? 513  VAL A N   1 
ATOM   2560 C  CA  . VAL A 1 310 ? 0.14573   13.77517 -25.48855 1.000 40.99069  ? 513  VAL A CA  1 
ATOM   2561 C  C   . VAL A 1 310 ? -0.06431  15.27590 -25.32403 1.000 41.84529  ? 513  VAL A C   1 
ATOM   2562 O  O   . VAL A 1 310 ? -1.20365  15.74912 -25.28978 1.000 43.19474  ? 513  VAL A O   1 
ATOM   2563 C  CB  . VAL A 1 310 ? 0.24130   13.08524 -24.11278 1.000 36.63121  ? 513  VAL A CB  1 
ATOM   2564 C  CG1 . VAL A 1 310 ? -1.00588  13.38862 -23.27894 1.000 38.32757  ? 513  VAL A CG1 1 
ATOM   2565 C  CG2 . VAL A 1 310 ? 0.44554   11.57748 -24.25862 1.000 35.47417  ? 513  VAL A CG2 1 
ATOM   2566 N  N   A PHE A 1 311 ? 1.01676   16.05134 -25.23601 0.501 41.40794  ? 514  PHE A N   1 
ATOM   2567 N  N   B PHE A 1 311 ? 1.01425   16.05460 -25.23570 0.499 41.41079  ? 514  PHE A N   1 
ATOM   2568 C  CA  A PHE A 1 311 ? 0.90272   17.45552 -24.86967 0.501 38.76678  ? 514  PHE A CA  1 
ATOM   2569 C  CA  B PHE A 1 311 ? 0.89873   17.45859 -24.87073 0.499 38.76772  ? 514  PHE A CA  1 
ATOM   2570 C  C   A PHE A 1 311 ? 1.33280   18.43325 -25.95479 0.501 46.08742  ? 514  PHE A C   1 
ATOM   2571 C  C   B PHE A 1 311 ? 1.33034   18.43452 -25.95651 0.499 46.08760  ? 514  PHE A C   1 
ATOM   2572 O  O   A PHE A 1 311 ? 1.12710   19.64084 -25.78449 0.501 49.65227  ? 514  PHE A O   1 
ATOM   2573 O  O   B PHE A 1 311 ? 1.12399   19.64214 -25.78836 0.499 49.65202  ? 514  PHE A O   1 
ATOM   2574 C  CB  A PHE A 1 311 ? 1.69926   17.71117 -23.58823 0.501 38.54646  ? 514  PHE A CB  1 
ATOM   2575 C  CB  B PHE A 1 311 ? 1.69380   17.71625 -23.58878 0.499 38.54868  ? 514  PHE A CB  1 
ATOM   2576 C  CG  A PHE A 1 311 ? 1.17200   16.94638 -22.41663 0.501 36.23184  ? 514  PHE A CG  1 
ATOM   2577 C  CG  B PHE A 1 311 ? 1.16858   16.94934 -22.41758 0.499 36.23242  ? 514  PHE A CG  1 
ATOM   2578 C  CD1 A PHE A 1 311 ? 0.05286   17.39912 -21.73428 0.501 35.88188  ? 514  PHE A CD1 1 
ATOM   2579 C  CD1 B PHE A 1 311 ? 0.04962   17.39944 -21.73356 0.499 35.88112  ? 514  PHE A CD1 1 
ATOM   2580 C  CD2 A PHE A 1 311 ? 1.75636   15.75269 -22.02531 0.501 34.28888  ? 514  PHE A CD2 1 
ATOM   2581 C  CD2 B PHE A 1 311 ? 1.75531   15.75584 -22.02814 0.499 34.28820  ? 514  PHE A CD2 1 
ATOM   2582 C  CE1 A PHE A 1 311 ? -0.45884  16.69231 -20.65949 0.501 32.52057  ? 514  PHE A CE1 1 
ATOM   2583 C  CE1 B PHE A 1 311 ? -0.46011  16.69066 -20.65907 0.499 32.52113  ? 514  PHE A CE1 1 
ATOM   2584 C  CE2 A PHE A 1 311 ? 1.25212   15.03609 -20.95001 0.501 33.42634  ? 514  PHE A CE2 1 
ATOM   2585 C  CE2 B PHE A 1 311 ? 1.25299   15.03725 -20.95302 0.499 33.42624  ? 514  PHE A CE2 1 
ATOM   2586 C  CZ  A PHE A 1 311 ? 0.14062   15.50696 -20.26516 0.501 33.34453  ? 514  PHE A CZ  1 
ATOM   2587 C  CZ  B PHE A 1 311 ? 0.14143   15.50572 -20.26667 0.499 33.34479  ? 514  PHE A CZ  1 
ATOM   2588 N  N   . ALA A 1 312 ? 1.89946   17.95765 -27.06147 1.000 47.59599  ? 515  ALA A N   1 
ATOM   2589 C  CA  . ALA A 1 312 ? 2.25556   18.85239 -28.15155 1.000 49.98521  ? 515  ALA A CA  1 
ATOM   2590 C  C   . ALA A 1 312 ? 0.99657   19.49731 -28.71849 1.000 61.69978  ? 515  ALA A C   1 
ATOM   2591 O  O   . ALA A 1 312 ? 0.01003   18.81071 -29.00723 1.000 62.88946  ? 515  ALA A O   1 
ATOM   2592 C  CB  . ALA A 1 312 ? 2.99972   18.09570 -29.25474 1.000 50.32151  ? 515  ALA A CB  1 
ATOM   2593 N  N   . HIS A 1 313 ? 1.02820   20.82319 -28.85439 1.000 54.49163  ? 516  HIS A N   1 
ATOM   2594 C  CA  . HIS A 1 313 ? -0.02977  21.62755 -29.46508 1.000 56.62538  ? 516  HIS A CA  1 
ATOM   2595 C  C   . HIS A 1 313 ? -1.29387  21.68190 -28.61799 1.000 51.68722  ? 516  HIS A C   1 
ATOM   2596 O  O   . HIS A 1 313 ? -2.35493  22.07802 -29.11826 1.000 54.19331  ? 516  HIS A O   1 
ATOM   2597 C  CB  . HIS A 1 313 ? -0.38266  21.13474 -30.87514 1.000 56.43469  ? 516  HIS A CB  1 
ATOM   2598 C  CG  . HIS A 1 313 ? 0.81175   20.84187 -31.72975 1.000 67.01325  ? 516  HIS A CG  1 
ATOM   2599 N  ND1 . HIS A 1 313 ? 1.50788   21.82609 -32.39692 1.000 62.22657  ? 516  HIS A ND1 1 
ATOM   2600 C  CD2 . HIS A 1 313 ? 1.43448   19.67517 -32.02412 1.000 59.21316  ? 516  HIS A CD2 1 
ATOM   2601 C  CE1 . HIS A 1 313 ? 2.50325   21.27878 -33.07147 1.000 65.58813  ? 516  HIS A CE1 1 
ATOM   2602 N  NE2 . HIS A 1 313 ? 2.48469   19.97532 -32.85685 1.000 69.07874  ? 516  HIS A NE2 1 
ATOM   2603 N  N   . ASP A 1 314 ? -1.20990  21.31238 -27.34550 1.000 48.77054  ? 517  ASP A N   1 
ATOM   2604 C  CA  . ASP A 1 314 ? -2.33821  21.33308 -26.43348 1.000 48.19749  ? 517  ASP A CA  1 
ATOM   2605 C  C   . ASP A 1 314 ? -1.91949  22.10494 -25.18782 1.000 54.05834  ? 517  ASP A C   1 
ATOM   2606 O  O   . ASP A 1 314 ? -0.80578  22.63147 -25.10396 1.000 46.34615  ? 517  ASP A O   1 
ATOM   2607 C  CB  . ASP A 1 314 ? -2.78779  19.90315 -26.09234 1.000 59.65610  ? 517  ASP A CB  1 
ATOM   2608 C  CG  . ASP A 1 314 ? -4.25820  19.81726 -25.72082 1.000 60.64801  ? 517  ASP A CG  1 
ATOM   2609 O  OD1 . ASP A 1 314 ? -4.88887  20.87401 -25.50000 1.000 59.16956  ? 517  ASP A OD1 1 
ATOM   2610 O  OD2 . ASP A 1 314 ? -4.78568  18.68580 -25.65851 1.000 63.73410  ? 517  ASP A OD2 1 
ATOM   2611 N  N   . THR A 1 315 ? -2.82087  22.17023 -24.21569 1.000 45.97414  ? 518  THR A N   1 
ATOM   2612 C  CA  . THR A 1 315 ? -2.50829  22.82091 -22.94992 1.000 49.24877  ? 518  THR A CA  1 
ATOM   2613 C  C   . THR A 1 315 ? -1.29391  22.17493 -22.28960 1.000 52.27330  ? 518  THR A C   1 
ATOM   2614 O  O   . THR A 1 315 ? -1.22445  20.94984 -22.13570 1.000 39.96038  ? 518  THR A O   1 
ATOM   2615 C  CB  . THR A 1 315 ? -3.72673  22.75480 -22.02359 1.000 47.49683  ? 518  THR A CB  1 
ATOM   2616 O  OG1 . THR A 1 315 ? -4.84323  23.39236 -22.66256 1.000 51.18814  ? 518  THR A OG1 1 
ATOM   2617 C  CG2 . THR A 1 315 ? -3.44162  23.44009 -20.69602 1.000 46.23160  ? 518  THR A CG2 1 
ATOM   2618 N  N   . SER A 1 316 ? -0.32181  22.99797 -21.90932 1.000 41.35326  ? 519  SER A N   1 
ATOM   2619 C  CA  . SER A 1 316 ? 0.74778   22.47808 -21.07340 1.000 38.68830  ? 519  SER A CA  1 
ATOM   2620 C  C   . SER A 1 316 ? 0.21276   22.22935 -19.66993 1.000 39.50651  ? 519  SER A C   1 
ATOM   2621 O  O   . SER A 1 316 ? -0.55450  23.04281 -19.14546 1.000 40.02562  ? 519  SER A O   1 
ATOM   2622 C  CB  . SER A 1 316 ? 1.92633   23.45102 -20.99647 1.000 47.01155  ? 519  SER A CB  1 
ATOM   2623 O  OG  . SER A 1 316 ? 2.88085   22.99165 -20.04784 1.000 43.33991  ? 519  SER A OG  1 
ATOM   2624 N  N   . PRO A 1 317 ? 0.58368   21.11526 -19.04023 1.000 34.58109  ? 520  PRO A N   1 
ATOM   2625 C  CA  . PRO A 1 317 ? 0.22309   20.91276 -17.63619 1.000 34.91247  ? 520  PRO A CA  1 
ATOM   2626 C  C   . PRO A 1 317 ? 1.13370   21.64455 -16.66448 1.000 33.22874  ? 520  PRO A C   1 
ATOM   2627 O  O   . PRO A 1 317 ? 0.94476   21.51240 -15.45182 1.000 32.39903  ? 520  PRO A O   1 
ATOM   2628 C  CB  . PRO A 1 317 ? 0.35549   19.39371 -17.47646 1.000 34.54712  ? 520  PRO A CB  1 
ATOM   2629 C  CG  . PRO A 1 317 ? 1.51148   19.08132 -18.33460 1.000 33.87954  ? 520  PRO A CG  1 
ATOM   2630 C  CD  . PRO A 1 317 ? 1.35497   19.97396 -19.56267 1.000 36.28369  ? 520  PRO A CD  1 
ATOM   2631 N  N   . ILE A 1 318 ? 2.10749   22.40347 -17.15773 1.000 35.39481  ? 521  ILE A N   1 
ATOM   2632 C  CA  . ILE A 1 318 ? 3.05366   23.13854 -16.32287 1.000 33.34211  ? 521  ILE A CA  1 
ATOM   2633 C  C   . ILE A 1 318 ? 2.66133   24.61235 -16.32347 1.000 34.32658  ? 521  ILE A C   1 
ATOM   2634 O  O   . ILE A 1 318 ? 2.42327   25.19696 -17.39039 1.000 36.59814  ? 521  ILE A O   1 
ATOM   2635 C  CB  . ILE A 1 318 ? 4.48910   22.95543 -16.84427 1.000 36.20431  ? 521  ILE A CB  1 
ATOM   2636 C  CG1 . ILE A 1 318 ? 4.86973   21.46906 -16.87809 1.000 32.46486  ? 521  ILE A CG1 1 
ATOM   2637 C  CG2 . ILE A 1 318 ? 5.47225   23.77704 -16.02557 1.000 37.88518  ? 521  ILE A CG2 1 
ATOM   2638 C  CD1 . ILE A 1 318 ? 6.02628   21.18592 -17.81483 1.000 34.23500  ? 521  ILE A CD1 1 
ATOM   2639 N  N   . ASN A 1 319 ? 2.59797   25.22637 -15.13820 1.000 34.04300  ? 522  ASN A N   1 
ATOM   2640 C  CA  . ASN A 1 319 ? 2.37933   26.66528 -15.06297 1.000 38.03284  ? 522  ASN A CA  1 
ATOM   2641 C  C   . ASN A 1 319 ? 3.36873   27.29567 -14.09052 1.000 35.48265  ? 522  ASN A C   1 
ATOM   2642 O  O   . ASN A 1 319 ? 3.91516   26.63526 -13.20392 1.000 34.53420  ? 522  ASN A O   1 
ATOM   2643 C  CB  . ASN A 1 319 ? 0.94128   27.02270 -14.64996 1.000 45.75722  ? 522  ASN A CB  1 
ATOM   2644 C  CG  . ASN A 1 319 ? 0.56402   28.46113 -15.03901 1.000 51.43220  ? 522  ASN A CG  1 
ATOM   2645 O  OD1 . ASN A 1 319 ? 1.13000   29.03047 -15.97590 1.000 50.63879  ? 522  ASN A OD1 1 
ATOM   2646 N  ND2 . ASN A 1 319 ? -0.39334  29.04431 -14.32317 1.000 51.35398  ? 522  ASN A ND2 1 
ATOM   2647 N  N   . ILE A 1 320 ? 3.59333   28.59299 -14.29637 1.000 37.76058  ? 523  ILE A N   1 
ATOM   2648 C  CA  . ILE A 1 320 ? 4.46587   29.43176 -13.48534 1.000 39.90237  ? 523  ILE A CA  1 
ATOM   2649 C  C   . ILE A 1 320 ? 3.67054   30.67632 -13.11200 1.000 40.56402  ? 523  ILE A C   1 
ATOM   2650 O  O   . ILE A 1 320 ? 3.14105   31.36409 -13.99543 1.000 42.44633  ? 523  ILE A O   1 
ATOM   2651 C  CB  . ILE A 1 320 ? 5.75382   29.83241 -14.23977 1.000 44.89810  ? 523  ILE A CB  1 
ATOM   2652 C  CG1 . ILE A 1 320 ? 6.53767   28.60407 -14.71814 1.000 48.62212  ? 523  ILE A CG1 1 
ATOM   2653 C  CG2 . ILE A 1 320 ? 6.63743   30.71083 -13.37244 1.000 47.06584  ? 523  ILE A CG2 1 
ATOM   2654 C  CD1 . ILE A 1 320 ? 6.22375   28.18249 -16.12936 1.000 42.34027  ? 523  ILE A CD1 1 
ATOM   2655 N  N   . GLU A 1 321 ? 3.56448   30.95986 -11.81025 1.000 40.04520  ? 524  GLU A N   1 
ATOM   2656 C  CA  . GLU A 1 321 ? 2.89310   32.17530 -11.36738 1.000 44.96452  ? 524  GLU A CA  1 
ATOM   2657 C  C   . GLU A 1 321 ? 3.68780   32.80586 -10.23745 1.000 40.87958  ? 524  GLU A C   1 
ATOM   2658 O  O   . GLU A 1 321 ? 4.40371   32.11603 -9.50527  1.000 41.32262  ? 524  GLU A O   1 
ATOM   2659 C  CB  . GLU A 1 321 ? 1.45085   31.91292 -10.91100 1.000 45.41924  ? 524  GLU A CB  1 
ATOM   2660 C  CG  . GLU A 1 321 ? 0.56269   31.30048 -11.97842 1.000 47.89392  ? 524  GLU A CG  1 
ATOM   2661 C  CD  . GLU A 1 321 ? -0.88600  31.16764 -11.54110 1.000 61.09392  ? 524  GLU A CD  1 
ATOM   2662 O  OE1 . GLU A 1 321 ? -1.54827  32.20890 -11.33552 1.000 62.04389  ? 524  GLU A OE1 1 
ATOM   2663 O  OE2 . GLU A 1 321 ? -1.35964  30.01945 -11.39526 1.000 64.22776  ? 524  GLU A OE2 1 
ATOM   2664 N  N   . ARG A 1 322 ? 3.56432   34.12759 -10.11591 1.000 43.36829  ? 525  ARG A N   1 
ATOM   2665 C  CA  . ARG A 1 322 ? 4.22206   34.87430 -9.05736  1.000 44.80427  ? 525  ARG A CA  1 
ATOM   2666 C  C   . ARG A 1 322 ? 3.19205   35.37775 -8.05601  1.000 43.94018  ? 525  ARG A C   1 
ATOM   2667 O  O   . ARG A 1 322 ? 2.00052   35.48623 -8.35540  1.000 48.27064  ? 525  ARG A O   1 
ATOM   2668 C  CB  . ARG A 1 322 ? 5.02904   36.04322 -9.62911  1.000 49.62681  ? 525  ARG A CB  1 
ATOM   2669 C  CG  . ARG A 1 322 ? 6.24736   35.60890 -10.42078 1.000 49.18238  ? 525  ARG A CG  1 
ATOM   2670 C  CD  . ARG A 1 322 ? 7.20572   36.75984 -10.68186 1.000 59.20536  ? 525  ARG A CD  1 
ATOM   2671 N  NE  . ARG A 1 322 ? 7.78685   37.33033 -9.46736  1.000 60.30649  ? 525  ARG A NE  1 
ATOM   2672 C  CZ  . ARG A 1 322 ? 7.37532   38.45338 -8.88833  1.000 67.76004  ? 525  ARG A CZ  1 
ATOM   2673 N  NH1 . ARG A 1 322 ? 6.33511   39.13095 -9.35007  1.000 59.38827  ? 525  ARG A NH1 1 
ATOM   2674 N  NH2 . ARG A 1 322 ? 8.02578   38.91101 -7.81989  1.000 67.48448  ? 525  ARG A NH2 1 
ATOM   2675 N  N   . CYS A 1 323 ? 3.66597   35.68312 -6.84877  1.000 46.85154  ? 526  CYS A N   1 
ATOM   2676 C  CA  . CYS A 1 323 ? 2.80876   36.25681 -5.82352  1.000 43.82215  ? 526  CYS A CA  1 
ATOM   2677 C  C   . CYS A 1 323 ? 3.60070   37.27331 -5.01850  1.000 47.94700  ? 526  CYS A C   1 
ATOM   2678 O  O   . CYS A 1 323 ? 4.71514   36.98684 -4.57251  1.000 46.00722  ? 526  CYS A O   1 
ATOM   2679 C  CB  . CYS A 1 323 ? 2.23134   35.17355 -4.90841  1.000 40.98357  ? 526  CYS A CB  1 
ATOM   2680 S  SG  . CYS A 1 323 ? 3.43575   33.95693 -4.29654  1.000 42.20564  ? 526  CYS A SG  1 
ATOM   2681 N  N   . GLU A 1 324 ? 3.02117   38.45874 -4.83841  1.000 47.70192  ? 527  GLU A N   1 
ATOM   2682 C  CA  . GLU A 1 324 ? 3.65614   39.53072 -4.08879  1.000 49.43527  ? 527  GLU A CA  1 
ATOM   2683 C  C   . GLU A 1 324 ? 2.85600   39.98997 -2.88057  1.000 51.62044  ? 527  GLU A C   1 
ATOM   2684 O  O   . GLU A 1 324 ? 3.34794   40.83410 -2.12117  1.000 57.69477  ? 527  GLU A O   1 
ATOM   2685 C  CB  . GLU A 1 324 ? 3.92071   40.73805 -5.00599  1.000 53.01761  ? 527  GLU A CB  1 
ATOM   2686 C  CG  . GLU A 1 324 ? 4.93440   40.43943 -6.08760  1.000 56.45462  ? 527  GLU A CG  1 
ATOM   2687 C  CD  . GLU A 1 324 ? 5.15611   41.59918 -7.03155  1.000 58.35743  ? 527  GLU A CD  1 
ATOM   2688 O  OE1 . GLU A 1 324 ? 4.55508   42.68095 -6.82225  1.000 65.18038  ? 527  GLU A OE1 1 
ATOM   2689 O  OE2 . GLU A 1 324 ? 5.93830   41.42564 -7.98986  1.000 72.72799  ? 527  GLU A OE2 1 
ATOM   2690 N  N   . THR A 1 325 ? 1.64457   39.47836 -2.68484  1.000 48.82339  ? 528  THR A N   1 
ATOM   2691 C  CA  . THR A 1 325 ? 0.81144   39.83143 -1.54634  1.000 53.58047  ? 528  THR A CA  1 
ATOM   2692 C  C   . THR A 1 325 ? 0.29730   38.56002 -0.88551  1.000 53.48146  ? 528  THR A C   1 
ATOM   2693 O  O   . THR A 1 325 ? 0.35307   37.46765 -1.45819  1.000 49.22112  ? 528  THR A O   1 
ATOM   2694 C  CB  . THR A 1 325 ? -0.37663  40.71481 -1.95987  1.000 58.91798  ? 528  THR A CB  1 
ATOM   2695 O  OG1 . THR A 1 325 ? -1.36031  39.91253 -2.62669  1.000 51.00313  ? 528  THR A OG1 1 
ATOM   2696 C  CG2 . THR A 1 325 ? 0.08007   41.82278 -2.90503  1.000 58.23989  ? 528  THR A CG2 1 
ATOM   2697 N  N   . LYS A 1 326 ? -0.20025  38.71385 0.34143   1.000 50.01380  ? 529  LYS A N   1 
ATOM   2698 C  CA  . LYS A 1 326 ? -0.83601  37.59487 1.02905   1.000 48.94252  ? 529  LYS A CA  1 
ATOM   2699 C  C   . LYS A 1 326 ? -2.00845  37.06341 0.21387   1.000 48.05345  ? 529  LYS A C   1 
ATOM   2700 O  O   . LYS A 1 326 ? -2.15517  35.84833 0.03376   1.000 45.88256  ? 529  LYS A O   1 
ATOM   2701 C  CB  . LYS A 1 326 ? -1.28152  38.03482 2.42644   1.000 48.98823  ? 529  LYS A CB  1 
ATOM   2702 C  CG  . LYS A 1 326 ? -2.12126  37.04953 3.20450   1.000 42.02844  ? 529  LYS A CG  1 
ATOM   2703 C  CD  . LYS A 1 326 ? -2.35164  37.58844 4.63229   1.000 42.19111  ? 529  LYS A CD  1 
ATOM   2704 C  CE  . LYS A 1 326 ? -2.99188  36.55579 5.52872   1.000 42.04566  ? 529  LYS A CE  1 
ATOM   2705 N  NZ  . LYS A 1 326 ? -4.33875  36.16578 5.03891   1.000 43.28690  ? 529  LYS A NZ  1 
ATOM   2706 N  N   . LYS A 1 327 ? -2.83428  37.97103 -0.31727  1.000 48.42667  ? 530  LYS A N   1 
ATOM   2707 C  CA  . LYS A 1 327 ? -3.99131  37.55998 -1.10549  1.000 55.06008  ? 530  LYS A CA  1 
ATOM   2708 C  C   . LYS A 1 327 ? -3.56740  36.76478 -2.33569  1.000 50.68279  ? 530  LYS A C   1 
ATOM   2709 O  O   . LYS A 1 327 ? -4.14750  35.71492 -2.63694  1.000 46.72101  ? 530  LYS A O   1 
ATOM   2710 C  CB  . LYS A 1 327 ? -4.81323  38.78605 -1.50907  1.000 51.40298  ? 530  LYS A CB  1 
ATOM   2711 N  N   . GLU A 1 328 ? -2.55611  37.25397 -3.06453  1.000 47.27460  ? 531  GLU A N   1 
ATOM   2712 C  CA  . GLU A 1 328 ? -2.05602  36.51225 -4.22036  1.000 44.78846  ? 531  GLU A CA  1 
ATOM   2713 C  C   . GLU A 1 328 ? -1.51421  35.14163 -3.81648  1.000 42.61534  ? 531  GLU A C   1 
ATOM   2714 O  O   . GLU A 1 328 ? -1.74869  34.14774 -4.51281  1.000 40.18974  ? 531  GLU A O   1 
ATOM   2715 C  CB  . GLU A 1 328 ? -0.97208  37.31246 -4.94603  1.000 46.53877  ? 531  GLU A CB  1 
ATOM   2716 C  CG  . GLU A 1 328 ? -1.43243  38.67475 -5.48759  1.000 50.23859  ? 531  GLU A CG  1 
ATOM   2717 C  CD  . GLU A 1 328 ? -0.38302  39.35130 -6.34470  1.000 54.83093  ? 531  GLU A CD  1 
ATOM   2718 O  OE1 . GLU A 1 328 ? 0.81249   39.01111 -6.22839  1.000 50.74073  ? 531  GLU A OE1 1 
ATOM   2719 O  OE2 . GLU A 1 328 ? -0.75701  40.23525 -7.14319  1.000 58.07954  ? 531  GLU A OE2 1 
ATOM   2720 N  N   . PHE A 1 329 ? -0.78259  35.06552 -2.70197  1.000 40.36845  ? 532  PHE A N   1 
ATOM   2721 C  CA  . PHE A 1 329 ? -0.19251  33.78759 -2.30630  1.000 37.51950  ? 532  PHE A CA  1 
ATOM   2722 C  C   . PHE A 1 329 ? -1.27078  32.77661 -1.93554  1.000 36.87196  ? 532  PHE A C   1 
ATOM   2723 O  O   . PHE A 1 329 ? -1.22228  31.61920 -2.36665  1.000 36.74587  ? 532  PHE A O   1 
ATOM   2724 C  CB  . PHE A 1 329 ? 0.78945   33.99002 -1.14725  1.000 40.77319  ? 532  PHE A CB  1 
ATOM   2725 C  CG  . PHE A 1 329 ? 1.19306   32.71819 -0.46065  1.000 37.32493  ? 532  PHE A CG  1 
ATOM   2726 C  CD1 . PHE A 1 329 ? 2.02672   31.80285 -1.08962  1.000 35.70635  ? 532  PHE A CD1 1 
ATOM   2727 C  CD2 . PHE A 1 329 ? 0.75043   32.43816 0.81852   1.000 38.09506  ? 532  PHE A CD2 1 
ATOM   2728 C  CE1 . PHE A 1 329 ? 2.40279   30.61616 -0.46091  1.000 34.46877  ? 532  PHE A CE1 1 
ATOM   2729 C  CE2 . PHE A 1 329 ? 1.12084   31.26842 1.46191   1.000 36.72073  ? 532  PHE A CE2 1 
ATOM   2730 C  CZ  . PHE A 1 329 ? 1.95261   30.34275 0.82213   1.000 36.78054  ? 532  PHE A CZ  1 
ATOM   2731 N  N   A GLU A 1 330 ? -2.26766  33.19711 -1.15207  0.638 38.23427  ? 533  GLU A N   1 
ATOM   2732 N  N   B GLU A 1 330 ? -2.25764  33.19982 -1.14046  0.362 38.35336  ? 533  GLU A N   1 
ATOM   2733 C  CA  A GLU A 1 330 ? -3.27731  32.24849 -0.69419  0.638 40.34133  ? 533  GLU A CA  1 
ATOM   2734 C  CA  B GLU A 1 330 ? -3.28631  32.26924 -0.68868  0.362 40.31711  ? 533  GLU A CA  1 
ATOM   2735 C  C   A GLU A 1 330 ? -4.21189  31.82560 -1.82574  0.638 39.14302  ? 533  GLU A C   1 
ATOM   2736 C  C   B GLU A 1 330 ? -4.18085  31.82116 -1.83960  0.362 39.22069  ? 533  GLU A C   1 
ATOM   2737 O  O   A GLU A 1 330 ? -4.63146  30.66420 -1.88325  0.638 38.41932  ? 533  GLU A O   1 
ATOM   2738 O  O   B GLU A 1 330 ? -4.54825  30.64320 -1.91901  0.362 38.45806  ? 533  GLU A O   1 
ATOM   2739 C  CB  A GLU A 1 330 ? -4.04501  32.83652 0.49536   0.638 41.15249  ? 533  GLU A CB  1 
ATOM   2740 C  CB  B GLU A 1 330 ? -4.10896  32.90045 0.43738   0.362 41.17007  ? 533  GLU A CB  1 
ATOM   2741 C  CG  A GLU A 1 330 ? -3.25921  32.68987 1.80251   0.638 40.82477  ? 533  GLU A CG  1 
ATOM   2742 C  CG  B GLU A 1 330 ? -4.80148  34.19336 0.06061   0.362 38.89958  ? 533  GLU A CG  1 
ATOM   2743 C  CD  A GLU A 1 330 ? -3.79022  33.51911 2.95487   0.638 39.39031  ? 533  GLU A CD  1 
ATOM   2744 C  CD  B GLU A 1 330 ? -5.11522  35.06548 1.26008   0.362 40.00338  ? 533  GLU A CD  1 
ATOM   2745 O  OE1 A GLU A 1 330 ? -4.70936  34.33927 2.73623   0.638 40.35270  ? 533  GLU A OE1 1 
ATOM   2746 O  OE1 B GLU A 1 330 ? -4.36148  35.01364 2.25678   0.362 38.86137  ? 533  GLU A OE1 1 
ATOM   2747 O  OE2 A GLU A 1 330 ? -3.26276  33.36055 4.07874   0.638 34.52213  ? 533  GLU A OE2 1 
ATOM   2748 O  OE2 B GLU A 1 330 ? -6.11932  35.80403 1.20519   0.362 42.17348  ? 533  GLU A OE2 1 
ATOM   2749 N  N   . GLN A 1 331 ? -4.53989  32.73435 -2.74595  1.000 39.90431  ? 534  GLN A N   1 
ATOM   2750 C  CA  . GLN A 1 331 ? -5.36156  32.32698 -3.88308  1.000 42.06392  ? 534  GLN A CA  1 
ATOM   2751 C  C   . GLN A 1 331 ? -4.61006  31.34151 -4.77150  1.000 40.60047  ? 534  GLN A C   1 
ATOM   2752 O  O   . GLN A 1 331 ? -5.18383  30.35444 -5.24776  1.000 40.00731  ? 534  GLN A O   1 
ATOM   2753 C  CB  . GLN A 1 331 ? -5.82550  33.55466 -4.67281  1.000 43.02894  ? 534  GLN A CB  1 
ATOM   2754 C  CG  . GLN A 1 331 ? -7.28068  33.90007 -4.38559  1.000 59.52704  ? 534  GLN A CG  1 
ATOM   2755 C  CD  . GLN A 1 331 ? -7.66654  35.29840 -4.81967  1.000 68.86692  ? 534  GLN A CD  1 
ATOM   2756 O  OE1 . GLN A 1 331 ? -7.24235  35.77950 -5.87169  1.000 66.09733  ? 534  GLN A OE1 1 
ATOM   2757 N  NE2 . GLN A 1 331 ? -8.47386  35.96395 -4.00214  1.000 67.55907  ? 534  GLN A NE2 1 
ATOM   2758 N  N   . LEU A 1 332 ? -3.30754  31.55218 -4.94560  1.000 38.09080  ? 535  LEU A N   1 
ATOM   2759 C  CA  . LEU A 1 332 ? -2.51169  30.64705 -5.76317  1.000 37.62555  ? 535  LEU A CA  1 
ATOM   2760 C  C   . LEU A 1 332 ? -2.37649  29.27939 -5.09788  1.000 38.78123  ? 535  LEU A C   1 
ATOM   2761 O  O   . LEU A 1 332 ? -2.53582  28.24174 -5.75014  1.000 37.42181  ? 535  LEU A O   1 
ATOM   2762 C  CB  . LEU A 1 332 ? -1.14856  31.28282 -6.02421  1.000 39.61340  ? 535  LEU A CB  1 
ATOM   2763 C  CG  . LEU A 1 332 ? -0.09521  30.62258 -6.89790  1.000 48.05462  ? 535  LEU A CG  1 
ATOM   2764 C  CD1 . LEU A 1 332 ? -0.71442  30.14153 -8.20346  1.000 51.67550  ? 535  LEU A CD1 1 
ATOM   2765 C  CD2 . LEU A 1 332 ? 1.00279   31.64277 -7.17203  1.000 51.33475  ? 535  LEU A CD2 1 
ATOM   2766 N  N   . MET A 1 333 ? -2.10800  29.25800 -3.78923  1.000 34.37531  ? 536  MET A N   1 
ATOM   2767 C  CA  . MET A 1 333 ? -1.98844  27.99195 -3.06962  1.000 34.21011  ? 536  MET A CA  1 
ATOM   2768 C  C   . MET A 1 333 ? -3.30376  27.22733 -3.07206  1.000 30.91803  ? 536  MET A C   1 
ATOM   2769 O  O   . MET A 1 333 ? -3.33369  26.01545 -3.32107  1.000 32.14272  ? 536  MET A O   1 
ATOM   2770 C  CB  . MET A 1 333 ? -1.54314  28.24942 -1.63539  1.000 34.48153  ? 536  MET A CB  1 
ATOM   2771 C  CG  . MET A 1 333 ? -0.08796  28.57909 -1.48786  1.000 41.00752  ? 536  MET A CG  1 
ATOM   2772 S  SD  . MET A 1 333 ? 0.97424   27.15951 -1.76193  1.000 39.42900  ? 536  MET A SD  1 
ATOM   2773 C  CE  . MET A 1 333 ? 0.08078   25.87002 -0.89511  1.000 42.30078  ? 536  MET A CE  1 
ATOM   2774 N  N   . ASN A 1 334 ? -4.40298  27.92397 -2.78110  1.000 31.11257  ? 537  ASN A N   1 
ATOM   2775 C  CA  . ASN A 1 334 ? -5.70847  27.27973 -2.73105  1.000 31.99386  ? 537  ASN A CA  1 
ATOM   2776 C  C   . ASN A 1 334 ? -6.11674  26.77454 -4.10715  1.000 34.71192  ? 537  ASN A C   1 
ATOM   2777 O  O   . ASN A 1 334 ? -6.58846  25.64165 -4.24481  1.000 37.71134  ? 537  ASN A O   1 
ATOM   2778 C  CB  . ASN A 1 334 ? -6.75277  28.25256 -2.18389  1.000 38.76410  ? 537  ASN A CB  1 
ATOM   2779 C  CG  . ASN A 1 334 ? -6.65149  28.41204 -0.68352  1.000 37.16954  ? 537  ASN A CG  1 
ATOM   2780 O  OD1 . ASN A 1 334 ? -6.31257  27.46177 0.01662   1.000 38.70288  ? 537  ASN A OD1 1 
ATOM   2781 N  ND2 . ASN A 1 334 ? -6.93239  29.61884 -0.18559  1.000 39.81259  ? 537  ASN A ND2 1 
ATOM   2782 N  N   . LYS A 1 335 ? -5.95168  27.60597 -5.13707  1.000 36.52787  ? 538  LYS A N   1 
ATOM   2783 C  CA  . LYS A 1 335 ? -6.25722  27.14744 -6.49316  1.000 33.84678  ? 538  LYS A CA  1 
ATOM   2784 C  C   . LYS A 1 335 ? -5.44914  25.90252 -6.84117  1.000 36.36862  ? 538  LYS A C   1 
ATOM   2785 O  O   . LYS A 1 335 ? -5.96769  24.95681 -7.44977  1.000 35.25289  ? 538  LYS A O   1 
ATOM   2786 C  CB  . LYS A 1 335 ? -5.97996  28.25989 -7.50329  1.000 35.90634  ? 538  LYS A CB  1 
ATOM   2787 C  CG  . LYS A 1 335 ? -6.34149  27.90648 -8.93637  1.000 44.40460  ? 538  LYS A CG  1 
ATOM   2788 C  CD  . LYS A 1 335 ? -6.11467  29.08177 -9.88414  1.000 49.64817  ? 538  LYS A CD  1 
ATOM   2789 C  CE  . LYS A 1 335 ? -4.63006  29.33239 -10.13091 1.000 55.24742  ? 538  LYS A CE  1 
ATOM   2790 N  NZ  . LYS A 1 335 ? -4.39180  30.32065 -11.23535 1.000 53.22727  ? 538  LYS A NZ  1 
ATOM   2791 N  N   . THR A 1 336 ? -4.17529  25.88424 -6.46545  1.000 31.07834  ? 539  THR A N   1 
ATOM   2792 C  CA  . THR A 1 336 ? -3.32693  24.74879 -6.80201  1.000 30.08827  ? 539  THR A CA  1 
ATOM   2793 C  C   . THR A 1 336 ? -3.75428  23.50287 -6.03504  1.000 32.41374  ? 539  THR A C   1 
ATOM   2794 O  O   . THR A 1 336 ? -3.89737  22.42167 -6.61535  1.000 34.34148  ? 539  THR A O   1 
ATOM   2795 C  CB  . THR A 1 336 ? -1.86592  25.09298 -6.52035  1.000 29.24014  ? 539  THR A CB  1 
ATOM   2796 O  OG1 . THR A 1 336 ? -1.49539  26.27037 -7.26045  1.000 33.90106  ? 539  THR A OG1 1 
ATOM   2797 C  CG2 . THR A 1 336 ? -0.98541  23.94996 -6.91726  1.000 32.24465  ? 539  THR A CG2 1 
ATOM   2798 N  N   . LEU A 1 337 ? -4.00028  23.64448 -4.73179  1.000 29.99006  ? 540  LEU A N   1 
ATOM   2799 C  CA  . LEU A 1 337 ? -4.38408  22.49401 -3.92134  1.000 29.77190  ? 540  LEU A CA  1 
ATOM   2800 C  C   . LEU A 1 337 ? -5.77245  21.98240 -4.29316  1.000 33.45975  ? 540  LEU A C   1 
ATOM   2801 O  O   . LEU A 1 337 ? -5.99976  20.76562 -4.34523  1.000 38.91350  ? 540  LEU A O   1 
ATOM   2802 C  CB  . LEU A 1 337 ? -4.31472  22.86679 -2.43550  1.000 27.70337  ? 540  LEU A CB  1 
ATOM   2803 C  CG  . LEU A 1 337 ? -2.88889  22.97287 -1.89320  1.000 27.97653  ? 540  LEU A CG  1 
ATOM   2804 C  CD1 . LEU A 1 337 ? -2.89620  23.70983 -0.56299  1.000 32.91447  ? 540  LEU A CD1 1 
ATOM   2805 C  CD2 . LEU A 1 337 ? -2.23326  21.60225 -1.74124  1.000 28.13916  ? 540  LEU A CD2 1 
ATOM   2806 N  N   . ASP A 1 338 ? -6.70352  22.88655 -4.58839  1.000 33.00039  ? 541  ASP A N   1 
ATOM   2807 C  CA  . ASP A 1 338 ? -8.06611  22.48294 -4.92383  1.000 36.01334  ? 541  ASP A CA  1 
ATOM   2808 C  C   . ASP A 1 338 ? -8.17953  21.88156 -6.31717  1.000 37.17800  ? 541  ASP A C   1 
ATOM   2809 O  O   . ASP A 1 338 ? -9.18100  21.22537 -6.61119  1.000 40.16672  ? 541  ASP A O   1 
ATOM   2810 C  CB  . ASP A 1 338 ? -9.02119  23.67257 -4.83443  1.000 43.45665  ? 541  ASP A CB  1 
ATOM   2811 C  CG  . ASP A 1 338 ? -9.10428  24.25939 -3.43644  1.000 48.12200  ? 541  ASP A CG  1 
ATOM   2812 O  OD1 . ASP A 1 338 ? -8.56234  23.65133 -2.48275  1.000 50.17792  ? 541  ASP A OD1 1 
ATOM   2813 O  OD2 . ASP A 1 338 ? -9.70252  25.34819 -3.30096  1.000 56.09892  ? 541  ASP A OD2 1 
ATOM   2814 N  N   . ASN A 1 339 ? -7.20678  22.11798 -7.19073  1.000 41.69930  ? 542  ASN A N   1 
ATOM   2815 C  CA  . ASN A 1 339 ? -7.23782  21.55561 -8.53415  1.000 45.32213  ? 542  ASN A CA  1 
ATOM   2816 C  C   . ASN A 1 339 ? -6.33467  20.34056 -8.66926  1.000 42.32730  ? 542  ASN A C   1 
ATOM   2817 O  O   . ASN A 1 339 ? -5.97768  19.95932 -9.79131  1.000 43.76217  ? 542  ASN A O   1 
ATOM   2818 C  CB  . ASN A 1 339 ? -6.86705  22.61604 -9.56987  1.000 42.08600  ? 542  ASN A CB  1 
ATOM   2819 C  CG  . ASN A 1 339 ? -7.98607  23.59162 -9.82443  1.000 50.29870  ? 542  ASN A CG  1 
ATOM   2820 O  OD1 . ASN A 1 339 ? -7.86128  24.78157 -9.54544  1.000 49.07435  ? 542  ASN A OD1 1 
ATOM   2821 N  ND2 . ASN A 1 339 ? -9.09502  23.09446 -10.35689 1.000 56.15085  ? 542  ASN A ND2 1 
ATOM   2822 N  N   . LYS A 1 340 ? -5.94711  19.73289 -7.54729  1.000 34.80085  ? 543  LYS A N   1 
ATOM   2823 C  CA  . LYS A 1 340 ? -5.26415  18.44726 -7.54832  1.000 43.64501  ? 543  LYS A CA  1 
ATOM   2824 C  C   . LYS A 1 340 ? -3.94759  18.51713 -8.33048  1.000 41.99457  ? 543  LYS A C   1 
ATOM   2825 O  O   . LYS A 1 340 ? -3.65795  17.67733 -9.17850  1.000 32.47505  ? 543  LYS A O   1 
ATOM   2826 C  CB  . LYS A 1 340 ? -6.19098  17.35456 -8.10271  1.000 43.16507  ? 543  LYS A CB  1 
ATOM   2827 C  CG  . LYS A 1 340 ? -7.47496  17.10918 -7.27842  1.000 42.69745  ? 543  LYS A CG  1 
ATOM   2828 C  CD  . LYS A 1 340 ? -8.64506  18.04110 -7.63783  1.000 51.01005  ? 543  LYS A CD  1 
ATOM   2829 C  CE  . LYS A 1 340 ? -9.85978  17.76691 -6.74604  1.000 48.91033  ? 543  LYS A CE  1 
ATOM   2830 N  NZ  . LYS A 1 340 ? -11.03498 18.66219 -6.98175  1.000 51.95921  ? 543  LYS A NZ  1 
ATOM   2831 N  N   . ARG A 1 341 ? -3.15444  19.55027 -8.04982  1.000 36.44436  ? 544  ARG A N   1 
ATOM   2832 C  CA  . ARG A 1 341 ? -1.86434  19.77498 -8.69086  1.000 31.59461  ? 544  ARG A CA  1 
ATOM   2833 C  C   . ARG A 1 341 ? -0.72745  19.67130 -7.68049  1.000 31.08143  ? 544  ARG A C   1 
ATOM   2834 O  O   . ARG A 1 341 ? -0.92338  19.87475 -6.47937  1.000 31.45673  ? 544  ARG A O   1 
ATOM   2835 C  CB  . ARG A 1 341 ? -1.82208  21.15899 -9.34552  1.000 30.09308  ? 544  ARG A CB  1 
ATOM   2836 C  CG  . ARG A 1 341 ? -2.81825  21.30304 -10.45161 1.000 33.62498  ? 544  ARG A CG  1 
ATOM   2837 C  CD  . ARG A 1 341 ? -3.01582  22.74793 -10.83209 1.000 33.95063  ? 544  ARG A CD  1 
ATOM   2838 N  NE  . ARG A 1 341 ? -4.04432  22.87309 -11.85970 1.000 36.48866  ? 544  ARG A NE  1 
ATOM   2839 C  CZ  . ARG A 1 341 ? -4.75481  23.96931 -12.08452 1.000 43.10451  ? 544  ARG A CZ  1 
ATOM   2840 N  NH1 . ARG A 1 341 ? -4.54511  25.08617 -11.40236 1.000 40.74515  ? 544  ARG A NH1 1 
ATOM   2841 N  NH2 . ARG A 1 341 ? -5.71177  23.94261 -13.00662 1.000 47.19220  ? 544  ARG A NH2 1 
ATOM   2842 N  N   . ALA A 1 342 ? 0.46698   19.35672 -8.18256  1.000 31.12646  ? 545  ALA A N   1 
ATOM   2843 C  CA  . ALA A 1 342 ? 1.68462   19.37376 -7.37906  1.000 28.20108  ? 545  ALA A CA  1 
ATOM   2844 C  C   . ALA A 1 342 ? 2.31453   20.76518 -7.40900  1.000 30.81384  ? 545  ALA A C   1 
ATOM   2845 O  O   . ALA A 1 342 ? 2.03964   21.57382 -8.30272  1.000 27.95464  ? 545  ALA A O   1 
ATOM   2846 C  CB  . ALA A 1 342 ? 2.69058   18.33542 -7.86733  1.000 26.97018  ? 545  ALA A CB  1 
ATOM   2847 N  N   . ILE A 1 343 ? 3.17815   21.03389 -6.42101  1.000 27.21708  ? 546  ILE A N   1 
ATOM   2848 C  CA  . ILE A 1 343 ? 3.60236   22.39367 -6.09200  1.000 25.69448  ? 546  ILE A CA  1 
ATOM   2849 C  C   . ILE A 1 343 ? 5.11737   22.46621 -5.96415  1.000 25.20215  ? 546  ILE A C   1 
ATOM   2850 O  O   . ILE A 1 343 ? 5.69949   21.84101 -5.06658  1.000 24.48424  ? 546  ILE A O   1 
ATOM   2851 C  CB  . ILE A 1 343 ? 2.96736   22.88822 -4.78128  1.000 29.65426  ? 546  ILE A CB  1 
ATOM   2852 C  CG1 . ILE A 1 343 ? 1.45313   22.69149 -4.79985  1.000 30.36265  ? 546  ILE A CG1 1 
ATOM   2853 C  CG2 . ILE A 1 343 ? 3.36470   24.34771 -4.52200  1.000 31.04648  ? 546  ILE A CG2 1 
ATOM   2854 C  CD1 . ILE A 1 343 ? 0.76633   23.17203 -3.52057  1.000 37.17332  ? 546  ILE A CD1 1 
ATOM   2855 N  N   . GLY A 1 344 ? 5.74489   23.25820 -6.82049  1.000 25.30327  ? 547  GLY A N   1 
ATOM   2856 C  CA  . GLY A 1 344 ? 7.12144   23.70467 -6.62817  1.000 25.89879  ? 547  GLY A CA  1 
ATOM   2857 C  C   . GLY A 1 344 ? 7.13780   25.16093 -6.20518  1.000 27.88600  ? 547  GLY A C   1 
ATOM   2858 O  O   . GLY A 1 344 ? 6.39402   25.98188 -6.74664  1.000 27.31349  ? 547  GLY A O   1 
ATOM   2859 N  N   . ILE A 1 345 ? 7.99177   25.49170 -5.23470  1.000 25.17860  ? 548  ILE A N   1 
ATOM   2860 C  CA  . ILE A 1 345 ? 8.13858   26.85961 -4.74491  1.000 26.96418  ? 548  ILE A CA  1 
ATOM   2861 C  C   . ILE A 1 345 ? 9.52007   27.38008 -5.12450  1.000 28.09933  ? 548  ILE A C   1 
ATOM   2862 O  O   . ILE A 1 345 ? 10.52245  26.69027 -4.92702  1.000 30.13665  ? 548  ILE A O   1 
ATOM   2863 C  CB  . ILE A 1 345 ? 7.94625   26.91086 -3.21627  1.000 29.11029  ? 548  ILE A CB  1 
ATOM   2864 C  CG1 . ILE A 1 345 ? 6.50155   26.58584 -2.83502  1.000 31.75738  ? 548  ILE A CG1 1 
ATOM   2865 C  CG2 . ILE A 1 345 ? 8.36700   28.24788 -2.65355  1.000 33.65553  ? 548  ILE A CG2 1 
ATOM   2866 C  CD1 . ILE A 1 345 ? 6.25832   26.55728 -1.33695  1.000 33.84223  ? 548  ILE A CD1 1 
ATOM   2867 N  N   A PHE A 1 346 ? 9.56585   28.59467 -5.64393  0.487 30.56318  ? 549  PHE A N   1 
ATOM   2868 N  N   B PHE A 1 346 ? 9.60096   28.59370 -5.67676  0.513 30.60666  ? 549  PHE A N   1 
ATOM   2869 C  CA  A PHE A 1 346 ? 10.81802  29.30109 -5.83612  0.487 32.36083  ? 549  PHE A CA  1 
ATOM   2870 C  CA  B PHE A 1 346 ? 10.91892  29.19782 -5.85803  0.513 32.08889  ? 549  PHE A CA  1 
ATOM   2871 C  C   A PHE A 1 346 ? 10.94258  30.27798 -4.67323  0.487 44.32715  ? 549  PHE A C   1 
ATOM   2872 C  C   B PHE A 1 346 ? 11.07796  30.31080 -4.82115  0.513 44.72303  ? 549  PHE A C   1 
ATOM   2873 O  O   A PHE A 1 346 ? 10.10997  31.17639 -4.51296  0.487 38.44942  ? 549  PHE A O   1 
ATOM   2874 O  O   B PHE A 1 346 ? 10.42045  31.35209 -4.90920  0.513 44.58314  ? 549  PHE A O   1 
ATOM   2875 C  CB  A PHE A 1 346 ? 10.84955  30.01012 -7.18708  0.487 42.80876  ? 549  PHE A CB  1 
ATOM   2876 C  CB  B PHE A 1 346 ? 11.21775  29.68422 -7.29020  0.513 42.55746  ? 549  PHE A CB  1 
ATOM   2877 C  CG  A PHE A 1 346 ? 12.05111  30.88447 -7.38686  0.487 42.48287  ? 549  PHE A CG  1 
ATOM   2878 C  CG  B PHE A 1 346 ? 10.02505  30.10508 -8.13542  0.513 42.21755  ? 549  PHE A CG  1 
ATOM   2879 C  CD1 A PHE A 1 346 ? 13.30326  30.33516 -7.62265  0.487 44.01126  ? 549  PHE A CD1 1 
ATOM   2880 C  CD1 B PHE A 1 346 ? 9.21714   29.16465 -8.76516  0.513 42.86537  ? 549  PHE A CD1 1 
ATOM   2881 C  CD2 A PHE A 1 346 ? 11.92536  32.26078 -7.35523  0.487 47.01800  ? 549  PHE A CD2 1 
ATOM   2882 C  CD2 B PHE A 1 346 ? 9.80843   31.45374 -8.41817  0.513 48.45456  ? 549  PHE A CD2 1 
ATOM   2883 C  CE1 A PHE A 1 346 ? 14.40998  31.15663 -7.81225  0.487 49.50861  ? 549  PHE A CE1 1 
ATOM   2884 C  CE1 B PHE A 1 346 ? 8.16217   29.56762 -9.59064  0.513 37.00614  ? 549  PHE A CE1 1 
ATOM   2885 C  CE2 A PHE A 1 346 ? 13.01989  33.07498 -7.54662  0.487 53.88569  ? 549  PHE A CE2 1 
ATOM   2886 C  CE2 B PHE A 1 346 ? 8.75742   31.86182 -9.24292  0.513 43.90580  ? 549  PHE A CE2 1 
ATOM   2887 C  CZ  A PHE A 1 346 ? 14.26359  32.52154 -7.77281  0.487 57.02250  ? 549  PHE A CZ  1 
ATOM   2888 C  CZ  B PHE A 1 346 ? 7.93329   30.91847 -9.82277  0.513 43.39397  ? 549  PHE A CZ  1 
ATOM   2889 N  N   . TRP A 1 347 ? 11.93744  30.05693 -3.82603  1.000 40.14282  ? 550  TRP A N   1 
ATOM   2890 C  CA  . TRP A 1 347 ? 12.21996  30.97310 -2.72933  1.000 43.38435  ? 550  TRP A CA  1 
ATOM   2891 C  C   . TRP A 1 347 ? 13.23676  32.01835 -3.15571  1.000 36.30457  ? 550  TRP A C   1 
ATOM   2892 O  O   . TRP A 1 347 ? 14.14816  31.74362 -3.93559  1.000 47.00607  ? 550  TRP A O   1 
ATOM   2893 C  CB  . TRP A 1 347 ? 12.77585  30.21355 -1.52425  1.000 40.69211  ? 550  TRP A CB  1 
ATOM   2894 C  CG  . TRP A 1 347 ? 11.74258  29.60380 -0.60830  1.000 36.97376  ? 550  TRP A CG  1 
ATOM   2895 C  CD1 . TRP A 1 347 ? 10.43452  29.97526 -0.46697  1.000 44.39331  ? 550  TRP A CD1 1 
ATOM   2896 C  CD2 . TRP A 1 347 ? 11.95151  28.52509 0.31033   1.000 37.52837  ? 550  TRP A CD2 1 
ATOM   2897 N  NE1 . TRP A 1 347 ? 9.81572   29.19020 0.48081   1.000 42.53896  ? 550  TRP A NE1 1 
ATOM   2898 C  CE2 . TRP A 1 347 ? 10.72343  28.29256 0.97295   1.000 28.09200  ? 550  TRP A CE2 1 
ATOM   2899 C  CE3 . TRP A 1 347 ? 13.05502  27.72698 0.62981   1.000 37.90006  ? 550  TRP A CE3 1 
ATOM   2900 C  CZ2 . TRP A 1 347 ? 10.57097  27.30188 1.93596   1.000 36.65893  ? 550  TRP A CZ2 1 
ATOM   2901 C  CZ3 . TRP A 1 347 ? 12.90030  26.73621 1.59253   1.000 37.09828  ? 550  TRP A CZ3 1 
ATOM   2902 C  CH2 . TRP A 1 347 ? 11.66536  26.53267 2.22996   1.000 35.64902  ? 550  TRP A CH2 1 
ATOM   2903 N  N   . GLN A 1 348 ? 13.10301  33.21771 -2.59418  1.000 41.59799  ? 551  GLN A N   1 
ATOM   2904 C  CA  . GLN A 1 348 ? 13.99705  34.30952 -2.95186  1.000 49.08278  ? 551  GLN A CA  1 
ATOM   2905 C  C   . GLN A 1 348 ? 14.19657  35.22147 -1.75062  1.000 57.32845  ? 551  GLN A C   1 
ATOM   2906 O  O   . GLN A 1 348 ? 13.30234  35.37385 -0.91397  1.000 51.37475  ? 551  GLN A O   1 
ATOM   2907 C  CB  . GLN A 1 348 ? 13.45089  35.11127 -4.13949  1.000 57.04375  ? 551  GLN A CB  1 
ATOM   2908 C  CG  . GLN A 1 348 ? 14.48769  35.96969 -4.82600  1.000 59.20548  ? 551  GLN A CG  1 
ATOM   2909 C  CD  . GLN A 1 348 ? 14.30558  35.97931 -6.32736  1.000 67.30375  ? 551  GLN A CD  1 
ATOM   2910 O  OE1 . GLN A 1 348 ? 13.18688  36.10490 -6.82371  1.000 70.53920  ? 551  GLN A OE1 1 
ATOM   2911 N  NE2 . GLN A 1 348 ? 15.40182  35.82080 -7.05974  1.000 61.28599  ? 551  GLN A NE2 1 
ATOM   2912 N  N   . GLY A 1 349 ? 15.38147  35.82919 -1.67840  1.000 55.10334  ? 552  GLY A N   1 
ATOM   2913 C  CA  . GLY A 1 349 ? 15.68624  36.75718 -0.60340  1.000 61.28218  ? 552  GLY A CA  1 
ATOM   2914 C  C   . GLY A 1 349 ? 17.15967  36.82435 -0.25171  1.000 59.51668  ? 552  GLY A C   1 
ATOM   2915 O  O   . GLY A 1 349 ? 18.01134  36.94229 -1.13991  1.000 60.56124  ? 552  GLY A O   1 
ATOM   2916 N  N   . SER A 1 350 ? 17.47398  36.75396 1.04126   1.000 62.23942  ? 553  SER A N   1 
ATOM   2917 C  CA  . SER A 1 350 ? 18.85229  36.76917 1.51085   1.000 62.36017  ? 553  SER A CA  1 
ATOM   2918 C  C   . SER A 1 350 ? 19.02585  35.71690 2.59514   1.000 69.92396  ? 553  SER A C   1 
ATOM   2919 O  O   . SER A 1 350 ? 18.20722  35.62457 3.51515   1.000 66.53305  ? 553  SER A O   1 
ATOM   2920 C  CB  . SER A 1 350 ? 19.24378  38.15865 2.04581   1.000 65.54135  ? 553  SER A CB  1 
ATOM   2921 N  N   . LYS A 1 351 ? 20.07653  34.91123 2.46433   1.000 80.87038  ? 554  LYS A N   1 
ATOM   2922 C  CA  . LYS A 1 351 ? 20.51216  33.97276 3.49719   1.000 76.41066  ? 554  LYS A CA  1 
ATOM   2923 C  C   . LYS A 1 351 ? 21.93082  34.39479 3.86044   1.000 88.47429  ? 554  LYS A C   1 
ATOM   2924 O  O   . LYS A 1 351 ? 22.88668  34.05996 3.15286   1.000 89.20913  ? 554  LYS A O   1 
ATOM   2925 C  CB  . LYS A 1 351 ? 20.44614  32.52782 3.00915   1.000 71.30725  ? 554  LYS A CB  1 
ATOM   2926 N  N   . GLY A 1 352 ? 22.06178  35.13913 4.95459   1.000 94.38691  ? 555  GLY A N   1 
ATOM   2927 C  CA  . GLY A 1 352 ? 23.28234  35.86373 5.22003   1.000 93.84007  ? 555  GLY A CA  1 
ATOM   2928 C  C   . GLY A 1 352 ? 23.34649  37.11458 4.36361   1.000 96.83121  ? 555  GLY A C   1 
ATOM   2929 O  O   . GLY A 1 352 ? 22.36282  37.53626 3.74721   1.000 97.58751  ? 555  GLY A O   1 
ATOM   2930 N  N   . ASN A 1 353 ? 24.53435  37.71315 4.31942   1.000 92.98358  ? 556  ASN A N   1 
ATOM   2931 C  CA  . ASN A 1 353 ? 24.76976  38.87114 3.45620   1.000 92.53241  ? 556  ASN A CA  1 
ATOM   2932 C  C   . ASN A 1 353 ? 24.97576  38.48143 1.99416   1.000 90.44105  ? 556  ASN A C   1 
ATOM   2933 O  O   . ASN A 1 353 ? 25.79096  39.08590 1.29197   1.000 100.35537 ? 556  ASN A O   1 
ATOM   2934 C  CB  . ASN A 1 353 ? 25.96458  39.66528 3.98011   1.000 83.16191  ? 556  ASN A CB  1 
ATOM   2935 N  N   . ARG A 1 354 ? 24.24393  37.48054 1.51387   1.000 87.37692  ? 557  ARG A N   1 
ATOM   2936 C  CA  . ARG A 1 354 ? 24.35187  36.97657 0.15553   1.000 82.49970  ? 557  ARG A CA  1 
ATOM   2937 C  C   . ARG A 1 354 ? 22.96344  36.77889 -0.43369  1.000 78.04512  ? 557  ARG A C   1 
ATOM   2938 O  O   . ARG A 1 354 ? 22.02560  36.43474 0.29166   1.000 77.18784  ? 557  ARG A O   1 
ATOM   2939 C  CB  . ARG A 1 354 ? 25.11935  35.64550 0.12443   1.000 77.20778  ? 557  ARG A CB  1 
ATOM   2940 N  N   . PRO A 1 355 ? 22.79712  36.99837 -1.74119  1.000 75.89298  ? 558  PRO A N   1 
ATOM   2941 C  CA  . PRO A 1 355 ? 21.50373  36.70470 -2.37254  1.000 63.29407  ? 558  PRO A CA  1 
ATOM   2942 C  C   . PRO A 1 355 ? 21.16106  35.23015 -2.24551  1.000 62.53000  ? 558  PRO A C   1 
ATOM   2943 O  O   . PRO A 1 355 ? 22.04035  34.36837 -2.16740  1.000 64.86775  ? 558  PRO A O   1 
ATOM   2944 C  CB  . PRO A 1 355 ? 21.71809  37.10200 -3.83799  1.000 55.22341  ? 558  PRO A CB  1 
ATOM   2945 C  CG  . PRO A 1 355 ? 23.19827  37.00353 -4.03894  1.000 75.76540  ? 558  PRO A CG  1 
ATOM   2946 C  CD  . PRO A 1 355 ? 23.79479  37.46359 -2.72216  1.000 70.63112  ? 558  PRO A CD  1 
ATOM   2947 N  N   . TYR A 1 356 ? 19.86264  34.94740 -2.21907  1.000 64.28456  ? 559  TYR A N   1 
ATOM   2948 C  CA  . TYR A 1 356 ? 19.37447  33.59106 -2.02848  1.000 56.27316  ? 559  TYR A CA  1 
ATOM   2949 C  C   . TYR A 1 356 ? 18.28947  33.29066 -3.04732  1.000 58.00595  ? 559  TYR A C   1 
ATOM   2950 O  O   . TYR A 1 356 ? 17.38010  34.10086 -3.25652  1.000 49.52051  ? 559  TYR A O   1 
ATOM   2951 C  CB  . TYR A 1 356 ? 18.83747  33.39426 -0.60835  1.000 56.00062  ? 559  TYR A CB  1 
ATOM   2952 C  CG  . TYR A 1 356 ? 18.34157  31.99454 -0.30196  1.000 52.63136  ? 559  TYR A CG  1 
ATOM   2953 C  CD1 . TYR A 1 356 ? 19.22559  30.98048 0.05100   1.000 52.00864  ? 559  TYR A CD1 1 
ATOM   2954 C  CD2 . TYR A 1 356 ? 16.98844  31.69459 -0.34496  1.000 56.18570  ? 559  TYR A CD2 1 
ATOM   2955 C  CE1 . TYR A 1 356 ? 18.77389  29.70470 0.34766   1.000 53.63178  ? 559  TYR A CE1 1 
ATOM   2956 C  CE2 . TYR A 1 356 ? 16.52783  30.42023 -0.05476  1.000 51.71878  ? 559  TYR A CE2 1 
ATOM   2957 C  CZ  . TYR A 1 356 ? 17.42383  29.43134 0.29382   1.000 46.14164  ? 559  TYR A CZ  1 
ATOM   2958 O  OH  . TYR A 1 356 ? 16.95812  28.17016 0.59044   1.000 43.86833  ? 559  TYR A OH  1 
ATOM   2959 N  N   . GLN A 1 357 ? 18.40267  32.12671 -3.67977  1.000 56.29274  ? 560  GLN A N   1 
ATOM   2960 C  CA  . GLN A 1 357 ? 17.38451  31.59029 -4.56332  1.000 54.16360  ? 560  GLN A CA  1 
ATOM   2961 C  C   . GLN A 1 357 ? 17.44720  30.08143 -4.41239  1.000 49.91541  ? 560  GLN A C   1 
ATOM   2962 O  O   . GLN A 1 357 ? 18.53495  29.51836 -4.25370  1.000 48.93546  ? 560  GLN A O   1 
ATOM   2963 C  CB  . GLN A 1 357 ? 17.61168  32.02048 -6.02142  1.000 59.91946  ? 560  GLN A CB  1 
ATOM   2964 N  N   . HIS A 1 358 ? 16.28331  29.43519 -4.43491  1.000 40.21967  ? 561  HIS A N   1 
ATOM   2965 C  CA  . HIS A 1 358 ? 16.24419  28.01390 -4.14807  1.000 41.83758  ? 561  HIS A CA  1 
ATOM   2966 C  C   . HIS A 1 358 ? 14.86874  27.48480 -4.52744  1.000 44.80157  ? 561  HIS A C   1 
ATOM   2967 O  O   . HIS A 1 358 ? 13.85787  28.14813 -4.27496  1.000 43.51668  ? 561  HIS A O   1 
ATOM   2968 C  CB  . HIS A 1 358 ? 16.54673  27.77900 -2.65825  1.000 42.86233  ? 561  HIS A CB  1 
ATOM   2969 C  CG  . HIS A 1 358 ? 16.79177  26.34939 -2.28783  1.000 44.22004  ? 561  HIS A CG  1 
ATOM   2970 N  ND1 . HIS A 1 358 ? 17.80878  25.59228 -2.83145  1.000 36.27668  ? 561  HIS A ND1 1 
ATOM   2971 C  CD2 . HIS A 1 358 ? 16.17500  25.55788 -1.38097  1.000 39.10587  ? 561  HIS A CD2 1 
ATOM   2972 C  CE1 . HIS A 1 358 ? 17.79300  24.38869 -2.28470  1.000 38.48398  ? 561  HIS A CE1 1 
ATOM   2973 N  NE2 . HIS A 1 358 ? 16.80251  24.33797 -1.41227  1.000 41.90474  ? 561  HIS A NE2 1 
ATOM   2974 N  N   . ALA A 1 359 ? 14.83346  26.30936 -5.15201  1.000 29.39002  ? 562  ALA A N   1 
ATOM   2975 C  CA  . ALA A 1 359 ? 13.57605  25.63991 -5.43494  1.000 27.76220  ? 562  ALA A CA  1 
ATOM   2976 C  C   . ALA A 1 359 ? 13.34216  24.55680 -4.39422  1.000 26.04853  ? 562  ALA A C   1 
ATOM   2977 O  O   . ALA A 1 359 ? 14.26562  23.81656 -4.04808  1.000 29.24663  ? 562  ALA A O   1 
ATOM   2978 C  CB  . ALA A 1 359 ? 13.57671  25.00460 -6.83283  1.000 31.46142  ? 562  ALA A CB  1 
ATOM   2979 N  N   . VAL A 1 360 ? 12.10262  24.44902 -3.91332  1.000 24.70863  ? 563  VAL A N   1 
ATOM   2980 C  CA  . VAL A 1 360 ? 11.69751  23.36790 -3.01479  1.000 22.89535  ? 563  VAL A CA  1 
ATOM   2981 C  C   . VAL A 1 360 ? 10.32229  22.85918 -3.44029  1.000 22.58912  ? 563  VAL A C   1 
ATOM   2982 O  O   . VAL A 1 360 ? 9.62236   23.48684 -4.24141  1.000 25.65526  ? 563  VAL A O   1 
ATOM   2983 C  CB  . VAL A 1 360 ? 11.67575  23.81651 -1.53256  1.000 25.19776  ? 563  VAL A CB  1 
ATOM   2984 C  CG1 . VAL A 1 360 ? 13.03128  24.32924 -1.11624  1.000 26.09592  ? 563  VAL A CG1 1 
ATOM   2985 C  CG2 . VAL A 1 360 ? 10.61771  24.88443 -1.31157  1.000 24.83159  ? 563  VAL A CG2 1 
ATOM   2986 N  N   . THR A 1 361 ? 9.92755   21.70636 -2.89037  1.000 21.87413  ? 564  THR A N   1 
ATOM   2987 C  CA  . THR A 1 361 ? 8.63128   21.11172 -3.18586  1.000 20.80388  ? 564  THR A CA  1 
ATOM   2988 C  C   . THR A 1 361 ? 7.69682   21.31928 -2.00210  1.000 22.15519  ? 564  THR A C   1 
ATOM   2989 O  O   . THR A 1 361 ? 8.09712   21.12590 -0.85495  1.000 22.54447  ? 564  THR A O   1 
ATOM   2990 C  CB  . THR A 1 361 ? 8.77844   19.61146 -3.46314  1.000 22.50901  ? 564  THR A CB  1 
ATOM   2991 O  OG1 . THR A 1 361 ? 9.87647   19.38820 -4.34654  1.000 21.85858  ? 564  THR A OG1 1 
ATOM   2992 C  CG2 . THR A 1 361 ? 7.50733   19.02540 -4.06028  1.000 19.69877  ? 564  THR A CG2 1 
ATOM   2993 N  N   . CYS A 1 362 ? 6.45032   21.69935 -2.27138  1.000 24.01257  ? 565  CYS A N   1 
ATOM   2994 C  CA  . CYS A 1 362 ? 5.45240   21.82993 -1.21310  1.000 22.78242  ? 565  CYS A CA  1 
ATOM   2995 C  C   . CYS A 1 362 ? 4.41373   20.71944 -1.34804  1.000 21.93294  ? 565  CYS A C   1 
ATOM   2996 O  O   . CYS A 1 362 ? 3.82889   20.53523 -2.41894  1.000 24.48536  ? 565  CYS A O   1 
ATOM   2997 C  CB  . CYS A 1 362 ? 4.77645   23.20433 -1.24736  1.000 23.20495  ? 565  CYS A CB  1 
ATOM   2998 S  SG  . CYS A 1 362 ? 3.53987   23.39271 0.06000   1.000 26.83259  ? 565  CYS A SG  1 
ATOM   2999 N  N   . TRP A 1 363 ? 4.18245   19.98406 -0.26348  1.000 20.94518  ? 566  TRP A N   1 
ATOM   3000 C  CA  . TRP A 1 363 ? 3.20715   18.90870 -0.26174  1.000 19.39732  ? 566  TRP A CA  1 
ATOM   3001 C  C   . TRP A 1 363 ? 1.94443   19.23270 0.52243   1.000 19.58434  ? 566  TRP A C   1 
ATOM   3002 O  O   . TRP A 1 363 ? 1.01974   18.41912 0.53242   1.000 20.11223  ? 566  TRP A O   1 
ATOM   3003 C  CB  . TRP A 1 363 ? 3.85171   17.62716 0.27915   1.000 19.67757  ? 566  TRP A CB  1 
ATOM   3004 C  CG  . TRP A 1 363 ? 4.89175   17.06711 -0.66969  1.000 18.79962  ? 566  TRP A CG  1 
ATOM   3005 C  CD1 . TRP A 1 363 ? 6.24120   16.99744 -0.46619  1.000 19.02283  ? 566  TRP A CD1 1 
ATOM   3006 C  CD2 . TRP A 1 363 ? 4.64836   16.49838 -1.96403  1.000 19.87799  ? 566  TRP A CD2 1 
ATOM   3007 N  NE1 . TRP A 1 363 ? 6.85296   16.40659 -1.56173  1.000 18.54234  ? 566  TRP A NE1 1 
ATOM   3008 C  CE2 . TRP A 1 363 ? 5.89439   16.10624 -2.49344  1.000 20.00541  ? 566  TRP A CE2 1 
ATOM   3009 C  CE3 . TRP A 1 363 ? 3.49626   16.31132 -2.73703  1.000 21.68627  ? 566  TRP A CE3 1 
ATOM   3010 C  CZ2 . TRP A 1 363 ? 6.02274   15.51475 -3.76099  1.000 16.88258  ? 566  TRP A CZ2 1 
ATOM   3011 C  CZ3 . TRP A 1 363 ? 3.63179   15.71961 -4.00532  1.000 20.10280  ? 566  TRP A CZ3 1 
ATOM   3012 C  CH2 . TRP A 1 363 ? 4.87998   15.33176 -4.48612  1.000 16.67917  ? 566  TRP A CH2 1 
ATOM   3013 N  N   . GLY A 1 364 ? 1.87501   20.38121 1.18474   1.000 21.07164  ? 567  GLY A N   1 
ATOM   3014 C  CA  . GLY A 1 364 ? 0.64283   20.73981 1.85452   1.000 22.23345  ? 567  GLY A CA  1 
ATOM   3015 C  C   . GLY A 1 364 ? 0.81970   21.98008 2.70148   1.000 22.91815  ? 567  GLY A C   1 
ATOM   3016 O  O   . GLY A 1 364 ? 1.91499   22.52989 2.81930   1.000 23.29418  ? 567  GLY A O   1 
ATOM   3017 N  N   . ALA A 1 365 ? -0.29608  22.41535 3.28035   1.000 23.70615  ? 568  ALA A N   1 
ATOM   3018 C  CA  . ALA A 1 365 ? -0.32683  23.66203 4.03653   1.000 23.28821  ? 568  ALA A CA  1 
ATOM   3019 C  C   . ALA A 1 365 ? -1.24873  23.54805 5.24271   1.000 26.41139  ? 568  ALA A C   1 
ATOM   3020 O  O   . ALA A 1 365 ? -2.25048  22.83028 5.21421   1.000 25.50474  ? 568  ALA A O   1 
ATOM   3021 C  CB  . ALA A 1 365 ? -0.79038  24.81134 3.13889   1.000 26.38321  ? 568  ALA A CB  1 
ATOM   3022 N  N   . ALA A 1 366 ? -0.90980  24.29535 6.30164   1.000 25.15468  ? 569  ALA A N   1 
ATOM   3023 C  CA  . ALA A 1 366 ? -1.73317  24.43204 7.49590   1.000 29.81337  ? 569  ALA A CA  1 
ATOM   3024 C  C   . ALA A 1 366 ? -2.51046  25.74604 7.45747   1.000 26.44186  ? 569  ALA A C   1 
ATOM   3025 O  O   . ALA A 1 366 ? -2.00884  26.76268 6.97255   1.000 25.54896  ? 569  ALA A O   1 
ATOM   3026 C  CB  . ALA A 1 366 ? -0.86872  24.39054 8.76122   1.000 27.75867  ? 569  ALA A CB  1 
ATOM   3027 N  N   . TYR A 1 367 ? -3.73700  25.72263 7.99179   1.000 26.97007  ? 570  TYR A N   1 
ATOM   3028 C  CA  . TYR A 1 367 ? -4.63089  26.87754 7.99468   1.000 28.23718  ? 570  TYR A CA  1 
ATOM   3029 C  C   . TYR A 1 367 ? -5.16146  27.14253 9.39796   1.000 26.35841  ? 570  TYR A C   1 
ATOM   3030 O  O   . TYR A 1 367 ? -5.49920  26.20335 10.12434  1.000 29.89399  ? 570  TYR A O   1 
ATOM   3031 C  CB  . TYR A 1 367 ? -5.83218  26.65756 7.07467   1.000 31.83691  ? 570  TYR A CB  1 
ATOM   3032 C  CG  . TYR A 1 367 ? -5.52119  26.47639 5.59991   1.000 26.70579  ? 570  TYR A CG  1 
ATOM   3033 C  CD1 . TYR A 1 367 ? -4.95263  25.30044 5.12429   1.000 30.22534  ? 570  TYR A CD1 1 
ATOM   3034 C  CD2 . TYR A 1 367 ? -5.83223  27.47834 4.68420   1.000 34.45117  ? 570  TYR A CD2 1 
ATOM   3035 C  CE1 . TYR A 1 367 ? -4.68527  25.13490 3.76934   1.000 31.58127  ? 570  TYR A CE1 1 
ATOM   3036 C  CE2 . TYR A 1 367 ? -5.56871  27.31635 3.33178   1.000 34.36658  ? 570  TYR A CE2 1 
ATOM   3037 C  CZ  . TYR A 1 367 ? -4.98833  26.13974 2.88865   1.000 32.74620  ? 570  TYR A CZ  1 
ATOM   3038 O  OH  . TYR A 1 367 ? -4.72421  25.97507 1.53980   1.000 32.84543  ? 570  TYR A OH  1 
ATOM   3039 N  N   . ASP A 1 368 ? -5.27899  28.41541 9.76515   1.000 30.87456  ? 571  ASP A N   1 
ATOM   3040 C  CA  . ASP A 1 368 ? -5.95492  28.76465 11.01019  1.000 33.00423  ? 571  ASP A CA  1 
ATOM   3041 C  C   . ASP A 1 368 ? -7.46824  28.85977 10.75791  1.000 36.36328  ? 571  ASP A C   1 
ATOM   3042 O  O   . ASP A 1 368 ? -7.95531  28.64740 9.64314   1.000 34.63667  ? 571  ASP A O   1 
ATOM   3043 C  CB  . ASP A 1 368 ? -5.35751  30.04400 11.61615  1.000 36.48687  ? 571  ASP A CB  1 
ATOM   3044 C  CG  . ASP A 1 368 ? -5.66303  31.31135 10.81007  1.000 32.84009  ? 571  ASP A CG  1 
ATOM   3045 O  OD1 . ASP A 1 368 ? -6.57035  31.31341 9.95433   1.000 34.18273  ? 571  ASP A OD1 1 
ATOM   3046 O  OD2 . ASP A 1 368 ? -4.99852  32.35482 11.05713  1.000 34.43000  ? 571  ASP A OD2 1 
ATOM   3047 N  N   . GLU A 1 369 ? -8.22979  29.15825 11.81263  1.000 32.24468  ? 572  GLU A N   1 
ATOM   3048 C  CA  . GLU A 1 369 ? -9.68738  29.19596 11.70623  1.000 39.58236  ? 572  GLU A CA  1 
ATOM   3049 C  C   . GLU A 1 369 ? -10.19991 30.32554 10.82212  1.000 38.28979  ? 572  GLU A C   1 
ATOM   3050 O  O   . GLU A 1 369 ? -11.36634 30.28594 10.41657  1.000 44.01602  ? 572  GLU A O   1 
ATOM   3051 C  CB  . GLU A 1 369 ? -10.31791 29.32294 13.09582  1.000 37.16981  ? 572  GLU A CB  1 
ATOM   3052 C  CG  . GLU A 1 369 ? -10.03657 28.14426 14.01321  1.000 38.61139  ? 572  GLU A CG  1 
ATOM   3053 C  CD  . GLU A 1 369 ? -10.27734 28.50182 15.46893  1.000 38.31040  ? 572  GLU A CD  1 
ATOM   3054 O  OE1 . GLU A 1 369 ? -11.42777 28.83869 15.80781  1.000 40.71003  ? 572  GLU A OE1 1 
ATOM   3055 O  OE2 . GLU A 1 369 ? -9.31077  28.47337 16.25779  1.000 40.07711  ? 572  GLU A OE2 1 
ATOM   3056 N  N   . ASP A 1 370 ? -9.38700  31.34773 10.55130  1.000 35.71070  ? 573  ASP A N   1 
ATOM   3057 C  CA  . ASP A 1 370 ? -9.73116  32.37403 9.57232   1.000 36.35005  ? 573  ASP A CA  1 
ATOM   3058 C  C   . ASP A 1 370 ? -9.32146  31.97897 8.15333   1.000 37.69205  ? 573  ASP A C   1 
ATOM   3059 O  O   . ASP A 1 370 ? -9.46631  32.79371 7.22951   1.000 40.35621  ? 573  ASP A O   1 
ATOM   3060 C  CB  . ASP A 1 370 ? -9.07935  33.71546 9.94574   1.000 37.75509  ? 573  ASP A CB  1 
ATOM   3061 C  CG  . ASP A 1 370 ? -9.68926  34.34668 11.19699  1.000 45.13399  ? 573  ASP A CG  1 
ATOM   3062 O  OD1 . ASP A 1 370 ? -10.81431 33.96564 11.59367  1.000 40.18182  ? 573  ASP A OD1 1 
ATOM   3063 O  OD2 . ASP A 1 370 ? -9.05070  35.26145 11.76527  1.000 47.67896  ? 573  ASP A OD2 1 
ATOM   3064 N  N   . ASN A 1 371 ? -8.82128  30.75606 7.97214   1.000 36.61577  ? 574  ASN A N   1 
ATOM   3065 C  CA  . ASN A 1 371 ? -8.30604  30.22952 6.70493   1.000 37.27791  ? 574  ASN A CA  1 
ATOM   3066 C  C   . ASN A 1 371 ? -7.06210  30.96594 6.21574   1.000 42.87018  ? 574  ASN A C   1 
ATOM   3067 O  O   . ASN A 1 371 ? -6.74281  30.91933 5.02034   1.000 41.50527  ? 574  ASN A O   1 
ATOM   3068 C  CB  . ASN A 1 371 ? -9.37981  30.23262 5.60994   1.000 45.89043  ? 574  ASN A CB  1 
ATOM   3069 C  CG  . ASN A 1 371 ? -10.53616 29.30898 5.93081   1.000 40.98299  ? 574  ASN A CG  1 
ATOM   3070 O  OD1 . ASN A 1 371 ? -10.37518 28.31449 6.63497   1.000 42.41205  ? 574  ASN A OD1 1 
ATOM   3071 N  ND2 . ASN A 1 371 ? -11.71370 29.63714 5.41641   1.000 49.52717  ? 574  ASN A ND2 1 
ATOM   3072 N  N   . ASN A 1 372 ? -6.35523  31.66058 7.10736   1.000 36.33369  ? 575  ASN A N   1 
ATOM   3073 C  CA  . ASN A 1 372 ? -5.02306  32.14215 6.77716   1.000 34.56587  ? 575  ASN A CA  1 
ATOM   3074 C  C   . ASN A 1 372 ? -4.08486  30.95192 6.67476   1.000 34.15844  ? 575  ASN A C   1 
ATOM   3075 O  O   . ASN A 1 372 ? -4.16784  30.01066 7.46968   1.000 33.06362  ? 575  ASN A O   1 
ATOM   3076 C  CB  . ASN A 1 372 ? -4.50850  33.10717 7.84666   1.000 33.76712  ? 575  ASN A CB  1 
ATOM   3077 C  CG  . ASN A 1 372 ? -5.43274  34.27930 8.06982   1.000 36.19784  ? 575  ASN A CG  1 
ATOM   3078 O  OD1 . ASN A 1 372 ? -5.80925  34.97071 7.12848   1.000 37.89928  ? 575  ASN A OD1 1 
ATOM   3079 N  ND2 . ASN A 1 372 ? -5.79464  34.52030 9.32769   1.000 37.50419  ? 575  ASN A ND2 1 
ATOM   3080 N  N   . ILE A 1 373 ? -3.19309  30.97799 5.69021   1.000 30.44364  ? 576  ILE A N   1 
ATOM   3081 C  CA  . ILE A 1 373 ? -2.17019  29.94308 5.59334   1.000 29.78820  ? 576  ILE A CA  1 
ATOM   3082 C  C   . ILE A 1 373 ? -1.02885  30.28304 6.54071   1.000 28.15950  ? 576  ILE A C   1 
ATOM   3083 O  O   . ILE A 1 373 ? -0.43182  31.35816 6.44209   1.000 31.22499  ? 576  ILE A O   1 
ATOM   3084 C  CB  . ILE A 1 373 ? -1.66311  29.80384 4.15285   1.000 36.79731  ? 576  ILE A CB  1 
ATOM   3085 C  CG1 . ILE A 1 373 ? -2.80080  29.33743 3.25360   1.000 34.96235  ? 576  ILE A CG1 1 
ATOM   3086 C  CG2 . ILE A 1 373 ? -0.47313  28.85596 4.12046   1.000 30.45883  ? 576  ILE A CG2 1 
ATOM   3087 C  CD1 . ILE A 1 373 ? -2.39590  29.16569 1.80136   1.000 32.85029  ? 576  ILE A CD1 1 
ATOM   3088 N  N   . ILE A 1 374 ? -0.68989  29.34599 7.42674   1.000 28.84924  ? 577  ILE A N   1 
ATOM   3089 C  CA  . ILE A 1 374 ? 0.24959   29.61814 8.51124   1.000 29.37533  ? 577  ILE A CA  1 
ATOM   3090 C  C   . ILE A 1 374 ? 1.50248   28.76130 8.44780   1.000 29.12863  ? 577  ILE A C   1 
ATOM   3091 O  O   . ILE A 1 374 ? 2.49161   29.08739 9.12117   1.000 28.25623  ? 577  ILE A O   1 
ATOM   3092 C  CB  . ILE A 1 374 ? -0.43440  29.45355 9.88201   1.000 26.70287  ? 577  ILE A CB  1 
ATOM   3093 C  CG1 . ILE A 1 374 ? -0.84370  27.99240 10.08003  1.000 28.18432  ? 577  ILE A CG1 1 
ATOM   3094 C  CG2 . ILE A 1 374 ? -1.64575  30.36742 9.93461   1.000 29.12841  ? 577  ILE A CG2 1 
ATOM   3095 C  CD1 . ILE A 1 374 ? -1.62512  27.72416 11.33590  1.000 30.08809  ? 577  ILE A CD1 1 
ATOM   3096 N  N   . CYS A 1 375 ? 1.51916   27.69337 7.65332   1.000 26.01128  ? 578  CYS A N   1 
ATOM   3097 C  CA  . CYS A 1 375 ? 2.68084   26.82398 7.61121   1.000 22.96334  ? 578  CYS A CA  1 
ATOM   3098 C  C   . CYS A 1 375 ? 2.61387   25.99872 6.33706   1.000 27.53660  ? 578  CYS A C   1 
ATOM   3099 O  O   . CYS A 1 375 ? 1.52680   25.64254 5.87259   1.000 25.74711  ? 578  CYS A O   1 
ATOM   3100 C  CB  . CYS A 1 375 ? 2.73470   25.90127 8.84273   1.000 22.55517  ? 578  CYS A CB  1 
ATOM   3101 S  SG  . CYS A 1 375 ? 4.31928   25.09668 9.16278   1.000 25.76917  ? 578  CYS A SG  1 
ATOM   3102 N  N   . LEU A 1 376 ? 3.78636   25.69903 5.78611   1.000 23.51155  ? 579  LEU A N   1 
ATOM   3103 C  CA  . LEU A 1 376 ? 3.91544   24.83204 4.61985   1.000 22.41056  ? 579  LEU A CA  1 
ATOM   3104 C  C   . LEU A 1 376 ? 4.75717   23.62247 4.98571   1.000 21.78376  ? 579  LEU A C   1 
ATOM   3105 O  O   . LEU A 1 376 ? 5.61737   23.69235 5.86858   1.000 22.45005  ? 579  LEU A O   1 
ATOM   3106 C  CB  . LEU A 1 376 ? 4.57188   25.54876 3.44145   1.000 22.03671  ? 579  LEU A CB  1 
ATOM   3107 C  CG  . LEU A 1 376 ? 3.89421   26.82493 2.94858   1.000 29.51021  ? 579  LEU A CG  1 
ATOM   3108 C  CD1 . LEU A 1 376 ? 4.65053   27.37292 1.74583   1.000 29.17326  ? 579  LEU A CD1 1 
ATOM   3109 C  CD2 . LEU A 1 376 ? 2.45782   26.50939 2.58795   1.000 27.36935  ? 579  LEU A CD2 1 
ATOM   3110 N  N   . TYR A 1 377 ? 4.52386   22.51317 4.29042   1.000 19.79821  ? 580  TYR A N   1 
ATOM   3111 C  CA  . TYR A 1 377 ? 5.27115   21.28357 4.54963   1.000 18.68868  ? 580  TYR A CA  1 
ATOM   3112 C  C   . TYR A 1 377 ? 6.14208   21.01204 3.33156   1.000 22.87070  ? 580  TYR A C   1 
ATOM   3113 O  O   . TYR A 1 377 ? 5.62680   20.82502 2.21933   1.000 22.36592  ? 580  TYR A O   1 
ATOM   3114 C  CB  . TYR A 1 377 ? 4.32441   20.12369 4.90109   1.000 20.28399  ? 580  TYR A CB  1 
ATOM   3115 C  CG  . TYR A 1 377 ? 3.61515   20.54263 6.16825   1.000 20.59657  ? 580  TYR A CG  1 
ATOM   3116 C  CD1 . TYR A 1 377 ? 4.19717   20.33063 7.42119   1.000 20.58659  ? 580  TYR A CD1 1 
ATOM   3117 C  CD2 . TYR A 1 377 ? 2.43702   21.26888 6.10337   1.000 21.44287  ? 580  TYR A CD2 1 
ATOM   3118 C  CE1 . TYR A 1 377 ? 3.59013   20.80630 8.57433   1.000 20.43207  ? 580  TYR A CE1 1 
ATOM   3119 C  CE2 . TYR A 1 377 ? 1.82066   21.74643 7.24788   1.000 23.64182  ? 580  TYR A CE2 1 
ATOM   3120 C  CZ  . TYR A 1 377 ? 2.39064   21.49273 8.48096   1.000 22.32903  ? 580  TYR A CZ  1 
ATOM   3121 O  OH  . TYR A 1 377 ? 1.76095   22.00989 9.59794   1.000 22.43065  ? 580  TYR A OH  1 
ATOM   3122 N  N   . ILE A 1 378 ? 7.45832   21.07100 3.52838   1.000 18.99175  ? 581  ILE A N   1 
ATOM   3123 C  CA  . ILE A 1 378 ? 8.40623   21.29174 2.43765   1.000 19.95348  ? 581  ILE A CA  1 
ATOM   3124 C  C   . ILE A 1 378 ? 9.34136   20.09311 2.31059   1.000 18.99172  ? 581  ILE A C   1 
ATOM   3125 O  O   . ILE A 1 378 ? 9.93175   19.64604 3.30039   1.000 19.64732  ? 581  ILE A O   1 
ATOM   3126 C  CB  . ILE A 1 378 ? 9.21657   22.58176 2.66011   1.000 19.77414  ? 581  ILE A CB  1 
ATOM   3127 C  CG1 . ILE A 1 378 ? 8.29595   23.81380 2.72357   1.000 22.05634  ? 581  ILE A CG1 1 
ATOM   3128 C  CG2 . ILE A 1 378 ? 10.33122  22.72506 1.61336   1.000 22.12404  ? 581  ILE A CG2 1 
ATOM   3129 C  CD1 . ILE A 1 378 ? 7.49801   24.08925 1.42333   1.000 24.19569  ? 581  ILE A CD1 1 
ATOM   3130 N  N   . ALA A 1 379 ? 9.50366   19.60126 1.08335   1.000 19.12392  ? 582  ALA A N   1 
ATOM   3131 C  CA  . ALA A 1 379 ? 10.63222  18.74040 0.75188   1.000 19.51843  ? 582  ALA A CA  1 
ATOM   3132 C  C   . ALA A 1 379 ? 11.77994  19.63966 0.33771   1.000 23.23102  ? 582  ALA A C   1 
ATOM   3133 O  O   . ALA A 1 379 ? 11.71359  20.30188 -0.71149  1.000 23.46124  ? 582  ALA A O   1 
ATOM   3134 C  CB  . ALA A 1 379 ? 10.27658  17.74928 -0.35265  1.000 18.63723  ? 582  ALA A CB  1 
ATOM   3135 N  N   . GLU A 1 380 ? 12.81376  19.68374 1.17188   1.000 20.80529  ? 583  GLU A N   1 
ATOM   3136 C  CA  . GLU A 1 380 ? 13.96390  20.56892 1.02125   1.000 21.28209  ? 583  GLU A CA  1 
ATOM   3137 C  C   . GLU A 1 380 ? 15.18023  19.69451 0.71778   1.000 27.19197  ? 583  GLU A C   1 
ATOM   3138 O  O   . GLU A 1 380 ? 15.72224  19.04256 1.61580   1.000 23.18830  ? 583  GLU A O   1 
ATOM   3139 C  CB  . GLU A 1 380 ? 14.16944  21.38521 2.30385   1.000 22.69012  ? 583  GLU A CB  1 
ATOM   3140 C  CG  . GLU A 1 380 ? 14.45530  22.87998 2.11528   1.000 25.72836  ? 583  GLU A CG  1 
ATOM   3141 C  CD  . GLU A 1 380 ? 15.80524  23.17275 1.48092   1.000 30.74974  ? 583  GLU A CD  1 
ATOM   3142 O  OE1 . GLU A 1 380 ? 16.27974  22.38004 0.63034   1.000 29.11232  ? 583  GLU A OE1 1 
ATOM   3143 O  OE2 . GLU A 1 380 ? 16.40397  24.22294 1.82201   1.000 35.91678  ? 583  GLU A OE2 1 
ATOM   3144 N  N   . SER A 1 381 ? 15.61889  19.67759 -0.54346  1.000 23.90776  ? 584  SER A N   1 
ATOM   3145 C  CA  . SER A 1 381 ? 16.66209  18.73059 -0.92967  1.000 24.99710  ? 584  SER A CA  1 
ATOM   3146 C  C   . SER A 1 381 ? 18.01812  19.05098 -0.32075  1.000 27.82453  ? 584  SER A C   1 
ATOM   3147 O  O   . SER A 1 381 ? 18.90532  18.18938 -0.36630  1.000 26.83208  ? 584  SER A O   1 
ATOM   3148 C  CB  . SER A 1 381 ? 16.77917  18.65787 -2.45625  1.000 24.71605  ? 584  SER A CB  1 
ATOM   3149 O  OG  . SER A 1 381 ? 17.22467  19.90975 -2.96800  1.000 28.52101  ? 584  SER A OG  1 
ATOM   3150 N  N   . ASN A 1 382 ? 18.19651  20.25961 0.23686   1.000 24.30971  ? 585  ASN A N   1 
ATOM   3151 C  CA  . ASN A 1 382 ? 19.39790  20.63750 0.96669   1.000 26.88066  ? 585  ASN A CA  1 
ATOM   3152 C  C   . ASN A 1 382 ? 19.42314  20.10887 2.39312   1.000 30.37777  ? 585  ASN A C   1 
ATOM   3153 O  O   . ASN A 1 382 ? 20.50024  20.07215 2.99589   1.000 32.74752  ? 585  ASN A O   1 
ATOM   3154 C  CB  . ASN A 1 382 ? 19.53332  22.16565 1.06447   1.000 27.53756  ? 585  ASN A CB  1 
ATOM   3155 C  CG  . ASN A 1 382 ? 20.12307  22.80019 -0.18381  1.000 33.17156  ? 585  ASN A CG  1 
ATOM   3156 O  OD1 . ASN A 1 382 ? 20.34599  22.13433 -1.17959  1.000 33.26583  ? 585  ASN A OD1 1 
ATOM   3157 N  ND2 . ASN A 1 382 ? 20.38612  24.10764 -0.12147  1.000 42.97736  ? 585  ASN A ND2 1 
ATOM   3158 N  N   . LEU A 1 383 ? 18.27450  19.78132 2.96044   1.000 26.27612  ? 586  LEU A N   1 
ATOM   3159 C  CA  . LEU A 1 383 ? 18.27010  19.44368 4.37742   1.000 25.04673  ? 586  LEU A CA  1 
ATOM   3160 C  C   . LEU A 1 383 ? 18.42348  17.93462 4.56130   1.000 23.32029  ? 586  LEU A C   1 
ATOM   3161 O  O   . LEU A 1 383 ? 18.04493  17.15009 3.68396   1.000 25.54377  ? 586  LEU A O   1 
ATOM   3162 C  CB  . LEU A 1 383 ? 16.97787  19.92899 5.03458   1.000 25.10632  ? 586  LEU A CB  1 
ATOM   3163 C  CG  . LEU A 1 383 ? 16.79178  21.45592 5.05221   1.000 26.87380  ? 586  LEU A CG  1 
ATOM   3164 C  CD1 . LEU A 1 383 ? 15.47631  21.83797 5.71605   1.000 28.95108  ? 586  LEU A CD1 1 
ATOM   3165 C  CD2 . LEU A 1 383 ? 17.95796  22.15683 5.75325   1.000 35.14719  ? 586  LEU A CD2 1 
ATOM   3166 N  N   . PRO A 1 384 ? 18.96580  17.50443 5.70375   1.000 25.87345  ? 587  PRO A N   1 
ATOM   3167 C  CA  . PRO A 1 384 ? 19.45706  16.12217 5.80685   1.000 28.91121  ? 587  PRO A CA  1 
ATOM   3168 C  C   . PRO A 1 384 ? 18.40972  15.04661 6.06747   1.000 24.19016  ? 587  PRO A C   1 
ATOM   3169 O  O   . PRO A 1 384 ? 18.61029  13.90141 5.64813   1.000 25.79396  ? 587  PRO A O   1 
ATOM   3170 C  CB  . PRO A 1 384 ? 20.44318  16.19998 6.97532   1.000 29.68594  ? 587  PRO A CB  1 
ATOM   3171 C  CG  . PRO A 1 384 ? 19.92508  17.34994 7.81269   1.000 30.65069  ? 587  PRO A CG  1 
ATOM   3172 C  CD  . PRO A 1 384 ? 19.46856  18.35484 6.79769   1.000 25.51506  ? 587  PRO A CD  1 
