data_9MDO
# 
_entry.id   9MDO 
# 
_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   9MDO         pdb_00009mdo 10.2210/pdb9mdo/pdb 
WWPDB D_1000290778 ?            ?                   
# 
_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                        9MDO 
_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           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB wild-type       9ARC unspecified 
PDB 'E64 inhibited' 9MDK unspecified 
PDB 'C412S mutant'  9MDM 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' 55413.320 1   ? Y559A 'residues 205-647' ? 
2 non-polymer syn 1,2-ETHANEDIOL                           62.068    17  ? ?     ?                  ? 
3 non-polymer syn 'CHLORIDE ION'                           35.453    2   ? ?     ?                  ? 
4 water       nat water                                    18.015    276 ? ?     ?                  ? 
# 
_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
FKWKETADTKFYNVRKLDKLYVQGQFPSNYFVINGIRNEQIQGRDISQCWAKTASNMLHWWFEQNKDYIEQYKQKAAIEE
WKRPLYKHDYIRGLQDEDEGKKSNIANIFRAYSHNNARGGYIEDGLTWYLYKRDGQKNLGSIYPGLFNDVFAHDTSPINI
ERCETKKEFEQLMNKTLDNKRAIGIFWQGSKGNRPAQHAVTCWGAAYDEDNNIICLYIAESNLPEAVLYPFGVRYKGNIY
EEAEKNRTYMFNYALSKPENIYIDGLTTLDKGEDQWKKWLEAHQKGELNSKLEGKPIPNPLLGLDSTRTGHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTVTIEIKKKPQIKYEEKQAVMPESAAGTYTFEVQTIDGKLDYEPYFTSSTLPWITGAPTISSRTDPNKDVISFTCLKNK
TVWNRRAYIKFKDKKTGQYIKGADGKADLTVNIIQKKNENPVVHYKWVDGIGAPTENQKIKMKIKNNGIETEDYFTDPFV
FKWKETADTKFYNVRKLDKLYVQGQFPSNYFVINGIRNEQIQGRDISQCWAKTASNMLHWWFEQNKDYIEQYKQKAAIEE
WKRPLYKHDYIRGLQDEDEGKKSNIANIFRAYSHNNARGGYIEDGLTWYLYKRDGQKNLGSIYPGLFNDVFAHDTSPINI
ERCETKKEFEQLMNKTLDNKRAIGIFWQGSKGNRPAQHAVTCWGAAYDEDNNIICLYIAESNLPEAVLYPFGVRYKGNIY
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 'CHLORIDE ION' CL  
4 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 CYS 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 ALA 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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   pET101/D 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       plasmid 
_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 
CL  non-polymer         . 'CHLORIDE ION'  ?                 'Cl -1'          35.453  
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 
PHE 'L-peptide linking' y PHENYLALANINE   ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   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 CYS 209 412 412 CYS CYS 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 ?   ?   ?   A . n 
A 1 351 LYS 351 554 ?   ?   ?   A . n 
A 1 352 GLY 352 555 ?   ?   ?   A . n 
A 1 353 ASN 353 556 ?   ?   ?   A . n 
A 1 354 ARG 354 557 ?   ?   ?   A . n 
A 1 355 PRO 355 558 ?   ?   ?   A . n 
A 1 356 ALA 356 559 559 ALA ALA 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 ?   ?   ?   A . n 
A 1 403 ALA 403 606 ?   ?   ?   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 445 648 648 LYS LYS A . n 
A 1 446 GLY 446 649 649 GLY GLY A . n 
A 1 447 GLU 447 650 650 GLU GLU 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 
# 
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  701 EDO EDO A . 
C 2 EDO 1   702  703 EDO EDO A . 
D 2 EDO 1   703  704 EDO EDO A . 
E 2 EDO 1   704  705 EDO EDO A . 
F 2 EDO 1   705  706 EDO EDO A . 
G 2 EDO 1   706  707 EDO EDO A . 
H 2 EDO 1   707  710 EDO EDO A . 
I 2 EDO 1   708  711 EDO EDO A . 
J 2 EDO 1   709  714 EDO EDO A . 
K 2 EDO 1   710  715 EDO EDO A . 
L 2 EDO 1   711  717 EDO EDO A . 
M 2 EDO 1   712  720 EDO EDO A . 
N 2 EDO 1   713  722 EDO EDO A . 
O 2 EDO 1   714  723 EDO EDO A . 
P 2 EDO 1   715  725 EDO EDO A . 
Q 3 CL  1   716  728 CL  CL  A . 
R 3 CL  1   717  729 CL  CL  A . 
S 2 EDO 1   718  730 EDO EDO A . 
T 2 EDO 1   719  731 EDO EDO A . 
U 4 HOH 1   801  288 HOH HOH A . 
U 4 HOH 2   802  149 HOH HOH A . 
U 4 HOH 3   803  302 HOH HOH A . 
U 4 HOH 4   804  294 HOH HOH A . 
U 4 HOH 5   805  304 HOH HOH A . 
U 4 HOH 6   806  280 HOH HOH A . 
U 4 HOH 7   807  27  HOH HOH A . 
U 4 HOH 8   808  70  HOH HOH A . 
U 4 HOH 9   809  56  HOH HOH A . 
U 4 HOH 10  810  176 HOH HOH A . 
U 4 HOH 11  811  82  HOH HOH A . 
U 4 HOH 12  812  278 HOH HOH A . 
U 4 HOH 13  813  308 HOH HOH A . 
U 4 HOH 14  814  66  HOH HOH A . 
U 4 HOH 15  815  47  HOH HOH A . 
U 4 HOH 16  816  269 HOH HOH A . 
U 4 HOH 17  817  233 HOH HOH A . 
U 4 HOH 18  818  65  HOH HOH A . 
U 4 HOH 19  819  1   HOH HOH A . 
U 4 HOH 20  820  282 HOH HOH A . 
U 4 HOH 21  821  249 HOH HOH A . 
U 4 HOH 22  822  163 HOH HOH A . 
U 4 HOH 23  823  92  HOH HOH A . 
U 4 HOH 24  824  6   HOH HOH A . 
U 4 HOH 25  825  12  HOH HOH A . 
U 4 HOH 26  826  212 HOH HOH A . 
U 4 HOH 27  827  80  HOH HOH A . 
U 4 HOH 28  828  96  HOH HOH A . 
U 4 HOH 29  829  159 HOH HOH A . 
U 4 HOH 30  830  241 HOH HOH A . 
U 4 HOH 31  831  227 HOH HOH A . 
U 4 HOH 32  832  195 HOH HOH A . 
U 4 HOH 33  833  43  HOH HOH A . 
U 4 HOH 34  834  102 HOH HOH A . 
U 4 HOH 35  835  88  HOH HOH A . 
U 4 HOH 36  836  17  HOH HOH A . 
U 4 HOH 37  837  91  HOH HOH A . 
U 4 HOH 38  838  34  HOH HOH A . 
U 4 HOH 39  839  258 HOH HOH A . 
U 4 HOH 40  840  273 HOH HOH A . 
U 4 HOH 41  841  3   HOH HOH A . 
U 4 HOH 42  842  167 HOH HOH A . 
U 4 HOH 43  843  8   HOH HOH A . 
U 4 HOH 44  844  15  HOH HOH A . 
U 4 HOH 45  845  63  HOH HOH A . 
U 4 HOH 46  846  16  HOH HOH A . 
U 4 HOH 47  847  24  HOH HOH A . 
U 4 HOH 48  848  121 HOH HOH A . 
U 4 HOH 49  849  94  HOH HOH A . 
U 4 HOH 50  850  110 HOH HOH A . 
U 4 HOH 51  851  119 HOH HOH A . 
U 4 HOH 52  852  10  HOH HOH A . 
U 4 HOH 53  853  107 HOH HOH A . 
U 4 HOH 54  854  210 HOH HOH A . 
U 4 HOH 55  855  2   HOH HOH A . 
U 4 HOH 56  856  122 HOH HOH A . 
U 4 HOH 57  857  14  HOH HOH A . 
U 4 HOH 58  858  93  HOH HOH A . 
U 4 HOH 59  859  205 HOH HOH A . 
U 4 HOH 60  860  230 HOH HOH A . 
U 4 HOH 61  861  33  HOH HOH A . 
U 4 HOH 62  862  114 HOH HOH A . 
U 4 HOH 63  863  58  HOH HOH A . 
U 4 HOH 64  864  46  HOH HOH A . 
U 4 HOH 65  865  81  HOH HOH A . 
U 4 HOH 66  866  26  HOH HOH A . 
U 4 HOH 67  867  67  HOH HOH A . 
U 4 HOH 68  868  21  HOH HOH A . 
U 4 HOH 69  869  141 HOH HOH A . 
U 4 HOH 70  870  285 HOH HOH A . 
U 4 HOH 71  871  42  HOH HOH A . 
U 4 HOH 72  872  171 HOH HOH A . 
U 4 HOH 73  873  90  HOH HOH A . 
U 4 HOH 74  874  224 HOH HOH A . 
U 4 HOH 75  875  11  HOH HOH A . 
U 4 HOH 76  876  152 HOH HOH A . 
U 4 HOH 77  877  135 HOH HOH A . 
U 4 HOH 78  878  207 HOH HOH A . 
U 4 HOH 79  879  103 HOH HOH A . 
U 4 HOH 80  880  243 HOH HOH A . 
U 4 HOH 81  881  242 HOH HOH A . 
U 4 HOH 82  882  146 HOH HOH A . 
U 4 HOH 83  883  48  HOH HOH A . 
U 4 HOH 84  884  4   HOH HOH A . 
U 4 HOH 85  885  49  HOH HOH A . 
U 4 HOH 86  886  22  HOH HOH A . 
U 4 HOH 87  887  31  HOH HOH A . 
U 4 HOH 88  888  310 HOH HOH A . 
U 4 HOH 89  889  251 HOH HOH A . 
U 4 HOH 90  890  5   HOH HOH A . 
U 4 HOH 91  891  177 HOH HOH A . 
U 4 HOH 92  892  262 HOH HOH A . 
U 4 HOH 93  893  137 HOH HOH A . 
U 4 HOH 94  894  216 HOH HOH A . 
U 4 HOH 95  895  45  HOH HOH A . 
U 4 HOH 96  896  299 HOH HOH A . 
U 4 HOH 97  897  125 HOH HOH A . 
U 4 HOH 98  898  115 HOH HOH A . 
U 4 HOH 99  899  147 HOH HOH A . 
U 4 HOH 100 900  109 HOH HOH A . 
U 4 HOH 101 901  142 HOH HOH A . 
U 4 HOH 102 902  23  HOH HOH A . 
U 4 HOH 103 903  54  HOH HOH A . 
U 4 HOH 104 904  133 HOH HOH A . 
U 4 HOH 105 905  37  HOH HOH A . 
U 4 HOH 106 906  9   HOH HOH A . 
U 4 HOH 107 907  32  HOH HOH A . 
U 4 HOH 108 908  236 HOH HOH A . 
U 4 HOH 109 909  75  HOH HOH A . 
U 4 HOH 110 910  169 HOH HOH A . 
U 4 HOH 111 911  257 HOH HOH A . 
U 4 HOH 112 912  203 HOH HOH A . 
U 4 HOH 113 913  51  HOH HOH A . 
U 4 HOH 114 914  198 HOH HOH A . 
U 4 HOH 115 915  77  HOH HOH A . 
U 4 HOH 116 916  28  HOH HOH A . 
U 4 HOH 117 917  79  HOH HOH A . 
U 4 HOH 118 918  229 HOH HOH A . 
U 4 HOH 119 919  181 HOH HOH A . 
U 4 HOH 120 920  106 HOH HOH A . 
U 4 HOH 121 921  60  HOH HOH A . 
U 4 HOH 122 922  53  HOH HOH A . 
U 4 HOH 123 923  202 HOH HOH A . 
U 4 HOH 124 924  118 HOH HOH A . 
U 4 HOH 125 925  303 HOH HOH A . 
U 4 HOH 126 926  73  HOH HOH A . 
U 4 HOH 127 927  139 HOH HOH A . 
U 4 HOH 128 928  59  HOH HOH A . 
U 4 HOH 129 929  18  HOH HOH A . 
U 4 HOH 130 930  38  HOH HOH A . 
U 4 HOH 131 931  25  HOH HOH A . 
U 4 HOH 132 932  260 HOH HOH A . 
U 4 HOH 133 933  291 HOH HOH A . 
U 4 HOH 134 934  213 HOH HOH A . 
U 4 HOH 135 935  105 HOH HOH A . 
U 4 HOH 136 936  101 HOH HOH A . 
U 4 HOH 137 937  98  HOH HOH A . 
U 4 HOH 138 938  246 HOH HOH A . 
U 4 HOH 139 939  68  HOH HOH A . 
U 4 HOH 140 940  86  HOH HOH A . 
U 4 HOH 141 941  158 HOH HOH A . 
U 4 HOH 142 942  116 HOH HOH A . 
U 4 HOH 143 943  13  HOH HOH A . 
U 4 HOH 144 944  300 HOH HOH A . 
U 4 HOH 145 945  271 HOH HOH A . 
U 4 HOH 146 946  263 HOH HOH A . 
U 4 HOH 147 947  35  HOH HOH A . 
U 4 HOH 148 948  143 HOH HOH A . 
U 4 HOH 149 949  74  HOH HOH A . 
U 4 HOH 150 950  255 HOH HOH A . 
U 4 HOH 151 951  306 HOH HOH A . 
U 4 HOH 152 952  64  HOH HOH A . 
U 4 HOH 153 953  162 HOH HOH A . 
U 4 HOH 154 954  293 HOH HOH A . 
U 4 HOH 155 955  39  HOH HOH A . 
U 4 HOH 156 956  57  HOH HOH A . 
U 4 HOH 157 957  78  HOH HOH A . 
U 4 HOH 158 958  151 HOH HOH A . 
U 4 HOH 159 959  29  HOH HOH A . 
U 4 HOH 160 960  89  HOH HOH A . 
U 4 HOH 161 961  173 HOH HOH A . 
U 4 HOH 162 962  85  HOH HOH A . 
U 4 HOH 163 963  134 HOH HOH A . 
U 4 HOH 164 964  140 HOH HOH A . 
U 4 HOH 165 965  209 HOH HOH A . 
U 4 HOH 166 966  211 HOH HOH A . 
U 4 HOH 167 967  245 HOH HOH A . 
U 4 HOH 168 968  148 HOH HOH A . 
U 4 HOH 169 969  52  HOH HOH A . 
U 4 HOH 170 970  20  HOH HOH A . 
U 4 HOH 171 971  170 HOH HOH A . 
U 4 HOH 172 972  72  HOH HOH A . 
U 4 HOH 173 973  295 HOH HOH A . 
U 4 HOH 174 974  112 HOH HOH A . 
U 4 HOH 175 975  244 HOH HOH A . 
U 4 HOH 176 976  309 HOH HOH A . 
U 4 HOH 177 977  178 HOH HOH A . 
U 4 HOH 178 978  206 HOH HOH A . 
U 4 HOH 179 979  50  HOH HOH A . 
U 4 HOH 180 980  157 HOH HOH A . 
U 4 HOH 181 981  166 HOH HOH A . 
U 4 HOH 182 982  44  HOH HOH A . 
U 4 HOH 183 983  95  HOH HOH A . 
U 4 HOH 184 984  144 HOH HOH A . 
U 4 HOH 185 985  120 HOH HOH A . 
U 4 HOH 186 986  108 HOH HOH A . 
U 4 HOH 187 987  123 HOH HOH A . 
U 4 HOH 188 988  248 HOH HOH A . 
U 4 HOH 189 989  179 HOH HOH A . 
U 4 HOH 190 990  41  HOH HOH A . 
U 4 HOH 191 991  175 HOH HOH A . 
U 4 HOH 192 992  154 HOH HOH A . 
U 4 HOH 193 993  117 HOH HOH A . 
U 4 HOH 194 994  36  HOH HOH A . 
U 4 HOH 195 995  259 HOH HOH A . 
U 4 HOH 196 996  188 HOH HOH A . 
U 4 HOH 197 997  99  HOH HOH A . 
U 4 HOH 198 998  76  HOH HOH A . 
U 4 HOH 199 999  231 HOH HOH A . 
U 4 HOH 200 1000 126 HOH HOH A . 
U 4 HOH 201 1001 55  HOH HOH A . 
U 4 HOH 202 1002 69  HOH HOH A . 
U 4 HOH 203 1003 71  HOH HOH A . 
U 4 HOH 204 1004 215 HOH HOH A . 
U 4 HOH 205 1005 83  HOH HOH A . 
U 4 HOH 206 1006 223 HOH HOH A . 
U 4 HOH 207 1007 218 HOH HOH A . 
U 4 HOH 208 1008 305 HOH HOH A . 
U 4 HOH 209 1009 186 HOH HOH A . 
U 4 HOH 210 1010 265 HOH HOH A . 
U 4 HOH 211 1011 155 HOH HOH A . 
U 4 HOH 212 1012 30  HOH HOH A . 
U 4 HOH 213 1013 153 HOH HOH A . 
U 4 HOH 214 1014 201 HOH HOH A . 
U 4 HOH 215 1015 145 HOH HOH A . 
U 4 HOH 216 1016 214 HOH HOH A . 
U 4 HOH 217 1017 264 HOH HOH A . 
U 4 HOH 218 1018 19  HOH HOH A . 
U 4 HOH 219 1019 292 HOH HOH A . 
U 4 HOH 220 1020 128 HOH HOH A . 
U 4 HOH 221 1021 138 HOH HOH A . 
U 4 HOH 222 1022 111 HOH HOH A . 
U 4 HOH 223 1023 160 HOH HOH A . 
U 4 HOH 224 1024 97  HOH HOH A . 
U 4 HOH 225 1025 277 HOH HOH A . 
U 4 HOH 226 1026 208 HOH HOH A . 
U 4 HOH 227 1027 165 HOH HOH A . 
U 4 HOH 228 1028 261 HOH HOH A . 
U 4 HOH 229 1029 270 HOH HOH A . 
U 4 HOH 230 1030 281 HOH HOH A . 
U 4 HOH 231 1031 124 HOH HOH A . 
U 4 HOH 232 1032 131 HOH HOH A . 
U 4 HOH 233 1033 238 HOH HOH A . 
U 4 HOH 234 1034 40  HOH HOH A . 
U 4 HOH 235 1035 274 HOH HOH A . 
U 4 HOH 236 1036 191 HOH HOH A . 
U 4 HOH 237 1037 200 HOH HOH A . 
U 4 HOH 238 1038 275 HOH HOH A . 
U 4 HOH 239 1039 267 HOH HOH A . 
U 4 HOH 240 1040 226 HOH HOH A . 
U 4 HOH 241 1041 297 HOH HOH A . 
U 4 HOH 242 1042 225 HOH HOH A . 
U 4 HOH 243 1043 130 HOH HOH A . 
U 4 HOH 244 1044 286 HOH HOH A . 
U 4 HOH 245 1045 182 HOH HOH A . 
U 4 HOH 246 1046 168 HOH HOH A . 
U 4 HOH 247 1047 268 HOH HOH A . 
U 4 HOH 248 1048 185 HOH HOH A . 
U 4 HOH 249 1049 240 HOH HOH A . 
U 4 HOH 250 1050 172 HOH HOH A . 
U 4 HOH 251 1051 164 HOH HOH A . 
U 4 HOH 252 1052 61  HOH HOH A . 
U 4 HOH 253 1053 187 HOH HOH A . 
U 4 HOH 254 1054 194 HOH HOH A . 
U 4 HOH 255 1055 161 HOH HOH A . 
U 4 HOH 256 1056 204 HOH HOH A . 
U 4 HOH 257 1057 113 HOH HOH A . 
U 4 HOH 258 1058 217 HOH HOH A . 
U 4 HOH 259 1059 250 HOH HOH A . 
U 4 HOH 260 1060 266 HOH HOH A . 
U 4 HOH 261 1061 62  HOH HOH A . 
U 4 HOH 262 1062 174 HOH HOH A . 
U 4 HOH 263 1063 196 HOH HOH A . 
U 4 HOH 264 1064 276 HOH HOH A . 
U 4 HOH 265 1065 129 HOH HOH A . 
U 4 HOH 266 1066 189 HOH HOH A . 
U 4 HOH 267 1067 199 HOH HOH A . 
U 4 HOH 268 1068 84  HOH HOH A . 
U 4 HOH 269 1069 156 HOH HOH A . 
U 4 HOH 270 1070 228 HOH HOH A . 
U 4 HOH 271 1071 192 HOH HOH A . 
U 4 HOH 272 1072 150 HOH HOH A . 
U 4 HOH 273 1073 136 HOH HOH A . 
U 4 HOH 274 1074 235 HOH HOH A . 
U 4 HOH 275 1075 289 HOH HOH A . 
U 4 HOH 276 1076 184 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 ? CD  ? A LYS 8   CD  
2  1 Y 1 A LYS 211 ? CE  ? A LYS 8   CE  
3  1 Y 1 A LYS 211 ? NZ  ? A LYS 8   NZ  
4  1 Y 1 A LYS 217 ? CE  ? A LYS 14  CE  
5  1 Y 1 A LYS 217 ? NZ  ? A LYS 14  NZ  
6  1 Y 1 A LYS 221 ? CG  ? A LYS 18  CG  
7  1 Y 1 A LYS 221 ? CD  ? A LYS 18  CD  
8  1 Y 1 A LYS 221 ? CE  ? A LYS 18  CE  
9  1 Y 1 A LYS 221 ? NZ  ? A LYS 18  NZ  
10 1 Y 1 A LYS 295 ? CE  ? A LYS 92  CE  
11 1 Y 1 A LYS 295 ? NZ  ? A LYS 92  NZ  
12 1 Y 1 A LYS 320 ? NZ  ? A LYS 117 NZ  
13 1 Y 1 A ASN 350 ? CG  ? A ASN 147 CG  
14 1 Y 1 A ASN 350 ? OD1 ? A ASN 147 OD1 
15 1 Y 1 A ASN 350 ? ND2 ? A ASN 147 ND2 
16 1 Y 1 A ILE 352 ? CG1 ? A ILE 149 CG1 
17 1 Y 1 A ILE 352 ? CG2 ? A ILE 149 CG2 
18 1 Y 1 A ILE 352 ? CD1 ? A ILE 149 CD1 
19 1 Y 1 A GLU 355 ? CG  ? A GLU 152 CG  
20 1 Y 1 A GLU 355 ? CD  ? A GLU 152 CD  
21 1 Y 1 A GLU 355 ? OE1 ? A GLU 152 OE1 
22 1 Y 1 A GLU 355 ? OE2 ? A GLU 152 OE2 
23 1 Y 1 A LYS 367 ? NZ  ? A LYS 164 NZ  
24 1 Y 1 A LYS 373 ? NZ  ? A LYS 170 NZ  
25 1 Y 1 A LYS 382 ? CE  ? A LYS 179 CE  
26 1 Y 1 A LYS 382 ? NZ  ? A LYS 179 NZ  
27 1 Y 1 A GLN 388 ? CD  ? A GLN 185 CD  
28 1 Y 1 A GLN 388 ? OE1 ? A GLN 185 OE1 
29 1 Y 1 A GLN 388 ? NE2 ? A GLN 185 NE2 
30 1 Y 1 A SER 391 ? OG  ? A SER 188 OG  
31 1 Y 1 A ARG 400 ? CD  ? A ARG 197 CD  
32 1 Y 1 A ARG 400 ? NE  ? A ARG 197 NE  
33 1 Y 1 A ARG 400 ? CZ  ? A ARG 197 CZ  
34 1 Y 1 A ARG 400 ? NH1 ? A ARG 197 NH1 
35 1 Y 1 A ARG 400 ? NH2 ? A ARG 197 NH2 
36 1 Y 1 A LYS 429 ? CD  ? A LYS 226 CD  
37 1 Y 1 A LYS 429 ? CE  ? A LYS 226 CE  
38 1 Y 1 A LYS 429 ? NZ  ? A LYS 226 NZ  
39 1 Y 1 A ARG 481 ? CG  ? A ARG 278 CG  
40 1 Y 1 A ARG 481 ? CD  ? A ARG 278 CD  
41 1 Y 1 A ARG 481 ? NE  ? A ARG 278 NE  
42 1 Y 1 A ARG 481 ? CZ  ? A ARG 278 CZ  
43 1 Y 1 A ARG 481 ? NH1 ? A ARG 278 NH1 
44 1 Y 1 A ARG 481 ? NH2 ? A ARG 278 NH2 
45 1 Y 1 A LYS 500 ? CD  ? A LYS 297 CD  
46 1 Y 1 A LYS 500 ? CE  ? A LYS 297 CE  
47 1 Y 1 A LYS 500 ? NZ  ? A LYS 297 NZ  
48 1 Y 1 A LYS 530 ? CD  ? A LYS 327 CD  
49 1 Y 1 A LYS 530 ? CE  ? A LYS 327 CE  
50 1 Y 1 A LYS 530 ? NZ  ? A LYS 327 NZ  
51 1 Y 1 A LYS 599 ? CG  ? A LYS 396 CG  
52 1 Y 1 A LYS 599 ? CD  ? A LYS 396 CD  
53 1 Y 1 A LYS 599 ? CE  ? A LYS 396 CE  
54 1 Y 1 A LYS 599 ? NZ  ? A LYS 396 NZ  
55 1 Y 1 A GLU 604 ? CG  ? A GLU 401 CG  
56 1 Y 1 A GLU 604 ? CD  ? A GLU 401 CD  
57 1 Y 1 A GLU 604 ? OE1 ? A GLU 401 OE1 
58 1 Y 1 A GLU 604 ? OE2 ? A GLU 401 OE2 
59 1 Y 1 A LYS 608 ? CE  ? A LYS 405 CE  
60 1 Y 1 A LYS 608 ? NZ  ? A LYS 405 NZ  
61 1 Y 1 A LYS 620 ? CG  ? A LYS 417 CG  
62 1 Y 1 A LYS 620 ? CD  ? A LYS 417 CD  
63 1 Y 1 A LYS 620 ? CE  ? A LYS 417 CE  
64 1 Y 1 A LYS 620 ? NZ  ? A LYS 417 NZ  
65 1 Y 1 A GLU 622 ? CG  ? A GLU 419 CG  
66 1 Y 1 A GLU 622 ? CD  ? A GLU 419 CD  
67 1 Y 1 A GLU 622 ? OE1 ? A GLU 419 OE1 
68 1 Y 1 A GLU 622 ? OE2 ? A GLU 419 OE2 
69 1 Y 1 A LYS 641 ? CE  ? A LYS 438 CE  
70 1 Y 1 A LYS 641 ? NZ  ? A LYS 438 NZ  
71 1 Y 1 A GLU 644 ? CD  ? A GLU 441 CD  
72 1 Y 1 A GLU 644 ? OE1 ? A GLU 441 OE1 
73 1 Y 1 A GLU 644 ? OE2 ? A GLU 441 OE2 
74 1 Y 1 A LYS 648 ? CG  ? A LYS 445 CG  
75 1 Y 1 A LYS 648 ? CD  ? A LYS 445 CD  
76 1 Y 1 A LYS 648 ? CE  ? A LYS 445 CE  
77 1 Y 1 A LYS 648 ? NZ  ? A LYS 445 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                     9MDO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     40.965 
_cell.length_a_esd                 ? 
_cell.length_b                     99.558 
_cell.length_b_esd                 ? 
_cell.length_c                     120.394 
_cell.length_c_esd                 ? 
_cell.volume                       491016.782 
_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                         9MDO 
_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                   9MDO 
_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          44.48 
_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              8.0 
_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 Tris, pH 8.0, 0.1 M Potassium Bromide, 22% PEG 20,000' 
_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         2022-01-17 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9865 
_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                        'SSRL BEAMLINE BL12-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9865 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          30.59 
_reflns.entry_id                                       9MDO 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.02 
_reflns.d_resolution_low                               46.00 
_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                                     204537 
_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                           98.02 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.04 
_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                                   0.993 
_reflns.pdbx_CC_star                                   0.998 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.149 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.02 
_reflns_shell.d_res_low                                     2.05 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.16 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             8262 
_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                               5.8 
_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                                  0.526 
_reflns_shell.pdbx_CC_star                                  0.830 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          89.5 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.617 
_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                               37.78 
_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                                 9MDO 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.02 
_refine.ls_d_res_low                             46.00 
_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                     61524 
_refine.ls_number_reflns_R_free                  3068 
_refine.ls_number_reflns_R_work                  58456 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.02 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1822 
_refine.ls_R_factor_R_free                       0.2322 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1796 
_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                 25.7170 
_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                            0.2801 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.02 
_refine_hist.d_res_low                        46.00 
_refine_hist.number_atoms_solvent             276 
_refine_hist.number_atoms_total               3840 
_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        3494 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         70 
_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' ? 0.0066  ? 3711 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.7845  ? 5005 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0523  ? 509  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0050  ? 649  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.9354 ? 1350 ? 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' 2.02 2.05  . . 94  2500 89.48 . . . . 0.3435 . . . . . . . . . . . 0.3975 
'X-RAY DIFFRACTION' 2.05 2.08  . . 137 2639 98.75 . . . . 0.3006 . . . . . . . . . . . 0.3334 
'X-RAY DIFFRACTION' 2.08 2.12  . . 126 2700 98.26 . . . . 0.2809 . . . . . . . . . . . 0.3205 
'X-RAY DIFFRACTION' 2.12 2.16  . . 174 2610 96.20 . . . . 0.2693 . . . . . . . . . . . 0.2522 
'X-RAY DIFFRACTION' 2.16 2.20  . . 110 2511 94.04 . . . . 0.2383 . . . . . . . . . . . 0.2722 
'X-RAY DIFFRACTION' 2.20 2.24  . . 155 2677 98.78 . . . . 0.2390 . . . . . . . . . . . 0.2754 
'X-RAY DIFFRACTION' 2.24 2.29  . . 137 2704 99.41 . . . . 0.2265 . . . . . . . . . . . 0.3139 
'X-RAY DIFFRACTION' 2.29 2.34  . . 141 2664 99.47 . . . . 0.2246 . . . . . . . . . . . 0.2413 
'X-RAY DIFFRACTION' 2.34 2.40  . . 188 2697 99.69 . . . . 0.2364 . . . . . . . . . . . 0.2969 
'X-RAY DIFFRACTION' 2.40 2.47  . . 129 2656 99.39 . . . . 0.2169 . . . . . . . . . . . 0.3274 
'X-RAY DIFFRACTION' 2.47 2.54  . . 151 2702 99.48 . . . . 0.2105 . . . . . . . . . . . 0.2580 
'X-RAY DIFFRACTION' 2.54 2.62  . . 155 2667 99.19 . . . . 0.2064 . . . . . . . . . . . 0.2700 
'X-RAY DIFFRACTION' 2.62 2.72  . . 139 2732 99.10 . . . . 0.1886 . . . . . . . . . . . 0.2841 
'X-RAY DIFFRACTION' 2.72 2.82  . . 116 2593 96.30 . . . . 0.1862 . . . . . . . . . . . 0.2335 
'X-RAY DIFFRACTION' 2.82 2.95  . . 153 2677 98.88 . . . . 0.1816 . . . . . . . . . . . 0.2422 
'X-RAY DIFFRACTION' 2.95 3.11  . . 137 2712 99.62 . . . . 0.1807 . . . . . . . . . . . 0.2762 
'X-RAY DIFFRACTION' 3.11 3.30  . . 145 2685 99.61 . . . . 0.1615 . . . . . . . . . . . 0.2136 
'X-RAY DIFFRACTION' 3.30 3.56  . . 103 2741 99.48 . . . . 0.1464 . . . . . . . . . . . 0.2358 
'X-RAY DIFFRACTION' 3.56 3.92  . . 171 2625 98.31 . . . . 0.1469 . . . . . . . . . . . 0.1941 
'X-RAY DIFFRACTION' 3.92 4.48  . . 124 2627 96.12 . . . . 0.1248 . . . . . . . . . . . 0.1811 
'X-RAY DIFFRACTION' 4.48 5.64  . . 144 2695 99.75 . . . . 0.1353 . . . . . . . . . . . 0.1700 
'X-RAY DIFFRACTION' 5.65 46.00 . . 139 2642 97.31 . . . . 0.1735 . . . . . . . . . . . 0.2011 
# 
_struct.entry_id                     9MDO 
_struct.title                        
'Crystal Structure of Y559A Prosegment Binding Loop 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        9MDO 
_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 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 2 ? 
L N N 2 ? 
M N N 2 ? 
N N N 2 ? 
O N N 2 ? 
P N N 2 ? 
Q N N 3 ? 
R N N 3 ? 
S N N 2 ? 
T N N 2 ? 
U N N 4 ? 
# 
_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              9MDO 
_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 9MDO MET A 1   ? UNP Q73QT1 ?   ?   'initiating methionine' 204 1  
1 9MDO ALA A 356 ? UNP Q73QT1 TYR 559 'engineered mutation'   559 2  
1 9MDO LYS A 445 ? UNP Q73QT1 ?   ?   'expression tag'        648 3  
1 9MDO GLY A 446 ? UNP Q73QT1 ?   ?   'expression tag'        649 4  
1 9MDO GLU A 447 ? UNP Q73QT1 ?   ?   'expression tag'        650 5  
1 9MDO LEU A 448 ? UNP Q73QT1 ?   ?   'expression tag'        651 6  
1 9MDO ASN A 449 ? UNP Q73QT1 ?   ?   'expression tag'        652 7  
1 9MDO SER A 450 ? UNP Q73QT1 ?   ?   'expression tag'        653 8  
1 9MDO LYS A 451 ? UNP Q73QT1 ?   ?   'expression tag'        654 9  
1 9MDO LEU A 452 ? UNP Q73QT1 ?   ?   'expression tag'        655 10 
1 9MDO GLU A 453 ? UNP Q73QT1 ?   ?   'expression tag'        656 11 
1 9MDO GLY A 454 ? UNP Q73QT1 ?   ?   'expression tag'        657 12 
1 9MDO LYS A 455 ? UNP Q73QT1 ?   ?   'expression tag'        658 13 
1 9MDO PRO A 456 ? UNP Q73QT1 ?   ?   'expression tag'        659 14 
1 9MDO ILE A 457 ? UNP Q73QT1 ?   ?   'expression tag'        660 15 
1 9MDO PRO A 458 ? UNP Q73QT1 ?   ?   'expression tag'        661 16 
1 9MDO ASN A 459 ? UNP Q73QT1 ?   ?   'expression tag'        662 17 
1 9MDO PRO A 460 ? UNP Q73QT1 ?   ?   'expression tag'        663 18 
1 9MDO LEU A 461 ? UNP Q73QT1 ?   ?   'expression tag'        664 19 
1 9MDO LEU A 462 ? UNP Q73QT1 ?   ?   'expression tag'        665 20 
1 9MDO GLY A 463 ? UNP Q73QT1 ?   ?   'expression tag'        666 21 
1 9MDO LEU A 464 ? UNP Q73QT1 ?   ?   'expression tag'        667 22 
1 9MDO ASP A 465 ? UNP Q73QT1 ?   ?   'expression tag'        668 23 
1 9MDO SER A 466 ? UNP Q73QT1 ?   ?   'expression tag'        669 24 
1 9MDO THR A 467 ? UNP Q73QT1 ?   ?   'expression tag'        670 25 
1 9MDO ARG A 468 ? UNP Q73QT1 ?   ?   'expression tag'        671 26 
1 9MDO THR A 469 ? UNP Q73QT1 ?   ?   'expression tag'        672 27 
1 9MDO GLY A 470 ? UNP Q73QT1 ?   ?   'expression tag'        673 28 
1 9MDO HIS A 471 ? UNP Q73QT1 ?   ?   'expression tag'        674 29 
1 9MDO HIS A 472 ? UNP Q73QT1 ?   ?   'expression tag'        675 30 
1 9MDO HIS A 473 ? UNP Q73QT1 ?   ?   'expression tag'        676 31 
1 9MDO HIS A 474 ? UNP Q73QT1 ?   ?   'expression tag'        677 32 
1 9MDO HIS A 475 ? UNP Q73QT1 ?   ?   'expression tag'        678 33 
1 9MDO 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,N,O,P,Q,R,S,T,U 
# 
_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 ? GLY A 446 ? GLY A 635 GLY A 649 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 7 ? 
AA4 ? 6 ? 
AA5 ? 2 ? 
AA6 ? 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 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 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 THR A 110 ? GLN A 115 ? THR A 313 GLN A 318 
AA3 1 HIS A 124 ? TRP A 127 ? HIS A 327 TRP A 330 
AA3 2 HIS A 358 ? TYR A 367 ? HIS A 561 TYR A 570 
AA3 3 ILE A 373 ? ALA A 379 ? ILE A 576 ALA A 582 
AA3 4 VAL A 387 ? TYR A 395 ? VAL A 590 TYR A 598 
AA3 5 ALA A 342 ? TRP A 347 ? ALA A 545 TRP A 550 
AA3 6 GLY A 425 ? LEU A 429 ? GLY A 628 LEU A 632 
AA3 7 ILE A 318 ? ARG A 322 ? ILE A 521 ARG A 525 
AA4 1 LYS A 139 ? ILE A 140 ? LYS A 342 ILE A 343 
AA4 2 LYS A 162 ? LYS A 164 ? LYS A 365 LYS A 367 
AA4 3 VAL A 387 ? TYR A 395 ? VAL A 590 TYR A 598 
AA4 4 ILE A 373 ? ALA A 379 ? ILE A 576 ALA A 582 
AA4 5 HIS A 358 ? TYR A 367 ? HIS A 561 TYR A 570 
AA4 6 THR A 408 ? ASN A 412 ? THR A 611 ASN A 615 
AA5 1 LYS A 143 ? ASN A 146 ? LYS A 346 ASN A 349 
AA5 2 ILE A 149 ? TYR A 154 ? ILE A 352 TYR A 357 
AA6 1 VAL A 192 ? ASN A 194 ? VAL A 395 ASN A 397 
AA6 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 LYS A 14  ? N LYS A 217 O GLN A 35  ? O GLN A 238 
AA1 2 3 N GLY A 28  ? N GLY A 231 O CYS A 76  ? O CYS A 279 
AA1 3 4 O SER A 73  ? O SER A 276 N THR A 60  ? N THR A 263 
AA2 1 2 N TYR A 46  ? N TYR A 249 O LYS A 90  ? O LYS A 293 
AA2 2 3 N ALA A 87  ? N ALA A 290 O ILE A 113 ? O ILE A 316 
AA3 1 2 N HIS A 124 ? N HIS A 327 O TYR A 367 ? O TYR A 570 
AA3 2 3 N TRP A 363 ? N TRP A 566 O TYR A 377 ? O TYR A 580 
AA3 3 4 N ILE A 378 ? N ILE A 581 O TYR A 389 ? O TYR A 592 
AA3 5 6 N GLY A 344 ? N GLY A 547 O THR A 427 ? O THR A 630 
AA3 6 7 O LEU A 426 ? O LEU A 629 N GLU A 321 ? N GLU A 524 
AA4 1 2 N ILE A 140 ? N ILE A 343 O LYS A 162 ? O LYS A 365 
AA4 2 3 N TRP A 163 ? N TRP A 366 O LEU A 388 ? O LEU A 591 
AA4 3 4 O TYR A 389 ? O TYR A 592 N ILE A 378 ? N ILE A 581 
AA4 4 5 O TYR A 377 ? O TYR A 580 N TRP A 363 ? N TRP A 566 
AA5 1 2 N ASN A 146 ? N ASN A 349 O ILE A 149 ? O ILE A 352 
AA6 1 2 N ILE A 193 ? N ILE A 396 O ILE A 201 ? O ILE A 404 
# 
_pdbx_entry_details.entry_id                   9MDO 
_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     N 
_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 GLN A 411 ? ? -97.57  35.95   
2 1 TYR A 449 ? ? -96.81  53.62   
3 1 SER A 476 ? ? -89.03  -139.49 
4 1 GLU A 527 ? ? -148.71 -2.11   
5 1 ASN A 609 ? ? 66.64   73.63   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 947 ? U HOH . 
2 1 A HOH 954 ? U HOH . 
# 
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 -1.09993689613 41.2803912121 18.4057097518  0.256137889963 ? -0.0324864610933 ? -0.00936698542701 
? 0.247754078771 ? 0.0407750812385 ? 0.197410778496 ? 0.553374030206 ? -0.973412612464 ? -0.497652811321 ? 3.05247078058 ? 
1.96326893238  ? 1.3114551405  ? 0.0266482627797   ? -0.0141338251717 ? 0.00617468159818 ? -0.0360865078505 ? -0.0589246731881 ? 
0.0143145412793  ? -0.134003909987  ? -0.056180948225 ? 0.0302195741442  ? 
2 'X-RAY DIFFRACTION' ? refined 27.3656509406  9.40907054948 -7.83546706143 0.226236243247 ? -0.0729801439049 ? 0.0035734360184   
? 0.630995498337 ? 0.001274711955  ? 0.468782190878 ? 1.42211398399  ? -0.390124735198 ? 0.908191727974  ? 1.60203619618 ? 
0.926295544612 ? 3.14324791768 ? -0.0401481031294  ? 0.113368304303   ? -0.238191629923  ? 0.00723823814813 ? 0.0864802521058  ? 
-0.354538354083  ? -0.0422297239035 ? 1.0164738383    ? -0.148643612831  ? 
3 'X-RAY DIFFRACTION' ? refined 6.71824492813  19.8428972863 -9.36088023744 0.239480174613 ? -0.0467706255897 ? -0.0224533939266  
? 0.212397226907 ? 0.0237760966984 ? 0.228121874845 ? 0.846203473636 ? -0.139121842512 ? -0.347278813989 ? 1.59650183529 ? 
0.901128498669 ? 2.73504265548 ? -0.00685434576583 ? 0.107403889539   ? 0.097243583885   ? -0.199960727794  ? -0.0049740301143 ? 
-0.0642301400408 ? -0.507006785841  ? 0.0520565266019 ? 0.00440784540161 ? 
# 
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 201 A 411 ? ? 
;chain 'A' and (resid 384 through 411 )
;
3 'X-RAY DIFFRACTION' 3 A 202 A 412 ? A 432 A 650 ? ? 
;chain 'A' and (resid 412 through 650 )
;
# 
_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                       1076 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.92 
_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 SER 553 ? A SER 350 
9  1 Y 1 A LYS 554 ? A LYS 351 
10 1 Y 1 A GLY 555 ? A GLY 352 
11 1 Y 1 A ASN 556 ? A ASN 353 
12 1 Y 1 A ARG 557 ? A ARG 354 
13 1 Y 1 A PRO 558 ? A PRO 355 
14 1 Y 1 A GLU 605 ? A GLU 402 
15 1 Y 1 A ALA 606 ? A ALA 403 
16 1 Y 1 A LEU 651 ? A LEU 448 
17 1 Y 1 A ASN 652 ? A ASN 449 
18 1 Y 1 A SER 653 ? A SER 450 
19 1 Y 1 A LYS 654 ? A LYS 451 
20 1 Y 1 A LEU 655 ? A LEU 452 
21 1 Y 1 A GLU 656 ? A GLU 453 
22 1 Y 1 A GLY 657 ? A GLY 454 
23 1 Y 1 A LYS 658 ? A LYS 455 
24 1 Y 1 A PRO 659 ? A PRO 456 
25 1 Y 1 A ILE 660 ? A ILE 457 
26 1 Y 1 A PRO 661 ? A PRO 458 
27 1 Y 1 A ASN 662 ? A ASN 459 
28 1 Y 1 A PRO 663 ? A PRO 460 
29 1 Y 1 A LEU 664 ? A LEU 461 
30 1 Y 1 A LEU 665 ? A LEU 462 
31 1 Y 1 A GLY 666 ? A GLY 463 
32 1 Y 1 A LEU 667 ? A LEU 464 
33 1 Y 1 A ASP 668 ? A ASP 465 
34 1 Y 1 A SER 669 ? A SER 466 
35 1 Y 1 A THR 670 ? A THR 467 
36 1 Y 1 A ARG 671 ? A ARG 468 
37 1 Y 1 A THR 672 ? A THR 469 
38 1 Y 1 A GLY 673 ? A GLY 470 
39 1 Y 1 A HIS 674 ? A HIS 471 
40 1 Y 1 A HIS 675 ? A HIS 472 
41 1 Y 1 A HIS 676 ? A HIS 473 
42 1 Y 1 A HIS 677 ? A HIS 474 
43 1 Y 1 A HIS 678 ? A HIS 475 
44 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  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
EDO C1   C  N N 89  
EDO O1   O  N N 90  
EDO C2   C  N N 91  
EDO O2   O  N N 92  
EDO H11  H  N N 93  
EDO H12  H  N N 94  
EDO HO1  H  N N 95  
EDO H21  H  N N 96  
EDO H22  H  N N 97  
EDO HO2  H  N N 98  
GLN N    N  N N 99  
GLN CA   C  N S 100 
GLN C    C  N N 101 
GLN O    O  N N 102 
GLN CB   C  N N 103 
GLN CG   C  N N 104 
GLN CD   C  N N 105 
GLN OE1  O  N N 106 
GLN NE2  N  N N 107 
GLN OXT  O  N N 108 
GLN H    H  N N 109 
GLN H2   H  N N 110 
GLN HA   H  N N 111 
GLN HB2  H  N N 112 
GLN HB3  H  N N 113 
GLN HG2  H  N N 114 
GLN HG3  H  N N 115 
GLN HE21 H  N N 116 
GLN HE22 H  N N 117 
GLN HXT  H  N N 118 
GLU N    N  N N 119 
GLU CA   C  N S 120 
GLU C    C  N N 121 
GLU O    O  N N 122 
GLU CB   C  N N 123 
GLU CG   C  N N 124 
GLU CD   C  N N 125 
GLU OE1  O  N N 126 
GLU OE2  O  N N 127 
GLU OXT  O  N N 128 
GLU H    H  N N 129 
GLU H2   H  N N 130 
GLU HA   H  N N 131 
GLU HB2  H  N N 132 
GLU HB3  H  N N 133 
GLU HG2  H  N N 134 
GLU HG3  H  N N 135 
GLU HE2  H  N N 136 
GLU HXT  H  N N 137 
GLY N    N  N N 138 
GLY CA   C  N N 139 
GLY C    C  N N 140 
GLY O    O  N N 141 
GLY OXT  O  N N 142 
GLY H    H  N N 143 
GLY H2   H  N N 144 
GLY HA2  H  N N 145 
GLY HA3  H  N N 146 
GLY HXT  H  N N 147 
HIS N    N  N N 148 
HIS CA   C  N S 149 
HIS C    C  N N 150 
HIS O    O  N N 151 
HIS CB   C  N N 152 
HIS CG   C  Y N 153 
HIS ND1  N  Y N 154 
HIS CD2  C  Y N 155 
HIS CE1  C  Y N 156 
HIS NE2  N  Y N 157 
HIS OXT  O  N N 158 
HIS H    H  N N 159 
HIS H2   H  N N 160 
HIS HA   H  N N 161 
HIS HB2  H  N N 162 
HIS HB3  H  N N 163 
HIS HD1  H  N N 164 
HIS HD2  H  N N 165 
HIS HE1  H  N N 166 
HIS HE2  H  N N 167 
HIS HXT  H  N N 168 
HOH O    O  N N 169 
HOH H1   H  N N 170 
HOH H2   H  N N 171 
ILE N    N  N N 172 
ILE CA   C  N S 173 
ILE C    C  N N 174 
ILE O    O  N N 175 
ILE CB   C  N S 176 
ILE CG1  C  N N 177 
ILE CG2  C  N N 178 
ILE CD1  C  N N 179 
ILE OXT  O  N N 180 
ILE H    H  N N 181 
ILE H2   H  N N 182 
ILE HA   H  N N 183 
ILE HB   H  N N 184 
ILE HG12 H  N N 185 
ILE HG13 H  N N 186 
ILE HG21 H  N N 187 
ILE HG22 H  N N 188 
ILE HG23 H  N N 189 
ILE HD11 H  N N 190 
ILE HD12 H  N N 191 
ILE HD13 H  N N 192 
ILE HXT  H  N N 193 
LEU N    N  N N 194 
LEU CA   C  N S 195 
LEU C    C  N N 196 
LEU O    O  N N 197 
LEU CB   C  N N 198 
LEU CG   C  N N 199 
LEU CD1  C  N N 200 
LEU CD2  C  N N 201 
LEU OXT  O  N N 202 
LEU H    H  N N 203 
LEU H2   H  N N 204 
LEU HA   H  N N 205 
LEU HB2  H  N N 206 
LEU HB3  H  N N 207 
LEU HG   H  N N 208 
LEU HD11 H  N N 209 
LEU HD12 H  N N 210 
LEU HD13 H  N N 211 
LEU HD21 H  N N 212 
LEU HD22 H  N N 213 
LEU HD23 H  N N 214 
LEU HXT  H  N N 215 
LYS N    N  N N 216 
LYS CA   C  N S 217 
LYS C    C  N N 218 
LYS O    O  N N 219 
LYS CB   C  N N 220 
LYS CG   C  N N 221 
LYS CD   C  N N 222 
LYS CE   C  N N 223 
LYS NZ   N  N N 224 
LYS OXT  O  N N 225 
LYS H    H  N N 226 
LYS H2   H  N N 227 
LYS HA   H  N N 228 
LYS HB2  H  N N 229 
LYS HB3  H  N N 230 
LYS HG2  H  N N 231 
LYS HG3  H  N N 232 
LYS HD2  H  N N 233 
LYS HD3  H  N N 234 
LYS HE2  H  N N 235 
LYS HE3  H  N N 236 
LYS HZ1  H  N N 237 
LYS HZ2  H  N N 238 
LYS HZ3  H  N N 239 
LYS HXT  H  N N 240 
MET N    N  N N 241 
MET CA   C  N S 242 
MET C    C  N N 243 
MET O    O  N N 244 
MET CB   C  N N 245 
MET CG   C  N N 246 
MET SD   S  N N 247 
MET CE   C  N N 248 
MET OXT  O  N N 249 
MET H    H  N N 250 
MET H2   H  N N 251 
MET HA   H  N N 252 
MET HB2  H  N N 253 
MET HB3  H  N N 254 
MET HG2  H  N N 255 
MET HG3  H  N N 256 
MET HE1  H  N N 257 
MET HE2  H  N N 258 
MET HE3  H  N N 259 
MET HXT  H  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 
PRO N    N  N N 284 
PRO CA   C  N S 285 
PRO C    C  N N 286 
PRO O    O  N N 287 
PRO CB   C  N N 288 
PRO CG   C  N N 289 
PRO CD   C  N N 290 
PRO OXT  O  N N 291 
PRO H    H  N N 292 
PRO HA   H  N N 293 
PRO HB2  H  N N 294 
PRO HB3  H  N N 295 
PRO HG2  H  N N 296 
PRO HG3  H  N N 297 
PRO HD2  H  N N 298 
PRO HD3  H  N N 299 
PRO HXT  H  N N 300 
SER N    N  N N 301 
SER CA   C  N S 302 
SER C    C  N N 303 
SER O    O  N N 304 
SER CB   C  N N 305 
SER OG   O  N N 306 
SER OXT  O  N N 307 
SER H    H  N N 308 
SER H2   H  N N 309 
SER HA   H  N N 310 
SER HB2  H  N N 311 
SER HB3  H  N N 312 
SER HG   H  N N 313 
SER HXT  H  N N 314 
THR N    N  N N 315 
THR CA   C  N S 316 
THR C    C  N N 317 
THR O    O  N N 318 
THR CB   C  N R 319 
THR OG1  O  N N 320 
THR CG2  C  N N 321 
THR OXT  O  N N 322 
THR H    H  N N 323 
THR H2   H  N N 324 
THR HA   H  N N 325 
THR HB   H  N N 326 
THR HG1  H  N N 327 
THR HG21 H  N N 328 
THR HG22 H  N N 329 
THR HG23 H  N N 330 
THR HXT  H  N N 331 
TRP N    N  N N 332 
TRP CA   C  N S 333 
TRP C    C  N N 334 
TRP O    O  N N 335 
TRP CB   C  N N 336 
TRP CG   C  Y N 337 
TRP CD1  C  Y N 338 
TRP CD2  C  Y N 339 
TRP NE1  N  Y N 340 
TRP CE2  C  Y N 341 
TRP CE3  C  Y N 342 
TRP CZ2  C  Y N 343 
TRP CZ3  C  Y N 344 
TRP CH2  C  Y N 345 
TRP OXT  O  N N 346 
TRP H    H  N N 347 
TRP H2   H  N N 348 
TRP HA   H  N N 349 
TRP HB2  H  N N 350 
TRP HB3  H  N N 351 
TRP HD1  H  N N 352 
TRP HE1  H  N N 353 
TRP HE3  H  N N 354 
TRP HZ2  H  N N 355 
TRP HZ3  H  N N 356 
TRP HH2  H  N N 357 
TRP HXT  H  N N 358 
TYR N    N  N N 359 
TYR CA   C  N S 360 
TYR C    C  N N 361 
TYR O    O  N N 362 
TYR CB   C  N N 363 
TYR CG   C  Y N 364 
TYR CD1  C  Y N 365 
TYR CD2  C  Y N 366 
TYR CE1  C  Y N 367 
TYR CE2  C  Y N 368 
TYR CZ   C  Y N 369 
TYR OH   O  N N 370 
TYR OXT  O  N N 371 
TYR H    H  N N 372 
TYR H2   H  N N 373 
TYR HA   H  N N 374 
TYR HB2  H  N N 375 
TYR HB3  H  N N 376 
TYR HD1  H  N N 377 
TYR HD2  H  N N 378 
TYR HE1  H  N N 379 
TYR HE2  H  N N 380 
TYR HH   H  N N 381 
TYR HXT  H  N N 382 
VAL N    N  N N 383 
VAL CA   C  N S 384 
VAL C    C  N N 385 
VAL O    O  N N 386 
VAL CB   C  N N 387 
VAL CG1  C  N N 388 
VAL CG2  C  N N 389 
VAL OXT  O  N N 390 
VAL H    H  N N 391 
VAL H2   H  N N 392 
VAL HA   H  N N 393 
VAL HB   H  N N 394 
VAL HG11 H  N N 395 
VAL HG12 H  N N 396 
VAL HG13 H  N N 397 
VAL HG21 H  N N 398 
VAL HG22 H  N N 399 
VAL HG23 H  N N 400 
VAL HXT  H  N N 401 
# 
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 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
# 
_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                    9MDO 
_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]   0.024411 
_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]   0.010044 
_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]   0.008306 
_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.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 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.
;
? 
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.
;
? 
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   ? -6.47150  80.94503 33.89377  1.000 52.37674 ? 211  LYS A N   1 
ATOM   2    C  CA  . LYS A 1 8   ? -6.98254  79.58554 33.73045  1.000 57.66464 ? 211  LYS A CA  1 
ATOM   3    C  C   . LYS A 1 8   ? -6.14286  78.78413 32.73054  1.000 54.86439 ? 211  LYS A C   1 
ATOM   4    O  O   . LYS A 1 8   ? -6.16396  79.06214 31.52702  1.000 50.84605 ? 211  LYS A O   1 
ATOM   5    C  CB  . LYS A 1 8   ? -8.44679  79.61784 33.28197  1.000 54.23642 ? 211  LYS A CB  1 
ATOM   6    C  CG  . LYS A 1 8   ? -9.15235  78.26704 33.33219  1.000 44.43488 ? 211  LYS A CG  1 
ATOM   7    N  N   . LYS A 1 9   ? -5.40773  77.79446 33.23654  1.000 47.58371 ? 212  LYS A N   1 
ATOM   8    C  CA  . LYS A 1 9   ? -4.55056  76.96884 32.39290  1.000 48.53912 ? 212  LYS A CA  1 
ATOM   9    C  C   . LYS A 1 9   ? -5.37296  76.09883 31.44351  1.000 43.97180 ? 212  LYS A C   1 
ATOM   10   O  O   . LYS A 1 9   ? -6.50487  75.70713 31.74005  1.000 40.74454 ? 212  LYS A O   1 
ATOM   11   C  CB  . LYS A 1 9   ? -3.65273  76.06864 33.24988  1.000 43.57350 ? 212  LYS A CB  1 
ATOM   12   C  CG  . LYS A 1 9   ? -2.61951  76.80443 34.08628  1.000 46.35033 ? 212  LYS A CG  1 
ATOM   13   C  CD  . LYS A 1 9   ? -1.62500  75.82672 34.70383  1.000 51.19803 ? 212  LYS A CD  1 
ATOM   14   C  CE  . LYS A 1 9   ? -0.53715  76.55005 35.49536  1.000 51.36372 ? 212  LYS A CE  1 
ATOM   15   N  NZ  . LYS A 1 9   ? -1.12170  77.44513 36.54512  1.000 47.74139 ? 212  LYS A NZ  1 
ATOM   16   N  N   . LYS A 1 10  ? -4.78318  75.78154 30.29496  1.000 35.10674 ? 213  LYS A N   1 
ATOM   17   C  CA  . LYS A 1 10  ? -5.40969  74.80336 29.41781  1.000 35.54459 ? 213  LYS A CA  1 
ATOM   18   C  C   . LYS A 1 10  ? -5.07104  73.39111 29.89093  1.000 35.37082 ? 213  LYS A C   1 
ATOM   19   O  O   . LYS A 1 10  ? -3.90063  73.09008 30.15124  1.000 31.21347 ? 213  LYS A O   1 
ATOM   20   C  CB  . LYS A 1 10  ? -4.96899  74.98755 27.96871  1.000 36.10583 ? 213  LYS A CB  1 
ATOM   21   C  CG  . LYS A 1 10  ? -5.72582  74.07245 27.01992  1.000 43.76567 ? 213  LYS A CG  1 
ATOM   22   C  CD  . LYS A 1 10  ? -5.06327  73.97787 25.66657  1.000 43.44551 ? 213  LYS A CD  1 
ATOM   23   C  CE  . LYS A 1 10  ? -5.65362  72.82545 24.85526  1.000 46.33984 ? 213  LYS A CE  1 
ATOM   24   N  NZ  . LYS A 1 10  ? -6.83443  73.22520 24.02162  1.000 53.93115 ? 213  LYS A NZ  1 
ATOM   25   N  N   . PRO A 1 11  ? -6.05813  72.51399 30.03217  1.000 33.29708 ? 214  PRO A N   1 
ATOM   26   C  CA  . PRO A 1 11  ? -5.76916  71.13723 30.44425  1.000 34.05336 ? 214  PRO A CA  1 
ATOM   27   C  C   . PRO A 1 11  ? -4.90099  70.41110 29.42157  1.000 35.95439 ? 214  PRO A C   1 
ATOM   28   O  O   . PRO A 1 11  ? -4.86046  70.75415 28.24072  1.000 33.56834 ? 214  PRO A O   1 
ATOM   29   C  CB  . PRO A 1 11  ? -7.16152  70.49957 30.54228  1.000 33.75275 ? 214  PRO A CB  1 
ATOM   30   C  CG  . PRO A 1 11  ? -8.10416  71.65379 30.70980  1.000 33.97821 ? 214  PRO A CG  1 
ATOM   31   C  CD  . PRO A 1 11  ? -7.50327  72.76163 29.89111  1.000 34.74902 ? 214  PRO A CD  1 
ATOM   32   N  N   . GLN A 1 12  ? -4.19271  69.38640 29.88992  1.000 35.20297 ? 215  GLN A N   1 
ATOM   33   C  CA  . GLN A 1 12  ? -3.41290  68.53616 28.99926  1.000 33.46558 ? 215  GLN A CA  1 
ATOM   34   C  C   . GLN A 1 12  ? -3.73089  67.07782 29.27887  1.000 30.55646 ? 215  GLN A C   1 
ATOM   35   O  O   . GLN A 1 12  ? -4.37313  66.73203 30.27790  1.000 31.67932 ? 215  GLN A O   1 
ATOM   36   C  CB  . GLN A 1 12  ? -1.90464  68.76244 29.15304  1.000 32.28323 ? 215  GLN A CB  1 
ATOM   37   C  CG  . GLN A 1 12  ? -1.47134  70.19013 28.97589  1.000 39.23941 ? 215  GLN A CG  1 
ATOM   38   C  CD  . GLN A 1 12  ? -0.05359  70.41175 29.45355  1.000 50.60941 ? 215  GLN A CD  1 
ATOM   39   O  OE1 . GLN A 1 12  ? 0.89373   69.85022 28.90006  1.000 55.21977 ? 215  GLN A OE1 1 
ATOM   40   N  NE2 . GLN A 1 12  ? 0.10104   71.22234 30.49688  1.000 47.62172 ? 215  GLN A NE2 1 
ATOM   41   N  N   . ILE A 1 13  ? -3.25863  66.21071 28.38166  1.000 29.44131 ? 216  ILE A N   1 
ATOM   42   C  CA  . ILE A 1 13  ? -3.27966  64.77900 28.62728  1.000 28.55617 ? 216  ILE A CA  1 
ATOM   43   C  C   . ILE A 1 13  ? -1.90423  64.20889 28.32236  1.000 30.17296 ? 216  ILE A C   1 
ATOM   44   O  O   . ILE A 1 13  ? -1.17228  64.71874 27.46981  1.000 32.53196 ? 216  ILE A O   1 
ATOM   45   C  CB  . ILE A 1 13  ? -4.37689  64.04393 27.82576  1.000 33.29956 ? 216  ILE A CB  1 
ATOM   46   C  CG1 . ILE A 1 13  ? -4.20065  64.22182 26.32368  1.000 35.39621 ? 216  ILE A CG1 1 
ATOM   47   C  CG2 . ILE A 1 13  ? -5.76347  64.50523 28.25129  1.000 24.82114 ? 216  ILE A CG2 1 
ATOM   48   C  CD1 . ILE A 1 13  ? -5.08591  63.23691 25.52091  1.000 33.84364 ? 216  ILE A CD1 1 
ATOM   49   N  N   . LYS A 1 14  ? -1.53650  63.16811 29.06618  1.000 28.12192 ? 217  LYS A N   1 
ATOM   50   C  CA  . LYS A 1 14  ? -0.25193  62.50624 28.90735  1.000 33.72952 ? 217  LYS A CA  1 
ATOM   51   C  C   . LYS A 1 14  ? -0.46013  61.00349 28.97718  1.000 30.67271 ? 217  LYS A C   1 
ATOM   52   O  O   . LYS A 1 14  ? -1.38094  60.51608 29.63585  1.000 31.63032 ? 217  LYS A O   1 
ATOM   53   C  CB  . LYS A 1 14  ? 0.77049   62.91771 29.98302  1.000 31.12720 ? 217  LYS A CB  1 
ATOM   54   C  CG  . LYS A 1 14  ? 1.29451   64.34460 29.90554  1.000 30.85893 ? 217  LYS A CG  1 
ATOM   55   C  CD  . LYS A 1 14  ? 2.33904   64.58143 30.99949  1.000 30.48127 ? 217  LYS A CD  1 
ATOM   56   N  N   . TYR A 1 15  ? 0.42854   60.27975 28.31014  1.000 30.33451 ? 218  TYR A N   1 
ATOM   57   C  CA  . TYR A 1 15  ? 0.43210   58.82784 28.28961  1.000 30.21397 ? 218  TYR A CA  1 
ATOM   58   C  C   . TYR A 1 15  ? 1.88034   58.37876 28.13247  1.000 40.04290 ? 218  TYR A C   1 
ATOM   59   O  O   . TYR A 1 15  ? 2.63964   59.00024 27.38606  1.000 36.55195 ? 218  TYR A O   1 
ATOM   60   C  CB  . TYR A 1 15  ? -0.42911  58.28240 27.14145  1.000 30.17903 ? 218  TYR A CB  1 
ATOM   61   C  CG  . TYR A 1 15  ? -0.37693  56.78210 27.05200  1.000 33.60510 ? 218  TYR A CG  1 
ATOM   62   C  CD1 . TYR A 1 15  ? -1.11520  55.99894 27.92463  1.000 34.43884 ? 218  TYR A CD1 1 
ATOM   63   C  CD2 . TYR A 1 15  ? 0.44100   56.14858 26.12732  1.000 33.02686 ? 218  TYR A CD2 1 
ATOM   64   C  CE1 . TYR A 1 15  ? -1.05625  54.63489 27.86890  1.000 35.16163 ? 218  TYR A CE1 1 
ATOM   65   C  CE2 . TYR A 1 15  ? 0.50878   54.77709 26.06022  1.000 33.61300 ? 218  TYR A CE2 1 
ATOM   66   C  CZ  . TYR A 1 15  ? -0.23950  54.02409 26.93268  1.000 37.24509 ? 218  TYR A CZ  1 
ATOM   67   O  OH  . TYR A 1 15  ? -0.17161  52.65108 26.87699  1.000 37.54699 ? 218  TYR A OH  1 
ATOM   68   N  N   . GLU A 1 16  ? 2.27322   57.30396 28.81920  1.000 38.63865 ? 219  GLU A N   1 
ATOM   69   C  CA  . GLU A 1 16  ? 3.65415   56.82548 28.68388  1.000 40.32059 ? 219  GLU A CA  1 
ATOM   70   C  C   . GLU A 1 16  ? 3.73590   55.94656 27.44062  1.000 41.74375 ? 219  GLU A C   1 
ATOM   71   O  O   . GLU A 1 16  ? 3.37076   54.76193 27.46966  1.000 37.63952 ? 219  GLU A O   1 
ATOM   72   C  CB  . GLU A 1 16  ? 4.11481   56.08931 29.94168  1.000 46.83806 ? 219  GLU A CB  1 
ATOM   73   C  CG  . GLU A 1 16  ? 5.53120   55.45164 29.88186  1.000 45.94387 ? 219  GLU A CG  1 
ATOM   74   C  CD  . GLU A 1 16  ? 6.57529   56.30143 29.15127  1.000 56.95002 ? 219  GLU A CD  1 
ATOM   75   O  OE1 . GLU A 1 16  ? 6.64139   56.22076 27.89962  1.000 57.03129 ? 219  GLU A OE1 1 
ATOM   76   O  OE2 . GLU A 1 16  ? 7.33617   57.04607 29.81834  1.000 56.74463 ? 219  GLU A OE2 1 
ATOM   77   N  N   . GLU A 1 17  ? 4.23330   56.53378 26.34042  1.000 35.13800 ? 220  GLU A N   1 
ATOM   78   C  CA  . GLU A 1 17  ? 4.22019   55.85732 25.04705  1.000 40.89290 ? 220  GLU A CA  1 
ATOM   79   C  C   . GLU A 1 17  ? 5.18738   54.67612 24.97900  1.000 38.42206 ? 220  GLU A C   1 
ATOM   80   O  O   . GLU A 1 17  ? 5.01133   53.80931 24.12068  1.000 40.18546 ? 220  GLU A O   1 
ATOM   81   C  CB  . GLU A 1 17  ? 4.52412   56.84801 23.91176  1.000 49.04386 ? 220  GLU A CB  1 
ATOM   82   C  CG  . GLU A 1 17  ? 3.30696   57.24672 23.05038  1.000 45.63095 ? 220  GLU A CG  1 
ATOM   83   C  CD  . GLU A 1 17  ? 3.67851   58.13879 21.84181  1.000 61.37917 ? 220  GLU A CD  1 
ATOM   84   O  OE1 . GLU A 1 17  ? 3.07034   59.22717 21.67865  1.000 52.95840 ? 220  GLU A OE1 1 
ATOM   85   O  OE2 . GLU A 1 17  ? 4.58214   57.75442 21.05710  1.000 60.38710 ? 220  GLU A OE2 1 
ATOM   86   N  N   . LYS A 1 18  ? 6.17616   54.59261 25.87305  1.000 43.28302 ? 221  LYS A N   1 
ATOM   87   C  CA  . LYS A 1 18  ? 6.98930   53.37773 25.96333  1.000 46.27525 ? 221  LYS A CA  1 
ATOM   88   C  C   . LYS A 1 18  ? 6.15112   52.12478 26.19589  1.000 46.09736 ? 221  LYS A C   1 
ATOM   89   O  O   . LYS A 1 18  ? 6.64240   51.01224 25.96987  1.000 42.53105 ? 221  LYS A O   1 
ATOM   90   C  CB  . LYS A 1 18  ? 8.02236   53.50891 27.08628  1.000 49.02847 ? 221  LYS A CB  1 
ATOM   91   N  N   . GLN A 1 19  ? 4.89450   52.28208 26.59498  1.000 37.01161 ? 222  GLN A N   1 
ATOM   92   C  CA  . GLN A 1 19  ? 4.03701   51.19116 27.03213  1.000 38.70964 ? 222  GLN A CA  1 
ATOM   93   C  C   . GLN A 1 19  ? 2.97117   50.91851 25.97994  1.000 33.15384 ? 222  GLN A C   1 
ATOM   94   O  O   . GLN A 1 19  ? 2.14657   51.79012 25.68846  1.000 37.44719 ? 222  GLN A O   1 
ATOM   95   C  CB  . GLN A 1 19  ? 3.40347   51.57064 28.36406  1.000 36.65822 ? 222  GLN A CB  1 
ATOM   96   C  CG  . GLN A 1 19  ? 2.56832   50.55336 29.03799  1.000 45.16551 ? 222  GLN A CG  1 
ATOM   97   C  CD  . GLN A 1 19  ? 2.39707   50.93563 30.48908  1.000 48.12965 ? 222  GLN A CD  1 
ATOM   98   O  OE1 . GLN A 1 19  ? 3.38236   51.04983 31.22158  1.000 57.45606 ? 222  GLN A OE1 1 
ATOM   99   N  NE2 . GLN A 1 19  ? 1.15585   51.19159 30.90288  1.000 45.23953 ? 222  GLN A NE2 1 
ATOM   100  N  N   . ALA A 1 20  ? 2.98837   49.72201 25.40723  1.000 34.04690 ? 223  ALA A N   1 
ATOM   101  C  CA  . ALA A 1 20  ? 1.89368   49.31413 24.54333  1.000 30.78392 ? 223  ALA A CA  1 
ATOM   102  C  C   . ALA A 1 20  ? 0.73024   48.82048 25.39489  1.000 32.20841 ? 223  ALA A C   1 
ATOM   103  O  O   . ALA A 1 20  ? 0.91446   48.37224 26.52462  1.000 30.70761 ? 223  ALA A O   1 
ATOM   104  C  CB  . ALA A 1 20  ? 2.33217   48.21462 23.57347  1.000 36.55683 ? 223  ALA A CB  1 
ATOM   105  N  N   . VAL A 1 21  ? -0.47657  48.91954 24.84184  1.000 32.33920 ? 224  VAL A N   1 
ATOM   106  C  CA  . VAL A 1 21  ? -1.68107  48.38435 25.46006  1.000 25.74322 ? 224  VAL A CA  1 
ATOM   107  C  C   . VAL A 1 21  ? -1.95787  47.03884 24.80406  1.000 31.11256 ? 224  VAL A C   1 
ATOM   108  O  O   . VAL A 1 21  ? -2.22226  46.97036 23.59707  1.000 23.44374 ? 224  VAL A O   1 
ATOM   109  C  CB  . VAL A 1 21  ? -2.87079  49.34230 25.29258  1.000 29.51153 ? 224  VAL A CB  1 
ATOM   110  C  CG1 . VAL A 1 21  ? -4.13342  48.70771 25.84857  1.000 25.62755 ? 224  VAL A CG1 1 
ATOM   111  C  CG2 . VAL A 1 21  ? -2.59216  50.69279 25.97131  1.000 25.60641 ? 224  VAL A CG2 1 
ATOM   112  N  N   . MET A 1 22  ? -1.88391  45.95535 25.57694  1.000 28.65223 ? 225  MET A N   1 
ATOM   113  C  CA  . MET A 1 22  ? -1.87360  44.61181 24.99957  1.000 30.71999 ? 225  MET A CA  1 
ATOM   114  C  C   . MET A 1 22  ? -3.01882  43.77226 25.54559  1.000 28.30245 ? 225  MET A C   1 
ATOM   115  O  O   . MET A 1 22  ? -2.82099  42.97341 26.46746  1.000 28.45042 ? 225  MET A O   1 
ATOM   116  C  CB  . MET A 1 22  ? -0.53322  43.92768 25.25376  1.000 32.68191 ? 225  MET A CB  1 
ATOM   117  C  CG  . MET A 1 22  ? 0.64449   44.72576 24.70611  1.000 35.17438 ? 225  MET A CG  1 
ATOM   118  S  SD  . MET A 1 22  ? 2.19905   43.81484 24.69029  1.000 50.88286 ? 225  MET A SD  1 
ATOM   119  C  CE  . MET A 1 22  ? 3.02517   44.52056 26.12458  1.000 47.31469 ? 225  MET A CE  1 
ATOM   120  N  N   . PRO A 1 23  ? -4.21380  43.88965 24.97126  1.000 25.40022 ? 226  PRO A N   1 
ATOM   121  C  CA  . PRO A 1 23  ? -5.32033  43.01728 25.39263  1.000 25.58094 ? 226  PRO A CA  1 
ATOM   122  C  C   . PRO A 1 23  ? -5.05574  41.55013 25.07765  1.000 29.56375 ? 226  PRO A C   1 
ATOM   123  O  O   . PRO A 1 23  ? -4.35198  41.21039 24.11958  1.000 27.96717 ? 226  PRO A O   1 
ATOM   124  C  CB  . PRO A 1 23  ? -6.51032  43.54208 24.58628  1.000 26.56814 ? 226  PRO A CB  1 
ATOM   125  C  CG  . PRO A 1 23  ? -5.89789  44.22911 23.40953  1.000 29.25373 ? 226  PRO A CG  1 
ATOM   126  C  CD  . PRO A 1 23  ? -4.59931  44.80144 23.88233  1.000 31.91752 ? 226  PRO A CD  1 
ATOM   127  N  N   . GLU A 1 24  ? -5.64904  40.67429 25.89028  1.000 26.36022 ? 227  GLU A N   1 
ATOM   128  C  CA  . GLU A 1 24  ? -5.53984  39.23434 25.66874  1.000 28.21214 ? 227  GLU A CA  1 
ATOM   129  C  C   . GLU A 1 24  ? -6.22446  38.84283 24.35380  1.000 29.89503 ? 227  GLU A C   1 
ATOM   130  O  O   . GLU A 1 24  ? -6.93604  39.63673 23.72950  1.000 25.83370 ? 227  GLU A O   1 
ATOM   131  C  CB  . GLU A 1 24  ? -6.14149  38.46177 26.84613  1.000 26.94895 ? 227  GLU A CB  1 
ATOM   132  C  CG  . GLU A 1 24  ? -5.24804  38.47478 28.10050  1.000 39.52189 ? 227  GLU A CG  1 
ATOM   133  C  CD  . GLU A 1 24  ? -5.75745  37.56905 29.24570  1.000 48.86327 ? 227  GLU A CD  1 
ATOM   134  O  OE1 . GLU A 1 24  ? -6.32885  38.08912 30.23517  1.000 50.62757 ? 227  GLU A OE1 1 
ATOM   135  O  OE2 . GLU A 1 24  ? -5.57847  36.32999 29.15931  1.000 57.67914 ? 227  GLU A OE2 1 
ATOM   136  N  N   . SER A 1 25  ? -6.01021  37.58903 23.92904  1.000 30.26457 ? 228  SER A N   1 
ATOM   137  C  CA  . SER A 1 25  ? -6.59427  37.14909 22.66108  1.000 29.49913 ? 228  SER A CA  1 
ATOM   138  C  C   . SER A 1 25  ? -8.11217  37.02275 22.74459  1.000 32.51381 ? 228  SER A C   1 
ATOM   139  O  O   . SER A 1 25  ? -8.79343  37.11086 21.71591  1.000 31.59745 ? 228  SER A O   1 
ATOM   140  C  CB  . SER A 1 25  ? -5.98063  35.81758 22.22856  1.000 33.50489 ? 228  SER A CB  1 
ATOM   141  O  OG  . SER A 1 25  ? -6.13063  34.85968 23.26379  1.000 34.64374 ? 228  SER A OG  1 
ATOM   142  N  N   . ALA A 1 26  ? -8.65475  36.81136 23.94380  1.000 27.88263 ? 229  ALA A N   1 
ATOM   143  C  CA  . ALA A 1 26  ? -10.09994 36.72906 24.12718  1.000 28.46740 ? 229  ALA A CA  1 
ATOM   144  C  C   . ALA A 1 26  ? -10.79548 37.99939 23.64378  1.000 28.15197 ? 229  ALA A C   1 
ATOM   145  O  O   . ALA A 1 26  ? -10.24932 39.10098 23.71808  1.000 25.54776 ? 229  ALA A O   1 
ATOM   146  C  CB  . ALA A 1 26  ? -10.43890 36.50374 25.60472  1.000 26.93963 ? 229  ALA A CB  1 
ATOM   147  N  N   . ALA A 1 27  ? -12.01918 37.83573 23.14713  1.000 26.22453 ? 230  ALA A N   1 
ATOM   148  C  CA  . ALA A 1 27  ? -12.86432 38.98289 22.84918  1.000 30.88793 ? 230  ALA A CA  1 
ATOM   149  C  C   . ALA A 1 27  ? -13.17770 39.75200 24.12699  1.000 33.65233 ? 230  ALA A C   1 
ATOM   150  O  O   . ALA A 1 27  ? -13.20462 39.19005 25.22517  1.000 37.64748 ? 230  ALA A O   1 
ATOM   151  C  CB  . ALA A 1 27  ? -14.16616 38.52916 22.19482  1.000 26.00093 ? 230  ALA A CB  1 
ATOM   152  N  N   . GLY A 1 28  ? -13.43295 41.04175 23.98538  1.000 31.23808 ? 231  GLY A N   1 
ATOM   153  C  CA  . GLY A 1 28  ? -13.88445 41.81846 25.12149  1.000 30.92089 ? 231  GLY A CA  1 
ATOM   154  C  C   . GLY A 1 28  ? -13.61848 43.29649 24.94366  1.000 30.49383 ? 231  GLY A C   1 
ATOM   155  O  O   . GLY A 1 28  ? -13.01519 43.74092 23.96606  1.000 32.67225 ? 231  GLY A O   1 
ATOM   156  N  N   . THR A 1 29  ? -14.08800 44.05171 25.93158  1.000 29.80926 ? 232  THR A N   1 
ATOM   157  C  CA  . THR A 1 29  ? -13.86479 45.49080 26.01888  1.000 28.87084 ? 232  THR A CA  1 
ATOM   158  C  C   . THR A 1 29  ? -12.71496 45.72988 27.00207  1.000 28.12385 ? 232  THR A C   1 
ATOM   159  O  O   . THR A 1 29  ? -12.84078 45.44336 28.19807  1.000 27.38725 ? 232  THR A O   1 
ATOM   160  C  CB  . THR A 1 29  ? -15.14405 46.20572 26.45802  1.000 36.22311 ? 232  THR A CB  1 
ATOM   161  O  OG1 . THR A 1 29  ? -16.18220 45.98355 25.48807  1.000 33.07101 ? 232  THR A OG1 1 
ATOM   162  C  CG2 . THR A 1 29  ? -14.90577 47.70476 26.60433  1.000 31.26996 ? 232  THR A CG2 1 
ATOM   163  N  N   . TYR A 1 30  ? -11.59767 46.23499 26.49191  1.000 23.81932 ? 233  TYR A N   1 
ATOM   164  C  CA  . TYR A 1 30  ? -10.36743 46.43595 27.24304  1.000 27.39606 ? 233  TYR A CA  1 
ATOM   165  C  C   . TYR A 1 30  ? -10.10353 47.92691 27.44448  1.000 28.56585 ? 233  TYR A C   1 
ATOM   166  O  O   . TYR A 1 30  ? -10.64867 48.78005 26.73444  1.000 25.66371 ? 233  TYR A O   1 
ATOM   167  C  CB  . TYR A 1 30  ? -9.18844  45.78290 26.51542  1.000 22.12412 ? 233  TYR A CB  1 
ATOM   168  C  CG  . TYR A 1 30  ? -9.32007  44.27522 26.38080  1.000 31.52780 ? 233  TYR A CG  1 
ATOM   169  C  CD1 . TYR A 1 30  ? -9.90380  43.69377 25.25701  1.000 26.53369 ? 233  TYR A CD1 1 
ATOM   170  C  CD2 . TYR A 1 30  ? -8.85771  43.43187 27.38416  1.000 31.16813 ? 233  TYR A CD2 1 
ATOM   171  C  CE1 . TYR A 1 30  ? -10.01512 42.30318 25.14701  1.000 27.86593 ? 233  TYR A CE1 1 
ATOM   172  C  CE2 . TYR A 1 30  ? -8.96487  42.04792 27.27928  1.000 26.97433 ? 233  TYR A CE2 1 
ATOM   173  C  CZ  . TYR A 1 30  ? -9.53663  41.49292 26.16921  1.000 25.31900 ? 233  TYR A CZ  1 
ATOM   174  O  OH  . TYR A 1 30  ? -9.63170  40.12176 26.09316  1.000 27.24190 ? 233  TYR A OH  1 
ATOM   175  N  N   . THR A 1 31  ? -9.25650  48.25036 28.42371  1.000 24.30731 ? 234  THR A N   1 
ATOM   176  C  CA  . THR A 1 31  ? -9.09507  49.64825 28.80030  1.000 21.93701 ? 234  THR A CA  1 
ATOM   177  C  C   . THR A 1 31  ? -7.63083  49.99831 29.02560  1.000 25.23081 ? 234  THR A C   1 
ATOM   178  O  O   . THR A 1 31  ? -6.77345  49.13102 29.21198  1.000 26.57051 ? 234  THR A O   1 
ATOM   179  C  CB  . THR A 1 31  ? -9.91447  50.00575 30.05596  1.000 22.60992 ? 234  THR A CB  1 
ATOM   180  O  OG1 . THR A 1 31  ? -9.39523  49.32305 31.20907  1.000 26.91294 ? 234  THR A OG1 1 
ATOM   181  C  CG2 . THR A 1 31  ? -11.37415 49.64418 29.85774  1.000 24.45546 ? 234  THR A CG2 1 
ATOM   182  N  N   . PHE A 1 32  ? -7.36085  51.30110 28.96555  1.000 25.21022 ? 235  PHE A N   1 
ATOM   183  C  CA  . PHE A 1 32  ? -6.10736  51.87053 29.42770  1.000 25.05177 ? 235  PHE A CA  1 
ATOM   184  C  C   . PHE A 1 32  ? -6.40638  53.25594 29.98202  1.000 26.79621 ? 235  PHE A C   1 
ATOM   185  O  O   . PHE A 1 32  ? -7.51230  53.78223 29.84083  1.000 25.37899 ? 235  PHE A O   1 
ATOM   186  C  CB  . PHE A 1 32  ? -5.06124  51.93684 28.31026  1.000 22.75973 ? 235  PHE A CB  1 
ATOM   187  C  CG  . PHE A 1 32  ? -5.46867  52.77866 27.14379  1.000 24.88164 ? 235  PHE A CG  1 
ATOM   188  C  CD1 . PHE A 1 32  ? -6.24099  52.23836 26.10921  1.000 25.96681 ? 235  PHE A CD1 1 
ATOM   189  C  CD2 . PHE A 1 32  ? -5.07600  54.11175 27.05757  1.000 26.89993 ? 235  PHE A CD2 1 
ATOM   190  C  CE1 . PHE A 1 32  ? -6.61740  53.02420 25.00774  1.000 22.73814 ? 235  PHE A CE1 1 
ATOM   191  C  CE2 . PHE A 1 32  ? -5.43974  54.89587 25.96253  1.000 25.76325 ? 235  PHE A CE2 1 
ATOM   192  C  CZ  . PHE A 1 32  ? -6.21037  54.35423 24.93875  1.000 24.24903 ? 235  PHE A CZ  1 
ATOM   193  N  N   . GLU A 1 33  ? -5.39924  53.85612 30.59609  1.000 25.78662 ? 236  GLU A N   1 
ATOM   194  C  CA  . GLU A 1 33  ? -5.57051  55.10070 31.31671  1.000 27.76334 ? 236  GLU A CA  1 
ATOM   195  C  C   . GLU A 1 33  ? -4.73097  56.18093 30.66301  1.000 30.42741 ? 236  GLU A C   1 
ATOM   196  O  O   . GLU A 1 33  ? -3.60433  55.93113 30.21764  1.000 28.59233 ? 236  GLU A O   1 
ATOM   197  C  CB  . GLU A 1 33  ? -5.18005  54.94030 32.80104  1.000 28.29799 ? 236  GLU A CB  1 
ATOM   198  C  CG  . GLU A 1 33  ? -6.05492  53.93927 33.52750  1.000 32.87243 ? 236  GLU A CG  1 
ATOM   199  C  CD  . GLU A 1 33  ? -5.64649  53.71459 34.97708  1.000 38.40087 ? 236  GLU A CD  1 
ATOM   200  O  OE1 . GLU A 1 33  ? -4.50678  54.06359 35.35488  1.000 42.51115 ? 236  GLU A OE1 1 
ATOM   201  O  OE2 . GLU A 1 33  ? -6.48012  53.19267 35.74239  1.000 36.48278 ? 236  GLU A OE2 1 
ATOM   202  N  N   . VAL A 1 34  ? -5.29231  57.38043 30.61848  1.000 28.32139 ? 237  VAL A N   1 
ATOM   203  C  CA  . VAL A 1 34  ? -4.60703  58.56880 30.14083  1.000 28.56673 ? 237  VAL A CA  1 
ATOM   204  C  C   . VAL A 1 34  ? -4.60410  59.58248 31.27971  1.000 29.57950 ? 237  VAL A C   1 
ATOM   205  O  O   . VAL A 1 34  ? -5.64792  59.83378 31.89178  1.000 25.86516 ? 237  VAL A O   1 
ATOM   206  C  CB  . VAL A 1 34  ? -5.30202  59.11869 28.88208  1.000 31.71653 ? 237  VAL A CB  1 
ATOM   207  C  CG1 . VAL A 1 34  ? -5.09477  60.61033 28.76033  1.000 32.13086 ? 237  VAL A CG1 1 
ATOM   208  C  CG2 . VAL A 1 34  ? -4.80628  58.37346 27.62534  1.000 27.24124 ? 237  VAL A CG2 1 
ATOM   209  N  N   A GLN A 1 35  ? -3.44050  60.15300 31.57300  0.506 29.63360 ? 238  GLN A N   1 
ATOM   210  N  N   B GLN A 1 35  ? -3.42853  60.13615 31.57570  0.494 29.47243 ? 238  GLN A N   1 
ATOM   211  C  CA  A GLN A 1 35  ? -3.33293  61.09665 32.67928  0.506 30.25940 ? 238  GLN A CA  1 
ATOM   212  C  CA  B GLN A 1 35  ? -3.30912  61.13335 32.63199  0.494 30.23585 ? 238  GLN A CA  1 
ATOM   213  C  C   A GLN A 1 35  ? -3.83008  62.47700 32.24788  0.506 30.71734 ? 238  GLN A C   1 
ATOM   214  C  C   B GLN A 1 35  ? -3.92835  62.45037 32.17866  0.494 30.79172 ? 238  GLN A C   1 
ATOM   215  O  O   A GLN A 1 35  ? -3.45542  62.97795 31.18492  0.506 28.72110 ? 238  GLN A O   1 
ATOM   216  O  O   B GLN A 1 35  ? -3.73620  62.88707 31.04186  0.494 28.44460 ? 238  GLN A O   1 
ATOM   217  C  CB  A GLN A 1 35  ? -1.89007  61.15963 33.18587  0.506 29.55131 ? 238  GLN A CB  1 
ATOM   218  C  CB  B GLN A 1 35  ? -1.83868  61.34226 33.01390  0.494 29.48312 ? 238  GLN A CB  1 
ATOM   219  C  CG  A GLN A 1 35  ? -1.53322  60.05311 34.19952  0.506 35.61860 ? 238  GLN A CG  1 
ATOM   220  C  CG  B GLN A 1 35  ? -1.62643  62.22549 34.24135  0.494 32.85745 ? 238  GLN A CG  1 
ATOM   221  C  CD  A GLN A 1 35  ? -1.50674  58.65172 33.59432  0.506 34.21732 ? 238  GLN A CD  1 
ATOM   222  C  CD  B GLN A 1 35  ? -0.16039  62.35874 34.64876  0.494 38.26086 ? 238  GLN A CD  1 
ATOM   223  O  OE1 A GLN A 1 35  ? -2.08807  57.70771 34.13939  0.506 33.81565 ? 238  GLN A OE1 1 
ATOM   224  O  OE1 B GLN A 1 35  ? 0.74596   62.20168 33.82941  0.494 40.87585 ? 238  GLN A OE1 1 
ATOM   225  N  NE2 A GLN A 1 35  ? -0.81427  58.50932 32.47377  0.506 37.25540 ? 238  GLN A NE2 1 
ATOM   226  N  NE2 B GLN A 1 35  ? 0.07303   62.65218 35.92282  0.494 32.43998 ? 238  GLN A NE2 1 
ATOM   227  N  N   . THR A 1 36  ? -4.69083  63.07628 33.06757  1.000 27.41891 ? 239  THR A N   1 
ATOM   228  C  CA  . THR A 1 36  ? -5.33749  64.34720 32.77494  1.000 27.43395 ? 239  THR A CA  1 
ATOM   229  C  C   . THR A 1 36  ? -4.75117  65.39927 33.70029  1.000 30.71277 ? 239  THR A C   1 
ATOM   230  O  O   . THR A 1 36  ? -4.92544  65.31349 34.92070  1.000 33.16242 ? 239  THR A O   1 
ATOM   231  C  CB  . THR A 1 36  ? -6.85935  64.24882 32.93974  1.000 29.44890 ? 239  THR A CB  1 
ATOM   232  O  OG1 . THR A 1 36  ? -7.17604  63.75117 34.24144  1.000 30.32812 ? 239  THR A OG1 1 
ATOM   233  C  CG2 . THR A 1 36  ? -7.45917  63.29814 31.89670  1.000 28.38778 ? 239  THR A CG2 1 
ATOM   234  N  N   . ILE A 1 37  ? -4.06866  66.38775 33.10964  1.000 33.07658 ? 240  ILE A N   1 
ATOM   235  C  CA  . ILE A 1 37  ? -3.28607  67.39964 33.81535  1.000 32.40850 ? 240  ILE A CA  1 
ATOM   236  C  C   . ILE A 1 37  ? -4.03636  68.72830 33.78888  1.000 34.84232 ? 240  ILE A C   1 
ATOM   237  O  O   . ILE A 1 37  ? -4.55916  69.13522 32.74484  1.000 33.67056 ? 240  ILE A O   1 
ATOM   238  C  CB  . ILE A 1 37  ? -1.88878  67.54508 33.16996  1.000 36.18899 ? 240  ILE A CB  1 
ATOM   239  C  CG1 . ILE A 1 37  ? -1.11787  66.21911 33.24742  1.000 38.35169 ? 240  ILE A CG1 1 
ATOM   240  C  CG2 . ILE A 1 37  ? -1.08128  68.70994 33.78546  1.000 29.56044 ? 240  ILE A CG2 1 
ATOM   241  C  CD1 . ILE A 1 37  ? -0.78962  65.79468 34.65645  1.000 42.68734 ? 240  ILE A CD1 1 
ATOM   242  N  N   . ASP A 1 38  ? -4.08845  69.39948 34.94875  1.000 32.69587 ? 241  ASP A N   1 
ATOM   243  C  CA  . ASP A 1 38  ? -4.68336  70.73534 35.10169  1.000 33.68970 ? 241  ASP A CA  1 
ATOM   244  C  C   . ASP A 1 38  ? -6.14907  70.76077 34.67859  1.000 35.76371 ? 241  ASP A C   1 
ATOM   245  O  O   . ASP A 1 38  ? -6.63517  71.74588 34.11352  1.000 33.85764 ? 241  ASP A O   1 
ATOM   246  C  CB  . ASP A 1 38  ? -3.88141  71.80331 34.34299  1.000 32.95170 ? 241  ASP A CB  1 
ATOM   247  C  CG  . ASP A 1 38  ? -2.52395  72.06841 34.97000  1.000 38.54417 ? 241  ASP A CG  1 
ATOM   248  O  OD1 . ASP A 1 38  ? -2.36704  71.86951 36.20263  1.000 46.73097 ? 241  ASP A OD1 1 
ATOM   249  O  OD2 . ASP A 1 38  ? -1.59843  72.47542 34.24440  1.000 42.18562 ? 241  ASP A OD2 1 
ATOM   250  N  N   . GLY A 1 39  ? -6.86279  69.68816 34.97351  1.000 31.65156 ? 242  GLY A N   1 
ATOM   251  C  CA  . GLY A 1 39  ? -8.26434  69.57608 34.62489  1.000 34.69784 ? 242  GLY A CA  1 
ATOM   252  C  C   . GLY A 1 39  ? -8.51310  68.53795 33.54420  1.000 36.82955 ? 242  GLY A C   1 
ATOM   253  O  O   . GLY A 1 39  ? -7.67336  67.68563 33.24211  1.000 32.29323 ? 242  GLY A O   1 
ATOM   254  N  N   . LYS A 1 40  ? -9.70580  68.62231 32.95250  1.000 37.64682 ? 243  LYS A N   1 
ATOM   255  C  CA  . LYS A 1 40  ? -10.19334 67.60879 32.02495  1.000 32.22558 ? 243  LYS A CA  1 
ATOM   256  C  C   . LYS A 1 40  ? -10.26751 68.20718 30.62272  1.000 38.89260 ? 243  LYS A C   1 
ATOM   257  O  O   . LYS A 1 40  ? -11.16021 69.00700 30.32599  1.000 36.95409 ? 243  LYS A O   1 
ATOM   258  C  CB  . LYS A 1 40  ? -11.54570 67.07876 32.48831  1.000 34.27556 ? 243  LYS A CB  1 
ATOM   259  C  CG  . LYS A 1 40  ? -11.46215 66.26104 33.76769  1.000 31.17308 ? 243  LYS A CG  1 
ATOM   260  C  CD  . LYS A 1 40  ? -10.67384 64.95367 33.51633  1.000 27.35661 ? 243  LYS A CD  1 
ATOM   261  C  CE  . LYS A 1 40  ? -10.66272 64.03458 34.74312  1.000 27.03679 ? 243  LYS A CE  1 
ATOM   262  N  NZ  . LYS A 1 40  ? -9.81432  62.79510 34.54523  1.000 27.67546 ? 243  LYS A NZ  1 
ATOM   263  N  N   . LEU A 1 41  ? -9.33133  67.81626 29.76641  1.000 31.43478 ? 244  LEU A N   1 
ATOM   264  C  CA  . LEU A 1 41  ? -9.32149  68.30900 28.39642  1.000 30.96986 ? 244  LEU A CA  1 
ATOM   265  C  C   . LEU A 1 41  ? -10.49206 67.71526 27.61952  1.000 37.37193 ? 244  LEU A C   1 
ATOM   266  O  O   . LEU A 1 41  ? -10.89729 66.57241 27.85503  1.000 33.98670 ? 244  LEU A O   1 
ATOM   267  C  CB  . LEU A 1 41  ? -7.99439  67.96014 27.71721  1.000 25.89237 ? 244  LEU A CB  1 
ATOM   268  C  CG  . LEU A 1 41  ? -7.84964  68.30417 26.21967  1.000 30.47885 ? 244  LEU A CG  1 
ATOM   269  C  CD1 . LEU A 1 41  ? -7.90550  69.82397 25.96235  1.000 37.02411 ? 244  LEU A CD1 1 
ATOM   270  C  CD2 . LEU A 1 41  ? -6.56842  67.71200 25.66470  1.000 29.67829 ? 244  LEU A CD2 1 
ATOM   271  N  N   . ASP A 1 42  ? -11.04147 68.50303 26.69262  1.000 32.34296 ? 245  ASP A N   1 
ATOM   272  C  CA  . ASP A 1 42  ? -12.17448 68.07941 25.86363  1.000 36.38021 ? 245  ASP A CA  1 
ATOM   273  C  C   . ASP A 1 42  ? -11.62697 67.51648 24.55781  1.000 36.17851 ? 245  ASP A C   1 
ATOM   274  O  O   . ASP A 1 42  ? -11.37047 68.24561 23.60001  1.000 41.29842 ? 245  ASP A O   1 
ATOM   275  C  CB  . ASP A 1 42  ? -13.12661 69.24747 25.61658  1.000 48.61282 ? 245  ASP A CB  1 
ATOM   276  C  CG  . ASP A 1 42  ? -14.38136 68.83574 24.86754  1.000 53.13566 ? 245  ASP A CG  1 
ATOM   277  O  OD1 . ASP A 1 42  ? -14.78769 67.65920 24.98194  1.000 50.53217 ? 245  ASP A OD1 1 
ATOM   278  O  OD2 . ASP A 1 42  ? -14.94993 69.68998 24.15049  1.000 56.30828 ? 245  ASP A OD2 1 
ATOM   279  N  N   . TYR A 1 43  ? -11.43899 66.19945 24.51608  1.000 38.53623 ? 246  TYR A N   1 
ATOM   280  C  CA  . TYR A 1 43  ? -10.83867 65.54007 23.36748  1.000 35.79699 ? 246  TYR A CA  1 
ATOM   281  C  C   . TYR A 1 43  ? -11.64311 64.30367 23.01199  1.000 35.80105 ? 246  TYR A C   1 
ATOM   282  O  O   . TYR A 1 43  ? -12.53704 63.87929 23.74834  1.000 32.93182 ? 246  TYR A O   1 
ATOM   283  C  CB  . TYR A 1 43  ? -9.38161  65.14484 23.63616  1.000 33.09245 ? 246  TYR A CB  1 
ATOM   284  C  CG  . TYR A 1 43  ? -9.24781  64.10473 24.71944  1.000 30.27859 ? 246  TYR A CG  1 
ATOM   285  C  CD1 . TYR A 1 43  ? -9.16950  64.47134 26.05767  1.000 35.07379 ? 246  TYR A CD1 1 
ATOM   286  C  CD2 . TYR A 1 43  ? -9.22556  62.75861 24.40891  1.000 30.50031 ? 246  TYR A CD2 1 
ATOM   287  C  CE1 . TYR A 1 43  ? -9.06302  63.51923 27.05136  1.000 31.43124 ? 246  TYR A CE1 1 
ATOM   288  C  CE2 . TYR A 1 43  ? -9.11773  61.81341 25.37651  1.000 29.73537 ? 246  TYR A CE2 1 
ATOM   289  C  CZ  . TYR A 1 43  ? -9.03604  62.19302 26.70242  1.000 32.90151 ? 246  TYR A CZ  1 
ATOM   290  O  OH  . TYR A 1 43  ? -8.92527  61.22223 27.66950  1.000 33.01106 ? 246  TYR A OH  1 
ATOM   291  N  N   . GLU A 1 44  ? -11.29786 63.71742 21.86627  1.000 34.29545 ? 247  GLU A N   1 
ATOM   292  C  CA  . GLU A 1 44  ? -11.94344 62.50846 21.40915  1.000 39.62624 ? 247  GLU A CA  1 
ATOM   293  C  C   . GLU A 1 44  ? -10.90334 61.52354 20.87822  1.000 31.57010 ? 247  GLU A C   1 
ATOM   294  O  O   . GLU A 1 44  ? -10.09116 61.88578 20.00477  1.000 34.51598 ? 247  GLU A O   1 
ATOM   295  C  CB  . GLU A 1 44  ? -12.98203 62.83622 20.33366  1.000 45.28434 ? 247  GLU A CB  1 
ATOM   296  C  CG  . GLU A 1 44  ? -13.77913 61.63543 19.86535  1.000 56.14555 ? 247  GLU A CG  1 
ATOM   297  C  CD  . GLU A 1 44  ? -14.89129 62.02190 18.90765  1.000 69.94636 ? 247  GLU A CD  1 
ATOM   298  O  OE1 . GLU A 1 44  ? -15.24123 61.18890 18.04042  1.000 61.10629 ? 247  GLU A OE1 1 
ATOM   299  O  OE2 . GLU A 1 44  ? -15.40796 63.16177 19.02431  1.000 72.36408 ? 247  GLU A OE2 1 
ATOM   300  N  N   . PRO A 1 45  ? -10.88246 60.29947 21.39090  1.000 33.18578 ? 248  PRO A N   1 
ATOM   301  C  CA  . PRO A 1 45  ? -9.96988  59.27741 20.86076  1.000 31.53468 ? 248  PRO A CA  1 
ATOM   302  C  C   . PRO A 1 45  ? -10.45440 58.73278 19.52942  1.000 32.40305 ? 248  PRO A C   1 
ATOM   303  O  O   . PRO A 1 45  ? -11.65493 58.62840 19.27982  1.000 37.62368 ? 248  PRO A O   1 
ATOM   304  C  CB  . PRO A 1 45  ? -10.00809 58.18480 21.93413  1.000 29.39986 ? 248  PRO A CB  1 
ATOM   305  C  CG  . PRO A 1 45  ? -11.38264 58.32506 22.53685  1.000 29.28443 ? 248  PRO A CG  1 
ATOM   306  C  CD  . PRO A 1 45  ? -11.70798 59.79781 22.50423  1.000 28.74090 ? 248  PRO A CD  1 
ATOM   307  N  N   . TYR A 1 46  ? -9.49777  58.37152 18.67093  1.000 35.24693 ? 249  TYR A N   1 
ATOM   308  C  CA  . TYR A 1 46  ? -9.80601  57.81588 17.35341  1.000 37.57340 ? 249  TYR A CA  1 
ATOM   309  C  C   . TYR A 1 46  ? -8.79083  56.74643 16.98566  1.000 31.69959 ? 249  TYR A C   1 
ATOM   310  O  O   . TYR A 1 46  ? -7.59377  56.90988 17.23979  1.000 31.69294 ? 249  TYR A O   1 
ATOM   311  C  CB  . TYR A 1 46  ? -9.76889  58.87353 16.23649  1.000 41.83171 ? 249  TYR A CB  1 
ATOM   312  C  CG  . TYR A 1 46  ? -10.83484 59.93747 16.25848  1.000 43.65203 ? 249  TYR A CG  1 
ATOM   313  C  CD1 . TYR A 1 46  ? -12.01810 59.78087 15.53742  1.000 46.09673 ? 249  TYR A CD1 1 
ATOM   314  C  CD2 . TYR A 1 46  ? -10.63472 61.12777 16.94795  1.000 44.97731 ? 249  TYR A CD2 1 
ATOM   315  C  CE1 . TYR A 1 46  ? -12.99145 60.76806 15.52881  1.000 50.80467 ? 249  TYR A CE1 1 
ATOM   316  C  CE2 . TYR A 1 46  ? -11.60577 62.12435 16.95572  1.000 52.14090 ? 249  TYR A CE2 1 
ATOM   317  C  CZ  . TYR A 1 46  ? -12.77832 61.93657 16.23995  1.000 61.26687 ? 249  TYR A CZ  1 
ATOM   318  O  OH  . TYR A 1 46  ? -13.73742 62.91819 16.24229  1.000 63.45923 ? 249  TYR A OH  1 
ATOM   319  N  N   . PHE A 1 47  ? -9.25467  55.67324 16.34585  1.000 31.56247 ? 250  PHE A N   1 
ATOM   320  C  CA  . PHE A 1 47  ? -8.31707  54.77110 15.68992  1.000 31.16311 ? 250  PHE A CA  1 
ATOM   321  C  C   . PHE A 1 47  ? -7.82014  55.41368 14.40596  1.000 35.51238 ? 250  PHE A C   1 
ATOM   322  O  O   . PHE A 1 47  ? -8.59002  56.03785 13.67160  1.000 37.38068 ? 250  PHE A O   1 
ATOM   323  C  CB  . PHE A 1 47  ? -8.95512  53.40965 15.39781  1.000 33.45852 ? 250  PHE A CB  1 
ATOM   324  C  CG  . PHE A 1 47  ? -9.08028  52.55238 16.61470  1.000 31.29913 ? 250  PHE A CG  1 
ATOM   325  C  CD1 . PHE A 1 47  ? -7.94851  52.00428 17.20389  1.000 29.16793 ? 250  PHE A CD1 1 
ATOM   326  C  CD2 . PHE A 1 47  ? -10.31464 52.33148 17.20116  1.000 31.55245 ? 250  PHE A CD2 1 
ATOM   327  C  CE1 . PHE A 1 47  ? -8.04346  51.22107 18.34807  1.000 32.62622 ? 250  PHE A CE1 1 
ATOM   328  C  CE2 . PHE A 1 47  ? -10.41745 51.56176 18.35622  1.000 35.27860 ? 250  PHE A CE2 1 
ATOM   329  C  CZ  . PHE A 1 47  ? -9.27796  51.00598 18.93119  1.000 31.20055 ? 250  PHE A CZ  1 
ATOM   330  N  N   . THR A 1 48  ? -6.51670  55.27081 14.14683  1.000 38.46951 ? 251  THR A N   1 
ATOM   331  C  CA  . THR A 1 48  ? -5.93368  55.83361 12.93585  1.000 35.40257 ? 251  THR A CA  1 
ATOM   332  C  C   . THR A 1 48  ? -6.43132  55.12911 11.68048  1.000 36.87926 ? 251  THR A C   1 
ATOM   333  O  O   . THR A 1 48  ? -6.34501  55.69735 10.59367  1.000 38.22136 ? 251  THR A O   1 
ATOM   334  C  CB  . THR A 1 48  ? -4.41147  55.76886 13.00383  1.000 35.71762 ? 251  THR A CB  1 
ATOM   335  O  OG1 . THR A 1 48  ? -3.99627  54.40195 13.05721  1.000 31.91285 ? 251  THR A OG1 1 
ATOM   336  C  CG2 . THR A 1 48  ? -3.89535  56.50511 14.24816  1.000 31.67219 ? 251  THR A CG2 1 
ATOM   337  N  N   . SER A 1 49  ? -6.95818  53.91664 11.80184  1.000 41.57599 ? 252  SER A N   1 
ATOM   338  C  CA  . SER A 1 49  ? -7.68445  53.27196 10.71778  1.000 45.86809 ? 252  SER A CA  1 
ATOM   339  C  C   . SER A 1 49  ? -9.07566  52.90981 11.21505  1.000 47.82107 ? 252  SER A C   1 
ATOM   340  O  O   . SER A 1 49  ? -9.21807  52.24885 12.24730  1.000 46.45965 ? 252  SER A O   1 
ATOM   341  C  CB  . SER A 1 49  ? -6.95760  52.02265 10.21503  1.000 48.43833 ? 252  SER A CB  1 
ATOM   342  O  OG  . SER A 1 49  ? -7.70990  51.39240 9.18854   1.000 57.79978 ? 252  SER A OG  1 
ATOM   343  N  N   . SER A 1 50  ? -10.09648 53.32328 10.47612  1.000 55.26543 ? 253  SER A N   1 
ATOM   344  C  CA  . SER A 1 50  ? -11.47013 53.03089 10.85959  1.000 61.50988 ? 253  SER A CA  1 
ATOM   345  C  C   . SER A 1 50  ? -11.96691 51.69091 10.33186  1.000 63.65996 ? 253  SER A C   1 
ATOM   346  O  O   . SER A 1 50  ? -13.02499 51.22157 10.76818  1.000 64.23199 ? 253  SER A O   1 
ATOM   347  C  CB  . SER A 1 50  ? -12.39386 54.14130 10.35963  1.000 61.34965 ? 253  SER A CB  1 
ATOM   348  O  OG  . SER A 1 50  ? -12.23412 54.29985 8.96070   1.000 66.36552 ? 253  SER A OG  1 
ATOM   349  N  N   . THR A 1 51  ? -11.22936 51.05819 9.42315   1.000 53.71151 ? 254  THR A N   1 
ATOM   350  C  CA  . THR A 1 51  ? -11.72735 49.90419 8.69190   1.000 61.26576 ? 254  THR A CA  1 
ATOM   351  C  C   . THR A 1 51  ? -11.19970 48.57500 9.22825   1.000 47.65396 ? 254  THR A C   1 
ATOM   352  O  O   . THR A 1 51  ? -11.39638 47.54333 8.58787   1.000 54.67464 ? 254  THR A O   1 
ATOM   353  C  CB  . THR A 1 51  ? -11.38606 50.04913 7.20660   1.000 56.48348 ? 254  THR A CB  1 
ATOM   354  O  OG1 . THR A 1 51  ? -9.96158  50.09080 7.03378   1.000 65.95674 ? 254  THR A OG1 1 
ATOM   355  C  CG2 . THR A 1 51  ? -11.98927 51.33017 6.65823   1.000 54.79343 ? 254  THR A CG2 1 
ATOM   356  N  N   . LEU A 1 52  ? -10.54750 48.57325 10.37472  1.000 45.64206 ? 255  LEU A N   1 
ATOM   357  C  CA  . LEU A 1 52  ? -10.04258 47.33454 10.96669  1.000 41.95814 ? 255  LEU A CA  1 
ATOM   358  C  C   . LEU A 1 52  ? -11.20154 46.42748 11.35787  1.000 43.16030 ? 255  LEU A C   1 
ATOM   359  O  O   . LEU A 1 52  ? -12.05569 46.83739 12.15495  1.000 41.26587 ? 255  LEU A O   1 
ATOM   360  C  CB  . LEU A 1 52  ? -9.19496  47.63742 12.18452  1.000 42.71686 ? 255  LEU A CB  1 
ATOM   361  C  CG  . LEU A 1 52  ? -7.90664  48.40310 11.93904  1.000 47.05912 ? 255  LEU A CG  1 
ATOM   362  C  CD1 . LEU A 1 52  ? -7.23879  48.68116 13.26913  1.000 39.64368 ? 255  LEU A CD1 1 
ATOM   363  C  CD2 . LEU A 1 52  ? -6.99875  47.60163 11.01105  1.000 49.41289 ? 255  LEU A CD2 1 
ATOM   364  N  N   . PRO A 1 53  ? -11.26823 45.19473 10.85012  1.000 39.31644 ? 256  PRO A N   1 
ATOM   365  C  CA  . PRO A 1 53  ? -12.44240 44.35853 11.13397  1.000 40.14604 ? 256  PRO A CA  1 
ATOM   366  C  C   . PRO A 1 53  ? -12.45267 43.74294 12.52577  1.000 35.29585 ? 256  PRO A C   1 
ATOM   367  O  O   . PRO A 1 53  ? -13.51531 43.28809 12.96262  1.000 37.82139 ? 256  PRO A O   1 
ATOM   368  C  CB  . PRO A 1 53  ? -12.37296 43.27918 10.04071  1.000 36.93607 ? 256  PRO A CB  1 
ATOM   369  C  CG  . PRO A 1 53  ? -10.92041 43.18194 9.70661   1.000 39.44635 ? 256  PRO A CG  1 
ATOM   370  C  CD  . PRO A 1 53  ? -10.35076 44.56504 9.88101   1.000 42.15858 ? 256  PRO A CD  1 
ATOM   371  N  N   . TRP A 1 54  ? -11.33570 43.71763 13.24349  1.000 37.07139 ? 257  TRP A N   1 
ATOM   372  C  CA  . TRP A 1 54  ? -11.30410 43.05752 14.54652  1.000 32.05744 ? 257  TRP A CA  1 
ATOM   373  C  C   . TRP A 1 54  ? -11.55739 44.01507 15.71187  1.000 39.73106 ? 257  TRP A C   1 
ATOM   374  O  O   . TRP A 1 54  ? -11.42412 43.61497 16.87666  1.000 34.49589 ? 257  TRP A O   1 
ATOM   375  C  CB  . TRP A 1 54  ? -9.97841  42.33016 14.73498  1.000 27.66124 ? 257  TRP A CB  1 
ATOM   376  C  CG  . TRP A 1 54  ? -8.73707  43.17183 14.57985  1.000 34.45147 ? 257  TRP A CG  1 
ATOM   377  C  CD1 . TRP A 1 54  ? -8.10055  43.48968 13.40990  1.000 36.22662 ? 257  TRP A CD1 1 
ATOM   378  C  CD2 . TRP A 1 54  ? -7.95352  43.75885 15.63307  1.000 29.33596 ? 257  TRP A CD2 1 
ATOM   379  N  NE1 . TRP A 1 54  ? -6.97798  44.24262 13.66896  1.000 30.23688 ? 257  TRP A NE1 1 
ATOM   380  C  CE2 . TRP A 1 54  ? -6.86695  44.42455 15.02472  1.000 27.57718 ? 257  TRP A CE2 1 
ATOM   381  C  CE3 . TRP A 1 54  ? -8.06390  43.78083 17.03175  1.000 34.24326 ? 257  TRP A CE3 1 
ATOM   382  C  CZ2 . TRP A 1 54  ? -5.90270  45.11370 15.76382  1.000 33.53150 ? 257  TRP A CZ2 1 
ATOM   383  C  CZ3 . TRP A 1 54  ? -7.09560  44.46630 17.77220  1.000 30.78201 ? 257  TRP A CZ3 1 
ATOM   384  C  CH2 . TRP A 1 54  ? -6.03414  45.12000 17.13510  1.000 33.24730 ? 257  TRP A CH2 1 
ATOM   385  N  N   . ILE A 1 55  ? -11.93704 45.25610 15.42868  1.000 36.57987 ? 258  ILE A N   1 
ATOM   386  C  CA  . ILE A 1 55  ? -12.29371 46.23278 16.44976  1.000 36.56214 ? 258  ILE A CA  1 
ATOM   387  C  C   . ILE A 1 55  ? -13.69676 46.72772 16.14338  1.000 37.75091 ? 258  ILE A C   1 
ATOM   388  O  O   . ILE A 1 55  ? -13.99557 47.08600 14.99769  1.000 37.21315 ? 258  ILE A O   1 
ATOM   389  C  CB  . ILE A 1 55  ? -11.28018 47.39215 16.49759  1.000 38.26826 ? 258  ILE A CB  1 
ATOM   390  C  CG1 . ILE A 1 55  ? -10.09779 47.00620 17.38749  1.000 41.00136 ? 258  ILE A CG1 1 
ATOM   391  C  CG2 . ILE A 1 55  ? -11.92780 48.66876 16.99253  1.000 39.92931 ? 258  ILE A CG2 1 
ATOM   392  C  CD1 . ILE A 1 55  ? -8.85511  47.81570 17.13817  1.000 41.60419 ? 258  ILE A CD1 1 
ATOM   393  N  N   . THR A 1 56  ? -14.55864 46.72084 17.15624  1.000 33.59460 ? 259  THR A N   1 
ATOM   394  C  CA  . THR A 1 56  ? -15.96898 47.08584 17.01326  1.000 36.20673 ? 259  THR A CA  1 
ATOM   395  C  C   . THR A 1 56  ? -16.14207 48.54494 17.42804  1.000 47.67645 ? 259  THR A C   1 
ATOM   396  O  O   . THR A 1 56  ? -16.22145 48.85068 18.62070  1.000 52.75629 ? 259  THR A O   1 
ATOM   397  C  CB  . THR A 1 56  ? -16.84919 46.17898 17.87136  1.000 43.70674 ? 259  THR A CB  1 
ATOM   398  O  OG1 . THR A 1 56  ? -16.50014 44.80666 17.65166  1.000 39.92334 ? 259  THR A OG1 1 
ATOM   399  C  CG2 . THR A 1 56  ? -18.31388 46.38218 17.53287  1.000 46.81824 ? 259  THR A CG2 1 
ATOM   400  N  N   . GLY A 1 57  ? -16.19685 49.45233 16.44927  1.000 40.07676 ? 260  GLY A N   1 
ATOM   401  C  CA  . GLY A 1 57  ? -16.47905 50.84784 16.73541  1.000 37.12234 ? 260  GLY A CA  1 
ATOM   402  C  C   . GLY A 1 57  ? -15.28243 51.66253 17.21197  1.000 36.65473 ? 260  GLY A C   1 
ATOM   403  O  O   . GLY A 1 57  ? -14.13966 51.20798 17.26703  1.000 40.27068 ? 260  GLY A O   1 
ATOM   404  N  N   . ALA A 1 58  ? -15.57306 52.91951 17.54647  1.000 33.46305 ? 261  ALA A N   1 
ATOM   405  C  CA  . ALA A 1 58  ? -14.57592 53.87752 17.99802  1.000 33.94810 ? 261  ALA A CA  1 
ATOM   406  C  C   . ALA A 1 58  ? -14.22961 53.64708 19.46681  1.000 32.34969 ? 261  ALA A C   1 
ATOM   407  O  O   . ALA A 1 58  ? -15.03484 53.10526 20.21876  1.000 33.83555 ? 261  ALA A O   1 
ATOM   408  C  CB  . ALA A 1 58  ? -15.09990 55.30221 17.81348  1.000 31.74461 ? 261  ALA A CB  1 
ATOM   409  N  N   . PRO A 1 59  ? -13.04013 54.05945 19.90054  1.000 30.20776 ? 262  PRO A N   1 
ATOM   410  C  CA  . PRO A 1 59  ? -12.74287 54.04946 21.33460  1.000 32.10664 ? 262  PRO A CA  1 
ATOM   411  C  C   . PRO A 1 59  ? -13.50349 55.16438 22.03280  1.000 35.51001 ? 262  PRO A C   1 
ATOM   412  O  O   . PRO A 1 59  ? -13.84170 56.18310 21.42547  1.000 36.55015 ? 262  PRO A O   1 
ATOM   413  C  CB  . PRO A 1 59  ? -11.23020 54.28514 21.38405  1.000 30.57525 ? 262  PRO A CB  1 
ATOM   414  C  CG  . PRO A 1 59  ? -10.92162 55.02873 20.12051  1.000 33.85186 ? 262  PRO A CG  1 
ATOM   415  C  CD  . PRO A 1 59  ? -11.95199 54.65921 19.10467  1.000 32.45538 ? 262  PRO A CD  1 
ATOM   416  N  N   . THR A 1 60  ? -13.79541 54.96774 23.31872  1.000 27.10508 ? 263  THR A N   1 
ATOM   417  C  CA  . THR A 1 60  ? -14.53356 55.97779 24.06576  1.000 27.86266 ? 263  THR A CA  1 
ATOM   418  C  C   . THR A 1 60  ? -13.88183 56.25733 25.40909  1.000 34.43810 ? 263  THR A C   1 
ATOM   419  O  O   . THR A 1 60  ? -13.16666 55.41888 25.97347  1.000 32.75422 ? 263  THR A O   1 
ATOM   420  C  CB  . THR A 1 60  ? -15.98621 55.57234 24.31124  1.000 34.55471 ? 263  THR A CB  1 
ATOM   421  O  OG1 . THR A 1 60  ? -16.01907 54.40947 25.14220  1.000 37.49566 ? 263  THR A OG1 1 
ATOM   422  C  CG2 . THR A 1 60  ? -16.70667 55.27593 22.99597  1.000 39.68369 ? 263  THR A CG2 1 
ATOM   423  N  N   . ILE A 1 61  ? -14.15663 57.44917 25.92619  1.000 30.67916 ? 264  ILE A N   1 
ATOM   424  C  CA  . ILE A 1 61  ? -13.81757 57.77984 27.30425  1.000 31.35165 ? 264  ILE A CA  1 
ATOM   425  C  C   . ILE A 1 61  ? -14.90854 57.17070 28.17363  1.000 31.76923 ? 264  ILE A C   1 
ATOM   426  O  O   . ILE A 1 61  ? -16.02820 57.67973 28.20852  1.000 33.51371 ? 264  ILE A O   1 
ATOM   427  C  CB  . ILE A 1 61  ? -13.72082 59.29567 27.51178  1.000 34.20488 ? 264  ILE A CB  1 
ATOM   428  C  CG1 . ILE A 1 61  ? -12.80585 59.92684 26.45654  1.000 32.74244 ? 264  ILE A CG1 1 
ATOM   429  C  CG2 . ILE A 1 61  ? -13.21269 59.62208 28.92003  1.000 27.35185 ? 264  ILE A CG2 1 
ATOM   430  C  CD1 . ILE A 1 61  ? -12.84676 61.43149 26.44076  1.000 30.52063 ? 264  ILE A CD1 1 
ATOM   431  N  N   . SER A 1 62  ? -14.60245 56.06205 28.84938  1.000 27.82703 ? 265  SER A N   1 
ATOM   432  C  CA  . SER A 1 62  ? -15.63296 55.40099 29.63396  1.000 28.65154 ? 265  SER A CA  1 
ATOM   433  C  C   . SER A 1 62  ? -15.68597 55.88323 31.07708  1.000 30.09009 ? 265  SER A C   1 
ATOM   434  O  O   . SER A 1 62  ? -16.63350 55.53818 31.78703  1.000 30.91178 ? 265  SER A O   1 
ATOM   435  C  CB  . SER A 1 62  ? -15.45858 53.87152 29.61954  1.000 30.70506 ? 265  SER A CB  1 
ATOM   436  O  OG  . SER A 1 62  ? -14.16310 53.47596 30.04236  1.000 33.15134 ? 265  SER A OG  1 
ATOM   437  N  N   . SER A 1 63  ? -14.71299 56.67224 31.52760  1.000 30.57553 ? 266  SER A N   1 
ATOM   438  C  CA  . SER A 1 63  ? -14.76352 57.19974 32.88823  1.000 29.20106 ? 266  SER A CA  1 
ATOM   439  C  C   . SER A 1 63  ? -13.84223 58.39980 33.01300  1.000 27.50444 ? 266  SER A C   1 
ATOM   440  O  O   . SER A 1 63  ? -12.67598 58.33560 32.60190  1.000 28.04408 ? 266  SER A O   1 
ATOM   441  C  CB  . SER A 1 63  ? -14.36454 56.13975 33.92234  1.000 29.97699 ? 266  SER A CB  1 
ATOM   442  O  OG  . SER A 1 63  ? -14.30572 56.73773 35.21591  1.000 36.47156 ? 266  SER A OG  1 
ATOM   443  N  N   . ARG A 1 64  ? -14.37111 59.48598 33.58308  1.000 28.79342 ? 267  ARG A N   1 
ATOM   444  C  CA  . ARG A 1 64  ? -13.58358 60.65951 33.94142  1.000 27.80064 ? 267  ARG A CA  1 
ATOM   445  C  C   . ARG A 1 64  ? -13.69739 60.98968 35.42597  1.000 34.10164 ? 267  ARG A C   1 
ATOM   446  O  O   . ARG A 1 64  ? -13.33480 62.09254 35.83206  1.000 30.26413 ? 267  ARG A O   1 
ATOM   447  C  CB  . ARG A 1 64  ? -14.01840 61.86998 33.11386  1.000 32.17534 ? 267  ARG A CB  1 
ATOM   448  C  CG  . ARG A 1 64  ? -14.17885 61.58051 31.63332  1.000 28.79723 ? 267  ARG A CG  1 
ATOM   449  C  CD  . ARG A 1 64  ? -14.13717 62.84916 30.78981  1.000 32.73729 ? 267  ARG A CD  1 
ATOM   450  N  NE  . ARG A 1 64  ? -12.77596 63.34551 30.61736  1.000 34.17208 ? 267  ARG A NE  1 
ATOM   451  C  CZ  . ARG A 1 64  ? -12.45681 64.38528 29.85799  1.000 40.41400 ? 267  ARG A CZ  1 
ATOM   452  N  NH1 . ARG A 1 64  ? -13.38055 65.06383 29.19318  1.000 34.24701 ? 267  ARG A NH1 1 
ATOM   453  N  NH2 . ARG A 1 64  ? -11.18006 64.75371 29.76094  1.000 33.06461 ? 267  ARG A NH2 1 
ATOM   454  N  N   . THR A 1 65  ? -14.19291 60.06070 36.25150  1.000 32.86057 ? 268  THR A N   1 
ATOM   455  C  CA  . THR A 1 65  ? -14.50336 60.42534 37.63037  1.000 33.22390 ? 268  THR A CA  1 
ATOM   456  C  C   . THR A 1 65  ? -13.25392 60.60878 38.48181  1.000 35.34023 ? 268  THR A C   1 
ATOM   457  O  O   . THR A 1 65  ? -13.30444 61.31869 39.49150  1.000 35.11486 ? 268  THR A O   1 
ATOM   458  C  CB  . THR A 1 65  ? -15.42370 59.38326 38.26717  1.000 37.12934 ? 268  THR A CB  1 
ATOM   459  O  OG1 . THR A 1 65  ? -14.73794 58.12860 38.36580  1.000 39.15745 ? 268  THR A OG1 1 
ATOM   460  C  CG2 . THR A 1 65  ? -16.68867 59.20863 37.42362  1.000 34.64640 ? 268  THR A CG2 1 
ATOM   461  N  N   . ASP A 1 66  ? -12.14608 60.00256 38.10787  1.000 26.96439 ? 269  ASP A N   1 
ATOM   462  C  CA  . ASP A 1 66  ? -10.89555 60.25619 38.80179  1.000 32.63438 ? 269  ASP A CA  1 
ATOM   463  C  C   . ASP A 1 66  ? -10.27858 61.53060 38.24029  1.000 31.87490 ? 269  ASP A C   1 
ATOM   464  O  O   . ASP A 1 66  ? -9.96121  61.57021 37.04619  1.000 27.09219 ? 269  ASP A O   1 
ATOM   465  C  CB  . ASP A 1 66  ? -9.94183  59.08051 38.62105  1.000 30.14229 ? 269  ASP A CB  1 
ATOM   466  C  CG  . ASP A 1 66  ? -8.65423  59.22439 39.43104  1.000 36.10312 ? 269  ASP A CG  1 
ATOM   467  O  OD1 . ASP A 1 66  ? -8.15832  60.35934 39.64453  1.000 31.45838 ? 269  ASP A OD1 1 
ATOM   468  O  OD2 . ASP A 1 66  ? -8.12401  58.17619 39.84840  1.000 40.09410 ? 269  ASP A OD2 1 
ATOM   469  N  N   . PRO A 1 67  ? -10.08598 62.58078 39.05259  1.000 32.26664 ? 270  PRO A N   1 
ATOM   470  C  CA  . PRO A 1 67  ? -9.56558  63.84391 38.50217  1.000 32.89691 ? 270  PRO A CA  1 
ATOM   471  C  C   . PRO A 1 67  ? -8.20792  63.70244 37.84944  1.000 30.42518 ? 270  PRO A C   1 
ATOM   472  O  O   . PRO A 1 67  ? -7.86873  64.51769 36.99232  1.000 27.60641 ? 270  PRO A O   1 
ATOM   473  C  CB  . PRO A 1 67  ? -9.50394  64.77023 39.72840  1.000 32.92965 ? 270  PRO A CB  1 
ATOM   474  C  CG  . PRO A 1 67  ? -10.50555 64.19671 40.67926  1.000 31.86050 ? 270  PRO A CG  1 
ATOM   475  C  CD  . PRO A 1 67  ? -10.40655 62.69983 40.48341  1.000 33.13358 ? 270  PRO A CD  1 
ATOM   476  N  N   . ASN A 1 68  ? -7.42592  62.69079 38.20174  1.000 29.05403 ? 271  ASN A N   1 
ATOM   477  C  CA  . ASN A 1 68  ? -6.10271  62.55684 37.61313  1.000 30.11724 ? 271  ASN A CA  1 
ATOM   478  C  C   . ASN A 1 68  ? -6.06430  61.71247 36.34866  1.000 27.68901 ? 271  ASN A C   1 
ATOM   479  O  O   . ASN A 1 68  ? -5.02512  61.69854 35.68551  1.000 28.95003 ? 271  ASN A O   1 
ATOM   480  C  CB  . ASN A 1 68  ? -5.11997  61.93624 38.60340  1.000 34.13660 ? 271  ASN A CB  1 
ATOM   481  C  CG  . ASN A 1 68  ? -4.92947  62.77670 39.84220  1.000 38.15498 ? 271  ASN A CG  1 
ATOM   482  O  OD1 . ASN A 1 68  ? -5.21203  63.97698 39.85477  1.000 44.70869 ? 271  ASN A OD1 1 
ATOM   483  N  ND2 . ASN A 1 68  ? -4.43748  62.14630 40.89552  1.000 42.08719 ? 271  ASN A ND2 1 
ATOM   484  N  N   . LYS A 1 69  ? -7.12431  60.98320 36.00426  1.000 27.13917 ? 272  LYS A N   1 
ATOM   485  C  CA  . LYS A 1 69  ? -6.99126  60.13070 34.82799  1.000 29.47373 ? 272  LYS A CA  1 
ATOM   486  C  C   . LYS A 1 69  ? -8.34661  59.87977 34.18739  1.000 28.23495 ? 272  LYS A C   1 
ATOM   487  O  O   . LYS A 1 69  ? -9.37831  59.85892 34.86492  1.000 28.84865 ? 272  LYS A O   1 
ATOM   488  C  CB  . LYS A 1 69  ? -6.31979  58.79146 35.17485  1.000 27.71576 ? 272  LYS A CB  1 
ATOM   489  C  CG  . LYS A 1 69  ? -7.18299  57.87297 36.01450  1.000 34.34942 ? 272  LYS A CG  1 
ATOM   490  C  CD  . LYS A 1 69  ? -6.37354  56.71152 36.58246  1.000 43.07857 ? 272  LYS A CD  1 
ATOM   491  C  CE  . LYS A 1 69  ? -7.18048  55.88096 37.59486  1.000 41.81322 ? 272  LYS A CE  1 
ATOM   492  N  NZ  . LYS A 1 69  ? -6.36460  54.72965 38.06879  1.000 43.24480 ? 272  LYS A NZ  1 
ATOM   493  N  N   . ASP A 1 70  ? -8.31718  59.69028 32.86651  1.000 23.56739 ? 273  ASP A N   1 
ATOM   494  C  CA  . ASP A 1 70  ? -9.43726  59.19088 32.08465  1.000 27.32762 ? 273  ASP A CA  1 
ATOM   495  C  C   . ASP A 1 70  ? -9.21996  57.71040 31.77799  1.000 28.03993 ? 273  ASP A C   1 
ATOM   496  O  O   . ASP A 1 70  ? -8.08632  57.25436 31.60709  1.000 29.17266 ? 273  ASP A O   1 
ATOM   497  C  CB  . ASP A 1 70  ? -9.58733  59.96649 30.76595  1.000 23.82529 ? 273  ASP A CB  1 
ATOM   498  C  CG  . ASP A 1 70  ? -10.14463 61.37739 30.95460  1.000 32.19837 ? 273  ASP A CG  1 
ATOM   499  O  OD1 . ASP A 1 70  ? -10.82049 61.64911 31.96728  1.000 28.26090 ? 273  ASP A OD1 1 
ATOM   500  O  OD2 . ASP A 1 70  ? -9.92257  62.22206 30.05407  1.000 34.31446 ? 273  ASP A OD2 1 
ATOM   501  N  N   . VAL A 1 71  ? -10.31383 56.95909 31.71667  1.000 24.30409 ? 274  VAL A N   1 
ATOM   502  C  CA  . VAL A 1 71  ? -10.28375 55.56925 31.27576  1.000 22.77661 ? 274  VAL A CA  1 
ATOM   503  C  C   . VAL A 1 71  ? -10.83307 55.50689 29.84833  1.000 30.51724 ? 274  VAL A C   1 
ATOM   504  O  O   . VAL A 1 71  ? -11.95379 55.96263 29.57552  1.000 27.16828 ? 274  VAL A O   1 
ATOM   505  C  CB  . VAL A 1 71  ? -11.07095 54.65266 32.22702  1.000 23.40316 ? 274  VAL A CB  1 
ATOM   506  C  CG1 . VAL A 1 71  ? -10.92064 53.18958 31.81369  1.000 23.27820 ? 274  VAL A CG1 1 
ATOM   507  C  CG2 . VAL A 1 71  ? -10.60175 54.83178 33.69093  1.000 23.61140 ? 274  VAL A CG2 1 
ATOM   508  N  N   . ILE A 1 72  ? -10.03432 54.95745 28.93700  1.000 25.04764 ? 275  ILE A N   1 
ATOM   509  C  CA  . ILE A 1 72  ? -10.41627 54.78332 27.53612  1.000 23.92935 ? 275  ILE A CA  1 
ATOM   510  C  C   . ILE A 1 72  ? -10.76953 53.31862 27.31607  1.000 28.79109 ? 275  ILE A C   1 
ATOM   511  O  O   . ILE A 1 72  ? -9.99422  52.43097 27.69754  1.000 26.57229 ? 275  ILE A O   1 
ATOM   512  C  CB  . ILE A 1 72  ? -9.27539  55.19404 26.58993  1.000 23.15035 ? 275  ILE A CB  1 
ATOM   513  C  CG1 . ILE A 1 72  ? -8.78618  56.61994 26.86670  1.000 26.35920 ? 275  ILE A CG1 1 
ATOM   514  C  CG2 . ILE A 1 72  ? -9.70391  55.00447 25.12732  1.000 28.06185 ? 275  ILE A CG2 1 
ATOM   515  C  CD1 . ILE A 1 72  ? -9.86127  57.66037 26.76344  1.000 27.94688 ? 275  ILE A CD1 1 
ATOM   516  N  N   . SER A 1 73  ? -11.91804 53.06459 26.68294  1.000 25.18471 ? 276  SER A N   1 
ATOM   517  C  CA  . SER A 1 73  ? -12.37569 51.72213 26.35196  1.000 23.92757 ? 276  SER A CA  1 
ATOM   518  C  C   . SER A 1 73  ? -12.42874 51.50781 24.83959  1.000 28.46041 ? 276  SER A C   1 
ATOM   519  O  O   . SER A 1 73  ? -12.74042 52.42568 24.07506  1.000 29.44619 ? 276  SER A O   1 
ATOM   520  C  CB  . SER A 1 73  ? -13.76824 51.44809 26.92879  1.000 24.60877 ? 276  SER A CB  1 
ATOM   521  O  OG  . SER A 1 73  ? -13.75399 51.44909 28.34633  1.000 31.99662 ? 276  SER A OG  1 
ATOM   522  N  N   . PHE A 1 74  ? -12.15472 50.26925 24.42433  1.000 27.83423 ? 277  PHE A N   1 
ATOM   523  C  CA  . PHE A 1 74  ? -12.34432 49.81739 23.04825  1.000 30.24264 ? 277  PHE A CA  1 
ATOM   524  C  C   . PHE A 1 74  ? -12.64508 48.32499 23.08481  1.000 32.60985 ? 277  PHE A C   1 
ATOM   525  O  O   . PHE A 1 74  ? -12.28055 47.62348 24.03810  1.000 25.95370 ? 277  PHE A O   1 
ATOM   526  C  CB  . PHE A 1 74  ? -11.11370 50.08828 22.17460  1.000 23.80127 ? 277  PHE A CB  1 
ATOM   527  C  CG  . PHE A 1 74  ? -9.88818  49.39669 22.66092  1.000 25.76843 ? 277  PHE A CG  1 
ATOM   528  C  CD1 . PHE A 1 74  ? -9.16385  49.91981 23.72427  1.000 28.44996 ? 277  PHE A CD1 1 
ATOM   529  C  CD2 . PHE A 1 74  ? -9.47392  48.20742 22.09014  1.000 33.09766 ? 277  PHE A CD2 1 
ATOM   530  C  CE1 . PHE A 1 74  ? -8.04506  49.27864 24.20623  1.000 30.20891 ? 277  PHE A CE1 1 
ATOM   531  C  CE2 . PHE A 1 74  ? -8.34907  47.55338 22.56577  1.000 29.66218 ? 277  PHE A CE2 1 
ATOM   532  C  CZ  . PHE A 1 74  ? -7.63401  48.08555 23.62613  1.000 31.91127 ? 277  PHE A CZ  1 
ATOM   533  N  N   . THR A 1 75  ? -13.30091 47.83600 22.03003  1.000 29.94862 ? 278  THR A N   1 
ATOM   534  C  CA  . THR A 1 75  ? -13.79406 46.46476 21.99486  1.000 30.95062 ? 278  THR A CA  1 
ATOM   535  C  C   . THR A 1 75  ? -13.13507 45.67526 20.87328  1.000 34.00435 ? 278  THR A C   1 
ATOM   536  O  O   . THR A 1 75  ? -13.11640 46.12059 19.71785  1.000 35.94769 ? 278  THR A O   1 
ATOM   537  C  CB  . THR A 1 75  ? -15.31417 46.44244 21.85520  1.000 33.14054 ? 278  THR A CB  1 
ATOM   538  O  OG1 . THR A 1 75  ? -15.88398 47.09314 22.99533  1.000 34.00352 ? 278  THR A OG1 1 
ATOM   539  C  CG2 . THR A 1 75  ? -15.83544 45.00476 21.80798  1.000 36.21136 ? 278  THR A CG2 1 
ATOM   540  N  N   . CYS A 1 76  ? -12.60570 44.50350 21.22990  1.000 28.92582 ? 279  CYS A N   1 
ATOM   541  C  CA  . CYS A 1 76  ? -11.89702 43.60384 20.33165  1.000 30.64993 ? 279  CYS A CA  1 
ATOM   542  C  C   . CYS A 1 76  ? -12.70714 42.33615 20.11040  1.000 33.17866 ? 279  CYS A C   1 
ATOM   543  O  O   . CYS A 1 76  ? -13.36330 41.83716 21.03272  1.000 29.86859 ? 279  CYS A O   1 
ATOM   544  C  CB  . CYS A 1 76  ? -10.53485 43.20486 20.90126  1.000 27.86258 ? 279  CYS A CB  1 
ATOM   545  S  SG  . CYS A 1 76  ? -9.34938  44.52531 21.11375  1.000 35.62934 ? 279  CYS A SG  1 
ATOM   546  N  N   . LEU A 1 77  ? -12.67199 41.83117 18.88009  1.000 31.14456 ? 280  LEU A N   1 
ATOM   547  C  CA  . LEU A 1 77  ? -13.06109 40.45278 18.62815  1.000 33.78258 ? 280  LEU A CA  1 
ATOM   548  C  C   . LEU A 1 77  ? -11.96105 39.51497 19.11206  1.000 27.30929 ? 280  LEU A C   1 
ATOM   549  O  O   . LEU A 1 77  ? -10.81654 39.92034 19.34793  1.000 23.70612 ? 280  LEU A O   1 
ATOM   550  C  CB  . LEU A 1 77  ? -13.31203 40.21029 17.13373  1.000 32.47850 ? 280  LEU A CB  1 
ATOM   551  C  CG  . LEU A 1 77  ? -14.38333 41.05951 16.46185  1.000 32.72370 ? 280  LEU A CG  1 
ATOM   552  C  CD1 . LEU A 1 77  ? -14.55821 40.63338 14.99300  1.000 33.59251 ? 280  LEU A CD1 1 
ATOM   553  C  CD2 . LEU A 1 77  ? -15.68243 40.92732 17.21820  1.000 33.83555 ? 280  LEU A CD2 1 
ATOM   554  N  N   . LYS A 1 78  ? -12.30899 38.24197 19.24612  1.000 28.08519 ? 281  LYS A N   1 
ATOM   555  C  CA  . LYS A 1 78  ? -11.28558 37.26580 19.56941  1.000 26.57227 ? 281  LYS A CA  1 
ATOM   556  C  C   . LYS A 1 78  ? -10.25047 37.23217 18.44971  1.000 32.06853 ? 281  LYS A C   1 
ATOM   557  O  O   . LYS A 1 78  ? -10.59173 37.27769 17.26468  1.000 27.94423 ? 281  LYS A O   1 
ATOM   558  C  CB  . LYS A 1 78  ? -11.91283 35.88456 19.77960  1.000 32.00499 ? 281  LYS A CB  1 
ATOM   559  C  CG  . LYS A 1 78  ? -10.90985 34.80358 20.14376  1.000 33.48962 ? 281  LYS A CG  1 
ATOM   560  C  CD  . LYS A 1 78  ? -11.56433 33.42392 20.20010  1.000 34.87765 ? 281  LYS A CD  1 
ATOM   561  C  CE  . LYS A 1 78  ? -10.51454 32.34622 20.42214  1.000 36.81770 ? 281  LYS A CE  1 
ATOM   562  N  NZ  . LYS A 1 78  ? -11.11339 30.99454 20.32172  1.000 44.80440 ? 281  LYS A NZ  1 
ATOM   563  N  N   . ASN A 1 79  ? -8.97654  37.20064 18.83311  1.000 28.42451 ? 282  ASN A N   1 
ATOM   564  C  CA  . ASN A 1 79  ? -7.88324  36.93391 17.89763  1.000 28.51547 ? 282  ASN A CA  1 
ATOM   565  C  C   . ASN A 1 79  ? -7.73399  35.41383 17.78781  1.000 32.21275 ? 282  ASN A C   1 
ATOM   566  O  O   . ASN A 1 79  ? -7.22542  34.75752 18.69944  1.000 30.22830 ? 282  ASN A O   1 
ATOM   567  C  CB  . ASN A 1 79  ? -6.60016  37.60695 18.37594  1.000 25.35230 ? 282  ASN A CB  1 
ATOM   568  C  CG  . ASN A 1 79  ? -5.46425  37.51358 17.36455  1.000 26.49689 ? 282  ASN A CG  1 
ATOM   569  O  OD1 . ASN A 1 79  ? -5.65490  37.05927 16.23956  1.000 26.50776 ? 282  ASN A OD1 1 
ATOM   570  N  ND2 . ASN A 1 79  ? -4.27232  37.96528 17.76404  1.000 22.90774 ? 282  ASN A ND2 1 
ATOM   571  N  N   . LYS A 1 80  ? -8.21006  34.84766 16.68015  1.000 31.23834 ? 283  LYS A N   1 
ATOM   572  C  CA  . LYS A 1 80  ? -8.07012  33.41900 16.43240  1.000 35.51967 ? 283  LYS A CA  1 
ATOM   573  C  C   . LYS A 1 80  ? -6.72694  33.05238 15.81957  1.000 36.41288 ? 283  LYS A C   1 
ATOM   574  O  O   . LYS A 1 80  ? -6.36820  31.87056 15.82638  1.000 40.13951 ? 283  LYS A O   1 
ATOM   575  C  CB  . LYS A 1 80  ? -9.18269  32.93308 15.50947  1.000 30.88020 ? 283  LYS A CB  1 
ATOM   576  C  CG  . LYS A 1 80  ? -10.55934 33.11917 16.07499  1.000 35.27513 ? 283  LYS A CG  1 
ATOM   577  C  CD  . LYS A 1 80  ? -11.62077 32.73055 15.06726  1.000 39.31095 ? 283  LYS A CD  1 
ATOM   578  C  CE  . LYS A 1 80  ? -12.99724 33.12550 15.57571  1.000 45.24444 ? 283  LYS A CE  1 
ATOM   579  N  NZ  . LYS A 1 80  ? -14.10896 32.50422 14.80301  1.000 45.58493 ? 283  LYS A NZ  1 
ATOM   580  N  N   . THR A 1 81  ? -5.98844  34.02986 15.29569  1.000 34.19051 ? 284  THR A N   1 
ATOM   581  C  CA  . THR A 1 81  ? -4.72000  33.81021 14.61639  1.000 30.39514 ? 284  THR A CA  1 
ATOM   582  C  C   . THR A 1 81  ? -3.58982  33.63573 15.62128  1.000 29.72024 ? 284  THR A C   1 
ATOM   583  O  O   . THR A 1 81  ? -3.71977  33.97341 16.80033  1.000 30.16757 ? 284  THR A O   1 
ATOM   584  C  CB  . THR A 1 81  ? -4.37603  34.99271 13.71694  1.000 29.72260 ? 284  THR A CB  1 
ATOM   585  O  OG1 . THR A 1 81  ? -3.81375  36.04885 14.52147  1.000 28.00946 ? 284  THR A OG1 1 
ATOM   586  C  CG2 . THR A 1 81  ? -5.61387  35.48158 13.00366  1.000 28.47827 ? 284  THR A CG2 1 
ATOM   587  N  N   . VAL A 1 82  ? -2.44909  33.14913 15.12791  1.000 24.00192 ? 285  VAL A N   1 
ATOM   588  C  CA  . VAL A 1 82  ? -1.27597  32.93435 15.96879  1.000 26.42186 ? 285  VAL A CA  1 
ATOM   589  C  C   . VAL A 1 82  ? -0.33219  34.13024 15.90431  1.000 29.12595 ? 285  VAL A C   1 
ATOM   590  O  O   . VAL A 1 82  ? 0.85521   34.00631 16.22459  1.000 29.05958 ? 285  VAL A O   1 
ATOM   591  C  CB  . VAL A 1 82  ? -0.54386  31.62602 15.59385  1.000 32.12325 ? 285  VAL A CB  1 
ATOM   592  C  CG1 . VAL A 1 82  ? -1.49071  30.45605 15.72000  1.000 33.23922 ? 285  VAL A CG1 1 
ATOM   593  C  CG2 . VAL A 1 82  ? 0.04573   31.69590 14.17993  1.000 30.46405 ? 285  VAL A CG2 1 
ATOM   594  N  N   . TRP A 1 83  ? -0.85563  35.30185 15.52938  1.000 31.96544 ? 286  TRP A N   1 
ATOM   595  C  CA  . TRP A 1 83  ? -0.05739  36.51343 15.38594  1.000 32.01819 ? 286  TRP A CA  1 
ATOM   596  C  C   . TRP A 1 83  ? -0.62135  37.64577 16.24132  1.000 34.46095 ? 286  TRP A C   1 
ATOM   597  O  O   . TRP A 1 83  ? -1.84272  37.78019 16.37764  1.000 32.30656 ? 286  TRP A O   1 
ATOM   598  C  CB  . TRP A 1 83  ? -0.01938  36.96634 13.92247  1.000 31.97319 ? 286  TRP A CB  1 
ATOM   599  C  CG  . TRP A 1 83  ? 0.42867   35.92118 12.92732  1.000 33.38742 ? 286  TRP A CG  1 
ATOM   600  C  CD1 . TRP A 1 83  ? 1.58048   35.18558 12.96828  1.000 31.80893 ? 286  TRP A CD1 1 
ATOM   601  C  CD2 . TRP A 1 83  ? -0.24847  35.53721 11.71628  1.000 28.35779 ? 286  TRP A CD2 1 
ATOM   602  N  NE1 . TRP A 1 83  ? 1.65409   34.36225 11.86961  1.000 30.89388 ? 286  TRP A NE1 1 
ATOM   603  C  CE2 . TRP A 1 83  ? 0.54451   34.55891 11.08744  1.000 28.93956 ? 286  TRP A CE2 1 
ATOM   604  C  CE3 . TRP A 1 83  ? -1.44942  35.91669 11.11501  1.000 28.28148 ? 286  TRP A CE3 1 
ATOM   605  C  CZ2 . TRP A 1 83  ? 0.17714   33.96170 9.88312   1.000 29.54766 ? 286  TRP A CZ2 1 
ATOM   606  C  CZ3 . TRP A 1 83  ? -1.81162  35.32583 9.91521   1.000 34.24834 ? 286  TRP A CZ3 1 
ATOM   607  C  CH2 . TRP A 1 83  ? -1.00329  34.35249 9.31779   1.000 31.21761 ? 286  TRP A CH2 1 
ATOM   608  N  N   . ASN A 1 84  ? 0.26702   38.46491 16.80860  1.000 31.92683 ? 287  ASN A N   1 
ATOM   609  C  CA  . ASN A 1 84  ? -0.17392  39.73209 17.36935  1.000 33.13114 ? 287  ASN A CA  1 
ATOM   610  C  C   . ASN A 1 84  ? -0.72829  40.60337 16.25201  1.000 34.60618 ? 287  ASN A C   1 
ATOM   611  O  O   . ASN A 1 84  ? -0.29204  40.51981 15.10125  1.000 29.84633 ? 287  ASN A O   1 
ATOM   612  C  CB  . ASN A 1 84  ? 0.97047   40.48932 18.03253  1.000 38.34816 ? 287  ASN A CB  1 
ATOM   613  C  CG  . ASN A 1 84  ? 1.69945   39.68928 19.08367  1.000 38.30712 ? 287  ASN A CG  1 
ATOM   614  O  OD1 . ASN A 1 84  ? 2.91571   39.81465 19.20319  1.000 44.55666 ? 287  ASN A OD1 1 
ATOM   615  N  ND2 . ASN A 1 84  ? 0.97783   38.88709 19.86249  1.000 36.36449 ? 287  ASN A ND2 1 
ATOM   616  N  N   . ARG A 1 85  ? -1.68841  41.45522 16.58573  1.000 25.84056 ? 288  ARG A N   1 
ATOM   617  C  CA  . ARG A 1 85  ? -2.20151  42.39505 15.59685  1.000 30.99849 ? 288  ARG A CA  1 
ATOM   618  C  C   . ARG A 1 85  ? -2.28827  43.78932 16.20615  1.000 33.15213 ? 288  ARG A C   1 
ATOM   619  O  O   . ARG A 1 85  ? -2.59354  43.94572 17.39741  1.000 25.87299 ? 288  ARG A O   1 
ATOM   620  C  CB  . ARG A 1 85  ? -3.54768  41.93732 15.03683  1.000 28.08247 ? 288  ARG A CB  1 
ATOM   621  C  CG  . ARG A 1 85  ? -4.55876  41.49420 16.08125  1.000 32.43250 ? 288  ARG A CG  1 
ATOM   622  C  CD  . ARG A 1 85  ? -5.75095  40.87661 15.37898  1.000 27.19885 ? 288  ARG A CD  1 
ATOM   623  N  NE  . ARG A 1 85  ? -6.87301  40.65892 16.27592  1.000 25.27447 ? 288  ARG A NE  1 
ATOM   624  C  CZ  . ARG A 1 85  ? -7.95193  39.96897 15.94848  1.000 28.34945 ? 288  ARG A CZ  1 
ATOM   625  N  NH1 . ARG A 1 85  ? -8.06067  39.38425 14.76724  1.000 29.38330 ? 288  ARG A NH1 1 
ATOM   626  N  NH2 . ARG A 1 85  ? -8.94688  39.86247 16.82668  1.000 24.23156 ? 288  ARG A NH2 1 
ATOM   627  N  N   . ARG A 1 86  ? -2.01123  44.79874 15.38539  1.000 26.45728 ? 289  ARG A N   1 
ATOM   628  C  CA  . ARG A 1 86  ? -1.70032  46.13268 15.87230  1.000 32.46038 ? 289  ARG A CA  1 
ATOM   629  C  C   . ARG A 1 86  ? -2.75035  47.14453 15.43283  1.000 35.17791 ? 289  ARG A C   1 
ATOM   630  O  O   . ARG A 1 86  ? -3.25115  47.09977 14.30008  1.000 36.76825 ? 289  ARG A O   1 
ATOM   631  C  CB  . ARG A 1 86  ? -0.31368  46.57746 15.39020  1.000 35.02962 ? 289  ARG A CB  1 
ATOM   632  C  CG  . ARG A 1 86  ? 0.81062   45.60378 15.75025  1.000 35.82848 ? 289  ARG A CG  1 
ATOM   633  C  CD  . ARG A 1 86  ? 2.18034   46.26800 15.62558  1.000 41.04416 ? 289  ARG A CD  1 
ATOM   634  N  NE  . ARG A 1 86  ? 2.50300   47.04778 16.81969  1.000 54.01106 ? 289  ARG A NE  1 
ATOM   635  C  CZ  . ARG A 1 86  ? 3.40581   48.02080 16.87534  1.000 50.14529 ? 289  ARG A CZ  1 
ATOM   636  N  NH1 . ARG A 1 86  ? 4.11897   48.36758 15.81423  1.000 60.12609 ? 289  ARG A NH1 1 
ATOM   637  N  NH2 . ARG A 1 86  ? 3.58745   48.67356 18.02106  1.000 44.55370 ? 289  ARG A NH2 1 
ATOM   638  N  N   . ALA A 1 87  ? -3.07832  48.05952 16.34437  1.000 33.17509 ? 290  ALA A N   1 
ATOM   639  C  CA  . ALA A 1 87  ? -3.87038  49.23918 16.02701  1.000 31.41155 ? 290  ALA A CA  1 
ATOM   640  C  C   . ALA A 1 87  ? -3.28855  50.41919 16.79305  1.000 32.64658 ? 290  ALA A C   1 
ATOM   641  O  O   . ALA A 1 87  ? -2.41049  50.25983 17.64956  1.000 30.02025 ? 290  ALA A O   1 
ATOM   642  C  CB  . ALA A 1 87  ? -5.35212  49.03572 16.34560  1.000 26.91721 ? 290  ALA A CB  1 
ATOM   643  N  N   . TYR A 1 88  ? -3.77270  51.61838 16.46344  1.000 28.82961 ? 291  TYR A N   1 
ATOM   644  C  CA  . TYR A 1 88  ? -3.22855  52.85059 17.00938  1.000 31.72268 ? 291  TYR A CA  1 
ATOM   645  C  C   . TYR A 1 88  ? -4.36636  53.81074 17.30806  1.000 35.69589 ? 291  TYR A C   1 
ATOM   646  O  O   . TYR A 1 88  ? -5.29898  53.95364 16.50945  1.000 29.59457 ? 291  TYR A O   1 
ATOM   647  C  CB  . TYR A 1 88  ? -2.23323  53.50695 16.04296  1.000 28.39908 ? 291  TYR A CB  1 
ATOM   648  C  CG  . TYR A 1 88  ? -1.17514  52.54764 15.55317  1.000 36.59263 ? 291  TYR A CG  1 
ATOM   649  C  CD1 . TYR A 1 88  ? 0.02416   52.40178 16.23811  1.000 30.64367 ? 291  TYR A CD1 1 
ATOM   650  C  CD2 . TYR A 1 88  ? -1.38482  51.76840 14.41546  1.000 32.16117 ? 291  TYR A CD2 1 
ATOM   651  C  CE1 . TYR A 1 88  ? 0.98698   51.51508 15.80609  1.000 37.05605 ? 291  TYR A CE1 1 
ATOM   652  C  CE2 . TYR A 1 88  ? -0.42560  50.88201 13.97849  1.000 33.19502 ? 291  TYR A CE2 1 
ATOM   653  C  CZ  . TYR A 1 88  ? 0.75452   50.75928 14.67742  1.000 35.66034 ? 291  TYR A CZ  1 
ATOM   654  O  OH  . TYR A 1 88  ? 1.71192   49.87908 14.24541  1.000 45.95234 ? 291  TYR A OH  1 
ATOM   655  N  N   . ILE A 1 89  ? -4.28820  54.46142 18.46380  1.000 28.22833 ? 292  ILE A N   1 
ATOM   656  C  CA  . ILE A 1 89  ? -5.27021  55.45743 18.87066  1.000 31.35059 ? 292  ILE A CA  1 
ATOM   657  C  C   . ILE A 1 89  ? -4.57384  56.80179 18.96215  1.000 28.88358 ? 292  ILE A C   1 
ATOM   658  O  O   . ILE A 1 89  ? -3.51918  56.92110 19.59631  1.000 37.36572 ? 292  ILE A O   1 
ATOM   659  C  CB  . ILE A 1 89  ? -5.92983  55.09363 20.21250  1.000 31.85509 ? 292  ILE A CB  1 
ATOM   660  C  CG1 . ILE A 1 89  ? -6.82084  53.87170 20.02710  1.000 30.44721 ? 292  ILE A CG1 1 
ATOM   661  C  CG2 . ILE A 1 89  ? -6.72742  56.29155 20.75336  1.000 29.83191 ? 292  ILE A CG2 1 
ATOM   662  C  CD1 . ILE A 1 89  ? -7.34383  53.26681 21.30407  1.000 27.33611 ? 292  ILE A CD1 1 
ATOM   663  N  N   . LYS A 1 90  ? -5.16316  57.80908 18.34246  1.000 32.80254 ? 293  LYS A N   1 
ATOM   664  C  CA  . LYS A 1 90  ? -4.74454  59.19209 18.50955  1.000 33.85576 ? 293  LYS A CA  1 
ATOM   665  C  C   . LYS A 1 90  ? -5.89109  59.98515 19.12637  1.000 31.38615 ? 293  LYS A C   1 
ATOM   666  O  O   . LYS A 1 90  ? -7.01365  59.48863 19.26388  1.000 29.89364 ? 293  LYS A O   1 
ATOM   667  C  CB  . LYS A 1 90  ? -4.31417  59.80041 17.16999  1.000 33.47354 ? 293  LYS A CB  1 
ATOM   668  C  CG  . LYS A 1 90  ? -3.00339  59.25017 16.62410  1.000 36.24583 ? 293  LYS A CG  1 
ATOM   669  C  CD  . LYS A 1 90  ? -2.60009  60.03289 15.36558  1.000 39.13402 ? 293  LYS A CD  1 
ATOM   670  C  CE  . LYS A 1 90  ? -1.21997  59.65768 14.83432  1.000 43.73915 ? 293  LYS A CE  1 
ATOM   671  N  NZ  . LYS A 1 90  ? -0.80319  60.63401 13.76403  1.000 53.02025 ? 293  LYS A NZ  1 
ATOM   672  N  N   . PHE A 1 91  ? -5.60948  61.24239 19.47100  1.000 28.89853 ? 294  PHE A N   1 
ATOM   673  C  CA  . PHE A 1 91  ? -6.52929  62.04941 20.25980  1.000 31.77899 ? 294  PHE A CA  1 
ATOM   674  C  C   . PHE A 1 91  ? -6.69667  63.41577 19.62085  1.000 31.47619 ? 294  PHE A C   1 
ATOM   675  O  O   . PHE A 1 91  ? -5.71037  64.11256 19.36489  1.000 39.81461 ? 294  PHE A O   1 
ATOM   676  C  CB  . PHE A 1 91  ? -6.02487  62.19486 21.69690  1.000 25.68512 ? 294  PHE A CB  1 
ATOM   677  C  CG  . PHE A 1 91  ? -5.83333  60.88090 22.39401  1.000 31.91902 ? 294  PHE A CG  1 
ATOM   678  C  CD1 . PHE A 1 91  ? -4.64980  60.16701 22.25113  1.000 33.81378 ? 294  PHE A CD1 1 
ATOM   679  C  CD2 . PHE A 1 91  ? -6.84607  60.34133 23.16226  1.000 25.57961 ? 294  PHE A CD2 1 
ATOM   680  C  CE1 . PHE A 1 91  ? -4.47449  58.93865 22.88531  1.000 37.36827 ? 294  PHE A CE1 1 
ATOM   681  C  CE2 . PHE A 1 91  ? -6.67232  59.11515 23.81250  1.000 31.86832 ? 294  PHE A CE2 1 
ATOM   682  C  CZ  . PHE A 1 91  ? -5.48771  58.41951 23.67353  1.000 32.43389 ? 294  PHE A CZ  1 
ATOM   683  N  N   . LYS A 1 92  ? -7.93826  63.80670 19.39647  1.000 28.00382 ? 295  LYS A N   1 
ATOM   684  C  CA  . LYS A 1 92  ? -8.24838  65.05217 18.70526  1.000 33.10169 ? 295  LYS A CA  1 
ATOM   685  C  C   . LYS A 1 92  ? -8.80688  66.05576 19.71168  1.000 35.05275 ? 295  LYS A C   1 
ATOM   686  O  O   . LYS A 1 92  ? -9.76050  65.74950 20.43440  1.000 35.75117 ? 295  LYS A O   1 
ATOM   687  C  CB  . LYS A 1 92  ? -9.23551  64.80091 17.56523  1.000 37.43141 ? 295  LYS A CB  1 
ATOM   688  C  CG  . LYS A 1 92  ? -9.26362  65.89075 16.48248  1.000 49.68771 ? 295  LYS A CG  1 
ATOM   689  C  CD  . LYS A 1 92  ? -8.68558  65.38952 15.16677  1.000 55.27685 ? 295  LYS A CD  1 
ATOM   690  N  N   . ASP A 1 93  ? -8.19173  67.23518 19.77621  1.000 34.18516 ? 296  ASP A N   1 
ATOM   691  C  CA  . ASP A 1 93  ? -8.70569  68.33493 20.58863  1.000 38.69989 ? 296  ASP A CA  1 
ATOM   692  C  C   . ASP A 1 93  ? -10.01661 68.82902 19.97972  1.000 43.66898 ? 296  ASP A C   1 
ATOM   693  O  O   . ASP A 1 93  ? -10.03167 69.30195 18.83957  1.000 36.35363 ? 296  ASP A O   1 
ATOM   694  C  CB  . ASP A 1 93  ? -7.65268  69.44864 20.64583  1.000 45.32783 ? 296  ASP A CB  1 
ATOM   695  C  CG  . ASP A 1 93  ? -8.07589  70.65556 21.48923  1.000 47.36840 ? 296  ASP A CG  1 
ATOM   696  O  OD1 . ASP A 1 93  ? -9.15971  71.23253 21.24609  1.000 45.66307 ? 296  ASP A OD1 1 
ATOM   697  O  OD2 . ASP A 1 93  ? -7.29211  71.04627 22.38352  1.000 42.04581 ? 296  ASP A OD2 1 
ATOM   698  N  N   . LYS A 1 94  ? -11.12080 68.71775 20.72908  1.000 39.14449 ? 297  LYS A N   1 
ATOM   699  C  CA  . LYS A 1 94  ? -12.42899 68.99644 20.13143  1.000 45.54412 ? 297  LYS A CA  1 
ATOM   700  C  C   . LYS A 1 94  ? -12.61176 70.47329 19.80661  1.000 46.56819 ? 297  LYS A C   1 
ATOM   701  O  O   . LYS A 1 94  ? -13.36473 70.80577 18.89035  1.000 48.16577 ? 297  LYS A O   1 
ATOM   702  C  CB  . LYS A 1 94  ? -13.56383 68.51991 21.04395  1.000 48.41129 ? 297  LYS A CB  1 
ATOM   703  C  CG  . LYS A 1 94  ? -13.92894 67.03462 20.87514  1.000 52.28207 ? 297  LYS A CG  1 
ATOM   704  C  CD  . LYS A 1 94  ? -15.42924 66.79289 21.06699  1.000 58.13410 ? 297  LYS A CD  1 
ATOM   705  C  CE  . LYS A 1 94  ? -15.73059 66.08847 22.38203  1.000 58.99007 ? 297  LYS A CE  1 
ATOM   706  N  NZ  . LYS A 1 94  ? -17.02767 66.54008 22.97231  1.000 65.58151 ? 297  LYS A NZ  1 
ATOM   707  N  N   . LYS A 1 95  ? -11.93510 71.37006 20.52626  1.000 48.16790 ? 298  LYS A N   1 
ATOM   708  C  CA  . LYS A 1 95  ? -12.06978 72.79763 20.24042  1.000 49.85705 ? 298  LYS A CA  1 
ATOM   709  C  C   . LYS A 1 95  ? -11.22245 73.21031 19.04150  1.000 56.20095 ? 298  LYS A C   1 
ATOM   710  O  O   . LYS A 1 95  ? -11.72760 73.84434 18.10665  1.000 57.11844 ? 298  LYS A O   1 
ATOM   711  C  CB  . LYS A 1 95  ? -11.69679 73.62540 21.47168  1.000 46.81489 ? 298  LYS A CB  1 
ATOM   712  C  CG  . LYS A 1 95  ? -12.73993 73.57893 22.58242  1.000 52.14308 ? 298  LYS A CG  1 
ATOM   713  C  CD  . LYS A 1 95  ? -12.35256 74.47776 23.74602  1.000 53.88782 ? 298  LYS A CD  1 
ATOM   714  C  CE  . LYS A 1 95  ? -13.36866 74.40673 24.88652  1.000 60.40319 ? 298  LYS A CE  1 
ATOM   715  N  NZ  . LYS A 1 95  ? -13.45617 73.05155 25.51672  1.000 57.23008 ? 298  LYS A NZ  1 
ATOM   716  N  N   . THR A 1 96  ? -9.93621  72.84965 19.04063  1.000 50.29558 ? 299  THR A N   1 
ATOM   717  C  CA  . THR A 1 96  ? -9.02674  73.27310 17.98089  1.000 48.83071 ? 299  THR A CA  1 
ATOM   718  C  C   . THR A 1 96  ? -9.01932  72.34202 16.78343  1.000 48.29626 ? 299  THR A C   1 
ATOM   719  O  O   . THR A 1 96  ? -8.48072  72.71615 15.74084  1.000 50.52549 ? 299  THR A O   1 
ATOM   720  C  CB  . THR A 1 96  ? -7.58951  73.37712 18.49330  1.000 45.31439 ? 299  THR A CB  1 
ATOM   721  O  OG1 . THR A 1 96  ? -7.05822  72.05337 18.67145  1.000 44.80436 ? 299  THR A OG1 1 
ATOM   722  C  CG2 . THR A 1 96  ? -7.53460  74.16350 19.82367  1.000 50.57555 ? 299  THR A CG2 1 
ATOM   723  N  N   . GLY A 1 97  ? -9.55946  71.13399 16.90989  1.000 49.00755 ? 300  GLY A N   1 
ATOM   724  C  CA  . GLY A 1 97  ? -9.51596  70.18760 15.82026  1.000 45.72578 ? 300  GLY A CA  1 
ATOM   725  C  C   . GLY A 1 97  ? -8.15612  69.59336 15.53931  1.000 52.73203 ? 300  GLY A C   1 
ATOM   726  O  O   . GLY A 1 97  ? -8.04321  68.74796 14.63927  1.000 48.91699 ? 300  GLY A O   1 
ATOM   727  N  N   . GLN A 1 98  ? -7.12490  69.99769 16.27468  1.000 44.63259 ? 301  GLN A N   1 
ATOM   728  C  CA  . GLN A 1 98  ? -5.78416  69.46533 16.09011  1.000 44.76988 ? 301  GLN A CA  1 
ATOM   729  C  C   . GLN A 1 98  ? -5.60037  68.18075 16.88804  1.000 41.62402 ? 301  GLN A C   1 
ATOM   730  O  O   . GLN A 1 98  ? -6.25852  67.96134 17.90898  1.000 37.94172 ? 301  GLN A O   1 
ATOM   731  C  CB  . GLN A 1 98  ? -4.73356  70.49298 16.51631  1.000 48.55977 ? 301  GLN A CB  1 
ATOM   732  C  CG  . GLN A 1 98  ? -4.79664  71.81864 15.75230  1.000 47.21653 ? 301  GLN A CG  1 
ATOM   733  C  CD  . GLN A 1 98  ? -4.25889  71.70295 14.32489  1.000 62.85428 ? 301  GLN A CD  1 
ATOM   734  O  OE1 . GLN A 1 98  ? -3.22890  72.29517 13.99472  1.000 59.51313 ? 301  GLN A OE1 1 
ATOM   735  N  NE2 . GLN A 1 98  ? -4.95420  70.94071 13.47545  1.000 55.05117 ? 301  GLN A NE2 1 
ATOM   736  N  N   . TYR A 1 99  ? -4.70263  67.32463 16.40347  1.000 38.49296 ? 302  TYR A N   1 
ATOM   737  C  CA  . TYR A 1 99  ? -4.30689  66.14997 17.16214  1.000 38.35178 ? 302  TYR A CA  1 
ATOM   738  C  C   . TYR A 1 99  ? -3.42049  66.56196 18.32724  1.000 40.66255 ? 302  TYR A C   1 
ATOM   739  O  O   . TYR A 1 99  ? -2.53297  67.40481 18.18392  1.000 34.39869 ? 302  TYR A O   1 
ATOM   740  C  CB  . TYR A 1 99  ? -3.55593  65.15761 16.28580  1.000 42.54045 ? 302  TYR A CB  1 
ATOM   741  C  CG  . TYR A 1 99  ? -4.42157  64.32499 15.37836  1.000 50.97921 ? 302  TYR A CG  1 
ATOM   742  C  CD1 . TYR A 1 99  ? -5.36093  63.44034 15.89272  1.000 46.96945 ? 302  TYR A CD1 1 
ATOM   743  C  CD2 . TYR A 1 99  ? -4.27947  64.40465 14.00031  1.000 54.99984 ? 302  TYR A CD2 1 
ATOM   744  C  CE1 . TYR A 1 99  ? -6.14682  62.66608 15.05006  1.000 58.07843 ? 302  TYR A CE1 1 
ATOM   745  C  CE2 . TYR A 1 99  ? -5.05590  63.64269 13.15446  1.000 57.67091 ? 302  TYR A CE2 1 
ATOM   746  C  CZ  . TYR A 1 99  ? -5.98482  62.77240 13.67946  1.000 64.14521 ? 302  TYR A CZ  1 
ATOM   747  O  OH  . TYR A 1 99  ? -6.75242  62.01270 12.82467  1.000 72.39661 ? 302  TYR A OH  1 
ATOM   748  N  N   . ILE A 1 100 ? -3.64565  65.93755 19.48128  1.000 32.58466 ? 303  ILE A N   1 
ATOM   749  C  CA  . ILE A 1 100 ? -2.90824  66.30290 20.67994  1.000 32.28925 ? 303  ILE A CA  1 
ATOM   750  C  C   . ILE A 1 100 ? -1.48271  65.76626 20.59179  1.000 33.84495 ? 303  ILE A C   1 
ATOM   751  O  O   . ILE A 1 100 ? -1.23526  64.66875 20.07326  1.000 29.83992 ? 303  ILE A O   1 
ATOM   752  C  CB  . ILE A 1 100 ? -3.66438  65.78336 21.91647  1.000 36.95673 ? 303  ILE A CB  1 
ATOM   753  C  CG1 . ILE A 1 100 ? -4.90983  66.63975 22.14333  1.000 41.55411 ? 303  ILE A CG1 1 
ATOM   754  C  CG2 . ILE A 1 100 ? -2.78232  65.77629 23.15284  1.000 34.80645 ? 303  ILE A CG2 1 
ATOM   755  C  CD1 . ILE A 1 100 ? -6.11964  65.86350 22.55319  1.000 38.55755 ? 303  ILE A CD1 1 
ATOM   756  N  N   . LYS A 1 101 ? -0.53196  66.54980 21.08031  1.000 32.17177 ? 304  LYS A N   1 
ATOM   757  C  CA  . LYS A 1 101 ? 0.87268   66.21927 20.93049  1.000 34.26638 ? 304  LYS A CA  1 
ATOM   758  C  C   . LYS A 1 101 ? 1.32879   65.29097 22.04396  1.000 36.60816 ? 304  LYS A C   1 
ATOM   759  O  O   . LYS A 1 101 ? 0.77498   65.29037 23.14607  1.000 37.72090 ? 304  LYS A O   1 
ATOM   760  C  CB  . LYS A 1 101 ? 1.72335   67.48878 20.93048  1.000 41.10315 ? 304  LYS A CB  1 
ATOM   761  C  CG  . LYS A 1 101 ? 1.30970   68.48470 19.86081  1.000 47.81640 ? 304  LYS A CG  1 
ATOM   762  C  CD  . LYS A 1 101 ? 0.97053   67.75555 18.54931  1.000 44.32377 ? 304  LYS A CD  1 
ATOM   763  C  CE  . LYS A 1 101 ? 2.08005   67.86106 17.54086  1.000 48.88043 ? 304  LYS A CE  1 
ATOM   764  N  NZ  . LYS A 1 101 ? 1.64177   67.38809 16.18516  1.000 49.65798 ? 304  LYS A NZ  1 
ATOM   765  N  N   . GLY A 1 102 ? 2.35023   64.49802 21.74344  1.000 37.77429 ? 305  GLY A N   1 
ATOM   766  C  CA  . GLY A 1 102 ? 2.97492   63.64949 22.73336  1.000 36.58325 ? 305  GLY A CA  1 
ATOM   767  C  C   . GLY A 1 102 ? 4.02050   64.39319 23.54281  1.000 38.35049 ? 305  GLY A C   1 
ATOM   768  O  O   . GLY A 1 102 ? 4.15380   65.61865 23.48736  1.000 39.46218 ? 305  GLY A O   1 
ATOM   769  N  N   . ALA A 1 103 ? 4.79697   63.61140 24.30159  1.000 42.54702 ? 306  ALA A N   1 
ATOM   770  C  CA  . ALA A 1 103 ? 5.70038   64.19332 25.29620  1.000 42.39387 ? 306  ALA A CA  1 
ATOM   771  C  C   . ALA A 1 103 ? 6.73579   65.12106 24.67327  1.000 45.89929 ? 306  ALA A C   1 
ATOM   772  O  O   . ALA A 1 103 ? 7.11930   66.11495 25.29307  1.000 45.76126 ? 306  ALA A O   1 
ATOM   773  C  CB  . ALA A 1 103 ? 6.40150   63.08663 26.08612  1.000 46.71506 ? 306  ALA A CB  1 
ATOM   774  N  N   . ASP A 1 104 ? 7.21178   64.82393 23.46385  1.000 45.03982 ? 307  ASP A N   1 
ATOM   775  C  CA  . ASP A 1 104 ? 8.23048   65.69064 22.88784  1.000 48.11482 ? 307  ASP A CA  1 
ATOM   776  C  C   . ASP A 1 104 ? 7.66242   66.98583 22.32481  1.000 52.77855 ? 307  ASP A C   1 
ATOM   777  O  O   . ASP A 1 104 ? 8.43848   67.82417 21.85746  1.000 59.36698 ? 307  ASP A O   1 
ATOM   778  C  CB  . ASP A 1 104 ? 9.03330   64.94779 21.80790  1.000 48.13363 ? 307  ASP A CB  1 
ATOM   779  C  CG  . ASP A 1 104 ? 8.20012   64.56905 20.57230  1.000 52.93004 ? 307  ASP A CG  1 
ATOM   780  O  OD1 . ASP A 1 104 ? 7.05901   65.05179 20.38990  1.000 48.66325 ? 307  ASP A OD1 1 
ATOM   781  O  OD2 . ASP A 1 104 ? 8.70804   63.75927 19.76879  1.000 59.46893 ? 307  ASP A OD2 1 
ATOM   782  N  N   . GLY A 1 105 ? 6.34379   67.17477 22.35858  1.000 50.81606 ? 308  GLY A N   1 
ATOM   783  C  CA  . GLY A 1 105 ? 5.73729   68.35777 21.77764  1.000 50.90897 ? 308  GLY A CA  1 
ATOM   784  C  C   . GLY A 1 105 ? 5.74026   68.41811 20.26133  1.000 48.19604 ? 308  GLY A C   1 
ATOM   785  O  O   . GLY A 1 105 ? 5.29651   69.42487 19.69829  1.000 49.11413 ? 308  GLY A O   1 
ATOM   786  N  N   . LYS A 1 106 ? 6.22016   67.38180 19.57763  1.000 47.68505 ? 309  LYS A N   1 
ATOM   787  C  CA  . LYS A 1 106 ? 6.26803   67.37691 18.12292  1.000 43.48836 ? 309  LYS A CA  1 
ATOM   788  C  C   . LYS A 1 106 ? 5.44436   66.25593 17.51277  1.000 45.03301 ? 309  LYS A C   1 
ATOM   789  O  O   . LYS A 1 106 ? 4.60535   66.51914 16.65075  1.000 42.58777 ? 309  LYS A O   1 
ATOM   790  C  CB  . LYS A 1 106 ? 7.72556   67.29296 17.64316  1.000 47.00762 ? 309  LYS A CB  1 
ATOM   791  C  CG  . LYS A 1 106 ? 8.57708   68.44329 18.16726  1.000 52.54871 ? 309  LYS A CG  1 
ATOM   792  C  CD  . LYS A 1 106 ? 9.88907   68.62829 17.40330  1.000 48.73548 ? 309  LYS A CD  1 
ATOM   793  C  CE  . LYS A 1 106 ? 10.70283  69.75352 18.04380  1.000 54.80412 ? 309  LYS A CE  1 
ATOM   794  N  NZ  . LYS A 1 106 ? 11.85189  70.20234 17.20911  1.000 54.45474 ? 309  LYS A NZ  1 
ATOM   795  N  N   . ALA A 1 107 ? 5.63932   65.00992 17.93589  1.000 45.84642 ? 310  ALA A N   1 
ATOM   796  C  CA  . ALA A 1 107 ? 4.83343   63.92509 17.40071  1.000 39.66015 ? 310  ALA A CA  1 
ATOM   797  C  C   . ALA A 1 107 ? 3.43786   63.94051 18.02070  1.000 45.55232 ? 310  ALA A C   1 
ATOM   798  O  O   . ALA A 1 107 ? 3.24908   64.36842 19.16801  1.000 43.59015 ? 310  ALA A O   1 
ATOM   799  C  CB  . ALA A 1 107 ? 5.50980   62.57595 17.65398  1.000 39.52952 ? 310  ALA A CB  1 
ATOM   800  N  N   . ASP A 1 108 ? 2.45367   63.47575 17.24368  1.000 39.85484 ? 311  ASP A N   1 
ATOM   801  C  CA  . ASP A 1 108 ? 1.10834   63.27329 17.77164  1.000 43.58370 ? 311  ASP A CA  1 
ATOM   802  C  C   . ASP A 1 108 ? 1.11841   62.17664 18.83318  1.000 37.76886 ? 311  ASP A C   1 
ATOM   803  O  O   . ASP A 1 108 ? 1.77910   61.14959 18.67527  1.000 36.74592 ? 311  ASP A O   1 
ATOM   804  C  CB  . ASP A 1 108 ? 0.12983   62.85989 16.66934  1.000 41.14287 ? 311  ASP A CB  1 
ATOM   805  C  CG  . ASP A 1 108 ? 0.10404   63.81407 15.48214  1.000 44.36200 ? 311  ASP A CG  1 
ATOM   806  O  OD1 . ASP A 1 108 ? 0.48331   64.99705 15.61632  1.000 49.60863 ? 311  ASP A OD1 1 
ATOM   807  O  OD2 . ASP A 1 108 ? -0.32100  63.35718 14.39711  1.000 50.11873 ? 311  ASP A OD2 1 
ATOM   808  N  N   . LEU A 1 109 ? 0.35380   62.38018 19.90302  1.000 39.93842 ? 312  LEU A N   1 
ATOM   809  C  CA  . LEU A 1 109 ? 0.19097   61.33629 20.90888  1.000 36.26711 ? 312  LEU A CA  1 
ATOM   810  C  C   . LEU A 1 109 ? -0.45957  60.11343 20.27985  1.000 36.86665 ? 312  LEU A C   1 
ATOM   811  O  O   . LEU A 1 109 ? -1.57128  60.19416 19.75061  1.000 38.34515 ? 312  LEU A O   1 
ATOM   812  C  CB  . LEU A 1 109 ? -0.65508  61.84993 22.06851  1.000 33.33234 ? 312  LEU A CB  1 
ATOM   813  C  CG  . LEU A 1 109 ? -0.73761  60.94553 23.30126  1.000 36.09255 ? 312  LEU A CG  1 
ATOM   814  C  CD1 . LEU A 1 109 ? 0.63464   60.78870 23.93165  1.000 40.49100 ? 312  LEU A CD1 1 
ATOM   815  C  CD2 . LEU A 1 109 ? -1.73000  61.49758 24.30730  1.000 36.27680 ? 312  LEU A CD2 1 
ATOM   816  N  N   . THR A 1 110 ? 0.23322   58.97998 20.32450  1.000 41.32334 ? 313  THR A N   1 
ATOM   817  C  CA  . THR A 1 110 ? -0.24406  57.75517 19.69091  1.000 40.42349 ? 313  THR A CA  1 
ATOM   818  C  C   . THR A 1 110 ? -0.10481  56.58688 20.65512  1.000 39.06679 ? 313  THR A C   1 
ATOM   819  O  O   . THR A 1 110 ? 0.99996   56.28955 21.11840  1.000 43.66730 ? 313  THR A O   1 
ATOM   820  C  CB  . THR A 1 110 ? 0.52719   57.48111 18.40073  1.000 39.27806 ? 313  THR A CB  1 
ATOM   821  O  OG1 . THR A 1 110 ? 0.31533   58.56600 17.50190  1.000 40.78331 ? 313  THR A OG1 1 
ATOM   822  C  CG2 . THR A 1 110 ? 0.03837   56.20916 17.74474  1.000 43.76995 ? 313  THR A CG2 1 
ATOM   823  N  N   . VAL A 1 111 ? -1.21695  55.92986 20.95975  1.000 36.89404 ? 314  VAL A N   1 
ATOM   824  C  CA  . VAL A 1 111 ? -1.21475  54.76374 21.83479  1.000 34.32820 ? 314  VAL A CA  1 
ATOM   825  C  C   . VAL A 1 111 ? -1.19887  53.50876 20.97204  1.000 29.28116 ? 314  VAL A C   1 
ATOM   826  O  O   . VAL A 1 111 ? -2.10410  53.29721 20.15953  1.000 33.16395 ? 314  VAL A O   1 
ATOM   827  C  CB  . VAL A 1 111 ? -2.42221  54.75877 22.78210  1.000 35.53831 ? 314  VAL A CB  1 
ATOM   828  C  CG1 . VAL A 1 111 ? -2.46331  53.43675 23.54536  1.000 27.87623 ? 314  VAL A CG1 1 
ATOM   829  C  CG2 . VAL A 1 111 ? -2.35069  55.93030 23.74735  1.000 32.26359 ? 314  VAL A CG2 1 
ATOM   830  N  N   . ASN A 1 112 ? -0.17487  52.67503 21.16140  1.000 31.98581 ? 315  ASN A N   1 
ATOM   831  C  CA  . ASN A 1 112 ? -0.02019  51.42749 20.41809  1.000 27.55635 ? 315  ASN A CA  1 
ATOM   832  C  C   . ASN A 1 112 ? -0.86322  50.32911 21.05643  1.000 32.83656 ? 315  ASN A C   1 
ATOM   833  O  O   . ASN A 1 112 ? -0.63818  49.97464 22.22000  1.000 25.55175 ? 315  ASN A O   1 
ATOM   834  C  CB  . ASN A 1 112 ? 1.44787   51.00991 20.40899  1.000 22.89734 ? 315  ASN A CB  1 
ATOM   835  C  CG  . ASN A 1 112 ? 2.32704   51.98816 19.66436  1.000 41.07267 ? 315  ASN A CG  1 
ATOM   836  O  OD1 . ASN A 1 112 ? 1.92922   52.53160 18.64450  1.000 43.90449 ? 315  ASN A OD1 1 
ATOM   837  N  ND2 . ASN A 1 112 ? 3.52965   52.21875 20.17475  1.000 48.15450 ? 315  ASN A ND2 1 
ATOM   838  N  N   . ILE A 1 113 ? -1.82006  49.78661 20.30101  1.000 26.53557 ? 316  ILE A N   1 
ATOM   839  C  CA  . ILE A 1 113 ? -2.58853  48.61121 20.71133  1.000 26.66255 ? 316  ILE A CA  1 
ATOM   840  C  C   . ILE A 1 113 ? -1.98754  47.38615 20.02881  1.000 30.06065 ? 316  ILE A C   1 
ATOM   841  O  O   . ILE A 1 113 ? -1.76719  47.39197 18.81125  1.000 31.31649 ? 316  ILE A O   1 
ATOM   842  C  CB  . ILE A 1 113 ? -4.07760  48.75541 20.34706  1.000 27.26248 ? 316  ILE A CB  1 
ATOM   843  C  CG1 . ILE A 1 113 ? -4.66062  50.07078 20.86544  1.000 30.26642 ? 316  ILE A CG1 1 
ATOM   844  C  CG2 . ILE A 1 113 ? -4.87601  47.58166 20.88273  1.000 27.73602 ? 316  ILE A CG2 1 
ATOM   845  C  CD1 . ILE A 1 113 ? -4.67185  50.15221 22.34339  1.000 29.00737 ? 316  ILE A CD1 1 
ATOM   846  N  N   . ILE A 1 114 ? -1.73779  46.33032 20.79641  1.000 28.02504 ? 317  ILE A N   1 
ATOM   847  C  CA  . ILE A 1 114 ? -1.25678  45.05302 20.25723  1.000 27.00688 ? 317  ILE A CA  1 
ATOM   848  C  C   . ILE A 1 114 ? -2.07841  43.94998 20.91091  1.000 27.34028 ? 317  ILE A C   1 
ATOM   849  O  O   . ILE A 1 114 ? -1.82659  43.59618 22.06825  1.000 27.30805 ? 317  ILE A O   1 
ATOM   850  C  CB  . ILE A 1 114 ? 0.23792   44.83483 20.51673  1.000 28.54154 ? 317  ILE A CB  1 
ATOM   851  C  CG1 . ILE A 1 114 ? 1.06161   46.03582 20.05522  1.000 25.28848 ? 317  ILE A CG1 1 
ATOM   852  C  CG2 . ILE A 1 114 ? 0.71581   43.55652 19.83228  1.000 30.48127 ? 317  ILE A CG2 1 
ATOM   853  C  CD1 . ILE A 1 114 ? 2.52056   45.94410 20.40615  1.000 30.83503 ? 317  ILE A CD1 1 
ATOM   854  N  N   . GLN A 1 115 ? -3.05576  43.39282 20.19063  1.000 24.78381 ? 318  GLN A N   1 
ATOM   855  C  CA  . GLN A 1 115 ? -3.79205  42.27005 20.75480  1.000 25.77282 ? 318  GLN A CA  1 
ATOM   856  C  C   . GLN A 1 115 ? -2.93983  41.01576 20.66007  1.000 27.27825 ? 318  GLN A C   1 
ATOM   857  O  O   . GLN A 1 115 ? -2.33544  40.74503 19.62033  1.000 33.76223 ? 318  GLN A O   1 
ATOM   858  C  CB  . GLN A 1 115 ? -5.13406  42.05108 20.06751  1.000 23.09834 ? 318  GLN A CB  1 
ATOM   859  C  CG  . GLN A 1 115 ? -5.98035  41.02138 20.81385  1.000 28.48661 ? 318  GLN A CG  1 
ATOM   860  C  CD  . GLN A 1 115 ? -7.35488  40.82679 20.22462  1.000 30.14497 ? 318  GLN A CD  1 
ATOM   861  O  OE1 . GLN A 1 115 ? -7.59069  41.16293 19.06176  1.000 30.76993 ? 318  GLN A OE1 1 
ATOM   862  N  NE2 . GLN A 1 115 ? -8.28557  40.28454 21.03018  1.000 24.85811 ? 318  GLN A NE2 1 
ATOM   863  N  N   . LYS A 1 116 ? -2.86909  40.26885 21.75360  1.000 24.52097 ? 319  LYS A N   1 
ATOM   864  C  CA  . LYS A 1 116 ? -1.99709  39.10444 21.81417  1.000 29.15749 ? 319  LYS A CA  1 
ATOM   865  C  C   . LYS A 1 116 ? -2.51943  37.95675 20.95008  1.000 26.46934 ? 319  LYS A C   1 
ATOM   866  O  O   . LYS A 1 116 ? -3.71916  37.82762 20.68875  1.000 23.01455 ? 319  LYS A O   1 
ATOM   867  C  CB  . LYS A 1 116 ? -1.83928  38.63666 23.25857  1.000 25.95021 ? 319  LYS A CB  1 
ATOM   868  C  CG  . LYS A 1 116 ? -0.88768  39.50425 24.05114  1.000 35.16851 ? 319  LYS A CG  1 
ATOM   869  C  CD  . LYS A 1 116 ? -0.64227  38.92775 25.44453  1.000 39.12963 ? 319  LYS A CD  1 
ATOM   870  C  CE  . LYS A 1 116 ? -1.41957  39.67596 26.50046  1.000 41.17961 ? 319  LYS A CE  1 
ATOM   871  N  NZ  . LYS A 1 116 ? -0.69329  39.68099 27.80330  1.000 47.02773 ? 319  LYS A NZ  1 
ATOM   872  N  N   . LYS A 1 117 ? -1.58680  37.10020 20.53432  1.000 32.09665 ? 320  LYS A N   1 
ATOM   873  C  CA  . LYS A 1 117 ? -1.88357  35.96830 19.65792  1.000 31.10648 ? 320  LYS A CA  1 
ATOM   874  C  C   . LYS A 1 117 ? -2.68894  34.88817 20.37823  1.000 34.46291 ? 320  LYS A C   1 
ATOM   875  O  O   . LYS A 1 117 ? -2.62667  34.73272 21.60437  1.000 30.03488 ? 320  LYS A O   1 
ATOM   876  C  CB  . LYS A 1 117 ? -0.58416  35.35050 19.14731  1.000 28.41141 ? 320  LYS A CB  1 
ATOM   877  C  CG  . LYS A 1 117 ? 0.13227   34.54061 20.22959  1.000 36.50224 ? 320  LYS A CG  1 
ATOM   878  C  CD  . LYS A 1 117 ? 1.57146   34.27319 19.85934  1.000 45.34942 ? 320  LYS A CD  1 
ATOM   879  C  CE  . LYS A 1 117 ? 1.84083   32.78081 19.77158  1.000 45.79788 ? 320  LYS A CE  1 
ATOM   880  N  N   . ASN A 1 118 ? -3.43998  34.12279 19.59485  1.000 30.43985 ? 321  ASN A N   1 
ATOM   881  C  CA  . ASN A 1 118 ? -4.15069  32.97077 20.12542  1.000 29.45444 ? 321  ASN A CA  1 
ATOM   882  C  C   . ASN A 1 118 ? -3.14615  31.88746 20.51211  1.000 34.23241 ? 321  ASN A C   1 
ATOM   883  O  O   . ASN A 1 118 ? -2.36443  31.43119 19.67451  1.000 33.58922 ? 321  ASN A O   1 
ATOM   884  C  CB  . ASN A 1 118 ? -5.14285  32.45533 19.08712  1.000 34.91695 ? 321  ASN A CB  1 
ATOM   885  C  CG  . ASN A 1 118 ? -6.03369  31.34933 19.61890  1.000 38.56376 ? 321  ASN A CG  1 
ATOM   886  O  OD1 . ASN A 1 118 ? -5.96470  30.98272 20.79690  1.000 37.00646 ? 321  ASN A OD1 1 
ATOM   887  N  ND2 . ASN A 1 118 ? -6.88464  30.81180 18.74779  1.000 37.48845 ? 321  ASN A ND2 1 
ATOM   888  N  N   . GLU A 1 119 ? -3.15154  31.48541 21.78164  1.000 33.36081 ? 322  GLU A N   1 
ATOM   889  C  CA  . GLU A 1 119 ? -2.24704  30.44421 22.25739  1.000 36.75367 ? 322  GLU A CA  1 
ATOM   890  C  C   . GLU A 1 119 ? -2.83157  29.04295 22.14745  1.000 37.27711 ? 322  GLU A C   1 
ATOM   891  O  O   . GLU A 1 119 ? -2.10707  28.06715 22.36893  1.000 41.19968 ? 322  GLU A O   1 
ATOM   892  C  CB  . GLU A 1 119 ? -1.84750  30.69401 23.72251  1.000 46.13725 ? 322  GLU A CB  1 
ATOM   893  C  CG  . GLU A 1 119 ? -1.01093  31.94366 23.96013  1.000 41.97785 ? 322  GLU A CG  1 
ATOM   894  C  CD  . GLU A 1 119 ? 0.41868   31.83104 23.43307  1.000 56.43829 ? 322  GLU A CD  1 
ATOM   895  O  OE1 . GLU A 1 119 ? 0.79022   30.76791 22.87109  1.000 56.95049 ? 322  GLU A OE1 1 
ATOM   896  O  OE2 . GLU A 1 119 ? 1.17236   32.82341 23.57914  1.000 61.68515 ? 322  GLU A OE2 1 
ATOM   897  N  N   . ASN A 1 120 ? -4.11519  28.90870 21.83491  1.000 37.85627 ? 323  ASN A N   1 
ATOM   898  C  CA  . ASN A 1 120 ? -4.73172  27.59964 21.61078  1.000 41.12743 ? 323  ASN A CA  1 
ATOM   899  C  C   . ASN A 1 120 ? -5.48650  27.58226 20.28097  1.000 35.93428 ? 323  ASN A C   1 
ATOM   900  O  O   . ASN A 1 120 ? -6.70560  27.39020 20.23881  1.000 33.63317 ? 323  ASN A O   1 
ATOM   901  C  CB  . ASN A 1 120 ? -5.64744  27.24150 22.77674  1.000 35.70748 ? 323  ASN A CB  1 
ATOM   902  C  CG  . ASN A 1 120 ? -4.89621  27.14426 24.08917  1.000 54.14240 ? 323  ASN A CG  1 
ATOM   903  O  OD1 . ASN A 1 120 ? -5.13235  27.92591 25.01352  1.000 57.35032 ? 323  ASN A OD1 1 
ATOM   904  N  ND2 . ASN A 1 120 ? -3.97406  26.18653 24.17566  1.000 57.62384 ? 323  ASN A ND2 1 
ATOM   905  N  N   . PRO A 1 121 ? -4.78038  27.75109 19.16586  1.000 34.98203 ? 324  PRO A N   1 
ATOM   906  C  CA  . PRO A 1 121 ? -5.46135  27.79801 17.86744  1.000 33.08054 ? 324  PRO A CA  1 
ATOM   907  C  C   . PRO A 1 121 ? -5.94002  26.42755 17.43011  1.000 38.21517 ? 324  PRO A C   1 
ATOM   908  O  O   . PRO A 1 121 ? -5.31532  25.40653 17.71985  1.000 37.86294 ? 324  PRO A O   1 
ATOM   909  C  CB  . PRO A 1 121 ? -4.37506  28.31061 16.92572  1.000 34.33599 ? 324  PRO A CB  1 
ATOM   910  C  CG  . PRO A 1 121 ? -3.12216  27.74192 17.51691  1.000 32.09024 ? 324  PRO A CG  1 
ATOM   911  C  CD  . PRO A 1 121 ? -3.31598  27.83160 19.01637  1.000 34.77226 ? 324  PRO A CD  1 
ATOM   912  N  N   . VAL A 1 122 ? -7.05622  26.41430 16.71019  1.000 35.44413 ? 325  VAL A N   1 
ATOM   913  C  CA  . VAL A 1 122 ? -7.55104  25.20696 16.06413  1.000 39.32065 ? 325  VAL A CA  1 
ATOM   914  C  C   . VAL A 1 122 ? -7.04404  25.23752 14.62533  1.000 40.10075 ? 325  VAL A C   1 
ATOM   915  O  O   . VAL A 1 122 ? -7.45801  26.08492 13.82818  1.000 37.65101 ? 325  VAL A O   1 
ATOM   916  C  CB  . VAL A 1 122 ? -9.07987  25.10550 16.13205  1.000 36.83838 ? 325  VAL A CB  1 
ATOM   917  C  CG1 . VAL A 1 122 ? -9.55784  23.78536 15.52862  1.000 36.81714 ? 325  VAL A CG1 1 
ATOM   918  C  CG2 . VAL A 1 122 ? -9.54890  25.21173 17.57232  1.000 40.23065 ? 325  VAL A CG2 1 
ATOM   919  N  N   . VAL A 1 123 ? -6.13717  24.31948 14.29433  1.000 33.31533 ? 326  VAL A N   1 
ATOM   920  C  CA  . VAL A 1 123 ? -5.45131  24.30392 13.00735  1.000 36.03486 ? 326  VAL A CA  1 
ATOM   921  C  C   . VAL A 1 123 ? -6.06564  23.22413 12.12944  1.000 33.72666 ? 326  VAL A C   1 
ATOM   922  O  O   . VAL A 1 123 ? -6.43015  22.15384 12.62135  1.000 35.88457 ? 326  VAL A O   1 
ATOM   923  C  CB  . VAL A 1 123 ? -3.94113  24.07104 13.20678  1.000 34.00256 ? 326  VAL A CB  1 
ATOM   924  C  CG1 . VAL A 1 123 ? -3.22096  23.97523 11.86961  1.000 32.94494 ? 326  VAL A CG1 1 
ATOM   925  C  CG2 . VAL A 1 123 ? -3.33802  25.19987 14.07326  1.000 37.06716 ? 326  VAL A CG2 1 
ATOM   926  N  N   . HIS A 1 124 ? -6.20250  23.50545 10.83147  1.000 31.50610 ? 327  HIS A N   1 
ATOM   927  C  CA  . HIS A 1 124 ? -6.56219  22.48175 9.85733   1.000 32.61179 ? 327  HIS A CA  1 
ATOM   928  C  C   . HIS A 1 124 ? -5.56288  22.49880 8.70633   1.000 29.19177 ? 327  HIS A C   1 
ATOM   929  O  O   . HIS A 1 124 ? -4.77275  23.43509 8.55035   1.000 29.94001 ? 327  HIS A O   1 
ATOM   930  C  CB  . HIS A 1 124 ? -8.00544  22.63946 9.34244   1.000 30.83704 ? 327  HIS A CB  1 
ATOM   931  C  CG  . HIS A 1 124 ? -8.26515  23.91023 8.59837   1.000 32.54121 ? 327  HIS A CG  1 
ATOM   932  N  ND1 . HIS A 1 124 ? -8.44632  25.12185 9.23130   1.000 37.77326 ? 327  HIS A ND1 1 
ATOM   933  C  CD2 . HIS A 1 124 ? -8.42154  24.15132 7.27420   1.000 33.45840 ? 327  HIS A CD2 1 
ATOM   934  C  CE1 . HIS A 1 124 ? -8.68071  26.05873 8.32781   1.000 39.87683 ? 327  HIS A CE1 1 
ATOM   935  N  NE2 . HIS A 1 124 ? -8.66846  25.49692 7.13148   1.000 38.11192 ? 327  HIS A NE2 1 
ATOM   936  N  N   . TYR A 1 125 ? -5.58218  21.43537 7.90828   1.000 23.89758 ? 328  TYR A N   1 
ATOM   937  C  CA  . TYR A 1 125 ? -4.51262  21.19337 6.94789   1.000 28.93080 ? 328  TYR A CA  1 
ATOM   938  C  C   . TYR A 1 125 ? -5.09666  20.84987 5.58306   1.000 29.21725 ? 328  TYR A C   1 
ATOM   939  O  O   . TYR A 1 125 ? -6.20074  20.31413 5.48978   1.000 27.35910 ? 328  TYR A O   1 
ATOM   940  C  CB  . TYR A 1 125 ? -3.59144  20.05462 7.44042   1.000 24.63603 ? 328  TYR A CB  1 
ATOM   941  C  CG  . TYR A 1 125 ? -2.95538  20.32969 8.78906   1.000 30.81181 ? 328  TYR A CG  1 
ATOM   942  C  CD1 . TYR A 1 125 ? -3.64947  20.09276 9.97504   1.000 26.46193 ? 328  TYR A CD1 1 
ATOM   943  C  CD2 . TYR A 1 125 ? -1.65925  20.82781 8.87589   1.000 26.02684 ? 328  TYR A CD2 1 
ATOM   944  C  CE1 . TYR A 1 125 ? -3.06533  20.36042 11.22203  1.000 27.55642 ? 328  TYR A CE1 1 
ATOM   945  C  CE2 . TYR A 1 125 ? -1.06986  21.08783 10.10839  1.000 27.99612 ? 328  TYR A CE2 1 
ATOM   946  C  CZ  . TYR A 1 125 ? -1.78139  20.85738 11.27252  1.000 28.11844 ? 328  TYR A CZ  1 
ATOM   947  O  OH  . TYR A 1 125 ? -1.18086  21.12152 12.48010  1.000 29.75949 ? 328  TYR A OH  1 
ATOM   948  N  N   . LYS A 1 126 ? -4.34721  21.17518 4.52324   1.000 29.39647 ? 329  LYS A N   1 
ATOM   949  C  CA  . LYS A 1 126 ? -4.64833  20.74140 3.15929   1.000 26.20900 ? 329  LYS A CA  1 
ATOM   950  C  C   . LYS A 1 126 ? -3.37875  20.18698 2.54209   1.000 25.29751 ? 329  LYS A C   1 
ATOM   951  O  O   . LYS A 1 126 ? -2.34610  20.86372 2.53419   1.000 25.86875 ? 329  LYS A O   1 
ATOM   952  C  CB  . LYS A 1 126 ? -5.19125  21.88184 2.28278   1.000 29.18742 ? 329  LYS A CB  1 
ATOM   953  C  CG  . LYS A 1 126 ? -6.58807  22.35159 2.66341   1.000 39.55125 ? 329  LYS A CG  1 
ATOM   954  C  CD  . LYS A 1 126 ? -6.94916  23.73391 2.07642   1.000 40.07398 ? 329  LYS A CD  1 
ATOM   955  C  CE  . LYS A 1 126 ? -7.35811  23.67848 0.61346   1.000 45.52504 ? 329  LYS A CE  1 
ATOM   956  N  NZ  . LYS A 1 126 ? -7.99944  24.97295 0.19729   1.000 51.69817 ? 329  LYS A NZ  1 
ATOM   957  N  N   . TRP A 1 127 ? -3.45616  18.95728 2.04065   1.000 21.88607 ? 330  TRP A N   1 
ATOM   958  C  CA  . TRP A 1 127 ? -2.32515  18.28179 1.42816   1.000 23.92833 ? 330  TRP A CA  1 
ATOM   959  C  C   . TRP A 1 127 ? -2.54011  18.14671 -0.07809  1.000 24.86489 ? 330  TRP A C   1 
ATOM   960  O  O   . TRP A 1 127 ? -3.67197  18.07877 -0.56135  1.000 22.29808 ? 330  TRP A O   1 
ATOM   961  C  CB  . TRP A 1 127 ? -2.11406  16.90654 2.07248   1.000 23.96432 ? 330  TRP A CB  1 
ATOM   962  C  CG  . TRP A 1 127 ? -2.04409  17.02915 3.57501   1.000 26.67290 ? 330  TRP A CG  1 
ATOM   963  C  CD1 . TRP A 1 127 ? -3.05825  16.81623 4.46684   1.000 23.38210 ? 330  TRP A CD1 1 
ATOM   964  C  CD2 . TRP A 1 127 ? -0.91449  17.44670 4.34425   1.000 23.80833 ? 330  TRP A CD2 1 
ATOM   965  N  NE1 . TRP A 1 127 ? -2.61868  17.04789 5.74524   1.000 24.07592 ? 330  TRP A NE1 1 
ATOM   966  C  CE2 . TRP A 1 127 ? -1.30944  17.44574 5.70110   1.000 24.57157 ? 330  TRP A CE2 1 
ATOM   967  C  CE3 . TRP A 1 127 ? 0.39820   17.81252 4.01958   1.000 21.86651 ? 330  TRP A CE3 1 
ATOM   968  C  CZ2 . TRP A 1 127 ? -0.44020  17.80504 6.73890   1.000 21.81299 ? 330  TRP A CZ2 1 
ATOM   969  C  CZ3 . TRP A 1 127 ? 1.26279   18.15825 5.04403   1.000 23.57993 ? 330  TRP A CZ3 1 
ATOM   970  C  CH2 . TRP A 1 127 ? 0.83413   18.15579 6.39397   1.000 25.96394 ? 330  TRP A CH2 1 
ATOM   971  N  N   . VAL A 1 128 ? -1.43354  18.14178 -0.81892  1.000 22.67739 ? 331  VAL A N   1 
ATOM   972  C  CA  . VAL A 1 128 ? -1.50147  17.87310 -2.24400  1.000 21.68987 ? 331  VAL A CA  1 
ATOM   973  C  C   . VAL A 1 128 ? -2.27427  16.57210 -2.48425  1.000 26.19792 ? 331  VAL A C   1 
ATOM   974  O  O   . VAL A 1 128 ? -2.12094  15.59169 -1.75073  1.000 25.10012 ? 331  VAL A O   1 
ATOM   975  C  CB  . VAL A 1 128 ? -0.07583  17.81772 -2.82102  1.000 23.21080 ? 331  VAL A CB  1 
ATOM   976  C  CG1 . VAL A 1 128 ? -0.07880  17.20668 -4.24638  1.000 21.68017 ? 331  VAL A CG1 1 
ATOM   977  C  CG2 . VAL A 1 128 ? 0.54496   19.22437 -2.82742  1.000 24.92684 ? 331  VAL A CG2 1 
ATOM   978  N  N   . ASP A 1 129 ? -3.12759  16.57526 -3.49730  1.000 25.90577 ? 332  ASP A N   1 
ATOM   979  C  CA  . ASP A 1 129 ? -3.97772  15.42019 -3.77147  1.000 25.81436 ? 332  ASP A CA  1 
ATOM   980  C  C   . ASP A 1 129 ? -3.14982  14.16293 -4.02677  1.000 30.18894 ? 332  ASP A C   1 
ATOM   981  O  O   . ASP A 1 129 ? -2.16082  14.18974 -4.76386  1.000 28.51891 ? 332  ASP A O   1 
ATOM   982  C  CB  . ASP A 1 129 ? -4.87122  15.71328 -4.97225  1.000 29.39547 ? 332  ASP A CB  1 
ATOM   983  C  CG  . ASP A 1 129 ? -5.82099  14.56494 -5.29524  1.000 43.59172 ? 332  ASP A CG  1 
ATOM   984  O  OD1 . ASP A 1 129 ? -6.82341  14.38979 -4.55874  1.000 38.23876 ? 332  ASP A OD1 1 
ATOM   985  O  OD2 . ASP A 1 129 ? -5.56874  13.84651 -6.29469  1.000 40.11553 ? 332  ASP A OD2 1 
ATOM   986  N  N   . GLY A 1 130 ? -3.53879  13.05857 -3.38317  1.000 31.24217 ? 333  GLY A N   1 
ATOM   987  C  CA  . GLY A 1 130 ? -2.95647  11.76727 -3.67093  1.000 24.51174 ? 333  GLY A CA  1 
ATOM   988  C  C   . GLY A 1 130 ? -1.80504  11.34246 -2.79575  1.000 29.19013 ? 333  GLY A C   1 
ATOM   989  O  O   . GLY A 1 130 ? -1.32052  10.21284 -2.95297  1.000 28.36480 ? 333  GLY A O   1 
ATOM   990  N  N   . ILE A 1 131 ? -1.33890  12.18440 -1.87290  1.000 21.77840 ? 334  ILE A N   1 
ATOM   991  C  CA  . ILE A 1 131 ? -0.22434  11.78731 -1.01703  1.000 21.82033 ? 334  ILE A CA  1 
ATOM   992  C  C   . ILE A 1 131 ? -0.68397  11.41884 0.39172   1.000 24.97440 ? 334  ILE A C   1 
ATOM   993  O  O   . ILE A 1 131 ? 0.14835   11.29394 1.29127   1.000 25.52341 ? 334  ILE A O   1 
ATOM   994  C  CB  . ILE A 1 131 ? 0.86426   12.87484 -0.95907  1.000 27.16059 ? 334  ILE A CB  1 
ATOM   995  C  CG1 . ILE A 1 131 ? 0.34122   14.13261 -0.24536  1.000 24.52797 ? 334  ILE A CG1 1 
ATOM   996  C  CG2 . ILE A 1 131 ? 1.37612   13.20102 -2.35505  1.000 23.12451 ? 334  ILE A CG2 1 
ATOM   997  C  CD1 . ILE A 1 131 ? 1.42940   15.01938 0.30270   1.000 21.13691 ? 334  ILE A CD1 1 
ATOM   998  N  N   . GLY A 1 132 ? -1.98808  11.25691 0.60689   1.000 23.16384 ? 335  GLY A N   1 
ATOM   999  C  CA  . GLY A 1 132 ? -2.49421  10.96882 1.93487   1.000 29.09556 ? 335  GLY A CA  1 
ATOM   1000 C  C   . GLY A 1 132 ? -2.29096  12.12157 2.90413   1.000 30.68579 ? 335  GLY A C   1 
ATOM   1001 O  O   . GLY A 1 132 ? -2.36308  13.29835 2.54787   1.000 25.65373 ? 335  GLY A O   1 
ATOM   1002 N  N   . ALA A 1 133 ? -2.03388  11.77781 4.16249   1.000 27.28193 ? 336  ALA A N   1 
ATOM   1003 C  CA  . ALA A 1 133 ? -1.87021  12.78916 5.19961   1.000 28.76475 ? 336  ALA A CA  1 
ATOM   1004 C  C   . ALA A 1 133 ? -1.12236  12.16505 6.36535   1.000 27.85692 ? 336  ALA A C   1 
ATOM   1005 O  O   . ALA A 1 133 ? -1.21093  10.94806 6.56801   1.000 27.22318 ? 336  ALA A O   1 
ATOM   1006 C  CB  . ALA A 1 133 ? -3.22969  13.33733 5.66167   1.000 28.02126 ? 336  ALA A CB  1 
ATOM   1007 N  N   . PRO A 1 134 ? -0.37360  12.94923 7.14251   1.000 27.10534 ? 337  PRO A N   1 
ATOM   1008 C  CA  . PRO A 1 134 ? 0.44633   12.35621 8.20543   1.000 27.45887 ? 337  PRO A CA  1 
ATOM   1009 C  C   . PRO A 1 134 ? -0.40695  11.78374 9.32468   1.000 27.49000 ? 337  PRO A C   1 
ATOM   1010 O  O   . PRO A 1 134 ? -1.39909  12.38361 9.74621   1.000 31.20461 ? 337  PRO A O   1 
ATOM   1011 C  CB  . PRO A 1 134 ? 1.30013   13.53161 8.70311   1.000 29.02939 ? 337  PRO A CB  1 
ATOM   1012 C  CG  . PRO A 1 134 ? 0.47430   14.74031 8.40711   1.000 27.80491 ? 337  PRO A CG  1 
ATOM   1013 C  CD  . PRO A 1 134 ? -0.21060  14.41495 7.08395   1.000 26.72139 ? 337  PRO A CD  1 
ATOM   1014 N  N   . THR A 1 135 ? -0.01601  10.59906 9.79093   1.000 32.91606 ? 338  THR A N   1 
ATOM   1015 C  CA  . THR A 1 135 ? -0.54122  10.06632 11.03830  1.000 31.56580 ? 338  THR A CA  1 
ATOM   1016 C  C   . THR A 1 135 ? 0.18839   10.70756 12.21094  1.000 31.06469 ? 338  THR A C   1 
ATOM   1017 O  O   . THR A 1 135 ? 1.26579   11.28357 12.05820  1.000 31.31797 ? 338  THR A O   1 
ATOM   1018 C  CB  . THR A 1 135 ? -0.36896  8.54944  11.10430  1.000 33.18841 ? 338  THR A CB  1 
ATOM   1019 O  OG1 . THR A 1 135 ? 1.02470   8.23628  11.17494  1.000 33.28265 ? 338  THR A OG1 1 
ATOM   1020 C  CG2 . THR A 1 135 ? -0.98084  7.87589  9.88252   1.000 31.36071 ? 338  THR A CG2 1 
ATOM   1021 N  N   . GLU A 1 136 ? -0.40318  10.59994 13.40017  1.000 37.41971 ? 339  GLU A N   1 
ATOM   1022 C  CA  . GLU A 1 136 ? 0.23619   11.19848 14.56760  1.000 32.55376 ? 339  GLU A CA  1 
ATOM   1023 C  C   . GLU A 1 136 ? 1.63709   10.63098 14.78106  1.000 32.62497 ? 339  GLU A C   1 
ATOM   1024 O  O   . GLU A 1 136 ? 2.56740   11.36307 15.13022  1.000 37.75396 ? 339  GLU A O   1 
ATOM   1025 C  CB  . GLU A 1 136 ? -0.64209  11.00021 15.80314  1.000 41.18451 ? 339  GLU A CB  1 
ATOM   1026 C  CG  . GLU A 1 136 ? -1.87598  11.91101 15.81537  1.000 49.03568 ? 339  GLU A CG  1 
ATOM   1027 C  CD  . GLU A 1 136 ? -1.52463  13.39578 15.66583  1.000 53.00130 ? 339  GLU A CD  1 
ATOM   1028 O  OE1 . GLU A 1 136 ? -0.68861  13.89725 16.45358  1.000 55.26535 ? 339  GLU A OE1 1 
ATOM   1029 O  OE2 . GLU A 1 136 ? -2.07479  14.05840 14.74958  1.000 54.93783 ? 339  GLU A OE2 1 
ATOM   1030 N  N   . ASN A 1 137 ? 1.82469   9.34440  14.51468  1.000 32.68452 ? 340  ASN A N   1 
ATOM   1031 C  CA  . ASN A 1 137 ? 3.14341   8.75307  14.67437  1.000 33.19115 ? 340  ASN A CA  1 
ATOM   1032 C  C   . ASN A 1 137 ? 4.15509   9.29550  13.67257  1.000 36.74358 ? 340  ASN A C   1 
ATOM   1033 O  O   . ASN A 1 137 ? 5.35972   9.21783  13.92883  1.000 34.61333 ? 340  ASN A O   1 
ATOM   1034 C  CB  . ASN A 1 137 ? 3.05414   7.22489  14.55084  1.000 39.14346 ? 340  ASN A CB  1 
ATOM   1035 C  CG  . ASN A 1 137 ? 2.41571   6.57849  15.76759  1.000 50.69139 ? 340  ASN A CG  1 
ATOM   1036 O  OD1 . ASN A 1 137 ? 2.38057   7.16873  16.85345  1.000 48.20004 ? 340  ASN A OD1 1 
ATOM   1037 N  ND2 . ASN A 1 137 ? 1.90590   5.35757  15.59565  1.000 51.85649 ? 340  ASN A ND2 1 
ATOM   1038 N  N   . GLN A 1 138 ? 3.70551   9.83548  12.54303  1.000 31.72838 ? 341  GLN A N   1 
ATOM   1039 C  CA  . GLN A 1 138 ? 4.61855   10.35457 11.53073  1.000 28.41370 ? 341  GLN A CA  1 
ATOM   1040 C  C   . GLN A 1 138 ? 5.00054   11.81836 11.74964  1.000 27.86706 ? 341  GLN A C   1 
ATOM   1041 O  O   . GLN A 1 138 ? 5.82856   12.34946 10.99720  1.000 27.00724 ? 341  GLN A O   1 
ATOM   1042 C  CB  . GLN A 1 138 ? 3.99697   10.16516 10.14026  1.000 26.57956 ? 341  GLN A CB  1 
ATOM   1043 C  CG  . GLN A 1 138 ? 3.95151   8.69100  9.69384   1.000 26.45390 ? 341  GLN A CG  1 
ATOM   1044 C  CD  . GLN A 1 138 ? 2.95475   8.42095  8.56728   1.000 31.91824 ? 341  GLN A CD  1 
ATOM   1045 O  OE1 . GLN A 1 138 ? 2.39313   9.35333  7.96521   1.000 26.48819 ? 341  GLN A OE1 1 
ATOM   1046 N  NE2 . GLN A 1 138 ? 2.72364   7.13131  8.27939   1.000 27.19879 ? 341  GLN A NE2 1 
ATOM   1047 N  N   . LYS A 1 139 ? 4.43264   12.48587 12.75318  1.000 25.36507 ? 342  LYS A N   1 
ATOM   1048 C  CA  . LYS A 1 139 ? 4.71180   13.89322 13.01603  1.000 24.67244 ? 342  LYS A CA  1 
ATOM   1049 C  C   . LYS A 1 139 ? 5.78640   14.03003 14.09165  1.000 29.49564 ? 342  LYS A C   1 
ATOM   1050 O  O   . LYS A 1 139 ? 5.58294   13.61083 15.23377  1.000 33.68191 ? 342  LYS A O   1 
ATOM   1051 C  CB  . LYS A 1 139 ? 3.44375   14.61295 13.45427  1.000 26.73589 ? 342  LYS A CB  1 
ATOM   1052 C  CG  . LYS A 1 139 ? 2.32080   14.59457 12.43820  1.000 27.92688 ? 342  LYS A CG  1 
ATOM   1053 C  CD  . LYS A 1 139 ? 1.28811   15.63811 12.87401  1.000 37.18518 ? 342  LYS A CD  1 
ATOM   1054 C  CE  . LYS A 1 139 ? -0.03985  15.45755 12.20181  1.000 38.01567 ? 342  LYS A CE  1 
ATOM   1055 N  NZ  . LYS A 1 139 ? -1.05817  16.31892 12.85645  1.000 38.18352 ? 342  LYS A NZ  1 
ATOM   1056 N  N   . ILE A 1 140 ? 6.91252   14.63983 13.74377  1.000 26.85895 ? 343  ILE A N   1 
ATOM   1057 C  CA  . ILE A 1 140 ? 8.05480   14.73728 14.64568  1.000 28.69102 ? 343  ILE A CA  1 
ATOM   1058 C  C   . ILE A 1 140 ? 8.20311   16.19326 15.08676  1.000 30.17268 ? 343  ILE A C   1 
ATOM   1059 O  O   . ILE A 1 140 ? 8.51249   17.07275 14.26626  1.000 23.13666 ? 343  ILE A O   1 
ATOM   1060 C  CB  . ILE A 1 140 ? 9.34518   14.22767 13.98683  1.000 28.06444 ? 343  ILE A CB  1 
ATOM   1061 C  CG1 . ILE A 1 140 ? 9.13707   12.85151 13.35468  1.000 28.53075 ? 343  ILE A CG1 1 
ATOM   1062 C  CG2 . ILE A 1 140 ? 10.48248  14.22432 15.01396  1.000 28.51342 ? 343  ILE A CG2 1 
ATOM   1063 C  CD1 . ILE A 1 140 ? 8.48478   11.80356 14.27036  1.000 31.22294 ? 343  ILE A CD1 1 
ATOM   1064 N  N   . LYS A 1 141 ? 8.01053   16.43967 16.38727  1.000 27.75485 ? 344  LYS A N   1 
ATOM   1065 C  CA  . LYS A 1 141 ? 8.22494   17.75971 16.96954  1.000 28.84472 ? 344  LYS A CA  1 
ATOM   1066 C  C   . LYS A 1 141 ? 9.70010   18.13150 16.89800  1.000 31.07662 ? 344  LYS A C   1 
ATOM   1067 O  O   . LYS A 1 141 ? 10.57890  17.26989 16.80559  1.000 27.78307 ? 344  LYS A O   1 
ATOM   1068 C  CB  . LYS A 1 141 ? 7.75330   17.79872 18.42622  1.000 29.92376 ? 344  LYS A CB  1 
ATOM   1069 C  CG  . LYS A 1 141 ? 6.23981   17.79697 18.60845  1.000 39.54184 ? 344  LYS A CG  1 
ATOM   1070 C  CD  . LYS A 1 141 ? 5.88943   17.44003 20.04801  1.000 42.40714 ? 344  LYS A CD  1 
ATOM   1071 C  CE  . LYS A 1 141 ? 4.44385   17.75838 20.36798  1.000 51.56527 ? 344  LYS A CE  1 
ATOM   1072 N  NZ  . LYS A 1 141 ? 3.52365   16.85404 19.63028  1.000 55.69536 ? 344  LYS A NZ  1 
ATOM   1073 N  N   A MET A 1 142 ? 9.96602   19.43253 16.98526  0.581 31.16167 ? 345  MET A N   1 
ATOM   1074 N  N   B MET A 1 142 ? 9.97138   19.43813 16.93371  0.419 31.31132 ? 345  MET A N   1 
ATOM   1075 C  CA  A MET A 1 142 ? 11.28606  19.98399 16.71381  0.581 34.33514 ? 345  MET A CA  1 
ATOM   1076 C  CA  B MET A 1 142 ? 11.30896  19.96719 16.68829  0.419 34.38874 ? 345  MET A CA  1 
ATOM   1077 C  C   A MET A 1 142 ? 11.80788  20.79599 17.89193  0.581 33.04832 ? 345  MET A C   1 
ATOM   1078 C  C   B MET A 1 142 ? 11.81036  20.78686 17.87281  0.419 33.02205 ? 345  MET A C   1 
ATOM   1079 O  O   A MET A 1 142 ? 11.06781  21.57643 18.50375  0.581 30.34827 ? 345  MET A O   1 
ATOM   1080 O  O   B MET A 1 142 ? 11.05637  21.55951 18.47614  0.419 30.28177 ? 345  MET A O   1 
ATOM   1081 C  CB  A MET A 1 142 ? 11.25115  20.86244 15.45875  0.581 32.36043 ? 345  MET A CB  1 
ATOM   1082 C  CB  B MET A 1 142 ? 11.34011  20.83590 15.41372  0.419 31.44605 ? 345  MET A CB  1 
ATOM   1083 C  CG  A MET A 1 142 ? 10.98449  20.07664 14.19901  0.581 31.54381 ? 345  MET A CG  1 
ATOM   1084 C  CG  B MET A 1 142 ? 12.74663  21.05338 14.85894  0.419 35.19023 ? 345  MET A CG  1 
ATOM   1085 S  SD  A MET A 1 142 ? 10.67197  21.17261 12.82338  0.581 32.53268 ? 345  MET A SD  1 
ATOM   1086 S  SD  B MET A 1 142 ? 12.78891  21.79786 13.21717  0.419 41.37298 ? 345  MET A SD  1 
ATOM   1087 C  CE  A MET A 1 142 ? 12.19449  22.10739 12.77109  0.581 35.20837 ? 345  MET A CE  1 
ATOM   1088 C  CE  B MET A 1 142 ? 11.19611  21.30719 12.58400  0.419 33.09863 ? 345  MET A CE  1 
ATOM   1089 N  N   . LYS A 1 143 ? 13.09623  20.62455 18.18215  1.000 33.35224 ? 346  LYS A N   1 
ATOM   1090 C  CA  . LYS A 1 143 ? 13.76063  21.40880 19.21736  1.000 38.23597 ? 346  LYS A CA  1 
ATOM   1091 C  C   . LYS A 1 143 ? 14.20498  22.77074 18.68209  1.000 43.82855 ? 346  LYS A C   1 
ATOM   1092 O  O   . LYS A 1 143 ? 14.55157  22.92617 17.50534  1.000 40.03678 ? 346  LYS A O   1 
ATOM   1093 C  CB  . LYS A 1 143 ? 14.97525  20.65990 19.76629  1.000 43.07592 ? 346  LYS A CB  1 
ATOM   1094 C  CG  . LYS A 1 143 ? 14.64544  19.62234 20.82668  1.000 45.49314 ? 346  LYS A CG  1 
ATOM   1095 C  CD  . LYS A 1 143 ? 15.82134  18.70120 21.09500  1.000 51.90086 ? 346  LYS A CD  1 
ATOM   1096 C  CE  . LYS A 1 143 ? 15.67910  17.99909 22.43633  1.000 54.81521 ? 346  LYS A CE  1 
ATOM   1097 N  NZ  . LYS A 1 143 ? 16.59840  18.54409 23.47798  1.000 65.53555 ? 346  LYS A NZ  1 
ATOM   1098 N  N   . ILE A 1 144 ? 14.18804  23.76129 19.56472  1.000 43.32421 ? 347  ILE A N   1 
ATOM   1099 C  CA  . ILE A 1 144 ? 14.68942  25.09077 19.24145  1.000 41.95110 ? 347  ILE A CA  1 
ATOM   1100 C  C   . ILE A 1 144 ? 16.21157  25.05823 19.27891  1.000 46.85093 ? 347  ILE A C   1 
ATOM   1101 O  O   . ILE A 1 144 ? 16.80747  24.51192 20.21426  1.000 47.41408 ? 347  ILE A O   1 
ATOM   1102 C  CB  . ILE A 1 144 ? 14.12294  26.12662 20.22293  1.000 42.92172 ? 347  ILE A CB  1 
ATOM   1103 C  CG1 . ILE A 1 144 ? 12.59311  26.05183 20.22089  1.000 36.16174 ? 347  ILE A CG1 1 
ATOM   1104 C  CG2 . ILE A 1 144 ? 14.61776  27.52407 19.88370  1.000 36.46449 ? 347  ILE A CG2 1 
ATOM   1105 C  CD1 . ILE A 1 144 ? 11.92412  27.01523 21.18910  1.000 30.36172 ? 347  ILE A CD1 1 
ATOM   1106 N  N   . LYS A 1 145 ? 16.84705  25.61103 18.24751  1.000 45.64744 ? 348  LYS A N   1 
ATOM   1107 C  CA  . LYS A 1 145 ? 18.29997  25.68428 18.18014  1.000 51.29652 ? 348  LYS A CA  1 
ATOM   1108 C  C   . LYS A 1 145 ? 18.78564  27.07824 18.56694  1.000 60.00081 ? 348  LYS A C   1 
ATOM   1109 O  O   . LYS A 1 145 ? 18.06938  28.07089 18.41544  1.000 54.72244 ? 348  LYS A O   1 
ATOM   1110 C  CB  . LYS A 1 145 ? 18.81455  25.35328 16.77899  1.000 49.95083 ? 348  LYS A CB  1 
ATOM   1111 C  CG  . LYS A 1 145 ? 18.57661  23.94063 16.30164  1.000 49.53052 ? 348  LYS A CG  1 
ATOM   1112 C  CD  . LYS A 1 145 ? 19.28051  23.72990 14.96845  1.000 53.51114 ? 348  LYS A CD  1 
ATOM   1113 C  CE  . LYS A 1 145 ? 19.09470  22.30993 14.46030  1.000 50.70343 ? 348  LYS A CE  1 
ATOM   1114 N  NZ  . LYS A 1 145 ? 17.69618  22.02951 13.99546  1.000 49.96886 ? 348  LYS A NZ  1 
ATOM   1115 N  N   . ASN A 1 146 ? 20.02050  27.14161 19.06456  1.000 61.62844 ? 349  ASN A N   1 
ATOM   1116 C  CA  . ASN A 1 146 ? 20.73161  28.40185 19.26241  1.000 72.96624 ? 349  ASN A CA  1 
ATOM   1117 C  C   . ASN A 1 146 ? 22.10372  28.27750 18.61845  1.000 78.11916 ? 349  ASN A C   1 
ATOM   1118 O  O   . ASN A 1 146 ? 22.92214  27.45756 19.05393  1.000 75.47018 ? 349  ASN A O   1 
ATOM   1119 C  CB  . ASN A 1 146 ? 20.86781  28.76016 20.74407  1.000 68.97183 ? 349  ASN A CB  1 
ATOM   1120 C  CG  . ASN A 1 146 ? 19.61297  29.40445 21.30683  1.000 73.75327 ? 349  ASN A CG  1 
ATOM   1121 O  OD1 . ASN A 1 146 ? 18.79213  29.95447 20.56854  1.000 70.17248 ? 349  ASN A OD1 1 
ATOM   1122 N  ND2 . ASN A 1 146 ? 19.46259  29.34606 22.62390  1.000 77.56725 ? 349  ASN A ND2 1 
ATOM   1123 N  N   . ASN A 1 147 ? 22.34600  29.08967 17.58647  1.000 89.93391 ? 350  ASN A N   1 
ATOM   1124 C  CA  . ASN A 1 147 ? 23.58248  29.06314 16.79625  1.000 88.15724 ? 350  ASN A CA  1 
ATOM   1125 C  C   . ASN A 1 147 ? 23.96989  27.63455 16.41567  1.000 82.45984 ? 350  ASN A C   1 
ATOM   1126 O  O   . ASN A 1 147 ? 25.11954  27.21217 16.55150  1.000 90.14276 ? 350  ASN A O   1 
ATOM   1127 C  CB  . ASN A 1 147 ? 24.71933  29.76743 17.53641  1.000 83.02869 ? 350  ASN A CB  1 
ATOM   1128 N  N   . GLY A 1 148 ? 22.97913  26.87844 15.93693  1.000 73.55390 ? 351  GLY A N   1 
ATOM   1129 C  CA  . GLY A 1 148 ? 23.19304  25.51930 15.48421  1.000 73.31924 ? 351  GLY A CA  1 
ATOM   1130 C  C   . GLY A 1 148 ? 23.12633  24.43993 16.54685  1.000 70.03830 ? 351  GLY A C   1 
ATOM   1131 O  O   . GLY A 1 148 ? 22.95806  23.26420 16.19830  1.000 70.57673 ? 351  GLY A O   1 
ATOM   1132 N  N   . ILE A 1 149 ? 23.26021  24.78721 17.82719  1.000 76.38027 ? 352  ILE A N   1 
ATOM   1133 C  CA  . ILE A 1 149 ? 23.22178  23.81019 18.91104  1.000 71.62406 ? 352  ILE A CA  1 
ATOM   1134 C  C   . ILE A 1 149 ? 21.79463  23.70612 19.43393  1.000 69.36988 ? 352  ILE A C   1 
ATOM   1135 O  O   . ILE A 1 149 ? 21.14633  24.72442 19.71140  1.000 60.73854 ? 352  ILE A O   1 
ATOM   1136 C  CB  . ILE A 1 149 ? 24.19731  24.19721 20.03510  1.000 76.13968 ? 352  ILE A CB  1 
ATOM   1137 N  N   . GLU A 1 150 ? 21.30157  22.47543 19.56329  1.000 66.14716 ? 353  GLU A N   1 
ATOM   1138 C  CA  . GLU A 1 150 ? 19.94830  22.26397 20.05889  1.000 62.66689 ? 353  GLU A CA  1 
ATOM   1139 C  C   . GLU A 1 150 ? 19.86817  22.60474 21.54157  1.000 61.46153 ? 353  GLU A C   1 
ATOM   1140 O  O   . GLU A 1 150 ? 20.78862  22.32142 22.31089  1.000 60.89117 ? 353  GLU A O   1 
ATOM   1141 C  CB  . GLU A 1 150 ? 19.50900  20.81645 19.81826  1.000 60.89528 ? 353  GLU A CB  1 
ATOM   1142 C  CG  . GLU A 1 150 ? 19.42332  20.44841 18.34693  1.000 64.70927 ? 353  GLU A CG  1 
ATOM   1143 C  CD  . GLU A 1 150 ? 18.57302  19.21217 18.07388  1.000 75.59812 ? 353  GLU A CD  1 
ATOM   1144 O  OE1 . GLU A 1 150 ? 18.82695  18.14518 18.68317  1.000 73.63638 ? 353  GLU A OE1 1 
ATOM   1145 O  OE2 . GLU A 1 150 ? 17.64679  19.31195 17.23640  1.000 71.82515 ? 353  GLU A OE2 1 
ATOM   1146 N  N   . THR A 1 151 ? 18.77041  23.24096 21.93660  1.000 54.84220 ? 354  THR A N   1 
ATOM   1147 C  CA  . THR A 1 151 ? 18.50795  23.50327 23.34217  1.000 53.13634 ? 354  THR A CA  1 
ATOM   1148 C  C   . THR A 1 151 ? 17.64541  22.38029 23.92089  1.000 56.85617 ? 354  THR A C   1 
ATOM   1149 O  O   . THR A 1 151 ? 17.40702  21.34943 23.28346  1.000 55.40366 ? 354  THR A O   1 
ATOM   1150 C  CB  . THR A 1 151 ? 17.82062  24.85422 23.52323  1.000 45.99469 ? 354  THR A CB  1 
ATOM   1151 O  OG1 . THR A 1 151 ? 16.48157  24.76811 23.02684  1.000 47.16632 ? 354  THR A OG1 1 
ATOM   1152 C  CG2 . THR A 1 151 ? 18.56051  25.93650 22.76814  1.000 53.72936 ? 354  THR A CG2 1 
ATOM   1153 N  N   . GLU A 1 152 ? 17.14306  22.58689 25.13712  1.000 51.33676 ? 355  GLU A N   1 
ATOM   1154 C  CA  . GLU A 1 152 ? 16.22300  21.65132 25.77002  1.000 56.67783 ? 355  GLU A CA  1 
ATOM   1155 C  C   . GLU A 1 152 ? 14.76197  21.90997 25.40715  1.000 51.93078 ? 355  GLU A C   1 
ATOM   1156 O  O   . GLU A 1 152 ? 13.90938  21.06144 25.69450  1.000 45.05373 ? 355  GLU A O   1 
ATOM   1157 C  CB  . GLU A 1 152 ? 16.39424  21.70119 27.29598  1.000 47.65924 ? 355  GLU A CB  1 
ATOM   1158 N  N   . ASP A 1 153 ? 14.45391  23.04144 24.78005  1.000 37.43515 ? 356  ASP A N   1 
ATOM   1159 C  CA  . ASP A 1 153 ? 13.07598  23.41892 24.52331  1.000 38.05449 ? 356  ASP A CA  1 
ATOM   1160 C  C   . ASP A 1 153 ? 12.60978  22.95431 23.14260  1.000 44.16100 ? 356  ASP A C   1 
ATOM   1161 O  O   . ASP A 1 153 ? 13.40431  22.67149 22.23975  1.000 43.80241 ? 356  ASP A O   1 
ATOM   1162 C  CB  . ASP A 1 153 ? 12.90519  24.93251 24.63790  1.000 34.86060 ? 356  ASP A CB  1 
ATOM   1163 C  CG  . ASP A 1 153 ? 13.29004  25.46096 26.01274  1.000 48.47740 ? 356  ASP A CG  1 
ATOM   1164 O  OD1 . ASP A 1 153 ? 13.11057  24.72385 27.01128  1.000 51.98409 ? 356  ASP A OD1 1 
ATOM   1165 O  OD2 . ASP A 1 153 ? 13.77435  26.61128 26.09223  1.000 52.77884 ? 356  ASP A OD2 1 
ATOM   1166 N  N   . TYR A 1 154 ? 11.29146  22.90717 22.98598  1.000 40.41746 ? 357  TYR A N   1 
ATOM   1167 C  CA  . TYR A 1 154 ? 10.64910  22.49811 21.75353  1.000 33.98323 ? 357  TYR A CA  1 
ATOM   1168 C  C   . TYR A 1 154 ? 9.73992   23.61351 21.27334  1.000 35.51266 ? 357  TYR A C   1 
ATOM   1169 O  O   . TYR A 1 154 ? 9.17903   24.35826 22.07943  1.000 34.39170 ? 357  TYR A O   1 
ATOM   1170 C  CB  . TYR A 1 154 ? 9.82341   21.21748 21.95649  1.000 33.25345 ? 357  TYR A CB  1 
ATOM   1171 C  CG  . TYR A 1 154 ? 10.63143  19.95001 22.04338  1.000 35.12699 ? 357  TYR A CG  1 
ATOM   1172 C  CD1 . TYR A 1 154 ? 11.17298  19.51623 23.25044  1.000 41.45508 ? 357  TYR A CD1 1 
ATOM   1173 C  CD2 . TYR A 1 154 ? 10.85014  19.17782 20.91388  1.000 35.90581 ? 357  TYR A CD2 1 
ATOM   1174 C  CE1 . TYR A 1 154 ? 11.92205  18.33323 23.31785  1.000 40.09727 ? 357  TYR A CE1 1 
ATOM   1175 C  CE2 . TYR A 1 154 ? 11.59004  18.01415 20.96892  1.000 37.76705 ? 357  TYR A CE2 1 
ATOM   1176 C  CZ  . TYR A 1 154 ? 12.12044  17.59167 22.16594  1.000 45.77462 ? 357  TYR A CZ  1 
ATOM   1177 O  OH  . TYR A 1 154 ? 12.84647  16.42234 22.18738  1.000 48.20781 ? 357  TYR A OH  1 
ATOM   1178 N  N   . PHE A 1 155 ? 9.60462   23.73494 19.94953  1.000 33.79748 ? 358  PHE A N   1 
ATOM   1179 C  CA  . PHE A 1 155 ? 8.49222   24.49487 19.39708  1.000 31.94519 ? 358  PHE A CA  1 
ATOM   1180 C  C   . PHE A 1 155 ? 7.19751   23.77889 19.76148  1.000 34.31764 ? 358  PHE A C   1 
ATOM   1181 O  O   . PHE A 1 155 ? 7.07606   22.56296 19.58388  1.000 32.40680 ? 358  PHE A O   1 
ATOM   1182 C  CB  . PHE A 1 155 ? 8.63013   24.64011 17.86934  1.000 30.40028 ? 358  PHE A CB  1 
ATOM   1183 C  CG  . PHE A 1 155 ? 9.82073   25.48602 17.43391  1.000 28.90132 ? 358  PHE A CG  1 
ATOM   1184 C  CD1 . PHE A 1 155 ? 9.76113   26.87201 17.47838  1.000 29.58996 ? 358  PHE A CD1 1 
ATOM   1185 C  CD2 . PHE A 1 155 ? 10.98524  24.88938 16.95938  1.000 30.44546 ? 358  PHE A CD2 1 
ATOM   1186 C  CE1 . PHE A 1 155 ? 10.84564  27.65471 17.06253  1.000 30.93964 ? 358  PHE A CE1 1 
ATOM   1187 C  CE2 . PHE A 1 155 ? 12.07030  25.66195 16.54550  1.000 30.51624 ? 358  PHE A CE2 1 
ATOM   1188 C  CZ  . PHE A 1 155 ? 12.00251  27.04392 16.60830  1.000 30.56458 ? 358  PHE A CZ  1 
ATOM   1189 N  N   . THR A 1 156 ? 6.23937   24.51871 20.30608  1.000 33.87205 ? 359  THR A N   1 
ATOM   1190 C  CA  . THR A 1 156 ? 5.03685   23.90123 20.84503  1.000 38.43260 ? 359  THR A CA  1 
ATOM   1191 C  C   . THR A 1 156 ? 3.78359   24.22288 20.04256  1.000 32.31185 ? 359  THR A C   1 
ATOM   1192 O  O   . THR A 1 156 ? 2.70893   23.71428 20.37146  1.000 40.51815 ? 359  THR A O   1 
ATOM   1193 C  CB  . THR A 1 156 ? 4.84652   24.31354 22.31164  1.000 40.20087 ? 359  THR A CB  1 
ATOM   1194 O  OG1 . THR A 1 156 ? 4.80678   25.74442 22.40772  1.000 33.99475 ? 359  THR A OG1 1 
ATOM   1195 C  CG2 . THR A 1 156 ? 5.99645   23.78206 23.15249  1.000 34.83126 ? 359  THR A CG2 1 
ATOM   1196 N  N   . ASP A 1 157 ? 3.88413   25.04011 19.00701  1.000 36.50960 ? 360  ASP A N   1 
ATOM   1197 C  CA  . ASP A 1 157 ? 2.72845   25.26743 18.15659  1.000 33.31376 ? 360  ASP A CA  1 
ATOM   1198 C  C   . ASP A 1 157 ? 2.33881   23.95711 17.47628  1.000 34.89728 ? 360  ASP A C   1 
ATOM   1199 O  O   . ASP A 1 157 ? 3.21522   23.16809 17.10677  1.000 32.38823 ? 360  ASP A O   1 
ATOM   1200 C  CB  . ASP A 1 157 ? 3.03284   26.34547 17.13350  1.000 34.14464 ? 360  ASP A CB  1 
ATOM   1201 C  CG  . ASP A 1 157 ? 3.23857   27.70011 17.78146  1.000 46.44309 ? 360  ASP A CG  1 
ATOM   1202 O  OD1 . ASP A 1 157 ? 3.07913   27.77685 19.01848  1.000 47.55098 ? 360  ASP A OD1 1 
ATOM   1203 O  OD2 . ASP A 1 157 ? 3.55373   28.67909 17.07240  1.000 49.93355 ? 360  ASP A OD2 1 
ATOM   1204 N  N   . PRO A 1 158 ? 1.03797   23.67719 17.33933  1.000 35.92787 ? 361  PRO A N   1 
ATOM   1205 C  CA  . PRO A 1 158 ? 0.61686   22.34334 16.88882  1.000 31.07497 ? 361  PRO A CA  1 
ATOM   1206 C  C   . PRO A 1 158 ? 1.01516   22.04213 15.45949  1.000 35.26320 ? 361  PRO A C   1 
ATOM   1207 O  O   . PRO A 1 158 ? 1.13755   20.86024 15.10173  1.000 28.83083 ? 361  PRO A O   1 
ATOM   1208 C  CB  . PRO A 1 158 ? -0.91233  22.38149 17.02733  1.000 35.17275 ? 361  PRO A CB  1 
ATOM   1209 C  CG  . PRO A 1 158 ? -1.22973  23.62770 17.76134  1.000 37.36083 ? 361  PRO A CG  1 
ATOM   1210 C  CD  . PRO A 1 158 ? -0.10303  24.57153 17.57767  1.000 32.80106 ? 361  PRO A CD  1 
ATOM   1211 N  N   . PHE A 1 159 ? 1.21658   23.06434 14.63770  1.000 27.94445 ? 362  PHE A N   1 
ATOM   1212 C  CA  . PHE A 1 159 ? 1.56561   22.87287 13.23625  1.000 30.33256 ? 362  PHE A CA  1 
ATOM   1213 C  C   . PHE A 1 159 ? 3.06157   22.74473 13.01524  1.000 27.25319 ? 362  PHE A C   1 
ATOM   1214 O  O   . PHE A 1 159 ? 3.47981   22.52611 11.87228  1.000 25.79878 ? 362  PHE A O   1 
ATOM   1215 C  CB  . PHE A 1 159 ? 1.02426   24.02922 12.38616  1.000 25.28857 ? 362  PHE A CB  1 
ATOM   1216 C  CG  . PHE A 1 159 ? 1.44345   25.38292 12.88937  1.000 29.72081 ? 362  PHE A CG  1 
ATOM   1217 C  CD1 . PHE A 1 159 ? 2.64180   25.94829 12.47970  1.000 27.56368 ? 362  PHE A CD1 1 
ATOM   1218 C  CD2 . PHE A 1 159 ? 0.65600   26.07254 13.80551  1.000 34.28391 ? 362  PHE A CD2 1 
ATOM   1219 C  CE1 . PHE A 1 159 ? 3.04385   27.18649 12.95948  1.000 33.22055 ? 362  PHE A CE1 1 
ATOM   1220 C  CE2 . PHE A 1 159 ? 1.05178   27.30816 14.29333  1.000 30.25448 ? 362  PHE A CE2 1 
ATOM   1221 C  CZ  . PHE A 1 159 ? 2.24472   27.87114 13.86681  1.000 29.82568 ? 362  PHE A CZ  1 
ATOM   1222 N  N   . VAL A 1 160 ? 3.88522   22.88683 14.05476  1.000 20.01165 ? 363  VAL A N   1 
ATOM   1223 C  CA  . VAL A 1 160 ? 5.33152   22.79846 13.87664  1.000 24.75164 ? 363  VAL A CA  1 
ATOM   1224 C  C   . VAL A 1 160 ? 5.73798   21.33767 14.05419  1.000 31.12195 ? 363  VAL A C   1 
ATOM   1225 O  O   . VAL A 1 160 ? 5.95786   20.86742 15.17075  1.000 30.38525 ? 363  VAL A O   1 
ATOM   1226 C  CB  . VAL A 1 160 ? 6.09136   23.72668 14.82135  1.000 30.08516 ? 363  VAL A CB  1 
ATOM   1227 C  CG1 . VAL A 1 160 ? 7.57416   23.68690 14.49195  1.000 27.93582 ? 363  VAL A CG1 1 
ATOM   1228 C  CG2 . VAL A 1 160 ? 5.57034   25.15020 14.68071  1.000 31.12617 ? 363  VAL A CG2 1 
ATOM   1229 N  N   . PHE A 1 161 ? 5.84437   20.61279 12.93863  1.000 25.88993 ? 364  PHE A N   1 
ATOM   1230 C  CA  . PHE A 1 161 ? 6.31304   19.23713 12.98058  1.000 25.53993 ? 364  PHE A CA  1 
ATOM   1231 C  C   . PHE A 1 161 ? 6.98555   18.90635 11.66218  1.000 25.76302 ? 364  PHE A C   1 
ATOM   1232 O  O   . PHE A 1 161 ? 6.68630   19.51490 10.62877  1.000 24.05956 ? 364  PHE A O   1 
ATOM   1233 C  CB  . PHE A 1 161 ? 5.17811   18.24499 13.24372  1.000 19.39874 ? 364  PHE A CB  1 
ATOM   1234 C  CG  . PHE A 1 161 ? 4.06128   18.30467 12.22910  1.000 27.09320 ? 364  PHE A CG  1 
ATOM   1235 C  CD1 . PHE A 1 161 ? 4.15596   17.62536 11.01909  1.000 26.75490 ? 364  PHE A CD1 1 
ATOM   1236 C  CD2 . PHE A 1 161 ? 2.90464   19.02068 12.49766  1.000 22.99730 ? 364  PHE A CD2 1 
ATOM   1237 C  CE1 . PHE A 1 161 ? 3.12886   17.68254 10.09287  1.000 25.71703 ? 364  PHE A CE1 1 
ATOM   1238 C  CE2 . PHE A 1 161 ? 1.86979   19.06114 11.58768  1.000 28.22509 ? 364  PHE A CE2 1 
ATOM   1239 C  CZ  . PHE A 1 161 ? 1.98271   18.39069 10.37786  1.000 22.58299 ? 364  PHE A CZ  1 
ATOM   1240 N  N   . LYS A 1 162 ? 7.90389   17.94521 11.71993  1.000 22.76271 ? 365  LYS A N   1 
ATOM   1241 C  CA  . LYS A 1 162 ? 8.42432   17.28529 10.53407  1.000 29.48664 ? 365  LYS A CA  1 
ATOM   1242 C  C   . LYS A 1 162 ? 7.52248   16.10936 10.18112  1.000 25.19575 ? 365  LYS A C   1 
ATOM   1243 O  O   . LYS A 1 162 ? 7.05628   15.38532 11.06199  1.000 25.88788 ? 365  LYS A O   1 
ATOM   1244 C  CB  . LYS A 1 162 ? 9.85309   16.80267 10.76590  1.000 22.83754 ? 365  LYS A CB  1 
ATOM   1245 C  CG  . LYS A 1 162 ? 10.81698  17.91969 11.13844  1.000 29.03169 ? 365  LYS A CG  1 
ATOM   1246 C  CD  . LYS A 1 162 ? 12.23208  17.38754 11.36561  1.000 29.16866 ? 365  LYS A CD  1 
ATOM   1247 C  CE  . LYS A 1 162 ? 12.40253  16.86684 12.77260  1.000 39.55783 ? 365  LYS A CE  1 
ATOM   1248 N  NZ  . LYS A 1 162 ? 13.84451  16.84310 13.14779  1.000 47.59359 ? 365  LYS A NZ  1 
ATOM   1249 N  N   . TRP A 1 163 ? 7.23267   15.94632 8.89515   1.000 23.11713 ? 366  TRP A N   1 
ATOM   1250 C  CA  . TRP A 1 163 ? 6.48827   14.77024 8.44934   1.000 21.05821 ? 366  TRP A CA  1 
ATOM   1251 C  C   . TRP A 1 163 ? 7.52178   13.73036 8.02704   1.000 23.48818 ? 366  TRP A C   1 
ATOM   1252 O  O   . TRP A 1 163 ? 8.09620   13.80975 6.94396   1.000 25.70411 ? 366  TRP A O   1 
ATOM   1253 C  CB  . TRP A 1 163 ? 5.51215   15.11112 7.32628   1.000 20.04083 ? 366  TRP A CB  1 
ATOM   1254 C  CG  . TRP A 1 163 ? 4.62081   13.95152 6.91663   1.000 21.80921 ? 366  TRP A CG  1 
ATOM   1255 C  CD1 . TRP A 1 163 ? 4.60182   12.68972 7.45900   1.000 23.32765 ? 366  TRP A CD1 1 
ATOM   1256 C  CD2 . TRP A 1 163 ? 3.62019   13.95826 5.89079   1.000 22.65314 ? 366  TRP A CD2 1 
ATOM   1257 N  NE1 . TRP A 1 163 ? 3.65330   11.91422 6.83004   1.000 24.72902 ? 366  TRP A NE1 1 
ATOM   1258 C  CE2 . TRP A 1 163 ? 3.04236   12.67016 5.85889   1.000 25.43592 ? 366  TRP A CE2 1 
ATOM   1259 C  CE3 . TRP A 1 163 ? 3.15341   14.93166 4.99534   1.000 23.34192 ? 366  TRP A CE3 1 
ATOM   1260 C  CZ2 . TRP A 1 163 ? 2.02928   12.32951 4.96133   1.000 29.91093 ? 366  TRP A CZ2 1 
ATOM   1261 C  CZ3 . TRP A 1 163 ? 2.13774   14.59228 4.10629   1.000 24.08020 ? 366  TRP A CZ3 1 
ATOM   1262 C  CH2 . TRP A 1 163 ? 1.59432   13.30008 4.09072   1.000 26.95170 ? 366  TRP A CH2 1 
ATOM   1263 N  N   . LYS A 1 164 ? 7.75302   12.75456 8.89492   1.000 22.08224 ? 367  LYS A N   1 
ATOM   1264 C  CA  . LYS A 1 164 ? 8.76076   11.72862 8.66007   1.000 29.36853 ? 367  LYS A CA  1 
ATOM   1265 C  C   . LYS A 1 164 ? 8.36550   10.79968 7.50408   1.000 24.41216 ? 367  LYS A C   1 
ATOM   1266 O  O   . LYS A 1 164 ? 7.22320   10.35857 7.40011   1.000 21.05365 ? 367  LYS A O   1 
ATOM   1267 C  CB  . LYS A 1 164 ? 8.94718   10.93667 9.95882   1.000 31.55841 ? 367  LYS A CB  1 
ATOM   1268 C  CG  . LYS A 1 164 ? 9.70543   9.64531  9.84235   1.000 37.22949 ? 367  LYS A CG  1 
ATOM   1269 C  CD  . LYS A 1 164 ? 9.98814   9.07970  11.23012  1.000 39.42281 ? 367  LYS A CD  1 
ATOM   1270 C  CE  . LYS A 1 164 ? 8.69380   8.81948  11.99265  1.000 43.97764 ? 367  LYS A CE  1 
ATOM   1271 N  N   . GLU A 1 165 ? 9.31589   10.50070 6.63042   1.000 21.33709 ? 368  GLU A N   1 
ATOM   1272 C  CA  . GLU A 1 165 ? 9.09300   9.48009  5.60958   1.000 23.19609 ? 368  GLU A CA  1 
ATOM   1273 C  C   . GLU A 1 165 ? 9.16926   8.07659  6.20997   1.000 26.46248 ? 368  GLU A C   1 
ATOM   1274 O  O   . GLU A 1 165 ? 10.11801  7.75477  6.92946   1.000 24.95538 ? 368  GLU A O   1 
ATOM   1275 C  CB  . GLU A 1 165 ? 10.12628  9.61114  4.48620   1.000 28.15143 ? 368  GLU A CB  1 
ATOM   1276 C  CG  . GLU A 1 165 ? 9.90421   8.64878  3.32270   1.000 26.56328 ? 368  GLU A CG  1 
ATOM   1277 C  CD  . GLU A 1 165 ? 10.69668  9.04406  2.07542   1.000 29.08142 ? 368  GLU A CD  1 
ATOM   1278 O  OE1 . GLU A 1 165 ? 11.88961  8.67542  1.99337   1.000 30.57801 ? 368  GLU A OE1 1 
ATOM   1279 O  OE2 . GLU A 1 165 ? 10.12927  9.71935  1.17412   1.000 23.36665 ? 368  GLU A OE2 1 
ATOM   1280 N  N   . THR A 1 166 ? 8.17281   7.24283  5.90866   1.000 24.45174 ? 369  THR A N   1 
ATOM   1281 C  CA  . THR A 1 166 ? 8.16702   5.83197  6.28394   1.000 29.86182 ? 369  THR A CA  1 
ATOM   1282 C  C   . THR A 1 166 ? 7.78682   4.99768  5.06818   1.000 27.86890 ? 369  THR A C   1 
ATOM   1283 O  O   . THR A 1 166 ? 7.47083   5.53076  4.00272   1.000 29.45376 ? 369  THR A O   1 
ATOM   1284 C  CB  . THR A 1 166 ? 7.18396   5.54321  7.42160   1.000 35.88477 ? 369  THR A CB  1 
ATOM   1285 O  OG1 . THR A 1 166 ? 5.84771   5.56107  6.89981   1.000 27.25483 ? 369  THR A OG1 1 
ATOM   1286 C  CG2 . THR A 1 166 ? 7.32780   6.57489  8.56581   1.000 31.91954 ? 369  THR A CG2 1 
ATOM   1287 N  N   . ALA A 1 167 ? 7.79814   3.67122  5.23496   1.000 27.69250 ? 370  ALA A N   1 
ATOM   1288 C  CA  . ALA A 1 167 ? 7.39182   2.78663  4.14496   1.000 27.19969 ? 370  ALA A CA  1 
ATOM   1289 C  C   . ALA A 1 167 ? 5.98985   3.11182  3.63933   1.000 23.92684 ? 370  ALA A C   1 
ATOM   1290 O  O   . ALA A 1 167 ? 5.67591   2.85159  2.46726   1.000 27.91562 ? 370  ALA A O   1 
ATOM   1291 C  CB  . ALA A 1 167 ? 7.45310   1.31806  4.60451   1.000 26.87334 ? 370  ALA A CB  1 
ATOM   1292 N  N   . ASP A 1 168 ? 5.13713   3.67114  4.49842   1.000 26.78649 ? 371  ASP A N   1 
ATOM   1293 C  CA  . ASP A 1 168 ? 3.73006   3.90908  4.19386   1.000 27.07878 ? 371  ASP A CA  1 
ATOM   1294 C  C   . ASP A 1 168 ? 3.41590   5.33769  3.72394   1.000 27.86567 ? 371  ASP A C   1 
ATOM   1295 O  O   . ASP A 1 168 ? 2.25649   5.62274  3.42008   1.000 27.64549 ? 371  ASP A O   1 
ATOM   1296 C  CB  . ASP A 1 168 ? 2.87435   3.58353  5.42879   1.000 33.46267 ? 371  ASP A CB  1 
ATOM   1297 C  CG  . ASP A 1 168 ? 3.12352   2.15815  5.96798   1.000 47.28098 ? 371  ASP A CG  1 
ATOM   1298 O  OD1 . ASP A 1 168 ? 3.09256   1.19035  5.15874   1.000 37.01672 ? 371  ASP A OD1 1 
ATOM   1299 O  OD2 . ASP A 1 168 ? 3.37923   2.01720  7.19477   1.000 38.56818 ? 371  ASP A OD2 1 
ATOM   1300 N  N   . THR A 1 169 ? 4.38371   6.24790  3.66444   1.000 24.81458 ? 372  THR A N   1 
ATOM   1301 C  CA  . THR A 1 169 ? 4.04738   7.60429  3.23026   1.000 23.36844 ? 372  THR A CA  1 
ATOM   1302 C  C   . THR A 1 169 ? 4.14145   7.72871  1.70527   1.000 24.07513 ? 372  THR A C   1 
ATOM   1303 O  O   . THR A 1 169 ? 4.84319   6.96600  1.03636   1.000 24.99672 ? 372  THR A O   1 
ATOM   1304 C  CB  . THR A 1 169 ? 4.95514   8.64382  3.91662   1.000 25.25365 ? 372  THR A CB  1 
ATOM   1305 O  OG1 . THR A 1 169 ? 6.33224   8.33568  3.67726   1.000 24.22823 ? 372  THR A OG1 1 
ATOM   1306 C  CG2 . THR A 1 169 ? 4.71506   8.65908  5.42510   1.000 24.90241 ? 372  THR A CG2 1 
ATOM   1307 N  N   . LYS A 1 170 ? 3.43528   8.72207  1.15535   1.000 24.44939 ? 373  LYS A N   1 
ATOM   1308 C  CA  . LYS A 1 170 ? 3.27258   8.83800  -0.29404  1.000 22.04857 ? 373  LYS A CA  1 
ATOM   1309 C  C   . LYS A 1 170 ? 3.73935   10.16934 -0.90354  1.000 23.16884 ? 373  LYS A C   1 
ATOM   1310 O  O   . LYS A 1 170 ? 3.45959   10.42082 -2.08550  1.000 20.19286 ? 373  LYS A O   1 
ATOM   1311 C  CB  . LYS A 1 170 ? 1.80740   8.59385  -0.65567  1.000 23.54487 ? 373  LYS A CB  1 
ATOM   1312 C  CG  . LYS A 1 170 ? 1.35181   7.15638  -0.40654  1.000 28.92718 ? 373  LYS A CG  1 
ATOM   1313 C  CD  . LYS A 1 170 ? -0.11324  7.08885  -0.03719  1.000 34.10099 ? 373  LYS A CD  1 
ATOM   1314 C  CE  . LYS A 1 170 ? -1.02412  7.34062  -1.21960  1.000 41.97953 ? 373  LYS A CE  1 
ATOM   1315 N  N   . PHE A 1 171 ? 4.43519   11.02408 -0.15329  1.000 19.45936 ? 374  PHE A N   1 
ATOM   1316 C  CA  . PHE A 1 171 ? 5.10894   12.17317 -0.74727  1.000 22.64892 ? 374  PHE A CA  1 
ATOM   1317 C  C   . PHE A 1 171 ? 6.48606   11.75743 -1.27257  1.000 22.10249 ? 374  PHE A C   1 
ATOM   1318 O  O   . PHE A 1 171 ? 6.96604   10.64406 -1.03184  1.000 20.21989 ? 374  PHE A O   1 
ATOM   1319 C  CB  . PHE A 1 171 ? 5.23708   13.32333 0.27010   1.000 18.18134 ? 374  PHE A CB  1 
ATOM   1320 C  CG  . PHE A 1 171 ? 6.03207   12.97294 1.52010   1.000 19.63575 ? 374  PHE A CG  1 
ATOM   1321 C  CD1 . PHE A 1 171 ? 7.42147   13.03373 1.52439   1.000 17.53286 ? 374  PHE A CD1 1 
ATOM   1322 C  CD2 . PHE A 1 171 ? 5.38259   12.61182 2.69395   1.000 20.30621 ? 374  PHE A CD2 1 
ATOM   1323 C  CE1 . PHE A 1 171 ? 8.15486   12.74090 2.66558   1.000 17.77488 ? 374  PHE A CE1 1 
ATOM   1324 C  CE2 . PHE A 1 171 ? 6.11047   12.28997 3.86221   1.000 22.30229 ? 374  PHE A CE2 1 
ATOM   1325 C  CZ  . PHE A 1 171 ? 7.49037   12.35035 3.85101   1.000 21.27151 ? 374  PHE A CZ  1 
ATOM   1326 N  N   . TYR A 1 172 ? 7.14096   12.67681 -1.98669  1.000 18.53880 ? 375  TYR A N   1 
ATOM   1327 C  CA  . TYR A 1 172 ? 8.48060   12.43813 -2.51140  1.000 18.07000 ? 375  TYR A CA  1 
ATOM   1328 C  C   . TYR A 1 172 ? 9.43026   13.54319 -2.05818  1.000 21.65030 ? 375  TYR A C   1 
ATOM   1329 O  O   . TYR A 1 172 ? 9.07471   14.72479 -2.06967  1.000 18.21260 ? 375  TYR A O   1 
ATOM   1330 C  CB  . TYR A 1 172 ? 8.44796   12.32867 -4.05468  1.000 19.46862 ? 375  TYR A CB  1 
ATOM   1331 C  CG  . TYR A 1 172 ? 7.45537   11.27288 -4.49080  1.000 20.05619 ? 375  TYR A CG  1 
ATOM   1332 C  CD1 . TYR A 1 172 ? 7.82749   9.94154  -4.56351  1.000 19.70687 ? 375  TYR A CD1 1 
ATOM   1333 C  CD2 . TYR A 1 172 ? 6.13636   11.60434 -4.76999  1.000 18.95218 ? 375  TYR A CD2 1 
ATOM   1334 C  CE1 . TYR A 1 172 ? 6.92374   8.97417  -4.92089  1.000 19.60365 ? 375  TYR A CE1 1 
ATOM   1335 C  CE2 . TYR A 1 172 ? 5.23045   10.64764 -5.13622  1.000 20.85836 ? 375  TYR A CE2 1 
ATOM   1336 C  CZ  . TYR A 1 172 ? 5.63191   9.32749  -5.20426  1.000 21.64385 ? 375  TYR A CZ  1 
ATOM   1337 O  OH  . TYR A 1 172 ? 4.73655   8.34980  -5.56362  1.000 22.50206 ? 375  TYR A OH  1 
ATOM   1338 N  N   . ASN A 1 173 ? 10.65037  13.15099 -1.66845  1.000 21.09271 ? 376  ASN A N   1 
ATOM   1339 C  CA  . ASN A 1 173 ? 11.66452  14.10041 -1.19386  1.000 21.95189 ? 376  ASN A CA  1 
ATOM   1340 C  C   . ASN A 1 173 ? 13.04481  13.56078 -1.57436  1.000 21.99756 ? 376  ASN A C   1 
ATOM   1341 O  O   . ASN A 1 173 ? 13.77768  13.02868 -0.74155  1.000 24.61410 ? 376  ASN A O   1 
ATOM   1342 C  CB  . ASN A 1 173 ? 11.57157  14.33809 0.31750   1.000 19.24637 ? 376  ASN A CB  1 
ATOM   1343 C  CG  . ASN A 1 173 ? 12.71418  15.20292 0.84355   1.000 23.60475 ? 376  ASN A CG  1 
ATOM   1344 O  OD1 . ASN A 1 173 ? 13.21657  16.08656 0.14544   1.000 23.20115 ? 376  ASN A OD1 1 
ATOM   1345 N  ND2 . ASN A 1 173 ? 13.16097  14.91854 2.05639   1.000 24.47026 ? 376  ASN A ND2 1 
ATOM   1346 N  N   . VAL A 1 174 ? 13.41500  13.71640 -2.85436  1.000 20.02671 ? 377  VAL A N   1 
ATOM   1347 C  CA  . VAL A 1 174 ? 14.75934  13.32303 -3.28146  1.000 20.26810 ? 377  VAL A CA  1 