ATOM   3173 N  N   . GLU A 1 385 ? 17.32985  15.34105 6.78513   1.000 21.61177  ? 588  GLU A N   1 
ATOM   3174 C  CA  . GLU A 1 385 ? 16.47519  14.24302 7.22606   1.000 21.24674  ? 588  GLU A CA  1 
ATOM   3175 C  C   . GLU A 1 385 ? 15.48638  13.81384 6.14287   1.000 23.69822  ? 588  GLU A C   1 
ATOM   3176 O  O   . GLU A 1 385 ? 15.05013  14.60705 5.29665   1.000 20.62301  ? 588  GLU A O   1 
ATOM   3177 C  CB  . GLU A 1 385 ? 15.74314  14.62110 8.51088   1.000 24.78204  ? 588  GLU A CB  1 
ATOM   3178 C  CG  . GLU A 1 385 ? 16.71978  14.77144 9.67712   1.000 25.17037  ? 588  GLU A CG  1 
ATOM   3179 C  CD  . GLU A 1 385 ? 16.05501  15.25151 10.95556  1.000 32.61438  ? 588  GLU A CD  1 
ATOM   3180 O  OE1 . GLU A 1 385 ? 14.81325  15.19642 11.04714  1.000 32.74349  ? 588  GLU A OE1 1 
ATOM   3181 O  OE2 . GLU A 1 385 ? 16.78167  15.67795 11.87777  1.000 42.05614  ? 588  GLU A OE2 1 
ATOM   3182 N  N   . ALA A 1 386 ? 15.14768  12.52410 6.15969   1.000 21.99109  ? 589  ALA A N   1 
ATOM   3183 C  CA  . ALA A 1 386 ? 14.17594  11.97670 5.20563   1.000 19.98031  ? 589  ALA A CA  1 
ATOM   3184 C  C   . ALA A 1 386 ? 12.76638  12.26470 5.71706   1.000 20.35777  ? 589  ALA A C   1 
ATOM   3185 O  O   . ALA A 1 386 ? 12.03045  11.38272 6.17740   1.000 20.17116  ? 589  ALA A O   1 
ATOM   3186 C  CB  . ALA A 1 386 ? 14.40476  10.48000 5.00957   1.000 23.35194  ? 589  ALA A CB  1 
ATOM   3187 N  N   . VAL A 1 387 ? 12.41981  13.55101 5.69133   1.000 16.63624  ? 590  VAL A N   1 
ATOM   3188 C  CA  . VAL A 1 387 ? 11.17132  14.07649 6.22473   1.000 15.87729  ? 590  VAL A CA  1 
ATOM   3189 C  C   . VAL A 1 387 ? 10.76117  15.26544 5.37164   1.000 17.22624  ? 590  VAL A C   1 
ATOM   3190 O  O   . VAL A 1 387 ? 11.56862  15.81623 4.62561   1.000 20.12109  ? 590  VAL A O   1 
ATOM   3191 C  CB  . VAL A 1 387 ? 11.29397  14.55974 7.68943   1.000 17.06951  ? 590  VAL A CB  1 
ATOM   3192 C  CG1 . VAL A 1 387 ? 11.83965  13.47138 8.61461   1.000 20.71612  ? 590  VAL A CG1 1 
ATOM   3193 C  CG2 . VAL A 1 387 ? 12.16744  15.83601 7.73951   1.000 19.30936  ? 590  VAL A CG2 1 
ATOM   3194 N  N   . LEU A 1 388 ? 9.51200   15.69863 5.53146   1.000 16.32884  ? 591  LEU A N   1 
ATOM   3195 C  CA  . LEU A 1 388 ? 9.13429   17.05802 5.14974   1.000 17.12065  ? 591  LEU A CA  1 
ATOM   3196 C  C   . LEU A 1 388 ? 9.29886   17.96700 6.35722   1.000 21.39371  ? 591  LEU A C   1 
ATOM   3197 O  O   . LEU A 1 388 ? 8.90764   17.60570 7.46605   1.000 20.55618  ? 591  LEU A O   1 
ATOM   3198 C  CB  . LEU A 1 388 ? 7.68601   17.13160 4.66941   1.000 19.20409  ? 591  LEU A CB  1 
ATOM   3199 C  CG  . LEU A 1 388 ? 7.32308   16.11992 3.58279   1.000 16.98147  ? 591  LEU A CG  1 
ATOM   3200 C  CD1 . LEU A 1 388 ? 5.88124   16.38352 3.12964   1.000 17.29415  ? 591  LEU A CD1 1 
ATOM   3201 C  CD2 . LEU A 1 388 ? 8.33126   16.26641 2.42106   1.000 17.34432  ? 591  LEU A CD2 1 
ATOM   3202 N  N   . TYR A 1 389 ? 9.84374   19.16133 6.12247   1.000 19.20784  ? 592  TYR A N   1 
ATOM   3203 C  CA  . TYR A 1 389 ? 10.07747  20.13918 7.18081   1.000 20.84962  ? 592  TYR A CA  1 
ATOM   3204 C  C   . TYR A 1 389 ? 8.98458   21.20129 7.17763   1.000 21.69430  ? 592  TYR A C   1 
ATOM   3205 O  O   . TYR A 1 389 ? 8.55136   21.64415 6.10980   1.000 19.31063  ? 592  TYR A O   1 
ATOM   3206 C  CB  . TYR A 1 389 ? 11.42181  20.83820 6.98450   1.000 21.15912  ? 592  TYR A CB  1 
ATOM   3207 C  CG  . TYR A 1 389 ? 12.65377  20.01311 7.26743   1.000 20.55087  ? 592  TYR A CG  1 
ATOM   3208 C  CD1 . TYR A 1 389 ? 13.17540  19.14929 6.32180   1.000 24.26509  ? 592  TYR A CD1 1 
ATOM   3209 C  CD2 . TYR A 1 389 ? 13.33127  20.14447 8.48381   1.000 23.17307  ? 592  TYR A CD2 1 
ATOM   3210 C  CE1 . TYR A 1 389 ? 14.31794  18.41905 6.58130   1.000 24.28201  ? 592  TYR A CE1 1 
ATOM   3211 C  CE2 . TYR A 1 389 ? 14.47648  19.42496 8.73959   1.000 24.22322  ? 592  TYR A CE2 1 
ATOM   3212 C  CZ  . TYR A 1 389 ? 14.96094  18.56156 7.78896   1.000 24.70122  ? 592  TYR A CZ  1 
ATOM   3213 O  OH  . TYR A 1 389 ? 16.10689  17.85101 8.03921   1.000 24.22145  ? 592  TYR A OH  1 
ATOM   3214 N  N   . PRO A 1 390 ? 8.53049   21.63887 8.34834   1.000 19.67587  ? 593  PRO A N   1 
ATOM   3215 C  CA  . PRO A 1 390 ? 7.58306   22.75896 8.41516   1.000 19.79901  ? 593  PRO A CA  1 
ATOM   3216 C  C   . PRO A 1 390 ? 8.29772   24.08786 8.20571   1.000 21.17479  ? 593  PRO A C   1 
ATOM   3217 O  O   . PRO A 1 390 ? 9.32466   24.36962 8.83085   1.000 22.62240  ? 593  PRO A O   1 
ATOM   3218 C  CB  . PRO A 1 390 ? 7.01599   22.65696 9.84095   1.000 21.04606  ? 593  PRO A CB  1 
ATOM   3219 C  CG  . PRO A 1 390 ? 8.16220   22.07369 10.62795  1.000 22.09506  ? 593  PRO A CG  1 
ATOM   3220 C  CD  . PRO A 1 390 ? 8.88743   21.12161 9.68390   1.000 19.29946  ? 593  PRO A CD  1 
ATOM   3221 N  N   . PHE A 1 391 ? 7.74389   24.91566 7.33197   1.000 21.76398  ? 594  PHE A N   1 
ATOM   3222 C  CA  . PHE A 1 391 ? 8.21716   26.28760 7.17133   1.000 23.32269  ? 594  PHE A CA  1 
ATOM   3223 C  C   . PHE A 1 391 ? 7.05232   27.20781 7.48513   1.000 25.70373  ? 594  PHE A C   1 
ATOM   3224 O  O   . PHE A 1 391 ? 6.02296   27.18078 6.80238   1.000 25.14199  ? 594  PHE A O   1 
ATOM   3225 C  CB  . PHE A 1 391 ? 8.79480   26.53944 5.77552   1.000 24.82991  ? 594  PHE A CB  1 
ATOM   3226 C  CG  . PHE A 1 391 ? 10.20711  26.07424 5.63962   1.000 25.73829  ? 594  PHE A CG  1 
ATOM   3227 C  CD1 . PHE A 1 391 ? 10.48039  24.73764 5.36615   1.000 23.66753  ? 594  PHE A CD1 1 
ATOM   3228 C  CD2 . PHE A 1 391 ? 11.26316  26.93626 5.89351   1.000 33.61269  ? 594  PHE A CD2 1 
ATOM   3229 C  CE1 . PHE A 1 391 ? 11.77772  24.28804 5.26594   1.000 24.67176  ? 594  PHE A CE1 1 
ATOM   3230 C  CE2 . PHE A 1 391 ? 12.57176  26.49165 5.80250   1.000 37.49527  ? 594  PHE A CE2 1 
ATOM   3231 C  CZ  . PHE A 1 391 ? 12.82665  25.15732 5.47953   1.000 33.16910  ? 594  PHE A CZ  1 
ATOM   3232 N  N   . GLY A 1 392 ? 7.18962   27.95452 8.57111   1.000 25.08247  ? 595  GLY A N   1 
ATOM   3233 C  CA  . GLY A 1 392 ? 6.14631   28.87769 8.95588   1.000 25.98236  ? 595  GLY A CA  1 
ATOM   3234 C  C   . GLY A 1 392 ? 5.97252   29.97952 7.93183   1.000 31.49490  ? 595  GLY A C   1 
ATOM   3235 O  O   . GLY A 1 392 ? 6.91430   30.39147 7.26341   1.000 30.99898  ? 595  GLY A O   1 
ATOM   3236 N  N   . VAL A 1 393 ? 4.75380   30.49427 7.85576   1.000 27.95415  ? 596  VAL A N   1 
ATOM   3237 C  CA  . VAL A 1 393 ? 4.41481   31.58585 6.95185   1.000 30.82705  ? 596  VAL A CA  1 
ATOM   3238 C  C   . VAL A 1 393 ? 4.25264   32.86785 7.75413   1.000 35.93173  ? 596  VAL A C   1 
ATOM   3239 O  O   . VAL A 1 393 ? 3.50847   32.89966 8.74017   1.000 38.72200  ? 596  VAL A O   1 
ATOM   3240 C  CB  . VAL A 1 393 ? 3.13840   31.25909 6.16792   1.000 32.98202  ? 596  VAL A CB  1 
ATOM   3241 C  CG1 . VAL A 1 393 ? 2.70389   32.47929 5.42344   1.000 48.14456  ? 596  VAL A CG1 1 
ATOM   3242 C  CG2 . VAL A 1 393 ? 3.40195   30.14587 5.21349   1.000 34.11044  ? 596  VAL A CG2 1 
ATOM   3243 N  N   . ARG A 1 394 ? 4.94223   33.93158 7.32260   1.000 34.71102  ? 597  ARG A N   1 
ATOM   3244 C  CA  . ARG A 1 394 ? 4.86000   35.24644 7.93931   1.000 43.40802  ? 597  ARG A CA  1 
ATOM   3245 C  C   . ARG A 1 394 ? 4.70620   36.28845 6.84507   1.000 42.24072  ? 597  ARG A C   1 
ATOM   3246 O  O   . ARG A 1 394 ? 5.23234   36.13007 5.74227   1.000 50.27388  ? 597  ARG A O   1 
ATOM   3247 C  CB  . ARG A 1 394 ? 6.10317   35.57506 8.76521   1.000 44.30156  ? 597  ARG A CB  1 
ATOM   3248 C  CG  . ARG A 1 394 ? 6.37783   34.64994 9.90955   1.000 45.51701  ? 597  ARG A CG  1 
ATOM   3249 C  CD  . ARG A 1 394 ? 5.62401   35.06186 11.15045  1.000 53.03730  ? 597  ARG A CD  1 
ATOM   3250 N  NE  . ARG A 1 394 ? 5.90914   34.16310 12.26083  1.000 49.15198  ? 597  ARG A NE  1 
ATOM   3251 C  CZ  . ARG A 1 394 ? 6.96170   34.26890 13.06070  1.000 59.87040  ? 597  ARG A CZ  1 
ATOM   3252 N  NH1 . ARG A 1 394 ? 7.85242   35.23719 12.90817  1.000 54.84025  ? 597  ARG A NH1 1 
ATOM   3253 N  NH2 . ARG A 1 394 ? 7.13103   33.37397 14.03094  1.000 58.86237  ? 597  ARG A NH2 1 
ATOM   3254 N  N   A TYR A 1 395 ? 4.02659   37.37618 7.20323   0.274 50.12566  ? 598  TYR A N   1 
ATOM   3255 N  N   B TYR A 1 395 ? 3.93389   37.32752 7.10664   0.726 50.12097  ? 598  TYR A N   1 
ATOM   3256 C  CA  A TYR A 1 395 ? 3.86371   38.55105 6.36160   0.274 51.80521  ? 598  TYR A CA  1 
ATOM   3257 C  CA  B TYR A 1 395 ? 3.66777   38.31175 6.07043   0.726 53.63106  ? 598  TYR A CA  1 
ATOM   3258 C  C   A TYR A 1 395 ? 4.26317   39.77337 7.18457   0.274 55.67700  ? 598  TYR A C   1 
ATOM   3259 C  C   B TYR A 1 395 ? 4.19421   39.66993 6.53446   0.726 56.40478  ? 598  TYR A C   1 
ATOM   3260 O  O   A TYR A 1 395 ? 3.73813   39.98534 8.28238   0.274 53.96328  ? 598  TYR A O   1 
ATOM   3261 O  O   B TYR A 1 395 ? 4.15553   39.98892 7.73008   0.726 55.58350  ? 598  TYR A O   1 
ATOM   3262 C  CB  A TYR A 1 395 ? 2.42227   38.65500 5.84206   0.274 51.94672  ? 598  TYR A CB  1 
ATOM   3263 C  CB  B TYR A 1 395 ? 2.16192   38.32423 5.69585   0.726 48.54936  ? 598  TYR A CB  1 
ATOM   3264 C  CG  A TYR A 1 395 ? 1.78385   37.32987 5.43045   0.274 49.08015  ? 598  TYR A CG  1 
ATOM   3265 C  CG  B TYR A 1 395 ? 1.54738   36.96249 5.30313   0.726 52.78480  ? 598  TYR A CG  1 
ATOM   3266 C  CD1 A TYR A 1 395 ? 1.09593   36.55152 6.35443   0.274 44.78032  ? 598  TYR A CD1 1 
ATOM   3267 C  CD1 B TYR A 1 395 ? 0.86444   36.19581 6.23465   0.726 46.65420  ? 598  TYR A CD1 1 
ATOM   3268 C  CD2 A TYR A 1 395 ? 1.84981   36.86477 4.11403   0.274 46.75537  ? 598  TYR A CD2 1 
ATOM   3269 C  CD2 B TYR A 1 395 ? 1.62564   36.46839 3.99296   0.726 38.52396  ? 598  TYR A CD2 1 
ATOM   3270 C  CE1 A TYR A 1 395 ? 0.50558   35.34452 5.98811   0.274 45.15062  ? 598  TYR A CE1 1 
ATOM   3271 C  CE1 B TYR A 1 395 ? 0.29354   34.96121 5.89228   0.726 43.95563  ? 598  TYR A CE1 1 
ATOM   3272 C  CE2 A TYR A 1 395 ? 1.25731   35.65579 3.73959   0.274 44.04149  ? 598  TYR A CE2 1 
ATOM   3273 C  CE2 B TYR A 1 395 ? 1.04178   35.22026 3.62291   0.726 36.40376  ? 598  TYR A CE2 1 
ATOM   3274 C  CZ  A TYR A 1 395 ? 0.58345   34.90475 4.68294   0.274 48.05725  ? 598  TYR A CZ  1 
ATOM   3275 C  CZ  B TYR A 1 395 ? 0.36987   34.47866 4.59399   0.726 47.76392  ? 598  TYR A CZ  1 
ATOM   3276 O  OH  A TYR A 1 395 ? -0.00781  33.70294 4.33044   0.274 41.92768  ? 598  TYR A OH  1 
ATOM   3277 O  OH  B TYR A 1 395 ? -0.21294  33.24059 4.30372   0.726 33.07179  ? 598  TYR A OH  1 
ATOM   3278 N  N   A LYS A 1 396 ? 5.20070   40.56880 6.65823   0.274 53.64071  ? 599  LYS A N   1 
ATOM   3279 N  N   B LYS A 1 396 ? 4.72151   40.45331 5.58239   0.726 51.94836  ? 599  LYS A N   1 
ATOM   3280 C  CA  A LYS A 1 396 ? 5.88703   41.60126 7.43066   0.274 58.06389  ? 599  LYS A CA  1 
ATOM   3281 C  CA  B LYS A 1 396 ? 5.60058   41.57441 5.92330   0.726 57.46554  ? 599  LYS A CA  1 
ATOM   3282 C  C   A LYS A 1 396 ? 5.06501   42.87271 7.63156   0.274 55.59204  ? 599  LYS A C   1 
ATOM   3283 C  C   B LYS A 1 396 ? 4.93132   42.55330 6.88376   0.726 59.67810  ? 599  LYS A C   1 
ATOM   3284 O  O   A LYS A 1 396 ? 5.45621   43.72349 8.44416   0.274 53.19303  ? 599  LYS A O   1 
ATOM   3285 O  O   B LYS A 1 396 ? 5.41228   42.77440 7.99982   0.726 57.98342  ? 599  LYS A O   1 
ATOM   3286 C  CB  A LYS A 1 396 ? 7.21385   41.95705 6.75344   0.274 56.08592  ? 599  LYS A CB  1 
ATOM   3287 C  CB  B LYS A 1 396 ? 6.05341   42.29142 4.65100   0.726 61.04264  ? 599  LYS A CB  1 
ATOM   3288 N  N   A GLY A 1 397 ? 3.95140   43.03537 6.91741   0.274 52.42435  ? 600  GLY A N   1 
ATOM   3289 N  N   B GLY A 1 397 ? 3.81900   43.14705 6.46973   0.726 53.30383  ? 600  GLY A N   1 
ATOM   3290 C  CA  A GLY A 1 397 ? 3.07802   44.17081 7.09333   0.274 54.24989  ? 600  GLY A CA  1 
ATOM   3291 C  CA  B GLY A 1 397 ? 3.15359   44.12398 7.30749   0.726 54.07672  ? 600  GLY A CA  1 
ATOM   3292 C  C   A GLY A 1 397 ? 1.70918   43.74533 7.59561   0.274 55.21728  ? 600  GLY A C   1 
ATOM   3293 C  C   B GLY A 1 397 ? 1.73382   43.74736 7.67052   0.726 55.13437  ? 600  GLY A C   1 
ATOM   3294 O  O   A GLY A 1 397 ? 1.41151   42.55652 7.74427   0.274 55.32735  ? 600  GLY A O   1 
ATOM   3295 O  O   B GLY A 1 397 ? 1.40942   42.56093 7.77699   0.726 55.41627  ? 600  GLY A O   1 
ATOM   3296 N  N   . ASN A 1 398 ? 0.88070   44.75297 7.85813   1.000 55.52129  ? 601  ASN A N   1 
ATOM   3297 C  CA  . ASN A 1 398 ? -0.49204  44.52923 8.30053   1.000 56.74317  ? 601  ASN A CA  1 
ATOM   3298 C  C   . ASN A 1 398 ? -1.24114  43.63352 7.32475   1.000 60.92869  ? 601  ASN A C   1 
ATOM   3299 O  O   . ASN A 1 398 ? -1.35018  43.94999 6.13619   1.000 67.99325  ? 601  ASN A O   1 
ATOM   3300 C  CB  . ASN A 1 398 ? -1.20005  45.88277 8.43528   1.000 58.55362  ? 601  ASN A CB  1 
ATOM   3301 C  CG  . ASN A 1 398 ? -2.35141  45.85758 9.43149   1.000 60.78990  ? 601  ASN A CG  1 
ATOM   3302 O  OD1 . ASN A 1 398 ? -2.46948  44.93914 10.24322  1.000 65.14845  ? 601  ASN A OD1 1 
ATOM   3303 N  ND2 . ASN A 1 398 ? -3.20158  46.88601 9.37881   1.000 61.83745  ? 601  ASN A ND2 1 
ATOM   3304 N  N   . ILE A 1 399 ? -1.74107  42.49538 7.81865   1.000 50.74999  ? 602  ILE A N   1 
ATOM   3305 C  CA  . ILE A 1 399 ? -2.49815  41.60683 6.93983   1.000 59.98526  ? 602  ILE A CA  1 
ATOM   3306 C  C   . ILE A 1 399 ? -3.94536  42.04266 6.78819   1.000 51.11364  ? 602  ILE A C   1 
ATOM   3307 O  O   . ILE A 1 399 ? -4.65060  41.52532 5.91132   1.000 62.25052  ? 602  ILE A O   1 
ATOM   3308 C  CB  . ILE A 1 399 ? -2.45654  40.14088 7.41506   1.000 49.36576  ? 602  ILE A CB  1 
ATOM   3309 C  CG1 . ILE A 1 399 ? -3.15489  39.95332 8.76136   1.000 46.51011  ? 602  ILE A CG1 1 
ATOM   3310 C  CG2 . ILE A 1 399 ? -1.02156  39.63386 7.50916   1.000 44.35675  ? 602  ILE A CG2 1 
ATOM   3311 C  CD1 . ILE A 1 399 ? -3.28820  38.50265 9.13667   1.000 43.45922  ? 602  ILE A CD1 1 
ATOM   3312 N  N   . TYR A 1 400 ? -4.40821  42.96483 7.62219   1.000 53.05000  ? 603  TYR A N   1 
ATOM   3313 C  CA  . TYR A 1 400 ? -5.77718  43.45110 7.55352   1.000 59.34007  ? 603  TYR A CA  1 
ATOM   3314 C  C   . TYR A 1 400 ? -5.91460  44.65897 6.64201   1.000 62.82892  ? 603  TYR A C   1 
ATOM   3315 O  O   . TYR A 1 400 ? -6.94602  44.80578 5.97722   1.000 69.85227  ? 603  TYR A O   1 
ATOM   3316 C  CB  . TYR A 1 400 ? -6.27810  43.76335 8.96638   1.000 55.56871  ? 603  TYR A CB  1 
ATOM   3317 C  CG  . TYR A 1 400 ? -6.28935  42.50725 9.80281   1.000 52.44482  ? 603  TYR A CG  1 
ATOM   3318 C  CD1 . TYR A 1 400 ? -7.33579  41.60563 9.70164   1.000 51.21195  ? 603  TYR A CD1 1 
ATOM   3319 C  CD2 . TYR A 1 400 ? -5.22690  42.19144 10.63957  1.000 50.90289  ? 603  TYR A CD2 1 
ATOM   3320 C  CE1 . TYR A 1 400 ? -7.34427  40.43290 10.43077  1.000 48.55135  ? 603  TYR A CE1 1 
ATOM   3321 C  CE2 . TYR A 1 400 ? -5.22559  41.01889 11.38091  1.000 48.24687  ? 603  TYR A CE2 1 
ATOM   3322 C  CZ  . TYR A 1 400 ? -6.29015  40.14124 11.26828  1.000 47.07663  ? 603  TYR A CZ  1 
ATOM   3323 O  OH  . TYR A 1 400 ? -6.31424  38.95681 11.98088  1.000 44.64816  ? 603  TYR A OH  1 
ATOM   3324 N  N   . GLU A 1 401 ? -4.89191  45.50778 6.58811   1.000 68.86534  ? 604  GLU A N   1 
ATOM   3325 C  CA  . GLU A 1 401 ? -4.79675  46.62576 5.64693   1.000 70.64780  ? 604  GLU A CA  1 
ATOM   3326 C  C   . GLU A 1 401 ? -3.61114  46.34718 4.72358   1.000 62.32169  ? 604  GLU A C   1 
ATOM   3327 O  O   . GLU A 1 401 ? -2.55865  46.98064 4.83755   1.000 70.92910  ? 604  GLU A O   1 
ATOM   3328 C  CB  . GLU A 1 401 ? -4.62949  47.91470 6.38504   1.000 66.13654  ? 604  GLU A CB  1 
ATOM   3329 N  N   A GLU A 1 402 ? -3.78605  45.39042 3.81337   0.793 70.15559  ? 605  GLU A N   1 
ATOM   3330 N  N   B GLU A 1 402 ? -3.78687  45.39759 3.80936   0.207 69.86786  ? 605  GLU A N   1 
ATOM   3331 C  CA  A GLU A 1 402 ? -2.67247  44.93071 2.99325   0.793 62.75976  ? 605  GLU A CA  1 
ATOM   3332 C  CA  B GLU A 1 402 ? -2.67164  44.93049 2.99719   0.207 62.83172  ? 605  GLU A CA  1 
ATOM   3333 C  C   A GLU A 1 402 ? -2.15001  46.05749 2.10783   0.793 67.55518  ? 605  GLU A C   1 
ATOM   3334 C  C   B GLU A 1 402 ? -2.14978  46.03770 2.08819   0.207 67.47789  ? 605  GLU A C   1 
ATOM   3335 O  O   A GLU A 1 402 ? -2.92093  46.82576 1.52391   0.793 65.31959  ? 605  GLU A O   1 
ATOM   3336 O  O   B GLU A 1 402 ? -2.92197  46.76648 1.45810   0.207 65.20765  ? 605  GLU A O   1 
ATOM   3337 C  CB  A GLU A 1 402 ? -3.09525  43.73872 2.13703   0.793 59.35174  ? 605  GLU A CB  1 
ATOM   3338 C  CB  B GLU A 1 402 ? -3.09293  43.72259 2.16402   0.207 59.49980  ? 605  GLU A CB  1 
ATOM   3339 C  CG  A GLU A 1 402 ? -2.95344  42.38031 2.82684   0.793 57.56322  ? 605  GLU A CG  1 
ATOM   3340 C  CG  B GLU A 1 402 ? -3.41737  42.48421 2.98429   0.207 58.85087  ? 605  GLU A CG  1 
ATOM   3341 C  CD  A GLU A 1 402 ? -2.25249  41.35533 1.94976   0.793 56.35101  ? 605  GLU A CD  1 
ATOM   3342 C  CD  B GLU A 1 402 ? -3.87684  41.32217 2.12475   0.207 56.81818  ? 605  GLU A CD  1 
ATOM   3343 O  OE1 A GLU A 1 402 ? -2.85757  40.88185 0.95665   0.793 56.48257  ? 605  GLU A OE1 1 
ATOM   3344 O  OE1 B GLU A 1 402 ? -3.91782  41.47355 0.88400   0.207 62.58068  ? 605  GLU A OE1 1 
ATOM   3345 O  OE2 A GLU A 1 402 ? -1.08071  41.03900 2.24669   0.793 49.61382  ? 605  GLU A OE2 1 
ATOM   3346 O  OE2 B GLU A 1 402 ? -4.20078  40.25808 2.69036   0.207 52.52060  ? 605  GLU A OE2 1 
ATOM   3347 N  N   . ALA A 1 403 ? -0.82667  46.16488 2.03422   1.000 73.41962  ? 606  ALA A N   1 
ATOM   3348 C  CA  . ALA A 1 403 ? -0.16825  47.10308 1.14122   1.000 75.95117  ? 606  ALA A CA  1 
ATOM   3349 C  C   . ALA A 1 403 ? 0.07965   46.42439 -0.20384  1.000 77.76035  ? 606  ALA A C   1 
ATOM   3350 O  O   . ALA A 1 403 ? -0.02595  45.20178 -0.33137  1.000 75.51570  ? 606  ALA A O   1 
ATOM   3351 C  CB  . ALA A 1 403 ? 1.14240   47.59995 1.75431   1.000 65.91357  ? 606  ALA A CB  1 
ATOM   3352 N  N   . GLU A 1 404 ? 0.42317   47.23372 -1.21653  1.000 72.35375  ? 607  GLU A N   1 
ATOM   3353 C  CA  . GLU A 1 404 ? 0.60905   46.71094 -2.57115  1.000 74.44889  ? 607  GLU A CA  1 
ATOM   3354 C  C   . GLU A 1 404 ? 1.60208   45.55422 -2.63101  1.000 63.58569  ? 607  GLU A C   1 
ATOM   3355 O  O   . GLU A 1 404 ? 1.53820   44.73883 -3.55943  1.000 68.24914  ? 607  GLU A O   1 
ATOM   3356 C  CB  . GLU A 1 404 ? 1.06981   47.83033 -3.51075  1.000 70.87176  ? 607  GLU A CB  1 
ATOM   3357 N  N   . LYS A 1 405 ? 2.51765   45.46793 -1.66909  1.000 68.98813  ? 608  LYS A N   1 
ATOM   3358 C  CA  . LYS A 1 405 ? 3.43294   44.33993 -1.54423  1.000 67.17297  ? 608  LYS A CA  1 
ATOM   3359 C  C   . LYS A 1 405 ? 3.46308   43.91838 -0.08572  1.000 66.68681  ? 608  LYS A C   1 
ATOM   3360 O  O   . LYS A 1 405 ? 3.77003   44.73199 0.79070   1.000 71.67677  ? 608  LYS A O   1 
ATOM   3361 C  CB  . LYS A 1 405 ? 4.84152   44.70581 -2.02906  1.000 65.24174  ? 608  LYS A CB  1 
ATOM   3362 N  N   . ASN A 1 406 ? 3.13860   42.65202 0.17523   1.000 56.59431  ? 609  ASN A N   1 
ATOM   3363 C  CA  . ASN A 1 406 ? 3.14587   42.10234 1.51755   1.000 61.83872  ? 609  ASN A CA  1 
ATOM   3364 C  C   . ASN A 1 406 ? 3.60625   40.65280 1.38773   1.000 51.37397  ? 609  ASN A C   1 
ATOM   3365 O  O   . ASN A 1 406 ? 2.82165   39.72480 1.57296   1.000 51.30814  ? 609  ASN A O   1 
ATOM   3366 C  CB  . ASN A 1 406 ? 1.76821   42.21676 2.17013   1.000 65.53864  ? 609  ASN A CB  1 
ATOM   3367 C  CG  . ASN A 1 406 ? 1.78845   41.87218 3.64283   1.000 54.53765  ? 609  ASN A CG  1 
ATOM   3368 O  OD1 . ASN A 1 406 ? 2.83046   41.93500 4.29331   1.000 62.00664  ? 609  ASN A OD1 1 
ATOM   3369 N  ND2 . ASN A 1 406 ? 0.62886   41.51255 4.18122   1.000 58.50170  ? 609  ASN A ND2 1 
ATOM   3370 N  N   . ARG A 1 407 ? 4.89063   40.48013 1.05927   1.000 48.16865  ? 610  ARG A N   1 
ATOM   3371 C  CA  . ARG A 1 407 ? 5.43463   39.17841 0.69052   1.000 53.61898  ? 610  ARG A CA  1 
ATOM   3372 C  C   . ARG A 1 407 ? 5.23876   38.15267 1.80030   1.000 43.54595  ? 610  ARG A C   1 
ATOM   3373 O  O   . ARG A 1 407 ? 5.08071   38.48841 2.98177   1.000 47.45286  ? 610  ARG A O   1 
ATOM   3374 C  CB  . ARG A 1 407 ? 6.92933   39.27056 0.37475   1.000 53.22539  ? 610  ARG A CB  1 
ATOM   3375 C  CG  . ARG A 1 407 ? 7.30995   40.32839 -0.65005  1.000 50.14708  ? 610  ARG A CG  1 
ATOM   3376 C  CD  . ARG A 1 407 ? 6.45322   40.22859 -1.89431  1.000 49.54477  ? 610  ARG A CD  1 
ATOM   3377 N  NE  . ARG A 1 407 ? 6.70038   39.01202 -2.66090  1.000 52.69931  ? 610  ARG A NE  1 
ATOM   3378 C  CZ  . ARG A 1 407 ? 7.53516   38.94602 -3.68831  1.000 54.07033  ? 610  ARG A CZ  1 
ATOM   3379 N  NH1 . ARG A 1 407 ? 8.26519   39.98820 -4.05033  1.000 59.42772  ? 610  ARG A NH1 1 
ATOM   3380 N  NH2 . ARG A 1 407 ? 7.63921   37.80762 -4.36955  1.000 48.30686  ? 610  ARG A NH2 1 
ATOM   3381 N  N   . THR A 1 408 ? 5.30751   36.88045 1.39326   1.000 48.86317  ? 611  THR A N   1 
ATOM   3382 C  CA  . THR A 1 408 ? 5.08615   35.71523 2.23912   1.000 41.55100  ? 611  THR A CA  1 
ATOM   3383 C  C   . THR A 1 408 ? 6.44917   35.17580 2.66558   1.000 36.71393  ? 611  THR A C   1 
ATOM   3384 O  O   . THR A 1 408 ? 7.03686   34.31627 1.99974   1.000 41.52183  ? 611  THR A O   1 
ATOM   3385 C  CB  . THR A 1 408 ? 4.26481   34.67060 1.46884   1.000 35.95699  ? 611  THR A CB  1 
ATOM   3386 O  OG1 . THR A 1 408 ? 3.08675   35.31569 0.94217   1.000 39.97534  ? 611  THR A OG1 1 
ATOM   3387 C  CG2 . THR A 1 408 ? 3.88636   33.51928 2.34357   1.000 43.50462  ? 611  THR A CG2 1 
ATOM   3388 N  N   . TYR A 1 409 ? 6.94012   35.66998 3.79261   1.000 38.34171  ? 612  TYR A N   1 
ATOM   3389 C  CA  . TYR A 1 409 ? 8.22156   35.26364 4.34314   1.000 45.17262  ? 612  TYR A CA  1 
ATOM   3390 C  C   . TYR A 1 409 ? 8.10344   33.90196 5.02257   1.000 45.97807  ? 612  TYR A C   1 
ATOM   3391 O  O   . TYR A 1 409 ? 7.01453   33.46598 5.40474   1.000 38.72570  ? 612  TYR A O   1 
ATOM   3392 C  CB  . TYR A 1 409 ? 8.73557   36.32151 5.32964   1.000 39.66553  ? 612  TYR A CB  1 
ATOM   3393 C  CG  . TYR A 1 409 ? 9.28048   37.52885 4.61050   1.000 47.64375  ? 612  TYR A CG  1 
ATOM   3394 C  CD1 . TYR A 1 409 ? 10.60499  37.57117 4.18223   1.000 53.15966  ? 612  TYR A CD1 1 
ATOM   3395 C  CD2 . TYR A 1 409 ? 8.46336   38.61147 4.31443   1.000 46.58991  ? 612  TYR A CD2 1 
ATOM   3396 C  CE1 . TYR A 1 409 ? 11.10496  38.68099 3.49533   1.000 51.24467  ? 612  TYR A CE1 1 
ATOM   3397 C  CE2 . TYR A 1 409 ? 8.95462   39.71482 3.62583   1.000 54.30140  ? 612  TYR A CE2 1 
ATOM   3398 C  CZ  . TYR A 1 409 ? 10.27234  39.73766 3.22023   1.000 48.06099  ? 612  TYR A CZ  1 
ATOM   3399 O  OH  . TYR A 1 409 ? 10.76059  40.83940 2.54613   1.000 60.92286  ? 612  TYR A OH  1 
ATOM   3400 N  N   . MET A 1 410 ? 9.25282   33.24110 5.17552   1.000 44.05307  ? 613  MET A N   1 
ATOM   3401 C  CA  . MET A 1 410 ? 9.35826   31.90140 5.74419   1.000 39.61360  ? 613  MET A CA  1 
ATOM   3402 C  C   . MET A 1 410 ? 9.97006   31.95324 7.14262   1.000 46.56719  ? 613  MET A C   1 
ATOM   3403 O  O   . MET A 1 410 ? 11.00410  32.59627 7.35113   1.000 42.72755  ? 613  MET A O   1 
ATOM   3404 C  CB  . MET A 1 410 ? 10.21484  31.01302 4.84935   1.000 42.27735  ? 613  MET A CB  1 
ATOM   3405 C  CG  . MET A 1 410 ? 9.62559   30.72647 3.48059   1.000 37.33334  ? 613  MET A CG  1 
ATOM   3406 S  SD  . MET A 1 410 ? 8.10920   29.78792 3.55898   1.000 39.59971  ? 613  MET A SD  1 
ATOM   3407 C  CE  . MET A 1 410 ? 6.81404   31.02457 3.58012   1.000 35.68542  ? 613  MET A CE  1 
ATOM   3408 N  N   . PHE A 1 411 ? 9.34006   31.27430 8.09811   1.000 46.11206  ? 614  PHE A N   1 
ATOM   3409 C  CA  . PHE A 1 411 ? 9.98441   30.99064 9.37532   1.000 41.84721  ? 614  PHE A CA  1 
ATOM   3410 C  C   . PHE A 1 411 ? 10.59166  29.59424 9.28520   1.000 47.23375  ? 614  PHE A C   1 
ATOM   3411 O  O   . PHE A 1 411 ? 9.93139   28.65082 8.83306   1.000 39.43753  ? 614  PHE A O   1 
ATOM   3412 C  CB  . PHE A 1 411 ? 8.99547   31.07928 10.54043  1.000 37.48228  ? 614  PHE A CB  1 
ATOM   3413 C  CG  . PHE A 1 411 ? 9.64274   30.94600 11.88809  1.000 44.88557  ? 614  PHE A CG  1 
ATOM   3414 C  CD1 . PHE A 1 411 ? 10.27242  32.03651 12.48098  1.000 49.38735  ? 614  PHE A CD1 1 
ATOM   3415 C  CD2 . PHE A 1 411 ? 9.63312   29.73699 12.56503  1.000 41.36603  ? 614  PHE A CD2 1 
ATOM   3416 C  CE1 . PHE A 1 411 ? 10.87633  31.92526 13.72857  1.000 43.34992  ? 614  PHE A CE1 1 
ATOM   3417 C  CE2 . PHE A 1 411 ? 10.23772  29.62036 13.82307  1.000 39.26161  ? 614  PHE A CE2 1 
ATOM   3418 C  CZ  . PHE A 1 411 ? 10.85846  30.71538 14.40311  1.000 35.82823  ? 614  PHE A CZ  1 
ATOM   3419 N  N   . ASN A 1 412 ? 11.85885  29.47300 9.66038   1.000 35.62198  ? 615  ASN A N   1 
ATOM   3420 C  CA  . ASN A 1 412 ? 12.63226  28.26281 9.38896   1.000 45.77896  ? 615  ASN A CA  1 
ATOM   3421 C  C   . ASN A 1 412 ? 12.75453  27.51383 10.70541  1.000 41.92796  ? 615  ASN A C   1 
ATOM   3422 O  O   . ASN A 1 412 ? 13.65436  27.77352 11.50471  1.000 41.98077  ? 615  ASN A O   1 
ATOM   3423 C  CB  . ASN A 1 412 ? 14.00146  28.59262 8.79699   1.000 48.23450  ? 615  ASN A CB  1 
ATOM   3424 C  CG  . ASN A 1 412 ? 14.76919  27.35189 8.37004   1.000 53.76975  ? 615  ASN A CG  1 
ATOM   3425 O  OD1 . ASN A 1 412 ? 14.57843  26.26405 8.91739   1.000 49.24445  ? 615  ASN A OD1 1 
ATOM   3426 N  ND2 . ASN A 1 412 ? 15.65382  27.51619 7.39309   1.000 44.77126  ? 615  ASN A ND2 1 
ATOM   3427 N  N   . TYR A 1 413 ? 11.83528  26.57829 10.93551  1.000 32.14835  ? 616  TYR A N   1 
ATOM   3428 C  CA  . TYR A 1 413 ? 11.81798  25.94514 12.24425  1.000 28.58781  ? 616  TYR A CA  1 
ATOM   3429 C  C   . TYR A 1 413 ? 13.07266  25.11069 12.46666  1.000 33.53752  ? 616  TYR A C   1 
ATOM   3430 O  O   . TYR A 1 413 ? 13.56291  25.02650 13.60106  1.000 36.23941  ? 616  TYR A O   1 
ATOM   3431 C  CB  . TYR A 1 413 ? 10.54358  25.10862 12.39378  1.000 24.63022  ? 616  TYR A CB  1 
ATOM   3432 C  CG  . TYR A 1 413 ? 9.30457   25.95707 12.61298  1.000 27.49779  ? 616  TYR A CG  1 
ATOM   3433 C  CD1 . TYR A 1 413 ? 9.03661   26.51772 13.86178  1.000 28.12313  ? 616  TYR A CD1 1 
ATOM   3434 C  CD2 . TYR A 1 413 ? 8.39652   26.18818 11.58902  1.000 26.64131  ? 616  TYR A CD2 1 
ATOM   3435 C  CE1 . TYR A 1 413 ? 7.90340   27.28900 14.07548  1.000 29.85598  ? 616  TYR A CE1 1 
ATOM   3436 C  CE2 . TYR A 1 413 ? 7.26150   26.96048 11.79916  1.000 27.03981  ? 616  TYR A CE2 1 
ATOM   3437 C  CZ  . TYR A 1 413 ? 7.02242   27.50354 13.04079  1.000 28.51638  ? 616  TYR A CZ  1 
ATOM   3438 O  OH  . TYR A 1 413 ? 5.89855   28.26440 13.24478  1.000 29.98066  ? 616  TYR A OH  1 
ATOM   3439 N  N   . ALA A 1 414 ? 13.63129  24.52835 11.39803  1.000 29.64049  ? 617  ALA A N   1 
ATOM   3440 C  CA  . ALA A 1 414 ? 14.83093  23.71034 11.55358  1.000 35.97751  ? 617  ALA A CA  1 
ATOM   3441 C  C   . ALA A 1 414 ? 16.02084  24.52973 12.03509  1.000 37.98387  ? 617  ALA A C   1 
ATOM   3442 O  O   . ALA A 1 414 ? 16.87811  24.00695 12.75921  1.000 38.38211  ? 617  ALA A O   1 
ATOM   3443 C  CB  . ALA A 1 414 ? 15.16271  23.00791 10.23734  1.000 37.26001  ? 617  ALA A CB  1 
ATOM   3444 N  N   . LEU A 1 415 ? 16.09232  25.80555 11.65293  1.000 36.86233  ? 618  LEU A N   1 
ATOM   3445 C  CA  . LEU A 1 415 ? 17.10843  26.71420 12.15622  1.000 39.90551  ? 618  LEU A CA  1 
ATOM   3446 C  C   . LEU A 1 415 ? 16.60920  27.56579 13.31386  1.000 39.26287  ? 618  LEU A C   1 
ATOM   3447 O  O   . LEU A 1 415 ? 17.40361  28.30173 13.89851  1.000 48.37878  ? 618  LEU A O   1 
ATOM   3448 C  CB  . LEU A 1 415 ? 17.61111  27.63259 11.03398  1.000 39.92648  ? 618  LEU A CB  1 
ATOM   3449 C  CG  . LEU A 1 415 ? 18.05899  26.98816 9.71963   1.000 45.59384  ? 618  LEU A CG  1 
ATOM   3450 C  CD1 . LEU A 1 415 ? 18.54704  28.06102 8.75667   1.000 51.57662  ? 618  LEU A CD1 1 
ATOM   3451 C  CD2 . LEU A 1 415 ? 19.13670  25.94921 9.94538   1.000 46.58414  ? 618  LEU A CD2 1 
ATOM   3452 N  N   . SER A 1 416 ? 15.31603  27.47759 13.64662  1.000 47.21037  ? 619  SER A N   1 
ATOM   3453 C  CA  . SER A 1 416 ? 14.70603  28.20543 14.76397  1.000 38.96535  ? 619  SER A CA  1 
ATOM   3454 C  C   . SER A 1 416 ? 14.83762  29.71708 14.59980  1.000 54.02472  ? 619  SER A C   1 
ATOM   3455 O  O   . SER A 1 416 ? 15.10330  30.44211 15.56256  1.000 50.89406  ? 619  SER A O   1 
ATOM   3456 C  CB  . SER A 1 416 ? 15.28991  27.77051 16.11696  1.000 47.67311  ? 619  SER A CB  1 
ATOM   3457 O  OG  . SER A 1 416 ? 14.88248  26.45622 16.45073  1.000 45.52933  ? 619  SER A OG  1 
ATOM   3458 N  N   . LYS A 1 417 ? 14.63668  30.21018 13.38093  1.000 45.70756  ? 620  LYS A N   1 
ATOM   3459 C  CA  . LYS A 1 417 ? 14.83162  31.63471 13.15568  1.000 46.63320  ? 620  LYS A CA  1 
ATOM   3460 C  C   . LYS A 1 417 ? 14.01282  32.07054 11.95449  1.000 52.42829  ? 620  LYS A C   1 
ATOM   3461 O  O   . LYS A 1 417 ? 13.79952  31.27604 11.02619  1.000 46.22761  ? 620  LYS A O   1 
ATOM   3462 C  CB  . LYS A 1 417 ? 16.31647  31.96125 12.93552  1.000 57.39145  ? 620  LYS A CB  1 
ATOM   3463 C  CG  . LYS A 1 417 ? 16.88302  31.46607 11.60920  1.000 49.12944  ? 620  LYS A CG  1 
ATOM   3464 C  CD  . LYS A 1 417 ? 18.40667  31.43209 11.65584  1.000 57.47159  ? 620  LYS A CD  1 
ATOM   3465 C  CE  . LYS A 1 417 ? 19.01575  32.01350 10.39608  1.000 59.49986  ? 620  LYS A CE  1 
ATOM   3466 N  NZ  . LYS A 1 417 ? 18.89276  33.50197 10.37292  1.000 75.42516  ? 620  LYS A NZ  1 
ATOM   3467 N  N   . PRO A 1 418 ? 13.52612  33.30826 11.94541  1.000 48.73230  ? 621  PRO A N   1 
ATOM   3468 C  CA  . PRO A 1 418 ? 13.03602  33.88692 10.69494  1.000 46.21449  ? 621  PRO A CA  1 
ATOM   3469 C  C   . PRO A 1 418 ? 14.20618  34.10603 9.75309   1.000 56.60273  ? 621  PRO A C   1 
ATOM   3470 O  O   . PRO A 1 418 ? 15.36057  34.23342 10.16837  1.000 51.52888  ? 621  PRO A O   1 
ATOM   3471 C  CB  . PRO A 1 418 ? 12.40402  35.21933 11.12318  1.000 49.99752  ? 621  PRO A CB  1 
ATOM   3472 C  CG  . PRO A 1 418 ? 12.32449  35.16055 12.63528  1.000 63.61813  ? 621  PRO A CG  1 
ATOM   3473 C  CD  . PRO A 1 418 ? 13.43822  34.25738 13.06651  1.000 52.89435  ? 621  PRO A CD  1 
ATOM   3474 N  N   . GLU A 1 419 ? 13.89560  34.12370 8.46309   1.000 58.20706  ? 622  GLU A N   1 
ATOM   3475 C  CA  . GLU A 1 419 ? 14.87979  34.44062 7.44321   1.000 53.70813  ? 622  GLU A CA  1 
ATOM   3476 C  C   . GLU A 1 419 ? 14.24479  35.39136 6.44875   1.000 43.84545  ? 622  GLU A C   1 
ATOM   3477 O  O   . GLU A 1 419 ? 13.03940  35.33370 6.19816   1.000 44.98405  ? 622  GLU A O   1 
ATOM   3478 C  CB  . GLU A 1 419 ? 15.38984  33.18269 6.73526   1.000 52.43697  ? 622  GLU A CB  1 
ATOM   3479 C  CG  . GLU A 1 419 ? 16.20243  32.27678 7.65119   1.000 57.25326  ? 622  GLU A CG  1 
ATOM   3480 C  CD  . GLU A 1 419 ? 16.62858  30.98365 6.98046   1.000 57.81326  ? 622  GLU A CD  1 
ATOM   3481 O  OE1 . GLU A 1 419 ? 15.74346  30.18183 6.57997   1.000 48.42254  ? 622  GLU A OE1 1 
ATOM   3482 O  OE2 . GLU A 1 419 ? 17.85837  30.78330 6.85598   1.000 54.19961  ? 622  GLU A OE2 1 
ATOM   3483 N  N   . ASN A 1 420 ? 15.06198  36.27804 5.88892   1.000 50.71447  ? 623  ASN A N   1 
ATOM   3484 C  CA  . ASN A 1 420 ? 14.56391  37.16729 4.84938   1.000 55.28992  ? 623  ASN A CA  1 
ATOM   3485 C  C   . ASN A 1 420 ? 14.39558  36.39312 3.55186   1.000 56.91576  ? 623  ASN A C   1 
ATOM   3486 O  O   . ASN A 1 420 ? 14.93116  36.77995 2.50793   1.000 59.77750  ? 623  ASN A O   1 
ATOM   3487 C  CB  . ASN A 1 420 ? 15.49153  38.35938 4.65528   1.000 55.53729  ? 623  ASN A CB  1 
ATOM   3488 C  CG  . ASN A 1 420 ? 15.01180  39.57386 5.40345   1.000 71.08622  ? 623  ASN A CG  1 
ATOM   3489 O  OD1 . ASN A 1 420 ? 15.44885  39.84454 6.52363   1.000 72.26210  ? 623  ASN A OD1 1 
ATOM   3490 N  ND2 . ASN A 1 420 ? 14.08122  40.30318 4.79966   1.000 77.63340  ? 623  ASN A ND2 1 
ATOM   3491 N  N   . ILE A 1 421 ? 13.64496  35.30182 3.62445   1.000 42.06530  ? 624  ILE A N   1 
ATOM   3492 C  CA  . ILE A 1 421 ? 13.36715  34.42188 2.49169   1.000 51.91239  ? 624  ILE A CA  1 
ATOM   3493 C  C   . ILE A 1 421 ? 11.86496  34.43144 2.26639   1.000 50.01343  ? 624  ILE A C   1 
ATOM   3494 O  O   . ILE A 1 421 ? 11.09668  34.16082 3.19634   1.000 46.10549  ? 624  ILE A O   1 
ATOM   3495 C  CB  . ILE A 1 421 ? 13.87158  32.99343 2.74207   1.000 58.93248  ? 624  ILE A CB  1 
ATOM   3496 C  CG1 . ILE A 1 421 ? 15.40039  32.97298 2.81870   1.000 53.39056  ? 624  ILE A CG1 1 
ATOM   3497 C  CG2 . ILE A 1 421 ? 13.34263  32.04289 1.67397   1.000 49.69232  ? 624  ILE A CG2 1 
ATOM   3498 C  CD1 . ILE A 1 421 ? 15.97148  31.61512 3.15410   1.000 56.10662  ? 624  ILE A CD1 1 
ATOM   3499 N  N   . TYR A 1 422 ? 11.44118  34.78147 1.05354   1.000 46.55229  ? 625  TYR A N   1 
ATOM   3500 C  CA  . TYR A 1 422 ? 10.02149  34.81325 0.74612   1.000 48.87989  ? 625  TYR A CA  1 
ATOM   3501 C  C   . TYR A 1 422 ? 9.72905   34.00484 -0.51210  1.000 50.36660  ? 625  TYR A C   1 
ATOM   3502 O  O   . TYR A 1 422 ? 10.62173  33.63637 -1.27780  1.000 50.25968  ? 625  TYR A O   1 
ATOM   3503 C  CB  . TYR A 1 422 ? 9.51594   36.24242 0.57023   1.000 41.49470  ? 625  TYR A CB  1 
ATOM   3504 C  CG  . TYR A 1 422 ? 10.23293  36.97442 -0.53697  1.000 48.26057  ? 625  TYR A CG  1 
ATOM   3505 C  CD1 . TYR A 1 422 ? 11.38558  37.70086 -0.27817  1.000 44.84314  ? 625  TYR A CD1 1 
ATOM   3506 C  CD2 . TYR A 1 422 ? 9.77547   36.90265 -1.85207  1.000 50.74222  ? 625  TYR A CD2 1 
ATOM   3507 C  CE1 . TYR A 1 422 ? 12.05811  38.36454 -1.30735  1.000 49.85844  ? 625  TYR A CE1 1 
ATOM   3508 C  CE2 . TYR A 1 422 ? 10.43681  37.55351 -2.87548  1.000 49.08945  ? 625  TYR A CE2 1 
ATOM   3509 C  CZ  . TYR A 1 422 ? 11.57343  38.28268 -2.59661  1.000 56.03723  ? 625  TYR A CZ  1 
ATOM   3510 O  OH  . TYR A 1 422 ? 12.22373  38.92453 -3.62280  1.000 56.93880  ? 625  TYR A OH  1 
ATOM   3511 N  N   . ILE A 1 423 ? 8.44319   33.75539 -0.71395  1.000 41.60977  ? 626  ILE A N   1 
ATOM   3512 C  CA  . ILE A 1 423 ? 7.94986   32.95518 -1.82952  1.000 38.26567  ? 626  ILE A CA  1 
ATOM   3513 C  C   . ILE A 1 423 ? 7.71930   33.88903 -3.01110  1.000 49.75767  ? 626  ILE A C   1 
ATOM   3514 O  O   . ILE A 1 423 ? 6.79118   34.70257 -3.00061  1.000 46.31841  ? 626  ILE A O   1 
ATOM   3515 C  CB  . ILE A 1 423 ? 6.66552   32.22316 -1.43806  1.000 33.13759  ? 626  ILE A CB  1 
ATOM   3516 C  CG1 . ILE A 1 423 ? 6.96450   31.24740 -0.28541  1.000 32.36438  ? 626  ILE A CG1 1 
ATOM   3517 C  CG2 . ILE A 1 423 ? 6.05509   31.51683 -2.64162  1.000 37.95200  ? 626  ILE A CG2 1 
ATOM   3518 C  CD1 . ILE A 1 423 ? 5.82417   30.33372 0.10401   1.000 37.97346  ? 626  ILE A CD1 1 
ATOM   3519 N  N   A ASP A 1 424 ? 8.56655   33.76803 -4.03299  0.653 41.94106  ? 627  ASP A N   1 
ATOM   3520 N  N   B ASP A 1 424 ? 8.56624   33.78634 -4.03903  0.347 42.03780  ? 627  ASP A N   1 
ATOM   3521 C  CA  A ASP A 1 424 ? 8.41164   34.59173 -5.22182  0.653 44.75132  ? 627  ASP A CA  1 
ATOM   3522 C  CA  B ASP A 1 424 ? 8.35993   34.62958 -5.21137  0.347 44.76413  ? 627  ASP A CA  1 
ATOM   3523 C  C   A ASP A 1 424 ? 7.29566   34.07946 -6.12314  0.653 41.76758  ? 627  ASP A C   1 
ATOM   3524 C  C   B ASP A 1 424 ? 7.25943   34.08606 -6.11203  0.347 41.86384  ? 627  ASP A C   1 
ATOM   3525 O  O   A ASP A 1 424 ? 6.64269   34.87247 -6.81044  0.653 44.74022  ? 627  ASP A O   1 
ATOM   3526 O  O   B ASP A 1 424 ? 6.58515   34.86358 -6.79650  0.347 44.74635  ? 627  ASP A O   1 
ATOM   3527 C  CB  A ASP A 1 424 ? 9.73180   34.64654 -5.98444  0.653 47.06408  ? 627  ASP A CB  1 
ATOM   3528 C  CB  B ASP A 1 424 ? 9.65619   34.78463 -6.00753  0.347 47.04488  ? 627  ASP A CB  1 
ATOM   3529 C  CG  A ASP A 1 424 ? 9.74734   35.72399 -7.02233  0.653 51.29581  ? 627  ASP A CG  1 
ATOM   3530 C  CG  B ASP A 1 424 ? 9.69847   36.07975 -6.79670  0.347 53.23766  ? 627  ASP A CG  1 
ATOM   3531 O  OD1 A ASP A 1 424 ? 9.66266   36.91567 -6.64308  0.653 56.83730  ? 627  ASP A OD1 1 
ATOM   3532 O  OD1 B ASP A 1 424 ? 8.89206   36.99019 -6.49742  0.347 52.17150  ? 627  ASP A OD1 1 
ATOM   3533 O  OD2 A ASP A 1 424 ? 9.83174   35.38370 -8.21962  0.653 49.01729  ? 627  ASP A OD2 1 
ATOM   3534 O  OD2 B ASP A 1 424 ? 10.53217  36.19092 -7.72137  0.347 58.60985  ? 627  ASP A OD2 1 
ATOM   3535 N  N   . GLY A 1 425 ? 7.05364   32.77620 -6.12281  1.000 37.58243  ? 628  GLY A N   1 
ATOM   3536 C  CA  . GLY A 1 425 ? 5.97711   32.21961 -6.91465  1.000 38.22783  ? 628  GLY A CA  1 
ATOM   3537 C  C   . GLY A 1 425 ? 5.99015   30.70825 -6.87413  1.000 36.74113  ? 628  GLY A C   1 
ATOM   3538 O  O   . GLY A 1 425 ? 6.83133   30.08303 -6.21879  1.000 32.86560  ? 628  GLY A O   1 
ATOM   3539 N  N   . LEU A 1 426 ? 5.04137   30.12600 -7.61153  1.000 33.50717  ? 629  LEU A N   1 
ATOM   3540 C  CA  . LEU A 1 426 ? 4.89717   28.68095 -7.69320  1.000 32.21737  ? 629  LEU A CA  1 
ATOM   3541 C  C   . LEU A 1 426 ? 5.05761   28.22508 -9.13331  1.000 33.29814  ? 629  LEU A C   1 
ATOM   3542 O  O   . LEU A 1 426 ? 4.60560   28.89972 -10.05520 1.000 34.95397  ? 629  LEU A O   1 
ATOM   3543 C  CB  . LEU A 1 426 ? 3.52456   28.20191 -7.19911  1.000 30.49492  ? 629  LEU A CB  1 
ATOM   3544 C  CG  . LEU A 1 426 ? 3.27567   27.88705 -5.71684  1.000 38.48821  ? 629  LEU A CG  1 
ATOM   3545 C  CD1 . LEU A 1 426 ? 3.74788   28.99059 -4.80199  1.000 40.79345  ? 629  LEU A CD1 1 
ATOM   3546 C  CD2 . LEU A 1 426 ? 1.79271   27.62748 -5.52180  1.000 34.84597  ? 629  LEU A CD2 1 
ATOM   3547 N  N   . THR A 1 427 ? 5.68177   27.06736 -9.30459  1.000 31.11760  ? 630  THR A N   1 
ATOM   3548 C  CA  . THR A 1 427 ? 5.60513   26.29156 -10.53718 1.000 31.98468  ? 630  THR A CA  1 
ATOM   3549 C  C   . THR A 1 427 ? 4.78212   25.05237 -10.21997 1.000 28.51015  ? 630  THR A C   1 
ATOM   3550 O  O   . THR A 1 427 ? 5.11678   24.30531 -9.29665  1.000 27.93738  ? 630  THR A O   1 
ATOM   3551 C  CB  . THR A 1 427 ? 6.99597   25.91356 -11.04230 1.000 31.08667  ? 630  THR A CB  1 
ATOM   3552 O  OG1 . THR A 1 427 ? 7.70160   27.11103 -11.39623 1.000 34.61834  ? 630  THR A OG1 1 
ATOM   3553 C  CG2 . THR A 1 427 ? 6.89721   24.98081 -12.28138 1.000 30.90179  ? 630  THR A CG2 1 
ATOM   3554 N  N   . THR A 1 428 ? 3.69572   24.84889 -10.95866 1.000 28.62964  ? 631  THR A N   1 
ATOM   3555 C  CA  . THR A 1 428 ? 2.75153   23.79525 -10.63507 1.000 28.80048  ? 631  THR A CA  1 
ATOM   3556 C  C   . THR A 1 428 ? 2.69678   22.78031 -11.75995 1.000 30.75445  ? 631  THR A C   1 
ATOM   3557 O  O   . THR A 1 428 ? 2.97171   23.10767 -12.91932 1.000 29.13042  ? 631  THR A O   1 
ATOM   3558 C  CB  . THR A 1 428 ? 1.35978   24.35257 -10.38533 1.000 30.27931  ? 631  THR A CB  1 
ATOM   3559 O  OG1 . THR A 1 428 ? 0.90795   25.02623 -11.56105 1.000 36.60301  ? 631  THR A OG1 1 
ATOM   3560 C  CG2 . THR A 1 428 ? 1.38989   25.33758 -9.19899  1.000 37.03953  ? 631  THR A CG2 1 
ATOM   3561 N  N   . LEU A 1 429 ? 2.35621   21.54179 -11.39935 1.000 29.46790  ? 632  LEU A N   1 
ATOM   3562 C  CA  . LEU A 1 429 ? 2.23217   20.45898 -12.37222 1.000 27.32093  ? 632  LEU A CA  1 
ATOM   3563 C  C   . LEU A 1 429 ? 0.85954   19.82128 -12.23748 1.000 27.45092  ? 632  LEU A C   1 
ATOM   3564 O  O   . LEU A 1 429 ? 0.52351   19.26329 -11.18514 1.000 31.65525  ? 632  LEU A O   1 
ATOM   3565 C  CB  . LEU A 1 429 ? 3.33818   19.42233 -12.20339 1.000 24.68524  ? 632  LEU A CB  1 
ATOM   3566 C  CG  . LEU A 1 429 ? 3.29249   18.23333 -13.17336 1.000 25.88887  ? 632  LEU A CG  1 
ATOM   3567 C  CD1 . LEU A 1 429 ? 3.47071   18.68882 -14.62837 1.000 28.12726  ? 632  LEU A CD1 1 
ATOM   3568 C  CD2 . LEU A 1 429 ? 4.33629   17.16755 -12.79305 1.000 26.31715  ? 632  LEU A CD2 1 
ATOM   3569 N  N   . ASP A 1 430 ? 0.08218   19.89756 -13.31085 1.000 27.70812  ? 633  ASP A N   1 
ATOM   3570 C  CA  . ASP A 1 430 ? -1.27043  19.37839 -13.37019 1.000 28.82087  ? 633  ASP A CA  1 
ATOM   3571 C  C   . ASP A 1 430 ? -1.23865  17.95196 -13.91337 1.000 33.17416  ? 633  ASP A C   1 
ATOM   3572 O  O   . ASP A 1 430 ? -0.32733  17.57844 -14.65665 1.000 27.84319  ? 633  ASP A O   1 
ATOM   3573 C  CB  . ASP A 1 430 ? -2.12292  20.28184 -14.26484 1.000 30.92186  ? 633  ASP A CB  1 
ATOM   3574 C  CG  . ASP A 1 430 ? -3.58828  19.92698 -14.24633 1.000 37.26118  ? 633  ASP A CG  1 
ATOM   3575 O  OD1 . ASP A 1 430 ? -4.31786  20.43902 -13.37383 1.000 36.04346  ? 633  ASP A OD1 1 
ATOM   3576 O  OD2 . ASP A 1 430 ? -4.02301  19.16565 -15.13312 1.000 35.68753  ? 633  ASP A OD2 1 
ATOM   3577 N  N   . LYS A 1 431 ? -2.22996  17.14947 -13.50818 1.000 26.36658  ? 634  LYS A N   1 
ATOM   3578 C  CA  . LYS A 1 431 ? -2.32279  15.76990 -14.00076 1.000 27.80663  ? 634  LYS A CA  1 
ATOM   3579 C  C   . LYS A 1 431 ? -2.42921  15.71068 -15.51979 1.000 29.74590  ? 634  LYS A C   1 
ATOM   3580 O  O   . LYS A 1 431 ? -1.99661  14.72283 -16.12649 1.000 29.60745  ? 634  LYS A O   1 
ATOM   3581 C  CB  . LYS A 1 431 ? -3.53418  15.07405 -13.38166 1.000 35.66824  ? 634  LYS A CB  1 
ATOM   3582 C  CG  . LYS A 1 431 ? -3.52321  13.55634 -13.43868 1.000 37.55357  ? 634  LYS A CG  1 
ATOM   3583 C  CD  . LYS A 1 431 ? -4.81735  12.98713 -12.85073 1.000 48.45819  ? 634  LYS A CD  1 
ATOM   3584 C  CE  . LYS A 1 431 ? -4.82535  11.45481 -12.77782 1.000 44.22714  ? 634  LYS A CE  1 
ATOM   3585 N  NZ  . LYS A 1 431 ? -4.99578  10.80226 -14.11072 1.000 45.19982  ? 634  LYS A NZ  1 
ATOM   3586 N  N   . GLY A 1 432 ? -3.01391  16.72880 -16.14727 1.000 28.87097  ? 635  GLY A N   1 
ATOM   3587 C  CA  . GLY A 1 432 ? -3.22286  16.69434 -17.59051 1.000 30.73930  ? 635  GLY A CA  1 
ATOM   3588 C  C   . GLY A 1 432 ? -4.29818  15.71999 -18.01952 1.000 34.26290  ? 635  GLY A C   1 
ATOM   3589 O  O   . GLY A 1 432 ? -4.14855  15.05947 -19.05739 1.000 32.75317  ? 635  GLY A O   1 
ATOM   3590 N  N   A GLU A 1 433 ? -5.40073  15.64271 -17.26688 0.499 34.39056  ? 636  GLU A N   1 
ATOM   3591 N  N   B GLU A 1 433 ? -5.39168  15.63145 -17.25652 0.501 34.37738  ? 636  GLU A N   1 
ATOM   3592 C  CA  A GLU A 1 433 ? -6.42999  14.63595 -17.52968 0.499 39.44907  ? 636  GLU A CA  1 
ATOM   3593 C  CA  B GLU A 1 433 ? -6.39741  14.59862 -17.49944 0.501 39.47168  ? 636  GLU A CA  1 
ATOM   3594 C  C   A GLU A 1 433 ? -7.04899  14.79776 -18.91609 0.499 40.35216  ? 636  GLU A C   1 
ATOM   3595 C  C   B GLU A 1 433 ? -7.07037  14.75985 -18.86026 0.501 40.31944  ? 636  GLU A C   1 
ATOM   3596 O  O   A GLU A 1 433 ? -7.18679  13.81856 -19.66063 0.499 39.21809  ? 636  GLU A O   1 
ATOM   3597 O  O   B GLU A 1 433 ? -7.28948  13.76962 -19.57034 0.501 39.30968  ? 636  GLU A O   1 
ATOM   3598 C  CB  A GLU A 1 433 ? -7.51142  14.70256 -16.44827 0.499 39.78477  ? 636  GLU A CB  1 
ATOM   3599 C  CB  B GLU A 1 433 ? -7.43466  14.61391 -16.37358 0.501 39.88066  ? 636  GLU A CB  1 
ATOM   3600 C  CG  A GLU A 1 433 ? -8.56396  13.60635 -16.54065 0.499 40.55796  ? 636  GLU A CG  1 
ATOM   3601 C  CG  B GLU A 1 433 ? -7.70442  13.24287 -15.77214 0.501 44.85630  ? 636  GLU A CG  1 
ATOM   3602 C  CD  A GLU A 1 433 ? -8.04276  12.24143 -16.12031 0.499 43.25254  ? 636  GLU A CD  1 
ATOM   3603 C  CD  B GLU A 1 433 ? -7.94594  13.28480 -14.27179 0.501 44.90227  ? 636  GLU A CD  1 
ATOM   3604 O  OE1 A GLU A 1 433 ? -7.01668  12.18135 -15.40855 0.499 46.30564  ? 636  GLU A OE1 1 
ATOM   3605 O  OE1 B GLU A 1 433 ? -8.14296  14.38668 -13.72036 0.501 50.51811  ? 636  GLU A OE1 1 
ATOM   3606 O  OE2 A GLU A 1 433 ? -8.66293  11.22697 -16.50380 0.499 48.99649  ? 636  GLU A OE2 1 
ATOM   3607 O  OE2 B GLU A 1 433 ? -7.93042  12.20776 -13.63961 0.501 48.59646  ? 636  GLU A OE2 1 
ATOM   3608 N  N   A ASP A 1 434 ? -7.45621  16.02151 -19.27760 0.499 39.24372  ? 637  ASP A N   1 
ATOM   3609 N  N   B ASP A 1 434 ? -7.41798  15.99318 -19.24432 0.501 39.24527  ? 637  ASP A N   1 
ATOM   3610 C  CA  A ASP A 1 434 ? -8.09995  16.21389 -20.57741 0.499 41.88285  ? 637  ASP A CA  1 
ATOM   3611 C  CA  B ASP A 1 434 ? -8.08336  16.18874 -20.53207 0.501 41.89411  ? 637  ASP A CA  1 
ATOM   3612 C  C   A ASP A 1 434 ? -7.15956  15.85149 -21.71718 0.499 39.90176  ? 637  ASP A C   1 
ATOM   3613 C  C   B ASP A 1 434 ? -7.15952  15.84178 -21.69368 0.501 39.86374  ? 637  ASP A C   1 
ATOM   3614 O  O   A ASP A 1 434 ? -7.58595  15.26617 -22.72112 0.499 41.49113  ? 637  ASP A O   1 
ATOM   3615 O  O   B ASP A 1 434 ? -7.60161  15.26073 -22.69329 0.501 41.46458  ? 637  ASP A O   1 
ATOM   3616 C  CB  A ASP A 1 434 ? -8.58886  17.65500 -20.74144 0.499 44.13230  ? 637  ASP A CB  1 
ATOM   3617 C  CB  B ASP A 1 434 ? -8.58865  17.62683 -20.66221 0.501 44.18249  ? 637  ASP A CB  1 
ATOM   3618 C  CG  A ASP A 1 434 ? -9.35582  17.86584 -22.04183 0.499 48.52510  ? 637  ASP A CG  1 
ATOM   3619 C  CG  B ASP A 1 434 ? -9.60344  17.98812 -19.59143 0.501 51.44915  ? 637  ASP A CG  1 
ATOM   3620 O  OD1 A ASP A 1 434 ? -10.51691 17.41147 -22.12840 0.499 51.72117  ? 637  ASP A OD1 1 
ATOM   3621 O  OD1 B ASP A 1 434 ? -10.26322 17.06986 -19.05975 0.501 51.06710  ? 637  ASP A OD1 1 
ATOM   3622 O  OD2 A ASP A 1 434 ? -8.80049  18.47358 -22.98758 0.499 52.30265  ? 637  ASP A OD2 1 
ATOM   3623 O  OD2 B ASP A 1 434 ? -9.74125  19.19145 -19.28320 0.501 52.72299  ? 637  ASP A OD2 1 
ATOM   3624 N  N   . GLN A 1 435 ? -5.87428  16.18648 -21.58203 1.000 38.84426  ? 638  GLN A N   1 
ATOM   3625 C  CA  . GLN A 1 435 ? -4.92697  15.84812 -22.64098 1.000 43.97663  ? 638  GLN A CA  1 
ATOM   3626 C  C   . GLN A 1 435 ? -4.73926  14.34199 -22.73398 1.000 37.34482  ? 638  GLN A C   1 
ATOM   3627 O  O   . GLN A 1 435 ? -4.69651  13.77922 -23.83928 1.000 38.54421  ? 638  GLN A O   1 
ATOM   3628 C  CB  . GLN A 1 435 ? -3.58302  16.53590 -22.39803 1.000 41.30803  ? 638  GLN A CB  1 
ATOM   3629 C  CG  . GLN A 1 435 ? -3.65783  18.05351 -22.29322 1.000 41.38471  ? 638  GLN A CG  1 
ATOM   3630 C  CD  . GLN A 1 435 ? -3.81104  18.50837 -20.85991 1.000 44.14403  ? 638  GLN A CD  1 
ATOM   3631 O  OE1 . GLN A 1 435 ? -4.65902  17.99806 -20.12578 1.000 40.02893  ? 638  GLN A OE1 1 
ATOM   3632 N  NE2 . GLN A 1 435 ? -2.95932  19.44210 -20.43680 1.000 44.64971  ? 638  GLN A NE2 1 
ATOM   3633 N  N   . TRP A 1 436 ? -4.63573  13.67783 -21.58212 1.000 39.22173  ? 639  TRP A N   1 
ATOM   3634 C  CA  . TRP A 1 436 ? -4.52397  12.22368 -21.56015 1.000 39.71306  ? 639  TRP A CA  1 
ATOM   3635 C  C   . TRP A 1 436 ? -5.75964  11.56662 -22.15318 1.000 41.20355  ? 639  TRP A C   1 
ATOM   3636 O  O   . TRP A 1 436 ? -5.65203  10.59061 -22.90812 1.000 38.28170  ? 639  TRP A O   1 
ATOM   3637 C  CB  . TRP A 1 436 ? -4.30265  11.73422 -20.12748 1.000 31.60836  ? 639  TRP A CB  1 
ATOM   3638 C  CG  . TRP A 1 436 ? -2.88765  11.57965 -19.74283 1.000 31.96025  ? 639  TRP A CG  1 
ATOM   3639 C  CD1 . TRP A 1 436 ? -2.22622  12.23919 -18.74504 1.000 28.90835  ? 639  TRP A CD1 1 
ATOM   3640 C  CD2 . TRP A 1 436 ? -1.94389  10.68957 -20.33061 1.000 29.12940  ? 639  TRP A CD2 1 
ATOM   3641 N  NE1 . TRP A 1 436 ? -0.92340  11.81356 -18.67946 1.000 27.85468  ? 639  TRP A NE1 1 
ATOM   3642 C  CE2 . TRP A 1 436 ? -0.72452  10.86089 -19.64587 1.000 29.67417  ? 639  TRP A CE2 1 
ATOM   3643 C  CE3 . TRP A 1 436 ? -2.00902  9.76638  -21.38552 1.000 30.13008  ? 639  TRP A CE3 1 
ATOM   3644 C  CZ2 . TRP A 1 436 ? 0.41984   10.13590 -19.97161 1.000 30.29342  ? 639  TRP A CZ2 1 
ATOM   3645 C  CZ3 . TRP A 1 436 ? -0.88397  9.05144  -21.69657 1.000 29.71513  ? 639  TRP A CZ3 1 
ATOM   3646 C  CH2 . TRP A 1 436 ? 0.31854   9.24056  -21.00576 1.000 28.65246  ? 639  TRP A CH2 1 
ATOM   3647 N  N   A LYS A 1 437 ? -6.94655  12.08432 -21.82739 0.534 37.40608  ? 640  LYS A N   1 
ATOM   3648 N  N   B LYS A 1 437 ? -6.94464  12.08449 -21.81983 0.466 37.41190  ? 640  LYS A N   1 
ATOM   3649 C  CA  A LYS A 1 437 ? -8.17244  11.49735 -22.36381 0.534 42.40553  ? 640  LYS A CA  1 
ATOM   3650 C  CA  B LYS A 1 437 ? -8.17892  11.51750 -22.35626 0.466 42.41015  ? 640  LYS A CA  1 
ATOM   3651 C  C   A LYS A 1 437 ? -8.23585  11.62449 -23.88242 0.534 45.32975  ? 640  LYS A C   1 
ATOM   3652 C  C   B LYS A 1 437 ? -8.22692  11.62463 -23.87626 0.466 45.31265  ? 640  LYS A C   1 
ATOM   3653 O  O   A LYS A 1 437 ? -8.64753  10.68435 -24.57674 0.534 45.60195  ? 640  LYS A O   1 
ATOM   3654 O  O   B LYS A 1 437 ? -8.61895  10.67166 -24.56436 0.466 45.64321  ? 640  LYS A O   1 
ATOM   3655 C  CB  A LYS A 1 437 ? -9.39395  12.14844 -21.71538 0.534 43.84745  ? 640  LYS A CB  1 
ATOM   3656 C  CB  B LYS A 1 437 ? -9.38583  12.21562 -21.73069 0.466 43.84759  ? 640  LYS A CB  1 
ATOM   3657 C  CG  A LYS A 1 437 ? -9.71191  11.61685 -20.32770 0.534 38.56967  ? 640  LYS A CG  1 
ATOM   3658 C  CG  B LYS A 1 437 ? -10.71936 11.76339 -22.29500 0.466 43.00647  ? 640  LYS A CG  1 
ATOM   3659 N  N   . LYS A 1 438 ? -7.83417  12.77794 -24.42158 1.000 42.65660  ? 641  LYS A N   1 
ATOM   3660 C  CA  . LYS A 1 438 ? -7.86860  12.95085 -25.87118 1.000 45.18401  ? 641  LYS A CA  1 
ATOM   3661 C  C   . LYS A 1 438 ? -6.85798  12.03809 -26.55138 1.000 44.33364  ? 641  LYS A C   1 
ATOM   3662 O  O   . LYS A 1 438 ? -7.12206  11.51215 -27.63991 1.000 46.20862  ? 641  LYS A O   1 
ATOM   3663 C  CB  . LYS A 1 438 ? -7.61608  14.41180 -26.23841 1.000 50.04698  ? 641  LYS A CB  1 
ATOM   3664 C  CG  . LYS A 1 438 ? -8.74575  15.35295 -25.84306 1.000 52.24113  ? 641  LYS A CG  1 
ATOM   3665 N  N   . TRP A 1 439 ? -5.70040  11.82911 -25.91885 1.000 44.81764  ? 642  TRP A N   1 
ATOM   3666 C  CA  . TRP A 1 439 ? -4.72482  10.89398 -26.46766 1.000 44.69783  ? 642  TRP A CA  1 
ATOM   3667 C  C   . TRP A 1 439 ? -5.28563  9.48055  -26.49165 1.000 47.67580  ? 642  TRP A C   1 
ATOM   3668 O  O   . TRP A 1 439 ? -5.20340  8.78756  -27.51037 1.000 43.71222  ? 642  TRP A O   1 
ATOM   3669 C  CB  . TRP A 1 439 ? -3.42373  10.93127 -25.66871 1.000 39.13523  ? 642  TRP A CB  1 
ATOM   3670 C  CG  . TRP A 1 439 ? -2.35554  10.11862 -26.33480 1.000 42.03097  ? 642  TRP A CG  1 
ATOM   3671 C  CD1 . TRP A 1 439 ? -1.47106  10.54907 -27.28413 1.000 45.44775  ? 642  TRP A CD1 1 
ATOM   3672 C  CD2 . TRP A 1 439 ? -2.08442  8.72297  -26.13760 1.000 41.53506  ? 642  TRP A CD2 1 
ATOM   3673 N  NE1 . TRP A 1 439 ? -0.65229  9.51804  -27.66775 1.000 45.93399  ? 642  TRP A NE1 1 
ATOM   3674 C  CE2 . TRP A 1 439 ? -1.00848  8.38534  -26.98440 1.000 41.35549  ? 642  TRP A CE2 1 
ATOM   3675 C  CE3 . TRP A 1 439 ? -2.63598  7.73115  -25.31408 1.000 43.16964  ? 642  TRP A CE3 1 
ATOM   3676 C  CZ2 . TRP A 1 439 ? -0.48173  7.08805  -27.05165 1.000 43.93406  ? 642  TRP A CZ2 1 
ATOM   3677 C  CZ3 . TRP A 1 439 ? -2.11133  6.44316  -25.37937 1.000 42.25103  ? 642  TRP A CZ3 1 
ATOM   3678 C  CH2 . TRP A 1 439 ? -1.04705  6.13322  -26.24839 1.000 36.68595  ? 642  TRP A CH2 1 
ATOM   3679 N  N   . LEU A 1 440 ? -5.86602  9.03869  -25.37349 1.000 43.31181  ? 643  LEU A N   1 
ATOM   3680 C  CA  . LEU A 1 440 ? -6.40146  7.68361  -25.30254 1.000 46.32021  ? 643  LEU A CA  1 
ATOM   3681 C  C   . LEU A 1 440 ? -7.56204  7.48946  -26.26883 1.000 55.72214  ? 643  LEU A C   1 
ATOM   3682 O  O   . LEU A 1 440 ? -7.68940  6.42591  -26.89010 1.000 55.78876  ? 643  LEU A O   1 
ATOM   3683 C  CB  . LEU A 1 440 ? -6.83483  7.36937  -23.87224 1.000 49.81536  ? 643  LEU A CB  1 
ATOM   3684 C  CG  . LEU A 1 440 ? -7.26771  5.92456  -23.61837 1.000 58.35982  ? 643  LEU A CG  1 
ATOM   3685 C  CD1 . LEU A 1 440 ? -6.16273  4.95360  -24.02563 1.000 52.96849  ? 643  LEU A CD1 1 
ATOM   3686 C  CD2 . LEU A 1 440 ? -7.64821  5.73005  -22.15773 1.000 58.35426  ? 643  LEU A CD2 1 
ATOM   3687 N  N   . GLU A 1 441 ? -8.41872  8.50422  -26.41740 1.000 47.77300  ? 644  GLU A N   1 
ATOM   3688 C  CA  . GLU A 1 441 ? -9.52259  8.38562  -27.36635 1.000 54.25764  ? 644  GLU A CA  1 
ATOM   3689 C  C   . GLU A 1 441 ? -9.02276  8.25684  -28.80138 1.000 55.39016  ? 644  GLU A C   1 
ATOM   3690 O  O   . GLU A 1 441 ? -9.64901  7.56743  -29.61710 1.000 51.51068  ? 644  GLU A O   1 
ATOM   3691 C  CB  . GLU A 1 441 ? -10.47137 9.57901  -27.22179 1.000 54.54174  ? 644  GLU A CB  1 
ATOM   3692 C  CG  . GLU A 1 441 ? -11.28561 9.54969  -25.92259 1.000 65.95754  ? 644  GLU A CG  1 
ATOM   3693 C  CD  . GLU A 1 441 ? -12.09155 10.82054 -25.67849 1.000 67.84307  ? 644  GLU A CD  1 
ATOM   3694 O  OE1 . GLU A 1 441 ? -11.89625 11.81080 -26.41410 1.000 69.65502  ? 644  GLU A OE1 1 
ATOM   3695 O  OE2 . GLU A 1 441 ? -12.92549 10.82703 -24.74688 1.000 70.20323  ? 644  GLU A OE2 1 
ATOM   3696 N  N   . ALA A 1 442 ? -7.89549  8.88641  -29.12948 1.000 51.83448  ? 645  ALA A N   1 
ATOM   3697 C  CA  . ALA A 1 442 ? -7.33917  8.77422  -30.47438 1.000 52.65897  ? 645  ALA A CA  1 
ATOM   3698 C  C   . ALA A 1 442 ? -6.53220  7.49819  -30.68998 1.000 57.17471  ? 645  ALA A C   1 
ATOM   3699 O  O   . ALA A 1 442 ? -6.06981  7.26376  -31.81374 1.000 62.39944  ? 645  ALA A O   1 
ATOM   3700 C  CB  . ALA A 1 442 ? -6.46482  9.99195  -30.79285 1.000 50.67572  ? 645  ALA A CB  1 
ATOM   3701 N  N   . HIS A 1 443 ? -6.35509  6.67083  -29.66238 1.000 55.90696  ? 646  HIS A N   1 
ATOM   3702 C  CA  . HIS A 1 443 ? -5.63437  5.40679  -29.77286 1.000 54.90721  ? 646  HIS A CA  1 
ATOM   3703 C  C   . HIS A 1 443 ? -6.53189  4.23095  -29.41007 1.000 58.66965  ? 646  HIS A C   1 
ATOM   3704 O  O   . HIS A 1 443 ? -6.11049  3.28532  -28.73969 1.000 61.65079  ? 646  HIS A O   1 
ATOM   3705 C  CB  . HIS A 1 443 ? -4.37929  5.40677  -28.90277 1.000 52.16647  ? 646  HIS A CB  1 
ATOM   3706 C  CG  . HIS A 1 443 ? -3.25662  6.21276  -29.47065 1.000 50.73097  ? 646  HIS A CG  1 
ATOM   3707 N  ND1 . HIS A 1 443 ? -3.19128  7.58525  -29.35174 1.000 49.68487  ? 646  HIS A ND1 1 
ATOM   3708 C  CD2 . HIS A 1 443 ? -2.15769  5.84147  -30.16806 1.000 51.33002  ? 646  HIS A CD2 1 
ATOM   3709 C  CE1 . HIS A 1 443 ? -2.10391  8.02466  -29.96078 1.000 52.03430  ? 646  HIS A CE1 1 
ATOM   3710 N  NE2 . HIS A 1 443 ? -1.45659  6.98660  -30.45995 1.000 57.09157  ? 646  HIS A NE2 1 
ATOM   3711 N  N   . GLN A 1 444 ? -7.78412  4.27772  -29.84745 1.000 57.74435  ? 647  GLN A N   1 
ATOM   3712 C  CA  . GLN A 1 444 ? -8.70523  3.17135  -29.62030 1.000 67.54806  ? 647  GLN A CA  1 
ATOM   3713 C  C   . GLN A 1 444 ? -8.73947  2.21850  -30.81437 1.000 63.15340  ? 647  GLN A C   1 
ATOM   3714 O  O   . GLN A 1 444 ? -7.71395  1.95814  -31.44825 1.000 67.54534  ? 647  GLN A O   1 
ATOM   3715 C  CB  . GLN A 1 444 ? -10.10660 3.70023  -29.33042 1.000 67.06021  ? 647  GLN A CB  1 
ATOM   3716 C  CG  . GLN A 1 444 ? -10.17985 4.57431  -28.09229 1.000 66.40738  ? 647  GLN A CG  1 
ATOM   3717 C  CD  . GLN A 1 444 ? -9.82224  3.82344  -26.82098 1.000 81.18188  ? 647  GLN A CD  1 
ATOM   3718 O  OE1 . GLN A 1 444 ? -10.63092 3.05983  -26.29141 1.000 92.21968  ? 647  GLN A OE1 1 
ATOM   3719 N  NE2 . GLN A 1 444 ? -8.60549  4.04005  -26.32224 1.000 74.57846  ? 647  GLN A NE2 1 
HETATM 3720 C  C1  . EDO B 2 .   ? 3.78707   30.78600 13.11890  1.000 40.59408  ? 701  EDO A C1  1 
HETATM 3721 O  O1  . EDO B 2 .   ? 3.87320   32.11031 13.59875  1.000 43.92262  ? 701  EDO A O1  1 
HETATM 3722 C  C2  . EDO B 2 .   ? 4.27406   30.75450 11.69948  1.000 36.10399  ? 701  EDO A C2  1 
HETATM 3723 O  O2  . EDO B 2 .   ? 3.56427   31.73506 10.96785  1.000 39.35393  ? 701  EDO A O2  1 
HETATM 3724 C  C1  . EDO C 2 .   ? 17.31319  4.15111  -8.67498  1.000 37.72399  ? 702  EDO A C1  1 
HETATM 3725 O  O1  . EDO C 2 .   ? 17.96771  3.66205  -9.82696  1.000 49.84636  ? 702  EDO A O1  1 
HETATM 3726 C  C2  . EDO C 2 .   ? 16.12340  3.27248  -8.39522  1.000 34.96425  ? 702  EDO A C2  1 
HETATM 3727 O  O2  . EDO C 2 .   ? 15.60134  2.86877  -9.64333  1.000 48.54225  ? 702  EDO A O2  1 
HETATM 3728 P  P   . PO4 D 3 .   ? 20.35184  25.50238 -5.64090  0.892 39.16976  ? 703  PO4 A P   1 
HETATM 3729 O  O1  . PO4 D 3 .   ? 21.58545  25.80240 -4.72198  0.892 57.63274  ? 703  PO4 A O1  1 
HETATM 3730 O  O2  . PO4 D 3 .   ? 20.58381  26.14959 -7.05246  0.892 47.69097  ? 703  PO4 A O2  1 
HETATM 3731 O  O3  . PO4 D 3 .   ? 20.26232  23.93779 -5.79472  0.892 29.71095  ? 703  PO4 A O3  1 
HETATM 3732 O  O4  . PO4 D 3 .   ? 19.04997  26.10836 -5.01459  0.892 42.62481  ? 703  PO4 A O4  1 
HETATM 3733 C  C1  . EDO E 2 .   ? -11.22452 53.44456 37.36319  1.000 38.99973  ? 704  EDO A C1  1 
HETATM 3734 O  O1  . EDO E 2 .   ? -9.95503  52.85947 37.52489  1.000 49.86915  ? 704  EDO A O1  1 
HETATM 3735 C  C2  . EDO E 2 .   ? -11.10944 54.91063 37.03403  1.000 38.99907  ? 704  EDO A C2  1 
HETATM 3736 O  O2  . EDO E 2 .   ? -12.37347 55.29608 36.53866  1.000 45.00105  ? 704  EDO A O2  1 
HETATM 3737 NA NA  . NA  F 4 .   ? 21.93889  25.13070 -2.63126  1.000 49.70258  ? 705  NA  A NA  1 
HETATM 3738 NA NA  . NA  G 4 .   ? -13.46291 48.25223 13.04076  0.827 43.68891  ? 706  NA  A NA  1 
HETATM 3739 C  C1  . EDO H 2 .   ? 18.21308  -0.08954 3.73399   1.000 30.10054  ? 707  EDO A C1  1 
HETATM 3740 O  O1  . EDO H 2 .   ? 18.38627  0.86145  4.75960   1.000 37.84890  ? 707  EDO A O1  1 
HETATM 3741 C  C2  . EDO H 2 .   ? 19.41161  -0.02602 2.81712   1.000 39.89048  ? 707  EDO A C2  1 
HETATM 3742 O  O2  . EDO H 2 .   ? 19.80038  1.30375  2.54773   1.000 32.08637  ? 707  EDO A O2  1 
HETATM 3743 C  C1  . EDO I 2 .   ? 7.95159   2.76773  -6.74121  1.000 43.72939  ? 708  EDO A C1  1 
HETATM 3744 O  O1  . EDO I 2 .   ? 9.25388   2.40823  -6.31349  1.000 33.05929  ? 708  EDO A O1  1 
HETATM 3745 C  C2  . EDO I 2 .   ? 7.61623   4.21866  -6.49067  1.000 34.71076  ? 708  EDO A C2  1 
HETATM 3746 O  O2  . EDO I 2 .   ? 7.55881   4.52098  -5.10084  1.000 37.12750  ? 708  EDO A O2  1 
HETATM 3747 C  C1  . EDO J 2 .   ? 1.34409   38.73950 10.65589  1.000 38.02320  ? 709  EDO A C1  1 
HETATM 3748 O  O1  . EDO J 2 .   ? 2.04162   39.96722 10.64431  1.000 48.63543  ? 709  EDO A O1  1 
HETATM 3749 C  C2  . EDO J 2 .   ? 2.30049   37.56770 10.73036  1.000 41.01052  ? 709  EDO A C2  1 
HETATM 3750 O  O2  . EDO J 2 .   ? 3.42328   37.73531 9.89404   1.000 38.19817  ? 709  EDO A O2  1 
HETATM 3751 C  C1  . EDO K 2 .   ? 0.62037   67.56192 25.74849  1.000 47.30247  ? 710  EDO A C1  1 
HETATM 3752 O  O1  . EDO K 2 .   ? 0.83905   68.86041 26.25788  1.000 54.20722  ? 710  EDO A O1  1 
HETATM 3753 C  C2  . EDO K 2 .   ? -0.68712  67.51168 24.99844  1.000 41.62369  ? 710  EDO A C2  1 
HETATM 3754 O  O2  . EDO K 2 .   ? -1.80518  67.40757 25.86727  1.000 33.02831  ? 710  EDO A O2  1 
HETATM 3755 C  C1  . EDO L 2 .   ? -12.01772 55.41854 13.90678  0.843 37.47909  ? 711  EDO A C1  1 
HETATM 3756 O  O1  . EDO L 2 .   ? -11.60601 55.54987 15.24685  0.843 37.40521  ? 711  EDO A O1  1 
HETATM 3757 C  C2  . EDO L 2 .   ? -13.01007 54.29213 13.81617  0.843 43.02791  ? 711  EDO A C2  1 
HETATM 3758 O  O2  . EDO L 2 .   ? -12.40762 53.11275 14.29559  0.843 51.33266  ? 711  EDO A O2  1 
HETATM 3759 O  O   . HOH M 5 .   ? 6.67176   0.13226  -27.50855 1.000 47.04587  ? 801  HOH A O   1 
HETATM 3760 O  O   . HOH M 5 .   ? -13.60218 29.16787 14.89251  1.000 46.95701  ? 802  HOH A O   1 
HETATM 3761 O  O   . HOH M 5 .   ? -0.89955  51.04603 29.29311  1.000 34.53395  ? 803  HOH A O   1 
HETATM 3762 O  O   . HOH M 5 .   ? -12.54244 28.19411 10.33709  1.000 52.85634  ? 804  HOH A O   1 
HETATM 3763 O  O   . HOH M 5 .   ? 28.51249  6.62825  6.83982   1.000 48.75165  ? 805  HOH A O   1 
HETATM 3764 O  O   . HOH M 5 .   ? 20.37986  12.49338 7.15799   1.000 37.83592  ? 806  HOH A O   1 
HETATM 3765 O  O   . HOH M 5 .   ? 7.12921   24.28662 -20.82910 1.000 50.93596  ? 807  HOH A O   1 
HETATM 3766 O  O   . HOH M 5 .   ? -15.04348 57.59873 19.98931  1.000 48.77654  ? 808  HOH A O   1 
HETATM 3767 O  O   . HOH M 5 .   ? 11.00850  20.93252 26.68178  1.000 34.77755  ? 809  HOH A O   1 
HETATM 3768 O  O   . HOH M 5 .   ? 10.55496  1.49837  -18.88158 1.000 43.45321  ? 810  HOH A O   1 
HETATM 3769 O  O   . HOH M 5 .   ? 10.95723  7.98048  -15.79692 1.000 26.13578  ? 811  HOH A O   1 
HETATM 3770 O  O   . HOH M 5 .   ? -1.84022  34.86164 23.69157  1.000 38.65966  ? 812  HOH A O   1 
HETATM 3771 O  O   . HOH M 5 .   ? -0.25624  8.60073  -4.70173  1.000 33.55498  ? 813  HOH A O   1 
HETATM 3772 O  O   . HOH M 5 .   ? -7.19606  73.82401 33.56413  1.000 38.26062  ? 814  HOH A O   1 
HETATM 3773 O  O   . HOH M 5 .   ? -5.71368  38.20937 2.66854   1.000 48.53430  ? 815  HOH A O   1 
HETATM 3774 O  O   . HOH M 5 .   ? -12.32182 30.19166 17.77513  1.000 44.74679  ? 816  HOH A O   1 
HETATM 3775 O  O   . HOH M 5 .   ? 2.56124   3.25103  -15.23872 1.000 36.06948  ? 817  HOH A O   1 
HETATM 3776 O  O   . HOH M 5 .   ? 11.83695  23.92352 8.95595   1.000 37.28743  ? 818  HOH A O   1 
HETATM 3777 O  O   . HOH M 5 .   ? -4.43515  17.84140 -11.60860 1.000 39.59363  ? 819  HOH A O   1 
HETATM 3778 O  O   . HOH M 5 .   ? 10.34811  10.24583 -29.08303 1.000 39.20968  ? 820  HOH A O   1 
HETATM 3779 O  O   . HOH M 5 .   ? -17.53783 43.13362 18.94737  1.000 37.00418  ? 821  HOH A O   1 
HETATM 3780 O  O   . HOH M 5 .   ? 28.93197  9.21465  8.09443   1.000 57.01875  ? 822  HOH A O   1 
HETATM 3781 O  O   . HOH M 5 .   ? 37.76151  7.57963  6.69831   1.000 41.11652  ? 823  HOH A O   1 
HETATM 3782 O  O   . HOH M 5 .   ? -1.24764  72.54290 31.67916  1.000 42.76910  ? 824  HOH A O   1 
HETATM 3783 O  O   . HOH M 5 .   ? 25.72338  3.60174  -1.99610  1.000 49.22190  ? 825  HOH A O   1 
HETATM 3784 O  O   . HOH M 5 .   ? -3.35158  14.00104 9.27179   1.000 38.03890  ? 826  HOH A O   1 
HETATM 3785 O  O   . HOH M 5 .   ? 4.40842   49.48536 15.37709  1.000 51.69273  ? 827  HOH A O   1 
HETATM 3786 O  O   . HOH M 5 .   ? -8.67559  33.29201 22.89038  1.000 42.68951  ? 828  HOH A O   1 
HETATM 3787 O  O   . HOH M 5 .   ? 25.84485  -1.94482 -15.38013 1.000 52.74598  ? 829  HOH A O   1 
HETATM 3788 O  O   . HOH M 5 .   ? -4.91722  32.52649 23.61427  1.000 36.38958  ? 830  HOH A O   1 
HETATM 3789 O  O   . HOH M 5 .   ? 17.47932  -1.16241 -33.35488 1.000 47.74700  ? 831  HOH A O   1 
HETATM 3790 O  O   . HOH M 5 .   ? 18.25389  26.00250 1.22986   1.000 43.19038  ? 832  HOH A O   1 
HETATM 3791 O  O   . HOH M 5 .   ? 25.91819  14.12541 -19.89824 1.000 53.44560  ? 833  HOH A O   1 
HETATM 3792 O  O   . HOH M 5 .   ? 13.55165  16.97821 -2.29809  1.000 20.40246  ? 834  HOH A O   1 
HETATM 3793 O  O   . HOH M 5 .   ? -4.08535  71.50308 19.73250  1.000 50.49973  ? 835  HOH A O   1 
HETATM 3794 O  O   . HOH M 5 .   ? 1.57266   37.10093 21.80741  1.000 47.98051  ? 836  HOH A O   1 
HETATM 3795 O  O   . HOH M 5 .   ? -10.28452 70.75911 23.59417  1.000 40.69119  ? 837  HOH A O   1 
HETATM 3796 O  O   . HOH M 5 .   ? 15.24198  1.58086  6.76793   1.000 45.84007  ? 838  HOH A O   1 
HETATM 3797 O  O   . HOH M 5 .   ? -9.03719  25.68429 11.54543  1.000 36.41046  ? 839  HOH A O   1 
HETATM 3798 O  O   . HOH M 5 .   ? -9.29616  36.20744 14.20759  1.000 30.74651  ? 840  HOH A O   1 
HETATM 3799 O  O   . HOH M 5 .   ? 5.70747   36.64224 -1.59021  1.000 32.70630  ? 841  HOH A O   1 
HETATM 3800 O  O   . HOH M 5 .   ? 28.53091  17.19515 1.70913   1.000 44.43742  ? 842  HOH A O   1 
HETATM 3801 O  O   . HOH M 5 .   ? 15.46243  11.00152 -0.06843  1.000 21.35935  ? 843  HOH A O   1 
HETATM 3802 O  O   . HOH M 5 .   ? 15.44430  24.10177 15.40698  1.000 44.97447  ? 844  HOH A O   1 
HETATM 3803 O  O   . HOH M 5 .   ? 18.43577  7.13561  0.87624   1.000 24.13357  ? 845  HOH A O   1 
HETATM 3804 O  O   . HOH M 5 .   ? 15.05616  28.98304 -18.70407 1.000 55.18973  ? 846  HOH A O   1 
HETATM 3805 O  O   . HOH M 5 .   ? -2.02262  74.73502 15.07649  1.000 41.11024  ? 847  HOH A O   1 
HETATM 3806 O  O   . HOH M 5 .   ? -2.53482  32.64282 11.98160  1.000 27.25103  ? 848  HOH A O   1 
HETATM 3807 O  O   . HOH M 5 .   ? 9.23205   25.27471 -28.95375 1.000 50.27724  ? 849  HOH A O   1 
HETATM 3808 O  O   . HOH M 5 .   ? 13.623    14.742   23.884    1.000 42.57602  ? 850  HOH A O   1 
HETATM 3809 O  O   . HOH M 5 .   ? -5.61632  18.53202 -2.54624  1.000 42.29362  ? 851  HOH A O   1 
HETATM 3810 O  O   . HOH M 5 .   ? -0.56086  18.35329 14.58903  1.000 34.84007  ? 852  HOH A O   1 
HETATM 3811 O  O   . HOH M 5 .   ? 15.62566  6.91066  -32.33219 1.000 33.81178  ? 853  HOH A O   1 
HETATM 3812 O  O   . HOH M 5 .   ? 35.626    13.268   -1.409    1.000 44.36706  ? 854  HOH A O   1 
HETATM 3813 O  O   . HOH M 5 .   ? 12.62806  19.53983 -3.09470  1.000 22.85027  ? 855  HOH A O   1 
HETATM 3814 O  O   . HOH M 5 .   ? 17.57057  18.47272 10.17765  1.000 38.92687  ? 856  HOH A O   1 
HETATM 3815 O  O   . HOH M 5 .   ? 17.98460  7.99027  4.66308   1.000 26.79752  ? 857  HOH A O   1 
HETATM 3816 O  O   . HOH M 5 .   ? 14.18795  18.69734 16.94024  1.000 42.46418  ? 858  HOH A O   1 
HETATM 3817 O  O   . HOH M 5 .   ? 16.14138  15.63443 14.47311  1.000 45.23822  ? 859  HOH A O   1 
HETATM 3818 O  O   . HOH M 5 .   ? 8.89465   25.59422 24.25966  1.000 42.75670  ? 860  HOH A O   1 
HETATM 3819 O  O   . HOH M 5 .   ? -6.80500  17.47918 4.63517   1.000 35.44488  ? 861  HOH A O   1 
HETATM 3820 O  O   . HOH M 5 .   ? -14.37001 62.18758 23.40273  1.000 46.75258  ? 862  HOH A O   1 
HETATM 3821 O  O   . HOH M 5 .   ? -7.69115  16.50086 -3.11296  1.000 48.46228  ? 863  HOH A O   1 
HETATM 3822 O  O   . HOH M 5 .   ? 2.41155   9.28965  -4.48572  1.000 30.50133  ? 864  HOH A O   1 
HETATM 3823 O  O   . HOH M 5 .   ? -6.16053  17.55084 -15.20045 1.000 36.52566  ? 865  HOH A O   1 
HETATM 3824 O  O   . HOH M 5 .   ? 10.32143  25.71990 -19.39741 1.000 44.55323  ? 866  HOH A O   1 
HETATM 3825 O  O   . HOH M 5 .   ? -3.59854  13.95052 0.06815   1.000 25.99073  ? 867  HOH A O   1 
HETATM 3826 O  O   . HOH M 5 .   ? 5.33170   28.52773 15.85256  1.000 32.83983  ? 868  HOH A O   1 
HETATM 3827 O  O   . HOH M 5 .   ? 19.34303  5.05618  -11.66004 1.000 37.51588  ? 869  HOH A O   1 
HETATM 3828 O  O   . HOH M 5 .   ? -7.34136  30.38166 2.45972   1.000 38.37394  ? 870  HOH A O   1 
HETATM 3829 O  O   . HOH M 5 .   ? 13.33548  13.54628 12.56385  1.000 48.25603  ? 871  HOH A O   1 
HETATM 3830 O  O   . HOH M 5 .   ? -12.57047 35.46304 12.97022  1.000 38.34014  ? 872  HOH A O   1 
HETATM 3831 O  O   . HOH M 5 .   ? 18.46376  8.47835  -6.29567  1.000 24.70691  ? 873  HOH A O   1 
HETATM 3832 O  O   . HOH M 5 .   ? -17.51918 43.66704 24.87194  1.000 41.42202  ? 874  HOH A O   1 
HETATM 3833 O  O   . HOH M 5 .   ? 7.34905   9.28157  1.28862   1.000 21.02634  ? 875  HOH A O   1 
HETATM 3834 O  O   . HOH M 5 .   ? 2.79053   31.92704 16.09704  1.000 35.90099  ? 876  HOH A O   1 
HETATM 3835 O  O   . HOH M 5 .   ? -8.36348  30.18661 22.03072  1.000 42.21590  ? 877  HOH A O   1 
HETATM 3836 O  O   . HOH M 5 .   ? 17.99407  3.13020  -23.63772 1.000 50.35269  ? 878  HOH A O   1 
HETATM 3837 O  O   . HOH M 5 .   ? -2.79029  6.31732  -9.40175  1.000 43.48540  ? 879  HOH A O   1 
HETATM 3838 O  O   . HOH M 5 .   ? -15.53077 49.73025 23.16275  1.000 43.60288  ? 880  HOH A O   1 
HETATM 3839 O  O   . HOH M 5 .   ? 12.85027  16.25506 17.07904  1.000 46.29888  ? 881  HOH A O   1 
HETATM 3840 O  O   . HOH M 5 .   ? -6.65021  66.44217 30.59838  1.000 26.10362  ? 882  HOH A O   1 
HETATM 3841 O  O   . HOH M 5 .   ? -9.53653  27.18223 -5.27600  1.000 53.70834  ? 883  HOH A O   1 
HETATM 3842 O  O   . HOH M 5 .   ? -1.02226  67.47499 15.57600  1.000 41.05653  ? 884  HOH A O   1 
HETATM 3843 O  O   . HOH M 5 .   ? 18.96519  15.15362 -9.46101  1.000 26.62494  ? 885  HOH A O   1 
HETATM 3844 O  O   . HOH M 5 .   ? -7.61391  60.81586 42.17230  1.000 31.30260  ? 886  HOH A O   1 
HETATM 3845 O  O   . HOH M 5 .   ? 1.11011   9.28324  2.84684   1.000 21.95772  ? 887  HOH A O   1 
HETATM 3846 O  O   . HOH M 5 .   ? 3.95605   0.18590  -27.41708 1.000 31.00521  ? 888  HOH A O   1 
HETATM 3847 O  O   . HOH M 5 .   ? 0.53170   8.99816  5.67323   1.000 23.56518  ? 889  HOH A O   1 
HETATM 3848 O  O   . HOH M 5 .   ? 3.91522   18.93599 -4.60395  1.000 21.62757  ? 890  HOH A O   1 
HETATM 3849 O  O   . HOH M 5 .   ? 18.58794  12.55236 -5.27179  1.000 23.07546  ? 891  HOH A O   1 
HETATM 3850 O  O   . HOH M 5 .   ? 12.33031  8.91040  7.49851   1.000 24.69943  ? 892  HOH A O   1 
HETATM 3851 O  O   . HOH M 5 .   ? 19.90718  16.73874 1.69690   1.000 31.93756  ? 893  HOH A O   1 
HETATM 3852 O  O   . HOH M 5 .   ? -5.09179  8.62531  -10.21385 1.000 50.16980  ? 894  HOH A O   1 
HETATM 3853 O  O   . HOH M 5 .   ? -8.73756  21.36459 5.02127   1.000 40.87494  ? 895  HOH A O   1 
HETATM 3854 O  O   . HOH M 5 .   ? 9.40195   63.52675 16.65821  1.000 46.68065  ? 896  HOH A O   1 
HETATM 3855 O  O   . HOH M 5 .   ? 24.80876  7.51954  -7.24275  1.000 32.73182  ? 897  HOH A O   1 
HETATM 3856 O  O   . HOH M 5 .   ? -14.06052 36.36889 24.83158  1.000 42.18686  ? 898  HOH A O   1 
HETATM 3857 O  O   . HOH M 5 .   ? 4.55030   4.22443  0.49803   1.000 25.39766  ? 899  HOH A O   1 
HETATM 3858 O  O   . HOH M 5 .   ? -3.72886  14.91948 -26.12302 1.000 43.05537  ? 900  HOH A O   1 
HETATM 3859 O  O   . HOH M 5 .   ? 3.89340   2.68500  -8.32658  1.000 43.72785  ? 901  HOH A O   1 
HETATM 3860 O  O   . HOH M 5 .   ? -11.18493 57.96354 35.47930  1.000 27.71182  ? 902  HOH A O   1 
HETATM 3861 O  O   . HOH M 5 .   ? 12.74101  6.49193  3.64659   1.000 24.19672  ? 903  HOH A O   1 
HETATM 3862 O  O   . HOH M 5 .   ? 18.42481  2.14252  -28.27224 1.000 44.90549  ? 904  HOH A O   1 
HETATM 3863 O  O   . HOH M 5 .   ? -9.28492  28.77611 18.98084  1.000 42.89633  ? 905  HOH A O   1 
HETATM 3864 O  O   . HOH M 5 .   ? -0.09587  23.35200 -13.48608 1.000 31.94546  ? 906  HOH A O   1 
HETATM 3865 O  O   . HOH M 5 .   ? -7.30629  36.96387 10.38035  1.000 32.84940  ? 907  HOH A O   1 
HETATM 3866 O  O   . HOH M 5 .   ? 10.90598  5.71401  8.59473   1.000 37.01558  ? 908  HOH A O   1 
HETATM 3867 O  O   . HOH M 5 .   ? 15.36663  16.51797 3.35242   1.000 23.52232  ? 909  HOH A O   1 
HETATM 3868 O  O   . HOH M 5 .   ? 0.723     3.946    -31.939   1.000 35.16646  ? 910  HOH A O   1 
HETATM 3869 O  O   . HOH M 5 .   ? -3.30841  67.57857 13.70123  1.000 49.39572  ? 911  HOH A O   1 
HETATM 3870 O  O   . HOH M 5 .   ? -3.04479  20.18588 14.42500  1.000 31.24955  ? 912  HOH A O   1 
HETATM 3871 O  O   . HOH M 5 .   ? -13.86752 58.49332 17.65301  1.000 39.33130  ? 913  HOH A O   1 
HETATM 3872 O  O   . HOH M 5 .   ? -1.12023  56.25646 31.32313  1.000 49.17132  ? 914  HOH A O   1 
HETATM 3873 O  O   . HOH M 5 .   ? -7.14049  29.33931 14.45489  1.000 30.72857  ? 915  HOH A O   1 
HETATM 3874 O  O   . HOH M 5 .   ? -2.45113  26.25225 -9.85053  1.000 29.49770  ? 916  HOH A O   1 
HETATM 3875 O  O   A HOH M 5 .   ? 8.17868   7.55320  -26.80894 0.512 25.10696  ? 917  HOH A O   1 
HETATM 3876 O  O   B HOH M 5 .   ? 8.51406   8.27789  -28.59008 0.488 28.77244  ? 917  HOH A O   1 
HETATM 3877 O  O   . HOH M 5 .   ? -0.44207  73.23909 37.48948  1.000 42.39257  ? 918  HOH A O   1 
HETATM 3878 O  O   . HOH M 5 .   ? 3.72812   67.70413 24.45534  1.000 46.17259  ? 919  HOH A O   1 
HETATM 3879 O  O   . HOH M 5 .   ? 11.37420  0.00000  0.00000   0.50  22.20403  ? 920  HOH A O   1 
HETATM 3880 O  O   . HOH M 5 .   ? 5.08096   47.41456 26.02015  1.000 41.99234  ? 921  HOH A O   1 
HETATM 3881 O  O   . HOH M 5 .   ? 4.91252   40.76457 16.64986  1.000 57.30549  ? 922  HOH A O   1 
HETATM 3882 O  O   . HOH M 5 .   ? -1.28395  39.76310 12.38746  1.000 27.23873  ? 923  HOH A O   1 
HETATM 3883 O  O   . HOH M 5 .   ? 8.69063   1.78354  -3.67611  1.000 29.36283  ? 924  HOH A O   1 
HETATM 3884 O  O   . HOH M 5 .   ? -0.48800  5.75521  -4.89965  1.000 44.66160  ? 925  HOH A O   1 
HETATM 3885 O  O   . HOH M 5 .   ? 1.90071   1.19215  2.62685   1.000 44.91768  ? 926  HOH A O   1 
HETATM 3886 O  O   . HOH M 5 .   ? 6.119     8.152    -31.313   1.000 37.08524  ? 927  HOH A O   1 
HETATM 3887 O  O   . HOH M 5 .   ? 31.38778  8.20321  -6.40607  1.000 47.68066  ? 928  HOH A O   1 
HETATM 3888 O  O   . HOH M 5 .   ? 14.73461  21.28642 -3.01094  1.000 24.48298  ? 929  HOH A O   1 
HETATM 3889 O  O   . HOH M 5 .   ? 4.12813   4.47126  8.76323   1.000 30.62165  ? 930  HOH A O   1 
HETATM 3890 O  O   . HOH M 5 .   ? 3.69629   5.25336  -13.95610 1.000 36.12941  ? 931  HOH A O   1 
HETATM 3891 O  O   . HOH M 5 .   ? -14.21136 52.37302 32.27302  1.000 31.17634  ? 932  HOH A O   1 
HETATM 3892 O  O   . HOH M 5 .   ? 1.51526   5.44398  11.23446  1.000 36.41865  ? 933  HOH A O   1 
HETATM 3893 O  O   . HOH M 5 .   ? -4.23272  24.26413 19.82019  1.000 42.48658  ? 934  HOH A O   1 
HETATM 3894 O  O   . HOH M 5 .   ? -2.66193  62.19737 18.98911  1.000 34.71159  ? 935  HOH A O   1 
HETATM 3895 O  O   . HOH M 5 .   ? 15.79281  6.82649  1.94963   1.000 25.50609  ? 936  HOH A O   1 
HETATM 3896 O  O   . HOH M 5 .   ? -4.45243  45.20005 12.23704  1.000 36.22646  ? 937  HOH A O   1 
HETATM 3897 O  O   . HOH M 5 .   ? 2.28107   40.09610 13.63990  1.000 42.83707  ? 938  HOH A O   1 
HETATM 3898 O  O   . HOH M 5 .   ? 0.63965   48.65640 17.65048  1.000 28.89371  ? 939  HOH A O   1 
HETATM 3899 O  O   . HOH M 5 .   ? -5.59073  38.91558 6.24236   1.000 56.33107  ? 940  HOH A O   1 
HETATM 3900 O  O   . HOH M 5 .   ? 1.49771   64.13930 25.71236  1.000 32.36185  ? 941  HOH A O   1 
HETATM 3901 O  O   . HOH M 5 .   ? 2.73954   6.79789  -30.70257 1.000 36.34366  ? 942  HOH A O   1 
HETATM 3902 O  O   . HOH M 5 .   ? -15.01440 37.29210 18.58292  1.000 38.04249  ? 943  HOH A O   1 
HETATM 3903 O  O   . HOH M 5 .   ? -3.13303  70.08286 25.81159  1.000 33.18982  ? 944  HOH A O   1 
HETATM 3904 O  O   . HOH M 5 .   ? 5.19000   5.94465  -4.32755  1.000 32.44287  ? 945  HOH A O   1 
HETATM 3905 O  O   . HOH M 5 .   ? 15.99559  0.52103  -25.25205 1.000 41.86100  ? 946  HOH A O   1 
HETATM 3906 O  O   . HOH M 5 .   ? -7.45510  19.21171 8.56219   1.000 31.18357  ? 947  HOH A O   1 
HETATM 3907 O  O   . HOH M 5 .   ? 17.78166  13.08677 -26.87012 1.000 38.40758  ? 948  HOH A O   1 
HETATM 3908 O  O   . HOH M 5 .   ? 4.45820   -1.05179 6.08113   1.000 39.53604  ? 949  HOH A O   1 
HETATM 3909 O  O   . HOH M 5 .   ? 17.02434  10.41227 -4.65191  1.000 23.64816  ? 950  HOH A O   1 
HETATM 3910 O  O   . HOH M 5 .   ? 7.40013   20.93678 17.28165  1.000 25.19244  ? 951  HOH A O   1 
HETATM 3911 O  O   . HOH M 5 .   ? 12.94142  17.93559 3.37107   1.000 19.77680  ? 952  HOH A O   1 
HETATM 3912 O  O   . HOH M 5 .   ? 15.94192  25.70473 4.16894   1.000 41.72398  ? 953  HOH A O   1 
HETATM 3913 O  O   . HOH M 5 .   ? -5.03476  58.21240 39.97552  1.000 42.25184  ? 954  HOH A O   1 
HETATM 3914 O  O   . HOH M 5 .   ? 19.87906  11.50970 -7.70408  1.000 25.98362  ? 955  HOH A O   1 
HETATM 3915 O  O   . HOH M 5 .   ? 12.28307  13.40332 -31.52356 1.000 47.29481  ? 956  HOH A O   1 
HETATM 3916 O  O   . HOH M 5 .   ? 4.09277   21.03993 18.48653  1.000 41.02715  ? 957  HOH A O   1 
HETATM 3917 O  O   . HOH M 5 .   ? -9.46036  26.16189 4.17953   1.000 43.69404  ? 958  HOH A O   1 
HETATM 3918 O  O   . HOH M 5 .   ? -12.68688 36.87809 15.18450  1.000 36.75284  ? 959  HOH A O   1 
HETATM 3919 O  O   . HOH M 5 .   ? 13.96131  14.50734 15.18943  1.000 47.24819  ? 960  HOH A O   1 
HETATM 3920 O  O   . HOH M 5 .   ? -12.42488 26.87612 7.94166   1.000 52.57772  ? 961  HOH A O   1 
HETATM 3921 O  O   . HOH M 5 .   ? 16.39956  10.81385 8.02751   1.000 29.06362  ? 962  HOH A O   1 
HETATM 3922 O  O   . HOH M 5 .   ? -3.21548  19.09600 -5.02267  1.000 29.90777  ? 963  HOH A O   1 
HETATM 3923 O  O   . HOH M 5 .   ? 27.78849  16.59063 4.69799   1.000 46.78575  ? 964  HOH A O   1 
HETATM 3924 O  O   . HOH M 5 .   ? -18.79198 54.10008 30.64062  1.000 52.30070  ? 965  HOH A O   1 
HETATM 3925 O  O   . HOH M 5 .   ? -3.33345  20.51312 -17.52655 1.000 33.78587  ? 966  HOH A O   1 
HETATM 3926 O  O   . HOH M 5 .   ? 21.05200  6.89741  7.05338   1.000 34.86914  ? 967  HOH A O   1 
HETATM 3927 O  O   . HOH M 5 .   ? 2.03926   52.61010 23.20388  1.000 30.61053  ? 968  HOH A O   1 
HETATM 3928 O  O   . HOH M 5 .   ? -5.55419  13.71094 -9.22241  1.000 45.61898  ? 969  HOH A O   1 
HETATM 3929 O  O   . HOH M 5 .   ? 22.74720  20.52379 -13.36375 1.000 42.40210  ? 970  HOH A O   1 
HETATM 3930 O  O   . HOH M 5 .   ? -3.92895  16.23500 8.08722   1.000 36.32525  ? 971  HOH A O   1 
HETATM 3931 O  O   . HOH M 5 .   ? -3.10377  51.76759 31.02753  1.000 27.70178  ? 972  HOH A O   1 
HETATM 3932 O  O   . HOH M 5 .   ? 11.94488  27.43359 -10.74009 1.000 42.28591  ? 973  HOH A O   1 
HETATM 3933 O  O   . HOH M 5 .   ? 23.19534  5.57399  7.84930   1.000 46.44144  ? 974  HOH A O   1 
HETATM 3934 O  O   . HOH M 5 .   ? 3.16721   36.73657 -1.52327  1.000 34.54398  ? 975  HOH A O   1 
HETATM 3935 O  O   . HOH M 5 .   ? -3.65205  38.28309 12.84145  1.000 27.95941  ? 976  HOH A O   1 
HETATM 3936 O  O   . HOH M 5 .   ? -13.69596 64.80342 25.75608  1.000 39.54478  ? 977  HOH A O   1 
HETATM 3937 O  O   . HOH M 5 .   ? 6.99876   13.87871 17.97317  1.000 25.09116  ? 978  HOH A O   1 
HETATM 3938 O  O   . HOH M 5 .   ? 19.20073  17.14190 11.47868  1.000 40.83315  ? 979  HOH A O   1 
HETATM 3939 O  O   . HOH M 5 .   ? 7.47052   1.26933  0.72858   1.000 25.65520  ? 980  HOH A O   1 
HETATM 3940 O  O   . HOH M 5 .   ? 13.26847  13.72054 -27.53614 1.000 42.83091  ? 981  HOH A O   1 
HETATM 3941 O  O   . HOH M 5 .   ? -3.30513  70.31865 38.47620  1.000 35.41472  ? 982  HOH A O   1 
HETATM 3942 O  O   . HOH M 5 .   ? 26.47739  12.19413 -18.70497 1.000 50.43756  ? 983  HOH A O   1 
HETATM 3943 O  O   . HOH M 5 .   ? 9.42633   22.87865 25.49400  1.000 37.80653  ? 984  HOH A O   1 
HETATM 3944 O  O   . HOH M 5 .   ? -3.455    63.622   42.810    1.000 41.18639  ? 985  HOH A O   1 
HETATM 3945 O  O   . HOH M 5 .   ? -7.04377  21.24423 -13.75308 1.000 49.44891  ? 986  HOH A O   1 
HETATM 3946 O  O   . HOH M 5 .   ? -14.09015 49.82163 20.11627  1.000 32.37179  ? 987  HOH A O   1 
HETATM 3947 O  O   . HOH M 5 .   ? -4.94942  51.71257 13.75373  1.000 29.15900  ? 988  HOH A O   1 
HETATM 3948 O  O   . HOH M 5 .   ? -4.04254  52.19278 37.57157  1.000 46.39495  ? 989  HOH A O   1 
HETATM 3949 O  O   . HOH M 5 .   ? 35.54740  11.45378 7.84077   1.000 50.02342  ? 990  HOH A O   1 
HETATM 3950 O  O   . HOH M 5 .   ? 2.80892   16.79335 16.35538  1.000 47.87290  ? 991  HOH A O   1 
HETATM 3951 O  O   . HOH M 5 .   ? 6.13455   2.34290  -9.89885  1.000 42.42833  ? 992  HOH A O   1 
HETATM 3952 O  O   . HOH M 5 .   ? -15.42990 59.19924 24.15988  1.000 39.47130  ? 993  HOH A O   1 
HETATM 3953 O  O   . HOH M 5 .   ? -1.07459  43.81344 12.52897  1.000 31.83362  ? 994  HOH A O   1 
HETATM 3954 O  O   . HOH M 5 .   ? 24.89458  20.42740 -9.64311  1.000 38.57430  ? 995  HOH A O   1 
HETATM 3955 O  O   . HOH M 5 .   ? -2.09003  17.12061 10.08334  1.000 33.40653  ? 996  HOH A O   1 
HETATM 3956 O  O   . HOH M 5 .   ? -13.29905 35.10325 22.93325  1.000 33.63806  ? 997  HOH A O   1 
HETATM 3957 O  O   . HOH M 5 .   ? -16.10133 41.47207 20.55150  1.000 34.13539  ? 998  HOH A O   1 
HETATM 3958 O  O   . HOH M 5 .   ? -3.20356  58.17150 37.59220  1.000 47.74167  ? 999  HOH A O   1 
HETATM 3959 O  O   . HOH M 5 .   ? -12.47058 30.88728 22.74353  1.000 47.72003  ? 1000 HOH A O   1 
HETATM 3960 O  O   . HOH M 5 .   ? -3.97333  35.87398 25.10504  1.000 42.98616  ? 1001 HOH A O   1 
HETATM 3961 O  O   . HOH M 5 .   ? -6.01258  66.98155 36.42237  1.000 37.92875  ? 1002 HOH A O   1 
HETATM 3962 O  O   . HOH M 5 .   ? -2.47939  67.83309 37.19302  1.000 35.89515  ? 1003 HOH A O   1 
HETATM 3963 O  O   . HOH M 5 .   ? 21.61468  17.47577 3.69324   1.000 32.12106  ? 1004 HOH A O   1 
HETATM 3964 O  O   . HOH M 5 .   ? 0.83914   6.32786  5.66310   1.000 28.23511  ? 1005 HOH A O   1 
HETATM 3965 O  O   . HOH M 5 .   ? 5.454     27.646   23.952    1.000 42.81474  ? 1006 HOH A O   1 
HETATM 3966 O  O   . HOH M 5 .   ? 26.27819  0.56648  -4.07666  1.000 52.38448  ? 1007 HOH A O   1 
HETATM 3967 O  O   . HOH M 5 .   ? -12.37218 49.97633 14.31919  1.000 45.67527  ? 1008 HOH A O   1 
HETATM 3968 O  O   . HOH M 5 .   ? 16.03664  4.94729  -30.41728 1.000 31.47593  ? 1009 HOH A O   1 
HETATM 3969 O  O   . HOH M 5 .   ? -2.12769  69.80320 19.39148  1.000 40.02805  ? 1010 HOH A O   1 
HETATM 3970 O  O   . HOH M 5 .   ? -4.57257  10.59132 -1.05928  1.000 38.74026  ? 1011 HOH A O   1 
HETATM 3971 O  O   . HOH M 5 .   ? -16.97303 59.54243 33.82827  1.000 39.38318  ? 1012 HOH A O   1 
HETATM 3972 O  O   . HOH M 5 .   ? 4.13667   60.57531 24.48397  1.000 35.93167  ? 1013 HOH A O   1 
HETATM 3973 O  O   . HOH M 5 .   ? 1.18484   55.94946 30.73247  1.000 37.09099  ? 1014 HOH A O   1 
HETATM 3974 O  O   . HOH M 5 .   ? -3.75871  70.04864 23.14938  1.000 37.91725  ? 1015 HOH A O   1 
HETATM 3975 O  O   . HOH M 5 .   ? -10.68944 71.24937 26.23416  1.000 42.62482  ? 1016 HOH A O   1 
HETATM 3976 O  O   . HOH M 5 .   ? 24.78306  12.30428 6.10765   1.000 52.43230  ? 1017 HOH A O   1 
HETATM 3977 O  O   . HOH M 5 .   ? -0.09620  26.62331 20.52437  1.000 46.33149  ? 1018 HOH A O   1 
HETATM 3978 O  O   . HOH M 5 .   ? -16.30184 34.26081 15.44023  1.000 51.43698  ? 1019 HOH A O   1 
HETATM 3979 O  O   . HOH M 5 .   ? -13.28664 32.21052 11.55744  1.000 44.66437  ? 1020 HOH A O   1 
HETATM 3980 O  O   . HOH M 5 .   ? 17.88903  25.63987 -8.47819  1.000 42.10552  ? 1021 HOH A O   1 
HETATM 3981 O  O   . HOH M 5 .   ? -7.41490  34.82977 25.55466  1.000 42.87876  ? 1022 HOH A O   1 
HETATM 3982 O  O   . HOH M 5 .   ? 8.61049   2.22163  7.73495   1.000 31.17241  ? 1023 HOH A O   1 
HETATM 3983 O  O   . HOH M 5 .   ? -10.93780 38.85071 14.10224  1.000 35.65230  ? 1024 HOH A O   1 
HETATM 3984 O  O   . HOH M 5 .   ? 2.90086   62.52871 14.19626  1.000 49.47216  ? 1025 HOH A O   1 
HETATM 3985 O  O   . HOH M 5 .   ? -3.78126  6.03638  -12.64897 1.000 34.44262  ? 1026 HOH A O   1 
HETATM 3986 O  O   . HOH M 5 .   ? 24.40776  5.85690  -3.46623  1.000 36.06818  ? 1027 HOH A O   1 
HETATM 3987 O  O   . HOH M 5 .   ? -15.58967 49.18208 13.23004  1.000 43.09790  ? 1028 HOH A O   1 
HETATM 3988 O  O   . HOH M 5 .   ? -3.48320  7.92311  -2.42805  1.000 43.23661  ? 1029 HOH A O   1 
HETATM 3989 O  O   . HOH M 5 .   ? 5.43923   10.51097 16.40654  1.000 33.47017  ? 1030 HOH A O   1 
HETATM 3990 O  O   . HOH M 5 .   ? 5.85812   58.73892 25.42130  1.000 36.56200  ? 1031 HOH A O   1 
HETATM 3991 O  O   . HOH M 5 .   ? 3.88543   53.70299 16.71859  1.000 48.96982  ? 1032 HOH A O   1 
HETATM 3992 O  O   . HOH M 5 .   ? 23.67731  16.79277 5.42773   1.000 39.74063  ? 1033 HOH A O   1 
HETATM 3993 O  O   . HOH M 5 .   ? -5.61380  21.88631 15.78772  1.000 42.01015  ? 1034 HOH A O   1 
HETATM 3994 O  O   . HOH M 5 .   ? 18.25408  18.56120 -23.51354 1.000 37.17124  ? 1035 HOH A O   1 
HETATM 3995 O  O   . HOH M 5 .   ? -4.08755  7.25433  -14.87926 1.000 40.60177  ? 1036 HOH A O   1 
HETATM 3996 O  O   . HOH M 5 .   ? -17.13481 59.13075 25.73240  1.000 58.45171  ? 1037 HOH A O   1 
HETATM 3997 O  O   . HOH M 5 .   ? 0.93538   27.60433 -18.61393 1.000 45.72011  ? 1038 HOH A O   1 
HETATM 3998 O  O   . HOH M 5 .   ? -15.98703 64.95748 29.41970  1.000 54.01138  ? 1039 HOH A O   1 
HETATM 3999 O  O   . HOH M 5 .   ? 4.99477   50.41515 22.36223  1.000 46.43308  ? 1040 HOH A O   1 
HETATM 4000 O  O   . HOH M 5 .   ? 2.72852   61.72562 26.52436  1.000 29.56237  ? 1041 HOH A O   1 
HETATM 4001 O  O   . HOH M 5 .   ? -0.69910  7.11794  14.31325  1.000 34.30278  ? 1042 HOH A O   1 
HETATM 4002 O  O   . HOH M 5 .   ? 14.75625  5.51077  -15.89125 1.000 39.76421  ? 1043 HOH A O   1 
HETATM 4003 O  O   . HOH M 5 .   ? -3.20432  8.85605  13.15296  1.000 40.54582  ? 1044 HOH A O   1 
HETATM 4004 O  O   A HOH M 5 .   ? 22.25320  3.78711  -10.90336 0.634 32.78586  ? 1045 HOH A O   1 
HETATM 4005 O  O   B HOH M 5 .   ? 23.00090  4.24720  -8.79200  0.366 27.14336  ? 1045 HOH A O   1 
HETATM 4006 O  O   . HOH M 5 .   ? 3.07360   37.37275 15.84031  1.000 40.70680  ? 1046 HOH A O   1 
HETATM 4007 O  O   . HOH M 5 .   ? -2.36641  8.62496  4.30610   1.000 28.37053  ? 1047 HOH A O   1 
HETATM 4008 O  O   . HOH M 5 .   ? 5.66416   26.84035 18.11839  1.000 37.86344  ? 1048 HOH A O   1 
HETATM 4009 O  O   . HOH M 5 .   ? -3.71786  10.00129 8.10613   1.000 38.23536  ? 1049 HOH A O   1 
HETATM 4010 O  O   . HOH M 5 .   ? 5.32841   65.23547 13.68133  1.000 39.04577  ? 1050 HOH A O   1 
HETATM 4011 O  O   . HOH M 5 .   ? 17.91122  25.92965 6.12221   1.000 48.62519  ? 1051 HOH A O   1 
HETATM 4012 O  O   . HOH M 5 .   ? 6.84244   61.87459 21.87228  1.000 49.46809  ? 1052 HOH A O   1 
HETATM 4013 O  O   . HOH M 5 .   ? -3.91079  49.30275 12.36415  1.000 40.99412  ? 1053 HOH A O   1 
HETATM 4014 O  O   . HOH M 5 .   ? 14.63560  18.21185 26.21586  1.000 49.75466  ? 1054 HOH A O   1 
HETATM 4015 O  O   . HOH M 5 .   ? 1.24457   47.66013 11.93111  1.000 42.07013  ? 1055 HOH A O   1 
HETATM 4016 O  O   . HOH M 5 .   ? 32.15146  16.18847 4.27044   1.000 42.50235  ? 1056 HOH A O   1 
HETATM 4017 O  O   . HOH M 5 .   ? 3.15557   19.14297 16.36934  1.000 44.19461  ? 1057 HOH A O   1 
HETATM 4018 O  O   . HOH M 5 .   ? 12.90271  11.65015 1.96190   1.000 22.63006  ? 1058 HOH A O   1 
HETATM 4019 O  O   . HOH M 5 .   ? 13.23422  -2.66534 -24.95299 1.000 35.18411  ? 1059 HOH A O   1 
HETATM 4020 O  O   . HOH M 5 .   ? -6.79749  26.86135 -12.50095 1.000 52.02099  ? 1060 HOH A O   1 
HETATM 4021 O  O   . HOH M 5 .   ? 8.84226   2.94276  -1.33052  1.000 26.52715  ? 1061 HOH A O   1 
HETATM 4022 O  O   . HOH M 5 .   ? -4.04279  0.76031  -17.58919 1.000 42.71991  ? 1062 HOH A O   1 
HETATM 4023 O  O   . HOH M 5 .   ? 6.98942   27.24796 20.66878  1.000 36.83500  ? 1063 HOH A O   1 
HETATM 4024 O  O   . HOH M 5 .   ? -1.39757  69.04552 21.92880  1.000 33.70499  ? 1064 HOH A O   1 
HETATM 4025 O  O   . HOH M 5 .   ? -6.86733  18.74202 -17.94423 1.000 44.32675  ? 1065 HOH A O   1 
HETATM 4026 O  O   . HOH M 5 .   ? 15.17504  11.52200 -29.48828 1.000 46.96994  ? 1066 HOH A O   1 
HETATM 4027 O  O   . HOH M 5 .   ? -7.57812  37.44030 7.77602   1.000 50.38262  ? 1067 HOH A O   1 
HETATM 4028 O  O   . HOH M 5 .   ? 14.10200  15.32188 19.39117  1.000 46.56000  ? 1068 HOH A O   1 
HETATM 4029 O  O   . HOH M 5 .   ? 19.56299  16.97522 -25.84370 1.000 47.94833  ? 1069 HOH A O   1 
HETATM 4030 O  O   . HOH M 5 .   ? 15.83618  28.22478 3.54581   1.000 46.28805  ? 1070 HOH A O   1 
HETATM 4031 O  O   . HOH M 5 .   ? -0.71451  41.81338 10.75446  1.000 35.93450  ? 1071 HOH A O   1 
HETATM 4032 O  O   . HOH M 5 .   ? 30.05161  16.68494 -2.00122  1.000 52.10957  ? 1072 HOH A O   1 
HETATM 4033 O  O   . HOH M 5 .   ? 6.79874   59.45002 27.57158  1.000 47.29898  ? 1073 HOH A O   1 
HETATM 4034 O  O   . HOH M 5 .   ? 0.519     24.654   -31.167   1.000 45.98517  ? 1074 HOH A O   1 
HETATM 4035 O  O   . HOH M 5 .   ? 26.159    34.899   20.750    1.000 53.35886  ? 1075 HOH A O   1 
HETATM 4036 O  O   . HOH M 5 .   ? 5.854     2.022    -3.712    1.000 37.84279  ? 1076 HOH A O   1 
HETATM 4037 O  O   . HOH M 5 .   ? -14.83137 47.50724 11.38698  1.000 54.17794  ? 1077 HOH A O   1 
HETATM 4038 O  O   . HOH M 5 .   ? 11.00099  4.69927  5.09665   1.000 23.47311  ? 1078 HOH A O   1 
HETATM 4039 O  O   . HOH M 5 .   ? 10.69714  2.00510  4.31753   1.000 26.74903  ? 1079 HOH A O   1 
HETATM 4040 O  O   . HOH M 5 .   ? 5.27375   48.54472 20.44391  1.000 55.21455  ? 1080 HOH A O   1 
HETATM 4041 O  O   . HOH M 5 .   ? -0.76879  7.09870  2.69826   1.000 34.05301  ? 1081 HOH A O   1 
HETATM 4042 O  O   . HOH M 5 .   ? 9.75731   0.41201  2.18887   1.000 23.88195  ? 1082 HOH A O   1 
HETATM 4043 O  O   . HOH M 5 .   ? 14.68156  6.67826  5.21662   1.000 44.14092  ? 1083 HOH A O   1 
HETATM 4044 O  O   . HOH M 5 .   ? 17.29324  28.70682 -7.70422  1.000 57.96042  ? 1084 HOH A O   1 
HETATM 4045 O  O   . HOH M 5 .   ? -16.88601 41.56883 23.32751  1.000 37.88344  ? 1085 HOH A O   1 
HETATM 4046 O  O   . HOH M 5 .   ? 4.50834   61.58638 28.60200  1.000 45.48520  ? 1086 HOH A O   1 
HETATM 4047 O  O   . HOH M 5 .   ? -9.35075  28.06299 2.33093   1.000 50.83654  ? 1087 HOH A O   1 
HETATM 4048 O  O   . HOH M 5 .   ? 10.925    -0.799   -6.786    1.000 39.56885  ? 1088 HOH A O   1 
HETATM 4049 O  O   . HOH M 5 .   ? 16.825    -2.073   -27.188   1.000 44.66351  ? 1089 HOH A O   1 
HETATM 4050 O  O   . HOH M 5 .   ? 31.47162  17.35037 1.96475   1.000 49.93699  ? 1090 HOH A O   1 
HETATM 4051 O  O   A HOH M 5 .   ? 15.62930  19.45140 12.69684  0.607 36.69120  ? 1091 HOH A O   1 
HETATM 4052 O  O   B HOH M 5 .   ? 14.29990  18.98409 14.23100  0.393 33.92475  ? 1091 HOH A O   1 
HETATM 4053 O  O   . HOH M 5 .   ? -11.52884 40.10352 11.92645  1.000 43.76876  ? 1092 HOH A O   1 
HETATM 4054 O  O   . HOH M 5 .   ? -3.37232  23.11369 -16.67721 1.000 46.89905  ? 1093 HOH A O   1 
HETATM 4055 O  O   . HOH M 5 .   ? 7.04055   30.54505 16.52501  1.000 47.02837  ? 1094 HOH A O   1 
HETATM 4056 O  O   . HOH M 5 .   ? -11.53976 58.37592 41.44937  1.000 45.61883  ? 1095 HOH A O   1 
HETATM 4057 O  O   . HOH M 5 .   ? 18.59351  5.91600  -14.15955 1.000 49.12640  ? 1096 HOH A O   1 
HETATM 4058 O  O   . HOH M 5 .   ? 17.634    7.683    -32.950   1.000 48.46692  ? 1097 HOH A O   1 
HETATM 4059 O  O   . HOH M 5 .   ? -9.85277  19.70180 6.94905   1.000 49.74110  ? 1098 HOH A O   1 
HETATM 4060 O  O   . HOH M 5 .   ? -12.61380 61.70814 43.10088  1.000 53.22269  ? 1099 HOH A O   1 
HETATM 4061 O  O   . HOH M 5 .   ? 7.89640   27.84956 23.09599  1.000 46.43873  ? 1100 HOH A O   1 
HETATM 4062 O  O   . HOH M 5 .   ? -0.38736  4.36608  7.26340   1.000 46.25728  ? 1101 HOH A O   1 
HETATM 4063 O  O   . HOH M 5 .   ? 8.06570   64.64138 14.31287  1.000 58.33771  ? 1102 HOH A O   1 
HETATM 4064 O  O   . HOH M 5 .   ? 16.72096  8.27054  7.02831   1.000 35.09027  ? 1103 HOH A O   1 
HETATM 4065 O  O   . HOH M 5 .   ? 4.52463   5.44525  11.53466  1.000 47.43623  ? 1104 HOH A O   1 
HETATM 4066 O  O   . HOH M 5 .   ? -10.49957 59.96078 42.84976  1.000 43.14034  ? 1105 HOH A O   1 
HETATM 4067 O  O   . HOH M 5 .   ? 30.37678  17.04252 5.98184   1.000 51.11121  ? 1106 HOH A O   1 
HETATM 4068 O  O   . HOH M 5 .   ? 14.77578  -1.08734 -23.54970 1.000 40.74352  ? 1107 HOH A O   1 
HETATM 4069 O  O   . HOH M 5 .   ? 12.64533  4.44112  7.13360   1.000 41.63311  ? 1108 HOH A O   1 
HETATM 4070 O  O   . HOH M 5 .   ? -11.32693 33.18842 23.65593  1.000 39.77606  ? 1109 HOH A O   1 
HETATM 4071 O  O   . HOH M 5 .   ? 18.89139  20.90255 9.15024   1.000 49.99316  ? 1110 HOH A O   1 
HETATM 4072 O  O   . HOH M 5 .   ? 38.40548  5.30847  7.36786   1.000 49.39147  ? 1111 HOH A O   1 
HETATM 4073 O  O   . HOH M 5 .   ? 23.71494  14.46624 7.10233   1.000 48.41815  ? 1112 HOH A O   1 
HETATM 4074 O  O   . HOH M 5 .   ? -11.88419 25.47362 11.97576  1.000 51.41264  ? 1113 HOH A O   1 
HETATM 4075 O  O   . HOH M 5 .   ? -15.34912 36.57814 15.99071  1.000 40.62731  ? 1114 HOH A O   1 
HETATM 4076 O  O   . HOH M 5 .   ? 36.863    8.920    10.633    1.000 49.03224  ? 1115 HOH A O   1 
HETATM 4077 O  O   . HOH M 5 .   ? 13.44592  9.83313  10.24734  1.000 43.96164  ? 1116 HOH A O   1 
HETATM 4078 O  O   . HOH M 5 .   ? 14.43228  15.52552 -29.04789 1.000 49.43644  ? 1117 HOH A O   1 
HETATM 4079 O  O   . HOH M 5 .   ? -17.05448 39.01280 19.72284  1.000 37.59831  ? 1118 HOH A O   1 
HETATM 4080 O  O   . HOH M 5 .   ? 12.27005  11.28173 12.05582  1.000 46.65484  ? 1119 HOH A O   1 
HETATM 4081 O  O   . HOH M 5 .   ? -18.45755 37.82057 21.64897  1.000 52.68564  ? 1120 HOH A 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   . LYS A 8   ? 0.79015 0.47546 0.51581 0.04818  -0.01620 -0.01828 211 LYS A N   
2    C CA  . LYS A 8   ? 0.76946 0.48917 0.52023 0.04370  -0.02151 -0.01828 211 LYS A CA  
3    C C   . LYS A 8   ? 0.74865 0.45106 0.48970 0.03853  -0.00704 -0.01343 211 LYS A C   
4    O O   . LYS A 8   ? 0.82099 0.48127 0.52548 0.04331  0.00130  -0.00967 211 LYS A O   
5    C CB  . LYS A 8   ? 0.74315 0.47592 0.48895 0.05432  -0.04162 -0.02151 211 LYS A CB  
6    N N   . LYS A 9   ? 0.66751 0.40017 0.43907 0.02944  -0.00403 -0.01395 212 LYS A N   
7    C CA  . LYS A 9   ? 0.70560 0.42749 0.47294 0.02415  0.00814  -0.01068 212 LYS A CA  
8    C C   . LYS A 9   ? 0.69450 0.40828 0.43976 0.03273  -0.00148 -0.00702 212 LYS A C   
9    O O   . LYS A 9   ? 0.69331 0.42797 0.44445 0.03900  -0.01806 -0.00924 212 LYS A O   
10   C CB  . LYS A 9   ? 0.66728 0.42464 0.47337 0.01418  0.01106  -0.01394 212 LYS A CB  
11   C CG  . LYS A 9   ? 0.67041 0.43839 0.50299 0.00631  0.02040  -0.02052 212 LYS A CG  
12   C CD  . LYS A 9   ? 0.66896 0.46673 0.53476 -0.00046 0.02182  -0.02548 212 LYS A CD  
13   C CE  . LYS A 9   ? 0.71243 0.52034 0.60717 -0.00713 0.03117  -0.03553 212 LYS A CE  
14   N NZ  . LYS A 9   ? 0.70099 0.53482 0.62629 -0.01122 0.03112  -0.04306 212 LYS A NZ  
15   N N   . LYS A 10  ? 0.62147 0.30470 0.34262 0.03263  0.01007  -0.00282 213 LYS A N   
16   C CA  . LYS A 10  ? 0.61026 0.28784 0.31330 0.04073  0.00113  -0.00021 213 LYS A CA  
17   C C   . LYS A 10  ? 0.60065 0.31454 0.33492 0.03327  -0.00103 -0.00037 213 LYS A C   
18   O O   . LYS A 10  ? 0.58343 0.30561 0.33687 0.02247  0.01148  -0.00037 213 LYS A O   
19   C CB  . LYS A 10  ? 0.63145 0.26080 0.29389 0.04428  0.01412  0.00464  213 LYS A CB  
20   C CG  . LYS A 10  ? 0.78304 0.40662 0.42691 0.05379  0.00414  0.00651  213 LYS A CG  
21   C CD  . LYS A 10  ? 0.79000 0.35822 0.38263 0.06250  0.01304  0.01092  213 LYS A CD  
22   C CE  . LYS A 10  ? 0.80260 0.36981 0.38150 0.07211  0.00206  0.01154  213 LYS A CE  
23   N NZ  . LYS A 10  ? 0.94511 0.45455 0.46704 0.08484  0.00703  0.01521  213 LYS A NZ  
24   N N   . PRO A 11  ? 0.57645 0.31132 0.31679 0.03894  -0.01612 -0.00205 214 PRO A N   
25   C CA  . PRO A 11  ? 0.54343 0.30730 0.30833 0.03227  -0.01678 -0.00162 214 PRO A CA  
26   C C   . PRO A 11  ? 0.57113 0.31766 0.32410 0.02946  -0.00614 0.00294  214 PRO A C   
27   O O   . PRO A 11  ? 0.59699 0.30852 0.31831 0.03510  -0.00104 0.00579  214 PRO A O   
28   C CB  . PRO A 11  ? 0.54341 0.32503 0.31163 0.03976  -0.03280 -0.00585 214 PRO A CB  
29   C CG  . PRO A 11  ? 0.61669 0.39160 0.37566 0.04798  -0.04212 -0.01076 214 PRO A CG  
30   C CD  . PRO A 11  ? 0.65928 0.39515 0.38886 0.05117  -0.03314 -0.00684 214 PRO A CD  
31   N N   . GLN A 12  ? 0.52696 0.29638 0.30344 0.02139  -0.00294 0.00326  215 GLN A N   
32   C CA  . GLN A 12  ? 0.56385 0.32265 0.33500 0.01748  0.00667  0.00644  215 GLN A CA  
33   C C   . GLN A 12  ? 0.54388 0.32798 0.32953 0.01700  -0.00137 0.00679  215 GLN A C   
34   O O   . GLN A 12  ? 0.48282 0.29258 0.28577 0.01702  -0.01055 0.00419  215 GLN A O   
35   C CB  . GLN A 12  ? 0.56584 0.32414 0.35354 0.00667  0.02209  0.00417  215 GLN A CB  
36   C CG  . GLN A 12  ? 0.66619 0.40045 0.44465 0.00447  0.03393  0.00216  215 GLN A CG  
37   C CD  . GLN A 12  ? 0.76285 0.50093 0.56500 -0.00698 0.04986  -0.00412 215 GLN A CD  
38   O OE1 . GLN A 12  ? 0.80088 0.53166 0.60427 -0.01236 0.06048  -0.00481 215 GLN A OE1 
39   N NE2 . GLN A 12  ? 0.74994 0.50121 0.57369 -0.01053 0.05118  -0.01059 215 GLN A NE2 
40   N N   . ILE A 13  ? 0.52177 0.29625 0.29888 0.01615  0.00366  0.00985  216 ILE A N   
41   C CA  . ILE A 13  ? 0.50170 0.29860 0.29414 0.01372  -0.00074 0.01028  216 ILE A CA  
42   C C   . ILE A 13  ? 0.49338 0.28873 0.29466 0.00566  0.01070  0.01099  216 ILE A C   
43   O O   . ILE A 13  ? 0.57881 0.35018 0.36778 0.00308  0.02290  0.01173  216 ILE A O   
44   C CB  . ILE A 13  ? 0.53783 0.33181 0.31643 0.02177  -0.00943 0.01107  216 ILE A CB  
45   C CG1 . ILE A 13  ? 0.54329 0.30458 0.29270 0.02678  -0.00374 0.01446  216 ILE A CG1 
46   C CG2 . ILE A 13  ? 0.51853 0.32119 0.29710 0.02922  -0.02189 0.00612  216 ILE A CG2 
47   C CD1 . ILE A 13  ? 0.56762 0.32780 0.30585 0.03577  -0.01326 0.01353  216 ILE A CD1 
48   N N   . LYS A 14  ? 0.46168 0.28103 0.28373 0.00179  0.00743  0.00959  217 LYS A N   
49   C CA  . LYS A 14  ? 0.46464 0.28703 0.29885 -0.00466 0.01528  0.00787  217 LYS A CA  
50   C C   . LYS A 14  ? 0.45277 0.28979 0.29157 -0.00383 0.00880  0.01000  217 LYS A C   
51   O O   . LYS A 14  ? 0.45186 0.30232 0.29255 -0.00057 -0.00033 0.01078  217 LYS A O   
52   C CB  . LYS A 14  ? 0.51492 0.35129 0.37317 -0.00949 0.01773  0.00047  217 LYS A CB  
53   C CG  . LYS A 14  ? 0.55039 0.37279 0.40780 -0.01179 0.02647  -0.00311 217 LYS A CG  
54   C CD  . LYS A 14  ? 0.63751 0.47520 0.52302 -0.01628 0.02926  -0.01351 217 LYS A CD  
55   C CE  . LYS A 14  ? 0.76262 0.58505 0.64815 -0.01954 0.04019  -0.01780 217 LYS A CE  
56   N NZ  . LYS A 14  ? 0.84309 0.68069 0.76010 -0.02402 0.04420  -0.03122 217 LYS A NZ  
57   N N   . TYR A 15  ? 0.47279 0.30602 0.31389 -0.00756 0.01514  0.01002  218 TYR A N   
58   C CA  . TYR A 15  ? 0.44949 0.29510 0.29595 -0.00762 0.01062  0.01151  218 TYR A CA  
59   C C   . TYR A 15  ? 0.51433 0.36112 0.37420 -0.01343 0.01806  0.00684  218 TYR A C   
60   O O   . TYR A 15  ? 0.53574 0.36650 0.39256 -0.01754 0.02960  0.00485  218 TYR A O   
61   C CB  . TYR A 15  ? 0.47742 0.31398 0.30635 -0.00331 0.00835  0.01690  218 TYR A CB  
62   C CG  . TYR A 15  ? 0.42028 0.26942 0.25553 -0.00392 0.00467  0.01821  218 TYR A CG  
63   C CD1 . TYR A 15  ? 0.46249 0.32656 0.30275 -0.00199 -0.00285 0.01809  218 TYR A CD1 
64   C CD2 . TYR A 15  ? 0.48521 0.32975 0.32109 -0.00705 0.01021  0.01894  218 TYR A CD2 
65   C CE1 . TYR A 15  ? 0.45691 0.32919 0.30082 -0.00283 -0.00455 0.01923  218 TYR A CE1 
66   C CE2 . TYR A 15  ? 0.45886 0.31443 0.30017 -0.00738 0.00658  0.02010  218 TYR A CE2 
67   C CZ  . TYR A 15  ? 0.46459 0.33327 0.30918 -0.00512 -0.00072 0.02047  218 TYR A CZ  
68   O OH  . TYR A 15  ? 0.46469 0.34104 0.31232 -0.00563 -0.00279 0.02162  218 TYR A OH  
69   N N   . GLU A 16  ? 0.53169 0.39515 0.40513 -0.01351 0.01218  0.00394  219 GLU A N   
70   C CA  . GLU A 16  ? 0.53370 0.40073 0.42227 -0.01777 0.01695  -0.00292 219 GLU A CA  
71   C C   . GLU A 16  ? 0.54537 0.40476 0.42398 -0.01908 0.02051  0.00239  219 GLU A C   
72   O O   . GLU A 16  ? 0.51502 0.38263 0.39116 -0.01638 0.01333  0.00606  219 GLU A O   
73   C CB  . GLU A 16  ? 0.52807 0.41275 0.43140 -0.01459 0.00708  -0.00939 219 GLU A CB  
74   C CG  . GLU A 16  ? 0.55565 0.44655 0.47594 -0.01687 0.00848  -0.01869 219 GLU A CG  
75   C CD  . GLU A 16  ? 0.67546 0.56009 0.61082 -0.02434 0.02209  -0.02818 219 GLU A CD  
76   O OE1 . GLU A 16  ? 0.60471 0.47662 0.53307 -0.02960 0.03278  -0.02491 219 GLU A OE1 
77   O OE2 . GLU A 16  ? 0.73027 0.62131 0.68413 -0.02503 0.02319  -0.03979 219 GLU A OE2 
78   N N   . GLU A 17  ? 0.51840 0.35959 0.38962 -0.02328 0.03283  0.00252  220 GLU A N   
79   C CA  . GLU A 17  ? 0.56664 0.39652 0.42333 -0.02323 0.03639  0.00835  220 GLU A CA  
80   C C   . GLU A 17  ? 0.55735 0.39990 0.42906 -0.02611 0.03514  0.00459  220 GLU A C   
81   O O   . GLU A 17  ? 0.58575 0.42524 0.44759 -0.02471 0.03401  0.01011  220 GLU A O   
82   C CB  . GLU A 17  ? 0.60162 0.40283 0.44149 -0.02649 0.05170  0.00906  220 GLU A CB  
83   C CG  . GLU A 17  ? 0.63444 0.41668 0.45040 -0.02086 0.05146  0.01433  220 GLU A CG  
84   C CD  . GLU A 17  ? 0.69333 0.43850 0.48188 -0.02169 0.06669  0.01658  220 GLU A CD  
85   O OE1 . GLU A 17  ? 0.72392 0.45761 0.50857 -0.02607 0.07694  0.01598  220 GLU A OE1 
86   O OE2 . GLU A 17  ? 0.73228 0.45717 0.50059 -0.01749 0.06879  0.01884  220 GLU A OE2 
87   N N   . LYS A 18  ? 0.57579 0.43285 0.47142 -0.02883 0.03390  -0.00593 221 LYS A N   
88   C CA  . LYS A 18  ? 0.54910 0.41890 0.45832 -0.02936 0.02948  -0.01077 221 LYS A CA  
89   C C   . LYS A 18  ? 0.51429 0.39376 0.41477 -0.02289 0.01630  -0.00332 221 LYS A C   
90   O O   . LYS A 18  ? 0.55451 0.43963 0.45851 -0.02260 0.01306  -0.00387 221 LYS A O   
91   C CB  . LYS A 18  ? 0.61088 0.49429 0.54774 -0.03076 0.02796  -0.02670 221 LYS A CB  
92   C CG  . LYS A 18  ? 0.66531 0.54078 0.61805 -0.03976 0.04455  -0.03834 221 LYS A CG  
93   N N   A GLN A 19  ? 0.49121 0.37199 0.38115 -0.01823 0.00978  0.00244  222 GLN A N   
94   N N   B GLN A 19  ? 0.49422 0.37395 0.38298 -0.01840 0.01036  0.00307  222 GLN A N   
95   C CA  A GLN A 19  ? 0.50644 0.39293 0.38735 -0.01365 0.00118  0.00837  222 GLN A CA  
96   C CA  B GLN A 19  ? 0.50612 0.39216 0.38643 -0.01364 0.00137  0.00865  222 GLN A CA  
97   C C   A GLN A 19  ? 0.46484 0.34438 0.33180 -0.01341 0.00365  0.01665  222 GLN A C   
98   C C   B GLN A 19  ? 0.46559 0.34534 0.33204 -0.01317 0.00330  0.01692  222 GLN A C   
99   O O   A GLN A 19  ? 0.48009 0.35238 0.33735 -0.01192 0.00520  0.01978  222 GLN A O   
100  O O   B GLN A 19  ? 0.47764 0.35121 0.33427 -0.01134 0.00405  0.02027  222 GLN A O   
101  C CB  A GLN A 19  ? 0.50996 0.40031 0.38725 -0.00950 -0.00514 0.00853  222 GLN A CB  
102  C CB  B GLN A 19  ? 0.51361 0.40299 0.39104 -0.00992 -0.00414 0.00848  222 GLN A CB  
103  C CG  A GLN A 19  ? 0.51371 0.41075 0.40160 -0.00631 -0.01120 -0.00043 222 GLN A CG  
104  C CG  B GLN A 19  ? 0.46873 0.36084 0.33652 -0.00599 -0.01028 0.01223  222 GLN A CG  
105  C CD  A GLN A 19  ? 0.56118 0.46080 0.44669 -0.00186 -0.01849 -0.00246 222 GLN A CD  
106  C CD  B GLN A 19  ? 0.52157 0.41476 0.38642 -0.00271 -0.01422 0.01045  222 GLN A CD  
107  O OE1 A GLN A 19  ? 0.60452 0.50119 0.47936 -0.00193 -0.01826 0.00430  222 GLN A OE1 
108  O OE1 B GLN A 19  ? 0.57507 0.47112 0.44825 -0.00076 -0.01725 0.00370  222 GLN A OE1 
109  N NE2 A GLN A 19  ? 0.63284 0.53704 0.52808 0.00299  -0.02548 -0.01318 222 GLN A NE2 
110  N NE2 B GLN A 19  ? 0.53126 0.42272 0.38610 -0.00207 -0.01384 0.01481  222 GLN A NE2 
111  N N   . ALA A 20  ? 0.42577 0.30745 0.29207 -0.01374 0.00297  0.01877  223 ALA A N   
112  C CA  . ALA A 20  ? 0.47970 0.35757 0.33524 -0.01196 0.00329  0.02454  223 ALA A CA  
113  C C   . ALA A 20  ? 0.42840 0.31259 0.28046 -0.00890 -0.00182 0.02626  223 ALA A C   
114  O O   . ALA A 20  ? 0.46703 0.35615 0.32128 -0.00853 -0.00484 0.02496  223 ALA A O   
115  C CB  . ALA A 20  ? 0.51975 0.39861 0.37747 -0.01367 0.00476  0.02550  223 ALA A CB  
116  N N   . VAL A 21  ? 0.42817 0.31017 0.27379 -0.00609 -0.00232 0.02766  224 VAL A N   
117  C CA  . VAL A 21  ? 0.43127 0.31984 0.27748 -0.00442 -0.00466 0.02632  224 VAL A CA  
118  C C   . VAL A 21  ? 0.42067 0.31305 0.26890 -0.00455 -0.00414 0.02681  224 VAL A C   
119  O O   . VAL A 21  ? 0.45803 0.34750 0.30363 -0.00189 -0.00467 0.02696  224 VAL A O   
120  C CB  . VAL A 21  ? 0.41677 0.30316 0.25931 -0.00021 -0.00686 0.02345  224 VAL A CB  
121  C CG1 . VAL A 21  ? 0.43392 0.32914 0.28239 0.00037  -0.00759 0.01848  224 VAL A CG1 
122  C CG2 . VAL A 21  ? 0.41182 0.29377 0.25216 -0.00032 -0.00696 0.02325  224 VAL A CG2 
123  N N   . MET A 22  ? 0.42397 0.32025 0.27435 -0.00688 -0.00283 0.02686  225 MET A N   
124  C CA  . MET A 22  ? 0.42104 0.31983 0.27360 -0.00795 -0.00144 0.02777  225 MET A CA  
125  C C   . MET A 22  ? 0.39720 0.29920 0.25229 -0.00919 0.00242  0.02423  225 MET A C   
126  O O   . MET A 22  ? 0.44694 0.34438 0.29690 -0.01149 0.00603  0.02519  225 MET A O   
127  C CB  . MET A 22  ? 0.42695 0.32340 0.27807 -0.00952 -0.00229 0.03028  225 MET A CB  
128  C CG  . MET A 22  ? 0.49115 0.38578 0.34515 -0.00993 -0.00344 0.03036  225 MET A CG  
129  S SD  . MET A 22  ? 0.63253 0.52818 0.49178 -0.01119 -0.00560 0.02851  225 MET A SD  
130  C CE  . MET A 22  ? 0.66622 0.56013 0.52357 -0.00837 -0.01017 0.02443  225 MET A CE  
131  N N   . PRO A 23  ? 0.39618 0.30400 0.25839 -0.00717 0.00231  0.01857  226 PRO A N   
132  C CA  . PRO A 23  ? 0.44906 0.36156 0.31919 -0.00966 0.00829  0.01172  226 PRO A CA  
133  C C   . PRO A 23  ? 0.44329 0.35549 0.31457 -0.01239 0.01239  0.01351  226 PRO A C   
134  O O   . PRO A 23  ? 0.42994 0.34325 0.30081 -0.01063 0.00841  0.01754  226 PRO A O   
135  C CB  . PRO A 23  ? 0.45258 0.37375 0.33365 -0.00457 0.00409  0.00232  226 PRO A CB  
136  C CG  . PRO A 23  ? 0.48335 0.39930 0.35548 0.00125  -0.00378 0.00624  226 PRO A CG  
137  C CD  . PRO A 23  ? 0.41332 0.32156 0.27565 -0.00151 -0.00317 0.01653  226 PRO A CD  
138  N N   A GLU A 24  ? 0.43419 0.34249 0.30532 -0.01710 0.02176  0.01033  227 GLU A N   
139  N N   B GLU A 24  ? 0.43618 0.34480 0.30774 -0.01705 0.02173  0.01011  227 GLU A N   
140  C CA  A GLU A 24  ? 0.48094 0.38743 0.35330 -0.01997 0.02750  0.01052  227 GLU A CA  
141  C CA  B GLU A 24  ? 0.48130 0.38809 0.35394 -0.01987 0.02730  0.01047  227 GLU A CA  
142  C C   A GLU A 24  ? 0.45408 0.37492 0.34503 -0.01785 0.02549  0.00273  227 GLU A C   
143  C C   B GLU A 24  ? 0.45375 0.37474 0.34477 -0.01774 0.02528  0.00278  227 GLU A C   
144  O O   A GLU A 24  ? 0.43558 0.36567 0.33656 -0.01331 0.01986  -0.00427 227 GLU A O   
145  O O   B GLU A 24  ? 0.43504 0.36525 0.33594 -0.01308 0.01947  -0.00407 227 GLU A O   
146  C CB  A GLU A 24  ? 0.50144 0.39568 0.36687 -0.02582 0.04121  0.00737  227 GLU A CB  
147  C CB  B GLU A 24  ? 0.50118 0.39586 0.36697 -0.02569 0.04089  0.00738  227 GLU A CB  
148  C CG  A GLU A 24  ? 0.54298 0.41804 0.38415 -0.02560 0.04276  0.01445  227 GLU A CG  
149  C CG  B GLU A 24  ? 0.54887 0.42647 0.39276 -0.02546 0.04209  0.01347  227 GLU A CG  
150  C CD  A GLU A 24  ? 0.68415 0.53867 0.51000 -0.03063 0.05852  0.01229  227 GLU A CD  
151  C CD  B GLU A 24  ? 0.57378 0.44645 0.40499 -0.02062 0.03137  0.02272  227 GLU A CD  
152  O OE1 A GLU A 24  ? 0.71769 0.56669 0.54368 -0.03412 0.06738  0.01055  227 GLU A OE1 
153  O OE1 B GLU A 24  ? 0.62940 0.49871 0.45661 -0.02007 0.03029  0.02611  227 GLU A OE1 
154  O OE2 A GLU A 24  ? 0.67687 0.51827 0.48854 -0.03112 0.06314  0.01229  227 GLU A OE2 
155  O OE2 B GLU A 24  ? 0.61316 0.48635 0.44073 -0.01746 0.02415  0.02500  227 GLU A OE2 
156  N N   . SER A 25  ? 0.45355 0.37513 0.34790 -0.01984 0.02914  0.00310  228 SER A N   
157  C CA  . SER A 25  ? 0.40273 0.33817 0.31484 -0.01663 0.02617  -0.00499 228 SER A CA  
158  C C   . SER A 25  ? 0.39685 0.34242 0.32951 -0.01786 0.03247  -0.02147 228 SER A C   
159  O O   . SER A 25  ? 0.41306 0.37211 0.36222 -0.01180 0.02608  -0.03197 228 SER A O   
160  C CB  . SER A 25  ? 0.41241 0.34700 0.32467 -0.01883 0.02887  -0.00108 228 SER A CB  
161  O OG  . SER A 25  ? 0.49668 0.42187 0.40610 -0.02594 0.04225  -0.00270 228 SER A OG  
162  N N   . ALA A 26  ? 0.38949 0.32798 0.32155 -0.02491 0.04493  -0.02573 229 ALA A N   
163  C CA  . ALA A 26  ? 0.42037 0.36934 0.37630 -0.02780 0.05348  -0.04453 229 ALA A CA  
164  C C   . ALA A 26  ? 0.41407 0.37624 0.38210 -0.01978 0.04156  -0.05454 229 ALA A C   
165  O O   . ALA A 26  ? 0.40263 0.35963 0.35545 -0.01528 0.03216  -0.04544 229 ALA A O   
166  C CB  . ALA A 26  ? 0.42652 0.36012 0.37482 -0.03790 0.07182  -0.04639 229 ALA A CB  
167  N N   . ALA A 27  ? 0.39200 0.37095 0.38818 -0.01712 0.04148  -0.07498 230 ALA A N   
168  C CA  . ALA A 27  ? 0.42145 0.41181 0.43046 -0.00885 0.03088  -0.08892 230 ALA A CA  
169  C C   . ALA A 27  ? 0.41515 0.39883 0.41945 -0.01533 0.03881  -0.08936 230 ALA A C   
170  O O   . ALA A 27  ? 0.42383 0.39798 0.42589 -0.02698 0.05661  -0.08866 230 ALA A O   
171  C CB  . ALA A 27  ? 0.40417 0.41489 0.44885 -0.00534 0.03087  -0.11553 230 ALA A CB  
172  N N   . GLY A 28  ? 0.35468 0.34063 0.35487 -0.00724 0.02607  -0.09068 231 GLY A N   
173  C CA  . GLY A 28  ? 0.39317 0.37513 0.39163 -0.01262 0.03244  -0.09296 231 GLY A CA  
174  C C   . GLY A 28  ? 0.41994 0.40013 0.40581 -0.00281 0.01647  -0.08803 231 GLY A C   
175  O O   . GLY A 28  ? 0.37765 0.35443 0.35021 0.00723  0.00249  -0.07989 231 GLY A O   
176  N N   . THR A 29  ? 0.37389 0.35419 0.36281 -0.00615 0.02013  -0.09355 232 THR A N   
177  C CA  . THR A 29  ? 0.34537 0.32126 0.32026 0.00119  0.00766  -0.08751 232 THR A CA  
178  C C   . THR A 29  ? 0.38333 0.34296 0.33310 -0.00565 0.01367  -0.06655 232 THR A C   
179  O O   . THR A 29  ? 0.41440 0.36848 0.36269 -0.01525 0.02710  -0.06598 232 THR A O   
180  C CB  . THR A 29  ? 0.36914 0.35627 0.36361 0.00274  0.00618  -0.10713 232 THR A CB  
181  O OG1 . THR A 29  ? 0.41951 0.42309 0.43951 0.01144  -0.00198 -0.12983 232 THR A OG1 
182  C CG2 . THR A 29  ? 0.39476 0.37505 0.37209 0.01029  -0.00641 -0.09954 232 THR A CG2 
183  N N   . TYR A 30  ? 0.35939 0.30985 0.28908 -0.00031 0.00444  -0.05088 233 TYR A N   
184  C CA  . TYR A 30  ? 0.37407 0.31134 0.28322 -0.00479 0.00755  -0.03362 233 TYR A CA  
185  C C   . TYR A 30  ? 0.38503 0.31827 0.28483 -0.00031 -0.00044 -0.02974 233 TYR A C   
186  O O   . TYR A 30  ? 0.37218 0.30883 0.27514 0.00789  -0.01012 -0.03691 233 TYR A O   
187  C CB  . TYR A 30  ? 0.37403 0.30485 0.27158 -0.00385 0.00537  -0.02114 233 TYR A CB  
188  C CG  . TYR A 30  ? 0.39164 0.32479 0.29646 -0.00879 0.01383  -0.02351 233 TYR A CG  
189  C CD1 . TYR A 30  ? 0.40845 0.33201 0.30459 -0.01647 0.02486  -0.01779 233 TYR A CD1 
190  C CD2 . TYR A 30  ? 0.40349 0.34616 0.32175 -0.00468 0.01058  -0.03212 233 TYR A CD2 
191  C CE1 . TYR A 30  ? 0.42985 0.35189 0.32963 -0.02106 0.03384  -0.01957 233 TYR A CE1 
192  C CE2 . TYR A 30  ? 0.40947 0.35449 0.33584 -0.00984 0.01937  -0.03474 233 TYR A CE2 
193  C CZ  . TYR A 30  ? 0.41288 0.34678 0.32940 -0.01861 0.03171  -0.02792 233 TYR A CZ  
194  O OH  . TYR A 30  ? 0.43710 0.36900 0.35787 -0.02398 0.04196  -0.02984 233 TYR A OH  
195  N N   . THR A 31  ? 0.36887 0.29345 0.25606 -0.00468 0.00319  -0.01940 234 THR A N   
196  C CA  . THR A 31  ? 0.37018 0.29179 0.25107 -0.00188 -0.00235 -0.01692 234 THR A CA  
197  C C   . THR A 31  ? 0.38314 0.29509 0.24954 -0.00248 -0.00368 -0.00370 234 THR A C   
198  O O   . THR A 31  ? 0.39784 0.30528 0.25859 -0.00577 0.00030  0.00272  234 THR A O   
199  C CB  . THR A 31  ? 0.41153 0.33565 0.29772 -0.00632 0.00352  -0.02363 234 THR A CB  
200  O OG1 . THR A 31  ? 0.39217 0.30714 0.26810 -0.01273 0.01305  -0.01701 234 THR A OG1 
201  C CG2 . THR A 31  ? 0.39078 0.32638 0.29675 -0.00707 0.00670  -0.04057 234 THR A CG2 
202  N N   . PHE A 32  ? 0.36917 0.27775 0.23064 0.00118  -0.00940 -0.00154 235 PHE A N   
203  C CA  . PHE A 32  ? 0.38760 0.28949 0.24095 -0.00003 -0.00967 0.00663  235 PHE A CA  
204  C C   . PHE A 32  ? 0.39672 0.29828 0.24970 0.00173  -0.01267 0.00444  235 PHE A C   
205  O O   . PHE A 32  ? 0.39203 0.29746 0.24939 0.00468  -0.01567 -0.00275 235 PHE A O   
206  C CB  . PHE A 32  ? 0.37561 0.27072 0.22337 0.00167  -0.01123 0.01241  235 PHE A CB  
207  C CG  . PHE A 32  ? 0.39659 0.28471 0.23825 0.00768  -0.01541 0.01084  235 PHE A CG  
208  C CD1 . PHE A 32  ? 0.39858 0.28680 0.23949 0.01259  -0.01846 0.00692  235 PHE A CD1 
209  C CD2 . PHE A 32  ? 0.41895 0.29762 0.25329 0.00945  -0.01622 0.01270  235 PHE A CD2 
210  C CE1 . PHE A 32  ? 0.41408 0.29033 0.24272 0.02102  -0.02370 0.00515  235 PHE A CE1 
211  C CE2 . PHE A 32  ? 0.41721 0.28230 0.23858 0.01638  -0.01932 0.01181  235 PHE A CE2 
212  C CZ  . PHE A 32  ? 0.43316 0.29576 0.24964 0.02299  -0.02374 0.00821  235 PHE A CZ  
213  N N   . GLU A 33  ? 0.37700 0.27482 0.22645 0.00049  -0.01255 0.00902  236 GLU A N   
214  C CA  . GLU A 33  ? 0.38394 0.28180 0.23379 0.00157  -0.01480 0.00731  236 GLU A CA  
215  C C   . GLU A 33  ? 0.42102 0.31101 0.26720 0.00343  -0.01615 0.01015  236 GLU A C   
216  O O   . GLU A 33  ? 0.42436 0.30988 0.26967 0.00184  -0.01365 0.01357  236 GLU A O   
217  C CB  . GLU A 33  ? 0.41215 0.31122 0.26121 -0.00072 -0.01296 0.00797  236 GLU A CB  
218  C CG  . GLU A 33  ? 0.45245 0.35272 0.30012 -0.00329 -0.00809 0.00504  236 GLU A CG  
219  C CD  . GLU A 33  ? 0.52801 0.42229 0.36662 -0.00367 -0.00585 0.00633  236 GLU A CD  
220  O OE1 . GLU A 33  ? 0.51462 0.40590 0.34976 -0.00096 -0.00983 0.00917  236 GLU A OE1 
221  O OE2 . GLU A 33  ? 0.50595 0.39716 0.34049 -0.00616 0.00027  0.00302  236 GLU A OE2 
222  N N   . VAL A 34  ? 0.40733 0.29436 0.25142 0.00643  -0.01899 0.00761  237 VAL A N   
223  C CA  . VAL A 34  ? 0.40868 0.28409 0.24677 0.00767  -0.01782 0.00958  237 VAL A CA  
224  C C   . VAL A 34  ? 0.44336 0.32327 0.28703 0.00676  -0.01894 0.00746  237 VAL A C   
225  O O   . VAL A 34  ? 0.42168 0.30835 0.26789 0.00836  -0.02276 0.00363  237 VAL A O   
226  C CB  . VAL A 34  ? 0.41340 0.27502 0.23770 0.01432  -0.02069 0.00854  237 VAL A CB  
227  C CG1 . VAL A 34  ? 0.51779 0.36269 0.33177 0.01548  -0.01754 0.01018  237 VAL A CG1 
228  C CG2 . VAL A 34  ? 0.43037 0.28472 0.24708 0.01596  -0.01921 0.01098  237 VAL A CG2 
229  N N   A GLN A 35  ? 0.41180 0.28891 0.25954 0.00409  -0.01531 0.00823  238 GLN A N   
230  N N   B GLN A 35  ? 0.41181 0.28906 0.25966 0.00405  -0.01530 0.00823  238 GLN A N   
231  C CA  A GLN A 35  ? 0.41728 0.29937 0.27188 0.00376  -0.01670 0.00533  238 GLN A CA  
232  C CA  B GLN A 35  ? 0.41761 0.29934 0.27200 0.00379  -0.01663 0.00536  238 GLN A CA  
233  C C   A GLN A 35  ? 0.44541 0.31764 0.29268 0.00666  -0.01744 0.00442  238 GLN A C   
234  C C   B GLN A 35  ? 0.44538 0.31740 0.29193 0.00694  -0.01772 0.00448  238 GLN A C   
235  O O   A GLN A 35  ? 0.42701 0.28249 0.26343 0.00769  -0.01319 0.00622  238 GLN A O   
236  O O   B GLN A 35  ? 0.42946 0.28473 0.26400 0.00863  -0.01430 0.00634  238 GLN A O   
237  C CB  A GLN A 35  ? 0.45469 0.33853 0.31987 0.00083  -0.01311 0.00310  238 GLN A CB  
238  C CB  B GLN A 35  ? 0.45302 0.33545 0.31767 0.00079  -0.01261 0.00313  238 GLN A CB  
239  C CG  A GLN A 35  ? 0.41385 0.30382 0.28345 -0.00008 -0.01373 0.00301  238 GLN A CG  
240  C CG  B GLN A 35  ? 0.43514 0.32520 0.30946 0.00141  -0.01523 -0.00144 238 GLN A CG  
241  C CD  A GLN A 35  ? 0.49808 0.39523 0.36379 0.00205  -0.01864 0.00373  238 GLN A CD  
242  C CD  B GLN A 35  ? 0.52118 0.41527 0.41047 -0.00026 -0.01281 -0.00763 238 GLN A CD  
243  O OE1 A GLN A 35  ? 0.49346 0.39029 0.35399 0.00176  -0.01827 0.00629  238 GLN A OE1 
244  O OE1 B GLN A 35  ? 0.52390 0.41234 0.41740 -0.00350 -0.00637 -0.00918 238 GLN A OE1 
245  N NE2 A GLN A 35  ? 0.51326 0.41469 0.38006 0.00391  -0.02185 0.00122  238 GLN A NE2 
246  N NE2 B GLN A 35  ? 0.51254 0.41645 0.41086 0.00245  -0.01806 -0.01297 238 GLN A NE2 
247  N N   . THR A 36  ? 0.40788 0.28770 0.25842 0.00842  -0.02236 0.00139  239 THR A N   
248  C CA  . THR A 36  ? 0.43402 0.30534 0.27756 0.01229  -0.02497 -0.00052 239 THR A CA  
249  C C   . THR A 36  ? 0.43098 0.30603 0.28366 0.01008  -0.02351 -0.00238 239 THR A C   
250  O O   . THR A 36  ? 0.44410 0.33366 0.30722 0.00890  -0.02647 -0.00473 239 THR A O   
251  C CB  . THR A 36  ? 0.41033 0.28886 0.25325 0.01657  -0.03258 -0.00526 239 THR A CB  
252  O OG1 . THR A 36  ? 0.43714 0.33251 0.29210 0.01297  -0.03307 -0.00776 239 THR A OG1 
253  C CG2 . THR A 36  ? 0.44127 0.31433 0.27579 0.02069  -0.03490 -0.00603 239 THR A CG2 
254  N N   . ILE A 37  ? 0.43848 0.29812 0.28571 0.00970  -0.01789 -0.00190 240 ILE A N   
255  C CA  . ILE A 37  ? 0.46092 0.32268 0.31943 0.00686  -0.01420 -0.00516 240 ILE A CA  
256  C C   . ILE A 37  ? 0.50476 0.35686 0.35414 0.01065  -0.01674 -0.00620 240 ILE A C   
257  O O   . ILE A 37  ? 0.48616 0.31770 0.31519 0.01510  -0.01631 -0.00407 240 ILE A O   
258  C CB  . ILE A 37  ? 0.50182 0.35216 0.36412 0.00181  -0.00245 -0.00626 240 ILE A CB  
259  C CG1 . ILE A 37  ? 0.59929 0.46027 0.47172 -0.00099 -0.00167 -0.00669 240 ILE A CG1 
260  C CG2 . ILE A 37  ? 0.54632 0.39951 0.42417 -0.00131 0.00243  -0.01261 240 ILE A CG2 
261  C CD1 . ILE A 37  ? 0.62284 0.50444 0.51510 -0.00120 -0.00675 -0.01239 240 ILE A CD1 
262  N N   . ASP A 38  ? 0.45209 0.31716 0.31441 0.01015  -0.02014 -0.00994 241 ASP A N   
263  C CA  . ASP A 38  ? 0.45096 0.30844 0.30745 0.01329  -0.02252 -0.01174 241 ASP A CA  
264  C C   . ASP A 38  ? 0.48733 0.34001 0.32882 0.02033  -0.03170 -0.01193 241 ASP A C   
265  O O   . ASP A 38  ? 0.60797 0.44249 0.43357 0.02561  -0.03331 -0.01250 241 ASP A O   
266  C CB  . ASP A 38  ? 0.54757 0.38070 0.39492 0.01144  -0.01125 -0.01132 241 ASP A CB  
267  C CG  . ASP A 38  ? 0.56667 0.40856 0.43656 0.00470  -0.00279 -0.01634 241 ASP A CG  
268  O OD1 . ASP A 38  ? 0.53291 0.39807 0.42246 0.00437  -0.00908 -0.02053 241 ASP A OD1 
269  O OD2 . ASP A 38  ? 0.62134 0.44578 0.48927 0.00015  0.01054  -0.01761 241 ASP A OD2 
270  N N   . GLY A 39  ? 0.47365 0.34106 0.31986 0.02111  -0.03765 -0.01313 242 GLY A N   
271  C CA  . GLY A 39  ? 0.45116 0.31878 0.29016 0.02771  -0.04676 -0.01762 242 GLY A CA  
272  C C   . GLY A 39  ? 0.44892 0.31096 0.27906 0.03040  -0.04748 -0.01670 242 GLY A C   
273  O O   . GLY A 39  ? 0.47939 0.34174 0.31129 0.02580  -0.04105 -0.01184 242 GLY A O   
274  N N   . LYS A 40  ? 0.48146 0.33903 0.30303 0.03895  -0.05656 -0.02303 243 LYS A N   
275  C CA  . LYS A 40  ? 0.45810 0.31333 0.27394 0.04340  -0.05973 -0.02532 243 LYS A CA  
276  C C   . LYS A 40  ? 0.52221 0.34741 0.30917 0.05458  -0.06366 -0.02454 243 LYS A C   
277  O O   . LYS A 40  ? 0.54799 0.36467 0.32442 0.06531  -0.07432 -0.03222 243 LYS A O   
278  C CB  . LYS A 40  ? 0.50116 0.37754 0.33392 0.04515  -0.06738 -0.03732 243 LYS A CB  
279  C CG  . LYS A 40  ? 0.43210 0.33113 0.28648 0.03425  -0.06064 -0.03760 243 LYS A CG  
280  C CD  . LYS A 40  ? 0.42000 0.31933 0.27440 0.02823  -0.05239 -0.02975 243 LYS A CD  
281  C CE  . LYS A 40  ? 0.42813 0.34355 0.29690 0.01963  -0.04590 -0.03066 243 LYS A CE  
282  N NZ  . LYS A 40  ? 0.38874 0.30192 0.25475 0.01517  -0.03909 -0.02302 243 LYS A NZ  
283  N N   . LEU A 41  ? 0.48393 0.29083 0.25609 0.05278  -0.05501 -0.01604 244 LEU A N   
284  C CA  . LEU A 41  ? 0.55494 0.32682 0.29317 0.06358  -0.05628 -0.01422 244 LEU A CA  
285  C C   . LEU A 41  ? 0.55475 0.32668 0.28575 0.07624  -0.06988 -0.02314 244 LEU A C   
286  O O   . LEU A 41  ? 0.55978 0.35446 0.31045 0.07294  -0.07167 -0.02680 244 LEU A O   
287  C CB  . LEU A 41  ? 0.52840 0.28243 0.25541 0.05701  -0.04172 -0.00440 244 LEU A CB  
288  C CG  . LEU A 41  ? 0.62326 0.33514 0.31016 0.06679  -0.03879 -0.00093 244 LEU A CG  
289  C CD1 . LEU A 41  ? 0.66572 0.34673 0.32689 0.07256  -0.03668 -0.00036 244 LEU A CD1 
290  C CD2 . LEU A 41  ? 0.61024 0.31311 0.29582 0.05688  -0.02274 0.00687  244 LEU A CD2 
291  N N   . ASP A 42  ? 0.57167 0.31632 0.27338 0.09186  -0.07978 -0.02799 245 ASP A N   
292  C CA  . ASP A 42  ? 0.60537 0.34635 0.29734 0.10746  -0.09496 -0.03913 245 ASP A CA  
293  C C   . ASP A 42  ? 0.65901 0.37313 0.32375 0.11161  -0.08937 -0.03155 245 ASP A C   
294  O O   . ASP A 42  ? 0.71712 0.38915 0.34047 0.12183  -0.08793 -0.02686 245 ASP A O   
295  C CB  . ASP A 42  ? 0.64438 0.36605 0.31436 0.12530  -0.11068 -0.04956 245 ASP A CB  
296  C CG  . ASP A 42  ? 0.71165 0.43783 0.38086 0.14278  -0.12997 -0.06676 245 ASP A CG  
297  O OD1 . ASP A 42  ? 0.77002 0.52042 0.46280 0.13880  -0.13024 -0.07169 245 ASP A OD1 
298  O OD2 . ASP A 42  ? 0.82221 0.52686 0.46706 0.16155  -0.14546 -0.07680 245 ASP A OD2 
299  N N   . TYR A 43  ? 0.62264 0.35850 0.30840 0.10349  -0.08500 -0.03016 246 TYR A N   
300  C CA  . TYR A 43  ? 0.63478 0.35045 0.29996 0.10586  -0.07941 -0.02347 246 TYR A CA  
301  C C   . TYR A 43  ? 0.65979 0.39605 0.34069 0.11216  -0.09026 -0.03401 246 TYR A C   
302  O O   . TYR A 43  ? 0.60728 0.37678 0.32071 0.11021  -0.09764 -0.04568 246 TYR A O   
303  C CB  . TYR A 43  ? 0.61535 0.33549 0.29131 0.08767  -0.06023 -0.01019 246 TYR A CB  
304  C CG  . TYR A 43  ? 0.52795 0.28977 0.24523 0.07411  -0.05762 -0.01130 246 TYR A CG  
305  C CD1 . TYR A 43  ? 0.53915 0.32359 0.28099 0.06434  -0.05512 -0.01188 246 TYR A CD1 
306  C CD2 . TYR A 43  ? 0.52576 0.30119 0.25427 0.07203  -0.05753 -0.01193 246 TYR A CD2 
307  C CE1 . TYR A 43  ? 0.52126 0.33654 0.29313 0.05372  -0.05217 -0.01268 246 TYR A CE1 
308  C CE2 . TYR A 43  ? 0.50790 0.31541 0.26844 0.06053  -0.05410 -0.01274 246 TYR A CE2 
309  C CZ  . TYR A 43  ? 0.49904 0.32432 0.27893 0.05175  -0.05117 -0.01288 246 TYR A CZ  
310  O OH  . TYR A 43  ? 0.46490 0.31548 0.26959 0.04183  -0.04713 -0.01345 246 TYR A OH  
311  N N   . GLU A 44  ? 0.61979 0.33511 0.27781 0.11910  -0.08956 -0.03063 247 GLU A N   
312  C CA  . GLU A 44  ? 0.64600 0.38003 0.31938 0.12460  -0.09837 -0.04034 247 GLU A CA  
313  C C   . GLU A 44  ? 0.63874 0.36904 0.30963 0.11525  -0.08546 -0.02855 247 GLU A C   
314  O O   . GLU A 44  ? 0.66744 0.36258 0.30434 0.11716  -0.07691 -0.01792 247 GLU A O   
315  C CB  . GLU A 44  ? 0.76670 0.47921 0.41326 0.14961  -0.11782 -0.05415 247 GLU A CB  
316  C CG  . GLU A 44  ? 0.85219 0.59235 0.52514 0.15639  -0.12980 -0.07063 247 GLU A CG  
317  C CD  . GLU A 44  ? 0.95012 0.67055 0.59858 0.18395  -0.15210 -0.08799 247 GLU A CD  
318  O OE1 . GLU A 44  ? 0.92463 0.63677 0.56194 0.19436  -0.15776 -0.09174 247 GLU A OE1 
319  O OE2 . GLU A 44  ? 0.96040 0.67523 0.60455 0.19558  -0.16386 -0.09747 247 GLU A OE2 
320  N N   . PRO A 45  ? 0.59949 0.36294 0.30439 0.10462  -0.08232 -0.03044 248 PRO A N   
321  C CA  . PRO A 45  ? 0.55849 0.31971 0.26210 0.09682  -0.07181 -0.02061 248 PRO A CA  
322  C C   . PRO A 45  ? 0.61230 0.36098 0.29908 0.11186  -0.08144 -0.02691 248 PRO A C   
323  O O   . PRO A 45  ? 0.64689 0.40427 0.33966 0.12553  -0.09703 -0.04260 248 PRO A O   
324  C CB  . PRO A 45  ? 0.53775 0.33765 0.28226 0.08136  -0.06619 -0.02161 248 PRO A CB  
325  C CG  . PRO A 45  ? 0.57783 0.39992 0.34422 0.08637  -0.07725 -0.03763 248 PRO A CG  
326  C CD  . PRO A 45  ? 0.59128 0.39355 0.33637 0.09824  -0.08623 -0.04178 248 PRO A CD  
327  N N   . TYR A 46  ? 0.58618 0.31528 0.25377 0.10937  -0.07204 -0.01617 249 TYR A N   
328  C CA  . TYR A 46  ? 0.60459 0.31696 0.25098 0.12387  -0.07977 -0.02015 249 TYR A CA  
329  C C   . TYR A 46  ? 0.62234 0.33858 0.27480 0.11181  -0.06687 -0.00984 249 TYR A C   
330  O O   . TYR A 46  ? 0.59509 0.30482 0.24639 0.09749  -0.05106 0.00224  249 TYR A O   
331  C CB  . TYR A 46  ? 0.65533 0.31653 0.24741 0.14135  -0.08316 -0.01773 249 TYR A CB  
332  C CG  . TYR A 46  ? 0.79148 0.43943 0.36662 0.15935  -0.09955 -0.02936 249 TYR A CG  
333  C CD1 . TYR A 46  ? 0.88680 0.52968 0.45071 0.18245  -0.12064 -0.04567 249 TYR A CD1 
334  C CD2 . TYR A 46  ? 0.86522 0.50465 0.43498 0.15462  -0.09494 -0.02547 249 TYR A CD2 
335  C CE1 . TYR A 46  ? 0.95760 0.59019 0.51246 0.19946  -0.13576 -0.05792 249 TYR A CE1 
336  C CE2 . TYR A 46  ? 0.87416 0.50041 0.42731 0.17182  -0.11078 -0.03657 249 TYR A CE2 
337  C CZ  . TYR A 46  ? 0.92774 0.55065 0.47402 0.19426  -0.13124 -0.05296 249 TYR A CZ  
338  O OH  . TYR A 46  ? 1.07718 0.69239 0.62110 0.21042  -0.14525 -0.06428 249 TYR A OH  
339  N N   . PHE A 47  ? 0.60891 0.33462 0.26762 0.11867  -0.07413 -0.01620 250 PHE A N   
340  C CA  . PHE A 47  ? 0.60834 0.32842 0.26249 0.11154  -0.06365 -0.00668 250 PHE A CA  
341  C C   . PHE A 47  ? 0.64651 0.31740 0.24999 0.12211  -0.05943 0.00039  250 PHE A C   
342  O O   . PHE A 47  ? 0.74390 0.38569 0.31342 0.14149  -0.07068 -0.00561 250 PHE A O   
343  C CB  . PHE A 47  ? 0.59544 0.34123 0.27300 0.11527  -0.07209 -0.01602 250 PHE A CB  
344  C CG  . PHE A 47  ? 0.56189 0.35018 0.28589 0.10035  -0.06894 -0.01977 250 PHE A CG  
345  C CD1 . PHE A 47  ? 0.53128 0.33163 0.27112 0.08177  -0.05461 -0.00827 250 PHE A CD1 
346  C CD2 . PHE A 47  ? 0.55467 0.36803 0.30474 0.10544  -0.07966 -0.03614 250 PHE A CD2 
347  C CE1 . PHE A 47  ? 0.53066 0.36311 0.30563 0.06957  -0.05114 -0.01110 250 PHE A CE1 
348  C CE2 . PHE A 47  ? 0.49798 0.34411 0.28575 0.09104  -0.07346 -0.03938 250 PHE A CE2 
349  C CZ  . PHE A 47  ? 0.51444 0.36780 0.31149 0.07368  -0.05923 -0.02585 250 PHE A CZ  