ATOM   1348 C  C   . VAL A 1 174 ? 15.76438  14.35129 -2.77356  1.000 25.78504 ? 377  VAL A C   1 
ATOM   1349 O  O   . VAL A 1 174 ? 15.52858  15.56798 -2.83518  1.000 26.64777 ? 377  VAL A O   1 
ATOM   1350 C  CB  . VAL A 1 174 ? 14.84905  13.15977 -4.81719  1.000 23.90551 ? 377  VAL A CB  1 
ATOM   1351 C  CG1 . VAL A 1 174 ? 13.91353  12.05369 -5.30324  1.000 19.89405 ? 377  VAL A CG1 1 
ATOM   1352 C  CG2 . VAL A 1 174 ? 14.51835  14.47459 -5.54396  1.000 21.10426 ? 377  VAL A CG2 1 
ATOM   1353 N  N   . ARG A 1 175 ? 16.88927  13.87158 -2.25341  1.000 24.49041 ? 378  ARG A N   1 
ATOM   1354 C  CA  . ARG A 1 175 ? 17.87071  14.73972 -1.62377  1.000 28.56177 ? 378  ARG A CA  1 
ATOM   1355 C  C   . ARG A 1 175 ? 19.12707  14.82022 -2.47872  1.000 29.88069 ? 378  ARG A C   1 
ATOM   1356 O  O   . ARG A 1 175 ? 19.41034  13.93913 -3.29953  1.000 27.23393 ? 378  ARG A O   1 
ATOM   1357 C  CB  . ARG A 1 175 ? 18.21324  14.25384 -0.20381  1.000 29.06692 ? 378  ARG A CB  1 
ATOM   1358 C  CG  . ARG A 1 175 ? 17.08885  14.47591 0.81458   1.000 27.38959 ? 378  ARG A CG  1 
ATOM   1359 C  CD  . ARG A 1 175 ? 17.29349  13.65849 2.10514   1.000 33.72284 ? 378  ARG A CD  1 
ATOM   1360 N  NE  . ARG A 1 175 ? 17.21717  12.21784 1.87894   1.000 33.99471 ? 378  ARG A NE  1 
ATOM   1361 C  CZ  . ARG A 1 175 ? 17.65728  11.29650 2.72971   1.000 36.75604 ? 378  ARG A CZ  1 
ATOM   1362 N  NH1 . ARG A 1 175 ? 18.17941  11.62700 3.90557   1.000 29.60431 ? 378  ARG A NH1 1 
ATOM   1363 N  NH2 . ARG A 1 175 ? 17.58663  10.01336 2.38700   1.000 30.13864 ? 378  ARG A NH2 1 
ATOM   1364 N  N   . LYS A 1 176 ? 19.86678  15.91221 -2.28846  1.000 26.98020 ? 379  LYS A N   1 
ATOM   1365 C  CA  . LYS A 1 176 ? 21.12155  16.10782 -3.00133  1.000 33.05396 ? 379  LYS A CA  1 
ATOM   1366 C  C   . LYS A 1 176 ? 22.19170  15.21328 -2.40103  1.000 35.88952 ? 379  LYS A C   1 
ATOM   1367 O  O   . LYS A 1 176 ? 22.51725  15.33842 -1.21393  1.000 35.30054 ? 379  LYS A O   1 
ATOM   1368 C  CB  . LYS A 1 176 ? 21.56738  17.56580 -2.92656  1.000 32.18755 ? 379  LYS A CB  1 
ATOM   1369 C  CG  . LYS A 1 176 ? 20.64766  18.56600 -3.57543  1.000 33.04568 ? 379  LYS A CG  1 
ATOM   1370 C  CD  . LYS A 1 176 ? 21.17253  19.97106 -3.30243  1.000 42.46824 ? 379  LYS A CD  1 
ATOM   1371 C  CE  . LYS A 1 176 ? 20.51336  21.00844 -4.19779  1.000 39.26942 ? 379  LYS A CE  1 
ATOM   1372 N  NZ  . LYS A 1 176 ? 20.84117  22.40592 -3.77900  1.000 45.26500 ? 379  LYS A NZ  1 
ATOM   1373 N  N   . LEU A 1 177 ? 22.74875  14.32213 -3.22314  1.000 29.70260 ? 380  LEU A N   1 
ATOM   1374 C  CA  . LEU A 1 177 ? 23.84924  13.49106 -2.76096  1.000 31.05989 ? 380  LEU A CA  1 
ATOM   1375 C  C   . LEU A 1 177 ? 25.05092  14.33776 -2.36118  1.000 38.50747 ? 380  LEU A C   1 
ATOM   1376 O  O   . LEU A 1 177 ? 25.73263  14.01635 -1.37917  1.000 38.08163 ? 380  LEU A O   1 
ATOM   1377 C  CB  . LEU A 1 177 ? 24.23859  12.48142 -3.83410  1.000 32.77770 ? 380  LEU A CB  1 
ATOM   1378 C  CG  . LEU A 1 177 ? 23.27971  11.31486 -4.06500  1.000 34.90234 ? 380  LEU A CG  1 
ATOM   1379 C  CD1 . LEU A 1 177 ? 22.01328  11.75853 -4.76508  1.000 33.17657 ? 380  LEU A CD1 1 
ATOM   1380 C  CD2 . LEU A 1 177 ? 23.97547  10.22079 -4.85960  1.000 35.48111 ? 380  LEU A CD2 1 
ATOM   1381 N  N   . ASP A 1 178 ? 25.30466  15.43575 -3.08902  1.000 37.12969 ? 381  ASP A N   1 
ATOM   1382 C  CA  . ASP A 1 178 ? 26.43459  16.31132 -2.78190  1.000 37.65247 ? 381  ASP A CA  1 
ATOM   1383 C  C   . ASP A 1 178 ? 26.32834  16.93106 -1.39128  1.000 41.43472 ? 381  ASP A C   1 
ATOM   1384 O  O   . ASP A 1 178 ? 27.34935  17.30817 -0.80344  1.000 42.79986 ? 381  ASP A O   1 
ATOM   1385 C  CB  . ASP A 1 178 ? 26.55080  17.41776 -3.83368  1.000 42.23295 ? 381  ASP A CB  1 
ATOM   1386 C  CG  . ASP A 1 178 ? 27.26741  16.95461 -5.10086  1.000 50.61008 ? 381  ASP A CG  1 
ATOM   1387 O  OD1 . ASP A 1 178 ? 27.78130  15.81936 -5.12143  1.000 54.17010 ? 381  ASP A OD1 1 
ATOM   1388 O  OD2 . ASP A 1 178 ? 27.31989  17.72255 -6.08324  1.000 49.94690 ? 381  ASP A OD2 1 
ATOM   1389 N  N   . LYS A 1 179 ? 25.11699  17.06473 -0.85729  1.000 39.93344 ? 382  LYS A N   1 
ATOM   1390 C  CA  . LYS A 1 179 ? 24.95893  17.55004 0.50925   1.000 41.24523 ? 382  LYS A CA  1 
ATOM   1391 C  C   . LYS A 1 179 ? 24.96023  16.41865 1.53850   1.000 43.83570 ? 382  LYS A C   1 
ATOM   1392 O  O   . LYS A 1 179 ? 25.52379  16.58153 2.62196   1.000 45.55178 ? 382  LYS A O   1 
ATOM   1393 C  CB  . LYS A 1 179 ? 23.67481  18.36689 0.63233   1.000 38.46501 ? 382  LYS A CB  1 
ATOM   1394 C  CG  . LYS A 1 179 ? 23.74064  19.72105 -0.07394  1.000 50.07287 ? 382  LYS A CG  1 
ATOM   1395 C  CD  . LYS A 1 179 ? 24.54233  20.76327 0.71674   1.000 47.64460 ? 382  LYS A CD  1 
ATOM   1396 N  N   . LEU A 1 180 ? 24.35371  15.26583 1.22482   1.000 36.44021 ? 383  LEU A N   1 
ATOM   1397 C  CA  . LEU A 1 180 ? 24.37055  14.14667 2.16074   1.000 38.55542 ? 383  LEU A CA  1 
ATOM   1398 C  C   . LEU A 1 180 ? 25.76198  13.55538 2.31665   1.000 43.82005 ? 383  LEU A C   1 
ATOM   1399 O  O   . LEU A 1 180 ? 26.10134  13.05693 3.39600   1.000 47.27252 ? 383  LEU A O   1 
ATOM   1400 C  CB  . LEU A 1 180 ? 23.41518  13.04668 1.69899   1.000 35.33847 ? 383  LEU A CB  1 
ATOM   1401 C  CG  . LEU A 1 180 ? 21.92689  13.30789 1.86253   1.000 37.89734 ? 383  LEU A CG  1 
ATOM   1402 C  CD1 . LEU A 1 180 ? 21.12517  12.15513 1.26808   1.000 33.18366 ? 383  LEU A CD1 1 
ATOM   1403 C  CD2 . LEU A 1 180 ? 21.58426  13.52478 3.34597   1.000 37.41275 ? 383  LEU A CD2 1 
ATOM   1404 N  N   . TYR A 1 181 ? 26.56212  13.58478 1.25337   1.000 34.59257 ? 384  TYR A N   1 
ATOM   1405 C  CA  . TYR A 1 181 ? 27.85198  12.90752 1.23585   1.000 36.05703 ? 384  TYR A CA  1 
ATOM   1406 C  C   . TYR A 1 181 ? 28.71643  13.31648 2.42372   1.000 41.59597 ? 384  TYR A C   1 
ATOM   1407 O  O   . TYR A 1 181 ? 28.87580  14.50448 2.71051   1.000 39.18115 ? 384  TYR A O   1 
ATOM   1408 C  CB  . TYR A 1 181 ? 28.56581  13.22899 -0.06997  1.000 36.60178 ? 384  TYR A CB  1 
ATOM   1409 C  CG  . TYR A 1 181 ? 29.86765  12.50225 -0.28832  1.000 38.28637 ? 384  TYR A CG  1 
ATOM   1410 C  CD1 . TYR A 1 181 ? 29.90533  11.11458 -0.37853  1.000 40.06609 ? 384  TYR A CD1 1 
ATOM   1411 C  CD2 . TYR A 1 181 ? 31.05651  13.20899 -0.45912  1.000 39.91809 ? 384  TYR A CD2 1 
ATOM   1412 C  CE1 . TYR A 1 181 ? 31.09978  10.45013 -0.60076  1.000 40.89265 ? 384  TYR A CE1 1 
ATOM   1413 C  CE2 . TYR A 1 181 ? 32.25210  12.55928 -0.68891  1.000 41.68573 ? 384  TYR A CE2 1 
ATOM   1414 C  CZ  . TYR A 1 181 ? 32.27108  11.17957 -0.75523  1.000 44.35023 ? 384  TYR A CZ  1 
ATOM   1415 O  OH  . TYR A 1 181 ? 33.46594  10.52881 -0.97267  1.000 44.19089 ? 384  TYR A OH  1 
ATOM   1416 N  N   . VAL A 1 182 ? 29.26087  12.32856 3.12849   1.000 38.67237 ? 385  VAL A N   1 
ATOM   1417 C  CA  . VAL A 1 182 ? 30.19570  12.57550 4.21488   1.000 40.03632 ? 385  VAL A CA  1 
ATOM   1418 C  C   . VAL A 1 182 ? 31.55203  12.08140 3.75218   1.000 41.78096 ? 385  VAL A C   1 
ATOM   1419 O  O   . VAL A 1 182 ? 31.78011  10.86650 3.67307   1.000 42.28904 ? 385  VAL A O   1 
ATOM   1420 C  CB  . VAL A 1 182 ? 29.78162  11.88727 5.52290   1.000 44.90020 ? 385  VAL A CB  1 
ATOM   1421 C  CG1 . VAL A 1 182 ? 30.87960  12.08903 6.57323   1.000 42.08458 ? 385  VAL A CG1 1 
ATOM   1422 C  CG2 . VAL A 1 182 ? 28.45439  12.43094 6.02206   1.000 41.19649 ? 385  VAL A CG2 1 
ATOM   1423 N  N   . GLN A 1 183 ? 32.45338  13.02611 3.46334   1.000 42.91692 ? 386  GLN A N   1 
ATOM   1424 C  CA  . GLN A 1 183 ? 33.77964  12.69442 2.95756   1.000 44.84815 ? 386  GLN A CA  1 
ATOM   1425 C  C   . GLN A 1 183 ? 34.50635  11.79711 3.94778   1.000 46.42529 ? 386  GLN A C   1 
ATOM   1426 O  O   . GLN A 1 183 ? 34.69134  12.16924 5.10987   1.000 47.09800 ? 386  GLN A O   1 
ATOM   1427 C  CB  . GLN A 1 183 ? 34.58632  13.97584 2.70644   1.000 46.10052 ? 386  GLN A CB  1 
ATOM   1428 C  CG  . GLN A 1 183 ? 33.92162  14.98040 1.74051   1.000 44.86896 ? 386  GLN A CG  1 
ATOM   1429 C  CD  . GLN A 1 183 ? 34.81175  16.18230 1.42544   1.000 46.53558 ? 386  GLN A CD  1 
ATOM   1430 O  OE1 . GLN A 1 183 ? 35.07293  17.03029 2.28867   1.000 47.33627 ? 386  GLN A OE1 1 
ATOM   1431 N  NE2 . GLN A 1 183 ? 35.29185  16.25028 0.18609   1.000 47.26282 ? 386  GLN A NE2 1 
ATOM   1432 N  N   . GLY A 1 184 ? 34.91107  10.61155 3.48925   1.000 47.15334 ? 387  GLY A N   1 
ATOM   1433 C  CA  . GLY A 1 184 ? 35.62675  9.67546  4.32900   1.000 48.89178 ? 387  GLY A CA  1 
ATOM   1434 C  C   . GLY A 1 184 ? 34.76242  8.71023  5.11801   1.000 48.08547 ? 387  GLY A C   1 
ATOM   1435 O  O   . GLY A 1 184 ? 35.30829  7.83802  5.80326   1.000 51.93574 ? 387  GLY A O   1 
ATOM   1436 N  N   . GLN A 1 185 ? 33.44267  8.84446  5.06667   1.000 45.92723 ? 388  GLN A N   1 
ATOM   1437 C  CA  . GLN A 1 185 ? 32.52913  7.86095  5.63758   1.000 45.25023 ? 388  GLN A CA  1 
ATOM   1438 C  C   . GLN A 1 185 ? 31.70364  7.14457  4.58303   1.000 46.04790 ? 388  GLN A C   1 
ATOM   1439 O  O   . GLN A 1 185 ? 31.50924  5.93178  4.67269   1.000 47.90521 ? 388  GLN A O   1 
ATOM   1440 C  CB  . GLN A 1 185 ? 31.57836  8.52774  6.63941   1.000 44.14691 ? 388  GLN A CB  1 
ATOM   1441 C  CG  . GLN A 1 185 ? 32.24351  9.03383  7.91504   1.000 53.50618 ? 388  GLN A CG  1 
ATOM   1442 N  N   . PHE A 1 186 ? 31.22302  7.86478  3.58098   1.000 42.45179 ? 389  PHE A N   1 
ATOM   1443 C  CA  . PHE A 1 186 ? 30.39329  7.27371  2.54664   1.000 41.17736 ? 389  PHE A CA  1 
ATOM   1444 C  C   . PHE A 1 186 ? 31.25012  6.46955  1.57344   1.000 49.17465 ? 389  PHE A C   1 
ATOM   1445 O  O   . PHE A 1 186 ? 32.45919  6.69147  1.47328   1.000 47.46776 ? 389  PHE A O   1 
ATOM   1446 C  CB  . PHE A 1 186 ? 29.62208  8.36352  1.80889   1.000 42.51001 ? 389  PHE A CB  1 
ATOM   1447 C  CG  . PHE A 1 186 ? 28.37198  8.82080  2.52118   1.000 42.22610 ? 389  PHE A CG  1 
ATOM   1448 C  CD1 . PHE A 1 186 ? 28.27302  8.75727  3.91008   1.000 45.99086 ? 389  PHE A CD1 1 
ATOM   1449 C  CD2 . PHE A 1 186 ? 27.28715  9.30149  1.79509   1.000 39.26835 ? 389  PHE A CD2 1 
ATOM   1450 C  CE1 . PHE A 1 186 ? 27.11340  9.17816  4.56290   1.000 43.18355 ? 389  PHE A CE1 1 
ATOM   1451 C  CE2 . PHE A 1 186 ? 26.13486  9.72139  2.43461   1.000 38.85187 ? 389  PHE A CE2 1 
ATOM   1452 C  CZ  . PHE A 1 186 ? 26.04557  9.66469  3.82233   1.000 43.63818 ? 389  PHE A CZ  1 
ATOM   1453 N  N   . PRO A 1 187 ? 30.65073  5.51384  0.85179   1.000 57.01827 ? 390  PRO A N   1 
ATOM   1454 C  CA  . PRO A 1 187 ? 31.42887  4.72485  -0.11233  1.000 57.68408 ? 390  PRO A CA  1 
ATOM   1455 C  C   . PRO A 1 187 ? 31.94305  5.58690  -1.25886  1.000 57.72855 ? 390  PRO A C   1 
ATOM   1456 O  O   . PRO A 1 187 ? 31.41319  6.65962  -1.56006  1.000 55.80920 ? 390  PRO A O   1 
ATOM   1457 C  CB  . PRO A 1 187 ? 30.42719  3.67527  -0.61525  1.000 59.49664 ? 390  PRO A CB  1 
ATOM   1458 C  CG  . PRO A 1 187 ? 29.30080  3.68899  0.36867   1.000 55.36947 ? 390  PRO A CG  1 
ATOM   1459 C  CD  . PRO A 1 187 ? 29.24176  5.08087  0.90109   1.000 48.14034 ? 390  PRO A CD  1 
ATOM   1460 N  N   . SER A 1 188 ? 33.00008  5.09059  -1.90794  1.000 53.25448 ? 391  SER A N   1 
ATOM   1461 C  CA  . SER A 1 188 ? 33.65235  5.83957  -2.97603  1.000 52.29469 ? 391  SER A CA  1 
ATOM   1462 C  C   . SER A 1 188 ? 32.83098  5.86629  -4.25999  1.000 51.25324 ? 391  SER A C   1 
ATOM   1463 O  O   . SER A 1 188 ? 33.01457  6.77807  -5.07399  1.000 53.75176 ? 391  SER A O   1 
ATOM   1464 C  CB  . SER A 1 188 ? 35.04175  5.25609  -3.25176  1.000 47.95412 ? 391  SER A CB  1 
ATOM   1465 N  N   . ASN A 1 189 ? 31.93630  4.89372  -4.46404  1.000 51.61721 ? 392  ASN A N   1 
ATOM   1466 C  CA  . ASN A 1 189 ? 31.06625  4.85816  -5.63571  1.000 52.41791 ? 392  ASN A CA  1 
ATOM   1467 C  C   . ASN A 1 189 ? 29.70591  5.51062  -5.38140  1.000 50.09762 ? 392  ASN A C   1 
ATOM   1468 O  O   . ASN A 1 189 ? 28.73598  5.18751  -6.07854  1.000 42.75417 ? 392  ASN A O   1 
ATOM   1469 C  CB  . ASN A 1 189 ? 30.87213  3.41566  -6.11613  1.000 52.39510 ? 392  ASN A CB  1 
ATOM   1470 C  CG  . ASN A 1 189 ? 30.19207  2.53178  -5.07546  1.000 57.64017 ? 392  ASN A CG  1 
ATOM   1471 O  OD1 . ASN A 1 189 ? 29.83610  2.98427  -3.98325  1.000 55.45986 ? 392  ASN A OD1 1 
ATOM   1472 N  ND2 . ASN A 1 189 ? 29.99869  1.26398  -5.41842  1.000 55.83632 ? 392  ASN A ND2 1 
ATOM   1473 N  N   . TYR A 1 190 ? 29.62739  6.43133  -4.41080  1.000 46.87792 ? 393  TYR A N   1 
ATOM   1474 C  CA  . TYR A 1 190 ? 28.34353  6.96756  -3.96633  1.000 45.30101 ? 393  TYR A CA  1 
ATOM   1475 C  C   . TYR A 1 190 ? 27.58493  7.66702  -5.08354  1.000 38.37338 ? 393  TYR A C   1 
ATOM   1476 O  O   . TYR A 1 190 ? 26.35234  7.58701  -5.13252  1.000 38.14190 ? 393  TYR A O   1 
ATOM   1477 C  CB  . TYR A 1 190 ? 28.56839  7.92891  -2.80996  1.000 41.41185 ? 393  TYR A CB  1 
ATOM   1478 C  CG  . TYR A 1 190 ? 27.32150  8.51966  -2.18224  1.000 39.31768 ? 393  TYR A CG  1 
ATOM   1479 C  CD1 . TYR A 1 190 ? 26.35756  7.71314  -1.58790  1.000 39.00015 ? 393  TYR A CD1 1 
ATOM   1480 C  CD2 . TYR A 1 190 ? 27.13517  9.89724  -2.14381  1.000 37.49536 ? 393  TYR A CD2 1 
ATOM   1481 C  CE1 . TYR A 1 190 ? 25.23382  8.27034  -0.98748  1.000 36.96476 ? 393  TYR A CE1 1 
ATOM   1482 C  CE2 . TYR A 1 190 ? 26.02603  10.45897 -1.54619  1.000 35.35775 ? 393  TYR A CE2 1 
ATOM   1483 C  CZ  . TYR A 1 190 ? 25.08391  9.64605  -0.96826  1.000 35.71780 ? 393  TYR A CZ  1 
ATOM   1484 O  OH  . TYR A 1 190 ? 23.99189  10.22426 -0.37293  1.000 34.09098 ? 393  TYR A OH  1 
ATOM   1485 N  N   . PHE A 1 191 ? 28.29280  8.33606  -5.99226  1.000 44.20278 ? 394  PHE A N   1 
ATOM   1486 C  CA  . PHE A 1 191 ? 27.68207  9.11870  -7.06099  1.000 43.40592 ? 394  PHE A CA  1 
ATOM   1487 C  C   . PHE A 1 191 ? 27.55944  8.36514  -8.38555  1.000 43.88484 ? 394  PHE A C   1 
ATOM   1488 O  O   . PHE A 1 191 ? 27.15785  8.96756  -9.38235  1.000 44.31233 ? 394  PHE A O   1 
ATOM   1489 C  CB  . PHE A 1 191 ? 28.48033  10.40569 -7.29183  1.000 44.24867 ? 394  PHE A CB  1 
ATOM   1490 C  CG  . PHE A 1 191 ? 28.67373  11.23183 -6.05521  1.000 40.92882 ? 394  PHE A CG  1 
ATOM   1491 C  CD1 . PHE A 1 191 ? 27.68777  12.11291 -5.63250  1.000 41.59978 ? 394  PHE A CD1 1 
ATOM   1492 C  CD2 . PHE A 1 191 ? 29.84592  11.14011 -5.31992  1.000 41.21896 ? 394  PHE A CD2 1 
ATOM   1493 C  CE1 . PHE A 1 191 ? 27.85977  12.88122 -4.48253  1.000 42.15894 ? 394  PHE A CE1 1 
ATOM   1494 C  CE2 . PHE A 1 191 ? 30.03193  11.91489 -4.17076  1.000 45.35039 ? 394  PHE A CE2 1 
ATOM   1495 C  CZ  . PHE A 1 191 ? 29.03817  12.78783 -3.75368  1.000 42.51168 ? 394  PHE A CZ  1 
ATOM   1496 N  N   . VAL A 1 192 ? 27.88962  7.07808  -8.43093  1.000 43.06714 ? 395  VAL A N   1 
ATOM   1497 C  CA  . VAL A 1 192 ? 27.86119  6.34210  -9.69207  1.000 42.42821 ? 395  VAL A CA  1 
ATOM   1498 C  C   . VAL A 1 192 ? 26.42357  6.01555  -10.07145 1.000 40.94027 ? 395  VAL A C   1 
ATOM   1499 O  O   . VAL A 1 192 ? 25.65158  5.48863  -9.26115  1.000 37.32494 ? 395  VAL A O   1 
ATOM   1500 C  CB  . VAL A 1 192 ? 28.70098  5.05939  -9.60954  1.000 45.46027 ? 395  VAL A CB  1 
ATOM   1501 C  CG1 . VAL A 1 192 ? 28.71258  4.36701  -10.97704 1.000 45.69135 ? 395  VAL A CG1 1 
ATOM   1502 C  CG2 . VAL A 1 192 ? 30.11618  5.36595  -9.15447  1.000 51.75725 ? 395  VAL A CG2 1 
ATOM   1503 N  N   . ILE A 1 193 ? 26.07328  6.30119  -11.31995 1.000 37.97739 ? 396  ILE A N   1 
ATOM   1504 C  CA  . ILE A 1 193 ? 24.76382  6.00103  -11.87418 1.000 40.84204 ? 396  ILE A CA  1 
ATOM   1505 C  C   . ILE A 1 193 ? 24.94040  5.00259  -13.00707 1.000 46.12549 ? 396  ILE A C   1 
ATOM   1506 O  O   . ILE A 1 193 ? 25.89779  5.09053  -13.78173 1.000 50.63873 ? 396  ILE A O   1 
ATOM   1507 C  CB  . ILE A 1 193 ? 24.07022  7.28421  -12.37415 1.000 43.45359 ? 396  ILE A CB  1 
ATOM   1508 C  CG1 . ILE A 1 193 ? 23.86605  8.25615  -11.21199 1.000 37.45065 ? 396  ILE A CG1 1 
ATOM   1509 C  CG2 . ILE A 1 193 ? 22.74080  6.96960  -13.04924 1.000 35.45886 ? 396  ILE A CG2 1 
ATOM   1510 C  CD1 . ILE A 1 193 ? 23.43098  9.61620  -11.64792 1.000 33.95182 ? 396  ILE A CD1 1 
ATOM   1511 N  N   . ASN A 1 194 ? 24.03047  4.04576  -13.09853 1.000 46.90141 ? 397  ASN A N   1 
ATOM   1512 C  CA  . ASN A 1 194 ? 23.96173  3.18128  -14.26796 1.000 51.50354 ? 397  ASN A CA  1 
ATOM   1513 C  C   . ASN A 1 194 ? 22.97826  3.81472  -15.24719 1.000 46.94106 ? 397  ASN A C   1 
ATOM   1514 O  O   . ASN A 1 194 ? 21.77863  3.88589  -14.97224 1.000 46.17014 ? 397  ASN A O   1 
ATOM   1515 C  CB  . ASN A 1 194 ? 23.54855  1.76520  -13.88126 1.000 50.76729 ? 397  ASN A CB  1 
ATOM   1516 C  CG  . ASN A 1 194 ? 23.65108  0.79358  -15.04962 1.000 65.95074 ? 397  ASN A CG  1 
ATOM   1517 O  OD1 . ASN A 1 194 ? 22.69529  0.08283  -15.37671 1.000 62.00493 ? 397  ASN A OD1 1 
ATOM   1518 N  ND2 . ASN A 1 194 ? 24.81497  0.77225  -15.69612 1.000 62.51638 ? 397  ASN A ND2 1 
ATOM   1519 N  N   . GLY A 1 195 ? 23.49021  4.29146  -16.37843 1.000 55.10240 ? 398  GLY A N   1 
ATOM   1520 C  CA  . GLY A 1 195 ? 22.70651  5.06165  -17.32323 1.000 57.43575 ? 398  GLY A CA  1 
ATOM   1521 C  C   . GLY A 1 195 ? 21.78965  4.21838  -18.18711 1.000 55.59690 ? 398  GLY A C   1 
ATOM   1522 O  O   . GLY A 1 195 ? 21.53245  3.04377  -17.91303 1.000 55.65262 ? 398  GLY A O   1 
ATOM   1523 N  N   . ILE A 1 196 ? 21.29381  4.83855  -19.26266 1.000 56.61160 ? 399  ILE A N   1 
ATOM   1524 C  CA  . ILE A 1 196 ? 20.28766  4.18348  -20.09645 1.000 66.11220 ? 399  ILE A CA  1 
ATOM   1525 C  C   . ILE A 1 196 ? 20.91308  3.04224  -20.89144 1.000 66.99050 ? 399  ILE A C   1 
ATOM   1526 O  O   . ILE A 1 196 ? 20.38802  1.92304  -20.91143 1.000 72.21983 ? 399  ILE A O   1 
ATOM   1527 C  CB  . ILE A 1 196 ? 19.58241  5.20468  -21.01150 1.000 62.89386 ? 399  ILE A CB  1 
ATOM   1528 C  CG1 . ILE A 1 196 ? 20.58298  6.17319  -21.63375 1.000 66.80645 ? 399  ILE A CG1 1 
ATOM   1529 C  CG2 . ILE A 1 196 ? 18.50571  5.97055  -20.24663 1.000 57.11755 ? 399  ILE A CG2 1 
ATOM   1530 C  CD1 . ILE A 1 196 ? 19.93524  7.33636  -22.35289 1.000 65.10699 ? 399  ILE A CD1 1 
ATOM   1531 N  N   . ARG A 1 197 ? 22.04882  3.29903  -21.54957 1.000 60.85589 ? 400  ARG A N   1 
ATOM   1532 C  CA  . ARG A 1 197 ? 22.79261  2.24571  -22.23241 1.000 63.33448 ? 400  ARG A CA  1 
ATOM   1533 C  C   . ARG A 1 197 ? 23.68667  1.45380  -21.27876 1.000 64.85711 ? 400  ARG A C   1 
ATOM   1534 O  O   . ARG A 1 197 ? 24.68186  0.86111  -21.72037 1.000 61.66030 ? 400  ARG A O   1 
ATOM   1535 C  CB  . ARG A 1 197 ? 23.62899  2.83188  -23.37691 1.000 59.76500 ? 400  ARG A CB  1 
ATOM   1536 C  CG  . ARG A 1 197 ? 22.83113  3.15615  -24.63153 1.000 49.81525 ? 400  ARG A CG  1 
ATOM   1537 N  N   . ASN A 1 198 ? 23.33353  1.43218  -19.99074 1.000 62.94196 ? 401  ASN A N   1 
ATOM   1538 C  CA  . ASN A 1 198 ? 24.10507  0.78442  -18.93062 1.000 61.28895 ? 401  ASN A CA  1 
ATOM   1539 C  C   . ASN A 1 198 ? 25.52397  1.34713  -18.80962 1.000 60.82812 ? 401  ASN A C   1 
ATOM   1540 O  O   . ASN A 1 198 ? 26.42547  0.67538  -18.29475 1.000 55.09522 ? 401  ASN A O   1 
ATOM   1541 C  CB  . ASN A 1 198 ? 24.13960  -0.73952 -19.11658 1.000 66.88185 ? 401  ASN A CB  1 
ATOM   1542 C  CG  . ASN A 1 198 ? 22.76032  -1.37839 -18.97892 1.000 69.28496 ? 401  ASN A CG  1 
ATOM   1543 O  OD1 . ASN A 1 198 ? 21.93786  -0.95420 -18.16108 1.000 60.68987 ? 401  ASN A OD1 1 
ATOM   1544 N  ND2 . ASN A 1 198 ? 22.50243  -2.40180 -19.78784 1.000 68.43853 ? 401  ASN A ND2 1 
ATOM   1545 N  N   . GLU A 1 199 ? 25.73986  2.57825  -19.26355 1.000 60.80046 ? 402  GLU A N   1 
ATOM   1546 C  CA  . GLU A 1 199 ? 27.01844  3.24198  -19.06898 1.000 64.58895 ? 402  GLU A CA  1 
ATOM   1547 C  C   . GLU A 1 199 ? 27.15156  3.71623  -17.61644 1.000 59.08837 ? 402  GLU A C   1 
ATOM   1548 O  O   . GLU A 1 199 ? 26.16266  3.92759  -16.91150 1.000 54.64977 ? 402  GLU A O   1 
ATOM   1549 C  CB  . GLU A 1 199 ? 27.16476  4.41590  -20.04673 1.000 57.95896 ? 402  GLU A CB  1 
ATOM   1550 C  CG  . GLU A 1 199 ? 26.36682  5.67403  -19.67430 1.000 63.17547 ? 402  GLU A CG  1 
ATOM   1551 C  CD  . GLU A 1 199 ? 24.98406  5.76354  -20.32339 1.000 60.93565 ? 402  GLU A CD  1 
ATOM   1552 O  OE1 . GLU A 1 199 ? 24.73405  6.74118  -21.06674 1.000 63.19823 ? 402  GLU A OE1 1 
ATOM   1553 O  OE2 . GLU A 1 199 ? 24.14180  4.87256  -20.08179 1.000 63.22154 ? 402  GLU A OE2 1 
ATOM   1554 N  N   . GLN A 1 200 ? 28.39534  3.86206  -17.16610 1.000 53.73138 ? 403  GLN A N   1 
ATOM   1555 C  CA  . GLN A 1 200 ? 28.69569  4.28573  -15.80323 1.000 55.46999 ? 403  GLN A CA  1 
ATOM   1556 C  C   . GLN A 1 200 ? 28.95207  5.78699  -15.79276 1.000 53.90244 ? 403  GLN A C   1 
ATOM   1557 O  O   . GLN A 1 200 ? 29.81964  6.27183  -16.52407 1.000 53.05359 ? 403  GLN A O   1 
ATOM   1558 C  CB  . GLN A 1 200 ? 29.90776  3.53350  -15.26308 1.000 47.86870 ? 403  GLN A CB  1 
ATOM   1559 C  CG  . GLN A 1 200 ? 29.74950  2.02680  -15.29110 1.000 57.34739 ? 403  GLN A CG  1 
ATOM   1560 C  CD  . GLN A 1 200 ? 28.92320  1.50154  -14.13283 1.000 63.21408 ? 403  GLN A CD  1 
ATOM   1561 O  OE1 . GLN A 1 200 ? 27.69018  1.52729  -14.16449 1.000 63.88380 ? 403  GLN A OE1 1 
ATOM   1562 N  NE2 . GLN A 1 200 ? 29.60358  1.01416  -13.09993 1.000 69.92038 ? 403  GLN A NE2 1 
ATOM   1563 N  N   . ILE A 1 201 ? 28.20238  6.51724  -14.96600 1.000 49.87199 ? 404  ILE A N   1 
ATOM   1564 C  CA  . ILE A 1 201 ? 28.26666  7.97504  -14.91104 1.000 48.82233 ? 404  ILE A CA  1 
ATOM   1565 C  C   . ILE A 1 201 ? 28.38472  8.42021  -13.45696 1.000 50.29984 ? 404  ILE A C   1 
ATOM   1566 O  O   . ILE A 1 201 ? 27.69525  7.89262  -12.57755 1.000 48.25266 ? 404  ILE A O   1 
ATOM   1567 C  CB  . ILE A 1 201 ? 27.02693  8.61817  -15.57014 1.000 53.68982 ? 404  ILE A CB  1 
ATOM   1568 C  CG1 . ILE A 1 201 ? 26.74345  7.98570  -16.93085 1.000 46.96577 ? 404  ILE A CG1 1 
ATOM   1569 C  CG2 . ILE A 1 201 ? 27.21642  10.11042 -15.73994 1.000 46.29791 ? 404  ILE A CG2 1 
ATOM   1570 C  CD1 . ILE A 1 201 ? 25.46464  8.48143  -17.55059 1.000 48.92331 ? 404  ILE A CD1 1 
ATOM   1571 N  N   . GLN A 1 202 ? 29.26298  9.39118  -13.20756 1.000 57.49810 ? 405  GLN A N   1 
ATOM   1572 C  CA  . GLN A 1 202 ? 29.44462  9.99963  -11.89017 1.000 56.45842 ? 405  GLN A CA  1 
ATOM   1573 C  C   . GLN A 1 202 ? 28.67282  11.31165 -11.88934 1.000 59.94041 ? 405  GLN A C   1 
ATOM   1574 O  O   . GLN A 1 202 ? 29.19000  12.34455 -12.31940 1.000 69.63508 ? 405  GLN A O   1 
ATOM   1575 C  CB  . GLN A 1 202 ? 30.92155  10.23591 -11.58782 1.000 61.66784 ? 405  GLN A CB  1 
ATOM   1576 C  CG  . GLN A 1 202 ? 31.69830  8.99021  -11.20429 1.000 67.34142 ? 405  GLN A CG  1 
ATOM   1577 C  CD  . GLN A 1 202 ? 32.05229  8.94990  -9.72833  1.000 79.09736 ? 405  GLN A CD  1 
ATOM   1578 O  OE1 . GLN A 1 202 ? 32.08769  9.98323  -9.05175  1.000 78.03796 ? 405  GLN A OE1 1 
ATOM   1579 N  NE2 . GLN A 1 202 ? 32.32410  7.75159  -9.22111  1.000 79.02068 ? 405  GLN A NE2 1 
ATOM   1580 N  N   . GLY A 1 203 ? 27.43710  11.27551 -11.40100 1.000 47.91929 ? 406  GLY A N   1 
ATOM   1581 C  CA  . GLY A 1 203 ? 26.56691  12.43831 -11.42215 1.000 45.73751 ? 406  GLY A CA  1 
ATOM   1582 C  C   . GLY A 1 203 ? 26.61804  13.20609 -10.11806 1.000 45.94821 ? 406  GLY A C   1 
ATOM   1583 O  O   . GLY A 1 203 ? 26.50318  12.62758 -9.03207  1.000 41.03824 ? 406  GLY A O   1 
ATOM   1584 N  N   . ARG A 1 204 ? 26.77936  14.52121 -10.23373 1.000 42.35230 ? 407  ARG A N   1 
ATOM   1585 C  CA  . ARG A 1 204 ? 26.77710  15.41379 -9.08540  1.000 47.40262 ? 407  ARG A CA  1 
ATOM   1586 C  C   . ARG A 1 204 ? 25.62197  16.40412 -9.21286  1.000 40.26595 ? 407  ARG A C   1 
ATOM   1587 O  O   . ARG A 1 204 ? 25.17433  16.71704 -10.31579 1.000 41.50983 ? 407  ARG A O   1 
ATOM   1588 C  CB  . ARG A 1 204 ? 28.12627  16.14226 -8.95063  1.000 46.67484 ? 407  ARG A CB  1 
ATOM   1589 C  CG  . ARG A 1 204 ? 29.37229  15.24605 -9.17979  1.000 50.30392 ? 407  ARG A CG  1 
ATOM   1590 C  CD  . ARG A 1 204 ? 29.43171  13.98515 -8.29298  1.000 49.05016 ? 407  ARG A CD  1 
ATOM   1591 N  NE  . ARG A 1 204 ? 29.86782  14.26070 -6.92544  1.000 47.86539 ? 407  ARG A NE  1 
ATOM   1592 C  CZ  . ARG A 1 204 ? 31.12731  14.20474 -6.50447  1.000 51.17554 ? 407  ARG A CZ  1 
ATOM   1593 N  NH1 . ARG A 1 204 ? 32.11816  13.85133 -7.31433  1.000 55.03026 ? 407  ARG A NH1 1 
ATOM   1594 N  NH2 . ARG A 1 204 ? 31.40428  14.52607 -5.24321  1.000 47.99300 ? 407  ARG A NH2 1 
ATOM   1595 N  N   . ASP A 1 205 ? 25.12760  16.88949 -8.06622  1.000 45.36342 ? 408  ASP A N   1 
ATOM   1596 C  CA  . ASP A 1 205 ? 23.85843  17.61003 -8.03167  1.000 37.29793 ? 408  ASP A CA  1 
ATOM   1597 C  C   . ASP A 1 205 ? 23.87570  18.82926 -7.10513  1.000 38.71486 ? 408  ASP A C   1 
ATOM   1598 O  O   . ASP A 1 205 ? 22.80559  19.26336 -6.65936  1.000 37.58735 ? 408  ASP A O   1 
ATOM   1599 C  CB  . ASP A 1 205 ? 22.71767  16.64895 -7.60874  1.000 32.41045 ? 408  ASP A CB  1 
ATOM   1600 C  CG  . ASP A 1 205 ? 23.00373  15.91895 -6.27483  1.000 39.19043 ? 408  ASP A CG  1 
ATOM   1601 O  OD1 . ASP A 1 205 ? 23.97634  16.28187 -5.57179  1.000 34.58518 ? 408  ASP A OD1 1 
ATOM   1602 O  OD2 . ASP A 1 205 ? 22.25085  14.97510 -5.92771  1.000 32.15314 ? 408  ASP A OD2 1 
ATOM   1603 N  N   . ILE A 1 206 ? 25.05093  19.41071 -6.83132  1.000 42.24282 ? 409  ILE A N   1 
ATOM   1604 C  CA  . ILE A 1 206 ? 25.18125  20.42732 -5.77910  1.000 45.61632 ? 409  ILE A CA  1 
ATOM   1605 C  C   . ILE A 1 206 ? 24.28335  21.64473 -6.02264  1.000 49.40451 ? 409  ILE A C   1 
ATOM   1606 O  O   . ILE A 1 206 ? 23.82241  22.28634 -5.06554  1.000 43.92095 ? 409  ILE A O   1 
ATOM   1607 C  CB  . ILE A 1 206 ? 26.65813  20.84986 -5.61881  1.000 45.77618 ? 409  ILE A CB  1 
ATOM   1608 C  CG1 . ILE A 1 206 ? 26.80293  21.89226 -4.51138  1.000 47.15050 ? 409  ILE A CG1 1 
ATOM   1609 C  CG2 . ILE A 1 206 ? 27.22827  21.40141 -6.92126  1.000 50.39566 ? 409  ILE A CG2 1 
ATOM   1610 C  CD1 . ILE A 1 206 ? 26.64983  21.32030 -3.13461  1.000 56.44163 ? 409  ILE A CD1 1 
ATOM   1611 N  N   . SER A 1 207 ? 24.00121  21.97973 -7.28406  1.000 40.78861 ? 410  SER A N   1 
ATOM   1612 C  CA  . SER A 1 207 ? 23.12788  23.10846 -7.58326  1.000 42.60809 ? 410  SER A CA  1 
ATOM   1613 C  C   . SER A 1 207 ? 21.84177  22.69879 -8.30135  1.000 41.63987 ? 410  SER A C   1 
ATOM   1614 O  O   . SER A 1 207 ? 21.22609  23.52696 -8.97370  1.000 45.98902 ? 410  SER A O   1 
ATOM   1615 C  CB  . SER A 1 207 ? 23.87760  24.15106 -8.40849  1.000 58.62053 ? 410  SER A CB  1 
ATOM   1616 O  OG  . SER A 1 207 ? 24.12846  23.65621 -9.70781  1.000 68.75639 ? 410  SER A OG  1 
ATOM   1617 N  N   . GLN A 1 208 ? 21.39277  21.45497 -8.14309  1.000 37.97338 ? 411  GLN A N   1 
ATOM   1618 C  CA  . GLN A 1 208 ? 20.23654  20.94092 -8.88132  1.000 37.91718 ? 411  GLN A CA  1 
ATOM   1619 C  C   . GLN A 1 208 ? 18.93946  21.00434 -8.07273  1.000 38.47568 ? 411  GLN A C   1 
ATOM   1620 O  O   . GLN A 1 208 ? 18.09020  20.11041 -8.19722  1.000 31.90928 ? 411  GLN A O   1 
ATOM   1621 C  CB  . GLN A 1 208 ? 20.49593  19.50455 -9.33960  1.000 38.51135 ? 411  GLN A CB  1 
ATOM   1622 C  CG  . GLN A 1 208 ? 21.42457  19.35223 -10.53458 1.000 39.19251 ? 411  GLN A CG  1 
ATOM   1623 C  CD  . GLN A 1 208 ? 21.21407  18.02511 -11.27301 1.000 39.90221 ? 411  GLN A CD  1 
ATOM   1624 O  OE1 . GLN A 1 208 ? 20.74537  17.04415 -10.69475 1.000 35.19559 ? 411  GLN A OE1 1 
ATOM   1625 N  NE2 . GLN A 1 208 ? 21.54667  18.00209 -12.55662 1.000 41.51296 ? 411  GLN A NE2 1 
ATOM   1626 N  N   . CYS A 1 209 ? 18.72728  22.03215 -7.24372  1.000 34.70032 ? 412  CYS A N   1 
ATOM   1627 C  CA  . CYS A 1 209 ? 17.47852  22.07424 -6.48775  1.000 34.87179 ? 412  CYS A CA  1 
ATOM   1628 C  C   . CYS A 1 209 ? 16.26669  22.20685 -7.41376  1.000 31.33277 ? 412  CYS A C   1 
ATOM   1629 O  O   . CYS A 1 209 ? 15.20461  21.63131 -7.13667  1.000 30.24253 ? 412  CYS A O   1 
ATOM   1630 C  CB  . CYS A 1 209 ? 17.51316  23.19562 -5.44064  1.000 41.98999 ? 412  CYS A CB  1 
ATOM   1631 S  SG  . CYS A 1 209 ? 17.90445  24.87293 -6.02441  1.000 62.47402 ? 412  CYS A SG  1 
ATOM   1632 N  N   . TRP A 1 210 ? 16.40511  22.93580 -8.53163  1.000 27.75412 ? 413  TRP A N   1 
ATOM   1633 C  CA  . TRP A 1 210 ? 15.33398  22.94389 -9.53222  1.000 26.25546 ? 413  TRP A CA  1 
ATOM   1634 C  C   . TRP A 1 210 ? 15.01050  21.52850 -10.00839 1.000 25.70192 ? 413  TRP A C   1 
ATOM   1635 O  O   . TRP A 1 210 ? 13.84014  21.19253 -10.23421 1.000 24.73411 ? 413  TRP A O   1 
ATOM   1636 C  CB  . TRP A 1 210 ? 15.71800  23.82943 -10.72853 1.000 28.52063 ? 413  TRP A CB  1 
ATOM   1637 C  CG  . TRP A 1 210 ? 16.95581  23.37215 -11.40570 1.000 35.30218 ? 413  TRP A CG  1 
ATOM   1638 C  CD1 . TRP A 1 210 ? 18.24648  23.68171 -11.06279 1.000 35.33413 ? 413  TRP A CD1 1 
ATOM   1639 C  CD2 . TRP A 1 210 ? 17.04085  22.49765 -12.54102 1.000 31.39473 ? 413  TRP A CD2 1 
ATOM   1640 N  NE1 . TRP A 1 210 ? 19.12487  23.05146 -11.91129 1.000 38.21574 ? 413  TRP A NE1 1 
ATOM   1641 C  CE2 . TRP A 1 210 ? 18.41223  22.31465 -12.82432 1.000 35.27485 ? 413  TRP A CE2 1 
ATOM   1642 C  CE3 . TRP A 1 210 ? 16.09213  21.84305 -13.33651 1.000 34.40755 ? 413  TRP A CE3 1 
ATOM   1643 C  CZ2 . TRP A 1 210 ? 18.85831  21.51832 -13.88249 1.000 42.71890 ? 413  TRP A CZ2 1 
ATOM   1644 C  CZ3 . TRP A 1 210 ? 16.53936  21.04604 -14.38994 1.000 33.90502 ? 413  TRP A CZ3 1 
ATOM   1645 C  CH2 . TRP A 1 210 ? 17.90922  20.89556 -14.65162 1.000 37.59718 ? 413  TRP A CH2 1 
ATOM   1646 N  N   . ALA A 1 211 ? 16.03732  20.68373 -10.17550 1.000 28.05699 ? 414  ALA A N   1 
ATOM   1647 C  CA  . ALA A 1 211 ? 15.81186  19.33252 -10.68536 1.000 28.05976 ? 414  ALA A CA  1 
ATOM   1648 C  C   . ALA A 1 211 ? 15.27287  18.39782 -9.61810  1.000 25.52482 ? 414  ALA A C   1 
ATOM   1649 O  O   . ALA A 1 211 ? 14.49986  17.48448 -9.93769  1.000 24.78828 ? 414  ALA A O   1 
ATOM   1650 C  CB  . ALA A 1 211 ? 17.10155  18.75246 -11.26830 1.000 28.54852 ? 414  ALA A CB  1 
ATOM   1651 N  N   . LYS A 1 212 ? 15.67631  18.58720 -8.35333  1.000 26.74723 ? 415  LYS A N   1 
ATOM   1652 C  CA  . LYS A 1 212 ? 15.10809  17.77104 -7.28798  1.000 27.21791 ? 415  LYS A CA  1 
ATOM   1653 C  C   . LYS A 1 212 ? 13.62302  18.05289 -7.13795  1.000 25.11847 ? 415  LYS A C   1 
ATOM   1654 O  O   . LYS A 1 212 ? 12.81937  17.12463 -7.00307  1.000 23.74992 ? 415  LYS A O   1 
ATOM   1655 C  CB  . LYS A 1 212 ? 15.84446  18.02668 -5.96481  1.000 24.92570 ? 415  LYS A CB  1 
ATOM   1656 C  CG  . LYS A 1 212 ? 17.33717  17.76406 -6.03563  1.000 23.96111 ? 415  LYS A CG  1 
ATOM   1657 C  CD  . LYS A 1 212 ? 17.64604  16.34070 -6.48532  1.000 24.01845 ? 415  LYS A CD  1 
ATOM   1658 C  CE  . LYS A 1 212 ? 19.16076  16.14343 -6.57882  1.000 27.43426 ? 415  LYS A CE  1 
ATOM   1659 N  NZ  . LYS A 1 212 ? 19.57917  14.77000 -7.02198  1.000 29.29583 ? 415  LYS A NZ  1 
ATOM   1660 N  N   . THR A 1 213 ? 13.24616  19.33100 -7.17914  1.000 22.30507 ? 416  THR A N   1 
ATOM   1661 C  CA  . THR A 1 213 ? 11.84005  19.71643 -7.10810  1.000 21.63623 ? 416  THR A CA  1 
ATOM   1662 C  C   . THR A 1 213 ? 11.05376  19.16829 -8.29467  1.000 25.11153 ? 416  THR A C   1 
ATOM   1663 O  O   . THR A 1 213 ? 9.94427   18.64681 -8.13829  1.000 25.21061 ? 416  THR A O   1 
ATOM   1664 C  CB  . THR A 1 213 ? 11.73562  21.24199 -7.07615  1.000 25.19771 ? 416  THR A CB  1 
ATOM   1665 O  OG1 . THR A 1 213 ? 12.44927  21.75518 -5.94179  1.000 25.90885 ? 416  THR A OG1 1 
ATOM   1666 C  CG2 . THR A 1 213 ? 10.27941  21.67623 -7.02408  1.000 24.75948 ? 416  THR A CG2 1 
ATOM   1667 N  N   . ALA A 1 214 ? 11.60269  19.31262 -9.49899  1.000 22.47615 ? 417  ALA A N   1 
ATOM   1668 C  CA  . ALA A 1 214 ? 10.95991  18.73895 -10.67497 1.000 23.06102 ? 417  ALA A CA  1 
ATOM   1669 C  C   . ALA A 1 214 ? 10.79151  17.23206 -10.52399 1.000 21.81988 ? 417  ALA A C   1 
ATOM   1670 O  O   . ALA A 1 214 ? 9.70911   16.69980 -10.79312 1.000 23.83727 ? 417  ALA A O   1 
ATOM   1671 C  CB  . ALA A 1 214 ? 11.76539  19.08269 -11.93131 1.000 23.20512 ? 417  ALA A CB  1 
ATOM   1672 N  N   . SER A 1 215 ? 11.83616  16.53030 -10.05982 1.000 22.81644 ? 418  SER A N   1 
ATOM   1673 C  CA  . SER A 1 215 ? 11.73419  15.07715 -9.89301  1.000 21.59975 ? 418  SER A CA  1 
ATOM   1674 C  C   . SER A 1 215 ? 10.63603  14.71020 -8.89643  1.000 25.23117 ? 418  SER A C   1 
ATOM   1675 O  O   . SER A 1 215 ? 9.83609   13.79987 -9.15100  1.000 23.82392 ? 418  SER A O   1 
ATOM   1676 C  CB  . SER A 1 215 ? 13.06418  14.48226 -9.43150  1.000 21.04547 ? 418  SER A CB  1 
ATOM   1677 O  OG  . SER A 1 215 ? 14.11729  14.70202 -10.33504 1.000 22.15527 ? 418  SER A OG  1 
ATOM   1678 N  N   . ASN A 1 216 ? 10.59450  15.39311 -7.74248  1.000 20.07882 ? 419  ASN A N   1 
ATOM   1679 C  CA  . ASN A 1 216 ? 9.53291   15.11810 -6.77612  1.000 21.05192 ? 419  ASN A CA  1 
ATOM   1680 C  C   . ASN A 1 216 ? 8.16394   15.26112 -7.42212  1.000 22.41779 ? 419  ASN A C   1 
ATOM   1681 O  O   . ASN A 1 216 ? 7.27345   14.43602 -7.20405  1.000 20.52912 ? 419  ASN A O   1 
ATOM   1682 C  CB  . ASN A 1 216 ? 9.61284   16.07042 -5.57130  1.000 21.47390 ? 419  ASN A CB  1 
ATOM   1683 C  CG  . ASN A 1 216 ? 10.81287  15.81998 -4.66313  1.000 24.05833 ? 419  ASN A CG  1 
ATOM   1684 O  OD1 . ASN A 1 216 ? 11.29349  14.69499 -4.51782  1.000 23.83442 ? 419  ASN A OD1 1 
ATOM   1685 N  ND2 . ASN A 1 216 ? 11.28535  16.88780 -4.01782  1.000 20.45362 ? 419  ASN A ND2 1 
ATOM   1686 N  N   . MET A 1 217 ? 7.96549   16.32519 -8.20055  1.000 20.48217 ? 420  MET A N   1 
ATOM   1687 C  CA  . MET A 1 217 ? 6.65998   16.55386 -8.80920  1.000 21.54788 ? 420  MET A CA  1 
ATOM   1688 C  C   . MET A 1 217 ? 6.36140   15.52069 -9.88629  1.000 20.98270 ? 420  MET A C   1 
ATOM   1689 O  O   . MET A 1 217 ? 5.20540   15.11382 -10.05821 1.000 21.88051 ? 420  MET A O   1 
ATOM   1690 C  CB  . MET A 1 217 ? 6.60265   17.97075 -9.38198  1.000 22.14729 ? 420  MET A CB  1 
ATOM   1691 C  CG  . MET A 1 217 ? 6.74228   19.07273 -8.30189  1.000 21.15583 ? 420  MET A CG  1 
ATOM   1692 S  SD  . MET A 1 217 ? 7.18368   20.68470 -8.97072  1.000 26.02063 ? 420  MET A SD  1 
ATOM   1693 C  CE  . MET A 1 217 ? 5.63020   21.24087 -9.60604  1.000 27.42520 ? 420  MET A CE  1 
ATOM   1694 N  N   . LEU A 1 218 ? 7.39060   15.07799 -10.61352 1.000 19.78850 ? 421  LEU A N   1 
ATOM   1695 C  CA  . LEU A 1 218 ? 7.18941   14.06581 -11.64560 1.000 22.16320 ? 421  LEU A CA  1 
ATOM   1696 C  C   . LEU A 1 218 ? 6.91691   12.68795 -11.04338 1.000 22.99049 ? 421  LEU A C   1 
ATOM   1697 O  O   . LEU A 1 218 ? 6.15295   11.90429 -11.61948 1.000 22.68518 ? 421  LEU A O   1 
ATOM   1698 C  CB  . LEU A 1 218 ? 8.40278   14.02418 -12.57921 1.000 19.13356 ? 421  LEU A CB  1 
ATOM   1699 C  CG  . LEU A 1 218 ? 8.49174   15.26188 -13.47536 1.000 21.80466 ? 421  LEU A CG  1 
ATOM   1700 C  CD1 . LEU A 1 218 ? 9.91928   15.54361 -13.95471 1.000 20.19806 ? 421  LEU A CD1 1 
ATOM   1701 C  CD2 . LEU A 1 218 ? 7.52651   15.12582 -14.66165 1.000 19.75010 ? 421  LEU A CD2 1 
ATOM   1702 N  N   . HIS A 1 219 ? 7.55015   12.34983 -9.91115  1.000 22.24276 ? 422  HIS A N   1 
ATOM   1703 C  CA  . HIS A 1 219 ? 7.21211   11.08497 -9.25050  1.000 19.54988 ? 422  HIS A CA  1 
ATOM   1704 C  C   . HIS A 1 219 ? 5.73133   11.04635 -8.93068  1.000 23.24863 ? 422  HIS A C   1 
ATOM   1705 O  O   . HIS A 1 219 ? 5.04468   10.05223 -9.21070  1.000 26.91111 ? 422  HIS A O   1 
ATOM   1706 C  CB  . HIS A 1 219 ? 8.02958   10.87138 -7.96210  1.000 19.90070 ? 422  HIS A CB  1 
ATOM   1707 C  CG  . HIS A 1 219 ? 9.35206   10.18538 -8.17405  1.000 20.73645 ? 422  HIS A CG  1 
ATOM   1708 N  ND1 . HIS A 1 219 ? 9.46129   8.88489  -8.62441  1.000 20.99553 ? 422  HIS A ND1 1 
ATOM   1709 C  CD2 . HIS A 1 219 ? 10.62090  10.61742 -7.97711  1.000 21.76949 ? 422  HIS A CD2 1 
ATOM   1710 C  CE1 . HIS A 1 219 ? 10.73718  8.54595  -8.69596  1.000 17.87623 ? 422  HIS A CE1 1 
ATOM   1711 N  NE2 . HIS A 1 219 ? 11.46332  9.58527  -8.32118  1.000 19.06023 ? 422  HIS A NE2 1 
ATOM   1712 N  N   . TRP A 1 220 ? 5.21766   12.14365 -8.36713  1.000 21.27902 ? 423  TRP A N   1 
ATOM   1713 C  CA  . TRP A 1 220 ? 3.79262   12.25982 -8.07061  1.000 20.52736 ? 423  TRP A CA  1 
ATOM   1714 C  C   . TRP A 1 220 ? 2.95146   12.13311 -9.33554  1.000 18.97701 ? 423  TRP A C   1 
ATOM   1715 O  O   . TRP A 1 220 ? 1.93243   11.43265 -9.34808  1.000 22.08323 ? 423  TRP A O   1 
ATOM   1716 C  CB  . TRP A 1 220 ? 3.53133   13.59836 -7.37159  1.000 18.97328 ? 423  TRP A CB  1 
ATOM   1717 C  CG  . TRP A 1 220 ? 2.08701   14.01423 -7.27821  1.000 20.77733 ? 423  TRP A CG  1 
ATOM   1718 C  CD1 . TRP A 1 220 ? 1.20514   13.71551 -6.26927  1.000 20.56930 ? 423  TRP A CD1 1 
ATOM   1719 C  CD2 . TRP A 1 220 ? 1.35906   14.82209 -8.22049  1.000 19.86484 ? 423  TRP A CD2 1 
ATOM   1720 N  NE1 . TRP A 1 220 ? -0.01695  14.30387 -6.52159  1.000 18.53518 ? 423  TRP A NE1 1 
ATOM   1721 C  CE2 . TRP A 1 220 ? 0.05041   14.98112 -7.71367  1.000 20.30518 ? 423  TRP A CE2 1 
ATOM   1722 C  CE3 . TRP A 1 220 ? 1.69556   15.44037 -9.43509  1.000 22.03373 ? 423  TRP A CE3 1 
ATOM   1723 C  CZ2 . TRP A 1 220 ? -0.93126  15.71253 -8.38895  1.000 24.94375 ? 423  TRP A CZ2 1 
ATOM   1724 C  CZ3 . TRP A 1 220 ? 0.71897   16.16874 -10.10232 1.000 24.27280 ? 423  TRP A CZ3 1 
ATOM   1725 C  CH2 . TRP A 1 220 ? -0.58094  16.29523 -9.57315  1.000 25.25995 ? 423  TRP A CH2 1 
ATOM   1726 N  N   . TRP A 1 221 ? 3.37288   12.79688 -10.40996 1.000 18.60849 ? 424  TRP A N   1 
ATOM   1727 C  CA  . TRP A 1 221 ? 2.62847   12.77294 -11.66965 1.000 19.04640 ? 424  TRP A CA  1 
ATOM   1728 C  C   . TRP A 1 221 ? 2.58704   11.36536 -12.26752 1.000 17.69138 ? 424  TRP A C   1 
ATOM   1729 O  O   . TRP A 1 221 ? 1.52794   10.89547 -12.69340 1.000 19.97194 ? 424  TRP A O   1 
ATOM   1730 C  CB  . TRP A 1 221 ? 3.27609   13.77271 -12.62828 1.000 19.31492 ? 424  TRP A CB  1 
ATOM   1731 C  CG  . TRP A 1 221 ? 2.48183   14.16651 -13.83212 1.000 21.00162 ? 424  TRP A CG  1 
ATOM   1732 C  CD1 . TRP A 1 221 ? 1.57187   15.17764 -13.92536 1.000 21.91258 ? 424  TRP A CD1 1 
ATOM   1733 C  CD2 . TRP A 1 221 ? 2.56633   13.57429 -15.14160 1.000 21.37921 ? 424  TRP A CD2 1 
ATOM   1734 N  NE1 . TRP A 1 221 ? 1.08202   15.25557 -15.22303 1.000 25.84705 ? 424  TRP A NE1 1 
ATOM   1735 C  CE2 . TRP A 1 221 ? 1.66758   14.27510 -15.97975 1.000 21.19927 ? 424  TRP A CE2 1 
ATOM   1736 C  CE3 . TRP A 1 221 ? 3.30471   12.50968 -15.67798 1.000 23.40821 ? 424  TRP A CE3 1 
ATOM   1737 C  CZ2 . TRP A 1 221 ? 1.49423   13.95559 -17.34105 1.000 24.77706 ? 424  TRP A CZ2 1 
ATOM   1738 C  CZ3 . TRP A 1 221 ? 3.12471   12.18193 -17.03097 1.000 28.29093 ? 424  TRP A CZ3 1 
ATOM   1739 C  CH2 . TRP A 1 221 ? 2.22082   12.90742 -17.84240 1.000 24.61261 ? 424  TRP A CH2 1 
ATOM   1740 N  N   . PHE A 1 222 ? 3.72524   10.66642 -12.27490 1.000 20.51724 ? 425  PHE A N   1 
ATOM   1741 C  CA  . PHE A 1 222 ? 3.74777   9.28991  -12.77585 1.000 21.53762 ? 425  PHE A CA  1 
ATOM   1742 C  C   . PHE A 1 222 ? 2.84050   8.39145  -11.95511 1.000 26.12285 ? 425  PHE A C   1 
ATOM   1743 O  O   . PHE A 1 222 ? 2.20209   7.47810  -12.49540 1.000 23.22152 ? 425  PHE A O   1 
ATOM   1744 C  CB  . PHE A 1 222 ? 5.17351   8.73367  -12.77046 1.000 21.27429 ? 425  PHE A CB  1 
ATOM   1745 C  CG  . PHE A 1 222 ? 5.91457   8.95754  -14.05935 1.000 20.24061 ? 425  PHE A CG  1 
ATOM   1746 C  CD1 . PHE A 1 222 ? 6.28077   10.23808 -14.44629 1.000 21.32014 ? 425  PHE A CD1 1 
ATOM   1747 C  CD2 . PHE A 1 222 ? 6.25034   7.88795  -14.87073 1.000 25.44330 ? 425  PHE A CD2 1 
ATOM   1748 C  CE1 . PHE A 1 222 ? 6.94851   10.45287 -15.63565 1.000 25.95569 ? 425  PHE A CE1 1 
ATOM   1749 C  CE2 . PHE A 1 222 ? 6.92742   8.08751  -16.05250 1.000 27.39923 ? 425  PHE A CE2 1 
ATOM   1750 C  CZ  . PHE A 1 222 ? 7.27857   9.37171  -16.43860 1.000 27.08882 ? 425  PHE A CZ  1 
ATOM   1751 N  N   . GLU A 1 223 ? 2.76326   8.64274  -10.64675 1.000 23.27385 ? 426  GLU A N   1 
ATOM   1752 C  CA  . GLU A 1 223 ? 1.92186   7.83274  -9.78467  1.000 18.30111 ? 426  GLU A CA  1 
ATOM   1753 C  C   . GLU A 1 223 ? 0.44994   8.14342  -10.01096 1.000 21.05228 ? 426  GLU A C   1 
ATOM   1754 O  O   . GLU A 1 223 ? -0.37148  7.22579  -10.13447 1.000 26.27923 ? 426  GLU A O   1 
ATOM   1755 C  CB  . GLU A 1 223 ? 2.32371   8.05271  -8.31205  1.000 21.49729 ? 426  GLU A CB  1 
ATOM   1756 C  CG  . GLU A 1 223 ? 1.56453   7.21694  -7.31641  1.000 21.61506 ? 426  GLU A CG  1 
ATOM   1757 C  CD  . GLU A 1 223 ? 1.91184   5.72598  -7.40472  1.000 32.29070 ? 426  GLU A CD  1 
ATOM   1758 O  OE1 . GLU A 1 223 ? 2.96775   5.36776  -7.99103  1.000 28.84223 ? 426  GLU A OE1 1 
ATOM   1759 O  OE2 . GLU A 1 223 ? 1.12355   4.90837  -6.88048  1.000 29.63391 ? 426  GLU A OE2 1 
ATOM   1760 N  N   . GLN A 1 224 ? 0.08710   9.43129  -10.06031 1.000 21.10330 ? 427  GLN A N   1 
ATOM   1761 C  CA  . GLN A 1 224 ? -1.31580  9.78088  -10.27501 1.000 23.76796 ? 427  GLN A CA  1 
ATOM   1762 C  C   . GLN A 1 224 ? -1.79609  9.30429  -11.64706 1.000 29.40217 ? 427  GLN A C   1 
ATOM   1763 O  O   . GLN A 1 224 ? -2.94715  8.87921  -11.79415 1.000 28.69185 ? 427  GLN A O   1 
ATOM   1764 C  CB  . GLN A 1 224 ? -1.53091  11.29243 -10.14755 1.000 22.84293 ? 427  GLN A CB  1 
ATOM   1765 C  CG  . GLN A 1 224 ? -1.09862  11.91600 -8.82007  1.000 24.69012 ? 427  GLN A CG  1 
ATOM   1766 C  CD  . GLN A 1 224 ? -1.46127  11.05555 -7.63062  1.000 30.03391 ? 427  GLN A CD  1 
ATOM   1767 O  OE1 . GLN A 1 224 ? -2.64222  10.84395 -7.32769  1.000 34.76887 ? 427  GLN A OE1 1 
ATOM   1768 N  NE2 . GLN A 1 224 ? -0.43863  10.53508 -6.95152  1.000 34.87587 ? 427  GLN A NE2 1 
ATOM   1769 N  N   . ASN A 1 225 ? -0.92596  9.35568  -12.65837 1.000 22.68433 ? 428  ASN A N   1 
ATOM   1770 C  CA  . ASN A 1 225 ? -1.29380  8.97210  -14.01751 1.000 23.73089 ? 428  ASN A CA  1 
ATOM   1771 C  C   . ASN A 1 225 ? -0.85235  7.56159  -14.36959 1.000 28.96414 ? 428  ASN A C   1 
ATOM   1772 O  O   . ASN A 1 225 ? -0.70768  7.25104  -15.55881 1.000 24.53408 ? 428  ASN A O   1 
ATOM   1773 C  CB  . ASN A 1 225 ? -0.70829  9.95808  -15.02521 1.000 21.83870 ? 428  ASN A CB  1 
ATOM   1774 C  CG  . ASN A 1 225 ? -1.47727  11.23172 -15.07266 1.000 25.04703 ? 428  ASN A CG  1 
ATOM   1775 O  OD1 . ASN A 1 225 ? -2.69690  11.21782 -14.91379 1.000 29.35408 ? 428  ASN A OD1 1 
ATOM   1776 N  ND2 . ASN A 1 225 ? -0.77773  12.35830 -15.26133 1.000 23.18244 ? 428  ASN A ND2 1 
ATOM   1777 N  N   . LYS A 1 226 ? -0.64375  6.70611  -13.35935 1.000 26.59048 ? 429  LYS A N   1 
ATOM   1778 C  CA  . LYS A 1 226 ? -0.09465  5.37075  -13.58923 1.000 27.12988 ? 429  LYS A CA  1 
ATOM   1779 C  C   . LYS A 1 226 ? -0.85879  4.60041  -14.66994 1.000 27.46423 ? 429  LYS A C   1 
ATOM   1780 O  O   . LYS A 1 226 ? -0.24648  3.96574  -15.53875 1.000 28.74767 ? 429  LYS A O   1 
ATOM   1781 C  CB  . LYS A 1 226 ? -0.09488  4.59274  -12.27212 1.000 28.53859 ? 429  LYS A CB  1 
ATOM   1782 C  CG  . LYS A 1 226 ? 0.46898   3.19383  -12.36435 1.000 33.28018 ? 429  LYS A CG  1 
ATOM   1783 N  N   . ASP A 1 227 ? -2.19293  4.64649  -14.63724 1.000 27.15360 ? 430  ASP A N   1 
ATOM   1784 C  CA  . ASP A 1 227 ? -2.97500  3.86169  -15.59051 1.000 31.21776 ? 430  ASP A CA  1 
ATOM   1785 C  C   . ASP A 1 227 ? -2.89409  4.43523  -17.00264 1.000 30.71582 ? 430  ASP A C   1 
ATOM   1786 O  O   . ASP A 1 227 ? -2.75446  3.67695  -17.96984 1.000 26.79627 ? 430  ASP A O   1 
ATOM   1787 C  CB  . ASP A 1 227 ? -4.42526  3.77166  -15.13727 1.000 31.69820 ? 430  ASP A CB  1 
ATOM   1788 C  CG  . ASP A 1 227 ? -4.58790  2.91487  -13.90467 1.000 45.14160 ? 430  ASP A CG  1 
ATOM   1789 O  OD1 . ASP A 1 227 ? -3.66571  2.11846  -13.60945 1.000 41.49708 ? 430  ASP A OD1 1 
ATOM   1790 O  OD2 . ASP A 1 227 ? -5.63916  3.03227  -13.23752 1.000 46.91029 ? 430  ASP A OD2 1 
ATOM   1791 N  N   . TYR A 1 228 ? -3.02666  5.76066  -17.14938 1.000 26.91566 ? 431  TYR A N   1 
ATOM   1792 C  CA  . TYR A 1 228 ? -2.79694  6.37382  -18.45541 1.000 31.05563 ? 431  TYR A CA  1 
ATOM   1793 C  C   . TYR A 1 228 ? -1.41975  6.01038  -18.99234 1.000 29.43733 ? 431  TYR A C   1 
ATOM   1794 O  O   . TYR A 1 228 ? -1.27997  5.64475  -20.16490 1.000 27.80670 ? 431  TYR A O   1 
ATOM   1795 C  CB  . TYR A 1 228 ? -2.94374  7.89462  -18.37825 1.000 29.32734 ? 431  TYR A CB  1 
ATOM   1796 C  CG  . TYR A 1 228 ? -4.36918  8.36167  -18.25542 1.000 31.63864 ? 431  TYR A CG  1 
ATOM   1797 C  CD1 . TYR A 1 228 ? -5.34547  7.95275  -19.15981 1.000 37.33655 ? 431  TYR A CD1 1 
ATOM   1798 C  CD2 . TYR A 1 228 ? -4.74393  9.20795  -17.22379 1.000 33.77370 ? 431  TYR A CD2 1 
ATOM   1799 C  CE1 . TYR A 1 228 ? -6.66110  8.38899  -19.03128 1.000 38.06121 ? 431  TYR A CE1 1 
ATOM   1800 C  CE2 . TYR A 1 228 ? -6.04027  9.64092  -17.09075 1.000 38.22839 ? 431  TYR A CE2 1 
ATOM   1801 C  CZ  . TYR A 1 228 ? -6.99100  9.23816  -17.98825 1.000 41.06088 ? 431  TYR A CZ  1 
ATOM   1802 O  OH  . TYR A 1 228 ? -8.27479  9.70074  -17.81743 1.000 53.15404 ? 431  TYR A OH  1 
ATOM   1803 N  N   . ILE A 1 229 ? -0.39330  6.07279  -18.14225 1.000 23.46365 ? 432  ILE A N   1 
ATOM   1804 C  CA  . ILE A 1 229 ? 0.95630   5.78816  -18.61768 1.000 21.62450 ? 432  ILE A CA  1 
ATOM   1805 C  C   . ILE A 1 229 ? 1.07214   4.32579  -19.03330 1.000 29.00446 ? 432  ILE A C   1 
ATOM   1806 O  O   . ILE A 1 229 ? 1.74689   4.00275  -20.01711 1.000 28.11430 ? 432  ILE A O   1 
ATOM   1807 C  CB  . ILE A 1 229 ? 1.99566   6.19676  -17.55001 1.000 24.31308 ? 432  ILE A CB  1 
ATOM   1808 C  CG1 . ILE A 1 229 ? 1.97044   7.72297  -17.34949 1.000 24.75569 ? 432  ILE A CG1 1 
ATOM   1809 C  CG2 . ILE A 1 229 ? 3.39271   5.74985  -17.94284 1.000 22.67197 ? 432  ILE A CG2 1 
ATOM   1810 C  CD1 . ILE A 1 229 ? 2.81377   8.22607  -16.14678 1.000 21.47639 ? 432  ILE A CD1 1 
ATOM   1811 N  N   . GLU A 1 230 ? 0.37561   3.42184  -18.33574 1.000 28.63947 ? 433  GLU A N   1 
ATOM   1812 C  CA  . GLU A 1 230 ? 0.36982   2.02181  -18.76877 1.000 27.99761 ? 433  GLU A CA  1 
ATOM   1813 C  C   . GLU A 1 230 ? -0.26078  1.86554  -20.15375 1.000 31.59838 ? 433  GLU A C   1 
ATOM   1814 O  O   . GLU A 1 230 ? 0.23791   1.10202  -20.99092 1.000 26.13739 ? 433  GLU A O   1 
ATOM   1815 C  CB  . GLU A 1 230 ? -0.36911  1.15337  -17.75109 1.000 30.76236 ? 433  GLU A CB  1 
ATOM   1816 C  CG  . GLU A 1 230 ? -0.31203  -0.33544 -18.06627 1.000 38.34426 ? 433  GLU A CG  1 
ATOM   1817 C  CD  . GLU A 1 230 ? 1.11893   -0.85683 -18.14328 1.000 46.96249 ? 433  GLU A CD  1 
ATOM   1818 O  OE1 . GLU A 1 230 ? 1.93668   -0.44561 -17.28458 1.000 51.29349 ? 433  GLU A OE1 1 
ATOM   1819 O  OE2 . GLU A 1 230 ? 1.42762   -1.65198 -19.07303 1.000 51.90042 ? 433  GLU A OE2 1 
ATOM   1820 N  N   A GLN A 1 231 ? -1.36914  2.56577  -20.40881 0.574 28.59113 ? 434  GLN A N   1 
ATOM   1821 N  N   B GLN A 1 231 ? -1.36637  2.56960  -20.40802 0.426 29.00972 ? 434  GLN A N   1 
ATOM   1822 C  CA  A GLN A 1 231 ? -1.96711  2.51103  -21.73632 0.574 30.21601 ? 434  GLN A CA  1 
ATOM   1823 C  CA  B GLN A 1 231 ? -1.96914  2.52148  -21.73373 0.426 30.25920 ? 434  GLN A CA  1 
ATOM   1824 C  C   A GLN A 1 231 ? -1.05876  3.14210  -22.78722 0.574 29.64175 ? 434  GLN A C   1 
ATOM   1825 C  C   B GLN A 1 231 ? -1.05831  3.14312  -22.78577 0.426 29.68086 ? 434  GLN A C   1 
ATOM   1826 O  O   A GLN A 1 231 ? -1.06156  2.70677  -23.94475 0.574 31.77543 ? 434  GLN A O   1 
ATOM   1827 O  O   B GLN A 1 231 ? -1.06193  2.70461  -23.94188 0.426 31.36250 ? 434  GLN A O   1 
ATOM   1828 C  CB  A GLN A 1 231 ? -3.33335  3.19239  -21.72329 0.574 32.31185 ? 434  GLN A CB  1 
ATOM   1829 C  CB  B GLN A 1 231 ? -3.32686  3.21999  -21.71548 0.426 32.33028 ? 434  GLN A CB  1 
ATOM   1830 C  CG  A GLN A 1 231 ? -4.36280  2.49582  -20.84993 0.574 31.59928 ? 434  GLN A CG  1 
ATOM   1831 C  CG  B GLN A 1 231 ? -4.34644  2.54196  -20.82040 0.426 31.65136 ? 434  GLN A CG  1 
ATOM   1832 C  CD  A GLN A 1 231 ? -5.70971  3.19232  -20.87247 0.574 32.30800 ? 434  GLN A CD  1 
ATOM   1833 C  CD  B GLN A 1 231 ? -4.56396  1.09295  -21.19549 0.426 34.43871 ? 434  GLN A CD  1 
ATOM   1834 O  OE1 A GLN A 1 231 ? -6.53429  2.94038  -21.74547 0.574 40.14916 ? 434  GLN A OE1 1 
ATOM   1835 O  OE1 B GLN A 1 231 ? -5.01521  0.78859  -22.29905 0.426 35.66014 ? 434  GLN A OE1 1 
ATOM   1836 N  NE2 A GLN A 1 231 ? -5.93701  4.07777  -19.90898 0.574 39.72014 ? 434  GLN A NE2 1 
ATOM   1837 N  NE2 B GLN A 1 231 ? -4.22745  0.18557  -20.28231 0.426 39.77765 ? 434  GLN A NE2 1 
ATOM   1838 N  N   . TYR A 1 232 ? -0.26582  4.14927  -22.40760 1.000 22.16618 ? 435  TYR A N   1 
ATOM   1839 C  CA  . TYR A 1 232 ? 0.66063   4.75986  -23.35940 1.000 26.77378 ? 435  TYR A CA  1 
ATOM   1840 C  C   . TYR A 1 232 ? 1.72444   3.75751  -23.79374 1.000 30.16996 ? 435  TYR A C   1 
ATOM   1841 O  O   . TYR A 1 232 ? 1.97464   3.58235  -24.99128 1.000 28.77930 ? 435  TYR A O   1 
ATOM   1842 C  CB  . TYR A 1 232 ? 1.30068   6.02084  -22.75784 1.000 23.35253 ? 435  TYR A CB  1 
ATOM   1843 C  CG  . TYR A 1 232 ? 2.05601   6.87396  -23.76340 1.000 22.07607 ? 435  TYR A CG  1 
ATOM   1844 C  CD1 . TYR A 1 232 ? 1.38993   7.79795  -24.56577 1.000 27.35738 ? 435  TYR A CD1 1 
ATOM   1845 C  CD2 . TYR A 1 232 ? 3.42572   6.73920  -23.92620 1.000 25.30313 ? 435  TYR A CD2 1 
ATOM   1846 C  CE1 . TYR A 1 232 ? 2.07134   8.57916  -25.48708 1.000 28.77812 ? 435  TYR A CE1 1 
ATOM   1847 C  CE2 . TYR A 1 232 ? 4.12177   7.50838  -24.86184 1.000 27.96405 ? 435  TYR A CE2 1 
ATOM   1848 C  CZ  . TYR A 1 232 ? 3.43784   8.43131  -25.62860 1.000 26.86221 ? 435  TYR A CZ  1 
ATOM   1849 O  OH  . TYR A 1 232 ? 4.12633   9.18952  -26.54651 1.000 31.97335 ? 435  TYR A OH  1 
ATOM   1850 N  N   . LYS A 1 233 ? 2.33991   3.06670  -22.82902 1.000 29.32722 ? 436  LYS A N   1 
ATOM   1851 C  CA  . LYS A 1 233 ? 3.30981   2.01789  -23.14245 1.000 31.27866 ? 436  LYS A CA  1 
ATOM   1852 C  C   . LYS A 1 233 ? 2.70182   0.90038  -23.98952 1.000 30.11685 ? 436  LYS A C   1 
ATOM   1853 O  O   . LYS A 1 233 ? 3.40502   0.28554  -24.79667 1.000 31.93755 ? 436  LYS A O   1 
ATOM   1854 C  CB  . LYS A 1 233 ? 3.88122   1.43427  -21.84728 1.000 30.90376 ? 436  LYS A CB  1 
ATOM   1855 C  CG  . LYS A 1 233 ? 4.63236   2.45325  -20.98362 1.000 31.10235 ? 436  LYS A CG  1 
ATOM   1856 C  CD  . LYS A 1 233 ? 4.67881   2.01504  -19.52543 1.000 36.39514 ? 436  LYS A CD  1 
ATOM   1857 C  CE  . LYS A 1 233 ? 5.43764   0.70636  -19.36265 1.000 35.55385 ? 436  LYS A CE  1 
ATOM   1858 N  NZ  . LYS A 1 233 ? 5.34568   0.20182  -17.96683 1.000 57.22212 ? 436  LYS A NZ  1 
ATOM   1859 N  N   . GLN A 1 234 ? 1.40964   0.61559  -23.82656 1.000 26.66071 ? 437  GLN A N   1 
ATOM   1860 C  CA  . GLN A 1 234 ? 0.79566   -0.40601 -24.67061 1.000 35.00476 ? 437  GLN A CA  1 
ATOM   1861 C  C   . GLN A 1 234 ? 0.36473   0.11735  -26.03970 1.000 38.59122 ? 437  GLN A C   1 
ATOM   1862 O  O   . GLN A 1 234 ? 0.26218   -0.66888 -26.98758 1.000 36.99478 ? 437  GLN A O   1 
ATOM   1863 C  CB  . GLN A 1 234 ? -0.40935  -1.02167 -23.96476 1.000 32.55845 ? 437  GLN A CB  1 
ATOM   1864 C  CG  . GLN A 1 234 ? -0.01933  -1.86900 -22.78092 1.000 45.49804 ? 437  GLN A CG  1 
ATOM   1865 C  CD  . GLN A 1 234 ? -1.20921  -2.34452 -21.98319 1.000 55.85217 ? 437  GLN A CD  1 
ATOM   1866 O  OE1 . GLN A 1 234 ? -2.28820  -1.74413 -22.02317 1.000 51.50512 ? 437  GLN A OE1 1 
ATOM   1867 N  NE2 . GLN A 1 234 ? -1.01834  -3.42685 -21.24010 1.000 65.24685 ? 437  GLN A NE2 1 
ATOM   1868 N  N   . LYS A 1 235 ? 0.09007   1.41119  -26.17844 1.000 29.71382 ? 438  LYS A N   1 
ATOM   1869 C  CA  . LYS A 1 235 ? -0.52870  1.89736  -27.40417 1.000 28.98106 ? 438  LYS A CA  1 
ATOM   1870 C  C   . LYS A 1 235 ? 0.37291   2.76257  -28.26930 1.000 35.64596 ? 438  LYS A C   1 
ATOM   1871 O  O   . LYS A 1 235 ? 0.24993   2.71914  -29.49656 1.000 37.20193 ? 438  LYS A O   1 
ATOM   1872 C  CB  . LYS A 1 235 ? -1.80639  2.67721  -27.08121 1.000 34.79188 ? 438  LYS A CB  1 
ATOM   1873 C  CG  . LYS A 1 235 ? -2.92337  1.80443  -26.54357 1.000 36.66352 ? 438  LYS A CG  1 
ATOM   1874 C  CD  . LYS A 1 235 ? -4.20932  2.58556  -26.33375 1.000 40.00316 ? 438  LYS A CD  1 
ATOM   1875 C  CE  . LYS A 1 235 ? -5.18234  1.84079  -25.42267 1.000 42.50460 ? 438  LYS A CE  1 
ATOM   1876 N  NZ  . LYS A 1 235 ? -5.75625  0.63093  -26.06094 1.000 48.15387 ? 438  LYS A NZ  1 
ATOM   1877 N  N   . ALA A 1 236 ? 1.26761   3.53878  -27.67647 1.000 29.37637 ? 439  ALA A N   1 
ATOM   1878 C  CA  . ALA A 1 236 ? 2.12453   4.43738  -28.43722 1.000 29.52223 ? 439  ALA A CA  1 
ATOM   1879 C  C   . ALA A 1 236 ? 3.28196   3.67711  -29.07602 1.000 25.75601 ? 439  ALA A C   1 
ATOM   1880 O  O   . ALA A 1 236 ? 3.65720   2.58583  -28.64249 1.000 28.59732 ? 439  ALA A O   1 
ATOM   1881 C  CB  . ALA A 1 236 ? 2.67396   5.54264  -27.53339 1.000 28.57874 ? 439  ALA A CB  1 
ATOM   1882 N  N   . ALA A 1 237 ? 3.85357   4.27377  -30.12144 1.000 27.68073 ? 440  ALA A N   1 
ATOM   1883 C  CA  . ALA A 1 237 ? 5.03713   3.72088  -30.78497 1.000 28.71911 ? 440  ALA A CA  1 
ATOM   1884 C  C   . ALA A 1 237 ? 6.24592   4.32096  -30.08576 1.000 29.90067 ? 440  ALA A C   1 
ATOM   1885 O  O   . ALA A 1 237 ? 6.76180   5.36519  -30.48246 1.000 30.76764 ? 440  ALA A O   1 
ATOM   1886 C  CB  . ALA A 1 237 ? 5.04248   4.03077  -32.28225 1.000 28.14621 ? 440  ALA A CB  1 
ATOM   1887 N  N   . ILE A 1 238 ? 6.70861   3.63622  -29.04120 1.000 27.40415 ? 441  ILE A N   1 
ATOM   1888 C  CA  . ILE A 1 238 ? 7.73376   4.17774  -28.15496 1.000 26.04857 ? 441  ILE A CA  1 
ATOM   1889 C  C   . ILE A 1 238 ? 9.08136   4.16861  -28.85424 1.000 25.02048 ? 441  ILE A C   1 
ATOM   1890 O  O   . ILE A 1 238 ? 9.48487   3.15743  -29.44487 1.000 27.38250 ? 441  ILE A O   1 
ATOM   1891 C  CB  . ILE A 1 238 ? 7.80092   3.36496  -26.85395 1.000 26.17848 ? 441  ILE A CB  1 
ATOM   1892 C  CG1 . ILE A 1 238 ? 6.41139   3.22956  -26.23719 1.000 25.91247 ? 441  ILE A CG1 1 
ATOM   1893 C  CG2 . ILE A 1 238 ? 8.76377   4.02733  -25.87357 1.000 28.67709 ? 441  ILE A CG2 1 
ATOM   1894 C  CD1 . ILE A 1 238 ? 5.98633   4.42167  -25.45832 1.000 26.17929 ? 441  ILE A CD1 1 
ATOM   1895 N  N   . GLU A 1 239 ? 9.79526   5.28926  -28.77063 1.000 27.60498 ? 442  GLU A N   1 
ATOM   1896 C  CA  . GLU A 1 239 ? 11.13265  5.36979  -29.33852 1.000 25.80320 ? 442  GLU A CA  1 
ATOM   1897 C  C   . GLU A 1 239 ? 12.08569  4.47748  -28.55030 1.000 28.16943 ? 442  GLU A C   1 
ATOM   1898 O  O   . GLU A 1 239 ? 12.07640  4.48713  -27.31381 1.000 29.34764 ? 442  GLU A O   1 
ATOM   1899 C  CB  . GLU A 1 239 ? 11.61100  6.80877  -29.33309 1.000 29.44127 ? 442  GLU A CB  1 
ATOM   1900 C  CG  . GLU A 1 239 ? 12.87676  7.02533  -30.11071 1.000 31.80015 ? 442  GLU A CG  1 
ATOM   1901 C  CD  . GLU A 1 239 ? 13.20684  8.50795  -30.27727 1.000 40.50318 ? 442  GLU A CD  1 
ATOM   1902 O  OE1 . GLU A 1 239 ? 12.38756  9.35134  -29.84844 1.000 39.18154 ? 442  GLU A OE1 1 
ATOM   1903 O  OE2 . GLU A 1 239 ? 14.28692  8.82060  -30.82686 1.000 40.80126 ? 442  GLU A OE2 1 
ATOM   1904 N  N   . GLU A 1 240 ? 12.90412  3.70313  -29.27178 1.000 28.42970 ? 443  GLU A N   1 
ATOM   1905 C  CA  . GLU A 1 240 ? 13.60502  2.57990  -28.65501 1.000 26.30598 ? 443  GLU A CA  1 
ATOM   1906 C  C   . GLU A 1 240 ? 14.42257  3.02236  -27.44587 1.000 37.59570 ? 443  GLU A C   1 
ATOM   1907 O  O   . GLU A 1 240 ? 14.31797  2.43149  -26.36666 1.000 32.45291 ? 443  GLU A O   1 
ATOM   1908 C  CB  . GLU A 1 240 ? 14.50531  1.88086  -29.66686 1.000 29.30625 ? 443  GLU A CB  1 
ATOM   1909 C  CG  . GLU A 1 240 ? 15.26348  0.71608  -29.03625 1.000 33.76359 ? 443  GLU A CG  1 
ATOM   1910 C  CD  . GLU A 1 240 ? 16.24490  0.04944  -29.97754 1.000 40.29258 ? 443  GLU A CD  1 
ATOM   1911 O  OE1 . GLU A 1 240 ? 15.80375  -0.54521 -30.98026 1.000 40.14256 ? 443  GLU A OE1 1 
ATOM   1912 O  OE2 . GLU A 1 240 ? 17.46335  0.11679  -29.71066 1.000 46.68007 ? 443  GLU A OE2 1 
ATOM   1913 N  N   . TRP A 1 241 ? 15.22397  4.07679  -27.59366 1.000 34.30800 ? 444  TRP A N   1 
ATOM   1914 C  CA  . TRP A 1 241 ? 16.09736  4.44805  -26.48654 1.000 34.99345 ? 444  TRP A CA  1 
ATOM   1915 C  C   . TRP A 1 241 ? 15.32177  4.90358  -25.25622 1.000 33.55667 ? 444  TRP A C   1 
ATOM   1916 O  O   . TRP A 1 241 ? 15.84270  4.79555  -24.13920 1.000 36.29750 ? 444  TRP A O   1 
ATOM   1917 C  CB  . TRP A 1 241 ? 17.11035  5.51584  -26.94099 1.000 34.43291 ? 444  TRP A CB  1 
ATOM   1918 C  CG  . TRP A 1 241 ? 16.60684  6.93777  -27.08494 1.000 32.01416 ? 444  TRP A CG  1 
ATOM   1919 C  CD1 . TRP A 1 241 ? 16.24077  7.55029  -28.24096 1.000 36.43300 ? 444  TRP A CD1 1 
ATOM   1920 C  CD2 . TRP A 1 241 ? 16.46872  7.92403  -26.04768 1.000 31.73889 ? 444  TRP A CD2 1 
ATOM   1921 N  NE1 . TRP A 1 241 ? 15.86354  8.84843  -27.99416 1.000 39.26168 ? 444  TRP A NE1 1 
ATOM   1922 C  CE2 . TRP A 1 241 ? 16.00098  9.10884  -26.65851 1.000 31.93535 ? 444  TRP A CE2 1 
ATOM   1923 C  CE3 . TRP A 1 241 ? 16.68613  7.91929  -24.66316 1.000 34.02623 ? 444  TRP A CE3 1 
ATOM   1924 C  CZ2 . TRP A 1 241 ? 15.74463  10.28030 -25.93861 1.000 31.91022 ? 444  TRP A CZ2 1 
ATOM   1925 C  CZ3 . TRP A 1 241 ? 16.42977  9.08898  -23.94233 1.000 36.43825 ? 444  TRP A CZ3 1 
ATOM   1926 C  CH2 . TRP A 1 241 ? 15.95541  10.25067 -24.58506 1.000 34.52478 ? 444  TRP A CH2 1 
ATOM   1927 N  N   . LYS A 1 242 ? 14.07878  5.36275  -25.41790 1.000 27.79813 ? 445  LYS A N   1 
ATOM   1928 C  CA  . LYS A 1 242 ? 13.31830  5.87571  -24.28320 1.000 30.88496 ? 445  LYS A CA  1 
ATOM   1929 C  C   . LYS A 1 242 ? 12.59810  4.79385  -23.49001 1.000 30.88687 ? 445  LYS A C   1 
ATOM   1930 O  O   . LYS A 1 242 ? 12.06734  5.09790  -22.41502 1.000 29.74197 ? 445  LYS A O   1 
ATOM   1931 C  CB  . LYS A 1 242 ? 12.27832  6.90812  -24.74733 1.000 32.52346 ? 445  LYS A CB  1 
ATOM   1932 C  CG  . LYS A 1 242 ? 12.85283  8.12891  -25.46751 1.000 34.02995 ? 445  LYS A CG  1 
ATOM   1933 C  CD  . LYS A 1 242 ? 11.76051  9.10736  -25.87558 1.000 27.74399 ? 445  LYS A CD  1 
ATOM   1934 C  CE  . LYS A 1 242 ? 12.33682  10.27341 -26.67894 1.000 32.89738 ? 445  LYS A CE  1 
ATOM   1935 N  NZ  . LYS A 1 242 ? 11.30660  11.31835 -26.90588 1.000 30.44482 ? 445  LYS A NZ  1 
ATOM   1936 N  N   . ARG A 1 243 ? 12.54971  3.55878  -23.98391 1.000 28.39987 ? 446  ARG A N   1 
ATOM   1937 C  CA  . ARG A 1 243 ? 11.73313  2.53414  -23.33490 1.000 29.11432 ? 446  ARG A CA  1 
ATOM   1938 C  C   . ARG A 1 243 ? 11.97748  2.39973  -21.82752 1.000 31.97726 ? 446  ARG A C   1 
ATOM   1939 O  O   . ARG A 1 243 ? 10.98710  2.27354  -21.09034 1.000 29.43396 ? 446  ARG A O   1 
ATOM   1940 C  CB  . ARG A 1 243 ? 11.92236  1.18093  -24.04225 1.000 26.25141 ? 446  ARG A CB  1 
ATOM   1941 C  CG  . ARG A 1 243 ? 11.39004  1.13547  -25.49596 1.000 28.82573 ? 446  ARG A CG  1 
ATOM   1942 C  CD  . ARG A 1 243 ? 11.51351  -0.25317 -26.13992 1.000 28.64782 ? 446  ARG A CD  1 
ATOM   1943 N  NE  . ARG A 1 243 ? 10.75736  -1.25102 -25.39210 1.000 33.42858 ? 446  ARG A NE  1 
ATOM   1944 C  CZ  . ARG A 1 243 ? 9.44869   -1.43919 -25.49086 1.000 30.81108 ? 446  ARG A CZ  1 
ATOM   1945 N  NH1 . ARG A 1 243 ? 8.72194   -0.78528 -26.37961 1.000 27.98712 ? 446  ARG A NH1 1 
ATOM   1946 N  NH2 . ARG A 1 243 ? 8.85359   -2.30203 -24.66979 1.000 31.44802 ? 446  ARG A NH2 1 
ATOM   1947 N  N   . PRO A 1 244 ? 13.21049  2.42494  -21.30188 1.000 31.34671 ? 447  PRO A N   1 
ATOM   1948 C  CA  . PRO A 1 244 ? 13.38180  2.28484  -19.84198 1.000 36.48480 ? 447  PRO A CA  1 
ATOM   1949 C  C   . PRO A 1 244 ? 12.83740  3.45055  -19.02199 1.000 38.24818 ? 447  PRO A C   1 
ATOM   1950 O  O   . PRO A 1 244 ? 12.69314  3.29941  -17.80126 1.000 34.40857 ? 447  PRO A O   1 
ATOM   1951 C  CB  . PRO A 1 244 ? 14.90219  2.17167  -19.67016 1.000 35.65417 ? 447  PRO A CB  1 
ATOM   1952 C  CG  . PRO A 1 244 ? 15.41333  1.76659  -21.00429 1.000 36.77138 ? 447  PRO A CG  1 
ATOM   1953 C  CD  . PRO A 1 244 ? 14.51086  2.40526  -21.99420 1.000 33.91566 ? 447  PRO A CD  1 
ATOM   1954 N  N   . LEU A 1 245 ? 12.52140  4.59109  -19.63098 1.000 31.27642 ? 448  LEU A N   1 
ATOM   1955 C  CA  . LEU A 1 245 ? 12.12125  5.76827  -18.86991 1.000 30.25615 ? 448  LEU A CA  1 
ATOM   1956 C  C   . LEU A 1 245 ? 10.63357  5.81702  -18.54979 1.000 31.54213 ? 448  LEU A C   1 
ATOM   1957 O  O   . LEU A 1 245 ? 10.18913  6.79279  -17.93195 1.000 30.25028 ? 448  LEU A O   1 
ATOM   1958 C  CB  . LEU A 1 245 ? 12.50719  7.05104  -19.61894 1.000 27.41729 ? 448  LEU A CB  1 
ATOM   1959 C  CG  . LEU A 1 245 ? 13.98328  7.46244  -19.65460 1.000 36.31003 ? 448  LEU A CG  1 
ATOM   1960 C  CD1 . LEU A 1 245 ? 14.78463  6.58964  -20.59041 1.000 44.32729 ? 448  LEU A CD1 1 
ATOM   1961 C  CD2 . LEU A 1 245 ? 14.12595  8.91713  -20.06626 1.000 39.33478 ? 448  LEU A CD2 1 
ATOM   1962 N  N   . TYR A 1 246 ? 9.85127   4.81814  -18.94931 1.000 23.82071 ? 449  TYR A N   1 
ATOM   1963 C  CA  . TYR A 1 246 ? 8.39666   4.89810  -18.80165 1.000 26.65856 ? 449  TYR A CA  1 
ATOM   1964 C  C   . TYR A 1 246 ? 7.93271   4.18642  -17.53509 1.000 33.51000 ? 449  TYR A C   1 
ATOM   1965 O  O   . TYR A 1 246 ? 7.05501   3.32069  -17.54007 1.000 35.64702 ? 449  TYR A O   1 
ATOM   1966 C  CB  . TYR A 1 246 ? 7.70319   4.34361  -20.04469 1.000 25.23694 ? 449  TYR A CB  1 
ATOM   1967 C  CG  . TYR A 1 246 ? 7.73055   5.32200  -21.20583 1.000 27.19914 ? 449  TYR A CG  1 
ATOM   1968 C  CD1 . TYR A 1 246 ? 6.74543   6.30029  -21.34081 1.000 22.20729 ? 449  TYR A CD1 1 
ATOM   1969 C  CD2 . TYR A 1 246 ? 8.75844   5.29614  -22.13131 1.000 25.33724 ? 449  TYR A CD2 1 
ATOM   1970 C  CE1 . TYR A 1 246 ? 6.76610   7.20708  -22.39374 1.000 25.98846 ? 449  TYR A CE1 1 
ATOM   1971 C  CE2 . TYR A 1 246 ? 8.80020   6.21113  -23.19604 1.000 25.43393 ? 449  TYR A CE2 1 
ATOM   1972 C  CZ  . TYR A 1 246 ? 7.79991   7.16144  -23.31115 1.000 25.27474 ? 449  TYR A CZ  1 
ATOM   1973 O  OH  . TYR A 1 246 ? 7.83591   8.06620  -24.34038 1.000 28.38447 ? 449  TYR A OH  1 
ATOM   1974 N  N   . LYS A 1 247 ? 8.53568   4.58166  -16.42486 1.000 31.11272 ? 450  LYS A N   1 
ATOM   1975 C  CA  . LYS A 1 247 ? 8.20519   4.06322  -15.10841 1.000 30.61495 ? 450  LYS A CA  1 
ATOM   1976 C  C   . LYS A 1 247 ? 8.80283   5.03184  -14.09549 1.000 29.14329 ? 450  LYS A C   1 
ATOM   1977 O  O   . LYS A 1 247 ? 9.61851   5.88851  -14.43692 1.000 24.36785 ? 450  LYS A O   1 
ATOM   1978 C  CB  . LYS A 1 247 ? 8.75782   2.64616  -14.91832 1.000 30.46784 ? 450  LYS A CB  1 
ATOM   1979 C  CG  . LYS A 1 247 ? 10.27602  2.59759  -15.07847 1.000 38.37622 ? 450  LYS A CG  1 
ATOM   1980 C  CD  . LYS A 1 247 ? 10.84110  1.19281  -14.90382 1.000 42.48725 ? 450  LYS A CD  1 
ATOM   1981 C  CE  . LYS A 1 247 ? 12.35440  1.23374  -14.96688 1.000 43.57528 ? 450  LYS A CE  1 
ATOM   1982 N  NZ  . LYS A 1 247 ? 12.96442  -0.09786 -14.73204 1.000 58.58275 ? 450  LYS A NZ  1 
ATOM   1983 N  N   . HIS A 1 248 ? 8.40781   4.88556  -12.83871 1.000 25.10430 ? 451  HIS A N   1 
ATOM   1984 C  CA  . HIS A 1 248 ? 9.10291   5.63328  -11.80679 1.000 30.81642 ? 451  HIS A CA  1 
ATOM   1985 C  C   . HIS A 1 248 ? 9.35438   4.70550  -10.63478 1.000 28.58172 ? 451  HIS A C   1 
ATOM   1986 O  O   . HIS A 1 248 ? 8.47694   3.92558  -10.26005 1.000 29.89343 ? 451  HIS A O   1 
ATOM   1987 C  CB  . HIS A 1 248 ? 8.32356   6.89831  -11.39975 1.000 22.88764 ? 451  HIS A CB  1 
ATOM   1988 C  CG  . HIS A 1 248 ? 7.20213   6.66724  -10.43030 1.000 29.24953 ? 451  HIS A CG  1 
ATOM   1989 N  ND1 . HIS A 1 248 ? 7.17357   7.25530  -9.18176  1.000 24.43000 ? 451  HIS A ND1 1 
ATOM   1990 C  CD2 . HIS A 1 248 ? 6.05565   5.95214  -10.53564 1.000 26.74497 ? 451  HIS A CD2 1 
ATOM   1991 C  CE1 . HIS A 1 248 ? 6.06227   6.90531  -8.55709  1.000 27.93101 ? 451  HIS A CE1 1 
ATOM   1992 N  NE2 . HIS A 1 248 ? 5.37031   6.10938  -9.35324  1.000 25.94433 ? 451  HIS A NE2 1 
ATOM   1993 N  N   . ASP A 1 249 ? 10.56950  4.75641  -10.10610 1.000 25.72037 ? 452  ASP A N   1 
ATOM   1994 C  CA  . ASP A 1 249 ? 10.97236  3.96256  -8.95121  1.000 24.87282 ? 452  ASP A CA  1 
ATOM   1995 C  C   . ASP A 1 249 ? 11.47800  4.91768  -7.88095  1.000 26.80564 ? 452  ASP A C   1 
ATOM   1996 O  O   . ASP A 1 249 ? 12.40061  5.69927  -8.13067  1.000 26.14102 ? 452  ASP A O   1 
ATOM   1997 C  CB  . ASP A 1 249 ? 12.06085  2.95658  -9.31752  1.000 30.09030 ? 452  ASP A CB  1 
ATOM   1998 C  CG  . ASP A 1 249 ? 11.58700  1.90737  -10.33932 1.000 43.56103 ? 452  ASP A CG  1 
ATOM   1999 O  OD1 . ASP A 1 249 ? 10.47132  1.36195  -10.18361 1.000 38.89265 ? 452  ASP A OD1 1 
ATOM   2000 O  OD2 . ASP A 1 249 ? 12.33497  1.63028  -11.30497 1.000 43.45321 ? 452  ASP A OD2 1 
ATOM   2001 N  N   . TYR A 1 250 ? 10.87004  4.85694  -6.70026  1.000 21.73556 ? 453  TYR A N   1 
ATOM   2002 C  CA  . TYR A 1 250 ? 11.27064  5.66788  -5.56160  1.000 26.47397 ? 453  TYR A CA  1 
ATOM   2003 C  C   . TYR A 1 250 ? 11.21967  4.73610  -4.36181  1.000 27.94502 ? 453  TYR A C   1 
ATOM   2004 O  O   . TYR A 1 250 ? 10.12779  4.34234  -3.92314  1.000 24.04739 ? 453  TYR A O   1 
ATOM   2005 C  CB  . TYR A 1 250 ? 10.34464  6.87106  -5.40347  1.000 21.99906 ? 453  TYR A CB  1 
ATOM   2006 C  CG  . TYR A 1 250 ? 10.61191  7.77889  -4.23067  1.000 23.76678 ? 453  TYR A CG  1 
ATOM   2007 C  CD1 . TYR A 1 250 ? 10.05277  7.50940  -2.98229  1.000 22.66450 ? 453  TYR A CD1 1 
ATOM   2008 C  CD2 . TYR A 1 250 ? 11.35774  8.95186  -4.38519  1.000 20.81063 ? 453  TYR A CD2 1 
ATOM   2009 C  CE1 . TYR A 1 250 ? 10.25607  8.36378  -1.90224  1.000 21.59445 ? 453  TYR A CE1 1 
ATOM   2010 C  CE2 . TYR A 1 250 ? 11.56979  9.81590  -3.30870  1.000 22.38673 ? 453  TYR A CE2 1 
ATOM   2011 C  CZ  . TYR A 1 250 ? 11.00743  9.51599  -2.07360  1.000 24.13533 ? 453  TYR A CZ  1 
ATOM   2012 O  OH  . TYR A 1 250 ? 11.21815  10.35673 -1.00423  1.000 24.81142 ? 453  TYR A OH  1 
ATOM   2013 N  N   . ILE A 1 251 ? 12.39169  4.36575  -3.85766  1.000 22.63447 ? 454  ILE A N   1 
ATOM   2014 C  CA  . ILE A 1 251 ? 12.53336  3.24795  -2.93126  1.000 23.55853 ? 454  ILE A CA  1 
ATOM   2015 C  C   . ILE A 1 251 ? 12.68143  3.82655  -1.53474  1.000 21.45628 ? 454  ILE A C   1 
ATOM   2016 O  O   . ILE A 1 251 ? 13.71241  4.42459  -1.20849  1.000 24.80268 ? 454  ILE A O   1 
ATOM   2017 C  CB  . ILE A 1 251 ? 13.73401  2.35906  -3.29334  1.000 23.19206 ? 454  ILE A CB  1 
ATOM   2018 C  CG1 . ILE A 1 251 ? 13.70088  1.94036  -4.76689  1.000 31.86841 ? 454  ILE A CG1 1 
ATOM   2019 C  CG2 . ILE A 1 251 ? 13.80955  1.15917  -2.35331  1.000 26.75557 ? 454  ILE A CG2 1 
ATOM   2020 C  CD1 . ILE A 1 251 ? 12.42283  1.24820  -5.17824  1.000 36.92720 ? 454  ILE A CD1 1 
ATOM   2021 N  N   . ARG A 1 252 ? 11.66130  3.66114  -0.70512  1.000 21.88119 ? 455  ARG A N   1 
ATOM   2022 C  CA  . ARG A 1 252 ? 11.74482  4.20907  0.64256   1.000 24.13801 ? 455  ARG A CA  1 
ATOM   2023 C  C   . ARG A 1 252 ? 12.48868  3.25968  1.58669   1.000 27.35720 ? 455  ARG A C   1 
ATOM   2024 O  O   . ARG A 1 252 ? 12.61323  2.05073  1.34012   1.000 26.99827 ? 455  ARG A O   1 
ATOM   2025 C  CB  . ARG A 1 252 ? 10.34788  4.50634  1.18451   1.000 30.60818 ? 455  ARG A CB  1 
ATOM   2026 C  CG  . ARG A 1 252 ? 9.63664   5.63448  0.44100   1.000 26.56814 ? 455  ARG A CG  1 
ATOM   2027 C  CD  . ARG A 1 252 ? 8.15742   5.71848  0.78897   1.000 25.25851 ? 455  ARG A CD  1 
ATOM   2028 N  NE  . ARG A 1 252 ? 7.50206   6.79113  0.03987   1.000 27.10801 ? 455  ARG A NE  1 
ATOM   2029 C  CZ  . ARG A 1 252 ? 7.01864   6.66801  -1.19155  1.000 24.52905 ? 455  ARG A CZ  1 
ATOM   2030 N  NH1 . ARG A 1 252 ? 7.05555   5.51531  -1.84075  1.000 22.51575 ? 455  ARG A NH1 1 
ATOM   2031 N  NH2 . ARG A 1 252 ? 6.47541   7.72492  -1.78381  1.000 22.36993 ? 455  ARG A NH2 1 
ATOM   2032 N  N   . GLY A 1 253 ? 13.00147  3.83882  2.67559   1.000 28.16856 ? 456  GLY A N   1 
ATOM   2033 C  CA  . GLY A 1 253 ? 13.69670  3.09930  3.71216   1.000 25.64969 ? 456  GLY A CA  1 
ATOM   2034 C  C   . GLY A 1 253 ? 15.17368  2.87075  3.48397   1.000 35.48054 ? 456  GLY A C   1 
ATOM   2035 O  O   . GLY A 1 253 ? 15.76353  2.02680  4.17492   1.000 31.84145 ? 456  GLY A O   1 
ATOM   2036 N  N   . LEU A 1 254 ? 15.78669  3.56074  2.52324   1.000 32.21844 ? 457  LEU A N   1 
ATOM   2037 C  CA  . LEU A 1 254 ? 17.22118  3.43491  2.30522   1.000 32.66039 ? 457  LEU A CA  1 
ATOM   2038 C  C   . LEU A 1 254 ? 17.98989  4.31295  3.28126   1.000 34.35705 ? 457  LEU A C   1 
ATOM   2039 O  O   . LEU A 1 254 ? 17.48993  5.33677  3.75644   1.000 34.98861 ? 457  LEU A O   1 
ATOM   2040 C  CB  . LEU A 1 254 ? 17.59992  3.84351  0.88081   1.000 32.33816 ? 457  LEU A CB  1 
ATOM   2041 C  CG  . LEU A 1 254 ? 16.94323  3.13477  -0.30413  1.000 33.84749 ? 457  LEU A CG  1 
ATOM   2042 C  CD1 . LEU A 1 254 ? 17.47033  3.67373  -1.64049  1.000 28.03824 ? 457  LEU A CD1 1 
ATOM   2043 C  CD2 . LEU A 1 254 ? 17.19766  1.66697  -0.18748  1.000 32.77576 ? 457  LEU A CD2 1 
ATOM   2044 N  N   A GLN A 1 255 ? 19.21959  3.90197  3.57798   0.599 35.15542 ? 458  GLN A N   1 
ATOM   2045 N  N   B GLN A 1 255 ? 19.21746  3.90548  3.58214   0.401 35.21790 ? 458  GLN A N   1 
ATOM   2046 C  CA  A GLN A 1 255 ? 20.12039  4.75529  4.33511   0.599 37.31485 ? 458  GLN A CA  1 
ATOM   2047 C  CA  B GLN A 1 255 ? 20.08556  4.77857  4.35188   0.401 37.37962 ? 458  GLN A CA  1 
ATOM   2048 C  C   A GLN A 1 255 ? 20.61387  5.90840  3.45695   0.599 36.36740 ? 458  GLN A C   1 
ATOM   2049 C  C   B GLN A 1 255 ? 20.60467  5.91112  3.46419   0.401 36.41222 ? 458  GLN A C   1 
ATOM   2050 O  O   A GLN A 1 255 ? 20.53614  5.86106  2.22223   0.599 33.47819 ? 458  GLN A O   1 
ATOM   2051 O  O   B GLN A 1 255 ? 20.53410  5.85125  2.23100   0.401 33.01121 ? 458  GLN A O   1 
ATOM   2052 C  CB  A GLN A 1 255 ? 21.29736  3.93921  4.87206   0.599 39.70144 ? 458  GLN A CB  1 
ATOM   2053 C  CB  B GLN A 1 255 ? 21.24270  3.98659  4.96276   0.401 39.70124 ? 458  GLN A CB  1 
ATOM   2054 C  CG  A GLN A 1 255 ? 20.88379  2.85686  5.85637   0.599 40.96150 ? 458  GLN A CG  1 
ATOM   2055 C  CG  B GLN A 1 255 ? 20.80310  2.97557  6.01881   0.401 40.96563 ? 458  GLN A CG  1 
ATOM   2056 C  CD  A GLN A 1 255 ? 22.03695  1.98428  6.29900   0.599 43.65876 ? 458  GLN A CD  1 
ATOM   2057 C  CD  B GLN A 1 255 ? 19.94576  3.60262  7.10740   0.401 41.31902 ? 458  GLN A CD  1 
ATOM   2058 O  OE1 A GLN A 1 255 ? 23.19650  2.25988  5.99166   0.599 43.40940 ? 458  GLN A OE1 1 
ATOM   2059 O  OE1 B GLN A 1 255 ? 20.37403  4.53026  7.79299   0.401 43.80570 ? 458  GLN A OE1 1 
ATOM   2060 N  NE2 A GLN A 1 255 ? 21.72254  0.91565  7.02663   0.599 44.83411 ? 458  GLN A NE2 1 
ATOM   2061 N  NE2 B GLN A 1 255 ? 18.72430  3.10328  7.26276   0.401 43.69692 ? 458  GLN A NE2 1 
ATOM   2062 N  N   . ASP A 1 256 ? 21.11347  6.96430  4.11462   1.000 34.59069 ? 459  ASP A N   1 
ATOM   2063 C  CA  . ASP A 1 256 ? 21.67946  8.10265  3.38283   1.000 35.11031 ? 459  ASP A CA  1 
ATOM   2064 C  C   . ASP A 1 256 ? 22.72875  7.65277  2.37299   1.000 37.33874 ? 459  ASP A C   1 
ATOM   2065 O  O   . ASP A 1 256 ? 22.80399  8.18653  1.25893   1.000 33.39740 ? 459  ASP A O   1 
ATOM   2066 C  CB  . ASP A 1 256 ? 22.30791  9.10615  4.35489   1.000 39.66176 ? 459  ASP A CB  1 
ATOM   2067 C  CG  . ASP A 1 256 ? 21.28111  9.96002  5.06789   1.000 39.92146 ? 459  ASP A CG  1 
ATOM   2068 O  OD1 . ASP A 1 256 ? 20.06454  9.81572  4.79504   1.000 36.31999 ? 459  ASP A OD1 1 
ATOM   2069 O  OD2 . ASP A 1 256 ? 21.69798  10.78306 5.90655   1.000 39.99447 ? 459  ASP A OD2 1 
ATOM   2070 N  N   . GLU A 1 257 ? 23.52946  6.64945  2.74494   1.000 33.11350 ? 460  GLU A N   1 
ATOM   2071 C  CA  . GLU A 1 257 ? 24.58526  6.09547  1.90623   1.000 36.89014 ? 460  GLU A CA  1 
ATOM   2072 C  C   . GLU A 1 257 ? 24.06439  5.41750  0.64341   1.000 39.44665 ? 460  GLU A C   1 
ATOM   2073 O  O   . GLU A 1 257 ? 24.86898  5.09036  -0.23729  1.000 38.39355 ? 460  GLU A O   1 
ATOM   2074 C  CB  . GLU A 1 257 ? 25.41024  5.09663  2.72288   1.000 37.77025 ? 460  GLU A CB  1 
ATOM   2075 C  CG  . GLU A 1 257 ? 26.15927  5.71742  3.90984   1.000 46.82551 ? 460  GLU A CG  1 
ATOM   2076 C  CD  . GLU A 1 257 ? 25.30804  5.89322  5.17569   1.000 49.03778 ? 460  GLU A CD  1 
ATOM   2077 O  OE1 . GLU A 1 257 ? 24.08194  5.66518  5.12841   1.000 41.84593 ? 460  GLU A OE1 1 
ATOM   2078 O  OE2 . GLU A 1 257 ? 25.87892  6.26098  6.23054   1.000 58.01592 ? 460  GLU A OE2 1 
ATOM   2079 N  N   . ASP A 1 258 ? 22.75388  5.19356  0.52787   1.000 35.15014 ? 461  ASP A N   1 
ATOM   2080 C  CA  . ASP A 1 258 ? 22.18593  4.51577  -0.62871  1.000 34.85309 ? 461  ASP A CA  1 
ATOM   2081 C  C   . ASP A 1 258 ? 21.29385  5.43387  -1.45847  1.000 31.79790 ? 461  ASP A C   1 
ATOM   2082 O  O   . ASP A 1 258 ? 20.54917  4.95662  -2.32022  1.000 33.46271 ? 461  ASP A O   1 
ATOM   2083 C  CB  . ASP A 1 258 ? 21.41642  3.27394  -0.17664  1.000 34.38964 ? 461  ASP A CB  1 
ATOM   2084 C  CG  . ASP A 1 258 ? 22.32310  2.22778  0.45615   1.000 45.57848 ? 461  ASP A CG  1 
ATOM   2085 O  OD1 . ASP A 1 258 ? 23.39616  1.94846  -0.11965  1.000 43.11656 ? 461  ASP A OD1 1 
ATOM   2086 O  OD2 . ASP A 1 258 ? 21.97621  1.69764  1.53596   1.000 44.75457 ? 461  ASP A OD2 1 
ATOM   2087 N  N   . GLU A 1 259 ? 21.37912  6.74708  -1.22879  1.000 33.52210 ? 462  GLU A N   1 
ATOM   2088 C  CA  . GLU A 1 259 ? 20.46375  7.69801  -1.85727  1.000 28.13467 ? 462  GLU A CA  1 
ATOM   2089 C  C   . GLU A 1 259 ? 20.56701  7.66245  -3.37305  1.000 31.26860 ? 462  GLU A C   1 
ATOM   2090 O  O   . GLU A 1 259 ? 19.58901  7.96523  -4.07086  1.000 32.76956 ? 462  GLU A O   1 
ATOM   2091 C  CB  . GLU A 1 259 ? 20.75209  9.10931  -1.33901  1.000 30.92451 ? 462  GLU A CB  1 
ATOM   2092 C  CG  . GLU A 1 259 ? 19.89672  10.20577 -1.96014  1.000 29.53572 ? 462  GLU A CG  1 
ATOM   2093 C  CD  . GLU A 1 259 ? 18.47682  10.20910 -1.42586  1.000 33.01739 ? 462  GLU A CD  1 
ATOM   2094 O  OE1 . GLU A 1 259 ? 18.23733  9.55408  -0.37933  1.000 33.99675 ? 462  GLU A OE1 1 
ATOM   2095 O  OE2 . GLU A 1 259 ? 17.60195  10.86376 -2.05004  1.000 30.38675 ? 462  GLU A OE2 1 
ATOM   2096 N  N   . GLY A 1 260 ? 21.73538  7.29259  -3.90111  1.000 32.43289 ? 463  GLY A N   1 
ATOM   2097 C  CA  . GLY A 1 260 ? 21.89581  7.16303  -5.33765  1.000 28.44369 ? 463  GLY A CA  1 
ATOM   2098 C  C   . GLY A 1 260 ? 21.10575  6.03369  -5.94834  1.000 32.17090 ? 463  GLY A C   1 
ATOM   2099 O  O   . GLY A 1 260 ? 20.97150  5.99072  -7.17688  1.000 31.75906 ? 463  GLY A O   1 
ATOM   2100 N  N   . LYS A 1 261 ? 20.58844  5.12288  -5.12489  1.000 33.32368 ? 464  LYS A N   1 
ATOM   2101 C  CA  . LYS A 1 261 ? 19.77645  4.00192  -5.57597  1.000 30.28823 ? 464  LYS A CA  1 
ATOM   2102 C  C   . LYS A 1 261 ? 18.29286  4.21692  -5.31431  1.000 30.99562 ? 464  LYS A C   1 
ATOM   2103 O  O   . LYS A 1 261 ? 17.50553  3.27198  -5.43526  1.000 30.70300 ? 464  LYS A O   1 
ATOM   2104 C  CB  . LYS A 1 261 ? 20.25591  2.71882  -4.89830  1.000 31.17073 ? 464  LYS A CB  1 
ATOM   2105 C  CG  . LYS A 1 261 ? 21.65428  2.33601  -5.30907  1.000 37.95587 ? 464  LYS A CG  1 
ATOM   2106 C  CD  . LYS A 1 261 ? 22.17925  1.15006  -4.52928  1.000 47.46212 ? 464  LYS A CD  1 
ATOM   2107 C  CE  . LYS A 1 261 ? 22.68516  1.55834  -3.15399  1.000 42.90987 ? 464  LYS A CE  1 
ATOM   2108 N  NZ  . LYS A 1 261 ? 23.44474  0.43689  -2.51318  1.000 48.37834 ? 464  LYS A NZ  1 
ATOM   2109 N  N   . LYS A 1 262 ? 17.89325  5.44200  -4.96963  1.000 27.77612 ? 465  LYS A N   1 
ATOM   2110 C  CA  . LYS A 1 262 ? 16.53853  5.71172  -4.50659  1.000 27.09796 ? 465  LYS A CA  1 
ATOM   2111 C  C   . LYS A 1 262 ? 15.55831  6.08738  -5.61910  1.000 27.95618 ? 465  LYS A C   1 
ATOM   2112 O  O   . LYS A 1 262 ? 14.41197  5.62103  -5.59316  1.000 25.65818 ? 465  LYS A O   1 
ATOM   2113 C  CB  . LYS A 1 262 ? 16.55959  6.82078  -3.45527  1.000 24.43483 ? 465  LYS A CB  1 
ATOM   2114 C  CG  . LYS A 1 262 ? 15.19498  7.10854  -2.84260  1.000 27.10614 ? 465  LYS A CG  1 
ATOM   2115 C  CD  . LYS A 1 262 ? 15.33852  8.00623  -1.60445  1.000 32.34918 ? 465  LYS A CD  1 
ATOM   2116 C  CE  . LYS A 1 262 ? 14.03507  8.09905  -0.81758  1.000 29.89241 ? 465  LYS A CE  1 
ATOM   2117 N  NZ  . LYS A 1 262 ? 14.25569  8.76326  0.48425   1.000 26.39417 ? 465  LYS A NZ  1 
ATOM   2118 N  N   . SER A 1 263 ? 15.96127  6.91449  -6.59272  1.000 22.83184 ? 466  SER A N   1 
ATOM   2119 C  CA  . SER A 1 263 ? 15.00139  7.51279  -7.53038  1.000 23.68717 ? 466  SER A CA  1 
ATOM   2120 C  C   . SER A 1 263 ? 15.51657  7.46154  -8.96156  1.000 24.61860 ? 466  SER A C   1 
ATOM   2121 O  O   . SER A 1 263 ? 16.57893  8.01757  -9.24694  1.000 22.56203 ? 466  SER A O   1 
ATOM   2122 C  CB  . SER A 1 263 ? 14.71502  8.96964  -7.14932  1.000 26.17195 ? 466  SER A CB  1 
ATOM   2123 O  OG  . SER A 1 263 ? 14.05299  9.64882  -8.20512  1.000 24.51600 ? 466  SER A OG  1 
ATOM   2124 N  N   . ASN A 1 264 ? 14.75777  6.84616  -9.87953  1.000 22.04815 ? 467  ASN A N   1 
ATOM   2125 C  CA  . ASN A 1 264 ? 15.22443  6.84476  -11.26852 1.000 26.35007 ? 467  ASN A CA  1 
ATOM   2126 C  C   . ASN A 1 264 ? 15.09473  8.23052  -11.90797 1.000 28.30222 ? 467  ASN A C   1 
ATOM   2127 O  O   . ASN A 1 264 ? 15.97067  8.64926  -12.67369 1.000 28.07705 ? 467  ASN A O   1 
ATOM   2128 C  CB  . ASN A 1 264 ? 14.48965  5.79412  -12.10613 1.000 22.91628 ? 467  ASN A CB  1 
ATOM   2129 C  CG  . ASN A 1 264 ? 13.03810  6.10019  -12.28195 1.000 28.25315 ? 467  ASN A CG  1 
ATOM   2130 O  OD1 . ASN A 1 264 ? 12.37567  6.53689  -11.34770 1.000 31.14586 ? 467  ASN A OD1 1 
ATOM   2131 N  ND2 . ASN A 1 264 ? 12.51895  5.87189  -13.48853 1.000 28.07684 ? 467  ASN A ND2 1 
ATOM   2132 N  N   . ILE A 1 265 ? 14.01199  8.95195  -11.61700 1.000 22.61172 ? 468  ILE A N   1 
ATOM   2133 C  CA  . ILE A 1 265 ? 13.83519  10.27071 -12.21211 1.000 25.69814 ? 468  ILE A CA  1 
ATOM   2134 C  C   . ILE A 1 265 ? 14.93347  11.21654 -11.74122 1.000 27.67829 ? 468  ILE A C   1 
ATOM   2135 O  O   . ILE A 1 265 ? 15.59017  11.88546 -12.55047 1.000 28.67829 ? 468  ILE A O   1 
ATOM   2136 C  CB  . ILE A 1 265 ? 12.43535  10.82239 -11.89390 1.000 25.57697 ? 468  ILE A CB  1 
ATOM   2137 C  CG1 . ILE A 1 265 ? 11.36217  9.91905  -12.50153 1.000 23.98953 ? 468  ILE A CG1 1 
ATOM   2138 C  CG2 . ILE A 1 265 ? 12.30790  12.26292 -12.40756 1.000 20.22209 ? 468  ILE A CG2 1 
ATOM   2139 C  CD1 . ILE A 1 265 ? 9.94474   10.28579 -12.11096 1.000 20.63412 ? 468  ILE A CD1 1 
ATOM   2140 N  N   . ALA A 1 266 ? 15.15466  11.29307 -10.42455 1.000 20.97784 ? 469  ALA A N   1 
ATOM   2141 C  CA  . ALA A 1 266 ? 16.23904  12.15061 -9.94765  1.000 28.30940 ? 469  ALA A CA  1 
ATOM   2142 C  C   . ALA A 1 266 ? 17.56294  11.75818 -10.59138 1.000 27.83007 ? 469  ALA A C   1 
ATOM   2143 O  O   . ALA A 1 266 ? 18.33803  12.62172 -11.01454 1.000 26.93870 ? 469  ALA A O   1 
ATOM   2144 C  CB  . ALA A 1 266 ? 16.34504  12.09904 -8.41637  1.000 21.56890 ? 469  ALA A CB  1 
ATOM   2145 N  N   . ASN A 1 267 ? 17.82205  10.45403 -10.71082 1.000 27.63082 ? 470  ASN A N   1 
ATOM   2146 C  CA  . ASN A 1 267 ? 19.07523  10.01130 -11.30765 1.000 26.61900 ? 470  ASN A CA  1 
ATOM   2147 C  C   . ASN A 1 267 ? 19.19086  10.42433 -12.77306 1.000 24.97675 ? 470  ASN A C   1 
ATOM   2148 O  O   . ASN A 1 267 ? 20.30530  10.62366 -13.26771 1.000 26.70364 ? 470  ASN A O   1 
ATOM   2149 C  CB  . ASN A 1 267 ? 19.20751  8.49303  -11.17929 1.000 28.70029 ? 470  ASN A CB  1 
ATOM   2150 C  CG  . ASN A 1 267 ? 19.67721  8.05956  -9.80747  1.000 37.28488 ? 470  ASN A CG  1 
ATOM   2151 O  OD1 . ASN A 1 267 ? 19.89669  8.88668  -8.91166  1.000 33.23929 ? 470  ASN A OD1 1 
ATOM   2152 N  ND2 . ASN A 1 267 ? 19.82837  6.74882  -9.62921  1.000 29.79464 ? 470  ASN A ND2 1 
ATOM   2153 N  N   . ILE A 1 268 ? 18.06775  10.53483 -13.48798 1.000 26.31475 ? 471  ILE A N   1 
ATOM   2154 C  CA  . ILE A 1 268 ? 18.13047  10.95182 -14.88892 1.000 25.27367 ? 471  ILE A CA  1 
ATOM   2155 C  C   . ILE A 1 268 ? 18.60609  12.39684 -14.98791 1.000 27.04271 ? 471  ILE A C   1 
ATOM   2156 O  O   . ILE A 1 268 ? 19.52957  12.71309 -15.75113 1.000 31.37928 ? 471  ILE A O   1 
ATOM   2157 C  CB  . ILE A 1 268 ? 16.77085  10.75435 -15.58506 1.000 26.29274 ? 471  ILE A CB  1 
ATOM   2158 C  CG1 . ILE A 1 268 ? 16.51137  9.27718  -15.87534 1.000 24.58283 ? 471  ILE A CG1 1 
ATOM   2159 C  CG2 . ILE A 1 268 ? 16.73552  11.51255 -16.90202 1.000 25.70681 ? 471  ILE A CG2 1 
ATOM   2160 C  CD1 . ILE A 1 268 ? 17.60236  8.62978  -16.71775 1.000 30.17093 ? 471  ILE A CD1 1 
ATOM   2161 N  N   . PHE A 1 269 ? 17.97914  13.29458 -14.21669 1.000 27.61234 ? 472  PHE A N   1 
ATOM   2162 C  CA  . PHE A 1 269 ? 18.44367  14.67861 -14.12772 1.000 26.24730 ? 472  PHE A CA  1 
ATOM   2163 C  C   . PHE A 1 269 ? 19.91193  14.74301 -13.74303 1.000 31.31168 ? 472  PHE A C   1 
ATOM   2164 O  O   . PHE A 1 269 ? 20.69431  15.49191 -14.33844 1.000 34.75319 ? 472  PHE A O   1 
ATOM   2165 C  CB  . PHE A 1 269 ? 17.59754  15.45679 -13.11814 1.000 30.06963 ? 472  PHE A CB  1 
ATOM   2166 C  CG  . PHE A 1 269 ? 16.25336  15.85183 -13.64052 1.000 27.92455 ? 472  PHE A CG  1 
ATOM   2167 C  CD1 . PHE A 1 269 ? 16.10777  16.99892 -14.41272 1.000 26.58090 ? 472  PHE A CD1 1 
ATOM   2168 C  CD2 . PHE A 1 269 ? 15.13922  15.07380 -13.38370 1.000 24.53546 ? 472  PHE A CD2 1 
ATOM   2169 C  CE1 . PHE A 1 269 ? 14.87394  17.36914 -14.91560 1.000 22.39943 ? 472  PHE A CE1 1 
ATOM   2170 C  CE2 . PHE A 1 269 ? 13.88901  15.43642 -13.89516 1.000 27.35353 ? 472  PHE A CE2 1 
ATOM   2171 C  CZ  . PHE A 1 269 ? 13.76302  16.59528 -14.65865 1.000 21.42089 ? 472  PHE A CZ  1 
ATOM   2172 N  N   . ARG A 1 270 ? 20.30969  13.94764 -12.75563 1.000 29.16950 ? 473  ARG A N   1 
ATOM   2173 C  CA  . ARG A 1 270 ? 21.67127  14.04009 -12.24576 1.000 29.14578 ? 473  ARG A CA  1 
ATOM   2174 C  C   . ARG A 1 270 ? 22.68507  13.48509 -13.24025 1.000 35.11258 ? 473  ARG A C   1 
ATOM   2175 O  O   . ARG A 1 270 ? 23.81684  13.97573 -13.32078 1.000 36.80287 ? 473  ARG A O   1 
ATOM   2176 C  CB  . ARG A 1 270 ? 21.76180  13.30177 -10.91183 1.000 29.31448 ? 473  ARG A CB  1 
ATOM   2177 C  CG  . ARG A 1 270 ? 23.14671  13.27014 -10.32396 1.000 31.51128 ? 473  ARG A CG  1 
ATOM   2178 C  CD  . ARG A 1 270 ? 23.07952  12.98426 -8.83547  1.000 28.94587 ? 473  ARG A CD  1 
ATOM   2179 N  NE  . ARG A 1 270 ? 22.45387  11.69898 -8.56023  1.000 33.20107 ? 473  ARG A NE  1 
ATOM   2180 C  CZ  . ARG A 1 270 ? 23.12580  10.56273 -8.41284  1.000 34.73645 ? 473  ARG A CZ  1 
ATOM   2181 N  NH1 . ARG A 1 270 ? 24.44132  10.51715 -8.54582  1.000 33.25975 ? 473  ARG A NH1 1 
ATOM   2182 N  NH2 . ARG A 1 270 ? 22.45959  9.44478  -8.13065  1.000 31.61266 ? 473  ARG A NH2 1 
ATOM   2183 N  N   . ALA A 1 271 ? 22.30999  12.45476 -13.99931 1.000 31.36620 ? 474  ALA A N   1 
ATOM   2184 C  CA  . ALA A 1 271 ? 23.24712  11.89872 -14.96819 1.000 32.40471 ? 474  ALA A CA  1 
ATOM   2185 C  C   . ALA A 1 271 ? 23.31633  12.71289 -16.25082 1.000 33.24762 ? 474  ALA A C   1 
ATOM   2186 O  O   . ALA A 1 271 ? 24.37748  12.77288 -16.87569 1.000 32.32117 ? 474  ALA A O   1 
ATOM   2187 C  CB  . ALA A 1 271 ? 22.86461  10.45878 -15.31603 1.000 32.41343 ? 474  ALA A CB  1 
ATOM   2188 N  N   . TYR A 1 272 ? 22.21529  13.33323 -16.67323 1.000 35.81906 ? 475  TYR A N   1 
ATOM   2189 C  CA  . TYR A 1 272 ? 22.13332  13.81746 -18.04287 1.000 35.35293 ? 475  TYR A CA  1 
ATOM   2190 C  C   . TYR A 1 272 ? 21.82383  15.30015 -18.19727 1.000 43.04134 ? 475  TYR A C   1 
ATOM   2191 O  O   . TYR A 1 272 ? 22.01832  15.83137 -19.29593 1.000 43.52088 ? 475  TYR A O   1 
ATOM   2192 C  CB  . TYR A 1 272 ? 21.08405  13.00698 -18.82368 1.000 33.33812 ? 475  TYR A CB  1 
ATOM   2193 C  CG  . TYR A 1 272 ? 21.44065  11.54424 -19.00413 1.000 28.95370 ? 475  TYR A CG  1 
ATOM   2194 C  CD1 . TYR A 1 272 ? 22.48437  11.15517 -19.83944 1.000 36.20817 ? 475  TYR A CD1 1 
ATOM   2195 C  CD2 . TYR A 1 272 ? 20.72587  10.55530 -18.35972 1.000 30.74739 ? 475  TYR A CD2 1 
ATOM   2196 C  CE1 . TYR A 1 272 ? 22.80717  9.80835  -20.01523 1.000 37.90173 ? 475  TYR A CE1 1 
ATOM   2197 C  CE2 . TYR A 1 272 ? 21.03777  9.21423  -18.52412 1.000 36.45163 ? 475  TYR A CE2 1 
ATOM   2198 C  CZ  . TYR A 1 272 ? 22.07473  8.84511  -19.34388 1.000 46.28897 ? 475  TYR A CZ  1 
ATOM   2199 O  OH  . TYR A 1 272 ? 22.36627  7.50884  -19.48911 1.000 49.54745 ? 475  TYR A OH  1 
ATOM   2200 N  N   . SER A 1 273 ? 21.34837  15.98903 -17.15911 1.000 38.75126 ? 476  SER A N   1 
ATOM   2201 C  CA  . SER A 1 273 ? 21.04077  17.40816 -17.32116 1.000 42.77956 ? 476  SER A CA  1 
ATOM   2202 C  C   . SER A 1 273 ? 22.26535  18.25634 -17.01501 1.000 50.56599 ? 476  SER A C   1 
ATOM   2203 O  O   . SER A 1 273 ? 23.37851  17.90119 -17.41395 1.000 55.09182 ? 476  SER A O   1 
ATOM   2204 C  CB  . SER A 1 273 ? 19.86315  17.82891 -16.44110 1.000 42.75712 ? 476  SER A CB  1 
ATOM   2205 O  OG  . SER A 1 273 ? 20.28278  18.03611 -15.11034 1.000 53.43266 ? 476  SER A OG  1 
ATOM   2206 N  N   . HIS A 1 274 ? 22.08097  19.38296 -16.32801 1.000 57.16096 ? 477  HIS A N   1 
ATOM   2207 C  CA  . HIS A 1 274 ? 23.17590  20.31245 -16.06953 1.000 60.62001 ? 477  HIS A CA  1 
ATOM   2208 C  C   . HIS A 1 274 ? 23.23233  20.65465 -14.58494 1.000 68.04407 ? 477  HIS A C   1 
ATOM   2209 O  O   . HIS A 1 274 ? 22.24699  20.52602 -13.85226 1.000 56.91125 ? 477  HIS A O   1 
ATOM   2210 C  CB  . HIS A 1 274 ? 23.04059  21.60930 -16.89629 1.000 52.71074 ? 477  HIS A CB  1 
ATOM   2211 C  CG  . HIS A 1 274 ? 22.04365  22.58163 -16.33969 1.000 65.13673 ? 477  HIS A CG  1 
ATOM   2212 N  ND1 . HIS A 1 274 ? 22.32682  23.40973 -15.27311 1.000 67.25292 ? 477  HIS A ND1 1 
ATOM   2213 C  CD2 . HIS A 1 274 ? 20.76358  22.85238 -16.69427 1.000 62.87511 ? 477  HIS A CD2 1 
ATOM   2214 C  CE1 . HIS A 1 274 ? 21.26594  24.14627 -14.99378 1.000 64.58623 ? 477  HIS A CE1 1 
ATOM   2215 N  NE2 . HIS A 1 274 ? 20.30304  23.82810 -15.84153 1.000 62.84752 ? 477  HIS A NE2 1 
ATOM   2216 N  N   . ASN A 1 275 ? 24.40033  21.12115 -14.15121 1.000 78.07453 ? 478  ASN A N   1 
ATOM   2217 C  CA  . ASN A 1 275 ? 24.62480  21.53969 -12.77407 1.000 78.33820 ? 478  ASN A CA  1 
ATOM   2218 C  C   . ASN A 1 275 ? 25.17528  22.96617 -12.72940 1.000 82.72303 ? 478  ASN A C   1 
ATOM   2219 O  O   . ASN A 1 275 ? 26.09400  23.27397 -11.96498 1.000 84.15000 ? 478  ASN A O   1 
ATOM   2220 C  CB  . ASN A 1 275 ? 25.55577  20.55768 -12.06004 1.000 79.57984 ? 478  ASN A CB  1 
ATOM   2221 C  CG  . ASN A 1 275 ? 25.31421  20.49482 -10.55228 1.000 74.13224 ? 478  ASN A CG  1 
ATOM   2222 O  OD1 . ASN A 1 275 ? 24.26722  20.91584 -10.05474 1.000 73.42813 ? 478  ASN A OD1 1 
ATOM   2223 N  ND2 . ASN A 1 275 ? 26.28927  19.96082 -9.82130  1.000 71.57147 ? 478  ASN A ND2 1 
ATOM   2224 N  N   . ASN A 1 276 ? 24.61138  23.85039 -13.56053 1.000 77.39178 ? 479  ASN A N   1 
ATOM   2225 C  CA  . ASN A 1 276 ? 25.02066  25.25338 -13.60876 1.000 74.37676 ? 479  ASN A CA  1 
ATOM   2226 C  C   . ASN A 1 276 ? 24.92019  25.89497 -12.23075 1.000 72.15604 ? 479  ASN A C   1 
ATOM   2227 O  O   . ASN A 1 276 ? 23.87118  25.84382 -11.58399 1.000 64.90552 ? 479  ASN A O   1 
ATOM   2228 C  CB  . ASN A 1 276 ? 24.14883  26.01344 -14.61843 1.000 74.01306 ? 479  ASN A CB  1 
ATOM   2229 C  CG  . ASN A 1 276 ? 24.34474  27.53162 -14.56296 1.000 88.51512 ? 479  ASN A CG  1 
ATOM   2230 O  OD1 . ASN A 1 276 ? 25.40171  28.03420 -14.16201 1.000 83.37443 ? 479  ASN A OD1 1 
ATOM   2231 N  ND2 . ASN A 1 276 ? 23.31560  28.26839 -14.97889 1.000 91.04135 ? 479  ASN A ND2 1 
ATOM   2232 N  N   . ALA A 1 277 ? 26.02575  26.50535 -11.78722 1.000 72.46013 ? 480  ALA A N   1 
ATOM   2233 C  CA  . ALA A 1 277 ? 26.06732  27.09695 -10.45181 1.000 74.57098 ? 480  ALA A CA  1 
ATOM   2234 C  C   . ALA A 1 277 ? 25.00909  28.18014 -10.27806 1.000 74.33494 ? 480  ALA A C   1 
ATOM   2235 O  O   . ALA A 1 277 ? 24.52977  28.40365 -9.15960  1.000 72.13737 ? 480  ALA A O   1 
ATOM   2236 C  CB  . ALA A 1 277 ? 27.45940  27.66273 -10.16975 1.000 65.23409 ? 480  ALA A CB  1 
ATOM   2237 N  N   . ARG A 1 278 ? 24.62521  28.85428 -11.36884 1.000 75.98061 ? 481  ARG A N   1 
ATOM   2238 C  CA  . ARG A 1 278 ? 23.56697  29.85683 -11.28752 1.000 80.30961 ? 481  ARG A CA  1 
ATOM   2239 C  C   . ARG A 1 278 ? 22.23025  29.22813 -10.90856 1.000 82.45295 ? 481  ARG A C   1 
ATOM   2240 O  O   . ARG A 1 278 ? 21.38943  29.88478 -10.28043 1.000 82.45097 ? 481  ARG A O   1 
ATOM   2241 C  CB  . ARG A 1 278 ? 23.44310  30.60013 -12.61942 1.000 82.98355 ? 481  ARG A CB  1 
ATOM   2242 N  N   . GLY A 1 279 ? 22.02213  27.96244 -11.26755 1.000 78.16980 ? 482  GLY A N   1 
ATOM   2243 C  CA  . GLY A 1 279 ? 20.77559  27.29059 -10.97810 1.000 67.86015 ? 482  GLY A CA  1 
ATOM   2244 C  C   . GLY A 1 279 ? 20.02189  26.93262 -12.24091 1.000 59.11229 ? 482  GLY A C   1 
ATOM   2245 O  O   . GLY A 1 279 ? 20.60841  26.78293 -13.31785 1.000 64.07713 ? 482  GLY A O   1 
ATOM   2246 N  N   . GLY A 1 280 ? 18.71692  26.79379 -12.10563 1.000 53.50543 ? 483  GLY A N   1 
ATOM   2247 C  CA  . GLY A 1 280 ? 17.84174  26.47606 -13.20738 1.000 42.62265 ? 483  GLY A CA  1 
ATOM   2248 C  C   . GLY A 1 280 ? 16.43410  26.76285 -12.76872 1.000 43.05667 ? 483  GLY A C   1 
ATOM   2249 O  O   . GLY A 1 280 ? 16.21284  27.41583 -11.74882 1.000 47.06725 ? 483  GLY A O   1 
ATOM   2250 N  N   . TYR A 1 281 ? 15.47715  26.24605 -13.52895 1.000 38.14771 ? 484  TYR A N   1 
ATOM   2251 C  CA  . TYR A 1 281 ? 14.07023  26.53450 -13.29952 1.000 37.55447 ? 484  TYR A CA  1 
ATOM   2252 C  C   . TYR A 1 281 ? 13.27779  25.23811 -13.24412 1.000 33.41219 ? 484  TYR A C   1 
ATOM   2253 O  O   . TYR A 1 281 ? 13.46829  24.35537 -14.08676 1.000 31.32711 ? 484  TYR A O   1 
ATOM   2254 C  CB  . TYR A 1 281 ? 13.50083  27.43995 -14.41020 1.000 40.25218 ? 484  TYR A CB  1 
ATOM   2255 C  CG  . TYR A 1 281 ? 14.21459  28.77171 -14.56427 1.000 45.25455 ? 484  TYR A CG  1 
ATOM   2256 C  CD1 . TYR A 1 281 ? 13.90028  29.85070 -13.74469 1.000 45.29343 ? 484  TYR A CD1 1 
ATOM   2257 C  CD2 . TYR A 1 281 ? 15.19468  28.95207 -15.53929 1.000 49.87548 ? 484  TYR A CD2 1 
ATOM   2258 C  CE1 . TYR A 1 281 ? 14.54912  31.06688 -13.88099 1.000 51.55878 ? 484  TYR A CE1 1 
ATOM   2259 C  CE2 . TYR A 1 281 ? 15.84869  30.17386 -15.68841 1.000 46.56802 ? 484  TYR A CE2 1 
ATOM   2260 C  CZ  . TYR A 1 281 ? 15.52187  31.22375 -14.85438 1.000 55.18812 ? 484  TYR A CZ  1 
ATOM   2261 O  OH  . TYR A 1 281 ? 16.16647  32.43545 -14.99385 1.000 61.62865 ? 484  TYR A OH  1 
ATOM   2262 N  N   . ILE A 1 282 ? 12.36293  25.15408 -12.27070 1.000 31.57196 ? 485  ILE A N   1 
ATOM   2263 C  CA  . ILE A 1 282 ? 11.50404  23.97846 -12.12989 1.000 29.65333 ? 485  ILE A CA  1 
ATOM   2264 C  C   . ILE A 1 282 ? 10.81696  23.65871 -13.45014 1.000 35.07567 ? 485  ILE A C   1 
ATOM   2265 O  O   . ILE A 1 282 ? 10.77109  22.50066 -13.88527 1.000 31.52240 ? 485  ILE A O   1 
ATOM   2266 C  CB  . ILE A 1 282 ? 10.45519  24.20208 -11.02894 1.000 28.69722 ? 485  ILE A CB  1 
ATOM   2267 C  CG1 . ILE A 1 282 ? 11.11734  24.49494 -9.68758  1.000 28.62578 ? 485  ILE A CG1 1 
ATOM   2268 C  CG2 . ILE A 1 282 ? 9.50134   22.97517 -10.96420 1.000 26.02181 ? 485  ILE A CG2 1 
ATOM   2269 C  CD1 . ILE A 1 282 ? 10.24129  25.30995 -8.74068  1.000 26.89619 ? 485  ILE A CD1 1 
ATOM   2270 N  N   . GLU A 1 283 ? 10.24077  24.68570 -14.08695 1.000 30.75445 ? 486  GLU A N   1 
ATOM   2271 C  CA  . GLU A 1 283 ? 9.42922   24.46097 -15.27950 1.000 34.69705 ? 486  GLU A CA  1 
ATOM   2272 C  C   . GLU A 1 283 ? 10.25725  23.92383 -16.42895 1.000 30.27133 ? 486  GLU A C   1 
ATOM   2273 O  O   . GLU A 1 283 ? 9.73614   23.17362 -17.26295 1.000 29.63380 ? 486  GLU A O   1 
ATOM   2274 C  CB  . GLU A 1 283 ? 8.73841   25.74934 -15.71295 1.000 29.97568 ? 486  GLU A CB  1 
ATOM   2275 C  CG  . GLU A 1 283 ? 9.68907   26.91413 -15.92317 1.000 33.98121 ? 486  GLU A CG  1 
ATOM   2276 C  CD  . GLU A 1 283 ? 9.90707   27.72483 -14.64772 1.000 42.92208 ? 486  GLU A CD  1 
ATOM   2277 O  OE1 . GLU A 1 283 ? 9.64255   27.19140 -13.54396 1.000 41.01907 ? 486  GLU A OE1 1 
ATOM   2278 O  OE2 . GLU A 1 283 ? 10.32985  28.89598 -14.74528 1.000 41.05574 ? 486  GLU A OE2 1 
ATOM   2279 N  N   . ASP A 1 284 ? 11.53274  24.30529 -16.50965 1.000 30.79532 ? 487  ASP A N   1 
ATOM   2280 C  CA  . ASP A 1 284 ? 12.37944  23.76697 -17.57200 1.000 32.14570 ? 487  ASP A CA  1 
ATOM   2281 C  C   . ASP A 1 284 ? 12.54816  22.26161 -17.41184 1.000 34.31878 ? 487  ASP A C   1 
ATOM   2282 O  O   . ASP A 1 284 ? 12.43551  21.50854 -18.38237 1.000 32.62823 ? 487  ASP A O   1 
ATOM   2283 C  CB  . ASP A 1 284 ? 13.75076  24.44476 -17.58464 1.000 33.16231 ? 487  ASP A CB  1 
ATOM   2284 C  CG  . ASP A 1 284 ? 13.69845  25.91497 -17.99913 1.000 43.96426 ? 487  ASP A CG  1 
ATOM   2285 O  OD1 . ASP A 1 284 ? 12.60258  26.45380 -18.28751 1.000 43.03881 ? 487  ASP A OD1 1 
ATOM   2286 O  OD2 . ASP A 1 284 ? 14.78199  26.53182 -18.03014 1.000 46.06637 ? 487  ASP A OD2 1 
ATOM   2287 N  N   . GLY A 1 285 ? 12.81639  21.80144 -16.18602 1.000 32.39296 ? 488  GLY A N   1 
ATOM   2288 C  CA  . GLY A 1 285 ? 12.99295  20.37303 -15.98097 1.000 26.90387 ? 488  GLY A CA  1 
ATOM   2289 C  C   . GLY A 1 285 ? 11.71668  19.59806 -16.23233 1.000 25.55307 ? 488  GLY A C   1 
ATOM   2290 O  O   . GLY A 1 285 ? 11.74557  18.49051 -16.77358 1.000 30.59120 ? 488  GLY A O   1 
ATOM   2291 N  N   . LEU A 1 286 ? 10.57668  20.17472 -15.85562 1.000 25.80116 ? 489  LEU A N   1 
ATOM   2292 C  CA  . LEU A 1 286 ? 9.29571   19.52321 -16.11441 1.000 31.46149 ? 489  LEU A CA  1 
ATOM   2293 C  C   . LEU A 1 286 ? 9.02269   19.41369 -17.61497 1.000 28.75470 ? 489  LEU A C   1 
ATOM   2294 O  O   . LEU A 1 286 ? 8.62381   18.35371 -18.10478 1.000 25.49887 ? 489  LEU A O   1 
ATOM   2295 C  CB  . LEU A 1 286 ? 8.17255   20.28462 -15.40729 1.000 22.06892 ? 489  LEU A CB  1 
ATOM   2296 C  CG  . LEU A 1 286 ? 8.18845   20.24765 -13.86958 1.000 25.24486 ? 489  LEU A CG  1 
ATOM   2297 C  CD1 . LEU A 1 286 ? 7.04520   21.05674 -13.32194 1.000 22.91969 ? 489  LEU A CD1 1 
ATOM   2298 C  CD2 . LEU A 1 286 ? 8.11202   18.79825 -13.34778 1.000 20.14864 ? 489  LEU A CD2 1 
ATOM   2299 N  N   . THR A 1 287 ? 9.21455   20.50567 -18.35438 1.000 26.41284 ? 490  THR A N   1 
ATOM   2300 C  CA  . THR A 1 287 ? 9.01034   20.46181 -19.80304 1.000 30.82823 ? 490  THR A CA  1 
ATOM   2301 C  C   . THR A 1 287 ? 9.91763   19.43049 -20.44566 1.000 31.27872 ? 490  THR A C   1 
ATOM   2302 O  O   . THR A 1 287 ? 9.46592   18.59007 -21.23122 1.000 32.60533 ? 490  THR A O   1 
ATOM   2303 C  CB  . THR A 1 287 ? 9.27564   21.83455 -20.42097 1.000 34.93617 ? 490  THR A CB  1 
ATOM   2304 O  OG1 . THR A 1 287 ? 8.43456   22.80173 -19.79390 1.000 30.00010 ? 490  THR A OG1 1 
ATOM   2305 C  CG2 . THR A 1 287 ? 8.99808   21.81009 -21.94723 1.000 30.50150 ? 490  THR A CG2 1 
ATOM   2306 N  N   . TRP A 1 288 ? 11.20958  19.48919 -20.11024 1.000 26.17139 ? 491  TRP A N   1 
ATOM   2307 C  CA  . TRP A 1 288 ? 12.20711  18.56806 -20.64214 1.000 33.28397 ? 491  TRP A CA  1 
ATOM   2308 C  C   . TRP A 1 288 ? 11.77504  17.10905 -20.50726 1.000 33.44935 ? 491  TRP A C   1 
ATOM   2309 O  O   . TRP A 1 288 ? 11.97019  16.29963 -21.42467 1.000 29.15037 ? 491  TRP A O   1 
ATOM   2310 C  CB  . TRP A 1 288 ? 13.51317  18.81834 -19.89819 1.000 29.00507 ? 491  TRP A CB  1 
ATOM   2311 C  CG  . TRP A 1 288 ? 14.71746  18.06360 -20.32419 1.000 29.23314 ? 491  TRP A CG  1 
ATOM   2312 C  CD1 . TRP A 1 288 ? 15.44548  18.24788 -21.46960 1.000 32.08330 ? 491  TRP A CD1 1 
ATOM   2313 C  CD2 . TRP A 1 288 ? 15.40732  17.07160 -19.56580 1.000 27.95740 ? 491  TRP A CD2 1 
ATOM   2314 N  NE1 . TRP A 1 288 ? 16.53360  17.41114 -21.47775 1.000 30.98680 ? 491  TRP A NE1 1 
ATOM   2315 C  CE2 . TRP A 1 288 ? 16.52957  16.67195 -20.32354 1.000 30.22823 ? 491  TRP A CE2 1 
ATOM   2316 C  CE3 . TRP A 1 288 ? 15.17175  16.45775 -18.32661 1.000 29.40184 ? 491  TRP A CE3 1 
ATOM   2317 C  CZ2 . TRP A 1 288 ? 17.41662  15.69404 -19.88420 1.000 33.23281 ? 491  TRP A CZ2 1 
ATOM   2318 C  CZ3 . TRP A 1 288 ? 16.05486  15.49085 -17.89115 1.000 27.13834 ? 491  TRP A CZ3 1 
ATOM   2319 C  CH2 . TRP A 1 288 ? 17.16544  15.11529 -18.67246 1.000 29.62746 ? 491  TRP A CH2 1 
ATOM   2320 N  N   . TYR A 1 289 ? 11.19954  16.75079 -19.36387 1.000 29.11948 ? 492  TYR A N   1 
ATOM   2321 C  CA  . TYR A 1 289 ? 10.83673  15.35825 -19.14264 1.000 25.27987 ? 492  TYR A CA  1 
ATOM   2322 C  C   . TYR A 1 289 ? 9.58772   14.95130 -19.91674 1.000 27.43359 ? 492  TYR A C   1 
ATOM   2323 O  O   . TYR A 1 289 ? 9.43106   13.76977 -20.24078 1.000 28.86745 ? 492  TYR A O   1 
ATOM   2324 C  CB  . TYR A 1 289 ? 10.61323  15.11041 -17.64919 1.000 25.22370 ? 492  TYR A CB  1 
ATOM   2325 C  CG  . TYR A 1 289 ? 11.12993  13.77628 -17.17379 1.000 23.09437 ? 492  TYR A CG  1 
ATOM   2326 C  CD1 . TYR A 1 289 ? 12.48094  13.59257 -16.90282 1.000 23.51931 ? 492  TYR A CD1 1 
ATOM   2327 C  CD2 . TYR A 1 289 ? 10.27652  12.70748 -16.99244 1.000 21.58328 ? 492  TYR A CD2 1 
ATOM   2328 C  CE1 . TYR A 1 289 ? 12.96219  12.37558 -16.46419 1.000 25.46568 ? 492  TYR A CE1 1 
ATOM   2329 C  CE2 . TYR A 1 289 ? 10.75342  11.48411 -16.55509 1.000 24.24765 ? 492  TYR A CE2 1 
ATOM   2330 C  CZ  . TYR A 1 289 ? 12.09528  11.33122 -16.29903 1.000 24.55443 ? 492  TYR A CZ  1 
ATOM   2331 O  OH  . TYR A 1 289 ? 12.56709  10.12685 -15.86748 1.000 26.96908 ? 492  TYR A OH  1 
ATOM   2332 N  N   . LEU A 1 290 ? 8.69275   15.89497 -20.21640 1.000 28.98501 ? 493  LEU A N   1 
ATOM   2333 C  CA  . LEU A 1 290 ? 7.33239   15.55555 -20.62560 1.000 28.65159 ? 493  LEU A CA  1 
ATOM   2334 C  C   . LEU A 1 290 ? 7.03797   15.79200 -22.09959 1.000 24.86410 ? 493  LEU A C   1 
ATOM   2335 O  O   . LEU A 1 290 ? 6.36103   14.97122 -22.71460 1.000 30.34345 ? 493  LEU A O   1 
ATOM   2336 C  CB  . LEU A 1 290 ? 6.31833   16.33103 -19.77965 1.000 30.59521 ? 493  LEU A CB  1 
ATOM   2337 C  CG  . LEU A 1 290 ? 6.26699   16.04480 -18.26864 1.000 22.22663 ? 493  LEU A CG  1 
ATOM   2338 C  CD1 . LEU A 1 290 ? 5.12687   16.83819 -17.63879 1.000 26.09850 ? 493  LEU A CD1 1 
ATOM   2339 C  CD2 . LEU A 1 290 ? 6.10408   14.55625 -17.96604 1.000 27.04882 ? 493  LEU A CD2 1 
ATOM   2340 N  N   . TYR A 1 291 ? 7.51819   16.87698 -22.70021 1.000 29.76097 ? 494  TYR A N   1 
ATOM   2341 C  CA  . TYR A 1 291 ? 7.21775   17.13254 -24.10651 1.000 32.01168 ? 494  TYR A CA  1 
ATOM   2342 C  C   . TYR A 1 291 ? 8.29678   18.03503 -24.70288 1.000 34.25835 ? 494  TYR A C   1 
ATOM   2343 O  O   . TYR A 1 291 ? 9.11533   18.61294 -23.98789 1.000 37.16933 ? 494  TYR A O   1 
ATOM   2344 C  CB  . TYR A 1 291 ? 5.81036   17.72584 -24.25891 1.000 33.28042 ? 494  TYR A CB  1 
ATOM   2345 C  CG  . TYR A 1 291 ? 5.56739   19.02325 -23.51958 1.000 31.99513 ? 494  TYR A CG  1 
ATOM   2346 C  CD1 . TYR A 1 291 ? 5.07875   19.01994 -22.22868 1.000 33.66815 ? 494  TYR A CD1 1 
ATOM   2347 C  CD2 . TYR A 1 291 ? 5.80092   20.25595 -24.13271 1.000 42.24215 ? 494  TYR A CD2 1 
ATOM   2348 C  CE1 . TYR A 1 291 ? 4.84018   20.19602 -21.54479 1.000 35.75886 ? 494  TYR A CE1 1 
ATOM   2349 C  CE2 . TYR A 1 291 ? 5.56753   21.45071 -23.45682 1.000 45.78694 ? 494  TYR A CE2 1 
ATOM   2350 C  CZ  . TYR A 1 291 ? 5.08397   21.41006 -22.15758 1.000 39.14476 ? 494  TYR A CZ  1 
ATOM   2351 O  OH  . TYR A 1 291 ? 4.84279   22.57450 -21.45854 1.000 44.88800 ? 494  TYR A OH  1 
ATOM   2352 N  N   . LYS A 1 292 ? 8.28378   18.16178 -26.02849 1.000 34.00368 ? 495  LYS A N   1 
ATOM   2353 C  CA  . LYS A 1 292 ? 9.37287   18.81462 -26.75110 1.000 38.31252 ? 495  LYS A CA  1 
ATOM   2354 C  C   . LYS A 1 292 ? 9.10825   20.30952 -26.89858 1.000 47.60190 ? 495  LYS A C   1 
ATOM   2355 O  O   . LYS A 1 292 ? 8.08341   20.70906 -27.46031 1.000 47.59852 ? 495  LYS A O   1 
ATOM   2356 C  CB  . LYS A 1 292 ? 9.55948   18.16905 -28.12242 1.000 35.32795 ? 495  LYS A CB  1 
ATOM   2357 C  CG  . LYS A 1 292 ? 10.29913  16.85273 -28.05870 1.000 39.75068 ? 495  LYS A CG  1 
ATOM   2358 C  CD  . LYS A 1 292 ? 9.76965   15.84433 -29.05822 1.000 47.40405 ? 495  LYS A CD  1 
ATOM   2359 C  CE  . LYS A 1 292 ? 10.32457  16.07466 -30.43337 1.000 42.00247 ? 495  LYS A CE  1 
ATOM   2360 N  NZ  . LYS A 1 292 ? 9.82249   15.07648 -31.43672 1.000 47.89165 ? 495  LYS A NZ  1 
ATOM   2361 N  N   . ARG A 1 293 ? 10.03878  21.13227 -26.40507 1.000 41.76630 ? 496  ARG A N   1 
ATOM   2362 C  CA  . ARG A 1 293 ? 9.99789   22.57582 -26.61162 1.000 48.93693 ? 496  ARG A CA  1 
ATOM   2363 C  C   . ARG A 1 293 ? 11.39927  23.07407 -26.95051 1.000 50.49818 ? 496  ARG A C   1 
ATOM   2364 O  O   . ARG A 1 293 ? 12.38985  22.55565 -26.42346 1.000 45.95307 ? 496  ARG A O   1 
ATOM   2365 C  CB  . ARG A 1 293 ? 9.44511   23.29505 -25.37853 1.000 50.64871 ? 496  ARG A CB  1 
ATOM   2366 C  CG  . ARG A 1 293 ? 9.11564   24.75096 -25.60677 1.000 59.93631 ? 496  ARG A CG  1 
ATOM   2367 C  CD  . ARG A 1 293 ? 7.69006   25.06217 -25.18717 1.000 69.79426 ? 496  ARG A CD  1 
ATOM   2368 N  NE  . ARG A 1 293 ? 6.71195   24.38669 -26.03450 1.000 63.95462 ? 496  ARG A NE  1 
ATOM   2369 C  CZ  . ARG A 1 293 ? 5.39929   24.42669 -25.83807 1.000 72.87032 ? 496  ARG A CZ  1 
ATOM   2370 N  NH1 . ARG A 1 293 ? 4.87075   25.09472 -24.82078 1.000 77.80104 ? 496  ARG A NH1 1 
ATOM   2371 N  NH2 . ARG A 1 293 ? 4.59607   23.77602 -26.67765 1.000 68.48103 ? 496  ARG A NH2 1 
ATOM   2372 N  N   . ASP A 1 294 ? 11.48102  24.07926 -27.83387 1.000 58.24570 ? 497  ASP A N   1 
ATOM   2373 C  CA  . ASP A 1 294 ? 12.78561  24.51841 -28.33316 1.000 56.36239 ? 497  ASP A CA  1 
ATOM   2374 C  C   . ASP A 1 294 ? 13.64905  25.12402 -27.23130 1.000 51.97022 ? 497  ASP A C   1 
ATOM   2375 O  O   . ASP A 1 294 ? 14.87975  25.01908 -27.28528 1.000 51.02162 ? 497  ASP A O   1 
ATOM   2376 C  CB  . ASP A 1 294 ? 12.62046  25.53012 -29.47275 1.000 61.18444 ? 497  ASP A CB  1 
ATOM   2377 C  CG  . ASP A 1 294 ? 11.95497  24.93337 -30.70815 1.000 76.72310 ? 497  ASP A CG  1 
ATOM   2378 O  OD1 . ASP A 1 294 ? 10.70541  24.87430 -30.74511 1.000 80.40591 ? 497  ASP A OD1 1 
ATOM   2379 O  OD2 . ASP A 1 294 ? 12.67777  24.52605 -31.64639 1.000 80.81964 ? 497  ASP A OD2 1 
ATOM   2380 N  N   . GLY A 1 295 ? 13.03161  25.76588 -26.23495 1.000 52.01225 ? 498  GLY A N   1 
ATOM   2381 C  CA  . GLY A 1 295 ? 13.80417  26.39771 -25.17563 1.000 51.52613 ? 498  GLY A CA  1 
ATOM   2382 C  C   . GLY A 1 295 ? 14.66250  25.43220 -24.37619 1.000 52.76886 ? 498  GLY A C   1 
ATOM   2383 O  O   . GLY A 1 295 ? 15.73383  25.80585 -23.88694 1.000 51.87650 ? 498  GLY A O   1 
ATOM   2384 N  N   . GLN A 1 296 ? 14.21544  24.18491 -24.23420 1.000 45.83304 ? 499  GLN A N   1 
ATOM   2385 C  CA  . GLN A 1 296 ? 14.91697  23.17898 -23.44691 1.000 52.06114 ? 499  GLN A CA  1 
ATOM   2386 C  C   . GLN A 1 296 ? 15.78313  22.26244 -24.30477 1.000 48.52742 ? 499  GLN A C   1 
ATOM   2387 O  O   . GLN A 1 296 ? 16.20569  21.20033 -23.82885 1.000 44.49008 ? 499  GLN A O   1 
ATOM   2388 C  CB  . GLN A 1 296 ? 13.91964  22.34723 -22.63789 1.000 42.41948 ? 499  GLN A CB  1 
ATOM   2389 C  CG  . GLN A 1 296 ? 13.41142  23.03514 -21.39286 1.000 48.19894 ? 499  GLN A CG  1 
ATOM   2390 C  CD  . GLN A 1 296 ? 12.63359  24.28706 -21.70192 1.000 47.45926 ? 499  GLN A CD  1 
ATOM   2391 O  OE1 . GLN A 1 296 ? 11.71997  24.27190 -22.52773 1.000 53.91806 ? 499  GLN A OE1 1 
ATOM   2392 N  NE2 . GLN A 1 296 ? 13.00535  25.39221 -21.05862 1.000 47.78959 ? 499  GLN A NE2 1 
ATOM   2393 N  N   . LYS A 1 297 ? 16.06723  22.66473 -25.54902 1.000 43.18556 ? 500  LYS A N   1 
ATOM   2394 C  CA  . LYS A 1 297 ? 16.83395  21.82705 -26.46702 1.000 51.69472 ? 500  LYS A CA  1 
ATOM   2395 C  C   . LYS A 1 297 ? 18.20150  21.45769 -25.89434 1.000 55.08613 ? 500  LYS A C   1 
ATOM   2396 O  O   . LYS A 1 297 ? 18.66397  20.32124 -26.06483 1.000 48.98307 ? 500  LYS A O   1 
ATOM   2397 C  CB  . LYS A 1 297 ? 16.98225  22.54514 -27.80996 1.000 44.09959 ? 500  LYS A CB  1 
ATOM   2398 C  CG  . LYS A 1 297 ? 17.94195  21.88743 -28.78189 1.000 58.96802 ? 500  LYS A CG  1 
ATOM   2399 N  N   . ASN A 1 298 ? 18.86574  22.39756 -25.20984 1.000 48.86247 ? 501  ASN A N   1 
ATOM   2400 C  CA  . ASN A 1 298 ? 20.17700  22.14352 -24.61767 1.000 51.61399 ? 501  ASN A CA  1 
ATOM   2401 C  C   . ASN A 1 298 ? 20.14292  22.11743 -23.08851 1.000 47.60349 ? 501  ASN A C   1 
ATOM   2402 O  O   . ASN A 1 298 ? 21.10896  22.52179 -22.43569 1.000 49.31690 ? 501  ASN A O   1 
ATOM   2403 C  CB  . ASN A 1 298 ? 21.19917  23.17302 -25.09323 1.000 42.78381 ? 501  ASN A CB  1 
ATOM   2404 C  CG  . ASN A 1 298 ? 21.30499  23.23473 -26.60096 1.000 51.07672 ? 501  ASN A CG  1 
ATOM   2405 O  OD1 . ASN A 1 298 ? 21.50977  24.30621 -27.16319 1.000 55.12478 ? 501  ASN A OD1 1 
ATOM   2406 N  ND2 . ASN A 1 298 ? 21.15668  22.08659 -27.26684 1.000 54.95262 ? 501  ASN A ND2 1 
ATOM   2407 N  N   . LEU A 1 299 ? 19.04572  21.63643 -22.50201 1.000 47.88544 ? 502  LEU A N   1 
ATOM   2408 C  CA  . LEU A 1 299 ? 19.01389  21.45734 -21.05367 1.000 42.17804 ? 502  LEU A CA  1 
ATOM   2409 C  C   . LEU A 1 299 ? 19.94218  20.32051 -20.62312 1.000 45.54733 ? 502  LEU A C   1 
ATOM   2410 O  O   . LEU A 1 299 ? 20.64863  20.43429 -19.61331 1.000 42.93282 ? 502  LEU A O   1 
ATOM   2411 C  CB  . LEU A 1 299 ? 17.57227  21.21188 -20.59415 1.000 41.56380 ? 502  LEU A CB  1 
ATOM   2412 C  CG  . LEU A 1 299 ? 17.22003  21.34607 -19.09894 1.000 42.65864 ? 502  LEU A CG  1 
ATOM   2413 C  CD1 . LEU A 1 299 ? 15.72251  21.46486 -18.90610 1.000 40.48223 ? 502  LEU A CD1 1 
ATOM   2414 C  CD2 . LEU A 1 299 ? 17.71054  20.15837 -18.29396 1.000 45.41271 ? 502  LEU A CD2 1 
ATOM   2415 N  N   . GLY A 1 300 ? 19.95857  19.22174 -21.37703 1.000 41.79217 ? 503  GLY A N   1 
ATOM   2416 C  CA  . GLY A 1 300 ? 20.82594  18.09676 -21.07600 1.000 42.71315 ? 503  GLY A CA  1 
ATOM   2417 C  C   . GLY A 1 300 ? 21.43761  17.45470 -22.30643 1.000 44.67505 ? 503  GLY A C   1 
ATOM   2418 O  O   . GLY A 1 300 ? 21.34538  18.00976 -23.40611 1.000 45.84084 ? 503  GLY A O   1 
ATOM   2419 N  N   A SER A 1 301 ? 22.07246  16.29228 -22.13289 0.279 43.88758 ? 504  SER A N   1 
ATOM   2420 N  N   B SER A 1 301 ? 22.06933  16.29058 -22.14159 0.721 44.04680 ? 504  SER A N   1 
ATOM   2421 C  CA  A SER A 1 301 ? 22.64871  15.55411 -23.25130 0.279 42.44457 ? 504  SER A CA  1 
ATOM   2422 C  CA  B SER A 1 301 ? 22.64840  15.55536 -23.26417 0.721 42.41682 ? 504  SER A CA  1 
ATOM   2423 C  C   A SER A 1 301 ? 21.63866  14.64570 -23.93860 0.279 40.87236 ? 504  SER A C   1 
ATOM   2424 C  C   B SER A 1 301 ? 21.66234  14.58820 -23.90664 0.721 40.87330 ? 504  SER A C   1 
ATOM   2425 O  O   A SER A 1 301 ? 21.94175  14.10382 -25.00499 0.279 41.04306 ? 504  SER A O   1 
ATOM   2426 O  O   B SER A 1 301 ? 22.00879  13.93801 -24.89481 0.721 40.96707 ? 504  SER A O   1 
ATOM   2427 C  CB  A SER A 1 301 ? 23.84383  14.72573 -22.77727 0.279 40.23539 ? 504  SER A CB  1 
ATOM   2428 C  CB  B SER A 1 301 ? 23.89562  14.78622 -22.81615 0.721 39.98589 ? 504  SER A CB  1 
ATOM   2429 O  OG  A SER A 1 301 ? 23.48782  13.91777 -21.66902 0.279 43.89904 ? 504  SER A OG  1 
ATOM   2430 O  OG  B SER A 1 301 ? 23.62724  14.02841 -21.65059 0.721 44.29666 ? 504  SER A OG  1 
ATOM   2431 N  N   . ILE A 1 302 ? 20.46073  14.45446 -23.34677 1.000 41.62927 ? 505  ILE A N   1 
ATOM   2432 C  CA  . ILE A 1 302 ? 19.35320  13.74532 -23.96982 1.000 40.91216 ? 505  ILE A CA  1 
ATOM   2433 C  C   . ILE A 1 302 ? 18.11992  14.61788 -23.76696 1.000 39.50547 ? 505  ILE A C   1 
ATOM   2434 O  O   . ILE A 1 302 ? 18.13899  15.58991 -23.00243 1.000 34.84235 ? 505  ILE A O   1 
ATOM   2435 C  CB  . ILE A 1 302 ? 19.12360  12.32578 -23.38028 1.000 40.32190 ? 505  ILE A CB  1 
ATOM   2436 C  CG1 . ILE A 1 302 ? 18.74855  12.40691 -21.89482 1.000 34.47506 ? 505  ILE A CG1 1 
ATOM   2437 C  CG2 . ILE A 1 302 ? 20.34320  11.42611 -23.60226 1.000 36.73898 ? 505  ILE A CG2 1 
ATOM   2438 C  CD1 . ILE A 1 302 ? 18.59056  11.06782 -21.20899 1.000 30.65125 ? 505  ILE A CD1 1 
ATOM   2439 N  N   . TYR A 1 303 ? 17.04303  14.26517 -24.46616 1.000 34.60752 ? 506  TYR A N   1 
ATOM   2440 C  CA  . TYR A 1 303 ? 15.75313  14.94321 -24.33495 1.000 34.43670 ? 506  TYR A CA  1 
ATOM   2441 C  C   . TYR A 1 303 ? 14.66269  13.88422 -24.19421 1.000 32.87705 ? 506  TYR A C   1 
ATOM   2442 O  O   . TYR A 1 303 ? 14.20128  13.33117 -25.20687 1.000 32.43914 ? 506  TYR A O   1 
ATOM   2443 C  CB  . TYR A 1 303 ? 15.47559  15.86355 -25.52981 1.000 34.79342 ? 506  TYR A CB  1 
ATOM   2444 C  CG  . TYR A 1 303 ? 14.45713  16.94628 -25.20891 1.000 37.58954 ? 506  TYR A CG  1 
ATOM   2445 C  CD1 . TYR A 1 303 ? 13.18288  16.61664 -24.77505 1.000 33.36712 ? 506  TYR A CD1 1 
ATOM   2446 C  CD2 . TYR A 1 303 ? 14.77810  18.28902 -25.30977 1.000 38.41019 ? 506  TYR A CD2 1 
ATOM   2447 C  CE1 . TYR A 1 303 ? 12.25978  17.57795 -24.46047 1.000 30.80680 ? 506  TYR A CE1 1 
ATOM   2448 C  CE2 . TYR A 1 303 ? 13.84750  19.26482 -25.00055 1.000 36.40286 ? 506  TYR A CE2 1 
ATOM   2449 C  CZ  . TYR A 1 303 ? 12.58963  18.89819 -24.57658 1.000 34.91516 ? 506  TYR A CZ  1 
ATOM   2450 O  OH  . TYR A 1 303 ? 11.64526  19.84865 -24.25378 1.000 36.80633 ? 506  TYR A OH  1 
ATOM   2451 N  N   . PRO A 1 304 ? 14.22506  13.56732 -22.96054 1.000 32.77064 ? 507  PRO A N   1 
ATOM   2452 C  CA  . PRO A 1 304 ? 13.15931  12.56597 -22.77539 1.000 28.30234 ? 507  PRO A CA  1 
ATOM   2453 C  C   . PRO A 1 304 ? 11.86225  12.90580 -23.49943 1.000 33.95757 ? 507  PRO A C   1 
ATOM   2454 O  O   . PRO A 1 304 ? 11.40458  12.11722 -24.33630 1.000 30.56767 ? 507  PRO A O   1 
ATOM   2455 C  CB  . PRO A 1 304 ? 12.95263  12.55080 -21.25329 1.000 25.43147 ? 507  PRO A CB  1 
ATOM   2456 C  CG  . PRO A 1 304 ? 14.26519  12.99127 -20.69748 1.000 28.77416 ? 507  PRO A CG  1 
ATOM   2457 C  CD  . PRO A 1 304 ? 14.80145  14.00536 -21.67891 1.000 30.97802 ? 507  PRO A CD  1 
ATOM   2458 N  N   . GLY A 1 305 ? 11.26528  14.06637 -23.19560 1.000 30.91296 ? 508  GLY A N   1 
ATOM   2459 C  CA  . GLY A 1 305 ? 10.04414  14.49938 -23.86100 1.000 30.60106 ? 508  GLY A CA  1 
ATOM   2460 C  C   . GLY A 1 305 ? 9.05224   13.36356 -24.04399 1.000 31.41494 ? 508  GLY A C   1 
ATOM   2461 O  O   . GLY A 1 305 ? 8.57434   13.12183 -25.15150 1.000 29.51544 ? 508  GLY A O   1 
ATOM   2462 N  N   . LEU A 1 306 ? 8.71786   12.68464 -22.94279 1.000 28.92025 ? 509  LEU A N   1 
ATOM   2463 C  CA  . LEU A 1 306 ? 8.22435   11.30710 -23.00340 1.000 26.34752 ? 509  LEU A CA  1 
ATOM   2464 C  C   . LEU A 1 306 ? 6.80212   11.19240 -23.53762 1.000 28.35469 ? 509  LEU A C   1 
ATOM   2465 O  O   . LEU A 1 306 ? 6.42234   10.12822 -24.04177 1.000 28.56080 ? 509  LEU A O   1 
ATOM   2466 C  CB  . LEU A 1 306 ? 8.28489   10.67533 -21.61410 1.000 24.15061 ? 509  LEU A CB  1 
ATOM   2467 C  CG  . LEU A 1 306 ? 9.68958   10.44035 -21.05859 1.000 31.23970 ? 509  LEU A CG  1 
ATOM   2468 C  CD1 . LEU A 1 306 ? 9.59182   10.03447 -19.59411 1.000 23.78817 ? 509  LEU A CD1 1 
ATOM   2469 C  CD2 . LEU A 1 306 ? 10.44362  9.38548  -21.88046 1.000 25.02699 ? 509  LEU A CD2 1 
ATOM   2470 N  N   . PHE A 1 307 ? 5.98983   12.23486 -23.38705 1.000 29.79967 ? 510  PHE A N   1 
ATOM   2471 C  CA  . PHE A 1 307 ? 4.58908   12.20423 -23.78171 1.000 25.08530 ? 510  PHE A CA  1 
ATOM   2472 C  C   . PHE A 1 307 ? 4.29392   13.34030 -24.73700 1.000 26.14774 ? 510  PHE A C   1 
ATOM   2473 O  O   . PHE A 1 307 ? 3.26855   14.02091 -24.62892 1.000 30.24072 ? 510  PHE A O   1 
ATOM   2474 C  CB  . PHE A 1 307 ? 3.68702   12.26787 -22.55375 1.000 21.71169 ? 510  PHE A CB  1 
ATOM   2475 C  CG  . PHE A 1 307 ? 4.04145   11.26942 -21.51528 1.000 26.95536 ? 510  PHE A CG  1 
ATOM   2476 C  CD1 . PHE A 1 307 ? 3.64159   9.94943  -21.64555 1.000 28.06211 ? 510  PHE A CD1 1 
ATOM   2477 C  CD2 . PHE A 1 307 ? 4.79768   11.63299 -20.41321 1.000 26.62767 ? 510  PHE A CD2 1 
ATOM   2478 C  CE1 . PHE A 1 307 ? 3.98027   9.01583  -20.68644 1.000 22.45244 ? 510  PHE A CE1 1 
ATOM   2479 C  CE2 . PHE A 1 307 ? 5.13108   10.69484 -19.44459 1.000 27.67065 ? 510  PHE A CE2 1 
ATOM   2480 C  CZ  . PHE A 1 307 ? 4.72377   9.38680  -19.59549 1.000 24.52714 ? 510  PHE A CZ  1 
ATOM   2481 N  N   . ASN A 1 308 ? 5.19762   13.55530 -25.69951 1.000 31.06460 ? 511  ASN A N   1 
ATOM   2482 C  CA  . ASN A 1 308 ? 5.09832   14.72798 -26.56583 1.000 34.89438 ? 511  ASN A CA  1 
ATOM   2483 C  C   . ASN A 1 308 ? 3.78769   14.74883 -27.34512 1.000 35.97506 ? 511  ASN A C   1 
ATOM   2484 O  O   . ASN A 1 308 ? 3.18570   15.81106 -27.52468 1.000 39.01562 ? 511  ASN A O   1 
ATOM   2485 C  CB  . ASN A 1 308 ? 6.29018   14.79756 -27.52483 1.000 29.69291 ? 511  ASN A CB  1 
ATOM   2486 C  CG  . ASN A 1 308 ? 6.27231   16.06245 -28.37283 1.000 40.74214 ? 511  ASN A CG  1 
ATOM   2487 O  OD1 . ASN A 1 308 ? 6.46983   17.16654 -27.86252 1.000 34.96846 ? 511  ASN A OD1 1 
ATOM   2488 N  ND2 . ASN A 1 308 ? 6.01593   15.90759 -29.67229 1.000 35.27340 ? 511  ASN A ND2 1 
ATOM   2489 N  N   . ASP A 1 309 ? 3.30569   13.59754 -27.78921 1.000 32.03232 ? 512  ASP A N   1 
ATOM   2490 C  CA  . ASP A 1 309 ? 2.06216   13.64275 -28.55024 1.000 36.61440 ? 512  ASP A CA  1 
ATOM   2491 C  C   . ASP A 1 309 ? 0.81598   13.71472 -27.67054 1.000 34.76047 ? 512  ASP A C   1 
ATOM   2492 O  O   . ASP A 1 309 ? -0.28436  13.86868 -28.20471 1.000 34.71270 ? 512  ASP A O   1 
ATOM   2493 C  CB  . ASP A 1 309 ? 1.96492   12.44625 -29.49729 1.000 37.64709 ? 512  ASP A CB  1 
ATOM   2494 C  CG  . ASP A 1 309 ? 1.97945   11.12410 -28.77084 1.000 38.25057 ? 512  ASP A CG  1 
ATOM   2495 O  OD1 . ASP A 1 309 ? 2.50700   11.08029 -27.63989 1.000 39.53155 ? 512  ASP A OD1 1 
ATOM   2496 O  OD2 . ASP A 1 309 ? 1.46516   10.12981 -29.33906 1.000 48.23949 ? 512  ASP A OD2 1 
ATOM   2497 N  N   . VAL A 1 310 ? 0.94703   13.62737 -26.34682 1.000 31.85634 ? 513  VAL A N   1 
ATOM   2498 C  CA  . VAL A 1 310 ? -0.19734  13.92409 -25.48451 1.000 34.11415 ? 513  VAL A CA  1 
ATOM   2499 C  C   . VAL A 1 310 ? -0.35297  15.43472 -25.28296 1.000 33.79904 ? 513  VAL A C   1 
ATOM   2500 O  O   . VAL A 1 310 ? -1.46977  15.96291 -25.31403 1.000 33.58716 ? 513  VAL A O   1 
ATOM   2501 C  CB  . VAL A 1 310 ? -0.07298  13.18579 -24.13809 1.000 29.24727 ? 513  VAL A CB  1 
ATOM   2502 C  CG1 . VAL A 1 310 ? -1.28083  13.50029 -23.24763 1.000 26.37889 ? 513  VAL A CG1 1 
ATOM   2503 C  CG2 . VAL A 1 310 ? 0.06041   11.68070 -24.36502 1.000 36.09138 ? 513  VAL A CG2 1 
ATOM   2504 N  N   . PHE A 1 311 ? 0.74998   16.16453 -25.12062 1.000 34.46952 ? 514  PHE A N   1 
ATOM   2505 C  CA  . PHE A 1 311 ? 0.67202   17.58434 -24.79407 1.000 32.18598 ? 514  PHE A CA  1 
ATOM   2506 C  C   . PHE A 1 311 ? 1.16342   18.53162 -25.88817 1.000 39.54536 ? 514  PHE A C   1 
ATOM   2507 O  O   . PHE A 1 311 ? 1.10609   19.75213 -25.69366 1.000 48.62127 ? 514  PHE A O   1 
ATOM   2508 C  CB  . PHE A 1 311 ? 1.43268   17.82514 -23.49228 1.000 28.89002 ? 514  PHE A CB  1 
ATOM   2509 C  CG  . PHE A 1 311 ? 0.93103   16.97738 -22.36748 1.000 29.72648 ? 514  PHE A CG  1 
ATOM   2510 C  CD1 . PHE A 1 311 ? -0.23737  17.31915 -21.69374 1.000 31.06932 ? 514  PHE A CD1 1 
ATOM   2511 C  CD2 . PHE A 1 311 ? 1.59449   15.81505 -22.00882 1.000 26.97337 ? 514  PHE A CD2 1 
ATOM   2512 C  CE1 . PHE A 1 311 ? -0.71878  16.53136 -20.64473 1.000 30.28491 ? 514  PHE A CE1 1 
ATOM   2513 C  CE2 . PHE A 1 311 ? 1.11866   15.00752 -20.96674 1.000 31.55450 ? 514  PHE A CE2 1 
ATOM   2514 C  CZ  . PHE A 1 311 ? -0.03682  15.36847 -20.28497 1.000 27.90852 ? 514  PHE A CZ  1 
ATOM   2515 N  N   . ALA A 1 312 ? 1.59504   18.01913 -27.04085 1.000 46.26598 ? 515  ALA A N   1 
ATOM   2516 C  CA  . ALA A 1 312 ? 2.16141   18.83122 -28.12181 1.000 49.23338 ? 515  ALA A CA  1 
ATOM   2517 C  C   . ALA A 1 312 ? 1.38352   20.10939 -28.42976 1.000 56.57073 ? 515  ALA A C   1 
ATOM   2518 O  O   . ALA A 1 312 ? 1.89219   21.21471 -28.21153 1.000 65.76462 ? 515  ALA A O   1 
ATOM   2519 C  CB  . ALA A 1 312 ? 2.26818   18.00597 -29.40903 1.000 51.13872 ? 515  ALA A CB  1 
ATOM   2520 N  N   . HIS A 1 313 ? 0.16631   19.98126 -28.95623 1.000 53.67870 ? 516  HIS A N   1 
ATOM   2521 C  CA  . HIS A 1 313 ? -0.59196  21.12072 -29.47046 1.000 62.25623 ? 516  HIS A CA  1 
ATOM   2522 C  C   . HIS A 1 313 ? -1.81984  21.42025 -28.61449 1.000 49.88935 ? 516  HIS A C   1 
ATOM   2523 O  O   . HIS A 1 313 ? -2.88981  21.76894 -29.12222 1.000 50.66365 ? 516  HIS A O   1 
ATOM   2524 C  CB  . HIS A 1 313 ? -0.98047  20.88177 -30.92736 1.000 51.75555 ? 516  HIS A CB  1 
ATOM   2525 C  CG  . HIS A 1 313 ? 0.19463   20.61634 -31.81373 1.000 65.61179 ? 516  HIS A CG  1 
ATOM   2526 N  ND1 . HIS A 1 313 ? 0.94999   21.62647 -32.37096 1.000 65.98268 ? 516  HIS A ND1 1 
ATOM   2527 C  CD2 . HIS A 1 313 ? 0.76139   19.45448 -32.21903 1.000 66.98956 ? 516  HIS A CD2 1 
ATOM   2528 C  CE1 . HIS A 1 313 ? 1.92195   21.09838 -33.09384 1.000 62.13968 ? 516  HIS A CE1 1 
ATOM   2529 N  NE2 . HIS A 1 313 ? 1.82895   19.78210 -33.01966 1.000 62.30177 ? 516  HIS A NE2 1 
ATOM   2530 N  N   . ASP A 1 314 ? -1.65625  21.31134 -27.29957 1.000 48.56842 ? 517  ASP A N   1 
ATOM   2531 C  CA  . ASP A 1 314 ? -2.75292  21.42687 -26.35565 1.000 40.89576 ? 517  ASP A CA  1 
ATOM   2532 C  C   . ASP A 1 314 ? -2.25285  22.18023 -25.12208 1.000 46.32982 ? 517  ASP A C   1 
ATOM   2533 O  O   . ASP A 1 314 ? -1.12215  22.67536 -25.07052 1.000 44.28064 ? 517  ASP A O   1 
ATOM   2534 C  CB  . ASP A 1 314 ? -3.29695  20.03080 -26.01302 1.000 52.59436 ? 517  ASP A CB  1 
ATOM   2535 C  CG  . ASP A 1 314 ? -4.73584  20.06137 -25.52465 1.000 57.91445 ? 517  ASP A CG  1 
ATOM   2536 O  OD1 . ASP A 1 314 ? -5.22569  21.16143 -25.17764 1.000 54.12465 ? 517  ASP A OD1 1 
ATOM   2537 O  OD2 . ASP A 1 314 ? -5.37201  18.98170 -25.48490 1.000 61.17256 ? 517  ASP A OD2 1 
ATOM   2538 N  N   . THR A 1 315 ? -3.11191  22.26321 -24.11771 1.000 47.39674 ? 518  THR A N   1 
ATOM   2539 C  CA  . THR A 1 315 ? -2.74798  22.90106 -22.86393 1.000 47.36713 ? 518  THR A CA  1 
ATOM   2540 C  C   . THR A 1 315 ? -1.52508  22.22265 -22.24611 1.000 45.73519 ? 518  THR A C   1 
ATOM   2541 O  O   . THR A 1 315 ? -1.46242  20.99241 -22.14107 1.000 36.19758 ? 518  THR A O   1 
ATOM   2542 C  CB  . THR A 1 315 ? -3.94492  22.84599 -21.91058 1.000 48.43854 ? 518  THR A CB  1 
ATOM   2543 O  OG1 . THR A 1 315 ? -5.11903  23.31901 -22.59806 1.000 41.81046 ? 518  THR A OG1 1 
ATOM   2544 C  CG2 . THR A 1 315 ? -3.68118  23.68936 -20.64796 1.000 39.17014 ? 518  THR A CG2 1 
ATOM   2545 N  N   . SER A 1 316 ? -0.53161  23.02619 -21.86972 1.000 42.31236 ? 519  SER A N   1 
ATOM   2546 C  CA  . SER A 1 316 ? 0.54288   22.49555 -21.04909 1.000 36.89046 ? 519  SER A CA  1 
ATOM   2547 C  C   . SER A 1 316 ? 0.00295   22.22797 -19.65175 1.000 30.87995 ? 519  SER A C   1 
ATOM   2548 O  O   . SER A 1 316 ? -0.78299  23.02725 -19.13895 1.000 35.24089 ? 519  SER A O   1 
ATOM   2549 C  CB  . SER A 1 316 ? 1.71395   23.46685 -20.94919 1.000 31.49243 ? 519  SER A CB  1 
ATOM   2550 O  OG  . SER A 1 316 ? 2.60457   23.00497 -19.93038 1.000 34.70984 ? 519  SER A OG  1 
ATOM   2551 N  N   . PRO A 1 317 ? 0.37036   21.10602 -19.02856 1.000 26.57811 ? 520  PRO A N   1 
ATOM   2552 C  CA  . PRO A 1 317 ? 0.02645   20.89788 -17.61771 1.000 28.92078 ? 520  PRO A CA  1 
ATOM   2553 C  C   . PRO A 1 317 ? 0.92284   21.66470 -16.66027 1.000 28.25153 ? 520  PRO A C   1 
ATOM   2554 O  O   . PRO A 1 317 ? 0.70880   21.59423 -15.44560 1.000 33.06897 ? 520  PRO A O   1 
ATOM   2555 C  CB  . PRO A 1 317 ? 0.21372   19.38030 -17.44844 1.000 27.85331 ? 520  PRO A CB  1 
ATOM   2556 C  CG  . PRO A 1 317 ? 1.36429   19.09481 -18.32797 1.000 28.38672 ? 520  PRO A CG  1 
ATOM   2557 C  CD  . PRO A 1 317 ? 1.13540   19.97021 -19.56508 1.000 24.61279 ? 520  PRO A CD  1 
ATOM   2558 N  N   . ILE A 1 318 ? 1.90891   22.39176 -17.17513 1.000 28.56446 ? 521  ILE A N   1 
ATOM   2559 C  CA  . ILE A 1 318 ? 2.85519   23.15377 -16.36650 1.000 29.81994 ? 521  ILE A CA  1 
ATOM   2560 C  C   . ILE A 1 318 ? 2.45569   24.62427 -16.39364 1.000 32.79537 ? 521  ILE A C   1 
ATOM   2561 O  O   . ILE A 1 318 ? 2.24251   25.19457 -17.46770 1.000 33.23958 ? 521  ILE A O   1 
ATOM   2562 C  CB  . ILE A 1 318 ? 4.28478   22.96741 -16.89882 1.000 36.00733 ? 521  ILE A CB  1 
ATOM   2563 C  CG1 . ILE A 1 318 ? 4.60272   21.47538 -17.01312 1.000 27.84886 ? 521  ILE A CG1 1 
ATOM   2564 C  CG2 . ILE A 1 318 ? 5.29066   23.73252 -16.03186 1.000 35.01223 ? 521  ILE A CG2 1 
ATOM   2565 C  CD1 . ILE A 1 318 ? 5.80195   21.17342 -17.85046 1.000 29.78904 ? 521  ILE A CD1 1 
ATOM   2566 N  N   . ASN A 1 319 ? 2.36191   25.24274 -15.22517 1.000 30.87120 ? 522  ASN A N   1 
ATOM   2567 C  CA  . ASN A 1 319 ? 2.10368   26.66884 -15.13863 1.000 30.66447 ? 522  ASN A CA  1 
ATOM   2568 C  C   . ASN A 1 319 ? 3.09789   27.31925 -14.18334 1.000 35.96324 ? 522  ASN A C   1 
ATOM   2569 O  O   . ASN A 1 319 ? 3.64897   26.66698 -13.28821 1.000 31.69110 ? 522  ASN A O   1 
ATOM   2570 C  CB  . ASN A 1 319 ? 0.66535   26.97055 -14.68991 1.000 29.61400 ? 522  ASN A CB  1 
ATOM   2571 C  CG  . ASN A 1 319 ? 0.23659   28.42523 -15.03108 1.000 46.72867 ? 522  ASN A CG  1 
ATOM   2572 O  OD1 . ASN A 1 319 ? -0.52541  29.05470 -14.29276 1.000 50.05455 ? 522  ASN A OD1 1 
ATOM   2573 N  ND2 . ASN A 1 319 ? 0.75388   28.95764 -16.14144 1.000 41.02544 ? 522  ASN A ND2 1 
ATOM   2574 N  N   . ILE A 1 320 ? 3.33293   28.61416 -14.39935 1.000 35.39918 ? 523  ILE A N   1 
ATOM   2575 C  CA  . ILE A 1 320 ? 4.22924   29.42703 -13.58478 1.000 36.02718 ? 523  ILE A CA  1 
ATOM   2576 C  C   . ILE A 1 320 ? 3.45690   30.66173 -13.15143 1.000 40.31430 ? 523  ILE A C   1 
ATOM   2577 O  O   . ILE A 1 320 ? 2.98339   31.42627 -14.00019 1.000 37.23811 ? 523  ILE A O   1 
ATOM   2578 C  CB  . ILE A 1 320 ? 5.50486   29.83220 -14.34713 1.000 41.91024 ? 523  ILE A CB  1 
ATOM   2579 C  CG1 . ILE A 1 320 ? 6.29216   28.59132 -14.79167 1.000 40.58230 ? 523  ILE A CG1 1 
ATOM   2580 C  CG2 . ILE A 1 320 ? 6.36945   30.75822 -13.48602 1.000 40.89224 ? 523  ILE A CG2 1 
ATOM   2581 C  CD1 . ILE A 1 320 ? 6.08351   28.21661 -16.26115 1.000 41.76441 ? 523  ILE A CD1 1 
ATOM   2582 N  N   . GLU A 1 321 ? 3.31772   30.86054 -11.84205 1.000 35.70907 ? 524  GLU A N   1 
ATOM   2583 C  CA  . GLU A 1 321 ? 2.53539   31.98435 -11.34460 1.000 38.54958 ? 524  GLU A CA  1 
ATOM   2584 C  C   . GLU A 1 321 ? 3.28033   32.70761 -10.23401 1.000 35.60124 ? 524  GLU A C   1 
ATOM   2585 O  O   . GLU A 1 321 ? 3.82869   32.08139 -9.32538  1.000 38.21205 ? 524  GLU A O   1 
ATOM   2586 C  CB  . GLU A 1 321 ? 1.15468   31.53418 -10.85458 1.000 40.52815 ? 524  GLU A CB  1 
ATOM   2587 C  CG  . GLU A 1 321 ? 0.22615   31.07428 -11.97644 1.000 52.31805 ? 524  GLU A CG  1 
ATOM   2588 C  CD  . GLU A 1 321 ? -1.25362  31.13140 -11.60716 1.000 56.78091 ? 524  GLU A CD  1 
ATOM   2589 O  OE1 . GLU A 1 321 ? -1.81140  32.25374 -11.52030 1.000 58.18197 ? 524  GLU A OE1 1 
ATOM   2590 O  OE2 . GLU A 1 321 ? -1.85633  30.05029 -11.40688 1.000 56.45015 ? 524  GLU A OE2 1 
ATOM   2591 N  N   . ARG A 1 322 ? 3.28427   34.03182 -10.31364 1.000 40.00215 ? 525  ARG A N   1 
ATOM   2592 C  CA  . ARG A 1 322 ? 3.97446   34.87717 -9.35536  1.000 43.99354 ? 525  ARG A CA  1 
ATOM   2593 C  C   . ARG A 1 322 ? 3.01149   35.33330 -8.27168  1.000 44.73146 ? 525  ARG A C   1 
ATOM   2594 O  O   . ARG A 1 322 ? 1.81129   35.48341 -8.50341  1.000 45.39661 ? 525  ARG A O   1 
ATOM   2595 C  CB  . ARG A 1 322 ? 4.60512   36.09358 -10.04380 1.000 44.80373 ? 525  ARG A CB  1 
ATOM   2596 C  CG  . ARG A 1 322 ? 5.85008   35.74502 -10.85629 1.000 50.66855 ? 525  ARG A CG  1 
ATOM   2597 C  CD  . ARG A 1 322 ? 6.73532   36.96526 -11.10703 1.000 69.76592 ? 525  ARG A CD  1 
ATOM   2598 N  NE  . ARG A 1 322 ? 8.15658   36.63211 -11.06216 1.000 70.00980 ? 525  ARG A NE  1 
ATOM   2599 C  CZ  . ARG A 1 322 ? 8.93307   36.80960 -9.99955  1.000 72.25507 ? 525  ARG A CZ  1 
ATOM   2600 N  NH1 . ARG A 1 322 ? 8.46206   37.34357 -8.87763  1.000 63.94851 ? 525  ARG A NH1 1 
ATOM   2601 N  NH2 . ARG A 1 322 ? 10.21253  36.44162 -10.06222 1.000 70.40482 ? 525  ARG A NH2 1 
ATOM   2602 N  N   . CYS A 1 323 ? 3.54708   35.53074 -7.07317  1.000 44.02519 ? 526  CYS A N   1 
ATOM   2603 C  CA  . CYS A 1 323 ? 2.78728   36.14486 -5.99954  1.000 50.04490 ? 526  CYS A CA  1 
ATOM   2604 C  C   . CYS A 1 323 ? 3.68325   37.12044 -5.25688  1.000 55.69611 ? 526  CYS A C   1 
ATOM   2605 O  O   . CYS A 1 323 ? 4.89249   36.91544 -5.13780  1.000 59.73096 ? 526  CYS A O   1 
ATOM   2606 C  CB  . CYS A 1 323 ? 2.22845   35.11104 -5.03434  1.000 48.68167 ? 526  CYS A CB  1 
ATOM   2607 S  SG  . CYS A 1 323 ? 3.47209   33.98266 -4.43269  1.000 47.79231 ? 526  CYS A SG  1 
ATOM   2608 N  N   . GLU A 1 324 ? 3.08115   38.18494 -4.77848  1.000 62.05845 ? 527  GLU A N   1 
ATOM   2609 C  CA  . GLU A 1 324 ? 3.81627   39.18352 -4.01726  1.000 62.57830 ? 527  GLU A CA  1 
ATOM   2610 C  C   . GLU A 1 324 ? 2.94607   39.85394 -2.96873  1.000 61.06261 ? 527  GLU A C   1 
ATOM   2611 O  O   . GLU A 1 324 ? 3.44251   40.72044 -2.24269  1.000 64.27685 ? 527  GLU A O   1 
ATOM   2612 C  CB  . GLU A 1 324 ? 4.41120   40.23768 -4.96531  1.000 66.36166 ? 527  GLU A CB  1 
ATOM   2613 C  CG  . GLU A 1 324 ? 3.38198   41.16247 -5.58107  1.000 69.20814 ? 527  GLU A CG  1 
ATOM   2614 C  CD  . GLU A 1 324 ? 4.01212   42.25973 -6.40795  1.000 87.11481 ? 527  GLU A CD  1 
ATOM   2615 O  OE1 . GLU A 1 324 ? 5.02268   41.97694 -7.08869  1.000 90.34982 ? 527  GLU A OE1 1 
ATOM   2616 O  OE2 . GLU A 1 324 ? 3.50192   43.40382 -6.36521  1.000 93.60098 ? 527  GLU A OE2 1 
ATOM   2617 N  N   . THR A 1 325 ? 1.66727   39.51570 -2.88502  1.000 49.20863 ? 528  THR A N   1 
ATOM   2618 C  CA  . THR A 1 325 ? 0.82565   39.94421 -1.78720  1.000 48.60826 ? 528  THR A CA  1 
ATOM   2619 C  C   . THR A 1 325 ? 0.32221   38.71364 -1.04817  1.000 46.57865 ? 528  THR A C   1 
ATOM   2620 O  O   . THR A 1 325 ? 0.37971   37.58525 -1.55043  1.000 44.74438 ? 528  THR A O   1 
ATOM   2621 C  CB  . THR A 1 325 ? -0.35279  40.78768 -2.27622  1.000 50.13573 ? 528  THR A CB  1 
ATOM   2622 O  OG1 . THR A 1 325 ? -1.33612  39.93344 -2.86330  1.000 55.26605 ? 528  THR A OG1 1 
ATOM   2623 C  CG2 . THR A 1 325 ? 0.11304   41.79280 -3.32262  1.000 57.86648 ? 528  THR A CG2 1 
ATOM   2624 N  N   . LYS A 1 326 ? -0.15271  38.94206 0.17072   1.000 38.31693 ? 529  LYS A N   1 
ATOM   2625 C  CA  . LYS A 1 326 ? -0.78083  37.86103 0.91331   1.000 42.49288 ? 529  LYS A CA  1 
ATOM   2626 C  C   . LYS A 1 326 ? -1.97492  37.29935 0.15295   1.000 41.08919 ? 529  LYS A C   1 
ATOM   2627 O  O   . LYS A 1 326 ? -2.14024  36.08038 0.05610   1.000 39.64756 ? 529  LYS A O   1 
ATOM   2628 C  CB  . LYS A 1 326 ? -1.20861  38.35434 2.28555   1.000 34.89047 ? 529  LYS A CB  1 
ATOM   2629 C  CG  . LYS A 1 326 ? -1.95321  37.32546 3.09818   1.000 33.77472 ? 529  LYS A CG  1 
ATOM   2630 C  CD  . LYS A 1 326 ? -2.26809  37.90160 4.47762   1.000 38.65152 ? 529  LYS A CD  1 
ATOM   2631 C  CE  . LYS A 1 326 ? -2.83696  36.82553 5.39995   1.000 38.40829 ? 529  LYS A CE  1 
ATOM   2632 N  NZ  . LYS A 1 326 ? -4.20168  36.37627 4.99680   1.000 40.70774 ? 529  LYS A NZ  1 
ATOM   2633 N  N   . LYS A 1 327 ? -2.81904  38.17612 -0.38987  1.000 41.94925 ? 530  LYS A N   1 
ATOM   2634 C  CA  . LYS A 1 327 ? -3.99998  37.71203 -1.10652  1.000 41.94162 ? 530  LYS A CA  1 
ATOM   2635 C  C   . LYS A 1 327 ? -3.61419  36.90376 -2.33877  1.000 41.81188 ? 530  LYS A C   1 
ATOM   2636 O  O   . LYS A 1 327 ? -4.23304  35.87415 -2.63063  1.000 42.09665 ? 530  LYS A O   1 
ATOM   2637 C  CB  . LYS A 1 327 ? -4.87782  38.90237 -1.49308  1.000 43.28419 ? 530  LYS A CB  1 
ATOM   2638 C  CG  . LYS A 1 327 ? -5.59713  39.55025 -0.32362  1.000 49.13407 ? 530  LYS A CG  1 
ATOM   2639 N  N   . GLU A 1 328 ? -2.59430  37.35595 -3.07577  1.000 44.55885 ? 531  GLU A N   1 
ATOM   2640 C  CA  . GLU A 1 328 ? -2.11291  36.58796 -4.22061  1.000 39.67766 ? 531  GLU A CA  1 
ATOM   2641 C  C   . GLU A 1 328 ? -1.60060  35.22103 -3.78972  1.000 39.38261 ? 531  GLU A C   1 
ATOM   2642 O  O   . GLU A 1 328 ? -1.87045  34.21371 -4.45394  1.000 40.24240 ? 531  GLU A O   1 
ATOM   2643 C  CB  . GLU A 1 328 ? -1.01362  37.35082 -4.95753  1.000 41.67659 ? 531  GLU A CB  1 
ATOM   2644 C  CG  . GLU A 1 328 ? -1.50005  38.59683 -5.69857  1.000 49.28857 ? 531  GLU A CG  1 
ATOM   2645 C  CD  . GLU A 1 328 ? -0.37192  39.38437 -6.34574  1.000 55.65235 ? 531  GLU A CD  1 
ATOM   2646 O  OE1 . GLU A 1 328 ? 0.79178   38.93643 -6.27872  1.000 54.68780 ? 531  GLU A OE1 1 
ATOM   2647 O  OE2 . GLU A 1 328 ? -0.64890  40.46283 -6.91995  1.000 71.58795 ? 531  GLU A OE2 1 
ATOM   2648 N  N   . PHE A 1 329 ? -0.85920  35.16163 -2.67925  1.000 40.19493 ? 532  PHE A N   1 
ATOM   2649 C  CA  . PHE A 1 329 ? -0.28447  33.88691 -2.25607  1.000 36.92821 ? 532  PHE A CA  1 
ATOM   2650 C  C   . PHE A 1 329 ? -1.36678  32.90694 -1.82485  1.000 37.72292 ? 532  PHE A C   1 
ATOM   2651 O  O   . PHE A 1 329 ? -1.33736  31.73309 -2.21238  1.000 36.76735 ? 532  PHE A O   1 
ATOM   2652 C  CB  . PHE A 1 329 ? 0.72274   34.10593 -1.12702  1.000 39.05672 ? 532  PHE A CB  1 
ATOM   2653 C  CG  . PHE A 1 329 ? 1.14270   32.84268 -0.43407  1.000 36.17070 ? 532  PHE A CG  1 
ATOM   2654 C  CD1 . PHE A 1 329 ? 2.02092   31.96382 -1.04188  1.000 40.19873 ? 532  PHE A CD1 1 
ATOM   2655 C  CD2 . PHE A 1 329 ? 0.66350   32.53691 0.82706   1.000 38.64097 ? 532  PHE A CD2 1 
ATOM   2656 C  CE1 . PHE A 1 329 ? 2.40222   30.79388 -0.41108  1.000 33.06375 ? 532  PHE A CE1 1 
ATOM   2657 C  CE2 . PHE A 1 329 ? 1.05167   31.37887 1.46963   1.000 34.89663 ? 532  PHE A CE2 1 
ATOM   2658 C  CZ  . PHE A 1 329 ? 1.91850   30.50432 0.84776   1.000 37.07174 ? 532  PHE A CZ  1 
ATOM   2659 N  N   A GLU A 1 330 ? -2.33291  33.36706 -1.02468  0.485 38.61454 ? 533  GLU A N   1 
ATOM   2660 N  N   B GLU A 1 330 ? -2.34557  33.37027 -1.04756  0.515 38.82367 ? 533  GLU A N   1 
ATOM   2661 C  CA  A GLU A 1 330 ? -3.36684  32.46274 -0.52796  0.485 38.13470 ? 533  GLU A CA  1 
ATOM   2662 C  CA  B GLU A 1 330 ? -3.35541  32.45021 -0.53530  0.515 37.48597 ? 533  GLU A CA  1 
ATOM   2663 C  C   A GLU A 1 330 ? -4.25787  31.97118 -1.66481  0.485 35.70987 ? 533  GLU A C   1 
ATOM   2664 C  C   B GLU A 1 330 ? -4.29238  31.97838 -1.64386  0.515 35.70074 ? 533  GLU A C   1 
ATOM   2665 O  O   A GLU A 1 330 ? -4.51626  30.76871 -1.78046  0.485 34.87534 ? 533  GLU A O   1 
ATOM   2666 O  O   B GLU A 1 330 ? -4.61046  30.78761 -1.72090  0.515 34.94775 ? 533  GLU A O   1 
ATOM   2667 C  CB  A GLU A 1 330 ? -4.18909  33.14157 0.57849   0.485 35.08285 ? 533  GLU A CB  1 
ATOM   2668 C  CB  B GLU A 1 330 ? -4.10845  33.10443 0.62864   0.515 35.23029 ? 533  GLU A CB  1 
ATOM   2669 C  CG  A GLU A 1 330 ? -4.80381  34.47639 0.20534   0.485 37.28218 ? 533  GLU A CG  1 
ATOM   2670 C  CG  B GLU A 1 330 ? -3.17814  33.28143 1.83889   0.515 36.13538 ? 533  GLU A CG  1 
ATOM   2671 C  CD  A GLU A 1 330 ? -5.17197  35.34433 1.41270   0.485 37.10455 ? 533  GLU A CD  1 
ATOM   2672 C  CD  B GLU A 1 330 ? -3.85247  33.79278 3.10849   0.515 38.37921 ? 533  GLU A CD  1 
ATOM   2673 O  OE1 A GLU A 1 330 ? -4.59736  35.15441 2.50586   0.485 33.79277 ? 533  GLU A OE1 1 
ATOM   2674 O  OE1 B GLU A 1 330 ? -4.79476  34.61736 3.00632   0.515 36.98883 ? 533  GLU A OE1 1 
ATOM   2675 O  OE2 A GLU A 1 330 ? -6.03295  36.23575 1.26016   0.485 34.60288 ? 533  GLU A OE2 1 
ATOM   2676 O  OE2 B GLU A 1 330 ? -3.40877  33.37873 4.21121   0.515 29.33274 ? 533  GLU A OE2 1 
ATOM   2677 N  N   . GLN A 1 331 ? -4.70702  32.88248 -2.53731  1.000 35.47702 ? 534  GLN A N   1 
ATOM   2678 C  CA  . GLN A 1 331 ? -5.54591  32.47778 -3.67216  1.000 38.30200 ? 534  GLN A CA  1 
ATOM   2679 C  C   . GLN A 1 331 ? -4.83424  31.46062 -4.55796  1.000 35.59387 ? 534  GLN A C   1 
ATOM   2680 O  O   . GLN A 1 331 ? -5.44608  30.49481 -5.03106  1.000 36.22218 ? 534  GLN A O   1 
ATOM   2681 C  CB  . GLN A 1 331 ? -5.95015  33.69984 -4.50417  1.000 40.14115 ? 534  GLN A CB  1 
ATOM   2682 C  CG  . GLN A 1 331 ? -7.04169  34.56873 -3.87282  1.000 42.00538 ? 534  GLN A CG  1 
ATOM   2683 C  CD  . GLN A 1 331 ? -7.13872  35.96650 -4.48952  1.000 52.76237 ? 534  GLN A CD  1 
ATOM   2684 O  OE1 . GLN A 1 331 ? -6.86913  36.16152 -5.67763  1.000 55.30648 ? 534  GLN A OE1 1 
ATOM   2685 N  NE2 . GLN A 1 331 ? -7.50550  36.95018 -3.66693  1.000 55.23530 ? 534  GLN A NE2 1 
ATOM   2686 N  N   . LEU A 1 332 ? -3.53574  31.65228 -4.77920  1.000 34.00399 ? 535  LEU A N   1 
ATOM   2687 C  CA  . LEU A 1 332 ? -2.79461  30.76200 -5.66122  1.000 31.53337 ? 535  LEU A CA  1 
ATOM   2688 C  C   . LEU A 1 332 ? -2.52272  29.40383 -5.00088  1.000 34.84221 ? 535  LEU A C   1 
ATOM   2689 O  O   . LEU A 1 332 ? -2.60602  28.35474 -5.66212  1.000 32.90344 ? 535  LEU A O   1 
ATOM   2690 C  CB  . LEU A 1 332 ? -1.51203  31.47182 -6.09279  1.000 34.78727 ? 535  LEU A CB  1 
ATOM   2691 C  CG  . LEU A 1 332 ? -0.43252  30.75011 -6.87736  1.000 46.23143 ? 535  LEU A CG  1 
ATOM   2692 C  CD1 . LEU A 1 332 ? -0.97662  30.24395 -8.21279  1.000 42.21922 ? 535  LEU A CD1 1 
ATOM   2693 C  CD2 . LEU A 1 332 ? 0.72182   31.71226 -7.07632  1.000 46.69081 ? 535  LEU A CD2 1 
ATOM   2694 N  N   . MET A 1 333 ? -2.21954  29.38965 -3.69603  1.000 31.60311 ? 536  MET A N   1 
ATOM   2695 C  CA  . MET A 1 333 ? -2.08862  28.11735 -2.98720  1.000 28.86342 ? 536  MET A CA  1 
ATOM   2696 C  C   . MET A 1 333 ? -3.41108  27.35863 -2.94815  1.000 28.96903 ? 536  MET A C   1 
ATOM   2697 O  O   . MET A 1 333 ? -3.45524  26.14649 -3.21085  1.000 29.38181 ? 536  MET A O   1 
ATOM   2698 C  CB  . MET A 1 333 ? -1.57493  28.34832 -1.56699  1.000 34.39662 ? 536  MET A CB  1 
ATOM   2699 C  CG  . MET A 1 333 ? -0.08942  28.62113 -1.47609  1.000 36.03459 ? 536  MET A CG  1 
ATOM   2700 S  SD  . MET A 1 333 ? 0.91462   27.15138 -1.70337  1.000 44.59867 ? 536  MET A SD  1 
ATOM   2701 C  CE  . MET A 1 333 ? -0.14272  25.87088 -1.02553  1.000 39.31495 ? 536  MET A CE  1 
ATOM   2702 N  N   . ASN A 1 334 ? -4.49928  28.04907 -2.60013  1.000 27.54626 ? 537  ASN A N   1 
ATOM   2703 C  CA  . ASN A 1 334 ? -5.80167  27.39415 -2.54049  1.000 30.45672 ? 537  ASN A CA  1 
ATOM   2704 C  C   . ASN A 1 334 ? -6.22931  26.88206 -3.90861  1.000 32.29549 ? 537  ASN A C   1 
ATOM   2705 O  O   . ASN A 1 334 ? -6.72326  25.75878 -4.02522  1.000 32.23435 ? 537  ASN A O   1 
ATOM   2706 C  CB  . ASN A 1 334 ? -6.85110  28.34826 -1.96740  1.000 33.54899 ? 537  ASN A CB  1 
ATOM   2707 C  CG  . ASN A 1 334 ? -6.70145  28.53492 -0.46518  1.000 40.46617 ? 537  ASN A CG  1 
ATOM   2708 O  OD1 . ASN A 1 334 ? -6.20617  27.64728 0.22971   1.000 41.45654 ? 537  ASN A OD1 1 
ATOM   2709 N  ND2 . ASN A 1 334 ? -7.12004  29.69372 0.03949   1.000 38.22373 ? 537  ASN A ND2 1 
ATOM   2710 N  N   . LYS A 1 335 ? -6.06183  27.69273 -4.95371  1.000 31.29555 ? 538  LYS A N   1 
ATOM   2711 C  CA  . LYS A 1 335 ? -6.38797  27.22724 -6.29997  1.000 31.18864 ? 538  LYS A CA  1 
ATOM   2712 C  C   . LYS A 1 335 ? -5.60066  25.96590 -6.64657  1.000 32.54388 ? 538  LYS A C   1 
ATOM   2713 O  O   . LYS A 1 335 ? -6.15878  24.98757 -7.15182  1.000 28.28597 ? 538  LYS A O   1 
ATOM   2714 C  CB  . LYS A 1 335 ? -6.10461  28.33425 -7.31275  1.000 28.01667 ? 538  LYS A CB  1 
ATOM   2715 C  CG  . LYS A 1 335 ? -6.40415  27.97334 -8.75456  1.000 40.21005 ? 538  LYS A CG  1 
ATOM   2716 C  CD  . LYS A 1 335 ? -6.23365  29.18365 -9.68885  1.000 42.88662 ? 538  LYS A CD  1 
ATOM   2717 C  CE  . LYS A 1 335 ? -4.76628  29.51731 -9.90092  1.000 47.41129 ? 538  LYS A CE  1 
ATOM   2718 N  NZ  . LYS A 1 335 ? -4.53973  30.34960 -11.12843 1.000 51.83083 ? 538  LYS A NZ  1 
ATOM   2719 N  N   . THR A 1 336 ? -4.30200  25.96717 -6.35570  1.000 29.69637 ? 539  THR A N   1 
ATOM   2720 C  CA  . THR A 1 336 ? -3.46107  24.83103 -6.70255  1.000 29.73611 ? 539  THR A CA  1 
ATOM   2721 C  C   . THR A 1 336 ? -3.84941  23.58933 -5.91313  1.000 31.60973 ? 539  THR A C   1 
ATOM   2722 O  O   . THR A 1 336 ? -3.98932  22.50308 -6.48219  1.000 30.84070 ? 539  THR A O   1 
ATOM   2723 C  CB  . THR A 1 336 ? -1.99885  25.17599 -6.45825  1.000 30.69468 ? 539  THR A CB  1 
ATOM   2724 O  OG1 . THR A 1 336 ? -1.67879  26.37917 -7.16479  1.000 28.86489 ? 539  THR A OG1 1 
ATOM   2725 C  CG2 . THR A 1 336 ? -1.12438  24.04858 -6.95440  1.000 27.23507 ? 539  THR A CG2 1 
ATOM   2726 N  N   . LEU A 1 337 ? -4.01690  23.72364 -4.59659  1.000 29.64249 ? 540  LEU A N   1 
ATOM   2727 C  CA  . LEU A 1 337 ? -4.38884  22.56459 -3.79238  1.000 30.85682 ? 540  LEU A CA  1 
ATOM   2728 C  C   . LEU A 1 337 ? -5.77464  22.05438 -4.16067  1.000 29.70579 ? 540  LEU A C   1 
ATOM   2729 O  O   . LEU A 1 337 ? -5.98429  20.84288 -4.27765  1.000 33.94607 ? 540  LEU A O   1 
ATOM   2730 C  CB  . LEU A 1 337 ? -4.31804  22.90679 -2.30540  1.000 24.65400 ? 540  LEU A CB  1 
ATOM   2731 C  CG  . LEU A 1 337 ? -2.90324  23.06513 -1.77910  1.000 25.88634 ? 540  LEU A CG  1 
ATOM   2732 C  CD1 . LEU A 1 337 ? -2.95922  23.79534 -0.43574  1.000 26.35071 ? 540  LEU A CD1 1 
ATOM   2733 C  CD2 . LEU A 1 337 ? -2.17018  21.71698 -1.64640  1.000 22.90633 ? 540  LEU A CD2 1 
ATOM   2734 N  N   . ASP A 1 338 ? -6.73209  22.95958 -4.36647  1.000 33.18807 ? 541  ASP A N   1 
ATOM   2735 C  CA  . ASP A 1 338 ? -8.08387  22.52841 -4.70141  1.000 36.63276 ? 541  ASP A CA  1 
ATOM   2736 C  C   . ASP A 1 338 ? -8.19930  21.93402 -6.10633  1.000 36.60644 ? 541  ASP A C   1 
ATOM   2737 O  O   . ASP A 1 338 ? -9.19056  21.25344 -6.38917  1.000 37.48909 ? 541  ASP A O   1 
ATOM   2738 C  CB  . ASP A 1 338 ? -9.05893  23.69500 -4.54142  1.000 37.58874 ? 541  ASP A CB  1 
ATOM   2739 C  CG  . ASP A 1 338 ? -9.45995  23.93055 -3.09196  1.000 52.51094 ? 541  ASP A CG  1 
ATOM   2740 O  OD1 . ASP A 1 338 ? -8.79971  23.38558 -2.16956  1.000 52.39099 ? 541  ASP A OD1 1 
ATOM   2741 O  OD2 . ASP A 1 338 ? -10.45013 24.66197 -2.87910  1.000 62.42212 ? 541  ASP A OD2 1 
ATOM   2742 N  N   . ASN A 1 339 ? -7.21439  22.13787 -6.97862  1.000 33.84168 ? 542  ASN A N   1 
ATOM   2743 C  CA  . ASN A 1 339 ? -7.25078  21.57145 -8.32286  1.000 37.11400 ? 542  ASN A CA  1 
ATOM   2744 C  C   . ASN A 1 339 ? -6.32783  20.37268 -8.49706  1.000 34.87972 ? 542  ASN A C   1 
ATOM   2745 O  O   . ASN A 1 339 ? -6.00332  20.02063 -9.63788  1.000 37.60868 ? 542  ASN A O   1 
ATOM   2746 C  CB  . ASN A 1 339 ? -6.90576  22.63591 -9.36330  1.000 32.80478 ? 542  ASN A CB  1 
ATOM   2747 C  CG  . ASN A 1 339 ? -8.07779  23.49581 -9.70030  1.000 42.84142 ? 542  ASN A CG  1 
ATOM   2748 O  OD1 . ASN A 1 339 ? -8.11731  24.67868 -9.35768  1.000 45.80272 ? 542  ASN A OD1 1 
ATOM   2749 N  ND2 . ASN A 1 339 ? -9.06326  22.90649 -10.36440 1.000 48.51143 ? 542  ASN A ND2 1 
ATOM   2750 N  N   . LYS A 1 340 ? -5.88744  19.74730 -7.40070  1.000 31.11295 ? 543  LYS A N   1 
ATOM   2751 C  CA  . LYS A 1 340 ? -5.16538  18.47698 -7.46793  1.000 32.20533 ? 543  LYS A CA  1 
ATOM   2752 C  C   . LYS A 1 340 ? -3.87820  18.61110 -8.28472  1.000 34.79249 ? 543  LYS A C   1 
ATOM   2753 O  O   . LYS A 1 340 ? -3.58080  17.79744 -9.16072  1.000 32.15955 ? 543  LYS A O   1 
ATOM   2754 C  CB  . LYS A 1 340 ? -6.05862  17.36308 -8.03665  1.000 37.82041 ? 543  LYS A CB  1 
ATOM   2755 C  CG  . LYS A 1 340 ? -7.29664  17.00073 -7.18613  1.000 44.54490 ? 543  LYS A CG  1 
ATOM   2756 C  CD  . LYS A 1 340 ? -8.46385  17.98401 -7.36433  1.000 51.46700 ? 543  LYS A CD  1 
ATOM   2757 C  CE  . LYS A 1 340 ? -9.68596  17.61961 -6.51312  1.000 49.47907 ? 543  LYS A CE  1 
ATOM   2758 N  NZ  . LYS A 1 340 ? -10.82076 18.57955 -6.74931  1.000 48.48400 ? 543  LYS A NZ  1 
ATOM   2759 N  N   . ARG A 1 341 ? -3.11617  19.66316 -8.00159  1.000 33.66221 ? 544  ARG A N   1 
ATOM   2760 C  CA  . ARG A 1 341 ? -1.83599  19.90728 -8.65411  1.000 29.36202 ? 544  ARG A CA  1 
ATOM   2761 C  C   . ARG A 1 341 ? -0.70300  19.81900 -7.63979  1.000 29.92002 ? 544  ARG A C   1 
ATOM   2762 O  O   . ARG A 1 341 ? -0.90751  20.06663 -6.44406  1.000 29.97218 ? 544  ARG A O   1 
ATOM   2763 C  CB  . ARG A 1 341 ? -1.82349  21.28787 -9.32239  1.000 29.91003 ? 544  ARG A CB  1 
ATOM   2764 C  CG  . ARG A 1 341 ? -2.93070  21.46266 -10.35612 1.000 33.24460 ? 544  ARG A CG  1 
ATOM   2765 C  CD  . ARG A 1 341 ? -3.07651  22.90323 -10.77503 1.000 29.25920 ? 544  ARG A CD  1 
ATOM   2766 N  NE  . ARG A 1 341 ? -4.11523  23.06287 -11.78195 1.000 36.10902 ? 544  ARG A NE  1 
ATOM   2767 C  CZ  . ARG A 1 341 ? -4.76846  24.19205 -12.02401 1.000 42.63157 ? 544  ARG A CZ  1 
ATOM   2768 N  NH1 . ARG A 1 341 ? -4.55562  25.28465 -11.30681 1.000 38.75621 ? 544  ARG A NH1 1 
ATOM   2769 N  NH2 . ARG A 1 341 ? -5.67747  24.21811 -12.99458 1.000 41.14442 ? 544  ARG A NH2 1 
ATOM   2770 N  N   . ALA A 1 342 ? 0.48774   19.45294 -8.12204  1.000 27.96437 ? 545  ALA A N   1 
ATOM   2771 C  CA  . ALA A 1 342 ? 1.69262   19.51649 -7.30477  1.000 26.17102 ? 545  ALA A CA  1 
ATOM   2772 C  C   . ALA A 1 342 ? 2.33336   20.90212 -7.42095  1.000 30.54047 ? 545  ALA A C   1 
ATOM   2773 O  O   . ALA A 1 342 ? 2.02410   21.68537 -8.32401  1.000 29.30000 ? 545  ALA A O   1 
ATOM   2774 C  CB  . ALA A 1 342 ? 2.68332   18.41743 -7.69721  1.000 18.89887 ? 545  ALA A CB  1 
ATOM   2775 N  N   . ILE A 1 343 ? 3.24608   21.19966 -6.49352  1.000 27.09930 ? 546  ILE A N   1 
ATOM   2776 C  CA  . ILE A 1 343 ? 3.61742   22.57558 -6.17087  1.000 25.87515 ? 546  ILE A CA  1 
ATOM   2777 C  C   . ILE A 1 343 ? 5.12915   22.68995 -6.02943  1.000 26.04424 ? 546  ILE A C   1 
ATOM   2778 O  O   . ILE A 1 343 ? 5.70629   22.10413 -5.10545  1.000 25.87158 ? 546  ILE A O   1 
ATOM   2779 C  CB  . ILE A 1 343 ? 2.95631   23.04935 -4.86465  1.000 31.19310 ? 546  ILE A CB  1 
ATOM   2780 C  CG1 . ILE A 1 343 ? 1.44273   22.86164 -4.89992  1.000 32.85122 ? 546  ILE A CG1 1 
ATOM   2781 C  CG2 . ILE A 1 343 ? 3.33843   24.49084 -4.56697  1.000 32.27016 ? 546  ILE A CG2 1 
ATOM   2782 C  CD1 . ILE A 1 343 ? 0.75089   23.29575 -3.60945  1.000 30.11410 ? 546  ILE A CD1 1 
ATOM   2783 N  N   . GLY A 1 344 ? 5.75508   23.48059 -6.89051  1.000 21.60376 ? 547  GLY A N   1 
ATOM   2784 C  CA  . GLY A 1 344 ? 7.11423   23.95347 -6.68625  1.000 23.69205 ? 547  GLY A CA  1 
ATOM   2785 C  C   . GLY A 1 344 ? 7.10532   25.42598 -6.29777  1.000 27.04892 ? 547  GLY A C   1 
ATOM   2786 O  O   . GLY A 1 344 ? 6.40287   26.22769 -6.90889  1.000 31.02359 ? 547  GLY A O   1 
ATOM   2787 N  N   . ILE A 1 345 ? 7.88258   25.76251 -5.26789  1.000 26.00007 ? 548  ILE A N   1 
ATOM   2788 C  CA  . ILE A 1 345 ? 8.05489   27.14208 -4.81097  1.000 25.39827 ? 548  ILE A CA  1 
ATOM   2789 C  C   . ILE A 1 345 ? 9.43727   27.61230 -5.23506  1.000 27.34443 ? 548  ILE A C   1 
ATOM   2790 O  O   . ILE A 1 345 ? 10.42818  26.89913 -5.03596  1.000 29.24527 ? 548  ILE A O   1 
ATOM   2791 C  CB  . ILE A 1 345 ? 7.89302   27.26539 -3.28284  1.000 28.46392 ? 548  ILE A CB  1 
ATOM   2792 C  CG1 . ILE A 1 345 ? 6.49734   26.81693 -2.84804  1.000 25.09038 ? 548  ILE A CG1 1 
ATOM   2793 C  CG2 . ILE A 1 345 ? 8.19929   28.71782 -2.80149  1.000 23.95298 ? 548  ILE A CG2 1 
ATOM   2794 C  CD1 . ILE A 1 345 ? 6.34462   26.70319 -1.32700  1.000 26.86660 ? 548  ILE A CD1 1 
ATOM   2795 N  N   . PHE A 1 346 ? 9.51385   28.81717 -5.79624  1.000 28.01181 ? 549  PHE A N   1 
ATOM   2796 C  CA  . PHE A 1 346 ? 10.78278  29.35452 -6.24646  1.000 32.38761 ? 549  PHE A CA  1 
ATOM   2797 C  C   . PHE A 1 346 ? 10.96217  30.77534 -5.73030  1.000 41.32263 ? 549  PHE A C   1 
ATOM   2798 O  O   . PHE A 1 346 ? 10.01545  31.43658 -5.29511  1.000 39.23444 ? 549  PHE A O   1 
ATOM   2799 C  CB  . PHE A 1 346 ? 10.91656  29.30850 -7.79232  1.000 35.43384 ? 549  PHE A CB  1 
ATOM   2800 C  CG  . PHE A 1 346 ? 9.86139   30.08693 -8.53420  1.000 35.32377 ? 549  PHE A CG  1 
ATOM   2801 C  CD1 . PHE A 1 346 ? 10.00898  31.45316 -8.76122  1.000 40.55393 ? 549  PHE A CD1 1 
ATOM   2802 C  CD2 . PHE A 1 346 ? 8.73631   29.44806 -9.03781  1.000 37.62774 ? 549  PHE A CD2 1 
ATOM   2803 C  CE1 . PHE A 1 346 ? 9.04400   32.16969 -9.45517  1.000 40.53286 ? 549  PHE A CE1 1 
ATOM   2804 C  CE2 . PHE A 1 346 ? 7.76617   30.15975 -9.73868  1.000 36.17355 ? 549  PHE A CE2 1 
ATOM   2805 C  CZ  . PHE A 1 346 ? 7.91665   31.52087 -9.93749  1.000 33.68116 ? 549  PHE A CZ  1 
ATOM   2806 N  N   . TRP A 1 347 ? 12.20847  31.22863 -5.78298  1.000 40.28176 ? 550  TRP A N   1 
ATOM   2807 C  CA  . TRP A 1 347 ? 12.56663  32.59309 -5.44625  1.000 47.13966 ? 550  TRP A CA  1 
ATOM   2808 C  C   . TRP A 1 347 ? 13.98665  32.82208 -5.92967  1.000 54.59196 ? 550  TRP A C   1 
ATOM   2809 O  O   . TRP A 1 347 ? 14.74468  31.87469 -6.15676  1.000 52.21980 ? 550  TRP A O   1 
ATOM   2810 C  CB  . TRP A 1 347 ? 12.44119  32.87233 -3.94054  1.000 47.65641 ? 550  TRP A CB  1 
ATOM   2811 C  CG  . TRP A 1 347 ? 13.40428  32.13736 -3.06876  1.000 38.66728 ? 550  TRP A CG  1 
ATOM   2812 C  CD1 . TRP A 1 347 ? 14.58869  32.61287 -2.56687  1.000 47.66536 ? 550  TRP A CD1 1 
ATOM   2813 C  CD2 . TRP A 1 347 ? 13.26263  30.80075 -2.56068  1.000 43.13388 ? 550  TRP A CD2 1 
ATOM   2814 N  NE1 . TRP A 1 347 ? 15.19262  31.65479 -1.78538  1.000 51.94548 ? 550  TRP A NE1 1 
ATOM   2815 C  CE2 . TRP A 1 347 ? 14.40155  30.53238 -1.76570  1.000 47.43599 ? 550  TRP A CE2 1 
ATOM   2816 C  CE3 . TRP A 1 347 ? 12.28734  29.80775 -2.69951  1.000 40.53030 ? 550  TRP A CE3 1 
ATOM   2817 C  CZ2 . TRP A 1 347 ? 14.59373  29.30926 -1.12148  1.000 41.43628 ? 550  TRP A CZ2 1 
ATOM   2818 C  CZ3 . TRP A 1 347 ? 12.47513  28.58682 -2.04737  1.000 39.04306 ? 550  TRP A CZ3 1 
ATOM   2819 C  CH2 . TRP A 1 347 ? 13.61940  28.35036 -1.27166  1.000 38.04760 ? 550  TRP A CH2 1 
ATOM   2820 N  N   . GLN A 1 348 ? 14.32107  34.08938 -6.12084  1.000 55.45432 ? 551  GLN A N   1 
ATOM   2821 C  CA  . GLN A 1 348 ? 15.66412  34.47982 -6.50727  1.000 58.56979 ? 551  GLN A CA  1 
ATOM   2822 C  C   . GLN A 1 348 ? 16.43976  34.81891 -5.24285  1.000 65.05716 ? 551  GLN A C   1 
ATOM   2823 O  O   . GLN A 1 348 ? 15.92160  35.51051 -4.35844  1.000 71.16421 ? 551  GLN A O   1 
ATOM   2824 C  CB  . GLN A 1 348 ? 15.60427  35.66654 -7.46457  1.000 60.35572 ? 551  GLN A CB  1 
ATOM   2825 C  CG  . GLN A 1 348 ? 16.93580  36.15933 -7.94780  1.000 64.80081 ? 551  GLN A CG  1 
ATOM   2826 C  CD  . GLN A 1 348 ? 16.79752  37.46090 -8.71027  1.000 77.42411 ? 551  GLN A CD  1 
ATOM   2827 O  OE1 . GLN A 1 348 ? 17.09861  38.54273 -8.18757  1.000 72.64174 ? 551  GLN A OE1 1 
ATOM   2828 N  NE2 . GLN A 1 348 ? 16.31654  37.36858 -9.94965  1.000 70.77460 ? 551  GLN A NE2 1 
ATOM   2829 N  N   . GLY A 1 349 ? 17.65817  34.30147 -5.13610  1.000 73.46525 ? 552  GLY A N   1 
ATOM   2830 C  CA  . GLY A 1 349 ? 18.44380  34.51211 -3.93237  1.000 78.25286 ? 552  GLY A CA  1 
ATOM   2831 C  C   . GLY A 1 349 ? 19.92761  34.24999 -4.09267  1.000 84.60299 ? 552  GLY A C   1 
ATOM   2832 O  O   . GLY A 1 349 ? 20.62066  33.97936 -3.11128  1.000 85.42964 ? 552  GLY A O   1 
ATOM   2833 N  N   . ALA A 1 356 ? 21.00593  33.72801 -8.26750  1.000 78.27766 ? 559  ALA A N   1 
ATOM   2834 C  CA  . ALA A 1 356 ? 20.67385  32.30204 -8.25561  1.000 85.39254 ? 559  ALA A CA  1 
ATOM   2835 C  C   . ALA A 1 356 ? 19.18083  32.06154 -8.01223  1.000 81.03282 ? 559  ALA A C   1 
ATOM   2836 O  O   . ALA A 1 356 ? 18.57142  32.72389 -7.16893  1.000 85.03303 ? 559  ALA A O   1 
ATOM   2837 C  CB  . ALA A 1 356 ? 21.49914  31.57699 -7.19957  1.000 83.72584 ? 559  ALA A CB  1 
ATOM   2838 N  N   . GLN A 1 357 ? 18.59866  31.11590 -8.75230  1.000 61.60493 ? 560  GLN A N   1 
ATOM   2839 C  CA  . GLN A 1 357 ? 17.19847  30.73649 -8.59339  1.000 62.53362 ? 560  GLN A CA  1 
ATOM   2840 C  C   . GLN A 1 357 ? 17.11740  29.48384 -7.72880  1.000 52.13831 ? 560  GLN A C   1 
ATOM   2841 O  O   . GLN A 1 357 ? 17.68379  28.44808 -8.08722  1.000 60.35328 ? 560  GLN A O   1 
ATOM   2842 C  CB  . GLN A 1 357 ? 16.54144  30.48733 -9.95056  1.000 57.68384 ? 560  GLN A CB  1 
ATOM   2843 C  CG  . GLN A 1 357 ? 15.06240  30.08181 -9.87803  1.000 62.85799 ? 560  GLN A CG  1 
ATOM   2844 C  CD  . GLN A 1 357 ? 14.10885  31.27190 -9.98545  1.000 67.73895 ? 560  GLN A CD  1 
ATOM   2845 O  OE1 . GLN A 1 357 ? 13.39757  31.43056 -10.98476 1.000 66.27109 ? 560  GLN A OE1 1 
ATOM   2846 N  NE2 . GLN A 1 357 ? 14.09447  32.11490 -8.95478  1.000 66.93419 ? 560  GLN A NE2 1 
ATOM   2847 N  N   . HIS A 1 358 ? 16.41772  29.57661 -6.60061  1.000 47.79633 ? 561  HIS A N   1 
ATOM   2848 C  CA  . HIS A 1 358 ? 16.22468  28.44723 -5.70115  1.000 43.74948 ? 561  HIS A CA  1 
ATOM   2849 C  C   . HIS A 1 358 ? 14.83703  27.84938 -5.87919  1.000 45.09146 ? 561  HIS A C   1 
ATOM   2850 O  O   . HIS A 1 358 ? 13.92481  28.49216 -6.40246  1.000 43.68064 ? 561  HIS A O   1 
ATOM   2851 C  CB  . HIS A 1 358 ? 16.41999  28.87593 -4.25104  1.000 48.30416 ? 561  HIS A CB  1 
ATOM   2852 C  CG  . HIS A 1 358 ? 17.77587  29.43274 -3.98244  1.000 56.19693 ? 561  HIS A CG  1 
ATOM   2853 N  ND1 . HIS A 1 358 ? 17.98975  30.76255 -3.69221  1.000 59.33092 ? 561  HIS A ND1 1 
ATOM   2854 C  CD2 . HIS A 1 358 ? 18.99473  28.84596 -3.98693  1.000 60.13584 ? 561  HIS A CD2 1 
ATOM   2855 C  CE1 . HIS A 1 358 ? 19.28195  30.96938 -3.51510  1.000 65.06490 ? 561  HIS A CE1 1 
ATOM   2856 N  NE2 . HIS A 1 358 ? 19.91388  29.82216 -3.68740  1.000 66.57008 ? 561  HIS A NE2 1 
ATOM   2857 N  N   . ALA A 1 359 ? 14.68347  26.60300 -5.42390  1.000 42.20168 ? 562  ALA A N   1 
ATOM   2858 C  CA  . ALA A 1 359 ? 13.44182  25.87331 -5.62453  1.000 29.70405 ? 562  ALA A CA  1 
ATOM   2859 C  C   . ALA A 1 359 ? 13.29995  24.78751 -4.56545  1.000 29.02880 ? 562  ALA A C   1 
ATOM   2860 O  O   . ALA A 1 359 ? 14.27118  24.10482 -4.24350  1.000 26.77809 ? 562  ALA A O   1 
ATOM   2861 C  CB  . ALA A 1 359 ? 13.38746  25.25335 -7.02319  1.000 30.67279 ? 562  ALA A CB  1 
ATOM   2862 N  N   . VAL A 1 360 ? 12.08224  24.63031 -4.04010  1.000 23.99366 ? 563  VAL A N   1 
ATOM   2863 C  CA  . VAL A 1 360 ? 11.72299  23.53062 -3.14214  1.000 21.48036 ? 563  VAL A CA  1 
ATOM   2864 C  C   . VAL A 1 360 ? 10.34439  23.03248 -3.55353  1.000 25.97900 ? 563  VAL A C   1 
ATOM   2865 O  O   . VAL A 1 360 ? 9.64180   23.66482 -4.34633  1.000 27.74243 ? 563  VAL A O   1 
ATOM   2866 C  CB  . VAL A 1 360 ? 11.72850  23.92382 -1.63968  1.000 23.96153 ? 563  VAL A CB  1 
ATOM   2867 C  CG1 . VAL A 1 360 ? 13.12314  24.32656 -1.18026  1.000 26.64193 ? 563  VAL A CG1 1 
ATOM   2868 C  CG2 . VAL A 1 360 ? 10.73307  25.05813 -1.33752  1.000 21.90534 ? 563  VAL A CG2 1 
ATOM   2869 N  N   . THR A 1 361 ? 9.96423   21.87901 -3.01134  1.000 21.79631 ? 564  THR A N   1 
ATOM   2870 C  CA  . THR A 1 361 ? 8.65214   21.29710 -3.24140  1.000 21.36731 ? 564  THR A CA  1 
ATOM   2871 C  C   . THR A 1 361 ? 7.78080   21.51740 -2.01346  1.000 26.14627 ? 564  THR A C   1 
ATOM   2872 O  O   . THR A 1 361 ? 8.24718   21.39157 -0.87919  1.000 23.94072 ? 564  THR A O   1 
ATOM   2873 C  CB  . THR A 1 361 ? 8.76348   19.78629 -3.51165  1.000 24.37569 ? 564  THR A CB  1 
ATOM   2874 O  OG1 . THR A 1 361 ? 9.88777   19.51200 -4.35685  1.000 22.68261 ? 564  THR A OG1 1 
ATOM   2875 C  CG2 . THR A 1 361 ? 7.50774   19.26190 -4.14885  1.000 22.83720 ? 564  THR A CG2 1 
ATOM   2876 N  N   . CYS A 1 362 ? 6.50460   21.79346 -2.22992  1.000 24.01560 ? 565  CYS A N   1 
ATOM   2877 C  CA  . CYS A 1 362 ? 5.57058   21.96843 -1.12453  1.000 24.79146 ? 565  CYS A CA  1 
ATOM   2878 C  C   . CYS A 1 362 ? 4.47427   20.92744 -1.25772  1.000 24.83915 ? 565  CYS A C   1 
ATOM   2879 O  O   . CYS A 1 362 ? 3.87476   20.79551 -2.32959  1.000 26.47463 ? 565  CYS A O   1 
ATOM   2880 C  CB  . CYS A 1 362 ? 4.97611   23.38306 -1.11031  1.000 23.28810 ? 565  CYS A CB  1 
ATOM   2881 S  SG  . CYS A 1 362 ? 3.63135   23.61022 0.04147   1.000 27.08788 ? 565  CYS A SG  1 
ATOM   2882 N  N   . TRP A 1 363 ? 4.22866   20.17668 -0.18283  1.000 19.23539 ? 566  TRP A N   1 
ATOM   2883 C  CA  . TRP A 1 363 ? 3.24548   19.09985 -0.20949  1.000 17.13326 ? 566  TRP A CA  1 
ATOM   2884 C  C   . TRP A 1 363 ? 1.99567   19.40971 0.59824   1.000 22.10777 ? 566  TRP A C   1 
ATOM   2885 O  O   . TRP A 1 363 ? 1.04420   18.61777 0.56683   1.000 21.59483 ? 566  TRP A O   1 
ATOM   2886 C  CB  . TRP A 1 363 ? 3.87925   17.79432 0.29056   1.000 18.76027 ? 566  TRP A CB  1 
ATOM   2887 C  CG  . TRP A 1 363 ? 4.88230   17.21281 -0.67730  1.000 18.92865 ? 566  TRP A CG  1 
ATOM   2888 C  CD1 . TRP A 1 363 ? 6.21606   17.11283 -0.49569  1.000 21.46068 ? 566  TRP A CD1 1 
ATOM   2889 C  CD2 . TRP A 1 363 ? 4.61283   16.67390 -1.97383  1.000 18.25010 ? 566  TRP A CD2 1 
ATOM   2890 N  NE1 . TRP A 1 363 ? 6.80345   16.52959 -1.57983  1.000 19.15807 ? 566  TRP A NE1 1 
ATOM   2891 C  CE2 . TRP A 1 363 ? 5.83703   16.24815 -2.50777  1.000 19.32800 ? 566  TRP A CE2 1 
ATOM   2892 C  CE3 . TRP A 1 363 ? 3.45364   16.51132 -2.73434  1.000 21.85036 ? 566  TRP A CE3 1 
ATOM   2893 C  CZ2 . TRP A 1 363 ? 5.94354   15.66951 -3.76996  1.000 19.32696 ? 566  TRP A CZ2 1 
ATOM   2894 C  CZ3 . TRP A 1 363 ? 3.55702   15.93187 -3.98614  1.000 21.72908 ? 566  TRP A CZ3 1 
ATOM   2895 C  CH2 . TRP A 1 363 ? 4.79842   15.51853 -4.49057  1.000 22.36373 ? 566  TRP A CH2 1 
ATOM   2896 N  N   . GLY A 1 364 ? 1.95702   20.53733 1.30394   1.000 19.23819 ? 567  GLY A N   1 
ATOM   2897 C  CA  . GLY A 1 364 ? 0.73338   20.91879 1.98750   1.000 21.00982 ? 567  GLY A CA  1 
ATOM   2898 C  C   . GLY A 1 364 ? 0.92542   22.18267 2.79472   1.000 24.73422 ? 567  GLY A C   1 
ATOM   2899 O  O   . GLY A 1 364 ? 2.02067   22.74963 2.85225   1.000 22.58594 ? 567  GLY A O   1 
ATOM   2900 N  N   . ALA A 1 365 ? -0.17060  22.61105 3.43097   1.000 22.01489 ? 568  ALA A N   1 
ATOM   2901 C  CA  . ALA A 1 365 ? -0.18940  23.85405 4.18228   1.000 27.55935 ? 568  ALA A CA  1 
ATOM   2902 C  C   . ALA A 1 365 ? -1.11742  23.73154 5.38417   1.000 26.48958 ? 568  ALA A C   1 
ATOM   2903 O  O   . ALA A 1 365 ? -2.10879  22.99170 5.35494   1.000 23.35059 ? 568  ALA A O   1 
ATOM   2904 C  CB  . ALA A 1 365 ? -0.62063  25.03796 3.30257   1.000 27.98398 ? 568  ALA A CB  1 
ATOM   2905 N  N   . ALA A 1 366 ? -0.76791  24.46521 6.44193   1.000 26.13650 ? 569  ALA A N   1 
ATOM   2906 C  CA  . ALA A 1 366 ? -1.57480  24.62249 7.64254   1.000 27.57733 ? 569  ALA A CA  1 
ATOM   2907 C  C   . ALA A 1 366 ? -2.34074  25.94496 7.60667   1.000 28.12249 ? 569  ALA A C   1 
ATOM   2908 O  O   . ALA A 1 366 ? -1.86792  26.94582 7.06324   1.000 28.46955 ? 569  ALA A O   1 
ATOM   2909 C  CB  . ALA A 1 366 ? -0.69728  24.57132 8.89514   1.000 27.59160 ? 569  ALA A CB  1 
ATOM   2910 N  N   . TYR A 1 367 ? -3.53783  25.93445 8.19073   1.000 24.15433 ? 570  TYR A N   1 
ATOM   2911 C  CA  . TYR A 1 367 ? -4.41478  27.09215 8.22986   1.000 27.26438 ? 570  TYR A CA  1 
ATOM   2912 C  C   . TYR A 1 367 ? -4.93046  27.31323 9.64427   1.000 31.81025 ? 570  TYR A C   1 
ATOM   2913 O  O   . TYR A 1 367 ? -5.20750  26.35458 10.37464  1.000 27.40632 ? 570  TYR A O   1 
ATOM   2914 C  CB  . TYR A 1 367 ? -5.63271  26.93278 7.31887   1.000 27.88763 ? 570  TYR A CB  1 
ATOM   2915 C  CG  . TYR A 1 367 ? -5.33980  26.71497 5.85389   1.000 29.52115 ? 570  TYR A CG  1 
ATOM   2916 C  CD1 . TYR A 1 367 ? -4.81441  25.51030 5.40354   1.000 28.47617 ? 570  TYR A CD1 1 
ATOM   2917 C  CD2 . TYR A 1 367 ? -5.64539  27.69985 4.91246   1.000 28.60963 ? 570  TYR A CD2 1 
ATOM   2918 C  CE1 . TYR A 1 367 ? -4.56106  25.30165 4.05993   1.000 30.53422 ? 570  TYR A CE1 1 
ATOM   2919 C  CE2 . TYR A 1 367 ? -5.40653  27.49721 3.56192   1.000 31.50197 ? 570  TYR A CE2 1 
ATOM   2920 C  CZ  . TYR A 1 367 ? -4.86535  26.29837 3.14945   1.000 35.13282 ? 570  TYR A CZ  1 
ATOM   2921 O  OH  . TYR A 1 367 ? -4.62436  26.09110 1.81873   1.000 36.86862 ? 570  TYR A OH  1 
ATOM   2922 N  N   . ASP A 1 368 ? -5.11031  28.58922 10.00381  1.000 29.09464 ? 571  ASP A N   1 
ATOM   2923 C  CA  . ASP A 1 368 ? -5.79200  28.94228 11.24151  1.000 31.12604 ? 571  ASP A CA  1 
ATOM   2924 C  C   . ASP A 1 368 ? -7.29482  29.03418 10.97656  1.000 37.40291 ? 571  ASP A C   1 
ATOM   2925 O  O   . ASP A 1 368 ? -7.76192  28.90003 9.84076   1.000 35.21253 ? 571  ASP A O   1 
ATOM   2926 C  CB  . ASP A 1 368 ? -5.23381  30.24800 11.83210  1.000 33.26980 ? 571  ASP A CB  1 
ATOM   2927 C  CG  . ASP A 1 368 ? -5.52726  31.48566 10.97297  1.000 36.29185 ? 571  ASP A CG  1 
ATOM   2928 O  OD1 . ASP A 1 368 ? -6.39549  31.44563 10.06844  1.000 36.87088 ? 571  ASP A OD1 1 
ATOM   2929 O  OD2 . ASP A 1 368 ? -4.86440  32.52733 11.20441  1.000 37.46383 ? 571  ASP A OD2 1 
ATOM   2930 N  N   . GLU A 1 369 ? -8.05573  29.30883 12.03757  1.000 34.61208 ? 572  GLU A N   1 
ATOM   2931 C  CA  . GLU A 1 369 ? -9.51154  29.32839 11.96226  1.000 36.95018 ? 572  GLU A CA  1 
ATOM   2932 C  C   . GLU A 1 369 ? -10.04593 30.46679 11.10393  1.000 37.15119 ? 572  GLU A C   1 
ATOM   2933 O  O   . GLU A 1 369 ? -11.21933 30.42412 10.72149  1.000 46.47508 ? 572  GLU A O   1 
ATOM   2934 C  CB  . GLU A 1 369 ? -10.11281 29.41613 13.37359  1.000 33.32419 ? 572  GLU A CB  1 
ATOM   2935 C  CG  . GLU A 1 369 ? -9.75959  28.24665 14.28419  1.000 37.88067 ? 572  GLU A CG  1 
ATOM   2936 C  CD  . GLU A 1 369 ? -10.06650 28.52413 15.75310  1.000 45.13912 ? 572  GLU A CD  1 
ATOM   2937 O  OE1 . GLU A 1 369 ? -11.26060 28.68854 16.09951  1.000 44.53560 ? 572  GLU A OE1 1 
ATOM   2938 O  OE2 . GLU A 1 369 ? -9.10881  28.58563 16.56106  1.000 42.74270 ? 572  GLU A OE2 1 
ATOM   2939 N  N   . ASP A 1 370 ? -9.23529  31.48811 10.81408  1.000 37.33822 ? 573  ASP A N   1 
ATOM   2940 C  CA  . ASP A 1 370 ? -9.60307  32.52202 9.84951   1.000 34.49991 ? 573  ASP A CA  1 
ATOM   2941 C  C   . ASP A 1 370 ? -9.21969  32.14230 8.42272   1.000 38.33628 ? 573  ASP A C   1 
ATOM   2942 O  O   . ASP A 1 370 ? -9.43963  32.93777 7.49892   1.000 34.87710 ? 573  ASP A O   1 
ATOM   2943 C  CB  . ASP A 1 370 ? -8.94693  33.86435 10.20952  1.000 34.11831 ? 573  ASP A CB  1 
ATOM   2944 C  CG  . ASP A 1 370 ? -9.57933  34.52758 11.43758  1.000 44.06953 ? 573  ASP A CG  1 
ATOM   2945 O  OD1 . ASP A 1 370 ? -10.59937 34.01668 11.95647  1.000 42.43360 ? 573  ASP A OD1 1 
ATOM   2946 O  OD2 . ASP A 1 370 ? -9.05221  35.57160 11.88351  1.000 44.32314 ? 573  ASP A OD2 1 
ATOM   2947 N  N   . ASN A 1 371 ? -8.63418  30.95938 8.23809   1.000 33.67722 ? 574  ASN A N   1 
ATOM   2948 C  CA  . ASN A 1 371 ? -8.17040  30.42494 6.95711   1.000 37.39025 ? 574  ASN A CA  1 
ATOM   2949 C  C   . ASN A 1 371 ? -6.94459  31.14684 6.41990   1.000 38.62263 ? 574  ASN A C   1 
ATOM   2950 O  O   . ASN A 1 371 ? -6.68104  31.10110 5.20980   1.000 34.33363 ? 574  ASN A O   1 
ATOM   2951 C  CB  . ASN A 1 371 ? -9.27411  30.42247 5.89232   1.000 37.52266 ? 574  ASN A CB  1 
ATOM   2952 C  CG  . ASN A 1 371 ? -10.42108 29.51344 6.25154   1.000 40.07682 ? 574  ASN A CG  1 
ATOM   2953 O  OD1 . ASN A 1 371 ? -10.22780 28.46549 6.86661   1.000 44.15678 ? 574  ASN A OD1 1 
ATOM   2954 N  ND2 . ASN A 1 371 ? -11.62971 29.91212 5.88060   1.000 44.26560 ? 574  ASN A ND2 1 
ATOM   2955 N  N   . ASN A 1 372 ? -6.18262  31.81067 7.28660   1.000 34.83911 ? 575  ASN A N   1 
ATOM   2956 C  CA  . ASN A 1 372 ? -4.87081  32.29062 6.88160   1.000 35.10474 ? 575  ASN A CA  1 
ATOM   2957 C  C   . ASN A 1 372 ? -3.92683  31.10898 6.77364   1.000 33.42727 ? 575  ASN A C   1 
ATOM   2958 O  O   . ASN A 1 372 ? -4.00449  30.16477 7.56327   1.000 32.85529 ? 575  ASN A O   1 
ATOM   2959 C  CB  . ASN A 1 372 ? -4.31020  33.29598 7.88737   1.000 39.84671 ? 575  ASN A CB  1 
ATOM   2960 C  CG  . ASN A 1 372 ? -5.22081  34.48008 8.10612   1.000 38.64398 ? 575  ASN A CG  1 
ATOM   2961 O  OD1 . ASN A 1 372 ? -5.45879  35.27077 7.19172   1.000 38.16034 ? 575  ASN A OD1 1 
ATOM   2962 N  ND2 . ASN A 1 372 ? -5.71736  34.62962 9.33973   1.000 39.60586 ? 575  ASN A ND2 1 
ATOM   2963 N  N   . ILE A 1 373 ? -3.03148  31.14782 5.79459   1.000 30.81309 ? 576  ILE A N   1 
ATOM   2964 C  CA  . ILE A 1 373 ? -2.00985  30.11031 5.69546   1.000 27.73219 ? 576  ILE A CA  1 
ATOM   2965 C  C   . ILE A 1 373 ? -0.88915  30.44927 6.66601   1.000 27.76290 ? 576  ILE A C   1 
ATOM   2966 O  O   . ILE A 1 373 ? -0.34272  31.55640 6.63273   1.000 27.12450 ? 576  ILE A O   1 
ATOM   2967 C  CB  . ILE A 1 373 ? -1.48533  29.97663 4.25923   1.000 33.58337 ? 576  ILE A CB  1 
ATOM   2968 C  CG1 . ILE A 1 373 ? -2.61375  29.50092 3.33994   1.000 32.17124 ? 576  ILE A CG1 1 
ATOM   2969 C  CG2 . ILE A 1 373 ? -0.30013  29.01170 4.21314   1.000 27.63379 ? 576  ILE A CG2 1 
ATOM   2970 C  CD1 . ILE A 1 373 ? -2.24225  29.43711 1.85889   1.000 35.79874 ? 576  ILE A CD1 1 
ATOM   2971 N  N   . ILE A 1 374 ? -0.55653  29.50592 7.54658   1.000 28.24145 ? 577  ILE A N   1 
ATOM   2972 C  CA  . ILE A 1 374 ? 0.38985   29.77202 8.62291   1.000 24.98795 ? 577  ILE A CA  1 
ATOM   2973 C  C   . ILE A 1 374 ? 1.65518   28.93321 8.53104   1.000 31.78144 ? 577  ILE A C   1 
ATOM   2974 O  O   . ILE A 1 374 ? 2.67534   29.31111 9.13349   1.000 26.82331 ? 577  ILE A O   1 
ATOM   2975 C  CB  . ILE A 1 374 ? -0.27402  29.57800 10.00051  1.000 27.44165 ? 577  ILE A CB  1 
ATOM   2976 C  CG1 . ILE A 1 374 ? -0.66368  28.12099 10.22949  1.000 28.25338 ? 577  ILE A CG1 1 
ATOM   2977 C  CG2 . ILE A 1 374 ? -1.50539  30.44207 10.12986  1.000 28.37191 ? 577  ILE A CG2 1 
ATOM   2978 C  CD1 . ILE A 1 374 ? -1.38306  27.93655 11.55075  1.000 28.96191 ? 577  ILE A CD1 1 
ATOM   2979 N  N   . CYS A 1 375 ? 1.64627   27.82446 7.79517   1.000 25.11345 ? 578  CYS A N   1 
ATOM   2980 C  CA  . CYS A 1 375 ? 2.82079   26.97879 7.67856   1.000 24.80077 ? 578  CYS A CA  1 
ATOM   2981 C  C   . CYS A 1 375 ? 2.73684   26.19371 6.37643   1.000 29.52460 ? 578  CYS A C   1 
ATOM   2982 O  O   . CYS A 1 375 ? 1.64434   25.84988 5.91327   1.000 28.74023 ? 578  CYS A O   1 
ATOM   2983 C  CB  . CYS A 1 375 ? 2.92754   26.03858 8.88563   1.000 26.40251 ? 578  CYS A CB  1 
ATOM   2984 S  SG  . CYS A 1 375 ? 4.53038   25.24032 9.12299   1.000 27.87522 ? 578  CYS A SG  1 
ATOM   2985 N  N   . LEU A 1 376 ? 3.90406   25.93171 5.78726   1.000 31.03897 ? 579  LEU A N   1 
ATOM   2986 C  CA  . LEU A 1 376 ? 4.04880   25.06958 4.62263   1.000 25.92177 ? 579  LEU A CA  1 
ATOM   2987 C  C   . LEU A 1 376 ? 4.88126   23.85729 5.00592   1.000 24.72933 ? 579  LEU A C   1 
ATOM   2988 O  O   . LEU A 1 376 ? 5.72926   23.93736 5.89435   1.000 23.63646 ? 579  LEU A O   1 
ATOM   2989 C  CB  . LEU A 1 376 ? 4.72793   25.79917 3.45418   1.000 22.39831 ? 579  LEU A CB  1 
ATOM   2990 C  CG  . LEU A 1 376 ? 3.98573   27.03511 2.94536   1.000 29.91479 ? 579  LEU A CG  1 
ATOM   2991 C  CD1 . LEU A 1 376 ? 4.74783   27.67870 1.80203   1.000 29.33268 ? 579  LEU A CD1 1 
ATOM   2992 C  CD2 . LEU A 1 376 ? 2.57335   26.66327 2.50095   1.000 26.79513 ? 579  LEU A CD2 1 
ATOM   2993 N  N   . TYR A 1 377 ? 4.64848   22.73791 4.32077   1.000 23.04337 ? 580  TYR A N   1 
ATOM   2994 C  CA  . TYR A 1 377 ? 5.38234   21.49815 4.56846   1.000 23.16458 ? 580  TYR A CA  1 
ATOM   2995 C  C   . TYR A 1 377 ? 6.20168   21.19992 3.32307   1.000 23.43473 ? 580  TYR A C   1 
ATOM   2996 O  O   . TYR A 1 377 ? 5.64345   20.94992 2.24797   1.000 22.21479 ? 580  TYR A O   1 
ATOM   2997 C  CB  . TYR A 1 377 ? 4.42228   20.36714 4.97034   1.000 19.84245 ? 580  TYR A CB  1 
ATOM   2998 C  CG  . TYR A 1 377 ? 3.74422   20.77733 6.25690   1.000 20.82779 ? 580  TYR A CG  1 
ATOM   2999 C  CD1 . TYR A 1 377 ? 4.35868   20.55979 7.48453   1.000 19.94191 ? 580  TYR A CD1 1 
ATOM   3000 C  CD2 . TYR A 1 377 ? 2.55672   21.49693 6.23979   1.000 23.89414 ? 580  TYR A CD2 1 
ATOM   3001 C  CE1 . TYR A 1 377 ? 3.76479   20.99500 8.67089   1.000 23.94990 ? 580  TYR A CE1 1 
ATOM   3002 C  CE2 . TYR A 1 377 ? 1.96357   21.94556 7.41862   1.000 23.48451 ? 580  TYR A CE2 1 
ATOM   3003 C  CZ  . TYR A 1 377 ? 2.57112   21.69070 8.62667   1.000 25.67917 ? 580  TYR A CZ  1 
ATOM   3004 O  OH  . TYR A 1 377 ? 1.99184   22.15998 9.78632   1.000 23.75781 ? 580  TYR A OH  1 
ATOM   3005 N  N   . ILE A 1 378 ? 7.52343   21.24291 3.47860   1.000 21.44588 ? 581  ILE A N   1 
ATOM   3006 C  CA  . ILE A 1 378 ? 8.47093   21.44756 2.38875   1.000 21.09866 ? 581  ILE A CA  1 
ATOM   3007 C  C   . ILE A 1 378 ? 9.38139   20.22734 2.26080   1.000 25.42071 ? 581  ILE A C   1 
ATOM   3008 O  O   . ILE A 1 378 ? 9.97917   19.78894 3.24775   1.000 22.33403 ? 581  ILE A O   1 
ATOM   3009 C  CB  . ILE A 1 378 ? 9.32571   22.70509 2.63920   1.000 24.53479 ? 581  ILE A CB  1 
ATOM   3010 C  CG1 . ILE A 1 378 ? 8.46527   23.97691 2.73346   1.000 20.96171 ? 581  ILE A CG1 1 
ATOM   3011 C  CG2 . ILE A 1 378 ? 10.47775  22.80284 1.62553   1.000 21.15952 ? 581  ILE A CG2 1 
ATOM   3012 C  CD1 . ILE A 1 378 ? 7.63221   24.27442 1.49599   1.000 22.67518 ? 581  ILE A CD1 1 
ATOM   3013 N  N   . ALA A 1 379 ? 9.53119   19.70915 1.04287   1.000 20.14794 ? 582  ALA A N   1 
ATOM   3014 C  CA  . ALA A 1 379 ? 10.65805  18.83911 0.73832   1.000 19.04630 ? 582  ALA A CA  1 
ATOM   3015 C  C   . ALA A 1 379 ? 11.80965  19.73216 0.29182   1.000 25.15848 ? 582  ALA A C   1 
ATOM   3016 O  O   . ALA A 1 379 ? 11.71780  20.41895 -0.73516  1.000 24.79397 ? 582  ALA A O   1 
ATOM   3017 C  CB  . ALA A 1 379 ? 10.30089  17.80349 -0.32880  1.000 21.92500 ? 582  ALA A CB  1 
ATOM   3018 N  N   . GLU A 1 380 ? 12.88555  19.72120 1.06063   1.000 26.05375 ? 583  GLU A N   1 
ATOM   3019 C  CA  . GLU A 1 380 ? 14.01299  20.62793 0.89007   1.000 27.05913 ? 583  GLU A CA  1 
ATOM   3020 C  C   . GLU A 1 380 ? 15.22331  19.76116 0.56113   1.000 29.33298 ? 583  GLU A C   1 
ATOM   3021 O  O   . GLU A 1 380 ? 15.81164  19.14830 1.45616   1.000 33.47318 ? 583  GLU A O   1 
ATOM   3022 C  CB  . GLU A 1 380 ? 14.23892  21.45641 2.16459   1.000 25.97551 ? 583  GLU A CB  1 
ATOM   3023 C  CG  . GLU A 1 380 ? 14.57322  22.93900 1.95978   1.000 30.30299 ? 583  GLU A CG  1 
ATOM   3024 C  CD  . GLU A 1 380 ? 15.90106  23.18897 1.24461   1.000 35.91250 ? 583  GLU A CD  1 
ATOM   3025 O  OE1 . GLU A 1 380 ? 16.26001  22.42861 0.30936   1.000 36.14060 ? 583  GLU A OE1 1 
ATOM   3026 O  OE2 . GLU A 1 380 ? 16.58809  24.17313 1.60980   1.000 41.54574 ? 583  GLU A OE2 1 
ATOM   3027 N  N   . SER A 1 381 ? 15.60679  19.71023 -0.71552  1.000 29.38532 ? 584  SER A N   1 
ATOM   3028 C  CA  . SER A 1 381 ? 16.62478  18.75074 -1.14010  1.000 28.79465 ? 584  SER A CA  1 
ATOM   3029 C  C   . SER A 1 381 ? 17.98775  19.04831 -0.53150  1.000 34.87933 ? 584  SER A C   1 
ATOM   3030 O  O   . SER A 1 381 ? 18.87986  18.19121 -0.58538  1.000 29.35354 ? 584  SER A O   1 
ATOM   3031 C  CB  . SER A 1 381 ? 16.73476  18.73848 -2.66879  1.000 25.98150 ? 584  SER A CB  1 
ATOM   3032 O  OG  . SER A 1 381 ? 17.29364  19.95905 -3.14111  1.000 30.47328 ? 584  SER A OG  1 
ATOM   3033 N  N   . ASN A 1 382 ? 18.17304  20.25007 0.02492   1.000 31.90934 ? 585  ASN A N   1 
ATOM   3034 C  CA  . ASN A 1 382 ? 19.40023  20.59518 0.72799   1.000 32.65994 ? 585  ASN A CA  1 
ATOM   3035 C  C   . ASN A 1 382 ? 19.41476  20.14342 2.18375   1.000 35.39427 ? 585  ASN A C   1 
ATOM   3036 O  O   . ASN A 1 382 ? 20.48380  20.12460 2.79800   1.000 33.69593 ? 585  ASN A O   1 
ATOM   3037 C  CB  . ASN A 1 382 ? 19.61112  22.10221 0.68751   1.000 34.30188 ? 585  ASN A CB  1 
ATOM   3038 C  CG  . ASN A 1 382 ? 20.54997  22.51214 -0.39481  1.000 47.59604 ? 585  ASN A CG  1 
ATOM   3039 O  OD1 . ASN A 1 382 ? 21.66084  21.99759 -0.48709  1.000 54.97298 ? 585  ASN A OD1 1 
ATOM   3040 N  ND2 . ASN A 1 382 ? 20.11135  23.43389 -1.24316  1.000 58.88387 ? 585  ASN A ND2 1 
ATOM   3041 N  N   . LEU A 1 383 ? 18.29690  19.82216 2.74064   1.000 32.47562 ? 586  LEU A N   1 
ATOM   3042 C  CA  . LEU A 1 383 ? 18.34635  19.49402 4.15839   1.000 28.16547 ? 586  LEU A CA  1 
ATOM   3043 C  C   . LEU A 1 383 ? 18.53348  17.98683 4.35426   1.000 32.93057 ? 586  LEU A C   1 
ATOM   3044 O  O   . LEU A 1 383 ? 18.17099  17.18281 3.47990   1.000 33.15802 ? 586  LEU A O   1 
ATOM   3045 C  CB  . LEU A 1 383 ? 17.07324  19.97735 4.85172   1.000 31.76099 ? 586  LEU A CB  1 
ATOM   3046 C  CG  . LEU A 1 383 ? 16.88848  21.50364 4.78725   1.000 35.04995 ? 586  LEU A CG  1 
ATOM   3047 C  CD1 . LEU A 1 383 ? 15.60228  21.94647 5.47237   1.000 32.31567 ? 586  LEU A CD1 1 
ATOM   3048 C  CD2 . LEU A 1 383 ? 18.08293  22.21845 5.38627   1.000 35.77562 ? 586  LEU A CD2 1 
ATOM   3049 N  N   . PRO A 1 384 ? 19.12367  17.57063 5.48450   1.000 36.14175 ? 587  PRO A N   1 
ATOM   3050 C  CA  . PRO A 1 384 ? 19.62776  16.19283 5.58153   1.000 31.05547 ? 587  PRO A CA  1 
ATOM   3051 C  C   . PRO A 1 384 ? 18.58134  15.12603 5.87957   1.000 30.41788 ? 587  PRO A C   1 
ATOM   3052 O  O   . PRO A 1 384 ? 18.71629  13.99129 5.41517   1.000 33.47935 ? 587  PRO A O   1 
ATOM   3053 C  CB  . PRO A 1 384 ? 20.65116  16.28888 6.71764   1.000 34.78628 ? 587  PRO A CB  1 
ATOM   3054 C  CG  . PRO A 1 384 ? 20.14115  17.38888 7.56743   1.000 37.12949 ? 587  PRO A CG  1 
ATOM   3055 C  CD  . PRO A 1 384 ? 19.55170  18.39677 6.62688   1.000 30.59200 ? 587  PRO A CD  1 
ATOM   3056 N  N   . GLU A 1 385 ? 17.55432  15.44385 6.65726   1.000 28.99071 ? 588  GLU A N   1 
ATOM   3057 C  CA  . GLU A 1 385 ? 16.65618  14.40160 7.12670   1.000 24.64952 ? 588  GLU A CA  1 
ATOM   3058 C  C   . GLU A 1 385 ? 15.65699  13.99685 6.05608   1.000 28.02011 ? 588  GLU A C   1 
ATOM   3059 O  O   . GLU A 1 385 ? 15.24087  14.80401 5.21893   1.000 27.87636 ? 588  GLU A O   1 
ATOM   3060 C  CB  . GLU A 1 385 ? 15.91658  14.85834 8.38447   1.000 30.06385 ? 588  GLU A CB  1 
ATOM   3061 C  CG  . GLU A 1 385 ? 16.81690  14.92212 9.60932   1.000 34.32168 ? 588  GLU A CG  1 
ATOM   3062 C  CD  . GLU A 1 385 ? 16.10625  15.43100 10.86004  1.000 42.50967 ? 588  GLU A CD  1 
ATOM   3063 O  OE1 . GLU A 1 385 ? 15.01227  14.92010 11.18449  1.000 43.64295 ? 588  GLU A OE1 1 
ATOM   3064 O  OE2 . GLU A 1 385 ? 16.65422  16.34254 11.52112  1.000 52.51311 ? 588  GLU A OE2 1 
ATOM   3065 N  N   . ALA A 1 386 ? 15.26711  12.72302 6.10166   1.000 25.48110 ? 589  ALA A N   1 
ATOM   3066 C  CA  . ALA A 1 386 ? 14.27867  12.14393 5.18792   1.000 25.11848 ? 589  ALA A CA  1 
ATOM   3067 C  C   . ALA A 1 386 ? 12.87361  12.45519 5.70880   1.000 27.13391 ? 589  ALA A C   1 
ATOM   3068 O  O   . ALA A 1 386 ? 12.11274  11.58864 6.14959   1.000 25.58473 ? 589  ALA A O   1 
ATOM   3069 C  CB  . ALA A 1 386 ? 14.50564  10.64488 5.05397   1.000 28.12621 ? 589  ALA A CB  1 
ATOM   3070 N  N   . VAL A 1 387 ? 12.54288  13.74307 5.68295   1.000 24.24957 ? 590  VAL A N   1 
ATOM   3071 C  CA  . VAL A 1 387 ? 11.28645  14.25509 6.21463   1.000 23.78377 ? 590  VAL A CA  1 
ATOM   3072 C  C   . VAL A 1 387 ? 10.87374  15.43946 5.34922   1.000 22.96527 ? 590  VAL A C   1 
ATOM   3073 O  O   . VAL A 1 387 ? 11.67412  15.98780 4.59143   1.000 23.03046 ? 590  VAL A O   1 
ATOM   3074 C  CB  . VAL A 1 387 ? 11.40475  14.71081 7.69817   1.000 25.20905 ? 590  VAL A CB  1 
ATOM   3075 C  CG1 . VAL A 1 387 ? 12.02898  13.63651 8.60070   1.000 22.04653 ? 590  VAL A CG1 1 
ATOM   3076 C  CG2 . VAL A 1 387 ? 12.21048  16.01348 7.79755   1.000 24.07128 ? 590  VAL A CG2 1 
ATOM   3077 N  N   . LEU A 1 388 ? 9.62529   15.86189 5.48915   1.000 23.54436 ? 591  LEU A N   1 
ATOM   3078 C  CA  . LEU A 1 388 ? 9.23955   17.21452 5.10681   1.000 21.88813 ? 591  LEU A CA  1 
ATOM   3079 C  C   . LEU A 1 388 ? 9.42257   18.14810 6.29519   1.000 25.25693 ? 591  LEU A C   1 