350  N N   . THR A 48  ? 0.70711 0.36616 0.30380 0.10962  -0.04247 0.01226  251 THR A N   
351  C CA  . THR A 48  ? 0.72031 0.32893 0.26755 0.11707  -0.03372 0.01914  251 THR A CA  
352  C C   . THR A 48  ? 0.78382 0.37944 0.31224 0.13326  -0.04339 0.01353  251 THR A C   
353  O O   . THR A 48  ? 0.81933 0.37824 0.31568 0.14188  -0.03801 0.01195  251 THR A O   
354  C CB  . THR A 48  ? 0.72900 0.33062 0.27996 0.09731  -0.01064 0.03026  251 THR A CB  
355  O OG1 . THR A 48  ? 0.72262 0.35492 0.30450 0.08757  -0.00900 0.03107  251 THR A OG1 
356  C CG2 . THR A 48  ? 0.72246 0.33873 0.29655 0.08197  -0.00127 0.03275  251 THR A CG2 
357  N N   . SER A 49  ? 0.75362 0.38377 0.31082 0.13555  -0.05544 0.00672  252 SER A N   
358  C CA  . SER A 49  ? 0.79621 0.41910 0.34036 0.15155  -0.06653 -0.00021 252 SER A CA  
359  C C   . SER A 49  ? 0.82728 0.47157 0.38658 0.16918  -0.09026 -0.01841 252 SER A C   
360  O O   . SER A 49  ? 0.87662 0.56064 0.47887 0.16042  -0.09382 -0.02563 252 SER A O   
361  C CB  . SER A 49  ? 0.84343 0.49063 0.41347 0.13829  -0.05882 0.00471  252 SER A CB  
362  O OG  . SER A 49  ? 1.00280 0.64437 0.56092 0.15458  -0.07065 -0.00259 252 SER A OG  
363  N N   . SER A 50  ? 1.03673 0.66025 0.57614 0.19025  -0.10163 -0.02945 253 SER A N   
364  C CA  . SER A 50  ? 1.05398 0.69968 0.61336 0.20878  -0.12462 -0.05023 253 SER A CA  
365  C C   . SER A 50  ? 1.05485 0.72557 0.63601 0.21089  -0.13087 -0.05708 253 SER A C   
366  O O   . SER A 50  ? 1.05141 0.74799 0.65949 0.22374  -0.14834 -0.07686 253 SER A O   
367  C CB  . SER A 50  ? 1.18856 0.79761 0.71815 0.23340  -0.13515 -0.06089 253 SER A CB  
368  N N   . THR A 51  ? 1.08003 0.74520 0.65435 0.19823  -0.11636 -0.04255 254 THR A N   
369  C CA  . THR A 51  ? 1.00349 0.69413 0.60056 0.19698  -0.11992 -0.04687 254 THR A CA  
370  C C   . THR A 51  ? 0.92458 0.65560 0.56989 0.16863  -0.10406 -0.03879 254 THR A C   
371  O O   . THR A 51  ? 0.84968 0.57891 0.49511 0.15346  -0.08886 -0.02442 254 THR A O   
372  C CB  . THR A 51  ? 1.04583 0.70496 0.61376 0.20067  -0.11108 -0.03857 254 THR A CB  
373  O OG1 . THR A 51  ? 1.02483 0.67580 0.58651 0.17882  -0.08928 -0.01870 254 THR A OG1 
374  C CG2 . THR A 51  ? 0.94393 0.55746 0.47142 0.21867  -0.11303 -0.04347 254 THR A CG2 
375  N N   . LEU A 52  ? 0.76622 0.53177 0.45105 0.16228  -0.10774 -0.04927 255 LEU A N   
376  C CA  . LEU A 52  ? 0.64639 0.44869 0.37506 0.13887  -0.09512 -0.04497 255 LEU A CA  
377  C C   . LEU A 52  ? 0.67084 0.50879 0.44027 0.14310  -0.10500 -0.06578 255 LEU A C   
378  O O   . LEU A 52  ? 0.68363 0.54094 0.47745 0.14217  -0.10892 -0.07846 255 LEU A O   
379  C CB  . LEU A 52  ? 0.64146 0.44619 0.37549 0.12563  -0.08635 -0.03755 255 LEU A CB  
380  N N   . PRO A 53  ? 0.59525 0.44212 0.37386 0.14809  -0.10869 -0.07161 256 PRO A N   
381  C CA  . PRO A 53  ? 0.52167 0.40247 0.34204 0.15210  -0.11674 -0.09443 256 PRO A CA  
382  C C   . PRO A 53  ? 0.56529 0.47838 0.42811 0.12969  -0.10237 -0.09487 256 PRO A C   
383  O O   . PRO A 53  ? 0.56211 0.50168 0.46120 0.13046  -0.10563 -0.11579 256 PRO A O   
384  C CB  . PRO A 53  ? 0.55712 0.43694 0.37429 0.16011  -0.12096 -0.09646 256 PRO A CB  
385  C CG  . PRO A 53  ? 0.65001 0.50758 0.43901 0.14853  -0.10717 -0.07078 256 PRO A CG  
386  C CD  . PRO A 53  ? 0.68980 0.51800 0.44479 0.14829  -0.10365 -0.05849 256 PRO A CD  
387  N N   . TRP A 54  ? 0.53004 0.43983 0.38860 0.11054  -0.08629 -0.07419 257 TRP A N   
388  C CA  . TRP A 54  ? 0.45431 0.38785 0.34492 0.09088  -0.07237 -0.07302 257 TRP A CA  
389  C C   . TRP A 54  ? 0.48933 0.42490 0.38423 0.08391  -0.06834 -0.07298 257 TRP A C   
390  O O   . TRP A 54  ? 0.43767 0.38657 0.35174 0.06809  -0.05585 -0.07033 257 TRP A O   
391  C CB  . TRP A 54  ? 0.41336 0.34318 0.29816 0.07595  -0.05925 -0.05325 257 TRP A CB  
392  C CG  . TRP A 54  ? 0.45842 0.36302 0.31064 0.07325  -0.05533 -0.03398 257 TRP A CG  
393  C CD1 . TRP A 54  ? 0.49124 0.37253 0.31405 0.08171  -0.05848 -0.02637 257 TRP A CD1 
394  C CD2 . TRP A 54  ? 0.46141 0.36107 0.30871 0.06075  -0.04594 -0.02175 257 TRP A CD2 
395  N NE1 . TRP A 54  ? 0.47384 0.33662 0.27630 0.07382  -0.04986 -0.01114 257 TRP A NE1 
396  C CE2 . TRP A 54  ? 0.49212 0.36727 0.31049 0.06163  -0.04333 -0.00865 257 TRP A CE2 
397  C CE3 . TRP A 54  ? 0.43184 0.34399 0.29568 0.04937  -0.03898 -0.02168 257 TRP A CE3 
398  C CZ2 . TRP A 54  ? 0.48959 0.35606 0.30011 0.05138  -0.03471 0.00264  257 TRP A CZ2 
399  C CZ3 . TRP A 54  ? 0.42993 0.33222 0.28238 0.04088  -0.03235 -0.00915 257 TRP A CZ3 
400  C CH2 . TRP A 54  ? 0.46521 0.34667 0.29364 0.04196  -0.03070 0.00193  257 TRP A CH2 
401  N N   . ILE A 55  ? 0.44013 0.36039 0.31508 0.09622  -0.07866 -0.07608 258 ILE A N   
402  C CA  . ILE A 55  ? 0.46106 0.38432 0.34126 0.09210  -0.07729 -0.07894 258 ILE A CA  
403  C C   . ILE A 55  ? 0.53432 0.46492 0.42532 0.10901  -0.09303 -0.10336 258 ILE A C   
404  O O   . ILE A 55  ? 0.55514 0.47087 0.42599 0.12857  -0.10805 -0.11029 258 ILE A O   
405  C CB  . ILE A 55  ? 0.53311 0.43037 0.37972 0.09045  -0.07451 -0.06035 258 ILE A CB  
406  C CG1 . ILE A 55  ? 0.50767 0.40348 0.35235 0.07291  -0.05926 -0.04096 258 ILE A CG1 
407  C CG2 . ILE A 55  ? 0.57872 0.47809 0.42906 0.09012  -0.07657 -0.06575 258 ILE A CG2 
408  C CD1 . ILE A 55  ? 0.62552 0.49931 0.44429 0.06918  -0.05427 -0.02539 258 ILE A CD1 
409  N N   . THR A 56  ? 0.48448 0.43636 0.40613 0.10243  -0.08980 -0.11781 259 THR A N   
410  C CA  . THR A 56  ? 0.48787 0.45253 0.42895 0.11721  -0.10431 -0.14584 259 THR A CA  
411  C C   . THR A 56  ? 0.56493 0.51627 0.48795 0.12322  -0.11140 -0.14475 259 THR A C   
412  O O   . THR A 56  ? 0.53822 0.49881 0.47496 0.10979  -0.10145 -0.14302 259 THR A O   
413  C CB  . THR A 56  ? 0.49093 0.48760 0.48062 0.10548  -0.09433 -0.16612 259 THR A CB  
414  O OG1 . THR A 56  ? 0.52553 0.53176 0.52938 0.09836  -0.08559 -0.16466 259 THR A OG1 
415  C CG2 . THR A 56  ? 0.59870 0.61187 0.61459 0.12147  -0.11004 -0.19984 259 THR A CG2 
416  N N   . GLY A 57  ? 0.59424 0.52098 0.48351 0.14386  -0.12813 -0.14547 260 GLY A N   
417  C CA  . GLY A 57  ? 0.57538 0.48674 0.44505 0.15167  -0.13607 -0.14571 260 GLY A CA  
418  C C   . GLY A 57  ? 0.60481 0.49062 0.44069 0.14150  -0.12480 -0.11736 260 GLY A C   
419  O O   . GLY A 57  ? 0.66582 0.54211 0.48878 0.13083  -0.11265 -0.09747 260 GLY A O   
420  N N   . ALA A 58  ? 0.54854 0.42412 0.37231 0.14524  -0.12924 -0.11770 261 ALA A N   
421  C CA  . ALA A 58  ? 0.60614 0.45830 0.40113 0.13748  -0.12008 -0.09581 261 ALA A CA  
422  C C   . ALA A 58  ? 0.54841 0.42223 0.37016 0.11464  -0.10396 -0.08776 261 ALA A C   
423  O O   . ALA A 58  ? 0.50316 0.40560 0.36113 0.10732  -0.10136 -0.10134 261 ALA A O   
424  C CB  . ALA A 58  ? 0.63883 0.46853 0.40738 0.15458  -0.13407 -0.10239 261 ALA A CB  
425  N N   . PRO A 59  ? 0.51734 0.37675 0.32184 0.10346  -0.09233 -0.06739 262 PRO A N   
426  C CA  . PRO A 59  ? 0.46834 0.34503 0.29387 0.08591  -0.08052 -0.06202 262 PRO A CA  
427  C C   . PRO A 59  ? 0.52054 0.40097 0.35117 0.09074  -0.08786 -0.07280 262 PRO A C   
428  O O   . PRO A 59  ? 0.54127 0.40415 0.35115 0.10669  -0.10069 -0.07896 262 PRO A O   
429  C CB  . PRO A 59  ? 0.50208 0.36063 0.30675 0.07637  -0.06907 -0.04044 262 PRO A CB  
430  C CG  . PRO A 59  ? 0.58220 0.41056 0.35249 0.08858  -0.07326 -0.03473 262 PRO A CG  
431  C CD  . PRO A 59  ? 0.56260 0.38678 0.32653 0.10804  -0.09010 -0.05156 262 PRO A CD  
432  N N   . THR A 60  ? 0.46165 0.36299 0.31797 0.07763  -0.07973 -0.07564 263 THR A N   
433  C CA  . THR A 60  ? 0.44565 0.35277 0.30970 0.08002  -0.08505 -0.08570 263 THR A CA  
434  C C   . THR A 60  ? 0.45325 0.36391 0.32099 0.06449  -0.07240 -0.07303 263 THR A C   
435  O O   . THR A 60  ? 0.44724 0.36217 0.31963 0.05173  -0.05999 -0.06188 263 THR A O   
436  C CB  . THR A 60  ? 0.49288 0.42529 0.39075 0.08247  -0.09000 -0.11100 263 THR A CB  
437  O OG1 . THR A 60  ? 0.55452 0.50538 0.47751 0.06681  -0.07499 -0.11164 263 THR A OG1 
438  C CG2 . THR A 60  ? 0.53536 0.46533 0.43115 0.10179  -0.10671 -0.12822 263 THR A CG2 
439  N N   . ILE A 61  ? 0.47680 0.38459 0.34111 0.06726  -0.07703 -0.07584 264 ILE A N   
440  C CA  . ILE A 61  ? 0.41898 0.33380 0.29122 0.05450  -0.06735 -0.06898 264 ILE A CA  
441  C C   . ILE A 61  ? 0.47269 0.41119 0.37576 0.04800  -0.06328 -0.08545 264 ILE A C   
442  O O   . ILE A 61  ? 0.46837 0.41557 0.38395 0.05471  -0.07184 -0.10278 264 ILE A O   
443  C CB  . ILE A 61  ? 0.40465 0.30632 0.26098 0.05982  -0.07321 -0.06544 264 ILE A CB  
444  C CG1 . ILE A 61  ? 0.48949 0.36274 0.31335 0.06703  -0.07524 -0.05235 264 ILE A CG1 
445  C CG2 . ILE A 61  ? 0.44234 0.35177 0.30708 0.04699  -0.06337 -0.05806 264 ILE A CG2 
446  C CD1 . ILE A 61  ? 0.47282 0.32941 0.27897 0.07277  -0.07985 -0.05000 264 ILE A CD1 
447  N N   . SER A 62  ? 0.40559 0.35258 0.32013 0.03515  -0.04951 -0.08144 265 SER A N   
448  C CA  . SER A 62  ? 0.41195 0.37649 0.35329 0.02711  -0.04093 -0.09717 265 SER A CA  
449  C C   . SER A 62  ? 0.41904 0.38565 0.36337 0.01735  -0.03191 -0.09487 265 SER A C   
450  O O   . SER A 62  ? 0.42514 0.40374 0.39051 0.01103  -0.02416 -0.11022 265 SER A O   
451  C CB  . SER A 62  ? 0.39041 0.35830 0.33920 0.01877  -0.02886 -0.09547 265 SER A CB  
452  O OG  . SER A 62  ? 0.41641 0.37204 0.34635 0.01161  -0.02073 -0.07450 265 SER A OG  
453  N N   . SER A 63  ? 0.36729 0.32230 0.29227 0.01580  -0.03177 -0.07778 266 SER A N   
454  C CA  . SER A 63  ? 0.37069 0.32716 0.29717 0.00895  -0.02563 -0.07665 266 SER A CA  
455  C C   . SER A 63  ? 0.37542 0.32169 0.28453 0.01300  -0.03251 -0.06376 266 SER A C   
456  O O   . SER A 63  ? 0.42995 0.36508 0.32336 0.01447  -0.03348 -0.04975 266 SER A O   
457  C CB  . SER A 63  ? 0.39464 0.34723 0.31810 -0.00272 -0.00956 -0.06971 266 SER A CB  
458  O OG  . SER A 63  ? 0.43183 0.38267 0.35246 -0.00742 -0.00466 -0.06841 266 SER A OG  
459  N N   . ARG A 64  ? 0.37453 0.32508 0.28855 0.01399  -0.03604 -0.06991 267 ARG A N   
460  C CA  . ARG A 64  ? 0.41861 0.36075 0.31937 0.01608  -0.04022 -0.05931 267 ARG A CA  
461  C C   . ARG A 64  ? 0.39861 0.34599 0.30472 0.00903  -0.03381 -0.06022 267 ARG A C   
462  O O   . ARG A 64  ? 0.44435 0.38907 0.34541 0.01104  -0.03814 -0.05624 267 ARG A O   
463  C CB  . ARG A 64  ? 0.43746 0.37464 0.33279 0.02757  -0.05381 -0.06476 267 ARG A CB  
464  C CG  . ARG A 64  ? 0.39387 0.32337 0.28137 0.03734  -0.06158 -0.06776 267 ARG A CG  
465  C CD  . ARG A 64  ? 0.43309 0.34557 0.30117 0.04964  -0.07315 -0.06672 267 ARG A CD  
466  N NE  . ARG A 64  ? 0.48008 0.37436 0.32787 0.04748  -0.06804 -0.04939 267 ARG A NE  
467  C CZ  . ARG A 64  ? 0.54900 0.42087 0.37376 0.05628  -0.07317 -0.04518 267 ARG A CZ  
468  N NH1 . ARG A 64  ? 0.54643 0.40949 0.36147 0.06971  -0.08585 -0.05577 267 ARG A NH1 
469  N NH2 . ARG A 64  ? 0.51070 0.36674 0.32110 0.05201  -0.06494 -0.03148 267 ARG A NH2 
470  N N   . THR A 65  ? 0.41395 0.36634 0.32845 0.00086  -0.02243 -0.06564 268 THR A N   
471  C CA  . THR A 65  ? 0.40415 0.35834 0.32112 -0.00534 -0.01503 -0.06845 268 THR A CA  
472  C C   . THR A 65  ? 0.45978 0.40366 0.35944 -0.00615 -0.01368 -0.05322 268 THR A C   
473  O O   . THR A 65  ? 0.43354 0.37828 0.33251 -0.00708 -0.01360 -0.05385 268 THR A O   
474  C CB  . THR A 65  ? 0.40643 0.36193 0.33162 -0.01430 0.00017  -0.07782 268 THR A CB  
475  O OG1 . THR A 65  ? 0.55903 0.50280 0.46977 -0.01730 0.00793  -0.06654 268 THR A OG1 
476  C CG2 . THR A 65  ? 0.44864 0.41774 0.39706 -0.01299 -0.00181 -0.09682 268 THR A CG2 
477  N N   . ASP A 66  ? 0.41257 0.34773 0.29995 -0.00525 -0.01317 -0.04137 269 ASP A N   
478  C CA  . ASP A 66  ? 0.41644 0.34377 0.29102 -0.00413 -0.01413 -0.03032 269 ASP A CA  
479  C C   . ASP A 66  ? 0.39547 0.32389 0.27118 0.00125  -0.02396 -0.02663 269 ASP A C   
480  O O   . ASP A 66  ? 0.38553 0.31118 0.26007 0.00433  -0.02778 -0.02407 269 ASP A O   
481  C CB  . ASP A 66  ? 0.44099 0.35929 0.30447 -0.00486 -0.01010 -0.02209 269 ASP A CB  
482  C CG  . ASP A 66  ? 0.46832 0.37914 0.32028 -0.00219 -0.01212 -0.01449 269 ASP A CG  
483  O OD1 . ASP A 66  ? 0.44212 0.35600 0.29695 0.00071  -0.01797 -0.01391 269 ASP A OD1 
484  O OD2 . ASP A 66  ? 0.49977 0.40128 0.34006 -0.00217 -0.00835 -0.01035 269 ASP A OD2 
485  N N   . PRO A 67  ? 0.36663 0.29673 0.24313 0.00244  -0.02706 -0.02661 270 PRO A N   
486  C CA  . PRO A 67  ? 0.36970 0.29804 0.24674 0.00671  -0.03397 -0.02388 270 PRO A CA  
487  C C   . PRO A 67  ? 0.38997 0.31057 0.26157 0.00763  -0.03334 -0.01607 270 PRO A C   
488  O O   . PRO A 67  ? 0.41301 0.32714 0.28228 0.01029  -0.03571 -0.01441 270 PRO A O   
489  C CB  . PRO A 67  ? 0.39081 0.32285 0.27047 0.00670  -0.03539 -0.02503 270 PRO A CB  
490  C CG  . PRO A 67  ? 0.41024 0.34660 0.29146 0.00305  -0.03042 -0.03108 270 PRO A CG  
491  C CD  . PRO A 67  ? 0.41589 0.34709 0.29097 0.00006  -0.02333 -0.02917 270 PRO A CD  
492  N N   . ASN A 68  ? 0.41612 0.33487 0.28410 0.00579  -0.02955 -0.01220 271 ASN A N   
493  C CA  . ASN A 68  ? 0.42883 0.34257 0.29565 0.00636  -0.02906 -0.00747 271 ASN A CA  
494  C C   . ASN A 68  ? 0.41457 0.32352 0.27779 0.00572  -0.02694 -0.00457 271 ASN A C   
495  O O   . ASN A 68  ? 0.39871 0.30266 0.26196 0.00557  -0.02552 -0.00168 271 ASN A O   
496  C CB  . ASN A 68  ? 0.42096 0.33449 0.28541 0.00711  -0.02869 -0.00663 271 ASN A CB  
497  C CG  . ASN A 68  ? 0.47285 0.38988 0.34015 0.00950  -0.03192 -0.00986 271 ASN A CG  
498  O OD1 . ASN A 68  ? 0.53782 0.45825 0.41212 0.00961  -0.03382 -0.01186 271 ASN A OD1 
499  N ND2 . ASN A 68  ? 0.57770 0.49176 0.43729 0.01255  -0.03299 -0.01063 271 ASN A ND2 
500  N N   A LYS A 69  ? 0.37247 0.28326 0.23440 0.00510  -0.02600 -0.00672 272 LYS A N   
501  N N   B LYS A 69  ? 0.37594 0.28669 0.23789 0.00515  -0.02607 -0.00675 272 LYS A N   
502  C CA  A LYS A 69  ? 0.40992 0.31687 0.26883 0.00523  -0.02463 -0.00448 272 LYS A CA  
503  C CA  B LYS A 69  ? 0.41000 0.31688 0.26888 0.00524  -0.02464 -0.00443 272 LYS A CA  
504  C C   A LYS A 69  ? 0.43086 0.34116 0.29235 0.00704  -0.02651 -0.01085 272 LYS A C   
505  C C   B LYS A 69  ? 0.42919 0.33952 0.29067 0.00693  -0.02637 -0.01076 272 LYS A C   
506  O O   A LYS A 69  ? 0.41513 0.33273 0.28312 0.00593  -0.02624 -0.01800 272 LYS A O   
507  O O   B LYS A 69  ? 0.41616 0.33378 0.28408 0.00560  -0.02577 -0.01778 272 LYS A O   
508  C CB  A LYS A 69  ? 0.41479 0.32106 0.27097 0.00254  -0.02045 -0.00108 272 LYS A CB  
509  C CB  B LYS A 69  ? 0.41558 0.32175 0.27175 0.00258  -0.02053 -0.00096 272 LYS A CB  
510  C CG  A LYS A 69  ? 0.47202 0.38027 0.32651 -0.00014 -0.01593 -0.00428 272 LYS A CG  
511  C CG  B LYS A 69  ? 0.46757 0.37508 0.32096 0.00032  -0.01662 -0.00341 272 LYS A CG  
512  C CD  A LYS A 69  ? 0.48789 0.38930 0.33296 -0.00091 -0.01237 -0.00014 272 LYS A CD  
513  C CD  B LYS A 69  ? 0.48882 0.38995 0.33369 -0.00057 -0.01290 0.00040  272 LYS A CD  
514  C CE  A LYS A 69  ? 0.58861 0.48466 0.42591 -0.00393 -0.00456 -0.00295 272 LYS A CE  
515  C CE  B LYS A 69  ? 0.54466 0.43846 0.37827 -0.00157 -0.00755 -0.00086 272 LYS A CE  
516  N NZ  A LYS A 69  ? 0.50636 0.38969 0.32773 -0.00275 -0.00144 0.00134  272 LYS A NZ  
517  N NZ  B LYS A 69  ? 0.55875 0.45424 0.39567 -0.00626 0.00003  -0.00702 272 LYS A NZ  
518  N N   . ASP A 70  ? 0.36508 0.26976 0.22218 0.01027  -0.02836 -0.00990 273 ASP A N   
519  C CA  . ASP A 70  ? 0.38105 0.28963 0.24195 0.01365  -0.03139 -0.01781 273 ASP A CA  
520  C C   . ASP A 70  ? 0.41763 0.32823 0.28033 0.01022  -0.02625 -0.01577 273 ASP A C   
521  O O   . ASP A 70  ? 0.43983 0.34485 0.29660 0.00791  -0.02302 -0.00726 273 ASP A O   
522  C CB  . ASP A 70  ? 0.36572 0.26289 0.21591 0.02261  -0.03875 -0.01918 273 ASP A CB  
523  C CG  . ASP A 70  ? 0.44908 0.34197 0.29542 0.02780  -0.04493 -0.02316 273 ASP A CG  
524  O OD1 . ASP A 70  ? 0.41338 0.31757 0.27087 0.02521  -0.04543 -0.02882 273 ASP A OD1 
525  O OD2 . ASP A 70  ? 0.48298 0.35841 0.31264 0.03494  -0.04880 -0.02084 273 ASP A OD2 
526  N N   . VAL A 71  ? 0.34377 0.26294 0.21666 0.00975  -0.02518 -0.02523 274 VAL A N   
527  C CA  . VAL A 71  ? 0.35279 0.27350 0.22824 0.00744  -0.02069 -0.02498 274 VAL A CA  
528  C C   . VAL A 71  ? 0.38815 0.30797 0.26362 0.01573  -0.02848 -0.03066 274 VAL A C   
529  O O   . VAL A 71  ? 0.39329 0.31788 0.27544 0.02207  -0.03558 -0.04264 274 VAL A O   
530  C CB  . VAL A 71  ? 0.38223 0.31085 0.26931 0.00060  -0.01152 -0.03314 274 VAL A CB  
531  C CG1 . VAL A 71  ? 0.40903 0.33763 0.29810 -0.00223 -0.00572 -0.03252 274 VAL A CG1 
532  C CG2 . VAL A 71  ? 0.36822 0.29202 0.24834 -0.00521 -0.00454 -0.02766 274 VAL A CG2 
533  N N   . ILE A 72  ? 0.36655 0.27919 0.23346 0.01698  -0.02817 -0.02314 275 ILE A N   
534  C CA  . ILE A 72  ? 0.40780 0.31655 0.27081 0.02580  -0.03517 -0.02777 275 ILE A CA  
535  C C   . ILE A 72  ? 0.40774 0.32673 0.28367 0.02248  -0.03076 -0.03286 275 ILE A C   
536  O O   . ILE A 72  ? 0.41072 0.32977 0.28644 0.01461  -0.02247 -0.02474 275 ILE A O   
537  C CB  . ILE A 72  ? 0.40549 0.29606 0.24804 0.02927  -0.03614 -0.01622 275 ILE A CB  
538  C CG1 . ILE A 72  ? 0.47191 0.35039 0.30233 0.03040  -0.03688 -0.01103 275 ILE A CG1 
539  C CG2 . ILE A 72  ? 0.44797 0.32983 0.28070 0.04037  -0.04375 -0.02107 275 ILE A CG2 
540  C CD1 . ILE A 72  ? 0.48593 0.36158 0.31294 0.03967  -0.04618 -0.02052 275 ILE A CD1 
541  N N   . SER A 73  ? 0.39201 0.31925 0.27954 0.02927  -0.03678 -0.04769 276 SER A N   
542  C CA  . SER A 73  ? 0.37382 0.31198 0.27719 0.02665  -0.03244 -0.05569 276 SER A CA  
543  C C   . SER A 73  ? 0.39718 0.33060 0.29395 0.03783  -0.04186 -0.05842 276 SER A C   
544  O O   . SER A 73  ? 0.42349 0.34774 0.30808 0.05057  -0.05389 -0.06263 276 SER A O   
545  C CB  . SER A 73  ? 0.37082 0.32588 0.30025 0.02458  -0.02997 -0.07583 276 SER A CB  
546  O OG  . SER A 73  ? 0.37656 0.33342 0.31025 0.01310  -0.01814 -0.07346 276 SER A OG  
547  N N   . PHE A 74  ? 0.36495 0.30245 0.26753 0.03399  -0.03651 -0.05658 277 PHE A N   
548  C CA  . PHE A 74  ? 0.39126 0.32646 0.29052 0.04468  -0.04507 -0.06150 277 PHE A CA  
549  C C   . PHE A 74  ? 0.37777 0.32746 0.29824 0.03818  -0.03732 -0.06833 277 PHE A C   
550  O O   . PHE A 74  ? 0.39048 0.34332 0.31677 0.02517  -0.02421 -0.06191 277 PHE A O   
551  C CB  . PHE A 74  ? 0.42645 0.34082 0.29721 0.04839  -0.04711 -0.04457 277 PHE A CB  
552  C CG  . PHE A 74  ? 0.39574 0.30803 0.26339 0.03592  -0.03565 -0.02904 277 PHE A CG  
553  C CD1 . PHE A 74  ? 0.47563 0.38464 0.33911 0.02724  -0.02907 -0.01939 277 PHE A CD1 
554  C CD2 . PHE A 74  ? 0.40253 0.31654 0.27205 0.03409  -0.03274 -0.02563 277 PHE A CD2 
555  C CE1 . PHE A 74  ? 0.46291 0.37011 0.32398 0.01817  -0.02100 -0.00802 277 PHE A CE1 
556  C CE2 . PHE A 74  ? 0.41860 0.33079 0.28562 0.02389  -0.02382 -0.01315 277 PHE A CE2 
557  C CZ  . PHE A 74  ? 0.44437 0.35305 0.30713 0.01655  -0.01856 -0.00509 277 PHE A CZ  
558  N N   . THR A 75  ? 0.39289 0.34942 0.32325 0.04833  -0.04569 -0.08225 278 THR A N   
559  C CA  . THR A 75  ? 0.34863 0.32157 0.30494 0.04279  -0.03829 -0.09381 278 THR A CA  
560  C C   . THR A 75  ? 0.39119 0.35927 0.33855 0.04698  -0.04104 -0.08660 278 THR A C   
561  O O   . THR A 75  ? 0.44211 0.40283 0.37711 0.06189  -0.05471 -0.08997 278 THR A O   
562  C CB  . THR A 75  ? 0.38841 0.37954 0.37399 0.05018  -0.04473 -0.12217 278 THR A CB  
563  O OG1 . THR A 75  ? 0.39722 0.39307 0.39206 0.04467  -0.04056 -0.12888 278 THR A OG1 
564  C CG2 . THR A 75  ? 0.39804 0.40636 0.41407 0.04294  -0.03427 -0.13638 278 THR A CG2 
565  N N   . CYS A 76  ? 0.37020 0.34023 0.32160 0.03473  -0.02820 -0.07731 279 CYS A N   
566  C CA  . CYS A 76  ? 0.36735 0.33458 0.31297 0.03618  -0.02873 -0.07000 279 CYS A CA  
567  C C   . CYS A 76  ? 0.38488 0.36954 0.35920 0.03403  -0.02386 -0.08628 279 CYS A C   
568  O O   . CYS A 76  ? 0.37096 0.36502 0.36541 0.02329  -0.01103 -0.09503 279 CYS A O   
569  C CB  . CYS A 76  ? 0.40156 0.35813 0.33139 0.02474  -0.01874 -0.04885 279 CYS A CB  
570  S SG  . CYS A 76  ? 0.43251 0.36989 0.33311 0.02525  -0.02177 -0.03060 279 CYS A SG  
571  N N   . LEU A 77  ? 0.38487 0.37189 0.36006 0.04399  -0.03269 -0.09076 280 LEU A N   
572  C CA  . LEU A 77  ? 0.40428 0.40578 0.40385 0.03988  -0.02604 -0.10124 280 LEU A CA  
573  C C   . LEU A 77  ? 0.37381 0.36817 0.36442 0.02558  -0.01193 -0.08260 280 LEU A C   
574  O O   . LEU A 77  ? 0.37221 0.35167 0.33808 0.02184  -0.01082 -0.06284 280 LEU A O   
575  C CB  . LEU A 77  ? 0.40700 0.41145 0.40688 0.05570  -0.04063 -0.10982 280 LEU A CB  
576  C CG  . LEU A 77  ? 0.44962 0.45808 0.45428 0.07445  -0.05840 -0.13038 280 LEU A CG  
577  C CD1 . LEU A 77  ? 0.37804 0.38517 0.37743 0.09197  -0.07340 -0.13805 280 LEU A CD1 
578  C CD2 . LEU A 77  ? 0.45354 0.48435 0.49733 0.07097  -0.05390 -0.15671 280 LEU A CD2 
579  N N   . LYS A 78  ? 0.38968 0.39426 0.40119 0.01826  -0.00132 -0.09065 281 LYS A N   
580  C CA  . LYS A 78  ? 0.40540 0.40119 0.40600 0.00740  0.00986  -0.07426 281 LYS A CA  
581  C C   . LYS A 78  ? 0.39356 0.38199 0.37476 0.01412  -0.00037 -0.05974 281 LYS A C   
582  O O   . LYS A 78  ? 0.38735 0.38140 0.37254 0.02563  -0.01166 -0.06723 281 LYS A O   
583  C CB  . LYS A 78  ? 0.41871 0.42461 0.44432 -0.00055 0.02339  -0.08696 281 LYS A CB  
584  C CG  . LYS A 78  ? 0.44200 0.43635 0.45377 -0.00998 0.03380  -0.07081 281 LYS A CG  
585  C CD  . LYS A 78  ? 0.41907 0.41961 0.45315 -0.01833 0.04935  -0.08336 281 LYS A CD  
586  C CE  . LYS A 78  ? 0.48947 0.47579 0.50529 -0.02518 0.05692  -0.06660 281 LYS A CE  
587  N NZ  . LYS A 78  ? 0.49742 0.48716 0.53300 -0.03303 0.07284  -0.07848 281 LYS A NZ  
588  N N   . ASN A 79  ? 0.37906 0.35392 0.33889 0.00771  0.00339  -0.04046 282 ASN A N   
589  C CA  . ASN A 79  ? 0.38567 0.35420 0.33094 0.01107  -0.00257 -0.02822 282 ASN A CA  
590  C C   . ASN A 79  ? 0.39587 0.37029 0.35225 0.00517  0.00470  -0.02857 282 ASN A C   
591  O O   . ASN A 79  ? 0.40215 0.37013 0.35359 -0.00440 0.01451  -0.02087 282 ASN A O   
592  C CB  . ASN A 79  ? 0.37698 0.33079 0.29936 0.00745  -0.00249 -0.01138 282 ASN A CB  
593  C CG  . ASN A 79  ? 0.39174 0.33861 0.30099 0.01061  -0.00749 -0.00149 282 ASN A CG  
594  O OD1 . ASN A 79  ? 0.39994 0.35112 0.31334 0.01671  -0.01206 -0.00572 282 ASN A OD1 
595  N ND2 . ASN A 79  ? 0.37389 0.31000 0.26841 0.00661  -0.00623 0.01004  282 ASN A ND2 
596  N N   . LYS A 80  ? 0.38815 0.37330 0.35814 0.01219  -0.00074 -0.03848 283 LYS A N   
597  C CA  . LYS A 80  ? 0.41893 0.41072 0.40094 0.00754  0.00533  -0.03973 283 LYS A CA  
598  C C   . LYS A 80  ? 0.38738 0.37120 0.35250 0.00727  0.00186  -0.02402 283 LYS A C   
599  O O   . LYS A 80  ? 0.39944 0.38509 0.36947 0.00130  0.00799  -0.02098 283 LYS A O   
600  C CB  . LYS A 80  ? 0.38762 0.39645 0.39469 0.01594  0.00022  -0.05932 283 LYS A CB  
601  C CG  . LYS A 80  ? 0.37312 0.39341 0.40352 0.01682  0.00309  -0.07993 283 LYS A CG  
602  C CD  . LYS A 80  ? 0.43735 0.47712 0.49765 0.02562  -0.00241 -0.10299 283 LYS A CD  
603  C CE  . LYS A 80  ? 0.41841 0.47182 0.50735 0.02555  0.00144  -0.12728 283 LYS A CE  
604  N NZ  . LYS A 80  ? 0.46759 0.54258 0.59037 0.03556  -0.00540 -0.15406 283 LYS A NZ  
605  N N   . THR A 81  ? 0.40072 0.37450 0.34623 0.01304  -0.00651 -0.01501 284 THR A N   
606  C CA  . THR A 81  ? 0.35172 0.31790 0.28324 0.01273  -0.00892 -0.00290 284 THR A CA  
607  C C   . THR A 81  ? 0.41495 0.37348 0.33762 0.00254  -0.00247 0.00890  284 THR A C   
608  O O   . THR A 81  ? 0.42046 0.37499 0.34054 -0.00230 0.00220  0.01004  284 THR A O   
609  C CB  . THR A 81  ? 0.38734 0.34103 0.29932 0.02164  -0.01681 0.00082  284 THR A CB  
610  O OG1 . THR A 81  ? 0.40889 0.35131 0.30730 0.01692  -0.01403 0.00910  284 THR A OG1 
611  C CG2 . THR A 81  ? 0.42010 0.37632 0.33480 0.03455  -0.02545 -0.01242 284 THR A CG2 
612  N N   . VAL A 82  ? 0.36976 0.32577 0.28743 0.00035  -0.00308 0.01644  285 VAL A N   
613  C CA  . VAL A 82  ? 0.34703 0.29624 0.25702 -0.00669 -0.00000 0.02489  285 VAL A CA  
614  C C   . VAL A 82  ? 0.39577 0.33535 0.29300 -0.00621 -0.00256 0.03044  285 VAL A C   
615  O O   . VAL A 82  ? 0.42450 0.36038 0.31832 -0.01031 -0.00217 0.03497  285 VAL A O   
616  C CB  . VAL A 82  ? 0.42875 0.38138 0.34313 -0.00987 0.00084  0.02767  285 VAL A CB  
617  C CG1 . VAL A 82  ? 0.42330 0.38293 0.35005 -0.01172 0.00613  0.02166  285 VAL A CG1 
618  C CG2 . VAL A 82  ? 0.41948 0.37388 0.33325 -0.00612 -0.00362 0.02902  285 VAL A CG2 
619  N N   . TRP A 83  ? 0.39849 0.33313 0.28910 -0.00090 -0.00495 0.02850  286 TRP A N   
620  C CA  . TRP A 83  ? 0.42290 0.34551 0.30068 -0.00101 -0.00475 0.03278  286 TRP A CA  
621  C C   . TRP A 83  ? 0.39193 0.31067 0.26547 0.00004  -0.00483 0.03126  286 TRP A C   
622  O O   . TRP A 83  ? 0.46714 0.39010 0.34431 0.00465  -0.00703 0.02538  286 TRP A O   
623  C CB  . TRP A 83  ? 0.43976 0.35227 0.30574 0.00542  -0.00639 0.03302  286 TRP A CB  
624  C CG  . TRP A 83  ? 0.44101 0.35676 0.31021 0.00534  -0.00647 0.03399  286 TRP A CG  
625  C CD1 . TRP A 83  ? 0.46095 0.38033 0.33653 -0.00194 -0.00352 0.03720  286 TRP A CD1 
626  C CD2 . TRP A 83  ? 0.45212 0.36729 0.31792 0.01403  -0.01069 0.03053  286 TRP A CD2 
627  N NE1 . TRP A 83  ? 0.45065 0.37247 0.32772 0.00041  -0.00462 0.03692  286 TRP A NE1 
628  C CE2 . TRP A 83  ? 0.44107 0.35999 0.31160 0.01037  -0.00895 0.03312  286 TRP A CE2 
629  C CE3 . TRP A 83  ? 0.45709 0.36923 0.31670 0.02593  -0.01719 0.02388  286 TRP A CE3 
630  C CZ2 . TRP A 83  ? 0.46233 0.38168 0.33079 0.01764  -0.01262 0.03050  286 TRP A CZ2 
631  C CZ3 . TRP A 83  ? 0.45965 0.37162 0.31664 0.03462  -0.02209 0.02007  286 TRP A CZ3 
632  C CH2 . TRP A 83  ? 0.46452 0.38013 0.32580 0.03009  -0.01935 0.02397  286 TRP A CH2 
633  N N   . ASN A 84  ? 0.41685 0.32861 0.28487 -0.00393 -0.00268 0.03478  287 ASN A N   
634  C CA  . ASN A 84  ? 0.43595 0.34129 0.29722 -0.00211 -0.00287 0.03396  287 ASN A CA  
635  C C   . ASN A 84  ? 0.45287 0.34677 0.30099 0.00573  -0.00493 0.03264  287 ASN A C   
636  O O   . ASN A 84  ? 0.45751 0.34239 0.29668 0.00820  -0.00397 0.03436  287 ASN A O   
637  C CB  . ASN A 84  ? 0.47040 0.37025 0.32975 -0.00733 -0.00002 0.03646  287 ASN A CB  
638  C CG  . ASN A 84  ? 0.54327 0.45017 0.41062 -0.01190 -0.00049 0.03662  287 ASN A CG  
639  O OD1 . ASN A 84  ? 0.54020 0.45227 0.41028 -0.01189 -0.00114 0.03601  287 ASN A OD1 
640  N ND2 . ASN A 84  ? 0.62093 0.52591 0.49110 -0.01528 0.00031  0.03592  287 ASN A ND2 
641  N N   . ARG A 85  ? 0.41974 0.31118 0.26380 0.01060  -0.00787 0.02912  288 ARG A N   
642  C CA  . ARG A 85  ? 0.41723 0.29333 0.24364 0.02059  -0.01153 0.02709  288 ARG A CA  
643  C C   . ARG A 85  ? 0.42902 0.29493 0.24598 0.02103  -0.01069 0.02775  288 ARG A C   
644  O O   . ARG A 85  ? 0.44175 0.31811 0.26997 0.01651  -0.01040 0.02646  288 ARG A O   
645  C CB  . ARG A 85  ? 0.46651 0.35047 0.29796 0.03077  -0.01978 0.01787  288 ARG A CB  
646  C CG  . ARG A 85  ? 0.45827 0.36225 0.31199 0.02779  -0.02066 0.01029  288 ARG A CG  
647  C CD  . ARG A 85  ? 0.45913 0.37342 0.32382 0.03718  -0.02770 -0.00218 288 ARG A CD  
648  N NE  . ARG A 85  ? 0.43184 0.36280 0.31838 0.03492  -0.02689 -0.01334 288 ARG A NE  
649  C CZ  . ARG A 85  ? 0.41298 0.35822 0.31853 0.04024  -0.03055 -0.02798 288 ARG A CZ  
650  N NH1 . ARG A 85  ? 0.40895 0.35534 0.31445 0.04901  -0.03690 -0.03259 288 ARG A NH1 
651  N NH2 . ARG A 85  ? 0.43811 0.39667 0.36431 0.03674  -0.02719 -0.03985 288 ARG A NH2 
652  N N   A ARG A 86  ? 0.50579 0.34849 0.29949 0.02683  -0.00950 0.02974  289 ARG A N   
653  N N   B ARG A 86  ? 0.50585 0.34865 0.29960 0.02692  -0.00961 0.02965  289 ARG A N   
654  C CA  A ARG A 86  ? 0.51089 0.33942 0.29318 0.02547  -0.00567 0.03183  289 ARG A CA  
655  C CA  B ARG A 86  ? 0.51025 0.33956 0.29339 0.02512  -0.00562 0.03183  289 ARG A CA  
656  C C   A ARG A 86  ? 0.52639 0.33991 0.28953 0.03839  -0.01294 0.02747  289 ARG A C   
657  C C   B ARG A 86  ? 0.52716 0.33909 0.28911 0.03791  -0.01211 0.02805  289 ARG A C   
658  O O   A ARG A 86  ? 0.54506 0.34558 0.29110 0.05028  -0.01883 0.02447  289 ARG A O   
659  O O   B ARG A 86  ? 0.55106 0.34670 0.29305 0.04930  -0.01663 0.02611  289 ARG A O   
660  C CB  A ARG A 86  ? 0.54643 0.35479 0.31544 0.01947  0.00573  0.03720  289 ARG A CB  
661  C CB  B ARG A 86  ? 0.54725 0.35971 0.32080 0.01774  0.00592  0.03720  289 ARG A CB  
662  C CG  A ARG A 86  ? 0.54442 0.36787 0.33492 0.00677  0.01204  0.03861  289 ARG A CG  
663  C CG  B ARG A 86  ? 0.53790 0.36880 0.33488 0.00589  0.01032  0.03819  289 ARG A CG  
664  C CD  A ARG A 86  ? 0.60143 0.40640 0.38415 -0.00014 0.02484  0.03977  289 ARG A CD  
665  C CD  B ARG A 86  ? 0.58381 0.40209 0.37732 -0.00115 0.02139  0.03961  289 ARG A CD  
666  N NE  A ARG A 86  ? 0.64996 0.47137 0.45679 -0.01066 0.02852  0.03717  289 ARG A NE  
667  N NE  B ARG A 86  ? 0.61205 0.44734 0.42893 -0.01082 0.02367  0.03727  289 ARG A NE  
668  C CZ  A ARG A 86  ? 0.64287 0.46914 0.46050 -0.01543 0.03056  0.03413  289 ARG A CZ  
669  C CZ  B ARG A 86  ? 0.62014 0.47129 0.45217 -0.01403 0.02087  0.03653  289 ARG A CZ  
670  N NH1 A ARG A 86  ? 0.54139 0.35805 0.34887 -0.01233 0.03064  0.03454  289 ARG A NH1 
671  N NH1 B ARG A 86  ? 0.66596 0.52030 0.49518 -0.01012 0.01715  0.03847  289 ARG A NH1 
672  N NH2 A ARG A 86  ? 0.71121 0.55230 0.55039 -0.02231 0.03136  0.02941  289 ARG A NH2 
673  N NH2 B ARG A 86  ? 0.67325 0.53676 0.52325 -0.02017 0.02088  0.03269  289 ARG A NH2 
674  N N   . ALA A 87  ? 0.52303 0.33733 0.28793 0.03720  -0.01352 0.02633  290 ALA A N   
675  C CA  . ALA A 87  ? 0.54714 0.34349 0.29130 0.04889  -0.01967 0.02256  290 ALA A CA  
676  C C   . ALA A 87  ? 0.50563 0.29218 0.24506 0.04199  -0.01206 0.02688  290 ALA A C   
677  O O   . ALA A 87  ? 0.50921 0.30863 0.26649 0.02960  -0.00483 0.03018  290 ALA A O   
678  C CB  . ALA A 87  ? 0.55019 0.36585 0.30962 0.05677  -0.03198 0.01157  290 ALA A CB  
679  N N   . TYR A 88  ? 0.53020 0.29254 0.24454 0.05116  -0.01427 0.02584  291 TYR A N   
680  C CA  . TYR A 88  ? 0.58277 0.33201 0.29021 0.04521  -0.00582 0.02944  291 TYR A CA  
681  C C   . TYR A 88  ? 0.59140 0.33493 0.28911 0.05538  -0.01539 0.02426  291 TYR A C   
682  O O   . TYR A 88  ? 0.58053 0.30802 0.25643 0.07071  -0.02531 0.01946  291 TYR A O   
683  C CB  . TYR A 88  ? 0.59503 0.30803 0.27335 0.04380  0.00784  0.03516  291 TYR A CB  
684  C CG  . TYR A 88  ? 0.62670 0.34455 0.31482 0.03435  0.01716  0.03835  291 TYR A CG  
685  C CD1 . TYR A 88  ? 0.65299 0.36235 0.32770 0.04151  0.01419  0.03883  291 TYR A CD1 
686  C CD2 . TYR A 88  ? 0.62775 0.35972 0.33982 0.01934  0.02759  0.03921  291 TYR A CD2 
687  C CE1 . TYR A 88  ? 0.64519 0.36022 0.33016 0.03269  0.02235  0.04127  291 TYR A CE1 
688  C CE2 . TYR A 88  ? 0.67915 0.41703 0.40227 0.01135  0.03478  0.04010  291 TYR A CE2 
689  C CZ  . TYR A 88  ? 0.65909 0.38832 0.36840 0.01747  0.03267  0.04173  291 TYR A CZ  
690  O OH  . TYR A 88  ? 0.67756 0.41321 0.39855 0.00936  0.03968  0.04224  291 TYR A OH  
691  N N   . ILE A 89  ? 0.56421 0.32031 0.27747 0.04821  -0.01363 0.02401  292 ILE A N   
692  C CA  . ILE A 89  ? 0.55906 0.31168 0.26581 0.05662  -0.02232 0.01868  292 ILE A CA  
693  C C   . ILE A 89  ? 0.57111 0.29838 0.25921 0.05380  -0.01273 0.02346  292 ILE A C   
694  O O   . ILE A 89  ? 0.57683 0.31068 0.27942 0.04065  -0.00148 0.02739  292 ILE A O   
695  C CB  . ILE A 89  ? 0.50531 0.29271 0.24490 0.05138  -0.02820 0.01303  292 ILE A CB  
696  C CG1 . ILE A 89  ? 0.49811 0.30731 0.25542 0.05418  -0.03555 0.00615  292 ILE A CG1 
697  C CG2 . ILE A 89  ? 0.52980 0.31388 0.26441 0.05863  -0.03595 0.00702  292 ILE A CG2 
698  C CD1 . ILE A 89  ? 0.49064 0.32995 0.27841 0.04684  -0.03679 0.00052  292 ILE A CD1 
699  N N   . LYS A 90  ? 0.57361 0.27116 0.22966 0.06696  -0.01749 0.02162  293 LYS A N   
700  C CA  . LYS A 90  ? 0.61388 0.28605 0.25092 0.06593  -0.00953 0.02457  293 LYS A CA  
701  C C   . LYS A 90  ? 0.64269 0.32258 0.28196 0.07498  -0.02335 0.01754  293 LYS A C   
702  O O   . LYS A 90  ? 0.61094 0.31487 0.26697 0.08159  -0.03780 0.00925  293 LYS A O   
703  C CB  . LYS A 90  ? 0.67245 0.29396 0.26228 0.07366  -0.00040 0.02913  293 LYS A CB  
704  C CG  . LYS A 90  ? 0.72750 0.34005 0.31757 0.06149  0.01746  0.03513  293 LYS A CG  
705  C CD  . LYS A 90  ? 0.79094 0.34726 0.33051 0.06757  0.03081  0.03953  293 LYS A CD  
706  C CE  . LYS A 90  ? 0.81970 0.36807 0.36270 0.05396  0.05049  0.04348  293 LYS A CE  
707  N NZ  . LYS A 90  ? 0.96487 0.46951 0.47291 0.05596  0.06722  0.04173  293 LYS A NZ  
708  N N   . PHE A 91  ? 0.66293 0.32239 0.28698 0.07463  -0.01780 0.01952  294 PHE A N   
709  C CA  . PHE A 91  ? 0.63057 0.30117 0.26234 0.07986  -0.02891 0.01322  294 PHE A CA  
710  C C   . PHE A 91  ? 0.69220 0.31857 0.28146 0.09132  -0.02814 0.01412  294 PHE A C   
711  O O   . PHE A 91  ? 0.78606 0.38484 0.35772 0.08418  -0.01113 0.02115  294 PHE A O   
712  C CB  . PHE A 91  ? 0.59697 0.29771 0.26430 0.06406  -0.02248 0.01456  294 PHE A CB  
713  C CG  . PHE A 91  ? 0.57283 0.31004 0.27552 0.05308  -0.02145 0.01468  294 PHE A CG  
714  C CD1 . PHE A 91  ? 0.60750 0.34483 0.31649 0.04262  -0.00913 0.02053  294 PHE A CD1 
715  C CD2 . PHE A 91  ? 0.49810 0.26691 0.22625 0.05343  -0.03197 0.00786  294 PHE A CD2 
716  C CE1 . PHE A 91  ? 0.59411 0.36158 0.33161 0.03429  -0.00937 0.02044  294 PHE A CE1 
717  C CE2 . PHE A 91  ? 0.52909 0.32524 0.28389 0.04393  -0.02953 0.00842  294 PHE A CE2 
718  C CZ  . PHE A 91  ? 0.57325 0.36802 0.33120 0.03521  -0.01924 0.01516  294 PHE A CZ  
719  N N   . LYS A 92  ? 0.72272 0.34145 0.29602 0.10916  -0.04598 0.00548  295 LYS A N   
720  C CA  . LYS A 92  ? 0.74174 0.31384 0.26815 0.12408  -0.04848 0.00526  295 LYS A CA  
721  C C   . LYS A 92  ? 0.79096 0.37549 0.33036 0.12412  -0.05510 0.00031  295 LYS A C   
722  O O   . LYS A 92  ? 0.73634 0.35674 0.30605 0.12700  -0.07041 -0.01008 295 LYS A O   
723  C CB  . LYS A 92  ? 0.80831 0.35703 0.30125 0.14831  -0.06655 -0.00297 295 LYS A CB  
724  C CG  . LYS A 92  ? 0.93120 0.43038 0.37813 0.16303  -0.06590 -0.00590 295 LYS A CG  
725  C CD  . LYS A 92  ? 1.07361 0.55624 0.50060 0.18487  -0.08082 -0.01862 295 LYS A CD  
726  C CE  . LYS A 92  ? 1.15686 0.64664 0.58939 0.20451  -0.10513 -0.03441 295 LYS A CE  
727  N NZ  . LYS A 92  ? 1.12423 0.60923 0.55059 0.22453  -0.12087 -0.04581 295 LYS A NZ  
728  N N   . ASP A 93  ? 0.79825 0.35305 0.31622 0.11986  -0.04187 0.00692  296 ASP A N   
729  C CA  . ASP A 93  ? 0.82182 0.37980 0.34391 0.12179  -0.04753 0.00293  296 ASP A CA  
730  C C   . ASP A 93  ? 0.85074 0.38319 0.33787 0.14689  -0.06843 -0.00671 296 ASP A C   
731  O O   . ASP A 93  ? 0.90673 0.38970 0.34476 0.15999  -0.06597 -0.00517 296 ASP A O   
732  C CB  . ASP A 93  ? 0.81060 0.33904 0.31663 0.11079  -0.02567 0.01191  296 ASP A CB  
733  C CG  . ASP A 93  ? 0.89337 0.42753 0.40758 0.11025  -0.02929 0.00870  296 ASP A CG  
734  O OD1 . ASP A 93  ? 0.92944 0.46268 0.43380 0.12599  -0.04872 0.00038  296 ASP A OD1 
735  O OD2 . ASP A 93  ? 0.87991 0.42005 0.41194 0.09433  -0.01289 0.01309  296 ASP A OD2 
736  N N   . LYS A 94  ? 0.83431 0.40221 0.35026 0.15316  -0.08800 -0.01962 297 LYS A N   
737  C CA  . LYS A 94  ? 0.91354 0.46349 0.40296 0.17891  -0.11140 -0.03338 297 LYS A CA  
738  C C   . LYS A 94  ? 0.96617 0.47615 0.42113 0.18936  -0.11165 -0.03349 297 LYS A C   
739  O O   . LYS A 94  ? 1.08814 0.56996 0.52000 0.20959  -0.12224 -0.04291 297 LYS A O   
740  C CB  . LYS A 94  ? 0.85187 0.45451 0.38989 0.18043  -0.12965 -0.05058 297 LYS A CB  
741  C CG  . LYS A 94  ? 0.95503 0.59409 0.52859 0.17177  -0.12840 -0.05328 297 LYS A CG  
742  C CD  . LYS A 94  ? 0.85521 0.54707 0.48186 0.16671  -0.13852 -0.06912 297 LYS A CD  
743  C CE  . LYS A 94  ? 0.97729 0.67269 0.60537 0.18923  -0.16254 -0.09129 297 LYS A CE  
744  N NZ  . LYS A 94  ? 1.03254 0.77864 0.71435 0.18190  -0.16873 -0.10906 297 LYS A NZ  
745  N N   . LYS A 95  ? 0.90002 0.40747 0.35637 0.17565  -0.09856 -0.02420 298 LYS A N   
746  C CA  . LYS A 95  ? 0.98500 0.45334 0.40693 0.18439  -0.09705 -0.02488 298 LYS A CA  
747  C C   . LYS A 95  ? 1.09523 0.51311 0.46987 0.18350  -0.07632 -0.01870 298 LYS A C   
748  O O   . LYS A 95  ? 1.10538 0.49346 0.44521 0.19634  -0.07996 -0.02402 298 LYS A O   
749  C CB  . LYS A 95  ? 0.97395 0.46280 0.42215 0.16847  -0.08868 -0.01967 298 LYS A CB  
750  N N   . THR A 96  ? 0.99017 0.40536 0.36926 0.16648  -0.05405 -0.00635 299 THR A N   
751  C CA  . THR A 96  ? 1.00850 0.38125 0.34807 0.16210  -0.03079 -0.00119 299 THR A CA  
752  C C   . THR A 96  ? 1.05841 0.41683 0.37726 0.17104  -0.03219 -0.00506 299 THR A C   
753  O O   . THR A 96  ? 1.13662 0.45474 0.41351 0.17349  -0.01755 -0.00429 299 THR A O   
754  C CB  . THR A 96  ? 1.08142 0.45836 0.44171 0.13762  -0.00316 0.01118  299 THR A CB  
755  O OG1 . THR A 96  ? 0.98937 0.39737 0.38415 0.12771  -0.00239 0.01561  299 THR A OG1 
756  C CG2 . THR A 96  ? 1.01835 0.40969 0.40318 0.12857  -0.00146 0.01407  299 THR A CG2 
757  N N   . GLY A 97  ? 1.09739 0.48786 0.44516 0.17575  -0.04858 -0.00918 300 GLY A N   
758  C CA  . GLY A 97  ? 1.00520 0.38582 0.33939 0.18340  -0.05007 -0.01258 300 GLY A CA  
759  C C   . GLY A 97  ? 1.08720 0.46613 0.42691 0.16531  -0.02630 -0.00102 300 GLY A C   
760  O O   . GLY A 97  ? 1.14253 0.51265 0.47070 0.17070  -0.02614 -0.00307 300 GLY A O   
761  N N   . GLN A 98  ? 1.02744 0.41453 0.38629 0.14462  -0.00657 0.00940  301 GLN A N   
762  C CA  . GLN A 98  ? 0.93165 0.31726 0.29946 0.12666  0.01730  0.01761  301 GLN A CA  
763  C C   . GLN A 98  ? 0.91941 0.35041 0.33463 0.11521  0.01248  0.02255  301 GLN A C   
764  O O   . GLN A 98  ? 0.90957 0.37239 0.35278 0.11521  -0.00238 0.02239  301 GLN A O   
765  C CB  . GLN A 98  ? 1.07276 0.44065 0.43720 0.11042  0.04337  0.02274  301 GLN A CB  
766  C CG  . GLN A 98  ? 1.09538 0.41664 0.41000 0.11936  0.05215  0.01899  301 GLN A CG  
767  C CD  . GLN A 98  ? 1.15410 0.43647 0.42908 0.12124  0.06984  0.01763  301 GLN A CD  
768  O OE1 . GLN A 98  ? 1.25070 0.53280 0.51874 0.12951  0.06159  0.01525  301 GLN A OE1 
769  N NE2 . GLN A 98  ? 1.16855 0.41766 0.41803 0.11330  0.09532  0.01854  301 GLN A NE2 
770  N N   . TYR A 99  ? 0.91761 0.35074 0.33955 0.10568  0.02528  0.02636  302 TYR A N   
771  C CA  . TYR A 99  ? 0.82132 0.29357 0.28488 0.09226  0.02501  0.03169  302 TYR A CA  
772  C C   . TYR A 99  ? 0.78521 0.27425 0.27987 0.07321  0.03962  0.03458  302 TYR A C   
773  O O   . TYR A 99  ? 0.84510 0.30365 0.32402 0.06547  0.06012  0.03657  302 TYR A O   
774  C CB  . TYR A 99  ? 0.92390 0.39424 0.38787 0.08661  0.03549  0.03359  302 TYR A CB  
775  C CG  . TYR A 99  ? 0.96063 0.43793 0.41710 0.10281  0.01586  0.02883  302 TYR A CG  
776  C CD1 . TYR A 99  ? 0.88306 0.39810 0.36618 0.10737  -0.00467 0.02686  302 TYR A CD1 
777  C CD2 . TYR A 99  ? 1.14195 0.58766 0.56444 0.11389  0.01825  0.02468  302 TYR A CD2 
778  C CE1 . TYR A 99  ? 1.01442 0.53824 0.49535 0.12195  -0.02212 0.01989  302 TYR A CE1 
779  C CE2 . TYR A 99  ? 1.16295 0.61531 0.58130 0.12954  -0.00031 0.01857  302 TYR A CE2 
780  C CZ  . TYR A 99  ? 1.22791 0.72061 0.67788 0.13330  -0.02038 0.01578  302 TYR A CZ  
781  O OH  . TYR A 99  ? 1.32899 0.83069 0.77932 0.14860  -0.03823 0.00740  302 TYR A OH  
782  N N   . ILE A 100 ? 0.72999 0.27397 0.27520 0.06524  0.02921  0.03096  303 ILE A N   
783  C CA  . ILE A 100 ? 0.73595 0.30736 0.31890 0.04963  0.03750  0.02952  303 ILE A CA  
784  C C   . ILE A 100 ? 0.67558 0.25179 0.27825 0.03279  0.05747  0.03073  303 ILE A C   
785  O O   . ILE A 100 ? 0.71242 0.29587 0.31984 0.03083  0.05823  0.03217  303 ILE A O   
786  C CB  . ILE A 100 ? 0.72077 0.34330 0.34356 0.04946  0.01884  0.02491  303 ILE A CB  
787  C CG1 . ILE A 100 ? 0.74170 0.35783 0.34876 0.06382  0.00263  0.02075  303 ILE A CG1 
788  C CG2 . ILE A 100 ? 0.67775 0.33300 0.34195 0.03386  0.02584  0.02325  303 ILE A CG2 
789  C CD1 . ILE A 100 ? 0.76088 0.41774 0.39621 0.06802  -0.01653 0.01429  303 ILE A CD1 
790  N N   . LYS A 101 ? 0.73670 0.30804 0.35149 0.02099  0.07395  0.02848  304 LYS A N   
791  C CA  . LYS A 101 ? 0.70249 0.27539 0.33694 0.00542  0.09430  0.02576  304 LYS A CA  
792  C C   . LYS A 101 ? 0.69595 0.32232 0.38250 -0.00355 0.08633  0.02091  304 LYS A C   
793  O O   . LYS A 101 ? 0.67042 0.32807 0.38003 -0.00192 0.07217  0.01888  304 LYS A O   
794  C CB  . LYS A 101 ? 0.75530 0.30056 0.38455 -0.00386 0.11699  0.02189  304 LYS A CB  
795  C CG  . LYS A 101 ? 0.86861 0.35226 0.43987 0.00496  0.12805  0.02677  304 LYS A CG  
796  C CD  . LYS A 101 ? 0.92775 0.37632 0.46969 0.00324  0.14615  0.02815  304 LYS A CD  
797  C CE  . LYS A 101 ? 0.96233 0.40712 0.47766 0.01903  0.12816  0.03318  304 LYS A CE  
798  N NZ  . LYS A 101 ? 0.92273 0.33627 0.40568 0.02119  0.14376  0.03073  304 LYS A NZ  
799  N N   . GLY A 102 ? 0.65903 0.29275 0.36165 -0.01255 0.09609  0.01844  305 GLY A N   
800  C CA  . GLY A 102 ? 0.68155 0.35894 0.42931 -0.02038 0.09053  0.01239  305 GLY A CA  
801  C C   . GLY A 102 ? 0.66049 0.34594 0.43755 -0.03173 0.10384  0.00178  305 GLY A C   
802  O O   . GLY A 102 ? 0.66119 0.32254 0.42716 -0.03430 0.11674  -0.00052 305 GLY A O   
803  N N   . ALA A 103 ? 0.70410 0.42253 0.51886 -0.03797 0.10085  -0.00622 306 ALA A N   
804  C CA  . ALA A 103 ? 0.64556 0.38262 0.49644 -0.04569 0.10650  -0.01965 306 ALA A CA  
805  C C   . ALA A 103 ? 0.65973 0.36815 0.50999 -0.05622 0.13315  -0.02841 306 ALA A C   
806  O O   . ALA A 103 ? 0.70402 0.41424 0.57031 -0.06030 0.13996  -0.03709 306 ALA A O   
807  C CB  . ALA A 103 ? 0.65065 0.42284 0.53690 -0.04798 0.09765  -0.02825 306 ALA A CB  
808  N N   . ASP A 104 ? 0.72055 0.40111 0.55264 -0.06126 0.15006  -0.02717 307 ASP A N   
809  C CA  . ASP A 104 ? 0.71784 0.36829 0.55001 -0.07337 0.17972  -0.03732 307 ASP A CA  
810  C C   . ASP A 104 ? 0.86645 0.46886 0.65347 -0.07057 0.19296  -0.02897 307 ASP A C   
811  O O   . ASP A 104 ? 0.85976 0.42737 0.63749 -0.08064 0.22115  -0.03574 307 ASP A O   
812  C CB  . ASP A 104 ? 0.71697 0.35434 0.54866 -0.08149 0.19597  -0.04144 307 ASP A CB  
813  C CG  . ASP A 104 ? 0.82146 0.42202 0.60052 -0.07383 0.19687  -0.02488 307 ASP A CG  
814  O OD1 . ASP A 104 ? 0.82642 0.41046 0.56903 -0.06143 0.18459  -0.01153 307 ASP A OD1 
815  O OD2 . ASP A 104 ? 0.93786 0.52646 0.71298 -0.07953 0.20923  -0.02679 307 ASP A OD2 
816  N N   . GLY A 105 ? 0.83121 0.42885 0.58957 -0.05712 0.17437  -0.01594 308 GLY A N   
817  C CA  . GLY A 105 ? 0.82750 0.37939 0.54155 -0.05188 0.18356  -0.00907 308 GLY A CA  
818  C C   . GLY A 105 ? 0.83881 0.33521 0.49855 -0.04831 0.19875  -0.00070 308 GLY A C   
819  O O   . GLY A 105 ? 0.96893 0.43324 0.58898 -0.04011 0.20311  0.00389  308 GLY A O   
820  N N   . LYS A 106 ? 0.84481 0.34232 0.50483 -0.05114 0.20276  -0.00030 309 LYS A N   
821  C CA  . LYS A 106 ? 0.95203 0.41824 0.56900 -0.04461 0.21287  0.00373  309 LYS A CA  
822  C C   . LYS A 106 ? 0.95148 0.41939 0.54836 -0.03256 0.19326  0.01364  309 LYS A C   
823  O O   . LYS A 106 ? 0.86827 0.31032 0.42024 -0.01715 0.18524  0.01993  309 LYS A O   
824  C CB  . LYS A 106 ? 0.86598 0.33066 0.50122 -0.05946 0.24107  -0.00848 309 LYS A CB  
825  C CG  . LYS A 106 ? 0.93504 0.39948 0.59124 -0.07071 0.26198  -0.02020 309 LYS A CG  
826  C CD  . LYS A 106 ? 0.95933 0.42044 0.63073 -0.08415 0.29205  -0.03380 309 LYS A CD  
827  C CE  . LYS A 106 ? 0.93331 0.39744 0.62819 -0.09444 0.31195  -0.04611 309 LYS A CE  
828  N NZ  . LYS A 106 ? 1.01710 0.47424 0.72275 -0.10682 0.34485  -0.06039 309 LYS A NZ  
829  N N   . ALA A 107 ? 0.82373 0.32185 0.45328 -0.03834 0.18447  0.01362  310 ALA A N   
830  C CA  . ALA A 107 ? 0.72662 0.23232 0.34165 -0.02705 0.16550  0.02222  310 ALA A CA  
831  C C   . ALA A 107 ? 0.80658 0.33282 0.41756 -0.01193 0.13699  0.02789  310 ALA A C   
832  O O   . ALA A 107 ? 0.83489 0.38627 0.47010 -0.01309 0.12855  0.02466  310 ALA A O   
833  C CB  . ALA A 107 ? 0.81319 0.36231 0.47285 -0.03589 0.16111  0.01678  310 ALA A CB  
834  N N   . ASP A 108 ? 0.78791 0.30400 0.36980 0.00239  0.12234  0.03472  311 ASP A N   
835  C CA  . ASP A 108 ? 0.71996 0.26165 0.30576 0.01580  0.09515  0.03671  311 ASP A CA  
836  C C   . ASP A 108 ? 0.66858 0.26798 0.30611 0.00904  0.08204  0.03331  311 ASP A C   
837  O O   . ASP A 108 ? 0.67252 0.28927 0.33047 0.00149  0.08562  0.03213  311 ASP A O   
838  C CB  . ASP A 108 ? 0.78771 0.30777 0.33566 0.03278  0.08275  0.04119  311 ASP A CB  
839  C CG  . ASP A 108 ? 0.90638 0.37900 0.40727 0.04288  0.09114  0.03970  311 ASP A CG  
840  O OD1 . ASP A 108 ? 0.93703 0.39044 0.42866 0.03884  0.10377  0.03769  311 ASP A OD1 
841  O OD2 . ASP A 108 ? 0.97544 0.43402 0.45206 0.05490  0.08480  0.03833  311 ASP A OD2 
842  N N   . LEU A 109 ? 0.67244 0.29885 0.32882 0.01208  0.06743  0.03142  312 LEU A N   
843  C CA  . LEU A 109 ? 0.63031 0.30462 0.32654 0.00839  0.05422  0.02898  312 LEU A CA  
844  C C   . LEU A 109 ? 0.61081 0.29490 0.30289 0.01576  0.04224  0.03140  312 LEU A C   
845  O O   . LEU A 109 ? 0.65443 0.32696 0.32365 0.02889  0.03087  0.03229  312 LEU A O   
846  C CB  . LEU A 109 ? 0.57963 0.27362 0.28866 0.01189  0.04181  0.02675  312 LEU A CB  
847  C CG  . LEU A 109 ? 0.60912 0.34637 0.35297 0.00903  0.02939  0.02424  312 LEU A CG  
848  C CD1 . LEU A 109 ? 0.62052 0.37652 0.39394 -0.00282 0.03745  0.02068  312 LEU A CD1 
849  C CD2 . LEU A 109 ? 0.59857 0.34684 0.34749 0.01331  0.01941  0.02197  312 LEU A CD2 
850  N N   . THR A 110 ? 0.58769 0.29315 0.30280 0.00809  0.04416  0.03085  313 THR A N   
851  C CA  . THR A 110 ? 0.54994 0.26306 0.26230 0.01334  0.03591  0.03285  313 THR A CA  
852  C C   . THR A 110 ? 0.58764 0.34008 0.33528 0.00723  0.02873  0.03086  313 THR A C   
853  O O   . THR A 110 ? 0.57518 0.33962 0.34398 -0.00271 0.03585  0.02853  313 THR A O   
854  C CB  . THR A 110 ? 0.67689 0.36401 0.37062 0.01100  0.04907  0.03530  313 THR A CB  
855  O OG1 . THR A 110 ? 0.70305 0.34624 0.35864 0.01598  0.05928  0.03734  313 THR A OG1 
856  C CG2 . THR A 110 ? 0.66399 0.35642 0.35151 0.01853  0.03938  0.03717  313 THR A CG2 
857  N N   . VAL A 111 ? 0.50277 0.27311 0.25589 0.01369  0.01517  0.03025  314 VAL A N   
858  C CA  . VAL A 111 ? 0.49362 0.29450 0.27297 0.00899  0.00975  0.02901  314 VAL A CA  
859  C C   . VAL A 111 ? 0.48194 0.28435 0.25947 0.01028  0.00891  0.03061  314 VAL A C   
860  O O   . VAL A 111 ? 0.53003 0.32267 0.29177 0.01934  0.00353  0.03036  314 VAL A O   
861  C CB  . VAL A 111 ? 0.52282 0.34181 0.31173 0.01300  -0.00100 0.02581  314 VAL A CB  
862  C CG1 . VAL A 111 ? 0.43488 0.27795 0.24454 0.00795  -0.00347 0.02507  314 VAL A CG1 
863  C CG2 . VAL A 111 ? 0.47737 0.29543 0.26843 0.01170  -0.00041 0.02431  314 VAL A CG2 
864  N N   . ASN A 112 ? 0.46672 0.28160 0.26068 0.00243  0.01295  0.03098  315 ASN A N   
865  C CA  . ASN A 112 ? 0.45360 0.27177 0.24837 0.00252  0.01259  0.03249  315 ASN A CA  
866  C C   . ASN A 112 ? 0.50719 0.34777 0.31583 0.00406  0.00369  0.03118  315 ASN A C   
867  O O   . ASN A 112 ? 0.47258 0.32844 0.29621 -0.00040 0.00229  0.03006  315 ASN A O   
868  C CB  . ASN A 112 ? 0.49235 0.31168 0.29815 -0.00639 0.02143  0.03185  315 ASN A CB  
869  C CG  . ASN A 112 ? 0.60621 0.40114 0.39997 -0.01001 0.03452  0.03106  315 ASN A CG  
870  O OD1 . ASN A 112 ? 0.64583 0.41608 0.41418 -0.00428 0.03753  0.03354  315 ASN A OD1 
871  N ND2 . ASN A 112 ? 0.69765 0.49751 0.50890 -0.01899 0.04278  0.02607  315 ASN A ND2 
872  N N   . ILE A 113 ? 0.46885 0.30903 0.27114 0.01092  -0.00160 0.03019  316 ILE A N   
873  C CA  . ILE A 113 ? 0.44026 0.29951 0.25659 0.01149  -0.00700 0.02714  316 ILE A CA  
874  C C   . ILE A 113 ? 0.48082 0.34363 0.30114 0.00890  -0.00487 0.02940  316 ILE A C   
875  O O   . ILE A 113 ? 0.48757 0.33733 0.29536 0.01252  -0.00355 0.03098  316 ILE A O   
876  C CB  . ILE A 113 ? 0.47182 0.33175 0.28437 0.02129  -0.01488 0.02055  316 ILE A CB  
877  C CG1 . ILE A 113 ? 0.51597 0.36957 0.32186 0.02537  -0.01800 0.01768  316 ILE A CG1 
878  C CG2 . ILE A 113 ? 0.44263 0.32295 0.27428 0.01957  -0.01701 0.01482  316 ILE A CG2 
879  C CD1 . ILE A 113 ? 0.52472 0.39001 0.34364 0.01791  -0.01545 0.01800  316 ILE A CD1 
880  N N   . ILE A 114 ? 0.43092 0.30848 0.26565 0.00335  -0.00429 0.02956  317 ILE A N   
881  C CA  . ILE A 114 ? 0.40601 0.28840 0.24565 0.00127  -0.00320 0.03110  317 ILE A CA  
882  C C   . ILE A 114 ? 0.40337 0.29937 0.25408 0.00050  -0.00479 0.02793  317 ILE A C   
883  O O   . ILE A 114 ? 0.43393 0.33437 0.28928 -0.00396 -0.00297 0.02857  317 ILE A O   
884  C CB  . ILE A 114 ? 0.45083 0.33305 0.29504 -0.00534 0.00081  0.03376  317 ILE A CB  
885  C CG1 . ILE A 114 ? 0.47684 0.34567 0.31424 -0.00704 0.00589  0.03416  317 ILE A CG1 
886  C CG2 . ILE A 114 ? 0.50621 0.39227 0.35444 -0.00678 0.00139  0.03496  317 ILE A CG2 
887  C CD1 . ILE A 114 ? 0.51399 0.38618 0.36237 -0.01347 0.00941  0.03213  317 ILE A CD1 
888  N N   . GLN A 115 ? 0.41870 0.31926 0.27259 0.00532  -0.00750 0.02325  318 GLN A N   
889  C CA  . GLN A 115 ? 0.41884 0.33124 0.28559 0.00270  -0.00557 0.01867  318 GLN A CA  
890  C C   . GLN A 115 ? 0.42643 0.34111 0.29604 -0.00163 -0.00277 0.02294  318 GLN A C   
891  O O   . GLN A 115 ? 0.42057 0.33325 0.28767 0.00046  -0.00445 0.02508  318 GLN A O   
892  C CB  . GLN A 115 ? 0.37938 0.29908 0.25456 0.00924  -0.00929 0.00833  318 GLN A CB  
893  C CG  . GLN A 115 ? 0.39743 0.32869 0.28902 0.00431  -0.00347 0.00148  318 GLN A CG  
894  C CD  . GLN A 115 ? 0.36227 0.30450 0.26940 0.01029  -0.00662 -0.01337 318 GLN A CD  
895  O OE1 . GLN A 115 ? 0.38914 0.33068 0.29338 0.02021  -0.01543 -0.01765 318 GLN A OE1 
896  N NE2 . GLN A 115 ? 0.37053 0.32129 0.29371 0.00486  0.00106  -0.02301 318 GLN A NE2 
897  N N   . LYS A 116 ? 0.40755 0.32373 0.27963 -0.00696 0.00161  0.02397  319 LYS A N   
898  C CA  . LYS A 116 ? 0.40264 0.31816 0.27428 -0.01021 0.00326  0.02799  319 LYS A CA  
899  C C   . LYS A 116 ? 0.39822 0.32087 0.27882 -0.00972 0.00464  0.02467  319 LYS A C   
900  O O   . LYS A 116 ? 0.38306 0.31215 0.27293 -0.00827 0.00638  0.01708  319 LYS A O   
901  C CB  . LYS A 116 ? 0.42901 0.33823 0.29428 -0.01360 0.00714  0.02942  319 LYS A CB  
902  C CG  . LYS A 116 ? 0.51199 0.41460 0.36888 -0.01307 0.00466  0.03159  319 LYS A CG  
903  C CD  . LYS A 116 ? 0.61895 0.51096 0.46409 -0.01387 0.00766  0.03251  319 LYS A CD  
904  C CE  . LYS A 116 ? 0.72659 0.61181 0.56294 -0.01199 0.00528  0.03262  319 LYS A CE  
905  N NZ  . LYS A 116 ? 0.68978 0.55918 0.50810 -0.01021 0.00700  0.03365  319 LYS A NZ  
906  N N   . LYS A 117 ? 0.41919 0.34174 0.29930 -0.01107 0.00387  0.02870  320 LYS A N   
907  C CA  . LYS A 117 ? 0.47529 0.40454 0.36387 -0.01098 0.00499  0.02646  320 LYS A CA  
908  C C   . LYS A 117 ? 0.39717 0.32702 0.29068 -0.01477 0.01262  0.02228  320 LYS A C   
909  O O   . LYS A 117 ? 0.42892 0.34947 0.31361 -0.01789 0.01745  0.02376  320 LYS A O   
910  C CB  . LYS A 117 ? 0.47720 0.40507 0.36333 -0.01245 0.00283  0.03185  320 LYS A CB  
911  C CG  . LYS A 117 ? 0.49869 0.41959 0.37776 -0.01563 0.00406  0.03497  320 LYS A CG  
912  C CD  . LYS A 117 ? 0.53699 0.45839 0.41656 -0.01619 0.00012  0.03751  320 LYS A CD  
913  N N   . ASN A 118 ? 0.41477 0.35354 0.32128 -0.01425 0.01465  0.01628  321 ASN A N   
914  C CA  . ASN A 118 ? 0.39463 0.33297 0.30803 -0.01915 0.02490  0.01080  321 ASN A CA  
915  C C   . ASN A 118 ? 0.49184 0.41940 0.39325 -0.02259 0.02782  0.01849  321 ASN A C   
916  O O   . ASN A 118 ? 0.45814 0.38989 0.36116 -0.02110 0.02246  0.02224  321 ASN A O   
917  C CB  . ASN A 118 ? 0.39295 0.34635 0.32760 -0.01667 0.02506  -0.00020 321 ASN A CB  
918  C CG  . ASN A 118 ? 0.52836 0.48265 0.47567 -0.02297 0.03865  -0.00969 321 ASN A CG  
919  O OD1 . ASN A 118 ? 0.47516 0.41463 0.41104 -0.02944 0.04973  -0.00717 321 ASN A OD1 
920  N ND2 . ASN A 118 ? 0.50791 0.47767 0.47809 -0.02058 0.03861  -0.02194 321 ASN A ND2 
921  N N   . GLU A 119 ? 0.49300 0.40439 0.37986 -0.02620 0.03584  0.02041  322 GLU A N   
922  C CA  . GLU A 119 ? 0.51222 0.40827 0.38223 -0.02707 0.03757  0.02661  322 GLU A CA  
923  C C   . GLU A 119 ? 0.55342 0.44696 0.42895 -0.03115 0.04810  0.02270  322 GLU A C   
924  O O   . GLU A 119 ? 0.61292 0.49398 0.47466 -0.03083 0.04835  0.02763  322 GLU A O   
925  C CB  . GLU A 119 ? 0.59794 0.47125 0.44271 -0.02672 0.04113  0.03022  322 GLU A CB  
926  C CG  . GLU A 119 ? 0.75554 0.63020 0.59465 -0.02256 0.03078  0.03344  322 GLU A CG  
927  C CD  . GLU A 119 ? 0.86567 0.74346 0.70273 -0.01836 0.01841  0.03762  322 GLU A CD  
928  O OE1 . GLU A 119 ? 0.94547 0.82020 0.77975 -0.01783 0.01716  0.03908  322 GLU A OE1 
929  O OE2 . GLU A 119 ? 0.93252 0.81585 0.77218 -0.01600 0.01073  0.03814  322 GLU A OE2 
930  N N   . ASN A 120 ? 0.50458 0.40910 0.40051 -0.03453 0.05676  0.01240  323 ASN A N   
931  C CA  . ASN A 120 ? 0.57012 0.47366 0.47601 -0.03947 0.06907  0.00590  323 ASN A CA  
932  C C   . ASN A 120 ? 0.48748 0.41784 0.42594 -0.03776 0.06563  -0.00529 323 ASN A C   
933  O O   . ASN A 120 ? 0.45180 0.39005 0.41075 -0.04124 0.07590  -0.01936 323 ASN A O   
934  C CB  . ASN A 120 ? 0.61847 0.50216 0.51537 -0.04654 0.08859  0.00021  323 ASN A CB  
935  C CG  . ASN A 120 ? 0.75504 0.60756 0.61382 -0.04550 0.09073  0.01097  323 ASN A CG  
936  O OD1 . ASN A 120 ? 0.85324 0.69495 0.70035 -0.04612 0.09466  0.01072  323 ASN A OD1 
937  N ND2 . ASN A 120 ? 0.85934 0.69690 0.69780 -0.04255 0.08670  0.01954  323 ASN A ND2 
938  N N   . PRO A 121 ? 0.45739 0.40122 0.40122 -0.03178 0.05137  -0.00101 324 PRO A N   
939  C CA  . PRO A 121 ? 0.42585 0.39183 0.39542 -0.02711 0.04569  -0.01169 324 PRO A CA  
940  C C   . PRO A 121 ? 0.47756 0.45007 0.46474 -0.03068 0.05445  -0.01997 324 PRO A C   
941  O O   . PRO A 121 ? 0.47069 0.43131 0.44677 -0.03513 0.06040  -0.01296 324 PRO A O   
942  C CB  . PRO A 121 ? 0.45308 0.42330 0.41452 -0.02036 0.03041  -0.00217 324 PRO A CB  
943  C CG  . PRO A 121 ? 0.42206 0.37770 0.36390 -0.02402 0.03108  0.01033  324 PRO A CG  
944  C CD  . PRO A 121 ? 0.43387 0.37208 0.36050 -0.02856 0.04022  0.01202  324 PRO A CD  
945  N N   . VAL A 122 ? 0.40415 0.39547 0.41950 -0.02777 0.05460  -0.03655 325 VAL A N   
946  C CA  . VAL A 122 ? 0.42328 0.42666 0.46146 -0.02901 0.05966  -0.04694 325 VAL A CA  
947  C C   . VAL A 122 ? 0.40231 0.41959 0.44433 -0.01877 0.04232  -0.04432 325 VAL A C   
948  O O   . VAL A 122 ? 0.34145 0.36810 0.38753 -0.00893 0.02983  -0.04967 325 VAL A O   
949  C CB  . VAL A 122 ? 0.42400 0.44134 0.49490 -0.03114 0.07003  -0.07059 325 VAL A CB  
950  C CG1 . VAL A 122 ? 0.47658 0.50846 0.57462 -0.03197 0.07488  -0.08324 325 VAL A CG1 
951  C CG2 . VAL A 122 ? 0.48141 0.48076 0.54542 -0.04259 0.09033  -0.07311 325 VAL A CG2 
952  N N   . VAL A 123 ? 0.39811 0.41367 0.43556 -0.02045 0.04168  -0.03603 326 VAL A N   
953  C CA  . VAL A 123 ? 0.36435 0.38847 0.40006 -0.01210 0.02705  -0.03096 326 VAL A CA  
954  C C   . VAL A 123 ? 0.33538 0.37666 0.39763 -0.00973 0.02787  -0.04391 326 VAL A C   
955  O O   . VAL A 123 ? 0.35544 0.39717 0.43124 -0.01772 0.04154  -0.05046 326 VAL A O   
956  C CB  . VAL A 123 ? 0.33711 0.34771 0.34869 -0.01542 0.02411  -0.01255 326 VAL A CB  
957  C CG1 . VAL A 123 ? 0.36783 0.38586 0.37832 -0.00860 0.01205  -0.00824 326 VAL A CG1 
958  C CG2 . VAL A 123 ? 0.38739 0.38276 0.37599 -0.01693 0.02267  -0.00243 326 VAL A CG2 
959  N N   . HIS A 124 ? 0.30708 0.36021 0.37519 0.00176  0.01394  -0.04834 327 HIS A N   
960  C CA  . HIS A 124 ? 0.29733 0.36663 0.38808 0.00562  0.01197  -0.05891 327 HIS A CA  
961  C C   . HIS A 124 ? 0.29624 0.36380 0.37152 0.01245  -0.00041 -0.04741 327 HIS A C   
962  O O   . HIS A 124 ? 0.28651 0.34146 0.33667 0.01530  -0.00723 -0.03489 327 HIS A O   
963  C CB  . HIS A 124 ? 0.28752 0.37573 0.40795 0.01514  0.00779  -0.08355 327 HIS A CB  
964  C CG  . HIS A 124 ? 0.34352 0.43114 0.45295 0.03043  -0.00881 -0.08730 327 HIS A CG  
965  N ND1 . HIS A 124 ? 0.35393 0.43193 0.45021 0.03103  -0.00967 -0.08546 327 HIS A ND1 
966  C CD2 . HIS A 124 ? 0.38763 0.48047 0.49515 0.04693  -0.02509 -0.09395 327 HIS A CD2 
967  C CE1 . HIS A 124 ? 0.35523 0.43153 0.44098 0.04699  -0.02557 -0.09023 327 HIS A CE1 
968  N NE2 . HIS A 124 ? 0.35920 0.44267 0.44944 0.05745  -0.03521 -0.09533 327 HIS A NE2 
969  N N   . TYR A 125 ? 0.24078 0.32025 0.33187 0.01404  -0.00152 -0.05232 328 TYR A N   
970  C CA  . TYR A 125 ? 0.27422 0.35101 0.35167 0.01717  -0.00954 -0.04068 328 TYR A CA  
971  C C   . TYR A 125 ? 0.22798 0.31994 0.32124 0.02989  -0.01967 -0.05352 328 TYR A C   
972  O O   . TYR A 125 ? 0.27691 0.38566 0.39966 0.03241  -0.01748 -0.07171 328 TYR A O   
973  C CB  . TYR A 125 ? 0.22698 0.29970 0.30271 0.00508  -0.00076 -0.02998 328 TYR A CB  
974  C CG  . TYR A 125 ? 0.25753 0.31262 0.31403 -0.00476 0.00703  -0.01821 328 TYR A CG  
975  C CD1 . TYR A 125 ? 0.31644 0.36629 0.37841 -0.01203 0.01977  -0.02351 328 TYR A CD1 
976  C CD2 . TYR A 125 ? 0.25755 0.30030 0.29063 -0.00628 0.00207  -0.00356 328 TYR A CD2 
977  C CE1 . TYR A 125 ? 0.32734 0.35804 0.36760 -0.01894 0.02580  -0.01302 328 TYR A CE1 
978  C CE2 . TYR A 125 ? 0.27925 0.30653 0.29544 -0.01304 0.00698  0.00500  328 TYR A CE2 
979  C CZ  . TYR A 125 ? 0.31724 0.33774 0.33514 -0.01847 0.01796  0.00090  328 TYR A CZ  
980  O OH  . TYR A 125 ? 0.32417 0.32647 0.32143 -0.02323 0.02183  0.00917  328 TYR A OH  
981  N N   . LYS A 126 ? 0.24088 0.32541 0.31393 0.03816  -0.03010 -0.04525 329 LYS A N   
982  C CA  . LYS A 126 ? 0.25642 0.35043 0.33666 0.05115  -0.04057 -0.05415 329 LYS A CA  
983  C C   . LYS A 126 ? 0.24590 0.33430 0.31298 0.04655  -0.04055 -0.03956 329 LYS A C   
984  O O   . LYS A 126 ? 0.27288 0.34377 0.31308 0.04357  -0.04040 -0.02506 329 LYS A O   
985  C CB  . LYS A 126 ? 0.26182 0.34607 0.32339 0.06944  -0.05412 -0.06034 329 LYS A CB  
986  C CG  . LYS A 126 ? 0.35381 0.44606 0.43068 0.07819  -0.05834 -0.07908 329 LYS A CG  
987  C CD  . LYS A 126 ? 0.40922 0.48913 0.46344 0.10022  -0.07495 -0.08599 329 LYS A CD  
988  C CE  . LYS A 126 ? 0.59424 0.68077 0.66139 0.11138  -0.08212 -0.10613 329 LYS A CE  
989  N NZ  . LYS A 126 ? 0.60343 0.67164 0.64032 0.13541  -0.10000 -0.11183 329 LYS A NZ  
990  N N   . TRP A 127 ? 0.22590 0.32966 0.31376 0.04586  -0.04028 -0.04498 330 TRP A N   
991  C CA  . TRP A 127 ? 0.23545 0.33700 0.31536 0.04151  -0.04058 -0.03344 330 TRP A CA  
992  C C   . TRP A 127 ? 0.18563 0.29079 0.26323 0.05678  -0.05206 -0.04023 330 TRP A C   
993  O O   . TRP A 127 ? 0.23143 0.34796 0.32454 0.06964  -0.05937 -0.05720 330 TRP A O   
994  C CB  . TRP A 127 ? 0.20394 0.31705 0.30546 0.02871  -0.03116 -0.03272 330 TRP A CB  
995  C CG  . TRP A 127 ? 0.18927 0.29340 0.28728 0.01611  -0.02000 -0.02695 330 TRP A CG  
996  C CD1 . TRP A 127 ? 0.21735 0.32573 0.33206 0.01162  -0.01067 -0.03687 330 TRP A CD1 
997  C CD2 . TRP A 127 ? 0.21761 0.30488 0.29210 0.00798  -0.01735 -0.01167 330 TRP A CD2 
998  N NE1 . TRP A 127 ? 0.22362 0.31608 0.32251 0.00146  -0.00220 -0.02680 330 TRP A NE1 
999  C CE2 . TRP A 127 ? 0.21075 0.29132 0.28578 -0.00000 -0.00752 -0.01185 330 TRP A CE2 
1000 C CE3 . TRP A 127 ? 0.21928 0.29634 0.27377 0.00665  -0.02162 0.00030  330 TRP A CE3 
1001 C CZ2 . TRP A 127 ? 0.23988 0.30398 0.29442 -0.00725 -0.00435 -0.00014 330 TRP A CZ2 
1002 C CZ3 . TRP A 127 ? 0.25489 0.31858 0.29405 -0.00156 -0.01797 0.01002  330 TRP A CZ3 
1003 C CH2 . TRP A 127 ? 0.24870 0.30616 0.28726 -0.00737 -0.01066 0.00985  330 TRP A CH2 
1004 N N   . VAL A 128 ? 0.21013 0.30443 0.26777 0.05609  -0.05376 -0.02842 331 VAL A N   
1005 C CA  . VAL A 128 ? 0.24261 0.33829 0.29601 0.06954  -0.06313 -0.03356 331 VAL A CA  
1006 C C   . VAL A 128 ? 0.22867 0.35116 0.31879 0.07183  -0.06525 -0.04778 331 VAL A C   
1007 O O   . VAL A 128 ? 0.20144 0.33704 0.31415 0.05826  -0.05642 -0.04662 331 VAL A O   
1008 C CB  . VAL A 128 ? 0.21588 0.29780 0.24780 0.06354  -0.06030 -0.01892 331 VAL A CB  
1009 C CG1 . VAL A 128 ? 0.20496 0.29030 0.23582 0.07490  -0.06796 -0.02367 331 VAL A CG1 
1010 C CG2 . VAL A 128 ? 0.28721 0.34018 0.28234 0.06435  -0.05778 -0.00913 331 VAL A CG2 
1011 N N   . ASP A 129 ? 0.19922 0.32777 0.29380 0.09006  -0.07701 -0.06229 332 ASP A N   
1012 C CA  . ASP A 129 ? 0.21899 0.37131 0.34946 0.09206  -0.07791 -0.07909 332 ASP A CA  
1013 C C   . ASP A 129 ? 0.25245 0.41235 0.39351 0.07970  -0.07109 -0.07081 332 ASP A C   
1014 O O   . ASP A 129 ? 0.22267 0.37472 0.34544 0.08081  -0.07432 -0.05944 332 ASP A O   
1015 C CB  . ASP A 129 ? 0.26519 0.40709 0.38186 0.10831  -0.08813 -0.09253 332 ASP A CB  
1016 C CG  . ASP A 129 ? 0.35483 0.50997 0.49834 0.10463  -0.08530 -0.10942 332 ASP A CG  
1017 O OD1 . ASP A 129 ? 0.39519 0.56073 0.56207 0.09987  -0.08071 -0.12250 332 ASP A OD1 
1018 O OD2 . ASP A 129 ? 0.34116 0.49522 0.48176 0.10609  -0.08723 -0.10999 332 ASP A OD2 
1019 N N   . GLY A 130 ? 0.19392 0.36652 0.36261 0.06767  -0.06073 -0.07667 333 GLY A N   
1020 C CA  . GLY A 130 ? 0.20012 0.37648 0.37664 0.05774  -0.05467 -0.07063 333 GLY A CA  
1021 C C   . GLY A 130 ? 0.20620 0.38480 0.38391 0.04381  -0.04781 -0.05583 333 GLY A C   
1022 O O   . GLY A 130 ? 0.21279 0.39227 0.39425 0.03618  -0.04348 -0.05027 333 GLY A O   
1023 N N   . ILE A 131 ? 0.15891 0.33028 0.32498 0.03875  -0.04554 -0.04755 334 ILE A N   