ATOM   3080 O  O   . LEU A 1 388 ? 9.06310   17.80109 7.42064   1.000 24.96408 ? 591  LEU A O   1 
ATOM   3081 C  CB  . LEU A 1 388 ? 7.78842   17.25123 4.64921   1.000 21.25613 ? 591  LEU A CB  1 
ATOM   3082 C  CG  . LEU A 1 388 ? 7.41917   16.24663 3.55676   1.000 23.93440 ? 591  LEU A CG  1 
ATOM   3083 C  CD1 . LEU A 1 388 ? 5.99180   16.49074 3.15118   1.000 21.67431 ? 591  LEU A CD1 1 
ATOM   3084 C  CD2 . LEU A 1 388 ? 8.38000   16.37936 2.36298   1.000 20.61326 ? 591  LEU A CD2 1 
ATOM   3085 N  N   . TYR A 1 389 ? 9.97128   19.34134 6.04087   1.000 24.96372 ? 592  TYR A N   1 
ATOM   3086 C  CA  . TYR A 1 389 ? 10.22118  20.29709 7.11896   1.000 22.84680 ? 592  TYR A CA  1 
ATOM   3087 C  C   . TYR A 1 389 ? 9.14377   21.37480 7.15226   1.000 24.18654 ? 592  TYR A C   1 
ATOM   3088 O  O   . TYR A 1 389 ? 8.63885   21.78987 6.08978   1.000 22.63670 ? 592  TYR A O   1 
ATOM   3089 C  CB  . TYR A 1 389 ? 11.56899  20.98299 6.93691   1.000 23.70805 ? 592  TYR A CB  1 
ATOM   3090 C  CG  . TYR A 1 389 ? 12.80547  20.14170 7.17043   1.000 25.51084 ? 592  TYR A CG  1 
ATOM   3091 C  CD1 . TYR A 1 389 ? 13.25007  19.22739 6.21567   1.000 27.84109 ? 592  TYR A CD1 1 
ATOM   3092 C  CD2 . TYR A 1 389 ? 13.57014  20.31610 8.31810   1.000 28.66421 ? 592  TYR A CD2 1 
ATOM   3093 C  CE1 . TYR A 1 389 ? 14.40479  18.49074 6.41844   1.000 22.90556 ? 592  TYR A CE1 1 
ATOM   3094 C  CE2 . TYR A 1 389 ? 14.72792  19.59158 8.52740   1.000 30.63467 ? 592  TYR A CE2 1 
ATOM   3095 C  CZ  . TYR A 1 389 ? 15.13585  18.67835 7.58171   1.000 29.56497 ? 592  TYR A CZ  1 
ATOM   3096 O  OH  . TYR A 1 389 ? 16.28653  17.95942 7.80545   1.000 32.38402 ? 592  TYR A OH  1 
ATOM   3097 N  N   . PRO A 1 390 ? 8.76876   21.87306 8.33118   1.000 22.95922 ? 593  PRO A N   1 
ATOM   3098 C  CA  . PRO A 1 390 ? 7.79646   22.97377 8.38277   1.000 23.24018 ? 593  PRO A CA  1 
ATOM   3099 C  C   . PRO A 1 390 ? 8.48102   24.31995 8.16718   1.000 21.60487 ? 593  PRO A C   1 
ATOM   3100 O  O   . PRO A 1 390 ? 9.54761   24.59783 8.71805   1.000 25.53493 ? 593  PRO A O   1 
ATOM   3101 C  CB  . PRO A 1 390 ? 7.20022   22.85618 9.79844   1.000 22.51685 ? 593  PRO A CB  1 
ATOM   3102 C  CG  . PRO A 1 390 ? 8.32012   22.31560 10.61309  1.000 24.46067 ? 593  PRO A CG  1 
ATOM   3103 C  CD  . PRO A 1 390 ? 9.16937   21.42949 9.68230   1.000 23.90825 ? 593  PRO A CD  1 
ATOM   3104 N  N   . PHE A 1 391 ? 7.86912   25.14593 7.32608   1.000 26.04777 ? 594  PHE A N   1 
ATOM   3105 C  CA  . PHE A 1 391 ? 8.31577   26.51632 7.06950   1.000 28.41767 ? 594  PHE A CA  1 
ATOM   3106 C  C   . PHE A 1 391 ? 7.17489   27.43687 7.46438   1.000 27.78156 ? 594  PHE A C   1 
ATOM   3107 O  O   . PHE A 1 391 ? 6.13162   27.45218 6.80069   1.000 23.86196 ? 594  PHE A O   1 
ATOM   3108 C  CB  . PHE A 1 391 ? 8.70143   26.73821 5.60095   1.000 27.28476 ? 594  PHE A CB  1 
ATOM   3109 C  CG  . PHE A 1 391 ? 10.09695  26.29053 5.26458   1.000 26.58941 ? 594  PHE A CG  1 
ATOM   3110 C  CD1 . PHE A 1 391 ? 10.45128  24.94334 5.35806   1.000 26.47451 ? 594  PHE A CD1 1 
ATOM   3111 C  CD2 . PHE A 1 391 ? 11.05470  27.20728 4.84860   1.000 30.02357 ? 594  PHE A CD2 1 
ATOM   3112 C  CE1 . PHE A 1 391 ? 11.72954  24.52640 5.04989   1.000 26.36093 ? 594  PHE A CE1 1 
ATOM   3113 C  CE2 . PHE A 1 391 ? 12.34276  26.79969 4.53418   1.000 30.27406 ? 594  PHE A CE2 1 
ATOM   3114 C  CZ  . PHE A 1 391 ? 12.68289  25.45309 4.63220   1.000 36.39953 ? 594  PHE A CZ  1 
ATOM   3115 N  N   . GLY A 1 392 ? 7.37214   28.19623 8.54164   1.000 26.22136 ? 595  GLY A N   1 
ATOM   3116 C  CA  . GLY A 1 392 ? 6.35545   29.14231 8.96052   1.000 32.36617 ? 595  GLY A CA  1 
ATOM   3117 C  C   . GLY A 1 392 ? 6.13997   30.21549 7.91103   1.000 33.54546 ? 595  GLY A C   1 
ATOM   3118 O  O   . GLY A 1 392 ? 7.06313   30.61580 7.20273   1.000 32.46904 ? 595  GLY A O   1 
ATOM   3119 N  N   . VAL A 1 393 ? 4.89700   30.67059 7.79308   1.000 27.59510 ? 596  VAL A N   1 
ATOM   3120 C  CA  . VAL A 1 393 ? 4.52581   31.69347 6.81961   1.000 31.24919 ? 596  VAL A CA  1 
ATOM   3121 C  C   . VAL A 1 393 ? 4.17897   32.96260 7.57735   1.000 30.71065 ? 596  VAL A C   1 
ATOM   3122 O  O   . VAL A 1 393 ? 3.45317   32.92047 8.57868   1.000 35.39978 ? 596  VAL A O   1 
ATOM   3123 C  CB  . VAL A 1 393 ? 3.35309   31.25672 5.92274   1.000 28.28937 ? 596  VAL A CB  1 
ATOM   3124 C  CG1 . VAL A 1 393 ? 3.02936   32.36835 4.93560   1.000 31.38434 ? 596  VAL A CG1 1 
ATOM   3125 C  CG2 . VAL A 1 393 ? 3.69991   29.97903 5.17413   1.000 30.16313 ? 596  VAL A CG2 1 
ATOM   3126 N  N   . ARG A 1 394 ? 4.71502   34.08323 7.11363   1.000 31.85042 ? 597  ARG A N   1 
ATOM   3127 C  CA  . ARG A 1 394 ? 4.42746   35.37972 7.69905   1.000 34.02244 ? 597  ARG A CA  1 
ATOM   3128 C  C   . ARG A 1 394 ? 4.30105   36.41062 6.58966   1.000 36.96046 ? 597  ARG A C   1 
ATOM   3129 O  O   . ARG A 1 394 ? 4.69079   36.17325 5.44175   1.000 37.67689 ? 597  ARG A O   1 
ATOM   3130 C  CB  . ARG A 1 394 ? 5.50291   35.77440 8.70639   1.000 38.23150 ? 597  ARG A CB  1 
ATOM   3131 C  CG  . ARG A 1 394 ? 5.26327   35.11370 10.01803  1.000 36.92694 ? 597  ARG A CG  1 
ATOM   3132 C  CD  . ARG A 1 394 ? 6.33012   35.38038 11.02724  1.000 47.90617 ? 597  ARG A CD  1 
ATOM   3133 N  NE  . ARG A 1 394 ? 6.18470   34.45667 12.14911  1.000 45.84997 ? 597  ARG A NE  1 
ATOM   3134 C  CZ  . ARG A 1 394 ? 7.02181   34.39738 13.17225  1.000 46.40882 ? 597  ARG A CZ  1 
ATOM   3135 N  NH1 . ARG A 1 394 ? 8.05856   35.21821 13.26308  1.000 50.14589 ? 597  ARG A NH1 1 
ATOM   3136 N  NH2 . ARG A 1 394 ? 6.81804   33.49258 14.12316  1.000 42.07031 ? 597  ARG A NH2 1 
ATOM   3137 N  N   . TYR A 1 395 ? 3.73278   37.55471 6.93385   1.000 36.86546 ? 598  TYR A N   1 
ATOM   3138 C  CA  . TYR A 1 395 ? 3.47977   38.58663 5.94227   1.000 41.67063 ? 598  TYR A CA  1 
ATOM   3139 C  C   . TYR A 1 395 ? 3.95842   39.92621 6.47862   1.000 45.51896 ? 598  TYR A C   1 
ATOM   3140 O  O   . TYR A 1 395 ? 3.73926   40.24894 7.64765   1.000 42.58238 ? 598  TYR A O   1 
ATOM   3141 C  CB  . TYR A 1 395 ? 1.99431   38.63122 5.56955   1.000 34.37023 ? 598  TYR A CB  1 
ATOM   3142 C  CG  . TYR A 1 395 ? 1.42421   37.26350 5.24946   1.000 43.58498 ? 598  TYR A CG  1 
ATOM   3143 C  CD1 . TYR A 1 395 ? 1.49427   36.73114 3.96484   1.000 35.11808 ? 598  TYR A CD1 1 
ATOM   3144 C  CD2 . TYR A 1 395 ? 0.82068   36.50215 6.23423   1.000 37.31735 ? 598  TYR A CD2 1 
ATOM   3145 C  CE1 . TYR A 1 395 ? 0.97574   35.47159 3.67914   1.000 30.96953 ? 598  TYR A CE1 1 
ATOM   3146 C  CE2 . TYR A 1 395 ? 0.30777   35.24642 5.95686   1.000 33.48480 ? 598  TYR A CE2 1 
ATOM   3147 C  CZ  . TYR A 1 395 ? 0.37568   34.73839 4.68063   1.000 36.84657 ? 598  TYR A CZ  1 
ATOM   3148 O  OH  . TYR A 1 395 ? -0.15578  33.47384 4.42765   1.000 34.09703 ? 598  TYR A OH  1 
ATOM   3149 N  N   . LYS A 1 396 ? 4.62565   40.69654 5.61815   1.000 45.54171 ? 599  LYS A N   1 
ATOM   3150 C  CA  . LYS A 1 396 ? 5.16085   41.98911 6.02365   1.000 48.24052 ? 599  LYS A CA  1 
ATOM   3151 C  C   . LYS A 1 396 ? 4.02539   42.96485 6.31534   1.000 50.90986 ? 599  LYS A C   1 
ATOM   3152 O  O   . LYS A 1 396 ? 3.07365   43.07798 5.53707   1.000 49.98792 ? 599  LYS A O   1 
ATOM   3153 C  CB  . LYS A 1 396 ? 6.07706   42.54519 4.93076   1.000 45.49019 ? 599  LYS A CB  1 
ATOM   3154 N  N   . GLY A 1 397 ? 4.11584   43.65536 7.44881   1.000 43.74904 ? 600  GLY A N   1 
ATOM   3155 C  CA  . GLY A 1 397 ? 3.18275   44.72435 7.75105   1.000 51.26198 ? 600  GLY A CA  1 
ATOM   3156 C  C   . GLY A 1 397 ? 1.89003   44.30739 8.41977   1.000 49.38912 ? 600  GLY A C   1 
ATOM   3157 O  O   . GLY A 1 397 ? 1.85915   43.34078 9.18610   1.000 60.57001 ? 600  GLY A O   1 
ATOM   3158 N  N   . ASN A 1 398 ? 0.81404   45.02465 8.10922   1.000 45.20978 ? 601  ASN A N   1 
ATOM   3159 C  CA  . ASN A 1 398 ? -0.46525  44.93572 8.80833   1.000 54.14217 ? 601  ASN A CA  1 
ATOM   3160 C  C   . ASN A 1 398 ? -1.48040  44.27593 7.87672   1.000 50.18988 ? 601  ASN A C   1 
ATOM   3161 O  O   . ASN A 1 398 ? -2.04932  44.94361 7.00601   1.000 53.00759 ? 601  ASN A O   1 
ATOM   3162 C  CB  . ASN A 1 398 ? -0.90153  46.33993 9.24414   1.000 52.57921 ? 601  ASN A CB  1 
ATOM   3163 C  CG  . ASN A 1 398 ? -1.99383  46.32808 10.30175  1.000 52.51490 ? 601  ASN A CG  1 
ATOM   3164 O  OD1 . ASN A 1 398 ? -2.96202  45.57115 10.19806  1.000 56.01092 ? 601  ASN A OD1 1 
ATOM   3165 N  ND2 . ASN A 1 398 ? -1.84129  47.16865 11.33150  1.000 50.19454 ? 601  ASN A ND2 1 
ATOM   3166 N  N   . ILE A 1 399 ? -1.72562  42.97241 8.08316   1.000 45.14947 ? 602  ILE A N   1 
ATOM   3167 C  CA  . ILE A 1 399 ? -2.56752  42.19202 7.17469   1.000 47.69870 ? 602  ILE A CA  1 
ATOM   3168 C  C   . ILE A 1 399 ? -4.02812  42.60746 7.19332   1.000 44.12611 ? 602  ILE A C   1 
ATOM   3169 O  O   . ILE A 1 399 ? -4.82362  42.06596 6.41539   1.000 50.27386 ? 602  ILE A O   1 
ATOM   3170 C  CB  . ILE A 1 399 ? -2.54678  40.66943 7.45714   1.000 45.55530 ? 602  ILE A CB  1 
ATOM   3171 C  CG1 . ILE A 1 399 ? -3.14664  40.34300 8.82883   1.000 42.55017 ? 602  ILE A CG1 1 
ATOM   3172 C  CG2 . ILE A 1 399 ? -1.13728  40.08498 7.36333   1.000 38.11132 ? 602  ILE A CG2 1 
ATOM   3173 C  CD1 . ILE A 1 399 ? -3.12084  38.85526 9.12539   1.000 43.85998 ? 602  ILE A CD1 1 
ATOM   3174 N  N   . TYR A 1 400 ? -4.41287  43.52809 8.06914   1.000 51.05063 ? 603  TYR A N   1 
ATOM   3175 C  CA  . TYR A 1 400 ? -5.78950  43.99037 8.13066   1.000 54.42675 ? 603  TYR A CA  1 
ATOM   3176 C  C   . TYR A 1 400 ? -5.99305  45.33992 7.45527   1.000 59.11442 ? 603  TYR A C   1 
ATOM   3177 O  O   . TYR A 1 400 ? -7.14217  45.72631 7.22525   1.000 67.06401 ? 603  TYR A O   1 
ATOM   3178 C  CB  . TYR A 1 400 ? -6.26609  44.06544 9.59400   1.000 45.76697 ? 603  TYR A CB  1 
ATOM   3179 C  CG  . TYR A 1 400 ? -6.28581  42.71332 10.29402  1.000 43.65986 ? 603  TYR A CG  1 
ATOM   3180 C  CD1 . TYR A 1 400 ? -7.35774  41.84530 10.14580  1.000 43.04188 ? 603  TYR A CD1 1 
ATOM   3181 C  CD2 . TYR A 1 400 ? -5.22419  42.31285 11.08919  1.000 42.49363 ? 603  TYR A CD2 1 
ATOM   3182 C  CE1 . TYR A 1 400 ? -7.36383  40.61068 10.77244  1.000 42.28959 ? 603  TYR A CE1 1 
ATOM   3183 C  CE2 . TYR A 1 400 ? -5.22484  41.10862 11.72579  1.000 40.80135 ? 603  TYR A CE2 1 
ATOM   3184 C  CZ  . TYR A 1 400 ? -6.29378  40.24835 11.56533  1.000 40.89692 ? 603  TYR A CZ  1 
ATOM   3185 O  OH  . TYR A 1 400 ? -6.29233  39.01823 12.18630  1.000 38.93258 ? 603  TYR A OH  1 
ATOM   3186 N  N   . GLU A 1 401 ? -4.91923  46.05303 7.12366   1.000 57.14608 ? 604  GLU A N   1 
ATOM   3187 C  CA  . GLU A 1 401 ? -5.02993  47.38778 6.52898   1.000 59.39126 ? 604  GLU A CA  1 
ATOM   3188 C  C   . GLU A 1 401 ? -5.02615  47.34933 4.99991   1.000 57.35131 ? 604  GLU A C   1 
ATOM   3189 O  O   . GLU A 1 401 ? -4.34357  46.52517 4.38337   1.000 56.22634 ? 604  GLU A O   1 
ATOM   3190 C  CB  . GLU A 1 401 ? -3.89424  48.28866 7.03192   1.000 58.75600 ? 604  GLU A CB  1 
ATOM   3191 N  N   . GLU A 1 404 ? -2.07674  47.97367 2.32355   1.000 70.86864 ? 607  GLU A N   1 
ATOM   3192 C  CA  . GLU A 1 404 ? -0.77878  47.31569 2.38981   1.000 54.48053 ? 607  GLU A CA  1 
ATOM   3193 C  C   . GLU A 1 404 ? -0.87025  45.95886 1.71208   1.000 64.36698 ? 607  GLU A C   1 
ATOM   3194 O  O   . GLU A 1 404 ? -1.80394  45.19786 1.97341   1.000 70.30440 ? 607  GLU A O   1 
ATOM   3195 C  CB  . GLU A 1 404 ? -0.31112  47.15061 3.84460   1.000 69.37845 ? 607  GLU A CB  1 
ATOM   3196 C  CG  . GLU A 1 404 ? -0.44586  48.39766 4.71949   1.000 64.04865 ? 607  GLU A CG  1 
ATOM   3197 C  CD  . GLU A 1 404 ? 0.19799   48.23962 6.10378   1.000 75.07146 ? 607  GLU A CD  1 
ATOM   3198 O  OE1 . GLU A 1 404 ? 1.03836   47.33070 6.28221   1.000 61.16991 ? 607  GLU A OE1 1 
ATOM   3199 O  OE2 . GLU A 1 404 ? -0.13597  49.03001 7.01978   1.000 77.23454 ? 607  GLU A OE2 1 
ATOM   3200 N  N   . LYS A 1 405 ? 0.10996   45.65723 0.84885   1.000 63.24951 ? 608  LYS A N   1 
ATOM   3201 C  CA  . LYS A 1 405 ? 0.10047   44.42104 0.06576   1.000 59.64181 ? 608  LYS A CA  1 
ATOM   3202 C  C   . LYS A 1 405 ? 0.45465   43.19001 0.89911   1.000 57.23073 ? 608  LYS A C   1 
ATOM   3203 O  O   . LYS A 1 405 ? -0.09208  42.10798 0.65590   1.000 54.70971 ? 608  LYS A O   1 
ATOM   3204 C  CB  . LYS A 1 405 ? 1.05857   44.55558 -1.12151  1.000 53.74190 ? 608  LYS A CB  1 
ATOM   3205 C  CG  . LYS A 1 405 ? 0.57979   45.53237 -2.18466  1.000 50.49096 ? 608  LYS A CG  1 
ATOM   3206 C  CD  . LYS A 1 405 ? 1.50452   45.54583 -3.39612  1.000 68.11491 ? 608  LYS A CD  1 
ATOM   3207 N  N   . ASN A 1 406 ? 1.35461   43.34197 1.87302   1.000 54.47183 ? 609  ASN A N   1 
ATOM   3208 C  CA  . ASN A 1 406 ? 1.77677   42.28794 2.78628   1.000 47.19539 ? 609  ASN A CA  1 
ATOM   3209 C  C   . ASN A 1 406 ? 2.53741   41.19776 2.04192   1.000 48.19838 ? 609  ASN A C   1 
ATOM   3210 O  O   . ASN A 1 406 ? 2.01961   40.09286 1.83140   1.000 45.33052 ? 609  ASN A O   1 
ATOM   3211 C  CB  . ASN A 1 406 ? 0.58233   41.69497 3.54765   1.000 44.97545 ? 609  ASN A CB  1 
ATOM   3212 C  CG  . ASN A 1 406 ? -0.29636  42.75556 4.19948   1.000 55.15441 ? 609  ASN A CG  1 
ATOM   3213 O  OD1 . ASN A 1 406 ? -1.47886  42.85918 3.88015   1.000 62.42641 ? 609  ASN A OD1 1 
ATOM   3214 N  ND2 . ASN A 1 406 ? 0.27006   43.53528 5.12771   1.000 53.55700 ? 609  ASN A ND2 1 
ATOM   3215 N  N   . ARG A 1 407 ? 3.77378   41.50565 1.65606   1.000 45.57155 ? 610  ARG A N   1 
ATOM   3216 C  CA  . ARG A 1 407 ? 4.64033   40.54066 0.99020   1.000 43.24653 ? 610  ARG A CA  1 
ATOM   3217 C  C   . ARG A 1 407 ? 4.75919   39.25807 1.80894   1.000 44.73619 ? 610  ARG A C   1 
ATOM   3218 O  O   . ARG A 1 407 ? 5.17082   39.28600 2.97486   1.000 43.80363 ? 610  ARG A O   1 
ATOM   3219 C  CB  . ARG A 1 407 ? 6.02074   41.15779 0.76932   1.000 48.30499 ? 610  ARG A CB  1 
ATOM   3220 C  CG  . ARG A 1 407 ? 6.95562   40.31891 -0.08608  1.000 51.20580 ? 610  ARG A CG  1 
ATOM   3221 C  CD  . ARG A 1 407 ? 6.64225   40.49019 -1.53823  1.000 47.49669 ? 610  ARG A CD  1 
ATOM   3222 N  NE  . ARG A 1 407 ? 7.07963   39.34730 -2.32924  1.000 58.06694 ? 610  ARG A NE  1 
ATOM   3223 C  CZ  . ARG A 1 407 ? 8.10577   39.36337 -3.16836  1.000 59.36404 ? 610  ARG A CZ  1 
ATOM   3224 N  NH1 . ARG A 1 407 ? 8.84752   40.44918 -3.33604  1.000 60.47793 ? 610  ARG A NH1 1 
ATOM   3225 N  NH2 . ARG A 1 407 ? 8.38672   38.26796 -3.86805  1.000 51.35045 ? 610  ARG A NH2 1 
ATOM   3226 N  N   . THR A 1 408 ? 4.40313   38.13011 1.19586   1.000 35.41676 ? 611  THR A N   1 
ATOM   3227 C  CA  . THR A 1 408 ? 4.50093   36.84574 1.87623   1.000 34.04030 ? 611  THR A CA  1 
ATOM   3228 C  C   . THR A 1 408 ? 5.96096   36.46798 2.07018   1.000 41.04085 ? 611  THR A C   1 
ATOM   3229 O  O   . THR A 1 408 ? 6.80713   36.76223 1.22243   1.000 44.49294 ? 611  THR A O   1 
ATOM   3230 C  CB  . THR A 1 408 ? 3.77958   35.76920 1.06852   1.000 35.14897 ? 611  THR A CB  1 
ATOM   3231 O  OG1 . THR A 1 408 ? 2.41217   36.15408 0.89731   1.000 42.71638 ? 611  THR A OG1 1 
ATOM   3232 C  CG2 . THR A 1 408 ? 3.84408   34.42807 1.74426   1.000 32.19186 ? 611  THR A CG2 1 
ATOM   3233 N  N   . TYR A 1 409 ? 6.27142   35.85049 3.20783   1.000 33.38310 ? 612  TYR A N   1 
ATOM   3234 C  CA  . TYR A 1 409 ? 7.57245   35.21993 3.33557   1.000 35.36497 ? 612  TYR A CA  1 
ATOM   3235 C  C   . TYR A 1 409 ? 7.45942   33.99924 4.24012   1.000 38.99051 ? 612  TYR A C   1 
ATOM   3236 O  O   . TYR A 1 409 ? 6.50492   33.84557 5.00572   1.000 34.39318 ? 612  TYR A O   1 
ATOM   3237 C  CB  . TYR A 1 409 ? 8.64929   36.20876 3.81784   1.000 37.82950 ? 612  TYR A CB  1 
ATOM   3238 C  CG  . TYR A 1 409 ? 8.48829   36.77637 5.21588   1.000 40.02675 ? 612  TYR A CG  1 
ATOM   3239 C  CD1 . TYR A 1 409 ? 8.91264   36.06035 6.32903   1.000 40.07776 ? 612  TYR A CD1 1 
ATOM   3240 C  CD2 . TYR A 1 409 ? 7.97024   38.05531 5.41224   1.000 35.60441 ? 612  TYR A CD2 1 
ATOM   3241 C  CE1 . TYR A 1 409 ? 8.78179   36.58063 7.62178   1.000 42.50985 ? 612  TYR A CE1 1 
ATOM   3242 C  CE2 . TYR A 1 409 ? 7.82989   38.58673 6.69098   1.000 42.95888 ? 612  TYR A CE2 1 
ATOM   3243 C  CZ  . TYR A 1 409 ? 8.24056   37.84399 7.79069   1.000 44.44564 ? 612  TYR A CZ  1 
ATOM   3244 O  OH  . TYR A 1 409 ? 8.11162   38.36666 9.05396   1.000 46.57932 ? 612  TYR A OH  1 
ATOM   3245 N  N   . MET A 1 410 ? 8.43037   33.10681 4.10201   1.000 37.72768 ? 613  MET A N   1 
ATOM   3246 C  CA  . MET A 1 410 ? 8.48907   31.88633 4.88694   1.000 38.48561 ? 613  MET A CA  1 
ATOM   3247 C  C   . MET A 1 410 ? 9.88791   31.76999 5.46600   1.000 39.46752 ? 613  MET A C   1 
ATOM   3248 O  O   . MET A 1 410 ? 10.80831  32.49346 5.06519   1.000 41.62527 ? 613  MET A O   1 
ATOM   3249 C  CB  . MET A 1 410 ? 8.12338   30.64258 4.05528   1.000 26.96741 ? 613  MET A CB  1 
ATOM   3250 C  CG  . MET A 1 410 ? 9.20022   30.20674 3.09666   1.000 34.12198 ? 613  MET A CG  1 
ATOM   3251 S  SD  . MET A 1 410 ? 8.70625   28.80210 2.05367   1.000 41.47588 ? 613  MET A SD  1 
ATOM   3252 C  CE  . MET A 1 410 ? 10.20826  28.56385 1.07820   1.000 32.76462 ? 613  MET A CE  1 
ATOM   3253 N  N   . PHE A 1 411 ? 10.02784  30.88384 6.44574   1.000 38.86654 ? 614  PHE A N   1 
ATOM   3254 C  CA  . PHE A 1 411 ? 11.28303  30.74344 7.17091   1.000 38.05623 ? 614  PHE A CA  1 
ATOM   3255 C  C   . PHE A 1 411 ? 11.42895  29.31172 7.67316   1.000 37.77985 ? 614  PHE A C   1 
ATOM   3256 O  O   . PHE A 1 411 ? 10.44504  28.61408 7.93121   1.000 35.42636 ? 614  PHE A O   1 
ATOM   3257 C  CB  . PHE A 1 411 ? 11.37108  31.72675 8.33750   1.000 37.02852 ? 614  PHE A CB  1 
ATOM   3258 C  CG  . PHE A 1 411 ? 10.34207  31.49472 9.42724   1.000 40.49577 ? 614  PHE A CG  1 
ATOM   3259 C  CD1 . PHE A 1 411 ? 9.15346   32.20647 9.44150   1.000 40.86776 ? 614  PHE A CD1 1 
ATOM   3260 C  CD2 . PHE A 1 411 ? 10.57698  30.58988 10.44855  1.000 36.40616 ? 614  PHE A CD2 1 
ATOM   3261 C  CE1 . PHE A 1 411 ? 8.21325   32.01054 10.44715  1.000 37.70711 ? 614  PHE A CE1 1 
ATOM   3262 C  CE2 . PHE A 1 411 ? 9.64137   30.39664 11.46351  1.000 37.35085 ? 614  PHE A CE2 1 
ATOM   3263 C  CZ  . PHE A 1 411 ? 8.45971   31.10217 11.45662  1.000 36.92778 ? 614  PHE A CZ  1 
ATOM   3264 N  N   . ASN A 1 412 ? 12.67909  28.89802 7.84456   1.000 38.57581 ? 615  ASN A N   1 
ATOM   3265 C  CA  . ASN A 1 412 ? 13.01395  27.52495 8.20573   1.000 36.80646 ? 615  ASN A CA  1 
ATOM   3266 C  C   . ASN A 1 412 ? 13.06318  27.38053 9.72994   1.000 33.22894 ? 615  ASN A C   1 
ATOM   3267 O  O   . ASN A 1 412 ? 13.99559  27.87197 10.36950  1.000 36.43242 ? 615  ASN A O   1 
ATOM   3268 C  CB  . ASN A 1 412 ? 14.35055  27.14409 7.57183   1.000 37.19421 ? 615  ASN A CB  1 
ATOM   3269 C  CG  . ASN A 1 412 ? 14.68675  25.67433 7.75132   1.000 39.42099 ? 615  ASN A CG  1 
ATOM   3270 O  OD1 . ASN A 1 412 ? 13.95269  24.93369 8.40558   1.000 36.28397 ? 615  ASN A OD1 1 
ATOM   3271 N  ND2 . ASN A 1 412 ? 15.79195  25.24252 7.15271   1.000 41.89280 ? 615  ASN A ND2 1 
ATOM   3272 N  N   . TYR A 1 413 ? 12.08289  26.65919 10.30301  1.000 28.12942 ? 616  TYR A N   1 
ATOM   3273 C  CA  . TYR A 1 413 ? 12.08866  26.37175 11.74491  1.000 33.27487 ? 616  TYR A CA  1 
ATOM   3274 C  C   . TYR A 1 413 ? 13.33269  25.60578 12.18227  1.000 38.95470 ? 616  TYR A C   1 
ATOM   3275 O  O   . TYR A 1 413 ? 13.74487  25.70390 13.34674  1.000 35.47546 ? 616  TYR A O   1 
ATOM   3276 C  CB  . TYR A 1 413 ? 10.84744  25.56596 12.14909  1.000 30.62256 ? 616  TYR A CB  1 
ATOM   3277 C  CG  . TYR A 1 413 ? 9.61260   26.38798 12.45101  1.000 27.30381 ? 616  TYR A CG  1 
ATOM   3278 C  CD1 . TYR A 1 413 ? 9.48955   27.06474 13.65107  1.000 29.52733 ? 616  TYR A CD1 1 
ATOM   3279 C  CD2 . TYR A 1 413 ? 8.55601   26.45544 11.54430  1.000 27.20601 ? 616  TYR A CD2 1 
ATOM   3280 C  CE1 . TYR A 1 413 ? 8.36298   27.80493 13.93761  1.000 33.62455 ? 616  TYR A CE1 1 
ATOM   3281 C  CE2 . TYR A 1 413 ? 7.42111   27.19825 11.82069  1.000 27.69778 ? 616  TYR A CE2 1 
ATOM   3282 C  CZ  . TYR A 1 413 ? 7.32944   27.87300 13.02548  1.000 30.66582 ? 616  TYR A CZ  1 
ATOM   3283 O  OH  . TYR A 1 413 ? 6.21021   28.62986 13.32144  1.000 30.23076 ? 616  TYR A OH  1 
ATOM   3284 N  N   . ALA A 1 414 ? 13.93224  24.82316 11.28283  1.000 32.63539 ? 617  ALA A N   1 
ATOM   3285 C  CA  . ALA A 1 414 ? 15.08896  24.01542 11.65421  1.000 37.29764 ? 617  ALA A CA  1 
ATOM   3286 C  C   . ALA A 1 414 ? 16.34768  24.83976 11.92306  1.000 42.57524 ? 617  ALA A C   1 
ATOM   3287 O  O   . ALA A 1 414 ? 17.34586  24.27564 12.37914  1.000 48.77256 ? 617  ALA A O   1 
ATOM   3288 C  CB  . ALA A 1 414 ? 15.36802  22.98301 10.56177  1.000 33.63611 ? 617  ALA A CB  1 
ATOM   3289 N  N   . LEU A 1 415 ? 16.33651  26.14374 11.66887  1.000 38.08089 ? 618  LEU A N   1 
ATOM   3290 C  CA  . LEU A 1 415 ? 17.52020  26.97455 11.83350  1.000 41.72046 ? 618  LEU A CA  1 
ATOM   3291 C  C   . LEU A 1 415 ? 17.32374  27.95242 12.98199  1.000 50.07170 ? 618  LEU A C   1 
ATOM   3292 O  O   . LEU A 1 415 ? 16.22851  28.49058 13.17208  1.000 53.21655 ? 618  LEU A O   1 
ATOM   3293 C  CB  . LEU A 1 415 ? 17.84176  27.76506 10.55321  1.000 42.59345 ? 618  LEU A CB  1 
ATOM   3294 C  CG  . LEU A 1 415 ? 18.22245  27.01597 9.27100   1.000 47.26888 ? 618  LEU A CG  1 
ATOM   3295 C  CD1 . LEU A 1 415 ? 18.23799  27.96756 8.07351   1.000 47.48544 ? 618  LEU A CD1 1 
ATOM   3296 C  CD2 . LEU A 1 415 ? 19.57644  26.35702 9.44001   1.000 52.32130 ? 618  LEU A CD2 1 
ATOM   3297 N  N   . SER A 1 416 ? 18.38917  28.17756 13.74580  1.000 49.35897 ? 619  SER A N   1 
ATOM   3298 C  CA  . SER A 1 416 ? 18.45573  29.36882 14.57732  1.000 55.75618 ? 619  SER A CA  1 
ATOM   3299 C  C   . SER A 1 416 ? 18.62152  30.58691 13.67570  1.000 61.63119 ? 619  SER A C   1 
ATOM   3300 O  O   . SER A 1 416 ? 19.40636  30.56717 12.72019  1.000 54.22790 ? 619  SER A O   1 
ATOM   3301 C  CB  . SER A 1 416 ? 19.61362  29.27337 15.56911  1.000 58.75902 ? 619  SER A CB  1 
ATOM   3302 O  OG  . SER A 1 416 ? 20.84755  29.08087 14.89897  1.000 66.31532 ? 619  SER A OG  1 
ATOM   3303 N  N   . LYS A 1 417 ? 17.86179  31.64429 13.97341  1.000 61.31543 ? 620  LYS A N   1 
ATOM   3304 C  CA  . LYS A 1 417 ? 17.82261  32.85023 13.14806  1.000 63.99587 ? 620  LYS A CA  1 
ATOM   3305 C  C   . LYS A 1 417 ? 17.60249  32.49304 11.68082  1.000 60.57555 ? 620  LYS A C   1 
ATOM   3306 O  O   . LYS A 1 417 ? 18.51707  32.64258 10.85887  1.000 58.50966 ? 620  LYS A O   1 
ATOM   3307 C  CB  . LYS A 1 417 ? 19.10864  33.66878 13.30802  1.000 55.33007 ? 620  LYS A CB  1 
ATOM   3308 N  N   . PRO A 1 418 ? 16.41909  32.00706 11.31425  1.000 53.66252 ? 621  PRO A N   1 
ATOM   3309 C  CA  . PRO A 1 418 ? 16.14963  31.74016 9.89631   1.000 49.93289 ? 621  PRO A CA  1 
ATOM   3310 C  C   . PRO A 1 418 ? 16.01559  33.03052 9.09856   1.000 54.03196 ? 621  PRO A C   1 
ATOM   3311 O  O   . PRO A 1 418 ? 15.43369  34.01499 9.56386   1.000 50.20014 ? 621  PRO A O   1 
ATOM   3312 C  CB  . PRO A 1 418 ? 14.83266  30.96000 9.92409   1.000 46.50118 ? 621  PRO A CB  1 
ATOM   3313 C  CG  . PRO A 1 418 ? 14.18939  31.34456 11.21666  1.000 49.20477 ? 621  PRO A CG  1 
ATOM   3314 C  CD  . PRO A 1 418 ? 15.28850  31.63943 12.18604  1.000 53.68064 ? 621  PRO A CD  1 
ATOM   3315 N  N   . GLU A 1 419 ? 16.56710  33.01477 7.88556   1.000 50.63033 ? 622  GLU A N   1 
ATOM   3316 C  CA  . GLU A 1 419 ? 16.43675  34.14619 6.98124   1.000 52.92635 ? 622  GLU A CA  1 
ATOM   3317 C  C   . GLU A 1 419 ? 15.03272  34.18677 6.40315   1.000 44.60632 ? 622  GLU A C   1 
ATOM   3318 O  O   . GLU A 1 419 ? 14.46073  33.15161 6.05229   1.000 40.38440 ? 622  GLU A O   1 
ATOM   3319 C  CB  . GLU A 1 419 ? 17.46046  34.05790 5.84654   1.000 51.74154 ? 622  GLU A CB  1 
ATOM   3320 N  N   . ASN A 1 420 ? 14.47771  35.38888 6.31221   1.000 39.43472 ? 623  ASN A N   1 
ATOM   3321 C  CA  . ASN A 1 420 ? 13.20105  35.57906 5.63666   1.000 40.79211 ? 623  ASN A CA  1 
ATOM   3322 C  C   . ASN A 1 420 ? 13.34145  35.25253 4.15327   1.000 44.11556 ? 623  ASN A C   1 
ATOM   3323 O  O   . ASN A 1 420 ? 14.17794  35.83145 3.45403   1.000 44.10644 ? 623  ASN A O   1 
ATOM   3324 C  CB  . ASN A 1 420 ? 12.71924  37.01199 5.82740   1.000 47.06064 ? 623  ASN A CB  1 
ATOM   3325 C  CG  . ASN A 1 420 ? 12.34335  37.30734 7.26961   1.000 52.61926 ? 623  ASN A CG  1 
ATOM   3326 O  OD1 . ASN A 1 420 ? 12.22127  36.39313 8.09174   1.000 50.87262 ? 623  ASN A OD1 1 
ATOM   3327 N  ND2 . ASN A 1 420 ? 12.13575  38.58546 7.57868   1.000 59.05823 ? 623  ASN A ND2 1 
ATOM   3328 N  N   . ILE A 1 421 ? 12.51753  34.33348 3.67442   1.000 40.95527 ? 624  ILE A N   1 
ATOM   3329 C  CA  . ILE A 1 421 ? 12.53998  33.88333 2.28967   1.000 44.69230 ? 624  ILE A CA  1 
ATOM   3330 C  C   . ILE A 1 421 ? 11.31703  34.47711 1.60455   1.000 42.16784 ? 624  ILE A C   1 
ATOM   3331 O  O   . ILE A 1 421 ? 10.17933  34.07008 1.87618   1.000 35.18863 ? 624  ILE A O   1 
ATOM   3332 C  CB  . ILE A 1 421 ? 12.54948  32.35030 2.19372   1.000 39.79367 ? 624  ILE A CB  1 
ATOM   3333 C  CG1 . ILE A 1 421 ? 13.80178  31.77287 2.86606   1.000 38.04285 ? 624  ILE A CG1 1 
ATOM   3334 C  CG2 . ILE A 1 421 ? 12.43349  31.89503 0.73824   1.000 41.85142 ? 624  ILE A CG2 1 
ATOM   3335 C  CD1 . ILE A 1 421 ? 13.72410  30.24076 3.11954   1.000 37.27432 ? 624  ILE A CD1 1 
ATOM   3336 N  N   . TYR A 1 422 ? 11.54048  35.43576 0.71386   1.000 38.92192 ? 625  TYR A N   1 
ATOM   3337 C  CA  . TYR A 1 422 ? 10.43692  36.07497 0.00363   1.000 44.89314 ? 625  TYR A CA  1 
ATOM   3338 C  C   . TYR A 1 422 ? 10.08120  35.24160 -1.22040  1.000 42.11145 ? 625  TYR A C   1 
ATOM   3339 O  O   . TYR A 1 422 ? 10.76180  35.29574 -2.24909  1.000 47.73333 ? 625  TYR A O   1 
ATOM   3340 C  CB  . TYR A 1 422 ? 10.79908  37.50795 -0.35333  1.000 39.52581 ? 625  TYR A CB  1 
ATOM   3341 C  CG  . TYR A 1 422 ? 10.88948  38.37516 0.88125   1.000 41.90482 ? 625  TYR A CG  1 
ATOM   3342 C  CD1 . TYR A 1 422 ? 9.74135   38.89562 1.47135   1.000 47.52165 ? 625  TYR A CD1 1 
ATOM   3343 C  CD2 . TYR A 1 422 ? 12.11532  38.64998 1.47605   1.000 45.67396 ? 625  TYR A CD2 1 
ATOM   3344 C  CE1 . TYR A 1 422 ? 9.81065   39.69194 2.61898   1.000 52.70922 ? 625  TYR A CE1 1 
ATOM   3345 C  CE2 . TYR A 1 422 ? 12.19761  39.44550 2.62264   1.000 58.59447 ? 625  TYR A CE2 1 
ATOM   3346 C  CZ  . TYR A 1 422 ? 11.03972  39.95931 3.18641   1.000 54.34992 ? 625  TYR A CZ  1 
ATOM   3347 O  OH  . TYR A 1 422 ? 11.11094  40.73835 4.31538   1.000 65.06950 ? 625  TYR A OH  1 
ATOM   3348 N  N   . ILE A 1 423 ? 9.00662   34.45984 -1.08651  1.000 35.32118 ? 626  ILE A N   1 
ATOM   3349 C  CA  . ILE A 1 423 ? 8.49382   33.64721 -2.18374  1.000 44.42960 ? 626  ILE A CA  1 
ATOM   3350 C  C   . ILE A 1 423 ? 8.22493   34.51605 -3.39986  1.000 46.31429 ? 626  ILE A C   1 
ATOM   3351 O  O   . ILE A 1 423 ? 7.54324   35.54320 -3.31580  1.000 45.22577 ? 626  ILE A O   1 
ATOM   3352 C  CB  . ILE A 1 423 ? 7.22201   32.91256 -1.74040  1.000 42.89445 ? 626  ILE A CB  1 
ATOM   3353 C  CG1 . ILE A 1 423 ? 7.53107   32.01460 -0.55201  1.000 35.35762 ? 626  ILE A CG1 1 
ATOM   3354 C  CG2 . ILE A 1 423 ? 6.63903   32.09693 -2.89010  1.000 44.08339 ? 626  ILE A CG2 1 
ATOM   3355 C  CD1 . ILE A 1 423 ? 6.31921   31.27318 -0.02596  1.000 43.26038 ? 626  ILE A CD1 1 
ATOM   3356 N  N   . ASP A 1 424 ? 8.77088   34.11506 -4.54256  1.000 45.76722 ? 627  ASP A N   1 
ATOM   3357 C  CA  . ASP A 1 424 ? 8.48222   34.85152 -5.76025  1.000 38.20158 ? 627  ASP A CA  1 
ATOM   3358 C  C   . ASP A 1 424 ? 7.29603   34.24877 -6.50833  1.000 45.81312 ? 627  ASP A C   1 
ATOM   3359 O  O   . ASP A 1 424 ? 6.49305   34.99136 -7.08695  1.000 40.11048 ? 627  ASP A O   1 
ATOM   3360 C  CB  . ASP A 1 424 ? 9.73177   34.91105 -6.64788  1.000 48.00844 ? 627  ASP A CB  1 
ATOM   3361 C  CG  . ASP A 1 424 ? 10.68571  36.02886 -6.23434  1.000 57.34495 ? 627  ASP A CG  1 
ATOM   3362 O  OD1 . ASP A 1 424 ? 10.18436  37.03541 -5.70083  1.000 55.18700 ? 627  ASP A OD1 1 
ATOM   3363 O  OD2 . ASP A 1 424 ? 11.91844  35.91667 -6.43927  1.000 60.00299 ? 627  ASP A OD2 1 
ATOM   3364 N  N   . GLY A 1 425 ? 7.13629   32.92832 -6.48412  1.000 37.60443 ? 628  GLY A N   1 
ATOM   3365 C  CA  . GLY A 1 425 ? 5.97285   32.34773 -7.12485  1.000 34.20429 ? 628  GLY A CA  1 
ATOM   3366 C  C   . GLY A 1 425 ? 5.91065   30.85213 -6.93352  1.000 34.40130 ? 628  GLY A C   1 
ATOM   3367 O  O   . GLY A 1 425 ? 6.72254   30.26254 -6.21753  1.000 36.36419 ? 628  GLY A O   1 
ATOM   3368 N  N   . LEU A 1 426 ? 4.91670   30.24567 -7.58458  1.000 27.54716 ? 629  LEU A N   1 
ATOM   3369 C  CA  . LEU A 1 426 ? 4.73737   28.79801 -7.60923  1.000 28.62350 ? 629  LEU A CA  1 
ATOM   3370 C  C   . LEU A 1 426 ? 4.84867   28.31040 -9.04414  1.000 34.20113 ? 629  LEU A C   1 
ATOM   3371 O  O   . LEU A 1 426 ? 4.35215   28.96393 -9.96725  1.000 33.81065 ? 629  LEU A O   1 
ATOM   3372 C  CB  . LEU A 1 426 ? 3.37017   28.36616 -7.04232  1.000 28.72781 ? 629  LEU A CB  1 
ATOM   3373 C  CG  . LEU A 1 426 ? 3.06032   28.40409 -5.52746  1.000 34.19244 ? 629  LEU A CG  1 
ATOM   3374 C  CD1 . LEU A 1 426 ? 3.17768   29.80127 -4.97280  1.000 49.75790 ? 629  LEU A CD1 1 
ATOM   3375 C  CD2 . LEU A 1 426 ? 1.65933   27.88582 -5.28661  1.000 35.47457 ? 629  LEU A CD2 1 
ATOM   3376 N  N   . THR A 1 427 ? 5.50419   27.17230 -9.23511  1.000 23.70607 ? 630  THR A N   1 
ATOM   3377 C  CA  . THR A 1 427 ? 5.40141   26.41660 -10.47868 1.000 28.44705 ? 630  THR A CA  1 
ATOM   3378 C  C   . THR A 1 427 ? 4.59619   25.15921 -10.18668 1.000 33.53438 ? 630  THR A C   1 
ATOM   3379 O  O   . THR A 1 427 ? 4.96475   24.37437 -9.29819  1.000 30.05250 ? 630  THR A O   1 
ATOM   3380 C  CB  . THR A 1 427 ? 6.77650   26.06036 -11.04079 1.000 31.38422 ? 630  THR A CB  1 
ATOM   3381 O  OG1 . THR A 1 427 ? 7.44828   27.25975 -11.45200 1.000 32.42441 ? 630  THR A OG1 1 
ATOM   3382 C  CG2 . THR A 1 427 ? 6.63681   25.10744 -12.23597 1.000 29.69205 ? 630  THR A CG2 1 
ATOM   3383 N  N   . THR A 1 428 ? 3.49672   24.97830 -10.91453 1.000 27.28826 ? 631  THR A N   1 
ATOM   3384 C  CA  . THR A 1 428 ? 2.53336   23.92269 -10.63180 1.000 27.21908 ? 631  THR A CA  1 
ATOM   3385 C  C   . THR A 1 428 ? 2.50329   22.89995 -11.75545 1.000 33.42805 ? 631  THR A C   1 
ATOM   3386 O  O   . THR A 1 428 ? 2.78119   23.22304 -12.91761 1.000 30.30086 ? 631  THR A O   1 
ATOM   3387 C  CB  . THR A 1 428 ? 1.12412   24.48766 -10.44274 1.000 33.48535 ? 631  THR A CB  1 
ATOM   3388 O  OG1 . THR A 1 428 ? 0.66633   25.04108 -11.67987 1.000 34.30221 ? 631  THR A OG1 1 
ATOM   3389 C  CG2 . THR A 1 428 ? 1.12037   25.59544 -9.41063  1.000 31.71764 ? 631  THR A CG2 1 
ATOM   3390 N  N   . LEU A 1 429 ? 2.15012   21.65884 -11.39320 1.000 31.52124 ? 632  LEU A N   1 
ATOM   3391 C  CA  . LEU A 1 429 ? 2.02521   20.55603 -12.34211 1.000 28.32564 ? 632  LEU A CA  1 
ATOM   3392 C  C   . LEU A 1 429 ? 0.64374   19.93157 -12.21099 1.000 28.24775 ? 632  LEU A C   1 
ATOM   3393 O  O   . LEU A 1 429 ? 0.30733   19.36624 -11.16849 1.000 30.46241 ? 632  LEU A O   1 
ATOM   3394 C  CB  . LEU A 1 429 ? 3.11052   19.49744 -12.12799 1.000 24.60027 ? 632  LEU A CB  1 
ATOM   3395 C  CG  . LEU A 1 429 ? 3.05248   18.31081 -13.10535 1.000 27.55814 ? 632  LEU A CG  1 
ATOM   3396 C  CD1 . LEU A 1 429 ? 3.08883   18.77715 -14.57264 1.000 26.96513 ? 632  LEU A CD1 1 
ATOM   3397 C  CD2 . LEU A 1 429 ? 4.16045   17.29324 -12.81168 1.000 21.83681 ? 632  LEU A CD2 1 
ATOM   3398 N  N   . ASP A 1 430 ? -0.14693  20.02846 -13.27062 1.000 25.86690 ? 633  ASP A N   1 
ATOM   3399 C  CA  . ASP A 1 430 ? -1.47475  19.44519 -13.31314 1.000 26.95231 ? 633  ASP A CA  1 
ATOM   3400 C  C   . ASP A 1 430 ? -1.39035  18.01683 -13.86562 1.000 27.53562 ? 633  ASP A C   1 
ATOM   3401 O  O   . ASP A 1 430 ? -0.46091  17.67739 -14.60701 1.000 25.74478 ? 633  ASP A O   1 
ATOM   3402 C  CB  . ASP A 1 430 ? -2.37113  20.33710 -14.17153 1.000 28.06962 ? 633  ASP A CB  1 
ATOM   3403 C  CG  . ASP A 1 430 ? -3.82086  19.95275 -14.10610 1.000 35.39884 ? 633  ASP A CG  1 
ATOM   3404 O  OD1 . ASP A 1 430 ? -4.28009  19.21704 -15.00916 1.000 34.94577 ? 633  ASP A OD1 1 
ATOM   3405 O  OD2 . ASP A 1 430 ? -4.50766  20.40688 -13.16541 1.000 36.18118 ? 633  ASP A OD2 1 
ATOM   3406 N  N   . LYS A 1 431 ? -2.36184  17.17083 -13.48613 1.000 25.49831 ? 634  LYS A N   1 
ATOM   3407 C  CA  . LYS A 1 431 ? -2.35881  15.79362 -13.98507 1.000 28.11257 ? 634  LYS A CA  1 
ATOM   3408 C  C   . LYS A 1 431 ? -2.50722  15.74511 -15.49704 1.000 25.83690 ? 634  LYS A C   1 
ATOM   3409 O  O   . LYS A 1 431 ? -2.03412  14.79130 -16.12804 1.000 24.21339 ? 634  LYS A O   1 
ATOM   3410 C  CB  . LYS A 1 431 ? -3.47509  14.96446 -13.34981 1.000 29.74503 ? 634  LYS A CB  1 
ATOM   3411 C  CG  . LYS A 1 431 ? -3.23423  14.61447 -11.88992 1.000 36.19365 ? 634  LYS A CG  1 
ATOM   3412 C  CD  . LYS A 1 431 ? -4.51300  14.12273 -11.21254 1.000 44.45211 ? 634  LYS A CD  1 
ATOM   3413 C  CE  . LYS A 1 431 ? -4.33566  14.04874 -9.69544  1.000 42.88791 ? 634  LYS A CE  1 
ATOM   3414 N  NZ  . LYS A 1 431 ? -5.59090  13.63303 -9.00261  1.000 45.70348 ? 634  LYS A NZ  1 
ATOM   3415 N  N   . GLY A 1 432 ? -3.17170  16.74776 -16.08790 1.000 24.25744 ? 635  GLY A N   1 
ATOM   3416 C  CA  . GLY A 1 432 ? -3.43672  16.77346 -17.51831 1.000 32.25109 ? 635  GLY A CA  1 
ATOM   3417 C  C   . GLY A 1 432 ? -4.45704  15.73938 -17.96584 1.000 35.59491 ? 635  GLY A C   1 
ATOM   3418 O  O   . GLY A 1 432 ? -4.26336  15.07352 -18.99861 1.000 26.58089 ? 635  GLY A O   1 
ATOM   3419 N  N   A GLU A 1 433 ? -5.56271  15.61127 -17.22788 0.501 32.11332 ? 636  GLU A N   1 
ATOM   3420 N  N   B GLU A 1 433 ? -5.55362  15.61689 -17.20862 0.499 32.42310 ? 636  GLU A N   1 
ATOM   3421 C  CA  A GLU A 1 433 ? -6.51464  14.53687 -17.49462 0.501 34.18120 ? 636  GLU A CA  1 
ATOM   3422 C  CA  B GLU A 1 433 ? -6.54433  14.57576 -17.47466 0.499 34.18171 ? 636  GLU A CA  1 
ATOM   3423 C  C   A GLU A 1 433 ? -7.22713  14.72271 -18.82841 0.501 35.72765 ? 636  GLU A C   1 
ATOM   3424 C  C   B GLU A 1 433 ? -7.23252  14.77791 -18.82067 0.499 35.74355 ? 636  GLU A C   1 
ATOM   3425 O  O   A GLU A 1 433 ? -7.42799  13.74976 -19.56581 0.501 35.11591 ? 636  GLU A O   1 
ATOM   3426 O  O   B GLU A 1 433 ? -7.40937  13.81732 -19.58095 0.499 35.15878 ? 636  GLU A O   1 
ATOM   3427 C  CB  A GLU A 1 433 ? -7.52791  14.43949 -16.35628 0.501 37.12167 ? 636  GLU A CB  1 
ATOM   3428 C  CB  B GLU A 1 433 ? -7.57990  14.53888 -16.34947 0.499 37.11358 ? 636  GLU A CB  1 
ATOM   3429 C  CG  A GLU A 1 433 ? -6.89244  14.21294 -15.00621 0.501 40.85159 ? 636  GLU A CG  1 
ATOM   3430 C  CG  B GLU A 1 433 ? -8.14072  13.15551 -16.05395 0.499 41.39679 ? 636  GLU A CG  1 
ATOM   3431 C  CD  A GLU A 1 433 ? -7.65839  13.20889 -14.16675 0.501 52.14196 ? 636  GLU A CD  1 
ATOM   3432 C  CD  B GLU A 1 433 ? -7.64223  12.60492 -14.72691 0.499 52.02804 ? 636  GLU A CD  1 
ATOM   3433 O  OE1 A GLU A 1 433 ? -7.83274  12.06144 -14.63296 0.501 55.24152 ? 636  GLU A OE1 1 
ATOM   3434 O  OE1 B GLU A 1 433 ? -7.11439  13.39823 -13.91444 0.499 52.63036 ? 636  GLU A OE1 1 
ATOM   3435 O  OE2 A GLU A 1 433 ? -8.09574  13.56761 -13.05009 0.501 48.10002 ? 636  GLU A OE2 1 
ATOM   3436 O  OE2 B GLU A 1 433 ? -7.77788  11.38263 -14.49097 0.499 56.79200 ? 636  GLU A OE2 1 
ATOM   3437 N  N   A ASP A 1 434 ? -7.62969  15.95322 -19.15647 0.501 33.44843 ? 637  ASP A N   1 
ATOM   3438 N  N   B ASP A 1 434 ? -7.63698  16.01413 -19.12969 0.499 33.69035 ? 637  ASP A N   1 
ATOM   3439 C  CA  A ASP A 1 434 ? -8.34337  16.16266 -20.41180 0.501 35.58001 ? 637  ASP A CA  1 
ATOM   3440 C  CA  B ASP A 1 434 ? -8.32252  16.27721 -20.39278 0.499 35.47671 ? 637  ASP A CA  1 
ATOM   3441 C  C   A ASP A 1 434 ? -7.44931  15.86320 -21.60870 0.501 33.82943 ? 637  ASP A C   1 
ATOM   3442 C  C   B ASP A 1 434 ? -7.45437  15.88887 -21.58363 0.499 33.83537 ? 637  ASP A C   1 
ATOM   3443 O  O   A ASP A 1 434 ? -7.90500  15.28662 -22.60240 0.501 32.59548 ? 637  ASP A O   1 
ATOM   3444 O  O   B ASP A 1 434 ? -7.93550  15.27775 -22.54529 0.499 32.86927 ? 637  ASP A O   1 
ATOM   3445 C  CB  A ASP A 1 434 ? -8.89657  17.58623 -20.48168 0.501 37.43184 ? 637  ASP A CB  1 
ATOM   3446 C  CB  B ASP A 1 434 ? -8.71813  17.75351 -20.47107 0.499 37.44053 ? 637  ASP A CB  1 
ATOM   3447 C  CG  A ASP A 1 434 ? -10.09308 17.78752 -19.56711 0.501 41.34766 ? 637  ASP A CG  1 
ATOM   3448 C  CG  B ASP A 1 434 ? -9.21334  18.15698 -21.84640 0.499 39.96478 ? 637  ASP A CG  1 
ATOM   3449 O  OD1 A ASP A 1 434 ? -10.37054 16.87809 -18.75541 0.501 41.21709 ? 637  ASP A OD1 1 
ATOM   3450 O  OD1 B ASP A 1 434 ? -10.32235 17.72224 -22.23402 0.499 43.59648 ? 637  ASP A OD1 1 
ATOM   3451 O  OD2 A ASP A 1 434 ? -10.75625 18.84739 -19.65743 0.501 44.39659 ? 637  ASP A OD2 1 
ATOM   3452 O  OD2 B ASP A 1 434 ? -8.49151  18.91210 -22.54067 0.499 45.27917 ? 637  ASP A OD2 1 
ATOM   3453 N  N   . GLN A 1 435 ? -6.16887  16.22608 -21.52569 1.000 30.61426 ? 638  GLN A N   1 
ATOM   3454 C  CA  . GLN A 1 435 ? -5.24998  15.89872 -22.60512 1.000 33.26393 ? 638  GLN A CA  1 
ATOM   3455 C  C   . GLN A 1 435 ? -5.05476  14.38682 -22.72686 1.000 31.23724 ? 638  GLN A C   1 
ATOM   3456 O  O   . GLN A 1 435 ? -5.00065  13.84993 -23.83930 1.000 30.29721 ? 638  GLN A O   1 
ATOM   3457 C  CB  . GLN A 1 435 ? -3.91514  16.61191 -22.37294 1.000 32.72209 ? 638  GLN A CB  1 
ATOM   3458 C  CG  . GLN A 1 435 ? -4.03285  18.13451 -22.18121 1.000 36.58859 ? 638  GLN A CG  1 
ATOM   3459 C  CD  . GLN A 1 435 ? -4.15215  18.54424 -20.70497 1.000 39.92033 ? 638  GLN A CD  1 
ATOM   3460 O  OE1 . GLN A 1 435 ? -5.07992  18.12593 -20.00761 1.000 33.17409 ? 638  GLN A OE1 1 
ATOM   3461 N  NE2 . GLN A 1 435 ? -3.20362  19.36297 -20.22775 1.000 36.50905 ? 638  GLN A NE2 1 
ATOM   3462 N  N   . TRP A 1 436 ? -4.96036  13.68785 -21.59299 1.000 29.55411 ? 639  TRP A N   1 
ATOM   3463 C  CA  . TRP A 1 436 ? -4.85882  12.23154 -21.61050 1.000 32.12264 ? 639  TRP A CA  1 
ATOM   3464 C  C   . TRP A 1 436 ? -6.10119  11.59105 -22.22565 1.000 35.12667 ? 639  TRP A C   1 
ATOM   3465 O  O   . TRP A 1 436 ? -5.99495  10.70031 -23.08265 1.000 37.12399 ? 639  TRP A O   1 
ATOM   3466 C  CB  . TRP A 1 436 ? -4.64026  11.71521 -20.19062 1.000 27.48229 ? 639  TRP A CB  1 
ATOM   3467 C  CG  . TRP A 1 436 ? -3.21136  11.60971 -19.77478 1.000 24.99185 ? 639  TRP A CG  1 
ATOM   3468 C  CD1 . TRP A 1 436 ? -2.58514  12.29502 -18.75943 1.000 24.60399 ? 639  TRP A CD1 1 
ATOM   3469 C  CD2 . TRP A 1 436 ? -2.22726  10.74627 -20.34014 1.000 26.42396 ? 639  TRP A CD2 1 
ATOM   3470 N  NE1 . TRP A 1 436 ? -1.26917  11.90694 -18.66640 1.000 26.12360 ? 639  TRP A NE1 1 
ATOM   3471 C  CE2 . TRP A 1 436 ? -1.02622  10.95520 -19.62646 1.000 26.08471 ? 639  TRP A CE2 1 
ATOM   3472 C  CE3 . TRP A 1 436 ? -2.24433  9.80899  -21.38578 1.000 27.67066 ? 639  TRP A CE3 1 
ATOM   3473 C  CZ2 . TRP A 1 436 ? 0.14231   10.26548 -19.92472 1.000 25.78485 ? 639  TRP A CZ2 1 
ATOM   3474 C  CZ3 . TRP A 1 436 ? -1.08063  9.12703  -21.68520 1.000 25.15179 ? 639  TRP A CZ3 1 
ATOM   3475 C  CH2 . TRP A 1 436 ? 0.09720   9.36023  -20.96204 1.000 24.57213 ? 639  TRP A CH2 1 
ATOM   3476 N  N   . LYS A 1 437 ? -7.29302  12.03285 -21.79683 1.000 30.35372 ? 640  LYS A N   1 
ATOM   3477 C  CA  . LYS A 1 437 ? -8.53528  11.48323 -22.33357 1.000 32.55981 ? 640  LYS A CA  1 
ATOM   3478 C  C   . LYS A 1 437 ? -8.63189  11.68740 -23.84234 1.000 37.14494 ? 640  LYS A C   1 
ATOM   3479 O  O   . LYS A 1 437 ? -9.07496  10.78872 -24.57111 1.000 33.52366 ? 640  LYS A O   1 
ATOM   3480 C  CB  . LYS A 1 437 ? -9.74871  12.11519 -21.64568 1.000 32.71015 ? 640  LYS A CB  1 
ATOM   3481 C  CG  . LYS A 1 437 ? -10.02374 11.61664 -20.23328 1.000 45.25443 ? 640  LYS A CG  1 
ATOM   3482 C  CD  . LYS A 1 437 ? -11.02344 12.55227 -19.52668 1.000 48.81151 ? 640  LYS A CD  1 
ATOM   3483 C  CE  . LYS A 1 437 ? -11.17869 12.24202 -18.04633 1.000 45.68768 ? 640  LYS A CE  1 
ATOM   3484 N  NZ  . LYS A 1 437 ? -12.15389 13.18412 -17.42841 1.000 47.17527 ? 640  LYS A NZ  1 
ATOM   3485 N  N   . LYS A 1 438 ? -8.23643  12.86830 -24.32891 1.000 31.70658 ? 641  LYS A N   1 
ATOM   3486 C  CA  . LYS A 1 438 ? -8.28489  13.12478 -25.76420 1.000 35.72333 ? 641  LYS A CA  1 
ATOM   3487 C  C   . LYS A 1 438 ? -7.30346  12.23228 -26.51331 1.000 31.09318 ? 641  LYS A C   1 
ATOM   3488 O  O   . LYS A 1 438 ? -7.61149  11.74117 -27.60605 1.000 33.50302 ? 641  LYS A O   1 
ATOM   3489 C  CB  . LYS A 1 438 ? -7.99746  14.60121 -26.04433 1.000 35.36186 ? 641  LYS A CB  1 
ATOM   3490 C  CG  . LYS A 1 438 ? -9.17369  15.52097 -25.76447 1.000 43.06230 ? 641  LYS A CG  1 
ATOM   3491 C  CD  . LYS A 1 438 ? -8.75073  16.99024 -25.73174 1.000 52.56088 ? 641  LYS A CD  1 
ATOM   3492 N  N   . TRP A 1 439 ? -6.11085  12.02899 -25.94719 1.000 31.21042 ? 642  TRP A N   1 
ATOM   3493 C  CA  . TRP A 1 439 ? -5.15498  11.11735 -26.55820 1.000 32.73548 ? 642  TRP A CA  1 
ATOM   3494 C  C   . TRP A 1 439 ? -5.72484  9.70378  -26.62000 1.000 37.63050 ? 642  TRP A C   1 
ATOM   3495 O  O   . TRP A 1 439 ? -5.67701  9.04824  -27.66665 1.000 34.64665 ? 642  TRP A O   1 
ATOM   3496 C  CB  . TRP A 1 439 ? -3.83182  11.12988 -25.79011 1.000 30.72190 ? 642  TRP A CB  1 
ATOM   3497 C  CG  . TRP A 1 439 ? -2.80232  10.23951 -26.43340 1.000 40.43569 ? 642  TRP A CG  1 
ATOM   3498 C  CD1 . TRP A 1 439 ? -1.98064  10.55750 -27.48138 1.000 37.02912 ? 642  TRP A CD1 1 
ATOM   3499 C  CD2 . TRP A 1 439 ? -2.50319  8.87724  -26.08926 1.000 36.05070 ? 642  TRP A CD2 1 
ATOM   3500 N  NE1 . TRP A 1 439 ? -1.18380  9.48305  -27.80012 1.000 35.46118 ? 642  TRP A NE1 1 
ATOM   3501 C  CE2 . TRP A 1 439 ? -1.48692  8.43911  -26.96563 1.000 37.83325 ? 642  TRP A CE2 1 
ATOM   3502 C  CE3 . TRP A 1 439 ? -2.98464  7.99293  -25.11442 1.000 41.65717 ? 642  TRP A CE3 1 
ATOM   3503 C  CZ2 . TRP A 1 439 ? -0.95548  7.14967  -26.91042 1.000 42.15576 ? 642  TRP A CZ2 1 
ATOM   3504 C  CZ3 . TRP A 1 439 ? -2.44945  6.71378  -25.05440 1.000 37.09952 ? 642  TRP A CZ3 1 
ATOM   3505 C  CH2 . TRP A 1 439 ? -1.45054  6.30398  -25.95220 1.000 37.40984 ? 642  TRP A CH2 1 
ATOM   3506 N  N   . LEU A 1 440 ? -6.28744  9.22748  -25.50744 1.000 35.28747 ? 643  LEU A N   1 
ATOM   3507 C  CA  . LEU A 1 440 ? -6.85781  7.88654  -25.47202 1.000 33.95306 ? 643  LEU A CA  1 
ATOM   3508 C  C   . LEU A 1 440 ? -8.04297  7.76251  -26.41865 1.000 41.18542 ? 643  LEU A C   1 
ATOM   3509 O  O   . LEU A 1 440 ? -8.15075  6.78933  -27.17307 1.000 43.94488 ? 643  LEU A O   1 
ATOM   3510 C  CB  . LEU A 1 440 ? -7.27010  7.54293  -24.04720 1.000 39.97009 ? 643  LEU A CB  1 
ATOM   3511 C  CG  . LEU A 1 440 ? -7.40863  6.06184  -23.74107 1.000 49.68006 ? 643  LEU A CG  1 
ATOM   3512 C  CD1 . LEU A 1 440 ? -6.15887  5.33133  -24.19756 1.000 43.96877 ? 643  LEU A CD1 1 
ATOM   3513 C  CD2 . LEU A 1 440 ? -7.60169  5.91002  -22.24683 1.000 50.29120 ? 643  LEU A CD2 1 
ATOM   3514 N  N   . GLU A 1 441 ? -8.93908  8.74798  -26.40203 1.000 36.77867 ? 644  GLU A N   1 
ATOM   3515 C  CA  . GLU A 1 441 ? -10.08302 8.72015  -27.30148 1.000 37.93900 ? 644  GLU A CA  1 
ATOM   3516 C  C   . GLU A 1 441 ? -9.63944  8.71629  -28.75804 1.000 44.56404 ? 644  GLU A C   1 
ATOM   3517 O  O   . GLU A 1 441 ? -10.26578 8.06622  -29.60327 1.000 43.60920 ? 644  GLU A O   1 
ATOM   3518 C  CB  . GLU A 1 441 ? -10.99943 9.91153  -27.01780 1.000 41.31523 ? 644  GLU A CB  1 
ATOM   3519 C  CG  . GLU A 1 441 ? -12.13861 10.08096 -28.01890 1.000 45.87507 ? 644  GLU A CG  1 
ATOM   3520 N  N   . ALA A 1 442 ? -8.56694  9.44570  -29.07849 1.000 42.32126 ? 645  ALA A N   1 
ATOM   3521 C  CA  . ALA A 1 442 ? -8.09926  9.46753  -30.46198 1.000 44.43655 ? 645  ALA A CA  1 
ATOM   3522 C  C   . ALA A 1 442 ? -7.57028  8.10489  -30.88343 1.000 45.47208 ? 645  ALA A C   1 
ATOM   3523 O  O   . ALA A 1 442 ? -7.69728  7.72202  -32.05368 1.000 47.38123 ? 645  ALA A O   1 
ATOM   3524 C  CB  . ALA A 1 442 ? -7.01844  10.53543 -30.64682 1.000 34.36960 ? 645  ALA A CB  1 
ATOM   3525 N  N   . HIS A 1 443 ? -6.98962  7.36072  -29.94202 1.000 39.42603 ? 646  HIS A N   1 
ATOM   3526 C  CA  . HIS A 1 443 ? -6.45912  6.04280  -30.26014 1.000 47.22732 ? 646  HIS A CA  1 
ATOM   3527 C  C   . HIS A 1 443 ? -7.58036  5.04427  -30.53159 1.000 50.80348 ? 646  HIS A C   1 
ATOM   3528 O  O   . HIS A 1 443 ? -7.57160  4.34871  -31.55654 1.000 51.53999 ? 646  HIS A O   1 
ATOM   3529 C  CB  . HIS A 1 443 ? -5.56516  5.56293  -29.12485 1.000 45.35961 ? 646  HIS A CB  1 
ATOM   3530 C  CG  . HIS A 1 443 ? -4.32050  4.89202  -29.59742 1.000 53.86133 ? 646  HIS A CG  1 
ATOM   3531 N  ND1 . HIS A 1 443 ? -3.10321  5.53752  -29.65051 1.000 50.48418 ? 646  HIS A ND1 1 
ATOM   3532 C  CD2 . HIS A 1 443 ? -4.10826  3.63961  -30.06691 1.000 52.81113 ? 646  HIS A CD2 1 
ATOM   3533 C  CE1 . HIS A 1 443 ? -2.19057  4.70486  -30.11983 1.000 51.71424 ? 646  HIS A CE1 1 
ATOM   3534 N  NE2 . HIS A 1 443 ? -2.77457  3.54787  -30.38107 1.000 60.15887 ? 646  HIS A NE2 1 
ATOM   3535 N  N   . GLN A 1 444 ? -8.56666  4.97333  -29.63122 1.000 47.66905 ? 647  GLN A N   1 
ATOM   3536 C  CA  . GLN A 1 444 ? -9.70206  4.07513  -29.82345 1.000 54.85529 ? 647  GLN A CA  1 
ATOM   3537 C  C   . GLN A 1 444 ? -10.51310 4.41757  -31.07308 1.000 61.58798 ? 647  GLN A C   1 
ATOM   3538 O  O   . GLN A 1 444 ? -11.18570 3.53588  -31.62680 1.000 57.20118 ? 647  GLN A O   1 
ATOM   3539 C  CB  . GLN A 1 444 ? -10.57819 4.08699  -28.56647 1.000 56.21255 ? 647  GLN A CB  1 
ATOM   3540 C  CG  . GLN A 1 444 ? -9.97512  3.26593  -27.41995 1.000 65.12628 ? 647  GLN A CG  1 
ATOM   3541 C  CD  . GLN A 1 444 ? -10.31398 3.79387  -26.02200 1.000 73.99276 ? 647  GLN A CD  1 
ATOM   3542 O  OE1 . GLN A 1 444 ? -11.27241 4.54755  -25.83747 1.000 80.41102 ? 647  GLN A OE1 1 
ATOM   3543 N  NE2 . GLN A 1 444 ? -9.51731  3.39368  -25.03082 1.000 62.74727 ? 647  GLN A NE2 1 
ATOM   3544 N  N   . LYS A 1 445 ? -10.44182 5.66515  -31.54976 1.000 56.24026 ? 648  LYS A N   1 
ATOM   3545 C  CA  . LYS A 1 445 ? -11.07752 6.01377  -32.81473 1.000 56.40586 ? 648  LYS A CA  1 
ATOM   3546 C  C   . LYS A 1 445 ? -10.25239 5.56056  -34.01301 1.000 58.55578 ? 648  LYS A C   1 
ATOM   3547 O  O   . LYS A 1 445 ? -10.81363 5.29478  -35.08101 1.000 57.74701 ? 648  LYS A O   1 
ATOM   3548 C  CB  . LYS A 1 445 ? -11.31673 7.52125  -32.89358 1.000 54.65617 ? 648  LYS A CB  1 
ATOM   3549 N  N   . GLY A 1 446 ? -8.93385  5.47217  -33.86935 1.000 56.29136 ? 649  GLY A N   1 
ATOM   3550 C  CA  . GLY A 1 446 ? -8.11284  4.99994  -34.96629 1.000 60.94168 ? 649  GLY A CA  1 
ATOM   3551 C  C   . GLY A 1 446 ? -7.97755  3.48937  -34.98587 1.000 60.53954 ? 649  GLY A C   1 
ATOM   3552 O  O   . GLY A 1 446 ? -7.10107  2.93895  -35.66249 1.000 60.12258 ? 649  GLY A O   1 
ATOM   3553 N  N   . GLU A 1 447 ? -8.85336  2.81457  -34.24762 1.000 56.26016 ? 650  GLU A N   1 
ATOM   3554 C  CA  . GLU A 1 447 ? -8.77943  1.37722  -34.04385 1.000 59.65519 ? 650  GLU A CA  1 
ATOM   3555 C  C   . GLU A 1 447 ? -8.96769  0.59802  -35.35018 1.000 65.13071 ? 650  GLU A C   1 
ATOM   3556 O  O   . GLU A 1 447 ? -9.68724  1.03346  -36.25209 1.000 64.86263 ? 650  GLU A O   1 
ATOM   3557 C  CB  . GLU A 1 447 ? -9.82924  0.95731  -33.01580 1.000 56.59609 ? 650  GLU A CB  1 
ATOM   3558 C  CG  . GLU A 1 447 ? -9.42645  -0.19626 -32.11450 1.000 66.96662 ? 650  GLU A CG  1 
ATOM   3559 C  CD  . GLU A 1 447 ? -8.36750  0.18740  -31.08552 1.000 69.72483 ? 650  GLU A CD  1 
ATOM   3560 O  OE1 . GLU A 1 447 ? -7.21775  0.47318  -31.48599 1.000 68.92087 ? 650  GLU A OE1 1 
ATOM   3561 O  OE2 . GLU A 1 447 ? -8.68150  0.19594  -29.87316 1.000 63.24691 ? 650  GLU A OE2 1 
HETATM 3562 C  C1  . EDO B 2 .   ? 3.94511   31.14095 13.09774  0.931 42.34769 ? 701  EDO A C1  1 
HETATM 3563 O  O1  . EDO B 2 .   ? 4.01981   32.44757 13.62431  0.931 34.79054 ? 701  EDO A O1  1 
HETATM 3564 C  C2  . EDO B 2 .   ? 4.27172   31.17090 11.63037  0.931 32.40657 ? 701  EDO A C2  1 
HETATM 3565 O  O2  . EDO B 2 .   ? 3.46999   32.15027 11.01659  0.931 35.61449 ? 701  EDO A O2  1 
HETATM 3566 C  C1  . EDO C 2 .   ? 7.31990   4.60838  -6.30943  0.820 32.04801 ? 702  EDO A C1  1 
HETATM 3567 O  O1  . EDO C 2 .   ? 7.22084   4.86677  -4.92135  0.820 36.63903 ? 702  EDO A O1  1 
HETATM 3568 C  C2  . EDO C 2 .   ? 7.54945   3.13905  -6.54964  0.820 33.98313 ? 702  EDO A C2  1 
HETATM 3569 O  O2  . EDO C 2 .   ? 8.89926   2.79793  -6.31237  0.820 34.49076 ? 702  EDO A O2  1 
HETATM 3570 C  C1  . EDO D 2 .   ? 23.93780  20.72540 -20.30425 1.000 55.00599 ? 703  EDO A C1  1 
HETATM 3571 O  O1  . EDO D 2 .   ? 24.19080  19.77093 -19.29397 1.000 58.45941 ? 703  EDO A O1  1 
HETATM 3572 C  C2  . EDO D 2 .   ? 23.84076  20.08610 -21.66998 1.000 54.90066 ? 703  EDO A C2  1 
HETATM 3573 O  O2  . EDO D 2 .   ? 24.82930  19.09166 -21.83069 1.000 59.00509 ? 703  EDO A O2  1 
HETATM 3574 C  C1  . EDO E 2 .   ? 6.60906   26.61529 -20.08225 0.811 51.35855 ? 704  EDO A C1  1 
HETATM 3575 O  O1  . EDO E 2 .   ? 7.58730   26.78397 -19.07707 0.811 46.99750 ? 704  EDO A O1  1 
HETATM 3576 C  C2  . EDO E 2 .   ? 5.64199   25.51970 -19.70645 0.811 40.84178 ? 704  EDO A C2  1 
HETATM 3577 O  O2  . EDO E 2 .   ? 4.36346   26.07263 -19.47195 0.811 46.56768 ? 704  EDO A O2  1 
HETATM 3578 C  C1  . EDO F 2 .   ? 12.76218  34.40505 12.37206  0.892 57.22286 ? 705  EDO A C1  1 
HETATM 3579 O  O1  . EDO F 2 .   ? 14.09928  34.85893 12.34067  0.892 64.11550 ? 705  EDO A O1  1 
HETATM 3580 C  C2  . EDO F 2 .   ? 12.18893  34.41048 10.97506  0.892 50.09159 ? 705  EDO A C2  1 
HETATM 3581 O  O2  . EDO F 2 .   ? 11.40664  35.56639 10.77898  0.892 51.83957 ? 705  EDO A O2  1 
HETATM 3582 C  C1  . EDO G 2 .   ? 2.15474   37.64019 10.41017  0.828 38.60733 ? 706  EDO A C1  1 
HETATM 3583 O  O1  . EDO G 2 .   ? 3.37904   38.11287 9.89137   0.828 44.66595 ? 706  EDO A O1  1 
HETATM 3584 C  C2  . EDO G 2 .   ? 1.08806   38.68802 10.21332  0.828 39.73634 ? 706  EDO A C2  1 
HETATM 3585 O  O2  . EDO G 2 .   ? 1.58888   39.95181 10.60820  0.828 45.68947 ? 706  EDO A O2  1 
HETATM 3586 C  C1  . EDO H 2 .   ? 19.39464  0.02961  2.66598   0.783 42.91011 ? 707  EDO A C1  1 
HETATM 3587 O  O1  . EDO H 2 .   ? 19.80690  1.37986  2.60774   0.783 35.79635 ? 707  EDO A O1  1 
HETATM 3588 C  C2  . EDO H 2 .   ? 18.15510  -0.11105 3.51578   0.783 37.35238 ? 707  EDO A C2  1 
HETATM 3589 O  O2  . EDO H 2 .   ? 18.29264  0.62985  4.70711   0.783 41.02318 ? 707  EDO A O2  1 
HETATM 3590 C  C1  . EDO I 2 .   ? 23.75100  14.26224 6.74203   0.876 50.07827 ? 708  EDO A C1  1 
HETATM 3591 O  O1  . EDO I 2 .   ? 24.81041  14.99568 6.16361   0.876 55.68646 ? 708  EDO A O1  1 
HETATM 3592 C  C2  . EDO I 2 .   ? 24.17201  12.83151 6.97534   0.876 50.45713 ? 708  EDO A C2  1 
HETATM 3593 O  O2  . EDO I 2 .   ? 24.75765  12.29000 5.81140   0.876 43.53691 ? 708  EDO A O2  1 
HETATM 3594 C  C1  . EDO J 2 .   ? 4.16888   36.93178 14.60674  0.817 52.60189 ? 709  EDO A C1  1 
HETATM 3595 O  O1  . EDO J 2 .   ? 4.33348   38.23773 14.09739  0.817 52.45915 ? 709  EDO A O1  1 
HETATM 3596 C  C2  . EDO J 2 .   ? 4.02071   36.99391 16.10673  0.817 43.31721 ? 709  EDO A C2  1 
HETATM 3597 O  O2  . EDO J 2 .   ? 3.00130   37.91211 16.40973  0.817 39.22534 ? 709  EDO A O2  1 
HETATM 3598 C  C1  . EDO K 2 .   ? 17.11647  3.92480  -8.71992  0.860 37.28535 ? 710  EDO A C1  1 
HETATM 3599 O  O1  . EDO K 2 .   ? 17.40718  3.68108  -10.08223 0.860 42.63505 ? 710  EDO A O1  1 
HETATM 3600 C  C2  . EDO K 2 .   ? 15.74961  3.35611  -8.45965  0.860 33.40414 ? 710  EDO A C2  1 
HETATM 3601 O  O2  . EDO K 2 .   ? 15.36486  2.69891  -9.64676  0.860 47.18854 ? 710  EDO A O2  1 
HETATM 3602 C  C1  . EDO L 2 .   ? 5.27390   6.02726  12.02467  0.835 36.02179 ? 711  EDO A C1  1 
HETATM 3603 O  O1  . EDO L 2 .   ? 6.28855   6.85402  12.55380  0.835 52.59440 ? 711  EDO A O1  1 
HETATM 3604 C  C2  . EDO L 2 .   ? 5.72071   4.59441  12.10937  0.835 47.52695 ? 711  EDO A C2  1 
HETATM 3605 O  O2  . EDO L 2 .   ? 5.13034   3.87563  11.05139  0.835 53.40139 ? 711  EDO A O2  1 
HETATM 3606 C  C1  . EDO M 2 .   ? 16.23316  35.16664 -0.31671  0.962 55.91184 ? 712  EDO A C1  1 
HETATM 3607 O  O1  . EDO M 2 .   ? 16.45071  34.30023 0.78305   0.962 60.27814 ? 712  EDO A O1  1 
HETATM 3608 C  C2  . EDO M 2 .   ? 15.17995  36.18659 0.03527   0.962 49.83299 ? 712  EDO A C2  1 
HETATM 3609 O  O2  . EDO M 2 .   ? 14.01121  35.92992 -0.70919  0.962 45.69735 ? 712  EDO A O2  1 
HETATM 3610 C  C1  . EDO N 2 .   ? 4.36377   53.58320 15.83774  0.897 60.64187 ? 713  EDO A C1  1 
HETATM 3611 O  O1  . EDO N 2 .   ? 5.18243   53.35822 16.96682  0.897 52.42856 ? 713  EDO A O1  1 
HETATM 3612 C  C2  . EDO N 2 .   ? 3.52463   54.82372 16.03539  0.897 51.75252 ? 713  EDO A C2  1 
HETATM 3613 O  O2  . EDO N 2 .   ? 3.24231   54.98230 17.40966  0.897 50.35622 ? 713  EDO A O2  1 
HETATM 3614 C  C1  . EDO O 2 .   ? -6.10769  10.08287 -5.31854  0.733 48.80593 ? 714  EDO A C1  1 
HETATM 3615 O  O1  . EDO O 2 .   ? -6.65969  11.11032 -6.10607  0.733 46.82916 ? 714  EDO A O1  1 
HETATM 3616 C  C2  . EDO O 2 .   ? -6.80498  10.09728 -3.98841  0.733 48.26696 ? 714  EDO A C2  1 
HETATM 3617 O  O2  . EDO O 2 .   ? -6.89283  11.43785 -3.56051  0.733 47.44874 ? 714  EDO A O2  1 
HETATM 3618 C  C1  . EDO P 2 .   ? 19.34983  22.37620 10.52263  0.836 56.81843 ? 715  EDO A C1  1 
HETATM 3619 O  O1  . EDO P 2 .   ? 19.15526  21.31095 11.43171  0.836 55.28446 ? 715  EDO A O1  1 
HETATM 3620 C  C2  . EDO P 2 .   ? 19.28819  21.87135 9.10103   0.836 49.39427 ? 715  EDO A C2  1 
HETATM 3621 O  O2  . EDO P 2 .   ? 20.29362  20.90163 8.89771   0.836 52.95353 ? 715  EDO A O2  1 
HETATM 3622 CL CL  . CL  Q 3 .   ? -12.44634 55.46243 15.31521  1.000 37.15299 ? 716  CL  A CL  1 
HETATM 3623 CL CL  . CL  R 3 .   ? -4.35283  10.14065 -0.89654  1.000 51.28666 ? 717  CL  A CL  1 
HETATM 3624 C  C1  . EDO S 2 .   ? -3.61459  10.13648 8.38960   0.712 30.75527 ? 718  EDO A C1  1 
HETATM 3625 O  O1  . EDO S 2 .   ? -3.42754  9.07411  7.48046   0.712 44.85562 ? 718  EDO A O1  1 
HETATM 3626 C  C2  . EDO S 2 .   ? -5.08161  10.27262 8.71615   0.712 45.44869 ? 718  EDO A C2  1 
HETATM 3627 O  O2  . EDO S 2 .   ? -5.66107  11.30167 7.94318   0.712 42.15687 ? 718  EDO A O2  1 
HETATM 3628 C  C1  . EDO T 2 .   ? -0.22440  43.55208 12.93676  0.982 31.61899 ? 719  EDO A C1  1 
HETATM 3629 O  O1  . EDO T 2 .   ? 0.71902   44.53366 12.63706  0.982 36.19392 ? 719  EDO A O1  1 
HETATM 3630 C  C2  . EDO T 2 .   ? -1.55326  44.01674 12.43136  0.982 28.68518 ? 719  EDO A C2  1 
HETATM 3631 O  O2  . EDO T 2 .   ? -2.18055  42.98503 11.70637  0.982 38.50285 ? 719  EDO A O2  1 
HETATM 3632 O  O   . HOH U 4 .   ? 14.22061  28.48875 14.15166  1.000 48.43496 ? 801  HOH A O   1 
HETATM 3633 O  O   . HOH U 4 .   ? 15.57927  37.60139 3.61838   1.000 51.64795 ? 802  HOH A O   1 
HETATM 3634 O  O   . HOH U 4 .   ? 20.68966  23.68423 -5.70026  1.000 50.06653 ? 803  HOH A O   1 
HETATM 3635 O  O   . HOH U 4 .   ? 8.97999   24.62420 -29.22326 1.000 57.86528 ? 804  HOH A O   1 
HETATM 3636 O  O   . HOH U 4 .   ? -3.49308  44.42164 3.44475   1.000 38.74296 ? 805  HOH A O   1 
HETATM 3637 O  O   . HOH U 4 .   ? 4.99669   55.34202 19.00549  1.000 55.73232 ? 806  HOH A O   1 
HETATM 3638 O  O   . HOH U 4 .   ? -4.49294  18.00524 -11.38464 1.000 39.04824 ? 807  HOH A O   1 
HETATM 3639 O  O   . HOH U 4 .   ? -0.15830  23.55413 -13.39268 1.000 25.34971 ? 808  HOH A O   1 
HETATM 3640 O  O   . HOH U 4 .   ? 15.51021  7.15411  -32.07583 1.000 38.35736 ? 809  HOH A O   1 
HETATM 3641 O  O   . HOH U 4 .   ? 8.96989   37.30048 11.05551  1.000 44.72218 ? 810  HOH A O   1 
HETATM 3642 O  O   . HOH U 4 .   ? -7.82360  48.92539 6.93057   1.000 55.28271 ? 811  HOH A O   1 
HETATM 3643 O  O   . HOH U 4 .   ? 1.39830   37.43064 21.77285  1.000 43.85235 ? 812  HOH A O   1 
HETATM 3644 O  O   . HOH U 4 .   ? 9.28606   0.79944  -7.72263  1.000 44.06341 ? 813  HOH A O   1 
HETATM 3645 O  O   . HOH U 4 .   ? -0.44342  8.73595  -4.73952  1.000 33.74017 ? 814  HOH A O   1 
HETATM 3646 O  O   . HOH U 4 .   ? 5.78751   28.86220 15.94721  1.000 39.60727 ? 815  HOH A O   1 
HETATM 3647 O  O   . HOH U 4 .   ? -7.07326  51.93568 6.81883   1.000 53.07918 ? 816  HOH A O   1 
HETATM 3648 O  O   . HOH U 4 .   ? 17.94549  24.72791 -24.41424 1.000 55.79102 ? 817  HOH A O   1 
HETATM 3649 O  O   . HOH U 4 .   ? 4.18009   4.91427  8.96464   1.000 33.78337 ? 818  HOH A O   1 
HETATM 3650 O  O   . HOH U 4 .   ? 13.58483  17.08866 -2.33490  1.000 23.91525 ? 819  HOH A O   1 
HETATM 3651 O  O   . HOH U 4 .   ? -11.20761 19.81191 -8.93731  1.000 53.96794 ? 820  HOH A O   1 
HETATM 3652 O  O   . HOH U 4 .   ? 3.33986   0.20864  -27.79265 1.000 40.99775 ? 821  HOH A O   1 
HETATM 3653 O  O   . HOH U 4 .   ? 2.53207   45.96634 11.57141  1.000 45.69472 ? 822  HOH A O   1 
HETATM 3654 O  O   . HOH U 4 .   ? 19.95380  12.21494 7.09085   1.000 43.90838 ? 823  HOH A O   1 
HETATM 3655 O  O   . HOH U 4 .   ? 15.49986  11.23598 -0.15610  1.000 29.49169 ? 824  HOH A O   1 
HETATM 3656 O  O   . HOH U 4 .   ? 10.93549  8.00662  -15.80026 1.000 24.55801 ? 825  HOH A O   1 
HETATM 3657 O  O   . HOH U 4 .   ? 9.94196   25.99881 -19.72415 1.000 42.19809 ? 826  HOH A O   1 
HETATM 3658 O  O   . HOH U 4 .   ? -0.34399  41.77659 10.37613  0.828 35.90186 ? 827  HOH A O   1 
HETATM 3659 O  O   . HOH U 4 .   ? 5.04055   6.03968  -4.22649  1.000 38.44464 ? 828  HOH A O   1 
HETATM 3660 O  O   . HOH U 4 .   ? -12.15451 30.22542 17.97621  1.000 51.30732 ? 829  HOH A O   1 
HETATM 3661 O  O   . HOH U 4 .   ? -3.24504  14.16784 9.42709   1.000 42.15338 ? 830  HOH A O   1 
HETATM 3662 O  O   . HOH U 4 .   ? 12.88985  13.98473 -27.33982 1.000 45.58889 ? 831  HOH A O   1 
HETATM 3663 O  O   . HOH U 4 .   ? -2.309    76.385   38.598    1.000 44.32027 ? 832  HOH A O   1 
HETATM 3664 O  O   . HOH U 4 .   ? -6.71613  29.53693 14.73186  1.000 34.12853 ? 833  HOH A O   1 
HETATM 3665 O  O   . HOH U 4 .   ? 19.04538  4.93373  -11.67056 1.000 40.85901 ? 834  HOH A O   1 
HETATM 3666 O  O   . HOH U 4 .   ? -9.10226  25.39465 11.73761  1.000 40.93161 ? 835  HOH A O   1 
HETATM 3667 O  O   . HOH U 4 .   ? 1.22358   9.54072  2.89080   1.000 24.83995 ? 836  HOH A O   1 
HETATM 3668 O  O   . HOH U 4 .   ? -12.56378 36.89291 15.60252  1.000 34.13959 ? 837  HOH A O   1 
HETATM 3669 O  O   . HOH U 4 .   ? 11.87796  23.48150 9.14109   1.000 32.95657 ? 838  HOH A O   1 
HETATM 3670 O  O   . HOH U 4 .   ? 15.92274  21.19488 15.73353  1.000 52.01601 ? 839  HOH A O   1 
HETATM 3671 O  O   . HOH U 4 .   ? -7.30435  30.91308 2.67017   1.000 37.39450 ? 840  HOH A O   1 
HETATM 3672 O  O   . HOH U 4 .   ? -7.15815  66.76013 30.81234  1.000 26.89896 ? 841  HOH A O   1 
HETATM 3673 O  O   . HOH U 4 .   ? -8.83254  28.72383 19.43507  1.000 47.32919 ? 842  HOH A O   1 
HETATM 3674 O  O   . HOH U 4 .   ? 19.87460  11.61652 -7.99825  1.000 28.65534 ? 843  HOH A O   1 
HETATM 3675 O  O   . HOH U 4 .   ? -2.43907  32.66158 12.24525  1.000 32.38777 ? 844  HOH A O   1 
HETATM 3676 O  O   . HOH U 4 .   ? 2.48530   9.19345  -4.46599  1.000 35.48250 ? 845  HOH A O   1 
HETATM 3677 O  O   . HOH U 4 .   ? 12.35174  9.04068  7.51446   1.000 28.06022 ? 846  HOH A O   1 
HETATM 3678 O  O   . HOH U 4 .   ? -9.21864  36.43176 14.37783  1.000 31.90278 ? 847  HOH A O   1 
HETATM 3679 O  O   . HOH U 4 .   ? -6.42761  17.67651 -14.94389 1.000 39.57901 ? 848  HOH A O   1 
HETATM 3680 O  O   . HOH U 4 .   ? -3.98981  15.04998 -25.97052 1.000 34.69241 ? 849  HOH A O   1 
HETATM 3681 O  O   . HOH U 4 .   ? 20.95904  7.02321  7.11267   1.000 38.43261 ? 850  HOH A O   1 
HETATM 3682 O  O   . HOH U 4 .   ? 3.03656   32.49287 16.08978  1.000 39.90326 ? 851  HOH A O   1 
HETATM 3683 O  O   . HOH U 4 .   ? 15.51512  16.57559 3.26004   1.000 22.81249 ? 852  HOH A O   1 
HETATM 3684 O  O   . HOH U 4 .   ? 28.68448  17.07343 1.48024   1.000 43.13972 ? 853  HOH A O   1 
HETATM 3685 O  O   . HOH U 4 .   ? -3.79468  -1.12240 -25.69485 1.000 54.74180 ? 854  HOH A O   1 
HETATM 3686 O  O   . HOH U 4 .   ? 7.49037   9.43327  1.29712   1.000 21.34689 ? 855  HOH A O   1 
HETATM 3687 O  O   . HOH U 4 .   ? -7.76842  74.09134 33.57884  1.000 39.36426 ? 856  HOH A O   1 
HETATM 3688 O  O   . HOH U 4 .   ? 18.97069  15.14137 -9.58429  1.000 27.03607 ? 857  HOH A O   1 
HETATM 3689 O  O   . HOH U 4 .   ? -0.86463  51.37514 29.10965  1.000 42.28625 ? 858  HOH A O   1 
HETATM 3690 O  O   . HOH U 4 .   ? 1.56645   59.66829 32.15316  1.000 44.12204 ? 859  HOH A O   1 
HETATM 3691 O  O   . HOH U 4 .   ? 10.61938  5.73621  8.60187   1.000 42.93818 ? 860  HOH A O   1 
HETATM 3692 O  O   . HOH U 4 .   ? -7.30050  37.05572 10.51893  1.000 38.80199 ? 861  HOH A O   1 
HETATM 3693 O  O   . HOH U 4 .   ? -3.30591  70.59141 38.35322  1.000 38.03271 ? 862  HOH A O   1 
HETATM 3694 O  O   . HOH U 4 .   ? 34.11283  8.85473  1.00893   1.000 37.12829 ? 863  HOH A O   1 
HETATM 3695 O  O   . HOH U 4 .   ? -2.51176  26.23403 -9.85992  1.000 33.09554 ? 864  HOH A O   1 
HETATM 3696 O  O   . HOH U 4 .   ? -2.712    43.155   29.139    1.000 31.73757 ? 865  HOH A O   1 
HETATM 3697 O  O   . HOH U 4 .   ? 0.12461   49.05040 17.88702  1.000 30.39318 ? 866  HOH A O   1 
HETATM 3698 O  O   . HOH U 4 .   ? -2.80858  20.50705 14.51998  1.000 30.37635 ? 867  HOH A O   1 
HETATM 3699 O  O   . HOH U 4 .   ? 12.62953  6.62267  3.55572   1.000 29.66574 ? 868  HOH A O   1 
HETATM 3700 O  O   . HOH U 4 .   ? -4.45769  32.92031 24.06737  1.000 38.61290 ? 869  HOH A O   1 
HETATM 3701 O  O   . HOH U 4 .   ? 10.24824  30.22782 -12.41203 1.000 44.94153 ? 870  HOH A O   1 
HETATM 3702 O  O   . HOH U 4 .   ? -5.00371  10.83353 -13.58644 1.000 43.16381 ? 871  HOH A O   1 
HETATM 3703 O  O   . HOH U 4 .   ? -17.46298 43.01667 19.41488  1.000 44.38299 ? 872  HOH A O   1 
HETATM 3704 O  O   . HOH U 4 .   ? 4.50353   4.34312  0.52356   1.000 30.63965 ? 873  HOH A O   1 
HETATM 3705 O  O   . HOH U 4 .   ? 2.37144   3.34842  -15.31101 1.000 34.50829 ? 874  HOH A O   1 
HETATM 3706 O  O   . HOH U 4 .   ? 18.50886  7.14713  0.83376   1.000 28.38130 ? 875  HOH A O   1 
HETATM 3707 O  O   . HOH U 4 .   ? 15.83273  7.13749  1.97435   1.000 39.90136 ? 876  HOH A O   1 
HETATM 3708 O  O   . HOH U 4 .   ? -16.06915 41.61491 21.01394  1.000 35.04805 ? 877  HOH A O   1 
HETATM 3709 O  O   . HOH U 4 .   ? 5.51562   58.89290 25.92758  1.000 42.28685 ? 878  HOH A O   1 
HETATM 3710 O  O   . HOH U 4 .   ? -3.72565  70.42357 25.79341  1.000 35.64523 ? 879  HOH A O   1 
HETATM 3711 O  O   . HOH U 4 .   ? 3.88913   2.81162  -8.11011  1.000 35.17560 ? 880  HOH A O   1 
HETATM 3712 O  O   . HOH U 4 .   ? -2.99385  0.25847  -15.48099 1.000 48.36150 ? 881  HOH A O   1 
HETATM 3713 O  O   . HOH U 4 .   ? 4.39959   -0.99202 6.13893   1.000 38.67566 ? 882  HOH A O   1 
HETATM 3714 O  O   . HOH U 4 .   ? -11.49279 58.36188 35.71847  1.000 25.71314 ? 883  HOH A O   1 
HETATM 3715 O  O   . HOH U 4 .   ? 7.74184   21.10148 17.22508  1.000 27.06893 ? 884  HOH A O   1 
HETATM 3716 O  O   . HOH U 4 .   ? 1.00861   64.49790 25.83031  1.000 34.36165 ? 885  HOH A O   1 
HETATM 3717 O  O   . HOH U 4 .   ? 0.68745   9.11317  5.83662   1.000 29.31031 ? 886  HOH A O   1 
HETATM 3718 O  O   . HOH U 4 .   ? 12.81576  19.64842 -3.12351  1.000 24.91385 ? 887  HOH A O   1 
HETATM 3719 O  O   . HOH U 4 .   ? 33.97288  6.20794  -7.66396  1.000 50.66805 ? 888  HOH A O   1 
HETATM 3720 O  O   . HOH U 4 .   ? -4.51701  71.99032 19.70632  1.000 45.53626 ? 889  HOH A O   1 
HETATM 3721 O  O   . HOH U 4 .   ? 13.05729  17.96281 3.16629   1.000 25.22942 ? 890  HOH A O   1 
HETATM 3722 O  O   . HOH U 4 .   ? 13.68782  11.76743 -29.65593 1.000 44.53610 ? 891  HOH A O   1 
HETATM 3723 O  O   . HOH U 4 .   ? 16.53603  26.38390 4.76279   1.000 51.51356 ? 892  HOH A O   1 
HETATM 3724 O  O   . HOH U 4 .   ? -0.63085  18.75950 14.93195  1.000 42.15475 ? 893  HOH A O   1 
HETATM 3725 O  O   . HOH U 4 .   ? -4.06804  0.98297  -17.65107 1.000 41.39379 ? 894  HOH A O   1 
HETATM 3726 O  O   . HOH U 4 .   ? 24.78284  7.39860  -7.39473  1.000 35.74390 ? 895  HOH A O   1 
HETATM 3727 O  O   . HOH U 4 .   ? 13.40296  36.44048 -3.71530  1.000 57.76052 ? 896  HOH A O   1 
HETATM 3728 O  O   . HOH U 4 .   ? -4.70663  70.37378 23.08079  1.000 40.16466 ? 897  HOH A O   1 
HETATM 3729 O  O   . HOH U 4 .   ? -1.91179  17.42796 10.47430  1.000 36.07883 ? 898  HOH A O   1 
HETATM 3730 O  O   . HOH U 4 .   ? -13.73081 29.33659 15.04284  1.000 46.11217 ? 899  HOH A O   1 
HETATM 3731 O  O   . HOH U 4 .   ? 1.94724   5.64637  11.48667  1.000 37.66652 ? 900  HOH A O   1 
HETATM 3732 O  O   . HOH U 4 .   ? 21.62737  17.73879 3.60825   1.000 42.29859 ? 901  HOH A O   1 
HETATM 3733 O  O   . HOH U 4 .   ? -1.66365  39.91383 12.77552  1.000 30.67625 ? 902  HOH A O   1 
HETATM 3734 O  O   . HOH U 4 .   ? -3.06504  62.44078 19.13355  1.000 30.05088 ? 903  HOH A O   1 
HETATM 3735 O  O   . HOH U 4 .   ? -14.14343 48.59701 12.61915  1.000 43.59595 ? 904  HOH A O   1 
HETATM 3736 O  O   . HOH U 4 .   ? -3.24544  52.27842 31.33310  1.000 33.61749 ? 905  HOH A O   1 
HETATM 3737 O  O   . HOH U 4 .   ? 3.88418   19.20213 -4.59763  1.000 21.94341 ? 906  HOH A O   1 
HETATM 3738 O  O   . HOH U 4 .   ? -4.738    2.210    -34.409   1.000 41.48695 ? 907  HOH A O   1 
HETATM 3739 O  O   . HOH U 4 .   ? 17.82091  8.19843  4.59551   1.000 37.39314 ? 908  HOH A O   1 
HETATM 3740 O  O   . HOH U 4 .   ? -14.36765 52.54632 32.65015  1.000 33.52734 ? 909  HOH A O   1 
HETATM 3741 O  O   . HOH U 4 .   ? 1.53374   64.04058 12.44065  1.000 45.48089 ? 910  HOH A O   1 
HETATM 3742 O  O   . HOH U 4 .   ? -10.48079 70.87958 23.69916  1.000 50.50601 ? 911  HOH A O   1 
HETATM 3743 O  O   . HOH U 4 .   ? 7.00677   62.23198 22.47312  1.000 44.67630 ? 912  HOH A O   1 
HETATM 3744 O  O   A HOH U 4 .   ? -3.645    14.108   0.214     0.507 19.09884 ? 913  HOH A O   1 
HETATM 3745 O  O   B HOH U 4 .   ? -5.515    13.258   -1.086    0.493 28.67726 ? 913  HOH A O   1 
HETATM 3746 O  O   . HOH U 4 .   ? 2.31405   40.37623 14.13268  1.000 45.06441 ? 914  HOH A O   1 
HETATM 3747 O  O   . HOH U 4 .   ? 1.84901   53.04833 23.21391  1.000 32.42183 ? 915  HOH A O   1 
HETATM 3748 O  O   . HOH U 4 .   ? 18.53722  12.45236 -5.49783  1.000 27.42694 ? 916  HOH A O   1 
HETATM 3749 O  O   . HOH U 4 .   ? 6.09279   7.93047  -31.36662 1.000 33.48707 ? 917  HOH A O   1 
HETATM 3750 O  O   . HOH U 4 .   ? -3.04895  6.54407  -9.70131  1.000 42.80196 ? 918  HOH A O   1 
HETATM 3751 O  O   . HOH U 4 .   ? -3.75212  32.08478 -13.52784 1.000 47.10538 ? 919  HOH A O   1 
HETATM 3752 O  O   . HOH U 4 .   ? 14.73792  30.39066 6.46050   1.000 35.54370 ? 920  HOH A O   1 
HETATM 3753 O  O   . HOH U 4 .   ? -4.50020  45.27723 12.52541  1.000 32.00586 ? 921  HOH A O   1 
HETATM 3754 O  O   . HOH U 4 .   ? -3.65691  38.40513 12.93360  1.000 30.38793 ? 922  HOH A O   1 
HETATM 3755 O  O   . HOH U 4 .   ? -13.98459 64.89428 25.92986  1.000 43.97094 ? 923  HOH A O   1 
HETATM 3756 O  O   . HOH U 4 .   ? -8.17309  30.23961 22.36781  1.000 40.83543 ? 924  HOH A O   1 
HETATM 3757 O  O   . HOH U 4 .   ? -2.81734  41.56318 0.20521   1.000 42.22045 ? 925  HOH A O   1 
HETATM 3758 O  O   . HOH U 4 .   ? 24.85227  16.58826 -13.13979 1.000 46.53046 ? 926  HOH A O   1 
HETATM 3759 O  O   . HOH U 4 .   ? 9.23449   63.86606 16.99972  1.000 44.09122 ? 927  HOH A O   1 
HETATM 3760 O  O   . HOH U 4 .   ? -0.639    45.966   28.109    1.000 33.69210 ? 928  HOH A O   1 
HETATM 3761 O  O   . HOH U 4 .   ? 18.33067  8.47213  -6.54842  1.000 26.18284 ? 929  HOH A O   1 
HETATM 3762 O  O   . HOH U 4 .   ? -17.18251 59.54001 33.87198  1.000 38.32191 ? 930  HOH A O   1 
HETATM 3763 O  O   . HOH U 4 .   ? 7.43411   1.41995  0.77888   1.000 30.47258 ? 931  HOH A O   1 
HETATM 3764 O  O   . HOH U 4 .   ? 11.92304  13.20539 -31.71950 1.000 50.85936 ? 932  HOH A O   1 
HETATM 3765 O  O   . HOH U 4 .   ? -7.29291  20.86149 -12.94588 1.000 50.64181 ? 933  HOH A O   1 
HETATM 3766 O  O   . HOH U 4 .   ? 19.03202  17.50800 -26.06767 1.000 46.96715 ? 934  HOH A O   1 
HETATM 3767 O  O   . HOH U 4 .   ? 24.24854  6.03834  -3.47702  1.000 41.73609 ? 935  HOH A O   1 
HETATM 3768 O  O   . HOH U 4 .   ? 9.86073   22.97571 25.44269  1.000 40.56707 ? 936  HOH A O   1 
HETATM 3769 O  O   . HOH U 4 .   ? -14.19444 49.92290 20.31500  1.000 35.74572 ? 937  HOH A O   1 
HETATM 3770 O  O   . HOH U 4 .   ? 17.568    -0.849   7.029     1.000 46.67047 ? 938  HOH A O   1 
HETATM 3771 O  O   . HOH U 4 .   ? 14.84632  21.41386 -3.14744  1.000 30.01285 ? 939  HOH A O   1 
HETATM 3772 O  O   . HOH U 4 .   ? -2.77732  9.03547  13.56841  1.000 38.10484 ? 940  HOH A O   1 
HETATM 3773 O  O   . HOH U 4 .   ? 5.75570   10.35371 16.51112  1.000 43.30927 ? 941  HOH A O   1 
HETATM 3774 O  O   . HOH U 4 .   ? -11.27614 70.96974 33.34399  1.000 40.38206 ? 942  HOH A O   1 
HETATM 3775 O  O   . HOH U 4 .   ? -3.56750  19.07609 -4.79477  1.000 27.13217 ? 943  HOH A O   1 
HETATM 3776 O  O   A HOH U 4 .   ? -6.55804  67.48876 36.76637  0.577 31.91911 ? 944  HOH A O   1 
HETATM 3777 O  O   B HOH U 4 .   ? -8.61125  67.25206 36.89886  0.423 28.85279 ? 944  HOH A O   1 
HETATM 3778 O  O   . HOH U 4 .   ? 31.21342  8.35340  -6.63463  1.000 52.97916 ? 945  HOH A O   1 
HETATM 3779 O  O   . HOH U 4 .   ? -2.84609  12.91745 12.15179  1.000 50.22829 ? 946  HOH A O   1 
HETATM 3780 O  O   . HOH U 4 .   ? 11.13863  0.00000  0.00000   0.50  34.58823 ? 947  HOH A O   1 
HETATM 3781 O  O   . HOH U 4 .   ? -0.98809  74.00608 37.51591  1.000 46.35669 ? 948  HOH A O   1 
HETATM 3782 O  O   . HOH U 4 .   ? -7.30516  19.33144 8.80251   1.000 30.05223 ? 949  HOH A O   1 
HETATM 3783 O  O   . HOH U 4 .   ? -17.58857 43.48791 25.49332  1.000 44.93871 ? 950  HOH A O   1 
HETATM 3784 O  O   . HOH U 4 .   ? 1.72121   22.22132 -24.36475 1.000 46.88978 ? 951  HOH A O   1 
HETATM 3785 O  O   . HOH U 4 .   ? -12.57871 35.68171 13.21228  1.000 42.95806 ? 952  HOH A O   1 
HETATM 3786 O  O   . HOH U 4 .   ? -7.827    60.998   42.429    1.000 42.45983 ? 953  HOH A O   1 
HETATM 3787 O  O   . HOH U 4 .   ? 25.50902  -0.00000 -0.00000  0.647 53.55729 ? 954  HOH A O   1 
HETATM 3788 O  O   . HOH U 4 .   ? 17.10189  10.51502 -4.86134  1.000 29.66087 ? 955  HOH A O   1 
HETATM 3789 O  O   . HOH U 4 .   ? -3.78530  6.22990  -12.54895 1.000 34.39877 ? 956  HOH A O   1 
HETATM 3790 O  O   . HOH U 4 .   ? 14.09786  4.53774  -15.49705 1.000 38.48556 ? 957  HOH A O   1 
HETATM 3791 O  O   . HOH U 4 .   ? 15.39078  27.27784 16.39667  1.000 45.48118 ? 958  HOH A O   1 
HETATM 3792 O  O   . HOH U 4 .   ? -5.23557  51.96210 13.97241  1.000 28.39875 ? 959  HOH A O   1 
HETATM 3793 O  O   . HOH U 4 .   ? -14.99463 37.20035 19.06505  1.000 35.84488 ? 960  HOH A O   1 
HETATM 3794 O  O   . HOH U 4 .   ? -3.92602  16.28411 8.20944   1.000 36.59903 ? 961  HOH A O   1 
HETATM 3795 O  O   . HOH U 4 .   ? 8.98066   2.84694  -1.43638  1.000 31.67758 ? 962  HOH A O   1 
HETATM 3796 O  O   . HOH U 4 .   ? -6.536    38.704   33.057    1.000 41.86657 ? 963  HOH A O   1 
HETATM 3797 O  O   . HOH U 4 .   ? 17.91785  18.58107 10.18525  1.000 45.88901 ? 964  HOH A O   1 
HETATM 3798 O  O   . HOH U 4 .   ? 22.02916  23.02830 -11.72122 1.000 51.88349 ? 965  HOH A O   1 
HETATM 3799 O  O   . HOH U 4 .   ? -8.49602  0.41644  -25.11644 1.000 54.05903 ? 966  HOH A O   1 
HETATM 3800 O  O   . HOH U 4 .   ? 13.87231  40.34815 5.16098   1.000 54.30245 ? 967  HOH A O   1 
HETATM 3801 O  O   . HOH U 4 .   ? -7.71161  21.55129 -21.57316 1.000 48.89194 ? 968  HOH A O   1 
HETATM 3802 O  O   . HOH U 4 .   ? 18.09454  18.63474 -23.75206 1.000 38.43704 ? 969  HOH A O   1 
HETATM 3803 O  O   . HOH U 4 .   ? -3.63751  20.55758 -17.52139 1.000 31.43225 ? 970  HOH A O   1 
HETATM 3804 O  O   . HOH U 4 .   ? -16.08954 59.24661 24.67824  1.000 39.17465 ? 971  HOH A O   1 
HETATM 3805 O  O   . HOH U 4 .   ? 0.91635   6.54278  6.05104   1.000 31.53173 ? 972  HOH A O   1 
HETATM 3806 O  O   . HOH U 4 .   ? 12.18967  34.30888 -9.65395  1.000 55.03510 ? 973  HOH A O   1 
HETATM 3807 O  O   . HOH U 4 .   ? 16.49053  10.82999 7.99240   1.000 37.49571 ? 974  HOH A O   1 
HETATM 3808 O  O   . HOH U 4 .   ? -16.29436 65.13705 29.59364  1.000 48.38090 ? 975  HOH A O   1 
HETATM 3809 O  O   . HOH U 4 .   ? -12.31338 55.53864 37.02678  1.000 37.32160 ? 976  HOH A O   1 
HETATM 3810 O  O   . HOH U 4 .   ? 11.71411  27.76522 -11.05790 1.000 44.78244 ? 977  HOH A O   1 
HETATM 3811 O  O   . HOH U 4 .   ? 3.96009   60.79997 24.63220  1.000 39.76777 ? 978  HOH A O   1 
HETATM 3812 O  O   . HOH U 4 .   ? 8.35779   7.53199  -27.20141 1.000 36.63444 ? 979  HOH A O   1 
HETATM 3813 O  O   . HOH U 4 .   ? 18.45601  2.45284  -28.19282 1.000 45.04667 ? 980  HOH A O   1 
HETATM 3814 O  O   . HOH U 4 .   ? 32.34201  15.81294 4.45643   1.000 44.73718 ? 981  HOH A O   1 
HETATM 3815 O  O   . HOH U 4 .   ? 8.64064   1.75498  -3.55305  1.000 29.51015 ? 982  HOH A O   1 
HETATM 3816 O  O   . HOH U 4 .   ? 14.78901  18.25188 26.03907  1.000 49.58489 ? 983  HOH A O   1 
HETATM 3817 O  O   . HOH U 4 .   ? 20.39685  16.55546 1.62238   1.000 41.70664 ? 984  HOH A O   1 
HETATM 3818 O  O   . HOH U 4 .   ? -3.68440  36.07527 24.99517  1.000 42.13471 ? 985  HOH A O   1 
HETATM 3819 O  O   . HOH U 4 .   ? -2.63692  68.23647 37.27169  1.000 40.25772 ? 986  HOH A O   1 
HETATM 3820 O  O   . HOH U 4 .   ? 1.13927   47.98735 12.02017  1.000 44.89473 ? 987  HOH A O   1 
HETATM 3821 O  O   . HOH U 4 .   ? 17.49136  2.36674  -23.63459 1.000 46.40648 ? 988  HOH A O   1 
HETATM 3822 O  O   . HOH U 4 .   ? 14.85263  18.33681 16.88573  1.000 49.94083 ? 989  HOH A O   1 
HETATM 3823 O  O   . HOH U 4 .   ? 7.14050   14.07889 18.00161  1.000 29.25865 ? 990  HOH A O   1 
HETATM 3824 O  O   . HOH U 4 .   ? 8.81627   2.51030  7.79467   1.000 43.65486 ? 991  HOH A O   1 
HETATM 3825 O  O   . HOH U 4 .   ? -8.65820  33.26062 23.44377  1.000 41.81108 ? 992  HOH A O   1 
HETATM 3826 O  O   . HOH U 4 .   ? 19.44762  -0.61179 -22.20989 1.000 55.58065 ? 993  HOH A O   1 
HETATM 3827 O  O   . HOH U 4 .   ? -2.31142  67.73046 25.96870  1.000 32.85345 ? 994  HOH A O   1 
HETATM 3828 O  O   . HOH U 4 .   ? 4.70600   20.77920 18.16282  1.000 46.93719 ? 995  HOH A O   1 
HETATM 3829 O  O   . HOH U 4 .   ? -12.14656 30.94438 23.14722  1.000 36.70262 ? 996  HOH A O   1 
HETATM 3830 O  O   . HOH U 4 .   ? -4.22622  52.39005 37.84465  1.000 42.05244 ? 997  HOH A O   1 
HETATM 3831 O  O   . HOH U 4 .   ? 17.66390  12.94459 -27.10621 1.000 37.99876 ? 998  HOH A O   1 
HETATM 3832 O  O   . HOH U 4 .   ? -0.69024  7.68362  14.65704  1.000 46.50970 ? 999  HOH A O   1 
HETATM 3833 O  O   . HOH U 4 .   ? 10.77289  -3.25348 -22.54489 1.000 46.56352 ? 1000 HOH A O   1 
HETATM 3834 O  O   . HOH U 4 .   ? 13.24527  -2.84775 -24.78383 1.000 34.27559 ? 1001 HOH A O   1 
HETATM 3835 O  O   . HOH U 4 .   ? 15.90783  5.01793  -30.38057 1.000 34.23890 ? 1002 HOH A O   1 
HETATM 3836 O  O   . HOH U 4 .   ? 3.19263   63.04482 14.34355  1.000 46.98666 ? 1003 HOH A O   1 
HETATM 3837 O  O   . HOH U 4 .   ? 22.00102  3.62869  -10.89479 1.000 39.59499 ? 1004 HOH A O   1 
HETATM 3838 O  O   . HOH U 4 .   ? 15.55038  19.34093 12.95197  1.000 43.46440 ? 1005 HOH A O   1 
HETATM 3839 O  O   . HOH U 4 .   ? 6.01875   27.10746 18.39761  1.000 43.12473 ? 1006 HOH A O   1 
HETATM 3840 O  O   . HOH U 4 .   ? 6.05866   18.33573 -31.49772 1.000 41.25501 ? 1007 HOH A O   1 
HETATM 3841 O  O   A HOH U 4 .   ? 5.88275   3.19044  -12.69033 0.554 23.64631 ? 1008 HOH A O   1 
HETATM 3842 O  O   B HOH U 4 .   ? 3.74989   5.38906  -13.56745 0.446 18.86581 ? 1008 HOH A O   1 
HETATM 3843 O  O   . HOH U 4 .   ? 15.90332  0.33236  -24.81318 1.000 40.94761 ? 1009 HOH A O   1 
HETATM 3844 O  O   . HOH U 4 .   ? 8.06084   60.84865 20.44688  1.000 55.24024 ? 1010 HOH A O   1 
HETATM 3845 O  O   . HOH U 4 .   ? 8.98868   9.85107  -28.26664 1.000 46.73562 ? 1011 HOH A O   1 
HETATM 3846 O  O   . HOH U 4 .   ? -11.04380 38.75807 14.27947  1.000 32.03926 ? 1012 HOH A O   1 
HETATM 3847 O  O   . HOH U 4 .   ? -4.31032  7.09063  -14.65741 1.000 35.87271 ? 1013 HOH A O   1 
HETATM 3848 O  O   . HOH U 4 .   ? -3.33497  60.74805 11.96353  1.000 56.15655 ? 1014 HOH A O   1 
HETATM 3849 O  O   . HOH U 4 .   ? -1.49535  25.98013 -22.06680 1.000 47.07484 ? 1015 HOH A O   1 
HETATM 3850 O  O   . HOH U 4 .   ? 26.56902  14.09679 8.57336   1.000 55.75500 ? 1016 HOH A O   1 
HETATM 3851 O  O   . HOH U 4 .   ? -1.52083  69.34076 22.05339  1.000 43.85703 ? 1017 HOH A O   1 
HETATM 3852 O  O   . HOH U 4 .   ? -13.50310 35.08903 23.23767  1.000 29.39494 ? 1018 HOH A O   1 
HETATM 3853 O  O   . HOH U 4 .   ? -7.62347  15.92138 -11.04882 1.000 52.53337 ? 1019 HOH A O   1 
HETATM 3854 O  O   . HOH U 4 .   ? 13.46281  16.21467 16.18732  1.000 48.92544 ? 1020 HOH A O   1 
HETATM 3855 O  O   . HOH U 4 .   ? 21.06718  26.61463 12.98124  1.000 52.34132 ? 1021 HOH A O   1 
HETATM 3856 O  O   . HOH U 4 .   ? -7.04541  18.65359 -17.55000 1.000 41.79084 ? 1022 HOH A O   1 
HETATM 3857 O  O   . HOH U 4 .   ? -16.63790 49.41500 13.34521  1.000 51.88469 ? 1023 HOH A O   1 
HETATM 3858 O  O   . HOH U 4 .   ? 7.39016   27.42716 20.64622  1.000 37.65013 ? 1024 HOH A O   1 
HETATM 3859 O  O   . HOH U 4 .   ? -13.41513 32.50997 11.72843  1.000 45.50812 ? 1025 HOH A O   1 
HETATM 3860 O  O   . HOH U 4 .   ? -11.58247 50.03492 13.30910  1.000 49.95258 ? 1026 HOH A O   1 
HETATM 3861 O  O   . HOH U 4 .   ? -0.12011  67.76452 24.88698  1.000 41.86585 ? 1027 HOH A O   1 
HETATM 3862 O  O   . HOH U 4 .   ? 0.39651   43.72164 -6.83427  1.000 67.44599 ? 1028 HOH A O   1 
HETATM 3863 O  O   . HOH U 4 .   ? -2.08982  8.62554  4.37489   1.000 32.02105 ? 1029 HOH A O   1 
HETATM 3864 O  O   . HOH U 4 .   ? -5.25934  22.23594 16.53950  1.000 45.19637 ? 1030 HOH A O   1 
HETATM 3865 O  O   . HOH U 4 .   ? -3.77599  49.63693 12.42354  1.000 38.70272 ? 1031 HOH A O   1 
HETATM 3866 O  O   . HOH U 4 .   ? 11.11303  4.75708  5.09425   1.000 34.71871 ? 1032 HOH A O   1 
HETATM 3867 O  O   . HOH U 4 .   ? 12.99851  11.68296 2.14157   1.000 33.01429 ? 1033 HOH A O   1 
HETATM 3868 O  O   . HOH U 4 .   ? 2.45550   62.12479 26.63188  1.000 31.16431 ? 1034 HOH A O   1 
HETATM 3869 O  O   . HOH U 4 .   ? -8.80119  31.71076 -1.82158  1.000 43.80572 ? 1035 HOH A O   1 
HETATM 3870 O  O   . HOH U 4 .   ? -17.76406 54.08465 34.46889  1.000 46.79133 ? 1036 HOH A O   1 
HETATM 3871 O  O   . HOH U 4 .   ? 14.18760  23.26692 29.72133  1.000 56.21284 ? 1037 HOH A O   1 
HETATM 3872 O  O   . HOH U 4 .   ? -9.89754  27.48172 -4.42283  1.000 45.90079 ? 1038 HOH A O   1 
HETATM 3873 O  O   . HOH U 4 .   ? -7.22659  35.13360 26.38900  1.000 43.75377 ? 1039 HOH A O   1 
HETATM 3874 O  O   . HOH U 4 .   ? -1.22654  53.48388 31.10122  1.000 48.28585 ? 1040 HOH A O   1 
HETATM 3875 O  O   . HOH U 4 .   ? -6.96840  38.24348 7.37875   1.000 48.91510 ? 1041 HOH A O   1 
HETATM 3876 O  O   . HOH U 4 .   ? 19.92640  16.91484 11.07932  1.000 47.61803 ? 1042 HOH A O   1 
HETATM 3877 O  O   . HOH U 4 .   ? 10.65651  2.11890  4.38197   1.000 33.97917 ? 1043 HOH A O   1 
HETATM 3878 O  O   . HOH U 4 .   ? -1.54155  16.91529 -28.93039 1.000 46.94345 ? 1044 HOH A O   1 
HETATM 3879 O  O   . HOH U 4 .   ? 16.730    -1.723   -26.964   1.000 46.29846 ? 1045 HOH A O   1 
HETATM 3880 O  O   . HOH U 4 .   ? -16.74182 41.58917 23.46113  1.000 44.50452 ? 1046 HOH A O   1 
HETATM 3881 O  O   . HOH U 4 .   ? -10.47444 71.85239 26.91840  1.000 42.61323 ? 1047 HOH A O   1 
HETATM 3882 O  O   . HOH U 4 .   ? 7.21167   31.02564 16.48006  1.000 44.52206 ? 1048 HOH A O   1 
HETATM 3883 O  O   . HOH U 4 .   ? -18.539   47.112   27.720    1.000 50.44281 ? 1049 HOH A O   1 
HETATM 3884 O  O   . HOH U 4 .   ? 5.92856   1.88992  -3.56251  1.000 34.22159 ? 1050 HOH A O   1 
HETATM 3885 O  O   . HOH U 4 .   ? 6.03918   59.91815 28.21413  1.000 39.51415 ? 1051 HOH A O   1 
HETATM 3886 O  O   . HOH U 4 .   ? 9.61013   0.40341  2.23459   1.000 26.85487 ? 1052 HOH A O   1 
HETATM 3887 O  O   . HOH U 4 .   ? -17.50252 59.40468 30.97220  1.000 51.24097 ? 1053 HOH A O   1 
HETATM 3888 O  O   . HOH U 4 .   ? 11.70767  22.78978 29.67558  1.000 48.74546 ? 1054 HOH A O   1 
HETATM 3889 O  O   . HOH U 4 .   ? 12.70832  -1.19378 -21.00419 1.000 41.69076 ? 1055 HOH A O   1 
HETATM 3890 O  O   . HOH U 4 .   ? 18.46998  3.60520  -30.34049 1.000 51.29314 ? 1056 HOH A O   1 
HETATM 3891 O  O   . HOH U 4 .   ? 18.22271  5.88690  -13.99997 1.000 42.97231 ? 1057 HOH A O   1 
HETATM 3892 O  O   . HOH U 4 .   ? 7.78126   64.98812 14.74479  1.000 46.08132 ? 1058 HOH A O   1 
HETATM 3893 O  O   . HOH U 4 .   ? -14.33425 39.76746 11.57525  1.000 50.81708 ? 1059 HOH A O   1 
HETATM 3894 O  O   . HOH U 4 .   ? 14.42881  -1.11827 -18.22364 1.000 50.10675 ? 1060 HOH A O   1 
HETATM 3895 O  O   . HOH U 4 .   ? -11.61788 39.89552 12.17857  1.000 36.15474 ? 1061 HOH A O   1 
HETATM 3896 O  O   . HOH U 4 .   ? -11.22352 33.23497 23.69347  1.000 38.10896 ? 1062 HOH A O   1 
HETATM 3897 O  O   . HOH U 4 .   ? -18.66881 57.35319 34.80745  1.000 57.32689 ? 1063 HOH A O   1 
HETATM 3898 O  O   . HOH U 4 .   ? -10.88542 60.29633 42.89967  1.000 44.27297 ? 1064 HOH A O   1 
HETATM 3899 O  O   . HOH U 4 .   ? 13.76509  9.79779  9.65925   1.000 46.39669 ? 1065 HOH A O   1 
HETATM 3900 O  O   . HOH U 4 .   ? -2.23386  72.49250 25.24137  1.000 45.71680 ? 1066 HOH A O   1 
HETATM 3901 O  O   . HOH U 4 .   ? -17.56274 39.22040 24.70611  1.000 46.90629 ? 1067 HOH A O   1 
HETATM 3902 O  O   . HOH U 4 .   ? -15.26875 36.57495 16.10010  1.000 37.55135 ? 1068 HOH A O   1 
HETATM 3903 O  O   . HOH U 4 .   ? 14.76460  -1.31712 -23.15617 1.000 44.27069 ? 1069 HOH A O   1 
HETATM 3904 O  O   . HOH U 4 .   ? -0.85686  4.70454  7.20769   1.000 47.71669 ? 1070 HOH A O   1 
HETATM 3905 O  O   . HOH U 4 .   ? 16.72139  29.39953 5.18443   1.000 44.64197 ? 1071 HOH A O   1 
HETATM 3906 O  O   . HOH U 4 .   ? -15.11416 35.21059 21.09076  1.000 38.03814 ? 1072 HOH A O   1 
HETATM 3907 O  O   . HOH U 4 .   ? -17.08741 38.98895 20.05647  1.000 40.51601 ? 1073 HOH A O   1 
HETATM 3908 O  O   . HOH U 4 .   ? -20.994   46.745   27.072    1.000 51.37408 ? 1074 HOH A O   1 
HETATM 3909 O  O   . HOH U 4 .   ? 11.78055  30.78871 14.52847  1.000 49.23216 ? 1075 HOH A O   1 
HETATM 3910 O  O   . HOH U 4 .   ? -18.03350 37.69761 22.13510  1.000 47.34704 ? 1076 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   ? 0.80032 0.55405 0.63571 0.00920  -0.00650 -0.04307 211 LYS A N   
2    C CA  . LYS A 8   ? 0.86014 0.63465 0.69621 0.01270  -0.01557 -0.03845 211 LYS A CA  
3    C C   . LYS A 8   ? 0.82924 0.59316 0.66220 0.00644  -0.00466 -0.03373 211 LYS A C   
4    O O   . LYS A 8   ? 0.79900 0.52855 0.60436 0.00940  0.00377  -0.02822 211 LYS A O   
5    C CB  . LYS A 8   ? 0.82676 0.59448 0.63950 0.02639  -0.02717 -0.03529 211 LYS A CB  
6    C CG  . LYS A 8   ? 0.69136 0.48561 0.51135 0.02979  -0.03702 -0.03383 211 LYS A CG  
7    N N   . LYS A 9   ? 0.71951 0.51047 0.57798 -0.00100 -0.00508 -0.03628 212 LYS A N   
8    C CA  . LYS A 9   ? 0.73281 0.51821 0.59325 -0.00764 0.00474  -0.03332 212 LYS A CA  
9    C C   . LYS A 9   ? 0.68430 0.46395 0.52248 -0.00012 -0.00022 -0.02439 212 LYS A C   
10   O O   . LYS A 9   ? 0.63982 0.43444 0.47385 0.00836  -0.01354 -0.02303 212 LYS A O   
11   C CB  . LYS A 9   ? 0.64847 0.46594 0.54118 -0.01471 0.00178  -0.03972 212 LYS A CB  
12   C CG  . LYS A 9   ? 0.67230 0.49686 0.59193 -0.02174 0.00611  -0.05213 212 LYS A CG  
13   C CD  . LYS A 9   ? 0.71514 0.56674 0.66342 -0.02619 0.00206  -0.06013 212 LYS A CD  
14   C CE  . LYS A 9   ? 0.70402 0.56422 0.68335 -0.03169 0.00457  -0.07652 212 LYS A CE  
15   N NZ  . LYS A 9   ? 0.65638 0.52222 0.63535 -0.02587 -0.00476 -0.08048 212 LYS A NZ  
16   N N   . LYS A 10  ? 0.58342 0.34135 0.40913 -0.00349 0.01143  -0.01989 213 LYS A N   
17   C CA  . LYS A 10  ? 0.59536 0.35124 0.40394 0.00335  0.00600  -0.01290 213 LYS A CA  
18   C C   . LYS A 10  ? 0.57317 0.36376 0.40701 -0.00200 0.00095  -0.01345 213 LYS A C   
19   O O   . LYS A 10  ? 0.51044 0.31014 0.36538 -0.01210 0.00859  -0.01721 213 LYS A O   
20   C CB  . LYS A 10  ? 0.62573 0.34083 0.40530 0.00356  0.02034  -0.00728 213 LYS A CB  
21   C CG  . LYS A 10  ? 0.73121 0.44187 0.48981 0.01357  0.01224  -0.00121 213 LYS A CG  
22   C CD  . LYS A 10  ? 0.74832 0.42177 0.48064 0.01220  0.02767  0.00438  213 LYS A CD  
23   C CE  . LYS A 10  ? 0.78766 0.46549 0.50755 0.02078  0.01820  0.00884  213 LYS A CE  
24   N NZ  . LYS A 10  ? 0.90646 0.55601 0.58667 0.03994  0.00718  0.01057  213 LYS A NZ  
25   N N   . PRO A 11  ? 0.54067 0.35036 0.37410 0.00479  -0.01146 -0.01142 214 PRO A N   
26   C CA  . PRO A 11  ? 0.53469 0.37204 0.38714 0.00029  -0.01478 -0.01115 214 PRO A CA  
27   C C   . PRO A 11  ? 0.56287 0.39050 0.41273 -0.00496 -0.00567 -0.00718 214 PRO A C   
28   O O   . PRO A 11  ? 0.54966 0.34850 0.37728 -0.00258 0.00167  -0.00309 214 PRO A O   
29   C CB  . PRO A 11  ? 0.52754 0.37898 0.37593 0.00889  -0.02627 -0.01048 214 PRO A CB  
30   C CG  . PRO A 11  ? 0.53737 0.37889 0.37476 0.01699  -0.03175 -0.01372 214 PRO A CG  
31   C CD  . PRO A 11  ? 0.56501 0.37228 0.38302 0.01706  -0.02277 -0.01153 214 PRO A CD  
32   N N   . GLN A 12  ? 0.53928 0.38876 0.40951 -0.01119 -0.00612 -0.00874 215 GLN A N   
33   C CA  . GLN A 12  ? 0.51842 0.36350 0.38962 -0.01614 0.00123  -0.00582 215 GLN A CA  
34   C C   . GLN A 12  ? 0.47095 0.33985 0.35020 -0.01474 -0.00712 -0.00360 215 GLN A C   
35   O O   . GLN A 12  ? 0.47681 0.36443 0.36243 -0.01158 -0.01605 -0.00518 215 GLN A O   
36   C CB  . GLN A 12  ? 0.49678 0.34152 0.38832 -0.02657 0.01184  -0.01270 215 GLN A CB  
37   C CG  . GLN A 12  ? 0.59390 0.41497 0.48205 -0.03031 0.02352  -0.01689 215 GLN A CG  