1024 C CA  . ILE A 131 ? 0.15039 0.31165 0.30534 0.02380  -0.03786 -0.03217 334 ILE A CA  
1025 C C   . ILE A 131 ? 0.13872 0.29729 0.30307 0.01262  -0.02531 -0.03351 334 ILE A C   
1026 O O   . ILE A 131 ? 0.20774 0.35316 0.35760 0.00244  -0.01999 -0.02172 334 ILE A O   
1027 C CB  . ILE A 131 ? 0.20416 0.34555 0.32673 0.02211  -0.04030 -0.01795 334 ILE A CB  
1028 C CG1 . ILE A 131 ? 0.19120 0.32030 0.30072 0.02294  -0.03789 -0.01778 334 ILE A CG1 
1029 C CG2 . ILE A 131 ? 0.19497 0.33284 0.30344 0.03177  -0.04904 -0.01604 334 ILE A CG2 
1030 C CD1 . ILE A 131 ? 0.19686 0.30718 0.27997 0.01652  -0.03624 -0.00412 334 ILE A CD1 
1031 N N   . GLY A 132 ? 0.17468 0.34375 0.36217 0.01490  -0.02022 -0.04910 335 GLY A N   
1032 C CA  . GLY A 132 ? 0.20258 0.36432 0.39559 0.00372  -0.00523 -0.05096 335 GLY A CA  
1033 C C   . GLY A 132 ? 0.19156 0.33510 0.36028 0.00113  -0.00335 -0.04265 335 GLY A C   
1034 O O   . GLY A 132 ? 0.20971 0.35095 0.36646 0.00965  -0.01247 -0.04207 335 GLY A O   
1035 N N   . ALA A 133 ? 0.18909 0.31693 0.34793 -0.01006 0.00888  -0.03630 336 ALA A N   
1036 C CA  . ALA A 133 ? 0.18079 0.29056 0.31710 -0.01329 0.01191  -0.02881 336 ALA A CA  
1037 C C   . ALA A 133 ? 0.20132 0.29033 0.31768 -0.02313 0.02007  -0.01707 336 ALA A C   
1038 O O   . ALA A 133 ? 0.22120 0.30796 0.34483 -0.02846 0.02864  -0.01909 336 ALA A O   
1039 C CB  . ALA A 133 ? 0.17949 0.29225 0.33052 -0.01307 0.02042  -0.04302 336 ALA A CB  
1040 N N   . PRO A 134 ? 0.19361 0.26560 0.28371 -0.02463 0.01732  -0.00589 337 PRO A N   
1041 C CA  . PRO A 134 ? 0.23149 0.28153 0.29931 -0.03074 0.02200  0.00370  337 PRO A CA  
1042 C C   . PRO A 134 ? 0.26900 0.30257 0.33419 -0.03724 0.03960  -0.00101 337 PRO A C   
1043 O O   . PRO A 134 ? 0.31896 0.35148 0.39017 -0.03866 0.04830  -0.00838 337 PRO A O   
1044 C CB  . PRO A 134 ? 0.25076 0.28918 0.29550 -0.02912 0.01451  0.01265  337 PRO A CB  
1045 C CG  . PRO A 134 ? 0.24190 0.29028 0.29496 -0.02481 0.01260  0.00714  337 PRO A CG  
1046 C CD  . PRO A 134 ? 0.20059 0.27131 0.27869 -0.01960 0.00868  -0.00206 337 PRO A CD  
1047 N N   . THR A 135 ? 0.24819 0.26609 0.30222 -0.04118 0.04569  0.00282  338 THR A N   
1048 C CA  . THR A 135 ? 0.30400 0.29431 0.34231 -0.04747 0.06408  0.00151  338 THR A CA  
1049 C C   . THR A 135 ? 0.31500 0.27754 0.31649 -0.04625 0.06181  0.01166  338 THR A C   
1050 O O   . THR A 135 ? 0.33215 0.29746 0.32242 -0.04119 0.04575  0.01926  338 THR A O   
1051 C CB  . THR A 135 ? 0.34937 0.32712 0.38300 -0.05074 0.07158  0.00231  338 THR A CB  
1052 O OG1 . THR A 135 ? 0.34202 0.31165 0.35396 -0.04609 0.05625  0.01346  338 THR A OG1 
1053 C CG2 . THR A 135 ? 0.34967 0.35698 0.42215 -0.05145 0.07290  -0.00867 338 THR A CG2 
1054 N N   . GLU A 136 ? 0.39083 0.32509 0.37343 -0.05093 0.07906  0.01045  339 GLU A N   
1055 C CA  . GLU A 136 ? 0.45234 0.35723 0.39676 -0.04816 0.07647  0.01949  339 GLU A CA  
1056 C C   . GLU A 136 ? 0.44160 0.33002 0.35896 -0.04215 0.06301  0.02880  339 GLU A C   
1057 O O   . GLU A 136 ? 0.44234 0.32630 0.34285 -0.03619 0.04855  0.03447  339 GLU A O   
1058 C CB  . GLU A 136 ? 0.55884 0.43076 0.48305 -0.05408 0.09945  0.01651  339 GLU A CB  
1059 C CG  . GLU A 136 ? 0.61572 0.50401 0.56579 -0.05906 0.11018  0.00574  339 GLU A CG  
1060 C CD  . GLU A 136 ? 0.70468 0.60966 0.65765 -0.05368 0.09410  0.00894  339 GLU A CD  
1061 O OE1 . GLU A 136 ? 0.71114 0.59396 0.63268 -0.05054 0.08983  0.01735  339 GLU A OE1 
1062 O OE2 . GLU A 136 ? 0.65832 0.59670 0.64326 -0.05164 0.08548  0.00252  339 GLU A OE2 
1063 N N   . ASN A 137 ? 0.40646 0.28750 0.32208 -0.04315 0.06675  0.02863  340 ASN A N   
1064 C CA  . ASN A 137 ? 0.49099 0.35818 0.38348 -0.03627 0.05225  0.03513  340 ASN A CA  
1065 C C   . ASN A 137 ? 0.49062 0.39005 0.40335 -0.03182 0.03014  0.03619  340 ASN A C   
1066 O O   . ASN A 137 ? 0.47085 0.36130 0.36610 -0.02525 0.01534  0.03934  340 ASN A O   
1067 C CB  . ASN A 137 ? 0.48467 0.33953 0.37415 -0.03849 0.06101  0.03399  340 ASN A CB  
1068 C CG  . ASN A 137 ? 0.68275 0.49160 0.53756 -0.04147 0.08297  0.03451  340 ASN A CG  
1069 O OD1 . ASN A 137 ? 0.73905 0.52036 0.56450 -0.03986 0.08863  0.03721  340 ASN A OD1 
1070 N ND2 . ASN A 137 ? 0.70501 0.50250 0.56098 -0.04593 0.09677  0.03174  340 ASN A ND2 
1071 N N   . GLN A 138 ? 0.34787 0.28235 0.29568 -0.03458 0.02787  0.03221  341 GLN A N   
1072 C CA  . GLN A 138 ? 0.32461 0.28517 0.28876 -0.03136 0.01057  0.03300  341 GLN A CA  
1073 C C   . GLN A 138 ? 0.35506 0.31882 0.31439 -0.02904 0.00305  0.03473  341 GLN A C   
1074 O O   . GLN A 138 ? 0.30555 0.28684 0.27608 -0.02733 -0.00861 0.03472  341 GLN A O   
1075 C CB  . GLN A 138 ? 0.25917 0.25150 0.25831 -0.03350 0.01111  0.02791  341 GLN A CB  
1076 C CG  . GLN A 138 ? 0.30706 0.30281 0.31620 -0.03513 0.01417  0.02578  341 GLN A CG  
1077 C CD  . GLN A 138 ? 0.31856 0.34061 0.36126 -0.03694 0.01957  0.01782  341 GLN A CD  
1078 O OE1 . GLN A 138 ? 0.25027 0.28913 0.30795 -0.03518 0.01782  0.01383  341 GLN A OE1 
1079 N NE2 . GLN A 138 ? 0.24065 0.26520 0.29451 -0.03927 0.02548  0.01434  341 GLN A NE2 
1080 N N   . LYS A 139 ? 0.33045 0.27671 0.27347 -0.02949 0.01075  0.03564  342 LYS A N   
1081 C CA  . LYS A 139 ? 0.32528 0.27432 0.26449 -0.02757 0.00478  0.03688  342 LYS A CA  
1082 C C   . LYS A 139 ? 0.37674 0.30266 0.28733 -0.02231 -0.00366 0.03972  342 LYS A C   
1083 O O   . LYS A 139 ? 0.46285 0.35952 0.34639 -0.02042 0.00255  0.04147  342 LYS A O   
1084 C CB  . LYS A 139 ? 0.33879 0.28499 0.27979 -0.03055 0.01701  0.03470  342 LYS A CB  
1085 C CG  . LYS A 139 ? 0.33038 0.30023 0.30119 -0.03327 0.02315  0.02817  342 LYS A CG  
1086 C CD  . LYS A 139 ? 0.40430 0.36952 0.37591 -0.03551 0.03405  0.02380  342 LYS A CD  
1087 C CE  . LYS A 139 ? 0.47909 0.46887 0.48133 -0.03551 0.03694  0.01397  342 LYS A CE  
1088 N NZ  . LYS A 139 ? 0.47518 0.46023 0.47911 -0.03761 0.04702  0.00774  342 LYS A NZ  
1089 N N   . ILE A 140 ? 0.33029 0.26721 0.24588 -0.01935 -0.01721 0.03871  343 ILE A N   
1090 C CA  . ILE A 140 ? 0.35523 0.27498 0.24953 -0.01255 -0.02861 0.03745  343 ILE A CA  
1091 C C   . ILE A 140 ? 0.32683 0.24762 0.21909 -0.01161 -0.03114 0.03664  343 ILE A C   
1092 O O   . ILE A 140 ? 0.33426 0.27622 0.24712 -0.01462 -0.03386 0.03478  343 ILE A O   
1093 C CB  . ILE A 140 ? 0.34599 0.27860 0.25199 -0.00992 -0.04257 0.03275  343 ILE A CB  
1094 C CG1 . ILE A 140 ? 0.34027 0.27744 0.25393 -0.01190 -0.03989 0.03370  343 ILE A CG1 
1095 C CG2 . ILE A 140 ? 0.43731 0.35110 0.32172 -0.00051 -0.05607 0.02785  343 ILE A CG2 
1096 C CD1 . ILE A 140 ? 0.45609 0.36329 0.34236 -0.00912 -0.03271 0.03677  343 ILE A CD1 
1097 N N   . LYS A 141 ? 0.36716 0.26223 0.23197 -0.00696 -0.02991 0.03784  344 LYS A N   
1098 C CA  . LYS A 141 ? 0.40494 0.30049 0.26748 -0.00545 -0.03309 0.03650  344 LYS A CA  
1099 C C   . LYS A 141 ? 0.41269 0.31658 0.28217 -0.00038 -0.04912 0.02906  344 LYS A C   
1100 O O   . LYS A 141 ? 0.43071 0.33342 0.29937 0.00423  -0.05919 0.02437  344 LYS A O   
1101 C CB  . LYS A 141 ? 0.46100 0.32536 0.29091 -0.00125 -0.02730 0.03926  344 LYS A CB  
1102 C CG  . LYS A 141 ? 0.52926 0.38362 0.35415 -0.00753 -0.00875 0.04359  344 LYS A CG  
1103 C CD  . LYS A 141 ? 0.72471 0.55575 0.52595 -0.00657 -0.00006 0.04548  344 LYS A CD  
1104 C CE  . LYS A 141 ? 0.70298 0.50978 0.48733 -0.01098 0.01937  0.04748  344 LYS A CE  
1105 N NZ  . LYS A 141 ? 0.84986 0.67906 0.66495 -0.01998 0.03028  0.04534  344 LYS A NZ  
1106 N N   . MET A 142 ? 0.37860 0.29073 0.25613 -0.00116 -0.05116 0.02625  345 MET A N   
1107 C CA  . MET A 142 ? 0.40193 0.32771 0.29584 0.00056  -0.06252 0.01645  345 MET A CA  
1108 C C   . MET A 142 ? 0.41205 0.32566 0.29288 0.00783  -0.07012 0.01057  345 MET A C   
1109 O O   . MET A 142 ? 0.40138 0.30673 0.27155 0.00706  -0.06348 0.01545  345 MET A O   
1110 C CB  . MET A 142 ? 0.34540 0.29466 0.26643 -0.00850 -0.05613 0.01628  345 MET A CB  
1111 C CG  . MET A 142 ? 0.31937 0.28220 0.25509 -0.01349 -0.05241 0.01890  345 MET A CG  
1112 S SD  . MET A 142 ? 0.36386 0.34401 0.31909 -0.02157 -0.04296 0.02095  345 MET A SD  
1113 C CE  . MET A 142 ? 0.43598 0.42640 0.40975 -0.02401 -0.04866 0.00844  345 MET A CE  
1114 N N   . LYS A 143 ? 0.42738 0.34141 0.31122 0.01540  -0.08485 -0.00164 346 LYS A N   
1115 C CA  . LYS A 143 ? 0.49188 0.39826 0.36874 0.02384  -0.09485 -0.01125 346 LYS A CA  
1116 C C   . LYS A 143 ? 0.49284 0.42095 0.39882 0.01608  -0.09102 -0.01768 346 LYS A C   
1117 O O   . LYS A 143 ? 0.46043 0.40887 0.39335 0.00702  -0.08605 -0.02062 346 LYS A O   
1118 C CB  . LYS A 143 ? 0.52695 0.42634 0.39829 0.03691  -0.11404 -0.02572 346 LYS A CB  
1119 C CG  . LYS A 143 ? 0.62380 0.48797 0.45147 0.04973  -0.11971 -0.02064 346 LYS A CG  
1120 C CD  . LYS A 143 ? 0.78800 0.64386 0.60818 0.06481  -0.14087 -0.03588 346 LYS A CD  
1121 C CE  . LYS A 143 ? 0.82989 0.64153 0.59675 0.08072  -0.14704 -0.03153 346 LYS A CE  
1122 N NZ  . LYS A 143 ? 0.94604 0.74577 0.70050 0.09527  -0.16606 -0.04307 346 LYS A NZ  
1123 N N   . ILE A 144 ? 0.51539 0.43618 0.41336 0.01982  -0.09228 -0.01994 347 ILE A N   
1124 C CA  . ILE A 144 ? 0.53083 0.46794 0.45345 0.01357  -0.08856 -0.02753 347 ILE A CA  
1125 C C   . ILE A 144 ? 0.64995 0.59839 0.59451 0.01870  -0.10191 -0.04898 347 ILE A C   
1126 O O   . ILE A 144 ? 0.62208 0.55944 0.55358 0.03244  -0.11807 -0.05890 347 ILE A O   
1127 C CB  . ILE A 144 ? 0.49010 0.41569 0.39692 0.01584  -0.08510 -0.02256 347 ILE A CB  
1128 C CG1 . ILE A 144 ? 0.47237 0.38966 0.36293 0.01001  -0.07137 -0.00458 347 ILE A CG1 
1129 C CG2 . ILE A 144 ? 0.52625 0.46641 0.45753 0.01020  -0.08156 -0.03186 347 ILE A CG2 
1130 C CD1 . ILE A 144 ? 0.50632 0.41001 0.37833 0.01245  -0.06754 0.00096  347 ILE A CD1 
1131 N N   . LYS A 145 ? 0.65600 0.62466 0.63302 0.00831  -0.09492 -0.05768 348 LYS A N   
1132 C CA  . LYS A 145 ? 0.65150 0.63460 0.65756 0.01039  -0.10419 -0.08163 348 LYS A CA  
1133 C C   . LYS A 145 ? 0.80295 0.79080 0.82354 0.00887  -0.10139 -0.09274 348 LYS A C   
1134 O O   . LYS A 145 ? 0.69591 0.68037 0.71114 0.00129  -0.08772 -0.08100 348 LYS A O   
1135 C CB  . LYS A 145 ? 0.64403 0.64484 0.67882 -0.00150 -0.09552 -0.08732 348 LYS A CB  
1136 C CG  . LYS A 145 ? 0.71534 0.71655 0.74499 0.00156  -0.10255 -0.08417 348 LYS A CG  
1137 C CD  . LYS A 145 ? 0.60230 0.62152 0.66235 -0.01012 -0.09407 -0.09239 348 LYS A CD  
1138 C CE  . LYS A 145 ? 0.70663 0.72664 0.76071 -0.00790 -0.09982 -0.08669 348 LYS A CE  
1139 N NZ  . LYS A 145 ? 0.75524 0.76160 0.77962 -0.00782 -0.09345 -0.06217 348 LYS A NZ  
1140 N N   A ASN A 146 ? 0.82483 0.82095 0.86516 0.01693  -0.11523 -0.11728 349 ASN A N   
1141 N N   B ASN A 146 ? 0.82519 0.82093 0.86485 0.01721  -0.11547 -0.11713 349 ASN A N   
1142 C CA  A ASN A 146 ? 0.86245 0.86704 0.92504 0.01513  -0.11290 -0.13341 349 ASN A CA  
1143 C CA  B ASN A 146 ? 0.86233 0.86694 0.92498 0.01518  -0.11297 -0.13351 349 ASN A CA  
1144 C C   A ASN A 146 ? 0.88448 0.90958 0.98903 0.01446  -0.11916 -0.16404 349 ASN A C   
1145 C C   B ASN A 146 ? 0.88430 0.90946 0.98889 0.01434  -0.11906 -0.16392 349 ASN A C   
1146 O O   A ASN A 146 ? 0.87597 0.90281 0.98232 0.02816  -0.13948 -0.17945 349 ASN A O   
1147 O O   B ASN A 146 ? 0.87574 0.90272 0.98218 0.02783  -0.13919 -0.17911 349 ASN A O   
1148 C CB  A ASN A 146 ? 0.84702 0.83702 0.88573 0.03056  -0.12674 -0.13428 349 ASN A CB  
1149 C CB  B ASN A 146 ? 0.84660 0.83716 0.88649 0.03050  -0.12678 -0.13508 349 ASN A CB  
1150 C CG  A ASN A 146 ? 0.84316 0.83851 0.89689 0.02553  -0.11835 -0.14071 349 ASN A CG  
1151 C CG  B ASN A 146 ? 0.86437 0.83994 0.87583 0.02637  -0.11466 -0.11062 349 ASN A CG  
1152 O OD1 A ASN A 146 ? 0.83311 0.82623 0.88650 0.03782  -0.13172 -0.15467 349 ASN A OD1 
1153 O OD1 B ASN A 146 ? 0.83030 0.78724 0.80969 0.03804  -0.12325 -0.10257 349 ASN A OD1 
1154 N ND2 A ASN A 146 ? 0.82866 0.82913 0.89370 0.00843  -0.09644 -0.13104 349 ASN A ND2 
1155 N ND2 B ASN A 146 ? 0.81550 0.79698 0.83687 0.01037  -0.09444 -0.09963 349 ASN A ND2 
1156 N N   . ASN A 147 ? 0.94568 0.98419 1.08275 -0.00127 -0.10095 -0.17382 350 ASN A N   
1157 C CA  . ASN A 147 ? 0.92257 0.98145 1.10321 -0.00521 -0.09897 -0.20126 350 ASN A CA  
1158 C C   . ASN A 147 ? 0.98010 1.04476 1.16296 -0.00265 -0.10348 -0.19961 350 ASN A C   
1159 O O   . ASN A 147 ? 0.99082 1.06764 1.19290 0.00766  -0.11029 -0.21363 350 ASN A O   
1160 C CB  . ASN A 147 ? 0.95932 1.02678 1.15511 0.01075  -0.11030 -0.21879 350 ASN A CB  
1161 C CG  . ASN A 147 ? 1.01877 1.08068 1.21150 0.00921  -0.10682 -0.22003 350 ASN A CG  
1162 O OD1 . ASN A 147 ? 1.00778 1.05233 1.16669 0.01636  -0.11788 -0.20838 350 ASN A OD1 
1163 N ND2 . ASN A 147 ? 1.05279 1.12841 1.27976 0.00012  -0.09039 -0.23407 350 ASN A ND2 
1164 N N   . GLY A 148 ? 0.93781 0.99407 1.10130 -0.01107 -0.09936 -0.18176 351 GLY A N   
1165 C CA  . GLY A 148 ? 0.91047 0.97152 1.07491 -0.01024 -0.10320 -0.17909 351 GLY A CA  
1166 C C   . GLY A 148 ? 0.86801 0.91992 1.00734 0.00926  -0.12560 -0.17505 351 GLY A C   
1167 O O   . GLY A 148 ? 0.89042 0.94556 1.03039 0.01158  -0.12871 -0.17300 351 GLY A O   
1168 N N   . ILE A 149 ? 0.91200 0.94941 1.02640 0.02363  -0.13981 -0.17323 352 ILE A N   
1169 C CA  . ILE A 149 ? 0.91084 0.93146 0.99428 0.04357  -0.15858 -0.16857 352 ILE A CA  
1170 C C   . ILE A 149 ? 0.82706 0.82295 0.86452 0.04533  -0.16084 -0.14569 352 ILE A C   
1171 O O   . ILE A 149 ? 0.76425 0.75322 0.79097 0.04184  -0.15118 -0.13506 352 ILE A O   
1172 C CB  . ILE A 149 ? 0.84103 0.86039 0.92956 0.06237  -0.17112 -0.18448 352 ILE A CB  
1173 N N   . GLU A 150 ? 0.85453 0.83653 0.86536 0.05041  -0.16547 -0.13225 353 GLU A N   
1174 C CA  . GLU A 150 ? 0.80570 0.76161 0.77246 0.05308  -0.15946 -0.10628 353 GLU A CA  
1175 C C   . GLU A 150 ? 0.78874 0.72123 0.72459 0.06977  -0.17196 -0.10923 353 GLU A C   
1176 O O   . GLU A 150 ? 0.87703 0.80112 0.80663 0.08711  -0.18993 -0.12470 353 GLU A O   
1177 C CB  . GLU A 150 ? 0.87295 0.81640 0.81809 0.05679  -0.16287 -0.09577 353 GLU A CB  
1178 C CG  . GLU A 150 ? 0.78832 0.74762 0.75083 0.03985  -0.14614 -0.08308 353 GLU A CG  
1179 C CD  . GLU A 150 ? 0.95739 0.90330 0.89779 0.04402  -0.14919 -0.07276 353 GLU A CD  
1180 O OE1 . GLU A 150 ? 1.02125 0.94441 0.93292 0.06020  -0.16466 -0.07706 353 GLU A OE1 
1181 O OE2 . GLU A 150 ? 0.83594 0.79193 0.78572 0.03205  -0.13619 -0.06086 353 GLU A OE2 
1182 N N   . THR A 151 ? 0.75950 0.68131 0.67772 0.06503  -0.15938 -0.09314 354 THR A N   
1183 C CA  . THR A 151 ? 0.76937 0.66336 0.65009 0.08029  -0.16842 -0.09133 354 THR A CA  
1184 C C   . THR A 151 ? 0.84791 0.70855 0.68101 0.08728  -0.16726 -0.07389 354 THR A C   
1185 O O   . THR A 151 ? 0.77144 0.63348 0.60445 0.08086  -0.16113 -0.06506 354 THR A O   
1186 C CB  . THR A 151 ? 0.74106 0.63731 0.62361 0.07210  -0.15508 -0.08277 354 THR A CB  
1187 O OG1 . THR A 151 ? 0.78441 0.66988 0.64694 0.06172  -0.13675 -0.05829 354 THR A OG1 
1188 C CG2 . THR A 151 ? 0.80566 0.73422 0.73608 0.05823  -0.14678 -0.09390 354 THR A CG2 
1189 N N   . GLU A 152 ? 0.86807 0.69636 0.65920 0.10036  -0.17182 -0.06934 355 GLU A N   
1190 C CA  . GLU A 152 ? 0.87745 0.66832 0.61970 0.10513  -0.16540 -0.05229 355 GLU A CA  
1191 C C   . GLU A 152 ? 0.76054 0.54980 0.49811 0.08853  -0.14035 -0.03104 355 GLU A C   
1192 O O   . GLU A 152 ? 0.71265 0.47314 0.41520 0.08871  -0.12993 -0.01738 355 GLU A O   
1193 C CB  . GLU A 152 ? 0.88839 0.64145 0.59006 0.12593  -0.17545 -0.05701 355 GLU A CB  
1194 C CG  . GLU A 152 ? 0.99482 0.74765 0.70812 0.14279  -0.19306 -0.07609 355 GLU A CG  
1195 C CD  . GLU A 152 ? 1.20779 0.92792 0.89182 0.16400  -0.20193 -0.08307 355 GLU A CD  
1196 O OE1 . GLU A 152 ? 1.26400 0.97923 0.93961 0.16466  -0.19916 -0.08109 355 GLU A OE1 
1197 O OE2 . GLU A 152 ? 1.23787 0.93575 0.90630 0.18083  -0.21206 -0.09079 355 GLU A OE2 
1198 N N   . ASP A 153 ? 0.67941 0.49783 0.45177 0.07441  -0.13001 -0.02952 356 ASP A N   
1199 C CA  . ASP A 153 ? 0.55692 0.37680 0.32866 0.06026  -0.10885 -0.01271 356 ASP A CA  
1200 C C   . ASP A 153 ? 0.58787 0.42863 0.38406 0.04571  -0.09674 -0.00490 356 ASP A C   
1201 O O   . ASP A 153 ? 0.59512 0.45764 0.41892 0.04281  -0.10260 -0.01288 356 ASP A O   
1202 C CB  . ASP A 153 ? 0.56424 0.40113 0.35647 0.05460  -0.10509 -0.01532 356 ASP A CB  
1203 C CG  . ASP A 153 ? 0.75480 0.57135 0.52274 0.06890  -0.11608 -0.02239 356 ASP A CG  
1204 O OD1 . ASP A 153 ? 0.73215 0.51388 0.45691 0.07793  -0.11526 -0.01537 356 ASP A OD1 
1205 O OD2 . ASP A 153 ? 0.73371 0.56709 0.52461 0.07143  -0.12487 -0.03586 356 ASP A OD2 
1206 N N   . TYR A 154 ? 0.54109 0.37504 0.32781 0.03697  -0.07969 0.00914  357 TYR A N   
1207 C CA  . TYR A 154 ? 0.53684 0.38860 0.34422 0.02479  -0.06809 0.01624  357 TYR A CA  
1208 C C   . TYR A 154 ? 0.49958 0.36666 0.32371 0.01388  -0.05475 0.02247  357 TYR A C   
1209 O O   . TYR A 154 ? 0.52890 0.38550 0.34031 0.01470  -0.05022 0.02513  357 TYR A O   
1210 C CB  . TYR A 154 ? 0.54485 0.37421 0.32760 0.02522  -0.05970 0.02441  357 TYR A CB  
1211 C CG  . TYR A 154 ? 0.56212 0.37995 0.33266 0.03356  -0.07060 0.02011  357 TYR A CG  
1212 C CD1 . TYR A 154 ? 0.65801 0.44400 0.39231 0.04886  -0.08250 0.01543  357 TYR A CD1 
1213 C CD2 . TYR A 154 ? 0.55378 0.39026 0.34631 0.02740  -0.06952 0.02049  357 TYR A CD2 
1214 C CE1 . TYR A 154 ? 0.67649 0.44967 0.39711 0.05808  -0.09377 0.01078  357 TYR A CE1 
1215 C CE2 . TYR A 154 ? 0.57824 0.40469 0.36031 0.03496  -0.07972 0.01632  357 TYR A CE2 
1216 C CZ  . TYR A 154 ? 0.64362 0.43831 0.38970 0.05042  -0.09209 0.01132  357 TYR A CZ  
1217 O OH  . TYR A 154 ? 0.72511 0.50776 0.45846 0.05956  -0.10369 0.00636  357 TYR A OH  
1218 N N   . PHE A 155 ? 0.42108 0.31154 0.27207 0.00473  -0.04914 0.02423  358 PHE A N   
1219 C CA  . PHE A 155 ? 0.41518 0.31608 0.27714 -0.00327 -0.03736 0.02993  358 PHE A CA  
1220 C C   . PHE A 155 ? 0.48748 0.37491 0.33467 -0.00525 -0.02574 0.03677  358 PHE A C   
1221 O O   . PHE A 155 ? 0.51174 0.39366 0.35442 -0.00560 -0.02283 0.03857  358 PHE A O   
1222 C CB  . PHE A 155 ? 0.43524 0.35913 0.32353 -0.01006 -0.03492 0.02956  358 PHE A CB  
1223 C CG  . PHE A 155 ? 0.37195 0.30784 0.27679 -0.01114 -0.04063 0.02196  358 PHE A CG  
1224 C CD1 . PHE A 155 ? 0.37860 0.31683 0.28753 -0.01322 -0.03749 0.02084  358 PHE A CD1 
1225 C CD2 . PHE A 155 ? 0.40990 0.35382 0.32697 -0.01048 -0.04808 0.01444  358 PHE A CD2 
1226 C CE1 . PHE A 155 ? 0.34851 0.29574 0.27366 -0.01561 -0.03956 0.01229  358 PHE A CE1 
1227 C CE2 . PHE A 155 ? 0.37611 0.33081 0.31160 -0.01297 -0.05060 0.00462  358 PHE A CE2 
1228 C CZ  . PHE A 155 ? 0.33339 0.28886 0.27269 -0.01583 -0.04550 0.00338  358 PHE A CZ  
1229 N N   . THR A 156 ? 0.50971 0.39202 0.35118 -0.00717 -0.01802 0.03922  359 THR A N   
1230 C CA  . THR A 156 ? 0.54823 0.41505 0.37576 -0.00957 -0.00507 0.04266  359 THR A CA  
1231 C C   . THR A 156 ? 0.50599 0.39020 0.35506 -0.01676 0.00517  0.04269  359 THR A C   
1232 O O   . THR A 156 ? 0.58560 0.46120 0.43085 -0.02019 0.01746  0.04238  359 THR A O   
1233 C CB  . THR A 156 ? 0.56075 0.40566 0.36400 -0.00599 -0.00250 0.04337  359 THR A CB  
1234 O OG1 . THR A 156 ? 0.59189 0.45120 0.40890 -0.00831 -0.00298 0.04244  359 THR A OG1 
1235 C CG2 . THR A 156 ? 0.63771 0.46401 0.41785 0.00425  -0.01522 0.04113  359 THR A CG2 
1236 N N   . ASP A 157 ? 0.49875 0.40499 0.36930 -0.01843 0.00092  0.04150  360 ASP A N   
1237 C CA  . ASP A 157 ? 0.51542 0.43638 0.40384 -0.02190 0.00760  0.03963  360 ASP A CA  
1238 C C   . ASP A 157 ? 0.46590 0.39180 0.36340 -0.02387 0.01178  0.03834  360 ASP A C   
1239 O O   . ASP A 157 ? 0.43568 0.36288 0.33315 -0.02277 0.00587  0.03981  360 ASP A O   
1240 C CB  . ASP A 157 ? 0.48971 0.42654 0.39172 -0.02113 0.00165  0.03904  360 ASP A CB  
1241 C CG  . ASP A 157 ? 0.59160 0.52534 0.48869 -0.02023 0.00133  0.03898  360 ASP A CG  
1242 O OD1 . ASP A 157 ? 0.72738 0.64955 0.61315 -0.02038 0.00554  0.03904  360 ASP A OD1 
1243 O OD2 . ASP A 157 ? 0.57920 0.51979 0.48188 -0.01941 -0.00214 0.03885  360 ASP A OD2 
1244 N N   . PRO A 158 ? 0.49328 0.42246 0.40046 -0.02683 0.02212  0.03394  361 PRO A N   
1245 C CA  . PRO A 158 ? 0.42304 0.35398 0.33819 -0.02928 0.02828  0.03147  361 PRO A CA  
1246 C C   . PRO A 158 ? 0.38809 0.33934 0.32183 -0.02764 0.02051  0.03063  361 PRO A C   
1247 O O   . PRO A 158 ? 0.38844 0.34060 0.32637 -0.02892 0.02238  0.03025  361 PRO A O   
1248 C CB  . PRO A 158 ? 0.47542 0.40790 0.40220 -0.03325 0.04209  0.02319  361 PRO A CB  
1249 C CG  . PRO A 158 ? 0.44767 0.38783 0.37942 -0.03133 0.03896  0.02067  361 PRO A CG  
1250 C CD  . PRO A 158 ? 0.48702 0.41788 0.39959 -0.02828 0.02934  0.02901  361 PRO A CD  
1251 N N   . PHE A 159 ? 0.36856 0.33306 0.31079 -0.02464 0.01278  0.03041  362 PHE A N   
1252 C CA  . PHE A 159 ? 0.31646 0.29587 0.27139 -0.02234 0.00617  0.02992  362 PHE A CA  
1253 C C   . PHE A 159 ? 0.32091 0.29797 0.26902 -0.02246 -0.00145 0.03504  362 PHE A C   
1254 O O   . PHE A 159 ? 0.30282 0.28993 0.25964 -0.02152 -0.00577 0.03490  362 PHE A O   
1255 C CB  . PHE A 159 ? 0.29323 0.28156 0.25440 -0.01775 0.00251  0.02680  362 PHE A CB  
1256 C CG  . PHE A 159 ? 0.36639 0.34606 0.31448 -0.01703 -0.00009 0.03043  362 PHE A CG  
1257 C CD1 . PHE A 159 ? 0.35511 0.33210 0.29679 -0.01701 -0.00512 0.03464  362 PHE A CD1 
1258 C CD2 . PHE A 159 ? 0.41217 0.38631 0.35605 -0.01720 0.00386  0.02836  362 PHE A CD2 
1259 C CE1 . PHE A 159 ? 0.44758 0.41660 0.37945 -0.01705 -0.00598 0.03654  362 PHE A CE1 
1260 C CE2 . PHE A 159 ? 0.42766 0.39429 0.36038 -0.01651 0.00146  0.03145  362 PHE A CE2 
1261 C CZ  . PHE A 159 ? 0.42224 0.38631 0.34924 -0.01643 -0.00332 0.03548  362 PHE A CZ  
1262 N N   . VAL A 160 ? 0.33803 0.30210 0.27152 -0.02296 -0.00360 0.03785  363 VAL A N   
1263 C CA  . VAL A 160 ? 0.31604 0.28025 0.24772 -0.02249 -0.01176 0.03864  363 VAL A CA  
1264 C C   . VAL A 160 ? 0.31540 0.27527 0.24422 -0.02229 -0.01337 0.03873  363 VAL A C   
1265 O O   . VAL A 160 ? 0.33252 0.27554 0.24445 -0.02034 -0.01366 0.03946  363 VAL A O   
1266 C CB  . VAL A 160 ? 0.35234 0.30686 0.27286 -0.02118 -0.01564 0.03835  363 VAL A CB  
1267 C CG1 . VAL A 160 ? 0.33864 0.29779 0.26500 -0.02106 -0.02361 0.03485  363 VAL A CG1 
1268 C CG2 . VAL A 160 ? 0.33003 0.28644 0.25149 -0.02151 -0.01243 0.03870  363 VAL A CG2 
1269 N N   . PHE A 161 ? 0.28311 0.25574 0.22581 -0.02335 -0.01434 0.03794  364 PHE A N   
1270 C CA  . PHE A 161 ? 0.28739 0.25745 0.22900 -0.02307 -0.01689 0.03776  364 PHE A CA  
1271 C C   . PHE A 161 ? 0.25991 0.24665 0.21804 -0.02407 -0.02207 0.03611  364 PHE A C   
1272 O O   . PHE A 161 ? 0.27354 0.27195 0.24260 -0.02474 -0.02041 0.03577  364 PHE A O   
1273 C CB  . PHE A 161 ? 0.28897 0.25376 0.22980 -0.02455 -0.00729 0.03799  364 PHE A CB  
1274 C CG  . PHE A 161 ? 0.28227 0.26406 0.24306 -0.02605 -0.00155 0.03496  364 PHE A CG  
1275 C CD1 . PHE A 161 ? 0.26800 0.26575 0.24558 -0.02592 -0.00407 0.03309  364 PHE A CD1 
1276 C CD2 . PHE A 161 ? 0.29165 0.27334 0.25458 -0.02637 0.00526  0.03236  364 PHE A CD2 
1277 C CE1 . PHE A 161 ? 0.26757 0.28003 0.26249 -0.02465 -0.00095 0.02816  364 PHE A CE1 
1278 C CE2 . PHE A 161 ? 0.28404 0.28157 0.26608 -0.02523 0.00799  0.02638  364 PHE A CE2 
1279 C CZ  . PHE A 161 ? 0.27014 0.28278 0.26768 -0.02363 0.00429  0.02401  364 PHE A CZ  
1280 N N   . LYS A 162 ? 0.27053 0.25590 0.22793 -0.02320 -0.02860 0.03450  365 LYS A N   
1281 C CA  . LYS A 162 ? 0.28842 0.28879 0.26174 -0.02473 -0.03194 0.03267  365 LYS A CA  
1282 C C   . LYS A 162 ? 0.26651 0.27016 0.24502 -0.02520 -0.02680 0.03418  365 LYS A C   
1283 O O   . LYS A 162 ? 0.27581 0.26551 0.24253 -0.02455 -0.02234 0.03549  365 LYS A O   
1284 C CB  . LYS A 162 ? 0.28405 0.28310 0.25719 -0.02326 -0.04196 0.02794  365 LYS A CB  
1285 C CG  . LYS A 162 ? 0.31175 0.30916 0.28444 -0.02292 -0.04660 0.02284  365 LYS A CG  
1286 C CD  . LYS A 162 ? 0.30822 0.30564 0.28404 -0.01996 -0.05814 0.01383  365 LYS A CD  
1287 C CE  . LYS A 162 ? 0.45604 0.43366 0.40964 -0.01205 -0.06525 0.01329  365 LYS A CE  
1288 N NZ  . LYS A 162 ? 0.49361 0.47150 0.45090 -0.00649 -0.07954 0.00078  365 LYS A NZ  
1289 N N   . TRP A 163 ? 0.23075 0.25080 0.22582 -0.02616 -0.02612 0.03324  366 TRP A N   
1290 C CA  . TRP A 163 ? 0.22075 0.24757 0.22587 -0.02644 -0.02232 0.03241  366 TRP A CA  
1291 C C   . TRP A 163 ? 0.22613 0.25742 0.23596 -0.02689 -0.02924 0.03157  366 TRP A C   
1292 O O   . TRP A 163 ? 0.21648 0.26045 0.23734 -0.02750 -0.03379 0.03003  366 TRP A O   
1293 C CB  . TRP A 163 ? 0.23423 0.27618 0.25435 -0.02482 -0.01951 0.02996  366 TRP A CB  
1294 C CG  . TRP A 163 ? 0.17905 0.23007 0.21387 -0.02468 -0.01492 0.02616  366 TRP A CG  
1295 C CD1 . TRP A 163 ? 0.19583 0.24083 0.23020 -0.02727 -0.01108 0.02604  366 TRP A CD1 
1296 C CD2 . TRP A 163 ? 0.18605 0.25255 0.23802 -0.02097 -0.01382 0.02036  366 TRP A CD2 
1297 N NE1 . TRP A 163 ? 0.19572 0.25340 0.24921 -0.02709 -0.00603 0.02032  366 TRP A NE1 
1298 C CE2 . TRP A 163 ? 0.18191 0.25438 0.24787 -0.02263 -0.00863 0.01588  366 TRP A CE2 
1299 C CE3 . TRP A 163 ? 0.19109 0.26465 0.24599 -0.01512 -0.01709 0.01747  366 TRP A CE3 
1300 C CZ2 . TRP A 163 ? 0.19613 0.28559 0.28391 -0.01877 -0.00741 0.00695  366 TRP A CZ2 
1301 C CZ3 . TRP A 163 ? 0.22357 0.31147 0.29589 -0.00940 -0.01760 0.00906  366 TRP A CZ3 
1302 C CH2 . TRP A 163 ? 0.18776 0.28557 0.27881 -0.01133 -0.01316 0.00307  366 TRP A CH2 
1303 N N   A LYS A 164 ? 0.23617 0.25435 0.23534 -0.02626 -0.02940 0.03216  367 LYS A N   
1304 N N   B LYS A 164 ? 0.23608 0.25416 0.23514 -0.02625 -0.02940 0.03217  367 LYS A N   
1305 C CA  A LYS A 164 ? 0.23459 0.25429 0.23547 -0.02530 -0.03772 0.03040  367 LYS A CA  
1306 C CA  B LYS A 164 ? 0.23471 0.25439 0.23563 -0.02532 -0.03754 0.03044  367 LYS A CA  
1307 C C   A LYS A 164 ? 0.22189 0.25825 0.24184 -0.02706 -0.03571 0.02949  367 LYS A C   
1308 C C   B LYS A 164 ? 0.22119 0.25827 0.24179 -0.02712 -0.03555 0.02948  367 LYS A C   
1309 O O   A LYS A 164 ? 0.21668 0.25330 0.24130 -0.02811 -0.02673 0.02962  367 LYS A O   
1310 O O   B LYS A 164 ? 0.21639 0.25519 0.24289 -0.02816 -0.02659 0.02948  367 LYS A O   
1311 C CB  A LYS A 164 ? 0.28128 0.27564 0.25810 -0.02180 -0.03879 0.03136  367 LYS A CB  
1312 C CB  B LYS A 164 ? 0.28007 0.27453 0.25730 -0.02200 -0.03805 0.03152  367 LYS A CB  
1313 C CG  A LYS A 164 ? 0.36233 0.35478 0.33814 -0.01931 -0.04692 0.02912  367 LYS A CG  
1314 C CG  B LYS A 164 ? 0.36296 0.35548 0.33854 -0.01908 -0.04778 0.02886  367 LYS A CG  
1315 C CD  A LYS A 164 ? 0.38037 0.33968 0.32358 -0.01347 -0.04761 0.03039  367 LYS A CD  
1316 C CD  B LYS A 164 ? 0.38046 0.33998 0.32337 -0.01299 -0.04910 0.02994  367 LYS A CD  
1317 C CE  A LYS A 164 ? 0.36938 0.31084 0.30008 -0.01650 -0.03020 0.03488  367 LYS A CE  
1318 C CE  B LYS A 164 ? 0.40974 0.36453 0.34807 -0.00816 -0.06021 0.02645  367 LYS A CE  
1319 N N   . GLU A 165 ? 0.19091 0.24151 0.22360 -0.02759 -0.04344 0.02699  368 GLU A N   
1320 C CA  . GLU A 165 ? 0.19130 0.25672 0.24069 -0.02847 -0.04326 0.02585  368 GLU A CA  
1321 C C   . GLU A 165 ? 0.20434 0.25831 0.24600 -0.02753 -0.04391 0.02605  368 GLU A C   
1322 O O   . GLU A 165 ? 0.22018 0.25956 0.24637 -0.02482 -0.05130 0.02517  368 GLU A O   
1323 C CB  . GLU A 165 ? 0.18163 0.26254 0.24444 -0.02977 -0.05032 0.02276  368 GLU A CB  
1324 C CG  . GLU A 165 ? 0.17755 0.27436 0.25739 -0.03015 -0.05087 0.02153  368 GLU A CG  
1325 C CD  . GLU A 165 ? 0.16683 0.27699 0.25799 -0.03188 -0.05433 0.01872  368 GLU A CD  
1326 O OE1 . GLU A 165 ? 0.22339 0.33607 0.31871 -0.03394 -0.06088 0.01453  368 GLU A OE1 
1327 O OE2 . GLU A 165 ? 0.18895 0.30480 0.28321 -0.03055 -0.05009 0.01959  368 GLU A OE2 
1328 N N   . THR A 166 ? 0.20283 0.26181 0.25445 -0.02880 -0.03627 0.02588  369 THR A N   
1329 C CA  . THR A 166 ? 0.21149 0.25841 0.25624 -0.02862 -0.03420 0.02601  369 THR A CA  
1330 C C   . THR A 166 ? 0.19288 0.26165 0.26294 -0.03026 -0.03308 0.02316  369 THR A C   
1331 O O   . THR A 166 ? 0.18457 0.27537 0.27428 -0.03031 -0.03450 0.02107  369 THR A O   
1332 C CB  . THR A 166 ? 0.26441 0.28710 0.29184 -0.02974 -0.02029 0.02751  369 THR A CB  
1333 O OG1 . THR A 166 ? 0.25552 0.29258 0.30455 -0.03314 -0.00840 0.02374  369 THR A OG1 
1334 C CG2 . THR A 166 ? 0.27564 0.27911 0.28002 -0.02792 -0.01999 0.03015  369 THR A CG2 
1335 N N   . ALA A 167 ? 0.23047 0.29027 0.29739 -0.03068 -0.03029 0.02283  370 ALA A N   
1336 C CA  . ALA A 167 ? 0.21418 0.29425 0.30623 -0.03228 -0.02804 0.01931  370 ALA A CA  
1337 C C   . ALA A 167 ? 0.23333 0.32854 0.34635 -0.03363 -0.01751 0.01457  370 ALA A C   
1338 O O   . ALA A 167 ? 0.21876 0.33761 0.35669 -0.03271 -0.01935 0.00997  370 ALA A O   
1339 C CB  . ALA A 167 ? 0.21098 0.27327 0.29300 -0.03303 -0.02306 0.01953  370 ALA A CB  
1340 N N   . ASP A 168 ? 0.21447 0.29682 0.31840 -0.03479 -0.00757 0.01409  371 ASP A N   
1341 C CA  . ASP A 168 ? 0.19270 0.28683 0.31730 -0.03573 0.00338  0.00616  371 ASP A CA  
1342 C C   . ASP A 168 ? 0.20147 0.30942 0.33277 -0.03174 -0.00186 0.00431  371 ASP A C   
1343 O O   . ASP A 168 ? 0.21852 0.33837 0.36852 -0.03024 0.00416  -0.00465 371 ASP A O   
1344 C CB  . ASP A 168 ? 0.22474 0.29354 0.33605 -0.04045 0.02077  0.00447  371 ASP A CB  
1345 C CG  . ASP A 168 ? 0.30060 0.34813 0.39905 -0.04377 0.02869  0.00624  371 ASP A CG  
1346 O OD1 . ASP A 168 ? 0.33000 0.39335 0.44876 -0.04420 0.02753  0.00238  371 ASP A OD1 
1347 O OD2 . ASP A 168 ? 0.47995 0.49337 0.54565 -0.04488 0.03526  0.01152  371 ASP A OD2 
1348 N N   . THR A 169 ? 0.19445 0.29973 0.31110 -0.02962 -0.01229 0.01084  372 THR A N   
1349 C CA  . THR A 169 ? 0.15411 0.26632 0.27174 -0.02576 -0.01528 0.00963  372 THR A CA  
1350 C C   . THR A 169 ? 0.15823 0.29099 0.29089 -0.02034 -0.02357 0.00651  372 THR A C   
1351 O O   . THR A 169 ? 0.17532 0.31708 0.31539 -0.02058 -0.02879 0.00723  372 THR A O   
1352 C CB  . THR A 169 ? 0.15920 0.25635 0.25364 -0.02645 -0.01989 0.01681  372 THR A CB  
1353 O OG1 . THR A 169 ? 0.14239 0.23941 0.23154 -0.02740 -0.02886 0.02057  372 THR A OG1 
1354 C CG2 . THR A 169 ? 0.19650 0.27081 0.27246 -0.02947 -0.01191 0.01918  372 THR A CG2 
1355 N N   . LYS A 170 ? 0.14267 0.28064 0.27736 -0.01440 -0.02505 0.00260  373 LYS A N   
1356 C CA  . LYS A 170 ? 0.10794 0.26116 0.25344 -0.00643 -0.03211 -0.00225 373 LYS A CA  
1357 C C   . LYS A 170 ? 0.12950 0.27513 0.25653 -0.00146 -0.03786 0.00195  373 LYS A C   
1358 O O   . LYS A 170 ? 0.15260 0.30432 0.28090 0.00721  -0.04339 -0.00184 373 LYS A O   
1359 C CB  . LYS A 170 ? 0.14633 0.31317 0.31366 -0.00005 -0.02965 -0.01541 373 LYS A CB  
1360 C CG  . LYS A 170 ? 0.17482 0.35034 0.36399 -0.00521 -0.02200 -0.02162 373 LYS A CG  
1361 C CD  . LYS A 170 ? 0.25887 0.43836 0.46166 -0.00018 -0.01646 -0.03496 373 LYS A CD  
1362 C CE  . LYS A 170 ? 0.46004 0.63871 0.67302 -0.00420 -0.00792 -0.03995 373 LYS A CE  
1363 N NZ  . LYS A 170 ? 0.56115 0.74176 0.79045 -0.00274 0.00027  -0.05589 373 LYS A NZ  
1364 N N   . PHE A 171 ? 0.14579 0.27591 0.25397 -0.00604 -0.03613 0.00894  374 PHE A N   
1365 C CA  . PHE A 171 ? 0.15607 0.27628 0.24629 -0.00371 -0.03893 0.01307  374 PHE A CA  
1366 C C   . PHE A 171 ? 0.14305 0.26427 0.23232 -0.00879 -0.04121 0.01669  374 PHE A C   
1367 O O   . PHE A 171 ? 0.13802 0.26746 0.23920 -0.01349 -0.04248 0.01661  374 PHE A O   
1368 C CB  . PHE A 171 ? 0.17342 0.27819 0.24728 -0.00692 -0.03551 0.01718  374 PHE A CB  
1369 C CG  . PHE A 171 ? 0.14474 0.24362 0.21615 -0.01560 -0.03369 0.02121  374 PHE A CG  
1370 C CD1 . PHE A 171 ? 0.15781 0.25314 0.22460 -0.02068 -0.03622 0.02387  374 PHE A CD1 
1371 C CD2 . PHE A 171 ? 0.16069 0.25535 0.23297 -0.01781 -0.02932 0.02069  374 PHE A CD2 
1372 C CE1 . PHE A 171 ? 0.18575 0.27455 0.24878 -0.02559 -0.03749 0.02518  374 PHE A CE1 
1373 C CE2 . PHE A 171 ? 0.17912 0.26314 0.24264 -0.02300 -0.02891 0.02414  374 PHE A CE2 
1374 C CZ  . PHE A 171 ? 0.20268 0.28431 0.26154 -0.02578 -0.03458 0.02603  374 PHE A CZ  
1375 N N   . TYR A 172 ? 0.15807 0.26902 0.23241 -0.00818 -0.04071 0.01896  375 TYR A N   
1376 C CA  . TYR A 172 ? 0.13669 0.24774 0.21160 -0.01424 -0.04067 0.01997  375 TYR A CA  
1377 C C   . TYR A 172 ? 0.16426 0.26030 0.22554 -0.02029 -0.03602 0.02174  375 TYR A C   
1378 O O   . TYR A 172 ? 0.19739 0.27932 0.24202 -0.01695 -0.03220 0.02332  375 TYR A O   
1379 C CB  . TYR A 172 ? 0.14051 0.25238 0.21193 -0.00807 -0.04150 0.01834  375 TYR A CB  
1380 C CG  . TYR A 172 ? 0.15316 0.28160 0.24070 -0.00073 -0.04685 0.01431  375 TYR A CG  
1381 C CD1 . TYR A 172 ? 0.14277 0.28739 0.25002 -0.00485 -0.04973 0.01279  375 TYR A CD1 
1382 C CD2 . TYR A 172 ? 0.13778 0.26639 0.22306 0.01051  -0.04929 0.01013  375 TYR A CD2 
1383 C CE1 . TYR A 172 ? 0.11352 0.26788 0.23531 0.00156  -0.05210 0.00657  375 TYR A CE1 
1384 C CE2 . TYR A 172 ? 0.15434 0.30046 0.25954 0.01719  -0.05381 0.00301  375 TYR A CE2 
1385 C CZ  . TYR A 172 ? 0.13296 0.29196 0.25694 0.01158  -0.05443 0.00230  375 TYR A CZ  
1386 O OH  . TYR A 172 ? 0.18910 0.34829 0.32416 0.01453  -0.05286 -0.00143 375 TYR A OH  
1387 N N   . ASN A 173 ? 0.14054 0.23988 0.21018 -0.02857 -0.03679 0.01980  376 ASN A N   
1388 C CA  . ASN A 173 ? 0.16032 0.24865 0.22349 -0.03508 -0.03227 0.01771  376 ASN A CA  
1389 C C   . ASN A 173 ? 0.18042 0.27623 0.25751 -0.04234 -0.03289 0.01126  376 ASN A C   
1390 O O   . ASN A 173 ? 0.19639 0.29899 0.28505 -0.04595 -0.03875 0.00655  376 ASN A O   
1391 C CB  . ASN A 173 ? 0.17445 0.25880 0.23535 -0.03622 -0.03460 0.01829  376 ASN A CB  
1392 C CG  . ASN A 173 ? 0.19343 0.27062 0.25383 -0.04265 -0.03177 0.01301  376 ASN A CG  
1393 O OD1 . ASN A 173 ? 0.22145 0.28959 0.27584 -0.04589 -0.02347 0.01105  376 ASN A OD1 
1394 N ND2 . ASN A 173 ? 0.19969 0.27887 0.26541 -0.04391 -0.03826 0.00936  376 ASN A ND2 
1395 N N   . VAL A 174 ? 0.16227 0.25490 0.23671 -0.04369 -0.02687 0.00977  377 VAL A N   
1396 C CA  . VAL A 174 ? 0.17737 0.27630 0.26632 -0.05191 -0.02497 0.00158  377 VAL A CA  
1397 C C   . VAL A 174 ? 0.19683 0.28644 0.28682 -0.06004 -0.01770 -0.00604 377 VAL A C   
1398 O O   . VAL A 174 ? 0.23675 0.30822 0.30935 -0.06050 -0.00775 -0.00383 377 VAL A O   
1399 C CB  . VAL A 174 ? 0.16925 0.26471 0.25275 -0.05108 -0.01880 0.00206  377 VAL A CB  
1400 C CG1 . VAL A 174 ? 0.15006 0.25984 0.23943 -0.04279 -0.02797 0.00659  377 VAL A CG1 
1401 C CG2 . VAL A 174 ? 0.18853 0.25807 0.24362 -0.04813 -0.00667 0.00592  377 VAL A CG2 
1402 N N   . ARG A 175 ? 0.17173 0.27342 0.28272 -0.06565 -0.02331 -0.01663 378 ARG A N   
1403 C CA  . ARG A 175 ? 0.18403 0.28098 0.30206 -0.07228 -0.01879 -0.02743 378 ARG A CA  
1404 C C   . ARG A 175 ? 0.19587 0.29476 0.33025 -0.08273 -0.00872 -0.04138 378 ARG A C   
1405 O O   . ARG A 175 ? 0.23216 0.34168 0.37819 -0.08464 -0.01054 -0.04461 378 ARG A O   
1406 C CB  . ARG A 175 ? 0.23612 0.34293 0.36518 -0.06889 -0.03369 -0.03293 378 ARG A CB  
1407 C CG  . ARG A 175 ? 0.19916 0.29765 0.30965 -0.06108 -0.03843 -0.02142 378 ARG A CG  
1408 C CD  . ARG A 175 ? 0.21714 0.32035 0.33155 -0.05562 -0.05356 -0.02520 378 ARG A CD  
1409 N NE  . ARG A 175 ? 0.19599 0.30926 0.31686 -0.05255 -0.06234 -0.02389 378 ARG A NE  
1410 C CZ  . ARG A 175 ? 0.21894 0.33206 0.33700 -0.04685 -0.07224 -0.02806 378 ARG A CZ  
1411 N NH1 . ARG A 175 ? 0.20745 0.31377 0.32260 -0.04327 -0.07976 -0.03552 378 ARG A NH1 
1412 N NH2 . ARG A 175 ? 0.20298 0.31964 0.31657 -0.04325 -0.07274 -0.02462 378 ARG A NH2 
1413 N N   . LYS A 176 ? 0.22332 0.31146 0.35966 -0.09026 0.00349  -0.05074 379 LYS A N   
1414 C CA  . LYS A 176 ? 0.24262 0.32982 0.39480 -0.10049 0.01618  -0.06591 379 LYS A CA  
1415 C C   . LYS A 176 ? 0.26034 0.36014 0.42738 -0.09234 0.00190  -0.07418 379 LYS A C   
1416 O O   . LYS A 176 ? 0.26001 0.36378 0.43226 -0.08736 -0.00815 -0.07931 379 LYS A O   
1417 C CB  . LYS A 176 ? 0.27907 0.34834 0.42765 -0.10947 0.03481  -0.07399 379 LYS A CB  
1418 C CG  . LYS A 176 ? 0.26678 0.30678 0.37873 -0.10808 0.05007  -0.05912 379 LYS A CG  
1419 C CD  . LYS A 176 ? 0.33463 0.35546 0.44442 -0.11759 0.06936  -0.06890 379 LYS A CD  
1420 C CE  . LYS A 176 ? 0.40522 0.38962 0.47329 -0.11577 0.08713  -0.05572 379 LYS A CE  
1421 N NZ  . LYS A 176 ? 0.35822 0.32253 0.42338 -0.12500 0.10621  -0.06481 379 LYS A NZ  
1422 N N   . LEU A 177 ? 0.21896 0.32280 0.39023 -0.09107 0.00196  -0.07581 380 LEU A N   
1423 C CA  . LEU A 177 ? 0.24069 0.35272 0.42315 -0.08474 -0.00769 -0.08484 380 LEU A CA  
1424 C C   . LEU A 177 ? 0.29438 0.40504 0.49093 -0.08773 0.00049  -0.10283 380 LEU A C   
1425 O O   . LEU A 177 ? 0.28504 0.40254 0.49077 -0.08062 -0.01026 -0.11157 380 LEU A O   
1426 C CB  . LEU A 177 ? 0.26615 0.38112 0.45070 -0.08456 -0.00574 -0.08455 380 LEU A CB  
1427 C CG  . LEU A 177 ? 0.29040 0.41041 0.46513 -0.07769 -0.01867 -0.06948 380 LEU A CG  
1428 C CD1 . LEU A 177 ? 0.25182 0.36943 0.41661 -0.08017 -0.01451 -0.05721 380 LEU A CD1 
1429 C CD2 . LEU A 177 ? 0.26222 0.38579 0.44145 -0.07603 -0.01930 -0.07245 380 LEU A CD2 
1430 N N   . ASP A 178 ? 0.29595 0.39599 0.49321 -0.09788 0.02101  -0.10930 381 ASP A N   
1431 C CA  . ASP A 178 ? 0.33469 0.43341 0.54696 -0.10124 0.03209  -0.12765 381 ASP A CA  
1432 C C   . ASP A 178 ? 0.36553 0.46643 0.58088 -0.09743 0.02358  -0.13029 381 ASP A C   
1433 O O   . ASP A 178 ? 0.34447 0.45035 0.57707 -0.09608 0.02631  -0.14708 381 ASP A O   
1434 C CB  . ASP A 178 ? 0.33894 0.41951 0.54465 -0.11356 0.05950  -0.13215 381 ASP A CB  
1435 C CG  . ASP A 178 ? 0.50511 0.58480 0.71725 -0.11729 0.07194  -0.14146 381 ASP A CG  
1436 O OD1 . ASP A 178 ? 0.59561 0.69148 0.82494 -0.11075 0.06110  -0.15023 381 ASP A OD1 
1437 O OD2 . ASP A 178 ? 0.52187 0.58183 0.71923 -0.12644 0.09345  -0.14016 381 ASP A OD2 
1438 N N   . LYS A 179 ? 0.28716 0.38520 0.48770 -0.09544 0.01409  -0.11551 382 LYS A N   
1439 C CA  . LYS A 179 ? 0.27089 0.37069 0.47241 -0.09089 0.00406  -0.11738 382 LYS A CA  
1440 C C   . LYS A 179 ? 0.33980 0.44973 0.54165 -0.07803 -0.01908 -0.11622 382 LYS A C   
1441 O O   . LYS A 179 ? 0.33353 0.44652 0.54272 -0.07175 -0.02727 -0.12639 382 LYS A O   
1442 C CB  . LYS A 179 ? 0.35082 0.44039 0.53537 -0.09576 0.00787  -0.10365 382 LYS A CB  
1443 C CG  . LYS A 179 ? 0.33512 0.40660 0.51302 -0.10756 0.03222  -0.10568 382 LYS A CG  
1444 C CD  . LYS A 179 ? 0.39237 0.46314 0.58393 -0.10852 0.03800  -0.12156 382 LYS A CD  
1445 C CE  . LYS A 179 ? 0.55432 0.60270 0.73137 -0.11831 0.05923  -0.11871 382 LYS A CE  
1446 N NZ  . LYS A 179 ? 0.64108 0.66932 0.80416 -0.12703 0.08316  -0.11688 382 LYS A NZ  
1447 N N   . LEU A 180 ? 0.27659 0.38940 0.46858 -0.07357 -0.02865 -0.10422 383 LEU A N   
1448 C CA  . LEU A 180 ? 0.27605 0.39269 0.46295 -0.06191 -0.04714 -0.10253 383 LEU A CA  
1449 C C   . LEU A 180 ? 0.36944 0.49182 0.57156 -0.05615 -0.05029 -0.11872 383 LEU A C   
1450 O O   . LEU A 180 ? 0.34141 0.46449 0.54413 -0.04590 -0.06317 -0.12565 383 LEU A O   
1451 C CB  . LEU A 180 ? 0.29923 0.41615 0.47174 -0.05965 -0.05298 -0.08602 383 LEU A CB  
1452 C CG  . LEU A 180 ? 0.30744 0.42162 0.46689 -0.06186 -0.05299 -0.07106 383 LEU A CG  
1453 C CD1 . LEU A 180 ? 0.21914 0.33580 0.36842 -0.05882 -0.05725 -0.05747 383 LEU A CD1 
1454 C CD2 . LEU A 180 ? 0.29987 0.41044 0.45227 -0.05629 -0.06282 -0.07150 383 LEU A CD2 
1455 N N   . TYR A 181 ? 0.16622 0.53809 0.34687 -0.08303 -0.04429 -0.00613 384 TYR A N   
1456 C CA  . TYR A 181 ? 0.19485 0.61354 0.39111 -0.07426 -0.04298 -0.01069 384 TYR A CA  
1457 C C   . TYR A 181 ? 0.27988 0.72134 0.47847 -0.08088 -0.04988 -0.01376 384 TYR A C   
1458 O O   . TYR A 181 ? 0.26848 0.70099 0.45622 -0.10403 -0.05074 -0.01419 384 TYR A O   
1459 C CB  . TYR A 181 ? 0.21182 0.64806 0.40962 -0.08704 -0.03311 -0.01299 384 TYR A CB  
1460 C CG  . TYR A 181 ? 0.22949 0.71735 0.44245 -0.07965 -0.03036 -0.01840 384 TYR A CG  
1461 C CD1 . TYR A 181 ? 0.21260 0.72037 0.43686 -0.05136 -0.03058 -0.01979 384 TYR A CD1 
1462 C CD2 . TYR A 181 ? 0.20924 0.72510 0.42230 -0.10082 -0.02697 -0.02241 384 TYR A CD2 
1463 C CE1 . TYR A 181 ? 0.20865 0.76436 0.44467 -0.04257 -0.02819 -0.02521 384 TYR A CE1 
1464 C CE2 . TYR A 181 ? 0.24606 0.81313 0.47322 -0.09426 -0.02430 -0.02802 384 TYR A CE2 
1465 C CZ  . TYR A 181 ? 0.21238 0.80001 0.45142 -0.06427 -0.02514 -0.02948 384 TYR A CZ  
1466 O OH  . TYR A 181 ? 0.29397 0.93371 0.54524 -0.05590 -0.02277 -0.03555 384 TYR A OH  
1467 N N   . VAL A 182 ? 0.22212 0.69173 0.43222 -0.05988 -0.05476 -0.01605 385 VAL A N   
1468 C CA  . VAL A 182 ? 0.20239 0.70286 0.41743 -0.06317 -0.06128 -0.02002 385 VAL A CA  
1469 C C   . VAL A 182 ? 0.21247 0.76529 0.44213 -0.05425 -0.05730 -0.02558 385 VAL A C   
1470 O O   . VAL A 182 ? 0.20907 0.77380 0.44486 -0.02744 -0.05694 -0.02612 385 VAL A O   
1471 C CB  . VAL A 182 ? 0.22144 0.71054 0.43416 -0.04484 -0.07177 -0.01831 385 VAL A CB  
1472 C CG1 . VAL A 182 ? 0.24426 0.77116 0.46341 -0.04632 -0.07844 -0.02318 385 VAL A CG1 
1473 C CG2 . VAL A 182 ? 0.29569 0.73595 0.49296 -0.05496 -0.07588 -0.01352 385 VAL A CG2 
1474 N N   . GLN A 183 ? 0.22861 0.81192 0.46119 -0.07629 -0.05413 -0.03002 386 GLN A N   
1475 C CA  . GLN A 183 ? 0.24077 0.87896 0.48718 -0.07017 -0.05000 -0.03622 386 GLN A CA  
1476 C C   . GLN A 183 ? 0.24697 0.91652 0.50259 -0.04382 -0.05796 -0.03946 386 GLN A C   
1477 O O   . GLN A 183 ? 0.25197 0.91918 0.50529 -0.04488 -0.06688 -0.03956 386 GLN A O   
1478 C CB  . GLN A 183 ? 0.26118 0.92656 0.50671 -0.10165 -0.04614 -0.04074 386 GLN A CB  
1479 C CG  . GLN A 183 ? 0.26255 0.89457 0.49347 -0.12742 -0.03779 -0.03767 386 GLN A CG  
1480 C CD  . GLN A 183 ? 0.28898 0.94624 0.51459 -0.15866 -0.03280 -0.04232 386 GLN A CD  
1481 O OE1 . GLN A 183 ? 0.30558 0.96958 0.52578 -0.17534 -0.03768 -0.04449 386 GLN A OE1 
1482 N NE2 . GLN A 183 ? 0.29573 0.96655 0.52116 -0.16762 -0.02284 -0.04410 386 GLN A NE2 
1483 N N   . GLY A 184 ? 0.24960 0.94607 0.51292 -0.01889 -0.05488 -0.04217 387 GLY A N   
1484 C CA  . GLY A 184 ? 0.26129 0.98620 0.52899 0.00978  -0.06167 -0.04559 387 GLY A CA  
1485 C C   . GLY A 184 ? 0.25389 0.93860 0.51059 0.03762  -0.06725 -0.04049 387 GLY A C   
1486 O O   . GLY A 184 ? 0.32730 1.02866 0.58211 0.06587  -0.07196 -0.04292 387 GLY A O   
1487 N N   . GLN A 185 ? 0.23585 0.86778 0.48275 0.03102  -0.06676 -0.03379 388 GLN A N   
1488 C CA  . GLN A 185 ? 0.23349 0.82577 0.46773 0.05494  -0.07150 -0.02895 388 GLN A CA  
1489 C C   . GLN A 185 ? 0.32532 0.88135 0.55216 0.06352  -0.06447 -0.02463 388 GLN A C   
1490 O O   . GLN A 185 ? 0.44294 0.97227 0.65732 0.08849  -0.06631 -0.02190 388 GLN A O   
1491 C CB  . GLN A 185 ? 0.28973 0.85141 0.51653 0.04260  -0.07983 -0.02509 388 GLN A CB  
1492 C CG  . GLN A 185 ? 0.45198 1.04478 0.68246 0.04270  -0.08882 -0.02917 388 GLN A CG  
1493 C CD  . GLN A 185 ? 0.49128 1.05963 0.71542 0.02268  -0.09616 -0.02656 388 GLN A CD  
1494 O OE1 . GLN A 185 ? 0.50597 1.09995 0.73534 0.00458  -0.09995 -0.03046 388 GLN A OE1 
1495 N NE2 . GLN A 185 ? 0.48392 1.00286 0.69516 0.02580  -0.09818 -0.02036 388 GLN A NE2 
1496 N N   . PHE A 186 ? 0.26281 0.81586 0.49438 0.04409  -0.05638 -0.02414 389 PHE A N   
1497 C CA  . PHE A 186 ? 0.25453 0.77654 0.47998 0.05117  -0.04960 -0.02069 389 PHE A CA  
1498 C C   . PHE A 186 ? 0.27099 0.81796 0.49934 0.06984  -0.04274 -0.02444 389 PHE A C   
1499 O O   . PHE A 186 ? 0.30127 0.89336 0.53859 0.07157  -0.04211 -0.02991 389 PHE A O   
1500 C CB  . PHE A 186 ? 0.23809 0.74023 0.46385 0.02156  -0.04462 -0.01814 389 PHE A CB  
1501 C CG  . PHE A 186 ? 0.24452 0.70408 0.46059 0.01210  -0.04983 -0.01297 389 PHE A CG  
1502 C CD1 . PHE A 186 ? 0.29597 0.75190 0.50878 0.01044  -0.05916 -0.01238 389 PHE A CD1 
1503 C CD2 . PHE A 186 ? 0.23506 0.65991 0.44461 0.00527  -0.04554 -0.00909 389 PHE A CD2 
1504 C CE1 . PHE A 186 ? 0.27125 0.68873 0.47370 0.00266  -0.06392 -0.00792 389 PHE A CE1 
1505 C CE2 . PHE A 186 ? 0.24040 0.62932 0.44042 -0.00248 -0.05031 -0.00488 389 PHE A CE2 
1506 C CZ  . PHE A 186 ? 0.22999 0.61485 0.42609 -0.00366 -0.05943 -0.00427 389 PHE A CZ  
1507 N N   . PRO A 187 ? 0.30031 0.81940 0.51982 0.08499  -0.03760 -0.02205 390 PRO A N   
1508 C CA  . PRO A 187 ? 0.31864 0.85751 0.53812 0.10235  -0.03054 -0.02567 390 PRO A CA  
1509 C C   . PRO A 187 ? 0.32095 0.89328 0.55415 0.07975  -0.02328 -0.02899 390 PRO A C   
1510 O O   . PRO A 187 ? 0.28227 0.84263 0.51872 0.05205  -0.02060 -0.02678 390 PRO A O   
1511 C CB  . PRO A 187 ? 0.38104 0.87460 0.58650 0.11530  -0.02602 -0.02180 390 PRO A CB  
1512 C CG  . PRO A 187 ? 0.39959 0.85415 0.59552 0.11471  -0.03263 -0.01680 390 PRO A CG  
1513 C CD  . PRO A 187 ? 0.30671 0.77543 0.51420 0.08803  -0.03809 -0.01639 390 PRO A CD  
1514 N N   . SER A 188 ? 0.37643 0.98957 0.61474 0.09235  -0.02006 -0.03445 391 SER A N   
1515 C CA  . SER A 188 ? 0.27452 0.92286 0.52448 0.07177  -0.01277 -0.03814 391 SER A CA  
1516 C C   . SER A 188 ? 0.31880 0.94246 0.56529 0.06273  -0.00333 -0.03564 391 SER A C   
1517 O O   . SER A 188 ? 0.29963 0.93794 0.55185 0.03824  0.00278  -0.03690 391 SER A O   
1518 C CB  . SER A 188 ? 0.32559 1.02593 0.58143 0.09013  -0.01164 -0.04500 391 SER A CB  
1519 O OG  . SER A 188 ? 0.45849 1.14564 0.70209 0.12442  -0.01040 -0.04518 391 SER A OG  
1520 N N   . ASN A 189 ? 0.36539 0.95076 0.60033 0.08150  -0.00177 -0.03237 392 ASN A N   
1521 C CA  . ASN A 189 ? 0.35139 0.91107 0.58192 0.07406  0.00676  -0.03015 392 ASN A CA  
1522 C C   . ASN A 189 ? 0.29038 0.80752 0.51608 0.05627  0.00480  -0.02458 392 ASN A C   
1523 O O   . ASN A 189 ? 0.31744 0.80620 0.53640 0.05615  0.01021  -0.02239 392 ASN A O   
1524 C CB  . ASN A 189 ? 0.40236 0.94622 0.62059 0.10531  0.01080  -0.03091 392 ASN A CB  
1525 C CG  . ASN A 189 ? 0.45446 0.96167 0.65740 0.12833  0.00422  -0.02800 392 ASN A CG  
1526 O OD1 . ASN A 189 ? 0.44654 0.94145 0.65034 0.12081  -0.00333 -0.02515 392 ASN A OD1 
1527 N ND2 . ASN A 189 ? 0.45838 0.94403 0.64362 0.15628  0.00739  -0.02869 392 ASN A ND2 
1528 N N   . TYR A 190 ? 0.28122 0.79442 0.50922 0.04177  -0.00288 -0.02268 393 TYR A N   
1529 C CA  . TYR A 190 ? 0.27863 0.75154 0.50020 0.02820  -0.00623 -0.01754 393 TYR A CA  
1530 C C   . TYR A 190 ? 0.28261 0.73668 0.50042 0.00782  0.00107  -0.01568 393 TYR A C   
1531 O O   . TYR A 190 ? 0.25816 0.67803 0.46869 0.00777  0.00133  -0.01224 393 TYR A O   
1532 C CB  . TYR A 190 ? 0.22528 0.70203 0.44892 0.01140  -0.01425 -0.01678 393 TYR A CB  
1533 C CG  . TYR A 190 ? 0.22526 0.66200 0.44060 -0.00018 -0.01927 -0.01184 393 TYR A CG  
1534 C CD1 . TYR A 190 ? 0.25551 0.66358 0.46437 0.01726  -0.02281 -0.00869 393 TYR A CD1 
1535 C CD2 . TYR A 190 ? 0.20952 0.63618 0.42047 -0.02777 -0.02059 -0.01058 393 TYR A CD2 
1536 C CE1 . TYR A 190 ? 0.19856 0.57420 0.40015 0.00696  -0.02754 -0.00459 393 TYR A CE1 
1537 C CE2 . TYR A 190 ? 0.17838 0.56863 0.37948 -0.03646 -0.02553 -0.00648 393 TYR A CE2 
1538 C CZ  . TYR A 190 ? 0.17280 0.54029 0.37091 -0.01927 -0.02909 -0.00360 393 TYR A CZ  
1539 O OH  . TYR A 190 ? 0.19339 0.52787 0.38177 -0.02763 -0.03396 0.00017  393 TYR A OH  
1540 N N   . PHE A 191 ? 0.24385 0.71983 0.46481 -0.00959 0.00707  -0.01810 394 PHE A N   
1541 C CA  . PHE A 191 ? 0.22164 0.67676 0.43455 -0.03115 0.01339  -0.01609 394 PHE A CA  
1542 C C   . PHE A 191 ? 0.27685 0.73204 0.48832 -0.02130 0.02287  -0.01735 394 PHE A C   
1543 O O   . PHE A 191 ? 0.26796 0.70767 0.47131 -0.03816 0.02882  -0.01604 394 PHE A O   
1544 C CB  . PHE A 191 ? 0.29226 0.76364 0.50326 -0.05805 0.01537  -0.01767 394 PHE A CB  
1545 C CG  . PHE A 191 ? 0.26309 0.73069 0.47174 -0.07088 0.00698  -0.01677 394 PHE A CG  
1546 C CD1 . PHE A 191 ? 0.24449 0.67179 0.43881 -0.08659 0.00339  -0.01252 394 PHE A CD1 
1547 C CD2 . PHE A 191 ? 0.30945 0.81390 0.52852 -0.06641 0.00263  -0.02055 394 PHE A CD2 
1548 C CE1 . PHE A 191 ? 0.26116 0.68297 0.45094 -0.09760 -0.00403 -0.01196 394 PHE A CE1 
1549 C CE2 . PHE A 191 ? 0.23733 0.73848 0.45333 -0.07851 -0.00483 -0.02011 394 PHE A CE2 
1550 C CZ  . PHE A 191 ? 0.25174 0.71039 0.45274 -0.09415 -0.00798 -0.01574 394 PHE A CZ  
1551 N N   . VAL A 192 ? 0.26939 0.73782 0.48478 0.00622  0.02449  -0.01987 395 VAL A N   
1552 C CA  . VAL A 192 ? 0.31532 0.78549 0.52736 0.01656  0.03423  -0.02194 395 VAL A CA  
1553 C C   . VAL A 192 ? 0.27876 0.70923 0.48047 0.01928  0.03664  -0.01909 395 VAL A C   
1554 O O   . VAL A 192 ? 0.24716 0.65534 0.44527 0.03188  0.03115  -0.01714 395 VAL A O   
1555 C CB  . VAL A 192 ? 0.34052 0.83362 0.55464 0.04709  0.03510  -0.02597 395 VAL A CB  
1556 C CG1 . VAL A 192 ? 0.37512 0.86398 0.58199 0.05872  0.04545  -0.02817 395 VAL A CG1 
1557 C CG2 . VAL A 192 ? 0.30956 0.84873 0.53493 0.04360  0.03298  -0.02973 395 VAL A CG2 
1558 N N   . ILE A 193 ? 0.28240 0.70482 0.47798 0.00754  0.04516  -0.01924 396 ILE A N   
1559 C CA  . ILE A 193 ? 0.28497 0.67227 0.46867 0.00887  0.04856  -0.01773 396 ILE A CA  
1560 C C   . ILE A 193 ? 0.30893 0.69584 0.48430 0.02552  0.05821  -0.02138 396 ILE A C   
1561 O O   . ILE A 193 ? 0.36364 0.78014 0.54394 0.02165  0.06545  -0.02405 396 ILE A O   
1562 C CB  . ILE A 193 ? 0.27166 0.63386 0.44497 -0.02009 0.04859  -0.01430 396 ILE A CB  
1563 C CG1 . ILE A 193 ? 0.25778 0.61674 0.43516 -0.03600 0.03932  -0.01095 396 ILE A CG1 
1564 C CG2 . ILE A 193 ? 0.29222 0.60097 0.44345 -0.01745 0.04867  -0.01277 396 ILE A CG2 
1565 C CD1 . ILE A 193 ? 0.23509 0.56948 0.39784 -0.06258 0.03958  -0.00784 396 ILE A CD1 
1566 N N   . ASN A 194 ? 0.35584 0.69849 0.51239 0.04206  0.05726  -0.02128 397 ASN A N   
1567 C CA  . ASN A 194 ? 0.44121 0.77046 0.58278 0.05552  0.06593  -0.02465 397 ASN A CA  
1568 C C   . ASN A 194 ? 0.36977 0.66641 0.49685 0.03524  0.06847  -0.02309 397 ASN A C   
1569 O O   . ASN A 194 ? 0.44308 0.69632 0.55634 0.03002  0.06289  -0.02096 397 ASN A O   
1570 C CB  . ASN A 194 ? 0.43882 0.73255 0.56191 0.08156  0.06393  -0.02593 397 ASN A CB  
1571 C CG  . ASN A 194 ? 0.54729 0.82985 0.65270 0.09883  0.07317  -0.03031 397 ASN A CG  
1572 O OD1 . ASN A 194 ? 0.62797 0.86419 0.71050 0.09681  0.07459  -0.03080 397 ASN A OD1 
1573 N ND2 . ASN A 194 ? 0.63899 0.96650 0.75465 0.11565  0.07954  -0.03416 397 ASN A ND2 
1574 N N   . GLY A 195 ? 0.39884 0.71835 0.52831 0.02414  0.07695  -0.02450 398 GLY A N   
1575 C CA  . GLY A 195 ? 0.46483 0.75692 0.57910 0.00473  0.07908  -0.02279 398 GLY A CA  
1576 C C   . GLY A 195 ? 0.48869 0.73932 0.57987 0.01496  0.08120  -0.02493 398 GLY A C   
1577 O O   . GLY A 195 ? 0.53794 0.77409 0.62141 0.03565  0.08132  -0.02760 398 GLY A O   
1578 N N   . ILE A 196 ? 0.42087 0.64975 0.49728 -0.00045 0.08281  -0.02397 399 ILE A N   
1579 C CA  . ILE A 196 ? 0.52899 0.71683 0.58272 0.00481  0.08245  -0.02618 399 ILE A CA  
1580 C C   . ILE A 196 ? 0.63509 0.82637 0.67862 0.02133  0.09234  -0.03111 399 ILE A C   
1581 O O   . ILE A 196 ? 0.71960 0.87677 0.74375 0.03059  0.09186  -0.03414 399 ILE A O   
1582 C CB  . ILE A 196 ? 0.56556 0.73101 0.60481 -0.01402 0.08014  -0.02408 399 ILE A CB  
1583 C CG1 . ILE A 196 ? 0.55329 0.74126 0.59121 -0.02617 0.08930  -0.02330 399 ILE A CG1 
1584 C CG2 . ILE A 196 ? 0.56962 0.72319 0.61323 -0.02566 0.06941  -0.01989 399 ILE A CG2 
1585 C CD1 . ILE A 196 ? 0.64769 0.80710 0.66292 -0.04045 0.08822  -0.02163 399 ILE A CD1 
1586 N N   . ARG A 197 ? 0.50778 0.73995 0.56240 0.02449  0.10167  -0.03253 400 ARG A N   
1587 C CA  . ARG A 197 ? 0.57218 0.81458 0.61935 0.04511  0.11144  -0.03763 400 ARG A CA  
1588 C C   . ARG A 197 ? 0.57587 0.84828 0.63777 0.06812  0.11176  -0.03965 400 ARG A C   
1589 O O   . ARG A 197 ? 0.61520 0.91970 0.68054 0.08438  0.12089  -0.04366 400 ARG A O   
1590 C CB  . ARG A 197 ? 0.57079 0.84157 0.61820 0.03552  0.12309  -0.03889 400 ARG A CB  
1591 C CG  . ARG A 197 ? 0.63437 0.86960 0.65832 0.02001  0.12428  -0.03802 400 ARG A CG  
1592 N N   . ASN A 198 ? 0.58581 0.84961 0.65540 0.07105  0.10184  -0.03711 401 ASN A N   
1593 C CA  . ASN A 198 ? 0.63413 0.92329 0.71559 0.09340  0.09986  -0.03840 401 ASN A CA  
1594 C C   . ASN A 198 ? 0.56681 0.92463 0.67653 0.09217  0.10457  -0.03965 401 ASN A C   
1595 O O   . ASN A 198 ? 0.61203 0.99609 0.72949 0.11385  0.10367  -0.04195 401 ASN A O   
1596 C CB  . ASN A 198 ? 0.72384 0.98848 0.78167 0.12396  0.10399  -0.04289 401 ASN A CB  
1597 C CG  . ASN A 198 ? 0.85352 1.05091 0.88100 0.12192  0.10023  -0.04281 401 ASN A CG  
1598 O OD1 . ASN A 198 ? 0.71230 0.88350 0.73891 0.11120  0.09139  -0.03955 401 ASN A OD1 
1599 N ND2 . ASN A 198 ? 0.81814 0.98897 0.82001 0.13113  0.10727  -0.04699 401 ASN A ND2 
1600 N N   . GLU A 199 ? 0.46821 0.84881 0.58936 0.06492  0.10782  -0.03785 402 GLU A N   
1601 C CA  . GLU A 199 ? 0.48105 0.91066 0.62354 0.05455  0.10825  -0.03786 402 GLU A CA  
1602 C C   . GLU A 199 ? 0.47945 0.92034 0.63841 0.04613  0.09672  -0.03467 402 GLU A C   
1603 O O   . GLU A 199 ? 0.46434 0.88082 0.62137 0.03818  0.09091  -0.03150 402 GLU A O   
1604 C CB  . GLU A 199 ? 0.49127 0.92793 0.63128 0.02631  0.11557  -0.03665 402 GLU A CB  
1605 C CG  . GLU A 199 ? 0.48714 0.90773 0.62634 -0.00363 0.11074  -0.03170 402 GLU A CG  
1606 C CD  . GLU A 199 ? 0.52423 0.89334 0.64018 -0.00988 0.11026  -0.02955 402 GLU A CD  
1607 O OE1 . GLU A 199 ? 0.56516 0.90101 0.66775 0.00980  0.10779  -0.03099 402 GLU A OE1 
1608 O OE2 . GLU A 199 ? 0.48132 0.83242 0.58692 -0.03449 0.10964  -0.02598 402 GLU A OE2 
1609 N N   . GLN A 200 ? 0.43423 0.91322 0.60833 0.04813  0.09332  -0.03605 403 GLN A N   
1610 C CA  . GLN A 200 ? 0.54902 1.04043 0.73622 0.04335  0.08223  -0.03411 403 GLN A CA  
1611 C C   . GLN A 200 ? 0.49892 1.00267 0.69267 0.00938  0.08107  -0.03197 403 GLN A C   
1612 O O   . GLN A 200 ? 0.45501 0.98578 0.65202 -0.00269 0.08701  -0.03421 403 GLN A O   
1613 C CB  . GLN A 200 ? 0.48822 1.01251 0.68377 0.06670  0.07824  -0.03766 403 GLN A CB  
1614 C CG  . GLN A 200 ? 0.57441 1.07926 0.75564 0.10213  0.07925  -0.03976 403 GLN A CG  
1615 C CD  . GLN A 200 ? 0.58132 1.04074 0.75030 0.11167  0.07403  -0.03679 403 GLN A CD  
1616 O OE1 . GLN A 200 ? 0.60995 1.03317 0.76212 0.11729  0.07944  -0.03689 403 GLN A OE1 
1617 N NE2 . GLN A 200 ? 0.53768 0.99842 0.71322 0.11341  0.06378  -0.03461 403 GLN A NE2 
1618 N N   . ILE A 201 ? 0.45910 0.94053 0.65187 -0.00557 0.07350  -0.02786 404 ILE A N   
1619 C CA  . ILE A 201 ? 0.39158 0.86902 0.58148 -0.03743 0.07191  -0.02528 404 ILE A CA  
1620 C C   . ILE A 201 ? 0.40280 0.88431 0.60034 -0.04188 0.06070  -0.02383 404 ILE A C   
1621 O O   . ILE A 201 ? 0.41593 0.87906 0.61455 -0.02919 0.05369  -0.02180 404 ILE A O   
1622 C CB  . ILE A 201 ? 0.36051 0.79554 0.53318 -0.05352 0.07427  -0.02125 404 ILE A CB  
1623 C CG1 . ILE A 201 ? 0.44263 0.87147 0.60483 -0.04892 0.08564  -0.02296 404 ILE A CG1 
1624 C CG2 . ILE A 201 ? 0.39780 0.82055 0.56030 -0.08397 0.07203  -0.01843 404 ILE A CG2 
1625 C CD1 . ILE A 201 ? 0.39811 0.78566 0.54105 -0.06170 0.08752  -0.01967 404 ILE A CD1 
1626 N N   . GLN A 202 ? 0.41715 0.92168 0.61808 -0.06055 0.05946  -0.02520 405 GLN A N   
1627 C CA  . GLN A 202 ? 0.43424 0.93857 0.63779 -0.07048 0.04974  -0.02395 405 GLN A CA  
1628 C C   . GLN A 202 ? 0.47484 0.93967 0.66046 -0.09665 0.04853  -0.01958 405 GLN A C   
1629 O O   . GLN A 202 ? 0.55710 1.02302 0.73219 -0.11973 0.05288  -0.02016 405 GLN A O   
1630 C CB  . GLN A 202 ? 0.44514 0.99586 0.65907 -0.07700 0.04930  -0.02872 405 GLN A CB  
1631 C CG  . GLN A 202 ? 0.52525 1.11647 0.75457 -0.04928 0.04870  -0.03333 405 GLN A CG  
1632 C CD  . GLN A 202 ? 0.57020 1.16538 0.80636 -0.03328 0.03787  -0.03310 405 GLN A CD  
1633 O OE1 . GLN A 202 ? 0.52459 1.09585 0.75627 -0.04466 0.03098  -0.02975 405 GLN A OE1 
1634 N NE2 . GLN A 202 ? 0.57819 1.20187 0.82259 -0.00578 0.03627  -0.03671 405 GLN A NE2 
1635 N N   . GLY A 203 ? 0.34658 0.77519 0.52599 -0.09275 0.04264  -0.01544 406 GLY A N   
1636 C CA  . GLY A 203 ? 0.31464 0.70234 0.47403 -0.11350 0.04040  -0.01124 406 GLY A CA  
1637 C C   . GLY A 203 ? 0.30513 0.68447 0.46256 -0.12114 0.03075  -0.00979 406 GLY A C   
1638 O O   . GLY A 203 ? 0.28530 0.66899 0.45430 -0.10546 0.02370  -0.00950 406 GLY A O   
1639 N N   . ARG A 204 ? 0.28687 0.65185 0.42656 -0.14515 0.03088  -0.00901 407 ARG A N   
1640 C CA  . ARG A 204 ? 0.31757 0.66918 0.44960 -0.15520 0.02271  -0.00773 407 ARG A CA  
1641 C C   . ARG A 204 ? 0.28351 0.58201 0.38819 -0.16670 0.02039  -0.00305 407 ARG A C   
1642 O O   . ARG A 204 ? 0.30884 0.58468 0.39745 -0.17272 0.02594  -0.00142 407 ARG A O   
1643 C CB  . ARG A 204 ? 0.33312 0.71223 0.46332 -0.17359 0.02437  -0.01153 407 ARG A CB  
1644 C CG  . ARG A 204 ? 0.35639 0.79167 0.51037 -0.16417 0.02831  -0.01699 407 ARG A CG  
1645 C CD  . ARG A 204 ? 0.40592 0.86494 0.58315 -0.13726 0.02199  -0.01811 407 ARG A CD  
1646 N NE  . ARG A 204 ? 0.35680 0.82601 0.53771 -0.14016 0.01354  -0.01908 407 ARG A NE  
1647 C CZ  . ARG A 204 ? 0.40697 0.92172 0.60120 -0.13951 0.01216  -0.02406 407 ARG A CZ  
1648 N NH1 . ARG A 204 ? 0.35014 0.90682 0.55610 -0.13510 0.01850  -0.02877 407 ARG A NH1 
1649 N NH2 . ARG A 204 ? 0.42969 0.94936 0.62498 -0.14314 0.00415  -0.02467 407 ARG A NH2 
1650 N N   . ASP A 205 ? 0.30147 0.57916 0.39913 -0.16824 0.01189  -0.00096 408 ASP A N   
1651 C CA  . ASP A 205 ? 0.23325 0.46081 0.30631 -0.17237 0.00827  0.00345  408 ASP A CA  
1652 C C   . ASP A 205 ? 0.25185 0.45498 0.30387 -0.18603 0.00222  0.00470  408 ASP A C   
1653 O O   . ASP A 205 ? 0.32239 0.48824 0.35818 -0.18363 -0.00351 0.00804  408 ASP A O   
1654 C CB  . ASP A 205 ? 0.26758 0.48590 0.35307 -0.15198 0.00361  0.00548  408 ASP A CB  
1655 C CG  . ASP A 205 ? 0.23110 0.47148 0.33845 -0.13766 -0.00318 0.00433  408 ASP A CG  
1656 O OD1 . ASP A 205 ? 0.25109 0.50972 0.36211 -0.14393 -0.00579 0.00237  408 ASP A OD1 
1657 O OD2 . ASP A 205 ? 0.23397 0.47275 0.35300 -0.12040 -0.00584 0.00526  408 ASP A OD2 
1658 N N   . ILE A 206 ? 0.29835 0.52114 0.34781 -0.20109 0.00366  0.00179  409 ILE A N   
1659 C CA  . ILE A 206 ? 0.35404 0.55703 0.38436 -0.21367 -0.00214 0.00239  409 ILE A CA  
1660 C C   . ILE A 206 ? 0.36671 0.51260 0.35504 -0.22589 -0.00240 0.00602  409 ILE A C   
1661 O O   . ILE A 206 ? 0.42700 0.54264 0.39635 -0.22834 -0.00889 0.00803  409 ILE A O   
1662 C CB  . ILE A 206 ? 0.34469 0.58340 0.37957 -0.22973 0.00029  -0.00221 409 ILE A CB  
1663 C CG1 . ILE A 206 ? 0.42117 0.64541 0.44137 -0.23994 -0.00661 -0.00204 409 ILE A CG1 
1664 C CG2 . ILE A 206 ? 0.41426 0.64850 0.42775 -0.25051 0.00928  -0.00379 409 ILE A CG2 
1665 C CD1 . ILE A 206 ? 0.49547 0.72357 0.53456 -0.22086 -0.01555 -0.00086 409 ILE A CD1 
1666 N N   . SER A 207 ? 0.41512 0.54300 0.38537 -0.23243 0.00433  0.00684  410 SER A N   
1667 C CA  . SER A 207 ? 0.45702 0.52760 0.38201 -0.24235 0.00398  0.01001  410 SER A CA  
1668 C C   . SER A 207 ? 0.45440 0.49633 0.37283 -0.22776 0.00310  0.01351  410 SER A C   
1669 O O   . SER A 207 ? 0.47986 0.47871 0.36137 -0.23363 0.00491  0.01559  410 SER A O   
1670 C CB  . SER A 207 ? 0.63989 0.70365 0.53819 -0.26474 0.01195  0.00787  410 SER A CB  
1671 O OG  . SER A 207 ? 0.71409 0.80252 0.62829 -0.26245 0.01992  0.00634  410 SER A OG  
1672 N N   . GLN A 208 ? 0.35160 0.41515 0.30260 -0.20860 0.00001  0.01391  411 GLN A N   
1673 C CA  . GLN A 208 ? 0.36241 0.40864 0.31226 -0.19616 0.00010  0.01626  411 GLN A CA  
1674 C C   . GLN A 208 ? 0.37586 0.39130 0.31695 -0.18441 -0.00916 0.01914  411 GLN A C   
1675 O O   . GLN A 208 ? 0.34565 0.36464 0.30152 -0.17089 -0.01101 0.01983  411 GLN A O   
1676 C CB  . GLN A 208 ? 0.37673 0.46712 0.36563 -0.18334 0.00431  0.01408  411 GLN A CB  
1677 C CG  . GLN A 208 ? 0.37542 0.48408 0.36520 -0.19119 0.01453  0.01204  411 GLN A CG  
1678 C CD  . GLN A 208 ? 0.41231 0.54881 0.42903 -0.17648 0.01910  0.01068  411 GLN A CD  
1679 O OE1 . GLN A 208 ? 0.34640 0.49647 0.38596 -0.16028 0.01485  0.01044  411 GLN A OE1 
1680 N NE2 . GLN A 208 ? 0.42239 0.56560 0.43365 -0.18233 0.02821  0.00952  411 GLN A NE2 
1681 N N   . SER A 209 ? 0.40815 0.39193 0.32297 -0.18943 -0.01506 0.02053  412 SER A N   
1682 C CA  . SER A 209 ? 0.39732 0.35377 0.30455 -0.17624 -0.02393 0.02279  412 SER A CA  
1683 C C   . SER A 209 ? 0.40702 0.33011 0.29253 -0.16440 -0.02443 0.02459  412 SER A C   
1684 O O   . SER A 209 ? 0.39977 0.32532 0.29823 -0.14165 -0.02888 0.02399  412 SER A O   
1685 C CB  . SER A 209 ? 0.44449 0.36916 0.32270 -0.18140 -0.02981 0.02371  412 SER A CB  
1686 O OG  . SER A 209 ? 0.54973 0.42682 0.37928 -0.19034 -0.02829 0.02518  412 SER A OG  
1687 N N   . TRP A 210 ? 0.47018 0.36564 0.32323 -0.17587 -0.01927 0.02595  413 TRP A N   
1688 C CA  . TRP A 210 ? 0.43849 0.30805 0.27193 -0.15915 -0.01963 0.02670  413 TRP A CA  
1689 C C   . TRP A 210 ? 0.39996 0.30854 0.27280 -0.14247 -0.01754 0.02413  413 TRP A C   
1690 O O   . TRP A 210 ? 0.40335 0.30301 0.27438 -0.12204 -0.02180 0.02328  413 TRP A O   
1691 C CB  . TRP A 210 ? 0.48646 0.32385 0.27980 -0.17655 -0.01287 0.02861  413 TRP A CB  
1692 C CG  . TRP A 210 ? 0.48745 0.36481 0.30457 -0.19343 -0.00247 0.02670  413 TRP A CG  
1693 C CD1 . TRP A 210 ? 0.51749 0.42388 0.34718 -0.20803 0.00176  0.02359  413 TRP A CD1 
1694 C CD2 . TRP A 210 ? 0.48280 0.38138 0.31572 -0.18886 0.00431  0.02576  413 TRP A CD2 
1695 N NE1 . TRP A 210 ? 0.45828 0.40170 0.31000 -0.21395 0.01083  0.02120  413 TRP A NE1 
1696 C CE2 . TRP A 210 ? 0.48764 0.42595 0.34143 -0.20393 0.01312  0.02283  413 TRP A CE2 
1697 C CE3 . TRP A 210 ? 0.46926 0.36201 0.30276 -0.16716 0.00271  0.02509  413 TRP A CE3 