38   C CD  . GLN A 12  ? 0.72468 0.55430 0.64394 -0.04073 0.03189  -0.02889 215 GLN A CD  
39   O OE1 . GLN A 12  ? 0.77927 0.60836 0.71048 -0.04785 0.04115  -0.03199 215 GLN A OE1 
40   N NE2 . GLN A 12  ? 0.67848 0.51743 0.61350 -0.04121 0.02803  -0.03765 215 GLN A NE2 
41   N N   . ILE A 13  ? 0.45855 0.32403 0.33606 -0.01746 -0.00237 -0.00005 216 ILE A N   
42   C CA  . ILE A 13  ? 0.43725 0.32345 0.32431 -0.01791 -0.00792 0.00145  216 ILE A CA  
43   C C   . ILE A 13  ? 0.45252 0.34076 0.35316 -0.02565 -0.00099 -0.00078 216 ILE A C   
44   O O   . ILE A 13  ? 0.48939 0.35930 0.38738 -0.03043 0.01043  -0.00146 216 ILE A O   
45   C CB  . ILE A 13  ? 0.50235 0.38728 0.37561 -0.01143 -0.01225 0.00682  216 ILE A CB  
46   C CG1 . ILE A 13  ? 0.54344 0.40339 0.39806 -0.00978 -0.00539 0.01102  216 ILE A CG1 
47   C CG2 . ILE A 13  ? 0.39585 0.28422 0.26302 -0.00362 -0.02024 0.00504  216 ILE A CG2 
48   C CD1 . ILE A 13  ? 0.52588 0.38856 0.37147 -0.00293 -0.01147 0.01409  216 ILE A CD1 
49   N N   . LYS A 14  ? 0.41511 0.32374 0.32966 -0.02657 -0.00708 -0.00309 217 LYS A N   
50   C CA  . LYS A 14  ? 0.47870 0.39344 0.40944 -0.03230 -0.00361 -0.00762 217 LYS A CA  
51   C C   . LYS A 14  ? 0.43596 0.36372 0.36574 -0.02990 -0.00986 -0.00352 217 LYS A C   
52   O O   . LYS A 14  ? 0.44801 0.38352 0.37028 -0.02482 -0.01689 -0.00033 217 LYS A O   
53   C CB  . LYS A 14  ? 0.43488 0.36043 0.38739 -0.03438 -0.00666 -0.01971 217 LYS A CB  
54   C CG  . LYS A 14  ? 0.43248 0.34637 0.39365 -0.03924 0.00217  -0.02702 217 LYS A CG  
55   C CD  . LYS A 14  ? 0.41363 0.34279 0.40173 -0.04006 -0.00340 -0.04238 217 LYS A CD  
56   N N   . TYR A 15  ? 0.42855 0.35737 0.36665 -0.03421 -0.00558 -0.00456 218 TYR A N   
57   C CA  . TYR A 15  ? 0.42342 0.36287 0.36171 -0.03263 -0.01041 -0.00139 218 TYR A CA  
58   C C   . TYR A 15  ? 0.53950 0.48479 0.49716 -0.03740 -0.00821 -0.00941 218 TYR A C   
59   O O   . TYR A 15  ? 0.49520 0.43161 0.46199 -0.04387 0.00231  -0.01380 218 TYR A O   
60   C CB  . TYR A 15  ? 0.43045 0.36257 0.35365 -0.03137 -0.00728 0.00794  218 TYR A CB  
61   C CG  . TYR A 15  ? 0.46980 0.41216 0.39488 -0.03078 -0.01070 0.01071  218 TYR A CG  
62   C CD1 . TYR A 15  ? 0.47875 0.43025 0.39952 -0.02660 -0.01715 0.01255  218 TYR A CD1 
63   C CD2 . TYR A 15  ? 0.46120 0.40196 0.39171 -0.03481 -0.00582 0.01095  218 TYR A CD2 
64   C CE1 . TYR A 15  ? 0.48594 0.44346 0.40658 -0.02622 -0.01876 0.01502  218 TYR A CE1 
65   C CE2 . TYR A 15  ? 0.46508 0.41479 0.39727 -0.03404 -0.00925 0.01328  218 TYR A CE2 
66   C CZ  . TYR A 15  ? 0.51028 0.46781 0.43705 -0.02964 -0.01581 0.01548  218 TYR A CZ  
67   O OH  . TYR A 15  ? 0.51235 0.47547 0.43879 -0.02900 -0.01774 0.01785  218 TYR A OH  
68   N N   . GLU A 16  ? 0.51561 0.47357 0.47891 -0.03394 -0.01711 -0.01247 219 GLU A N   
69   C CA  . GLU A 16  ? 0.52734 0.49293 0.51174 -0.03691 -0.01731 -0.02274 219 GLU A CA  
70   C C   . GLU A 16  ? 0.54739 0.50977 0.52891 -0.04100 -0.01040 -0.01615 219 GLU A C   
71   O O   . GLU A 16  ? 0.49692 0.46387 0.46934 -0.03727 -0.01593 -0.01011 219 GLU A O   
72   C CB  . GLU A 16  ? 0.60487 0.58173 0.59303 -0.02870 -0.03182 -0.03043 219 GLU A CB  
73   C CG  . GLU A 16  ? 0.58235 0.56947 0.59384 -0.02887 -0.03606 -0.04392 219 GLU A CG  
74   C CD  . GLU A 16  ? 0.71149 0.70018 0.75217 -0.03872 -0.02472 -0.05624 219 GLU A CD  
75   O OE1 . GLU A 16  ? 0.71478 0.69606 0.75609 -0.04715 -0.01098 -0.05069 219 GLU A OE1 
76   O OE2 . GLU A 16  ? 0.69916 0.69488 0.76200 -0.03801 -0.02841 -0.07252 219 GLU A OE2 
77   N N   . GLU A 17  ? 0.46519 0.41698 0.45291 -0.04872 0.00316  -0.01765 220 GLU A N   
78   C CA  . GLU A 17  ? 0.54327 0.48725 0.52322 -0.05200 0.01124  -0.01055 220 GLU A CA  
79   C C   . GLU A 17  ? 0.50187 0.45908 0.49892 -0.05334 0.00795  -0.01674 220 GLU A C   
80   O O   . GLU A 17  ? 0.52786 0.48248 0.51653 -0.05390 0.01056  -0.00957 220 GLU A O   
81   C CB  . GLU A 17  ? 0.65524 0.57732 0.63088 -0.05906 0.02891  -0.01053 220 GLU A CB  
82   C CG  . GLU A 17  ? 0.62990 0.53073 0.57314 -0.05479 0.03270  0.00250  220 GLU A CG  
83   C CD  . GLU A 17  ? 0.84406 0.71433 0.77373 -0.05991 0.05166  0.00335  220 GLU A CD  
84   O OE1 . GLU A 17  ? 0.75091 0.60065 0.66062 -0.05700 0.05579  0.00694  220 GLU A OE1 
85   O OE2 . GLU A 17  ? 0.83120 0.69520 0.76803 -0.06650 0.06342  0.00014  220 GLU A OE2 
86   N N   . LYS A 18  ? 0.55089 0.52234 0.57133 -0.05234 0.00057  -0.03094 221 LYS A N   
87   C CA  . LYS A 18  ? 0.57988 0.56438 0.61398 -0.05029 -0.00682 -0.03766 221 LYS A CA  
88   C C   . LYS A 18  ? 0.58437 0.57069 0.59643 -0.04289 -0.01664 -0.02555 221 LYS A C   
89   O O   . LYS A 18  ? 0.53552 0.52805 0.55242 -0.04162 -0.02042 -0.02716 221 LYS A O   
90   C CB  . LYS A 18  ? 0.60167 0.60053 0.66066 -0.04575 -0.01838 -0.05671 221 LYS A CB  
91   N N   . GLN A 19  ? 0.47881 0.45916 0.46829 -0.03871 -0.01920 -0.01451 222 GLN A N   
92   C CA  . GLN A 19  ? 0.50656 0.48721 0.47702 -0.03240 -0.02617 -0.00547 222 GLN A CA  
93   C C   . GLN A 19  ? 0.44280 0.41713 0.39977 -0.03516 -0.01863 0.00675  222 GLN A C   
94   O O   . GLN A 19  ? 0.50228 0.46957 0.45097 -0.03602 -0.01407 0.01118  222 GLN A O   
95   C CB  . GLN A 19  ? 0.48546 0.46404 0.44335 -0.02562 -0.03337 -0.00539 222 GLN A CB  
96   C CG  . GLN A 19  ? 0.60153 0.57593 0.53862 -0.01954 -0.03743 0.00179  222 GLN A CG  
97   C CD  . GLN A 19  ? 0.64459 0.61422 0.56990 -0.01185 -0.04465 -0.00197 222 GLN A CD  
98   O OE1 . GLN A 19  ? 0.76007 0.73170 0.69130 -0.00595 -0.05418 -0.01267 222 GLN A OE1 
99   N NE2 . GLN A 19  ? 0.61522 0.57855 0.52512 -0.01125 -0.04048 0.00490  222 GLN A NE2 
100  N N   . ALA A 20  ? 0.45398 0.43063 0.40902 -0.03532 -0.01857 0.01077  223 ALA A N   
101  C CA  . ALA A 20  ? 0.41792 0.39051 0.36122 -0.03570 -0.01428 0.02013  223 ALA A CA  
102  C C   . ALA A 20  ? 0.43970 0.41306 0.37100 -0.03118 -0.01786 0.02430  223 ALA A C   
103  O O   . ALA A 20  ? 0.42193 0.39583 0.34899 -0.02748 -0.02288 0.02221  223 ALA A O   
104  C CB  . ALA A 20  ? 0.48899 0.46390 0.43611 -0.03785 -0.01219 0.02202  223 ALA A CB  
105  N N   . VAL A 21  ? 0.44416 0.41544 0.36914 -0.03074 -0.01473 0.02876  224 VAL A N   
106  C CA  . VAL A 21  ? 0.36227 0.33495 0.28090 -0.02834 -0.01453 0.03053  224 VAL A CA  
107  C C   . VAL A 21  ? 0.42870 0.40457 0.34887 -0.02915 -0.01262 0.03303  224 VAL A C   
108  O O   . VAL A 21  ? 0.33022 0.30714 0.25339 -0.02946 -0.01159 0.03399  224 VAL A O   
109  C CB  . VAL A 21  ? 0.41112 0.38246 0.32773 -0.02667 -0.01336 0.02977  224 VAL A CB  
110  C CG1 . VAL A 21  ? 0.36101 0.33562 0.27710 -0.02568 -0.01066 0.02860  224 VAL A CG1 
111  C CG2 . VAL A 21  ? 0.36356 0.33102 0.27835 -0.02603 -0.01493 0.02740  224 VAL A CG2 
112  N N   . MET A 22  ? 0.39952 0.37414 0.31499 -0.02851 -0.01212 0.03380  225 MET A N   
113  C CA  . MET A 22  ? 0.42442 0.40096 0.34183 -0.02972 -0.01016 0.03585  225 MET A CA  
114  C C   . MET A 22  ? 0.39623 0.36977 0.30937 -0.03008 -0.00349 0.03592  225 MET A C   
115  O O   . MET A 22  ? 0.40537 0.36925 0.30636 -0.02877 -0.00106 0.03723  225 MET A O   
116  C CB  . MET A 22  ? 0.45057 0.42518 0.36602 -0.02857 -0.01458 0.03566  225 MET A CB  
117  C CG  . MET A 22  ? 0.47737 0.45605 0.40304 -0.02995 -0.01829 0.03237  225 MET A CG  
118  S SD  . MET A 22  ? 0.67327 0.65463 0.60542 -0.02875 -0.02399 0.02811  225 MET A SD  
119  C CE  . MET A 22  ? 0.62957 0.60829 0.55989 -0.02291 -0.03260 0.01985  225 MET A CE  
120  N N   . PRO A 23  ? 0.35431 0.33397 0.27681 -0.03125 0.00016  0.03307  226 PRO A N   
121  C CA  . PRO A 23  ? 0.35618 0.33452 0.28126 -0.03342 0.00944  0.03003  226 PRO A CA  
122  C C   . PRO A 23  ? 0.40729 0.38359 0.33241 -0.03537 0.01316  0.03202  226 PRO A C   
123  O O   . PRO A 23  ? 0.38383 0.36542 0.31337 -0.03495 0.00755  0.03422  226 PRO A O   
124  C CB  . PRO A 23  ? 0.35939 0.34903 0.30105 -0.03275 0.00895  0.02285  226 PRO A CB  
125  C CG  . PRO A 23  ? 0.39209 0.38513 0.33428 -0.02937 -0.00062 0.02488  226 PRO A CG  
126  C CD  . PRO A 23  ? 0.43205 0.41802 0.36265 -0.02960 -0.00394 0.03072  226 PRO A CD  
127  N N   . GLU A 24  ? 0.37213 0.33835 0.29109 -0.03779 0.02441  0.03094  227 GLU A N   
128  C CA  . GLU A 24  ? 0.39771 0.35883 0.31540 -0.03998 0.03031  0.03233  227 GLU A CA  
129  C C   . GLU A 24  ? 0.40512 0.38322 0.34754 -0.04231 0.03014  0.02646  227 GLU A C   
130  O O   . GLU A 24  ? 0.34409 0.33524 0.30223 -0.04108 0.02608  0.02018  227 GLU A O   
131  C CB  . GLU A 24  ? 0.39351 0.33438 0.29604 -0.04246 0.04617  0.03181  227 GLU A CB  
132  C CG  . GLU A 24  ? 0.57170 0.48902 0.44093 -0.03672 0.04433  0.03827  227 GLU A CG  
133  C CD  . GLU A 24  ? 0.70850 0.59590 0.55218 -0.03758 0.06207  0.03927  227 GLU A CD  
134  O OE1 . GLU A 24  ? 0.73965 0.61360 0.57037 -0.03750 0.07084  0.03779  227 GLU A OE1 
135  O OE2 . GLU A 24  ? 0.82771 0.70203 0.66180 -0.03823 0.06853  0.04161  227 GLU A OE2 
136  N N   . SER A 25  ? 0.40965 0.38620 0.35407 -0.04419 0.03345  0.02759  228 SER A N   
137  C CA  . SER A 25  ? 0.38693 0.37944 0.35446 -0.04506 0.03176  0.02099  228 SER A CA  
138  C C   . SER A 25  ? 0.41562 0.41526 0.40450 -0.04848 0.04209  0.00840  228 SER A C   
139  O O   . SER A 25  ? 0.39106 0.40720 0.40230 -0.04623 0.03662  -0.00118 228 SER A O   
140  C CB  . SER A 25  ? 0.43945 0.42873 0.40486 -0.04645 0.03306  0.02471  228 SER A CB  
141  O OG  . SER A 25  ? 0.46428 0.43527 0.41675 -0.05007 0.04685  0.02630  228 SER A OG  
142  N N   . ALA A 26  ? 0.36362 0.34985 0.34594 -0.05313 0.05716  0.00658  229 ALA A N   
143  C CA  . ALA A 26  ? 0.36071 0.35370 0.36723 -0.05795 0.07008  -0.00804 229 ALA A CA  
144  C C   . ALA A 26  ? 0.34433 0.35591 0.36941 -0.05319 0.05913  -0.01750 229 ALA A C   
145  O O   . ALA A 26  ? 0.31647 0.32701 0.32721 -0.04807 0.04768  -0.01055 229 ALA A O   
146  C CB  . ALA A 26  ? 0.35488 0.32454 0.34417 -0.06353 0.08987  -0.00688 229 ALA A CB  
147  N N   . ALA A 27  ? 0.30345 0.33145 0.36151 -0.05425 0.06255  -0.03517 230 ALA A N   
148  C CA  . ALA A 27  ? 0.35145 0.39477 0.42738 -0.04852 0.05316  -0.04751 230 ALA A CA  
149  C C   . ALA A 27  ? 0.39289 0.42638 0.45937 -0.05195 0.06284  -0.04676 230 ALA A C   
150  O O   . ALA A 27  ? 0.45295 0.46935 0.50814 -0.05994 0.08170  -0.04330 230 ALA A O   
151  C CB  . ALA A 27  ? 0.26901 0.33254 0.38636 -0.04842 0.05539  -0.07087 230 ALA A CB  
152  N N   . GLY A 28  ? 0.35916 0.40044 0.42731 -0.04511 0.05043  -0.05018 231 GLY A N   
153  C CA  . GLY A 28  ? 0.35861 0.39369 0.42255 -0.04786 0.05890  -0.05229 231 GLY A CA  
154  C C   . GLY A 28  ? 0.35615 0.39374 0.40875 -0.03918 0.04190  -0.04820 231 GLY A C   
155  O O   . GLY A 28  ? 0.38568 0.42594 0.42978 -0.03133 0.02521  -0.04252 231 GLY A O   
156  N N   . THR A 29  ? 0.34930 0.38313 0.40019 -0.04108 0.04840  -0.05135 232 THR A N   
157  C CA  . THR A 29  ? 0.34182 0.37488 0.38026 -0.03419 0.03548  -0.04729 232 THR A CA  
158  C C   . THR A 29  ? 0.34980 0.36366 0.35511 -0.03675 0.03862  -0.02943 232 THR A C   
159  O O   . THR A 29  ? 0.34784 0.34922 0.34352 -0.04255 0.05349  -0.02781 232 THR A O   
160  C CB  . THR A 29  ? 0.42427 0.46740 0.48465 -0.03362 0.03902  -0.06429 232 THR A CB  
161  O OG1 . THR A 29  ? 0.36645 0.42937 0.46073 -0.02890 0.03282  -0.08438 232 THR A OG1 
162  C CG2 . THR A 29  ? 0.36750 0.40768 0.41293 -0.02646 0.02620  -0.05953 232 THR A CG2 
163  N N   . TYR A 30  ? 0.30251 0.31234 0.29018 -0.03183 0.02522  -0.01763 233 TYR A N   
164  C CA  . TYR A 30  ? 0.36152 0.35659 0.32282 -0.03260 0.02460  -0.00372 233 TYR A CA  
165  C C   . TYR A 30  ? 0.37951 0.37327 0.33259 -0.02806 0.01533  -0.00157 233 TYR A C   
166  O O   . TYR A 30  ? 0.33696 0.33857 0.29957 -0.02309 0.00709  -0.00779 233 TYR A O   
167  C CB  . TYR A 30  ? 0.29857 0.29096 0.25108 -0.03198 0.01858  0.00560  233 TYR A CB  
168  C CG  . TYR A 30  ? 0.41629 0.40768 0.37394 -0.03637 0.02767  0.00483  233 TYR A CG  
169  C CD1 . TYR A 30  ? 0.34213 0.34612 0.31991 -0.03593 0.02592  -0.00261 233 TYR A CD1 
170  C CD2 . TYR A 30  ? 0.42298 0.39829 0.36298 -0.03966 0.03754  0.01086  233 TYR A CD2 
171  C CE1 . TYR A 30  ? 0.35733 0.36022 0.34123 -0.04057 0.03515  -0.00389 233 TYR A CE1 
172  C CE2 . TYR A 30  ? 0.37090 0.34142 0.31258 -0.04360 0.04717  0.01058  233 TYR A CE2 
173  C CZ  . TYR A 30  ? 0.33707 0.32250 0.30243 -0.04497 0.04659  0.00330  233 TYR A CZ  
174  O OH  . TYR A 30  ? 0.36226 0.34252 0.33028 -0.04945 0.05704  0.00257  233 TYR A OH  
175  N N   . THR A 31  ? 0.33583 0.31791 0.26982 -0.02852 0.01595  0.00628  234 THR A N   
176  C CA  . THR A 31  ? 0.30826 0.28879 0.23645 -0.02523 0.00946  0.00676  234 THR A CA  
177  C C   . THR A 31  ? 0.35755 0.33034 0.27077 -0.02385 0.00283  0.01517  234 THR A C   
178  O O   . THR A 31  ? 0.37917 0.34636 0.28403 -0.02477 0.00355  0.02002  234 THR A O   
179  C CB  . THR A 31  ? 0.31899 0.29525 0.24484 -0.02657 0.01802  0.00184  234 THR A CB  
180  O OG1 . THR A 31  ? 0.38539 0.34592 0.29127 -0.02819 0.02595  0.00730  234 THR A OG1 
181  C CG2 . THR A 31  ? 0.33201 0.31801 0.27918 -0.02903 0.02642  -0.01024 234 THR A CG2 
182  N N   . PHE A 32  ? 0.35775 0.33046 0.26967 -0.02124 -0.00386 0.01503  235 PHE A N   
183  C CA  . PHE A 32  ? 0.36067 0.32750 0.26369 -0.02035 -0.00881 0.01874  235 PHE A CA  
184  C C   . PHE A 32  ? 0.38368 0.34911 0.28534 -0.01825 -0.01125 0.01577  235 PHE A C   
185  O O   . PHE A 32  ? 0.36274 0.33170 0.26984 -0.01703 -0.01024 0.01146  235 PHE A O   
186  C CB  . PHE A 32  ? 0.33025 0.29772 0.23679 -0.02108 -0.01328 0.02163  235 PHE A CB  
187  C CG  . PHE A 32  ? 0.35621 0.32321 0.26597 -0.01940 -0.01536 0.02063  235 PHE A CG  
188  C CD1 . PHE A 32  ? 0.36748 0.33779 0.28135 -0.01760 -0.01545 0.01931  235 PHE A CD1 
189  C CD2 . PHE A 32  ? 0.38503 0.34550 0.29154 -0.01835 -0.01745 0.02011  235 PHE A CD2 
190  C CE1 . PHE A 32  ? 0.32970 0.29436 0.23989 -0.01266 -0.01931 0.01773  235 PHE A CE1 
191  C CE2 . PHE A 32  ? 0.37475 0.32755 0.27659 -0.01494 -0.01880 0.01977  235 PHE A CE2 
192  C CZ  . PHE A 32  ? 0.35545 0.30908 0.25683 -0.01104 -0.02057 0.01872  235 PHE A CZ  
193  N N   . GLU A 33  ? 0.37406 0.33520 0.27051 -0.01723 -0.01535 0.01636  236 GLU A N   
194  C CA  . GLU A 33  ? 0.40048 0.35956 0.29484 -0.01522 -0.01755 0.01331  236 GLU A CA  
195  C C   . GLU A 33  ? 0.43291 0.39059 0.33261 -0.01583 -0.02153 0.01273  236 GLU A C   
196  O O   . GLU A 33  ? 0.40844 0.36571 0.31223 -0.01780 -0.02264 0.01331  236 GLU A O   
197  C CB  . GLU A 33  ? 0.41338 0.36608 0.29573 -0.01227 -0.01842 0.01212  236 GLU A CB  
198  C CG  . GLU A 33  ? 0.47705 0.42363 0.34832 -0.01204 -0.01026 0.01291  236 GLU A CG  
199  C CD  . GLU A 33  ? 0.55885 0.49132 0.40889 -0.00669 -0.01073 0.01250  236 GLU A CD  
200  O OE1 . GLU A 33  ? 0.61272 0.54324 0.45927 -0.00210 -0.02036 0.01063  236 GLU A OE1 
201  O OE2 . GLU A 33  ? 0.54274 0.46438 0.37907 -0.00648 -0.00092 0.01265  236 GLU A OE2 
202  N N   . VAL A 34  ? 0.40690 0.36242 0.30676 -0.01437 -0.02230 0.01057  237 VAL A N   
203  C CA  . VAL A 34  ? 0.41154 0.36059 0.31327 -0.01517 -0.02318 0.00950  237 VAL A CA  
204  C C   . VAL A 34  ? 0.42469 0.37319 0.32601 -0.01350 -0.02565 0.00533  237 VAL A C   
205  O O   . VAL A 34  ? 0.37826 0.32862 0.27587 -0.01077 -0.02613 0.00394  237 VAL A O   
206  C CB  . VAL A 34  ? 0.45560 0.39695 0.35253 -0.01298 -0.02222 0.01091  237 VAL A CB  
207  C CG1 . VAL A 34  ? 0.46626 0.39579 0.35878 -0.01209 -0.02162 0.00922  237 VAL A CG1 
208  C CG2 . VAL A 34  ? 0.40070 0.33798 0.29636 -0.01464 -0.01963 0.01462  237 VAL A CG2 
209  N N   A GLN A 35  ? 0.42388 0.37069 0.33137 -0.01522 -0.02686 0.00164  238 GLN A N   
210  N N   B GLN A 35  ? 0.42180 0.36869 0.32934 -0.01524 -0.02688 0.00164  238 GLN A N   
211  C CA  A GLN A 35  ? 0.43140 0.37839 0.33993 -0.01300 -0.03032 -0.00371 238 GLN A CA  
212  C CA  B GLN A 35  ? 0.43108 0.37781 0.33993 -0.01318 -0.03016 -0.00373 238 GLN A CA  
213  C C   A GLN A 35  ? 0.44026 0.37946 0.34740 -0.01314 -0.02807 -0.00423 238 GLN A C   
214  C C   B GLN A 35  ? 0.44153 0.38050 0.34791 -0.01301 -0.02789 -0.00374 238 GLN A C   
215  O O   A GLN A 35  ? 0.41804 0.34753 0.32570 -0.01598 -0.02322 -0.00309 238 GLN A O   
216  O O   B GLN A 35  ? 0.41555 0.34460 0.32061 -0.01522 -0.02327 -0.00178 238 GLN A O   
217  C CB  A GLN A 35  ? 0.41762 0.36768 0.33752 -0.01370 -0.03387 -0.01104 238 GLN A CB  
218  C CB  B GLN A 35  ? 0.41658 0.36565 0.33799 -0.01459 -0.03287 -0.01121 238 GLN A CB  
219  C CG  A GLN A 35  ? 0.49492 0.44922 0.40920 -0.00848 -0.04053 -0.01308 238 GLN A CG  
220  C CG  B GLN A 35  ? 0.45796 0.40854 0.38194 -0.01087 -0.03849 -0.01887 238 GLN A CG  
221  C CD  A GLN A 35  ? 0.47809 0.43348 0.38854 -0.00965 -0.03851 -0.00747 238 GLN A CD  
222  C CD  B GLN A 35  ? 0.51886 0.47466 0.46022 -0.01073 -0.04330 -0.03045 238 GLN A CD  
223  O OE1 A GLN A 35  ? 0.47859 0.43145 0.37480 -0.00616 -0.03865 -0.00363 238 GLN A OE1 
224  O OE1 B GLN A 35  ? 0.54658 0.50375 0.50276 -0.01610 -0.03911 -0.03384 238 GLN A OE1 
225  N NE2 A GLN A 35  ? 0.51206 0.46910 0.43437 -0.01489 -0.03503 -0.00738 238 GLN A NE2 
226  N NE2 B GLN A 35  ? 0.44450 0.40305 0.38502 -0.00393 -0.05223 -0.03834 238 GLN A NE2 
227  N N   . THR A 36  ? 0.39963 0.34003 0.30213 -0.00954 -0.03070 -0.00600 239 THR A N   
228  C CA  . THR A 36  ? 0.40362 0.33625 0.30250 -0.00781 -0.03017 -0.00695 239 THR A CA  
229  C C   . THR A 36  ? 0.44358 0.37549 0.34787 -0.00792 -0.03215 -0.01288 239 THR A C   
230  O O   . THR A 36  ? 0.47258 0.41128 0.37616 -0.00499 -0.03638 -0.01601 239 THR A O   
231  C CB  . THR A 36  ? 0.42966 0.36620 0.32306 -0.00339 -0.03191 -0.00686 239 THR A CB  
232  O OG1 . THR A 36  ? 0.43813 0.38288 0.33132 -0.00248 -0.03260 -0.00898 239 THR A OG1 
233  C CG2 . THR A 36  ? 0.41626 0.35422 0.30813 -0.00261 -0.03072 -0.00382 239 THR A CG2 
234  N N   . ILE A 37  ? 0.47578 0.39699 0.38399 -0.01107 -0.02792 -0.01499 240 ILE A N   
235  C CA  . ILE A 37  ? 0.46398 0.38452 0.38287 -0.01272 -0.02821 -0.02287 240 ILE A CA  
236  C C   . ILE A 37  ? 0.50112 0.41073 0.41200 -0.01034 -0.02726 -0.02305 240 ILE A C   
237  O O   . ILE A 37  ? 0.49565 0.38989 0.39379 -0.00925 -0.02302 -0.01832 240 ILE A O   
238  C CB  . ILE A 37  ? 0.50888 0.42407 0.44207 -0.01978 -0.02073 -0.02770 240 ILE A CB  
239  C CG1 . ILE A 37  ? 0.52900 0.45649 0.47170 -0.02093 -0.02361 -0.02925 240 ILE A CG1 
240  C CG2 . ILE A 37  ? 0.41982 0.33408 0.36926 -0.02245 -0.01920 -0.03889 240 ILE A CG2 
241  C CD1 . ILE A 37  ? 0.57706 0.51883 0.52603 -0.01555 -0.03468 -0.03639 240 ILE A CD1 
242  N N   . ASP A 38  ? 0.47022 0.38592 0.38615 -0.00800 -0.03223 -0.02906 241 ASP A N   
243  C CA  . ASP A 38  ? 0.48762 0.39415 0.39829 -0.00567 -0.03214 -0.03083 241 ASP A CA  
244  C C   . ASP A 38  ? 0.52045 0.42289 0.41551 0.00005  -0.03450 -0.02547 241 ASP A C   
245  O O   . ASP A 38  ? 0.50476 0.39191 0.38976 0.00286  -0.03312 -0.02489 241 ASP A O   
246  C CB  . ASP A 38  ? 0.48331 0.37149 0.39722 -0.01088 -0.02270 -0.03351 241 ASP A CB  
247  C CG  . ASP A 38  ? 0.54389 0.43941 0.48121 -0.01625 -0.02096 -0.04441 241 ASP A CG  
248  O OD1 . ASP A 38  ? 0.63881 0.55105 0.58571 -0.01272 -0.03051 -0.05087 241 ASP A OD1 
249  O OD2 . ASP A 38  ? 0.59106 0.47445 0.53734 -0.02341 -0.00973 -0.04816 241 ASP A OD2 
250  N N   . GLY A 39  ? 0.46474 0.37973 0.35815 0.00245  -0.03800 -0.02326 242 GLY A N   
251  C CA  . GLY A 39  ? 0.50552 0.42135 0.39149 0.00771  -0.04051 -0.02223 242 GLY A CA  
252  C C   . GLY A 39  ? 0.53379 0.44919 0.41637 0.00798  -0.03915 -0.01789 242 GLY A C   
253  O O   . GLY A 39  ? 0.47476 0.39192 0.36032 0.00352  -0.03598 -0.01445 242 GLY A O   
254  N N   . LYS A 40  ? 0.54638 0.46010 0.42393 0.01431  -0.04276 -0.01978 243 LYS A N   
255  C CA  . LYS A 40  ? 0.47709 0.39351 0.35383 0.01648  -0.04354 -0.01854 243 LYS A CA  
256  C C   . LYS A 40  ? 0.57425 0.46913 0.43436 0.02313  -0.04585 -0.01686 243 LYS A C   
257  O O   . LYS A 40  ? 0.55516 0.44181 0.40711 0.03217  -0.05222 -0.02176 243 LYS A O   
258  C CB  . LYS A 40  ? 0.49410 0.42690 0.38132 0.01962  -0.04618 -0.02576 243 LYS A CB  
259  C CG  . LYS A 40  ? 0.44720 0.39390 0.34333 0.01331  -0.04049 -0.02600 243 LYS A CG  
260  C CD  . LYS A 40  ? 0.39798 0.34704 0.29440 0.00805  -0.03609 -0.01979 243 LYS A CD  
261  C CE  . LYS A 40  ? 0.39098 0.34733 0.28896 0.00407  -0.03015 -0.01986 243 LYS A CE  
262  N NZ  . LYS A 40  ? 0.39992 0.35609 0.29553 0.00027  -0.02708 -0.01397 243 LYS A NZ  
263  N N   . LEU A 41  ? 0.48612 0.36941 0.33884 0.01972  -0.04064 -0.01060 244 LEU A N   
264  C CA  . LEU A 41  ? 0.49691 0.35299 0.32682 0.02664  -0.04055 -0.00796 244 LEU A CA  
265  C C   . LEU A 41  ? 0.57849 0.43756 0.40391 0.03732  -0.04988 -0.01220 244 LEU A C   
266  O O   . LEU A 41  ? 0.52234 0.40404 0.36497 0.03499  -0.05166 -0.01475 244 LEU A O   
267  C CB  . LEU A 41  ? 0.43872 0.28169 0.26338 0.01903  -0.03007 -0.00117 244 LEU A CB  
268  C CG  . LEU A 41  ? 0.51804 0.32673 0.31329 0.02555  -0.02627 0.00297  244 LEU A CG  
269  C CD1 . LEU A 41  ? 0.61955 0.39620 0.39100 0.03121  -0.02337 0.00273  244 LEU A CD1 
270  C CD2 . LEU A 41  ? 0.50985 0.31147 0.30631 0.01592  -0.01411 0.00822  244 LEU A CD2 
271  N N   . ASP A 42  ? 0.53104 0.36535 0.33250 0.05009  -0.05603 -0.01434 245 ASP A N   
272  C CA  . ASP A 42  ? 0.58377 0.41859 0.37992 0.06392  -0.06820 -0.02182 245 ASP A CA  
273  C C   . ASP A 42  ? 0.59501 0.40923 0.37039 0.06703  -0.06550 -0.01553 245 ASP A C   
274  O O   . ASP A 42  ? 0.68365 0.46085 0.42465 0.07572  -0.06451 -0.01168 245 ASP A O   
275  C CB  . ASP A 42  ? 0.75018 0.56786 0.52902 0.07965  -0.07963 -0.02984 245 ASP A CB  
276  C CG  . ASP A 42  ? 0.80588 0.62827 0.58476 0.09621  -0.09559 -0.04244 245 ASP A CG  
277  O OD1 . ASP A 42  ? 0.75463 0.60537 0.56000 0.09251  -0.09713 -0.04809 245 ASP A OD1 
278  O OD2 . ASP A 42  ? 0.86384 0.65996 0.61566 0.11383  -0.10682 -0.04789 245 ASP A OD2 
279  N N   . TYR A 43  ? 0.61181 0.44703 0.40537 0.06013  -0.06315 -0.01429 246 TYR A N   
280  C CA  . TYR A 43  ? 0.58781 0.40710 0.36521 0.06121  -0.05948 -0.00811 246 TYR A CA  
281  C C   . TYR A 43  ? 0.57509 0.41638 0.36881 0.06601  -0.06822 -0.01534 246 TYR A C   
282  O O   . TYR A 43  ? 0.52000 0.39009 0.34117 0.06532  -0.07359 -0.02486 246 TYR A O   
283  C CB  . TYR A 43  ? 0.55077 0.37139 0.33520 0.04471  -0.04422 0.00189  246 TYR A CB  
284  C CG  . TYR A 43  ? 0.49194 0.34867 0.30984 0.03302  -0.04231 0.00095  246 TYR A CG  
285  C CD1 . TYR A 43  ? 0.54183 0.41433 0.37648 0.02599  -0.04041 -0.00079 246 TYR A CD1 
286  C CD2 . TYR A 43  ? 0.48602 0.35771 0.31515 0.03030  -0.04241 0.00160  246 TYR A CD2 
287  C CE1 . TYR A 43  ? 0.47960 0.37792 0.33672 0.01762  -0.03834 -0.00139 246 TYR A CE1 
288  C CE2 . TYR A 43  ? 0.45951 0.35754 0.31275 0.02104  -0.03971 0.00115  246 TYR A CE2 
289  C CZ  . TYR A 43  ? 0.49185 0.40136 0.35690 0.01522  -0.03753 -0.00014 246 TYR A CZ  
290  O OH  . TYR A 43  ? 0.48117 0.41034 0.36277 0.00796  -0.03435 -0.00021 246 TYR A OH  
291  N N   . GLU A 44  ? 0.56658 0.39280 0.34369 0.07028  -0.06786 -0.01150 247 GLU A N   
292  C CA  . GLU A 44  ? 0.62264 0.46796 0.41502 0.07469  -0.07550 -0.01856 247 GLU A CA  
293  C C   . GLU A 44  ? 0.52210 0.36514 0.31228 0.06561  -0.06578 -0.00873 247 GLU A C   
294  O O   . GLU A 44  ? 0.57996 0.39141 0.34008 0.06754  -0.05949 -0.00034 247 GLU A O   
295  C CB  . GLU A 44  ? 0.70688 0.53505 0.47867 0.09698  -0.09225 -0.02948 247 GLU A CB  
296  C CG  . GLU A 44  ? 0.82984 0.68067 0.62276 0.10311  -0.10213 -0.04113 247 GLU A CG  
297  C CD  . GLU A 44  ? 1.01484 0.85164 0.79117 0.12799  -0.12247 -0.05644 247 GLU A CD  
298  O OE1 . GLU A 44  ? 0.90139 0.74129 0.67907 0.13736  -0.13125 -0.06383 247 GLU A OE1 
299  O OE2 . GLU A 44  ? 1.05528 0.87742 0.81681 0.13935  -0.13081 -0.06209 247 GLU A OE2 
300  N N   . PRO A 45  ? 0.52268 0.39575 0.34248 0.05548  -0.06277 -0.00975 248 PRO A N   
301  C CA  . PRO A 45  ? 0.50197 0.37480 0.32140 0.04808  -0.05533 -0.00189 248 PRO A CA  
302  C C   . PRO A 45  ? 0.52077 0.38365 0.32675 0.06116  -0.06420 -0.00631 248 PRO A C   
303  O O   . PRO A 45  ? 0.58154 0.45328 0.39471 0.07346  -0.07730 -0.01909 248 PRO A O   
304  C CB  . PRO A 45  ? 0.45266 0.35874 0.30566 0.03566  -0.05096 -0.00332 248 PRO A CB  
305  C CG  . PRO A 45  ? 0.43922 0.36304 0.31042 0.04110  -0.05864 -0.01618 248 PRO A CG  
306  C CD  . PRO A 45  ? 0.44434 0.35011 0.29757 0.05031  -0.06442 -0.01854 248 PRO A CD  
307  N N   . TYR A 46  ? 0.56885 0.41363 0.35675 0.05886  -0.05710 0.00264  249 TYR A N   
308  C CA  . TYR A 46  ? 0.60844 0.44011 0.37907 0.07162  -0.06474 -0.00034 249 TYR A CA  
309  C C   . TYR A 46  ? 0.53120 0.36664 0.30659 0.06076  -0.05460 0.00799  249 TYR A C   
310  O O   . TYR A 46  ? 0.53447 0.36239 0.30733 0.04801  -0.04059 0.01770  249 TYR A O   
311  C CB  . TYR A 46  ? 0.69392 0.47928 0.41622 0.08763  -0.06756 0.00190  249 TYR A CB  
312  C CG  . TYR A 46  ? 0.72573 0.49911 0.43374 0.10428  -0.08128 -0.00768 249 TYR A CG  
313  C CD1 . TYR A 46  ? 0.75930 0.53141 0.46076 0.12538  -0.10108 -0.02187 249 TYR A CD1 
314  C CD2 . TYR A 46  ? 0.74889 0.51075 0.44929 0.10038  -0.07549 -0.00407 249 TYR A CD2 
315  C CE1 . TYR A 46  ? 0.82719 0.58772 0.51543 0.14272  -0.11570 -0.03278 249 TYR A CE1 
316  C CE2 . TYR A 46  ? 0.84851 0.59808 0.53453 0.11649  -0.08870 -0.01317 249 TYR A CE2 
317  C CZ  . TYR A 46  ? 0.96653 0.71524 0.64609 0.13798  -0.10913 -0.02763 249 TYR A CZ  
318  O OH  . TYR A 46  ? 1.00269 0.73958 0.66888 0.15559  -0.12409 -0.03872 249 TYR A OH  
319  N N   . PHE A 47  ? 0.52294 0.36983 0.30646 0.06646  -0.06205 0.00251  250 PHE A N   
320  C CA  . PHE A 47  ? 0.52077 0.36328 0.30001 0.06004  -0.05392 0.01023  250 PHE A CA  
321  C C   . PHE A 47  ? 0.60582 0.40409 0.33940 0.07039  -0.05074 0.01597  250 PHE A C   
322  O O   . PHE A 47  ? 0.64689 0.42140 0.35201 0.08917  -0.06206 0.01019  250 PHE A O   
323  C CB  . PHE A 47  ? 0.53387 0.40140 0.33600 0.06268  -0.06209 0.00229  250 PHE A CB  
324  C CG  . PHE A 47  ? 0.48110 0.38492 0.32320 0.04840  -0.05779 0.00020  250 PHE A CG  
325  C CD1 . PHE A 47  ? 0.44821 0.35976 0.30028 0.03249  -0.04535 0.01017  250 PHE A CD1 
326  C CD2 . PHE A 47  ? 0.46779 0.39514 0.33592 0.05147  -0.06532 -0.01288 250 PHE A CD2 
327  C CE1 . PHE A 47  ? 0.47370 0.41155 0.35440 0.02149  -0.04123 0.00888  250 PHE A CE1 
328  C CE2 . PHE A 47  ? 0.49595 0.44964 0.39483 0.03808  -0.05780 -0.01404 250 PHE A CE2 
329  C CZ  . PHE A 47  ? 0.44240 0.39902 0.34406 0.02390  -0.04609 -0.00223 250 PHE A CZ  
330  N N   . THR A 48  ? 0.65056 0.43534 0.37576 0.05874  -0.03465 0.02630  251 THR A N   
331  C CA  . THR A 48  ? 0.64234 0.38052 0.32227 0.06611  -0.02615 0.03235  251 THR A CA  
332  C C   . THR A 48  ? 0.67246 0.39774 0.33104 0.08207  -0.03657 0.02886  251 THR A C   
333  O O   . THR A 48  ? 0.72042 0.40040 0.33142 0.09547  -0.03446 0.03156  251 THR A O   
334  C CB  . THR A 48  ? 0.64737 0.37836 0.33137 0.04792  -0.00452 0.04112  251 THR A CB  
335  O OG1 . THR A 48  ? 0.58002 0.34011 0.29241 0.03871  -0.00404 0.04149  251 THR A OG1 
336  C CG2 . THR A 48  ? 0.58447 0.32824 0.29069 0.03386  0.00399  0.04202  251 THR A CG2 
337  N N   . SER A 49  ? 0.70946 0.47052 0.39973 0.08176  -0.04724 0.02234  252 SER A N   
338  C CA  . SER A 49  ? 0.77048 0.52540 0.44690 0.09947  -0.06177 0.01474  252 SER A CA  
339  C C   . SER A 49  ? 0.77274 0.56238 0.48186 0.10767  -0.08083 -0.00091 252 SER A C   
340  O O   . SER A 49  ? 0.72760 0.55679 0.48086 0.09341  -0.07857 -0.00354 252 SER A O   
341  C CB  . SER A 49  ? 0.79661 0.56095 0.48288 0.09104  -0.05482 0.01931  252 SER A CB  
342  O OG  . SER A 49  ? 0.92045 0.68049 0.59519 0.10911  -0.07031 0.01040  252 SER A OG  
343  N N   . SER A 50  ? 0.88000 0.65296 0.56687 0.13127  -0.09902 -0.01270 253 SER A N   
344  C CA  . SER A 50  ? 0.93662 0.74250 0.65798 0.14037  -0.11735 -0.03192 253 SER A CA  
345  C C   . SER A 50  ? 0.94726 0.77766 0.69388 0.14493  -0.12714 -0.04354 253 SER A C   
346  O O   . SER A 50  ? 0.92946 0.79430 0.71676 0.14719  -0.13785 -0.06112 253 SER A O   
347  C CB  . SER A 50  ? 0.95415 0.73302 0.64384 0.16581  -0.13536 -0.04327 253 SER A CB  
348  O OG  . SER A 50  ? 1.04997 0.78467 0.68695 0.18632  -0.14234 -0.04176 253 SER A OG  
349  N N   . THR A 51  ? 0.83366 0.64757 0.55957 0.14543  -0.12225 -0.03532 254 THR A N   
350  C CA  . THR A 51  ? 0.91887 0.74864 0.66030 0.15436  -0.13402 -0.04736 254 THR A CA  
351  C C   . THR A 51  ? 0.72111 0.58573 0.50380 0.13198  -0.12107 -0.04215 254 THR A C   
352  O O   . THR A 51  ? 0.80249 0.67820 0.59670 0.13652  -0.12730 -0.04934 254 THR A O   
353  C CB  . THR A 51  ? 0.89173 0.67641 0.57797 0.17390  -0.13978 -0.04376 254 THR A CB  
354  O OG1 . THR A 51  ? 1.02827 0.78875 0.68904 0.15885  -0.11757 -0.02240 254 THR A OG1 
355  C CG2 . THR A 51  ? 0.89914 0.64405 0.53872 0.19942  -0.15422 -0.05013 254 THR A CG2 
356  N N   . LEU A 52  ? 0.68360 0.56382 0.48677 0.10966  -0.10437 -0.03076 255 LEU A N   
357  C CA  . LEU A 52  ? 0.61571 0.52498 0.45353 0.09013  -0.09278 -0.02590 255 LEU A CA  
358  C C   . LEU A 52  ? 0.60384 0.54939 0.48667 0.09029  -0.10052 -0.04395 255 LEU A C   
359  O O   . LEU A 52  ? 0.56737 0.52861 0.47194 0.09005  -0.10348 -0.05437 255 LEU A O   
360  C CB  . LEU A 52  ? 0.62025 0.53564 0.46716 0.07012  -0.07639 -0.01266 255 LEU A CB  
361  C CG  . LEU A 52  ? 0.69656 0.58153 0.50994 0.06515  -0.06454 0.00323  255 LEU A CG  
362  C CD1 . LEU A 52  ? 0.59292 0.49014 0.42322 0.04739  -0.05216 0.01114  255 LEU A CD1 
363  C CD2 . LEU A 52  ? 0.73408 0.60835 0.53504 0.06283  -0.05849 0.01041  255 LEU A CD2 
364  N N   . PRO A 53  ? 0.54476 0.50441 0.44467 0.08968  -0.10219 -0.04916 256 PRO A N   
365  C CA  . PRO A 53  ? 0.52941 0.52171 0.47425 0.09027  -0.10813 -0.06959 256 PRO A CA  
366  C C   . PRO A 53  ? 0.44747 0.46519 0.42842 0.06880  -0.09180 -0.06746 256 PRO A C   
367  O O   . PRO A 53  ? 0.45884 0.50070 0.47750 0.06746  -0.09264 -0.08550 256 PRO A O   
368  C CB  . PRO A 53  ? 0.48764 0.48185 0.43391 0.09701  -0.11435 -0.07449 256 PRO A CB  
369  C CG  . PRO A 53  ? 0.53737 0.50969 0.45172 0.08884  -0.10306 -0.05178 256 PRO A CG  
370  C CD  . PRO A 53  ? 0.59297 0.53739 0.47147 0.09020  -0.09921 -0.03908 256 PRO A CD  
371  N N   . TRP A 54  ? 0.47557 0.48697 0.44600 0.05293  -0.07676 -0.04799 257 TRP A N   
372  C CA  . TRP A 54  ? 0.39730 0.42658 0.39416 0.03514  -0.06188 -0.04553 257 TRP A CA  
373  C C   . TRP A 54  ? 0.49391 0.52343 0.49226 0.03022  -0.05687 -0.04443 257 TRP A C   
374  O O   . TRP A 54  ? 0.42069 0.45810 0.43190 0.01654  -0.04369 -0.04024 257 TRP A O   
375  C CB  . TRP A 54  ? 0.34683 0.37057 0.33360 0.02258  -0.05055 -0.02796 257 TRP A CB  
376  C CG  . TRP A 54  ? 0.45087 0.45285 0.40528 0.02163  -0.04844 -0.01157 257 TRP A CG  
377  C CD1 . TRP A 54  ? 0.48889 0.47118 0.41638 0.02968  -0.05300 -0.00585 257 TRP A CD1 
378  C CD2 . TRP A 54  ? 0.39036 0.38696 0.33732 0.01159  -0.03948 -0.00044 257 TRP A CD2 
379  N NE1 . TRP A 54  ? 0.42528 0.39114 0.33244 0.02363  -0.04536 0.00728  257 TRP A NE1 
380  C CE2 . TRP A 54  ? 0.38376 0.35988 0.30417 0.01304  -0.03848 0.01005  257 TRP A CE2 
381  C CE3 . TRP A 54  ? 0.44545 0.45085 0.40478 0.00206  -0.03169 0.00060  257 TRP A CE3 
382  C CZ2 . TRP A 54  ? 0.46468 0.43292 0.37645 0.00500  -0.03101 0.01941  257 TRP A CZ2 
383  C CZ3 . TRP A 54  ? 0.40909 0.40518 0.35531 -0.00407 -0.02643 0.01112  257 TRP A CZ3 
384  C CH2 . TRP A 54  ? 0.45260 0.43238 0.37827 -0.00275 -0.02665 0.01939  257 TRP A CH2 
385  N N   . ILE A 55  ? 0.46284 0.48138 0.44565 0.04213  -0.06719 -0.04841 258 ILE A N   
386  C CA  . ILE A 55  ? 0.46156 0.48094 0.44669 0.03931  -0.06431 -0.04944 258 ILE A CA  
387  C C   . ILE A 55  ? 0.46835 0.49676 0.46926 0.05354  -0.07778 -0.07124 258 ILE A C   
388  O O   . ILE A 55  ? 0.47029 0.48785 0.45579 0.07109  -0.09357 -0.07862 258 ILE A O   
389  C CB  . ILE A 55  ? 0.50284 0.49814 0.45304 0.03949  -0.06301 -0.03307 258 ILE A CB  
390  C CG1 . ILE A 55  ? 0.53825 0.53321 0.48641 0.02295  -0.04848 -0.01719 258 ILE A CG1 
391  C CG2 . ILE A 55  ? 0.52637 0.51784 0.47292 0.04548  -0.06797 -0.03890 258 ILE A CG2 
392  C CD1 . ILE A 55  ? 0.56298 0.53582 0.48197 0.02181  -0.04573 -0.00285 258 ILE A CD1 
393  N N   . THR A 56  ? 0.39967 0.44636 0.43041 0.04699  -0.07161 -0.08292 259 THR A N   
394  C CA  . THR A 56  ? 0.41945 0.48062 0.47562 0.05873  -0.08302 -0.10809 259 THR A CA  
395  C C   . THR A 56  ? 0.57412 0.62409 0.61328 0.06509  -0.08872 -0.10677 259 THR A C   
396  O O   . THR A 56  ? 0.63339 0.68900 0.68211 0.05354  -0.07681 -0.10389 259 THR A O   
397  C CB  . THR A 56  ? 0.49025 0.57761 0.59280 0.04628  -0.06945 -0.12414 259 THR A CB  
398  O OG1 . THR A 56  ? 0.43640 0.53009 0.55042 0.03733  -0.06020 -0.12113 259 THR A OG1 
399  C CG2 . THR A 56  ? 0.51162 0.61823 0.64903 0.05905  -0.08215 -0.15539 259 THR A CG2 
400  N N   . GLY A 57  ? 0.49378 0.52463 0.50432 0.08427  -0.10655 -0.10873 260 GLY A N   
401  C CA  . GLY A 57  ? 0.46598 0.48454 0.45996 0.09275  -0.11368 -0.10995 260 GLY A CA  
402  C C   . GLY A 57  ? 0.47941 0.47470 0.43861 0.08390  -0.10340 -0.08513 260 GLY A C   
403  O O   . GLY A 57  ? 0.53230 0.51960 0.47820 0.07214  -0.09177 -0.06687 260 GLY A O   
404  N N   . ALA A 58  ? 0.44672 0.43158 0.39315 0.09053  -0.10865 -0.08678 261 ALA A N   
405  C CA  . ALA A 58  ? 0.47013 0.43309 0.38666 0.08392  -0.10025 -0.06737 261 ALA A CA  
406  C C   . ALA A 58  ? 0.43735 0.41712 0.37467 0.06364  -0.08344 -0.05985 261 ALA A C   
407  O O   . ALA A 58  ? 0.43690 0.44091 0.40779 0.05743  -0.07907 -0.07179 261 ALA A O   
408  C CB  . ALA A 58  ? 0.45550 0.40002 0.35063 0.09963  -0.11255 -0.07342 261 ALA A CB  
409  N N   . PRO A 59  ? 0.42173 0.38706 0.33897 0.05379  -0.07333 -0.04160 262 PRO A N   
410  C CA  . PRO A 59  ? 0.43746 0.41420 0.36825 0.03876  -0.06080 -0.03595 262 PRO A CA  
411  C C   . PRO A 59  ? 0.47878 0.45716 0.41328 0.04288  -0.06450 -0.04384 262 PRO A C   
412  O O   . PRO A 59  ? 0.50261 0.46616 0.41997 0.05615  -0.07556 -0.04799 262 PRO A O   
413  C CB  . PRO A 59  ? 0.43120 0.39094 0.33958 0.03085  -0.05286 -0.01786 262 PRO A CB  
414  C CG  . PRO A 59  ? 0.49144 0.42490 0.36987 0.04257  -0.05991 -0.01464 262 PRO A CG  
415  C CD  . PRO A 59  ? 0.47229 0.40789 0.35297 0.05716  -0.07276 -0.02762 262 PRO A CD  
416  N N   . THR A 60  ? 0.36060 0.35439 0.31487 0.03237  -0.05494 -0.04623 263 THR A N   
417  C CA  . THR A 60  ? 0.36720 0.36419 0.32727 0.03518  -0.05716 -0.05431 263 THR A CA  
418  C C   . THR A 60  ? 0.45229 0.44783 0.40838 0.02322  -0.04549 -0.04384 263 THR A C   
419  O O   . THR A 60  ? 0.43019 0.42761 0.38672 0.01260  -0.03501 -0.03491 263 THR A O   
420  C CB  . THR A 60  ? 0.43344 0.45243 0.42706 0.03749  -0.05823 -0.07552 263 THR A CB  
421  O OG1 . THR A 60  ? 0.45978 0.49188 0.47300 0.02341  -0.04216 -0.07547 263 THR A OG1 
422  C CG2 . THR A 60  ? 0.49450 0.51744 0.49587 0.05181  -0.07280 -0.09016 263 THR A CG2 
423  N N   . ILE A 61  ? 0.40790 0.39895 0.35882 0.02662  -0.04868 -0.04614 264 ILE A N   
424  C CA  . ILE A 61  ? 0.41636 0.40822 0.36664 0.01752  -0.03930 -0.04061 264 ILE A CA  
425  C C   . ILE A 61  ? 0.40760 0.41652 0.38297 0.01256  -0.03074 -0.05312 264 ILE A C   
426  O O   . ILE A 61  ? 0.42163 0.43935 0.41239 0.01827  -0.03517 -0.06796 264 ILE A O   
427  C CB  . ILE A 61  ? 0.46108 0.44137 0.39718 0.02292  -0.04537 -0.03911 264 ILE A CB  
428  C CG1 . ILE A 61  ? 0.45803 0.41698 0.36906 0.02845  -0.05127 -0.02955 264 ILE A CG1 
429  C CG2 . ILE A 61  ? 0.37518 0.35530 0.30876 0.01426  -0.03680 -0.03297 264 ILE A CG2 
430  C CD1 . ILE A 61  ? 0.44041 0.38369 0.33555 0.03546  -0.05699 -0.02971 264 ILE A CD1 
431  N N   . SER A 62  ? 0.35549 0.36716 0.33465 0.00233  -0.01761 -0.04848 265 SER A N   
432  C CA  . SER A 62  ? 0.35508 0.37774 0.35581 -0.00368 -0.00489 -0.06059 265 SER A CA  
433  C C   . SER A 62  ? 0.37755 0.39453 0.37120 -0.00886 0.00511  -0.05874 265 SER A C   
434  O O   . SER A 62  ? 0.38052 0.40342 0.39057 -0.01382 0.01786  -0.07017 265 SER A O   
435  C CB  . SER A 62  ? 0.37884 0.40274 0.38507 -0.01149 0.00692  -0.05834 265 SER A CB  
436  O OG  . SER A 62  ? 0.42265 0.43257 0.40438 -0.01598 0.01065  -0.04103 265 SER A OG  
437  N N   . SER A 63  ? 0.39531 0.40036 0.36606 -0.00784 0.00064  -0.04625 266 SER A N   
438  C CA  . SER A 63  ? 0.38287 0.38164 0.34499 -0.01076 0.00805  -0.04533 266 SER A CA  
439  C C   . SER A 63  ? 0.37020 0.36036 0.31449 -0.00652 -0.00253 -0.03630 266 SER A C   
440  O O   . SER A 63  ? 0.38368 0.36679 0.31507 -0.00625 -0.00775 -0.02568 266 SER A O   
441  C CB  . SER A 63  ? 0.40091 0.38840 0.34968 -0.01798 0.02330  -0.03886 266 SER A CB  
442  O OG  . SER A 63  ? 0.49148 0.46875 0.42552 -0.01836 0.02851  -0.03720 266 SER A OG  
443  N N   . ARG A 64  ? 0.38562 0.37673 0.33166 -0.00379 -0.00461 -0.04203 267 ARG A N   
444  C CA  . ARG A 64  ? 0.38094 0.36342 0.31194 -0.00090 -0.01194 -0.03532 267 ARG A CA  
445  C C   . ARG A 64  ? 0.46476 0.44264 0.38831 -0.00311 -0.00469 -0.03621 267 ARG A C   
446  O O   . ARG A 64  ? 0.42010 0.39364 0.33616 -0.00021 -0.01068 -0.03455 267 ARG A O   
447  C CB  . ARG A 64  ? 0.43462 0.41828 0.36961 0.00681  -0.02378 -0.04064 267 ARG A CB  
448  C CG  . ARG A 64  ? 0.39021 0.37494 0.32902 0.01203  -0.03136 -0.04249 267 ARG A CG  
449  C CD  . ARG A 64  ? 0.44738 0.42122 0.37526 0.02142  -0.04333 -0.04281 267 ARG A CD  
450  N NE  . ARG A 64  ? 0.47699 0.43520 0.38620 0.01924  -0.04343 -0.03019 267 ARG A NE  
451  C CZ  . ARG A 64  ? 0.56678 0.50814 0.46063 0.02545  -0.04945 -0.02763 267 ARG A CZ  
452  N NH1 . ARG A 64  ? 0.49185 0.42760 0.38179 0.03651  -0.05856 -0.03569 267 ARG A NH1 
453  N NH2 . ARG A 64  ? 0.48223 0.41014 0.36394 0.02104  -0.04577 -0.01817 267 ARG A NH2 
454  N N   . THR A 65  ? 0.44976 0.42566 0.37313 -0.00798 0.00930  -0.03908 268 THR A N   
455  C CA  . THR A 65  ? 0.46022 0.42836 0.37378 -0.00887 0.01768  -0.04153 268 THR A CA  
456  C C   . THR A 65  ? 0.50064 0.45397 0.38816 -0.00648 0.01406  -0.03129 268 THR A C   
457  O O   . THR A 65  ? 0.50341 0.45017 0.38063 -0.00421 0.01486  -0.03279 268 THR A O   
458  C CB  . THR A 65  ? 0.50970 0.47409 0.42695 -0.01498 0.03732  -0.04828 268 THR A CB  
459  O OG1 . THR A 65  ? 0.54499 0.49685 0.44596 -0.01773 0.04439  -0.03961 268 THR A OG1 
460  C CG2 . THR A 65  ? 0.46098 0.44392 0.41151 -0.01694 0.03995  -0.06304 268 THR A CG2 
461  N N   . ASP A 66  ? 0.39922 0.34789 0.27742 -0.00607 0.00920  -0.02282 269 ASP A N   
462  C CA  . ASP A 66  ? 0.48095 0.41892 0.34009 -0.00198 0.00213  -0.01690 269 ASP A CA  
463  C C   . ASP A 66  ? 0.46579 0.41102 0.33430 0.00035  -0.01099 -0.01690 269 ASP A C   
464  O O   . ASP A 66  ? 0.39956 0.35101 0.27881 -0.00097 -0.01596 -0.01482 269 ASP A O   
465  C CB  . ASP A 66  ? 0.45535 0.38624 0.30368 -0.00194 0.00178  -0.01042 269 ASP A CB  
466  C CG  . ASP A 66  ? 0.54055 0.46065 0.37055 0.00443  -0.00707 -0.00802 269 ASP A CG  
467  O OD1 . ASP A 66  ? 0.47915 0.40291 0.31322 0.00748  -0.01650 -0.01069 269 ASP A OD1 
468  O OD2 . ASP A 66  ? 0.60145 0.50871 0.41323 0.00723  -0.00517 -0.00481 269 ASP A OD2 
469  N N   . PRO A 67  ? 0.47359 0.41564 0.33676 0.00382  -0.01554 -0.01940 270 PRO A N   
470  C CA  . PRO A 67  ? 0.47690 0.42338 0.34966 0.00500  -0.02521 -0.02033 270 PRO A CA  
471  C C   . PRO A 67  ? 0.44487 0.39072 0.32043 0.00411  -0.03105 -0.01673 270 PRO A C   
472  O O   . PRO A 67  ? 0.40590 0.35273 0.29029 0.00293  -0.03456 -0.01679 270 PRO A O   
473  C CB  . PRO A 67  ? 0.48138 0.42340 0.34640 0.00894  -0.02795 -0.02430 270 PRO A CB  
474  C CG  . PRO A 67  ? 0.47320 0.40999 0.32736 0.00926  -0.01782 -0.02640 270 PRO A CG  
475  C CD  . PRO A 67  ? 0.49335 0.42531 0.34027 0.00691  -0.01065 -0.02207 270 PRO A CD  
476  N N   . ASN A 68  ? 0.43147 0.37356 0.29890 0.00490  -0.03125 -0.01442 271 ASN A N   
477  C CA  . ASN A 68  ? 0.44212 0.38567 0.31653 0.00389  -0.03667 -0.01373 271 ASN A CA  
478  C C   . ASN A 68  ? 0.40822 0.35493 0.28891 -0.00050 -0.03327 -0.00885 271 ASN A C   
479  O O   . ASN A 68  ? 0.42112 0.36895 0.30990 -0.00259 -0.03581 -0.00880 271 ASN A O   
480  C CB  . ASN A 68  ? 0.49847 0.43660 0.36197 0.00934  -0.04207 -0.01622 271 ASN A CB  
481  C CG  . ASN A 68  ? 0.55320 0.48706 0.40946 0.01573  -0.04802 -0.02256 271 ASN A CG  
482  O OD1 . ASN A 68  ? 0.63212 0.56950 0.49711 0.01451  -0.04889 -0.02555 271 ASN A OD1 
483  N ND2 . ASN A 68  ? 0.61249 0.53648 0.45016 0.02396  -0.05290 -0.02506 271 ASN A ND2 
484  N N   . LYS A 69  ? 0.40127 0.34962 0.28027 -0.00208 -0.02707 -0.00629 272 LYS A N   
485  C CA  . LYS A 69  ? 0.42796 0.37929 0.31261 -0.00521 -0.02521 -0.00244 272 LYS A CA  
486  C C   . LYS A 69  ? 0.40881 0.36489 0.29910 -0.00607 -0.02068 -0.00359 272 LYS A C   
487  O O   . LYS A 69  ? 0.41624 0.37374 0.30614 -0.00556 -0.01593 -0.00757 272 LYS A O   
488  C CB  . LYS A 69  ? 0.40926 0.35761 0.28620 -0.00512 -0.02405 0.00036  272 LYS A CB  
489  C CG  . LYS A 69  ? 0.49933 0.44187 0.36392 -0.00438 -0.01609 0.00078  272 LYS A CG  
490  C CD  . LYS A 69  ? 0.61847 0.55101 0.46731 -0.00154 -0.01627 0.00346  272 LYS A CD  
491  C CE  . LYS A 69  ? 0.61408 0.53199 0.44264 -0.00021 -0.00520 0.00414  272 LYS A CE  
492  N NZ  . LYS A 69  ? 0.64424 0.54715 0.45172 0.00458  -0.00618 0.00723  272 LYS A NZ  
493  N N   . ASP A 70  ? 0.34705 0.30505 0.24335 -0.00684 -0.02209 -0.00175 273 ASP A N   
494  C CA  . ASP A 70  ? 0.39024 0.35404 0.29404 -0.00606 -0.02024 -0.00480 273 ASP A CA  
495  C C   . ASP A 70  ? 0.39793 0.36430 0.30316 -0.00928 -0.01580 -0.00169 273 ASP A C   
496  O O   . ASP A 70  ? 0.41499 0.37788 0.31556 -0.01107 -0.01687 0.00382  273 ASP A O   
497  C CB  . ASP A 70  ? 0.34703 0.30699 0.25123 -0.00187 -0.02632 -0.00554 273 ASP A CB  
498  C CG  . ASP A 70  ? 0.45507 0.41110 0.35722 0.00283  -0.03063 -0.01016 273 ASP A CG  
499  O OD1 . ASP A 70  ? 0.40195 0.36355 0.30829 0.00288  -0.02895 -0.01515 273 ASP A OD1 
500  O OD2 . ASP A 70  ? 0.48838 0.43298 0.38243 0.00689  -0.03486 -0.00888 273 ASP A OD2 
501  N N   . VAL A 71  ? 0.34548 0.31843 0.25954 -0.01018 -0.01036 -0.00688 274 VAL A N   
502  C CA  . VAL A 71  ? 0.32406 0.29957 0.24178 -0.01324 -0.00549 -0.00525 274 VAL A CA  
503  C C   . VAL A 71  ? 0.41592 0.39840 0.34519 -0.01001 -0.01088 -0.00954 274 VAL A C   
504  O O   . VAL A 71  ? 0.36748 0.35665 0.30814 -0.00610 -0.01338 -0.01932 274 VAL A O   
505  C CB  . VAL A 71  ? 0.33157 0.30656 0.25109 -0.01722 0.00720  -0.00942 274 VAL A CB  
506  C CG1 . VAL A 71  ? 0.32946 0.30422 0.25079 -0.02079 0.01327  -0.00706 274 VAL A CG1 
507  C CG2 . VAL A 71  ? 0.34480 0.30702 0.24530 -0.01735 0.01160  -0.00567 274 VAL A CG2 
508  N N   . ILE A 72  ? 0.34863 0.32874 0.27432 -0.01031 -0.01365 -0.00355 275 ILE A N   
509  C CA  . ILE A 72  ? 0.33177 0.31454 0.26289 -0.00568 -0.01934 -0.00677 275 ILE A CA  
510  C C   . ILE A 72  ? 0.38677 0.37786 0.32930 -0.00912 -0.01375 -0.00935 275 ILE A C   
511  O O   . ILE A 72  ? 0.36134 0.34960 0.29868 -0.01454 -0.00808 -0.00237 275 ILE A O   
512  C CB  . ILE A 72  ? 0.33031 0.30151 0.24779 -0.00392 -0.02407 0.00136  275 ILE A CB  
513  C CG1 . ILE A 72  ? 0.37815 0.33855 0.28483 -0.00234 -0.02646 0.00379  275 ILE A CG1 
514  C CG2 . ILE A 72  ? 0.39366 0.36247 0.31010 0.00305  -0.03010 -0.00180 275 ILE A CG2 
515  C CD1 . ILE A 72  ? 0.39899 0.35767 0.30519 0.00508  -0.03206 -0.00363 275 ILE A CD1 
516  N N   . SER A 73  ? 0.33247 0.33333 0.29111 -0.00509 -0.01612 -0.02080 276 SER A N   
517  C CA  . SER A 73  ? 0.30833 0.31839 0.28241 -0.00815 -0.01068 -0.02621 276 SER A CA  
518  C C   . SER A 73  ? 0.36448 0.37633 0.34056 -0.00058 -0.02107 -0.02914 276 SER A C   
519  O O   . SER A 73  ? 0.38013 0.38799 0.35069 0.00951  -0.03251 -0.03357 276 SER A O   
520  C CB  . SER A 73  ? 0.30490 0.32717 0.30295 -0.01033 -0.00288 -0.04186 276 SER A CB  
521  O OG  . SER A 73  ? 0.40225 0.41875 0.39472 -0.01761 0.00986  -0.03894 276 SER A OG  
522  N N   . PHE A 74  ? 0.35364 0.36895 0.33498 -0.00436 -0.01706 -0.02710 277 PHE A N   
523  C CA  . PHE A 74  ? 0.38161 0.40005 0.36743 0.00276  -0.02570 -0.03199 277 PHE A CA  
524  C C   . PHE A 74  ? 0.40163 0.43094 0.40645 -0.00389 -0.01682 -0.03677 277 PHE A C   
525  O O   . PHE A 74  ? 0.31842 0.34552 0.32219 -0.01387 -0.00398 -0.03055 277 PHE A O   
526  C CB  . PHE A 74  ? 0.31331 0.31649 0.27455 0.00579  -0.03134 -0.01875 277 PHE A CB  
527  C CG  . PHE A 74  ? 0.34214 0.34121 0.29573 -0.00407 -0.02278 -0.00578 277 PHE A CG  
528  C CD1 . PHE A 74  ? 0.38134 0.37426 0.32536 -0.00949 -0.01806 0.00188  277 PHE A CD1 
529  C CD2 . PHE A 74  ? 0.43299 0.43477 0.38980 -0.00673 -0.02070 -0.00296 277 PHE A CD2 
530  C CE1 . PHE A 74  ? 0.40691 0.39628 0.34461 -0.01602 -0.01290 0.01082  277 PHE A CE1 
531  C CE2 . PHE A 74  ? 0.39300 0.39095 0.34308 -0.01429 -0.01444 0.00725  277 PHE A CE2 
532  C CZ  . PHE A 74  ? 0.42675 0.41846 0.36728 -0.01827 -0.01124 0.01347  277 PHE A CZ  
533  N N   . THR A 75  ? 0.35981 0.39835 0.37975 0.00287  -0.02404 -0.04845 278 THR A N   
534  C CA  . THR A 75  ? 0.36043 0.41125 0.40431 -0.00303 -0.01541 -0.05712 278 THR A CA  
535  C C   . THR A 75  ? 0.40220 0.45067 0.43915 -0.00018 -0.02107 -0.05136 278 THR A C   
536  O O   . THR A 75  ? 0.43116 0.47583 0.45885 0.01176  -0.03554 -0.05362 278 THR A O   
537  C CB  . THR A 75  ? 0.37074 0.43958 0.44887 0.00149  -0.01750 -0.08167 278 THR A CB  
538  O OG1 . THR A 75  ? 0.37870 0.44928 0.46399 -0.00311 -0.00919 -0.08675 278 THR A OG1 
539  C CG2 . THR A 75  ? 0.39587 0.47728 0.50272 -0.00600 -0.00602 -0.09277 278 THR A CG2 
540  N N   . CYS A 76  ? 0.33764 0.38540 0.37601 -0.01027 -0.00931 -0.04409 279 CYS A N   
541  C CA  . CYS A 76  ? 0.36191 0.40784 0.39481 -0.00983 -0.01209 -0.03770 279 CYS A CA  
542  C C   . CYS A 76  ? 0.37973 0.43947 0.44144 -0.01320 -0.00565 -0.05130 279 CYS A C   
543  O O   . CYS A 76  ? 0.33041 0.39477 0.40969 -0.02190 0.00900  -0.05876 279 CYS A O   
544  C CB  . CYS A 76  ? 0.33786 0.37129 0.34950 -0.01797 -0.00470 -0.01930 279 CYS A CB  
545  S SG  . CYS A 76  ? 0.45075 0.46925 0.43375 -0.01588 -0.01045 -0.00495 279 CYS A SG  
546  N N   . LEU A 77  ? 0.35099 0.41541 0.41695 -0.00630 -0.01533 -0.05537 280 LEU A N   
547  C CA  . LEU A 77  ? 0.37291 0.44806 0.46261 -0.01116 -0.00821 -0.06433 280 LEU A CA  
548  C C   . LEU A 77  ? 0.29989 0.36399 0.37374 -0.02178 0.00359  -0.04712 280 LEU A C   
549  O O   . LEU A 77  ? 0.26794 0.31862 0.31416 -0.02280 0.00196  -0.02999 280 LEU A O   
550  C CB  . LEU A 77  ? 0.35155 0.43411 0.44837 0.00127  -0.02413 -0.07427 280 LEU A CB  
551  C CG  . LEU A 77  ? 0.34763 0.43885 0.45687 0.01659  -0.04057 -0.09380 280 LEU A CG  
552  C CD1 . LEU A 77  ? 0.35651 0.45146 0.46839 0.03056  -0.05672 -0.10375 280 LEU A CD1 
553  C CD2 . LEU A 77  ? 0.34255 0.45191 0.49113 0.01170  -0.03194 -0.11538 280 LEU A CD2 
554  N N   . LYS A 78  ? 0.30170 0.37104 0.39437 -0.02915 0.01537  -0.05349 281 LYS A N   
555  C CA  . LYS A 78  ? 0.29218 0.34938 0.36807 -0.03665 0.02421  -0.03852 281 LYS A CA  
556  C C   . LYS A 78  ? 0.36784 0.42298 0.42763 -0.03013 0.01034  -0.02834 281 LYS A C   
557  O O   . LYS A 78  ? 0.30939 0.37369 0.37868 -0.02151 -0.00151 -0.03684 281 LYS A O   
558  C CB  . LYS A 78  ? 0.35228 0.41302 0.45074 -0.04505 0.04001  -0.04837 281 LYS A CB  
559  C CG  . LYS A 78  ? 0.38301 0.42796 0.46148 -0.05147 0.04907  -0.03366 281 LYS A CG  
560  C CD  . LYS A 78  ? 0.39293 0.43905 0.49322 -0.05938 0.06543  -0.04414 281 LYS A CD  
561  C CE  . LYS A 78  ? 0.43115 0.45968 0.50807 -0.06326 0.07148  -0.02932 281 LYS A CE  
562  N NZ  . LYS A 78  ? 0.52552 0.55385 0.62300 -0.07056 0.08713  -0.03940 281 LYS A NZ  
563  N N   . ASN A 79  ? 0.33454 0.37633 0.36914 -0.03324 0.01157  -0.01148 282 ASN A N   
564  C CA  . ASN A 79  ? 0.34102 0.37970 0.36274 -0.03010 0.00330  -0.00228 282 ASN A CA  
565  C C   . ASN A 79  ? 0.38460 0.42471 0.41463 -0.03533 0.01048  -0.00232 282 ASN A C   
566  O O   . ASN A 79  ? 0.36620 0.39594 0.38640 -0.04172 0.02008  0.00496  282 ASN A O   
567  C CB  . ASN A 79  ? 0.31312 0.33953 0.31062 -0.03117 0.00147  0.01171  282 ASN A CB  
568  C CG  . ASN A 79  ? 0.33226 0.35542 0.31908 -0.02854 -0.00541 0.01898  282 ASN A CG  
569  O OD1 . ASN A 79  ? 0.32878 0.35680 0.32159 -0.02451 -0.01005 0.01501  282 ASN A OD1 
570  N ND2 . ASN A 79  ? 0.29454 0.30924 0.26660 -0.03054 -0.00577 0.02804  282 ASN A ND2 
571  N N   . LYS A 80  ? 0.36315 0.41417 0.40959 -0.03132 0.00528  -0.01145 283 LYS A N   
572  C CA  . LYS A 80  ? 0.41361 0.46669 0.46929 -0.03581 0.01127  -0.01222 283 LYS A CA  
573  C C   . LYS A 80  ? 0.43283 0.47982 0.47087 -0.03457 0.00536  0.00027  283 LYS A C   
574  O O   . LYS A 80  ? 0.47988 0.52512 0.52012 -0.03892 0.01083  0.00275  283 LYS A O   
575  C CB  . LYS A 80  ? 0.33976 0.40909 0.42446 -0.03157 0.00762  -0.03003 283 LYS A CB  
576  C CG  . LYS A 80  ? 0.38361 0.46230 0.49439 -0.03381 0.01502  -0.04698 283 LYS A CG  
577  C CD  . LYS A 80  ? 0.41743 0.51514 0.56107 -0.02723 0.00777  -0.06856 283 LYS A CD  
578  C CE  . LYS A 80  ? 0.47842 0.58825 0.65241 -0.02818 0.01319  -0.08908 283 LYS A CE  
579  N NZ  . LYS A 80  ? 0.46192 0.59276 0.67734 -0.02381 0.00940  -0.11512 283 LYS A NZ  
580  N N   . THR A 81  ? 0.41181 0.45424 0.43304 -0.02914 -0.00417 0.00714  284 THR A N   
581  C CA  . THR A 81  ? 0.37012 0.40716 0.37760 -0.02832 -0.00838 0.01649  284 THR A CA  
582  C C   . THR A 81  ? 0.36871 0.39688 0.36364 -0.03439 -0.00340 0.02676  284 THR A C   
583  O O   . THR A 81  ? 0.37772 0.40059 0.36792 -0.03727 0.00145  0.02835  284 THR A O   
584  C CB  . THR A 81  ? 0.36849 0.39940 0.36144 -0.02098 -0.01670 0.01855  284 THR A CB  
585  O OG1 . THR A 81  ? 0.35377 0.37639 0.33407 -0.02344 -0.01472 0.02506  284 THR A OG1 
586  C CG2 . THR A 81  ? 0.34898 0.38445 0.34861 -0.01152 -0.02420 0.00694  284 THR A CG2 
587  N N   . VAL A 82  ? 0.29905 0.32495 0.28797 -0.03500 -0.00567 0.03243  285 VAL A N   
588  C CA  . VAL A 82  ? 0.33530 0.35415 0.31445 -0.03827 -0.00426 0.03902  285 VAL A CA  
589  C C   . VAL A 82  ? 0.37364 0.38867 0.34434 -0.03737 -0.00786 0.04206  285 VAL A C   
590  O O   . VAL A 82  ? 0.37475 0.38718 0.34221 -0.03880 -0.00919 0.04438  285 VAL A O   
591  C CB  . VAL A 82  ? 0.40656 0.42618 0.38779 -0.03962 -0.00445 0.04086  285 VAL A CB  
592  C CG1 . VAL A 82  ? 0.41725 0.43840 0.40729 -0.04151 0.00147  0.03717  285 VAL A CG1 
593  C CG2 . VAL A 82  ? 0.38334 0.40734 0.36682 -0.03761 -0.00891 0.04091  285 VAL A CG2 
594  N N   . TRP A 83  ? 0.41089 0.42475 0.37890 -0.03461 -0.00925 0.04044  286 TRP A N   
595  C CA  . TRP A 83  ? 0.41651 0.42376 0.37628 -0.03446 -0.00986 0.04255  286 TRP A CA  
596  C C   . TRP A 83  ? 0.44981 0.45404 0.40552 -0.03367 -0.00966 0.04177  286 TRP A C   
597  O O   . TRP A 83  ? 0.42062 0.42766 0.37922 -0.03115 -0.01009 0.03831  286 TRP A O   
598  C CB  . TRP A 83  ? 0.42027 0.42149 0.37308 -0.03055 -0.01058 0.04223  286 TRP A CB  
599  C CG  . TRP A 83  ? 0.43663 0.43990 0.39204 -0.03042 -0.01071 0.04250  286 TRP A CG  
600  C CD1 . TRP A 83  ? 0.41389 0.41997 0.37473 -0.03506 -0.00885 0.04405  286 TRP A CD1 
601  C CD2 . TRP A 83  ? 0.37419 0.37654 0.32674 -0.02413 -0.01396 0.03979  286 TRP A CD2 
602  N NE1 . TRP A 83  ? 0.40170 0.40883 0.36329 -0.03329 -0.00940 0.04364  286 TRP A NE1 
603  C CE2 . TRP A 83  ? 0.37978 0.38423 0.33557 -0.02635 -0.01266 0.04117  286 TRP A CE2 
604  C CE3 . TRP A 83  ? 0.37540 0.37564 0.32352 -0.01543 -0.01936 0.03462  286 TRP A CE3 
605  C CZ2 . TRP A 83  ? 0.38859 0.39226 0.34182 -0.02061 -0.01582 0.03869  286 TRP A CZ2 
606  C CZ3 . TRP A 83  ? 0.45203 0.45148 0.39777 -0.00835 -0.02405 0.03077  286 TRP A CZ3 
607  C CH2 . TRP A 83  ? 0.41250 0.41340 0.36023 -0.01125 -0.02187 0.03336  286 TRP A CH2 
608  N N   . ASN A 84  ? 0.42055 0.42021 0.37232 -0.03575 -0.00903 0.04317  287 ASN A N   
609  C CA  . ASN A 84  ? 0.43889 0.43432 0.38562 -0.03455 -0.00897 0.04246  287 ASN A CA  
610  C C   . ASN A 84  ? 0.46269 0.45081 0.40139 -0.03003 -0.00937 0.04171  287 ASN A C   
611  O O   . ASN A 84  ? 0.40642 0.38813 0.33948 -0.02868 -0.00815 0.04268  287 ASN A O   
612  C CB  . ASN A 84  ? 0.50620 0.49827 0.45259 -0.03736 -0.00833 0.04217  287 ASN A CB  
613  C CG  . ASN A 84  ? 0.50317 0.49898 0.45334 -0.03839 -0.01100 0.04116  287 ASN A CG  
614  O OD1 . ASN A 84  ? 0.58015 0.57682 0.53598 -0.03987 -0.01232 0.03794  287 ASN A OD1 
615  N ND2 . ASN A 84  ? 0.47983 0.47568 0.42617 -0.03691 -0.01135 0.04238  287 ASN A ND2 
616  N N   . ARG A 85  ? 0.35341 0.33972 0.28870 -0.02651 -0.01117 0.03954  288 ARG A N   
617  C CA  . ARG A 85  ? 0.42688 0.40170 0.34922 -0.01947 -0.01337 0.03812  288 ARG A CA  
618  C C   . ARG A 85  ? 0.45927 0.42619 0.37417 -0.01894 -0.01253 0.03826  288 ARG A C   
619  O O   . ARG A 85  ? 0.36182 0.33665 0.28459 -0.02167 -0.01273 0.03712  288 ARG A O   
620  C CB  . ARG A 85  ? 0.38650 0.36737 0.31314 -0.01181 -0.01972 0.03167  288 ARG A CB  
621  C CG  . ARG A 85  ? 0.43077 0.42658 0.37494 -0.01393 -0.01991 0.02612  288 ARG A CG  
622  C CD  . ARG A 85  ? 0.35769 0.36234 0.31341 -0.00728 -0.02532 0.01620  288 ARG A CD  
623  N NE  . ARG A 85  ? 0.32285 0.33998 0.29749 -0.00935 -0.02310 0.00762  288 ARG A NE  
624  C CZ  . ARG A 85  ? 0.35119 0.38050 0.34547 -0.00630 -0.02514 -0.00452 288 ARG A CZ  
625  N NH1 . ARG A 85  ? 0.36276 0.39429 0.35938 0.00012  -0.03163 -0.00909 288 ARG A NH1 
626  N NH2 . ARG A 85  ? 0.28940 0.32860 0.30268 -0.00980 -0.01979 -0.01376 288 ARG A NH2 
627  N N   . ARG A 86  ? 0.38666 0.33488 0.28371 -0.01515 -0.01049 0.03975  289 ARG A N   
628  C CA  . ARG A 86  ? 0.46895 0.40622 0.35818 -0.01670 -0.00680 0.04074  289 ARG A CA  
629  C C   . ARG A 86  ? 0.51372 0.43719 0.38569 -0.00637 -0.01169 0.03834  289 ARG A C   
630  O O   . ARG A 86  ? 0.54333 0.45434 0.39935 0.00329  -0.01580 0.03690  289 ARG A O   
631  C CB  . ARG A 86  ? 0.50874 0.43104 0.39119 -0.02259 0.00354  0.04344  289 ARG A CB  
632  C CG  . ARG A 86  ? 0.50787 0.44421 0.40924 -0.03125 0.00664  0.04304  289 ARG A CG  
633  C CD  . ARG A 86  ? 0.57644 0.50255 0.48051 -0.03871 0.01766  0.04119  289 ARG A CD  
634  N NE  . ARG A 86  ? 0.73497 0.66707 0.65014 -0.04248 0.01743  0.03758  289 ARG A NE  
635  C CZ  . ARG A 86  ? 0.68803 0.61034 0.60692 -0.04813 0.02695  0.03349  289 ARG A CZ  
636  N NH1 . ARG A 86  ? 0.82332 0.72664 0.73455 -0.05196 0.04033  0.03282  289 ARG A NH1 
637  N NH2 . ARG A 86  ? 0.61084 0.54089 0.54112 -0.05007 0.02429  0.02907  289 ARG A NH2 
638  N N   . ALA A 87  ? 0.48734 0.41200 0.36116 -0.00696 -0.01250 0.03701  290 ALA A N   
639  C CA  . ALA A 87  ? 0.47645 0.38491 0.33213 0.00265  -0.01659 0.03465  290 ALA A CA  
640  C C   . ALA A 87  ? 0.49575 0.39610 0.34857 -0.00289 -0.01026 0.03682  290 ALA A C   
641  O O   . ALA A 87  ? 0.45377 0.36484 0.32202 -0.01299 -0.00499 0.03816  290 ALA A O   
642  C CB  . ALA A 87  ? 0.41088 0.33446 0.27739 0.01023  -0.02733 0.02660  290 ALA A CB  
643  N N   . TYR A 88  ? 0.46112 0.34106 0.29321 0.00511  -0.01175 0.03594  291 TYR A N   
644  C CA  . TYR A 88  ? 0.50372 0.37137 0.33023 0.00057  -0.00460 0.03755  291 TYR A CA  
645  C C   . TYR A 88  ? 0.55870 0.42145 0.37613 0.01002  -0.01286 0.03368  291 TYR A C   
646  O O   . TYR A 88  ? 0.49110 0.34216 0.29119 0.02332  -0.02149 0.03038  291 TYR A O   
647  C CB  . TYR A 88  ? 0.48024 0.31554 0.28326 -0.00115 0.00858  0.04162  291 TYR A CB  
648  C CG  . TYR A 88  ? 0.57999 0.41876 0.39161 -0.00925 0.01684  0.04366  291 TYR A CG  
649  C CD1 . TYR A 88  ? 0.49254 0.34407 0.32772 -0.02238 0.02535  0.04219  291 TYR A CD1 
650  C CD2 . TYR A 88  ? 0.53132 0.36170 0.32895 -0.00264 0.01467  0.04529  291 TYR A CD2 
651  C CE1 . TYR A 88  ? 0.56863 0.42500 0.41433 -0.02919 0.03188  0.04210  291 TYR A CE1 
652  C CE2 . TYR A 88  ? 0.54018 0.37448 0.34660 -0.01015 0.02224  0.04675  291 TYR A CE2 
653  C CZ  . TYR A 88  ? 0.55875 0.40639 0.38979 -0.02364 0.03098  0.04508  291 TYR A CZ  
654  O OH  . TYR A 88  ? 0.68376 0.53646 0.52576 -0.03052 0.03767  0.04468  291 TYR A OH  
655  N N   . ILE A 89  ? 0.45709 0.32892 0.28654 0.00437  -0.01150 0.03266  292 ILE A N   
656  C CA  . ILE A 89  ? 0.50001 0.36809 0.32307 0.01200  -0.01831 0.02862  292 ILE A CA  
657  C C   . ILE A 89  ? 0.48148 0.32637 0.28959 0.00919  -0.00943 0.03143  292 ILE A C   
658  O O   . ILE A 89  ? 0.58262 0.43283 0.40428 -0.00228 -0.00052 0.03289  292 ILE A O   
659  C CB  . ILE A 89  ? 0.48789 0.38535 0.33710 0.00827  -0.02358 0.02403  292 ILE A CB  
660  C CG1 . ILE A 89  ? 0.45922 0.37535 0.32229 0.01173  -0.03028 0.01904  292 ILE A CG1 
661  C CG2 . ILE A 89  ? 0.46531 0.35845 0.30972 0.01403  -0.02833 0.01971  292 ILE A CG2 
662  C CD1 . ILE A 89  ? 0.40364 0.34437 0.29064 0.00584  -0.03021 0.01511  292 ILE A CD1 
663  N N   . LYS A 90  ? 0.54909 0.36752 0.32974 0.02046  -0.01224 0.03064  293 LYS A N   
664  C CA  . LYS A 90  ? 0.57563 0.37003 0.34070 0.01902  -0.00400 0.03230  293 LYS A CA  
665  C C   . LYS A 90  ? 0.54317 0.34203 0.30733 0.02783  -0.01539 0.02707  293 LYS A C   
666  O O   . LYS A 90  ? 0.51466 0.33233 0.28883 0.03575  -0.02872 0.02106  293 LYS A O   
667  C CB  . LYS A 90  ? 0.59932 0.34822 0.32431 0.02511  0.00597  0.03675  293 LYS A CB  
668  C CG  . LYS A 90  ? 0.63639 0.37733 0.36346 0.01373  0.02206  0.04091  293 LYS A CG  
669  C CD  . LYS A 90  ? 0.70563 0.39372 0.38757 0.01930  0.03624  0.04527  293 LYS A CD  
670  C CE  . LYS A 90  ? 0.76669 0.44332 0.45188 0.00602  0.05680  0.04770  293 LYS A CE  
671  N NZ  . LYS A 90  ? 0.91920 0.53770 0.55763 0.00962  0.07589  0.05160  293 LYS A NZ  
672  N N   . PHE A 91  ? 0.52111 0.30211 0.27479 0.02625  -0.00917 0.02788  294 PHE A N   
673  C CA  . PHE A 91  ? 0.55394 0.34215 0.31137 0.03202  -0.01847 0.02277  294 PHE A CA  
674  C C   . PHE A 91  ? 0.57629 0.32323 0.29643 0.04228  -0.01623 0.02381  294 PHE A C   
675  O O   . PHE A 91  ? 0.69588 0.41581 0.40108 0.03561  -0.00058 0.02857  294 PHE A O   
676  C CB  . PHE A 91  ? 0.45844 0.27177 0.24571 0.01886  -0.01433 0.02173  294 PHE A CB  
677  C CG  . PHE A 91  ? 0.51614 0.36349 0.33315 0.01049  -0.01615 0.02106  294 PHE A CG  
678  C CD1 . PHE A 91  ? 0.53582 0.38680 0.36214 0.00059  -0.00736 0.02448  294 PHE A CD1 
679  C CD2 . PHE A 91  ? 0.42151 0.29455 0.25585 0.01291  -0.02556 0.01609  294 PHE A CD2 
680  C CE1 . PHE A 91  ? 0.56420 0.44242 0.41321 -0.00525 -0.00987 0.02394  294 PHE A CE1 
681  C CE2 . PHE A 91  ? 0.48568 0.38356 0.34161 0.00569  -0.02507 0.01610  294 PHE A CE2 
682  C CZ  . PHE A 91  ? 0.49053 0.39001 0.35181 -0.00253 -0.01822 0.02052  294 PHE A CZ  
683  N N   . LYS A 92  ? 0.53887 0.28012 0.24503 0.05851  -0.03116 0.01786  295 LYS A N   
684  C CA  . LYS A 92  ? 0.63215 0.32958 0.29598 0.07265  -0.03221 0.01813  295 LYS A CA  
685  C C   . LYS A 92  ? 0.65076 0.35675 0.32434 0.07374  -0.03770 0.01321  295 LYS A C   
686  O O   . LYS A 92  ? 0.63956 0.37894 0.33988 0.07658  -0.05107 0.00485  295 LYS A O   
687  C CB  . LYS A 92  ? 0.70249 0.38190 0.33783 0.09460  -0.04808 0.01284  295 LYS A CB  
688  C CG  . LYS A 92  ? 0.89758 0.51672 0.47361 0.11153  -0.04631 0.01584  295 LYS A CG  
689  C CD  . LYS A 92  ? 0.99144 0.57632 0.53251 0.11643  -0.03827 0.02229  295 LYS A CD  
690  N N   . ASP A 93  ? 0.65655 0.33221 0.31012 0.07039  -0.02551 0.01765  296 ASP A N   
691  C CA  . ASP A 93  ? 0.71263 0.38912 0.36867 0.07330  -0.03044 0.01333  296 ASP A CA  
692  C C   . ASP A 93  ? 0.79153 0.44883 0.41887 0.09693  -0.04896 0.00616  296 ASP A C   
693  O O   . ASP A 93  ? 0.73033 0.34056 0.31038 0.11111  -0.04829 0.00893  296 ASP A O   
694  C CB  . ASP A 93  ? 0.81284 0.45685 0.45256 0.06400  -0.01087 0.01917  296 ASP A CB  
695  C CG  . ASP A 93  ? 0.83855 0.48115 0.48008 0.06611  -0.01447 0.01516  296 ASP A CG  
696  O OD1 . ASP A 93  ? 0.82897 0.45750 0.44852 0.08374  -0.02899 0.01045  296 ASP A OD1 
697  O OD2 . ASP A 93  ? 0.75912 0.41409 0.42433 0.05089  -0.00332 0.01550  296 ASP A OD2 
698  N N   . LYS A 94  ? 0.71379 0.40525 0.36828 0.10224  -0.06536 -0.00441 297 LYS A N   
699  C CA  . LYS A 94  ? 0.80474 0.48536 0.44036 0.12599  -0.08613 -0.01570 297 LYS A CA  
700  C C   . LYS A 94  ? 0.84717 0.48229 0.43992 0.13996  -0.08806 -0.01532 297 LYS A C   
701  O O   . LYS A 94  ? 0.88924 0.49462 0.44622 0.16344  -0.10300 -0.02180 297 LYS A O   
702  C CB  . LYS A 94  ? 0.80976 0.53936 0.49029 0.12657  -0.10053 -0.02987 297 LYS A CB  
703  C CG  . LYS A 94  ? 0.83768 0.60091 0.54788 0.12430  -0.10581 -0.03593 297 LYS A CG  
704  C CD  . LYS A 94  ? 0.89371 0.68502 0.63010 0.13711  -0.12487 -0.05613 297 LYS A CD  
705  C CE  . LYS A 94  ? 0.87143 0.71063 0.65929 0.12006  -0.11895 -0.06143 297 LYS A CE  
706  N NZ  . LYS A 94  ? 0.94060 0.79979 0.75141 0.12864  -0.13120 -0.07991 297 LYS A NZ  
707  N N   . LYS A 95  ? 0.86974 0.49671 0.46371 0.12736  -0.07390 -0.00885 298 LYS A N   
708  C CA  . LYS A 95  ? 0.92058 0.50124 0.47252 0.13965  -0.07353 -0.00799 298 LYS A CA  
709  C C   . LYS A 95  ? 1.03992 0.55881 0.53665 0.14386  -0.05750 0.00292  298 LYS A C   
710  O O   . LYS A 95  ? 1.08527 0.55562 0.52935 0.16641  -0.06562 0.00147  298 LYS A O   
711  C CB  . LYS A 95  ? 0.86941 0.46440 0.44494 0.12469  -0.06403 -0.00668 298 LYS A CB  
712  C CG  . LYS A 95  ? 0.90810 0.54950 0.52360 0.12601  -0.08032 -0.01853 298 LYS A CG  
713  C CD  . LYS A 95  ? 0.92152 0.57172 0.55425 0.11328  -0.07141 -0.01706 298 LYS A CD  
714  C CE  . LYS A 95  ? 0.97650 0.67103 0.64752 0.11373  -0.08516 -0.02864 298 LYS A CE  
715  N NZ  . LYS A 95  ? 0.90601 0.64855 0.61992 0.10197  -0.08554 -0.03132 298 LYS A NZ  
716  N N   . THR A 96  ? 0.96245 0.47986 0.46870 0.12335  -0.03435 0.01273  299 THR A N   
717  C CA  . THR A 96  ? 0.98018 0.43779 0.43738 0.12350  -0.01321 0.02247  299 THR A CA  
718  C C   . THR A 96  ? 0.98776 0.42801 0.41927 0.13329  -0.01567 0.02515  299 THR A C   
719  O O   . THR A 96  ? 1.05288 0.43459 0.43227 0.13884  -0.00017 0.03244  299 THR A O   
720  C CB  . THR A 96  ? 0.92548 0.38829 0.40797 0.09648  0.01471  0.02860  299 THR A CB  
721  O OG1 . THR A 96  ? 0.89161 0.39655 0.41419 0.08231  0.01687  0.02933  299 THR A OG1 
722  C CG2 . THR A 96  ? 0.97197 0.46092 0.48874 0.08529  0.01574  0.02443  299 THR A CG2 
723  N N   . GLY A 97  ? 0.96966 0.45687 0.43554 0.13470  -0.03246 0.01937  300 GLY A N   
724  C CA  . GLY A 97  ? 0.93872 0.41368 0.38497 0.14292  -0.03504 0.02119  300 GLY A CA  
725  C C   . GLY A 97  ? 1.02676 0.49721 0.47961 0.12271  -0.01001 0.03106  300 GLY A C   
726  O O   . GLY A 97  ? 0.98641 0.44780 0.42441 0.12803  -0.01070 0.03312  300 GLY A O   
727  N N   . GLN A 98  ? 0.91381 0.39146 0.39056 0.10037  0.01124  0.03536  301 GLN A N   
728  C CA  . GLN A 98  ? 0.91101 0.38848 0.40156 0.08028  0.03507  0.04129  301 GLN A CA  
729  C C   . GLN A 98  ? 0.82951 0.37196 0.38005 0.06600  0.02783  0.03824  301 GLN A C   
730  O O   . GLN A 98  ? 0.75592 0.34296 0.34274 0.06508  0.01179  0.03246  301 GLN A O   
731  C CB  . GLN A 98  ? 0.96509 0.42158 0.45838 0.06341  0.06087  0.04345  301 GLN A CB  
732  C CG  . GLN A 98  ? 0.99287 0.37783 0.42332 0.07540  0.07341  0.04733  301 GLN A CG  
733  C CD  . GLN A 98  ? 1.21886 0.56158 0.60774 0.07914  0.09094  0.04968  301 GLN A CD  
734  O OE1 . GLN A 98  ? 1.18672 0.50555 0.56896 0.06597  0.11969  0.04911  301 GLN A OE1 
735  N NE2 . GLN A 98  ? 1.12671 0.46960 0.49539 0.09652  0.07344  0.04818  301 GLN A NE2 
736  N N   . TYR A 99  ? 0.78674 0.33106 0.34476 0.05536  0.04077  0.04194  302 TYR A N   
737  C CA  . TYR A 99  ? 0.74879 0.34825 0.36014 0.04065  0.03738  0.03964  302 TYR A CA  
738  C C   . TYR A 99  ? 0.75765 0.37992 0.40742 0.02170  0.04889  0.03681  302 TYR A C   
739  O O   . TYR A 99  ? 0.69120 0.28433 0.33146 0.01285  0.06960  0.03740  302 TYR A O   
740  C CB  . TYR A 99  ? 0.80510 0.39840 0.41284 0.03538  0.04774  0.04348  302 TYR A CB  
741  C CG  . TYR A 99  ? 0.92017 0.51008 0.50673 0.05229  0.03158  0.04391  302 TYR A CG  
742  C CD1 . TYR A 99  ? 0.84448 0.47930 0.46084 0.05740  0.00967  0.03846  302 TYR A CD1 
743  C CD2 . TYR A 99  ? 1.00440 0.54440 0.54095 0.06315  0.03953  0.04860  302 TYR A CD2 
744  C CE1 . TYR A 99  ? 0.99034 0.62413 0.59224 0.07276  -0.00517 0.03603  302 TYR A CE1 
745  C CE2 . TYR A 99  ? 1.04566 0.58255 0.56302 0.08028  0.02304  0.04721  302 TYR A CE2 
746  C CZ  . TYR A 99  ? 1.09949 0.68538 0.65235 0.08484  0.00015  0.04013  302 TYR A CZ  
747  O OH  . TYR A 99  ? 1.20938 0.79383 0.74753 0.10186  -0.01631 0.03607  302 TYR A OH  
748  N N   . ILE A 100 ? 0.62409 0.29696 0.31702 0.01580  0.03618  0.03251  303 ILE A N   
749  C CA  . ILE A 100 ? 0.60081 0.29697 0.32907 0.00141  0.04241  0.02801  303 ILE A CA  
750  C C   . ILE A 100 ? 0.61098 0.31332 0.36165 -0.01430 0.05872  0.02645  303 ILE A C   
751  O O   . ILE A 100 ? 0.55582 0.26717 0.31079 -0.01569 0.05834  0.02857  303 ILE A O   
752  C CB  . ILE A 100 ? 0.63439 0.37613 0.39367 0.00263  0.02379  0.02403  303 ILE A CB  
753  C CG1 . ILE A 100 ? 0.70058 0.43490 0.44338 0.01556  0.01152  0.02226  303 ILE A CG1 
754  C CG2 . ILE A 100 ? 0.58545 0.35503 0.38200 -0.01088 0.02762  0.01886  303 ILE A CG2 
755  C CD1 . ILE A 100 ? 0.64804 0.41297 0.40400 0.02365  -0.00697 0.01890  303 ILE A CD1 
756  N N   . LYS A 101 ? 0.58578 0.28366 0.35293 -0.02598 0.07311  0.02095  304 LYS A N   
757  C CA  . LYS A 101 ? 0.60355 0.30413 0.39429 -0.04075 0.09046  0.01562  304 LYS A CA  
758  C C   . LYS A 101 ? 0.60142 0.35148 0.43804 -0.04739 0.07886  0.00861  304 LYS A C   
759  O O   . LYS A 101 ? 0.60173 0.37850 0.45299 -0.04367 0.06294  0.00658  304 LYS A O   
760  C CB  . LYS A 101 ? 0.69886 0.37201 0.49086 -0.05060 0.11260  0.00928  304 LYS A CB  
761  C CG  . LYS A 101 ? 0.82063 0.43628 0.55989 -0.04308 0.12624  0.01662  304 LYS A CG  
762  C CD  . LYS A 101 ? 0.79746 0.38774 0.49890 -0.03387 0.12701  0.02592  304 LYS A CD  
763  C CE  . LYS A 101 ? 0.87222 0.42463 0.56039 -0.04427 0.15684  0.02520  304 LYS A CE  
764  N NZ  . LYS A 101 ? 0.91069 0.42668 0.54941 -0.03197 0.15823  0.03517  304 LYS A NZ  
765  N N   . GLY A 102 ? 0.60649 0.36569 0.46307 -0.05633 0.08730  0.00444  305 GLY A N   
766  C CA  . GLY A 102 ? 0.56420 0.36439 0.46140 -0.06154 0.07735  -0.00402 305 GLY A CA  
767  C C   . GLY A 102 ? 0.57233 0.38176 0.50306 -0.07119 0.08496  -0.01876 305 GLY A C   
768  O O   . GLY A 102 ? 0.59573 0.38286 0.52080 -0.07471 0.09759  -0.02207 305 GLY A O   
769  N N   . ALA A 103 ? 0.60263 0.44479 0.56917 -0.07465 0.07661  -0.02924 306 ALA A N   
770  C CA  . ALA A 103 ? 0.58292 0.44175 0.58610 -0.08029 0.07677  -0.04658 306 ALA A CA  
771  C C   . ALA A 103 ? 0.62979 0.46669 0.64749 -0.09306 0.10270  -0.05810 306 ALA A C   
772  O O   . ALA A 103 ? 0.62138 0.45902 0.65833 -0.09720 0.10731  -0.06997 306 ALA A O   
773  C CB  . ALA A 103 ? 0.61543 0.50920 0.65033 -0.07891 0.06181  -0.05726 306 ALA A CB  
774  N N   . ASP A 104 ? 0.62867 0.44459 0.63804 -0.09989 0.12147  -0.05587 307 ASP A N   
775  C CA  . ASP A 104 ? 0.67074 0.46272 0.69468 -0.11367 0.15044  -0.06831 307 ASP A CA  
776  C C   . ASP A 104 ? 0.75755 0.50453 0.74327 -0.11379 0.16768  -0.05927 307 ASP A C   
777  O O   . ASP A 104 ? 0.84751 0.56769 0.84048 -0.12573 0.19534  -0.06896 307 ASP A O   
778  C CB  . ASP A 104 ? 0.67262 0.45482 0.70141 -0.12203 0.16795  -0.07086 307 ASP A CB  
779  C CG  . ASP A 104 ? 0.76235 0.51136 0.73739 -0.11537 0.17279  -0.04944 307 ASP A CG  
780  O OD1 . ASP A 104 ? 0.72970 0.45678 0.66251 -0.10501 0.16655  -0.03428 307 ASP A OD1 
781  O OD2 . ASP A 104 ? 0.84595 0.59143 0.82217 -0.11960 0.18188  -0.04939 307 ASP A OD2 
782  N N   . GLY A 105 ? 0.74945 0.48600 0.69533 -0.10070 0.15298  -0.04253 308 GLY A N   
783  C CA  . GLY A 105 ? 0.77989 0.47067 0.68375 -0.09760 0.16648  -0.03363 308 GLY A CA  
784  C C   . GLY A 105 ? 0.77704 0.41750 0.63669 -0.09782 0.18866  -0.02361 308 GLY A C   
785  O O   . GLY A 105 ? 0.81794 0.41227 0.63590 -0.09377 0.20149  -0.01647 308 GLY A O   
786  N N   . LYS A 106 ? 0.76782 0.41243 0.63156 -0.10119 0.19347  -0.02285 309 LYS A N   
787  C CA  . LYS A 106 ? 0.74618 0.34088 0.56530 -0.10062 0.21500  -0.01366 309 LYS A CA  
788  C C   . LYS A 106 ? 0.77369 0.37294 0.56442 -0.08714 0.19643  0.00023  309 LYS A C   
789  O O   . LYS A 106 ? 0.77412 0.33359 0.51044 -0.07435 0.19643  0.01296  309 LYS A O   
790  C CB  . LYS A 106 ? 0.78410 0.36999 0.63198 -0.11904 0.24546  -0.02756 309 LYS A CB  
791  C CG  . LYS A 106 ? 0.84204 0.43168 0.72288 -0.12967 0.26295  -0.04478 309 LYS A CG  
792  C CD  . LYS A 106 ? 0.78902 0.37507 0.68764 -0.13871 0.29194  -0.05863 309 LYS A CD  
793  C CE  . LYS A 106 ? 0.84983 0.44578 0.78671 -0.14841 0.30743  -0.07733 309 LYS A CE  
794  N NZ  . LYS A 106 ? 0.84755 0.42951 0.79197 -0.15590 0.34099  -0.09021 309 LYS A NZ  
795  N N   . ALA A 107 ? 0.75724 0.40255 0.58217 -0.08830 0.17968  -0.00289 310 ALA A N   
796  C CA  . ALA A 107 ? 0.68445 0.33616 0.48629 -0.07615 0.16227  0.00892  310 ALA A CA  
797  C C   . ALA A 107 ? 0.75811 0.42617 0.54650 -0.06106 0.13472  0.01654  310 ALA A C   
798  O O   . ALA A 107 ? 0.71733 0.40998 0.52892 -0.06178 0.12385  0.01144  310 ALA A O   
799  C CB  . ALA A 107 ? 0.65577 0.34870 0.49747 -0.08255 0.15481  0.00283  310 ALA A CB  
800  N N   . ASP A 108 ? 0.70292 0.35682 0.45457 -0.04697 0.12374  0.02714  311 ASP A N   
801  C CA  . ASP A 108 ? 0.74518 0.41979 0.49101 -0.03315 0.09751  0.03142  311 ASP A CA  
802  C C   . ASP A 108 ? 0.63907 0.36770 0.42828 -0.03707 0.08047  0.02735  311 ASP A C   
803  O O   . ASP A 108 ? 0.61406 0.35974 0.42238 -0.04332 0.08231  0.02567  311 ASP A O   
804  C CB  . ASP A 108 ? 0.73568 0.38771 0.43985 -0.01691 0.08841  0.03962  311 ASP A CB  
805  C CG  . ASP A 108 ? 0.81520 0.40528 0.46507 -0.00926 0.10445  0.04462  311 ASP A CG  
806  O OD1 . ASP A 108 ? 0.89427 0.45686 0.53376 -0.01407 0.12005  0.04302  311 ASP A OD1 
807  O OD2 . ASP A 108 ? 0.90775 0.47405 0.52249 0.00277  0.10127  0.04987  311 ASP A OD2 
808  N N   . LEU A 109 ? 0.65457 0.40700 0.45591 -0.03251 0.06429  0.02584  312 LEU A N   
809  C CA  . LEU A 109 ? 0.58319 0.37908 0.41572 -0.03374 0.04867  0.02327  312 LEU A CA  
810  C C   . LEU A 109 ? 0.59099 0.39492 0.41485 -0.02673 0.03905  0.02857  312 LEU A C   
811  O O   . LEU A 109 ? 0.62154 0.41400 0.42140 -0.01498 0.03076  0.03233  312 LEU A O   
812  C CB  . LEU A 109 ? 0.53822 0.35061 0.37765 -0.02895 0.03556  0.02133  312 LEU A CB  
813  C CG  . LEU A 109 ? 0.55114 0.40165 0.41856 -0.03064 0.02284  0.01806  312 LEU A CG  
814  C CD1 . LEU A 109 ? 0.59274 0.45715 0.48858 -0.04074 0.02824  0.01019  312 LEU A CD1 
815  C CD2 . LEU A 109 ? 0.55007 0.41064 0.41764 -0.02490 0.01215  0.01683  312 LEU A CD2 
816  N N   . THR A 110 ? 0.63394 0.45767 0.47849 -0.03307 0.03937  0.02720  313 THR A N   
817  C CA  . THR A 110 ? 0.62180 0.45320 0.46091 -0.02795 0.03215  0.03146  313 THR A CA  
818  C C   . THR A 110 ? 0.58330 0.45012 0.45094 -0.03163 0.02265  0.02897  313 THR A C   
819  O O   . THR A 110 ? 0.63041 0.50905 0.51970 -0.03991 0.02679  0.02416  313 THR A O   
820  C CB  . THR A 110 ? 0.61936 0.42811 0.44492 -0.03092 0.04565  0.03381  313 THR A CB  
821  O OG1 . THR A 110 ? 0.66374 0.43188 0.45396 -0.02542 0.05535  0.03697  313 THR A OG1 
822  C CG2 . THR A 110 ? 0.67489 0.49241 0.49576 -0.02514 0.03729  0.03751  313 THR A CG2 
823  N N   . VAL A 111 ? 0.55091 0.43268 0.41822 -0.02489 0.01045  0.03073  314 VAL A N   
824  C CA  . VAL A 111 ? 0.50299 0.41138 0.38995 -0.02726 0.00338  0.02945  314 VAL A CA  
825  C C   . VAL A 111 ? 0.43819 0.35001 0.32435 -0.02657 0.00289  0.03229  314 VAL A C   
826  O O   . VAL A 111 ? 0.49381 0.39931 0.36696 -0.01949 -0.00068 0.03422  314 VAL A O   
827  C CB  . VAL A 111 ? 0.51332 0.43450 0.40248 -0.02232 -0.00566 0.02830  314 VAL A CB  
828  C CG1 . VAL A 111 ? 0.40547 0.34611 0.30760 -0.02426 -0.00966 0.02800  314 VAL A CG1 
829  C CG2 . VAL A 111 ? 0.47162 0.39127 0.36298 -0.02325 -0.00567 0.02523  314 VAL A CG2 
830  N N   . ASN A 112 ? 0.46399 0.38634 0.36499 -0.03279 0.00509  0.03098  315 ASN A N   
831  C CA  . ASN A 112 ? 0.40589 0.33278 0.30834 -0.03304 0.00490  0.03333  315 ASN A CA  
832  C C   . ASN A 112 ? 0.46488 0.40919 0.37357 -0.03016 -0.00345 0.03405  315 ASN A C   
833  O O   . ASN A 112 ? 0.36560 0.32134 0.28391 -0.03200 -0.00659 0.03211  315 ASN A O   
834  C CB  . ASN A 112 ? 0.34041 0.27161 0.25798 -0.04051 0.01043  0.02978  315 ASN A CB  
835  C CG  . ASN A 112 ? 0.57808 0.49020 0.49230 -0.04554 0.02337  0.02732  315 ASN A CG  
836  O OD1 . ASN A 112 ? 0.62856 0.51851 0.52109 -0.04247 0.02960  0.03147  315 ASN A OD1 
837  N ND2 . ASN A 112 ? 0.65874 0.57722 0.59369 -0.05257 0.02799  0.01907  315 ASN A ND2 
838  N N   . ILE A 113 ? 0.38736 0.33136 0.28951 -0.02504 -0.00639 0.03563  316 ILE A N   
839  C CA  . ILE A 113 ? 0.38119 0.34002 0.29185 -0.02394 -0.01065 0.03485  316 ILE A CA  
840  C C   . ILE A 113 ? 0.42162 0.38410 0.33645 -0.02627 -0.00931 0.03679  316 ILE A C   
841  O O   . ILE A 113 ? 0.44326 0.39633 0.35029 -0.02440 -0.00755 0.03818  316 ILE A O   
842  C CB  . ILE A 113 ? 0.38938 0.34923 0.29723 -0.01674 -0.01526 0.03132  316 ILE A CB  
843  C CG1 . ILE A 113 ? 0.43095 0.38554 0.33350 -0.01343 -0.01713 0.02879  316 ILE A CG1 
844  C CG2 . ILE A 113 ? 0.38595 0.36084 0.30706 -0.01781 -0.01589 0.02817  316 ILE A CG2 
845  C CD1 . ILE A 113 ? 0.40935 0.37275 0.32005 -0.01776 -0.01580 0.02793  316 ILE A CD1 
846  N N   . ILE A 114 ? 0.38934 0.36238 0.31311 -0.02937 -0.00989 0.03692  317 ILE A N   
847  C CA  . ILE A 114 ? 0.37341 0.35091 0.30181 -0.03117 -0.00937 0.03838  317 ILE A CA  
848  C C   . ILE A 114 ? 0.37350 0.35895 0.30636 -0.03090 -0.00981 0.03771  317 ILE A C   
849  O O   . ILE A 114 ? 0.37330 0.35913 0.30515 -0.03221 -0.00937 0.03795  317 ILE A O   
850  C CB  . ILE A 114 ? 0.39082 0.36900 0.32463 -0.03531 -0.00844 0.03791  317 ILE A CB  
851  C CG1 . ILE A 114 ? 0.35283 0.32207 0.28595 -0.03770 -0.00413 0.03613  317 ILE A CG1 
852  C CG2 . ILE A 114 ? 0.41252 0.39479 0.35084 -0.03662 -0.00820 0.03904  317 ILE A CG2 
853  C CD1 . ILE A 114 ? 0.41758 0.39064 0.36337 -0.04201 -0.00315 0.03105  317 ILE A CD1 
854  N N   . GLN A 115 ? 0.33850 0.32797 0.27520 -0.02857 -0.01003 0.03569  318 GLN A N   
855  C CA  . GLN A 115 ? 0.34665 0.34220 0.29040 -0.03016 -0.00683 0.03355  318 GLN A CA  
856  C C   . GLN A 115 ? 0.36545 0.36135 0.30965 -0.03289 -0.00560 0.03690  318 GLN A C   
857  O O   . GLN A 115 ? 0.44686 0.44368 0.39227 -0.03256 -0.00776 0.03835  318 GLN A O   
858  C CB  . GLN A 115 ? 0.30703 0.30952 0.26108 -0.02692 -0.00748 0.02650  318 GLN A CB  
859  C CG  . GLN A 115 ? 0.37011 0.37750 0.33475 -0.03064 0.00007  0.02196  318 GLN A CG  
860  C CD  . GLN A 115 ? 0.38164 0.39943 0.36431 -0.02785 -0.00026 0.01042  318 GLN A CD  
861  O OE1 . GLN A 115 ? 0.38765 0.40881 0.37265 -0.02111 -0.00884 0.00637  318 GLN A OE1 
862  N NE2 . GLN A 115 ? 0.30943 0.33054 0.30453 -0.03228 0.00960  0.00337  318 GLN A NE2 
863  N N   . LYS A 116 ? 0.33313 0.32528 0.27328 -0.03476 -0.00181 0.03803  319 LYS A N   
864  C CA  . LYS A 116 ? 0.39389 0.38321 0.33075 -0.03565 -0.00194 0.04090  319 LYS A CA  
865  C C   . LYS A 116 ? 0.35502 0.34968 0.30102 -0.03707 0.00106  0.03964  319 LYS A C   
866  O O   . LYS A 116 ? 0.30640 0.30607 0.26198 -0.03760 0.00501  0.03484  319 LYS A O   
867  C CB  . LYS A 116 ? 0.36221 0.33921 0.28457 -0.03460 0.00101  0.04233  319 LYS A CB  
868  C CG  . LYS A 116 ? 0.48344 0.45571 0.39710 -0.03132 -0.00554 0.04231  319 LYS A CG  
869  C CD  . LYS A 116 ? 0.54618 0.50157 0.43899 -0.02682 -0.00498 0.04320  319 LYS A CD  
870  C CE  . LYS A 116 ? 0.57859 0.52534 0.46072 -0.02576 -0.00043 0.04261  319 LYS A CE  
871  N NZ  . LYS A 116 ? 0.66598 0.59575 0.52511 -0.01803 -0.00570 0.04220  319 LYS A NZ  
872  N N   . LYS A 117 ? 0.42653 0.42109 0.37191 -0.03737 -0.00126 0.04216  320 LYS A N   
873  C CA  . LYS A 117 ? 0.40938 0.40910 0.36343 -0.03851 0.00063  0.04112  320 LYS A CA  
874  C C   . LYS A 117 ? 0.45411 0.44790 0.40742 -0.04085 0.00967  0.03962  320 LYS A C   
875  O O   . LYS A 117 ? 0.40732 0.38764 0.34623 -0.04082 0.01434  0.04168  320 LYS A O   
876  C CB  . LYS A 117 ? 0.37547 0.37561 0.32842 -0.03833 -0.00382 0.04391  320 LYS A CB  
877  C CG  . LYS A 117 ? 0.48529 0.47512 0.42652 -0.03719 -0.00400 0.04596  320 LYS A CG  
878  C CD  . LYS A 117 ? 0.59589 0.58821 0.53897 -0.03581 -0.01097 0.04573  320 LYS A CD  
879  C CE  . LYS A 117 ? 0.60375 0.59225 0.54411 -0.03504 -0.01063 0.04679  320 LYS A CE  
880  N N   . ASN A 118 ? 0.39587 0.39726 0.36345 -0.04245 0.01305  0.03513  321 ASN A N   
881  C CA  . ASN A 118 ? 0.38484 0.37952 0.35478 -0.04629 0.02470  0.03234  321 ASN A CA  
882  C C   . ASN A 118 ? 0.45512 0.43645 0.40911 -0.04600 0.02554  0.03880  321 ASN A C   
883  O O   . ASN A 118 ? 0.44371 0.43133 0.40119 -0.04464 0.01847  0.04079  321 ASN A O   
884  C CB  . ASN A 118 ? 0.44112 0.45017 0.43540 -0.04755 0.02661  0.02309  321 ASN A CB  
885  C CG  . ASN A 118 ? 0.48656 0.48941 0.48928 -0.05339 0.04220  0.01706  321 ASN A CG  
886  O OD1 . ASN A 118 ? 0.47923 0.46250 0.46435 -0.05632 0.05333  0.02117  321 ASN A OD1 
887  N ND2 . ASN A 118 ? 0.45954 0.47668 0.48817 -0.05453 0.04383  0.00611  321 ASN A ND2 
888  N N   . GLU A 119 ? 0.45779 0.41819 0.39157 -0.04611 0.03395  0.04163  322 GLU A N   
889  C CA  . GLU A 119 ? 0.51376 0.45613 0.42658 -0.04306 0.03366  0.04688  322 GLU A CA  
890  C C   . GLU A 119 ? 0.52304 0.45584 0.43748 -0.04727 0.04666  0.04527  322 GLU A C   
891  O O   . GLU A 119 ? 0.58373 0.50093 0.48074 -0.04411 0.04595  0.04939  322 GLU A O   
892  C CB  . GLU A 119 ? 0.65146 0.56878 0.53276 -0.03768 0.03464  0.05076  322 GLU A CB  
893  C CG  . GLU A 119 ? 0.59725 0.52191 0.47580 -0.03251 0.02063  0.05134  322 GLU A CG  
894  C CD  . GLU A 119 ? 0.77651 0.70967 0.65822 -0.02782 0.00571  0.05152  322 GLU A CD  
895  O OE1 . GLU A 119 ? 0.78208 0.71550 0.66627 -0.02787 0.00491  0.05218  322 GLU A OE1 
896  O OE2 . GLU A 119 ? 0.83985 0.77999 0.72391 -0.02454 -0.00442 0.04964  322 GLU A OE2 
897  N N   . ASN A 120 ? 0.52048 0.46155 0.45634 -0.05386 0.05851  0.03778  323 ASN A N   
898  C CA  . ASN A 120 ? 0.56097 0.49603 0.50565 -0.05931 0.07240  0.03345  323 ASN A CA  
899  C C   . ASN A 120 ? 0.47259 0.43700 0.45574 -0.06245 0.06933  0.02312  323 ASN A C   
900  O O   . ASN A 120 ? 0.43405 0.40419 0.43967 -0.06813 0.08184  0.01182  323 ASN A O   
901  C CB  . ASN A 120 ? 0.50506 0.41449 0.43717 -0.06457 0.09498  0.03072  323 ASN A CB  
902  C CG  . ASN A 120 ? 0.76566 0.63950 0.65201 -0.05854 0.09732  0.04079  323 ASN A CG  
903  O OD1 . ASN A 120 ? 0.81539 0.67735 0.68631 -0.05714 0.10124  0.04183  323 ASN A OD1 
904  N ND2 . ASN A 120 ? 0.82358 0.67929 0.68658 -0.05336 0.09347  0.04738  323 ASN A ND2 
905  N N   . PRO A 121 ? 0.45185 0.43400 0.44331 -0.05811 0.05301  0.02509  324 PRO A N   
906  C CA  . PRO A 121 ? 0.40951 0.41596 0.43144 -0.05780 0.04746  0.01501  324 PRO A CA  
907  C C   . PRO A 121 ? 0.46840 0.47654 0.50706 -0.06208 0.05655  0.00809  324 PRO A C   
908  O O   . PRO A 121 ? 0.47392 0.46683 0.49787 -0.06368 0.06167  0.01459  324 PRO A O   
909  C CB  . PRO A 121 ? 0.42416 0.44012 0.44032 -0.05166 0.03018  0.02139  324 PRO A CB  
910  C CG  . PRO A 121 ? 0.40875 0.40885 0.40169 -0.05116 0.02939  0.03183  324 PRO A CG  
911  C CD  . PRO A 121 ? 0.45620 0.43533 0.42966 -0.05276 0.03965  0.03483  324 PRO A CD  
912  N N   . VAL A 122 ? 0.41652 0.44329 0.48691 -0.06290 0.05751  -0.00674 325 VAL A N   
913  C CA  . VAL A 122 ? 0.45537 0.48955 0.54908 -0.06613 0.06353  -0.01671 325 VAL A CA  
914  C C   . VAL A 122 ? 0.45730 0.50876 0.55759 -0.05828 0.04469  -0.01679 325 VAL A C   
915  O O   . VAL A 122 ? 0.41723 0.48434 0.52899 -0.05120 0.03207  -0.02428 325 VAL A O   
916  C CB  . VAL A 122 ? 0.40839 0.45381 0.53749 -0.07104 0.07571  -0.03692 325 VAL A CB  
917  C CG1 . VAL A 122 ? 0.39676 0.44933 0.55279 -0.07530 0.08365  -0.04898 325 VAL A CG1 
918  C CG2 . VAL A 122 ? 0.46164 0.48652 0.58042 -0.07909 0.09650  -0.03624 325 VAL A CG2 
919  N N   . VAL A 123 ? 0.37679 0.42244 0.46660 -0.05850 0.04287  -0.00864 326 VAL A N   
920  C CA  . VAL A 123 ? 0.40743 0.46451 0.49721 -0.05161 0.02706  -0.00632 326 VAL A CA  
921  C C   . VAL A 123 ? 0.36529 0.43472 0.48144 -0.05188 0.02817  -0.01868 326 VAL A C   
922  O O   . VAL A 123 ? 0.39168 0.45448 0.51729 -0.05927 0.04266  -0.02261 326 VAL A O   
923  C CB  . VAL A 123 ? 0.39487 0.43927 0.45780 -0.05120 0.02311  0.00936  326 VAL A CB  
924  C CG1 . VAL A 123 ? 0.37789 0.43229 0.44157 -0.04558 0.01028  0.01094  326 VAL A CG1 
925  C CG2 . VAL A 123 ? 0.44441 0.47872 0.48526 -0.05012 0.02077  0.01858  326 VAL A CG2 
926  N N   . HIS A 124 ? 0.32867 0.41342 0.45499 -0.04319 0.01355  -0.02562 327 HIS A N   
927  C CA  . HIS A 124 ? 0.33131 0.42807 0.47972 -0.04117 0.01082  -0.03670 327 HIS A CA  
928  C C   . HIS A 124 ? 0.29308 0.39073 0.42535 -0.03330 -0.00342 -0.02881 327 HIS A C   
929  O O   . HIS A 124 ? 0.31292 0.40350 0.42116 -0.02907 -0.01072 -0.01799 327 HIS A O   
930  C CB  . HIS A 124 ? 0.29128 0.40650 0.47389 -0.03633 0.00722  -0.05971 327 HIS A CB  
931  C CG  . HIS A 124 ? 0.31289 0.43443 0.48909 -0.02311 -0.01031 -0.06441 327 HIS A CG  
932  N ND1 . HIS A 124 ? 0.38465 0.50110 0.54947 -0.02208 -0.01075 -0.06119 327 HIS A ND1 
933  C CD2 . HIS A 124 ? 0.32180 0.45102 0.49845 -0.00906 -0.02792 -0.07283 327 HIS A CD2 
934  C CE1 . HIS A 124 ? 0.41257 0.53231 0.57026 -0.00818 -0.02755 -0.06682 327 HIS A CE1 
935  N NE2 . HIS A 124 ? 0.38658 0.51241 0.54909 0.00060  -0.03830 -0.07383 327 HIS A NE2 
936  N N   . TYR A 125 ? 0.21896 0.32404 0.36500 -0.03208 -0.00549 -0.03490 328 TYR A N   
937  C CA  . TYR A 125 ? 0.28890 0.39174 0.41860 -0.02705 -0.01485 -0.02621 328 TYR A CA  
938  C C   . TYR A 125 ? 0.28287 0.39876 0.42850 -0.01695 -0.02630 -0.04045 328 TYR A C   
939  O O   . TYR A 125 ? 0.24494 0.37365 0.42093 -0.01673 -0.02471 -0.05774 328 TYR A O   
940  C CB  . TYR A 125 ? 0.23959 0.33379 0.36268 -0.03551 -0.00608 -0.01584 328 TYR A CB  
941  C CG  . TYR A 125 ? 0.32961 0.40803 0.43307 -0.04231 0.00257  -0.00318 328 TYR A CG  
942  C CD1 . TYR A 125 ? 0.27557 0.34584 0.38402 -0.04944 0.01641  -0.00571 328 TYR A CD1 
943  C CD2 . TYR A 125 ? 0.27954 0.34984 0.35951 -0.04100 -0.00259 0.00960  328 TYR A CD2 
944  C CE1 . TYR A 125 ? 0.30320 0.35539 0.38843 -0.05314 0.02290  0.00552  328 TYR A CE1 
945  C CE2 . TYR A 125 ? 0.31482 0.37131 0.37759 -0.04486 0.00256  0.01862  328 TYR A CE2 
946  C CZ  . TYR A 125 ? 0.31960 0.36612 0.38266 -0.04991 0.01426  0.01711  328 TYR A CZ  
947  O OH  . TYR A 125 ? 0.35331 0.38294 0.39447 -0.05128 0.01780  0.02573  328 TYR A OH  
948  N N   . LYS A 126 ? 0.29359 0.40481 0.41853 -0.00816 -0.03726 -0.03456 329 LYS A N   
949  C CA  . LYS A 126 ? 0.24866 0.36708 0.38007 0.00314  -0.04902 -0.04557 329 LYS A CA  
950  C C   . LYS A 126 ? 0.24564 0.35653 0.35902 0.00216  -0.04933 -0.03346 329 LYS A C   
951  O O   . LYS A 126 ? 0.26620 0.36385 0.35284 0.00135  -0.04818 -0.01974 329 LYS A O   
952  C CB  . LYS A 126 ? 0.29221 0.40688 0.40989 0.01955  -0.06363 -0.05354 329 LYS A CB  
953  C CG  . LYS A 126 ? 0.41170 0.53787 0.55320 0.02378  -0.06715 -0.07120 329 LYS A CG  
954  C CD  . LYS A 126 ? 0.42949 0.54538 0.54776 0.04013  -0.08113 -0.07509 329 LYS A CD  
955  C CE  . LYS A 126 ? 0.50151 0.61577 0.61247 0.06044  -0.09958 -0.08886 329 LYS A CE  
956  N NZ  . LYS A 126 ? 0.59005 0.69319 0.68105 0.07834  -0.11392 -0.09705 329 LYS A NZ  
957  N N   . TRP A 127 ? 0.19368 0.31356 0.32433 0.00166  -0.04993 -0.04001 330 TRP A N   
958  C CA  . TRP A 127 ? 0.22535 0.34038 0.34344 0.00064  -0.05021 -0.03083 330 TRP A CA  
959  C C   . TRP A 127 ? 0.23808 0.35479 0.35188 0.01490  -0.06311 -0.04008 330 TRP A C   
960  O O   . TRP A 127 ? 0.19638 0.32319 0.32765 0.02440  -0.07200 -0.05720 330 TRP A O   
961  C CB  . TRP A 127 ? 0.21796 0.33812 0.35446 -0.01084 -0.04030 -0.02945 330 TRP A CB  
962  C CG  . TRP A 127 ? 0.25487 0.36817 0.39041 -0.02198 -0.02810 -0.02193 330 TRP A CG  
963  C CD1 . TRP A 127 ? 0.20582 0.32195 0.36065 -0.02797 -0.01880 -0.02994 330 TRP A CD1 
964  C CD2 . TRP A 127 ? 0.23028 0.33099 0.34333 -0.02726 -0.02390 -0.00661 330 TRP A CD2 
965  N NE1 . TRP A 127 ? 0.22381 0.32666 0.36430 -0.03597 -0.00893 -0.01868 330 TRP A NE1 
966  C CE2 . TRP A 127 ? 0.24117 0.33561 0.35682 -0.03484 -0.01349 -0.00493 330 TRP A CE2 
967  C CE3 . TRP A 127 ? 0.21481 0.30865 0.30736 -0.02617 -0.02732 0.00397  330 TRP A CE3 
968  C CZ2 . TRP A 127 ? 0.21716 0.29849 0.31314 -0.03920 -0.00933 0.00708  330 TRP A CZ2 
969  C CZ3 . TRP A 127 ? 0.24407 0.32849 0.32337 -0.03168 -0.02283 0.01391  330 TRP A CZ3 
970  C CH2 . TRP A 127 ? 0.27615 0.35431 0.35605 -0.03710 -0.01532 0.01546  330 TRP A CH2 
971  N N   . VAL A 128 ? 0.22204 0.32765 0.31196 0.01723  -0.06419 -0.03010 331 VAL A N   
972  C CA  . VAL A 128 ? 0.21348 0.31640 0.29423 0.03071  -0.07483 -0.03732 331 VAL A CA  
973  C C   . VAL A 128 ? 0.25279 0.37492 0.36769 0.03146  -0.07886 -0.05225 331 VAL A C   
974  O O   . VAL A 128 ? 0.22849 0.36000 0.36520 0.01862  -0.06947 -0.05033 331 VAL A O   
975  C CB  . VAL A 128 ? 0.24604 0.33478 0.30109 0.02852  -0.07010 -0.02401 331 VAL A CB  
976  C CG1 . VAL A 128 ? 0.23013 0.31615 0.27747 0.04082  -0.07905 -0.03118 331 VAL A CG1 
977  C CG2 . VAL A 128 ? 0.28599 0.35341 0.30771 0.03005  -0.06581 -0.01358 331 VAL A CG2 
978  N N   . ASP A 129 ? 0.24653 0.37258 0.36519 0.04751  -0.09295 -0.06843 332 ASP A N   
979  C CA  . ASP A 129 ? 0.22607 0.37247 0.38229 0.04934  -0.09769 -0.08687 332 ASP A CA  
980  C C   . ASP A 129 ? 0.27858 0.42810 0.44037 0.04151  -0.09201 -0.08050 332 ASP A C   
981  O O   . ASP A 129 ? 0.27109 0.40770 0.40480 0.04528  -0.09369 -0.06986 332 ASP A O   
982  C CB  . ASP A 129 ? 0.27172 0.41947 0.42570 0.07183  -0.11752 -0.10642 332 ASP A CB  
983  C CG  . ASP A 129 ? 0.42862 0.60033 0.62733 0.07487  -0.12381 -0.12996 332 ASP A CG  
984  O OD1 . ASP A 129 ? 0.34286 0.53076 0.57928 0.06836  -0.11887 -0.14458 332 ASP A OD1 
985  O OD2 . ASP A 129 ? 0.38575 0.55760 0.58086 0.08307  -0.13158 -0.13425 332 ASP A OD2 
986  N N   . GLY A 130 ? 0.27500 0.43960 0.47246 0.02993  -0.08342 -0.08720 333 GLY A N   
987  C CA  . GLY A 130 ? 0.18528 0.35401 0.39205 0.02426  -0.07965 -0.08487 333 GLY A CA  
988  C C   . GLY A 130 ? 0.25127 0.41081 0.44701 0.00904  -0.06578 -0.06560 333 GLY A C   
989  O O   . GLY A 130 ? 0.23724 0.39943 0.44106 0.00422  -0.06251 -0.06393 333 GLY A O   
990  N N   . ILE A 131 ? 0.16705 0.31566 0.34477 0.00244  -0.05869 -0.05223 334 ILE A N   
991  C CA  . ILE A 131 ? 0.17425 0.31369 0.34114 -0.00928 -0.04840 -0.03653 334 ILE A CA  
992  C C   . ILE A 131 ? 0.21063 0.34748 0.39080 -0.02068 -0.03546 -0.03593 334 ILE A C   
993  O O   . ILE A 131 ? 0.22619 0.35141 0.39217 -0.02802 -0.02829 -0.02343 334 ILE A O   
994  C CB  . ILE A 131 ? 0.25637 0.38318 0.39243 -0.00866 -0.04897 -0.02230 334 ILE A CB  
995  C CG1 . ILE A 131 ? 0.22697 0.34911 0.35587 -0.00868 -0.04727 -0.02092 334 ILE A CG1 
996  C CG2 . ILE A 131 ? 0.21261 0.33535 0.33067 0.00166  -0.05735 -0.02227 334 ILE A CG2 
997  C CD1 . ILE A 131 ? 0.19582 0.30589 0.30140 -0.01286 -0.04329 -0.00709 334 ILE A CD1 
998  N N   . GLY A 132 ? 0.17609 0.32169 0.38234 -0.02154 -0.03198 -0.05060 335 GLY A N   
999  C CA  . GLY A 132 ? 0.25028 0.38886 0.46636 -0.03274 -0.01622 -0.05073 335 GLY A CA  
1000 C C   . GLY A 132 ? 0.28110 0.40849 0.47633 -0.03524 -0.01266 -0.04004 335 GLY A C   
1001 O O   . GLY A 132 ? 0.21966 0.35006 0.40500 -0.02813 -0.02174 -0.03967 335 GLY A O   
1002 N N   . ALA A 133 ? 0.24657 0.35788 0.43214 -0.04456 0.00084  -0.03138 336 ALA A N   
1003 C CA  . ALA A 133 ? 0.27574 0.37530 0.44189 -0.04691 0.00480  -0.02212 336 ALA A CA  
1004 C C   . ALA A 133 ? 0.27872 0.35583 0.42389 -0.05326 0.01517  -0.01005 336 ALA A C   
1005 O O   . ALA A 133 ? 0.27175 0.34037 0.42224 -0.05773 0.02438  -0.01208 336 ALA A O   
1006 C CB  . ALA A 133 ? 0.25834 0.36291 0.44343 -0.04924 0.01198  -0.03416 336 ALA A CB  
1007 N N   . PRO A 134 ? 0.28165 0.34679 0.40144 -0.05257 0.01342  0.00157  337 PRO A N   
1008 C CA  . PRO A 134 ? 0.30210 0.34374 0.39747 -0.05467 0.01916  0.01176  337 PRO A CA  
1009 C C   . PRO A 134 ? 0.31055 0.33117 0.40277 -0.06122 0.03779  0.00966  337 PRO A C   
1010 O O   . PRO A 134 ? 0.35419 0.37583 0.45560 -0.06479 0.04627  0.00405  337 PRO A O   
1011 C CB  . PRO A 134 ? 0.33036 0.36805 0.40457 -0.05104 0.01116  0.02066  337 PRO A CB  
1012 C CG  . PRO A 134 ? 0.30652 0.35779 0.39215 -0.05057 0.00948  0.01569  337 PRO A CG  
1013 C CD  . PRO A 134 ? 0.27783 0.34868 0.38879 -0.04858 0.00530  0.00490  337 PRO A CD  
1014 N N   . THR A 135 ? 0.39121 0.39034 0.46912 -0.06260 0.04530  0.01355  338 THR A N   
1015 C CA  . THR A 135 ? 0.39061 0.35760 0.45114 -0.06766 0.06512  0.01507  338 THR A CA  
1016 C C   . THR A 135 ? 0.40483 0.34822 0.42726 -0.06259 0.06230  0.02645  338 THR A C   
1017 O O   . THR A 135 ? 0.40898 0.36043 0.42053 -0.05550 0.04495  0.03239  338 THR A O   
1018 C CB  . THR A 135 ? 0.42057 0.36693 0.47351 -0.06944 0.07468  0.01540  338 THR A CB  
1019 O OG1 . THR A 135 ? 0.43406 0.37033 0.46020 -0.06092 0.06039  0.02531  338 THR A OG1 
1020 C CG2 . THR A 135 ? 0.37574 0.34759 0.46824 -0.07343 0.07516  0.00303  338 THR A CG2 
1021 N N   . GLU A 136 ? 0.50226 0.41495 0.50457 -0.06612 0.08045  0.02809  339 GLU A N   
1022 C CA  . GLU A 136 ? 0.46204 0.34956 0.42530 -0.05952 0.07715  0.03782  339 GLU A CA  
1023 C C   . GLU A 136 ? 0.47857 0.34941 0.41162 -0.04889 0.06298  0.04553  339 GLU A C   
1024 O O   . GLU A 136 ? 0.54862 0.42045 0.46541 -0.04053 0.04724  0.04998  339 GLU A O   
1025 C CB  . GLU A 136 ? 0.59114 0.44147 0.53222 -0.06447 0.10169  0.03830  339 GLU A CB  
1026 C CG  . GLU A 136 ? 0.67530 0.54343 0.64440 -0.07305 0.11234  0.02983  339 GLU A CG  
1027 C CD  . GLU A 136 ? 0.71526 0.60880 0.68975 -0.06813 0.09364  0.03215  339 GLU A CD  
1028 O OE1 . GLU A 136 ? 0.76051 0.63730 0.70202 -0.06034 0.08492  0.04123  339 GLU A OE1 
1029 O OE2 . GLU A 136 ? 0.71597 0.64471 0.72670 -0.07103 0.08716  0.02391  339 GLU A OE2 
1030 N N   . ASN A 137 ? 0.48493 0.34300 0.41393 -0.04867 0.06713  0.04520  340 ASN A N   
1031 C CA  . ASN A 137 ? 0.50518 0.34837 0.40756 -0.03733 0.05215  0.05035  340 ASN A CA  
1032 C C   . ASN A 137 ? 0.52975 0.41119 0.45515 -0.03311 0.02871  0.04836  340 ASN A C   
1033 O O   . ASN A 137 ? 0.51111 0.38583 0.41821 -0.02272 0.01304  0.05027  340 ASN A O   
1034 C CB  . ASN A 137 ? 0.59100 0.41144 0.48483 -0.03839 0.06280  0.04995  340 ASN A CB  
1035 C CG  . ASN A 137 ? 0.76775 0.53542 0.62287 -0.03942 0.08667  0.05364  340 ASN A CG  
1036 O OD1 . ASN A 137 ? 0.75562 0.49710 0.57865 -0.03487 0.09050  0.05833  340 ASN A OD1 
1037 N ND2 . ASN A 137 ? 0.78831 0.53739 0.64460 -0.04542 0.10432  0.05118  340 ASN A ND2 
1038 N N   . GLN A 138 ? 0.44089 0.35990 0.40475 -0.04004 0.02634  0.04319  341 GLN A N   
1039 C CA  . GLN A 138 ? 0.38214 0.33254 0.36491 -0.03700 0.00829  0.04132  341 GLN A CA  
1040 C C   . GLN A 138 ? 0.37139 0.33381 0.35362 -0.03478 -0.00059 0.04244  341 GLN A C   
1041 O O   . GLN A 138 ? 0.34886 0.33305 0.34424 -0.03283 -0.01283 0.04051  341 GLN A O   
1042 C CB  . GLN A 138 ? 0.33767 0.31679 0.35545 -0.04314 0.00967  0.03510  341 GLN A CB  
1043 C CG  . GLN A 138 ? 0.33628 0.30953 0.35932 -0.04433 0.01412  0.03268  341 GLN A CG  
1044 C CD  . GLN A 138 ? 0.38647 0.38271 0.44356 -0.05043 0.01919  0.02409  341 GLN A CD  
1045 O OE1 . GLN A 138 ? 0.30410 0.32223 0.38010 -0.05184 0.01626  0.01957  341 GLN A OE1 
1046 N NE2 . GLN A 138 ? 0.32648 0.31636 0.39059 -0.05280 0.02603  0.02062  341 GLN A NE2 
1047 N N   . LYS A 139 ? 0.34966 0.29708 0.31702 -0.03548 0.00677  0.04497  342 LYS A N   
1048 C CA  . LYS A 139 ? 0.33755 0.29522 0.30468 -0.03379 -0.00049 0.04570  342 LYS A CA  
1049 C C   . LYS A 139 ? 0.41478 0.35252 0.35340 -0.02397 -0.01032 0.04800  342 LYS A C   
1050 O O   . LYS A 139 ? 0.48880 0.39406 0.39690 -0.01964 -0.00407 0.05139  342 LYS A O   
1051 C CB  . LYS A 139 ? 0.36349 0.31885 0.33350 -0.03966 0.01199  0.04555  342 LYS A CB  
1052 C CG  . LYS A 139 ? 0.36123 0.33786 0.36201 -0.04706 0.01904  0.03950  342 LYS A CG  
1053 C CD  . LYS A 139 ? 0.47595 0.45509 0.48183 -0.05082 0.02655  0.03738  342 LYS A CD  
1054 C CE  . LYS A 139 ? 0.47193 0.46576 0.50673 -0.05689 0.03561  0.02792  342 LYS A CE  
1055 N NZ  . LYS A 139 ? 0.47360 0.46542 0.51179 -0.06036 0.04470  0.02447  342 LYS A NZ  
1056 N N   . ILE A 140 ? 0.37252 0.32766 0.32034 -0.01983 -0.02503 0.04471  343 ILE A N   
1057 C CA  . ILE A 140 ? 0.40698 0.34841 0.33474 -0.00876 -0.03804 0.04240  343 ILE A CA  
1058 C C   . ILE A 140 ? 0.42202 0.37192 0.35249 -0.00847 -0.04202 0.04087  343 ILE A C   
1059 O O   . ILE A 140 ? 0.31567 0.29196 0.27146 -0.01347 -0.04501 0.03742  343 ILE A O   
1060 C CB  . ILE A 140 ? 0.39005 0.34532 0.33095 -0.00389 -0.05181 0.03567  343 ILE A CB  
1061 C CG1 . ILE A 140 ? 0.39661 0.34792 0.33951 -0.00562 -0.04742 0.03720  343 ILE A CG1 
1062 C CG2 . ILE A 140 ? 0.40759 0.34735 0.32845 0.01016  -0.06739 0.02971  343 ILE A CG2 
1063 C CD1 . ILE A 140 ? 0.45420 0.36800 0.36413 -0.00188 -0.03800 0.04284  343 ILE A CD1 
1064 N N   . LYS A 141 ? 0.40951 0.33386 0.31119 -0.00212 -0.04126 0.04329  344 LYS A N   
1065 C CA  . LYS A 141 ? 0.42179 0.35112 0.32306 -0.00011 -0.04641 0.04110  344 LYS A CA  
1066 C C   . LYS A 141 ? 0.44125 0.38492 0.35460 0.00733  -0.06416 0.03093  344 LYS A C   
1067 O O   . LYS A 141 ? 0.40112 0.34186 0.31265 0.01483  -0.07437 0.02546  344 LYS A O   
1068 C CB  . LYS A 141 ? 0.45966 0.35430 0.32300 0.00698  -0.04225 0.04532  344 LYS A CB  
1069 C CG  . LYS A 141 ? 0.58720 0.47057 0.44464 -0.00250 -0.02184 0.05250  344 LYS A CG  
1070 C CD  . LYS A 141 ? 0.65322 0.49258 0.46547 0.00550  -0.01477 0.05685  344 LYS A CD  
1071 C CE  . LYS A 141 ? 0.77267 0.60329 0.58329 -0.00471 0.00639  0.06113  344 LYS A CE  
1072 N NZ  . LYS A 141 ? 0.81826 0.65220 0.64571 -0.01560 0.02276  0.06173  344 LYS A NZ  
1073 N N   A MET A 142 ? 0.43280 0.39147 0.35974 0.00541  -0.06742 0.02678  345 MET A N   
1074 N N   B MET A 142 ? 0.43392 0.39366 0.36211 0.00503  -0.06729 0.02671  345 MET A N   
1075 C CA  A MET A 142 ? 0.45868 0.43732 0.40858 0.00842  -0.08009 0.01431  345 MET A CA  
1076 C CA  B MET A 142 ? 0.45902 0.43810 0.40950 0.00839  -0.08023 0.01412  345 MET A CA  
1077 C C   A MET A 142 ? 0.44867 0.41920 0.38781 0.01815  -0.09083 0.00706  345 MET A C   
1078 C C   B MET A 142 ? 0.44814 0.41893 0.38762 0.01803  -0.09076 0.00707  345 MET A C   
1079 O O   A MET A 142 ? 0.42139 0.38357 0.34813 0.01638  -0.08481 0.01277  345 MET A O   
1080 O O   B MET A 142 ? 0.42037 0.38278 0.34742 0.01614  -0.08455 0.01293  345 MET A O   
1081 C CB  A MET A 142 ? 0.41356 0.42002 0.39597 -0.00456 -0.07194 0.01344  345 MET A CB  
1082 C CB  B MET A 142 ? 0.40113 0.40865 0.38503 -0.00443 -0.07254 0.01267  345 MET A CB  
1083 C CG  A MET A 142 ? 0.39582 0.41208 0.39061 -0.01157 -0.06499 0.01724  345 MET A CG  
1084 C CG  B MET A 142 ? 0.43259 0.45994 0.44454 -0.00404 -0.08063 -0.00155 345 MET A CG  
1085 S SD  A MET A 142 ? 0.39346 0.43071 0.41193 -0.02391 -0.05382 0.01865  345 MET A SD  
1086 S SD  B MET A 142 ? 0.49324 0.54365 0.53509 -0.01866 -0.06725 -0.00177 345 MET A SD  
1087 C CE  A MET A 142 ? 0.41508 0.46652 0.45615 -0.02390 -0.05961 0.00422  345 MET A CE  
1088 C CE  B MET A 142 ? 0.39566 0.43899 0.42296 -0.02441 -0.05543 0.01434  345 MET A CE  
1089 N N   . LYS A 143 ? 0.44871 0.42330 0.39522 0.02895  -0.10756 -0.00742 346 LYS A N   
1090 C CA  . LYS A 143 ? 0.51298 0.48417 0.45565 0.03989  -0.12103 -0.01892 346 LYS A CA  
1091 C C   . LYS A 143 ? 0.56125 0.56173 0.54231 0.02966  -0.11774 -0.02786 346 LYS A C   
1092 O O   . LYS A 143 ? 0.49500 0.51836 0.50786 0.01833  -0.11046 -0.03125 346 LYS A O   
1093 C CB  . LYS A 143 ? 0.57851 0.54247 0.51571 0.05797  -0.14268 -0.03474 346 LYS A CB  
1094 C CG  . LYS A 143 ? 0.64044 0.56276 0.52534 0.07455  -0.14945 -0.02811 346 LYS A CG  
1095 C CD  . LYS A 143 ? 0.72577 0.64092 0.60530 0.09298  -0.17134 -0.04359 346 LYS A CD  
1096 C CE  . LYS A 143 ? 0.79892 0.66543 0.61838 0.11497  -0.18202 -0.04060 346 LYS A CE  
1097 N NZ  . LYS A 143 ? 0.93931 0.79978 0.75096 0.13580  -0.20628 -0.05950 346 LYS A NZ  
1098 N N   . ILE A 144 ? 0.55811 0.55455 0.53346 0.03392  -0.12183 -0.03170 347 ILE A N   
1099 C CA  . ILE A 144 ? 0.52147 0.54148 0.53100 0.02573  -0.11902 -0.04216 347 ILE A CA  
1100 C C   . ILE A 144 ? 0.56786 0.60459 0.60767 0.03342  -0.13456 -0.06651 347 ILE A C   
1101 O O   . ILE A 144 ? 0.58377 0.60871 0.60904 0.05138  -0.15407 -0.07753 347 ILE A O   
1102 C CB  . ILE A 144 ? 0.54267 0.55228 0.53588 0.02819  -0.11854 -0.03863 347 ILE A CB  
1103 C CG1 . ILE A 144 ? 0.47164 0.46504 0.43731 0.02118  -0.10326 -0.01710 347 ILE A CG1 
1104 C CG2 . ILE A 144 ? 0.44183 0.47372 0.46993 0.01906  -0.11394 -0.04940 347 ILE A CG2 
1105 C CD1 . ILE A 144 ? 0.40802 0.38978 0.35580 0.02313  -0.10126 -0.01261 347 ILE A CD1 
1106 N N   . LYS A 145 ? 0.53043 0.59254 0.61142 0.02069  -0.12562 -0.07635 348 LYS A N   
1107 C CA  . LYS A 145 ? 0.58250 0.66465 0.70189 0.02492  -0.13672 -0.10298 348 LYS A CA  
1108 C C   . LYS A 145 ? 0.67968 0.77462 0.82546 0.02193  -0.13603 -0.11833 348 LYS A C   
1109 O O   . LYS A 145 ? 0.61489 0.70771 0.75660 0.01100  -0.12111 -0.10686 348 LYS A O   
1110 C CB  . LYS A 145 ? 0.54883 0.64929 0.69978 0.01194  -0.12446 -0.10728 348 LYS A CB  
1111 C CG  . LYS A 145 ? 0.55177 0.64449 0.68568 0.01496  -0.12658 -0.09710 348 LYS A CG  
1112 C CD  . LYS A 145 ? 0.58382 0.69634 0.75303 0.00313  -0.11563 -0.10566 348 LYS A CD  
1113 C CE  . LYS A 145 ? 0.55506 0.66156 0.70988 0.00624  -0.11843 -0.09679 348 LYS A CE  
1114 N NZ  . LYS A 145 ? 0.56093 0.65270 0.68496 -0.00086 -0.10505 -0.07025 348 LYS A NZ  
1115 N N   . ASN A 146 ? 0.68614 0.79471 0.86075 0.03243  -0.15297 -0.14625 349 ASN A N   
1116 C CA  . ASN A 146 ? 0.81087 0.93748 1.02404 0.02794  -0.15126 -0.16749 349 ASN A CA  
1117 C C   . ASN A 146 ? 0.85145 1.00161 1.11511 0.02455  -0.14939 -0.19390 349 ASN A C   
1118 O O   . ASN A 146 ? 0.81885 0.96639 1.08229 0.04151  -0.16380 -0.20630 349 ASN A O   
1119 C CB  . ASN A 146 ? 0.76815 0.88590 0.96657 0.04702  -0.17352 -0.17863 349 ASN A CB  
1120 C CG  . ASN A 146 ? 0.84867 0.94595 1.00767 0.04502  -0.16582 -0.15493 349 ASN A CG  
1121 O OD1 . ASN A 146 ? 0.80473 0.90112 0.96038 0.02749  -0.14322 -0.13612 349 ASN A OD1 
1122 N ND2 . ASN A 146 ? 0.91353 0.99260 1.04107 0.06423  -0.18508 -0.15690 349 ASN A ND2 
1123 N N   . ASN A 147 ? 0.98525 1.14928 1.28256 0.00409  -0.12479 -0.19764 350 ASN A N   
1124 C CA  . ASN A 147 ? 0.94504 1.12283 1.28170 -0.00134 -0.11087 -0.21601 350 ASN A CA  
1125 C C   . ASN A 147 ? 0.87472 1.05224 1.20614 0.00667  -0.11939 -0.21625 350 ASN A C   
1126 O O   . ASN A 147 ? 0.96243 1.14709 1.31550 0.01755  -0.12560 -0.23655 350 ASN A O   
1127 C CB  . ASN A 147 ? 0.86689 1.05381 1.23401 0.00883  -0.11518 -0.24274 350 ASN A CB  
1128 N N   . GLY A 148 ? 0.77402 0.94330 1.07739 0.00180  -0.11981 -0.19423 351 GLY A N   
1129 C CA  . GLY A 148 ? 0.77412 0.94180 1.06988 0.00743  -0.12604 -0.19140 351 GLY A CA  
1130 C C   . GLY A 148 ? 0.74872 0.90102 1.01140 0.03054  -0.15279 -0.18979 351 GLY A C   
1131 O O   . GLY A 148 ? 0.76309 0.90905 1.00945 0.03432  -0.15784 -0.18131 351 GLY A O   
1132 N N   . ILE A 149 ? 0.83667 0.97939 1.08604 0.04683  -0.16895 -0.19749 352 ILE A N   
1133 C CA  . ILE A 149 ? 0.79714 0.91680 1.00745 0.07081  -0.19229 -0.19586 352 ILE A CA  
1134 C C   . ILE A 149 ? 0.79281 0.88973 0.95320 0.07253  -0.19717 -0.17106 352 ILE A C   
1135 O O   . ILE A 149 ? 0.68461 0.78203 0.84115 0.06557  -0.19249 -0.16483 352 ILE A O   
1136 C CB  . ILE A 149 ? 0.85196 0.96915 1.07185 0.09041  -0.20692 -0.21908 352 ILE A CB  
1137 N N   . GLU A 150 ? 0.77220 0.84743 0.89367 0.08189  -0.20529 -0.15718 353 GLU A N   
1138 C CA  . GLU A 150 ? 0.75562 0.80120 0.82424 0.08346  -0.20142 -0.13050 353 GLU A CA  
1139 C C   . GLU A 150 ? 0.75942 0.78148 0.79435 0.10303  -0.21863 -0.13478 353 GLU A C   
1140 O O   . GLU A 150 ? 0.75600 0.76893 0.78866 0.12173  -0.23279 -0.15171 353 GLU A O   
1141 C CB  . GLU A 150 ? 0.75116 0.77567 0.78691 0.08800  -0.20126 -0.11536 353 GLU A CB  
1142 C CG  . GLU A 150 ? 0.78357 0.82827 0.84682 0.06907  -0.18355 -0.10835 353 GLU A CG  
1143 C CD  . GLU A 150 ? 0.94062 0.96305 0.96871 0.06882  -0.17681 -0.08737 353 GLU A CD  
1144 O OE1 . GLU A 150 ? 0.93283 0.93282 0.93220 0.08628  -0.19228 -0.08997 353 GLU A OE1 
1145 O OE2 . GLU A 150 ? 0.89127 0.91747 0.92028 0.05180  -0.15606 -0.06941 353 GLU A OE2 
1146 N N   . THR A 151 ? 0.68977 0.69631 0.69768 0.09659  -0.20559 -0.11538 354 THR A N   
1147 C CA  . THR A 151 ? 0.69120 0.66935 0.65839 0.11452  -0.21857 -0.11516 354 THR A CA  
1148 C C   . THR A 151 ? 0.77393 0.70805 0.67830 0.12509  -0.21728 -0.09484 354 THR A C   
1149 O O   . THR A 151 ? 0.76006 0.68827 0.65675 0.12054  -0.21002 -0.08467 354 THR A O   
1150 C CB  . THR A 151 ? 0.59675 0.58117 0.56967 0.10209  -0.20463 -0.10713 354 THR A CB  
1151 O OG1 . THR A 151 ? 0.62160 0.59575 0.57476 0.08577  -0.18072 -0.07974 354 THR A OG1 
1152 C CG2 . THR A 151 ? 0.66113 0.68542 0.69492 0.08757  -0.19901 -0.12420 354 THR A CG2 
1153 N N   . GLU A 152 ? 0.73066 0.63132 0.58858 0.13865  -0.22221 -0.08884 355 GLU A N   
1154 C CA  . GLU A 152 ? 0.83538 0.68820 0.62993 0.14688  -0.21539 -0.06898 355 GLU A CA  
1155 C C   . GLU A 152 ? 0.77970 0.62784 0.56559 0.12522  -0.18565 -0.04391 355 GLU A C   
1156 O O   . GLU A 152 ? 0.71885 0.53153 0.46146 0.12645  -0.17365 -0.02745 355 GLU A O   
1157 C CB  . GLU A 152 ? 0.74826 0.56270 0.49988 0.16894  -0.22453 -0.07472 355 GLU A CB  
1158 N N   . ASP A 153 ? 0.57166 0.45308 0.39762 0.10603  -0.17313 -0.04213 356 ASP A N   
1159 C CA  . ASP A 153 ? 0.58292 0.46094 0.40204 0.08839  -0.14846 -0.02201 356 ASP A CA  
1160 C C   . ASP A 153 ? 0.64459 0.54305 0.49028 0.06943  -0.13174 -0.01233 356 ASP A C   
1161 O O   . ASP A 153 ? 0.62095 0.54392 0.49942 0.06588  -0.13692 -0.02132 356 ASP A O   
1162 C CB  . ASP A 153 ? 0.52813 0.42630 0.37011 0.08005  -0.14474 -0.02487 356 ASP A CB  
1163 C CG  . ASP A 153 ? 0.71566 0.59434 0.53192 0.09879  -0.16115 -0.03474 356 ASP A CG  
1164 O OD1 . ASP A 153 ? 0.79096 0.62869 0.55551 0.11587  -0.16725 -0.03079 356 ASP A OD1 
1165 O OD2 . ASP A 153 ? 0.75259 0.65437 0.59840 0.09702  -0.16738 -0.04689 356 ASP A OD2 
1166 N N   . TYR A 154 ? 0.60495 0.49330 0.43742 0.05755  -0.11142 0.00458  357 TYR A N   
1167 C CA  . TYR A 154 ? 0.51090 0.41560 0.36472 0.04115  -0.09571 0.01358  357 TYR A CA  
1168 C C   . TYR A 154 ? 0.51760 0.44045 0.39127 0.02577  -0.08118 0.02016  357 TYR A C   
1169 O O   . TYR A 154 ? 0.51224 0.42392 0.37057 0.02689  -0.07761 0.02338  357 TYR A O   
1170 C CB  . TYR A 154 ? 0.52283 0.39691 0.34374 0.04227  -0.08462 0.02510  357 TYR A CB  
1171 C CG  . TYR A 154 ? 0.55736 0.41539 0.36192 0.05490  -0.09633 0.02037  357 TYR A CG  
1172 C CD1 . TYR A 154 ? 0.66320 0.48603 0.42588 0.07544  -0.11025 0.01571  357 TYR A CD1 
1173 C CD2 . TYR A 154 ? 0.55338 0.42923 0.38165 0.04786  -0.09438 0.02007  357 TYR A CD2 
1174 C CE1 . TYR A 154 ? 0.65765 0.46326 0.40260 0.08909  -0.12262 0.01056  357 TYR A CE1 
1175 C CE2 . TYR A 154 ? 0.58638 0.44804 0.40056 0.05958  -0.10552 0.01530  357 TYR A CE2 
1176 C CZ  . TYR A 154 ? 0.71337 0.53987 0.48599 0.08029  -0.11981 0.01048  357 TYR A CZ  
1177 O OH  . TYR A 154 ? 0.75473 0.56541 0.51154 0.09340  -0.13202 0.00514  357 TYR A OH  
1178 N N   . PHE A 155 ? 0.47651 0.42551 0.38213 0.01270  -0.07351 0.02158  358 PHE A N   
1179 C CA  . PHE A 155 ? 0.44582 0.40531 0.36264 -0.00004 -0.05892 0.02944  358 PHE A CA  
1180 C C   . PHE A 155 ? 0.49052 0.42887 0.38452 -0.00220 -0.04592 0.03966  358 PHE A C   
1181 O O   . PHE A 155 ? 0.47295 0.40039 0.35797 -0.00107 -0.04291 0.04236  358 PHE A O   
1182 C CB  . PHE A 155 ? 0.40703 0.39254 0.35550 -0.01047 -0.05439 0.02839  358 PHE A CB  
1183 C CG  . PHE A 155 ? 0.37326 0.37805 0.34681 -0.01155 -0.06120 0.01754  358 PHE A CG  
1184 C CD1 . PHE A 155 ? 0.37621 0.38876 0.35931 -0.01591 -0.05806 0.01563  358 PHE A CD1 
1185 C CD2 . PHE A 155 ? 0.38434 0.39887 0.37359 -0.00896 -0.06902 0.00808  358 PHE A CD2 
1186 C CE1 . PHE A 155 ? 0.37987 0.40793 0.38777 -0.01859 -0.06055 0.00430  358 PHE A CE1 
1187 C CE2 . PHE A 155 ? 0.37027 0.40239 0.38681 -0.01168 -0.07188 -0.00439 358 PHE A CE2 
1188 C CZ  . PHE A 155 ? 0.36585 0.40383 0.39164 -0.01689 -0.06669 -0.00639 358 PHE A CZ  
1189 N N   . THR A 156 ? 0.48993 0.42155 0.37551 -0.00554 -0.03713 0.04406  359 THR A N   
1190 C CA  . THR A 156 ? 0.56227 0.47111 0.42688 -0.00777 -0.02253 0.05092  359 THR A CA  
1191 C C   . THR A 156 ? 0.47201 0.39698 0.35871 -0.01999 -0.00907 0.05328  359 THR A C   
1192 O O   . THR A 156 ? 0.58377 0.49408 0.46166 -0.02397 0.00529  0.05603  359 THR A O   
1193 C CB  . THR A 156 ? 0.60465 0.48610 0.43670 -0.00010 -0.02162 0.05244  359 THR A CB  
1194 O OG1 . THR A 156 ? 0.51603 0.41387 0.36174 -0.00254 -0.02496 0.05010  359 THR A OG1 
1195 C CG2 . THR A 156 ? 0.55336 0.41274 0.35733 0.01569  -0.03653 0.04860  359 THR A CG2 
1196 N N   . ASP A 157 ? 0.50688 0.45926 0.42106 -0.02525 -0.01280 0.05082  360 ASP A N   
1197 C CA  . ASP A 157 ? 0.45536 0.42179 0.38863 -0.03344 -0.00353 0.05098  360 ASP A CA  
1198 C C   . ASP A 157 ? 0.47290 0.43964 0.41340 -0.03643 0.00233  0.05081  360 ASP A C   
1199 O O   . ASP A 157 ? 0.44113 0.40827 0.38121 -0.03359 -0.00397 0.05066  360 ASP A O   
1200 C CB  . ASP A 157 ? 0.45178 0.44054 0.40502 -0.03578 -0.00946 0.04867  360 ASP A CB  
1201 C CG  . ASP A 157 ? 0.60919 0.59759 0.55785 -0.03427 -0.01273 0.04815  360 ASP A CG  
1202 O OD1 . ASP A 157 ? 0.63457 0.60695 0.56520 -0.03098 -0.01129 0.04944  360 ASP A OD1 
1203 O OD2 . ASP A 157 ? 0.64515 0.64632 0.60578 -0.03604 -0.01574 0.04638  360 ASP A OD2 
1204 N N   . PRO A 158 ? 0.48303 0.44986 0.43221 -0.04199 0.01446  0.04912  361 PRO A N   
1205 C CA  . PRO A 158 ? 0.42031 0.38421 0.37618 -0.04505 0.02202  0.04744  361 PRO A CA  
1206 C C   . PRO A 158 ? 0.45923 0.44475 0.43586 -0.04539 0.01388  0.04499  361 PRO A C   
1207 O O   . PRO A 158 ? 0.37800 0.36052 0.35692 -0.04597 0.01598  0.04448  361 PRO A O   
1208 C CB  . PRO A 158 ? 0.46787 0.43206 0.43648 -0.05152 0.03680  0.04209  361 PRO A CB  
1209 C CG  . PRO A 158 ? 0.49849 0.46064 0.46042 -0.05100 0.03728  0.04269  361 PRO A CG  
1210 C CD  . PRO A 158 ? 0.43950 0.41051 0.39628 -0.04570 0.02172  0.04642  361 PRO A CD  
1211 N N   . PHE A 159 ? 0.35633 0.36023 0.34521 -0.04470 0.00577  0.04357  362 PHE A N   
1212 C CA  . PHE A 159 ? 0.37617 0.39637 0.37996 -0.04419 -0.00055 0.04135  362 PHE A CA  
1213 C C   . PHE A 159 ? 0.33864 0.35960 0.33726 -0.04147 -0.00909 0.04370  362 PHE A C   
1214 O O   . PHE A 159 ? 0.31327 0.34504 0.32192 -0.04133 -0.01283 0.04209  362 PHE A O   
1215 C CB  . PHE A 159 ? 0.30458 0.33783 0.31844 -0.04339 -0.00354 0.03820  362 PHE A CB  
1216 C CG  . PHE A 159 ? 0.36486 0.39527 0.36912 -0.04229 -0.00641 0.04098  362 PHE A CG  
1217 C CD1 . PHE A 159 ? 0.33790 0.37041 0.33899 -0.04112 -0.01198 0.04273  362 PHE A CD1 
1218 C CD2 . PHE A 159 ? 0.42578 0.45098 0.42587 -0.04313 -0.00206 0.04062  362 PHE A CD2 
1219 C CE1 . PHE A 159 ? 0.41252 0.44228 0.40744 -0.04087 -0.01332 0.04377  362 PHE A CE1 
1220 C CE2 . PHE A 159 ? 0.37840 0.40097 0.37016 -0.04205 -0.00486 0.04282  362 PHE A CE2 
1221 C CZ  . PHE A 159 ? 0.37288 0.39785 0.36252 -0.04096 -0.01057 0.04425  362 PHE A CZ  
1222 N N   . VAL A 160 ? 0.25550 0.26526 0.23960 -0.03854 -0.01262 0.04570  363 VAL A N   
1223 C CA  . VAL A 160 ? 0.31408 0.32733 0.29904 -0.03543 -0.02167 0.04387  363 VAL A CA  
1224 C C   . VAL A 160 ? 0.40005 0.40407 0.37837 -0.03239 -0.02352 0.04395  363 VAL A C   
1225 O O   . VAL A 160 ? 0.40357 0.38869 0.36224 -0.02718 -0.02507 0.04508  363 VAL A O   
1226 C CB  . VAL A 160 ? 0.38589 0.39445 0.36276 -0.03188 -0.02748 0.04218  363 VAL A CB  
1227 C CG1 . VAL A 160 ? 0.35266 0.36951 0.33927 -0.02941 -0.03635 0.03594  363 VAL A CG1 
1228 C CG2 . VAL A 160 ? 0.39531 0.41037 0.37698 -0.03521 -0.02413 0.04271  363 VAL A CG2 
1229 N N   . PHE A 161 ? 0.32584 0.34044 0.31742 -0.03446 -0.02361 0.04264  364 PHE A N   
1230 C CA  . PHE A 161 ? 0.32557 0.33252 0.31231 -0.03151 -0.02602 0.04227  364 PHE A CA  
1231 C C   . PHE A 161 ? 0.31672 0.34077 0.32138 -0.03299 -0.03010 0.03895  364 PHE A C   
1232 O O   . PHE A 161 ? 0.28640 0.32395 0.30380 -0.03666 -0.02769 0.03823  364 PHE A O   
1233 C CB  . PHE A 161 ? 0.25432 0.24820 0.23454 -0.03378 -0.01561 0.04492  364 PHE A CB  
1234 C CG  . PHE A 161 ? 0.34008 0.34901 0.34033 -0.03975 -0.00873 0.04290  364 PHE A CG  
1235 C CD1 . PHE A 161 ? 0.32616 0.34835 0.34205 -0.04080 -0.01082 0.04016  364 PHE A CD1 
1236 C CD2 . PHE A 161 ? 0.28688 0.29642 0.29050 -0.04298 -0.00133 0.04205  364 PHE A CD2 
1237 C CE1 . PHE A 161 ? 0.30291 0.33809 0.33613 -0.04350 -0.00721 0.03601  364 PHE A CE1 
1238 C CE2 . PHE A 161 ? 0.34177 0.36551 0.36515 -0.04597 0.00227  0.03691  364 PHE A CE2 
1239 C CZ  . PHE A 161 ? 0.26138 0.29766 0.29900 -0.04551 -0.00143 0.03357  364 PHE A CZ  
1240 N N   . LYS A 162 ? 0.28059 0.30115 0.28314 -0.02890 -0.03647 0.03650  365 LYS A N   
1241 C CA  . LYS A 162 ? 0.35630 0.38992 0.37413 -0.03033 -0.03867 0.03349  365 LYS A CA  
1242 C C   . LYS A 162 ? 0.30344 0.33269 0.32119 -0.03208 -0.03271 0.03617  365 LYS A C   
1243 O O   . LYS A 162 ? 0.32342 0.33423 0.32598 -0.03027 -0.02887 0.03887  365 LYS A O   
1244 C CB  . LYS A 162 ? 0.27168 0.30536 0.29068 -0.02467 -0.04913 0.02726  365 LYS A CB  
1245 C CG  . LYS A 162 ? 0.34590 0.38599 0.37118 -0.02307 -0.05496 0.02062  365 LYS A CG  
1246 C CD  . LYS A 162 ? 0.34448 0.38732 0.37648 -0.01626 -0.06695 0.01012  365 LYS A CD  
1247 C CE  . LYS A 162 ? 0.49127 0.51273 0.49902 -0.00483 -0.07671 0.00921  365 LYS A CE  
1248 N NZ  . LYS A 162 ? 0.58803 0.61490 0.60542 0.00407  -0.09178 -0.00540 365 LYS A NZ  
1249 N N   . TRP A 163 ? 0.26706 0.31081 0.30048 -0.03538 -0.03071 0.03467  366 TRP A N   
1250 C CA  . TRP A 163 ? 0.23951 0.28238 0.27822 -0.03680 -0.02625 0.03444  366 TRP A CA  
1251 C C   . TRP A 163 ? 0.26869 0.31342 0.31033 -0.03419 -0.03240 0.03230  366 TRP A C   
1252 O O   . TRP A 163 ? 0.28796 0.34690 0.34178 -0.03470 -0.03578 0.02932  366 TRP A O   
1253 C CB  . TRP A 163 ? 0.21716 0.27381 0.27049 -0.03930 -0.02292 0.03188  366 TRP A CB  
1254 C CG  . TRP A 163 ? 0.23559 0.29353 0.29954 -0.04081 -0.01822 0.02855  366 TRP A CG  
1255 C CD1 . TRP A 163 ? 0.26027 0.30588 0.32019 -0.04162 -0.01404 0.02910  366 TRP A CD1 
1256 C CD2 . TRP A 163 ? 0.23657 0.30731 0.31683 -0.04083 -0.01726 0.02248  366 TRP A CD2 
1257 N NE1 . TRP A 163 ? 0.27046 0.32224 0.34689 -0.04405 -0.00876 0.02349  366 TRP A NE1 
1258 C CE2 . TRP A 163 ? 0.26894 0.33788 0.35963 -0.04296 -0.01199 0.01838  366 TRP A CE2 
1259 C CE3 . TRP A 163 ? 0.24009 0.32142 0.32537 -0.03782 -0.02097 0.01901  366 TRP A CE3 
1260 C CZ2 . TRP A 163 ? 0.31454 0.39614 0.42580 -0.04249 -0.01133 0.00909  366 TRP A CZ2 
1261 C CZ3 . TRP A 163 ? 0.24080 0.33225 0.34189 -0.03526 -0.02209 0.01028  366 TRP A CZ3 
1262 C CH2 . TRP A 163 ? 0.27129 0.36493 0.38782 -0.03775 -0.01780 0.00451  366 TRP A CH2 
1263 N N   . LYS A 164 ? 0.26130 0.28867 0.28905 -0.03073 -0.03319 0.03357  367 LYS A N   
1264 C CA  . LYS A 164 ? 0.35381 0.38023 0.38183 -0.02653 -0.04061 0.03078  367 LYS A CA  
1265 C C   . LYS A 164 ? 0.28243 0.31927 0.32585 -0.02982 -0.03742 0.02928  367 LYS A C   
1266 O O   . LYS A 164 ? 0.23997 0.27337 0.28660 -0.03348 -0.02854 0.03022  367 LYS A O   
1267 C CB  . LYS A 164 ? 0.39978 0.39784 0.40146 -0.01978 -0.04200 0.03297  367 LYS A CB  
1268 C CG  . LYS A 164 ? 0.47578 0.46616 0.47261 -0.01409 -0.04860 0.03047  367 LYS A CG  
1269 C CD  . LYS A 164 ? 0.52668 0.48253 0.48868 -0.00398 -0.05189 0.03238  367 LYS A CD  
1270 C CE  . LYS A 164 ? 0.60024 0.52926 0.54146 -0.00756 -0.03533 0.03943  367 LYS A CE  
1271 N N   . GLU A 165 ? 0.23514 0.28530 0.29028 -0.02854 -0.04426 0.02521  368 GLU A N   
1272 C CA  . GLU A 165 ? 0.25203 0.31001 0.31931 -0.03004 -0.04295 0.02331  368 GLU A CA  
1273 C C   . GLU A 165 ? 0.30299 0.34324 0.35923 -0.02681 -0.04309 0.02412  368 GLU A C   
1274 O O   . GLU A 165 ? 0.29225 0.32073 0.33521 -0.02048 -0.05079 0.02321  368 GLU A O   
1275 C CB  . GLU A 165 ? 0.30431 0.37972 0.38560 -0.02980 -0.04866 0.01851  368 GLU A CB  
1276 C CG  . GLU A 165 ? 0.27719 0.36160 0.37049 -0.03066 -0.04794 0.01623  368 GLU A CG  
1277 C CD  . GLU A 165 ? 0.30046 0.39979 0.40471 -0.03131 -0.04971 0.01207  368 GLU A CD  
1278 O OE1 . GLU A 165 ? 0.31648 0.41944 0.42590 -0.02988 -0.05466 0.00757  368 GLU A OE1 
1279 O OE2 . GLU A 165 ? 0.22545 0.33069 0.33168 -0.03250 -0.04579 0.01231  368 GLU A OE2 
1280 N N   . THR A 166 ? 0.27682 0.31383 0.33840 -0.03027 -0.03481 0.02436  369 THR A N   
1281 C CA  . THR A 166 ? 0.35484 0.37320 0.40658 -0.02833 -0.03201 0.02489  369 THR A CA  
1282 C C   . THR A 166 ? 0.31724 0.35086 0.39079 -0.03161 -0.03009 0.02053  369 THR A C   
1283 O O   . THR A 166 ? 0.32340 0.37949 0.41622 -0.03404 -0.03145 0.01711  369 THR A O   
1284 C CB  . THR A 166 ? 0.44649 0.43706 0.47990 -0.03038 -0.01861 0.02861  369 THR A CB  
1285 O OG1 . THR A 166 ? 0.32676 0.32780 0.38100 -0.03829 -0.00689 0.02506  369 THR A OG1 
1286 C CG2 . THR A 166 ? 0.40780 0.38479 0.42021 -0.02734 -0.01959 0.03270  369 THR A CG2 
1287 N N   . ALA A 167 ? 0.32199 0.34045 0.38975 -0.03056 -0.02698 0.02027  370 ALA A N   
1288 C CA  . ALA A 167 ? 0.30406 0.33600 0.39341 -0.03354 -0.02483 0.01513  370 ALA A CA  
1289 C C   . ALA A 167 ? 0.25120 0.29605 0.36186 -0.03973 -0.01561 0.01006  370 ALA A C   
1290 O O   . ALA A 167 ? 0.28758 0.35258 0.42050 -0.04030 -0.01836 0.00355  370 ALA A O   
1291 C CB  . ALA A 167 ? 0.31211 0.31981 0.38914 -0.03224 -0.01960 0.01583  370 ALA A CB  
1292 N N   . ASP A 168 ? 0.29321 0.32669 0.39786 -0.04329 -0.00552 0.01133  371 ASP A N   
1293 C CA  . ASP A 168 ? 0.28582 0.32993 0.41312 -0.04877 0.00391  0.00345  371 ASP A CA  
1294 C C   . ASP A 168 ? 0.28618 0.35037 0.42222 -0.04725 -0.00271 0.00153  371 ASP A C   
1295 O O   . ASP A 168 ? 0.27311 0.34815 0.42914 -0.04960 0.00200  -0.00723 371 ASP A O   
1296 C CB  . ASP A 168 ? 0.37892 0.39622 0.49628 -0.05458 0.02232  0.00390  371 ASP A CB  
1297 C CG  . ASP A 168 ? 0.56885 0.55738 0.67023 -0.05545 0.03180  0.00642  371 ASP A CG  
1298 O OD1 . ASP A 168 ? 0.43003 0.42747 0.54897 -0.05636 0.03120  0.00068  371 ASP A OD1 
1299 O OD2 . ASP A 168 ? 0.48091 0.43549 0.54901 -0.05395 0.03920  0.01415  371 ASP A OD2 
1300 N N   . THR A 169 ? 0.25064 0.31901 0.37318 -0.04310 -0.01296 0.00779  372 THR A N   
1301 C CA  . THR A 169 ? 0.22624 0.30848 0.35317 -0.04153 -0.01726 0.00636  372 THR A CA  
1302 C C   . THR A 169 ? 0.22455 0.32615 0.36404 -0.03704 -0.02622 0.00093  372 THR A C   
1303 O O   . THR A 169 ? 0.23407 0.33973 0.37596 -0.03525 -0.03080 0.00050  372 THR A O   
1304 C CB  . THR A 169 ? 0.25909 0.33440 0.36603 -0.03997 -0.02132 0.01436  372 THR A CB  
1305 O OG1 . THR A 169 ? 0.24817 0.32402 0.34837 -0.03706 -0.02912 0.01707  372 THR A OG1 
1306 C CG2 . THR A 169 ? 0.26728 0.32104 0.35787 -0.04228 -0.01324 0.01901  372 THR A CG2 
1307 N N   . LYS A 170 ? 0.22451 0.33555 0.36891 -0.03396 -0.02903 -0.00351 373 LYS A N   
1308 C CA  . LYS A 170 ? 0.18752 0.31133 0.33889 -0.02710 -0.03724 -0.01020 373 LYS A CA  
1309 C C   . LYS A 170 ? 0.20776 0.33061 0.34194 -0.02172 -0.04264 -0.00650 373 LYS A C   
1310 O O   . LYS A 170 ? 0.16904 0.29638 0.30182 -0.01383 -0.04900 -0.01214 373 LYS A O   
1311 C CB  . LYS A 170 ? 0.19567 0.32944 0.36949 -0.02476 -0.03717 -0.02372 373 LYS A CB  
1312 C CG  . LYS A 170 ? 0.25652 0.39161 0.45097 -0.03012 -0.03015 -0.03032 373 LYS A CG  
1313 C CD  . LYS A 170 ? 0.31208 0.45251 0.53109 -0.03292 -0.02301 -0.04360 373 LYS A CD  
1314 C CE  . LYS A 170 ? 0.39912 0.55780 0.63811 -0.02326 -0.03393 -0.06007 373 LYS A CE  
1315 N N   . PHE A 171 ? 0.16851 0.28307 0.28778 -0.02490 -0.03991 0.00192  374 PHE A N   
1316 C CA  . PHE A 171 ? 0.21582 0.32627 0.31847 -0.02160 -0.04176 0.00553  374 PHE A CA  
1317 C C   . PHE A 171 ? 0.21039 0.32035 0.30905 -0.02284 -0.04187 0.00812  374 PHE A C   
1318 O O   . PHE A 171 ? 0.18249 0.29566 0.29011 -0.02565 -0.04243 0.00793  374 PHE A O   
1319 C CB  . PHE A 171 ? 0.16507 0.26826 0.25748 -0.02493 -0.03811 0.01116  374 PHE A CB  
1320 C CG  . PHE A 171 ? 0.18513 0.28393 0.27701 -0.03099 -0.03533 0.01625  374 PHE A CG  
1321 C CD1 . PHE A 171 ? 0.16033 0.25782 0.24801 -0.03256 -0.03607 0.01846  374 PHE A CD1 
1322 C CD2 . PHE A 171 ? 0.19441 0.28827 0.28886 -0.03405 -0.03180 0.01717  374 PHE A CD2 
1323 C CE1 . PHE A 171 ? 0.16554 0.25827 0.25156 -0.03484 -0.03690 0.02053  374 PHE A CE1 
1324 C CE2 . PHE A 171 ? 0.22555 0.30965 0.31219 -0.03646 -0.03073 0.02159  374 PHE A CE2 
1325 C CZ  . PHE A 171 ? 0.21390 0.29807 0.29626 -0.03572 -0.03510 0.02279  374 PHE A CZ  
1326 N N   . TYR A 172 ? 0.17198 0.27591 0.25650 -0.02080 -0.04010 0.00977  375 TYR A N   
1327 C CA  . TYR A 172 ? 0.16681 0.26999 0.24979 -0.02311 -0.03743 0.01012  375 TYR A CA  
1328 C C   . TYR A 172 ? 0.21676 0.31333 0.29252 -0.02781 -0.03111 0.01276  375 TYR A C   
1329 O O   . TYR A 172 ? 0.18058 0.26824 0.24318 -0.02651 -0.02767 0.01489  375 TYR A O   
1330 C CB  . TYR A 172 ? 0.18904 0.28827 0.26241 -0.01647 -0.03778 0.00690  375 TYR A CB  
1331 C CG  . TYR A 172 ? 0.18997 0.29786 0.27422 -0.01102 -0.04537 0.00167  375 TYR A CG  
1332 C CD1 . TYR A 172 ? 0.17738 0.29448 0.27691 -0.01334 -0.04761 -0.00060 375 TYR A CD1 
1333 C CD2 . TYR A 172 ? 0.17681 0.28442 0.25887 -0.00340 -0.05060 -0.00286 375 TYR A CD2 
1334 C CE1 . TYR A 172 ? 0.16900 0.29427 0.28158 -0.00937 -0.05319 -0.00671 375 TYR A CE1 
1335 C CE2 . TYR A 172 ? 0.19225 0.31008 0.29019 0.00119  -0.05724 -0.01100 375 TYR A CE2 
1336 C CZ  . TYR A 172 ? 0.19409 0.32061 0.30766 -0.00250 -0.05766 -0.01262 375 TYR A CZ  
1337 O OH  . TYR A 172 ? 0.19527 0.33217 0.32753 0.00119  -0.06296 -0.02204 375 TYR A OH  
1338 N N   . ASN A 173 ? 0.20477 0.30590 0.29075 -0.03270 -0.03005 0.01087  376 ASN A N   
1339 C CA  . ASN A 173 ? 0.21641 0.31463 0.30304 -0.03759 -0.02438 0.00945  376 ASN A CA  
1340 C C   . ASN A 173 ? 0.21047 0.31481 0.31052 -0.04088 -0.02217 0.00251  376 ASN A C   
1341 O O   . ASN A 173 ? 0.23631 0.34846 0.35045 -0.04213 -0.02790 -0.00188 376 ASN A O   
1342 C CB  . ASN A 173 ? 0.18048 0.28006 0.27074 -0.03908 -0.02877 0.01108  376 ASN A CB  
1343 C CG  . ASN A 173 ? 0.23360 0.33331 0.32997 -0.04328 -0.02506 0.00631  376 ASN A CG  
1344 O OD1 . ASN A 173 ? 0.23094 0.32579 0.32480 -0.04652 -0.01526 0.00382  376 ASN A OD1 
1345 N ND2 . ASN A 173 ? 0.24089 0.34415 0.34472 -0.04260 -0.03236 0.00359  376 ASN A ND2 
1346 N N   . VAL A 174 ? 0.18937 0.28811 0.28344 -0.04124 -0.01375 0.00034  377 VAL A N   
1347 C CA  . VAL A 174 ? 0.18554 0.28992 0.29463 -0.04562 -0.00870 -0.00817 377 VAL A CA  
1348 C C   . VAL A 174 ? 0.25231 0.35601 0.37139 -0.05234 -0.00006 -0.01493 377 VAL A C   
1349 O O   . VAL A 174 ? 0.27195 0.36304 0.37750 -0.05430 0.00933  -0.01201 377 VAL A O   
1350 C CB  . VAL A 174 ? 0.23869 0.33382 0.33579 -0.04410 0.00005  -0.00879 377 VAL A CB  
1351 C CG1 . VAL A 174 ? 0.18807 0.28717 0.28064 -0.03680 -0.01038 -0.00511 377 VAL A CG1 
1352 C CG2 . VAL A 174 ? 0.21974 0.29234 0.28979 -0.04322 0.01311  -0.00489 377 VAL A CG2 
1353 N N   . ARG A 175 ? 0.22311 0.34030 0.36712 -0.05515 -0.00383 -0.02564 378 ARG A N   
1354 C CA  . ARG A 175 ? 0.26767 0.38871 0.42884 -0.06069 0.00154  -0.03617 378 ARG A CA  
1355 C C   . ARG A 175 ? 0.27731 0.40102 0.45700 -0.06781 0.01574  -0.04969 378 ARG A C   
1356 O O   . ARG A 175 ? 0.24150 0.36835 0.42491 -0.06733 0.01674  -0.05210 378 ARG A O   
1357 C CB  . ARG A 175 ? 0.26458 0.39830 0.44153 -0.05634 -0.01557 -0.04196 378 ARG A CB  
1358 C CG  . ARG A 175 ? 0.25173 0.37876 0.41018 -0.05134 -0.02463 -0.03032 378 ARG A CG  
1359 C CD  . ARG A 175 ? 0.32868 0.46058 0.49205 -0.04405 -0.04205 -0.03368 378 ARG A CD  
1360 N NE  . ARG A 175 ? 0.33161 0.46568 0.49435 -0.03934 -0.05037 -0.03227 378 ARG A NE  
1361 C CZ  . ARG A 175 ? 0.36531 0.50029 0.53096 -0.03190 -0.06455 -0.03748 378 ARG A CZ  
1362 N NH1 . ARG A 175 ? 0.27435 0.40813 0.44235 -0.02663 -0.07409 -0.04487 378 ARG A NH1 
1363 N NH2 . ARG A 175 ? 0.28196 0.41703 0.44614 -0.02837 -0.06993 -0.03597 378 ARG A NH2 
1364 N N   . LYS A 176 ? 0.23700 0.35877 0.42936 -0.07509 0.02841  -0.05947 379 LYS A N   
1365 C CA  . LYS A 176 ? 0.30567 0.42951 0.52072 -0.08400 0.04582  -0.07563 379 LYS A CA  
1366 C C   . LYS A 176 ? 0.32045 0.46935 0.57384 -0.08257 0.03237  -0.09360 379 LYS A C   
1367 O O   . LYS A 176 ? 0.30284 0.46432 0.57410 -0.07923 0.01870  -0.10221 379 LYS A O   
1368 C CB  . LYS A 176 ? 0.29656 0.40991 0.51651 -0.09308 0.06530  -0.08268 379 LYS A CB  
1369 C CG  . LYS A 176 ? 0.33065 0.41460 0.51033 -0.09376 0.08031  -0.06702 379 LYS A CG  
1370 C CD  . LYS A 176 ? 0.45046 0.52475 0.63839 -0.10299 0.09873  -0.07551 379 LYS A CD  
1371 C CE  . LYS A 176 ? 0.43637 0.47425 0.58145 -0.10425 0.11925  -0.06271 379 LYS A CE  
1372 N NZ  . LYS A 176 ? 0.51457 0.54115 0.66414 -0.11238 0.13555  -0.06863 379 LYS A NZ  
1373 N N   . LEU A 177 ? 0.23639 0.39120 0.50097 -0.08371 0.03531  -0.10030 380 LEU A N   
1374 C CA  . LEU A 177 ? 0.23321 0.41132 0.53560 -0.08164 0.02284  -0.12010 380 LEU A CA  
1375 C C   . LEU A 177 ? 0.31982 0.49902 0.64427 -0.08416 0.03153  -0.13889 380 LEU A C   
1376 O O   . LEU A 177 ? 0.30657 0.49539 0.64497 -0.07445 0.01444  -0.15036 380 LEU A O   
1377 C CB  . LEU A 177 ? 0.25273 0.43334 0.55933 -0.08227 0.02718  -0.12316 380 LEU A CB  
1378 C CG  . LEU A 177 ? 0.28849 0.46670 0.57093 -0.07346 0.01227  -0.10638 380 LEU A CG  
1379 C CD1 . LEU A 177 ? 0.28747 0.44357 0.52952 -0.07308 0.02149  -0.08521 380 LEU A CD1 
1380 C CD2 . LEU A 177 ? 0.28698 0.47510 0.58603 -0.07364 0.01232  -0.11594 380 LEU A CD2 
1381 N N   . ASP A 178 ? 0.30662 0.47269 0.63145 -0.09599 0.05875  -0.14258 381 ASP A N   
1382 C CA  . ASP A 178 ? 0.30618 0.47156 0.65288 -0.09887 0.06993  -0.16199 381 ASP A CA  
1383 C C   . ASP A 178 ? 0.34986 0.52215 0.70232 -0.09296 0.05481  -0.16454 381 ASP A C   
1384 O O   . ASP A 178 ? 0.35680 0.53599 0.73341 -0.08990 0.05375  -0.18412 381 ASP A O   
1385 C CB  . ASP A 178 ? 0.37514 0.51736 0.71215 -0.11248 0.10430  -0.16232 381 ASP A CB  
1386 C CG  . ASP A 178 ? 0.48282 0.61678 0.82335 -0.11782 0.12310  -0.17061 381 ASP A CG  
1387 O OD1 . ASP A 178 ? 0.51726 0.66734 0.87362 -0.11138 0.10893  -0.17843 381 ASP A OD1 
1388 O OD2 . ASP A 178 ? 0.48866 0.59652 0.81258 -0.12776 0.15265  -0.16908 381 ASP A OD2 
1389 N N   . LYS A 179 ? 0.33837 0.50875 0.67017 -0.09102 0.04378  -0.14668 382 LYS A N   
1390 C CA  . LYS A 179 ? 0.35209 0.52826 0.68679 -0.08434 0.02762  -0.14843 382 LYS A CA  
1391 C C   . LYS A 179 ? 0.38137 0.56868 0.71550 -0.06894 -0.00266 -0.14916 382 LYS A C   
1392 O O   . LYS A 179 ? 0.39758 0.59041 0.74276 -0.06006 -0.01608 -0.16124 382 LYS A O   
1393 C CB  . LYS A 179 ? 0.32776 0.49378 0.63996 -0.09005 0.03266  -0.13043 382 LYS A CB  
1394 C CG  . LYS A 179 ? 0.48232 0.63061 0.78961 -0.10294 0.06234  -0.13055 382 LYS A CG  
1395 C CD  . LYS A 179 ? 0.44443 0.59472 0.77113 -0.10318 0.06564  -0.14652 382 LYS A CD  
1396 N N   . LEU A 180 ? 0.29249 0.48031 0.61176 -0.06467 -0.01302 -0.13707 383 LEU A N   
1397 C CA  . LEU A 180 ? 0.32024 0.51170 0.63299 -0.04972 -0.03895 -0.13704 383 LEU A CA  
1398 C C   . LEU A 180 ? 0.37787 0.57585 0.71124 -0.04162 -0.04518 -0.15741 383 LEU A C   
1399 O O   . LEU A 180 ? 0.42213 0.62030 0.75371 -0.02767 -0.06528 -0.16428 383 LEU A O   
1400 C CB  . LEU A 180 ? 0.28718 0.47567 0.57985 -0.04772 -0.04566 -0.12023 383 LEU A CB  
1401 C CG  . LEU A 180 ? 0.33320 0.51040 0.59632 -0.04856 -0.04585 -0.09840 383 LEU A CG  
1402 C CD1 . LEU A 180 ? 0.28274 0.45336 0.52473 -0.04520 -0.04916 -0.08329 383 LEU A CD1 
1403 C CD2 . LEU A 180 ? 0.33278 0.50488 0.58386 -0.03916 -0.06216 -0.09610 383 LEU A CD2 
1404 N N   . TYR A 181 ? 0.27225 0.60894 0.43317 -0.10491 -0.05883 0.03250  384 TYR A N   
1405 C CA  . TYR A 181 ? 0.26933 0.64746 0.45321 -0.09718 -0.06107 0.03091  384 TYR A CA  
1406 C C   . TYR A 181 ? 0.33219 0.73225 0.51602 -0.09817 -0.07392 0.03046  384 TYR A C   
1407 O O   . TYR A 181 ? 0.30515 0.70433 0.47923 -0.11597 -0.08049 0.02801  384 TYR A O   
1408 C CB  . TYR A 181 ? 0.26217 0.66687 0.46166 -0.11086 -0.05503 0.02524  384 TYR A CB  
1409 C CG  . TYR A 181 ? 0.25816 0.71180 0.48474 -0.10187 -0.05556 0.02099  384 TYR A CG  
1410 C CD1 . TYR A 181 ? 0.27541 0.73342 0.51350 -0.07731 -0.05304 0.02138  384 TYR A CD1 
1411 C CD2 . TYR A 181 ? 0.25994 0.75599 0.50078 -0.11834 -0.05878 0.01556  384 TYR A CD2 
1412 C CE1 . TYR A 181 ? 0.26237 0.76638 0.52498 -0.06601 -0.05483 0.01542  384 TYR A CE1 
1413 C CE2 . TYR A 181 ? 0.25608 0.80344 0.52435 -0.10926 -0.05905 0.00951  384 TYR A CE2 
1414 C CZ  . TYR A 181 ? 0.28488 0.83643 0.56379 -0.08145 -0.05752 0.00890  384 TYR A CZ  
1415 O OH  . TYR A 181 ? 0.25651 0.86020 0.56234 -0.06918 -0.05931 0.00097  384 TYR A OH  
1416 N N   . VAL A 182 ? 0.28664 0.70344 0.47929 -0.07823 -0.07894 0.03242  385 VAL A N   
1417 C CA  . VAL A 182 ? 0.29456 0.73710 0.48954 -0.07575 -0.09243 0.03071  385 VAL A CA  
1418 C C   . VAL A 182 ? 0.28967 0.78346 0.51435 -0.07037 -0.09454 0.02400  385 VAL A C   
1419 O O   . VAL A 182 ? 0.29017 0.79169 0.52493 -0.04810 -0.09360 0.02475  385 VAL A O   
1420 C CB  . VAL A 182 ? 0.36907 0.79041 0.54653 -0.05546 -0.09882 0.03794  385 VAL A CB  
1421 C CG1 . VAL A 182 ? 0.32190 0.77408 0.50304 -0.05065 -0.11437 0.03471  385 VAL A CG1 
1422 C CG2 . VAL A 182 ? 0.34603 0.72378 0.49546 -0.06125 -0.09592 0.04298  385 VAL A CG2 
1423 N N   . GLN A 183 ? 0.28786 0.81676 0.52602 -0.09085 -0.09793 0.01686  386 GLN A N   
1424 C CA  . GLN A 183 ? 0.28265 0.86909 0.55228 -0.08913 -0.09871 0.00841  386 GLN A CA  
1425 C C   . GLN A 183 ? 0.29175 0.90182 0.57038 -0.06287 -0.11116 0.00657  386 GLN A C   
1426 O O   . GLN A 183 ? 0.30416 0.91288 0.57247 -0.06154 -0.12409 0.00727  386 GLN A O   
1427 C CB  . GLN A 183 ? 0.28480 0.90261 0.56421 -0.11941 -0.10126 0.00190  386 GLN A CB  
1428 C CG  . GLN A 183 ? 0.28575 0.87047 0.54859 -0.14562 -0.09026 0.00427  386 GLN A CG  
1429 C CD  . GLN A 183 ? 0.30540 0.89642 0.56632 -0.17060 -0.08886 -0.00107 386 GLN A CD  
1430 O OE1 . GLN A 183 ? 0.32083 0.90552 0.57222 -0.18113 -0.09986 -0.00247 386 GLN A OE1 
1431 N NE2 . GLN A 183 ? 0.30759 0.91146 0.57671 -0.17995 -0.07564 -0.00390 386 GLN A NE2 
1432 N N   . GLY A 184 ? 0.28883 0.91837 0.58441 -0.04041 -0.10848 0.00363  387 GLY A N   
1433 C CA  . GLY A 184 ? 0.30183 0.95150 0.60434 -0.01218 -0.12154 0.00123  387 GLY A CA  
1434 C C   . GLY A 184 ? 0.31762 0.91592 0.59349 0.01201  -0.12487 0.01226  387 GLY A C   
1435 O O   . GLY A 184 ? 0.36320 0.97049 0.63963 0.03787  -0.13652 0.01161  387 GLY A O   
1436 N N   . GLN A 185 ? 0.31599 0.86133 0.56771 0.00425  -0.11555 0.02218  388 GLN A N   
1437 C CA  . GLN A 185 ? 0.33169 0.82824 0.55938 0.02354  -0.11500 0.03329  388 GLN A CA  
1438 C C   . GLN A 185 ? 0.35087 0.81958 0.57916 0.02660  -0.10120 0.03612  388 GLN A C   
1439 O O   . GLN A 185 ? 0.38348 0.83079 0.60590 0.04828  -0.10226 0.04064  388 GLN A O   
1440 C CB  . GLN A 185 ? 0.34046 0.79888 0.53804 0.01367  -0.11613 0.04219  388 GLN A CB  
1441 C CG  . GLN A 185 ? 0.45613 0.93142 0.64544 0.01617  -0.13189 0.04091  388 GLN A CG  
1442 N N   . PHE A 186 ? 0.30436 0.77070 0.53791 0.00555  -0.08946 0.03330  389 PHE A N   
1443 C CA  . PHE A 186 ? 0.29687 0.73709 0.53059 0.00735  -0.07707 0.03469  389 PHE A CA  
1444 C C   . PHE A 186 ? 0.37910 0.85190 0.63742 0.02122  -0.07562 0.02579  389 PHE A C   
1445 O O   . PHE A 186 ? 0.33399 0.85681 0.61276 0.02198  -0.08105 0.01696  389 PHE A O   
1446 C CB  . PHE A 186 ? 0.31996 0.74672 0.54850 -0.01812 -0.06689 0.03376  389 PHE A CB  
1447 C CG  . PHE A 186 ? 0.33953 0.72281 0.54206 -0.02583 -0.06533 0.04178  389 PHE A CG  
1448 C CD1 . PHE A 186 ? 0.39693 0.76800 0.58251 -0.01828 -0.07387 0.04836  389 PHE A CD1 
1449 C CD2 . PHE A 186 ? 0.31378 0.67011 0.50813 -0.03922 -0.05553 0.04182  389 PHE A CD2 
1450 C CE1 . PHE A 186 ? 0.38106 0.71672 0.54300 -0.02476 -0.07127 0.05456  389 PHE A CE1 
1451 C CE2 . PHE A 186 ? 0.32728 0.64905 0.49987 -0.04469 -0.05414 0.04702  389 PHE A CE2 
1452 C CZ  . PHE A 186 ? 0.39613 0.70894 0.55298 -0.03782 -0.06133 0.05326  389 PHE A CZ  
1453 N N   . PRO A 187 ? 0.48723 0.93450 0.74471 0.03281  -0.06873 0.02675  390 PRO A N   
1454 C CA  . PRO A 187 ? 0.47847 0.95555 0.75771 0.04835  -0.06769 0.01671  390 PRO A CA  
1455 C C   . PRO A 187 ? 0.45913 0.97711 0.75719 0.02942  -0.05879 0.00700  390 PRO A C   
1456 O O   . PRO A 187 ? 0.44053 0.94904 0.73093 0.00441  -0.05164 0.00930  390 PRO A O   
1457 C CB  . PRO A 187 ? 0.52034 0.95083 0.78944 0.06023  -0.06203 0.02066  390 PRO A CB  
1458 C CG  . PRO A 187 ? 0.49335 0.87396 0.73647 0.05530  -0.06240 0.03390  390 PRO A CG  
1459 C CD  . PRO A 187 ? 0.40001 0.79178 0.63732 0.03274  -0.06217 0.03588  390 PRO A CD  
1460 N N   . SER A 188 ? 0.37942 0.94320 0.70081 0.04240  -0.05956 -0.00426 391 SER A N   
1461 C CA  . SER A 188 ? 0.34555 0.95583 0.68557 0.02457  -0.05038 -0.01364 391 SER A CA  
1462 C C   . SER A 188 ? 0.34222 0.92899 0.67618 0.01581  -0.03659 -0.01416 391 SER A C   
1463 O O   . SER A 188 ? 0.36533 0.97355 0.70343 -0.00684 -0.02737 -0.01737 391 SER A O   
1464 C CB  . SER A 188 ? 0.26046 0.93294 0.62863 0.04285  -0.05488 -0.02706 391 SER A CB  
1465 N N   . ASN A 189 ? 0.36539 0.90752 0.68831 0.03246  -0.03553 -0.01108 392 ASN A N   
1466 C CA  . ASN A 189 ? 0.38637 0.90275 0.70252 0.02612  -0.02426 -0.01232 392 ASN A CA  
1467 C C   . ASN A 189 ? 0.38175 0.84674 0.67499 0.00831  -0.02077 -0.00227 392 ASN A C   
1468 O O   . ASN A 189 ? 0.30277 0.73403 0.58766 0.00932  -0.01478 -0.00215 392 ASN A O   
1469 C CB  . ASN A 189 ? 0.39095 0.88979 0.71004 0.05389  -0.02574 -0.01710 392 ASN A CB  
1470 C CG  . ASN A 189 ? 0.47846 0.92894 0.78266 0.06951  -0.03473 -0.00775 392 ASN A CG  
1471 O OD1 . ASN A 189 ? 0.46130 0.89324 0.75269 0.06049  -0.03887 0.00233  392 ASN A OD1 
1472 N ND2 . ASN A 189 ? 0.46318 0.89136 0.76698 0.09250  -0.03777 -0.01101 392 ASN A ND2 
1473 N N   . TYR A 190 ? 0.34562 0.80632 0.62921 -0.00704 -0.02515 0.00457  393 TYR A N   
1474 C CA  . TYR A 190 ? 0.34860 0.76233 0.61031 -0.01932 -0.02380 0.01297  393 TYR A CA  
1475 C C   . TYR A 190 ? 0.26908 0.66629 0.52264 -0.03604 -0.01434 0.01065  393 TYR A C   
1476 O O   . TYR A 190 ? 0.28432 0.64057 0.52433 -0.03697 -0.01170 0.01394  393 TYR A O   
1477 C CB  . TYR A 190 ? 0.30046 0.71928 0.55372 -0.03215 -0.03101 0.01805  393 TYR A CB  
1478 C CG  . TYR A 190 ? 0.29599 0.67148 0.52642 -0.04238 -0.03099 0.02534  393 TYR A CG  
1479 C CD1 . TYR A 190 ? 0.30787 0.64664 0.52732 -0.03005 -0.03112 0.03175  393 TYR A CD1 
1480 C CD2 . TYR A 190 ? 0.27777 0.65001 0.49688 -0.06454 -0.03135 0.02534  393 TYR A CD2 
1481 C CE1 . TYR A 190 ? 0.29930 0.60548 0.49971 -0.03910 -0.03028 0.03693  393 TYR A CE1 
1482 C CE2 . TYR A 190 ? 0.26962 0.60571 0.46811 -0.07122 -0.03244 0.02985  393 TYR A CE2 
1483 C CZ  . TYR A 190 ? 0.28670 0.59317 0.47724 -0.05817 -0.03132 0.03512  393 TYR A CZ  
1484 O OH  . TYR A 190 ? 0.28219 0.55919 0.45392 -0.06463 -0.03149 0.03812  393 TYR A OH  
1485 N N   . PHE A 191 ? 0.32990 0.75885 0.59076 -0.04926 -0.00926 0.00480  394 PHE A N   
1486 C CA  . PHE A 191 ? 0.32923 0.74210 0.57790 -0.06618 -0.00143 0.00320  394 PHE A CA  
1487 C C   . PHE A 191 ? 0.33257 0.74741 0.58744 -0.05546 0.00647  -0.00383 394 PHE A C   
1488 O O   . PHE A 191 ? 0.34511 0.74959 0.58896 -0.06794 0.01286  -0.00587 394 PHE A O   
1489 C CB  . PHE A 191 ? 0.33118 0.77193 0.57814 -0.09099 -0.00015 0.00257  394 PHE A CB  
1490 C CG  . PHE A 191 ? 0.29164 0.73145 0.53202 -0.10270 -0.00918 0.00774  394 PHE A CG  
1491 C CD1 . PHE A 191 ? 0.32165 0.72038 0.53858 -0.11473 -0.01264 0.01258  394 PHE A CD1 
1492 C CD2 . PHE A 191 ? 0.27578 0.75708 0.53327 -0.10035 -0.01530 0.00623  394 PHE A CD2 
1493 C CE1 . PHE A 191 ? 0.33198 0.72877 0.54110 -0.12415 -0.02190 0.01610  394 PHE A CE1 
1494 C CE2 . PHE A 191 ? 0.33085 0.81093 0.58133 -0.11080 -0.02488 0.00999  394 PHE A CE2 
1495 C CZ  . PHE A 191 ? 0.31765 0.75443 0.54317 -0.12282 -0.02806 0.01504  394 PHE A CZ  
1496 N N   . VAL A 192 ? 0.31382 0.73911 0.58342 -0.03182 0.00508  -0.00801 395 VAL A N   
1497 C CA  . VAL A 192 ? 0.30237 0.73181 0.57790 -0.01986 0.01141  -0.01651 395 VAL A CA  
1498 C C   . VAL A 192 ? 0.30515 0.68357 0.56682 -0.01680 0.01295  -0.01545 395 VAL A C   
1499 O O   . VAL A 192 ? 0.27182 0.61733 0.52903 -0.00927 0.00798  -0.01012 395 VAL A O   
1500 C CB  . VAL A 192 ? 0.32590 0.78100 0.62038 0.00668  0.00728  -0.02297 395 VAL A CB  
1501 C CG1 . VAL A 192 ? 0.32510 0.78644 0.62453 0.01940  0.01353  -0.03363 395 VAL A CG1 
1502 C CG2 . VAL A 192 ? 0.38168 0.89205 0.69281 0.00511  0.00443  -0.02567 395 VAL A CG2 
1503 N N   . ILE A 193 ? 0.27159 0.64505 0.52633 -0.02273 0.01994  -0.02095 396 ILE A N   
1504 C CA  . ILE A 193 ? 0.32569 0.65658 0.56954 -0.01931 0.02105  -0.02290 396 ILE A CA  
1505 C C   . ILE A 193 ? 0.38736 0.72583 0.63937 -0.00166 0.02422  -0.03339 396 ILE A C   
1506 O O   . ILE A 193 ? 0.42995 0.80596 0.68813 -0.00073 0.02941  -0.03960 396 ILE A O   
1507 C CB  . ILE A 193 ? 0.37172 0.68390 0.59541 -0.04025 0.02413  -0.02124 396 ILE A CB  
1508 C CG1 . ILE A 193 ? 0.30224 0.60423 0.51649 -0.05551 0.01933  -0.01236 396 ILE A CG1 
1509 C CG2 . ILE A 193 ? 0.28651 0.55984 0.50092 -0.03507 0.02441  -0.02580 396 ILE A CG2 
1510 C CD1 . ILE A 193 ? 0.27043 0.55657 0.46302 -0.07566 0.02022  -0.01108 396 ILE A CD1 
1511 N N   . ASN A 194 ? 0.40855 0.71284 0.66066 0.01192  0.02115  -0.03599 397 ASN A N   
1512 C CA  . ASN A 194 ? 0.46623 0.76866 0.72201 0.02768  0.02294  -0.04726 397 ASN A CA  
1513 C C   . ASN A 194 ? 0.42129 0.70068 0.66158 0.01679  0.02686  -0.05090 397 ASN A C   
1514 O O   . ASN A 194 ? 0.42608 0.66886 0.65931 0.01201  0.02397  -0.04846 397 ASN A O   
1515 C CB  . ASN A 194 ? 0.46342 0.73878 0.72673 0.04778  0.01596  -0.04894 397 ASN A CB  
1516 C CG  . ASN A 194 ? 0.65414 0.92971 0.92198 0.06696  0.01578  -0.06230 397 ASN A CG  
1517 O OD1 . ASN A 194 ? 0.61713 0.85637 0.88241 0.07370  0.01250  -0.06646 397 ASN A OD1 
1518 N ND2 . ASN A 194 ? 0.59388 0.91260 0.86885 0.07544  0.01933  -0.07011 397 ASN A ND2 
1519 N N   . GLY A 195 ? 0.51901 0.82142 0.75321 0.01291  0.03337  -0.05701 398 GLY A N   
1520 C CA  . GLY A 195 ? 0.56175 0.84412 0.77643 0.00180  0.03641  -0.05961 398 GLY A CA  
1521 C C   . GLY A 195 ? 0.54829 0.80292 0.76121 0.01651  0.03393  -0.07001 398 GLY A C   
1522 O O   . GLY A 195 ? 0.54901 0.79050 0.77504 0.03282  0.02894  -0.07380 398 GLY A O   
1523 N N   . ILE A 196 ? 0.57106 0.81445 0.76547 0.01030  0.03654  -0.07480 399 ILE A N   
1524 C CA  . ILE A 196 ? 0.70213 0.91679 0.89304 0.02251  0.03269  -0.08560 399 ILE A CA  
1525 C C   . ILE A 196 ? 0.70410 0.93627 0.90497 0.04356  0.03388  -0.09705 399 ILE A C   
1526 O O   . ILE A 196 ? 0.77368 0.98529 0.98505 0.05920  0.02764  -0.10426 399 ILE A O   
1527 C CB  . ILE A 196 ? 0.67600 0.87235 0.84132 0.01179  0.03335  -0.08800 399 ILE A CB  
1528 C CG1 . ILE A 196 ? 0.72205 0.94601 0.87028 -0.00070 0.04178  -0.08414 399 ILE A CG1 
1529 C CG2 . ILE A 196 ? 0.61530 0.78165 0.77325 -0.00091 0.02771  -0.08186 399 ILE A CG2 
1530 C CD1 . ILE A 196 ? 0.71899 0.91877 0.83601 -0.01376 0.04106  -0.08313 399 ILE A CD1 
1531 N N   . ARG A 197 ? 0.61466 0.88547 0.81212 0.04403  0.04174  -0.09946 400 ARG A N   
1532 C CA  . ARG A 197 ? 0.63453 0.92951 0.84238 0.06603  0.04313  -0.11149 400 ARG A CA  
1533 C C   . ARG A 197 ? 0.63849 0.95648 0.86931 0.07815  0.04027  -0.10975 400 ARG A C   
1534 O O   . ARG A 197 ? 0.58314 0.93646 0.82321 0.09425  0.04288  -0.11867 400 ARG A O   
1535 C CB  . ARG A 197 ? 0.58161 0.91318 0.77601 0.06195  0.05398  -0.11601 400 ARG A CB  
1536 C CG  . ARG A 197 ? 0.47176 0.77948 0.64151 0.06110  0.05494  -0.12292 400 ARG A CG  
1537 N N   . ASN A 198 ? 0.61804 0.91680 0.85667 0.07206  0.03447  -0.09921 401 ASN A N   
1538 C CA  . ASN A 198 ? 0.58593 0.90062 0.84215 0.08229  0.03004  -0.09533 401 ASN A CA  
1539 C C   . ASN A 198 ? 0.55894 0.92960 0.82265 0.07742  0.03667  -0.09361 401 ASN A C   
1540 O O   . ASN A 198 ? 0.47251 0.86874 0.75211 0.09272  0.03303  -0.09603 401 ASN A O   
1541 C CB  . ASN A 198 ? 0.65781 0.95941 0.92399 0.11023  0.02207  -0.10603 401 ASN A CB  
1542 C CG  . ASN A 198 ? 0.70816 0.95385 0.97050 0.11209  0.01444  -0.10613 401 ASN A CG  
1543 O OD1 . ASN A 198 ? 0.60896 0.82879 0.86818 0.09628  0.01313  -0.09534 401 ASN A OD1 
1544 N ND2 . ASN A 198 ? 0.70289 0.93158 0.96589 0.13116  0.00935  -0.11936 401 ASN A ND2 
1545 N N   . GLU A 199 ? 0.55615 0.94588 0.80811 0.05587  0.04564  -0.08968 402 GLU A N   
1546 C CA  . GLU A 199 ? 0.58398 1.02653 0.84358 0.04507  0.05241  -0.08674 402 GLU A CA  
1547 C C   . GLU A 199 ? 0.51272 0.95349 0.77887 0.03275  0.04725  -0.07420 402 GLU A C   
1548 O O   . GLU A 199 ? 0.47331 0.87181 0.73132 0.02541  0.04160  -0.06595 402 GLU A O   
1549 C CB  . GLU A 199 ? 0.50129 0.95874 0.74214 0.02308  0.06356  -0.08534 402 GLU A CB  
1550 C CG  . GLU A 199 ? 0.58568 1.00867 0.80603 -0.00349 0.06272  -0.07283 402 GLU A CG  
1551 C CD  . GLU A 199 ? 0.58144 0.95304 0.78080 -0.00294 0.05960  -0.07479 402 GLU A CD  
1552 O OE1 . GLU A 199 ? 0.62137 0.98327 0.79661 -0.01928 0.06432  -0.07235 402 GLU A OE1 
1553 O OE2 . GLU A 199 ? 0.61864 0.95879 0.82471 0.01314  0.05183  -0.07878 402 GLU A OE2 
1554 N N   . GLN A 200 ? 0.42326 0.91332 0.70496 0.03147  0.04900  -0.07404 403 GLN A N   
1555 C CA  . GLN A 200 ? 0.44129 0.93632 0.73000 0.02169  0.04329  -0.06388 403 GLN A CA  
1556 C C   . GLN A 200 ? 0.42018 0.92969 0.69817 -0.01004 0.04971  -0.05594 403 GLN A C   
1557 O O   . GLN A 200 ? 0.39436 0.94677 0.67467 -0.02047 0.05896  -0.05985 403 GLN A O   
1558 C CB  . GLN A 200 ? 0.32204 0.86211 0.63464 0.04057  0.03884  -0.06974 403 GLN A CB  
1559 C CG  . GLN A 200 ? 0.44536 0.96808 0.76550 0.07342  0.03070  -0.07806 403 GLN A CG  
1560 C CD  . GLN A 200 ? 0.53827 1.01027 0.85331 0.07975  0.01959  -0.06866 403 GLN A CD  
1561 O OE1 . GLN A 200 ? 0.56808 0.99033 0.86887 0.07305  0.01901  -0.06349 403 GLN A OE1 
1562 N NE2 . GLN A 200 ? 0.61483 1.10079 0.94103 0.09285  0.01066  -0.06676 403 GLN A NE2 
1563 N N   . ILE A 201 ? 0.38538 0.85893 0.65060 -0.02567 0.04474  -0.04512 404 ILE A N   
1564 C CA  . ILE A 201 ? 0.37708 0.85103 0.62691 -0.05565 0.04806  -0.03729 404 ILE A CA  
1565 C C   . ILE A 201 ? 0.39559 0.86626 0.64932 -0.06397 0.03970  -0.02871 404 ILE A C   
1566 O O   . ILE A 201 ? 0.37955 0.81980 0.63403 -0.05210 0.03184  -0.02530 404 ILE A O   
1567 C CB  . ILE A 201 ? 0.46439 0.88909 0.68649 -0.06651 0.04929  -0.03458 404 ILE A CB  
1568 C CG1 . ILE A 201 ? 0.38200 0.80314 0.59935 -0.05321 0.05517  -0.04406 404 ILE A CG1 
1569 C CG2 . ILE A 201 ? 0.37771 0.80176 0.57965 -0.09646 0.05250  -0.02763 404 ILE A CG2 
1570 C CD1 . ILE A 201 ? 0.43188 0.80379 0.62319 -0.05936 0.05401  -0.04317 404 ILE A CD1 
1571 N N   . GLN A 202 ? 0.47570 0.97798 0.73098 -0.08532 0.04153  -0.02535 405 GLN A N   
1572 C CA  . GLN A 202 ? 0.46262 0.96356 0.71898 -0.09621 0.03311  -0.01807 405 GLN A CA  
1573 C C   . GLN A 202 ? 0.52931 0.99056 0.75759 -0.12071 0.03190  -0.01067 405 GLN A C   
1574 O O   . GLN A 202 ? 0.65073 1.12570 0.86939 -0.14500 0.03609  -0.00857 405 GLN A O   
1575 C CB  . GLN A 202 ? 0.50133 1.06315 0.77862 -0.10433 0.03395  -0.02076 405 GLN A CB  
1576 C CG  . GLN A 202 ? 0.55144 1.15078 0.85645 -0.07683 0.03022  -0.02828 405 GLN A CG  
1577 C CD  . GLN A 202 ? 0.69509 1.30081 1.00944 -0.07225 0.01820  -0.02448 405 GLN A CD  
1578 O OE1 . GLN A 202 ? 0.68629 1.28660 0.99220 -0.09357 0.01412  -0.01815 405 GLN A OE1 
1579 N NE2 . GLN A 202 ? 0.68603 1.30091 1.01548 -0.04350 0.01134  -0.02865 405 GLN A NE2 
1580 N N   . GLY A 203 ? 0.39816 0.81008 0.61247 -0.11455 0.02582  -0.00707 406 GLY A N   
1581 C CA  . GLY A 203 ? 0.39364 0.76410 0.58007 -0.13241 0.02287  -0.00227 406 GLY A CA  
1582 C C   . GLY A 203 ? 0.40055 0.76341 0.58186 -0.14342 0.01361  0.00364  406 GLY A C   
1583 O O   . GLY A 203 ? 0.33492 0.69735 0.52699 -0.13003 0.00774  0.00524  406 GLY A O   
1584 N N   . ARG A 204 ? 0.36450 0.71831 0.52638 -0.16798 0.01173  0.00700  407 ARG A N   
1585 C CA  . ARG A 204 ? 0.43583 0.77720 0.58806 -0.18014 0.00159  0.01141  407 ARG A CA  
1586 C C   . ARG A 204 ? 0.37431 0.66188 0.49373 -0.18892 -0.00393 0.01309  407 ARG A C   
1587 O O   . ARG A 204 ? 0.40293 0.66950 0.50476 -0.19391 0.00020  0.01192  407 ARG A O   
1588 C CB  . ARG A 204 ? 0.41146 0.79129 0.57068 -0.20253 0.00131  0.01281  407 ARG A CB  
1589 C CG  . ARG A 204 ? 0.42598 0.86719 0.61814 -0.19491 0.00840  0.00841  407 ARG A CG  
1590 C CD  . ARG A 204 ? 0.39719 0.85380 0.61269 -0.16657 0.00422  0.00607  407 ARG A CD  
1591 N NE  . ARG A 204 ? 0.37666 0.84386 0.59814 -0.16855 -0.00657 0.00827  407 ARG A NE  
1592 C CZ  . ARG A 204 ? 0.39746 0.90898 0.63800 -0.16968 -0.00898 0.00516  407 ARG A CZ  
1593 N NH1 . ARG A 204 ? 0.42962 0.97700 0.68428 -0.16691 -0.00073 -0.00059 407 ARG A NH1 
1594 N NH2 . ARG A 204 ? 0.35598 0.87009 0.59745 -0.17093 -0.02022 0.00685  407 ARG A NH2 
1595 N N   . ASP A 205 ? 0.44951 0.71476 0.55933 -0.18884 -0.01416 0.01495  408 ASP A N   
1596 C CA  . ASP A 205 ? 0.37337 0.58852 0.45526 -0.18903 -0.02075 0.01400  408 ASP A CA  
1597 C C   . ASP A 205 ? 0.40429 0.60022 0.46648 -0.20319 -0.03289 0.01583  408 ASP A C   
1598 O O   . ASP A 205 ? 0.40817 0.56802 0.45195 -0.19696 -0.04037 0.01355  408 ASP A O   
1599 C CB  . ASP A 205 ? 0.31372 0.51394 0.40379 -0.16511 -0.02014 0.01133  408 ASP A CB  
1600 C CG  . ASP A 205 ? 0.38631 0.60714 0.49562 -0.15344 -0.02245 0.01394  408 ASP A CG  
1601 O OD1 . ASP A 205 ? 0.31880 0.56215 0.43313 -0.16236 -0.02701 0.01663  408 ASP A OD1 
1602 O OD2 . ASP A 205 ? 0.29660 0.51022 0.41485 -0.13586 -0.02009 0.01338  408 ASP A OD2 
1603 N N   . ILE A 206 ? 0.43985 0.65975 0.50543 -0.22208 -0.03553 0.01861  409 ILE A N   
1604 C CA  . ILE A 206 ? 0.49222 0.69794 0.54304 -0.23375 -0.04856 0.01940  409 ILE A CA  
1605 C C   . ILE A 206 ? 0.57132 0.72223 0.58359 -0.24271 -0.05790 0.01811  409 ILE A C   
1606 O O   . ILE A 206 ? 0.51511 0.64189 0.51179 -0.24100 -0.06993 0.01603  409 ILE A O   
1607 C CB  . ILE A 206 ? 0.47776 0.72104 0.54049 -0.25537 -0.04951 0.02158  409 ILE A CB  
1608 C CG1 . ILE A 206 ? 0.50730 0.73120 0.55301 -0.26370 -0.06365 0.02121  409 ILE A CG1 
1609 C CG2 . ILE A 206 ? 0.54147 0.78190 0.59143 -0.27170 -0.04113 0.02359  409 ILE A CG2 
1610 C CD1 . ILE A 206 ? 0.61502 0.85393 0.67558 -0.24805 -0.07081 0.01968  409 ILE A CD1 
1611 N N   . SER A 207 ? 0.47556 0.60455 0.46967 -0.25037 -0.05363 0.01856  410 SER A N   
1612 C CA  . SER A 207 ? 0.53044 0.60361 0.48486 -0.25609 -0.06416 0.01675  410 SER A CA  
1613 C C   . SER A 207 ? 0.53012 0.57643 0.47558 -0.23638 -0.06151 0.01190  410 SER A C   
1614 O O   . SER A 207 ? 0.61066 0.61380 0.52291 -0.24076 -0.06818 0.01022  410 SER A O   
1615 C CB  . SER A 207 ? 0.74597 0.80531 0.67603 -0.28571 -0.06545 0.02191  410 SER A CB  
1616 O OG  . SER A 207 ? 0.86803 0.94190 0.80250 -0.28858 -0.05185 0.02430  410 SER A OG  
1617 N N   . GLN A 208 ? 0.46715 0.53563 0.44004 -0.21457 -0.05337 0.00909  411 GLN A N   
1618 C CA  . GLN A 208 ? 0.47374 0.52329 0.44364 -0.19701 -0.05000 0.00352  411 GLN A CA  
1619 C C   . GLN A 208 ? 0.49048 0.51676 0.45466 -0.17964 -0.05806 -0.00335 411 GLN A C   
1620 O O   . GLN A 208 ? 0.40104 0.43112 0.38024 -0.16186 -0.05273 -0.00801 411 GLN A O   
1621 C CB  . GLN A 208 ? 0.45836 0.54401 0.46089 -0.18495 -0.03616 0.00377  411 GLN A CB  
1622 C CG  . GLN A 208 ? 0.45958 0.56496 0.46460 -0.19644 -0.02656 0.00692  411 GLN A CG  
1623 C CD  . GLN A 208 ? 0.45478 0.57913 0.48219 -0.17897 -0.01574 0.00327  411 GLN A CD  
1624 O OE1 . GLN A 208 ? 0.38487 0.51842 0.43398 -0.16120 -0.01411 0.00070  411 GLN A OE1 
1625 N NE2 . GLN A 208 ? 0.47654 0.60445 0.49631 -0.18452 -0.00867 0.00306  411 GLN A NE2 
1626 N N   . CYS A 209 ? 0.38785 0.47375 0.45685 -0.17018 0.01153  -0.01683 412 CYS A N   
1627 C CA  . CYS A 209 ? 0.40211 0.46486 0.45800 -0.15577 0.00296  -0.01105 412 CYS A CA  
1628 C C   . CYS A 209 ? 0.37511 0.40673 0.40866 -0.14738 0.00547  -0.00169 412 CYS A C   
1629 O O   . CYS A 209 ? 0.36365 0.38991 0.39551 -0.13109 -0.00076 0.00264  412 CYS A O   
1630 C CB  . CYS A 209 ? 0.50131 0.54755 0.54657 -0.16449 -0.00028 -0.01442 412 CYS A CB  
1631 S SG  . CYS A 209 ? 0.78035 0.79309 0.80028 -0.18815 0.01047  -0.01539 412 CYS A SG  
1632 N N   . TRP A 210 ? 0.34242 0.35404 0.35807 -0.15827 0.01464  0.00108  413 TRP A N   
1633 C CA  . TRP A 210 ? 0.33876 0.32513 0.33370 -0.14844 0.01589  0.00940  413 TRP A CA  
1634 C C   . TRP A 210 ? 0.31887 0.32802 0.32966 -0.13469 0.01346  0.01062  413 TRP A C   
1635 O O   . TRP A 210 ? 0.31313 0.31089 0.31576 -0.12061 0.00885  0.01550  413 TRP A O   
1636 C CB  . TRP A 210 ? 0.38317 0.34568 0.35480 -0.16269 0.02694  0.01211  413 TRP A CB  
1637 C CG  . TRP A 210 ? 0.45452 0.44457 0.44223 -0.17554 0.03614  0.00702  413 TRP A CG  
1638 C CD1 . TRP A 210 ? 0.44315 0.45363 0.44576 -0.19377 0.04196  -0.00141 413 TRP A CD1 
1639 C CD2 . TRP A 210 ? 0.39909 0.40252 0.39124 -0.17115 0.04086  0.00860  413 TRP A CD2 
1640 N NE1 . TRP A 210 ? 0.46573 0.50315 0.48314 -0.20026 0.05041  -0.00526 413 TRP A NE1 
1641 C CE2 . TRP A 210 ? 0.43266 0.46472 0.44290 -0.18639 0.05008  0.00104  413 TRP A CE2 
1642 C CE3 . TRP A 210 ? 0.44278 0.43850 0.42605 -0.15601 0.03810  0.01455  413 TRP A CE3 
1643 C CZ2 . TRP A 210 ? 0.51813 0.56885 0.53615 -0.18621 0.05733  -0.00018 413 TRP A CZ2 
1644 C CZ3 . TRP A 210 ? 0.42854 0.44136 0.41834 -0.15663 0.04474  0.01337  413 TRP A CZ3 
1645 C CH2 . TRP A 210 ? 0.46107 0.50004 0.46741 -0.17122 0.05457  0.00633  413 TRP A CH2 
1646 N N   . ALA A 211 ? 0.33015 0.37212 0.36377 -0.13854 0.01666  0.00530  414 ALA A N   
1647 C CA  . ALA A 211 ? 0.31986 0.38015 0.36613 -0.12626 0.01552  0.00586  414 ALA A CA  
1648 C C   . ALA A 211 ? 0.27915 0.35131 0.33936 -0.11151 0.00604  0.00523  414 ALA A C   
1649 O O   . ALA A 211 ? 0.26943 0.34190 0.33051 -0.09958 0.00380  0.00778  414 ALA A O   
1650 C CB  . ALA A 211 ? 0.31016 0.40003 0.37452 -0.13379 0.02284  -0.00008 414 ALA A CB  
1651 N N   . LYS A 212 ? 0.28846 0.36966 0.35816 -0.11284 0.00083  0.00145  415 LYS A N   
1652 C CA  . LYS A 212 ? 0.28994 0.37688 0.36734 -0.09917 -0.00741 0.00172  415 LYS A CA  
1653 C C   . LYS A 212 ? 0.27738 0.33869 0.33833 -0.09103 -0.01061 0.00727  415 LYS A C   
1654 O O   . LYS A 212 ? 0.25856 0.32140 0.32244 -0.07953 -0.01341 0.00905  415 LYS A O   
1655 C CB  . LYS A 212 ? 0.25343 0.35322 0.34042 -0.10231 -0.01283 -0.00355 415 LYS A CB  
1656 C CG  . LYS A 212 ? 0.22416 0.35540 0.33086 -0.10945 -0.01093 -0.01098 415 LYS A CG  
1657 C CD  . LYS A 212 ? 0.21284 0.36539 0.33437 -0.09827 -0.01046 -0.01193 415 LYS A CD  
1658 C CE  . LYS A 212 ? 0.23731 0.42478 0.38028 -0.10415 -0.00853 -0.02067 415 LYS A CE  
1659 N NZ  . LYS A 212 ? 0.24908 0.45766 0.40637 -0.09179 -0.00785 -0.02265 415 LYS A NZ  
1660 N N   . THR A 213 ? 0.25561 0.29309 0.29880 -0.09699 -0.00972 0.00937  416 THR A N   
1661 C CA  . THR A 213 ? 0.25988 0.27459 0.28761 -0.08795 -0.01284 0.01367  416 THR A CA  
1662 C C   . THR A 213 ? 0.30640 0.31818 0.32954 -0.08066 -0.01127 0.01711  416 THR A C   
1663 O O   . THR A 213 ? 0.30764 0.31871 0.33154 -0.06968 -0.01494 0.01817  416 THR A O   
1664 C CB  . THR A 213 ? 0.32122 0.30820 0.32797 -0.09518 -0.01154 0.01503  416 THR A CB  
1665 O OG1 . THR A 213 ? 0.32793 0.31785 0.33864 -0.10306 -0.01332 0.01055  416 THR A OG1 
1666 C CG2 . THR A 213 ? 0.32814 0.29326 0.31934 -0.08325 -0.01532 0.01866  416 THR A CG2 
1667 N N   . ALA A 214 ? 0.27542 0.28569 0.29289 -0.08755 -0.00544 0.01818  417 ALA A N   
1668 C CA  . ALA A 214 ? 0.28491 0.29402 0.29729 -0.08105 -0.00432 0.02060  417 ALA A CA  
1669 C C   . ALA A 214 ? 0.25551 0.28678 0.28677 -0.07319 -0.00611 0.01804  417 ALA A C   
1670 O O   . ALA A 214 ? 0.28213 0.31180 0.31178 -0.06416 -0.00903 0.01875  417 ALA A O   
1671 C CB  . ALA A 214 ? 0.29147 0.29627 0.29395 -0.09112 0.00352  0.02165  417 ALA A CB  
1672 N N   . SER A 215 ? 0.25554 0.30721 0.30418 -0.07615 -0.00458 0.01441  418 SER A N   
1673 C CA  . SER A 215 ? 0.23017 0.29762 0.29290 -0.06792 -0.00577 0.01230  418 SER A CA  
1674 C C   . SER A 215 ? 0.27772 0.33996 0.34099 -0.05925 -0.01114 0.01297  418 SER A C   
1675 O O   . SER A 215 ? 0.25898 0.32230 0.32392 -0.05285 -0.01141 0.01263  418 SER A O   
1676 C CB  . SER A 215 ? 0.21046 0.29928 0.28989 -0.06988 -0.00458 0.00817  418 SER A CB  
1677 O OG  . SER A 215 ? 0.22019 0.31898 0.30263 -0.07838 0.00179  0.00597  418 SER A OG  
1678 N N   . ASN A 216 ? 0.21489 0.27163 0.27639 -0.06001 -0.01467 0.01312  419 ASN A N   
1679 C CA  . ASN A 216 ? 0.22935 0.28067 0.28986 -0.05265 -0.01830 0.01343  419 ASN A CA  
1680 C C   . ASN A 216 ? 0.25238 0.29439 0.30500 -0.04795 -0.01867 0.01462  419 ASN A C   
1681 O O   . ASN A 216 ? 0.22602 0.27129 0.28271 -0.04244 -0.01899 0.01333  419 ASN A O   
1682 C CB  . ASN A 216 ? 0.23891 0.28241 0.29458 -0.05460 -0.02159 0.01320  419 ASN A CB  
1683 C CG  . ASN A 216 ? 0.26458 0.32045 0.32907 -0.05726 -0.02348 0.01066  419 ASN A CG  
1684 O OD1 . ASN A 216 ? 0.25415 0.32313 0.32832 -0.05308 -0.02362 0.00948  419 ASN A OD1 
1685 N ND2 . ASN A 216 ? 0.22214 0.27299 0.28201 -0.06350 -0.02552 0.00925  419 ASN A ND2 
1686 N N   . MET A 217 ? 0.23603 0.26596 0.27625 -0.05003 -0.01868 0.01661  420 MET A N   
1687 C CA  . MET A 217 ? 0.25465 0.27737 0.28670 -0.04321 -0.02091 0.01711  420 MET A CA  
1688 C C   . MET A 217 ? 0.24262 0.27545 0.27917 -0.04117 -0.01949 0.01567  420 MET A C   
1689 O O   . MET A 217 ? 0.25203 0.28884 0.29048 -0.03511 -0.02173 0.01337  420 MET A O   
1690 C CB  . MET A 217 ? 0.27519 0.27807 0.28823 -0.04423 -0.02180 0.02023  420 MET A CB  
1691 C CG  . MET A 217 ? 0.26975 0.25857 0.27551 -0.04609 -0.02323 0.02075  420 MET A CG  
1692 S SD  . MET A 217 ? 0.34952 0.30942 0.32973 -0.05195 -0.02146 0.02464  420 MET A SD  
1693 C CE  . MET A 217 ? 0.37794 0.32256 0.34154 -0.03704 -0.02676 0.02641  420 MET A CE  
1694 N N   . LEU A 218 ? 0.22476 0.26339 0.26372 -0.04656 -0.01547 0.01588  421 LEU A N   
1695 C CA  . LEU A 218 ? 0.25117 0.29800 0.29293 -0.04497 -0.01362 0.01383  421 LEU A CA  
1696 C C   . LEU A 218 ? 0.25348 0.31122 0.30884 -0.04214 -0.01286 0.01033  421 LEU A C   
1697 O O   . LEU A 218 ? 0.24778 0.30958 0.30458 -0.03970 -0.01279 0.00732  421 LEU A O   
1698 C CB  . LEU A 218 ? 0.21267 0.26215 0.25217 -0.05136 -0.00834 0.01449  421 LEU A CB  
1699 C CG  . LEU A 218 ? 0.25806 0.29205 0.27837 -0.05495 -0.00742 0.01814  421 LEU A CG  
1700 C CD1 . LEU A 218 ? 0.23747 0.27349 0.25648 -0.06511 -0.00024 0.01863  421 LEU A CD1 
1701 C CD2 . LEU A 218 ? 0.23770 0.26684 0.24588 -0.04927 -0.00982 0.01813  421 LEU A CD2 
1702 N N   . HIS A 219 ? 0.24017 0.30133 0.30363 -0.04270 -0.01221 0.01033  422 HIS A N   
1703 C CA  . HIS A 219 ? 0.20233 0.26728 0.27320 -0.03946 -0.01106 0.00795  422 HIS A CA  
1704 C C   . HIS A 219 ? 0.25041 0.31274 0.32019 -0.03697 -0.01258 0.00607  422 HIS A C   
1705 O O   . HIS A 219 ? 0.29483 0.36007 0.36759 -0.03662 -0.01045 0.00256  422 HIS A O   
1706 C CB  . HIS A 219 ? 0.20492 0.27094 0.28028 -0.03846 -0.01159 0.00890  422 HIS A CB  
1707 C CG  . HIS A 219 ? 0.21059 0.28517 0.29213 -0.03794 -0.00959 0.00804  422 HIS A CG  
1708 N ND1 . HIS A 219 ? 0.21247 0.28879 0.29647 -0.03459 -0.00632 0.00590  422 HIS A ND1 
1709 C CD2 . HIS A 219 ? 0.21915 0.30238 0.30561 -0.03997 -0.01034 0.00797  422 HIS A CD2 
1710 C CE1 . HIS A 219 ? 0.16778 0.25355 0.25789 -0.03268 -0.00543 0.00484  422 HIS A CE1 
1711 N NE2 . HIS A 219 ? 0.17952 0.27200 0.27268 -0.03633 -0.00789 0.00568  422 HIS A NE2 
1712 N N   . TRP A 220 ? 0.22849 0.28590 0.29412 -0.03565 -0.01580 0.00741  423 TRP A N   
1713 C CA  . TRP A 220 ? 0.21832 0.27697 0.28465 -0.03236 -0.01721 0.00450  423 TRP A CA  
1714 C C   . TRP A 220 ? 0.19685 0.26163 0.26256 -0.03063 -0.01880 0.00126  423 TRP A C   
1715 O O   . TRP A 220 ? 0.23126 0.30445 0.30335 -0.03032 -0.01786 -0.00393 423 TRP A O   
1716 C CB  . TRP A 220 ? 0.20326 0.25424 0.26340 -0.02967 -0.02057 0.00634  423 TRP A CB  
1717 C CG  . TRP A 220 ? 0.22488 0.27913 0.28544 -0.02409 -0.02284 0.00275  423 TRP A CG  
1718 C CD1 . TRP A 220 ? 0.21862 0.27780 0.28512 -0.02273 -0.02083 -0.00089 423 TRP A CD1 
1719 C CD2 . TRP A 220 ? 0.21550 0.26941 0.26987 -0.01818 -0.02753 0.00186  423 TRP A CD2 
1720 N NE1 . TRP A 220 ? 0.19035 0.25594 0.25796 -0.01637 -0.02388 -0.00494 423 TRP A NE1 
1721 C CE2 . TRP A 220 ? 0.21652 0.27869 0.27630 -0.01236 -0.02891 -0.00319 423 TRP A CE2 
1722 C CE3 . TRP A 220 ? 0.24920 0.29579 0.29220 -0.01668 -0.03054 0.00481  423 TRP A CE3 
1723 C CZ2 . TRP A 220 ? 0.27531 0.34111 0.33132 -0.00320 -0.03463 -0.00591 423 TRP A CZ2 
1724 C CZ3 . TRP A 220 ? 0.28039 0.32608 0.31579 -0.00778 -0.03616 0.00329  423 TRP A CZ3 
1725 C CH2 . TRP A 220 ? 0.28686 0.34325 0.32965 -0.00019 -0.03888 -0.00228 423 TRP A CH2 
1726 N N   . TRP A 221 ? 0.19646 0.25712 0.25346 -0.03021 -0.02095 0.00375  424 TRP A N   
1727 C CA  . TRP A 221 ? 0.20194 0.26712 0.25462 -0.02723 -0.02389 0.00098  424 TRP A CA  
1728 C C   . TRP A 221 ? 0.17932 0.25386 0.23901 -0.03074 -0.02052 -0.00364 424 TRP A C   
1729 O O   . TRP A 221 ? 0.20362 0.28793 0.26729 -0.02945 -0.02237 -0.00959 424 TRP A O   
1730 C CB  . TRP A 221 ? 0.21446 0.26799 0.25143 -0.02687 -0.02550 0.00588  424 TRP A CB  
1731 C CG  . TRP A 221 ? 0.23990 0.29261 0.26546 -0.02095 -0.03065 0.00467  424 TRP A CG  
1732 C CD1 . TRP A 221 ? 0.25648 0.30370 0.27240 -0.01207 -0.03721 0.00497  424 TRP A CD1 
1733 C CD2 . TRP A 221 ? 0.24515 0.30174 0.26542 -0.02204 -0.03033 0.00278  424 TRP A CD2 
1734 N NE1 . TRP A 221 ? 0.31001 0.35777 0.31430 -0.00678 -0.04194 0.00369  424 TRP A NE1 
1735 C CE2 . TRP A 221 ? 0.24841 0.30202 0.25505 -0.01353 -0.03767 0.00220  424 TRP A CE2 
1736 C CE3 . TRP A 221 ? 0.26763 0.32949 0.29229 -0.02825 -0.02478 0.00105  424 TRP A CE3 
1737 C CZ2 . TRP A 221 ? 0.29649 0.35224 0.29268 -0.01191 -0.03998 0.00013  424 TRP A CZ2 
1738 C CZ3 . TRP A 221 ? 0.33204 0.39573 0.34716 -0.02736 -0.02603 -0.00139 424 TRP A CZ3 
1739 C CH2 . TRP A 221 ? 0.29124 0.35202 0.29191 -0.01964 -0.03377 -0.00178 424 TRP A CH2 
1740 N N   . PHE A 222 ? 0.21519 0.28755 0.27682 -0.03500 -0.01557 -0.00198 425 PHE A N   
1741 C CA  . PHE A 222 ? 0.22506 0.30214 0.29113 -0.03766 -0.01163 -0.00654 425 PHE A CA  
1742 C C   . PHE A 222 ? 0.27931 0.35964 0.35360 -0.03923 -0.00943 -0.01133 425 PHE A C   
1743 O O   . PHE A 222 ? 0.24019 0.32525 0.31687 -0.04200 -0.00769 -0.01750 425 PHE A O   
1744 C CB  . PHE A 222 ? 0.22239 0.29651 0.28942 -0.03949 -0.00680 -0.00417 425 PHE A CB  
1745 C CG  . PHE A 222 ? 0.21150 0.28608 0.27147 -0.04065 -0.00551 -0.00334 425 PHE A CG  
1746 C CD1 . PHE A 222 ? 0.22952 0.29987 0.28068 -0.04130 -0.00739 0.00109  425 PHE A CD1 
1747 C CD2 . PHE A 222 ? 0.27671 0.35343 0.33659 -0.04158 -0.00140 -0.00716 425 PHE A CD2 
1748 C CE1 . PHE A 222 ? 0.29178 0.36065 0.33376 -0.04364 -0.00461 0.00198  425 PHE A CE1 
1749 C CE2 . PHE A 222 ? 0.30383 0.38112 0.35609 -0.04292 0.00090  -0.00681 425 PHE A CE2 
1750 C CZ  . PHE A 222 ? 0.30413 0.37783 0.34729 -0.04437 -0.00037 -0.00208 425 PHE A CZ  
1751 N N   . GLU A 223 ? 0.24336 0.32028 0.32065 -0.03860 -0.00882 -0.00910 426 GLU A N   
1752 C CA  . GLU A 223 ? 0.17843 0.25599 0.26093 -0.04140 -0.00493 -0.01323 426 GLU A CA  
1753 C C   . GLU A 223 ? 0.20728 0.29740 0.29521 -0.04146 -0.00748 -0.01957 426 GLU A C   
1754 O O   . GLU A 223 ? 0.26957 0.36603 0.36289 -0.04662 -0.00390 -0.02665 426 GLU A O   
1755 C CB  . GLU A 223 ? 0.22211 0.29135 0.30334 -0.04021 -0.00343 -0.00879 426 GLU A CB  
1756 C CG  . GLU A 223 ? 0.22442 0.28998 0.30687 -0.04382 0.00233  -0.01195 426 GLU A CG  
1757 C CD  . GLU A 223 ? 0.36421 0.41974 0.44295 -0.04738 0.00863  -0.01342 426 GLU A CD  
1758 O OE1 . GLU A 223 ? 0.32283 0.37429 0.39876 -0.04485 0.00805  -0.01106 426 GLU A OE1 
1759 O OE2 . GLU A 223 ? 0.33254 0.38319 0.41021 -0.05286 0.01496  -0.01736 426 GLU A OE2 
1760 N N   . GLN A 224 ? 0.20711 0.30117 0.29355 -0.03565 -0.01356 -0.01795 427 GLN A N   
1761 C CA  . GLN A 224 ? 0.23366 0.34294 0.32647 -0.03284 -0.01725 -0.02484 427 GLN A CA  
1762 C C   . GLN A 224 ? 0.30086 0.42145 0.39484 -0.03367 -0.02028 -0.03102 427 GLN A C   
1763 O O   . GLN A 224 ? 0.28295 0.42043 0.38678 -0.03576 -0.02065 -0.04021 427 GLN A O   
1764 C CB  . GLN A 224 ? 0.22438 0.33180 0.31174 -0.02370 -0.02392 -0.02149 427 GLN A CB  
1765 C CG  . GLN A 224 ? 0.25251 0.34850 0.33710 -0.02270 -0.02186 -0.01634 427 GLN A CG  
1766 C CD  . GLN A 224 ? 0.31671 0.41526 0.40918 -0.02838 -0.01465 -0.01948 427 GLN A CD  
1767 O OE1 . GLN A 224 ? 0.36905 0.48130 0.47071 -0.02899 -0.01275 -0.02673 427 GLN A OE1 
1768 N NE2 . GLN A 224 ? 0.38379 0.46942 0.47191 -0.03252 -0.01031 -0.01446 427 GLN A NE2 
1769 N N   . ASN A 225 ? 0.22164 0.33450 0.30576 -0.03278 -0.02210 -0.02703 428 ASN A N   
1770 C CA  . ASN A 225 ? 0.23290 0.35436 0.31441 -0.03291 -0.02553 -0.03251 428 ASN A CA  
1771 C C   . ASN A 225 ? 0.29970 0.41818 0.38262 -0.04128 -0.01882 -0.03600 428 ASN A C   
1772 O O   . ASN A 225 ? 0.24526 0.36515 0.32177 -0.04172 -0.02057 -0.03858 428 ASN A O   
1773 C CB  . ASN A 225 ? 0.21702 0.32993 0.28282 -0.02644 -0.03114 -0.02644 428 ASN A CB  
1774 C CG  . ASN A 225 ? 0.25846 0.37406 0.31915 -0.01638 -0.03948 -0.02564 428 ASN A CG  
1775 O OD1 . ASN A 225 ? 0.30400 0.43669 0.37463 -0.01287 -0.04357 -0.03321 428 ASN A OD1 
1776 N ND2 . ASN A 225 ? 0.24583 0.34431 0.29069 -0.01163 -0.04161 -0.01706 428 ASN A ND2 
1777 N N   . LYS A 226 ? 0.26999 0.38189 0.35844 -0.04719 -0.01112 -0.03612 429 LYS A N   
1778 C CA  . LYS A 226 ? 0.28062 0.38340 0.36679 -0.05343 -0.00415 -0.03834 429 LYS A CA  
1779 C C   . LYS A 226 ? 0.28121 0.39373 0.36858 -0.05859 -0.00469 -0.04855 429 LYS A C   
1780 O O   . LYS A 226 ? 0.30205 0.40797 0.38226 -0.05999 -0.00272 -0.04966 429 LYS A O   
1781 C CB  . LYS A 226 ? 0.30092 0.39349 0.38992 -0.05818 0.00360  -0.03789 429 LYS A CB  
1782 C CG  . LYS A 226 ? 0.36794 0.44541 0.45114 -0.06288 0.01117  -0.03958 429 LYS A CG  
1783 N N   . ASP A 227 ? 0.26828 0.39826 0.36518 -0.06150 -0.00735 -0.05715 430 ASP A N   
1784 C CA  . ASP A 227 ? 0.31480 0.45687 0.41447 -0.06805 -0.00813 -0.06885 430 ASP A CA  
1785 C C   . ASP A 227 ? 0.30877 0.45825 0.40004 -0.06117 -0.01735 -0.06945 430 ASP A C   
1786 O O   . ASP A 227 ? 0.26175 0.40949 0.34690 -0.06532 -0.01647 -0.07486 430 ASP A O   
1787 C CB  . ASP A 227 ? 0.30861 0.47227 0.42352 -0.07369 -0.00838 -0.07950 430 ASP A CB  
1788 C CG  . ASP A 227 ? 0.48079 0.63420 0.60019 -0.08411 0.00331  -0.08090 430 ASP A CG  
1789 O OD1 . ASP A 227 ? 0.44632 0.57498 0.55540 -0.08735 0.01096  -0.07563 430 ASP A OD1 
1790 O OD2 . ASP A 227 ? 0.49353 0.66324 0.62560 -0.08845 0.00511  -0.08750 430 ASP A OD2 
1791 N N   . TYR A 228 ? 0.25961 0.41518 0.34788 -0.05053 -0.02605 -0.06433 431 TYR A N   
1792 C CA  . TYR A 228 ? 0.31680 0.47236 0.39082 -0.04311 -0.03398 -0.06248 431 TYR A CA  
1793 C C   . TYR A 228 ? 0.30722 0.44333 0.36793 -0.04494 -0.02817 -0.05594 431 TYR A C   
1794 O O   . TYR A 228 ? 0.29001 0.42593 0.34059 -0.04562 -0.02965 -0.05962 431 TYR A O   
1795 C CB  . TYR A 228 ? 0.29706 0.45259 0.36465 -0.03093 -0.04231 -0.05545 431 TYR A CB  
1796 C CG  . TYR A 228 ? 0.31507 0.49374 0.39331 -0.02496 -0.05083 -0.06362 431 TYR A CG  
1797 C CD1 . TYR A 228 ? 0.37874 0.57900 0.46087 -0.02485 -0.05779 -0.07558 431 TYR A CD1 
1798 C CD2 . TYR A 228 ? 0.33903 0.52001 0.42420 -0.01898 -0.05212 -0.06051 431 TYR A CD2 
1799 C CE1 . TYR A 228 ? 0.37486 0.60157 0.46972 -0.01820 -0.06624 -0.08459 431 TYR A CE1 
1800 C CE2 . TYR A 228 ? 0.38374 0.58846 0.48030 -0.01204 -0.05955 -0.06893 431 TYR A CE2 
1801 C CZ  . TYR A 228 ? 0.40959 0.63853 0.51201 -0.01129 -0.06676 -0.08105 431 TYR A CZ  
1802 O OH  . TYR A 228 ? 0.54874 0.80573 0.66514 -0.00309 -0.07466 -0.09055 431 TYR A OH  
1803 N N   . ILE A 229 ? 0.23634 0.35779 0.29738 -0.04559 -0.02149 -0.04728 432 ILE A N   
1804 C CA  . ILE A 229 ? 0.22096 0.32845 0.27221 -0.04628 -0.01593 -0.04203 432 ILE A CA  
1805 C C   . ILE A 229 ? 0.31526 0.41981 0.36697 -0.05294 -0.00965 -0.04957 432 ILE A C   
1806 O O   . ILE A 229 ? 0.30917 0.40843 0.35062 -0.05285 -0.00745 -0.05016 432 ILE A O   
1807 C CB  . ILE A 229 ? 0.25759 0.35462 0.31157 -0.04491 -0.01146 -0.03267 432 ILE A CB  
1808 C CG1 . ILE A 229 ? 0.26520 0.36117 0.31423 -0.03908 -0.01733 -0.02562 432 ILE A CG1 
1809 C CG2 . ILE A 229 ? 0.24167 0.32958 0.29019 -0.04571 -0.00497 -0.02943 432 ILE A CG2 
1810 C CD1 . ILE A 229 ? 0.22490 0.31302 0.27808 -0.03879 -0.01418 -0.01805 432 ILE A CD1 
1811 N N   . GLU A 230 ? 0.30671 0.41312 0.36834 -0.05935 -0.00599 -0.05610 433 GLU A N   
1812 C CA  . GLU A 230 ? 0.30162 0.40144 0.36072 -0.06656 0.00025  -0.06430 433 GLU A CA  
1813 C C   . GLU A 230 ? 0.34563 0.45631 0.39866 -0.06848 -0.00507 -0.07350 433 GLU A C   
1814 O O   . GLU A 230 ? 0.28243 0.38473 0.32594 -0.07060 -0.00132 -0.07727 433 GLU A O   
1815 C CB  . GLU A 230 ? 0.33456 0.43167 0.40260 -0.07499 0.00606  -0.06984 433 GLU A CB  
1816 C CG  . GLU A 230 ? 0.43722 0.52037 0.49932 -0.08327 0.01416  -0.07778 433 GLU A CG  
1817 C CD  . GLU A 230 ? 0.55675 0.61917 0.60844 -0.07773 0.02012  -0.07157 433 GLU A CD  
1818 O OE1 . GLU A 230 ? 0.61339 0.66911 0.66642 -0.07105 0.02129  -0.06179 433 GLU A OE1 
1819 O OE2 . GLU A 230 ? 0.62492 0.67956 0.66750 -0.07947 0.02324  -0.07729 433 GLU A OE2 
1820 N N   A GLN A 231 ? 0.29953 0.42942 0.35738 -0.06678 -0.01427 -0.07796 434 GLN A N   
1821 N N   B GLN A 231 ? 0.30484 0.43472 0.36268 -0.06674 -0.01428 -0.07791 434 GLN A N   
1822 C CA  A GLN A 231 ? 0.31851 0.46047 0.36909 -0.06668 -0.02150 -0.08673 434 GLN A CA  
1823 C CA  B GLN A 231 ? 0.31903 0.46106 0.36962 -0.06661 -0.02156 -0.08668 434 GLN A CA  
1824 C C   A GLN A 231 ? 0.32051 0.45349 0.35225 -0.05885 -0.02422 -0.07959 434 GLN A C   
1825 C C   B GLN A 231 ? 0.32100 0.45398 0.35276 -0.05884 -0.02422 -0.07958 434 GLN A C   
1826 O O   A GLN A 231 ? 0.35132 0.48463 0.37137 -0.06019 -0.02578 -0.08582 434 GLN A O   
1827 O O   B GLN A 231 ? 0.34608 0.47938 0.36617 -0.06021 -0.02576 -0.08583 434 GLN A O   
1828 C CB  A GLN A 231 ? 0.33343 0.50038 0.39389 -0.06373 -0.03213 -0.09317 434 GLN A CB  
1829 C CB  B GLN A 231 ? 0.33370 0.50061 0.39410 -0.06349 -0.03223 -0.09292 434 GLN A CB  
1830 C CG  A GLN A 231 ? 0.31346 0.49390 0.39327 -0.07402 -0.02835 -0.10330 434 GLN A CG  
1831 C CG  B GLN A 231 ? 0.31417 0.49443 0.39401 -0.07361 -0.02844 -0.10279 434 GLN A CG  
1832 C CD  A GLN A 231 ? 0.30811 0.51884 0.40061 -0.06984 -0.03906 -0.11130 434 GLN A CD  
1833 C CD  B GLN A 231 ? 0.35037 0.52759 0.43056 -0.08742 -0.02153 -0.11477 434 GLN A CD  
1834 O OE1 A GLN A 231 ? 0.40001 0.63087 0.49461 -0.07177 -0.04629 -0.12360 434 GLN A OE1 
1835 O OE1 B GLN A 231 ? 0.36366 0.55209 0.43917 -0.08964 -0.02718 -0.12485 434 GLN A OE1 
1836 N NE2 A GLN A 231 ? 0.39758 0.61290 0.49870 -0.06326 -0.04056 -0.10518 434 GLN A NE2 
1837 N NE2 B GLN A 231 ? 0.42296 0.58238 0.50603 -0.09651 -0.00930 -0.11380 434 GLN A NE2 
1838 N N   . TYR A 232 ? 0.23028 0.35433 0.25760 -0.05189 -0.02393 -0.06717 435 TYR A N   
1839 C CA  . TYR A 232 ? 0.29839 0.41211 0.30679 -0.04680 -0.02402 -0.06027 435 TYR A CA  
1840 C C   . TYR A 232 ? 0.34704 0.44924 0.35004 -0.05131 -0.01393 -0.06159 435 TYR A C   
1841 O O   . TYR A 232 ? 0.33550 0.43492 0.32306 -0.05098 -0.01387 -0.06456 435 TYR A O   
1842 C CB  . TYR A 232 ? 0.25861 0.36430 0.26437 -0.04116 -0.02421 -0.04777 435 TYR A CB  
1843 C CG  . TYR A 232 ? 0.25343 0.34819 0.23718 -0.03712 -0.02453 -0.04081 435 TYR A CG  
1844 C CD1 . TYR A 232 ? 0.32594 0.42085 0.29267 -0.02998 -0.03427 -0.03978 435 TYR A CD1 
1845 C CD2 . TYR A 232 ? 0.29948 0.38368 0.27824 -0.04019 -0.01475 -0.03580 435 TYR A CD2 
1846 C CE1 . TYR A 232 ? 0.35711 0.43725 0.29907 -0.02718 -0.03327 -0.03279 435 TYR A CE1 
1847 C CE2 . TYR A 232 ? 0.34368 0.41752 0.30130 -0.03877 -0.01291 -0.03003 435 TYR A CE2 
1848 C CZ  . TYR A 232 ? 0.33781 0.40736 0.27547 -0.03287 -0.02171 -0.02800 435 TYR A CZ  
1849 O OH  . TYR A 232 ? 0.41590 0.47060 0.32834 -0.03235 -0.01860 -0.02163 435 TYR A OH  
1850 N N   . LYS A 233 ? 0.33506 0.42996 0.34928 -0.05445 -0.00548 -0.05987 436 LYS A N   
1851 C CA  . LYS A 233 ? 0.36473 0.44875 0.37497 -0.05653 0.00395  -0.06218 436 LYS A CA  
1852 C C   . LYS A 233 ? 0.35206 0.43581 0.35643 -0.06200 0.00463  -0.07448 436 LYS A C   
1853 O O   . LYS A 233 ? 0.38131 0.45703 0.37514 -0.06198 0.01025  -0.07751 436 LYS A O   
1854 C CB  . LYS A 233 ? 0.35880 0.43444 0.38096 -0.05685 0.01086  -0.05886 436 LYS A CB  
1855 C CG  . LYS A 233 ? 0.35916 0.43539 0.38719 -0.05212 0.01056  -0.04786 436 LYS A CG  
1856 C CD  . LYS A 233 ? 0.42415 0.49496 0.46374 -0.05225 0.01348  -0.04557 436 LYS A CD  
1857 C CE  . LYS A 233 ? 0.41816 0.47630 0.45643 -0.05129 0.02166  -0.04842 436 LYS A CE  
1858 N NZ  . LYS A 233 ? 0.69366 0.74242 0.73810 -0.05102 0.02411  -0.04628 436 LYS A NZ  
1859 N N   . GLN A 234 ? 0.30274 0.39615 0.31410 -0.06732 -0.00050 -0.08275 437 GLN A N   
1860 C CA  . GLN A 234 ? 0.40996 0.50445 0.41561 -0.07435 -0.00030 -0.09600 437 GLN A CA  
1861 C C   . GLN A 234 ? 0.45632 0.56182 0.44815 -0.07152 -0.00941 -0.10039 437 GLN A C   
1862 O O   . GLN A 234 ? 0.44043 0.54344 0.42176 -0.07576 -0.00834 -0.11012 437 GLN A O   
1863 C CB  . GLN A 234 ? 0.37176 0.47400 0.39132 -0.08374 -0.00081 -0.10527 437 GLN A CB  
1864 C CG  . GLN A 234 ? 0.53937 0.62394 0.56541 -0.08811 0.00986  -0.10300 437 GLN A CG  
1865 C CD  . GLN A 234 ? 0.66413 0.75526 0.70274 -0.09883 0.01109  -0.11101 437 GLN A CD  
1866 O OE1 . GLN A 234 ? 0.59789 0.71246 0.64662 -0.10067 0.00297  -0.11597 437 GLN A OE1 
1867 N NE2 . GLN A 234 ? 0.79064 0.86063 0.82780 -0.10558 0.02174  -0.11257 437 GLN A NE2 
1868 N N   . LYS A 235 ? 0.34155 0.45697 0.33046 -0.06391 -0.01860 -0.09379 438 LYS A N   
1869 C CA  . LYS A 235 ? 0.33393 0.45945 0.30777 -0.05984 -0.02921 -0.09855 438 LYS A CA  
1870 C C   . LYS A 235 ? 0.42975 0.54380 0.38084 -0.05210 -0.02926 -0.08886 438 LYS A C   
1871 O O   . LYS A 235 ? 0.45598 0.56989 0.38764 -0.05046 -0.03340 -0.09365 438 LYS A O   
1872 C CB  . LYS A 235 ? 0.39729 0.54350 0.38115 -0.05564 -0.04176 -0.10106 438 LYS A CB  
1873 C CG  . LYS A 235 ? 0.40847 0.57169 0.41288 -0.06533 -0.04250 -0.11453 438 LYS A CG  
1874 C CD  . LYS A 235 ? 0.43827 0.62748 0.45419 -0.05993 -0.05528 -0.11906 438 LYS A CD  
1875 C CE  . LYS A 235 ? 0.45586 0.66207 0.49705 -0.07131 -0.05223 -0.13037 438 LYS A CE  
1876 N NZ  . LYS A 235 ? 0.52389 0.73881 0.56693 -0.08408 -0.05108 -0.14715 438 LYS A NZ  
1877 N N   . ALA A 236 ? 0.35350 0.45756 0.30511 -0.04834 -0.02432 -0.07606 439 ALA A N   
1878 C CA  . ALA A 236 ? 0.36665 0.45879 0.29627 -0.04332 -0.02262 -0.06682 439 ALA A CA  
1879 C C   . ALA A 236 ? 0.32546 0.40711 0.24604 -0.04725 -0.01063 -0.06822 439 ALA A C   
1880 O O   . ALA A 236 ? 0.35754 0.43790 0.29113 -0.05189 -0.00269 -0.07318 439 ALA A O   
1881 C CB  . ALA A 236 ? 0.35513 0.44106 0.28967 -0.04009 -0.02078 -0.05408 439 ALA A CB  
1882 N N   . ALA A 237 ? 0.36100 0.43359 0.25715 -0.04472 -0.00884 -0.06382 440 ALA A N   
1883 C CA  . ALA A 237 ? 0.38021 0.44432 0.26667 -0.04773 0.00374  -0.06478 440 ALA A CA  
1884 C C   . ALA A 237 ? 0.39385 0.45362 0.28862 -0.04842 0.01330  -0.05446 440 ALA A C   
1885 O O   . ALA A 237 ? 0.41277 0.46484 0.29143 -0.04787 0.01559  -0.04622 440 ALA A O   
1886 C CB  . ALA A 237 ? 0.38614 0.44286 0.24043 -0.04594 0.00223  -0.06608 440 ALA A CB  
1887 N N   . ILE A 238 ? 0.35287 0.41680 0.27156 -0.05001 0.01908  -0.05545 441 ILE A N   
1888 C CA  . ILE A 238 ? 0.33119 0.39574 0.26280 -0.05030 0.02567  -0.04708 441 ILE A CA  
1889 C C   . ILE A 238 ? 0.32156 0.38431 0.24480 -0.05208 0.03803  -0.04625 441 ILE A C   
1890 O O   . ILE A 238 ? 0.35228 0.41509 0.27303 -0.05190 0.04476  -0.05385 441 ILE A O   
1891 C CB  . ILE A 238 ? 0.32290 0.39195 0.27982 -0.04981 0.02713  -0.04904 441 ILE A CB  
1892 C CG1 . ILE A 238 ? 0.31592 0.38783 0.28080 -0.04993 0.01701  -0.05187 441 ILE A CG1 
1893 C CG2 . ILE A 238 ? 0.34903 0.42121 0.31936 -0.04943 0.03129  -0.04086 441 ILE A CG2 
1894 C CD1 . ILE A 238 ? 0.31682 0.39119 0.28669 -0.04826 0.01007  -0.04385 441 ILE A CD1 
1895 N N   . GLU A 239 ? 0.35623 0.41736 0.27527 -0.05442 0.04198  -0.03781 442 GLU A N   
1896 C CA  . GLU A 239 ? 0.33433 0.39745 0.24862 -0.05799 0.05532  -0.03754 442 GLU A CA  
1897 C C   . GLU A 239 ? 0.35133 0.42716 0.29182 -0.05608 0.06273  -0.04171 442 GLU A C   
1898 O O   . GLU A 239 ? 0.35765 0.43887 0.31856 -0.05418 0.05884  -0.03913 442 GLU A O   
1899 C CB  . GLU A 239 ? 0.38572 0.44315 0.28977 -0.06321 0.05822  -0.02811 442 GLU A CB  
1900 C CG  . GLU A 239 ? 0.41808 0.47729 0.31289 -0.06950 0.07307  -0.02843 442 GLU A CG  
1901 C CD  . GLU A 239 ? 0.53823 0.58545 0.41526 -0.07709 0.07669  -0.01921 442 GLU A CD  
1902 O OE1 . GLU A 239 ? 0.52797 0.56324 0.39751 -0.07536 0.06641  -0.01247 442 GLU A OE1 
1903 O OE2 . GLU A 239 ? 0.54368 0.59278 0.41380 -0.08503 0.09056  -0.01924 442 GLU A OE2 
1904 N N   . GLU A 240 ? 0.35395 0.43403 0.29223 -0.05532 0.07315  -0.04843 443 GLU A N   
1905 C CA  . GLU A 240 ? 0.31678 0.40628 0.27645 -0.04954 0.07824  -0.05449 443 GLU A CA  
1906 C C   . GLU A 240 ? 0.44749 0.55017 0.43080 -0.04886 0.07942  -0.04989 443 GLU A C   
1907 O O   . GLU A 240 ? 0.37603 0.48062 0.37641 -0.04306 0.07486  -0.05047 443 GLU A O   
1908 C CB  . GLU A 240 ? 0.35563 0.44925 0.30863 -0.04801 0.09052  -0.06231 443 GLU A CB  
1909 C CG  . GLU A 240 ? 0.40244 0.50442 0.37600 -0.03904 0.09532  -0.06881 443 GLU A CG  
1910 C CD  . GLU A 240 ? 0.48440 0.59286 0.45367 -0.03573 0.10827  -0.07737 443 GLU A CD  
1911 O OE1 . GLU A 240 ? 0.49303 0.58949 0.44271 -0.03576 0.11011  -0.08344 443 GLU A OE1 
1912 O OE2 . GLU A 240 ? 0.55341 0.68069 0.53954 -0.03294 0.11660  -0.07899 443 GLU A OE2 
1913 N N   . TRP A 241 ? 0.40332 0.51401 0.38622 -0.05548 0.08553  -0.04554 444 TRP A N   
1914 C CA  . TRP A 241 ? 0.39878 0.52542 0.40540 -0.05560 0.08688  -0.04329 444 TRP A CA  
1915 C C   . TRP A 241 ? 0.37972 0.50072 0.39457 -0.05472 0.07504  -0.03686 444 TRP A C   
1916 O O   . TRP A 241 ? 0.40370 0.53612 0.43932 -0.05122 0.07328  -0.03661 444 TRP A O   
1917 C CB  . TRP A 241 ? 0.38928 0.52579 0.39322 -0.06594 0.09721  -0.04127 444 TRP A CB  
1918 C CG  . TRP A 241 ? 0.36986 0.49128 0.35526 -0.07580 0.09427  -0.03231 444 TRP A CG  
1919 C CD1 . TRP A 241 ? 0.44154 0.54588 0.39687 -0.08176 0.09741  -0.02914 444 TRP A CD1 
1920 C CD2 . TRP A 241 ? 0.36445 0.48409 0.35739 -0.07985 0.08799  -0.02556 444 TRP A CD2 
1921 N NE1 . TRP A 241 ? 0.48642 0.57636 0.42898 -0.08828 0.09331  -0.02043 444 TRP A NE1 