1698 C CZ2 . TRP A 210 ? 0.50882 0.47432 0.37943 -0.20418 0.02190  0.02132  413 TRP A CZ2 
1699 C CZ3 . TRP A 210 ? 0.49088 0.40905 0.34049 -0.16756 0.01092  0.02329  413 TRP A CZ3 
1700 C CH2 . TRP A 210 ? 0.47616 0.42834 0.34280 -0.18733 0.02109  0.02210  413 TRP A CH2 
1701 N N   . ALA A 211 ? 0.38037 0.33255 0.28699 -0.15085 -0.01094 0.02231  414 ALA A N   
1702 C CA  . ALA A 211 ? 0.33757 0.32052 0.27507 -0.13617 -0.00794 0.01972  414 ALA A CA  
1703 C C   . ALA A 211 ? 0.27624 0.28001 0.24387 -0.11954 -0.01341 0.01812  414 ALA A C   
1704 O O   . ALA A 211 ? 0.28508 0.29639 0.26590 -0.10401 -0.01378 0.01610  414 ALA A O   
1705 C CB  . ALA A 211 ? 0.31893 0.33807 0.27623 -0.14873 0.00178  0.01812  414 ALA A CB  
1706 N N   . LYS A 212 ? 0.29938 0.31124 0.27584 -0.12387 -0.01739 0.01876  415 LYS A N   
1707 C CA  . LYS A 212 ? 0.27913 0.30273 0.27694 -0.10819 -0.02259 0.01780  415 LYS A CA  
1708 C C   . LYS A 212 ? 0.27488 0.26982 0.25547 -0.09417 -0.02859 0.01802  415 LYS A C   
1709 O O   . LYS A 212 ? 0.24299 0.24757 0.23929 -0.07975 -0.02997 0.01605  415 LYS A O   
1710 C CB  . LYS A 212 ? 0.27328 0.30864 0.27973 -0.11579 -0.02627 0.01849  415 LYS A CB  
1711 C CG  . LYS A 212 ? 0.26046 0.33171 0.28544 -0.12918 -0.02143 0.01724  415 LYS A CG  
1712 C CD  . LYS A 212 ? 0.23752 0.34335 0.29208 -0.11702 -0.01635 0.01482  415 LYS A CD  
1713 C CE  . LYS A 212 ? 0.22916 0.37602 0.30210 -0.12761 -0.01213 0.01282  415 LYS A CE  
1714 N NZ  . LYS A 212 ? 0.23389 0.41431 0.33159 -0.11454 -0.00663 0.01019  415 LYS A NZ  
1715 N N   . THR A 213 ? 0.31872 0.27821 0.26475 -0.09835 -0.03201 0.02001  416 THR A N   
1716 C CA  . THR A 213 ? 0.31610 0.25039 0.24270 -0.08235 -0.03804 0.01967  416 THR A CA  
1717 C C   . THR A 213 ? 0.34815 0.28611 0.27604 -0.07130 -0.03644 0.01730  416 THR A C   
1718 O O   . THR A 213 ? 0.29507 0.24267 0.23431 -0.05634 -0.03958 0.01454  416 THR A O   
1719 C CB  . THR A 213 ? 0.37916 0.26943 0.26151 -0.08758 -0.04165 0.02230  416 THR A CB  
1720 O OG1 . THR A 213 ? 0.40917 0.29574 0.28950 -0.09907 -0.04373 0.02376  416 THR A OG1 
1721 C CG2 . THR A 213 ? 0.38848 0.25568 0.24953 -0.06641 -0.04836 0.02133  416 THR A CG2 
1722 N N   . ALA A 214 ? 0.33312 0.26583 0.24979 -0.07992 -0.03116 0.01785  417 ALA A N   
1723 C CA  . ALA A 214 ? 0.34347 0.28191 0.26249 -0.07025 -0.02965 0.01515  417 ALA A CA  
1724 C C   . ALA A 214 ? 0.26638 0.23968 0.22292 -0.06367 -0.02746 0.01164  417 ALA A C   
1725 O O   . ALA A 214 ? 0.27693 0.25551 0.23802 -0.05172 -0.03001 0.00817  417 ALA A O   
1726 C CB  . ALA A 214 ? 0.33270 0.26207 0.23526 -0.08223 -0.02286 0.01642  417 ALA A CB  
1727 N N   . SER A 215 ? 0.28289 0.27953 0.26390 -0.07131 -0.02286 0.01205  418 SER A N   
1728 C CA  . SER A 215 ? 0.23691 0.25899 0.24645 -0.06443 -0.02015 0.00903  418 SER A CA  
1729 C C   . SER A 215 ? 0.24401 0.26742 0.26186 -0.05385 -0.02545 0.00734  418 SER A C   
1730 O O   . SER A 215 ? 0.24482 0.27650 0.27215 -0.04696 -0.02470 0.00369  418 SER A O   
1731 C CB  . SER A 215 ? 0.25621 0.30175 0.28640 -0.07099 -0.01530 0.00985  418 SER A CB  
1732 O OG  . SER A 215 ? 0.26418 0.31710 0.29111 -0.08087 -0.00870 0.01024  418 SER A OG  
1733 N N   . ASN A 216 ? 0.23437 0.24936 0.24708 -0.05379 -0.03032 0.00955  419 ASN A N   
1734 C CA  . ASN A 216 ? 0.26192 0.27929 0.28118 -0.04415 -0.03439 0.00781  419 ASN A CA  
1735 C C   . ASN A 216 ? 0.21844 0.23116 0.22734 -0.03469 -0.03756 0.00430  419 ASN A C   
1736 O O   . ASN A 216 ? 0.20960 0.23603 0.23115 -0.02919 -0.03746 0.00042  419 ASN A O   
1737 C CB  . ASN A 216 ? 0.22165 0.22691 0.23155 -0.04470 -0.03933 0.01067  419 ASN A CB  
1738 C CG  . ASN A 216 ? 0.24008 0.25592 0.26331 -0.05272 -0.03779 0.01303  419 ASN A CG  
1739 O OD1 . ASN A 216 ? 0.21018 0.24514 0.25378 -0.05219 -0.03394 0.01211  419 ASN A OD1 
1740 N ND2 . ASN A 216 ? 0.24184 0.24395 0.25076 -0.05945 -0.04134 0.01574  419 ASN A ND2 
1741 N N   . MET A 217 ? 0.25557 0.24873 0.23901 -0.03295 -0.04056 0.00530  420 MET A N   
1742 C CA  . MET A 217 ? 0.24973 0.24034 0.22074 -0.02095 -0.04509 0.00159  420 MET A CA  
1743 C C   . MET A 217 ? 0.25786 0.26505 0.24082 -0.02124 -0.04178 -0.00272 420 MET A C   
1744 O O   . MET A 217 ? 0.24303 0.26464 0.23170 -0.01355 -0.04455 -0.00792 420 MET A O   
1745 C CB  . MET A 217 ? 0.31400 0.27348 0.24855 -0.01730 -0.04917 0.00416  420 MET A CB  
1746 C CG  . MET A 217 ? 0.32587 0.26293 0.24213 -0.01632 -0.05306 0.00773  420 MET A CG  
1747 S SD  . MET A 217 ? 0.40818 0.29633 0.27324 -0.01879 -0.05524 0.01208  420 MET A SD  
1748 C CE  . MET A 217 ? 0.42496 0.30567 0.26715 0.00636  -0.06302 0.00799  420 MET A CE  
1749 N N   . LEU A 218 ? 0.23985 0.24706 0.22641 -0.03067 -0.03563 -0.00121 421 LEU A N   
1750 C CA  . LEU A 218 ? 0.27023 0.28948 0.26541 -0.03137 -0.03180 -0.00530 421 LEU A CA  
1751 C C   . LEU A 218 ? 0.23265 0.27107 0.25187 -0.03192 -0.02901 -0.00893 421 LEU A C   
1752 O O   . LEU A 218 ? 0.20846 0.25614 0.23136 -0.03029 -0.02890 -0.01432 421 LEU A O   
1753 C CB  . LEU A 218 ? 0.23966 0.25440 0.23135 -0.04028 -0.02499 -0.00274 421 LEU A CB  
1754 C CG  . LEU A 218 ? 0.29501 0.28702 0.25702 -0.04184 -0.02612 -0.00017 421 LEU A CG  
1755 C CD1 . LEU A 218 ? 0.34414 0.33515 0.30471 -0.05443 -0.01798 0.00300  421 LEU A CD1 
1756 C CD2 . LEU A 218 ? 0.35891 0.34773 0.30767 -0.03341 -0.02931 -0.00445 421 LEU A CD2 
1757 N N   . HIS A 219 ? 0.19820 0.24068 0.23083 -0.03489 -0.02679 -0.00631 422 HIS A N   
1758 C CA  . HIS A 219 ? 0.20729 0.26068 0.25581 -0.03498 -0.02411 -0.00935 422 HIS A CA  
1759 C C   . HIS A 219 ? 0.20022 0.26152 0.24898 -0.03103 -0.02839 -0.01399 422 HIS A C   
1760 O O   . HIS A 219 ? 0.19922 0.26961 0.25366 -0.03357 -0.02622 -0.01937 422 HIS A O   
1761 C CB  . HIS A 219 ? 0.20576 0.25967 0.26426 -0.03635 -0.02252 -0.00537 422 HIS A CB  
1762 C CG  . HIS A 219 ? 0.20352 0.26066 0.26912 -0.03862 -0.01674 -0.00362 422 HIS A CG  
1763 N ND1 . HIS A 219 ? 0.22478 0.28347 0.29451 -0.03747 -0.01128 -0.00670 422 HIS A ND1 
1764 C CD2 . HIS A 219 ? 0.21133 0.27222 0.27959 -0.04136 -0.01556 0.00025  422 HIS A CD2 
1765 C CE1 . HIS A 219 ? 0.21690 0.28070 0.29161 -0.03630 -0.00717 -0.00463 422 HIS A CE1 
1766 N NE2 . HIS A 219 ? 0.20165 0.27054 0.27774 -0.03938 -0.00967 -0.00067 422 HIS A NE2 
1767 N N   . TRP A 220 ? 0.20383 0.26243 0.24490 -0.02515 -0.03425 -0.01251 423 TRP A N   
1768 C CA  . TRP A 220 ? 0.22039 0.29257 0.26199 -0.01905 -0.03852 -0.01758 423 TRP A CA  
1769 C C   . TRP A 220 ? 0.19595 0.27850 0.23254 -0.01645 -0.04089 -0.02361 423 TRP A C   
1770 O O   . TRP A 220 ? 0.21564 0.31860 0.26115 -0.01811 -0.04094 -0.03026 423 TRP A O   
1771 C CB  . TRP A 220 ? 0.21719 0.28069 0.24600 -0.00975 -0.04459 -0.01471 423 TRP A CB  
1772 C CG  . TRP A 220 ? 0.22344 0.30289 0.24863 0.00137  -0.05010 -0.02018 423 TRP A CG  
1773 C CD1 . TRP A 220 ? 0.21911 0.31761 0.25541 0.00353  -0.04995 -0.02364 423 TRP A CD1 
1774 C CD2 . TRP A 220 ? 0.21631 0.29593 0.22413 0.01350  -0.05667 -0.02305 423 TRP A CD2 
1775 N NE1 . TRP A 220 ? 0.21700 0.33269 0.24697 0.01636  -0.05588 -0.02907 423 TRP A NE1 
1776 C CE2 . TRP A 220 ? 0.24610 0.35015 0.25806 0.02393  -0.06070 -0.02886 423 TRP A CE2 
1777 C CE3 . TRP A 220 ? 0.27101 0.33263 0.25851 0.01709  -0.05932 -0.02145 423 TRP A CE3 
1778 C CZ2 . TRP A 220 ? 0.27774 0.39114 0.27496 0.04047  -0.06838 -0.03341 423 TRP A CZ2 
1779 C CZ3 . TRP A 220 ? 0.30400 0.36914 0.27359 0.03292  -0.06693 -0.02538 423 TRP A CZ3 
1780 C CH2 . TRP A 220 ? 0.31783 0.40989 0.29285 0.04567  -0.07190 -0.03146 423 TRP A CH2 
1781 N N   . TRP A 221 ? 0.22206 0.29122 0.24299 -0.01356 -0.04280 -0.02172 424 TRP A N   
1782 C CA  . TRP A 221 ? 0.21714 0.29405 0.22974 -0.00935 -0.04622 -0.02721 424 TRP A CA  
1783 C C   . TRP A 221 ? 0.19458 0.28266 0.21914 -0.01932 -0.04091 -0.03232 424 TRP A C   
1784 O O   . TRP A 221 ? 0.21963 0.32684 0.24703 -0.01924 -0.04367 -0.03985 424 TRP A O   
1785 C CB  . TRP A 221 ? 0.23124 0.28419 0.21991 -0.00533 -0.04807 -0.02278 424 TRP A CB  
1786 C CG  . TRP A 221 ? 0.25251 0.30637 0.22367 0.00376  -0.05390 -0.02701 424 TRP A CG  
1787 C CD1 . TRP A 221 ? 0.30858 0.35862 0.25952 0.01946  -0.06257 -0.02818 424 TRP A CD1 
1788 C CD2 . TRP A 221 ? 0.30200 0.35738 0.26990 -0.00036 -0.05184 -0.03030 424 TRP A CD2 
1789 N NE1 . TRP A 221 ? 0.32341 0.37411 0.25926 0.02583  -0.06667 -0.03208 424 TRP A NE1 
1790 C CE2 . TRP A 221 ? 0.31259 0.36669 0.25899 0.01284  -0.06013 -0.03349 424 TRP A CE2 
1791 C CE3 . TRP A 221 ? 0.25523 0.31196 0.23401 -0.01214 -0.04407 -0.03120 424 TRP A CE3 
1792 C CZ2 . TRP A 221 ? 0.32099 0.37564 0.25737 0.01296  -0.06106 -0.03742 424 TRP A CZ2 
1793 C CZ3 . TRP A 221 ? 0.29611 0.35224 0.26452 -0.01229 -0.04434 -0.03526 424 TRP A CZ3 
1794 C CH2 . TRP A 221 ? 0.29622 0.35178 0.24423 -0.00059 -0.05292 -0.03827 424 TRP A CH2 
1795 N N   . PHE A 222 ? 0.22408 0.30092 0.25392 -0.02759 -0.03347 -0.02891 425 PHE A N   
1796 C CA  . PHE A 222 ? 0.21414 0.29471 0.25035 -0.03587 -0.02781 -0.03359 425 PHE A CA  
1797 C C   . PHE A 222 ? 0.23177 0.32640 0.27943 -0.04182 -0.02662 -0.03878 425 PHE A C   
1798 O O   . PHE A 222 ? 0.22887 0.33180 0.27667 -0.04894 -0.02532 -0.04590 425 PHE A O   
1799 C CB  . PHE A 222 ? 0.19890 0.26527 0.23727 -0.03961 -0.02010 -0.02878 425 PHE A CB  
1800 C CG  . PHE A 222 ? 0.21367 0.27081 0.24083 -0.03891 -0.01784 -0.02730 425 PHE A CG  
1801 C CD1 . PHE A 222 ? 0.27278 0.32185 0.28880 -0.03572 -0.02040 -0.02242 425 PHE A CD1 
1802 C CD2 . PHE A 222 ? 0.28903 0.34230 0.31364 -0.04225 -0.01215 -0.03073 425 PHE A CD2 
1803 C CE1 . PHE A 222 ? 0.27544 0.31543 0.27917 -0.03701 -0.01694 -0.02104 425 PHE A CE1 
1804 C CE2 . PHE A 222 ? 0.30925 0.35506 0.32297 -0.04148 -0.00902 -0.02952 425 PHE A CE2 
1805 C CZ  . PHE A 222 ? 0.30058 0.34111 0.30476 -0.03949 -0.01109 -0.02466 425 PHE A CZ  
1806 N N   . GLU A 223 ? 0.20094 0.29751 0.25614 -0.04063 -0.02669 -0.03565 426 GLU A N   
1807 C CA  . GLU A 223 ? 0.22550 0.33443 0.28925 -0.04778 -0.02440 -0.04031 426 GLU A CA  
1808 C C   . GLU A 223 ? 0.20787 0.34459 0.27392 -0.04646 -0.03015 -0.04807 426 GLU A C   
1809 O O   . GLU A 223 ? 0.23215 0.38364 0.30201 -0.05736 -0.02781 -0.05571 426 GLU A O   
1810 C CB  . GLU A 223 ? 0.19651 0.29941 0.26574 -0.04587 -0.02292 -0.03468 426 GLU A CB  
1811 C CG  . GLU A 223 ? 0.25058 0.36208 0.32562 -0.05477 -0.01878 -0.03870 426 GLU A CG  
1812 C CD  . GLU A 223 ? 0.37427 0.47002 0.44445 -0.06629 -0.01080 -0.04084 426 GLU A CD  
1813 O OE1 . GLU A 223 ? 0.31628 0.39401 0.38075 -0.06417 -0.00828 -0.03788 426 GLU A OE1 
1814 O OE2 . GLU A 223 ? 0.36820 0.46825 0.43771 -0.07756 -0.00651 -0.04571 426 GLU A OE2 
1815 N N   . GLN A 224 ? 0.23085 0.37531 0.29245 -0.03311 -0.03779 -0.04682 427 GLN A N   
1816 C CA  . GLN A 224 ? 0.21051 0.38653 0.27455 -0.02770 -0.04411 -0.05475 427 GLN A CA  
1817 C C   . GLN A 224 ? 0.26046 0.44878 0.32094 -0.03161 -0.04646 -0.06216 427 GLN A C   
1818 O O   . GLN A 224 ? 0.26566 0.48608 0.33364 -0.03642 -0.04860 -0.07148 427 GLN A O   
1819 C CB  . GLN A 224 ? 0.29847 0.47408 0.35181 -0.00849 -0.05233 -0.05173 427 GLN A CB  
1820 C CG  . GLN A 224 ? 0.26886 0.43172 0.32219 -0.00349 -0.05137 -0.04509 427 GLN A CG  
1821 C CD  . GLN A 224 ? 0.36107 0.53717 0.43057 -0.01434 -0.04510 -0.04699 427 GLN A CD  
1822 O OE1 . GLN A 224 ? 0.37326 0.58100 0.45198 -0.01544 -0.04561 -0.05434 427 GLN A OE1 
1823 N NE2 . GLN A 224 ? 0.38723 0.54030 0.45904 -0.02241 -0.03899 -0.04063 427 GLN A NE2 
1824 N N   . ASN A 225 ? 0.23590 0.40111 0.28474 -0.03051 -0.04590 -0.05864 428 ASN A N   
1825 C CA  . ASN A 225 ? 0.25215 0.42438 0.29378 -0.03269 -0.04861 -0.06501 428 ASN A CA  
1826 C C   . ASN A 225 ? 0.25053 0.41191 0.29373 -0.04958 -0.04047 -0.06776 428 ASN A C   
1827 O O   . ASN A 225 ? 0.27522 0.43163 0.30871 -0.05173 -0.04113 -0.07111 428 ASN A O   
1828 C CB  . ASN A 225 ? 0.25132 0.40252 0.27400 -0.02032 -0.05275 -0.05984 428 ASN A CB  
1829 C CG  . ASN A 225 ? 0.34049 0.50177 0.35206 -0.00191 -0.06292 -0.06050 428 ASN A CG  
1830 O OD1 . ASN A 225 ? 0.36059 0.55493 0.37845 0.00301  -0.06902 -0.06851 428 ASN A OD1 
1831 N ND2 . ASN A 225 ? 0.30359 0.43616 0.29611 0.00851  -0.06468 -0.05250 428 ASN A ND2 
1832 N N   . LYS A 226 ? 0.25594 0.41013 0.30727 -0.06064 -0.03283 -0.06654 429 LYS A N   
1833 C CA  . LYS A 226 ? 0.25825 0.39047 0.30356 -0.07284 -0.02458 -0.06739 429 LYS A CA  
1834 C C   . LYS A 226 ? 0.27714 0.42095 0.31666 -0.08480 -0.02533 -0.07798 429 LYS A C   
1835 O O   . LYS A 226 ? 0.34204 0.46498 0.36946 -0.08934 -0.02131 -0.07898 429 LYS A O   
1836 C CB  . LYS A 226 ? 0.32359 0.44247 0.37304 -0.08098 -0.01682 -0.06455 429 LYS A CB  
1837 C CG  . LYS A 226 ? 0.37526 0.51432 0.43152 -0.09340 -0.01549 -0.07112 429 LYS A CG  
1838 C CD  . LYS A 226 ? 0.42000 0.53710 0.47520 -0.09807 -0.00773 -0.06586 429 LYS A CD  
1839 C CE  . LYS A 226 ? 0.57302 0.70862 0.63426 -0.10831 -0.00548 -0.06991 429 LYS A CE  
1840 N NZ  . LYS A 226 ? 0.63711 0.74747 0.69372 -0.11206 0.00167  -0.06452 429 LYS A NZ  
1841 N N   . ASP A 227 ? 0.27856 0.45745 0.32586 -0.08970 -0.03062 -0.08652 430 ASP A N   
1842 C CA  . ASP A 227 ? 0.33831 0.52538 0.37847 -0.09968 -0.03019 -0.09421 430 ASP A CA  
1843 C C   . ASP A 227 ? 0.32179 0.51399 0.35305 -0.09083 -0.03835 -0.09747 430 ASP A C   
1844 O O   . ASP A 227 ? 0.33471 0.51705 0.35419 -0.09979 -0.03682 -0.10249 430 ASP A O   
1845 C CB  . ASP A 227 ? 0.32954 0.54710 0.37854 -0.10259 -0.02993 -0.09785 430 ASP A CB  
1846 C CG  . ASP A 227 ? 0.50740 0.71575 0.55846 -0.11550 -0.02037 -0.09614 430 ASP A CG  
1847 O OD1 . ASP A 227 ? 0.45935 0.63438 0.50150 -0.12425 -0.01355 -0.09323 430 ASP A OD1 
1848 O OD2 . ASP A 227 ? 0.53751 0.77109 0.59678 -0.11617 -0.01943 -0.09807 430 ASP A OD2 
1849 N N   . TYR A 228 ? 0.31432 0.51813 0.34673 -0.07264 -0.04711 -0.09462 431 TYR A N   
1850 C CA  . TYR A 228 ? 0.29345 0.49183 0.31090 -0.06132 -0.05358 -0.09492 431 TYR A CA  
1851 C C   . TYR A 228 ? 0.31611 0.47398 0.32028 -0.06256 -0.04595 -0.08812 431 TYR A C   
1852 O O   . TYR A 228 ? 0.31511 0.46451 0.30537 -0.06409 -0.04674 -0.09165 431 TYR A O   
1853 C CB  . TYR A 228 ? 0.30152 0.50688 0.31498 -0.03918 -0.06237 -0.09015 431 TYR A CB  
1854 C CG  . TYR A 228 ? 0.34092 0.58201 0.36145 -0.03006 -0.06922 -0.09523 431 TYR A CG  
1855 C CD1 . TYR A 228 ? 0.38468 0.63668 0.41315 -0.01865 -0.07058 -0.09158 431 TYR A CD1 
1856 C CD2 . TYR A 228 ? 0.49817 0.75805 0.51650 -0.03157 -0.07212 -0.10216 431 TYR A CD2 
1857 C CE1 . TYR A 228 ? 0.46013 0.74172 0.49403 -0.00825 -0.07376 -0.09532 431 TYR A CE1 
1858 C CE2 . TYR A 228 ? 0.55438 0.84676 0.58016 -0.02184 -0.07588 -0.10592 431 TYR A CE2 
1859 C CZ  . TYR A 228 ? 0.55178 0.85524 0.58522 -0.00980 -0.07622 -0.10275 431 TYR A CZ  
1860 O OH  . TYR A 228 ? 0.63131 0.96864 0.67109 0.00115  -0.07885 -0.10768 431 TYR A OH  
1861 N N   . ILE A 229 ? 0.27879 0.41406 0.28704 -0.06132 -0.03863 -0.07889 432 ILE A N   
1862 C CA  . ILE A 229 ? 0.32861 0.43209 0.32708 -0.06072 -0.03091 -0.07256 432 ILE A CA  
1863 C C   . ILE A 229 ? 0.36551 0.45546 0.35706 -0.07409 -0.02386 -0.07817 432 ILE A C   
1864 O O   . ILE A 229 ? 0.35815 0.42876 0.33616 -0.07286 -0.01989 -0.07755 432 ILE A O   
1865 C CB  . ILE A 229 ? 0.30848 0.39871 0.31514 -0.05599 -0.02599 -0.06255 432 ILE A CB  
1866 C CG1 . ILE A 229 ? 0.27074 0.36428 0.27493 -0.04309 -0.03261 -0.05685 432 ILE A CG1 
1867 C CG2 . ILE A 229 ? 0.29584 0.36132 0.29641 -0.05651 -0.01694 -0.05768 432 ILE A CG2 
1868 C CD1 . ILE A 229 ? 0.26116 0.34910 0.27513 -0.04026 -0.03036 -0.04891 432 ILE A CD1 
1869 N N   A GLU A 230 ? 0.36167 0.45884 0.35902 -0.08745 -0.02154 -0.08387 433 GLU A N   
1870 N N   B GLU A 230 ? 0.36161 0.45896 0.35889 -0.08749 -0.02160 -0.08397 433 GLU A N   
1871 C CA  A GLU A 230 ? 0.36523 0.44424 0.34897 -0.10178 -0.01526 -0.09031 433 GLU A CA  
1872 C CA  B GLU A 230 ? 0.36550 0.44415 0.34909 -0.10168 -0.01519 -0.09024 433 GLU A CA  
1873 C C   A GLU A 230 ? 0.40947 0.49717 0.38110 -0.10593 -0.02065 -0.09910 433 GLU A C   
1874 C C   B GLU A 230 ? 0.40934 0.49717 0.38095 -0.10642 -0.02059 -0.09932 433 GLU A C   
1875 O O   A GLU A 230 ? 0.40242 0.46545 0.35619 -0.10944 -0.01593 -0.10128 433 GLU A O   
1876 O O   B GLU A 230 ? 0.40325 0.46658 0.35689 -0.11086 -0.01581 -0.10192 433 GLU A O   
1877 C CB  A GLU A 230 ? 0.39164 0.47533 0.37953 -0.11837 -0.01170 -0.09531 433 GLU A CB  
1878 C CB  B GLU A 230 ? 0.39265 0.47418 0.38013 -0.11795 -0.01119 -0.09477 433 GLU A CB  
1879 C CG  A GLU A 230 ? 0.40312 0.46283 0.37039 -0.13611 -0.00524 -0.10294 433 GLU A CG  
1880 C CG  B GLU A 230 ? 0.40643 0.46927 0.39898 -0.11395 -0.00441 -0.08611 433 GLU A CG  
1881 C CD  A GLU A 230 ? 0.48065 0.49727 0.42968 -0.12885 0.00317  -0.09750 433 GLU A CD  
1882 C CD  B GLU A 230 ? 0.45768 0.48434 0.43699 -0.10570 0.00313  -0.07996 433 GLU A CD  
1883 O OE1 A GLU A 230 ? 0.53928 0.54425 0.49467 -0.11593 0.00686  -0.08801 433 GLU A OE1 
1884 O OE1 B GLU A 230 ? 0.54507 0.55053 0.50511 -0.11091 0.00707  -0.08463 433 GLU A OE1 
1885 O OE2 A GLU A 230 ? 0.58306 0.57931 0.51087 -0.13528 0.00583  -0.10324 433 GLU A OE2 
1886 O OE2 B GLU A 230 ? 0.44989 0.47121 0.43750 -0.09350 0.00491  -0.07102 433 GLU A OE2 
1887 N N   . GLN A 231 ? 0.37582 0.49892 0.35544 -0.10373 -0.03096 -0.10451 434 GLN A N   
1888 C CA  . GLN A 231 ? 0.36617 0.50105 0.33403 -0.10524 -0.03796 -0.11300 434 GLN A CA  
1889 C C   . GLN A 231 ? 0.37178 0.48411 0.32465 -0.09046 -0.03804 -0.10682 434 GLN A C   
1890 O O   . GLN A 231 ? 0.37717 0.47717 0.31259 -0.09413 -0.03773 -0.11168 434 GLN A O   
1891 C CB  . GLN A 231 ? 0.41416 0.59104 0.39481 -0.09827 -0.04836 -0.11637 434 GLN A CB  
1892 C CG  . GLN A 231 ? 0.40405 0.60076 0.39838 -0.11039 -0.04454 -0.11885 434 GLN A CG  
1893 C CD  . GLN A 231 ? 0.59851 0.78257 0.58072 -0.12941 -0.03894 -0.12499 434 GLN A CD  
1894 O OE1 . GLN A 231 ? 0.62939 0.81903 0.60200 -0.13008 -0.04386 -0.13038 434 GLN A OE1 
1895 N NE2 . GLN A 231 ? 0.63517 0.79824 0.61419 -0.14442 -0.02873 -0.12395 434 GLN A NE2 
1896 N N   . TYR A 232 ? 0.33629 0.44195 0.29369 -0.07518 -0.03792 -0.09636 435 TYR A N   
1897 C CA  . TYR A 232 ? 0.36025 0.44330 0.30247 -0.06402 -0.03584 -0.08979 435 TYR A CA  
1898 C C   . TYR A 232 ? 0.38306 0.43639 0.31502 -0.06977 -0.02449 -0.08842 435 TYR A C   
1899 O O   . TYR A 232 ? 0.37462 0.41420 0.28864 -0.06805 -0.02308 -0.09029 435 TYR A O   
1900 C CB  . TYR A 232 ? 0.36462 0.44372 0.31292 -0.05165 -0.03596 -0.07906 435 TYR A CB  
1901 C CG  . TYR A 232 ? 0.33124 0.39120 0.26146 -0.04187 -0.03500 -0.07293 435 TYR A CG  
1902 C CD1 . TYR A 232 ? 0.37105 0.43539 0.28520 -0.03164 -0.04447 -0.07437 435 TYR A CD1 
1903 C CD2 . TYR A 232 ? 0.35186 0.39001 0.27906 -0.04266 -0.02434 -0.06608 435 TYR A CD2 
1904 C CE1 . TYR A 232 ? 0.40849 0.45033 0.30092 -0.02448 -0.04255 -0.06855 435 TYR A CE1 
1905 C CE2 . TYR A 232 ? 0.39502 0.41738 0.30487 -0.03672 -0.02199 -0.06086 435 TYR A CE2 
1906 C CZ  . TYR A 232 ? 0.42801 0.44949 0.31910 -0.02873 -0.03068 -0.06182 435 TYR A CZ  
1907 O OH  . TYR A 232 ? 0.47407 0.47506 0.34324 -0.02456 -0.02727 -0.05634 435 TYR A OH  
1908 N N   . LYS A 233 ? 0.38822 0.43044 0.32907 -0.07477 -0.01632 -0.08528 436 LYS A N   
1909 C CA  . LYS A 233 ? 0.40894 0.42268 0.33785 -0.07668 -0.00569 -0.08442 436 LYS A CA  
1910 C C   . LYS A 233 ? 0.41102 0.41380 0.32076 -0.08764 -0.00522 -0.09471 436 LYS A C   
1911 O O   . LYS A 233 ? 0.45626 0.43489 0.34824 -0.08520 0.00149  -0.09515 436 LYS A O   
1912 C CB  . LYS A 233 ? 0.44679 0.45075 0.38548 -0.07867 0.00124  -0.08033 436 LYS A CB  
1913 C CG  . LYS A 233 ? 0.45266 0.46293 0.40739 -0.06800 0.00225  -0.07000 436 LYS A CG  
1914 C CD  . LYS A 233 ? 0.51696 0.52671 0.48420 -0.07072 0.00479  -0.06723 436 LYS A CD  
1915 C CE  . LYS A 233 ? 0.55604 0.53882 0.51148 -0.07131 0.01421  -0.06763 436 LYS A CE  
1916 N NZ  . LYS A 233 ? 0.75277 0.73302 0.71853 -0.07010 0.01653  -0.06291 436 LYS A NZ  
1917 N N   . GLN A 234 ? 0.40431 0.42584 0.31639 -0.10024 -0.01207 -0.10367 437 GLN A N   
1918 C CA  . GLN A 234 ? 0.46193 0.47323 0.35415 -0.11422 -0.01196 -0.11448 437 GLN A CA  
1919 C C   . GLN A 234 ? 0.47050 0.49041 0.35042 -0.10965 -0.01938 -0.11907 437 GLN A C   
1920 O O   . GLN A 234 ? 0.47700 0.47664 0.33442 -0.11583 -0.01682 -0.12523 437 GLN A O   
1921 C CB  . GLN A 234 ? 0.48655 0.51754 0.38544 -0.13360 -0.01548 -0.12358 437 GLN A CB  
1922 C CG  . GLN A 234 ? 0.60695 0.61756 0.50653 -0.14258 -0.00631 -0.12111 437 GLN A CG  
1923 C CD  . GLN A 234 ? 0.70050 0.73499 0.61211 -0.15758 -0.00816 -0.12470 437 GLN A CD  
1924 O OE1 . GLN A 234 ? 0.75128 0.81834 0.67179 -0.16018 -0.01545 -0.12863 437 GLN A OE1 
1925 N NE2 . GLN A 234 ? 0.67510 0.69348 0.58731 -0.16388 -0.00054 -0.12105 437 GLN A NE2 
1926 N N   . LYS A 235 ? 0.43864 0.48473 0.32893 -0.09813 -0.02867 -0.11636 438 LYS A N   
1927 C CA  . LYS A 235 ? 0.41237 0.47088 0.28956 -0.09390 -0.03825 -0.12222 438 LYS A CA  
1928 C C   . LYS A 235 ? 0.42195 0.46544 0.28707 -0.07647 -0.03766 -0.11384 438 LYS A C   
1929 O O   . LYS A 235 ? 0.45170 0.49043 0.29689 -0.07348 -0.04182 -0.11807 438 LYS A O   
1930 C CB  . LYS A 235 ? 0.43470 0.53721 0.32656 -0.09352 -0.05147 -0.12834 438 LYS A CB  
1931 C CG  . LYS A 235 ? 0.53570 0.65604 0.43980 -0.11125 -0.05121 -0.13513 438 LYS A CG  
1932 C CD  . LYS A 235 ? 0.56370 0.72661 0.49094 -0.10498 -0.05956 -0.13469 438 LYS A CD  
1933 C CE  . LYS A 235 ? 0.62638 0.81091 0.56133 -0.12015 -0.05974 -0.14134 438 LYS A CE  
1934 N NZ  . LYS A 235 ? 0.70594 0.86900 0.63888 -0.14064 -0.04805 -0.14213 438 LYS A NZ  
1935 N N   . ALA A 236 ? 0.39715 0.43202 0.27146 -0.06672 -0.03223 -0.10257 439 ALA A N   
1936 C CA  . ALA A 236 ? 0.37013 0.39034 0.23119 -0.05375 -0.03046 -0.09459 439 ALA A CA  
1937 C C   . ALA A 236 ? 0.43891 0.43113 0.28455 -0.05475 -0.01856 -0.09284 439 ALA A C   
1938 O O   . ALA A 236 ? 0.44086 0.42125 0.28867 -0.06171 -0.01032 -0.09486 439 ALA A O   
1939 C CB  . ALA A 236 ? 0.36019 0.38201 0.23513 -0.04604 -0.02865 -0.08394 439 ALA A CB  
1940 N N   . ALA A 237 ? 0.38612 0.36604 0.21277 -0.04666 -0.01740 -0.08919 440 ALA A N   
1941 C CA  . ALA A 237 ? 0.40279 0.35979 0.21483 -0.04553 -0.00510 -0.08689 440 ALA A CA  
1942 C C   . ALA A 237 ? 0.45196 0.40685 0.27619 -0.04108 0.00407  -0.07606 440 ALA A C   
1943 O O   . ALA A 237 ? 0.49043 0.44182 0.30628 -0.03622 0.00461  -0.06957 440 ALA A O   
1944 C CB  . ALA A 237 ? 0.45663 0.40221 0.24000 -0.04105 -0.00772 -0.08927 440 ALA A CB  
1945 N N   . ILE A 238 ? 0.40773 0.36435 0.25011 -0.04349 0.01101  -0.07430 441 ILE A N   
1946 C CA  . ILE A 238 ? 0.37346 0.33586 0.23231 -0.04042 0.01718  -0.06506 441 ILE A CA  
1947 C C   . ILE A 238 ? 0.39773 0.35184 0.24766 -0.03666 0.02986  -0.06128 441 ILE A C   
1948 O O   . ILE A 238 ? 0.42590 0.36942 0.26590 -0.03481 0.03708  -0.06561 441 ILE A O   
1949 C CB  . ILE A 238 ? 0.39862 0.36781 0.27937 -0.04285 0.01855  -0.06480 441 ILE A CB  
1950 C CG1 . ILE A 238 ? 0.50618 0.48868 0.39712 -0.04736 0.00681  -0.06799 441 ILE A CG1 
1951 C CG2 . ILE A 238 ? 0.39444 0.37120 0.29161 -0.03934 0.02517  -0.05607 441 ILE A CG2 
1952 C CD1 . ILE A 238 ? 0.49507 0.48461 0.40674 -0.05019 0.00763  -0.06630 441 ILE A CD1 
1953 N N   . GLU A 239 ? 0.39934 0.35787 0.25050 -0.03606 0.03304  -0.05364 442 GLU A N   
1954 C CA  . GLU A 239 ? 0.41284 0.37074 0.25846 -0.03461 0.04616  -0.05026 442 GLU A CA  
1955 C C   . GLU A 239 ? 0.42205 0.38978 0.28621 -0.03064 0.05481  -0.05039 442 GLU A C   
1956 O O   . GLU A 239 ? 0.43110 0.40889 0.31600 -0.03091 0.05172  -0.04828 442 GLU A O   
1957 C CB  . GLU A 239 ? 0.45853 0.41996 0.30207 -0.03889 0.04807  -0.04230 442 GLU A CB  
1958 C CG  . GLU A 239 ? 0.50304 0.46365 0.33344 -0.04079 0.06113  -0.03980 442 GLU A CG  
1959 C CD  . GLU A 239 ? 0.52388 0.47945 0.34190 -0.04894 0.06244  -0.03268 442 GLU A CD  
1960 O OE1 . GLU A 239 ? 0.53293 0.47950 0.34629 -0.05023 0.05176  -0.03006 442 GLU A OE1 
1961 O OE2 . GLU A 239 ? 0.57540 0.53518 0.38610 -0.05425 0.07476  -0.03001 442 GLU A OE2 
1962 N N   . GLU A 240 ? 0.44428 0.40776 0.29832 -0.02508 0.06535  -0.05322 443 GLU A N   
1963 C CA  . GLU A 240 ? 0.45586 0.42330 0.32028 -0.01669 0.07248  -0.05503 443 GLU A CA  
1964 C C   . GLU A 240 ? 0.47859 0.46976 0.36983 -0.01555 0.07467  -0.04898 443 GLU A C   
1965 O O   . GLU A 240 ? 0.45474 0.44686 0.35875 -0.01160 0.07209  -0.04942 443 GLU A O   
1966 C CB  . GLU A 240 ? 0.45376 0.41709 0.30237 -0.00821 0.08475  -0.05799 443 GLU A CB  
1967 C CG  . GLU A 240 ? 0.53555 0.49669 0.38700 0.00502  0.09149  -0.06099 443 GLU A CG  
1968 C CD  . GLU A 240 ? 0.50950 0.47221 0.34690 0.01682  0.10477  -0.06356 443 GLU A CD  
1969 O OE1 . GLU A 240 ? 0.50956 0.44848 0.32005 0.01872  0.10675  -0.06908 443 GLU A OE1 
1970 O OE2 . GLU A 240 ? 0.64928 0.63992 0.50271 0.02444  0.11340  -0.06049 443 GLU A OE2 
1971 N N   . TRP A 241 ? 0.42434 0.43365 0.32212 -0.02029 0.07947  -0.04352 444 TRP A N   
1972 C CA  . TRP A 241 ? 0.43980 0.47508 0.36252 -0.02021 0.08210  -0.03880 444 TRP A CA  
1973 C C   . TRP A 241 ? 0.46477 0.49959 0.40198 -0.02525 0.07087  -0.03585 444 TRP A C   
1974 O O   . TRP A 241 ? 0.41136 0.46284 0.36861 -0.02225 0.07111  -0.03356 444 TRP A O   
1975 C CB  . TRP A 241 ? 0.42661 0.48176 0.35062 -0.02851 0.09047  -0.03443 444 TRP A CB  
1976 C CG  . TRP A 241 ? 0.43505 0.48118 0.35046 -0.04291 0.08454  -0.02946 444 TRP A CG  
1977 C CD1 . TRP A 241 ? 0.50131 0.52762 0.39026 -0.04925 0.08455  -0.02884 444 TRP A CD1 
1978 C CD2 . TRP A 241 ? 0.41227 0.46496 0.34071 -0.05109 0.07804  -0.02444 444 TRP A CD2 
1979 N NE1 . TRP A 241 ? 0.48922 0.50666 0.37166 -0.05967 0.07836  -0.02366 444 TRP A NE1 
1980 C CE2 . TRP A 241 ? 0.49847 0.53165 0.40495 -0.06143 0.07443  -0.02102 444 TRP A CE2 
1981 C CE3 . TRP A 241 ? 0.43466 0.50500 0.38796 -0.04977 0.07470  -0.02260 444 TRP A CE3 
1982 C CZ2 . TRP A 241 ? 0.47958 0.50828 0.38681 -0.07022 0.06792  -0.01601 444 TRP A CZ2 
1983 C CZ3 . TRP A 241 ? 0.45610 0.52485 0.41278 -0.05981 0.06806  -0.01774 444 TRP A CZ3 
1984 C CH2 . TRP A 241 ? 0.49758 0.54471 0.43068 -0.06981 0.06495  -0.01460 444 TRP A CH2 
1985 N N   . LYS A 242 ? 0.38839 0.40617 0.31553 -0.03114 0.06082  -0.03640 445 LYS A N   
1986 C CA  . LYS A 242 ? 0.38688 0.40626 0.32672 -0.03498 0.05078  -0.03381 445 LYS A CA  
1987 C C   . LYS A 242 ? 0.41007 0.42335 0.35722 -0.03083 0.04590  -0.03783 445 LYS A C   
1988 O O   . LYS A 242 ? 0.40008 0.41731 0.35958 -0.03330 0.03893  -0.03584 445 LYS A O   
1989 C CB  . LYS A 242 ? 0.38143 0.38861 0.30664 -0.04067 0.04173  -0.03286 445 LYS A CB  
1990 C CG  . LYS A 242 ? 0.40104 0.40497 0.31100 -0.04657 0.04600  -0.02834 445 LYS A CG  
1991 C CD  . LYS A 242 ? 0.40617 0.39340 0.29754 -0.04833 0.03573  -0.02714 445 LYS A CD  
1992 C CE  . LYS A 242 ? 0.46687 0.44197 0.33499 -0.05497 0.04058  -0.02230 445 LYS A CE  
1993 N NZ  . LYS A 242 ? 0.42475 0.37869 0.26947 -0.05300 0.02971  -0.02088 445 LYS A NZ  
1994 N N   . ARG A 243 ? 0.42783 0.42866 0.36424 -0.02567 0.04973  -0.04357 446 ARG A N   
1995 C CA  . ARG A 243 ? 0.43990 0.42842 0.37615 -0.02554 0.04554  -0.04797 446 ARG A CA  
1996 C C   . ARG A 243 ? 0.54064 0.53718 0.49525 -0.02239 0.04513  -0.04444 446 ARG A C   
1997 O O   . ARG A 243 ? 0.49526 0.48775 0.45451 -0.02751 0.03843  -0.04554 446 ARG A O   
1998 C CB  . ARG A 243 ? 0.47202 0.44012 0.38804 -0.02055 0.05162  -0.05444 446 ARG A CB  
1999 C CG  . ARG A 243 ? 0.42468 0.38194 0.32051 -0.02526 0.04965  -0.05930 446 ARG A CG  
2000 C CD  . ARG A 243 ? 0.47876 0.41241 0.35139 -0.02070 0.05593  -0.06600 446 ARG A CD  
2001 N NE  . ARG A 243 ? 0.49178 0.40742 0.35910 -0.02395 0.05379  -0.07039 446 ARG A NE  
2002 C CZ  . ARG A 243 ? 0.55290 0.46105 0.41386 -0.03656 0.04592  -0.07602 446 ARG A CZ  
2003 N NH1 . ARG A 243 ? 0.47871 0.39693 0.33790 -0.04401 0.03827  -0.07845 446 ARG A NH1 
2004 N NH2 . ARG A 243 ? 0.59050 0.48152 0.44530 -0.04190 0.04576  -0.07960 446 ARG A NH2 
2005 N N   . PRO A 244 ? 0.61357 0.62427 0.57923 -0.01441 0.05155  -0.04054 447 PRO A N   
2006 C CA  . PRO A 244 ? 0.65165 0.67027 0.63351 -0.01059 0.04972  -0.03726 447 PRO A CA  
2007 C C   . PRO A 244 ? 0.68612 0.71572 0.68283 -0.01932 0.04149  -0.03284 447 PRO A C   
2008 O O   . PRO A 244 ? 0.66542 0.69646 0.67231 -0.01770 0.03848  -0.03100 447 PRO A O   
2009 C CB  . PRO A 244 ? 0.58119 0.62064 0.57208 -0.00003 0.05777  -0.03481 447 PRO A CB  
2010 C CG  . PRO A 244 ? 0.66430 0.69652 0.63832 0.00554  0.06555  -0.03886 447 PRO A CG  
2011 C CD  . PRO A 244 ? 0.57721 0.59761 0.53916 -0.00652 0.06149  -0.04045 447 PRO A CD  
2012 N N   . LEU A 245 ? 0.42720 0.46143 0.42203 -0.02724 0.03787  -0.03099 448 LEU A N   
2013 C CA  . LEU A 245 ? 0.45847 0.50039 0.46318 -0.03325 0.03079  -0.02647 448 LEU A CA  
2014 C C   . LEU A 245 ? 0.43845 0.47172 0.44097 -0.03681 0.02182  -0.02895 448 LEU A C   
2015 O O   . LEU A 245 ? 0.52731 0.56497 0.53515 -0.03966 0.01556  -0.02572 448 LEU A O   
2016 C CB  . LEU A 245 ? 0.42631 0.47225 0.42405 -0.03930 0.03150  -0.02292 448 LEU A CB  
2017 C CG  . LEU A 245 ? 0.53009 0.59323 0.53396 -0.04053 0.04018  -0.01975 448 LEU A CG  
2018 C CD1 . LEU A 245 ? 0.65075 0.71490 0.64577 -0.03558 0.04952  -0.02323 448 LEU A CD1 
2019 C CD2 . LEU A 245 ? 0.57640 0.63935 0.57293 -0.05133 0.03887  -0.01508 448 LEU A CD2 
2020 N N   . TYR A 246 ? 0.42521 0.44750 0.41900 -0.03720 0.02124  -0.03510 449 TYR A N   
2021 C CA  . TYR A 246 ? 0.36776 0.38918 0.36071 -0.04225 0.01323  -0.03897 449 TYR A CA  
2022 C C   . TYR A 246 ? 0.59337 0.61277 0.59520 -0.04349 0.01337  -0.03965 449 TYR A C   
2023 O O   . TYR A 246 ? 0.69153 0.70033 0.68590 -0.04766 0.01471  -0.04522 449 TYR A O   
2024 C CB  . TYR A 246 ? 0.46533 0.47906 0.44246 -0.04549 0.01198  -0.04622 449 TYR A CB  
2025 C CG  . TYR A 246 ? 0.47453 0.48937 0.44051 -0.04401 0.00944  -0.04529 449 TYR A CG  
2026 C CD1 . TYR A 246 ? 0.40422 0.42591 0.36725 -0.04406 -0.00001 -0.04588 449 TYR A CD1 
2027 C CD2 . TYR A 246 ? 0.39909 0.40745 0.35502 -0.04126 0.01679  -0.04374 449 TYR A CD2 
2028 C CE1 . TYR A 246 ? 0.35462 0.37150 0.30159 -0.04113 -0.00257 -0.04459 449 TYR A CE1 
2029 C CE2 . TYR A 246 ? 0.38806 0.39339 0.32970 -0.04088 0.01527  -0.04243 449 TYR A CE2 
2030 C CZ  . TYR A 246 ? 0.36304 0.37000 0.29847 -0.04068 0.00535  -0.04263 449 TYR A CZ  
2031 O OH  . TYR A 246 ? 0.39697 0.39514 0.31233 -0.03879 0.00357  -0.04097 449 TYR A OH  
2032 N N   . LYS A 247 ? 0.31439 0.34215 0.32956 -0.04119 0.01194  -0.03389 450 LYS A N   
2033 C CA  . LYS A 247 ? 0.61163 0.63628 0.63440 -0.03912 0.01395  -0.03211 450 LYS A CA  
2034 C C   . LYS A 247 ? 0.40163 0.43852 0.43804 -0.03769 0.01006  -0.02586 450 LYS A C   
2035 O O   . LYS A 247 ? 0.35855 0.40350 0.39745 -0.03690 0.00985  -0.02196 450 LYS A O   
2036 C CB  . LYS A 247 ? 0.54682 0.56272 0.56463 -0.03118 0.02202  -0.03177 450 LYS A CB  
2037 C CG  . LYS A 247 ? 0.71150 0.71472 0.72726 -0.02718 0.02444  -0.03158 450 LYS A CG  
2038 C CD  . LYS A 247 ? 0.57948 0.56892 0.58257 -0.01621 0.03207  -0.03293 450 LYS A CD  
2039 C CE  . LYS A 247 ? 0.75204 0.76149 0.76787 -0.00469 0.03444  -0.02810 450 LYS A CE  
2040 N NZ  . LYS A 247 ? 0.83184 0.83023 0.84088 0.00929  0.03794  -0.02743 450 LYS A NZ  
2041 N N   A HIS A 248 ? 0.39224 0.42927 0.43451 -0.03952 0.00675  -0.02549 451 HIS A N   
2042 N N   B HIS A 248 ? 0.37951 0.41531 0.42224 -0.03808 0.00819  -0.02487 451 HIS A N   
2043 C CA  A HIS A 248 ? 0.30677 0.35174 0.35978 -0.03754 0.00355  -0.01989 451 HIS A CA  
2044 C CA  B HIS A 248 ? 0.30656 0.35184 0.35967 -0.03770 0.00326  -0.01984 451 HIS A CA  
2045 C C   A HIS A 248 ? 0.34808 0.38549 0.40313 -0.03462 0.00626  -0.01931 451 HIS A C   
2046 C C   B HIS A 248 ? 0.30833 0.35067 0.36745 -0.03454 0.00418  -0.01734 451 HIS A C   
2047 O O   A HIS A 248 ? 0.28656 0.31464 0.33617 -0.03888 0.00679  -0.02295 451 HIS A O   
2048 O O   B HIS A 248 ? 0.26762 0.31008 0.32975 -0.03693 0.00068  -0.01701 451 HIS A O   
2049 C CB  A HIS A 248 ? 0.28710 0.33827 0.34137 -0.04044 -0.00396 -0.01948 451 HIS A CB  
2050 C CB  B HIS A 248 ? 0.28234 0.33223 0.33411 -0.04157 -0.00353 -0.02189 451 HIS A CB  
2051 C CG  A HIS A 248 ? 0.32334 0.37604 0.38168 -0.04241 -0.00667 -0.02123 451 HIS A CG  
2052 C CG  B HIS A 248 ? 0.28869 0.33733 0.33807 -0.04654 -0.00370 -0.02805 451 HIS A CG  
2053 N ND1 A HIS A 248 ? 0.19192 0.24789 0.25630 -0.04054 -0.01022 -0.01722 451 HIS A ND1 
2054 N ND1 B HIS A 248 ? 0.32498 0.38016 0.37973 -0.04896 -0.00694 -0.02894 451 HIS A ND1 
2055 C CD2 A HIS A 248 ? 0.30908 0.36217 0.36511 -0.04763 -0.00622 -0.02708 451 HIS A CD2 
2056 C CD2 B HIS A 248 ? 0.34523 0.38760 0.38612 -0.05143 -0.00055 -0.03420 451 HIS A CD2 
2057 C CE1 A HIS A 248 ? 0.25045 0.30899 0.31666 -0.04318 -0.01116 -0.02017 451 HIS A CE1 
2058 C CE1 B HIS A 248 ? 0.31680 0.37256 0.36786 -0.05658 -0.00531 -0.03553 451 HIS A CE1 
2059 N NE2 A HIS A 248 ? 0.28123 0.33940 0.34301 -0.04856 -0.00855 -0.02631 451 HIS A NE2 
2060 N NE2 B HIS A 248 ? 0.35728 0.40389 0.39906 -0.05881 -0.00176 -0.03889 451 HIS A NE2 
2061 N N   . ASP A 249 ? 0.27188 0.31293 0.33195 -0.02750 0.00877  -0.01550 452 ASP A N   
2062 C CA  . ASP A 249 ? 0.23906 0.27317 0.29952 -0.02160 0.00982  -0.01367 452 ASP A CA  
2063 C C   . ASP A 249 ? 0.18929 0.23720 0.26194 -0.02082 0.00480  -0.00860 452 ASP A C   
2064 O O   . ASP A 249 ? 0.22185 0.28554 0.30217 -0.02101 0.00377  -0.00608 452 ASP A O   
2065 C CB  . ASP A 249 ? 0.33310 0.36219 0.38763 -0.01025 0.01568  -0.01403 452 ASP A CB  
2066 C CG  . ASP A 249 ? 0.46750 0.47696 0.50487 -0.01054 0.02107  -0.01929 452 ASP A CG  
2067 O OD1 . ASP A 249 ? 0.40353 0.39546 0.43009 -0.01868 0.02122  -0.02274 452 ASP A OD1 
2068 O OD2 . ASP A 249 ? 0.57387 0.58671 0.60798 -0.00369 0.02542  -0.02042 452 ASP A OD2 
2069 N N   . TYR A 250 ? 0.21351 0.25446 0.28586 -0.02128 0.00227  -0.00743 453 TYR A N   
2070 C CA  . TYR A 250 ? 0.18146 0.23174 0.26235 -0.02045 -0.00285 -0.00303 453 TYR A CA  
2071 C C   . TYR A 250 ? 0.20368 0.24086 0.27891 -0.01449 -0.00174 -0.00211 453 TYR A C   
2072 O O   . TYR A 250 ? 0.23674 0.26045 0.30461 -0.01914 -0.00092 -0.00382 453 TYR A O   
2073 C CB  . TYR A 250 ? 0.20468 0.25739 0.28684 -0.02776 -0.00807 -0.00277 453 TYR A CB  
2074 C CG  . TYR A 250 ? 0.16973 0.22678 0.25618 -0.02751 -0.01342 0.00131  453 TYR A CG  
2075 C CD1 . TYR A 250 ? 0.16838 0.23502 0.25801 -0.03029 -0.01659 0.00416  453 TYR A CD1 
2076 C CD2 . TYR A 250 ? 0.19123 0.24096 0.27576 -0.02625 -0.01486 0.00197  453 TYR A CD2 
2077 C CE1 . TYR A 250 ? 0.18914 0.25675 0.27929 -0.03177 -0.02184 0.00733  453 TYR A CE1 
2078 C CE2 . TYR A 250 ? 0.18755 0.23943 0.27374 -0.02583 -0.02010 0.00544  453 TYR A CE2 
2079 C CZ  . TYR A 250 ? 0.18725 0.24740 0.27594 -0.02849 -0.02387 0.00795  453 TYR A CZ  
2080 O OH  . TYR A 250 ? 0.17966 0.23901 0.26679 -0.02956 -0.02919 0.01082  453 TYR A OH  
2081 N N   A ILE A 251 ? 0.22027 0.26239 0.29748 -0.00418 -0.00154 0.00021  454 ILE A N   
2082 N N   B ILE A 251 ? 0.22053 0.26238 0.29749 -0.00410 -0.00134 0.00010  454 ILE A N   
2083 C CA  A ILE A 251 ? 0.24641 0.27040 0.31154 0.00550  0.00035  0.00089  454 ILE A CA  
2084 C CA  B ILE A 251 ? 0.24623 0.27037 0.31150 0.00540  0.00028  0.00092  454 ILE A CA  
2085 C C   A ILE A 251 ? 0.22654 0.25494 0.29615 0.00709  -0.00534 0.00470  454 ILE A C   
2086 C C   B ILE A 251 ? 0.22600 0.25533 0.29639 0.00630  -0.00554 0.00470  454 ILE A C   
2087 O O   A ILE A 251 ? 0.22437 0.27200 0.30380 0.01333  -0.00937 0.00701  454 ILE A O   
2088 O O   B ILE A 251 ? 0.22624 0.27628 0.30778 0.01072  -0.00987 0.00701  454 ILE A O   
2089 C CB  A ILE A 251 ? 0.24803 0.27370 0.30849 0.02062  0.00369  0.00035  454 ILE A CB  
2090 C CB  B ILE A 251 ? 0.24795 0.27394 0.30866 0.02083  0.00342  0.00053  454 ILE A CB  
2091 C CG1 A ILE A 251 ? 0.25475 0.27904 0.31165 0.01890  0.00908  -0.00341 454 ILE A CG1 
2092 C CG1 B ILE A 251 ? 0.25819 0.27387 0.30954 0.02038  0.00976  -0.00356 454 ILE A CG1 
2093 C CG2 A ILE A 251 ? 0.24846 0.24431 0.28688 0.03213  0.00627  0.00064  454 ILE A CG2 
2094 C CG2 B ILE A 251 ? 0.24499 0.24872 0.28855 0.03385  0.00393  0.00199  454 ILE A CG2 
2095 C CD1 A ILE A 251 ? 0.28059 0.27806 0.32187 0.00901  0.01283  -0.00701 454 ILE A CD1 
2096 C CD1 B ILE A 251 ? 0.26763 0.29252 0.31730 0.03649  0.01297  -0.00442 454 ILE A CD1 
2097 N N   . ARG A 252 ? 0.21800 0.22983 0.27948 0.00122  -0.00536 0.00484  455 ARG A N   
2098 C CA  . ARG A 252 ? 0.21332 0.22605 0.27608 0.00280  -0.01031 0.00826  455 ARG A CA  
2099 C C   . ARG A 252 ? 0.22502 0.22482 0.27568 0.01682  -0.01021 0.01042  455 ARG A C   
2100 O O   . ARG A 252 ? 0.28382 0.26332 0.31821 0.02431  -0.00498 0.00908  455 ARG A O   
2101 C CB  . ARG A 252 ? 0.21778 0.21982 0.27544 -0.00752 -0.00937 0.00721  455 ARG A CB  
2102 C CG  . ARG A 252 ? 0.21628 0.23433 0.28504 -0.01684 -0.01187 0.00536  455 ARG A CG  
2103 C CD  . ARG A 252 ? 0.22136 0.23566 0.28634 -0.02502 -0.01033 0.00268  455 ARG A CD  
2104 N NE  . ARG A 252 ? 0.21051 0.24012 0.28326 -0.02922 -0.01382 0.00074  455 ARG A NE  
2105 C CZ  . ARG A 252 ? 0.20918 0.24401 0.28287 -0.03368 -0.01185 -0.00348 455 ARG A CZ  
2106 N NH1 . ARG A 252 ? 0.24436 0.27009 0.31222 -0.03634 -0.00613 -0.00643 455 ARG A NH1 
2107 N NH2 . ARG A 252 ? 0.20518 0.25188 0.28238 -0.03458 -0.01605 -0.00489 455 ARG A NH2 
2108 N N   . GLY A 253 ? 0.21427 0.22408 0.26993 0.02144  -0.01655 0.01360  456 GLY A N   
2109 C CA  . GLY A 253 ? 0.24721 0.24473 0.28938 0.03620  -0.01812 0.01583  456 GLY A CA  
2110 C C   . GLY A 253 ? 0.32079 0.34070 0.37026 0.05171  -0.02156 0.01591  456 GLY A C   
2111 O O   . GLY A 253 ? 0.33838 0.34820 0.37391 0.06845  -0.02319 0.01719  456 GLY A O   
2112 N N   . LEU A 254 ? 0.25759 0.30826 0.32683 0.04728  -0.02245 0.01426  457 LEU A N   
2113 C CA  . LEU A 254 ? 0.27027 0.35221 0.35068 0.05983  -0.02504 0.01329  457 LEU A CA  
2114 C C   . LEU A 254 ? 0.23532 0.34457 0.32847 0.05918  -0.03402 0.01481  457 LEU A C   
2115 O O   . LEU A 254 ? 0.25765 0.36730 0.35595 0.04415  -0.03772 0.01624  457 LEU A O   
2116 C CB  . LEU A 254 ? 0.23713 0.34223 0.33268 0.05175  -0.02128 0.01069  457 LEU A CB  
2117 C CG  . LEU A 254 ? 0.33118 0.41298 0.41447 0.05262  -0.01290 0.00834  457 LEU A CG  
2118 C CD1 . LEU A 254 ? 0.24217 0.34721 0.33880 0.04590  -0.00931 0.00591  457 LEU A CD1 
2119 C CD2 . LEU A 254 ? 0.37083 0.43451 0.43516 0.07370  -0.01007 0.00760  457 LEU A CD2 
2120 N N   . GLN A 255 ? 0.25931 0.39207 0.35596 0.07643  -0.03781 0.01392  458 GLN A N   
2121 C CA  . GLN A 255 ? 0.28337 0.45213 0.39525 0.07475  -0.04677 0.01384  458 GLN A CA  
2122 C C   . GLN A 255 ? 0.21544 0.42081 0.34982 0.05604  -0.04664 0.01171  458 GLN A C   
2123 O O   . GLN A 255 ? 0.20769 0.41680 0.34684 0.05104  -0.03971 0.01006  458 GLN A O   
2124 C CB  . GLN A 255 ? 0.28746 0.47804 0.39792 0.10020  -0.05112 0.01233  458 GLN A CB  
2125 C CG  . GLN A 255 ? 0.41519 0.56632 0.49787 0.11884  -0.05267 0.01501  458 GLN A CG  
2126 C CD  . GLN A 255 ? 0.55093 0.71931 0.62685 0.14898  -0.05675 0.01328  458 GLN A CD  
2127 O OE1 . GLN A 255 ? 0.55302 0.76687 0.64781 0.15340  -0.05777 0.00933  458 GLN A OE1 
2128 N NE2 . GLN A 255 ? 0.49912 0.62740 0.54438 0.16769  -0.05776 0.01582  458 GLN A NE2 
2129 N N   . ASP A 256 ? 0.21366 0.44338 0.35864 0.04450  -0.05417 0.01162  459 ASP A N   
2130 C CA  . ASP A 256 ? 0.21913 0.47952 0.38017 0.02352  -0.05376 0.00959  459 ASP A CA  
2131 C C   . ASP A 256 ? 0.24410 0.54455 0.42033 0.03012  -0.04907 0.00570  459 ASP A C   
2132 O O   . ASP A 256 ? 0.20023 0.50947 0.38263 0.01524  -0.04302 0.00440  459 ASP A O   
2133 C CB  . ASP A 256 ? 0.22700 0.50960 0.39412 0.01113  -0.06300 0.00907  459 ASP A CB  
2134 C CG  . ASP A 256 ? 0.30155 0.54597 0.45322 0.00002  -0.06673 0.01247  459 ASP A CG  
2135 O OD1 . ASP A 256 ? 0.22908 0.43477 0.36801 0.00118  -0.06206 0.01497  459 ASP A OD1 
2136 O OD2 . ASP A 256 ? 0.29230 0.54783 0.44425 -0.00997 -0.07450 0.01205  459 ASP A OD2 
2137 N N   . GLU A 257 ? 0.21051 0.52635 0.38674 0.05277  -0.05052 0.00365  460 GLU A N   
2138 C CA  . GLU A 257 ? 0.24709 0.59140 0.43077 0.06124  -0.04468 -0.00057 460 GLU A CA  
2139 C C   . GLU A 257 ? 0.26686 0.60013 0.44787 0.06937  -0.03577 -0.00074 460 GLU A C   
2140 O O   . GLU A 257 ? 0.28736 0.64279 0.47341 0.07516  -0.02988 -0.00425 460 GLU A O   
2141 C CB  . GLU A 257 ? 0.24691 0.60333 0.42507 0.08623  -0.04885 -0.00256 460 GLU A CB  
2142 C CG  . GLU A 257 ? 0.30200 0.67845 0.48482 0.07896  -0.05750 -0.00376 460 GLU A CG  
2143 C CD  . GLU A 257 ? 0.39365 0.74010 0.56509 0.07866  -0.06552 0.00042  460 GLU A CD  
2144 O OE1 . GLU A 257 ? 0.28196 0.59361 0.44352 0.07935  -0.06442 0.00448  460 GLU A OE1 
2145 O OE2 . GLU A 257 ? 0.46723 0.82642 0.63902 0.07787  -0.07297 -0.00061 460 GLU A OE2 
2146 N N   . ASP A 258 ? 0.23714 0.52539 0.40362 0.06714  -0.03320 0.00259  461 ASP A N   
2147 C CA  . ASP A 258 ? 0.27018 0.53286 0.42612 0.07088  -0.02396 0.00202  461 ASP A CA  
2148 C C   . ASP A 258 ? 0.25065 0.49586 0.40670 0.04587  -0.02010 0.00324  461 ASP A C   
2149 O O   . ASP A 258 ? 0.24995 0.46628 0.39438 0.04584  -0.01389 0.00308  461 ASP A O   
2150 C CB  . ASP A 258 ? 0.27535 0.49038 0.40565 0.08901  -0.02266 0.00371  461 ASP A CB  
2151 C CG  . ASP A 258 ? 0.33883 0.56424 0.46122 0.11944  -0.02473 0.00211  461 ASP A CG  
2152 O OD1 . ASP A 258 ? 0.32497 0.59156 0.46047 0.13069  -0.02311 -0.00158 461 ASP A OD1 
2153 O OD2 . ASP A 258 ? 0.41270 0.60530 0.51397 0.13308  -0.02780 0.00438  461 ASP A OD2 
2154 N N   . GLU A 259 ? 0.21035 0.47106 0.37638 0.02495  -0.02404 0.00413  462 GLU A N   
2155 C CA  . GLU A 259 ? 0.16111 0.39958 0.32145 0.00418  -0.02176 0.00568  462 GLU A CA  
2156 C C   . GLU A 259 ? 0.16539 0.40968 0.32705 -0.00033 -0.01335 0.00362  462 GLU A C   
2157 O O   . GLU A 259 ? 0.15923 0.37580 0.31049 -0.00905 -0.01050 0.00451  462 GLU A O   
2158 C CB  . GLU A 259 ? 0.19712 0.44782 0.36202 -0.01611 -0.02745 0.00679  462 GLU A CB  
2159 C CG  . GLU A 259 ? 0.18565 0.40891 0.33884 -0.03488 -0.02612 0.00861  462 GLU A CG  
2160 C CD  . GLU A 259 ? 0.15887 0.34198 0.29787 -0.03144 -0.02874 0.01104  462 GLU A CD  
2161 O OE1 . GLU A 259 ? 0.20571 0.38074 0.34299 -0.01963 -0.03229 0.01196  462 GLU A OE1 
2162 O OE2 . GLU A 259 ? 0.17681 0.33703 0.30508 -0.04006 -0.02715 0.01178  462 GLU A OE2 
2163 N N   . GLY A 260 ? 0.17170 0.45323 0.34535 0.00689  -0.00937 0.00048  463 GLY A N   
2164 C CA  . GLY A 260 ? 0.14899 0.43592 0.32235 0.00361  -0.00052 -0.00163 463 GLY A CA  
2165 C C   . GLY A 260 ? 0.20593 0.45996 0.36456 0.01841  0.00449  -0.00235 463 GLY A C   
2166 O O   . GLY A 260 ? 0.20935 0.45942 0.36375 0.01458  0.01135  -0.00392 463 GLY A O   
2167 N N   . LYS A 261 ? 0.21465 0.44297 0.36256 0.03372  0.00152  -0.00143 464 LYS A N   
2168 C CA  . LYS A 261 ? 0.23274 0.42420 0.36192 0.04437  0.00628  -0.00248 464 LYS A CA  
2169 C C   . LYS A 261 ? 0.25856 0.41098 0.37546 0.03259  0.00424  -0.00055 464 LYS A C   
2170 O O   . LYS A 261 ? 0.27611 0.39629 0.37602 0.03836  0.00733  -0.00170 464 LYS A O   
2171 C CB  . LYS A 261 ? 0.28143 0.46621 0.40032 0.06993  0.00603  -0.00340 464 LYS A CB  
2172 C CG  . LYS A 261 ? 0.36701 0.59190 0.49589 0.08690  0.00904  -0.00666 464 LYS A CG  
2173 C CD  . LYS A 261 ? 0.45365 0.67418 0.57035 0.11605  0.00675  -0.00739 464 LYS A CD  
2174 C CE  . LYS A 261 ? 0.37427 0.62136 0.50402 0.11863  -0.00255 -0.00571 464 LYS A CE  
2175 N NZ  . LYS A 261 ? 0.41233 0.66673 0.53207 0.15082  -0.00547 -0.00717 464 LYS A NZ  
2176 N N   . LYS A 262 ? 0.20514 0.36013 0.32851 0.01585  -0.00057 0.00179  465 LYS A N   
2177 C CA  . LYS A 262 ? 0.18672 0.31138 0.30018 0.00804  -0.00343 0.00323  465 LYS A CA  
2178 C C   . LYS A 262 ? 0.22903 0.33921 0.33603 -0.00307 -0.00066 0.00175  465 LYS A C   
2179 O O   . LYS A 262 ? 0.21659 0.30260 0.31289 -0.00384 0.00017  0.00044  465 LYS A O   
2180 C CB  . LYS A 262 ? 0.16408 0.29527 0.28359 -0.00064 -0.01073 0.00624  465 LYS A CB  
2181 C CG  . LYS A 262 ? 0.17688 0.28061 0.28655 -0.00544 -0.01356 0.00742  465 LYS A CG  
2182 C CD  . LYS A 262 ? 0.19511 0.30288 0.30765 -0.00912 -0.02057 0.01026  465 LYS A CD  
2183 C CE  . LYS A 262 ? 0.19937 0.28356 0.30243 -0.01232 -0.02262 0.01104  465 LYS A CE  
2184 N NZ  . LYS A 262 ? 0.19421 0.28050 0.29767 -0.01340 -0.02921 0.01372  465 LYS A NZ  
2185 N N   . SER A 263 ? 0.17756 0.30220 0.28916 -0.01248 0.00071  0.00161  466 SER A N   
2186 C CA  . SER A 263 ? 0.17732 0.28781 0.28048 -0.02240 0.00122  0.00075  466 SER A CA  
2187 C C   . SER A 263 ? 0.19921 0.31891 0.30097 -0.02420 0.00741  -0.00120 466 SER A C   
2188 O O   . SER A 263 ? 0.18939 0.33095 0.29812 -0.02910 0.00930  -0.00030 466 SER A O   
2189 C CB  . SER A 263 ? 0.17894 0.28751 0.28052 -0.03387 -0.00461 0.00353  466 SER A CB  
2190 O OG  . SER A 263 ? 0.20644 0.30505 0.29763 -0.04110 -0.00389 0.00278  466 SER A OG  
2191 N N   . ASN A 264 ? 0.21434 0.31829 0.30611 -0.02182 0.01089  -0.00429 467 ASN A N   
2192 C CA  . ASN A 264 ? 0.22535 0.33615 0.31349 -0.02339 0.01693  -0.00615 467 ASN A CA  
2193 C C   . ASN A 264 ? 0.22717 0.33783 0.30994 -0.03664 0.01534  -0.00433 467 ASN A C   
2194 O O   . ASN A 264 ? 0.21990 0.34419 0.30266 -0.04161 0.02034  -0.00411 467 ASN A O   
2195 C CB  . ASN A 264 ? 0.24926 0.34114 0.32505 -0.01794 0.02074  -0.01041 467 ASN A CB  
2196 C CG  . ASN A 264 ? 0.29294 0.36597 0.35929 -0.02515 0.01627  -0.01199 467 ASN A CG  
2197 O OD1 . ASN A 264 ? 0.33462 0.40197 0.40306 -0.02747 0.01088  -0.01097 467 ASN A OD1 
2198 N ND2 . ASN A 264 ? 0.33867 0.40462 0.39438 -0.02808 0.01839  -0.01497 467 ASN A ND2 
2199 N N   . ILE A 265 ? 0.22084 0.31555 0.29649 -0.04184 0.00885  -0.00315 468 ILE A N   
2200 C CA  . ILE A 265 ? 0.22488 0.31172 0.28815 -0.05165 0.00674  -0.00126 468 ILE A CA  
2201 C C   . ILE A 265 ? 0.21012 0.30933 0.27664 -0.06121 0.00699  0.00226  468 ILE A C   
2202 O O   . ILE A 265 ? 0.24755 0.34909 0.30551 -0.07077 0.01112  0.00317  468 ILE A O   
2203 C CB  . ILE A 265 ? 0.24047 0.30904 0.29400 -0.05094 -0.00086 -0.00135 468 ILE A CB  
2204 C CG1 . ILE A 265 ? 0.24800 0.30970 0.29859 -0.04509 -0.00084 -0.00611 468 ILE A CG1 
2205 C CG2 . ILE A 265 ? 0.23370 0.28819 0.26787 -0.05794 -0.00365 0.00099  468 ILE A CG2 
2206 C CD1 . ILE A 265 ? 0.24441 0.29741 0.28864 -0.04345 -0.00809 -0.00753 468 ILE A CD1 
2207 N N   . ALA A 266 ? 0.18628 0.29286 0.26313 -0.06051 0.00278  0.00400  469 ALA A N   
2208 C CA  . ALA A 266 ? 0.20948 0.33008 0.28917 -0.07191 0.00258  0.00639  469 ALA A CA  
2209 C C   . ALA A 266 ? 0.22173 0.37266 0.31314 -0.07435 0.01043  0.00478  469 ALA A C   
2210 O O   . ALA A 266 ? 0.21197 0.37346 0.29946 -0.08918 0.01365  0.00562  469 ALA A O   
2211 C CB  . ALA A 266 ? 0.19027 0.31565 0.27953 -0.06924 -0.00374 0.00786  469 ALA A CB  
2212 N N   . ASN A 267 ? 0.21134 0.37531 0.31421 -0.06020 0.01430  0.00207  470 ASN A N   
2213 C CA  . ASN A 267 ? 0.22571 0.42177 0.33968 -0.05846 0.02209  -0.00020 470 ASN A CA  
2214 C C   . ASN A 267 ? 0.23767 0.43045 0.33957 -0.06759 0.02952  -0.00101 470 ASN A C   
2215 O O   . ASN A 267 ? 0.23407 0.45532 0.34223 -0.07532 0.03629  -0.00208 470 ASN A O   
2216 C CB  . ASN A 267 ? 0.16166 0.36426 0.28373 -0.03771 0.02426  -0.00299 470 ASN A CB  
2217 C CG  . ASN A 267 ? 0.19731 0.41401 0.33203 -0.02801 0.01901  -0.00243 470 ASN A CG  
2218 O OD1 . ASN A 267 ? 0.20104 0.42547 0.34096 -0.03752 0.01337  -0.00024 470 ASN A OD1 
2219 N ND2 . ASN A 267 ? 0.20225 0.41831 0.33800 -0.00858 0.02059  -0.00447 470 ASN A ND2 
2220 N N   . ILE A 268 ? 0.24162 0.40265 0.32601 -0.06690 0.02853  -0.00094 471 ILE A N   
2221 C CA  . ILE A 268 ? 0.24439 0.39750 0.31280 -0.07533 0.03475  -0.00131 471 ILE A CA  
2222 C C   . ILE A 268 ? 0.26933 0.42064 0.32622 -0.09553 0.03542  0.00179  471 ILE A C   
2223 O O   . ILE A 268 ? 0.26660 0.43139 0.31892 -0.10672 0.04383  0.00140  471 ILE A O   
2224 C CB  . ILE A 268 ? 0.25528 0.37551 0.30613 -0.06959 0.03141  -0.00229 471 ILE A CB  
2225 C CG1 . ILE A 268 ? 0.29809 0.41936 0.35476 -0.05423 0.03411  -0.00644 471 ILE A CG1 
2226 C CG2 . ILE A 268 ? 0.31833 0.42283 0.34619 -0.07958 0.03519  -0.00150 471 ILE A CG2 
2227 C CD1 . ILE A 268 ? 0.31447 0.45410 0.37317 -0.05056 0.04447  -0.00906 471 ILE A CD1 
2228 N N   . PHE A 269 ? 0.25991 0.39229 0.30880 -0.10128 0.02723  0.00472  472 PHE A N   
2229 C CA  . PHE A 269 ? 0.27058 0.39516 0.30331 -0.12165 0.02770  0.00755  472 PHE A CA  
2230 C C   . PHE A 269 ? 0.30030 0.46602 0.35201 -0.13348 0.03284  0.00640  472 PHE A C   
2231 O O   . PHE A 269 ? 0.28745 0.45956 0.32837 -0.15314 0.03955  0.00674  472 PHE A O   
2232 C CB  . PHE A 269 ? 0.29213 0.38773 0.31149 -0.12266 0.01756  0.01040  472 PHE A CB  
2233 C CG  . PHE A 269 ? 0.25771 0.31400 0.25139 -0.11538 0.01271  0.01143  472 PHE A CG  
2234 C CD1 . PHE A 269 ? 0.33775 0.36322 0.29729 -0.12607 0.01413  0.01369  472 PHE A CD1 
2235 C CD2 . PHE A 269 ? 0.28132 0.33204 0.28301 -0.09786 0.00675  0.00972  472 PHE A CD2 
2236 C CE1 . PHE A 269 ? 0.35571 0.34724 0.29020 -0.11578 0.00848  0.01417  472 PHE A CE1 
2237 C CE2 . PHE A 269 ? 0.31099 0.33344 0.29136 -0.09023 0.00163  0.00953  472 PHE A CE2 
2238 C CZ  . PHE A 269 ? 0.32852 0.32232 0.27558 -0.09745 0.00195  0.01172  472 PHE A CZ  
2239 N N   . ARG A 270 ? 0.25423 0.44886 0.33267 -0.12231 0.02968  0.00473  473 ARG A N   
2240 C CA  . ARG A 270 ? 0.21055 0.44652 0.30710 -0.12974 0.03210  0.00275  473 ARG A CA  
2241 C C   . ARG A 270 ? 0.27526 0.54362 0.38159 -0.12690 0.04234  -0.00086 473 ARG A C   
2242 O O   . ARG A 270 ? 0.29777 0.58818 0.40645 -0.13595 0.04513  -0.00287 473 ARG A O   
2243 C CB  . ARG A 270 ? 0.23656 0.48965 0.35444 -0.11445 0.02455  0.00202  473 ARG A CB  
2244 C CG  . ARG A 270 ? 0.19470 0.47913 0.32454 -0.11632 0.02336  -0.00038 473 ARG A CG  
2245 C CD  . ARG A 270 ? 0.23416 0.52462 0.37686 -0.10417 0.01424  -0.00008 473 ARG A CD  
2246 N NE  . ARG A 270 ? 0.21481 0.51061 0.37091 -0.08200 0.01323  -0.00050 473 ARG A NE  
2247 C CZ  . ARG A 270 ? 0.17094 0.49743 0.34305 -0.06365 0.01554  -0.00360 473 ARG A CZ  
2248 N NH1 . ARG A 270 ? 0.18145 0.54062 0.36129 -0.06446 0.01885  -0.00681 473 ARG A NH1 
2249 N NH2 . ARG A 270 ? 0.16480 0.48412 0.34075 -0.04270 0.01437  -0.00369 473 ARG A NH2 
2250 N N   . ALA A 271 ? 0.26383 0.53367 0.37328 -0.11418 0.04798  -0.00227 474 ALA A N   
2251 C CA  . ALA A 271 ? 0.24249 0.54350 0.35986 -0.11017 0.05853  -0.00594 474 ALA A CA  
2252 C C   . ALA A 271 ? 0.28726 0.57233 0.38162 -0.12833 0.06647  -0.00507 474 ALA A C   
2253 O O   . ALA A 271 ? 0.31110 0.62002 0.40762 -0.13398 0.07324  -0.00757 474 ALA A O   
2254 C CB  . ALA A 271 ? 0.25534 0.55375 0.37813 -0.08449 0.06040  -0.00840 474 ALA A CB  
2255 N N   . TYR A 272 ? 0.29863 0.53913 0.36747 -0.13508 0.06448  -0.00174 475 TYR A N   
2256 C CA  . TYR A 272 ? 0.34916 0.56991 0.39254 -0.14633 0.07269  -0.00103 475 TYR A CA  
2257 C C   . TYR A 272 ? 0.47900 0.66423 0.49053 -0.16977 0.07148  0.00312  475 TYR A C   
2258 O O   . TYR A 272 ? 0.44597 0.61499 0.43317 -0.18083 0.07871  0.00366  475 TYR A O   
2259 C CB  . TYR A 272 ? 0.33741 0.52736 0.36885 -0.12754 0.07081  -0.00166 475 TYR A CB  
2260 C CG  . TYR A 272 ? 0.34770 0.56453 0.40024 -0.10660 0.07488  -0.00609 475 TYR A CG  
2261 C CD1 . TYR A 272 ? 0.34512 0.59353 0.40355 -0.10687 0.08710  -0.00930 475 TYR A CD1 
2262 C CD2 . TYR A 272 ? 0.29128 0.49967 0.35430 -0.08659 0.06722  -0.00726 475 TYR A CD2 
2263 C CE1 . TYR A 272 ? 0.41379 0.68273 0.48658 -0.08526 0.09089  -0.01353 475 TYR A CE1 
2264 C CE2 . TYR A 272 ? 0.32120 0.54607 0.39612 -0.06722 0.07120  -0.01123 475 TYR A CE2 
2265 C CZ  . TYR A 272 ? 0.37464 0.62883 0.45366 -0.06526 0.08275  -0.01436 475 TYR A CZ  
2266 O OH  . TYR A 272 ? 0.42525 0.69230 0.51155 -0.04330 0.08685  -0.01854 475 TYR A OH  
2267 N N   . SER A 273 ? 0.50442 0.58241 0.49482 -0.21380 0.10962  -0.00241 476 SER A N   
2268 C CA  . SER A 273 ? 0.57129 0.60911 0.51960 -0.22852 0.10988  0.00240  476 SER A CA  
2269 C C   . SER A 273 ? 0.71041 0.74926 0.65755 -0.24525 0.11789  -0.00260 476 SER A C   
2270 O O   . SER A 273 ? 0.63985 0.71204 0.62302 -0.24366 0.11722  -0.00845 476 SER A O   
2271 C CB  . SER A 273 ? 0.68270 0.70699 0.62770 -0.22180 0.09752  0.00786  476 SER A CB  
2272 O OG  . SER A 273 ? 0.84280 0.81810 0.73846 -0.23174 0.09680  0.01478  476 SER A OG  
2273 N N   . HIS A 274 ? 0.76467 0.76594 0.66849 -0.26142 0.12600  -0.00040 477 HIS A N   
2274 C CA  . HIS A 274 ? 0.83287 0.83082 0.73149 -0.27998 0.13514  -0.00603 477 HIS A CA  
2275 C C   . HIS A 274 ? 0.89248 0.87906 0.78923 -0.28429 0.12814  -0.00548 477 HIS A C   
2276 O O   . HIS A 274 ? 0.88500 0.84870 0.76689 -0.27611 0.11797  0.00152  477 HIS A O   
2277 C CB  . HIS A 274 ? 0.89138 0.84794 0.74106 -0.29582 0.14732  -0.00370 477 HIS A CB  
2278 C CG  . HIS A 274 ? 0.89869 0.86973 0.75112 -0.29614 0.15692  -0.00692 477 HIS A CG  
2279 N ND1 . HIS A 274 ? 0.88842 0.90407 0.78104 -0.29682 0.16314  -0.01646 477 HIS A ND1 
2280 C CD2 . HIS A 274 ? 0.80393 0.74980 0.62213 -0.29544 0.16122  -0.00199 477 HIS A CD2 
2281 C CE1 . HIS A 274 ? 0.83053 0.84753 0.71457 -0.29702 0.17139  -0.01780 477 HIS A CE1 
2282 N NE2 . HIS A 274 ? 0.84856 0.82460 0.68771 -0.29673 0.17046  -0.00938 477 HIS A NE2 
2283 N N   . ASN A 275 ? 1.04149 1.04472 0.95298 -0.29799 0.13403  -0.01380 478 ASN A N   
2284 C CA  . ASN A 275 ? 1.08716 1.09140 1.00629 -0.30232 0.12759  -0.01630 478 ASN A CA  
2285 C C   . ASN A 275 ? 1.14990 1.10061 1.02031 -0.31905 0.13271  -0.01379 478 ASN A C   
2286 O O   . ASN A 275 ? 1.08569 1.00570 0.92160 -0.33232 0.14476  -0.01315 478 ASN A O   
2287 C CB  . ASN A 275 ? 1.01836 1.06984 0.97827 -0.30893 0.13078  -0.02771 478 ASN A CB  
2288 N N   . ASN A 276 ? 1.20764 1.14491 1.07381 -0.31771 0.12376  -0.01234 479 ASN A N   
2289 C CA  . ASN A 276 ? 1.26351 1.15082 1.08689 -0.33288 0.12832  -0.01143 479 ASN A CA  
2290 C C   . ASN A 276 ? 1.24493 1.14388 1.08610 -0.33289 0.11911  -0.01565 479 ASN A C   
2291 O O   . ASN A 276 ? 1.12858 1.03251 0.98107 -0.31610 0.10567  -0.01052 479 ASN A O   
2292 C CB  . ASN A 276 ? 1.25614 1.08376 1.02785 -0.32539 0.12585  0.00113  479 ASN A CB  
2293 C CG  . ASN A 276 ? 1.39146 1.16064 1.11419 -0.33884 0.13175  0.00274  479 ASN A CG  
2294 O OD1 . ASN A 276 ? 1.44401 1.21348 1.16524 -0.35898 0.14267  -0.00621 479 ASN A OD1 
2295 N ND2 . ASN A 276 ? 1.41896 1.13667 1.10050 -0.32699 0.12482  0.01375  479 ASN A ND2 
2296 N N   . ALA A 277 ? 1.22193 1.12618 1.06551 -0.35249 0.12676  -0.02581 480 ALA A N   
2297 C CA  . ALA A 277 ? 1.19725 1.11265 1.05555 -0.35505 0.11886  -0.03142 480 ALA A CA  
2298 C C   . ALA A 277 ? 1.24502 1.10395 1.06206 -0.35234 0.11340  -0.02395 480 ALA A C   
2299 O O   . ALA A 277 ? 1.21508 1.08126 1.04411 -0.34744 0.10301  -0.02574 480 ALA A O   
2300 C CB  . ALA A 277 ? 1.16896 1.10312 1.03736 -0.37885 0.12966  -0.04553 480 ALA A CB  
2301 N N   . ARG A 278 ? 1.34108 1.14266 1.10824 -0.35439 0.11998  -0.01571 481 ARG A N   
2302 C CA  . ARG A 278 ? 1.38081 1.12404 1.10508 -0.34662 0.11398  -0.00687 481 ARG A CA  
2303 C C   . ARG A 278 ? 1.33299 1.07418 1.06000 -0.32094 0.09940  0.00412  481 ARG A C   
2304 O O   . ARG A 278 ? 1.41673 1.10567 1.10287 -0.31038 0.09470  0.01348  481 ARG A O   
2305 C CB  . ARG A 278 ? 1.32411 1.00393 0.99064 -0.35697 0.12687  -0.00224 481 ARG A CB  
2306 N N   . GLY A 279 ? 0.98392 0.77986 0.75732 -0.30990 0.09251  0.00276  482 GLY A N   
2307 C CA  . GLY A 279 ? 0.88560 0.68420 0.66519 -0.28776 0.08023  0.01152  482 GLY A CA  
2308 C C   . GLY A 279 ? 0.91660 0.68655 0.66534 -0.28030 0.08324  0.02083  482 GLY A C   
2309 O O   . GLY A 279 ? 1.01647 0.78029 0.75137 -0.29094 0.09512  0.01974  482 GLY A O   
2310 N N   . GLY A 280 ? 0.89757 0.64990 0.63463 -0.26146 0.07187  0.02976  483 GLY A N   
2311 C CA  . GLY A 280 ? 0.82527 0.55110 0.53195 -0.25086 0.07147  0.03913  483 GLY A CA  
2312 C C   . GLY A 280 ? 0.72572 0.41319 0.40460 -0.23095 0.05781  0.04853  483 GLY A C   
2313 O O   . GLY A 280 ? 0.79625 0.46686 0.47065 -0.22825 0.05140  0.04762  483 GLY A O   
2314 N N   . TYR A 281 ? 0.73086 0.40598 0.39133 -0.21552 0.05260  0.05689  484 TYR A N   
2315 C CA  . TYR A 281 ? 0.71997 0.35904 0.35175 -0.19210 0.03819  0.06575  484 TYR A CA  
2316 C C   . TYR A 281 ? 0.68915 0.36248 0.34742 -0.17782 0.02900  0.06829  484 TYR A C   
2317 O O   . TYR A 281 ? 0.65606 0.35651 0.32620 -0.18130 0.03464  0.06786  484 TYR A O   
2318 C CB  . TYR A 281 ? 0.74835 0.33115 0.32105 -0.18184 0.03849  0.07408  484 TYR A CB  
2319 C CG  . TYR A 281 ? 0.84286 0.38617 0.38515 -0.19696 0.04935  0.07186  484 TYR A CG  
2320 C CD1 . TYR A 281 ? 1.04221 0.54150 0.55605 -0.18825 0.04414  0.07357  484 TYR A CD1 
2321 C CD2 . TYR A 281 ? 0.91416 0.46470 0.45621 -0.21994 0.06566  0.06717  484 TYR A CD2 
2322 C CE1 . TYR A 281 ? 1.00705 0.46817 0.49074 -0.20364 0.05574  0.07111  484 TYR A CE1 
2323 C CE2 . TYR A 281 ? 0.99723 0.51075 0.50986 -0.23531 0.07684  0.06463  484 TYR A CE2 
2324 C CZ  . TYR A 281 ? 1.14583 0.61395 0.62870 -0.22775 0.07215  0.06677  484 TYR A CZ  
2325 O OH  . TYR A 281 ? 1.27514 0.70432 0.72684 -0.24417 0.08468  0.06380  484 TYR A OH  
2326 N N   . ILE A 282 ? 0.60630 0.28509 0.27938 -0.15909 0.01495  0.06768  485 ILE A N   
2327 C CA  . ILE A 282 ? 0.55141 0.27722 0.26350 -0.13556 0.00394  0.06291  485 ILE A CA  
2328 C C   . ILE A 282 ? 0.60351 0.32402 0.29271 -0.12112 0.00090  0.06643  485 ILE A C   
2329 O O   . ILE A 282 ? 0.54810 0.31189 0.26809 -0.11865 0.00267  0.06103  485 ILE A O   
2330 C CB  . ILE A 282 ? 0.59123 0.31329 0.31091 -0.11273 -0.01094 0.06138  485 ILE A CB  
2331 C CG1 . ILE A 282 ? 0.57827 0.30744 0.31946 -0.12582 -0.00910 0.05699  485 ILE A CG1 
2332 C CG2 . ILE A 282 ? 0.51288 0.28115 0.27054 -0.09035 -0.02011 0.05552  485 ILE A CG2 
2333 C CD1 . ILE A 282 ? 0.58849 0.29209 0.31686 -0.10701 -0.02108 0.05732  485 ILE A CD1 
2334 N N   . GLU A 283 ? 0.64872 0.31493 0.28188 -0.10983 -0.00427 0.07515  486 GLU A N   
2335 C CA  . GLU A 283 ? 0.64630 0.30710 0.25343 -0.09161 -0.01076 0.07834  486 GLU A CA  
2336 C C   . GLU A 283 ? 0.67458 0.34755 0.27732 -0.11067 0.00343  0.07841  486 GLU A C   
2337 O O   . GLU A 283 ? 0.68276 0.37854 0.28820 -0.09887 -0.00074 0.07560  486 GLU A O   
2338 C CB  . GLU A 283 ? 0.71741 0.31267 0.25986 -0.07464 -0.01881 0.08913  486 GLU A CB  
2339 C CG  . GLU A 283 ? 0.80618 0.35189 0.31224 -0.09484 -0.00473 0.09395  486 GLU A CG  
2340 C CD  . GLU A 283 ? 0.80861 0.33906 0.32506 -0.10383 -0.00268 0.09041  486 GLU A CD  
2341 O OE1 . GLU A 283 ? 0.76960 0.32639 0.32052 -0.10154 -0.00929 0.08690  486 GLU A OE1 
2342 O OE2 . GLU A 283 ? 0.86199 0.35345 0.35004 -0.11349 0.00587  0.09067  486 GLU A OE2 
2343 N N   . ASP A 284 ? 0.67313 0.33323 0.26976 -0.14078 0.02076  0.08010  487 ASP A N   
2344 C CA  . ASP A 284 ? 0.69557 0.36878 0.28933 -0.16005 0.03626  0.07915  487 ASP A CA  
2345 C C   . ASP A 284 ? 0.62469 0.36758 0.28113 -0.16044 0.03800  0.06765  487 ASP A C   
2346 O O   . ASP A 284 ? 0.61208 0.37395 0.26872 -0.15755 0.04089  0.06497  487 ASP A O   
2347 C CB  . ASP A 284 ? 0.70914 0.37147 0.30356 -0.18594 0.05235  0.07535  487 ASP A CB  
2348 C CG  . ASP A 284 ? 0.90397 0.50502 0.44407 -0.18270 0.05315  0.08127  487 ASP A CG  
2349 O OD1 . ASP A 284 ? 0.86106 0.42713 0.36335 -0.15864 0.04059  0.08925  487 ASP A OD1 
2350 O OD2 . ASP A 284 ? 0.96132 0.55173 0.49800 -0.20298 0.06631  0.07684  487 ASP A OD2 
2351 N N   . GLY A 285 ? 0.56450 0.34378 0.27197 -0.16349 0.03672  0.06074  488 GLY A N   
2352 C CA  . GLY A 285 ? 0.49995 0.34002 0.26453 -0.16101 0.03861  0.05085  488 GLY A CA  
2353 C C   . GLY A 285 ? 0.48164 0.34047 0.25624 -0.13487 0.02576  0.04707  488 GLY A C   
2354 O O   . GLY A 285 ? 0.46950 0.36402 0.26948 -0.13392 0.03044  0.04001  488 GLY A O   
2355 N N   . LEU A 286 ? 0.49020 0.32671 0.24636 -0.11375 0.01009  0.05022  489 LEU A N   
2356 C CA  . LEU A 286 ? 0.50080 0.35782 0.26675 -0.08957 -0.00243 0.04462  489 LEU A CA  
2357 C C   . LEU A 286 ? 0.49903 0.34790 0.23182 -0.08651 -0.00181 0.04531  489 LEU A C   
2358 O O   . LEU A 286 ? 0.48693 0.37203 0.24327 -0.08090 -0.00205 0.03609  489 LEU A O   
2359 C CB  . LEU A 286 ? 0.47563 0.31043 0.22646 -0.06723 -0.01897 0.04725  489 LEU A CB  
2360 C CG  . LEU A 286 ? 0.44169 0.28848 0.22632 -0.06525 -0.02204 0.04468  489 LEU A CG  
2361 C CD1 . LEU A 286 ? 0.48609 0.30628 0.24868 -0.04247 -0.03734 0.04711  489 LEU A CD1 
2362 C CD2 . LEU A 286 ? 0.39058 0.29190 0.23251 -0.06272 -0.01960 0.03417  489 LEU A CD2 
2363 N N   . THR A 287 ? 0.55638 0.35550 0.23165 -0.09026 -0.00043 0.05592  490 THR A N   
2364 C CA  . THR A 287 ? 0.59435 0.38152 0.23068 -0.08729 0.00043  0.05794  490 THR A CA  
2365 C C   . THR A 287 ? 0.63273 0.45475 0.29477 -0.10706 0.01696  0.05067  490 THR A C   
2366 O O   . THR A 287 ? 0.58920 0.43651 0.25610 -0.09985 0.01501  0.04316  490 THR A O   
2367 C CB  . THR A 287 ? 0.67435 0.39539 0.24115 -0.09195 0.00358  0.07249  490 THR A CB  
2368 O OG1 . THR A 287 ? 0.74399 0.42988 0.28516 -0.07077 -0.01176 0.07901  490 THR A OG1 
2369 C CG2 . THR A 287 ? 0.71506 0.42179 0.23671 -0.08752 0.00425  0.07558  490 THR A CG2 
2370 N N   . TRP A 288 ? 0.57547 0.40082 0.25498 -0.13203 0.03344  0.05149  491 TRP A N   
2371 C CA  . TRP A 288 ? 0.57618 0.43411 0.28143 -0.15144 0.05102  0.04453  491 TRP A CA  
2372 C C   . TRP A 288 ? 0.49424 0.40600 0.25162 -0.14127 0.04855  0.03155  491 TRP A C   
2373 O O   . TRP A 288 ? 0.49430 0.42693 0.25682 -0.14606 0.05721  0.02470  491 TRP A O   
2374 C CB  . TRP A 288 ? 0.59275 0.45474 0.32007 -0.17551 0.06514  0.04528  491 TRP A CB  
2375 C CG  . TRP A 288 ? 0.55119 0.44593 0.30615 -0.19667 0.08453  0.03831  491 TRP A CG  
2376 C CD1 . TRP A 288 ? 0.58364 0.46634 0.31186 -0.21215 0.09912  0.03870  491 TRP A CD1 
2377 C CD2 . TRP A 288 ? 0.46711 0.41228 0.28373 -0.20184 0.09090  0.02908  491 TRP A CD2 
2378 N NE1 . TRP A 288 ? 0.56064 0.48784 0.33963 -0.21865 0.10917  0.02676  491 TRP A NE1 
2379 C CE2 . TRP A 288 ? 0.48442 0.44877 0.31616 -0.21064 0.10362  0.02132  491 TRP A CE2 
2380 C CE3 . TRP A 288 ? 0.47371 0.44905 0.33746 -0.19056 0.08250  0.02483  491 TRP A CE3 
2381 C CZ2 . TRP A 288 ? 0.44067 0.45032 0.32879 -0.20613 0.10701  0.01105  491 TRP A CZ2 
2382 C CZ3 . TRP A 288 ? 0.44544 0.46460 0.36252 -0.18879 0.08796  0.01553  491 TRP A CZ3 
2383 C CH2 . TRP A 288 ? 0.43287 0.46712 0.36083 -0.19367 0.09853  0.00912  491 TRP A CH2 
2384 N N   . TYR A 289 ? 0.44061 0.37302 0.23540 -0.12813 0.03836  0.02762  492 TYR A N   
2385 C CA  . TYR A 289 ? 0.38996 0.36861 0.23336 -0.11991 0.03836  0.01545  492 TYR A CA  
2386 C C   . TYR A 289 ? 0.45532 0.44025 0.28502 -0.10253 0.02741  0.00886  492 TYR A C   
2387 O O   . TYR A 289 ? 0.42068 0.43870 0.27757 -0.10224 0.03277  -0.00267 492 TYR A O   
2388 C CB  . TYR A 289 ? 0.36150 0.35702 0.24516 -0.11191 0.03234  0.01380  492 TYR A CB  
2389 C CG  . TYR A 289 ? 0.31963 0.35744 0.25710 -0.11628 0.04319  0.00511  492 TYR A CG  
2390 C CD1 . TYR A 289 ? 0.33349 0.38353 0.29115 -0.13289 0.05656  0.00640  492 TYR A CD1 
2391 C CD2 . TYR A 289 ? 0.30188 0.36682 0.26892 -0.10365 0.04076  -0.00493 492 TYR A CD2 
2392 C CE1 . TYR A 289 ? 0.29498 0.38146 0.29901 -0.13339 0.06598  -0.00061 492 TYR A CE1 
2393 C CE2 . TYR A 289 ? 0.28224 0.37914 0.29426 -0.10634 0.05211  -0.01178 492 TYR A CE2 
2394 C CZ  . TYR A 289 ? 0.30164 0.40807 0.33048 -0.11974 0.06416  -0.00879 492 TYR A CZ  
2395 O OH  . TYR A 289 ? 0.31224 0.44624 0.38199 -0.11703 0.07365  -0.01447 492 TYR A OH  
2396 N N   . LEU A 290 ? 0.46644 0.42081 0.25412 -0.08760 0.01223  0.01498  493 LEU A N   
2397 C CA  . LEU A 290 ? 0.43642 0.40471 0.21935 -0.06670 -0.00264 0.00673  493 LEU A CA  
2398 C C   . LEU A 290 ? 0.49404 0.44772 0.22897 -0.06344 -0.00558 0.00740  493 LEU A C   
2399 O O   . LEU A 290 ? 0.47549 0.45831 0.22028 -0.05496 -0.01069 -0.00511 493 LEU A O   
2400 C CB  . LEU A 290 ? 0.44219 0.39547 0.21715 -0.04601 -0.02059 0.01040  493 LEU A CB  
2401 C CG  . LEU A 290 ? 0.39434 0.36722 0.21732 -0.04481 -0.02025 0.00711  493 LEU A CG  
2402 C CD1 . LEU A 290 ? 0.45762 0.41446 0.26931 -0.02411 -0.03707 0.00996  493 LEU A CD1 
2403 C CD2 . LEU A 290 ? 0.36251 0.38425 0.23774 -0.04523 -0.01459 -0.00826 493 LEU A CD2 
2404 N N   . TYR A 291 ? 0.54449 0.45308 0.22559 -0.06985 -0.00240 0.02097  494 TYR A N   
2405 C CA  . TYR A 291 ? 0.61359 0.50449 0.24244 -0.06447 -0.00591 0.02301  494 TYR A CA  
2406 C C   . TYR A 291 ? 0.68418 0.52752 0.26335 -0.08266 0.00831  0.03751  494 TYR A C   
2407 O O   . TYR A 291 ? 0.67184 0.49336 0.25391 -0.09692 0.01758  0.04576  494 TYR A O   
2408 C CB  . TYR A 291 ? 0.66097 0.53988 0.25851 -0.03461 -0.02989 0.02427  494 TYR A CB  
2409 C CG  . TYR A 291 ? 0.72222 0.55852 0.29507 -0.02309 -0.03935 0.03778  494 TYR A CG  
2410 C CD1 . TYR A 291 ? 0.70161 0.55511 0.31582 -0.01388 -0.04708 0.03355  494 TYR A CD1 
2411 C CD2 . TYR A 291 ? 0.83690 0.61270 0.34198 -0.02129 -0.03941 0.05451  494 TYR A CD2 
2412 C CE1 . TYR A 291 ? 0.73509 0.54887 0.32616 -0.00317 -0.05509 0.04465  494 TYR A CE1 
2413 C CE2 . TYR A 291 ? 0.89674 0.62957 0.37743 -0.01074 -0.04676 0.06608  494 TYR A CE2 
2414 C CZ  . TYR A 291 ? 0.89992 0.65314 0.42465 -0.00157 -0.05492 0.06056  494 TYR A CZ  
2415 O OH  . TYR A 291 ? 0.87410 0.58374 0.37388 0.00887  -0.06148 0.07094  494 TYR A OH  
2416 N N   . LYS A 292 ? 0.69888 0.52602 0.23041 -0.08270 0.01034  0.03977  495 LYS A N   
2417 C CA  . LYS A 292 ? 0.74736 0.53264 0.23182 -0.10348 0.02819  0.05148  495 LYS A CA  
2418 C C   . LYS A 292 ? 0.98517 0.70442 0.40339 -0.09360 0.02077  0.06951  495 LYS A C   
2419 O O   . LYS A 292 ? 0.93211 0.63695 0.31789 -0.06621 0.00144  0.07271  495 LYS A O   
2420 C CB  . LYS A 292 ? 0.78444 0.57991 0.24454 -0.10909 0.03605  0.04580  495 LYS A CB  
2421 C CG  . LYS A 292 ? 0.85523 0.71015 0.37785 -0.12099 0.04712  0.02780  495 LYS A CG  
2422 C CD  . LYS A 292 ? 0.89527 0.75465 0.39363 -0.13457 0.06221  0.02285  495 LYS A CD  
2423 C CE  . LYS A 292 ? 0.88889 0.75985 0.36039 -0.11436 0.04597  0.01499  495 LYS A CE  
2424 N NZ  . LYS A 292 ? 0.94997 0.82337 0.39383 -0.12801 0.06117  0.00984  495 LYS A NZ  
2425 N N   . ARG A 293 ? 0.89860 0.58622 0.31332 -0.11319 0.03565  0.07823  496 ARG A N   
2426 C CA  . ARG A 293 ? 0.96252 0.59355 0.33655 -0.10704 0.03445  0.09087  496 ARG A CA  
2427 C C   . ARG A 293 ? 0.94487 0.55756 0.31588 -0.13700 0.05857  0.09256  496 ARG A C   
2428 O O   . ARG A 293 ? 0.92648 0.56616 0.33971 -0.16073 0.07278  0.08565  496 ARG A O   
2429 C CB  . ARG A 293 ? 1.10472 0.71593 0.48615 -0.09573 0.02304  0.09550  496 ARG A CB  
2430 C CG  . ARG A 293 ? 1.21635 0.81043 0.57118 -0.05944 -0.00059 0.09975  496 ARG A CG  
2431 C CD  . ARG A 293 ? 1.25079 0.83302 0.62092 -0.04829 -0.01101 0.10152  496 ARG A CD  
2432 N NE  . ARG A 293 ? 1.35145 0.88594 0.70519 -0.06218 0.00063  0.10867  496 ARG A NE  
2433 C CZ  . ARG A 293 ? 1.37675 0.86602 0.69790 -0.04477 -0.00652 0.11547  496 ARG A CZ  
2434 N NH1 . ARG A 293 ? 1.38054 0.86787 0.68469 -0.01144 -0.02565 0.11698  496 ARG A NH1 
2435 N NH2 . ARG A 293 ? 1.37302 0.82093 0.68028 -0.06132 0.00612  0.11897  496 ARG A NH2 
2436 N N   . ASP A 294 ? 1.02927 0.59914 0.35235 -0.13487 0.06274  0.10050  497 ASP A N   
2437 C CA  . ASP A 294 ? 1.01483 0.56617 0.33144 -0.16280 0.08538  0.10041  497 ASP A CA  
2438 C C   . ASP A 294 ? 1.00204 0.54373 0.34359 -0.18166 0.09418  0.09843  497 ASP A C   
2439 O O   . ASP A 294 ? 1.04993 0.60801 0.41714 -0.20819 0.11207  0.09095  497 ASP A O   
2440 C CB  . ASP A 294 ? 1.11755 0.61616 0.37211 -0.15473 0.08685  0.11067  497 ASP A CB  
2441 C CG  . ASP A 294 ? 1.33271 0.84333 0.56118 -0.13407 0.07610  0.11202  497 ASP A CG  
2442 O OD1 . ASP A 294 ? 1.41615 0.91659 0.61819 -0.14324 0.08800  0.11318  497 ASP A OD1 
2443 O OD2 . ASP A 294 ? 1.35014 0.88350 0.58602 -0.10889 0.05550  0.11038  497 ASP A OD2 
2444 N N   . GLY A 295 ? 1.06977 0.58840 0.40591 -0.16728 0.08118  0.10332  498 GLY A N   
2445 C CA  . GLY A 295 ? 1.05063 0.55969 0.40728 -0.18423 0.08839  0.10026  498 GLY A CA  
2446 C C   . GLY A 295 ? 1.01680 0.58253 0.43696 -0.20359 0.09585  0.08874  498 GLY A C   
2447 O O   . GLY A 295 ? 0.99095 0.56161 0.43213 -0.22552 0.10823  0.08227  498 GLY A O   
2448 N N   . GLN A 296 ? 0.96607 0.57726 0.41790 -0.19477 0.08827  0.08489  499 GLN A N   
2449 C CA  . GLN A 296 ? 0.84059 0.50835 0.35535 -0.20879 0.09419  0.07412  499 GLN A CA  
2450 C C   . GLN A 296 ? 0.79051 0.49650 0.32961 -0.22403 0.10936  0.06497  499 GLN A C   
2451 O O   . GLN A 296 ? 0.83534 0.59346 0.42931 -0.23016 0.11311  0.05514  499 GLN A O   
2452 C CB  . GLN A 296 ? 0.82020 0.51574 0.35810 -0.19118 0.07885  0.07400  499 GLN A CB  
2453 C CG  . GLN A 296 ? 0.88394 0.56133 0.42489 -0.18142 0.06636  0.07823  499 GLN A CG  
2454 C CD  . GLN A 296 ? 1.05614 0.67276 0.54171 -0.16482 0.05669  0.08822  499 GLN A CD  
2455 O OE1 . GLN A 296 ? 1.04825 0.64965 0.50232 -0.13999 0.04261  0.09361  499 GLN A OE1 
2456 N NE2 . GLN A 296 ? 0.98048 0.56566 0.45623 -0.17710 0.06387  0.08881  499 GLN A NE2 
2457 N N   . LYS A 297 ? 0.89900 0.58006 0.39934 -0.22835 0.11793  0.06766  500 LYS A N   
2458 C CA  . LYS A 297 ? 0.87859 0.59335 0.39927 -0.24174 0.13250  0.05847  500 LYS A CA  
2459 C C   . LYS A 297 ? 0.88057 0.63054 0.45281 -0.26166 0.14509  0.04687  500 LYS A C   
2460 O O   . LYS A 297 ? 0.90952 0.70601 0.52249 -0.26678 0.15259  0.03633  500 LYS A O   
2461 C CB  . LYS A 297 ? 0.89053 0.56547 0.35606 -0.24435 0.14030  0.06430  500 LYS A CB  
2462 N N   . ASN A 298 ? 0.87125 0.60127 0.44257 -0.27068 0.14651  0.04757  501 ASN A N   
2463 C CA  . ASN A 298 ? 0.86032 0.62293 0.47500 -0.28753 0.15656  0.03614  501 ASN A CA  
2464 C C   . ASN A 298 ? 0.85995 0.65330 0.52081 -0.28251 0.14669  0.03217  501 ASN A C   
2465 O O   . ASN A 298 ? 0.82725 0.64008 0.51633 -0.29386 0.15173  0.02438  501 ASN A O   
2466 C CB  . ASN A 298 ? 0.94013 0.66136 0.51934 -0.30477 0.16810  0.03710  501 ASN A CB  
2467 N N   . LEU A 299 ? 0.71196 0.51012 0.37938 -0.26551 0.13266  0.03722  502 LEU A N   
2468 C CA  . LEU A 299 ? 0.65378 0.48066 0.36433 -0.25995 0.12337  0.03382  502 LEU A CA  
2469 C C   . LEU A 299 ? 0.69675 0.58616 0.46990 -0.26060 0.12742  0.02188  502 LEU A C   
2470 O O   . LEU A 299 ? 0.67185 0.58479 0.47852 -0.26364 0.12619  0.01624  502 LEU A O   
2471 C CB  . LEU A 299 ? 0.69011 0.50771 0.39197 -0.24181 0.10851  0.04173  502 LEU A CB  
2472 C CG  . LEU A 299 ? 0.63614 0.47433 0.37413 -0.23446 0.09761  0.04033  502 LEU A CG  
2473 C CD1 . LEU A 299 ? 0.64918 0.44958 0.35307 -0.21966 0.08335  0.05134  502 LEU A CD1 
2474 C CD2 . LEU A 299 ? 0.65027 0.54886 0.44788 -0.22767 0.09693  0.03163  502 LEU A CD2 
2475 N N   . GLY A 300 ? 0.64361 0.55912 0.43127 -0.25590 0.13176  0.01784  503 GLY A N   
2476 C CA  . GLY A 300 ? 0.60848 0.57815 0.45251 -0.25107 0.13437  0.00753  503 GLY A CA  
2477 C C   . GLY A 300 ? 0.63479 0.61684 0.47813 -0.25616 0.14654  0.00168  503 GLY A C   
2478 O O   . GLY A 300 ? 0.65408 0.60418 0.45292 -0.26405 0.15310  0.00557  503 GLY A O   
2479 N N   . SER A 301 ? 0.56967 0.59607 0.46071 -0.25009 0.14917  -0.00712 504 SER A N   
2480 C CA  . SER A 301 ? 0.58982 0.63087 0.48474 -0.25349 0.16062  -0.01380 504 SER A CA  
2481 C C   . SER A 301 ? 0.56758 0.61236 0.45772 -0.24280 0.15911  -0.01443 504 SER A C   
2482 O O   . SER A 301 ? 0.61666 0.66785 0.50214 -0.24618 0.16872  -0.01982 504 SER A O   
2483 C CB  . SER A 301 ? 0.60694 0.69032 0.55124 -0.24975 0.16390  -0.02227 504 SER A CB  
2484 O OG  . SER A 301 ? 0.55024 0.65909 0.53355 -0.23161 0.15263  -0.02190 504 SER A OG  
2485 N N   . ILE A 302 ? 0.54822 0.59066 0.44003 -0.23087 0.14791  -0.01023 505 ILE A N   
2486 C CA  . ILE A 302 ? 0.48792 0.53043 0.36813 -0.22314 0.14608  -0.01114 505 ILE A CA  
2487 C C   . ILE A 302 ? 0.55865 0.56684 0.39713 -0.22301 0.13729  -0.00063 505 ILE A C   
2488 O O   . ILE A 302 ? 0.52868 0.51675 0.35731 -0.22574 0.13145  0.00648  505 ILE A O   
2489 C CB  . ILE A 302 ? 0.46701 0.54651 0.39684 -0.20579 0.14127  -0.01828 505 ILE A CB  
2490 C CG1 . ILE A 302 ? 0.40773 0.49183 0.35909 -0.19551 0.12902  -0.01370 505 ILE A CG1 
2491 C CG2 . ILE A 302 ? 0.47837 0.58581 0.44524 -0.20254 0.14810  -0.02566 505 ILE A CG2 
2492 C CD1 . ILE A 302 ? 0.39799 0.50969 0.39099 -0.17709 0.12401  -0.01887 505 ILE A CD1 
2493 N N   . TYR A 303 ? 0.53214 0.53314 0.34330 -0.21867 0.13586  0.00010  506 TYR A N   
2494 C CA  . TYR A 303 ? 0.57826 0.54819 0.34511 -0.21320 0.12517  0.01064  506 TYR A CA  
2495 C C   . TYR A 303 ? 0.50416 0.50253 0.29518 -0.19519 0.11517  0.00261  506 TYR A C   
2496 O O   . TYR A 303 ? 0.52587 0.53151 0.30358 -0.19001 0.11575  -0.00429 506 TYR A O   
2497 C CB  . TYR A 303 ? 0.60208 0.52564 0.29845 -0.21589 0.12556  0.01948  506 TYR A CB  
2498 C CG  . TYR A 303 ? 0.65609 0.53612 0.30602 -0.20285 0.10871  0.03230  506 TYR A CG  
2499 C CD1 . TYR A 303 ? 0.67653 0.56898 0.34010 -0.17689 0.08761  0.02898  506 TYR A CD1 
2500 C CD2 . TYR A 303 ? 0.73320 0.56330 0.34084 -0.20869 0.10923  0.04383  506 TYR A CD2 
2501 C CE1 . TYR A 303 ? 0.66253 0.51960 0.29229 -0.15933 0.06948  0.03843  506 TYR A CE1 
2502 C CE2 . TYR A 303 ? 0.73764 0.52496 0.30272 -0.19344 0.09339  0.05544  506 TYR A CE2 
2503 C CZ  . TYR A 303 ? 0.68491 0.48796 0.26327 -0.16709 0.07247  0.05238  506 TYR A CZ  
2504 O OH  . TYR A 303 ? 0.73389 0.49999 0.27837 -0.14695 0.05451  0.06155  506 TYR A OH  
2505 N N   . PRO A 304 ? 0.47578 0.49085 0.30546 -0.18290 0.10407  0.00124  507 PRO A N   
2506 C CA  . PRO A 304 ? 0.40028 0.44192 0.25899 -0.16407 0.09387  -0.00858 507 PRO A CA  
2507 C C   . PRO A 304 ? 0.50602 0.53066 0.32571 -0.14833 0.07842  -0.00904 507 PRO A C   
2508 O O   . PRO A 304 ? 0.45769 0.50149 0.28042 -0.14439 0.07987  -0.02005 507 PRO A O   
2509 C CB  . PRO A 304 ? 0.37122 0.42141 0.26495 -0.15524 0.08466  -0.00613 507 PRO A CB  
2510 C CG  . PRO A 304 ? 0.38406 0.43434 0.28956 -0.17328 0.09661  -0.00089 507 PRO A CG  
2511 C CD  . PRO A 304 ? 0.45911 0.47455 0.31245 -0.18830 0.10342  0.00651  507 PRO A CD  
2512 N N   . GLY A 305 ? 0.47342 0.46359 0.25685 -0.13856 0.06354  0.00172  508 GLY A N   
2513 C CA  . GLY A 305 ? 0.52025 0.49469 0.26489 -0.11989 0.04632  0.00209  508 GLY A CA  
2514 C C   . GLY A 305 ? 0.45641 0.46993 0.23200 -0.10669 0.03910  -0.01389 508 GLY A C   
2515 O O   . GLY A 305 ? 0.50207 0.52123 0.25510 -0.10269 0.03654  -0.02091 508 GLY A O   
2516 N N   . LEU A 306 ? 0.41094 0.45108 0.23709 -0.10094 0.03671  -0.02042 509 LEU A N   
2517 C CA  . LEU A 306 ? 0.37013 0.45015 0.23668 -0.09682 0.03897  -0.03756 509 LEU A CA  
2518 C C   . LEU A 306 ? 0.38605 0.47621 0.24030 -0.07888 0.02138  -0.04716 509 LEU A C   
2519 O O   . LEU A 306 ? 0.41362 0.53442 0.29061 -0.07856 0.02433  -0.06362 509 LEU A O   
2520 C CB  . LEU A 306 ? 0.31780 0.41829 0.23814 -0.09628 0.04345  -0.04031 509 LEU A CB  
2521 C CG  . LEU A 306 ? 0.34224 0.44475 0.28440 -0.11217 0.06055  -0.03457 509 LEU A CG  
2522 C CD1 . LEU A 306 ? 0.33195 0.44978 0.31869 -0.10691 0.06070  -0.03497 509 LEU A CD1 
2523 C CD2 . LEU A 306 ? 0.35742 0.47899 0.31156 -0.12431 0.07845  -0.04398 509 LEU A CD2 
2524 N N   . PHE A 307 ? 0.41396 0.48051 0.23373 -0.06370 0.00345  -0.03862 510 PHE A N   
2525 C CA  . PHE A 307 ? 0.41626 0.49790 0.22738 -0.04408 -0.01519 -0.04878 510 PHE A CA  
2526 C C   . PHE A 307 ? 0.49733 0.54576 0.24355 -0.03268 -0.02857 -0.03845 510 PHE A C   
2527 O O   . PHE A 307 ? 0.49564 0.53800 0.22332 -0.01124 -0.04815 -0.03713 510 PHE A O   
2528 C CB  . PHE A 307 ? 0.38516 0.47948 0.22873 -0.03021 -0.02608 -0.05186 510 PHE A CB  
2529 C CG  . PHE A 307 ? 0.35341 0.47438 0.25544 -0.04046 -0.01196 -0.05989 510 PHE A CG  
2530 C CD1 . PHE A 307 ? 0.34487 0.50300 0.28198 -0.04308 -0.00614 -0.07902 510 PHE A CD1 
2531 C CD2 . PHE A 307 ? 0.32036 0.42750 0.23948 -0.04754 -0.00400 -0.04858 510 PHE A CD2 
2532 C CE1 . PHE A 307 ? 0.26319 0.43957 0.24889 -0.05138 0.00835  -0.08515 510 PHE A CE1 
2533 C CE2 . PHE A 307 ? 0.29782 0.42736 0.26644 -0.05437 0.00852  -0.05469 510 PHE A CE2 
2534 C CZ  . PHE A 307 ? 0.25865 0.42036 0.25936 -0.05560 0.01512  -0.07210 510 PHE A CZ  
2535 N N   . ASN A 308 ? 0.51203 0.53761 0.22171 -0.04633 -0.01715 -0.03090 511 ASN A N   
2536 C CA  . ASN A 308 ? 0.59319 0.57862 0.23358 -0.03702 -0.02666 -0.01836 511 ASN A CA  
2537 C C   . ASN A 308 ? 0.72359 0.72831 0.34443 -0.01463 -0.04717 -0.02930 511 ASN A C   
2538 O O   . ASN A 308 ? 0.76978 0.74870 0.34683 0.00673  -0.06527 -0.02027 511 ASN A O   
2539 C CB  . ASN A 308 ? 0.63690 0.60085 0.24567 -0.05836 -0.00742 -0.01174 511 ASN A CB  
2540 C CG  . ASN A 308 ? 0.70524 0.61723 0.23661 -0.05129 -0.01338 0.00462  511 ASN A CG  
2541 O OD1 . ASN A 308 ? 0.73257 0.60233 0.23696 -0.04743 -0.01659 0.02060  511 ASN A OD1 
2542 N ND2 . ASN A 308 ? 0.74141 0.65337 0.23372 -0.04946 -0.01419 0.00072  511 ASN A ND2 
2543 N N   A ASP A 309 ? 0.58257 0.63331 0.23600 -0.01891 -0.04439 -0.04970 512 ASP A N   
2544 N N   B ASP A 309 ? 0.58188 0.63255 0.23448 -0.01814 -0.04512 -0.04970 512 ASP A N   
2545 C CA  A ASP A 309 ? 0.64739 0.72807 0.29172 -0.00054 -0.06322 -0.06525 512 ASP A CA  
2546 C CA  B ASP A 309 ? 0.65373 0.72831 0.28872 0.00183  -0.06526 -0.06274 512 ASP A CA  
2547 C C   A ASP A 309 ? 0.63351 0.72555 0.29016 0.02443  -0.08532 -0.06780 512 ASP A C   
2548 C C   B ASP A 309 ? 0.62904 0.72929 0.29389 0.02333  -0.08469 -0.07142 512 ASP A C   
2549 O O   A ASP A 309 ? 0.63583 0.73477 0.26214 0.04704  -0.10652 -0.07199 512 ASP A O   
2550 O O   B ASP A 309 ? 0.62021 0.74703 0.27566 0.04161  -0.10337 -0.08434 512 ASP A O   
2551 C CB  A ASP A 309 ? 0.61610 0.74637 0.30813 -0.01404 -0.05249 -0.08929 512 ASP A CB  
2552 C CB  B ASP A 309 ? 0.64164 0.75707 0.29821 -0.01059 -0.05632 -0.08429 512 ASP A CB  
2553 C CG  A ASP A 309 ? 0.61973 0.77583 0.28813 -0.00480 -0.06506 -0.10561 512 ASP A CG  
2554 C CG  B ASP A 309 ? 0.59319 0.74795 0.32205 -0.02296 -0.04393 -0.10084 512 ASP A CG  
2555 O OD1 A ASP A 309 ? 0.69341 0.82482 0.30100 0.00994  -0.07921 -0.09566 512 ASP A OD1 
2556 O OD1 B ASP A 309 ? 0.59862 0.74164 0.35659 -0.03228 -0.03199 -0.09149 512 ASP A OD1 
2557 O OD2 A ASP A 309 ? 0.56352 0.76358 0.27223 -0.01226 -0.06049 -0.12886 512 ASP A OD2 
2558 O OD2 B ASP A 309 ? 0.61258 0.80887 0.36734 -0.02341 -0.04584 -0.12356 512 ASP A OD2 
2559 N N   . VAL A 310 ? 0.53820 0.63394 0.23861 0.02177  -0.08090 -0.06589 513 VAL A N   
2560 C CA  . VAL A 310 ? 0.57443 0.68738 0.29565 0.04335  -0.09885 -0.07149 513 VAL A CA  
2561 C C   . VAL A 310 ? 0.61722 0.68369 0.28902 0.06365  -0.11356 -0.05168 513 VAL A C   
2562 O O   . VAL A 310 ? 0.63393 0.71052 0.29676 0.08977  -0.13469 -0.05595 513 VAL A O   
2563 C CB  . VAL A 310 ? 0.49094 0.62487 0.27601 0.03261  -0.08714 -0.07762 513 VAL A CB  
2564 C CG1 . VAL A 310 ? 0.49910 0.65180 0.30537 0.05419  -0.10415 -0.08446 513 VAL A CG1 
2565 C CG2 . VAL A 310 ? 0.44754 0.62142 0.27889 0.01362  -0.07087 -0.09666 513 VAL A CG2 
2566 N N   A PHE A 311 ? 0.63986 0.65489 0.27857 0.05227  -0.10220 -0.03081 514 PHE A N   
2567 N N   B PHE A 311 ? 0.63995 0.65491 0.27856 0.05235  -0.10226 -0.03079 514 PHE A N   
2568 C CA  A PHE A 311 ? 0.63729 0.60227 0.23340 0.06828  -0.11218 -0.01201 514 PHE A CA  
2569 C CA  B PHE A 311 ? 0.63736 0.60230 0.23333 0.06839  -0.11227 -0.01200 514 PHE A CA  
2570 C C   A PHE A 311 ? 0.77345 0.68498 0.29268 0.07201  -0.11341 0.00540  514 PHE A C   
2571 C C   B PHE A 311 ? 0.77349 0.68501 0.29262 0.07208  -0.11346 0.00540  514 PHE A C   
2572 O O   A PHE A 311 ? 0.84525 0.71280 0.32851 0.08677  -0.12090 0.02083  514 PHE A O   
2573 O O   B PHE A 311 ? 0.84527 0.71284 0.32845 0.08684  -0.12095 0.02083  514 PHE A O   
2574 C CB  A PHE A 311 ? 0.63261 0.57716 0.25482 0.05269  -0.09836 -0.00232 514 PHE A CB  
2575 C CB  B PHE A 311 ? 0.63273 0.57719 0.25475 0.05285  -0.09848 -0.00229 514 PHE A CB  
2576 C CG  A PHE A 311 ? 0.56684 0.55462 0.25518 0.05362  -0.09880 -0.01622 514 PHE A CG  
2577 C CG  B PHE A 311 ? 0.56691 0.55464 0.25512 0.05371  -0.09887 -0.01621 514 PHE A CG  
2578 C CD1 A PHE A 311 ? 0.55714 0.55219 0.25402 0.07758  -0.11580 -0.01967 514 PHE A CD1 
2579 C CD1 B PHE A 311 ? 0.55710 0.55221 0.25401 0.07764  -0.11585 -0.01969 514 PHE A CD1 
2580 C CD2 A PHE A 311 ? 0.51389 0.53470 0.25423 0.03187  -0.08168 -0.02631 514 PHE A CD2 
2581 C CD2 B PHE A 311 ? 0.51398 0.53469 0.25413 0.03192  -0.08173 -0.02628 514 PHE A CD2 
2582 C CE1 A PHE A 311 ? 0.48214 0.51581 0.23769 0.07748  -0.11446 -0.03275 514 PHE A CE1 
2583 C CE1 B PHE A 311 ? 0.48209 0.51584 0.23772 0.07748  -0.11447 -0.03278 514 PHE A CE1 
2584 C CE2 A PHE A 311 ? 0.47253 0.52847 0.26905 0.03295  -0.08065 -0.03817 514 PHE A CE2 
2585 C CE2 B PHE A 311 ? 0.47258 0.52848 0.26898 0.03295  -0.08065 -0.03816 514 PHE A CE2 
2586 C CZ  A PHE A 311 ? 0.46687 0.52929 0.27077 0.05471  -0.09653 -0.04149 514 PHE A CZ  
2587 C CZ  B PHE A 311 ? 0.46687 0.52931 0.27077 0.05468  -0.09652 -0.04150 514 PHE A CZ  
2588 N N   . ALA A 312 ? 0.79844 0.71275 0.29725 0.05782  -0.10354 0.00323  515 ALA A N   
2589 C CA  . ALA A 312 ? 0.86750 0.73380 0.29791 0.06006  -0.10218 0.01952  515 ALA A CA  
2590 C C   . ALA A 312 ? 1.01826 0.88969 0.43636 0.08925  -0.12286 0.02020  515 ALA A C   
2591 O O   . ALA A 312 ? 1.00788 0.92861 0.45303 0.10146  -0.13648 0.00276  515 ALA A O   
2592 C CB  . ALA A 312 ? 0.87463 0.74967 0.28769 0.04010  -0.08793 0.01392  515 ALA A CB  
2593 N N   . HIS A 313 ? 0.95736 0.77667 0.33640 0.09953  -0.12391 0.03911  516 HIS A N   
2594 C CA  . HIS A 313 ? 0.99492 0.80565 0.35094 0.12779  -0.14106 0.04292  516 HIS A CA  
2595 C C   . HIS A 313 ? 0.90930 0.75005 0.30453 0.15184  -0.15880 0.03256  516 HIS A C   
2596 O O   . HIS A 313 ? 0.94073 0.79049 0.32787 0.17689  -0.17464 0.02966  516 HIS A O   
2597 C CB  . HIS A 313 ? 0.99037 0.82622 0.32767 0.13157  -0.14734 0.03541  516 HIS A CB  
2598 C CG  . HIS A 313 ? 1.14055 0.95877 0.44688 0.10647  -0.12855 0.04104  516 HIS A CG  
2599 N ND1 . HIS A 313 ? 1.11658 0.87803 0.36972 0.10236  -0.11777 0.06024  516 HIS A ND1 
2600 C CD2 . HIS A 313 ? 1.02602 0.87555 0.34826 0.08407  -0.11682 0.02862  516 HIS A CD2 
2601 C CE1 . HIS A 313 ? 1.16378 0.92483 0.40344 0.07830  -0.10010 0.05969  516 HIS A CE1 
2602 N NE2 . HIS A 313 ? 1.17685 0.99063 0.45719 0.06725  -0.09909 0.04065  516 HIS A NE2 
2603 N N   . ASP A 314 ? 0.85317 0.70959 0.29029 0.14529  -0.15580 0.02660  517 ASP A N   
2604 C CA  . ASP A 314 ? 0.82245 0.70819 0.30065 0.16533  -0.16916 0.01598  517 ASP A CA  
2605 C C   . ASP A 314 ? 0.90905 0.75610 0.38882 0.16298  -0.16264 0.02744  517 ASP A C   
2606 O O   . ASP A 314 ? 0.83763 0.63632 0.28699 0.14593  -0.14853 0.04280  517 ASP A O   
2607 C CB  . ASP A 314 ? 0.92517 0.87957 0.46192 0.15886  -0.17172 -0.00767 517 ASP A CB  
2608 C CG  . ASP A 314 ? 0.91070 0.90714 0.48651 0.18224  -0.18685 -0.02310 517 ASP A CG  
2609 O OD1 . ASP A 314 ? 0.90518 0.87731 0.46568 0.20424  -0.19527 -0.01545 517 ASP A OD1 
2610 O OD2 . ASP A 314 ? 0.91518 0.96889 0.53753 0.17785  -0.18848 -0.04423 517 ASP A OD2 
2611 N N   . THR A 315 ? 0.78698 0.65629 0.30353 0.17875  -0.17167 0.01866  518 THR A N   
2612 C CA  . THR A 315 ? 0.83689 0.67495 0.35939 0.17658  -0.16616 0.02679  518 THR A CA  
2613 C C   . THR A 315 ? 0.87154 0.70696 0.40764 0.14784  -0.15153 0.02912  518 THR A C   
2614 O O   . THR A 315 ? 0.68776 0.57017 0.26038 0.13718  -0.15005 0.01516  518 THR A O   
2615 C CB  . THR A 315 ? 0.78818 0.66186 0.35463 0.19640  -0.17699 0.01305  518 THR A CB  
2616 O OG1 . THR A 315 ? 0.83949 0.71481 0.39061 0.22384  -0.19004 0.01027  518 THR A OG1 
2617 C CG2 . THR A 315 ? 0.78108 0.62282 0.35269 0.19449  -0.17142 0.02048  518 THR A CG2 
2618 N N   . SER A 316 ? 0.76138 0.54164 0.26822 0.13446  -0.13966 0.04539  519 SER A N   
2619 C CA  . SER A 316 ? 0.72308 0.50075 0.24615 0.10871  -0.12661 0.04709  519 SER A CA  
2620 C C   . SER A 316 ? 0.70996 0.51295 0.27815 0.11638  -0.13271 0.03842  519 SER A C   
2621 O O   . SER A 316 ? 0.71990 0.51077 0.29012 0.13535  -0.14019 0.03937  519 SER A O   
2622 C CB  . SER A 316 ? 0.86219 0.57708 0.34696 0.08913  -0.11068 0.06480  519 SER A CB  
2623 O OG  . SER A 316 ? 0.80430 0.52451 0.31790 0.06329  -0.09718 0.06442  519 SER A OG  
2624 N N   . PRO A 317 ? 0.61337 0.46056 0.24000 0.09673  -0.12170 0.02722  520 PRO A N   
2625 C CA  . PRO A 317 ? 0.59463 0.46328 0.26861 0.09894  -0.12190 0.02022  520 PRO A CA  
2626 C C   . PRO A 317 ? 0.58945 0.41708 0.25601 0.08394  -0.11115 0.03249  520 PRO A C   
2627 O O   . PRO A 317 ? 0.56226 0.40424 0.26452 0.08419  -0.11021 0.02774  520 PRO A O   
2628 C CB  . PRO A 317 ? 0.55050 0.47761 0.28452 0.08249  -0.11180 0.00469  520 PRO A CB  
2629 C CG  . PRO A 317 ? 0.55083 0.46735 0.26910 0.05934  -0.09762 0.01044  520 PRO A CG  
2630 C CD  . PRO A 317 ? 0.61571 0.49429 0.26862 0.07195  -0.10691 0.02037  520 PRO A CD  
2631 N N   . ILE A 318 ? 0.64869 0.42659 0.26956 0.06989  -0.10237 0.04702  521 ILE A N   
2632 C CA  . ILE A 318 ? 0.63880 0.37767 0.25037 0.05213  -0.09116 0.05700  521 ILE A CA  
2633 C C   . ILE A 318 ? 0.69142 0.36764 0.24519 0.07014  -0.09988 0.06914  521 ILE A C   
2634 O O   . ILE A 318 ? 0.74198 0.39287 0.25571 0.08049  -0.10269 0.07473  521 ILE A O   
2635 C CB  . ILE A 318 ? 0.68154 0.40926 0.28480 0.02020  -0.07222 0.06282  521 ILE A CB  
2636 C CG1 . ILE A 318 ? 0.59546 0.38337 0.25469 0.00526  -0.06328 0.05071  521 ILE A CG1 
2637 C CG2 . ILE A 318 ? 0.71908 0.40858 0.31180 0.00041  -0.06099 0.07113  521 ILE A CG2 
2638 C CD1 . ILE A 318 ? 0.62373 0.40721 0.26984 -0.01923 -0.04729 0.05424  521 ILE A CD1 
2639 N N   . ASN A 319 ? 0.69187 0.34925 0.25236 0.07243  -0.10054 0.07046  522 ASN A N   
2640 C CA  . ASN A 319 ? 0.77112 0.37741 0.29655 0.08257  -0.10050 0.07663  522 ASN A CA  
2641 C C   . ASN A 319 ? 0.75143 0.32392 0.27284 0.05950  -0.08801 0.08137  522 ASN A C   
2642 O O   . ASN A 319 ? 0.72263 0.31560 0.27392 0.04321  -0.08403 0.07937  522 ASN A O   
2643 C CB  . ASN A 319 ? 0.85995 0.48025 0.39836 0.11517  -0.11508 0.06838  522 ASN A CB  
2644 C CG  . ASN A 319 ? 0.96283 0.53320 0.45816 0.12993  -0.11576 0.07365  522 ASN A CG  
2645 O OD1 . ASN A 319 ? 0.97869 0.51165 0.43370 0.12191  -0.10863 0.08257  522 ASN A OD1 
2646 N ND2 . ASN A 319 ? 0.95969 0.52912 0.46241 0.15141  -0.12344 0.06759  522 ASN A ND2 
2647 N N   . ILE A 320 ? 0.81025 0.33114 0.29334 0.05810  -0.08185 0.08682  523 ILE A N   
2648 C CA  . ILE A 320 ? 0.85262 0.33753 0.32595 0.03704  -0.06993 0.08882  523 ILE A CA  
2649 C C   . ILE A 320 ? 0.88062 0.33017 0.33046 0.05858  -0.07547 0.08757  523 ILE A C   
2650 O O   . ILE A 320 ? 0.92473 0.34802 0.34002 0.07589  -0.07880 0.09104  523 ILE A O   
2651 C CB  . ILE A 320 ? 0.93554 0.38971 0.38068 0.00764  -0.05258 0.09499  523 ILE A CB  
2652 C CG1 . ILE A 320 ? 0.96302 0.45403 0.43037 -0.01373 -0.04543 0.09547  523 ILE A CG1 
2653 C CG2 . ILE A 320 ? 0.97525 0.39889 0.41414 -0.01498 -0.04057 0.09361  523 ILE A CG2 
2654 C CD1 . ILE A 320 ? 0.88702 0.38585 0.33587 -0.00386 -0.04827 0.09868  523 ILE A CD1 
2655 N N   . GLU A 321 ? 0.86841 0.31748 0.33565 0.05834  -0.07643 0.08247  524 GLU A N   
2656 C CA  . GLU A 321 ? 0.95027 0.36431 0.39386 0.07619  -0.07962 0.08059  524 GLU A CA  
2657 C C   . GLU A 321 ? 0.90684 0.29705 0.34934 0.05462  -0.06973 0.07854  524 GLU A C   
2658 O O   . GLU A 321 ? 0.89375 0.30904 0.36729 0.03374  -0.06545 0.07596  524 GLU A O   
2659 C CB  . GLU A 321 ? 0.93711 0.38348 0.40513 0.10875  -0.09494 0.07284  524 GLU A CB  
2660 C CG  . GLU A 321 ? 0.95660 0.43357 0.42958 0.13101  -0.10594 0.07179  524 GLU A CG  
2661 C CD  . GLU A 321 ? 1.10435 0.61494 0.60200 0.16169  -0.11945 0.06157  524 GLU A CD  
2662 O OE1 . GLU A 321 ? 1.13296 0.61614 0.60829 0.17972  -0.12236 0.06015  524 GLU A OE1 
2663 O OE2 . GLU A 321 ? 1.11180 0.67712 0.65144 0.16693  -0.12618 0.05405  524 GLU A OE2 
2664 N N   . ARG A 322 ? 0.96691 0.30867 0.37222 0.05984  -0.06608 0.07938  525 ARG A N   
2665 C CA  . ARG A 322 ? 0.99540 0.31194 0.39502 0.04121  -0.05710 0.07611  525 ARG A CA  
2666 C C   . ARG A 322 ? 0.98375 0.29788 0.38790 0.06478  -0.06576 0.07009  525 ARG A C   
2667 O O   . ARG A 322 ? 1.03809 0.35768 0.43830 0.09566  -0.07656 0.06912  525 ARG A O   
2668 C CB  . ARG A 322 ? 1.09131 0.35144 0.44284 0.02410  -0.04304 0.08078  525 ARG A CB  
2669 C CG  . ARG A 322 ? 1.08454 0.34901 0.43515 -0.00569 -0.03088 0.08443  525 ARG A CG  
2670 C CD  . ARG A 322 ? 1.24191 0.45541 0.55221 -0.02880 -0.01419 0.08585  525 ARG A CD  
2671 N NE  . ARG A 322 ? 1.25691 0.46105 0.57341 -0.04753 -0.00718 0.07890  525 ARG A NE  
2672 C CZ  . ARG A 322 ? 1.37377 0.53785 0.66296 -0.03779 -0.00659 0.07712  525 ARG A CZ  
2673 N NH1 . ARG A 322 ? 1.29003 0.42087 0.54559 -0.00767 -0.01320 0.08165  525 ARG A NH1 
2674 N NH2 . ARG A 322 ? 1.36989 0.52845 0.66576 -0.05848 0.00085  0.07016  525 ARG A NH2 
2675 N N   . CYS A 323 ? 1.01926 0.32803 0.43285 0.04945  -0.06066 0.06504  526 CYS A N   
2676 C CA  . CYS A 323 ? 0.98260 0.28504 0.39739 0.06836  -0.06642 0.05901  526 CYS A CA  
2677 C C   . CYS A 323 ? 1.05499 0.31851 0.44827 0.04710  -0.05519 0.05674  526 CYS A C   
2678 O O   . CYS A 323 ? 1.02263 0.29514 0.43030 0.01711  -0.04706 0.05475  526 CYS A O   
2679 C CB  . CYS A 323 ? 0.91183 0.26861 0.37675 0.07798  -0.07591 0.05204  526 CYS A CB  
2680 S SG  . CYS A 323 ? 0.90087 0.29587 0.40688 0.04584  -0.07095 0.05050  526 CYS A SG  
2681 N N   . GLU A 324 ? 1.07696 0.29911 0.43639 0.06267  -0.05465 0.05633  527 GLU A N   
2682 C CA  . GLU A 324 ? 1.12062 0.30193 0.45576 0.04480  -0.04377 0.05354  527 GLU A CA  
2683 C C   . GLU A 324 ? 1.14716 0.32634 0.48784 0.06156  -0.04888 0.04669  527 GLU A C   
2684 O O   . GLU A 324 ? 1.24001 0.38838 0.56375 0.04670  -0.04029 0.04306  527 GLU A O   
2685 C CB  . GLU A 324 ? 1.20501 0.32503 0.48438 0.04256  -0.03376 0.05996  527 GLU A CB  
2686 C CG  . GLU A 324 ? 1.25282 0.36920 0.52300 0.01927  -0.02462 0.06558  527 GLU A CG  
2687 C CD  . GLU A 324 ? 1.31662 0.37097 0.52973 0.01807  -0.01395 0.07199  527 GLU A CD  
2688 O OE1 . GLU A 324 ? 1.42902 0.43985 0.60769 0.03503  -0.01334 0.07247  527 GLU A OE1 
2689 O OE2 . GLU A 324 ? 1.50450 0.55265 0.70619 0.00019  -0.00541 0.07654  527 GLU A OE2 
2690 N N   . THR A 325 ? 1.09299 0.30497 0.45711 0.09108  -0.06168 0.04388  528 THR A N   
2691 C CA  . THR A 325 ? 1.14905 0.36476 0.52201 0.10813  -0.06628 0.03661  528 THR A CA  
2692 C C   . THR A 325 ? 1.10945 0.38742 0.53518 0.11605  -0.07557 0.03029  528 THR A C   
2693 O O   . THR A 325 ? 1.03401 0.34996 0.48620 0.11491  -0.08007 0.03216  528 THR A O   
2694 C CB  . THR A 325 ? 1.23528 0.42451 0.57882 0.14118  -0.07146 0.03808  528 THR A CB  
2695 O OG1 . THR A 325 ? 1.11363 0.34443 0.47982 0.16617  -0.08352 0.03795  528 THR A OG1 
2696 C CG2 . THR A 325 ? 1.26552 0.39311 0.55422 0.13639  -0.06257 0.04620  528 THR A CG2 
2697 N N   . LYS A 326 ? 1.05781 0.34473 0.49775 0.12367  -0.07737 0.02250  529 LYS A N   
2698 C CA  . LYS A 326 ? 1.00961 0.35302 0.49697 0.13397  -0.08496 0.01564  529 LYS A CA  
2699 C C   . LYS A 326 ? 0.98237 0.35850 0.48494 0.16188  -0.09482 0.01552  529 LYS A C   
2700 O O   . LYS A 326 ? 0.92669 0.35065 0.46599 0.16254  -0.09942 0.01376  529 LYS A O   
2701 C CB  . LYS A 326 ? 1.00895 0.35027 0.50211 0.13994  -0.08408 0.00714  529 LYS A CB  
2702 C CG  . LYS A 326 ? 0.88788 0.28336 0.42565 0.15374  -0.09022 -0.00095 529 LYS A CG  
2703 C CD  . LYS A 326 ? 0.89309 0.27918 0.43080 0.15490  -0.08694 -0.00911 529 LYS A CD  
2704 C CE  . LYS A 326 ? 0.85913 0.29775 0.44066 0.16309  -0.09011 -0.01747 529 LYS A CE  
2705 N NZ  . LYS A 326 ? 0.85623 0.33039 0.45808 0.19020  -0.09695 -0.02026 529 LYS A NZ  
2706 N N   . LYS A 327 ? 1.00529 0.35576 0.47895 0.18474  -0.09790 0.01695  530 LYS A N   
2707 C CA  . LYS A 327 ? 1.07446 0.45674 0.56083 0.21184  -0.10794 0.01523  530 LYS A CA  
2708 C C   . LYS A 327 ? 1.01190 0.41042 0.50339 0.20486  -0.11006 0.02119  530 LYS A C   
2709 O O   . LYS A 327 ? 0.93309 0.38242 0.45968 0.21410  -0.11697 0.01698  530 LYS A O   
2710 C CB  . LYS A 327 ? 1.05348 0.39833 0.50126 0.23680  -0.11064 0.01666  530 LYS A CB  
2711 N N   . GLU A 328 ? 0.99456 0.35054 0.45112 0.18751  -0.10312 0.03039  531 GLU A N   
2712 C CA  . GLU A 328 ? 0.95764 0.32677 0.41735 0.17854  -0.10370 0.03648  531 GLU A CA  
2713 C C   . GLU A 328 ? 0.89902 0.31574 0.40443 0.16062  -0.10342 0.03387  531 GLU A C   
2714 O O   . GLU A 328 ? 0.84800 0.30244 0.37658 0.16529  -0.10875 0.03392  531 GLU A O   
2715 C CB  . GLU A 328 ? 1.01330 0.32730 0.42766 0.15907  -0.09352 0.04607  531 GLU A CB  
2716 C CG  . GLU A 328 ? 1.09516 0.35542 0.45826 0.17675  -0.09247 0.05023  531 GLU A CG  
2717 C CD  . GLU A 328 ? 1.18534 0.39376 0.50423 0.15697  -0.08107 0.05949  531 GLU A CD  
2718 O OE1 . GLU A 328 ? 1.13110 0.33948 0.45734 0.12539  -0.07176 0.06116  531 GLU A OE1 
2719 O OE2 . GLU A 328 ? 1.25428 0.42209 0.53039 0.17308  -0.08086 0.06475  531 GLU A OE2 
2720 N N   . PHE A 329 ? 0.86695 0.28214 0.38473 0.14035  -0.09727 0.03137  532 PHE A N   
2721 C CA  . PHE A 329 ? 0.80388 0.26005 0.36165 0.12350  -0.09666 0.02976  532 PHE A CA  
2722 C C   . PHE A 329 ? 0.76252 0.27450 0.36395 0.14307  -0.10489 0.02167  532 PHE A C   
2723 O O   . PHE A 329 ? 0.73854 0.28895 0.36869 0.14078  -0.10749 0.02179  532 PHE A O   
2724 C CB  . PHE A 329 ? 0.84922 0.29123 0.40875 0.09891  -0.08904 0.02778  532 PHE A CB  
2725 C CG  . PHE A 329 ? 0.77704 0.26212 0.37901 0.08708  -0.08979 0.02450  532 PHE A CG  
2726 C CD1 . PHE A 329 ? 0.74606 0.24881 0.36182 0.06963  -0.08782 0.02981  532 PHE A CD1 
2727 C CD2 . PHE A 329 ? 0.77145 0.27802 0.39797 0.09348  -0.09176 0.01627  532 PHE A CD2 
2728 C CE1 . PHE A 329 ? 0.70528 0.24561 0.35876 0.05993  -0.08856 0.02746  532 PHE A CE1 
2729 C CE2 . PHE A 329 ? 0.72977 0.27288 0.39257 0.08394  -0.09206 0.01353  532 PHE A CE2 
2730 C CZ  . PHE A 329 ? 0.72040 0.28009 0.39700 0.06757  -0.09084 0.01938  532 PHE A CZ  
2731 N N   A GLU A 330 ? 0.77587 0.29388 0.38298 0.16173  -0.10800 0.01396  533 GLU A N   
2732 N N   B GLU A 330 ? 0.77747 0.29525 0.38453 0.16151  -0.10793 0.01397  533 GLU A N   
2733 C CA  A GLU A 330 ? 0.76963 0.34286 0.42030 0.17676  -0.11314 0.00452  533 GLU A CA  
2734 C CA  B GLU A 330 ? 0.76966 0.34234 0.41986 0.17698  -0.11314 0.00449  533 GLU A CA  
2735 C C   A GLU A 330 ? 0.74182 0.34398 0.40145 0.19604  -0.12079 0.00253  533 GLU A C   
2736 C C   B GLU A 330 ? 0.74310 0.34473 0.40238 0.19552  -0.12069 0.00277  533 GLU A C   
2737 O O   A GLU A 330 ? 0.70286 0.35545 0.40145 0.19864  -0.12324 -0.00337 533 GLU A O   
2738 O O   B GLU A 330 ? 0.70395 0.35541 0.40186 0.19727  -0.12301 -0.00273 533 GLU A O   
2739 C CB  A GLU A 330 ? 0.77927 0.35119 0.43314 0.18889  -0.11275 -0.00358 533 GLU A CB  
2740 C CB  B GLU A 330 ? 0.78056 0.35118 0.43254 0.19048  -0.11312 -0.00354 533 GLU A CB  
2741 C CG  A GLU A 330 ? 0.77341 0.34073 0.43701 0.17003  -0.10626 -0.00548 533 GLU A CG  
2742 C CG  B GLU A 330 ? 0.77583 0.31090 0.39128 0.20968  -0.11601 -0.00263 533 GLU A CG  
2743 C CD  A GLU A 330 ? 0.76305 0.31517 0.41843 0.17863  -0.10430 -0.01191 533 GLU A CD  
2744 C CD  B GLU A 330 ? 0.80017 0.31418 0.40559 0.21466  -0.11287 -0.00753 533 GLU A CD  
2745 O OE1 A GLU A 330 ? 0.78514 0.32436 0.42372 0.19884  -0.10751 -0.01383 533 GLU A OE1 
2746 O OE1 B GLU A 330 ? 0.78695 0.29268 0.39693 0.19650  -0.10675 -0.00847 533 GLU A OE1 
2747 O OE2 A GLU A 330 ? 0.69851 0.25046 0.36271 0.16532  -0.09965 -0.01511 533 GLU A OE2 
2748 O OE2 B GLU A 330 ? 0.83466 0.34062 0.42712 0.23724  -0.11674 -0.01081 533 GLU A OE2 
2749 N N   . GLN A 331 ? 0.77386 0.34501 0.39731 0.20932  -0.12426 0.00677  534 GLN A N   
2750 C CA  . GLN A 331 ? 0.79004 0.38855 0.41964 0.22707  -0.13235 0.00453  534 GLN A CA  
2751 C C   . GLN A 331 ? 0.76242 0.37767 0.40255 0.21215  -0.13167 0.00991  534 GLN A C   
2752 O O   . GLN A 331 ? 0.72908 0.39161 0.39941 0.21928  -0.13674 0.00386  534 GLN A O   
2753 C CB  . GLN A 331 ? 0.83102 0.38861 0.41528 0.24578  -0.13629 0.00874  534 GLN A CB  
2754 C CG  . GLN A 331 ? 1.03013 0.60859 0.62304 0.27381  -0.14369 -0.00140 534 GLN A CG  
2755 C CD  . GLN A 331 ? 1.18097 0.71018 0.72548 0.29275  -0.14623 0.00314  534 GLN A CD  
2756 O OE1 . GLN A 331 ? 1.17019 0.66367 0.67754 0.29329  -0.14624 0.01240  534 GLN A OE1 
2757 N NE2 . GLN A 331 ? 1.16596 0.69159 0.70938 0.30867  -0.14771 -0.00317 534 GLN A NE2 
2758 N N   . LEU A 332 ? 0.75010 0.32950 0.36768 0.18947  -0.12454 0.02019  535 LEU A N   
2759 C CA  . LEU A 332 ? 0.73706 0.33008 0.36245 0.17370  -0.12293 0.02609  535 LEU A CA  
2760 C C   . LEU A 332 ? 0.71861 0.36169 0.39321 0.16445  -0.12232 0.02045  535 LEU A C   
2761 O O   . LEU A 332 ? 0.68104 0.36198 0.37883 0.16580  -0.12566 0.01846  535 LEU A O   
2762 C CB  . LEU A 332 ? 0.79119 0.33360 0.38034 0.14937  -0.11359 0.03731  535 LEU A CB  
2763 C CG  . LEU A 332 ? 0.89882 0.44221 0.48482 0.12824  -0.10886 0.04547  535 LEU A CG  
2764 C CD1 . LEU A 332 ? 0.93784 0.50287 0.52273 0.14378  -0.11613 0.04604  535 LEU A CD1 
2765 C CD2 . LEU A 332 ? 0.97340 0.46062 0.51647 0.10725  -0.09810 0.05405  535 LEU A CD2 
2766 N N   . MET A 333 ? 0.65732 0.30124 0.34755 0.15570  -0.11790 0.01722  536 MET A N   
2767 C CA  . MET A 333 ? 0.62543 0.31379 0.36062 0.14829  -0.11642 0.01200  536 MET A CA  
2768 C C   . MET A 333 ? 0.55372 0.29523 0.32580 0.16733  -0.12122 -0.00014 536 MET A C   
2769 O O   . MET A 333 ? 0.54435 0.32754 0.34939 0.16403  -0.12126 -0.00386 536 MET A O   
2770 C CB  . MET A 333 ? 0.63144 0.30722 0.37148 0.13784  -0.11105 0.01020  536 MET A CB  
2771 C CG  . MET A 333 ? 0.73380 0.37260 0.45170 0.11182  -0.10489 0.01928  536 MET A CG  
2772 S SD  . MET A 333 ? 0.68939 0.36777 0.44095 0.08735  -0.09919 0.02233  536 MET A SD  
2773 C CE  . MET A 333 ? 0.68566 0.42824 0.49334 0.09854  -0.09910 0.01047  536 MET A CE  
2774 N N   . ASN A 334 ? 0.55778 0.29921 0.32515 0.18601  -0.12442 -0.00735 537 ASN A N   
2775 C CA  . ASN A 334 ? 0.54050 0.33274 0.34237 0.20148  -0.12764 -0.02053 537 ASN A CA  
2776 C C   . ASN A 334 ? 0.56596 0.38186 0.37107 0.20916  -0.13394 -0.02239 537 ASN A C   
2777 O O   . ASN A 334 ? 0.57493 0.44030 0.41762 0.20851  -0.13355 -0.03171 537 ASN A O   
2778 C CB  . ASN A 334 ? 0.63287 0.41601 0.42398 0.21963  -0.13024 -0.02691 537 ASN A CB  
2779 C CG  . ASN A 334 ? 0.61071 0.38939 0.41218 0.21349  -0.12364 -0.02982 537 ASN A CG  
2780 O OD1 . ASN A 334 ? 0.61130 0.41580 0.44343 0.20091  -0.11760 -0.03251 537 ASN A OD1 
2781 N ND2 . ASN A 334 ? 0.66461 0.40919 0.43889 0.22280  -0.12438 -0.02927 537 ASN A ND2 
2782 N N   . LYS A 335 ? 0.61421 0.39462 0.37906 0.21581  -0.13884 -0.01427 538 LYS A N   
2783 C CA  . LYS A 335 ? 0.57393 0.37442 0.33767 0.22280  -0.14511 -0.01536 538 LYS A CA  
2784 C C   . LYS A 335 ? 0.58973 0.41558 0.37653 0.20470  -0.14180 -0.01322 538 LYS A C   
2785 O O   . LYS A 335 ? 0.55192 0.42249 0.36504 0.20797  -0.14484 -0.02202 538 LYS A O   
2786 C CB  . LYS A 335 ? 0.63415 0.38452 0.34561 0.22973  -0.14865 -0.00430 538 LYS A CB  
2787 C CG  . LYS A 335 ? 0.73824 0.50604 0.44290 0.23921  -0.15583 -0.00506 538 LYS A CG  
2788 C CD  . LYS A 335 ? 0.84084 0.55513 0.49044 0.24744  -0.15813 0.00633  538 LYS A CD  
2789 C CE  . LYS A 335 ? 0.93696 0.60552 0.55667 0.22354  -0.14922 0.02149  538 LYS A CE  
2790 N NZ  . LYS A 335 ? 0.94548 0.56488 0.51203 0.22920  -0.14951 0.03216  538 LYS A NZ  
2791 N N   . THR A 336 ? 0.53507 0.33366 0.31211 0.18488  -0.13542 -0.00251 539 THR A N   
2792 C CA  . THR A 336 ? 0.50942 0.32910 0.30470 0.16808  -0.13270 0.00060  539 THR A CA  
2793 C C   . THR A 336 ? 0.50252 0.37710 0.35195 0.16619  -0.12952 -0.01197 539 THR A C   
2794 O O   . THR A 336 ? 0.50445 0.41983 0.38053 0.16351  -0.12986 -0.01866 539 THR A O   
2795 C CB  . THR A 336 ? 0.52138 0.29779 0.29182 0.14627  -0.12627 0.01461  539 THR A CB  
2796 O OG1 . THR A 336 ? 0.61440 0.33895 0.33474 0.14516  -0.12566 0.02478  539 THR A OG1 
2797 C CG2 . THR A 336 ? 0.54034 0.34781 0.33699 0.12162  -0.11648 0.01481  539 THR A CG2 
2798 N N   . LEU A 337 ? 0.46574 0.34220 0.33155 0.16653  -0.12471 -0.01651 540 LEU A N   
2799 C CA  . LEU A 337 ? 0.43075 0.35482 0.34562 0.16252  -0.11800 -0.02797 540 LEU A CA  
2800 C C   . LEU A 337 ? 0.45358 0.42299 0.39475 0.17400  -0.11923 -0.04356 540 LEU A C   
2801 O O   . LEU A 337 ? 0.49583 0.50832 0.47438 0.16648  -0.11320 -0.05306 540 LEU A O   
2802 C CB  . LEU A 337 ? 0.40763 0.31817 0.32680 0.15978  -0.11186 -0.02828 540 LEU A CB  
2803 C CG  . LEU A 337 ? 0.42445 0.30669 0.33184 0.13820  -0.10504 -0.01687 540 LEU A CG  
2804 C CD1 . LEU A 337 ? 0.49829 0.35622 0.39609 0.14073  -0.10338 -0.01703 540 LEU A CD1 
2805 C CD2 . LEU A 337 ? 0.40240 0.32088 0.34588 0.11726  -0.09322 -0.01807 540 LEU A CD2 
2806 N N   . ASP A 338 ? 0.45762 0.41732 0.37893 0.19100  -0.12624 -0.04697 541 ASP A N   
2807 C CA  . ASP A 338 ? 0.47415 0.47619 0.41800 0.20197  -0.12865 -0.06261 541 ASP A CA  
2808 C C   . ASP A 338 ? 0.48043 0.50550 0.42666 0.20315  -0.13402 -0.06640 541 ASP A C   
2809 O O   . ASP A 338 ? 0.49556 0.56305 0.46754 0.20661  -0.13406 -0.08149 541 ASP A O   
2810 C CB  . ASP A 338 ? 0.58157 0.56705 0.50253 0.22210  -0.13587 -0.06533 541 ASP A CB  
2811 C CG  . ASP A 338 ? 0.64661 0.61472 0.56709 0.22212  -0.13062 -0.06450 541 ASP A CG  
2812 O OD1 . ASP A 338 ? 0.66354 0.63798 0.60501 0.20707  -0.12104 -0.06354 541 ASP A OD1 
2813 O OD2 . ASP A 338 ? 0.76229 0.70945 0.65977 0.23800  -0.13603 -0.06477 541 ASP A OD2 
2814 N N   . ASN A 339 ? 0.55659 0.55371 0.47408 0.19946  -0.13828 -0.05359 542 ASN A N   
2815 C CA  . ASN A 339 ? 0.59603 0.61364 0.51236 0.19974  -0.14333 -0.05650 542 ASN A CA  
2816 C C   . ASN A 339 ? 0.54274 0.58213 0.48338 0.17996  -0.13665 -0.05618 542 ASN A C   
2817 O O   . ASN A 339 ? 0.56179 0.60804 0.49293 0.17630  -0.14040 -0.05475 542 ASN A O   
2818 C CB  . ASN A 339 ? 0.58732 0.56026 0.45149 0.20896  -0.15193 -0.04303 542 ASN A CB  
2819 C CG  . ASN A 339 ? 0.70057 0.66518 0.54537 0.23207  -0.15990 -0.04755 542 ASN A CG  
2820 O OD1 . ASN A 339 ? 0.71148 0.63063 0.52249 0.23994  -0.16130 -0.03818 542 ASN A OD1 
2821 N ND2 . ASN A 339 ? 0.75293 0.76178 0.61877 0.24280  -0.16485 -0.06301 542 ASN A ND2 
2822 N N   . LYS A 340 ? 0.43391 0.48392 0.40445 0.16729  -0.12632 -0.05765 543 LYS A N   
2823 C CA  . LYS A 340 ? 0.52647 0.60328 0.52856 0.14699  -0.11530 -0.06060 543 LYS A CA  
2824 C C   . LYS A 340 ? 0.52431 0.57221 0.49908 0.12964  -0.11129 -0.04603 543 LYS A C   
2825 O O   . LYS A 340 ? 0.39350 0.46195 0.37845 0.11835  -0.10662 -0.04973 543 LYS A O   
2826 C CB  . LYS A 340 ? 0.49154 0.62029 0.52825 0.14614  -0.11245 -0.07943 543 LYS A CB  
2827 C CG  . LYS A 340 ? 0.46930 0.62142 0.53159 0.14880  -0.10527 -0.09361 543 LYS A CG  
2828 C CD  . LYS A 340 ? 0.58161 0.73202 0.62452 0.16957  -0.11721 -0.09929 543 LYS A CD  
2829 C CE  . LYS A 340 ? 0.53821 0.71344 0.60672 0.17001  -0.11043 -0.11348 543 LYS A CE  
2830 N NZ  . LYS A 340 ? 0.58075 0.75885 0.63462 0.19106  -0.12175 -0.12062 543 LYS A NZ  
2831 N N   . ARG A 341 ? 0.48188 0.48154 0.42130 0.12680  -0.11222 -0.03059 544 ARG A N   
2832 C CA  . ARG A 341 ? 0.43981 0.40905 0.35159 0.10898  -0.10699 -0.01696 544 ARG A CA  
2833 C C   . ARG A 341 ? 0.43452 0.39037 0.35606 0.08812  -0.09430 -0.00937 544 ARG A C   
2834 O O   . ARG A 341 ? 0.43639 0.38952 0.36930 0.09120  -0.09288 -0.01068 544 ARG A O   
2835 C CB  . ARG A 341 ? 0.45572 0.37565 0.31203 0.12128  -0.11791 -0.00552 544 ARG A CB  
2836 C CG  . ARG A 341 ? 0.50205 0.43325 0.34229 0.14354  -0.13208 -0.01113 544 ARG A CG  
2837 C CD  . ARG A 341 ? 0.54232 0.42102 0.32663 0.16283  -0.14382 0.00014  544 ARG A CD  
2838 N NE  . ARG A 341 ? 0.57082 0.46694 0.34864 0.18078  -0.15185 -0.00732 544 ARG A NE  
2839 C CZ  . ARG A 341 ? 0.67181 0.54286 0.42310 0.19919  -0.15702 -0.00575 544 ARG A CZ  
2840 N NH1 . ARG A 341 ? 0.66549 0.49056 0.39207 0.20132  -0.15416 0.00257  544 ARG A NH1 
2841 N NH2 . ARG A 341 ? 0.71664 0.61026 0.46619 0.21601  -0.16529 -0.01392 544 ARG A NH2 
2842 N N   . ALA A 342 ? 0.43876 0.38837 0.35554 0.06742  -0.08531 -0.00222 545 ALA A N   
2843 C CA  . ALA A 342 ? 0.40411 0.34148 0.32592 0.04777  -0.07501 0.00522  545 ALA A CA  
2844 C C   . ALA A 342 ? 0.46923 0.35538 0.34617 0.04363  -0.07808 0.01675  545 ALA A C   
2845 O O   . ALA A 342 ? 0.45555 0.31247 0.29413 0.05265  -0.08537 0.02151  545 ALA A O   
2846 C CB  . ALA A 342 ? 0.37439 0.33386 0.31650 0.02790  -0.06292 0.00564  545 ALA A CB  
2847 N N   . ILE A 343 ? 0.42650 0.30085 0.30677 0.02959  -0.07196 0.02085  546 ILE A N   
2848 C CA  . ILE A 343 ? 0.43622 0.26194 0.27812 0.02589  -0.07419 0.02846  546 ILE A CA  
2849 C C   . ILE A 343 ? 0.43299 0.25118 0.27339 -0.00146 -0.06373 0.03369  546 ILE A C   
2850 O O   . ILE A 343 ? 0.40465 0.24918 0.27645 -0.01189 -0.05809 0.03080  546 ILE A O   
2851 C CB  . ILE A 343 ? 0.48800 0.30541 0.33332 0.03810  -0.07905 0.02485  546 ILE A CB  
2852 C CG1 . ILE A 343 ? 0.48760 0.32265 0.34340 0.06476  -0.08811 0.01692  546 ILE A CG1 
2853 C CG2 . ILE A 343 ? 0.53869 0.30058 0.34035 0.03421  -0.08073 0.03157  546 ILE A CG2 
2854 C CD1 . ILE A 343 ? 0.57489 0.40308 0.43444 0.07776  -0.09166 0.01223  546 ILE A CD1 
2855 N N   . GLY A 344 ? 0.45884 0.24092 0.26165 -0.01246 -0.06099 0.04099  547 GLY A N   
2856 C CA  . GLY A 344 ? 0.47482 0.24077 0.26845 -0.03900 -0.05136 0.04475  547 GLY A CA  
2857 C C   . GLY A 344 ? 0.53225 0.24311 0.28418 -0.04019 -0.05361 0.04879  547 GLY A C   
2858 O O   . GLY A 344 ? 0.55136 0.22219 0.26424 -0.02450 -0.05977 0.05340  547 GLY A O   
2859 N N   . ILE A 345 ? 0.49665 0.20462 0.25540 -0.05815 -0.04871 0.04650  548 ILE A N   
2860 C CA  . ILE A 345 ? 0.54966 0.20470 0.27016 -0.06381 -0.04861 0.04828  548 ILE A CA  
2861 C C   . ILE A 345 ? 0.57645 0.21167 0.27953 -0.09584 -0.03629 0.05024  548 ILE A C   
2862 O O   . ILE A 345 ? 0.57781 0.25323 0.31402 -0.11530 -0.02962 0.04602  548 ILE A O   
2863 C CB  . ILE A 345 ? 0.56612 0.23328 0.30666 -0.05964 -0.05302 0.04134  548 ILE A CB  
2864 C CG1 . ILE A 345 ? 0.59163 0.27121 0.34380 -0.02853 -0.06337 0.03865  548 ILE A CG1 
2865 C CG2 . ILE A 345 ? 0.65245 0.26894 0.35736 -0.07227 -0.05037 0.04079  548 ILE A CG2 
2866 C CD1 . ILE A 345 ? 0.60728 0.30008 0.37850 -0.02370 -0.06640 0.03180  548 ILE A CD1 
2867 N N   A PHE A 346 ? 0.64562 0.21889 0.29675 -0.10081 -0.03262 0.05608  549 PHE A N   
2868 N N   B PHE A 346 ? 0.64633 0.21947 0.29712 -0.10164 -0.03221 0.05620  549 PHE A N   
2869 C CA  A PHE A 346 ? 0.67846 0.23588 0.31522 -0.13035 -0.01908 0.05386  549 PHE A CA  
2870 C CA  B PHE A 346 ? 0.67222 0.23439 0.31262 -0.13253 -0.01837 0.05363  549 PHE A CA  
2871 C C   A PHE A 346 ? 0.83979 0.37660 0.46784 -0.13471 -0.01934 0.04707  549 PHE A C   
2872 C C   B PHE A 346 ? 0.84552 0.38186 0.47189 -0.13755 -0.01754 0.04727  549 PHE A C   
2873 O O   A PHE A 346 ? 0.78897 0.28576 0.38617 -0.11642 -0.02413 0.04857  549 PHE A O   
2874 O O   B PHE A 346 ? 0.87128 0.36223 0.46045 -0.12312 -0.01952 0.04948  549 PHE A O   
2875 C CB  A PHE A 346 ? 0.83658 0.35776 0.43220 -0.12954 -0.01216 0.05976  549 PHE A CB  
2876 C CB  B PHE A 346 ? 0.82449 0.36095 0.43155 -0.13762 -0.00918 0.05892  549 PHE A CB  
2877 C CG  A PHE A 346 ? 0.84284 0.34822 0.42310 -0.15632 0.00263  0.05543  549 PHE A CG  
2878 C CG  B PHE A 346 ? 0.84508 0.34473 0.41427 -0.10925 -0.01691 0.06687  549 PHE A CG  
2879 C CD1 A PHE A 346 ? 0.84011 0.38392 0.44820 -0.18206 0.01350  0.05049  549 PHE A CD1 
2880 C CD1 B PHE A 346 ? 0.84404 0.36322 0.42143 -0.08978 -0.02580 0.07208  549 PHE A CD1 
2881 C CD2 A PHE A 346 ? 0.93131 0.38508 0.47007 -0.15462 0.00618  0.05544  549 PHE A CD2 
2882 C CD2 B PHE A 346 ? 0.95618 0.40412 0.48075 -0.10323 -0.01415 0.06842  549 PHE A CD2 
2883 C CE1 A PHE A 346 ? 0.91803 0.44987 0.51320 -0.20570 0.02724  0.04512  549 PHE A CE1 
2884 C CE1 B PHE A 346 ? 0.78904 0.28258 0.33444 -0.06247 -0.03393 0.07724  549 PHE A CE1 
2885 C CE2 A PHE A 346 ? 1.02890 0.46643 0.55208 -0.17991 0.02072  0.05101  549 PHE A CE2 
2886 C CE2 B PHE A 346 ? 0.91927 0.33810 0.41085 -0.07588 -0.02147 0.07466  549 PHE A CE2 
2887 C CZ  A PHE A 346 ? 1.04577 0.52317 0.59765 -0.20566 0.03110  0.04555  549 PHE A CZ  
2888 C CZ  B PHE A 346 ? 0.90021 0.34464 0.40392 -0.05503 -0.03199 0.07847  549 PHE A CZ  
2889 N N   . TRP A 347 ? 0.76637 0.33506 0.42381 -0.15684 -0.01502 0.03870  550 TRP A N   
2890 C CA  . TRP A 347 ? 0.81536 0.36823 0.46481 -0.16503 -0.01415 0.03088  550 TRP A CA  
2891 C C   . TRP A 347 ? 0.74083 0.27167 0.36691 -0.18775 -0.00026 0.02750  550 TRP A C   
2892 O O   . TRP A 347 ? 0.86669 0.41739 0.50194 -0.20483 0.00934  0.02706  550 TRP A O   
2893 C CB  . TRP A 347 ? 0.75033 0.35252 0.44327 -0.17594 -0.01813 0.02216  550 TRP A CB  
2894 C CG  . TRP A 347 ? 0.69529 0.30632 0.40322 -0.15450 -0.03152 0.02207  550 TRP A CG  
2895 C CD1 . TRP A 347 ? 0.80657 0.38653 0.49364 -0.12630 -0.03946 0.02563  550 TRP A CD1 
2896 C CD2 . TRP A 347 ? 0.66527 0.33911 0.42153 -0.15076 -0.03688 0.01633  550 TRP A CD2 
2897 N NE1 . TRP A 347 ? 0.75822 0.37897 0.47909 -0.10761 -0.04807 0.02161  550 TRP A NE1 
2898 C CE2 . TRP A 347 ? 0.54353 0.21915 0.30470 -0.12197 -0.04642 0.01677  550 TRP A CE2 
2899 C CE3 . TRP A 347 ? 0.63888 0.36741 0.43374 -0.16765 -0.03420 0.01094  550 TRP A CE3 
2900 C CZ2 . TRP A 347 ? 0.62268 0.34786 0.42234 -0.11147 -0.05179 0.01293  550 TRP A CZ2 
2901 C CZ3 . TRP A 347 ? 0.59988 0.37744 0.43225 -0.15425 -0.04127 0.00792  550 TRP A CZ3 
2902 C CH2 . TRP A 347 ? 0.58282 0.35605 0.41563 -0.12724 -0.04922 0.00941  550 TRP A CH2 
2903 N N   . GLN A 348 ? 0.83093 0.32170 0.42790 -0.18830 0.00159  0.02406  551 GLN A N   
2904 C CA  . GLN A 348 ? 0.94370 0.40688 0.51434 -0.20990 0.01567  0.02046  551 GLN A CA  
2905 C C   . GLN A 348 ? 1.05615 0.50308 0.61899 -0.21852 0.01675  0.01129  551 GLN A C   
2906 O O   . GLN A 348 ? 0.98664 0.42023 0.54513 -0.20053 0.00706  0.01085  551 GLN A O   
2907 C CB  . GLN A 348 ? 1.07930 0.48723 0.60087 -0.19842 0.02052  0.02969  551 GLN A CB  
2908 C CG  . GLN A 348 ? 1.12292 0.50712 0.61950 -0.22303 0.03741  0.02719  551 GLN A CG  
2909 C CD  . GLN A 348 ? 1.24273 0.60319 0.71131 -0.21665 0.04242  0.03665  551 GLN A CD  
2910 O OE1 . GLN A 348 ? 1.30228 0.63282 0.74507 -0.19004 0.03446  0.04549  551 GLN A OE1 
2911 N NE2 . GLN A 348 ? 1.15896 0.53582 0.63381 -0.23987 0.05519  0.03400  551 GLN A NE2 
2912 N N   . GLY A 349 ? 1.02768 0.47689 0.58910 -0.24622 0.02911  0.00300  552 GLY A N   
2913 C CA  . GLY A 349 ? 1.11413 0.54761 0.66671 -0.25795 0.03188  -0.00703 552 GLY A CA  
2914 C C   . GLY A 349 ? 1.07126 0.54161 0.64849 -0.28951 0.04114  -0.01973 552 GLY A C   
2915 O O   . GLY A 349 ? 1.08435 0.55829 0.65841 -0.30677 0.05327  -0.02040 552 GLY A O   
2916 N N   . SER A 350 ? 1.08791 0.58727 0.68964 -0.29652 0.03532  -0.03079 553 SER A N   
2917 C CA  . SER A 350 ? 1.06587 0.60804 0.69549 -0.32382 0.04140  -0.04471 553 SER A CA  
2918 C C   . SER A 350 ? 1.12505 0.72987 0.80187 -0.31966 0.02772  -0.05158 553 SER A C   
2919 O O   . SER A 350 ? 1.08450 0.68300 0.76045 -0.30429 0.01644  -0.05177 553 SER A O   
2920 C CB  . SER A 350 ? 1.12827 0.63266 0.72934 -0.34171 0.05101  -0.05465 553 SER A CB  
2921 N N   . LYS A 351 ? 1.23043 0.89522 0.94705 -0.33159 0.02878  -0.05717 554 LYS A N   
2922 C CA  . LYS A 351 ? 1.13739 0.86667 0.89920 -0.33001 0.01701  -0.06547 554 LYS A CA  
2923 C C   . LYS A 351 ? 1.27359 1.03555 1.05248 -0.35562 0.02392  -0.08094 554 LYS A C   
2924 O O   . LYS A 351 ? 1.26595 1.05945 1.06415 -0.36723 0.03171  -0.08336 554 LYS A O   
2925 C CB  . LYS A 351 ? 1.04620 0.82104 0.84211 -0.31633 0.01091  -0.05782 554 LYS A CB  
2926 N N   . GLY A 352 ? 1.35350 1.10793 1.12485 -0.36416 0.02126  -0.09223 555 GLY A N   
2927 C CA  . GLY A 352 ? 1.33992 1.10948 1.11610 -0.39072 0.03018  -0.10755 555 GLY A CA  
2928 C C   . GLY A 352 ? 1.41281 1.12059 1.14574 -0.40654 0.04818  -0.10598 555 GLY A C   
2929 O O   . GLY A 352 ? 1.45437 1.10361 1.14990 -0.39451 0.05173  -0.09336 555 GLY A O   
2930 N N   . ASN A 353 ? 1.35814 1.07954 1.09527 -0.43332 0.05982  -0.11936 556 ASN A N   
2931 C CA  . ASN A 353 ? 1.38446 1.05040 1.08094 -0.45168 0.07933  -0.11922 556 ASN A CA  
2932 C C   . ASN A 353 ? 1.36032 1.02306 1.05296 -0.45179 0.08944  -0.10920 556 ASN A C   
2933 O O   . ASN A 353 ? 1.49441 1.14506 1.17358 -0.47399 0.10632  -0.11482 556 ASN A O   
2934 C CB  . ASN A 353 ? 1.25869 0.94049 0.96060 -0.48220 0.08916  -0.13896 556 ASN A CB  
2935 N N   . ARG A 354 ? 1.31472 0.98738 1.01783 -0.42792 0.08001  -0.09516 557 ARG A N   
2936 C CA  . ARG A 354 ? 1.25327 0.92649 0.95485 -0.42510 0.08745  -0.08550 557 ARG A CA  
2937 C C   . ARG A 354 ? 1.22082 0.84982 0.89472 -0.39910 0.08156  -0.06747 557 ARG A C   
2938 O O   . ARG A 354 ? 1.20910 0.83647 0.88721 -0.37908 0.06731  -0.06271 557 ARG A O   
2939 C CB  . ARG A 354 ? 1.14214 0.89321 0.89819 -0.42279 0.08116  -0.08931 557 ARG A CB  
2940 N N   . PRO A 355 ? 1.21553 0.80829 0.85977 -0.39857 0.09209  -0.05792 558 PRO A N   
2941 C CA  . PRO A 355 ? 1.07546 0.63306 0.69637 -0.37221 0.08504  -0.04135 558 PRO A CA  
2942 C C   . PRO A 355 ? 1.03368 0.64482 0.69736 -0.35371 0.07081  -0.03648 558 PRO A C   
2943 O O   . PRO A 355 ? 1.02854 0.70060 0.73553 -0.36116 0.07016  -0.04308 558 PRO A O   
2944 C CB  . PRO A 355 ? 0.99611 0.51833 0.58380 -0.37939 0.09992  -0.03502 558 PRO A CB  
2945 C CG  . PRO A 355 ? 1.23359 0.79796 0.84719 -0.40640 0.11209  -0.04768 558 PRO A CG  
2946 C CD  . PRO A 355 ? 1.15569 0.74087 0.78710 -0.42154 0.11057  -0.06251 558 PRO A CD  
2947 N N   . TYR A 356 ? 1.06812 0.65557 0.71883 -0.32844 0.05960  -0.02526 559 TYR A N   
2948 C CA  . TYR A 356 ? 0.93994 0.57120 0.62698 -0.31010 0.04636  -0.02045 559 TYR A CA  
2949 C C   . TYR A 356 ? 0.98001 0.58016 0.64380 -0.28920 0.04340  -0.00602 559 TYR A C   
2950 O O   . TYR A 356 ? 0.90593 0.44850 0.52713 -0.27705 0.04253  0.00084  559 TYR A O   
2951 C CB  . TYR A 356 ? 0.92670 0.57132 0.62974 -0.29955 0.03250  -0.02448 559 TYR A CB  
2952 C CG  . TYR A 356 ? 0.85705 0.54593 0.59677 -0.28175 0.01955  -0.02041 559 TYR A CG  
2953 C CD1 . TYR A 356 ? 0.81077 0.56682 0.59849 -0.28767 0.01699  -0.02705 559 TYR A CD1 
2954 C CD2 . TYR A 356 ? 0.91518 0.57855 0.64108 -0.25785 0.00999  -0.01043 559 TYR A CD2 
2955 C CE1 . TYR A 356 ? 0.80803 0.60235 0.62738 -0.27123 0.00626  -0.02317 559 TYR A CE1 
2956 C CE2 . TYR A 356 ? 0.83497 0.53683 0.59328 -0.24330 -0.00059 -0.00733 559 TYR A CE2 
2957 C CZ  . TYR A 356 ? 0.72754 0.49386 0.53178 -0.25068 -0.00192 -0.01343 559 TYR A CZ  
2958 O OH  . TYR A 356 ? 0.67652 0.47912 0.51116 -0.23593 -0.01142 -0.01001 559 TYR A OH  
2959 N N   . GLN A 357 ? 0.93569 0.57540 0.62777 -0.28398 0.04175  -0.00213 560 GLN A N   
2960 C CA  . GLN A 357 ? 0.91867 0.54163 0.59767 -0.26363 0.03690  0.01015  560 GLN A CA  
2961 C C   . GLN A 357 ? 0.82818 0.51216 0.55622 -0.25655 0.02988  0.01007  560 GLN A C   
2962 O O   . GLN A 357 ? 0.78654 0.52133 0.55145 -0.26946 0.03409  0.00223  560 GLN A O   
2963 C CB  . GLN A 357 ? 1.01274 0.60469 0.65924 -0.26968 0.04899  0.01558  560 GLN A CB  
2964 N N   . HIS A 358 ? 0.70679 0.38599 0.43539 -0.23481 0.01921  0.01822  561 HIS A N   
2965 C CA  . HIS A 358 ? 0.69382 0.42787 0.46795 -0.22748 0.01265  0.01788  561 HIS A CA  
2966 C C   . HIS A 358 ? 0.74123 0.45665 0.50438 -0.20476 0.00360  0.02806  561 HIS A C   
2967 O O   . HIS A 358 ? 0.75027 0.42091 0.48226 -0.19016 -0.00350 0.03237  561 HIS A O   
2968 C CB  . HIS A 358 ? 0.68538 0.45307 0.49013 -0.22986 0.00520  0.00929  561 HIS A CB  
2969 C CG  . HIS A 358 ? 0.66552 0.49518 0.51946 -0.22425 0.00037  0.00742  561 HIS A CG  
2970 N ND1 . HIS A 358 ? 0.53907 0.41501 0.42427 -0.23100 0.00780  0.00420  561 HIS A ND1 
2971 C CD2 . HIS A 358 ? 0.58581 0.43785 0.46218 -0.21122 -0.01081 0.00790  561 HIS A CD2 
2972 C CE1 . HIS A 358 ? 0.53817 0.46154 0.46250 -0.22039 0.00158  0.00341  561 HIS A CE1 
2973 N NE2 . HIS A 358 ? 0.58741 0.49782 0.50696 -0.20936 -0.00950 0.00595  561 HIS A NE2 
2974 N N   . ALA A 359 ? 0.52597 0.27613 0.31459 -0.20038 0.00412  0.03116  562 ALA A N   
2975 C CA  . ALA A 359 ? 0.50590 0.25417 0.29476 -0.17533 -0.00503 0.03805  562 ALA A CA  
2976 C C   . ALA A 359 ? 0.45060 0.25192 0.28721 -0.16069 -0.01303 0.03308  562 ALA A C   
2977 O O   . ALA A 359 ? 0.46351 0.31099 0.33674 -0.17191 -0.00916 0.02797  562 ALA A O   
2978 C CB  . ALA A 359 ? 0.55018 0.30760 0.33761 -0.17399 0.00103  0.04286  562 ALA A CB  
2979 N N   . VAL A 360 ? 0.43623 0.23093 0.27165 -0.13479 -0.02349 0.03455  563 VAL A N   
2980 C CA  . VAL A 360 ? 0.38493 0.22416 0.26083 -0.11881 -0.02934 0.03105  563 VAL A CA  
2981 C C   . VAL A 360 ? 0.38073 0.22013 0.25742 -0.09260 -0.03529 0.03355  563 VAL A C   
2982 O O   . VAL A 360 ? 0.44212 0.24636 0.28630 -0.08387 -0.03800 0.03758  563 VAL A O   
2983 C CB  . VAL A 360 ? 0.41403 0.25088 0.29249 -0.11757 -0.03529 0.02636  563 VAL A CB  
2984 C CG1 . VAL A 360 ? 0.42372 0.26497 0.30284 -0.14458 -0.03032 0.02134  563 VAL A CG1 
2985 C CG2 . VAL A 360 ? 0.43809 0.22549 0.27990 -0.10382 -0.04176 0.02791  563 VAL A CG2 
2986 N N   . THR A 361 ? 0.34603 0.22562 0.25948 -0.07967 -0.03708 0.03059  564 THR A N   
2987 C CA  . THR A 361 ? 0.32731 0.21482 0.24832 -0.05719 -0.04147 0.02989  564 THR A CA  
2988 C C   . THR A 361 ? 0.34517 0.22816 0.26846 -0.04072 -0.04851 0.02678  564 THR A C   
2989 O O   . THR A 361 ? 0.33998 0.23755 0.27906 -0.04418 -0.04806 0.02462  564 THR A O   
2990 C CB  . THR A 361 ? 0.32100 0.25366 0.28058 -0.05559 -0.03542 0.02763  564 THR A CB  
2991 O OG1 . THR A 361 ? 0.30903 0.25063 0.27086 -0.07324 -0.02730 0.02933  564 THR A OG1 
2992 C CG2 . THR A 361 ? 0.28076 0.22152 0.24618 -0.03718 -0.03820 0.02489  564 THR A CG2 
2993 N N   . CYS A 362 ? 0.37996 0.24489 0.28751 -0.02188 -0.05510 0.02597  565 CYS A N   
2994 C CA  . CYS A 362 ? 0.36303 0.22727 0.27533 -0.00479 -0.06051 0.02157  565 CYS A CA  
2995 C C   . CYS A 362 ? 0.33128 0.22931 0.27276 0.01118  -0.06019 0.01632  565 CYS A C   
2996 O O   . CYS A 362 ? 0.36360 0.26486 0.30187 0.01899  -0.06237 0.01529  565 CYS A O   
2997 C CB  . CYS A 362 ? 0.39683 0.21494 0.26991 0.00614  -0.06801 0.02259  565 CYS A CB  
2998 S SG  . CYS A 362 ? 0.44018 0.25924 0.32010 0.02768  -0.07342 0.01556  565 CYS A SG  
2999 N N   . TRP A 363 ? 0.30164 0.22425 0.26993 0.01533  -0.05692 0.01237  566 TRP A N   
3000 C CA  . TRP A 363 ? 0.26239 0.21553 0.25909 0.02752  -0.05373 0.00602  566 TRP A CA  
3001 C C   . TRP A 363 ? 0.26586 0.21580 0.26246 0.04518  -0.05769 -0.00050 566 TRP A C   
3002 O O   . TRP A 363 ? 0.25622 0.23163 0.27632 0.05464  -0.05428 -0.00782 566 TRP A O   
3003 C CB  . TRP A 363 ? 0.24529 0.22909 0.27328 0.01923  -0.04364 0.00648  566 TRP A CB  
3004 C CG  . TRP A 363 ? 0.22783 0.22328 0.26320 0.00534  -0.03840 0.01032  566 TRP A CG  
3005 C CD1 . TRP A 363 ? 0.22847 0.22796 0.26635 -0.00932 -0.03498 0.01538  566 TRP A CD1 
3006 C CD2 . TRP A 363 ? 0.23536 0.24259 0.27733 0.00524  -0.03583 0.00786  566 TRP A CD2 
3007 N NE1 . TRP A 363 ? 0.21509 0.22776 0.26167 -0.01822 -0.02935 0.01647  566 TRP A NE1 
3008 C CE2 . TRP A 363 ? 0.23236 0.24798 0.27977 -0.00985 -0.02971 0.01216  566 TRP A CE2 
3009 C CE3 . TRP A 363 ? 0.25558 0.26918 0.29922 0.01657  -0.03864 0.00120  566 TRP A CE3 
3010 C CZ2 . TRP A 363 ? 0.18717 0.21430 0.24000 -0.01426 -0.02515 0.01051  566 TRP A CZ2 
3011 C CZ3 . TRP A 363 ? 0.22965 0.25594 0.27822 0.01178  -0.03530 -0.00074 566 TRP A CZ3 
3012 C CH2 . TRP A 363 ? 0.18349 0.21462 0.23561 -0.00356 -0.02816 0.00419  566 TRP A CH2 
3013 N N   . GLY A 364 ? 0.30297 0.22300 0.27465 0.04904  -0.06351 0.00062  567 GLY A N   
3014 C CA  . GLY A 364 ? 0.31887 0.23598 0.28991 0.06726  -0.06689 -0.00653 567 GLY A CA  
3015 C C   . GLY A 364 ? 0.34910 0.23029 0.29139 0.06827  -0.07143 -0.00499 567 GLY A C   
3016 O O   . GLY A 364 ? 0.36693 0.22701 0.29114 0.05298  -0.07160 0.00085  567 GLY A O   
3017 N N   . ALA A 365 ? 0.36189 0.23773 0.30111 0.08608  -0.07440 -0.01193 568 ALA A N   
3018 C CA  . ALA A 365 ? 0.37897 0.21729 0.28859 0.09038  -0.07861 -0.01235 568 ALA A CA  
3019 C C   . ALA A 365 ? 0.41052 0.26048 0.33251 0.10333  -0.07565 -0.02110 568 ALA A C   
3020 O O   . ALA A 365 ? 0.38035 0.26081 0.32790 0.11534  -0.07280 -0.02835 568 ALA A O   
3021 C CB  . ALA A 365 ? 0.44124 0.24315 0.31805 0.10341  -0.08750 -0.01073 568 ALA A CB  
3022 N N   . ALA A 366 ? 0.40933 0.23445 0.31198 0.09972  -0.07558 -0.02163 569 ALA A N   
3023 C CA  . ALA A 366 ? 0.46640 0.29404 0.37233 0.11186  -0.07262 -0.03002 569 ALA A CA  
3024 C C   . ALA A 366 ? 0.44506 0.23666 0.32295 0.12987  -0.07934 -0.03466 569 ALA A C   
3025 O O   . ALA A 366 ? 0.45793 0.20926 0.30355 0.12647  -0.08491 -0.02963 569 ALA A O   
3026 C CB  . ALA A 366 ? 0.44326 0.26748 0.34396 0.09737  -0.06830 -0.02876 569 ALA A CB  
3027 N N   . TYR A 367 ? 0.44175 0.25050 0.33249 0.14624  -0.07644 -0.04403 570 TYR A N   
3028 C CA  . TYR A 367 ? 0.46951 0.26144 0.34194 0.15916  -0.07932 -0.04786 570 TYR A CA  
3029 C C   . TYR A 367 ? 0.44527 0.23791 0.31832 0.16382  -0.07324 -0.05572 570 TYR A C   
3030 O O   . TYR A 367 ? 0.47081 0.29509 0.36994 0.16276  -0.06517 -0.06080 570 TYR A O   
3031 C CB  . TYR A 367 ? 0.49881 0.32133 0.38951 0.17236  -0.08143 -0.05195 570 TYR A CB  
3032 C CG  . TYR A 367 ? 0.43486 0.25767 0.32217 0.17111  -0.08791 -0.04571 570 TYR A CG  
3033 C CD1 . TYR A 367 ? 0.46387 0.31090 0.37365 0.16071  -0.08568 -0.04291 570 TYR A CD1 
3034 C CD2 . TYR A 367 ? 0.55006 0.34850 0.41042 0.18144  -0.09566 -0.04281 570 TYR A CD2 
3035 C CE1 . TYR A 367 ? 0.48230 0.32971 0.38794 0.15982  -0.09137 -0.03769 570 TYR A CE1 
3036 C CE2 . TYR A 367 ? 0.55144 0.34890 0.40543 0.18093  -0.10112 -0.03719 570 TYR A CE2 
3037 C CZ  . TYR A 367 ? 0.51494 0.33736 0.39191 0.16965  -0.09904 -0.03482 570 TYR A CZ  
3038 O OH  . TYR A 367 ? 0.51906 0.34041 0.38851 0.16915  -0.10429 -0.02947 570 TYR A OH  
3039 N N   . ASP A 368 ? 0.52411 0.28133 0.36764 0.16892  -0.07579 -0.05683 571 ASP A N   
3040 C CA  . ASP A 368 ? 0.55063 0.30912 0.39425 0.17575  -0.07007 -0.06518 571 ASP A CA  
3041 C C   . ASP A 368 ? 0.57805 0.36371 0.43988 0.19300  -0.06938 -0.07182 571 ASP A C   
3042 O O   . ASP A 368 ? 0.54668 0.34995 0.41940 0.19942  -0.07416 -0.07057 571 ASP A O   
3043 C CB  . ASP A 368 ? 0.62434 0.33291 0.42908 0.17174  -0.07187 -0.06469 571 ASP A CB  
3044 C CG  . ASP A 368 ? 0.59796 0.27401 0.37580 0.18101  -0.07774 -0.06139 571 ASP A CG  
3045 O OD1 . ASP A 368 ? 0.60559 0.29931 0.39388 0.19519  -0.08124 -0.06145 571 ASP A OD1 
3046 O OD2 . ASP A 368 ? 0.64459 0.27531 0.38829 0.17389  -0.07844 -0.05936 571 ASP A OD2 
3047 N N   . GLU A 369 ? 0.52322 0.31352 0.38841 0.20025  -0.06342 -0.07995 572 GLU A N   
3048 C CA  . GLU A 369 ? 0.59994 0.41877 0.48524 0.21546  -0.06195 -0.08785 572 GLU A CA  
3049 C C   . GLU A 369 ? 0.59726 0.39543 0.46214 0.23101  -0.07172 -0.08642 572 GLU A C   
3050 O O   . GLU A 369 ? 0.65512 0.48019 0.53710 0.24467  -0.07361 -0.09253 572 GLU A O   
3051 C CB  . GLU A 369 ? 0.56552 0.39015 0.45661 0.21889  -0.05222 -0.09689 572 GLU A CB  
3052 C CG  . GLU A 369 ? 0.56942 0.41730 0.48034 0.20624  -0.04073 -0.09922 572 GLU A CG  
3053 C CD  . GLU A 369 ? 0.57184 0.40982 0.47396 0.20743  -0.03176 -0.10638 572 GLU A CD  
3054 O OE1 . GLU A 369 ? 0.59460 0.44519 0.50701 0.21849  -0.02735 -0.11459 572 GLU A OE1 
3055 O OE2 . GLU A 369 ? 0.60739 0.42456 0.49081 0.19763  -0.02959 -0.10443 572 GLU A OE2 
3056 N N   . ASP A 370 ? 0.59317 0.34320 0.42047 0.22928  -0.07729 -0.07916 573 ASP A N   
3057 C CA  . ASP A 370 ? 0.61778 0.34286 0.42050 0.24334  -0.08589 -0.07560 573 ASP A CA  
3058 C C   . ASP A 370 ? 0.63398 0.36304 0.43510 0.24027  -0.09286 -0.06797 573 ASP A C   
3059 O O   . ASP A 370 ? 0.68438 0.38883 0.46014 0.25093  -0.09988 -0.06355 573 ASP A O   
3060 C CB  . ASP A 370 ? 0.66933 0.33602 0.42917 0.24148  -0.08610 -0.07152 573 ASP A CB  
3061 C CG  . ASP A 370 ? 0.76643 0.42525 0.52320 0.24941  -0.08029 -0.08014 573 ASP A CG  
3062 O OD1 . ASP A 370 ? 0.68212 0.37794 0.46666 0.26105  -0.07741 -0.08893 573 ASP A OD1 
3063 O OD2 . ASP A 370 ? 0.82378 0.43827 0.54953 0.24319  -0.07798 -0.07881 573 ASP A OD2 
3064 N N   . ASN A 371 ? 0.60246 0.36035 0.42843 0.22662  -0.09039 -0.06644 574 ASN A N   
3065 C CA  . ASN A 371 ? 0.60853 0.37216 0.43570 0.22089  -0.09545 -0.05962 574 ASN A CA  
3066 C C   . ASN A 371 ? 0.70892 0.42205 0.49790 0.21037  -0.09838 -0.04868 574 ASN A C   
3067 O O   . ASN A 371 ? 0.69714 0.40369 0.47618 0.20936  -0.10329 -0.04225 574 ASN A O   
3068 C CB  . ASN A 371 ? 0.70751 0.49400 0.54211 0.23790  -0.10258 -0.06308 574 ASN A CB  
3069 C CG  . ASN A 371 ? 0.61310 0.45456 0.48951 0.24325  -0.09891 -0.07466 574 ASN A CG  
3070 O OD1 . ASN A 371 ? 0.61334 0.48089 0.51723 0.23079  -0.09027 -0.07778 574 ASN A OD1 
3071 N ND2 . ASN A 371 ? 0.71448 0.57275 0.59457 0.26149  -0.10487 -0.08138 574 ASN A ND2 
3072 N N   . ASN A 372 ? 0.64593 0.32250 0.41208 0.20120  -0.09471 -0.04712 575 ASN A N   
3073 C CA  . ASN A 372 ? 0.64813 0.28169 0.38353 0.18408  -0.09496 -0.03809 575 ASN A CA  
3074 C C   . ASN A 372 ? 0.62898 0.28361 0.38528 0.16639  -0.09338 -0.03471 575 ASN A C   
3075 O O   . ASN A 372 ? 0.59455 0.28180 0.37992 0.16347  -0.08949 -0.03987 575 ASN A O   
3076 C CB  . ASN A 372 ? 0.66035 0.25363 0.36902 0.17596  -0.09074 -0.03979 575 ASN A CB  
3077 C CG  . ASN A 372 ? 0.70514 0.27632 0.39390 0.19410  -0.09122 -0.04351 575 ASN A CG  
3078 O OD1 . ASN A 372 ? 0.73989 0.29188 0.40823 0.20586  -0.09534 -0.03934 575 ASN A OD1 
3079 N ND2 . ASN A 372 ? 0.72002 0.29220 0.41277 0.19710  -0.08677 -0.05148 575 ASN A ND2 
3080 N N   . ILE A 373 ? 0.59350 0.22893 0.33429 0.15468  -0.09557 -0.02584 576 ILE A N   
3081 C CA  . ILE A 373 ? 0.57480 0.22482 0.33220 0.13665  -0.09422 -0.02180 576 ILE A CA  
3082 C C   . ILE A 373 ? 0.56936 0.19038 0.31019 0.11638  -0.09085 -0.02159 576 ILE A C   
3083 O O   . ILE A 373 ? 0.63399 0.21177 0.34064 0.10589  -0.08973 -0.01857 576 ILE A O   
3084 C CB  . ILE A 373 ? 0.66912 0.31184 0.41717 0.13069  -0.09720 -0.01273 576 ILE A CB  
3085 C CG1 . ILE A 373 ? 0.62823 0.30517 0.39501 0.15005  -0.10143 -0.01529 576 ILE A CG1 
3086 C CG2 . ILE A 373 ? 0.58110 0.23321 0.34299 0.10984  -0.09545 -0.00779 576 ILE A CG2 
3087 C CD1 . ILE A 373 ? 0.60680 0.27831 0.36306 0.14634  -0.10468 -0.00718 576 ILE A CD1 
3088 N N   . ILE A 374 ? 0.56209 0.20752 0.32653 0.10945  -0.08874 -0.02543 577 ILE A N   
3089 C CA  . ILE A 374 ? 0.57517 0.21053 0.33042 0.08904  -0.08503 -0.02797 577 ILE A CA  
3090 C C   . ILE A 374 ? 0.55522 0.22133 0.33021 0.06363  -0.08231 -0.02279 577 ILE A C   
3091 O O   . ILE A 374 ? 0.55056 0.20787 0.31517 0.04385  -0.08094 -0.02458 577 ILE A O   
3092 C CB  . ILE A 374 ? 0.53280 0.18318 0.29861 0.09977  -0.08210 -0.03754 577 ILE A CB  
3093 C CG1 . ILE A 374 ? 0.51841 0.22581 0.32665 0.10412  -0.07817 -0.03798 577 ILE A CG1 
3094 C CG2 . ILE A 374 ? 0.57412 0.20648 0.32614 0.12201  -0.08272 -0.04244 577 ILE A CG2 
3095 C CD1 . ILE A 374 ? 0.53353 0.25717 0.35252 0.11535  -0.07305 -0.04689 577 ILE A CD1 
3096 N N   . CYS A 375 ? 0.49420 0.19687 0.29724 0.06355  -0.08158 -0.01755 578 CYS A N   
3097 C CA  . CYS A 375 ? 0.43841 0.17208 0.26202 0.04241  -0.07854 -0.01307 578 CYS A CA  
3098 C C   . CYS A 375 ? 0.48208 0.23909 0.32509 0.04412  -0.07797 -0.00711 578 CYS A C   
3099 O O   . CYS A 375 ? 0.45171 0.22051 0.30605 0.06289  -0.07914 -0.00874 578 CYS A O   
3100 C CB  . CYS A 375 ? 0.41272 0.18308 0.26120 0.04192  -0.07496 -0.01647 578 CYS A CB  
3101 S SG  . CYS A 375 ? 0.43689 0.23929 0.30293 0.01797  -0.07301 -0.01230 578 CYS A SG  
3102 N N   . LEU A 376 ? 0.42658 0.19256 0.27420 0.02398  -0.07595 -0.00173 579 LEU A N   
3103 C CA  . LEU A 376 ? 0.39817 0.18851 0.26482 0.02223  -0.07404 0.00337  579 LEU A CA  
3104 C C   . LEU A 376 ? 0.36524 0.19837 0.26408 0.01022  -0.06902 0.00481  579 LEU A C   
3105 O O   . LEU A 376 ? 0.37174 0.21018 0.27108 -0.00224 -0.06848 0.00368  579 LEU A O   
3106 C CB  . LEU A 376 ? 0.41186 0.17246 0.25298 0.00992  -0.07449 0.00899  579 LEU A CB  
3107 C CG  . LEU A 376 ? 0.53683 0.24625 0.33817 0.02179  -0.07901 0.00998  579 LEU A CG  
3108 C CD1 . LEU A 376 ? 0.55099 0.23139 0.32607 0.00723  -0.07685 0.01705  579 LEU A CD1 
3109 C CD2 . LEU A 376 ? 0.50291 0.22377 0.31323 0.04943  -0.08380 0.00767  579 LEU A CD2 
3110 N N   . TYR A 377 ? 0.32132 0.18488 0.24604 0.01461  -0.06556 0.00675  580 TYR A N   
3111 C CA  . TYR A 377 ? 0.28463 0.18623 0.23922 0.00633  -0.05978 0.00879  580 TYR A CA  
3112 C C   . TYR A 377 ? 0.33372 0.24263 0.29263 -0.00718 -0.05730 0.01330  580 TYR A C   
3113 O O   . TYR A 377 ? 0.32745 0.23562 0.28674 -0.00172 -0.05690 0.01413  580 TYR A O   
3114 C CB  . TYR A 377 ? 0.28658 0.21604 0.26808 0.02104  -0.05464 0.00610  580 TYR A CB  
3115 C CG  . TYR A 377 ? 0.29667 0.21610 0.26980 0.03150  -0.05595 0.00139  580 TYR A CG  
3116 C CD1 . TYR A 377 ? 0.29325 0.22079 0.26815 0.02701  -0.05436 0.00188  580 TYR A CD1 
3117 C CD2 . TYR A 377 ? 0.31822 0.21841 0.27810 0.04612  -0.05962 -0.00384 580 TYR A CD2 
3118 C CE1 . TYR A 377 ? 0.29930 0.21483 0.26220 0.03553  -0.05526 -0.00289 580 TYR A CE1 
3119 C CE2 . TYR A 377 ? 0.35286 0.24209 0.30333 0.05535  -0.06010 -0.00908 580 TYR A CE2 
3120 C CZ  . TYR A 377 ? 0.33336 0.22991 0.28513 0.04926  -0.05726 -0.00864 580 TYR A CZ  
3121 O OH  . TYR A 377 ? 0.34295 0.22689 0.28242 0.05821  -0.05720 -0.01448 580 TYR A OH  
3122 N N   . ILE A 378 ? 0.28164 0.19782 0.24214 -0.02497 -0.05597 0.01507  581 ILE A N   
3123 C CA  . ILE A 378 ? 0.29698 0.20950 0.25167 -0.04178 -0.05346 0.01801  581 ILE A CA  
3124 C C   . ILE A 378 ? 0.26051 0.21413 0.24696 -0.04931 -0.04758 0.01953  581 ILE A C   
3125 O O   . ILE A 378 ? 0.25606 0.23246 0.25799 -0.05105 -0.04767 0.01858  581 ILE A O   
3126 C CB  . ILE A 378 ? 0.31367 0.19687 0.24079 -0.05933 -0.05560 0.01658  581 ILE A CB  
3127 C CG1 . ILE A 378 ? 0.37027 0.20589 0.26188 -0.05030 -0.06038 0.01554  581 ILE A CG1 
3128 C CG2 . ILE A 378 ? 0.34425 0.22806 0.26830 -0.08022 -0.05020 0.01867  581 ILE A CG2 
3129 C CD1 . ILE A 378 ? 0.41137 0.22306 0.28489 -0.03991 -0.06106 0.01961  581 ILE A CD1 
3130 N N   . ALA A 379 ? 0.25681 0.21900 0.25081 -0.05285 -0.04269 0.02176  582 ALA A N   
3131 C CA  . ALA A 379 ? 0.24280 0.23762 0.26118 -0.06375 -0.03630 0.02271  582 ALA A CA  
3132 C C   . ALA A 379 ? 0.29854 0.28244 0.30170 -0.08591 -0.03521 0.02214  582 ALA A C   
3133 O O   . ALA A 379 ? 0.31782 0.27545 0.29815 -0.09329 -0.03332 0.02379  582 ALA A O   
3134 C CB  . ALA A 379 ? 0.22150 0.23122 0.25541 -0.05806 -0.03001 0.02376  582 ALA A CB  
3135 N N   . GLU A 380 ? 0.25757 0.26124 0.27170 -0.09659 -0.03615 0.01926  583 GLU A N   
3136 C CA  . GLU A 380 ? 0.26909 0.26730 0.27223 -0.12051 -0.03460 0.01566  583 GLU A CA  
3137 C C   . GLU A 380 ? 0.31842 0.36154 0.35321 -0.13017 -0.02863 0.01394  583 GLU A C   
3138 O O   . GLU A 380 ? 0.24777 0.32635 0.30693 -0.12558 -0.03144 0.01187  583 GLU A O   
3139 C CB  . GLU A 380 ? 0.29369 0.28312 0.28531 -0.12546 -0.04162 0.01055  583 GLU A CB  
3140 C CG  . GLU A 380 ? 0.35747 0.30557 0.31452 -0.14517 -0.04097 0.00685  583 GLU A CG  
3141 C CD  . GLU A 380 ? 0.41559 0.37593 0.37683 -0.17260 -0.03344 0.00249  583 GLU A CD  
3142 O OE1 . GLU A 380 ? 0.37896 0.36624 0.36094 -0.17528 -0.02693 0.00467  583 GLU A OE1 
3143 O OE2 . GLU A 380 ? 0.49294 0.43538 0.43635 -0.19302 -0.03279 -0.00437 583 GLU A OE2 
3144 N N   . SER A 381 ? 0.27777 0.31961 0.31101 -0.14225 -0.02031 0.01475  584 SER A N   
3145 C CA  . SER A 381 ? 0.26605 0.35204 0.33169 -0.14815 -0.01338 0.01272  584 SER A CA  
3146 C C   . SER A 381 ? 0.28897 0.40103 0.36720 -0.16150 -0.01358 0.00496  584 SER A C   
3147 O O   . SER A 381 ? 0.25506 0.40331 0.36112 -0.15464 -0.00963 0.00220  584 SER A O   
3148 C CB  . SER A 381 ? 0.26799 0.34472 0.32639 -0.15699 -0.00323 0.01451  584 SER A CB  
3149 O OG  . SER A 381 ? 0.33675 0.38178 0.36514 -0.17475 0.00057  0.01233  584 SER A OG  
3150 N N   . ASN A 382 ? 0.25908 0.34921 0.31537 -0.17577 -0.01778 0.00042  585 ASN A N   
3151 C CA  . ASN A 382 ? 0.28012 0.39422 0.34700 -0.18499 -0.01924 -0.00886 585 ASN A CA  
3152 C C   . ASN A 382 ? 0.30749 0.45342 0.39330 -0.17365 -0.03044 -0.01078 585 ASN A C   
3153 O O   . ASN A 382 ? 0.32140 0.49920 0.42366 -0.17628 -0.03269 -0.01829 585 ASN A O   
3154 C CB  . ASN A 382 ? 0.31222 0.38787 0.34621 -0.20448 -0.01838 -0.01411 585 ASN A CB  
3155 C CG  . ASN A 382 ? 0.39547 0.45104 0.41386 -0.21910 -0.00581 -0.01520 585 ASN A CG  
3156 O OD1 . ASN A 382 ? 0.38878 0.45664 0.41853 -0.21514 0.00145  -0.01203 585 ASN A OD1 
3157 N ND2 . ASN A 382 ? 0.53980 0.56289 0.53025 -0.23607 -0.00260 -0.02007 585 ASN A ND2 
3158 N N   . LEU A 383 ? 0.26119 0.39574 0.34144 -0.15880 -0.03753 -0.00436 586 LEU A N   
3159 C CA  . LEU A 383 ? 0.23552 0.39142 0.32472 -0.14500 -0.04748 -0.00577 586 LEU A CA  
3160 C C   . LEU A 383 ? 0.19005 0.38554 0.31047 -0.12408 -0.04670 -0.00037 586 LEU A C   
3161 O O   . LEU A 383 ? 0.21554 0.40960 0.34541 -0.11543 -0.03879 0.00564  586 LEU A O   
3162 C CB  . LEU A 383 ? 0.25902 0.37398 0.32093 -0.13193 -0.05273 -0.00239 586 LEU A CB  
3163 C CG  . LEU A 383 ? 0.30749 0.37859 0.33500 -0.14923 -0.05411 -0.00787 586 LEU A CG  
3164 C CD1 . LEU A 383 ? 0.35406 0.38829 0.35766 -0.13250 -0.05898 -0.00496 586 LEU A CD1 
3165 C CD2 . LEU A 383 ? 0.40540 0.49569 0.43434 -0.17076 -0.05837 -0.01964 586 LEU A CD2 
3166 N N   . PRO A 384 ? 0.20650 0.43567 0.34091 -0.11494 -0.05468 -0.00253 587 PRO A N   
3167 C CA  . PRO A 384 ? 0.22176 0.49093 0.38581 -0.09711 -0.05293 0.00178  587 PRO A CA  
3168 C C   . PRO A 384 ? 0.16607 0.42263 0.33041 -0.07086 -0.04974 0.01252  587 PRO A C   
3169 O O   . PRO A 384 ? 0.17304 0.44863 0.35838 -0.05880 -0.04289 0.01721  587 PRO A O   
3170 C CB  . PRO A 384 ? 0.21942 0.51897 0.38954 -0.09397 -0.06276 -0.00503 587 PRO A CB  
3171 C CG  . PRO A 384 ? 0.24700 0.52604 0.39154 -0.10497 -0.07237 -0.00947 587 PRO A CG  
3172 C CD  . PRO A 384 ? 0.20262 0.43955 0.32728 -0.12487 -0.06508 -0.01140 587 PRO A CD  
3173 N N   . GLU A 385 ? 0.15115 0.37664 0.29336 -0.06162 -0.05319 0.01562  588 GLU A N   
3174 C CA  . GLU A 385 ? 0.14786 0.36695 0.29247 -0.03768 -0.04896 0.02430  588 GLU A CA  
3175 C C   . GLU A 385 ? 0.18654 0.38195 0.33193 -0.03447 -0.03799 0.02813  588 GLU A C   
3176 O O   . GLU A 385 ? 0.15958 0.33135 0.29266 -0.04690 -0.03656 0.02531  588 GLU A O   
3177 C CB  . GLU A 385 ? 0.20618 0.40653 0.32889 -0.02837 -0.05565 0.02513  588 GLU A CB  
3178 C CG  . GLU A 385 ? 0.20133 0.43070 0.32433 -0.02713 -0.06694 0.02166  588 GLU A CG  
3179 C CD  . GLU A 385 ? 0.31039 0.52056 0.40825 -0.01997 -0.07363 0.02115  588 GLU A CD  
3180 O OE1 . GLU A 385 ? 0.32723 0.50538 0.41149 -0.01140 -0.06790 0.02508  588 GLU A OE1 
3181 O OE2 . GLU A 385 ? 0.42532 0.65496 0.51766 -0.02307 -0.08453 0.01561  588 GLU A OE2 
3182 N N   . ALA A 386 ? 0.15843 0.35992 0.31721 -0.01727 -0.02992 0.03426  589 ALA A N   
3183 C CA  . ALA A 386 ? 0.13802 0.32128 0.29985 -0.01377 -0.01916 0.03601  589 ALA A CA  
3184 C C   . ALA A 386 ? 0.15882 0.31216 0.30253 -0.00636 -0.01932 0.03644  589 ALA A C   
3185 O O   . ALA A 386 ? 0.15736 0.30511 0.30394 0.00790  -0.01220 0.03997  589 ALA A O   
3186 C CB  . ALA A 386 ? 0.16812 0.36786 0.35129 -0.00037 -0.00852 0.04065  589 ALA A CB  
3187 N N   . VAL A 387 ? 0.12500 0.25823 0.24887 -0.01643 -0.02681 0.03221  590 VAL A N   
3188 C CA  . VAL A 387 ? 0.13045 0.23687 0.23595 -0.00998 -0.02883 0.03082  590 VAL A CA  
3189 C C   . VAL A 387 ? 0.16125 0.24356 0.24971 -0.02100 -0.03285 0.02659  590 VAL A C   
3190 O O   . VAL A 387 ? 0.19811 0.28208 0.28431 -0.03566 -0.03476 0.02513  590 VAL A O   
3191 C CB  . VAL A 387 ? 0.15115 0.25529 0.24213 -0.00602 -0.03664 0.03047  590 VAL A CB  
3192 C CG1 . VAL A 387 ? 0.18610 0.31291 0.28810 0.00639  -0.03451 0.03595  590 VAL A CG1 
3193 C CG2 . VAL A 387 ? 0.18444 0.28681 0.26242 -0.02303 -0.04674 0.02528  590 VAL A CG2 
3194 N N   . LEU A 388 ? 0.16230 0.22117 0.23695 -0.01334 -0.03378 0.02446  591 LEU A N   
3195 C CA  . LEU A 388 ? 0.19008 0.22007 0.24036 -0.01991 -0.04029 0.02103  591 LEU A CA  
3196 C C   . LEU A 388 ? 0.25464 0.27202 0.28620 -0.02183 -0.04766 0.01848  591 LEU A C   
3197 O O   . LEU A 388 ? 0.24214 0.26408 0.27482 -0.01114 -0.04740 0.01852  591 LEU A O   
3198 C CB  . LEU A 388 ? 0.22381 0.23700 0.26886 -0.00840 -0.03877 0.01867  591 LEU A CB  
3199 C CG  . LEU A 388 ? 0.18430 0.21222 0.24870 -0.00507 -0.03123 0.01890  591 LEU A CG  
3200 C CD1 . LEU A 388 ? 0.19487 0.20934 0.25289 0.00594  -0.03240 0.01411  591 LEU A CD1 
3201 C CD2 . LEU A 388 ? 0.18775 0.21933 0.25192 -0.01947 -0.03077 0.02093  591 LEU A CD2 
3202 N N   . TYR A 389 ? 0.23973 0.23842 0.25166 -0.03621 -0.05303 0.01572  592 TYR A N   
3203 C CA  . TYR A 389 ? 0.27206 0.25614 0.26399 -0.04142 -0.05969 0.01120  592 TYR A CA  
3204 C C   . TYR A 389 ? 0.30519 0.24892 0.27017 -0.03530 -0.06229 0.00821  592 TYR A C   
3205 O O   . TYR A 389 ? 0.28568 0.20797 0.24007 -0.03556 -0.06136 0.00939  592 TYR A O   
3206 C CB  . TYR A 389 ? 0.27669 0.26403 0.26323 -0.06377 -0.06241 0.00785  592 TYR A CB  
3207 C CG  . TYR A 389 ? 0.24608 0.27687 0.25788 -0.06971 -0.06244 0.00813  592 TYR A CG  
3208 C CD1 . TYR A 389 ? 0.27741 0.33240 0.31215 -0.07188 -0.05651 0.01186  592 TYR A CD1 
3209 C CD2 . TYR A 389 ? 0.27343 0.32202 0.28502 -0.07261 -0.06902 0.00365  592 TYR A CD2 
3210 C CE1 . TYR A 389 ? 0.25616 0.35191 0.31453 -0.07495 -0.05680 0.01156  592 TYR A CE1 
3211 C CE2 . TYR A 389 ? 0.26484 0.35610 0.29943 -0.07555 -0.07071 0.00334  592 TYR A CE2 
3212 C CZ  . TYR A 389 ? 0.25511 0.36975 0.31368 -0.07590 -0.06445 0.00748  592 TYR A CZ  
3213 O OH  . TYR A 389 ? 0.22652 0.38491 0.30887 -0.07638 -0.06628 0.00671  592 TYR A OH  
3214 N N   . PRO A 390 ? 0.28787 0.22008 0.23965 -0.02848 -0.06566 0.00424  593 PRO A N   
3215 C CA  . PRO A 390 ? 0.31175 0.20412 0.23640 -0.02216 -0.06822 0.00026  593 PRO A CA  
3216 C C   . PRO A 390 ? 0.34863 0.20978 0.24613 -0.04024 -0.07150 -0.00331 593 PRO A C   
3217 O O   . PRO A 390 ? 0.36495 0.23458 0.26001 -0.05584 -0.07384 -0.00736 593 PRO A O   
3218 C CB  . PRO A 390 ? 0.32762 0.22274 0.24929 -0.01043 -0.06905 -0.00357 593 PRO A CB  
3219 C CG  . PRO A 390 ? 0.32662 0.25267 0.26022 -0.01938 -0.07061 -0.00288 593 PRO A CG  
3220 C CD  . PRO A 390 ? 0.27314 0.22793 0.23222 -0.02500 -0.06722 0.00321  593 PRO A CD  
3221 N N   . PHE A 391 ? 0.37568 0.19993 0.25133 -0.03801 -0.07140 -0.00241 594 PHE A N   
3222 C CA  . PHE A 391 ? 0.42042 0.20276 0.26298 -0.05341 -0.07230 -0.00572 594 PHE A CA  
3223 C C   . PHE A 391 ? 0.47375 0.21418 0.28869 -0.03689 -0.07461 -0.00874 594 PHE A C   
3224 O O   . PHE A 391 ? 0.47171 0.20033 0.28324 -0.01858 -0.07514 -0.00536 594 PHE A O   
3225 C CB  . PHE A 391 ? 0.44666 0.21562 0.28115 -0.06725 -0.06853 -0.00077 594 PHE A CB  
3226 C CG  . PHE A 391 ? 0.44055 0.24263 0.29475 -0.08983 -0.06555 -0.00148 594 PHE A CG  
3227 C CD1 . PHE A 391 ? 0.38675 0.23605 0.27645 -0.08582 -0.06379 0.00250  594 PHE A CD1 
3228 C CD2 . PHE A 391 ? 0.54960 0.33861 0.38892 -0.11470 -0.06416 -0.00781 594 PHE A CD2 
3229 C CE1 . PHE A 391 ? 0.38150 0.26452 0.29139 -0.10383 -0.06133 0.00112  594 PHE A CE1 
3230 C CE2 . PHE A 391 ? 0.57879 0.40543 0.44043 -0.13495 -0.06175 -0.01049 594 PHE A CE2 
3231 C CZ  . PHE A 391 ? 0.49604 0.37071 0.39353 -0.12808 -0.06075 -0.00563 594 PHE A CZ  
3232 N N   . GLY A 392 ? 0.47770 0.20020 0.27512 -0.04182 -0.07637 -0.01626 595 GLY A N   
3233 C CA  . GLY A 392 ? 0.51184 0.19321 0.28216 -0.02602 -0.07776 -0.02041 595 GLY A CA  
3234 C C   . GLY A 392 ? 0.61085 0.23892 0.34689 -0.02693 -0.07660 -0.01745 595 GLY A C   
3235 O O   . GLY A 392 ? 0.61399 0.22631 0.33752 -0.04818 -0.07345 -0.01523 595 GLY A O   
3236 N N   . VAL A 393 ? 0.58151 0.18023 0.30039 -0.00308 -0.07856 -0.01787 596 VAL A N   
3237 C CA  . VAL A 393 ? 0.64946 0.19166 0.33018 0.00277  -0.07825 -0.01413 596 VAL A CA  
3238 C C   . VAL A 393 ? 0.74168 0.23580 0.38777 0.00302  -0.07673 -0.02153 596 VAL A C   
3239 O O   . VAL A 393 ? 0.77374 0.27338 0.42414 0.01856  -0.07853 -0.02851 596 VAL A O   
3240 C CB  . VAL A 393 ? 0.67305 0.22036 0.35976 0.03276  -0.08247 -0.00940 596 VAL A CB  
3241 C CG1 . VAL A 393 ? 0.89197 0.39501 0.54229 0.04243  -0.08149 -0.00559 596 VAL A CG1 
3242 C CG2 . VAL A 393 ? 0.66384 0.25282 0.37939 0.02880  -0.08234 -0.00253 596 VAL A CG2 
3243 N N   . ARG A 394 ? 0.74688 0.20714 0.36484 -0.01440 -0.07051 -0.01948 597 ARG A N   
3244 C CA  . ARG A 394 ? 0.87884 0.30252 0.46795 -0.01592 -0.06581 -0.02486 597 ARG A CA  
3245 C C   . ARG A 394 ? 0.88828 0.27161 0.44507 -0.01182 -0.06072 -0.01704 597 ARG A C   
3246 O O   . ARG A 394 ? 0.99187 0.37334 0.54496 -0.02193 -0.05815 -0.00945 597 ARG A O   
3247 C CB  . ARG A 394 ? 0.89124 0.31449 0.47752 -0.04769 -0.06141 -0.03371 597 ARG A CB  
3248 C CG  . ARG A 394 ? 0.88506 0.34697 0.49741 -0.05372 -0.06710 -0.04273 597 ARG A CG  
3249 C CD  . ARG A 394 ? 0.98552 0.43927 0.59038 -0.03881 -0.06839 -0.05167 597 ARG A CD  
3250 N NE  . ARG A 394 ? 0.91723 0.40787 0.54245 -0.04420 -0.07389 -0.06049 597 ARG A NE  
3251 C CZ  . ARG A 394 ? 1.04801 0.55284 0.67395 -0.06919 -0.07421 -0.06976 597 ARG A CZ  
3252 N NH1 . ARG A 394 ? 0.99550 0.48158 0.60660 -0.09268 -0.06791 -0.07268 597 ARG A NH1 
3253 N NH2 . ARG A 394 ? 1.01146 0.56398 0.66106 -0.06827 -0.07912 -0.07397 597 ARG A NH2 
3254 N N   A TYR A 395 ? 1.00761 0.35763 0.53930 0.00215  -0.05863 -0.01957 598 TYR A N   
3255 N N   B TYR A 395 ? 1.00694 0.35811 0.53932 0.00468  -0.05919 -0.01873 598 TYR A N   
3256 C CA  A TYR A 395 ? 1.05677 0.36068 0.55091 0.00679  -0.05322 -0.01365 598 TYR A CA  
3257 C CA  B TYR A 395 ? 1.07618 0.38695 0.57461 0.01262  -0.05523 -0.01127 598 TYR A CA  
3258 C C   A TYR A 395 ? 1.12733 0.39313 0.59501 -0.00687 -0.04527 -0.02096 598 TYR A C   
3259 C C   B TYR A 395 ? 1.13791 0.40248 0.60273 -0.00316 -0.04579 -0.01579 598 TYR A C   
3260 O O   A TYR A 395 ? 1.10407 0.37101 0.57529 0.00274  -0.04704 -0.02900 598 TYR A O   
3261 O O   B TYR A 395 ? 1.12773 0.39000 0.59418 -0.00604 -0.04490 -0.02522 598 TYR A O   
3262 C CB  A TYR A 395 ? 1.06058 0.36278 0.55037 0.04320  -0.05958 -0.00923 598 TYR A CB  
3263 C CB  B TYR A 395 ? 1.01045 0.32518 0.50903 0.05002  -0.06238 -0.00822 598 TYR A CB  
3264 C CG  A TYR A 395 ? 0.99609 0.34724 0.52149 0.06002  -0.06850 -0.00666 598 TYR A CG  
3265 C CG  B TYR A 395 ? 1.03493 0.40016 0.57049 0.06594  -0.07108 -0.00606 598 TYR A CG  
3266 C CD1 A TYR A 395 ? 0.91834 0.30746 0.47564 0.07355  -0.07377 -0.01352 598 TYR A CD1 
3267 C CD1 B TYR A 395 ? 0.93410 0.33706 0.50149 0.07911  -0.07596 -0.01307 598 TYR A CD1 
3268 C CD2 A TYR A 395 ? 0.96356 0.32288 0.49006 0.06214  -0.07058 0.00190  598 TYR A CD2 
3269 C CD2 B TYR A 395 ? 0.85055 0.22505 0.38813 0.06768  -0.07326 0.00231  598 TYR A CD2 
3270 C CE1 A TYR A 395 ? 0.89668 0.33123 0.48760 0.08767  -0.08016 -0.01224 598 TYR A CE1 
3271 C CE1 B TYR A 395 ? 0.87285 0.32235 0.47492 0.09245  -0.08207 -0.01216 598 TYR A CE1 
3272 C CE2 A TYR A 395 ? 0.90279 0.30777 0.46281 0.07668  -0.07805 0.00305  598 TYR A CE2 
3273 C CE2 B TYR A 395 ? 0.79635 0.21804 0.36878 0.08172  -0.08055 0.00318  598 TYR A CE2 
3274 C CZ  A TYR A 395 ? 0.93013 0.37285 0.52298 0.08911  -0.08250 -0.00422 598 TYR A CZ  
3275 C CZ  B TYR A 395 ? 0.91672 0.37603 0.52206 0.09382  -0.08458 -0.00435 598 TYR A CZ  
3276 O OH  A TYR A 395 ? 0.82547 0.31466 0.45293 0.10211  -0.08814 -0.00420 598 TYR A OH  
3277 O OH  B TYR A 395 ? 0.70254 0.20990 0.34413 0.10616  -0.08985 -0.00493 598 TYR A OH  
3278 N N   A LYS A 396 ? 1.12118 0.35416 0.56276 -0.03009 -0.03551 -0.01899 599 LYS A N   
3279 N N   B LYS A 396 ? 1.10408 0.33183 0.53789 -0.01458 -0.03783 -0.00970 599 LYS A N   
3280 C CA  A LYS A 396 ? 1.19387 0.39691 0.61539 -0.05167 -0.02632 -0.02773 599 LYS A CA  
3281 C CA  B LYS A 396 ? 1.19595 0.38516 0.60232 -0.03968 -0.02620 -0.01472 599 LYS A CA  
3282 C C   A LYS A 396 ? 1.19092 0.34432 0.57700 -0.03328 -0.02262 -0.02830 599 LYS A C   
3283 C C   B LYS A 396 ? 1.24048 0.39922 0.62780 -0.02685 -0.02476 -0.02152 599 LYS A C   
3284 O O   A LYS A 396 ? 1.17388 0.30256 0.54465 -0.04773 -0.01556 -0.03716 599 LYS A O   
3285 O O   B LYS A 396 ? 1.21611 0.37773 0.60926 -0.04334 -0.02179 -0.03228 599 LYS A O   
3286 C CB  A LYS A 396 ? 1.17732 0.36719 0.58650 -0.08466 -0.01555 -0.02651 599 LYS A CB  
3287 C CB  B LYS A 396 ? 1.26573 0.41595 0.63767 -0.04852 -0.01699 -0.00630 599 LYS A CB  
3288 N N   A GLY A 397 ? 1.15969 0.29938 0.53281 -0.00208 -0.02723 -0.02003 600 GLY A N   
3289 N N   B GLY A 397 ? 1.17634 0.30766 0.54130 0.00284  -0.02705 -0.01623 600 GLY A N   
3290 C CA  A GLY A 397 ? 1.20757 0.30425 0.54942 0.01906  -0.02494 -0.02045 600 GLY A CA  
3291 C CA  B GLY A 397 ? 1.20291 0.30328 0.54848 0.01630  -0.02486 -0.02232 600 GLY A CA  
3292 C C   A GLY A 397 ? 1.20400 0.32753 0.56647 0.05294  -0.03536 -0.02270 600 GLY A C   
3293 C C   B GLY A 397 ? 1.20259 0.32654 0.56573 0.05202  -0.03519 -0.02333 600 GLY A C   
3294 O O   A GLY A 397 ? 1.17612 0.35019 0.57588 0.06027  -0.04383 -0.02345 600 GLY A O   
3295 O O   B GLY A 397 ? 1.17715 0.35130 0.57711 0.06020  -0.04380 -0.02371 600 GLY A O   
3296 N N   . ASN A 398 ? 1.22773 0.31651 0.56531 0.07310  -0.03358 -0.02433 601 ASN A N   
3297 C CA  . ASN A 398 ? 1.22971 0.34173 0.58455 0.10625  -0.04188 -0.02744 601 ASN A CA  
3298 C C   . ASN A 398 ? 1.26333 0.41269 0.63899 0.12833  -0.05205 -0.02028 601 ASN A C   
3299 O O   . ASN A 398 ? 1.36730 0.49576 0.72038 0.13656  -0.05270 -0.01134 601 ASN A O   
3300 C CB  . ASN A 398 ? 1.28149 0.34333 0.59996 0.12472  -0.03751 -0.02839 601 ASN A CB  
3301 C CG  . ASN A 398 ? 1.29674 0.37920 0.63380 0.14927  -0.04200 -0.03697 601 ASN A CG  
3302 O OD1 . ASN A 398 ? 1.32424 0.45303 0.69808 0.14726  -0.04593 -0.04390 601 ASN A OD1 
3303 N ND2 . ASN A 398 ? 1.33084 0.37760 0.64110 0.17265  -0.04056 -0.03677 601 ASN A ND2 
3304 N N   . ILE A 399 ? 1.10170 0.30668 0.51989 0.13707  -0.05943 -0.02489 602 ILE A N   
3305 C CA  . ILE A 399 ? 1.19762 0.44240 0.63914 0.15707  -0.06864 -0.02020 602 ILE A CA  
3306 C C   . ILE A 399 ? 1.08553 0.33249 0.52407 0.19185  -0.07405 -0.02173 602 ILE A C   
3307 O O   . ILE A 399 ? 1.21308 0.48755 0.66460 0.21008  -0.08173 -0.01847 602 ILE A O   
3308 C CB  . ILE A 399 ? 1.02729 0.33207 0.51632 0.15183  -0.07323 -0.02445 602 ILE A CB  
3309 C CG1 . ILE A 399 ? 0.97569 0.30439 0.48710 0.16185  -0.07336 -0.03518 602 ILE A CG1 
3310 C CG2 . ILE A 399 ? 0.96171 0.26817 0.45547 0.11866  -0.06915 -0.02301 602 ILE A CG2 
3311 C CD1 . ILE A 399 ? 0.90284 0.28959 0.45882 0.16089  -0.07710 -0.03886 602 ILE A CD1 
3312 N N   . TYR A 400 ? 1.12398 0.34474 0.54693 0.20122  -0.07031 -0.02760 603 TYR A N   
3313 C CA  . TYR A 400 ? 1.20419 0.42630 0.62416 0.23438  -0.07502 -0.03003 603 TYR A CA  
3314 C C   . TYR A 400 ? 1.28291 0.44928 0.65503 0.24667  -0.07357 -0.02242 603 TYR A C   
3315 O O   . TYR A 400 ? 1.37031 0.54429 0.73948 0.27506  -0.08078 -0.02069 603 TYR A O   
3316 C CB  . TYR A 400 ? 1.15192 0.37731 0.58212 0.23994  -0.07134 -0.04109 603 TYR A CB  
3317 C CG  . TYR A 400 ? 1.07796 0.36037 0.55433 0.23171  -0.07280 -0.04839 603 TYR A CG  
3318 C CD1 . TYR A 400 ? 1.03136 0.36903 0.54543 0.25079  -0.07941 -0.05195 603 TYR A CD1 
3319 C CD2 . TYR A 400 ? 1.05701 0.33859 0.53849 0.20398  -0.06728 -0.05194 603 TYR A CD2 
3320 C CE1 . TYR A 400 ? 0.96770 0.35512 0.52191 0.24284  -0.07906 -0.05814 603 TYR A CE1 
3321 C CE2 . TYR A 400 ? 0.99397 0.32513 0.51406 0.19780  -0.06840 -0.05796 603 TYR A CE2 
3322 C CZ  . TYR A 400 ? 0.95019 0.33266 0.50584 0.21742  -0.07361 -0.06055 603 TYR A CZ  
3323 O OH  . TYR A 400 ? 0.89142 0.32123 0.48378 0.21134  -0.07301 -0.06620 603 TYR A OH  
3324 N N   . GLU A 401 ? 1.39024 0.50167 0.72466 0.22544  -0.06404 -0.01840 604 GLU A N   
3325 C CA  . GLU A 401 ? 1.44943 0.50152 0.73335 0.23186  -0.06003 -0.00986 604 GLU A CA  
3326 C C   . GLU A 401 ? 1.35224 0.39219 0.62351 0.20575  -0.05590 -0.00145 604 GLU A C   
3327 O O   . GLU A 401 ? 1.48436 0.48199 0.72863 0.17952  -0.04470 -0.00018 604 GLU A O   
3328 C CB  . GLU A 401 ? 1.42285 0.41811 0.67193 0.22782  -0.04978 -0.01343 604 GLU A CB  
3329 N N   A GLU A 402 ? 1.43152 0.51042 0.72366 0.21202  -0.06427 0.00323  605 GLU A N   
3330 N N   B GLU A 402 ? 1.42809 0.50664 0.71993 0.21208  -0.06424 0.00327  605 GLU A N   
3331 C CA  A GLU A 402 ? 1.33980 0.41688 0.62791 0.18664  -0.06062 0.01010  605 GLU A CA  
3332 C CA  B GLU A 402 ? 1.34068 0.41779 0.62885 0.18660  -0.06061 0.01007  605 GLU A CA  
3333 C C   A GLU A 402 ? 1.44100 0.45193 0.67385 0.18069  -0.05148 0.01854  605 GLU A C   
3334 C C   B GLU A 402 ? 1.43965 0.45132 0.67288 0.18073  -0.05163 0.01864  605 GLU A C   
3335 O O   A GLU A 402 ? 1.43363 0.41339 0.63483 0.20651  -0.05359 0.02272  605 GLU A O   
3336 O O   B GLU A 402 ? 1.43112 0.41309 0.63338 0.20671  -0.05407 0.02306  605 GLU A O   
3337 C CB  A GLU A 402 ? 1.26885 0.39827 0.58798 0.19803  -0.07138 0.01297  605 GLU A CB  
3338 C CB  B GLU A 402 ? 1.27012 0.40044 0.59016 0.19779  -0.07140 0.01278  605 GLU A CB  
3339 C CG  A GLU A 402 ? 1.20753 0.39927 0.58034 0.18725  -0.07575 0.00673  605 GLU A CG  
3340 C CG  B GLU A 402 ? 1.22186 0.41731 0.59689 0.19793  -0.07792 0.00478  605 GLU A CG  
3341 C CD  A GLU A 402 ? 1.17765 0.39617 0.56727 0.17161  -0.07739 0.01214  605 GLU A CD  
3342 C CD  B GLU A 402 ? 1.16900 0.41529 0.57454 0.20891  -0.08751 0.00659  605 GLU A CD  
3343 O OE1 A GLU A 402 ? 1.16987 0.41011 0.56610 0.18898  -0.08505 0.01557  605 GLU A OE1 
3344 O OE1 B GLU A 402 ? 1.25402 0.48578 0.63799 0.21622  -0.08980 0.01391  605 GLU A OE1 
3345 O OE2 A GLU A 402 ? 1.09038 0.30842 0.48630 0.14154  -0.07086 0.01238  605 GLU A OE2 
3346 O OE2 B GLU A 402 ? 1.08184 0.38176 0.53195 0.21001  -0.09210 0.00025  605 GLU A OE2 
3347 N N   . ALA A 403 ? 1.52636 0.51599 0.74727 0.14615  -0.04061 0.02041  606 ALA A N   
3348 C CA  . ALA A 403 ? 1.59497 0.52507 0.76576 0.13467  -0.02954 0.02808  606 ALA A CA  
3349 C C   . ALA A 403 ? 1.61242 0.55812 0.78400 0.13347  -0.03285 0.03651  606 ALA A C   
3350 O O   . ALA A 403 ? 1.55119 0.55358 0.76449 0.13449  -0.04202 0.03557  606 ALA A O   
3351 C CB  . ALA A 403 ? 1.48118 0.38306 0.64018 0.09584  -0.01462 0.02386  606 ALA A CB  
3352 N N   . GLU A 404 ? 1.57767 0.47039 0.70105 0.13088  -0.02435 0.04459  607 GLU A N   
3353 C CA  . GLU A 404 ? 1.60343 0.50428 0.72101 0.13176  -0.02670 0.05281  607 GLU A CA  
3354 C C   . GLU A 404 ? 1.43786 0.38426 0.59385 0.10196  -0.02549 0.05148  607 GLU A C   
3355 O O   . GLU A 404 ? 1.48315 0.45775 0.65225 0.10682  -0.03165 0.05617  607 GLU A O   
3356 C CB  . GLU A 404 ? 1.60197 0.43246 0.65838 0.12623  -0.01380 0.06089  607 GLU A CB  
3357 N N   . LYS A 405 ? 1.49753 0.45215 0.67155 0.07168  -0.01776 0.04478  608 LYS A N   
3358 C CA  . LYS A 405 ? 1.44509 0.44749 0.65969 0.04471  -0.01745 0.04222  608 LYS A CA  
3359 C C   . LYS A 405 ? 1.41486 0.45151 0.66742 0.03741  -0.02099 0.03224  608 LYS A C   
3360 O O   . LYS A 405 ? 1.49193 0.50086 0.73060 0.02558  -0.01327 0.02631  608 LYS A O   
3361 C CB  . LYS A 405 ? 1.43659 0.41212 0.63018 0.00791  -0.00138 0.04390  608 LYS A CB  
3362 N N   . ASN A 406 ? 1.25195 0.34739 0.55098 0.04448  -0.03212 0.02998  609 ASN A N   
3363 C CA  . ASN A 406 ? 1.29415 0.42528 0.63016 0.03892  -0.03601 0.02082  609 ASN A CA  
3364 C C   . ASN A 406 ? 1.12867 0.31538 0.50793 0.02730  -0.04113 0.02095  609 ASN A C   
3365 O O   . ASN A 406 ? 1.10307 0.33175 0.51466 0.04652  -0.05183 0.01955  609 ASN A O   
3366 C CB  . ASN A 406 ? 1.33516 0.47560 0.67941 0.07222  -0.04546 0.01679  609 ASN A CB  
3367 C CG  . ASN A 406 ? 1.17718 0.34395 0.55105 0.06590  -0.04702 0.00662  609 ASN A CG  
3368 O OD1 . ASN A 406 ? 1.27164 0.43541 0.64893 0.03692  -0.03993 0.00171  609 ASN A OD1 
3369 N ND2 . ASN A 406 ? 1.21082 0.40547 0.60651 0.09278  -0.05601 0.00240  609 ASN A ND2 
3370 N N   . ARG A 407 ? 1.08776 0.27487 0.46756 -0.00476 -0.03243 0.02205  610 ARG A N   
3371 C CA  . ARG A 407 ? 1.12942 0.36333 0.54452 -0.01703 -0.03553 0.02383  610 ARG A CA  
3372 C C   . ARG A 407 ? 0.97118 0.25309 0.43028 -0.01462 -0.04378 0.01695  610 ARG A C   
3373 O O   . ARG A 407 ? 1.02036 0.29958 0.48305 -0.01416 -0.04428 0.00915  610 ARG A O   
3374 C CB  . ARG A 407 ? 1.12721 0.35673 0.53838 -0.05465 -0.02322 0.02343  610 ARG A CB  
3375 C CG  . ARG A 407 ? 1.12029 0.29928 0.48580 -0.06250 -0.01178 0.02903  610 ARG A CG  
3376 C CD  . ARG A 407 ? 1.12225 0.29029 0.46994 -0.03596 -0.01749 0.03874  610 ARG A CD  
3377 N NE  . ARG A 407 ? 1.13934 0.34845 0.51454 -0.03960 -0.02139 0.04293  610 ARG A NE  
3378 C CZ  . ARG A 407 ? 1.16261 0.36541 0.52641 -0.05830 -0.01241 0.04751  610 ARG A CZ  
3379 N NH1 . ARG A 407 ? 1.25721 0.41633 0.58444 -0.07696 0.00160  0.04796  610 ARG A NH1 
3380 N NH2 . ARG A 407 ? 1.06842 0.30929 0.45773 -0.05863 -0.01661 0.05126  610 ARG A NH2 
3381 N N   . THR A 408 ? 1.01356 0.33821 0.50481 -0.01442 -0.04933 0.01976  611 THR A N   
3382 C CA  . THR A 408 ? 0.89133 0.26290 0.42452 -0.01017 -0.05711 0.01480  611 THR A CA  
3383 C C   . THR A 408 ? 0.81578 0.20976 0.36943 -0.04394 -0.05203 0.01096  611 THR A C   
3384 O O   . THR A 408 ? 0.86199 0.28172 0.43393 -0.05601 -0.05122 0.01503  611 THR A O   
3385 C CB  . THR A 408 ? 0.80244 0.20633 0.35743 0.01214  -0.06575 0.01989  611 THR A CB  
3386 O OG1 . THR A 408 ? 0.86664 0.25159 0.40064 0.04134  -0.07006 0.02214  611 THR A OG1 
3387 C CG2 . THR A 408 ? 0.86954 0.31811 0.46533 0.01996  -0.07270 0.01460  611 THR A CG2 
3388 N N   . TYR A 409 ? 0.83891 0.22680 0.39110 -0.05889 -0.04883 0.00210  612 TYR A N   
3389 C CA  . TYR A 409 ? 0.90940 0.32436 0.48259 -0.09043 -0.04508 -0.00454 612 TYR A CA  
3390 C C   . TYR A 409 ? 0.89038 0.35341 0.50317 -0.08620 -0.05417 -0.00797 612 TYR A C   
3391 O O   . TYR A 409 ? 0.79323 0.26333 0.41484 -0.06000 -0.06197 -0.00796 612 TYR A O   
3392 C CB  . TYR A 409 ? 0.85231 0.24567 0.40913 -0.10671 -0.03924 -0.01448 612 TYR A CB  
3393 C CG  . TYR A 409 ? 0.97908 0.33020 0.50097 -0.12129 -0.02727 -0.01215 612 TYR A CG  
3394 C CD1 . TYR A 409 ? 1.04329 0.40617 0.57036 -0.15261 -0.01788 -0.01426 612 TYR A CD1 
3395 C CD2 . TYR A 409 ? 0.99510 0.29606 0.47905 -0.10287 -0.02477 -0.00810 612 TYR A CD2 
3396 C CE1 . TYR A 409 ? 1.04400 0.36597 0.53710 -0.16644 -0.00525 -0.01263 612 TYR A CE1 
3397 C CE2 . TYR A 409 ? 1.11912 0.37690 0.56719 -0.11593 -0.01293 -0.00563 612 TYR A CE2 
3398 C CZ  . TYR A 409 ? 1.03557 0.30282 0.48771 -0.14820 -0.00278 -0.00792 612 TYR A CZ  
3399 O OH  . TYR A 409 ? 1.22572 0.44835 0.64072 -0.16182 0.01051  -0.00621 612 TYR A OH  
3400 N N   . MET A 410 ? 0.84572 0.34469 0.48340 -0.11210 -0.05251 -0.01174 613 MET A N   
3401 C CA  . MET A 410 ? 0.75724 0.31190 0.43600 -0.11032 -0.05963 -0.01425 613 MET A CA  
3402 C C   . MET A 410 ? 0.83400 0.41126 0.52409 -0.12406 -0.06191 -0.02636 613 MET A C   
3403 O O   . MET A 410 ? 0.79069 0.36103 0.47174 -0.15099 -0.05688 -0.03374 613 MET A O   
3404 C CB  . MET A 410 ? 0.76835 0.36371 0.47429 -0.12460 -0.05612 -0.00894 613 MET A CB  
3405 C CG  . MET A 410 ? 0.71132 0.29595 0.41123 -0.11022 -0.05489 0.00247  613 MET A CG  
3406 S SD  . MET A 410 ? 0.72328 0.33531 0.44602 -0.07168 -0.06353 0.00661  613 MET A SD  
3407 C CE  . MET A 410 ? 0.71021 0.25735 0.38833 -0.04730 -0.06720 0.00723  613 MET A CE  
3408 N N   . PHE A 411 ? 0.81021 0.41998 0.52186 -0.10475 -0.06837 -0.02855 614 PHE A N   
3409 C CA  . PHE A 411 ? 0.73874 0.38413 0.46713 -0.11529 -0.07194 -0.03817 614 PHE A CA  
3410 C C   . PHE A 411 ? 0.77067 0.48175 0.54224 -0.11664 -0.07396 -0.03381 614 PHE A C   
3411 O O   . PHE A 411 ? 0.65792 0.39062 0.44991 -0.09716 -0.07444 -0.02515 614 PHE A O   
3412 C CB  . PHE A 411 ? 0.68749 0.32694 0.40973 -0.09410 -0.07624 -0.04302 614 PHE A CB  
3413 C CG  . PHE A 411 ? 0.76876 0.43742 0.49927 -0.10479 -0.08027 -0.05339 614 PHE A CG  
3414 C CD1 . PHE A 411 ? 0.84363 0.48453 0.54833 -0.12622 -0.07950 -0.06587 614 PHE A CD1 
3415 C CD2 . PHE A 411 ? 0.69595 0.41822 0.45755 -0.09365 -0.08449 -0.05110 614 PHE A CD2 
3416 C CE1 . PHE A 411 ? 0.75506 0.42590 0.46615 -0.13582 -0.08467 -0.07678 614 PHE A CE1 
3417 C CE2 . PHE A 411 ? 0.65918 0.40816 0.42443 -0.10139 -0.08942 -0.06007 614 PHE A CE2 
3418 C CZ  . PHE A 411 ? 0.63166 0.35731 0.37234 -0.12226 -0.09040 -0.07335 614 PHE A CZ  
3419 N N   . ASN A 412 ? 0.60857 0.35103 0.39387 -0.13970 -0.07467 -0.04058 615 ASN A N   
3420 C CA  . ASN A 412 ? 0.70495 0.50572 0.52872 -0.14311 -0.07547 -0.03654 615 ASN A CA  
3421 C C   . ASN A 412 ? 0.63528 0.47909 0.47870 -0.13355 -0.08271 -0.04024 615 ASN A C   
3422 O O   . ASN A 412 ? 0.62904 0.49226 0.47379 -0.14938 -0.08689 -0.05040 615 ASN A O   
3423 C CB  . ASN A 412 ? 0.73114 0.54235 0.55920 -0.17403 -0.07097 -0.04175 615 ASN A CB  
3424 C CG  . ASN A 412 ? 0.76835 0.63825 0.63641 -0.17523 -0.07081 -0.03738 615 ASN A CG  
3425 O OD1 . ASN A 412 ? 0.68958 0.59876 0.58272 -0.15690 -0.07580 -0.03344 615 ASN A OD1 
3426 N ND2 . ASN A 412 ? 0.65157 0.52542 0.52410 -0.19694 -0.06374 -0.03826 615 ASN A ND2 
3427 N N   . TYR A 413 ? 0.50186 0.36047 0.35916 -0.10769 -0.08383 -0.03247 616 TYR A N   
3428 C CA  . TYR A 413 ? 0.44305 0.33254 0.31062 -0.09667 -0.08925 -0.03480 616 TYR A CA  
3429 C C   . TYR A 413 ? 0.47851 0.42201 0.37375 -0.10550 -0.09293 -0.03537 616 TYR A C   
3430 O O   . TYR A 413 ? 0.50482 0.47172 0.40039 -0.10659 -0.09967 -0.04163 616 TYR A O   
3431 C CB  . TYR A 413 ? 0.38974 0.28073 0.26536 -0.06903 -0.08675 -0.02668 616 TYR A CB  
3432 C CG  . TYR A 413 ? 0.44987 0.29589 0.29903 -0.05716 -0.08533 -0.02963 616 TYR A CG  
3433 C CD1 . TYR A 413 ? 0.46870 0.30157 0.29829 -0.05426 -0.08828 -0.03787 616 TYR A CD1 
3434 C CD2 . TYR A 413 ? 0.45008 0.26867 0.29350 -0.04730 -0.08144 -0.02491 616 TYR A CD2 
3435 C CE1 . TYR A 413 ? 0.51167 0.30453 0.31819 -0.04184 -0.08630 -0.04147 616 TYR A CE1 
3436 C CE2 . TYR A 413 ? 0.47537 0.25595 0.29607 -0.03349 -0.08088 -0.02827 616 TYR A CE2 
3437 C CZ  . TYR A 413 ? 0.50419 0.27190 0.30740 -0.03076 -0.08277 -0.03659 616 TYR A CZ  
3438 O OH  . TYR A 413 ? 0.54210 0.27307 0.32396 -0.01571 -0.08150 -0.04070 616 TYR A OH  
3439 N N   . ALA A 414 ? 0.41487 0.37920 0.33214 -0.11138 -0.08897 -0.02975 617 ALA A N   
3440 C CA  . ALA A 414 ? 0.46777 0.48565 0.41356 -0.11729 -0.09223 -0.03064 617 ALA A CA  
3441 C C   . ALA A 414 ? 0.49007 0.52178 0.43136 -0.14229 -0.09761 -0.04451 617 ALA A C   
3442 O O   . ALA A 414 ? 0.47379 0.55189 0.43267 -0.14244 -0.10485 -0.04879 617 ALA A O   
3443 C CB  . ALA A 414 ? 0.47094 0.50496 0.43981 -0.11945 -0.08532 -0.02326 617 ALA A CB  
3444 N N   . LEU A 415 ? 0.49710 0.48928 0.41422 -0.16326 -0.09401 -0.05225 618 LEU A N   
3445 C CA  . LEU A 415 ? 0.53606 0.53488 0.44529 -0.19008 -0.09739 -0.06815 618 LEU A CA  
3446 C C   . LEU A 415 ? 0.54766 0.51713 0.42703 -0.18912 -0.10244 -0.07718 618 LEU A C   
3447 O O   . LEU A 415 ? 0.66316 0.63968 0.53534 -0.21039 -0.10582 -0.09227 618 LEU A O   
3448 C CB  . LEU A 415 ? 0.54971 0.51944 0.44788 -0.21799 -0.08756 -0.07262 618 LEU A CB  
3449 C CG  . LEU A 415 ? 0.60720 0.59615 0.52901 -0.22077 -0.07935 -0.06414 618 LEU A CG  
3450 C CD1 . LEU A 415 ? 0.69941 0.65447 0.60580 -0.23998 -0.06539 -0.06658 618 LEU A CD1 
3451 C CD2 . LEU A 415 ? 0.58257 0.64183 0.54558 -0.21738 -0.08310 -0.06584 618 LEU A CD2 
3452 N N   . SER A 416 ? 0.66391 0.60262 0.52725 -0.16508 -0.10203 -0.06950 619 SER A N   
3453 C CA  . SER A 416 ? 0.57858 0.48856 0.41337 -0.16030 -0.10565 -0.07749 619 SER A CA  
3454 C C   . SER A 416 ? 0.79694 0.65613 0.59962 -0.18392 -0.10111 -0.08940 619 SER A C   
3455 O O   . SER A 416 ? 0.76578 0.61752 0.55044 -0.19534 -0.10511 -0.10346 619 SER A O   
3456 C CB  . SER A 416 ? 0.67124 0.62620 0.51392 -0.15774 -0.11630 -0.08513 619 SER A CB  
3457 O OG  . SER A 416 ? 0.62739 0.61366 0.48886 -0.13104 -0.11875 -0.07277 619 SER A OG  
3458 N N   . LYS A 417 ? 0.70788 0.52864 0.50016 -0.19115 -0.09208 -0.08395 620 LYS A N   
3459 C CA  . LYS A 417 ? 0.74565 0.51727 0.50893 -0.21028 -0.08383 -0.09218 620 LYS A CA  
3460 C C   . LYS A 417 ? 0.84431 0.56129 0.58643 -0.20266 -0.07517 -0.08097 620 LYS A C   
3461 O O   . LYS A 417 ? 0.75741 0.48507 0.51396 -0.19474 -0.07479 -0.06969 620 LYS A O   
3462 C CB  . LYS A 417 ? 0.86459 0.66881 0.64722 -0.23563 -0.07836 -0.10000 620 LYS A CB  
3463 C CG  . LYS A 417 ? 0.74722 0.56900 0.55047 -0.24304 -0.07146 -0.09121 620 LYS A CG  
3464 C CD  . LYS A 417 ? 0.82655 0.69900 0.65811 -0.26293 -0.06926 -0.10062 620 LYS A CD  
3465 C CE  . LYS A 417 ? 0.85958 0.71359 0.68756 -0.28000 -0.05450 -0.09796 620 LYS A CE  
3466 N NZ  . LYS A 417 ? 1.09273 0.88895 0.88413 -0.29256 -0.04456 -0.10311 620 LYS A NZ  
3467 N N   . PRO A 418 ? 0.82713 0.48824 0.53624 -0.20166 -0.06796 -0.08284 621 PRO A N   
3468 C CA  . PRO A 418 ? 0.81841 0.43137 0.50616 -0.19681 -0.05863 -0.07202 621 PRO A CA  
3469 C C   . PRO A 418 ? 0.94283 0.56814 0.63968 -0.22066 -0.04896 -0.07098 621 PRO A C   
3470 O O   . PRO A 418 ? 0.86199 0.52069 0.57519 -0.24202 -0.04727 -0.08132 621 PRO A O   
3471 C CB  . PRO A 418 ? 0.89717 0.45415 0.54836 -0.19078 -0.05353 -0.07596 621 PRO A CB  
3472 C CG  . PRO A 418 ? 1.06238 0.63771 0.71710 -0.18838 -0.06122 -0.08836 621 PRO A CG  
3473 C CD  . PRO A 418 ? 0.89335 0.53400 0.58239 -0.20433 -0.06777 -0.09475 621 PRO A CD  
3474 N N   . GLU A 419 ? 0.97486 0.57538 0.66137 -0.21536 -0.04273 -0.05887 622 GLU A N   
3475 C CA  . GLU A 419 ? 0.91664 0.51964 0.60438 -0.23583 -0.03132 -0.05698 622 GLU A CA  
3476 C C   . GLU A 419 ? 0.82610 0.36617 0.47366 -0.22811 -0.02237 -0.04741 622 GLU A C   
3477 O O   . GLU A 419 ? 0.85593 0.36638 0.48688 -0.20287 -0.02705 -0.03861 622 GLU A O   
3478 C CB  . GLU A 419 ? 0.87212 0.52529 0.59495 -0.23835 -0.03302 -0.05145 622 GLU A CB  
3479 C CG  . GLU A 419 ? 0.89726 0.61767 0.66044 -0.24592 -0.04122 -0.06073 622 GLU A CG  
3480 C CD  . GLU A 419 ? 0.87572 0.64631 0.67462 -0.24450 -0.04277 -0.05458 622 GLU A CD  
3481 O OE1 . GLU A 419 ? 0.75668 0.52430 0.55886 -0.22660 -0.04782 -0.04449 622 GLU A OE1 
3482 O OE2 . GLU A 419 ? 0.80724 0.62059 0.63151 -0.26061 -0.03857 -0.06055 622 GLU A OE2 
3483 N N   . ASN A 420 ? 0.92480 0.44588 0.55624 -0.24875 -0.00960 -0.04971 623 ASN A N   
3484 C CA  . ASN A 420 ? 1.01598 0.47832 0.60647 -0.24201 -0.00057 -0.04003 623 ASN A CA  
3485 C C   . ASN A 420 ? 1.03155 0.50297 0.62801 -0.23358 -0.00016 -0.02765 623 ASN A C   
3486 O O   . ASN A 420 ? 1.07802 0.53398 0.65927 -0.24557 0.01094  -0.02384 623 ASN A O   
3487 C CB  . ASN A 420 ? 1.03535 0.47142 0.60340 -0.26767 0.01418  -0.04679 623 ASN A CB  
3488 C CG  . ASN A 420 ? 1.25973 0.64670 0.79452 -0.26441 0.01669  -0.05203 623 ASN A CG  
3489 O OD1 . ASN A 420 ? 1.26611 0.66822 0.81130 -0.27691 0.01523  -0.06516 623 ASN A OD1 
3490 N ND2 . ASN A 420 ? 1.37535 0.70451 0.86986 -0.24583 0.01984  -0.04216 623 ASN A ND2 
3491 N N   . ILE A 421 ? 0.82841 0.32406 0.44582 -0.21328 -0.01176 -0.02210 624 ILE A N   
3492 C CA  . ILE A 421 ? 0.94572 0.45425 0.57247 -0.20309 -0.01318 -0.01113 624 ILE A CA  
3493 C C   . ILE A 421 ? 0.93948 0.41504 0.54576 -0.17039 -0.02138 -0.00214 624 ILE A C   
3494 O O   . ILE A 421 ? 0.88564 0.36601 0.50016 -0.15373 -0.03113 -0.00502 624 ILE A O   
3495 C CB  . ILE A 421 ? 0.99678 0.57057 0.67181 -0.20845 -0.01928 -0.01351 624 ILE A CB  
3496 C CG1 . ILE A 421 ? 0.90559 0.51900 0.60400 -0.23740 -0.01119 -0.02268 624 ILE A CG1 
3497 C CG2 . ILE A 421 ? 0.87363 0.45710 0.55735 -0.19409 -0.02187 -0.00222 624 ILE A CG2 
3498 C CD1 . ILE A 421 ? 0.90090 0.58282 0.64808 -0.24047 -0.01743 -0.02589 624 ILE A CD1 
3499 N N   . TYR A 422 ? 0.91540 0.35893 0.49444 -0.16000 -0.01752 0.00764  625 TYR A N   
3500 C CA  . TYR A 422 ? 0.95890 0.37765 0.52066 -0.12649 -0.02606 0.01522  625 TYR A CA  
3501 C C   . TYR A 422 ? 0.97154 0.40321 0.53895 -0.11618 -0.02818 0.02490  625 TYR A C   
3502 O O   . TYR A 422 ? 0.96178 0.41035 0.53751 -0.13541 -0.02076 0.02683  625 TYR A O   
3503 C CB  . TYR A 422 ? 0.90008 0.26095 0.41558 -0.11635 -0.02160 0.01689  625 TYR A CB  
3504 C CG  . TYR A 422 ? 1.00577 0.33671 0.49121 -0.13282 -0.00884 0.02101  625 TYR A CG  
3505 C CD1 . TYR A 422 ? 0.96853 0.28957 0.44574 -0.16298 0.00364  0.01396  625 TYR A CD1 
3506 C CD2 . TYR A 422 ? 1.04893 0.36401 0.51503 -0.11854 -0.00903 0.03097  625 TYR A CD2 
3507 C CE1 . TYR A 422 ? 1.05089 0.34372 0.49979 -0.17878 0.01693  0.01700  625 TYR A CE1 
3508 C CE2 . TYR A 422 ? 1.04773 0.33356 0.48388 -0.13361 0.00338  0.03449  625 TYR A CE2 
3509 C CZ  . TYR A 422 ? 1.14266 0.41647 0.57002 -0.16383 0.01687  0.02760  625 TYR A CZ  
3510 O OH  . TYR A 422 ? 1.17432 0.41804 0.57106 -0.17902 0.03050  0.03049  625 TYR A OH  
3511 N N   . ILE A 423 ? 0.86375 0.28983 0.42740 -0.08465 -0.03819 0.02982  626 ILE A N   
3512 C CA  . ILE A 423 ? 0.81449 0.25514 0.38429 -0.07005 -0.04257 0.03791  626 ILE A CA  
3513 C C   . ILE A 423 ? 0.98843 0.38671 0.51543 -0.06259 -0.03791 0.04439  626 ILE A C   
3514 O O   . ILE A 423 ? 0.96392 0.33119 0.46478 -0.03983 -0.04205 0.04518  626 ILE A O   
3515 C CB  . ILE A 423 ? 0.73535 0.19788 0.32584 -0.03908 -0.05576 0.03771  626 ILE A CB  
3516 C CG1 . ILE A 423 ? 0.69922 0.20072 0.32976 -0.04768 -0.05933 0.03162  626 ILE A CG1 
3517 C CG2 . ILE A 423 ? 0.79035 0.26737 0.38428 -0.02191 -0.06078 0.04484  626 ILE A CG2 
3518 C CD1 . ILE A 423 ? 0.74738 0.28647 0.40897 -0.01977 -0.06928 0.02952  626 ILE A CD1 
3519 N N   A ASP A 424 ? 0.89185 0.28996 0.41176 -0.08135 -0.02889 0.04851  627 ASP A N   
3520 N N   B ASP A 424 ? 0.89352 0.29092 0.41281 -0.08133 -0.02880 0.04854  627 ASP A N   
3521 C CA  A ASP A 424 ? 0.95548 0.31222 0.43265 -0.07526 -0.02379 0.05491  627 ASP A CA  
3522 C CA  B ASP A 424 ? 0.95655 0.31176 0.43252 -0.07400 -0.02412 0.05494  627 ASP A CA  
3523 C C   A ASP A 424 ? 0.91663 0.27987 0.39048 -0.04525 -0.03447 0.06143  627 ASP A C   
3524 C C   B ASP A 424 ? 0.91795 0.28100 0.39169 -0.04437 -0.03481 0.06141  627 ASP A C   
3525 O O   A ASP A 424 ? 0.97828 0.30575 0.41590 -0.02678 -0.03603 0.06554  627 ASP A O   
3526 O O   B ASP A 424 ? 0.97806 0.30602 0.41608 -0.02535 -0.03664 0.06550  627 ASP A O   
3527 C CB  A ASP A 424 ? 0.98709 0.34298 0.45815 -0.10640 -0.00919 0.05567  627 ASP A CB  
3528 C CB  B ASP A 424 ? 0.99052 0.34042 0.45654 -0.10455 -0.00920 0.05598  627 ASP A CB  
3529 C CG  A ASP A 424 ? 1.07469 0.37868 0.49563 -0.10496 -0.00093 0.06091  627 ASP A CG  
3530 C CG  B ASP A 424 ? 1.10566 0.39804 0.51909 -0.10441 -0.00024 0.05981  627 ASP A CG  
3531 O OD1 A ASP A 424 ? 1.16962 0.43072 0.55921 -0.10428 0.00341  0.05901  627 ASP A OD1 
3532 O OD1 B ASP A 424 ? 1.11394 0.36903 0.49930 -0.08493 -0.00425 0.06038  627 ASP A OD1 
3533 O OD2 A ASP A 424 ? 1.04901 0.35332 0.46011 -0.10417 0.00160  0.06695  627 ASP A OD2 
3534 O OD2 B ASP A 424 ? 1.18112 0.46512 0.58066 -0.12331 0.01145  0.06200  627 ASP A OD2 
3535 N N   . GLY A 425 ? 0.83591 0.24519 0.34687 -0.03958 -0.04193 0.06182  628 GLY A N   
3536 C CA  . GLY A 425 ? 0.83889 0.26211 0.35148 -0.01138 -0.05272 0.06586  628 GLY A CA  
3537 C C   . GLY A 425 ? 0.78860 0.26379 0.34361 -0.01281 -0.05770 0.06575  628 GLY A C   
3538 O O   . GLY A 425 ? 0.72210 0.22138 0.30526 -0.03503 -0.05284 0.06326  628 GLY A O   
3539 N N   . LEU A 426 ? 0.73991 0.23395 0.29926 0.01140  -0.06748 0.06777  629 LEU A N   
3540 C CA  . LEU A 426 ? 0.69518 0.23770 0.29123 0.01372  -0.07292 0.06749  629 LEU A CA  
3541 C C   . LEU A 426 ? 0.71135 0.25957 0.29426 0.01172  -0.07114 0.07321  629 LEU A C   
3542 O O   . LEU A 426 ? 0.75118 0.27494 0.30198 0.02527  -0.07299 0.07588  629 LEU A O   
3543 C CB  . LEU A 426 ? 0.65400 0.22845 0.27621 0.04495  -0.08676 0.06059  629 LEU A CB  
3544 C CG  . LEU A 426 ? 0.73257 0.33598 0.39382 0.04684  -0.08808 0.05115  629 LEU A CG  
3545 C CD1 . LEU A 426 ? 0.78532 0.34303 0.42162 0.03653  -0.08383 0.05214  629 LEU A CD1 
3546 C CD2 . LEU A 426 ? 0.67327 0.30030 0.35042 0.07958  -0.10034 0.04436  629 LEU A CD2 
3547 N N   . THR A 427 ? 0.65329 0.25223 0.27681 -0.00504 -0.06478 0.06889  630 THR A N   
3548 C CA  . THR A 427 ? 0.65498 0.27859 0.28170 -0.00292 -0.06460 0.06974  630 THR A CA  
3549 C C   . THR A 427 ? 0.57267 0.25882 0.25177 0.01244  -0.07216 0.05907  630 THR A C   
3550 O O   . THR A 427 ? 0.53777 0.26172 0.26201 0.00259  -0.06775 0.05233  630 THR A O   
3551 C CB  . THR A 427 ? 0.63870 0.27107 0.27138 -0.03507 -0.04884 0.07156  630 THR A CB  
3552 O OG1 . THR A 427 ? 0.72108 0.29227 0.30199 -0.05085 -0.04002 0.08064  630 THR A OG1 
3553 C CG2 . THR A 427 ? 0.62377 0.28661 0.26374 -0.03278 -0.04795 0.07054  630 THR A CG2 
3554 N N   . THR A 428 ? 0.57322 0.26956 0.24502 0.03672  -0.08331 0.05702  631 THR A N   
3555 C CA  . THR A 428 ? 0.54130 0.29312 0.25986 0.05201  -0.09028 0.04503  631 THR A CA  
3556 C C   . THR A 428 ? 0.54963 0.33710 0.28179 0.04996  -0.08907 0.04054  631 THR A C   
3557 O O   . THR A 428 ? 0.54930 0.31340 0.24412 0.04768  -0.08850 0.04731  631 THR A O   
3558 C CB  . THR A 428 ? 0.56616 0.31052 0.27379 0.08389  -0.10553 0.04156  631 THR A CB  
3559 O OG1 . THR A 428 ? 0.67256 0.38603 0.33216 0.10081  -0.11453 0.04809  631 THR A OG1 
3560 C CG2 . THR A 428 ? 0.66792 0.37646 0.36296 0.08619  -0.10572 0.04456  631 THR A CG2 
3561 N N   . LEU A 429 ? 0.49809 0.33975 0.28181 0.04987  -0.08735 0.02886  632 LEU A N   
3562 C CA  . LEU A 429 ? 0.45226 0.33154 0.25427 0.04740  -0.08527 0.02153  632 LEU A CA  
3563 C C   . LEU A 429 ? 0.43047 0.35035 0.26219 0.06807  -0.09510 0.00758  632 LEU A C   
3564 O O   . LEU A 429 ? 0.46171 0.40815 0.33289 0.06879  -0.09229 -0.00017 632 LEU A O   
3565 C CB  . LEU A 429 ? 0.39842 0.30423 0.23527 0.02227  -0.06929 0.01953  632 LEU A CB  
3566 C CG  . LEU A 429 ? 0.39453 0.33752 0.25161 0.01772  -0.06454 0.01083  632 LEU A CG  
3567 C CD1 . LEU A 429 ? 0.44537 0.36565 0.25769 0.01734  -0.06682 0.01639  632 LEU A CD1 
3568 C CD2 . LEU A 429 ? 0.37822 0.34761 0.27410 -0.00349 -0.04834 0.00833  632 LEU A CD2 
3569 N N   . ASP A 430 ? 0.43842 0.36401 0.25036 0.08419  -0.10609 0.00378  633 ASP A N   
3570 C CA  . ASP A 430 ? 0.43023 0.39735 0.26749 0.10414  -0.11688 -0.01161 633 ASP A CA  
3571 C C   . ASP A 430 ? 0.45727 0.47200 0.33120 0.09143  -0.10881 -0.02455 633 ASP A C   
3572 O O   . ASP A 430 ? 0.39432 0.40430 0.25929 0.07416  -0.09954 -0.02025 633 ASP A O   
3573 C CB  . ASP A 430 ? 0.47742 0.42644 0.27104 0.13054  -0.13498 -0.00951 633 ASP A CB  
3574 C CG  . ASP A 430 ? 0.53393 0.52815 0.35368 0.15399  -0.14846 -0.02683 633 ASP A CG  
3575 O OD1 . ASP A 430 ? 0.51597 0.50879 0.34473 0.16969  -0.15398 -0.02973 633 ASP A OD1 
3576 O OD2 . ASP A 430 ? 0.49745 0.52935 0.32917 0.15558  -0.15224 -0.03876 633 ASP A OD2 
3577 N N   . LYS A 431 ? 0.34203 0.40192 0.25786 0.09895  -0.11068 -0.04138 634 LYS A N   
3578 C CA  . LYS A 431 ? 0.33390 0.43774 0.28489 0.08704  -0.10211 -0.05608 634 LYS A CA  
3579 C C   . LYS A 431 ? 0.36541 0.47495 0.28985 0.09028  -0.10941 -0.05933 634 LYS A C   
3580 O O   . LYS A 431 ? 0.35178 0.48164 0.29153 0.07423  -0.09888 -0.06613 634 LYS A O   
3581 C CB  . LYS A 431 ? 0.40390 0.55240 0.39893 0.09570  -0.10361 -0.07516 634 LYS A CB  
3582 C CG  . LYS A 431 ? 0.40014 0.58797 0.43876 0.07852  -0.08858 -0.09022 634 LYS A CG  
3583 C CD  . LYS A 431 ? 0.51100 0.74056 0.58963 0.08650  -0.08940 -0.11021 634 LYS A CD  
3584 C CE  . LYS A 431 ? 0.43213 0.69470 0.55360 0.06763  -0.07114 -0.12547 634 LYS A CE  
3585 N NZ  . LYS A 431 ? 0.43617 0.72390 0.55731 0.06233  -0.07259 -0.13882 634 LYS A NZ  
3586 N N   . GLY A 432 ? 0.37404 0.46547 0.25745 0.11197  -0.12713 -0.05494 635 GLY A N   
3587 C CA  . GLY A 432 ? 0.40512 0.50332 0.25951 0.11827  -0.13614 -0.05845 635 GLY A CA  
3588 C C   . GLY A 432 ? 0.41841 0.57598 0.30745 0.12435  -0.14218 -0.08263 635 GLY A C   
3589 O O   . GLY A 432 ? 0.39429 0.57027 0.27991 0.11574  -0.13998 -0.09042 635 GLY A O   
3590 N N   A GLU A 433 ? 0.39906 0.58653 0.32109 0.13787  -0.14832 -0.09558 636 GLU A N   
3591 N N   B GLU A 433 ? 0.39868 0.58635 0.32115 0.13762  -0.14816 -0.09563 636 GLU A N   
3592 C CA  A GLU A 433 ? 0.43162 0.67138 0.39589 0.13596  -0.14453 -0.11868 636 GLU A CA  
3593 C CA  B GLU A 433 ? 0.43132 0.67152 0.39690 0.13505  -0.14394 -0.11881 636 GLU A CA  
3594 C C   A GLU A 433 ? 0.44777 0.69715 0.38828 0.14755  -0.15487 -0.12373 636 GLU A C   
3595 C C   B GLU A 433 ? 0.44597 0.69688 0.38911 0.14714  -0.15435 -0.12443 636 GLU A C   
3596 O O   A GLU A 433 ? 0.41670 0.69910 0.37431 0.13663  -0.15012 -0.13863 636 GLU A O   
3597 O O   B GLU A 433 ? 0.41509 0.70091 0.37759 0.13684  -0.14958 -0.14027 636 GLU A O   
3598 C CB  A GLU A 433 ? 0.41906 0.67571 0.41686 0.14552  -0.14237 -0.12808 636 GLU A CB  
3599 C CB  B GLU A 433 ? 0.41900 0.67645 0.41983 0.14334  -0.14091 -0.12826 636 GLU A CB  
3600 C CG  A GLU A 433 ? 0.39815 0.70433 0.43854 0.13976  -0.13417 -0.15278 636 GLU A CG  
3601 C CG  B GLU A 433 ? 0.45158 0.74714 0.50561 0.12455  -0.12349 -0.14646 636 GLU A CG  
3602 C CD  A GLU A 433 ? 0.41312 0.73855 0.49173 0.11346  -0.11461 -0.16219 636 GLU A CD  
3603 C CD  B GLU A 433 ? 0.44574 0.73597 0.52437 0.12309  -0.11450 -0.14559 636 GLU A CD  
3604 O OE1 A GLU A 433 ? 0.45709 0.76284 0.53948 0.10207  -0.10713 -0.15049 636 GLU A OE1 
3605 O OE1 B GLU A 433 ? 0.53169 0.79689 0.59088 0.13912  -0.12340 -0.13501 636 GLU A OE1 
3606 O OE2 A GLU A 433 ? 0.46668 0.82468 0.57028 0.10422  -0.10568 -0.18134 636 GLU A OE2 
3607 O OE2 B GLU A 433 ? 0.47567 0.78156 0.58922 0.10501  -0.09687 -0.15470 636 GLU A OE2 
3608 N N   A ASP A 434 ? 0.45644 0.67669 0.35795 0.16979  -0.16818 -0.11208 637 ASP A N   
3609 N N   B ASP A 434 ? 0.45614 0.67641 0.35860 0.16889  -0.16764 -0.11203 637 ASP A N   
3610 C CA  A ASP A 434 ? 0.49396 0.72429 0.37310 0.18307  -0.17893 -0.11662 637 ASP A CA  
3611 C CA  B ASP A 434 ? 0.49349 0.72420 0.37409 0.18241  -0.17843 -0.11677 637 ASP A CA  
3612 C C   A ASP A 434 ? 0.48208 0.70207 0.33193 0.16903  -0.17690 -0.11109 637 ASP A C   
3613 C C   B ASP A 434 ? 0.48122 0.70152 0.33189 0.16885  -0.17673 -0.11123 637 ASP A C   
3614 O O   A ASP A 434 ? 0.49105 0.74084 0.34459 0.16818  -0.17956 -0.12386 637 ASP A O   
3615 O O   B ASP A 434 ? 0.49017 0.74051 0.34478 0.16824  -0.17948 -0.12410 637 ASP A O   
3616 C CB  A ASP A 434 ? 0.54787 0.74215 0.38681 0.20944  -0.19190 -0.10323 637 ASP A CB  
3617 C CB  B ASP A 434 ? 0.54735 0.74254 0.38884 0.20884  -0.19132 -0.10364 637 ASP A CB  
3618 C CG  A ASP A 434 ? 0.60602 0.81400 0.42371 0.22611  -0.20415 -0.10886 637 ASP A CG  
3619 C CG  B ASP A 434 ? 0.62610 0.83388 0.49485 0.22333  -0.19273 -0.11187 637 ASP A CG  
3620 O OD1 A ASP A 434 ? 0.62011 0.87517 0.46989 0.23500  -0.20800 -0.12929 637 ASP A OD1 
3621 O OD1 B ASP A 434 ? 0.58979 0.84344 0.50709 0.21628  -0.18602 -0.13172 637 ASP A OD1 
3622 O OD2 A ASP A 434 ? 0.68253 0.85434 0.45039 0.22970  -0.20918 -0.09337 637 ASP A OD2 
3623 O OD2 B ASP A 434 ? 0.66463 0.83424 0.50436 0.24055  -0.19881 -0.09910 637 ASP A OD2 
3624 N N   . GLN A 435 ? 0.49291 0.67085 0.31214 0.15709  -0.17114 -0.09312 638 GLN A N   
3625 C CA  . GLN A 435 ? 0.57211 0.73841 0.36039 0.14206  -0.16632 -0.08857 638 GLN A CA  
3626 C C   . GLN A 435 ? 0.45796 0.67123 0.28974 0.12025  -0.15432 -0.10913 638 GLN A C   
3627 O O   . GLN A 435 ? 0.47068 0.69985 0.29398 0.11335  -0.15299 -0.11743 638 GLN A O   
3628 C CB  . GLN A 435 ? 0.57089 0.68162 0.31700 0.13247  -0.15960 -0.06623 638 GLN A CB  
3629 C CG  . GLN A 435 ? 0.60509 0.66074 0.30660 0.15007  -0.16709 -0.04507 638 GLN A CG  
3630 C CD  . GLN A 435 ? 0.63649 0.68118 0.35960 0.15553  -0.16664 -0.04128 638 GLN A CD  
3631 O OE1 . GLN A 435 ? 0.55456 0.64011 0.32625 0.16091  -0.16857 -0.05679 638 GLN A OE1 
3632 N NE2 . GLN A 435 ? 0.67350 0.66197 0.36101 0.15163  -0.16185 -0.02129 638 GLN A NE2 
3633 N N   . TRP A 436 ? 0.45931 0.69315 0.33779 0.10874  -0.14418 -0.11768 639 TRP A N   
3634 C CA  . TRP A 436 ? 0.43635 0.71159 0.36098 0.08709  -0.12930 -0.13782 639 TRP A CA  
3635 C C   . TRP A 436 ? 0.43191 0.74979 0.38385 0.09229  -0.13174 -0.15839 639 TRP A C   
3636 O O   . TRP A 436 ? 0.38314 0.72440 0.34699 0.07776  -0.12316 -0.17222 639 TRP A O   
3637 C CB  . TRP A 436 ? 0.31740 0.59476 0.28882 0.07467  -0.11316 -0.13772 639 TRP A CB  
3638 C CG  . TRP A 436 ? 0.33402 0.57670 0.30363 0.05419  -0.09353 -0.12084 639 TRP A CG  
3639 C CD1 . TRP A 436 ? 0.30884 0.51608 0.27347 0.05271  -0.08861 -0.10218 639 TRP A CD1 
3640 C CD2 . TRP A 436 ? 0.29616 0.53958 0.27104 0.03241  -0.07603 -0.12267 639 TRP A CD2 
3641 N NE1 . TRP A 436 ? 0.30036 0.48967 0.26832 0.03159  -0.07007 -0.09266 639 TRP A NE1 
3642 C CE2 . TRP A 436 ? 0.31418 0.52464 0.28866 0.01959  -0.06171 -0.10459 639 TRP A CE2 
3643 C CE3 . TRP A 436 ? 0.29838 0.56832 0.27810 0.02275  -0.07109 -0.13904 639 TRP A CE3 
3644 C CZ2 . TRP A 436 ? 0.32164 0.52689 0.30248 -0.00083 -0.04284 -0.10217 639 TRP A CZ2 
3645 C CZ3 . TRP A 436 ? 0.29467 0.55541 0.27896 0.00205  -0.05138 -0.13624 639 TRP A CZ3 
3646 C CH2 . TRP A 436 ? 0.29133 0.52075 0.27658 -0.00876 -0.03758 -0.11777 639 TRP A CH2 
3647 N N   A LYS A 437 ? 0.37693 0.70573 0.33860 0.11257  -0.14211 -0.16193 640 LYS A N   
3648 N N   B LYS A 437 ? 0.37698 0.70572 0.33878 0.11254  -0.14206 -0.16191 640 LYS A N   
3649 C CA  A LYS A 437 ? 0.41734 0.78961 0.40427 0.11799  -0.14412 -0.18334 640 LYS A CA  
3650 C CA  B LYS A 437 ? 0.41764 0.78953 0.40423 0.11835  -0.14434 -0.18312 640 LYS A CA  
3651 C C   A LYS A 437 ? 0.46538 0.83949 0.41745 0.12379  -0.15446 -0.18387 640 LYS A C   
3652 C C   B LYS A 437 ? 0.46524 0.83913 0.41730 0.12368  -0.15438 -0.18376 640 LYS A C   
3653 O O   A LYS A 437 ? 0.45029 0.86006 0.42232 0.11502  -0.14975 -0.20274 640 LYS A O   
3654 O O   B LYS A 437 ? 0.45089 0.86025 0.42310 0.11447  -0.14937 -0.20259 640 LYS A O   
3655 C CB  A LYS A 437 ? 0.42833 0.81025 0.42743 0.13964  -0.15287 -0.18719 640 LYS A CB  
3656 C CB  B LYS A 437 ? 0.42973 0.80981 0.42647 0.14066  -0.15369 -0.18619 640 LYS A CB  
3657 C CG  A LYS A 437 ? 0.34194 0.73760 0.38594 0.13069  -0.13890 -0.19627 640 LYS A CG  
3658 C CG  B LYS A 437 ? 0.39669 0.82241 0.41494 0.14888  -0.15739 -0.20901 640 LYS A CG  
3659 N N   . LYS A 438 ? 0.46327 0.79645 0.36103 0.13795  -0.16730 -0.16314 641 LYS A N   
3660 C CA  . LYS A 438 ? 0.50924 0.83907 0.36848 0.14374  -0.17664 -0.16170 641 LYS A CA  
3661 C C   . LYS A 438 ? 0.49996 0.83091 0.35360 0.11870  -0.16382 -0.16556 641 LYS A C   
3662 O O   . LYS A 438 ? 0.51817 0.87074 0.36680 0.11571  -0.16563 -0.17716 641 LYS A O   
3663 C CB  . LYS A 438 ? 0.60823 0.88611 0.40723 0.16299  -0.18961 -0.13688 641 LYS A CB  
3664 C CG  . LYS A 438 ? 0.63578 0.91369 0.43546 0.19118  -0.20313 -0.13538 641 LYS A CG  
3665 N N   . TRP A 439 ? 0.51290 0.82213 0.36784 0.10062  -0.15012 -0.15722 642 TRP A N   
3666 C CA  . TRP A 439 ? 0.51017 0.82310 0.36504 0.07596  -0.13446 -0.16338 642 TRP A CA  
3667 C C   . TRP A 439 ? 0.51301 0.87565 0.42280 0.06189  -0.12292 -0.18983 642 TRP A C   
3668 O O   . TRP A 439 ? 0.45910 0.83678 0.36498 0.05193  -0.11816 -0.20092 642 TRP A O   
3669 C CB  . TRP A 439 ? 0.45006 0.73558 0.30132 0.05998  -0.12057 -0.15157 642 TRP A CB  
3670 C CG  . TRP A 439 ? 0.48895 0.77409 0.33394 0.03602  -0.10282 -0.15630 642 TRP A CG  
3671 C CD1 . TRP A 439 ? 0.56030 0.81165 0.35486 0.03092  -0.09895 -0.14208 642 TRP A CD1 
3672 C CD2 . TRP A 439 ? 0.45719 0.76969 0.35127 0.01333  -0.08193 -0.17361 642 TRP A CD2 
3673 N NE1 . TRP A 439 ? 0.55814 0.81709 0.37006 0.00681  -0.07724 -0.14993 642 TRP A NE1 
3674 C CE2 . TRP A 439 ? 0.46812 0.76305 0.34015 -0.00343 -0.06680 -0.16899 642 TRP A CE2 
3675 C CE3 . TRP A 439 ? 0.44688 0.79379 0.39958 0.00551  -0.07298 -0.19222 642 TRP A CE3 
3676 C CZ2 . TRP A 439 ? 0.48357 0.79497 0.39076 -0.02560 -0.04422 -0.18280 642 TRP A CZ2 
3677 C CZ3 . TRP A 439 ? 0.42044 0.77966 0.40524 -0.01725 -0.04991 -0.20492 642 TRP A CZ3 
3678 C CH2 . TRP A 439 ? 0.36331 0.70505 0.32554 -0.03155 -0.03632 -0.20027 642 TRP A CH2 
3679 N N   . LEU A 440 ? 0.43357 0.81910 0.39299 0.06036  -0.11666 -0.19999 643 LEU A N   
3680 C CA  . LEU A 440 ? 0.44119 0.86760 0.45117 0.04552  -0.10166 -0.22421 643 LEU A CA  
3681 C C   . LEU A 440 ? 0.54820 1.00846 0.56053 0.05596  -0.11168 -0.24035 643 LEU A C   
3682 O O   . LEU A 440 ? 0.53402 1.02025 0.56544 0.04149  -0.10081 -0.25830 643 LEU A O   
3683 C CB  . LEU A 440 ? 0.46705 0.90372 0.52199 0.04319  -0.09174 -0.22951 643 LEU A CB  
3684 C CG  . LEU A 440 ? 0.54913 1.01623 0.65204 0.02527  -0.07032 -0.25223 643 LEU A CG  
3685 C CD1 . LEU A 440 ? 0.48219 0.94173 0.58864 0.00138  -0.05147 -0.25519 643 LEU A CD1 
3686 C CD2 . LEU A 440 ? 0.53891 1.00395 0.67433 0.02395  -0.05943 -0.25381 643 LEU A CD2 
3687 N N   . GLU A 441 ? 0.45391 0.91434 0.44691 0.08129  -0.13179 -0.23487 644 GLU A N   
3688 C CA  . GLU A 441 ? 0.52431 1.01921 0.51802 0.09294  -0.14283 -0.25063 644 GLU A CA  
3689 C C   . GLU A 441 ? 0.55309 1.04172 0.50976 0.08821  -0.14724 -0.24934 644 GLU A C   
3690 O O   . GLU A 441 ? 0.48790 1.01204 0.45723 0.08513  -0.14752 -0.26863 644 GLU A O   
3691 C CB  . GLU A 441 ? 0.53402 1.02666 0.51166 0.12290  -0.16303 -0.24374 644 GLU A CB  
3692 C CG  . GLU A 441 ? 0.65897 1.16913 0.67798 0.12791  -0.15777 -0.25243 644 GLU A CG  
3693 C CD  . GLU A 441 ? 0.69196 1.19322 0.69254 0.15779  -0.17599 -0.24390 644 GLU A CD  
3694 O OE1 . GLU A 441 ? 0.74000 1.21347 0.69310 0.17497  -0.19203 -0.22735 644 GLU A OE1 
3695 O OE2 . GLU A 441 ? 0.70556 1.22491 0.73694 0.16380  -0.17280 -0.25399 644 GLU A OE2 
3696 N N   . ALA A 442 ? 0.53882 0.98228 0.44837 0.08637  -0.14921 -0.22781 645 ALA A N   
3697 C CA  . ALA A 442 ? 0.56648 0.99857 0.43575 0.08032  -0.15078 -0.22573 645 ALA A CA  
3698 C C   . ALA A 442 ? 0.61339 1.05518 0.50381 0.05146  -0.12867 -0.23815 645 ALA A C   
3699 O O   . ALA A 442 ? 0.69173 1.12685 0.55232 0.04414  -0.12711 -0.23932 645 ALA A O   
3700 C CB  . ALA A 442 ? 0.58161 0.95749 0.38635 0.08911  -0.15879 -0.19773 645 ALA A CB  
3701 N N   . HIS A 443 ? 0.57659 1.03167 0.51594 0.03533  -0.11052 -0.24727 646 HIS A N   
3702 C CA  . HIS A 443 ? 0.55304 1.01604 0.51715 0.00863  -0.08694 -0.25955 646 HIS A CA  
3703 C C   . HIS A 443 ? 0.56726 1.07311 0.58881 -0.00081 -0.07456 -0.28442 646 HIS A C   
3704 O O   . HIS A 443 ? 0.59269 1.10028 0.64948 -0.01968 -0.05227 -0.29159 646 HIS A O   
3705 C CB  . HIS A 443 ? 0.52829 0.95995 0.49385 -0.00511 -0.07135 -0.24625 646 HIS A CB  
3706 C CG  . HIS A 443 ? 0.54245 0.93337 0.45172 -0.00497 -0.07411 -0.22630 646 HIS A CG  
3707 N ND1 . HIS A 443 ? 0.55394 0.91367 0.42018 0.01346  -0.09107 -0.20500 646 HIS A ND1 
3708 C CD2 . HIS A 443 ? 0.56282 0.93709 0.45039 -0.02150 -0.05961 -0.22432 646 HIS A CD2 
3709 C CE1 . HIS A 443 ? 0.61110 0.93622 0.42974 0.00725  -0.08627 -0.19058 646 HIS A CE1 
3710 N NE2 . HIS A 443 ? 0.66760 1.00251 0.49911 -0.01400 -0.06705 -0.20229 646 HIS A NE2 
3711 N N   . GLN A 444 ? 0.54169 1.08087 0.57146 0.01240  -0.08741 -0.29794 647 GLN A N   
3712 C CA  . GLN A 444 ? 0.63552 1.21611 0.71489 0.00282  -0.07427 -0.32357 647 GLN A CA  
3713 C C   . GLN A 444 ? 0.57197 1.17481 0.65276 -0.01104 -0.06716 -0.34165 647 GLN A C   
3714 O O   . GLN A 444 ? 0.64197 1.22376 0.70069 -0.02357 -0.05994 -0.33592 647 GLN A O   
3715 C CB  . GLN A 444 ? 0.61557 1.22462 0.70779 0.02379  -0.08953 -0.33165 647 GLN A CB  
3716 C CG  . GLN A 444 ? 0.61333 1.20208 0.70777 0.03715  -0.09484 -0.31621 647 GLN A CG  
3717 C CD  . GLN A 444 ? 0.79122 1.37123 0.92209 0.01962  -0.07084 -0.31872 647 GLN A CD  
3718 O OE1 . GLN A 444 ? 0.91114 1.51513 1.07766 0.01317  -0.05741 -0.33762 647 GLN A OE1 
3719 N NE2 . GLN A 444 ? 0.72417 1.26702 0.84246 0.01186  -0.06457 -0.29995 647 GLN A NE2 
# 