1922 C CE2 . TRP A 241 ? 0.38277 0.48201 0.34861 -0.08775 0.08789  -0.01843 444 TRP A CE2 
1923 C CE3 . TRP A 241 ? 0.38135 0.51267 0.39882 -0.07687 0.08224  -0.02495 444 TRP A CE3 
1924 C CZ2 . TRP A 241 ? 0.38672 0.47598 0.34974 -0.09279 0.08278  -0.01112 444 TRP A CZ2 
1925 C CZ3 . TRP A 241 ? 0.41511 0.53865 0.43073 -0.08285 0.07708  -0.01805 444 TRP A CZ3 
1926 C CH2 . TRP A 241 ? 0.40695 0.50910 0.39574 -0.09070 0.07759  -0.01139 444 TRP A CH2 
1927 N N   . LYS A 242 ? 0.31741 0.42226 0.31653 -0.05659 0.06651  -0.03248 445 LYS A N   
1928 C CA  . LYS A 242 ? 0.35561 0.45595 0.36193 -0.05582 0.05626  -0.02690 445 LYS A CA  
1929 C C   . LYS A 242 ? 0.35284 0.45077 0.36995 -0.04871 0.04987  -0.03015 445 LYS A C   
1930 O O   . LYS A 242 ? 0.33621 0.43228 0.36157 -0.04773 0.04281  -0.02631 445 LYS A O   
1931 C CB  . LYS A 242 ? 0.38819 0.47384 0.37372 -0.05931 0.04955  -0.02128 445 LYS A CB  
1932 C CG  . LYS A 242 ? 0.41501 0.49476 0.38321 -0.06716 0.05568  -0.01622 445 LYS A CG  
1933 C CD  . LYS A 242 ? 0.34950 0.41076 0.29389 -0.06713 0.04747  -0.01026 445 LYS A CD  
1934 C CE  . LYS A 242 ? 0.42703 0.47542 0.34750 -0.07510 0.05492  -0.00469 445 LYS A CE  
1935 N NZ  . LYS A 242 ? 0.41123 0.43839 0.30715 -0.07249 0.04577  0.00214  445 LYS A NZ  
1936 N N   . ARG A 243 ? 0.32272 0.41840 0.33794 -0.04448 0.05297  -0.03728 446 ARG A N   
1937 C CA  . ARG A 243 ? 0.33269 0.42058 0.35293 -0.04011 0.04805  -0.04058 446 ARG A CA  
1938 C C   . ARG A 243 ? 0.36241 0.45285 0.39973 -0.03586 0.04524  -0.03738 446 ARG A C   
1939 O O   . ARG A 243 ? 0.33225 0.41508 0.37102 -0.03620 0.03901  -0.03607 446 ARG A O   
1940 C CB  . ARG A 243 ? 0.29997 0.38258 0.31488 -0.03626 0.05398  -0.04931 446 ARG A CB  
1941 C CG  . ARG A 243 ? 0.34100 0.41823 0.33602 -0.04042 0.05494  -0.05389 446 ARG A CG  
1942 C CD  . ARG A 243 ? 0.34347 0.41298 0.33204 -0.03703 0.06075  -0.06364 446 ARG A CD  
1943 N NE  . ARG A 243 ? 0.40646 0.46433 0.39934 -0.03555 0.05733  -0.06726 446 ARG A NE  
1944 C CZ  . ARG A 243 ? 0.37771 0.42866 0.36432 -0.04109 0.05093  -0.07046 446 ARG A CZ  
1945 N NH1 . ARG A 243 ? 0.34457 0.39936 0.31946 -0.04611 0.04572  -0.07120 446 ARG A NH1 
1946 N NH2 . ARG A 243 ? 0.38775 0.42787 0.37926 -0.04156 0.04981  -0.07338 446 ARG A NH2 
1947 N N   . PRO A 244 ? 0.34630 0.44825 0.39648 -0.03181 0.04921  -0.03664 447 PRO A N   
1948 C CA  . PRO A 244 ? 0.40653 0.50973 0.47000 -0.02663 0.04494  -0.03368 447 PRO A CA  
1949 C C   . PRO A 244 ? 0.42795 0.53131 0.49400 -0.03180 0.03801  -0.02674 447 PRO A C   
1950 O O   . PRO A 244 ? 0.37779 0.47851 0.45107 -0.02813 0.03368  -0.02436 447 PRO A O   
1951 C CB  . PRO A 244 ? 0.38573 0.50647 0.46250 -0.02091 0.05007  -0.03592 447 PRO A CB  
1952 C CG  . PRO A 244 ? 0.40058 0.52550 0.47106 -0.02103 0.05858  -0.04189 447 PRO A CG  
1953 C CD  . PRO A 244 ? 0.37305 0.48881 0.42678 -0.03065 0.05800  -0.04009 447 PRO A CD  
1954 N N   . LEU A 245 ? 0.34226 0.44599 0.40011 -0.03932 0.03694  -0.02341 448 LEU A N   
1955 C CA  . LEU A 245 ? 0.32943 0.43176 0.38841 -0.04318 0.03105  -0.01717 448 LEU A CA  
1956 C C   . LEU A 245 ? 0.35132 0.44261 0.40452 -0.04315 0.02386  -0.01587 448 LEU A C   
1957 O O   . LEU A 245 ? 0.33581 0.42478 0.38878 -0.04506 0.01883  -0.01121 448 LEU A O   
1958 C CB  . LEU A 245 ? 0.29610 0.39980 0.34583 -0.05074 0.03372  -0.01377 448 LEU A CB  
1959 C CG  . LEU A 245 ? 0.40100 0.51917 0.45945 -0.05473 0.04097  -0.01448 448 LEU A CG  
1960 C CD1 . LEU A 245 ? 0.49900 0.62643 0.55881 -0.05267 0.04959  -0.02072 448 LEU A CD1 
1961 C CD2 . LEU A 245 ? 0.44515 0.55781 0.49158 -0.06460 0.04298  -0.00965 448 LEU A CD2 
1962 N N   . TYR A 246 ? 0.25693 0.34229 0.30585 -0.04153 0.02359  -0.02077 449 TYR A N   
1963 C CA  . TYR A 246 ? 0.29594 0.37590 0.34106 -0.04295 0.01733  -0.02154 449 TYR A CA  
1964 C C   . TYR A 246 ? 0.38115 0.45684 0.43523 -0.04115 0.01617  -0.02230 449 TYR A C   
1965 O O   . TYR A 246 ? 0.41038 0.48087 0.46318 -0.04259 0.01624  -0.02738 449 TYR A O   
1966 C CB  . TYR A 246 ? 0.28227 0.36002 0.31660 -0.04460 0.01734  -0.02775 449 TYR A CB  
1967 C CG  . TYR A 246 ? 0.31163 0.39012 0.33169 -0.04622 0.01591  -0.02560 449 TYR A CG  
1968 C CD1 . TYR A 246 ? 0.25131 0.32865 0.26382 -0.04596 0.00807  -0.02304 449 TYR A CD1 
1969 C CD2 . TYR A 246 ? 0.29031 0.36949 0.30289 -0.04719 0.02276  -0.02600 449 TYR A CD2 
1970 C CE1 . TYR A 246 ? 0.30669 0.37965 0.30110 -0.04603 0.00649  -0.02014 449 TYR A CE1 
1971 C CE2 . TYR A 246 ? 0.29856 0.37430 0.29351 -0.04936 0.02265  -0.02327 449 TYR A CE2 
1972 C CZ  . TYR A 246 ? 0.30173 0.37242 0.28617 -0.04846 0.01418  -0.01983 449 TYR A CZ  
1973 O OH  . TYR A 246 ? 0.35118 0.41367 0.31364 -0.04923 0.01380  -0.01626 449 TYR A OH  
1974 N N   . LYS A 247 ? 0.34767 0.42493 0.40954 -0.03892 0.01548  -0.01753 450 LYS A N   
1975 C CA  . LYS A 247 ? 0.34166 0.41280 0.40877 -0.03677 0.01454  -0.01675 450 LYS A CA  
1976 C C   . LYS A 247 ? 0.31955 0.39522 0.39254 -0.03537 0.01152  -0.01093 450 LYS A C   
1977 O O   . LYS A 247 ? 0.25606 0.33947 0.33034 -0.03665 0.01156  -0.00858 450 LYS A O   
1978 C CB  . LYS A 247 ? 0.34260 0.40570 0.40934 -0.03207 0.01962  -0.02002 450 LYS A CB  
1979 C CG  . LYS A 247 ? 0.43848 0.50972 0.50993 -0.02628 0.02233  -0.01934 450 LYS A CG  
1980 C CD  . LYS A 247 ? 0.49437 0.55620 0.56375 -0.01834 0.02665  -0.02278 450 LYS A CD  
1981 C CE  . LYS A 247 ? 0.50077 0.57651 0.57839 -0.01092 0.02836  -0.02312 450 LYS A CE  
1982 N NZ  . LYS A 247 ? 0.69498 0.76113 0.76976 0.00035  0.03152  -0.02638 450 LYS A NZ  
1983 N N   . HIS A 248 ? 0.26952 0.33952 0.34481 -0.03379 0.00960  -0.00913 451 HIS A N   
1984 C CA  . HIS A 248 ? 0.33900 0.41283 0.41905 -0.03184 0.00667  -0.00470 451 HIS A CA  
1985 C C   . HIS A 248 ? 0.31332 0.37920 0.39345 -0.02603 0.00721  -0.00418 451 HIS A C   
1986 O O   . HIS A 248 ? 0.33576 0.38950 0.41056 -0.02649 0.00916  -0.00553 451 HIS A O   
1987 C CB  . HIS A 248 ? 0.23906 0.31279 0.31777 -0.03548 0.00215  -0.00173 451 HIS A CB  
1988 C CG  . HIS A 248 ? 0.32244 0.38889 0.40003 -0.03539 0.00100  -0.00197 451 HIS A CG  
1989 N ND1 . HIS A 248 ? 0.26201 0.32605 0.34017 -0.03432 -0.00172 0.00114  451 HIS A ND1 
1990 C CD2 . HIS A 248 ? 0.29270 0.35488 0.36861 -0.03745 0.00295  -0.00580 451 HIS A CD2 
1991 C CE1 . HIS A 248 ? 0.30886 0.36709 0.38530 -0.03527 -0.00069 -0.00035 451 HIS A CE1 
1992 N NE2 . HIS A 248 ? 0.28397 0.34184 0.35996 -0.03778 0.00236  -0.00481 451 HIS A NE2 
1993 N N   . ASP A 249 ? 0.27316 0.34584 0.35826 -0.02071 0.00579  -0.00281 452 ASP A N   
1994 C CA  . ASP A 249 ? 0.26593 0.33068 0.34844 -0.01252 0.00467  -0.00166 452 ASP A CA  
1995 C C   . ASP A 249 ? 0.28637 0.35900 0.37312 -0.01173 -0.00106 0.00137  452 ASP A C   
1996 O O   . ASP A 249 ? 0.26937 0.35872 0.36515 -0.01338 -0.00295 0.00067  452 ASP A O   
1997 C CB  . ASP A 249 ? 0.33053 0.39801 0.41475 -0.00340 0.00697  -0.00450 452 ASP A CB  
1998 C CG  . ASP A 249 ? 0.50716 0.56333 0.58463 -0.00396 0.01312  -0.00835 452 ASP A CG  
1999 O OD1 . ASP A 249 ? 0.45691 0.49579 0.52504 -0.00786 0.01554  -0.00869 452 ASP A OD1 
2000 O OD2 . ASP A 249 ? 0.50136 0.56672 0.58295 -0.00135 0.01609  -0.01192 452 ASP A OD2 
2001 N N   . TYR A 250 ? 0.22869 0.28905 0.30812 -0.01042 -0.00306 0.00405  453 TYR A N   
2002 C CA  . TYR A 250 ? 0.28679 0.35178 0.36732 -0.00923 -0.00879 0.00638  453 TYR A CA  
2003 C C   . TYR A 250 ? 0.31466 0.36360 0.38353 -0.00083 -0.00969 0.00844  453 TYR A C   
2004 O O   . TYR A 250 ? 0.27469 0.30609 0.33291 -0.00339 -0.00613 0.00983  453 TYR A O   
2005 C CB  . TYR A 250 ? 0.23074 0.29465 0.31047 -0.01772 -0.00992 0.00780  453 TYR A CB  
2006 C CG  . TYR A 250 ? 0.25291 0.31859 0.33152 -0.01782 -0.01527 0.00951  453 TYR A CG  
2007 C CD1 . TYR A 250 ? 0.24676 0.29916 0.31523 -0.01471 -0.01615 0.01148  453 TYR A CD1 
2008 C CD2 . TYR A 250 ? 0.20875 0.28751 0.29445 -0.02255 -0.01854 0.00870  453 TYR A CD2 
2009 C CE1 . TYR A 250 ? 0.23393 0.28704 0.29952 -0.01491 -0.02114 0.01245  453 TYR A CE1 
2010 C CE2 . TYR A 250 ? 0.22932 0.30843 0.31285 -0.02383 -0.02346 0.00921  453 TYR A CE2 
2011 C CZ  . TYR A 250 ? 0.25895 0.32561 0.33247 -0.01941 -0.02517 0.01102  453 TYR A CZ  
2012 O OH  . TYR A 250 ? 0.26888 0.33524 0.33860 -0.02047 -0.03015 0.01093  453 TYR A OH  
2013 N N   . ILE A 251 ? 0.24496 0.30004 0.31500 0.00929  -0.01411 0.00817  454 ILE A N   
2014 C CA  . ILE A 251 ? 0.26783 0.30440 0.32288 0.02076  -0.01497 0.01031  454 ILE A CA  
2015 C C   . ILE A 251 ? 0.24368 0.27914 0.29241 0.02351  -0.02166 0.01289  454 ILE A C   
2016 O O   . ILE A 251 ? 0.27623 0.33163 0.33453 0.02722  -0.02901 0.01105  454 ILE A O   
2017 C CB  . ILE A 251 ? 0.25983 0.30321 0.31815 0.03389  -0.01661 0.00777  454 ILE A CB  
2018 C CG1 . ILE A 251 ? 0.36581 0.41351 0.43154 0.03041  -0.00992 0.00415  454 ILE A CG1 
2019 C CG2 . ILE A 251 ? 0.32057 0.33815 0.35788 0.04764  -0.01753 0.01079  454 ILE A CG2 
2020 C CD1 . ILE A 251 ? 0.44217 0.46545 0.49545 0.02368  -0.00202 0.00482  454 ILE A CD1 
2021 N N   . ARG A 252 ? 0.26173 0.27521 0.29444 0.02085  -0.01876 0.01625  455 ARG A N   
2022 C CA  . ARG A 252 ? 0.29431 0.30469 0.31813 0.02334  -0.02457 0.01853  455 ARG A CA  
2023 C C   . ARG A 252 ? 0.34506 0.34225 0.35215 0.03894  -0.02938 0.02090  455 ARG A C   
2024 O O   . ARG A 252 ? 0.34939 0.33034 0.34608 0.04728  -0.02599 0.02195  455 ARG A O   
2025 C CB  . ARG A 252 ? 0.38527 0.37919 0.39851 0.01410  -0.01877 0.02053  455 ARG A CB  
2026 C CG  . ARG A 252 ? 0.32449 0.33237 0.35261 0.00184  -0.01666 0.01810  455 ARG A CG  
2027 C CD  . ARG A 252 ? 0.31487 0.30953 0.33531 -0.00586 -0.00971 0.01841  455 ARG A CD  
2028 N NE  . ARG A 252 ? 0.32930 0.33759 0.36308 -0.01427 -0.00917 0.01581  455 ARG A NE  
2029 C CZ  . ARG A 252 ? 0.29142 0.30608 0.33449 -0.01901 -0.00562 0.01334  455 ARG A CZ  
2030 N NH1 . ARG A 252 ? 0.26829 0.27721 0.30999 -0.01797 -0.00131 0.01240  455 ARG A NH1 
2031 N NH2 . ARG A 252 ? 0.25766 0.28286 0.30943 -0.02417 -0.00672 0.01155  455 ARG A NH2 
2032 N N   . GLY A 253 ? 0.35481 0.35790 0.35756 0.04362  -0.03792 0.02144  456 GLY A N   
2033 C CA  . GLY A 253 ? 0.33304 0.32427 0.31726 0.05991  -0.04480 0.02380  456 GLY A CA  
2034 C C   . GLY A 253 ? 0.44528 0.46059 0.44224 0.07368  -0.05431 0.01979  456 GLY A C   
2035 O O   . GLY A 253 ? 0.40862 0.41236 0.38885 0.09097  -0.06023 0.02162  456 GLY A O   
2036 N N   . LEU A 254 ? 0.38381 0.43169 0.40865 0.06722  -0.05551 0.01410  457 LEU A N   
2037 C CA  . LEU A 254 ? 0.37412 0.45154 0.41529 0.07881  -0.06383 0.00840  457 LEU A CA  
2038 C C   . LEU A 254 ? 0.38620 0.48604 0.43316 0.08051  -0.07574 0.00473  457 LEU A C   
2039 O O   . LEU A 254 ? 0.39485 0.49390 0.44065 0.06791  -0.07612 0.00522  457 LEU A O   
2040 C CB  . LEU A 254 ? 0.35226 0.45623 0.42021 0.06923  -0.05871 0.00302  457 LEU A CB  
2041 C CG  . LEU A 254 ? 0.37692 0.46567 0.44346 0.06546  -0.04746 0.00454  457 LEU A CG  
2042 C CD1 . LEU A 254 ? 0.28547 0.40293 0.37692 0.05639  -0.04346 -0.00117 457 LEU A CD1 
2043 C CD2 . LEU A 254 ? 0.37512 0.44422 0.42599 0.08360  -0.04726 0.00612  457 LEU A CD2 
2044 N N   A GLN A 255 ? 0.38724 0.50802 0.44049 0.09686  -0.08588 0.00009  458 GLN A N   
2045 N N   B GLN A 255 ? 0.38806 0.50880 0.44126 0.09682  -0.08589 0.00010  458 GLN A N   
2046 C CA  A GLN A 255 ? 0.40069 0.55175 0.46535 0.09745  -0.09805 -0.00625 458 GLN A CA  
2047 C CA  B GLN A 255 ? 0.40191 0.55223 0.46611 0.09699  -0.09792 -0.00608 458 GLN A CA  
2048 C C   A GLN A 255 ? 0.36601 0.55338 0.46240 0.07942  -0.09544 -0.01405 458 GLN A C   
2049 C C   B GLN A 255 ? 0.36674 0.55383 0.46293 0.07937  -0.09544 -0.01399 458 GLN A C   
2050 O O   A GLN A 255 ? 0.32278 0.51616 0.43308 0.07176  -0.08598 -0.01505 458 GLN A O   
2051 O O   B GLN A 255 ? 0.31702 0.51017 0.42709 0.07193  -0.08603 -0.01500 458 GLN A O   
2052 C CB  A GLN A 255 ? 0.42612 0.59267 0.48968 0.12180  -0.11055 -0.01018 458 GLN A CB  
2053 C CB  B GLN A 255 ? 0.42720 0.59214 0.48913 0.12128  -0.11082 -0.00982 458 GLN A CB  
2054 C CG  A GLN A 255 ? 0.46803 0.59405 0.49427 0.14061  -0.11394 -0.00187 458 GLN A CG  
2055 C CG  B GLN A 255 ? 0.46939 0.59370 0.49341 0.13928  -0.11451 -0.00145 458 GLN A CG  
2056 C CD  A GLN A 255 ? 0.49937 0.63774 0.52173 0.16816  -0.12689 -0.00534 458 GLN A CD  
2057 C CD  B GLN A 255 ? 0.48903 0.58992 0.49098 0.13003  -0.11513 0.00367  458 GLN A CD  
2058 O OE1 A GLN A 255 ? 0.47153 0.65528 0.52256 0.17327  -0.13484 -0.01543 458 GLN A OE1 
2059 O OE1 B GLN A 255 ? 0.51113 0.63340 0.51989 0.12564  -0.12442 -0.00132 458 GLN A OE1 
2060 N NE2 A GLN A 255 ? 0.54004 0.63760 0.52584 0.18648  -0.12878 0.00266  458 GLN A NE2 
2061 N NE2 B GLN A 255 ? 0.54232 0.59995 0.51802 0.12612  -0.10452 0.01267  458 GLN A NE2 
2062 N N   . ASP A 256 ? 0.33327 0.54253 0.43850 0.07175  -0.10345 -0.01977 459 ASP A N   
2063 C CA  . ASP A 256 ? 0.31988 0.56167 0.45249 0.05331  -0.10071 -0.02785 459 ASP A CA  
2064 C C   . ASP A 256 ? 0.32853 0.60370 0.48647 0.05815  -0.09891 -0.03510 459 ASP A C   
2065 O O   . ASP A 256 ? 0.26897 0.55650 0.44348 0.04281  -0.08935 -0.03790 459 ASP A O   
2066 C CB  . ASP A 256 ? 0.36843 0.63185 0.50668 0.04718  -0.11142 -0.03517 459 ASP A CB  
2067 C CG  . ASP A 256 ? 0.38782 0.62263 0.50639 0.03531  -0.10990 -0.03011 459 ASP A CG  
2068 O OD1 . ASP A 256 ? 0.35863 0.55988 0.46148 0.03157  -0.10044 -0.02129 459 ASP A OD1 
2069 O OD2 . ASP A 256 ? 0.38419 0.63174 0.50367 0.02977  -0.11827 -0.03600 459 ASP A OD2 
2070 N N   . GLU A 257 ? 0.27023 0.55862 0.42931 0.08061  -0.10773 -0.03814 460 GLU A N   
2071 C CA  . GLU A 257 ? 0.29888 0.62101 0.48177 0.08965  -0.10701 -0.04613 460 GLU A CA  
2072 C C   . GLU A 257 ? 0.33788 0.64186 0.51906 0.08879  -0.09338 -0.04144 460 GLU A C   
2073 O O   . GLU A 257 ? 0.30836 0.64010 0.51032 0.09263  -0.08984 -0.04847 460 GLU A O   
2074 C CB  . GLU A 257 ? 0.30776 0.64117 0.48617 0.11830  -0.12091 -0.04928 460 GLU A CB  
2075 C CG  . GLU A 257 ? 0.41608 0.76756 0.59551 0.11800  -0.13310 -0.05506 460 GLU A CG  
2076 C CD  . GLU A 257 ? 0.46382 0.78528 0.61411 0.12156  -0.14171 -0.04776 460 GLU A CD  
2077 O OE1 . GLU A 257 ? 0.39495 0.67334 0.52167 0.11773  -0.13343 -0.03673 460 GLU A OE1 
2078 O OE2 . GLU A 257 ? 0.57609 0.90640 0.72185 0.12347  -0.15162 -0.05165 460 GLU A OE2 
2079 N N   . ASP A 258 ? 0.30581 0.56619 0.46354 0.08368  -0.08556 -0.03088 461 ASP A N   
2080 C CA  . ASP A 258 ? 0.30948 0.55126 0.46352 0.08255  -0.07350 -0.02706 461 ASP A CA  
2081 C C   . ASP A 258 ? 0.27362 0.50517 0.42938 0.05889  -0.06262 -0.02400 461 ASP A C   
2082 O O   . ASP A 258 ? 0.30418 0.51492 0.45233 0.05605  -0.05321 -0.01986 461 ASP A O   
2083 C CB  . ASP A 258 ? 0.32751 0.52704 0.45210 0.09815  -0.07306 -0.01860 461 ASP A CB  
2084 C CG  . ASP A 258 ? 0.46944 0.67399 0.58834 0.12491  -0.08306 -0.02101 461 ASP A CG  
2085 O OD1 . ASP A 258 ? 0.42043 0.65747 0.56034 0.13427  -0.08477 -0.02925 461 ASP A OD1 
2086 O OD2 . ASP A 258 ? 0.47730 0.65341 0.56976 0.13731  -0.08915 -0.01495 461 ASP A OD2 
2087 N N   . GLU A 259 ? 0.28790 0.53334 0.45245 0.04242  -0.06416 -0.02657 462 GLU A N   
2088 C CA  . GLU A 259 ? 0.22582 0.45634 0.38682 0.02230  -0.05545 -0.02278 462 GLU A CA  
2089 C C   . GLU A 259 ? 0.25925 0.49773 0.43109 0.01448  -0.04471 -0.02467 462 GLU A C   
2090 O O   . GLU A 259 ? 0.28829 0.50588 0.45093 0.00419  -0.03708 -0.01968 462 GLU A O   
2091 C CB  . GLU A 259 ? 0.25432 0.49856 0.42211 0.00730  -0.05923 -0.02655 462 GLU A CB  
2092 C CG  . GLU A 259 ? 0.24415 0.47176 0.40631 -0.01194 -0.05106 -0.02297 462 GLU A CG  
2093 C CD  . GLU A 259 ? 0.30767 0.49934 0.44751 -0.01106 -0.05058 -0.01452 462 GLU A CD  
2094 O OE1 . GLU A 259 ? 0.32792 0.50795 0.45586 0.00128  -0.05670 -0.01183 462 GLU A OE1 
2095 O OE2 . GLU A 259 ? 0.28194 0.45727 0.41535 -0.02221 -0.04395 -0.01090 462 GLU A OE2 
2096 N N   . GLY A 260 ? 0.25729 0.52683 0.44818 0.01997  -0.04411 -0.03239 463 GLY A N   
2097 C CA  . GLY A 260 ? 0.20140 0.47848 0.40085 0.01376  -0.03321 -0.03468 463 GLY A CA  
2098 C C   . GLY A 260 ? 0.26254 0.51246 0.44735 0.02306  -0.02781 -0.02942 463 GLY A C   
2099 O O   . GLY A 260 ? 0.25690 0.50620 0.44360 0.01620  -0.01840 -0.03012 463 GLY A O   
2100 N N   . LYS A 261 ? 0.29050 0.51667 0.45898 0.03759  -0.03305 -0.02457 464 LYS A N   
2101 C CA  . LYS A 261 ? 0.26743 0.46392 0.41947 0.04505  -0.02769 -0.02008 464 LYS A CA  
2102 C C   . LYS A 261 ? 0.29383 0.45704 0.42683 0.03606  -0.02541 -0.01232 464 LYS A C   
2103 O O   . LYS A 261 ? 0.30424 0.44061 0.42173 0.04105  -0.02166 -0.00884 464 LYS A O   
2104 C CB  . LYS A 261 ? 0.28350 0.47315 0.42770 0.06779  -0.03338 -0.02057 464 LYS A CB  
2105 C CG  . LYS A 261 ? 0.35156 0.57516 0.51543 0.07976  -0.03494 -0.02939 464 LYS A CG  
2106 C CD  . LYS A 261 ? 0.47760 0.69397 0.63177 0.10539  -0.04269 -0.02986 464 LYS A CD  
2107 C CE  . LYS A 261 ? 0.41532 0.64462 0.57045 0.11283  -0.05588 -0.03039 464 LYS A CE  
2108 N NZ  . LYS A 261 ? 0.48725 0.71603 0.63487 0.14099  -0.06476 -0.03238 464 LYS A NZ  
2109 N N   . LYS A 262 ? 0.25219 0.41698 0.38619 0.02263  -0.02710 -0.01043 465 LYS A N   
2110 C CA  . LYS A 262 ? 0.25809 0.39564 0.37587 0.01629  -0.02626 -0.00420 465 LYS A CA  
2111 C C   . LYS A 262 ? 0.27320 0.40072 0.38829 0.00405  -0.01858 -0.00249 465 LYS A C   
2112 O O   . LYS A 262 ? 0.25581 0.36085 0.35824 0.00358  -0.01565 0.00089  465 LYS A O   
2113 C CB  . LYS A 262 ? 0.22296 0.36482 0.34064 0.01051  -0.03273 -0.00344 465 LYS A CB  
2114 C CG  . LYS A 262 ? 0.27081 0.38673 0.37236 0.00569  -0.03185 0.00208  465 LYS A CG  
2115 C CD  . LYS A 262 ? 0.33740 0.45570 0.43603 0.00358  -0.03902 0.00218  465 LYS A CD  
2116 C CE  . LYS A 262 ? 0.32049 0.41331 0.40197 0.00189  -0.03781 0.00702  465 LYS A CE  
2117 N NZ  . LYS A 262 ? 0.27800 0.37123 0.35363 0.00251  -0.04498 0.00672  465 LYS A NZ  
2118 N N   . SER A 263 ? 0.19954 0.34294 0.32502 -0.00603 -0.01513 -0.00512 466 SER A N   
2119 C CA  . SER A 263 ? 0.21593 0.34858 0.33550 -0.01702 -0.00995 -0.00287 466 SER A CA  
2120 C C   . SER A 263 ? 0.22188 0.36597 0.34755 -0.02111 -0.00334 -0.00613 466 SER A C   
2121 O O   . SER A 263 ? 0.18529 0.34978 0.32218 -0.02568 -0.00202 -0.00975 466 SER A O   
2122 C CB  . SER A 263 ? 0.24851 0.37974 0.36617 -0.02753 -0.01242 -0.00092 466 SER A CB  
2123 O OG  . SER A 263 ? 0.23199 0.35564 0.34387 -0.03645 -0.00798 0.00068  466 SER A OG  
2124 N N   . ASN A 264 ? 0.19603 0.32777 0.31393 -0.02091 0.00135  -0.00560 467 ASN A N   
2125 C CA  . ASN A 264 ? 0.24643 0.38755 0.36720 -0.02510 0.00797  -0.00873 467 ASN A CA  
2126 C C   . ASN A 264 ? 0.27216 0.41393 0.38927 -0.03810 0.01011  -0.00690 467 ASN A C   
2127 O O   . ASN A 264 ? 0.26307 0.41850 0.38523 -0.04417 0.01536  -0.00967 467 ASN A O   
2128 C CB  . ASN A 264 ? 0.21039 0.33801 0.32231 -0.02152 0.01198  -0.00969 467 ASN A CB  
2129 C CG  . ASN A 264 ? 0.28764 0.39793 0.38792 -0.02690 0.01077  -0.00652 467 ASN A CG  
2130 O OD1 . ASN A 264 ? 0.32768 0.43034 0.42537 -0.02781 0.00627  -0.00330 467 ASN A OD1 
2131 N ND2 . ASN A 264 ? 0.28936 0.39485 0.38259 -0.02997 0.01458  -0.00822 467 ASN A ND2 
2132 N N   . ILE A 265 ? 0.20875 0.33472 0.31568 -0.04221 0.00679  -0.00251 468 ILE A N   
2133 C CA  . ILE A 265 ? 0.25230 0.37304 0.35108 -0.05250 0.00841  -0.00011 468 ILE A CA  
2134 C C   . ILE A 265 ? 0.27080 0.40370 0.37715 -0.05996 0.00876  -0.00144 468 ILE A C   
2135 O O   . ILE A 265 ? 0.28223 0.42024 0.38717 -0.06936 0.01469  -0.00261 468 ILE A O   
2136 C CB  . ILE A 265 ? 0.26089 0.36310 0.34782 -0.05240 0.00381  0.00405  468 ILE A CB  
2137 C CG1 . ILE A 265 ? 0.24522 0.33975 0.32653 -0.04744 0.00405  0.00341  468 ILE A CG1 
2138 C CG2 . ILE A 265 ? 0.20027 0.29277 0.27531 -0.06087 0.00469  0.00705  468 ILE A CG2 
2139 C CD1 . ILE A 265 ? 0.20918 0.29161 0.28321 -0.04593 -0.00059 0.00548  468 ILE A CD1 
2140 N N   . ALA A 266 ? 0.18213 0.31949 0.29544 -0.05697 0.00288  -0.00184 469 ALA A N   
2141 C CA  . ALA A 266 ? 0.26722 0.41912 0.38928 -0.06503 0.00262  -0.00492 469 ALA A CA  
2142 C C   . ALA A 266 ? 0.24766 0.42521 0.38455 -0.06703 0.00833  -0.01112 469 ALA A C   
2143 O O   . ALA A 266 ? 0.23198 0.41938 0.37219 -0.07960 0.01363  -0.01400 469 ALA A O   
2144 C CB  . ALA A 266 ? 0.17889 0.33436 0.30627 -0.05947 -0.00562 -0.00557 469 ALA A CB  
2145 N N   . ASN A 267 ? 0.23914 0.42668 0.38402 -0.05506 0.00833  -0.01372 470 ASN A N   
2146 C CA  . ASN A 267 ? 0.21223 0.42655 0.37262 -0.05450 0.01383  -0.02070 470 ASN A CA  
2147 C C   . ASN A 267 ? 0.19398 0.40690 0.34812 -0.06541 0.02445  -0.02119 470 ASN A C   
2148 O O   . ASN A 267 ? 0.20404 0.44023 0.37035 -0.07213 0.03125  -0.02735 470 ASN A O   
2149 C CB  . ASN A 267 ? 0.23525 0.45425 0.40098 -0.03721 0.01176  -0.02293 470 ASN A CB  
2150 C CG  . ASN A 267 ? 0.33750 0.56691 0.51225 -0.02567 0.00248  -0.02481 470 ASN A CG  
2151 O OD1 . ASN A 267 ? 0.28305 0.51845 0.46144 -0.03097 -0.00300 -0.02504 470 ASN A OD1 
2152 N ND2 . ASN A 267 ? 0.24240 0.47153 0.41813 -0.00921 0.00045  -0.02625 470 ASN A ND2 
2153 N N   . ILE A 268 ? 0.22581 0.41317 0.36087 -0.06707 0.02614  -0.01544 471 ILE A N   
2154 C CA  . ILE A 268 ? 0.21788 0.40033 0.34207 -0.07655 0.03558  -0.01517 471 ILE A CA  
2155 C C   . ILE A 268 ? 0.24226 0.42354 0.36171 -0.09309 0.04009  -0.01454 471 ILE A C   
2156 O O   . ILE A 268 ? 0.29169 0.48617 0.41441 -0.10333 0.04993  -0.01865 471 ILE A O   
2157 C CB  . ILE A 268 ? 0.24631 0.40257 0.35013 -0.07307 0.03426  -0.00975 471 ILE A CB  
2158 C CG1 . ILE A 268 ? 0.22295 0.38109 0.32999 -0.06083 0.03399  -0.01252 471 ILE A CG1 
2159 C CG2 . ILE A 268 ? 0.24834 0.39382 0.33459 -0.08354 0.04219  -0.00781 471 ILE A CG2 
2160 C CD1 . ILE A 268 ? 0.28436 0.46166 0.40033 -0.05987 0.04268  -0.01904 471 ILE A CD1 
2161 N N   . PHE A 269 ? 0.25825 0.42225 0.36864 -0.09657 0.03397  -0.00984 472 PHE A N   
2162 C CA  . PHE A 269 ? 0.24462 0.40366 0.34900 -0.11253 0.03783  -0.00969 472 PHE A CA  
2163 C C   . PHE A 269 ? 0.29007 0.48207 0.41757 -0.12039 0.04162  -0.01845 472 PHE A C   
2164 O O   . PHE A 269 ? 0.33217 0.52988 0.45842 -0.13633 0.05155  -0.02165 472 PHE A O   
2165 C CB  . PHE A 269 ? 0.30347 0.44140 0.39764 -0.11179 0.02927  -0.00484 472 PHE A CB  
2166 C CG  . PHE A 269 ? 0.29513 0.40122 0.36466 -0.10819 0.02728  0.00275  472 PHE A CG  
2167 C CD1 . PHE A 269 ? 0.29356 0.37628 0.34011 -0.11865 0.03289  0.00670  472 PHE A CD1 
2168 C CD2 . PHE A 269 ? 0.25483 0.35425 0.32315 -0.09427 0.02004  0.00541  472 PHE A CD2 
2169 C CE1 . PHE A 269 ? 0.25770 0.31249 0.28089 -0.11265 0.02960  0.01321  472 PHE A CE1 
2170 C CE2 . PHE A 269 ? 0.30525 0.38059 0.35347 -0.09021 0.01744  0.01077  472 PHE A CE2 
2171 C CZ  . PHE A 269 ? 0.24476 0.29854 0.27060 -0.09815 0.02139  0.01469  472 PHE A CZ  
2172 N N   . ARG A 270 ? 0.24854 0.46306 0.39671 -0.10933 0.03398  -0.02296 473 ARG A N   
2173 C CA  . ARG A 270 ? 0.22846 0.47831 0.40064 -0.11488 0.03487  -0.03250 473 ARG A CA  
2174 C C   . ARG A 270 ? 0.28995 0.56758 0.47659 -0.11681 0.04518  -0.03985 473 ARG A C   
2175 O O   . ARG A 270 ? 0.30053 0.59892 0.49890 -0.12693 0.05053  -0.04707 473 ARG A O   
2176 C CB  . ARG A 270 ? 0.22107 0.48506 0.40768 -0.09939 0.02235  -0.03478 473 ARG A CB  
2177 C CG  . ARG A 270 ? 0.22649 0.53126 0.43953 -0.10122 0.02046  -0.04572 473 ARG A CG  
2178 C CD  . ARG A 270 ? 0.19063 0.49997 0.40922 -0.08906 0.00644  -0.04622 473 ARG A CD  
2179 N NE  . ARG A 270 ? 0.24993 0.54813 0.46343 -0.06765 0.00021  -0.04150 473 ARG A NE  
2180 C CZ  . ARG A 270 ? 0.25701 0.57783 0.48499 -0.05140 -0.00311 -0.04660 473 ARG A CZ  
2181 N NH1 . ARG A 270 ? 0.21709 0.57786 0.46876 -0.05260 -0.00135 -0.05728 473 ARG A NH1 
2182 N NH2 . ARG A 270 ? 0.22687 0.52948 0.44478 -0.03348 -0.00787 -0.04141 473 ARG A NH2 
2183 N N   . ALA A 271 ? 0.24560 0.51827 0.42790 -0.10477 0.04744  -0.03794 474 ALA A N   
2184 C CA  . ALA A 271 ? 0.24611 0.54424 0.44089 -0.10542 0.05793  -0.04541 474 ALA A CA  
2185 C C   . ALA A 271 ? 0.26628 0.55238 0.44461 -0.12337 0.07195  -0.04395 474 ALA A C   
2186 O O   . ALA A 271 ? 0.24548 0.55044 0.43215 -0.12939 0.08129  -0.05070 474 ALA A O   
2187 C CB  . ALA A 271 ? 0.24740 0.54256 0.44161 -0.08588 0.05575  -0.04484 474 ALA A CB  
2188 N N   . TYR A 272 ? 0.32138 0.56876 0.47083 -0.12806 0.07183  -0.03419 475 TYR A N   
2189 C CA  . TYR A 272 ? 0.32839 0.55881 0.45604 -0.13968 0.08426  -0.03148 475 TYR A CA  
2190 C C   . TYR A 272 ? 0.44372 0.64479 0.54687 -0.15701 0.08821  -0.02538 475 TYR A C   
2191 O O   . TYR A 272 ? 0.46032 0.64872 0.54456 -0.16946 0.10048  -0.02399 475 TYR A O   
2192 C CB  . TYR A 272 ? 0.31609 0.52482 0.42579 -0.12654 0.08188  -0.02594 475 TYR A CB  
2193 C CG  . TYR A 272 ? 0.24723 0.47846 0.37441 -0.11153 0.08184  -0.03228 475 TYR A CG  
2194 C CD1 . TYR A 272 ? 0.32753 0.58314 0.46508 -0.11494 0.09402  -0.04031 475 TYR A CD1 
2195 C CD2 . TYR A 272 ? 0.27031 0.49629 0.40166 -0.09420 0.07072  -0.03055 475 TYR A CD2 
2196 C CE1 . TYR A 272 ? 0.33830 0.61187 0.48993 -0.09942 0.09408  -0.04650 475 TYR A CE1 
2197 C CE2 . TYR A 272 ? 0.33369 0.57436 0.47696 -0.08009 0.07112  -0.03613 475 TYR A CE2 
2198 C CZ  . TYR A 272 ? 0.44717 0.71114 0.60046 -0.08176 0.08226  -0.04406 475 TYR A CZ  
2199 O OH  . TYR A 272 ? 0.48115 0.75693 0.64449 -0.06594 0.08243  -0.04985 475 TYR A OH  
2200 N N   . SER A 273 ? 0.39521 0.58213 0.49503 -0.15793 0.07891  -0.02162 476 SER A N   
2201 C CA  . SER A 273 ? 0.46596 0.62028 0.53919 -0.17317 0.08293  -0.01586 476 SER A CA  
2202 C C   . SER A 273 ? 0.55734 0.72423 0.63971 -0.18844 0.08908  -0.02285 476 SER A C   
2203 O O   . SER A 273 ? 0.60042 0.79391 0.69891 -0.19023 0.09576  -0.03077 476 SER A O   
2204 C CB  . SER A 273 ? 0.47911 0.60594 0.53952 -0.16437 0.06983  -0.00849 476 SER A CB  
2205 O OG  . SER A 273 ? 0.60236 0.74555 0.68228 -0.16604 0.06303  -0.01316 476 SER A OG  
2206 N N   . HIS A 274 ? 0.65209 0.79738 0.72239 -0.19672 0.08580  -0.02040 477 HIS A N   
2207 C CA  . HIS A 274 ? 0.69310 0.84345 0.76673 -0.21019 0.09078  -0.02696 477 HIS A CA  
2208 C C   . HIS A 274 ? 0.78019 0.93786 0.86732 -0.20884 0.07970  -0.03014 477 HIS A C   
2209 O O   . HIS A 274 ? 0.64422 0.79001 0.72814 -0.20048 0.06965  -0.02497 477 HIS A O   
2210 C CB  . HIS A 274 ? 0.61880 0.72797 0.65600 -0.22541 0.10118  -0.02163 477 HIS A CB  
2211 C CG  . HIS A 274 ? 0.79802 0.86710 0.80979 -0.22712 0.09536  -0.01380 477 HIS A CG  
2212 N ND1 . HIS A 274 ? 0.82489 0.89050 0.83992 -0.23352 0.09096  -0.01748 477 HIS A ND1 
2213 C CD2 . HIS A 274 ? 0.79224 0.82270 0.77402 -0.22233 0.09289  -0.00288 477 HIS A CD2 
2214 C CE1 . HIS A 274 ? 0.81332 0.83905 0.80162 -0.23228 0.08648  -0.00929 477 HIS A CE1 
2215 N NE2 . HIS A 274 ? 0.80538 0.80928 0.77325 -0.22500 0.08721  -0.00019 477 HIS A NE2 
2216 N N   . ASN A 275 ? 0.89599 1.07331 0.99718 -0.21794 0.08189  -0.03919 478 ASN A N   
2217 C CA  . ASN A 275 ? 0.89279 1.07828 1.00543 -0.21867 0.07233  -0.04369 478 ASN A CA  
2218 C C   . ASN A 275 ? 0.95968 1.12668 1.05673 -0.23783 0.07950  -0.04684 478 ASN A C   
2219 O O   . ASN A 275 ? 0.96484 1.15403 1.07844 -0.24388 0.07726  -0.05604 478 ASN A O   
2220 C CB  . ASN A 275 ? 0.88059 1.11398 1.02909 -0.20843 0.06516  -0.05334 478 ASN A CB  
2221 C CG  . ASN A 275 ? 0.80562 1.04626 0.96481 -0.20048 0.05073  -0.05489 478 ASN A CG  
2222 O OD1 . ASN A 275 ? 0.81178 1.02389 0.95427 -0.19940 0.04525  -0.04803 478 ASN A OD1 
2223 N ND2 . ASN A 275 ? 0.75159 1.03033 0.93747 -0.19428 0.04434  -0.06420 478 ASN A ND2 
2224 N N   . ASN A 276 ? 0.91757 1.04231 0.98066 -0.24723 0.08813  -0.03935 479 ASN A N   
2225 C CA  . ASN A 276 ? 0.89500 0.99409 0.93689 -0.26532 0.09604  -0.04131 479 ASN A CA  
2226 C C   . ASN A 276 ? 0.86754 0.96193 0.91212 -0.26721 0.08678  -0.04423 479 ASN A C   
2227 O O   . ASN A 276 ? 0.78413 0.86075 0.82124 -0.25721 0.07705  -0.03791 479 ASN A O   
2228 C CB  . ASN A 276 ? 0.92183 0.96887 0.92146 -0.26966 0.10376  -0.03047 479 ASN A CB  
2229 C CG  . ASN A 276 ? 1.12715 1.13775 1.09827 -0.28606 0.11065  -0.03092 479 ASN A CG  
2230 O OD1 . ASN A 276 ? 1.05252 1.08010 1.03523 -0.29941 0.11481  -0.04083 479 ASN A OD1 
2231 N ND2 . ASN A 276 ? 1.18922 1.14850 1.12144 -0.28452 0.11180  -0.02042 479 ASN A ND2 
2232 N N   . ALA A 277 ? 0.86245 0.97334 0.91736 -0.28073 0.09017  -0.05453 480 ALA A N   
2233 C CA  . ALA A 277 ? 0.88807 0.99830 0.94698 -0.28350 0.08154  -0.05902 480 ALA A CA  
2234 C C   . ALA A 277 ? 0.91524 0.97146 0.93769 -0.28669 0.08130  -0.05061 480 ALA A C   
2235 O O   . ALA A 277 ? 0.88969 0.93896 0.91224 -0.28202 0.07120  -0.05068 480 ALA A O   
2236 C CB  . ALA A 277 ? 0.75694 0.89186 0.82980 -0.30000 0.08711  -0.07201 480 ALA A CB  
2237 N N   . ARG A 278 ? 0.96046 0.97673 0.94973 -0.29342 0.09202  -0.04342 481 ARG A N   
2238 C CA  . ARG A 278 ? 1.04613 1.00776 0.99751 -0.29322 0.09138  -0.03474 481 ARG A CA  
2239 C C   . ARG A 278 ? 1.07754 1.02852 1.02679 -0.27419 0.07956  -0.02584 481 ARG A C   
2240 O O   . ARG A 278 ? 1.09517 1.01318 1.02441 -0.27048 0.07399  -0.02164 481 ARG A O   
2241 C CB  . ARG A 278 ? 1.10581 1.02692 1.02027 -0.30153 0.10459  -0.02845 481 ARG A CB  
2242 N N   . GLY A 279 ? 1.00753 0.98581 0.97675 -0.26217 0.07595  -0.02352 482 GLY A N   
2243 C CA  . GLY A 279 ? 0.87992 0.85050 0.84796 -0.24558 0.06576  -0.01577 482 GLY A CA  
2244 C C   . GLY A 279 ? 0.78234 0.73269 0.73096 -0.23903 0.07019  -0.00600 482 GLY A C   
2245 O O   . GLY A 279 ? 0.84384 0.80050 0.79030 -0.24479 0.08010  -0.00656 482 GLY A O   
2246 N N   . GLY A 280 ? 0.72441 0.65051 0.65805 -0.22693 0.06268  0.00258  483 GLY A N   
2247 C CA  . GLY A 280 ? 0.60093 0.50521 0.51333 -0.21896 0.06463  0.01240  483 GLY A CA  
2248 C C   . GLY A 280 ? 0.62320 0.49644 0.51632 -0.20126 0.05364  0.01984  483 GLY A C   
2249 O O   . GLY A 280 ? 0.67981 0.53954 0.56899 -0.20172 0.04849  0.01808  483 GLY A O   
2250 N N   . TYR A 281 ? 0.56700 0.43246 0.44998 -0.18342 0.04932  0.02686  484 TYR A N   
2251 C CA  . TYR A 281 ? 0.57453 0.41324 0.43913 -0.16353 0.03888  0.03314  484 TYR A CA  
2252 C C   . TYR A 281 ? 0.50468 0.37274 0.39209 -0.14347 0.02910  0.03333  484 TYR A C   
2253 O O   . TYR A 281 ? 0.46870 0.35619 0.36540 -0.14169 0.03186  0.03335  484 TYR A O   
2254 C CB  . TYR A 281 ? 0.63960 0.43019 0.45961 -0.16105 0.04293  0.04184  484 TYR A CB  
2255 C CG  . TYR A 281 ? 0.72581 0.47797 0.51569 -0.18180 0.05438  0.04267  484 TYR A CG  
2256 C CD1 . TYR A 281 ? 0.74358 0.46266 0.51470 -0.18263 0.05176  0.04296  484 TYR A CD1 
2257 C CD2 . TYR A 281 ? 0.78936 0.53728 0.56840 -0.20079 0.06869  0.04247  484 TYR A CD2 
2258 C CE1 . TYR A 281 ? 0.84134 0.52981 0.58785 -0.19765 0.06129  0.04144  484 TYR A CE1 
2259 C CE2 . TYR A 281 ? 0.76298 0.48548 0.52090 -0.21271 0.07723  0.03982  484 TYR A CE2 
2260 C CZ  . TYR A 281 ? 0.88754 0.58026 0.62910 -0.21148 0.07349  0.03939  484 TYR A CZ  
2261 O OH  . TYR A 281 ? 0.98544 0.65167 0.70449 -0.22438 0.08248  0.03641  484 TYR A OH  
2262 N N   . ILE A 282 ? 0.47881 0.34774 0.37304 -0.12913 0.01863  0.03309  485 ILE A N   
2263 C CA  . ILE A 282 ? 0.43979 0.33326 0.35364 -0.11156 0.01018  0.03276  485 ILE A CA  
2264 C C   . ILE A 282 ? 0.51601 0.40156 0.41514 -0.10191 0.00984  0.03754  485 ILE A C   
2265 O O   . ILE A 282 ? 0.45668 0.36794 0.37309 -0.09707 0.00903  0.03585  485 ILE A O   
2266 C CB  . ILE A 282 ? 0.42947 0.31650 0.34439 -0.09825 0.00086  0.03246  485 ILE A CB  
2267 C CG1 . ILE A 282 ? 0.42190 0.31635 0.34939 -0.10721 0.00042  0.02732  485 ILE A CG1 
2268 C CG2 . ILE A 282 ? 0.38121 0.29256 0.31495 -0.08214 -0.00615 0.03162  485 ILE A CG2 
2269 C CD1 . ILE A 282 ? 0.41162 0.28387 0.32644 -0.09868 -0.00539 0.02759  485 ILE A CD1 
2270 N N   . GLU A 283 ? 0.48525 0.33319 0.35009 -0.09791 0.00979  0.04330  486 GLU A N   
2271 C CA  . GLU A 283 ? 0.54390 0.38284 0.39158 -0.08561 0.00679  0.04766  486 GLU A CA  
2272 C C   . GLU A 283 ? 0.48513 0.33343 0.33160 -0.09576 0.01560  0.04799  486 GLU A C   
2273 O O   . GLU A 283 ? 0.47358 0.33209 0.32028 -0.08625 0.01250  0.04855  486 GLU A O   
2274 C CB  . GLU A 283 ? 0.51285 0.30618 0.31990 -0.07801 0.00459  0.05405  486 GLU A CB  
2275 C CG  . GLU A 283 ? 0.58456 0.34278 0.36380 -0.09582 0.01547  0.05718  486 GLU A CG  
2276 C CD  . GLU A 283 ? 0.70127 0.44729 0.48228 -0.10230 0.01547  0.05446  486 GLU A CD  
2277 O OE1 . GLU A 283 ? 0.65826 0.43160 0.46868 -0.09673 0.00891  0.04933  486 GLU A OE1 
2278 O OE2 . GLU A 283 ? 0.70074 0.40769 0.45150 -0.11332 0.02240  0.05729  486 GLU A OE2 
2279 N N   . ASP A 284 ? 0.49309 0.33893 0.33807 -0.11547 0.02700  0.04673  487 ASP A N   
2280 C CA  . ASP A 284 ? 0.50573 0.36390 0.35176 -0.12570 0.03693  0.04586  487 ASP A CA  
2281 C C   . ASP A 284 ? 0.50606 0.40876 0.38913 -0.12065 0.03427  0.03987  487 ASP A C   
2282 O O   . ASP A 284 ? 0.48198 0.39382 0.36392 -0.11623 0.03570  0.03997  487 ASP A O   
2283 C CB  . ASP A 284 ? 0.52170 0.37448 0.36383 -0.14942 0.05066  0.04363  487 ASP A CB  
2284 C CG  . ASP A 284 ? 0.69027 0.49177 0.48840 -0.15749 0.05669  0.05008  487 ASP A CG  
2285 O OD1 . ASP A 284 ? 0.69933 0.46781 0.46814 -0.14235 0.04928  0.05686  487 ASP A OD1 
2286 O OD2 . ASP A 284 ? 0.72114 0.51542 0.51375 -0.17930 0.06922  0.04775  487 ASP A OD2 
2287 N N   . GLY A 285 ? 0.46298 0.39126 0.37654 -0.12072 0.03033  0.03456  488 GLY A N   
2288 C CA  . GLY A 285 ? 0.37063 0.33602 0.31558 -0.11494 0.02799  0.02935  488 GLY A CA  
2289 C C   . GLY A 285 ? 0.35259 0.32036 0.29795 -0.09759 0.01908  0.03074  488 GLY A C   
2290 O O   . GLY A 285 ? 0.40624 0.39288 0.36321 -0.09357 0.01987  0.02807  488 GLY A O   
2291 N N   . LEU A 286 ? 0.36609 0.31535 0.29889 -0.08736 0.01083  0.03395  489 LEU A N   
2292 C CA  . LEU A 286 ? 0.43582 0.38979 0.36978 -0.07190 0.00238  0.03384  489 LEU A CA  
2293 C C   . LEU A 286 ? 0.41145 0.35610 0.32499 -0.06893 0.00383  0.03620  489 LEU A C   
2294 O O   . LEU A 286 ? 0.36121 0.32302 0.28461 -0.06291 0.00149  0.03304  489 LEU A O   
2295 C CB  . LEU A 286 ? 0.32510 0.26322 0.25020 -0.06136 -0.00616 0.03571  489 LEU A CB  
2296 C CG  . LEU A 286 ? 0.35531 0.30378 0.30010 -0.06156 -0.00892 0.03271  489 LEU A CG  
2297 C CD1 . LEU A 286 ? 0.33531 0.26690 0.26864 -0.05041 -0.01617 0.03409  489 LEU A CD1 
2298 C CD2 . LEU A 286 ? 0.27089 0.25014 0.24452 -0.05837 -0.01054 0.02778  489 LEU A CD2 
2299 N N   . THR A 287 ? 0.40210 0.31708 0.28439 -0.07324 0.00780  0.04162  490 THR A N   
2300 C CA  . THR A 287 ? 0.47016 0.37308 0.32809 -0.07041 0.00939  0.04442  490 THR A CA  
2301 C C   . THR A 287 ? 0.46369 0.38921 0.33555 -0.07898 0.01798  0.04041  490 THR A C   
2302 O O   . THR A 287 ? 0.47703 0.41281 0.34902 -0.07202 0.01530  0.03822  490 THR A O   
2303 C CB  . THR A 287 ? 0.54876 0.41145 0.36720 -0.07607 0.01473  0.05157  490 THR A CB  
2304 O OG1 . THR A 287 ? 0.49869 0.33820 0.30298 -0.06626 0.00660  0.05490  490 THR A OG1 
2305 C CG2 . THR A 287 ? 0.50810 0.35491 0.29591 -0.07143 0.01562  0.05519  490 THR A CG2 
2306 N N   . TRP A 288 ? 0.39179 0.32657 0.27603 -0.09398 0.02828  0.03837  491 TRP A N   
2307 C CA  . TRP A 288 ? 0.46887 0.42733 0.36844 -0.10185 0.03752  0.03353  491 TRP A CA  
2308 C C   . TRP A 288 ? 0.45347 0.43943 0.37802 -0.09131 0.03170  0.02803  491 TRP A C   
2309 O O   . TRP A 288 ? 0.39596 0.39147 0.32015 -0.09066 0.03578  0.02521  491 TRP A O   
2310 C CB  . TRP A 288 ? 0.40385 0.37619 0.32202 -0.11660 0.04597  0.03005  491 TRP A CB  
2311 C CG  . TRP A 288 ? 0.39200 0.39088 0.32785 -0.12548 0.05658  0.02402  491 TRP A CG  
2312 C CD1 . TRP A 288 ? 0.43496 0.42891 0.35516 -0.13619 0.06912  0.02396  491 TRP A CD1 
2313 C CD2 . TRP A 288 ? 0.35211 0.38636 0.32378 -0.12433 0.05634  0.01674  491 TRP A CD2 
2314 N NE1 . TRP A 288 ? 0.40095 0.42839 0.34801 -0.14147 0.07684  0.01619  491 TRP A NE1 
2315 C CE2 . TRP A 288 ? 0.37263 0.42476 0.35114 -0.13326 0.06847  0.01178  491 TRP A CE2 
2316 C CE3 . TRP A 288 ? 0.35631 0.40778 0.35305 -0.11556 0.04713  0.01393  491 TRP A CE3 
2317 C CZ2 . TRP A 288 ? 0.38814 0.47578 0.39877 -0.13187 0.07057  0.00379  491 TRP A CZ2 
2318 C CZ3 . TRP A 288 ? 0.30757 0.39066 0.33290 -0.11457 0.04912  0.00701  491 TRP A CZ3 
2319 C CH2 . TRP A 288 ? 0.33047 0.43204 0.36320 -0.12176 0.06024  0.00182  491 TRP A CH2 
2320 N N   . TYR A 289 ? 0.38835 0.38521 0.33285 -0.08374 0.02311  0.02615  492 TYR A N   
2321 C CA  . TYR A 289 ? 0.32496 0.34419 0.29137 -0.07572 0.01914  0.02088  492 TYR A CA  
2322 C C   . TYR A 289 ? 0.35793 0.37192 0.31250 -0.06543 0.01221  0.02056  492 TYR A C   
2323 O O   . TYR A 289 ? 0.36765 0.39621 0.33297 -0.06196 0.01212  0.01559  492 TYR A O   
2324 C CB  . TYR A 289 ? 0.31339 0.34334 0.30166 -0.07195 0.01332  0.01916  492 TYR A CB  
2325 C CG  . TYR A 289 ? 0.27032 0.32371 0.28345 -0.07014 0.01498  0.01369  492 TYR A CG  
2326 C CD1 . TYR A 289 ? 0.26601 0.33445 0.29317 -0.07683 0.02154  0.01094  492 TYR A CD1 
2327 C CD2 . TYR A 289 ? 0.24613 0.30611 0.26783 -0.06162 0.01016  0.01072  492 TYR A CD2 
2328 C CE1 . TYR A 289 ? 0.27750 0.36520 0.32488 -0.07227 0.02216  0.00610  492 TYR A CE1 
2329 C CE2 . TYR A 289 ? 0.26874 0.34408 0.30848 -0.05915 0.01212  0.00633  492 TYR A CE2 
2330 C CZ  . TYR A 289 ? 0.26442 0.35259 0.31595 -0.06316 0.01761  0.00444  492 TYR A CZ  
2331 O OH  . TYR A 289 ? 0.28549 0.38679 0.35242 -0.05791 0.01864  0.00026  492 TYR A OH  
2332 N N   . LEU A 290 ? 0.39181 0.38543 0.32406 -0.05994 0.00601  0.02499  493 LEU A N   
2333 C CA  . LEU A 290 ? 0.38905 0.38362 0.31596 -0.04812 -0.00374 0.02306  493 LEU A CA  
2334 C C   . LEU A 290 ? 0.35520 0.33603 0.25350 -0.04496 -0.00456 0.02488  493 LEU A C   
2335 O O   . LEU A 290 ? 0.42047 0.41211 0.32033 -0.03909 -0.00923 0.02001  493 LEU A O   
2336 C CB  . LEU A 290 ? 0.41671 0.40341 0.34236 -0.03968 -0.01291 0.02496  493 LEU A CB  
2337 C CG  . LEU A 290 ? 0.29761 0.29758 0.24932 -0.04016 -0.01420 0.02251  493 LEU A CG  
2338 C CD1 . LEU A 290 ? 0.35092 0.34274 0.29796 -0.03033 -0.02294 0.02356  493 LEU A CD1 
2339 C CD2 . LEU A 290 ? 0.34260 0.36636 0.31876 -0.03974 -0.01388 0.01589  493 LEU A CD2 
2340 N N   . TYR A 291 ? 0.43501 0.39077 0.30500 -0.04919 0.00005  0.03142  494 TYR A N   
2341 C CA  . TYR A 291 ? 0.47993 0.41886 0.31751 -0.04512 -0.00100 0.03395  494 TYR A CA  
2342 C C   . TYR A 291 ? 0.52566 0.43954 0.33646 -0.05683 0.01101  0.04038  494 TYR A C   
2343 O O   . TYR A 291 ? 0.56213 0.47100 0.37914 -0.06735 0.01835  0.04258  494 TYR A O   
2344 C CB  . TYR A 291 ? 0.50575 0.43275 0.32601 -0.02912 -0.01514 0.03569  494 TYR A CB  
2345 C CG  . TYR A 291 ? 0.50112 0.40525 0.30930 -0.02535 -0.01842 0.04179  494 TYR A CG  
2346 C CD1 . TYR A 291 ? 0.50965 0.42669 0.34289 -0.02137 -0.02375 0.03909  494 TYR A CD1 
2347 C CD2 . TYR A 291 ? 0.65674 0.52316 0.42512 -0.02559 -0.01565 0.05016  494 TYR A CD2 
2348 C CE1 . TYR A 291 ? 0.54734 0.44262 0.36871 -0.01729 -0.02658 0.04381  494 TYR A CE1 
2349 C CE2 . TYR A 291 ? 0.71458 0.55593 0.46918 -0.02170 -0.01835 0.05536  494 TYR A CE2 
2350 C CZ  . TYR A 291 ? 0.61601 0.47304 0.39827 -0.01722 -0.02409 0.05177  494 TYR A CZ  
2351 O OH  . TYR A 291 ? 0.70165 0.53365 0.47024 -0.01286 -0.02658 0.05601  494 TYR A OH  
2352 N N   . LYS A 292 ? 0.53826 0.43598 0.31774 -0.05580 0.01332  0.04286  495 LYS A N   
2353 C CA  . LYS A 292 ? 0.60893 0.48460 0.36218 -0.06937 0.02770  0.04784  495 LYS A CA  
2354 C C   . LYS A 292 ? 0.75394 0.58720 0.46752 -0.06745 0.02646  0.05732  495 LYS A C   
2355 O O   . LYS A 292 ? 0.76969 0.58351 0.45533 -0.05246 0.01540  0.06097  495 LYS A O   
2356 C CB  . LYS A 292 ? 0.57645 0.45344 0.31241 -0.07008 0.03262  0.04577  495 LYS A CB  
2357 C CG  . LYS A 292 ? 0.60959 0.52138 0.37937 -0.07691 0.04018  0.03699  495 LYS A CG  
2358 C CD  . LYS A 292 ? 0.70508 0.62695 0.46911 -0.06901 0.03582  0.03159  495 LYS A CD  
2359 C CE  . LYS A 292 ? 0.65487 0.55798 0.38306 -0.07507 0.04635  0.03415  495 LYS A CE  
2360 N NZ  . LYS A 292 ? 0.72876 0.64133 0.44957 -0.06760 0.04189  0.02792  495 LYS A NZ  
2361 N N   . ARG A 293 ? 0.68613 0.50456 0.39623 -0.08235 0.03763  0.06068  496 ARG A N   
2362 C CA  . ARG A 293 ? 0.80672 0.57836 0.47430 -0.08424 0.04020  0.06979  496 ARG A CA  
2363 C C   . ARG A 293 ? 0.83555 0.59318 0.48996 -0.10778 0.06026  0.07158  496 ARG A C   
2364 O O   . ARG A 293 ? 0.75617 0.54450 0.44534 -0.12213 0.06961  0.06506  496 ARG A O   
2365 C CB  . ARG A 293 ? 0.82845 0.59151 0.50446 -0.07767 0.03132  0.07130  496 ARG A CB  
2366 C CG  . ARG A 293 ? 0.97959 0.68990 0.60782 -0.07385 0.03062  0.08063  496 ARG A CG  
2367 C CD  . ARG A 293 ? 1.10823 0.81165 0.73199 -0.04973 0.01223  0.08185  496 ARG A CD  
2368 N NE  . ARG A 293 ? 1.03170 0.74801 0.65028 -0.03154 0.00007  0.08012  496 ARG A NE  
2369 C CZ  . ARG A 293 ? 1.14257 0.86375 0.76242 -0.00931 -0.01689 0.07866  496 ARG A CZ  
2370 N NH1 . ARG A 293 ? 1.20569 0.91907 0.83132 -0.00106 -0.02348 0.07913  496 ARG A NH1 
2371 N NH2 . ARG A 293 ? 1.08321 0.81943 0.69933 0.00482  -0.02737 0.07556  496 ARG A NH2 
2372 N N   . ASP A 294 ? 0.96617 0.67746 0.56945 -0.11159 0.06704  0.08001  497 ASP A N   
2373 C CA  . ASP A 294 ? 0.95252 0.64955 0.53944 -0.13593 0.08831  0.08116  497 ASP A CA  
2374 C C   . ASP A 294 ? 0.88911 0.58920 0.49632 -0.15446 0.09728  0.07856  497 ASP A C   
2375 O O   . ASP A 294 ? 0.86517 0.58368 0.48973 -0.17460 0.11276  0.07265  497 ASP A O   
2376 C CB  . ASP A 294 ? 1.05026 0.69509 0.57938 -0.13411 0.09245  0.08976  497 ASP A CB  
2377 C CG  . ASP A 294 ? 1.25686 0.89778 0.76048 -0.11922 0.08605  0.09210  497 ASP A CG  
2378 O OD1 . ASP A 294 ? 1.31091 0.94347 0.80068 -0.09668 0.06800  0.09553  497 ASP A OD1 
2379 O OD2 . ASP A 294 ? 1.30721 0.95638 0.80719 -0.12906 0.09817  0.08905  497 ASP A OD2 
2380 N N   . GLY A 295 ? 0.89345 0.58000 0.50278 -0.14633 0.08659  0.08075  498 GLY A N   
2381 C CA  . GLY A 295 ? 0.88178 0.56872 0.50726 -0.16384 0.09405  0.07776  498 GLY A CA  
2382 C C   . GLY A 295 ? 0.85963 0.60326 0.54209 -0.17394 0.09734  0.06673  498 GLY A C   
2383 O O   . GLY A 295 ? 0.83996 0.59328 0.53783 -0.19350 0.10824  0.06135  498 GLY A O   
2384 N N   . GLN A 296 ? 0.74752 0.53067 0.46326 -0.15907 0.08687  0.06186  499 GLN A N   
2385 C CA  . GLN A 296 ? 0.79212 0.62654 0.55942 -0.16392 0.08770  0.05200  499 GLN A CA  
2386 C C   . GLN A 296 ? 0.73382 0.59614 0.51387 -0.17184 0.09920  0.04652  499 GLN A C   
2387 O O   . GLN A 296 ? 0.65483 0.56002 0.47557 -0.16989 0.09775  0.03847  499 GLN A O   
2388 C CB  . GLN A 296 ? 0.65277 0.51076 0.44822 -0.14349 0.07027  0.04960  499 GLN A CB  
2389 C CG  . GLN A 296 ? 0.72792 0.57525 0.52817 -0.13900 0.06109  0.05090  499 GLN A CG  
2390 C CD  . GLN A 296 ? 0.74995 0.54743 0.50585 -0.13324 0.05771  0.05963  499 GLN A CD  
2391 O OE1 . GLN A 296 ? 0.84587 0.62588 0.57690 -0.11850 0.05097  0.06450  499 GLN A OE1 
2392 N NE2 . GLN A 296 ? 0.76622 0.53936 0.51021 -0.14442 0.06214  0.06118  499 GLN A NE2 
2393 N N   . LYS A 297 ? 0.68670 0.52356 0.43059 -0.18018 0.11102  0.05069  500 LYS A N   
2394 C CA  . LYS A 297 ? 0.78387 0.64463 0.53567 -0.18688 0.12290  0.04537  500 LYS A CA  
2395 C C   . LYS A 297 ? 0.79945 0.70163 0.59194 -0.20355 0.13446  0.03500  500 LYS A C   
2396 O O   . LYS A 297 ? 0.69965 0.64017 0.52131 -0.20032 0.13678  0.02727  500 LYS A O   
2397 C CB  . LYS A 297 ? 0.71769 0.53872 0.41917 -0.19553 0.13536  0.05197  500 LYS A CB  
2398 C CG  . LYS A 297 ? 0.89517 0.73975 0.60560 -0.20315 0.14882  0.04479  500 LYS A CG  
2399 N N   . ASN A 298 ? 0.72001 0.61764 0.51891 -0.21612 0.13810  0.03254  501 ASN A N   
2400 C CA  . ASN A 298 ? 0.72669 0.66678 0.56762 -0.22628 0.14386  0.02050  501 ASN A CA  
2401 C C   . ASN A 298 ? 0.65855 0.61894 0.53123 -0.22424 0.13344  0.01695  501 ASN A C   
2402 O O   . ASN A 298 ? 0.66714 0.64561 0.56107 -0.23382 0.13599  0.00915  501 ASN A O   
2403 C CB  . ASN A 298 ? 0.62397 0.55044 0.45118 -0.24265 0.15632  0.01704  501 ASN A CB  
2404 C CG  . ASN A 298 ? 0.74668 0.65232 0.54168 -0.24548 0.16721  0.02011  501 ASN A CG  
2405 O OD1 . ASN A 298 ? 0.82050 0.69098 0.58301 -0.25506 0.17466  0.02318  501 ASN A OD1 
2406 N ND2 . ASN A 298 ? 0.78674 0.71239 0.58882 -0.23696 0.16829  0.01897  501 ASN A ND2 
2407 N N   . LEU A 299 ? 0.66172 0.62008 0.53763 -0.21099 0.12091  0.02194  502 LEU A N   
2408 C CA  . LEU A 299 ? 0.57118 0.55185 0.47954 -0.20564 0.10948  0.01761  502 LEU A CA  
2409 C C   . LEU A 299 ? 0.58092 0.61508 0.53458 -0.20479 0.11058  0.00669  502 LEU A C   
2410 O O   . LEU A 299 ? 0.53111 0.58874 0.51140 -0.20913 0.10800  -0.00028 502 LEU A O   
2411 C CB  . LEU A 299 ? 0.57032 0.53595 0.47297 -0.18330 0.09180  0.02381  502 LEU A CB  
2412 C CG  . LEU A 299 ? 0.57534 0.54793 0.49757 -0.17704 0.07955  0.02236  502 LEU A CG  
2413 C CD1 . LEU A 299 ? 0.56174 0.50932 0.46709 -0.15850 0.06588  0.02949  502 LEU A CD1 
2414 C CD2 . LEU A 299 ? 0.58065 0.59912 0.54571 -0.17078 0.07466  0.01411  502 LEU A CD2 
2415 N N   . GLY A 300 ? 0.52468 0.57700 0.48623 -0.19525 0.11227  0.00446  503 GLY A N   
2416 C CA  . GLY A 300 ? 0.50741 0.60718 0.50832 -0.19160 0.11355  -0.00577 503 GLY A CA  
2417 C C   . GLY A 300 ? 0.52774 0.64195 0.52776 -0.19446 0.12652  -0.01006 503 GLY A C   
2418 O O   . GLY A 300 ? 0.56237 0.64921 0.53016 -0.20181 0.13562  -0.00541 503 GLY A O   
2419 N N   A SER A 301 ? 0.49351 0.64757 0.52645 -0.18570 0.12613  -0.01900 504 SER A N   
2420 N N   B SER A 301 ? 0.49562 0.64956 0.52839 -0.18570 0.12618  -0.01897 504 SER A N   
2421 C CA  A SER A 301 ? 0.46998 0.63863 0.50409 -0.18398 0.13666  -0.02423 504 SER A CA  
2422 C CA  B SER A 301 ? 0.46978 0.63825 0.50362 -0.18404 0.13676  -0.02420 504 SER A CA  
2423 C C   A SER A 301 ? 0.45967 0.61455 0.47874 -0.16867 0.13179  -0.02007 504 SER A C   
2424 C C   B SER A 301 ? 0.45845 0.61519 0.47936 -0.16808 0.13156  -0.02049 504 SER A C   
2425 O O   A SER A 301 ? 0.46232 0.62253 0.47460 -0.16849 0.14160  -0.02339 504 SER A O   
2426 O O   B SER A 301 ? 0.45763 0.62334 0.47559 -0.16667 0.14078  -0.02465 504 SER A O   
2427 C CB  A SER A 301 ? 0.41372 0.62749 0.48755 -0.17736 0.13648  -0.03613 504 SER A CB  
2428 C CB  B SER A 301 ? 0.41097 0.62427 0.48404 -0.17833 0.13716  -0.03622 504 SER A CB  
2429 O OG  A SER A 301 ? 0.44592 0.67796 0.54408 -0.16311 0.12380  -0.03778 504 SER A OG  
2430 O OG  B SER A 301 ? 0.45036 0.68340 0.54930 -0.16461 0.12440  -0.03832 504 SER A OG  
2431 N N   . ILE A 302 ? 0.47683 0.61405 0.49084 -0.15469 0.11597  -0.01385 505 ILE A N   
2432 C CA  . ILE A 302 ? 0.47925 0.59894 0.47629 -0.14038 0.10878  -0.00997 505 ILE A CA  
2433 C C   . ILE A 302 ? 0.48184 0.56610 0.45309 -0.13801 0.09842  -0.00005 505 ILE A C   
2434 O O   . ILE A 302 ? 0.42630 0.50112 0.39642 -0.14497 0.09597  0.00329  505 ILE A O   
2435 C CB  . ILE A 302 ? 0.45625 0.59673 0.47907 -0.12304 0.09950  -0.01506 505 ILE A CB  
2436 C CG1 . ILE A 302 ? 0.37530 0.51905 0.41554 -0.11694 0.08668  -0.01326 505 ILE A CG1 
2437 C CG2 . ILE A 302 ? 0.39137 0.56603 0.43851 -0.12196 0.10911  -0.02534 505 ILE A CG2 
2438 C CD1 . ILE A 302 ? 0.31410 0.47412 0.37639 -0.10111 0.07867  -0.01759 505 ILE A CD1 
2439 N N   . TYR A 303 ? 0.43295 0.49854 0.38344 -0.12764 0.09209  0.00371  506 TYR A N   
2440 C CA  . TYR A 303 ? 0.44817 0.48426 0.37600 -0.12127 0.08053  0.01175  506 TYR A CA  
2441 C C   . TYR A 303 ? 0.42402 0.46521 0.35994 -0.10508 0.06817  0.01001  506 TYR A C   
2442 O O   . TYR A 303 ? 0.42510 0.46115 0.34629 -0.09982 0.06795  0.00887  506 TYR A O   
2443 C CB  . TYR A 303 ? 0.47764 0.48097 0.36339 -0.12674 0.08578  0.01838  506 TYR A CB  
2444 C CG  . TYR A 303 ? 0.53139 0.50319 0.39365 -0.12234 0.07570  0.02681  506 TYR A CG  
2445 C CD1 . TYR A 303 ? 0.47725 0.44728 0.34327 -0.10672 0.06017  0.02792  506 TYR A CD1 
2446 C CD2 . TYR A 303 ? 0.55961 0.50353 0.39627 -0.13390 0.08234  0.03285  506 TYR A CD2 
2447 C CE1 . TYR A 303 ? 0.45969 0.40425 0.30657 -0.10071 0.05089  0.03441  506 TYR A CE1 
2448 C CE2 . TYR A 303 ? 0.55204 0.46515 0.36596 -0.12761 0.07289  0.04021  506 TYR A CE2 
2449 C CZ  . TYR A 303 ? 0.53041 0.44561 0.35060 -0.10998 0.05681  0.04076  506 TYR A CZ  
2450 O OH  . TYR A 303 ? 0.57044 0.45805 0.36999 -0.10162 0.04713  0.04697  506 TYR A OH  
2451 N N   . PRO A 304 ? 0.41212 0.46292 0.37009 -0.09791 0.05830  0.00914  507 PRO A N   
2452 C CA  . PRO A 304 ? 0.35177 0.40647 0.31712 -0.08496 0.04806  0.00686  507 PRO A CA  
2453 C C   . PRO A 304 ? 0.43888 0.47296 0.37838 -0.07859 0.04012  0.01059  507 PRO A C   
2454 O O   . PRO A 304 ? 0.39761 0.43337 0.33046 -0.07355 0.03881  0.00704  507 PRO A O   
2455 C CB  . PRO A 304 ? 0.30551 0.36807 0.29271 -0.08136 0.04054  0.00705  507 PRO A CB  
2456 C CG  . PRO A 304 ? 0.33921 0.41398 0.34009 -0.09087 0.04792  0.00583  507 PRO A CG  
2457 C CD  . PRO A 304 ? 0.37933 0.44023 0.35747 -0.10259 0.05750  0.00885  507 PRO A CD  
2458 N N   . GLY A 305 ? 0.41176 0.42672 0.33608 -0.07794 0.03433  0.01693  508 GLY A N   
2459 C CA  . GLY A 305 ? 0.42242 0.41881 0.32147 -0.06954 0.02546  0.02026  508 GLY A CA  
2460 C C   . GLY A 305 ? 0.42510 0.43476 0.33376 -0.05975 0.01719  0.01427  508 GLY A C   
2461 O O   . GLY A 305 ? 0.40886 0.41339 0.29921 -0.05592 0.01503  0.01278  508 GLY A O   
2462 N N   . LEU A 306 ? 0.37925 0.40471 0.31487 -0.05640 0.01266  0.01050  509 LEU A N   
2463 C CA  . LEU A 306 ? 0.33661 0.37748 0.28700 -0.05215 0.01012  0.00296  509 LEU A CA  
2464 C C   . LEU A 306 ? 0.36603 0.40520 0.30612 -0.04430 -0.00035 0.00016  509 LEU A C   
2465 O O   . LEU A 306 ? 0.36432 0.41260 0.30825 -0.04296 -0.00124 -0.00688 509 LEU A O   
2466 C CB  . LEU A 306 ? 0.29528 0.34902 0.27331 -0.05153 0.00926  0.00055  509 LEU A CB  
2467 C CG  . LEU A 306 ? 0.37718 0.43956 0.37022 -0.05701 0.01802  0.00053  509 LEU A CG  
2468 C CD1 . LEU A 306 ? 0.27303 0.34337 0.28743 -0.05439 0.01473  -0.00031 509 LEU A CD1 
2469 C CD2 . LEU A 306 ? 0.29487 0.36582 0.29023 -0.05820 0.02600  -0.00495 509 LEU A CD2 
2470 N N   . PHE A 307 ? 0.39169 0.42061 0.31995 -0.03864 -0.00864 0.00443  510 PHE A N   
2471 C CA  . PHE A 307 ? 0.33302 0.36527 0.25484 -0.02942 -0.02019 0.00065  510 PHE A CA  
2472 C C   . PHE A 307 ? 0.36417 0.37649 0.25284 -0.02337 -0.02512 0.00634  510 PHE A C   
2473 O O   . PHE A 307 ? 0.41976 0.42846 0.30079 -0.01326 -0.03576 0.00723  510 PHE A O   
2474 C CB  . PHE A 307 ? 0.28033 0.32257 0.22205 -0.02485 -0.02708 -0.00133 510 PHE A CB  
2475 C CG  . PHE A 307 ? 0.33322 0.38880 0.30216 -0.03065 -0.02154 -0.00509 510 PHE A CG  
2476 C CD1 . PHE A 307 ? 0.33841 0.40771 0.32012 -0.03241 -0.02101 -0.01357 510 PHE A CD1 
2477 C CD2 . PHE A 307 ? 0.32668 0.37900 0.30606 -0.03441 -0.01680 -0.00039 510 PHE A CD2 
2478 C CE1 . PHE A 307 ? 0.25834 0.33445 0.26030 -0.03680 -0.01552 -0.01622 510 PHE A CE1 
2479 C CE2 . PHE A 307 ? 0.32926 0.39178 0.33031 -0.03790 -0.01256 -0.00341 510 PHE A CE2 
2480 C CZ  . PHE A 307 ? 0.28280 0.35543 0.29369 -0.03861 -0.01170 -0.01079 510 PHE A CZ  
2481 N N   . ASN A 308 ? 0.43838 0.43666 0.30527 -0.02884 -0.01702 0.01009  511 ASN A N   
2482 C CA  . ASN A 308 ? 0.50820 0.48006 0.33757 -0.02437 -0.01939 0.01745  511 ASN A CA  
2483 C C   . ASN A 308 ? 0.52709 0.49979 0.34001 -0.01076 -0.03353 0.01411  511 ASN A C   
2484 O O   . ASN A 308 ? 0.57958 0.53397 0.36886 -0.00046 -0.04178 0.01948  511 ASN A O   
2485 C CB  . ASN A 308 ? 0.45380 0.41204 0.26235 -0.03437 -0.00632 0.02079  511 ASN A CB  
2486 C CG  . ASN A 308 ? 0.61961 0.54410 0.38431 -0.03138 -0.00666 0.02971  511 ASN A CG  
2487 O OD1 . ASN A 308 ? 0.55689 0.46095 0.31080 -0.03277 -0.00510 0.03704  511 ASN A OD1 
2488 N ND2 . ASN A 308 ? 0.56268 0.47847 0.29908 -0.02701 -0.00878 0.02903  511 ASN A ND2 
2489 N N   . ASP A 309 ? 0.46618 0.45997 0.29093 -0.00978 -0.03715 0.00456  512 ASP A N   
2490 C CA  . ASP A 309 ? 0.52761 0.52590 0.33767 0.00293  -0.05167 -0.00010 512 ASP A CA  
2491 C C   . ASP A 309 ? 0.49048 0.50755 0.32271 0.01229  -0.06394 -0.00526 512 ASP A C   
2492 O O   . ASP A 309 ? 0.49045 0.51518 0.31329 0.02451  -0.07750 -0.00999 512 ASP A O   
2493 C CB  . ASP A 309 ? 0.53580 0.54852 0.34610 -0.00024 -0.05148 -0.00968 512 ASP A CB  
2494 C CG  . ASP A 309 ? 0.52273 0.56027 0.37035 -0.00866 -0.04691 -0.01907 512 ASP A CG  
2495 O OD1 . ASP A 309 ? 0.53070 0.57065 0.40067 -0.01454 -0.03977 -0.01618 512 ASP A OD1 
2496 O OD2 . ASP A 309 ? 0.64267 0.69530 0.49491 -0.00943 -0.05050 -0.02950 512 ASP A OD2 
2497 N N   . VAL A 310 ? 0.44127 0.46715 0.30197 0.00747  -0.05974 -0.00504 513 VAL A N   
2498 C CA  . VAL A 310 ? 0.45939 0.49962 0.33717 0.01670  -0.06991 -0.00876 513 VAL A CA  
2499 C C   . VAL A 310 ? 0.47065 0.48718 0.32638 0.02754  -0.07496 0.00058  513 VAL A C   
2500 O O   . VAL A 310 ? 0.46765 0.48958 0.31893 0.04231  -0.08772 -0.00208 513 VAL A O   
2501 C CB  . VAL A 310 ? 0.37990 0.43739 0.29397 0.00762  -0.06329 -0.01267 513 VAL A CB  
2502 C CG1 . VAL A 310 ? 0.33253 0.40587 0.26387 0.01640  -0.07231 -0.01723 513 VAL A CG1 
2503 C CG2 . VAL A 310 ? 0.45495 0.53009 0.38627 -0.00220 -0.05801 -0.02173 513 VAL A CG2 
2504 N N   . PHE A 311 ? 0.49325 0.48287 0.33356 0.02079  -0.06516 0.01085  514 PHE A N   
2505 C CA  . PHE A 311 ? 0.48042 0.44311 0.29939 0.02892  -0.06809 0.01954  514 PHE A CA  
2506 C C   . PHE A 311 ? 0.60116 0.52696 0.37443 0.03145  -0.06627 0.02902  514 PHE A C   
2507 O O   . PHE A 311 ? 0.73352 0.63055 0.48332 0.03832  -0.06820 0.03671  514 PHE A O   
2508 C CB  . PHE A 311 ? 0.43364 0.39271 0.27134 0.01843  -0.05858 0.02312  514 PHE A CB  
2509 C CG  . PHE A 311 ? 0.42086 0.41073 0.29788 0.01669  -0.05990 0.01504  514 PHE A CG  
2510 C CD1 . PHE A 311 ? 0.43080 0.43137 0.31833 0.02874  -0.06962 0.01114  514 PHE A CD1 
2511 C CD2 . PHE A 311 ? 0.37184 0.37934 0.27368 0.00380  -0.05114 0.01092  514 PHE A CD2 
2512 C CE1 . PHE A 311 ? 0.40039 0.42806 0.32224 0.02564  -0.06915 0.00356  514 PHE A CE1 
2513 C CE2 . PHE A 311 ? 0.41135 0.44259 0.34499 0.00184  -0.05149 0.00408  514 PHE A CE2 
2514 C CZ  . PHE A 311 ? 0.35869 0.39974 0.30197 0.01167  -0.05987 0.00050  514 PHE A CZ  
2515 N N   . ALA A 312 ? 0.69248 0.61577 0.44965 0.02656  -0.06242 0.02852  515 ALA A N   
2516 C CA  . ALA A 312 ? 0.75770 0.64414 0.46880 0.02639  -0.05800 0.03768  515 ALA A CA  
2517 C C   . ALA A 312 ? 0.87314 0.72932 0.54697 0.04462  -0.06942 0.04441  515 ALA A C   
2518 O O   . ALA A 312 ? 1.00961 0.83024 0.65890 0.04235  -0.06338 0.05404  515 ALA A O   
2519 C CB  . ALA A 312 ? 0.78380 0.67729 0.48194 0.02444  -0.05726 0.03348  515 ALA A CB  
2520 N N   . HIS A 313 ? 0.83429 0.70321 0.50205 0.06300  -0.08597 0.03894  516 HIS A N   
2521 C CA  . HIS A 313 ? 0.96619 0.80597 0.59329 0.08409  -0.09863 0.04487  516 HIS A CA  
2522 C C   . HIS A 313 ? 0.79592 0.65525 0.44440 0.10199  -0.11327 0.03918  516 HIS A C   
2523 O O   . HIS A 313 ? 0.81054 0.67191 0.44254 0.12396  -0.12987 0.03649  516 HIS A O   
2524 C CB  . HIS A 313 ? 0.84520 0.68107 0.44021 0.09402  -0.10736 0.04338  516 HIS A CB  
2525 C CG  . HIS A 313 ? 1.03516 0.85118 0.60661 0.07713  -0.09212 0.04854  516 HIS A CG  
2526 N ND1 . HIS A 313 ? 1.07262 0.83876 0.59567 0.07368  -0.08267 0.06139  516 HIS A ND1 
2527 C CD2 . HIS A 313 ? 1.03902 0.87783 0.62845 0.06220  -0.08344 0.04205  516 HIS A CD2 
2528 C CE1 . HIS A 313 ? 1.02837 0.79052 0.54214 0.05704  -0.06858 0.06218  516 HIS A CE1 
2529 N NE2 . HIS A 313 ? 1.00254 0.80846 0.55618 0.05085  -0.06921 0.05052  516 HIS A NE2 
2530 N N   . ASP A 314 ? 0.76223 0.63640 0.44675 0.09332  -0.10714 0.03699  517 ASP A N   
2531 C CA  . ASP A 314 ? 0.64779 0.54647 0.35959 0.10681  -0.11796 0.02989  517 ASP A CA  
2532 C C   . ASP A 314 ? 0.72077 0.60051 0.43904 0.10068  -0.10924 0.03591  517 ASP A C   
2533 O O   . ASP A 314 ? 0.71169 0.55923 0.41154 0.08700  -0.09639 0.04517  517 ASP A O   
2534 C CB  . ASP A 314 ? 0.76258 0.71390 0.52187 0.10057  -0.12029 0.01586  517 ASP A CB  
2535 C CG  . ASP A 314 ? 0.81204 0.79483 0.59361 0.11821  -0.13495 0.00558  517 ASP A CG  
2536 O OD1 . ASP A 314 ? 0.77481 0.74034 0.54134 0.13499  -0.14196 0.00947  517 ASP A OD1 
2537 O OD2 . ASP A 314 ? 0.82851 0.85322 0.64255 0.11485  -0.13875 -0.00708 517 ASP A OD2 
2538 N N   . THR A 315 ? 0.71810 0.61958 0.46318 0.11018  -0.11595 0.02953  518 THR A N   
2539 C CA  . THR A 315 ? 0.71946 0.60699 0.47329 0.10508  -0.10872 0.03334  518 THR A CA  
2540 C C   . THR A 315 ? 0.68907 0.58285 0.46580 0.07937  -0.09270 0.03451  518 THR A C   
2541 O O   . THR A 315 ? 0.54647 0.47426 0.35461 0.06917  -0.08972 0.02720  518 THR A O   
2542 C CB  . THR A 315 ? 0.71249 0.63118 0.49678 0.11852  -0.11790 0.02380  518 THR A CB  
2543 O OG1 . THR A 315 ? 0.63325 0.55489 0.40047 0.14397  -0.13433 0.02040  518 THR A OG1 
2544 C CG2 . THR A 315 ? 0.60091 0.50005 0.38733 0.11693  -0.11201 0.02786  518 THR A CG2 
2545 N N   . SER A 316 ? 0.66280 0.52271 0.42217 0.06904  -0.08245 0.04328  519 SER A N   
2546 C CA  . SER A 316 ? 0.58228 0.45220 0.36720 0.04761  -0.06931 0.04297  519 SER A CA  
2547 C C   . SER A 316 ? 0.48610 0.38113 0.30607 0.04955  -0.07149 0.03646  519 SER A C   
2548 O O   . SER A 316 ? 0.54624 0.43258 0.36018 0.06377  -0.07854 0.03614  519 SER A O   
2549 C CB  . SER A 316 ? 0.53548 0.36618 0.29491 0.03500  -0.05812 0.05218  519 SER A CB  
2550 O OG  . SER A 316 ? 0.56110 0.40751 0.35021 0.01745  -0.04823 0.04994  519 SER A OG  
2551 N N   . PRO A 317 ? 0.41006 0.33502 0.26477 0.03672  -0.06554 0.03102  520 PRO A N   
2552 C CA  . PRO A 317 ? 0.42407 0.36719 0.30759 0.03607  -0.06522 0.02616  520 PRO A CA  
2553 C C   . PRO A 317 ? 0.42441 0.34566 0.30336 0.02669  -0.05765 0.03141  520 PRO A C   
2554 O O   . PRO A 317 ? 0.47516 0.40746 0.37385 0.02612  -0.05707 0.02802  520 PRO A O   
2555 C CB  . PRO A 317 ? 0.38889 0.36535 0.30406 0.02525  -0.06083 0.01960  520 PRO A CB  
2556 C CG  . PRO A 317 ? 0.40298 0.36932 0.30627 0.01353  -0.05332 0.02397  520 PRO A CG  
2557 C CD  . PRO A 317 ? 0.37577 0.31682 0.24259 0.02296  -0.05838 0.02914  520 PRO A CD  
2558 N N   . ILE A 318 ? 0.44729 0.33803 0.29999 0.01844  -0.05142 0.03890  521 ILE A N   
2559 C CA  . ILE A 318 ? 0.47210 0.34184 0.31909 0.00679  -0.04369 0.04283  521 ILE A CA  
2560 C C   . ILE A 318 ? 0.53418 0.36467 0.34722 0.01724  -0.04733 0.04799  521 ILE A C   
2561 O O   . ILE A 318 ? 0.55883 0.36437 0.33975 0.02500  -0.05008 0.05294  521 ILE A O   
2562 C CB  . ILE A 318 ? 0.55419 0.41780 0.39613 -0.01205 -0.03249 0.04619  521 ILE A CB  
2563 C CG1 . ILE A 318 ? 0.42861 0.32876 0.30076 -0.01866 -0.02980 0.04087  521 ILE A CG1 
2564 C CG2 . ILE A 318 ? 0.54817 0.39479 0.38734 -0.02602 -0.02468 0.04828  521 ILE A CG2 
2565 C CD1 . ILE A 318 ? 0.45568 0.35415 0.32201 -0.03275 -0.02002 0.04289  521 ILE A CD1 
2566 N N   . ASN A 319 ? 0.51125 0.33341 0.32830 0.01810  -0.04730 0.04693  522 ASN A N   
2567 C CA  . ASN A 319 ? 0.53381 0.31416 0.31714 0.02682  -0.04932 0.05155  522 ASN A CA  
2568 C C   . ASN A 319 ? 0.60811 0.36948 0.38885 0.01046  -0.04060 0.05273  522 ASN A C   
2569 O O   . ASN A 319 ? 0.53545 0.32269 0.34598 -0.00169 -0.03654 0.04836  522 ASN A O   
2570 C CB  . ASN A 319 ? 0.51759 0.30383 0.30378 0.05016  -0.06047 0.04734  522 ASN A CB  
2571 C CG  . ASN A 319 ? 0.76481 0.50309 0.50757 0.06555  -0.06481 0.05293  522 ASN A CG  
2572 O OD1 . ASN A 319 ? 0.81017 0.54103 0.55065 0.08003  -0.07000 0.05014  522 ASN A OD1 
2573 N ND2 . ASN A 319 ? 0.71640 0.41980 0.42257 0.06238  -0.06182 0.06082  522 ASN A ND2 
2574 N N   . ILE A 320 ? 0.62938 0.34363 0.37199 0.01022  -0.03791 0.05844  523 ILE A N   
2575 C CA  . ILE A 320 ? 0.64848 0.33817 0.38222 -0.00579 -0.02976 0.05899  523 ILE A CA  
2576 C C   . ILE A 320 ? 0.72495 0.37639 0.43041 0.00987  -0.03469 0.06039  523 ILE A C   
2577 O O   . ILE A 320 ? 0.71050 0.32572 0.37865 0.02300  -0.03789 0.06613  523 ILE A O   
2578 C CB  . ILE A 320 ? 0.73906 0.40321 0.45013 -0.02719 -0.01796 0.06407  523 ILE A CB  
2579 C CG1 . ILE A 320 ? 0.69939 0.40321 0.43935 -0.04111 -0.01274 0.06176  523 ILE A CG1 
2580 C CG2 . ILE A 320 ? 0.73809 0.37640 0.43922 -0.04469 -0.00984 0.06305  523 ILE A CG2 
2581 C CD1 . ILE A 320 ? 0.72051 0.42203 0.44432 -0.03523 -0.01339 0.06616  523 ILE A CD1 
2582 N N   . GLU A 321 ? 0.65949 0.31709 0.38020 0.00991  -0.03552 0.05512  524 GLU A N   
2583 C CA  . GLU A 321 ? 0.71509 0.33852 0.41110 0.02645  -0.04015 0.05510  524 GLU A CA  
2584 C C   . GLU A 321 ? 0.68640 0.28882 0.37746 0.01083  -0.03328 0.05257  524 GLU A C   
2585 O O   . GLU A 321 ? 0.69861 0.33218 0.42109 -0.00293 -0.03040 0.04715  524 GLU A O   
2586 C CB  . GLU A 321 ? 0.72217 0.37681 0.44091 0.05020  -0.05070 0.04913  524 GLU A CB  
2587 C CG  . GLU A 321 ? 0.86685 0.53667 0.58432 0.06919  -0.05952 0.05036  524 GLU A CG  
2588 C CD  . GLU A 321 ? 0.91444 0.60133 0.64165 0.09623  -0.07029 0.04426  524 GLU A CD  
2589 O OE1 . GLU A 321 ? 0.95391 0.60511 0.65164 0.11365  -0.07443 0.04556  524 GLU A OE1 
2590 O OE2 . GLU A 321 ? 0.88167 0.61749 0.64569 0.09989  -0.07406 0.03758  524 GLU A OE2 
2591 N N   . ARG A 322 ? 0.77434 0.32198 0.42358 0.01365  -0.03109 0.05625  525 ARG A N   
2592 C CA  . ARG A 322 ? 0.83801 0.35789 0.47566 -0.00180 -0.02435 0.05342  525 ARG A CA  
2593 C C   . ARG A 322 ? 0.84852 0.36374 0.48733 0.01699  -0.03079 0.04800  525 ARG A C   
2594 O O   . ARG A 322 ? 0.86032 0.37285 0.49169 0.04387  -0.03935 0.04843  525 ARG A O   
2595 C CB  . ARG A 322 ? 0.88586 0.34293 0.47355 -0.01266 -0.01608 0.05998  525 ARG A CB  
2596 C CG  . ARG A 322 ? 0.95828 0.42016 0.54673 -0.03911 -0.00565 0.06317  525 ARG A CG  
2597 C CD  . ARG A 322 ? 1.22054 0.64913 0.78112 -0.05694 0.00590  0.06185  525 ARG A CD  
2598 N NE  . ARG A 322 ? 1.21042 0.65978 0.78985 -0.08819 0.01683  0.05827  525 ARG A NE  
2599 C CZ  . ARG A 322 ? 1.22950 0.69004 0.82583 -0.10674 0.02110  0.05054  525 ARG A CZ  
2600 N NH1 . ARG A 322 ? 1.12909 0.57768 0.72298 -0.09901 0.01639  0.04610  525 ARG A NH1 
2601 N NH2 . ARG A 322 ? 1.19041 0.67730 0.80735 -0.13268 0.02994  0.04627  525 ARG A NH2 
2602 N N   . CYS A 323 ? 0.83540 0.35261 0.48474 0.00299  -0.02681 0.04193  526 CYS A N   
2603 C CA  . CYS A 323 ? 0.91777 0.42206 0.56165 0.01776  -0.03063 0.03645  526 CYS A CA  
2604 C C   . CYS A 323 ? 1.00918 0.47548 0.63155 -0.00200 -0.02304 0.03358  526 CYS A C   
2605 O O   . CYS A 323 ? 1.05419 0.52910 0.68621 -0.02901 -0.01615 0.03220  526 CYS A O   
2606 C CB  . CYS A 323 ? 0.86776 0.42674 0.55518 0.02481  -0.03546 0.02925  526 CYS A CB  
2607 S SG  . CYS A 323 ? 0.82850 0.43273 0.55466 -0.00322 -0.03054 0.02564  526 CYS A SG  
2608 N N   . GLU A 324 ? 1.11321 0.53826 0.70647 0.01190  -0.02444 0.03178  527 GLU A N   
2609 C CA  . GLU A 324 ? 1.13348 0.53330 0.71091 -0.00559 -0.01725 0.02667  527 GLU A CA  
2610 C C   . GLU A 324 ? 1.12172 0.50775 0.69064 0.01269  -0.02087 0.02038  527 GLU A C   
2611 O O   . GLU A 324 ? 1.17416 0.53906 0.72901 0.00044  -0.01570 0.01548  527 GLU A O   
2612 C CB  . GLU A 324 ? 1.20463 0.56892 0.74790 -0.01597 -0.00947 0.03123  527 GLU A CB  
2613 C CG  . GLU A 324 ? 1.26292 0.59413 0.77254 0.01038  -0.01311 0.03494  527 GLU A CG  
2614 C CD  . GLU A 324 ? 1.51591 0.80657 0.98748 -0.00126 -0.00453 0.03867  527 GLU A CD  
2615 O OE1 . GLU A 324 ? 1.55409 0.85039 1.02840 -0.02363 0.00268  0.04147  527 GLU A OE1 
2616 O OE2 . GLU A 324 ? 1.62157 0.87476 1.06009 0.01195  -0.00451 0.03833  527 GLU A OE2 
2617 N N   . THR A 325 ? 0.96454 0.36348 0.54169 0.04165  -0.02920 0.01965  528 THR A N   
2618 C CA  . THR A 325 ? 0.95820 0.35392 0.53477 0.05898  -0.03212 0.01209  528 THR A CA  
2619 C C   . THR A 325 ? 0.89981 0.35046 0.51950 0.06525  -0.03650 0.00652  528 THR A C   
2620 O O   . THR A 325 ? 0.85137 0.34687 0.50184 0.06149  -0.03848 0.00917  528 THR A O   
2621 C CB  . THR A 325 ? 0.99134 0.36846 0.54513 0.08885  -0.03673 0.01345  528 THR A CB  
2622 O OG1 . THR A 325 ? 1.03875 0.44837 0.61274 0.11159  -0.04514 0.01496  528 THR A OG1 
2623 C CG2 . THR A 325 ? 1.11479 0.45242 0.63145 0.08240  -0.03234 0.02031  528 THR A CG2 
2624 N N   . LYS A 326 ? 0.79254 0.24649 0.41684 0.07294  -0.03664 -0.00184 529 LYS A N   
2625 C CA  . LYS A 326 ? 0.81271 0.32389 0.47793 0.07987  -0.03914 -0.00768 529 LYS A CA  
2626 C C   . LYS A 326 ? 0.77954 0.32053 0.46113 0.10460  -0.04539 -0.00619 529 LYS A C   
2627 O O   . LYS A 326 ? 0.73249 0.32411 0.44983 0.10170  -0.04672 -0.00657 529 LYS A O   
2628 C CB  . LYS A 326 ? 0.72058 0.22379 0.38131 0.08679  -0.03748 -0.01700 529 LYS A CB  
2629 C CG  . LYS A 326 ? 0.67599 0.23325 0.37405 0.09467  -0.03835 -0.02331 529 LYS A CG  
2630 C CD  . LYS A 326 ? 0.74515 0.28955 0.43388 0.09954  -0.03538 -0.03264 529 LYS A CD  
2631 C CE  . LYS A 326 ? 0.71306 0.30951 0.43677 0.10203  -0.03395 -0.03878 529 LYS A CE  
2632 N NZ  . LYS A 326 ? 0.72495 0.35344 0.46832 0.12631  -0.03650 -0.04098 529 LYS A NZ  
2633 N N   . LYS A 327 ? 0.80979 0.31946 0.46463 0.12946  -0.04957 -0.00512 530 LYS A N   
2634 C CA  . LYS A 327 ? 0.79432 0.33456 0.46471 0.15468  -0.05696 -0.00542 530 LYS A CA  
2635 C C   . LYS A 327 ? 0.78214 0.34262 0.46390 0.14576  -0.05934 0.00235  530 LYS A C   
2636 O O   . LYS A 327 ? 0.75827 0.36840 0.47281 0.15233  -0.06318 0.00016  530 LYS A O   
2637 C CB  . LYS A 327 ? 0.83625 0.33636 0.47199 0.18393  -0.06200 -0.00560 530 LYS A CB  
2638 C CG  . LYS A 327 ? 0.91159 0.40952 0.54576 0.19748  -0.06018 -0.01527 530 LYS A CG  
2639 N N   . GLU A 328 ? 0.83890 0.36100 0.49314 0.12977  -0.05623 0.01076  531 GLU A N   
2640 C CA  . GLU A 328 ? 0.76793 0.30803 0.43161 0.11909  -0.05700 0.01782  531 GLU A CA  
2641 C C   . GLU A 328 ? 0.73145 0.32586 0.43905 0.09917  -0.05394 0.01513  531 GLU A C   
2642 O O   . GLU A 328 ? 0.72161 0.35413 0.45328 0.10116  -0.05714 0.01629  531 GLU A O   
2643 C CB  . GLU A 328 ? 0.82314 0.31150 0.44888 0.10199  -0.05152 0.02634  531 GLU A CB  
2644 C CG  . GLU A 328 ? 0.95033 0.39030 0.53211 0.12016  -0.05384 0.03046  531 GLU A CG  
2645 C CD  . GLU A 328 ? 1.05477 0.45517 0.60460 0.09751  -0.04490 0.03657  531 GLU A CD  
2646 O OE1 . GLU A 328 ? 1.03818 0.44245 0.59726 0.06965  -0.03792 0.03837  531 GLU A OE1 
2647 O OE2 . GLU A 328 ? 1.27931 0.64587 0.79483 0.10749  -0.04450 0.03880  531 GLU A OE2 
2648 N N   . PHE A 329 ? 0.73776 0.33499 0.45448 0.08046  -0.04814 0.01121  532 PHE A N   
2649 C CA  . PHE A 329 ? 0.66845 0.31229 0.42236 0.06253  -0.04560 0.00932  532 PHE A CA  
2650 C C   . PHE A 329 ? 0.65139 0.34320 0.43871 0.07642  -0.04886 0.00354  532 PHE A C   
2651 O O   . PHE A 329 ? 0.61755 0.34757 0.43187 0.07111  -0.04939 0.00442  532 PHE A O   
2652 C CB  . PHE A 329 ? 0.69848 0.33367 0.45183 0.04174  -0.04018 0.00578  532 PHE A CB  
2653 C CG  . PHE A 329 ? 0.63450 0.31612 0.42370 0.02887  -0.03889 0.00269  532 PHE A CG  
2654 C CD1 . PHE A 329 ? 0.67250 0.37649 0.47838 0.01303  -0.03748 0.00663  532 PHE A CD1 
2655 C CD2 . PHE A 329 ? 0.65459 0.35528 0.45832 0.03343  -0.03868 -0.00415 532 PHE A CD2 
2656 C CE1 . PHE A 329 ? 0.55915 0.30227 0.39485 0.00357  -0.03678 0.00411  532 PHE A CE1 
2657 C CE2 . PHE A 329 ? 0.58540 0.32353 0.41698 0.02262  -0.03745 -0.00615 532 PHE A CE2 
2658 C CZ  . PHE A 329 ? 0.60094 0.35950 0.44812 0.00844  -0.03693 -0.00186 532 PHE A CZ  
2659 N N   A GLU A 330 ? 0.66393 0.35390 0.44935 0.09360  -0.05013 -0.00308 533 GLU A N   
2660 N N   B GLU A 330 ? 0.66666 0.35655 0.45192 0.09392  -0.05024 -0.00301 533 GLU A N   
2661 C CA  A GLU A 330 ? 0.63171 0.36806 0.44918 0.10439  -0.05116 -0.00993 533 GLU A CA  
2662 C CA  B GLU A 330 ? 0.62334 0.35994 0.44101 0.10414  -0.05114 -0.00986 533 GLU A CA  
2663 C C   A GLU A 330 ? 0.58886 0.34971 0.41825 0.11995  -0.05720 -0.00924 533 GLU A C   
2664 C C   B GLU A 330 ? 0.58856 0.34976 0.41815 0.12051  -0.05723 -0.00948 533 GLU A C   
2665 O O   A GLU A 330 ? 0.55385 0.35750 0.41376 0.11553  -0.05688 -0.01130 533 GLU A O   
2666 O O   B GLU A 330 ? 0.55421 0.35891 0.41474 0.11695  -0.05694 -0.01200 533 GLU A O   
2667 C CB  A GLU A 330 ? 0.59755 0.32622 0.40922 0.11929  -0.04998 -0.01815 533 GLU A CB  
2668 C CB  B GLU A 330 ? 0.59911 0.32811 0.41137 0.11746  -0.04959 -0.01805 533 GLU A CB  
2669 C CG  A GLU A 330 ? 0.64938 0.33810 0.42907 0.14149  -0.05412 -0.01843 533 GLU A CG  
2670 C CG  B GLU A 330 ? 0.61719 0.33212 0.42367 0.09873  -0.04381 -0.01986 533 GLU A CG  
2671 C CD  A GLU A 330 ? 0.65894 0.32636 0.42451 0.15036  -0.05104 -0.02587 533 GLU A CD  
2672 C CD  B GLU A 330 ? 0.64863 0.35878 0.45083 0.10937  -0.04103 -0.02866 533 GLU A CD  
2673 O OE1 A GLU A 330 ? 0.61423 0.28446 0.38529 0.13407  -0.04540 -0.02894 533 GLU A OE1 
2674 O OE1 B GLU A 330 ? 0.64097 0.33525 0.42918 0.13187  -0.04341 -0.03235 533 GLU A OE1 
2675 O OE2 A GLU A 330 ? 0.64030 0.28697 0.38748 0.17486  -0.05467 -0.02892 533 GLU A OE2 
2676 O OE2 B GLU A 330 ? 0.52735 0.24863 0.33852 0.09584  -0.03661 -0.03204 533 GLU A OE2 
2677 N N   . GLN A 331 ? 0.60412 0.33636 0.40749 0.13799  -0.06299 -0.00642 534 GLN A N   
2678 C CA  . GLN A 331 ? 0.62943 0.38444 0.44144 0.15418  -0.07052 -0.00626 534 GLN A CA  
2679 C C   . GLN A 331 ? 0.58428 0.35847 0.40965 0.13672  -0.06989 -0.00045 534 GLN A C   
2680 O O   . GLN A 331 ? 0.57007 0.38500 0.42120 0.14075  -0.07314 -0.00374 534 GLN A O   
2681 C CB  . GLN A 331 ? 0.67949 0.39211 0.45359 0.17615  -0.07743 -0.00243 534 GLN A CB  
2682 C CG  . GLN A 331 ? 0.70903 0.41264 0.47435 0.20261  -0.08081 -0.01014 534 GLN A CG  
2683 C CD  . GLN A 331 ? 0.88080 0.52573 0.59820 0.22167  -0.08586 -0.00479 534 GLN A CD  
2684 O OE1 . GLN A 331 ? 0.92806 0.55064 0.62270 0.22397  -0.09023 0.00354  534 GLN A OE1 
2685 N NE2 . GLN A 331 ? 0.92781 0.54418 0.62670 0.23530  -0.08463 -0.00946 534 GLN A NE2 
2686 N N   . LEU A 332 ? 0.57890 0.32536 0.38774 0.11654  -0.06516 0.00712  535 LEU A N   
2687 C CA  . LEU A 332 ? 0.53901 0.30102 0.35810 0.10079  -0.06386 0.01240  535 LEU A CA  
2688 C C   . LEU A 332 ? 0.55372 0.35972 0.41040 0.08540  -0.05946 0.00846  535 LEU A C   
2689 O O   . LEU A 332 ? 0.51255 0.34877 0.38886 0.08203  -0.06060 0.00860  535 LEU A O   
2690 C CB  . LEU A 332 ? 0.60440 0.32361 0.39375 0.08439  -0.05913 0.02049  535 LEU A CB  
2691 C CG  . LEU A 332 ? 0.74429 0.47239 0.53990 0.06418  -0.05509 0.02590  535 LEU A CG  
2692 C CD1 . LEU A 332 ? 0.68856 0.43071 0.48487 0.07496  -0.06072 0.02858  535 LEU A CD1 
2693 C CD2 . LEU A 332 ? 0.77574 0.45845 0.53985 0.04847  -0.04893 0.03164  535 LEU A CD2 
2694 N N   . MET A 333 ? 0.50921 0.31750 0.37406 0.07666  -0.05456 0.00474  536 MET A N   
2695 C CA  . MET A 333 ? 0.45129 0.29772 0.34767 0.06530  -0.05073 0.00109  536 MET A CA  
2696 C C   . MET A 333 ? 0.43205 0.31600 0.35264 0.07849  -0.05282 -0.00577 536 MET A C   
2697 O O   . MET A 333 ? 0.41920 0.33446 0.36272 0.07148  -0.05152 -0.00680 536 MET A O   
2698 C CB  . MET A 333 ? 0.52435 0.36272 0.41984 0.05573  -0.04599 -0.00171 536 MET A CB  
2699 C CG  . MET A 333 ? 0.55596 0.37347 0.43972 0.03612  -0.04299 0.00289  536 MET A CG  
2700 S SD  . MET A 333 ? 0.64550 0.49475 0.55430 0.01790  -0.04043 0.00548  536 MET A SD  
2701 C CE  . MET A 333 ? 0.55568 0.44493 0.49318 0.02513  -0.03953 -0.00016 536 MET A CE  
2702 N N   . ASN A 334 ? 0.41620 0.29805 0.33238 0.09720  -0.05547 -0.01150 537 ASN A N   
2703 C CA  . ASN A 334 ? 0.43159 0.35281 0.37282 0.10923  -0.05683 -0.02000 537 ASN A CA  
2704 C C   . ASN A 334 ? 0.44601 0.38617 0.39490 0.11534  -0.06312 -0.01936 537 ASN A C   
2705 O O   . ASN A 334 ? 0.42370 0.40175 0.39931 0.11140  -0.06186 -0.02441 537 ASN A O   
2706 C CB  . ASN A 334 ? 0.47497 0.39053 0.40922 0.13010  -0.05877 -0.02710 537 ASN A CB  
2707 C CG  . ASN A 334 ? 0.56446 0.47410 0.49897 0.12396  -0.05134 -0.03093 537 ASN A CG  
2708 O OD1 . ASN A 334 ? 0.56721 0.49177 0.51618 0.10681  -0.04499 -0.03088 537 ASN A OD1 
2709 N ND2 . ASN A 334 ? 0.55026 0.43588 0.46619 0.13886  -0.05231 -0.03427 537 ASN A ND2 
2710 N N   . LYS A 335 ? 0.45107 0.36346 0.37456 0.12462  -0.06965 -0.01349 538 LYS A N   
2711 C CA  . LYS A 335 ? 0.44348 0.37125 0.37030 0.13022  -0.07628 -0.01246 538 LYS A CA  
2712 C C   . LYS A 335 ? 0.44875 0.39525 0.39252 0.10898  -0.07167 -0.00951 538 LYS A C   
2713 O O   . LYS A 335 ? 0.37622 0.35703 0.34149 0.10897  -0.07358 -0.01434 538 LYS A O   
2714 C CB  . LYS A 335 ? 0.42970 0.31561 0.31919 0.14089  -0.08250 -0.00453 538 LYS A CB  
2715 C CG  . LYS A 335 ? 0.58166 0.47813 0.46801 0.14818  -0.09021 -0.00278 538 LYS A CG  
2716 C CD  . LYS A 335 ? 0.64571 0.49498 0.48881 0.16163  -0.09625 0.00540  538 LYS A CD  
2717 C CE  . LYS A 335 ? 0.72448 0.53385 0.54309 0.14088  -0.08848 0.01609  538 LYS A CE  
2718 N NZ  . LYS A 335 ? 0.80815 0.57588 0.58531 0.14935  -0.09287 0.02484  538 LYS A NZ  
2719 N N   . THR A 336 ? 0.42279 0.34797 0.35757 0.09086  -0.06551 -0.00261 539 THR A N   
2720 C CA  . THR A 336 ? 0.41364 0.35391 0.36228 0.07263  -0.06129 0.00029  539 THR A CA  
2721 C C   . THR A 336 ? 0.41495 0.39151 0.39456 0.06557  -0.05663 -0.00640 539 THR A C   
2722 O O   . THR A 336 ? 0.39153 0.39262 0.38765 0.06047  -0.05632 -0.00839 539 THR A O   
2723 C CB  . THR A 336 ? 0.43974 0.35265 0.37387 0.05612  -0.05597 0.00743  539 THR A CB  
2724 O OG1 . THR A 336 ? 0.43980 0.31490 0.34204 0.06102  -0.05854 0.01337  539 THR A OG1 
2725 C CG2 . THR A 336 ? 0.38622 0.31498 0.33360 0.04036  -0.05233 0.01007  539 THR A CG2 
2726 N N   . LEU A 337 ? 0.38776 0.36549 0.37304 0.06453  -0.05228 -0.01001 540 LEU A N   
2727 C CA  . LEU A 337 ? 0.38500 0.39232 0.39509 0.05714  -0.04642 -0.01578 540 LEU A CA  
2728 C C   . LEU A 337 ? 0.35309 0.39331 0.38229 0.06705  -0.04856 -0.02470 540 LEU A C   
2729 O O   . LEU A 337 ? 0.39201 0.45739 0.44039 0.05831  -0.04500 -0.02822 540 LEU A O   
2730 C CB  . LEU A 337 ? 0.30990 0.30900 0.31784 0.05496  -0.04122 -0.01782 540 LEU A CB  
2731 C CG  . LEU A 337 ? 0.33719 0.31341 0.33297 0.04135  -0.03855 -0.01121 540 LEU A CG  
2732 C CD1 . LEU A 337 ? 0.35081 0.31293 0.33746 0.04337  -0.03586 -0.01389 540 LEU A CD1 
2733 C CD2 . LEU A 337 ? 0.28978 0.28103 0.29952 0.02648  -0.03420 -0.00916 540 LEU A CD2 
2734 N N   . ASP A 338 ? 0.39875 0.43947 0.42277 0.08548  -0.05448 -0.02919 541 ASP A N   
2735 C CA  . ASP A 338 ? 0.42319 0.50059 0.46810 0.09571  -0.05735 -0.03968 541 ASP A CA  
2736 C C   . ASP A 338 ? 0.41637 0.50849 0.46602 0.09583  -0.06362 -0.03968 541 ASP A C   
2737 O O   . ASP A 338 ? 0.40823 0.53636 0.47982 0.09847  -0.06490 -0.04946 541 ASP A O   
2738 C CB  . ASP A 338 ? 0.43822 0.51369 0.47629 0.11828  -0.06310 -0.04527 541 ASP A CB  
2739 C CG  . ASP A 338 ? 0.62376 0.70296 0.66845 0.11909  -0.05542 -0.05110 541 ASP A CG  
2740 O OD1 . ASP A 338 ? 0.62307 0.69705 0.67050 0.10223  -0.04640 -0.04846 541 ASP A OD1 
2741 O OD2 . ASP A 338 ? 0.74600 0.83360 0.79215 0.13785  -0.05867 -0.05872 541 ASP A OD2 
2742 N N   . ASN A 339 ? 0.39634 0.46304 0.42645 0.09170  -0.06681 -0.02996 542 ASN A N   
2743 C CA  . ASN A 339 ? 0.43356 0.51161 0.46500 0.09130  -0.07227 -0.02970 542 ASN A CA  
2744 C C   . ASN A 339 ? 0.40121 0.48310 0.44096 0.07087  -0.06553 -0.02615 542 ASN A C   
2745 O O   . ASN A 339 ? 0.43787 0.51914 0.47195 0.06849  -0.06893 -0.02347 542 ASN A O   
2746 C CB  . ASN A 339 ? 0.39963 0.44650 0.40031 0.10296  -0.08054 -0.02190 542 ASN A CB  
2747 C CG  . ASN A 339 ? 0.52718 0.57910 0.52150 0.12737  -0.09072 -0.02741 542 ASN A CG  
2748 O OD1 . ASN A 339 ? 0.58076 0.60503 0.55450 0.13987  -0.09301 -0.02434 542 ASN A OD1 
2749 N ND2 . ASN A 339 ? 0.58115 0.66904 0.59303 0.13506  -0.09725 -0.03654 542 ASN A ND2 
2750 N N   . LYS A 340 ? 0.34904 0.43325 0.39987 0.05732  -0.05626 -0.02608 543 LYS A N   
2751 C CA  . LYS A 340 ? 0.35746 0.44817 0.41802 0.04042  -0.04990 -0.02434 543 LYS A CA  
2752 C C   . LYS A 340 ? 0.40352 0.47134 0.44709 0.03434  -0.05089 -0.01484 543 LYS A C   
2753 O O   . LYS A 340 ? 0.36658 0.44184 0.41350 0.02816  -0.05071 -0.01457 543 LYS A O   
2754 C CB  . LYS A 340 ? 0.41115 0.53412 0.49174 0.03797  -0.05000 -0.03347 543 LYS A CB  
2755 C CG  . LYS A 340 ? 0.48004 0.63081 0.58165 0.03920  -0.04600 -0.04460 543 LYS A CG  
2756 C CD  . LYS A 340 ? 0.56246 0.72694 0.66611 0.05806  -0.05406 -0.05156 543 LYS A CD  
2757 C CE  . LYS A 340 ? 0.51874 0.71526 0.64598 0.05831  -0.04865 -0.06415 543 LYS A CE  
2758 N NZ  . LYS A 340 ? 0.49913 0.71287 0.63018 0.07927  -0.05751 -0.07216 543 LYS A NZ  
2759 N N   . ARG A 341 ? 0.40481 0.44460 0.42960 0.03542  -0.05124 -0.00786 544 ARG A N   
2760 C CA  . ARG A 341 ? 0.36291 0.38102 0.37170 0.02771  -0.05033 0.00040  544 ARG A CA  
2761 C C   . ARG A 341 ? 0.37308 0.38098 0.38277 0.01545  -0.04401 0.00405  544 ARG A C   
2762 O O   . ARG A 341 ? 0.37305 0.37968 0.38608 0.01621  -0.04208 0.00200  544 ARG A O   
2763 C CB  . ARG A 341 ? 0.38771 0.37867 0.37007 0.03769  -0.05579 0.00519  544 ARG A CB  
2764 C CG  . ARG A 341 ? 0.42846 0.42826 0.40643 0.05298  -0.06415 0.00178  544 ARG A CG  
2765 C CD  . ARG A 341 ? 0.39823 0.36684 0.34665 0.06639  -0.06984 0.00641  544 ARG A CD  
2766 N NE  . ARG A 341 ? 0.48402 0.46152 0.42644 0.08342  -0.07950 0.00312  544 ARG A NE  
2767 C CZ  . ARG A 341 ? 0.57978 0.53891 0.50111 0.10238  -0.08707 0.00384  544 ARG A CZ  
2768 N NH1 . ARG A 341 ? 0.54656 0.47558 0.45042 0.10640  -0.08532 0.00737  544 ARG A NH1 
2769 N NH2 . ARG A 341 ? 0.55845 0.52952 0.47532 0.11861  -0.09716 0.00026  544 ARG A NH2 
2770 N N   . ALA A 342 ? 0.35106 0.35352 0.35794 0.00473  -0.04100 0.00865  545 ALA A N   
2771 C CA  . ALA A 342 ? 0.33147 0.32511 0.33780 -0.00589 -0.03668 0.01171  545 ALA A CA  
2772 C C   . ALA A 342 ? 0.40319 0.36921 0.38800 -0.00739 -0.03738 0.01623  545 ALA A C   
2773 O O   . ALA A 342 ? 0.39843 0.34886 0.36598 -0.00116 -0.04033 0.01867  545 ALA A O   
2774 C CB  . ALA A 342 ? 0.23239 0.23710 0.24858 -0.01598 -0.03278 0.01292  545 ALA A CB  
2775 N N   . ILE A 343 ? 0.36237 0.32089 0.34638 -0.01606 -0.03465 0.01704  546 ILE A N   
2776 C CA  . ILE A 343 ? 0.36246 0.29385 0.32683 -0.01786 -0.03484 0.01900  546 ILE A CA  
2777 C C   . ILE A 343 ? 0.36622 0.29353 0.32982 -0.03340 -0.03087 0.02056  546 ILE A C   
2778 O O   . ILE A 343 ? 0.35460 0.29623 0.33217 -0.03926 -0.02989 0.01816  546 ILE A O   
2779 C CB  . ILE A 343 ? 0.43155 0.35835 0.39530 -0.01151 -0.03628 0.01544  546 ILE A CB  
2780 C CG1 . ILE A 343 ? 0.44700 0.38477 0.41643 0.00354  -0.03938 0.01189  546 ILE A CG1 
2781 C CG2 . ILE A 343 ? 0.46338 0.35846 0.40428 -0.01367 -0.03623 0.01683  546 ILE A CG2 
2782 C CD1 . ILE A 343 ? 0.41310 0.34846 0.38264 0.01013  -0.03940 0.00748  546 ILE A CD1 
2783 N N   . GLY A 344 ? 0.32236 0.22992 0.26856 -0.03990 -0.02856 0.02402  547 GLY A N   
2784 C CA  . GLY A 344 ? 0.35251 0.25272 0.29496 -0.05585 -0.02416 0.02396  547 GLY A CA  
2785 C C   . GLY A 344 ? 0.41440 0.28076 0.33258 -0.05805 -0.02377 0.02443  547 GLY A C   
2786 O O   . GLY A 344 ? 0.48083 0.32128 0.37665 -0.04964 -0.02491 0.02767  547 GLY A O   
2787 N N   . ILE A 345 ? 0.40020 0.26610 0.32158 -0.06861 -0.02265 0.02072  548 ILE A N   
2788 C CA  . ILE A 345 ? 0.41136 0.24411 0.30955 -0.07418 -0.02132 0.01979  548 ILE A CA  
2789 C C   . ILE A 345 ? 0.44032 0.26595 0.33270 -0.09495 -0.01475 0.01913  548 ILE A C   
2790 O O   . ILE A 345 ? 0.44748 0.30209 0.36162 -0.10571 -0.01330 0.01566  548 ILE A O   
2791 C CB  . ILE A 345 ? 0.44701 0.28343 0.35106 -0.07222 -0.02475 0.01449  548 ILE A CB  
2792 C CG1 . ILE A 345 ? 0.39955 0.24414 0.30962 -0.05306 -0.02930 0.01423  548 ILE A CG1 
2793 C CG2 . ILE A 345 ? 0.41043 0.21055 0.28913 -0.08034 -0.02278 0.01230  548 ILE A CG2 
2794 C CD1 . ILE A 345 ? 0.41695 0.26951 0.33435 -0.05122 -0.03160 0.00904  548 ILE A CD1 
2795 N N   . PHE A 346 ? 0.47169 0.25855 0.33408 -0.10056 -0.01041 0.02190  549 PHE A N   
2796 C CA  . PHE A 346 ? 0.53306 0.31021 0.38731 -0.12273 -0.00209 0.02072  549 PHE A CA  
2797 C C   . PHE A 346 ? 0.66910 0.40544 0.49553 -0.13220 0.00093  0.01862  549 PHE A C   
2798 O O   . PHE A 346 ? 0.65808 0.36695 0.46569 -0.11880 -0.00309 0.01983  549 PHE A O   
2799 C CB  . PHE A 346 ? 0.57942 0.34653 0.42037 -0.12524 0.00391  0.02694  549 PHE A CB  
2800 C CG  . PHE A 346 ? 0.60330 0.32914 0.40970 -0.11084 0.00257  0.03409  549 PHE A CG  
2801 C CD1 . PHE A 346 ? 0.69863 0.37486 0.46737 -0.11843 0.00807  0.03659  549 PHE A CD1 
2802 C CD2 . PHE A 346 ? 0.62782 0.36381 0.43805 -0.08964 -0.00427 0.03783  549 PHE A CD2 
2803 C CE1 . PHE A 346 ? 0.72343 0.35933 0.45730 -0.10238 0.00585  0.04352  549 PHE A CE1 
2804 C CE2 . PHE A 346 ? 0.63155 0.33254 0.41034 -0.07413 -0.00715 0.04364  549 PHE A CE2 
2805 C CZ  . PHE A 346 ? 0.62990 0.28011 0.36972 -0.07913 -0.00254 0.04689  549 PHE A CZ  
2806 N N   . TRP A 347 ? 0.65743 0.39108 0.48201 -0.15604 0.00858  0.01444  550 TRP A N   
2807 C CA  . TRP A 347 ? 0.76756 0.45990 0.56363 -0.17045 0.01383  0.01163  550 TRP A CA  
2808 C C   . TRP A 347 ? 0.85825 0.55816 0.65784 -0.19761 0.02440  0.00733  550 TRP A C   
2809 O O   . TRP A 347 ? 0.80383 0.54679 0.63349 -0.20509 0.02566  0.00429  550 TRP A O   
2810 C CB  . TRP A 347 ? 0.77134 0.46605 0.57334 -0.16891 0.00754  0.00428  550 TRP A CB  
2811 C CG  . TRP A 347 ? 0.63036 0.37180 0.46701 -0.18034 0.00463  -0.00459 550 TRP A CG  
2812 C CD1 . TRP A 347 ? 0.74090 0.48821 0.58196 -0.20407 0.00839  -0.01377 550 TRP A CD1 
2813 C CD2 . TRP A 347 ? 0.66012 0.44837 0.53040 -0.16787 -0.00322 -0.00574 550 TRP A CD2 
2814 N NE1 . TRP A 347 ? 0.76695 0.56388 0.64287 -0.20505 0.00200  -0.02054 550 TRP A NE1 
2815 C CE2 . TRP A 347 ? 0.69666 0.51661 0.58908 -0.18277 -0.00483 -0.01512 550 TRP A CE2 
2816 C CE3 . TRP A 347 ? 0.61730 0.42276 0.49991 -0.14608 -0.00885 -0.00028 550 TRP A CE3 
2817 C CZ2 . TRP A 347 ? 0.59563 0.45999 0.51877 -0.17447 -0.01221 -0.01792 550 TRP A CZ2 
2818 C CZ3 . TRP A 347 ? 0.57416 0.42212 0.48718 -0.14030 -0.01469 -0.00325 550 TRP A CZ3 
2819 C CH2 . TRP A 347 ? 0.54642 0.42146 0.47776 -0.15340 -0.01650 -0.01137 550 TRP A CH2 
2820 N N   . GLN A 348 ? 0.88904 0.55618 0.66179 -0.20559 0.03173  0.00634  551 GLN A N   
2821 C CA  . GLN A 348 ? 0.92210 0.60291 0.70037 -0.22620 0.04197  0.00056  551 GLN A CA  
2822 C C   . GLN A 348 ? 0.99267 0.69208 0.78712 -0.23834 0.04005  -0.01073 551 GLN A C   
2823 O O   . GLN A 348 ? 1.08368 0.75770 0.86254 -0.23375 0.03577  -0.01251 551 GLN A O   
2824 C CB  . GLN A 348 ? 0.97440 0.60723 0.71162 -0.22926 0.05152  0.00569  551 GLN A CB  
2825 C CG  . GLN A 348 ? 1.02770 0.66883 0.76560 -0.25141 0.06357  -0.00019 551 GLN A CG  
2826 C CD  . GLN A 348 ? 1.22106 0.80784 0.91286 -0.25451 0.07261  0.00430  551 GLN A CD  
2827 O OE1 . GLN A 348 ? 1.17459 0.73704 0.84842 -0.26413 0.07650  -0.00049 551 GLN A OE1 
2828 N NE2 . GLN A 348 ? 1.15100 0.71683 0.82128 -0.24576 0.07571  0.01348  551 GLN A NE2 
2829 N N   . GLY A 349 ? 1.07349 0.81842 0.89944 -0.25207 0.04247  -0.01879 552 GLY A N   
2830 C CA  . GLY A 349 ? 1.12032 0.88859 0.96435 -0.26231 0.03901  -0.03015 552 GLY A CA  
2831 C C   . GLY A 349 ? 1.17714 0.98860 1.04878 -0.27863 0.04433  -0.03923 552 GLY A C   
2832 O O   . GLY A 349 ? 1.16756 1.01377 1.06461 -0.28326 0.03840  -0.04891 552 GLY A O   
2833 N N   . ALA A 356 ? 1.10144 0.91407 0.95868 -0.29266 0.07541  -0.02685 559 ALA A N   
2834 C CA  . ALA A 356 ? 1.16971 1.01872 1.05610 -0.27839 0.06708  -0.02443 559 ALA A CA  
2835 C C   . ALA A 356 ? 1.12814 0.95082 0.99992 -0.25978 0.05765  -0.01489 559 ALA A C   
2836 O O   . ALA A 356 ? 1.19283 0.98897 1.04906 -0.25599 0.05227  -0.01461 559 ALA A O   
2837 C CB  . ALA A 356 ? 1.11720 1.01931 1.04469 -0.27993 0.05953  -0.03516 559 ALA A CB  
2838 N N   . GLN A 357 ? 0.87801 0.70824 0.75446 -0.24827 0.05589  -0.00771 560 GLN A N   
2839 C CA  . GLN A 357 ? 0.89982 0.71048 0.76570 -0.23061 0.04688  0.00080  560 GLN A CA  
2840 C C   . GLN A 357 ? 0.74162 0.59573 0.64366 -0.22275 0.03648  -0.00296 560 GLN A C   
2841 O O   . GLN A 357 ? 0.82332 0.71732 0.75251 -0.22272 0.03729  -0.00540 560 GLN A O   
2842 C CB  . GLN A 357 ? 0.85208 0.64196 0.69769 -0.22267 0.05081  0.01110  560 GLN A CB  
2843 C CG  . GLN A 357 ? 0.92710 0.69908 0.76213 -0.20172 0.04077  0.01969  560 GLN A CG  
2844 C CD  . GLN A 357 ? 1.02273 0.73648 0.81456 -0.19344 0.03986  0.02653  560 GLN A CD  
2845 O OE1 . GLN A 357 ? 1.02176 0.70856 0.78768 -0.18182 0.04042  0.03509  560 GLN A OE1 
2846 N NE2 . GLN A 357 ? 1.02079 0.71740 0.80501 -0.19636 0.03757  0.02200  560 GLN A NE2 
2847 N N   . HIS A 358 ? 0.69000 0.53532 0.59072 -0.21518 0.02691  -0.00369 561 HIS A N   
2848 C CA  . HIS A 358 ? 0.61529 0.50022 0.54677 -0.19995 0.01585  -0.00657 561 HIS A CA  
2849 C C   . HIS A 358 ? 0.63644 0.51368 0.56315 -0.17461 0.00906  0.00190  561 HIS A C   
2850 O O   . HIS A 358 ? 0.64022 0.48021 0.53924 -0.16672 0.01013  0.00873  561 HIS A O   
2851 C CB  . HIS A 358 ? 0.67070 0.55819 0.60645 -0.20384 0.00935  -0.01422 561 HIS A CB  
2852 C CG  . HIS A 358 ? 0.76273 0.66515 0.70735 -0.22432 0.01441  -0.02419 561 HIS A CG  
2853 N ND1 . HIS A 358 ? 0.82007 0.69183 0.74241 -0.23433 0.01882  -0.02726 561 HIS A ND1 
2854 C CD2 . HIS A 358 ? 0.78760 0.73527 0.76202 -0.23040 0.01551  -0.03171 561 HIS A CD2 
2855 C CE1 . HIS A 358 ? 0.87829 0.77679 0.81709 -0.24775 0.02247  -0.03646 561 HIS A CE1 
2856 N NE2 . HIS A 358 ? 0.87118 0.81625 0.84193 -0.24493 0.02024  -0.03940 561 HIS A NE2 
2857 N N   . ALA A 359 ? 0.57901 0.49197 0.53249 -0.16168 0.00196  0.00080  562 ALA A N   
2858 C CA  . ALA A 359 ? 0.42089 0.33323 0.37451 -0.14030 -0.00334 0.00714  562 ALA A CA  
2859 C C   . ALA A 359 ? 0.39407 0.33709 0.37180 -0.12933 -0.01131 0.00405  562 ALA A C   
2860 O O   . ALA A 359 ? 0.34785 0.32216 0.34744 -0.13472 -0.01218 -0.00103 562 ALA A O   
2861 C CB  . ALA A 359 ? 0.43076 0.34925 0.38541 -0.13751 0.00132  0.01196  562 ALA A CB  
2862 N N   . VAL A 360 ? 0.33519 0.26874 0.30772 -0.11347 -0.01674 0.00690  563 VAL A N   
2863 C CA  . VAL A 360 ? 0.28974 0.24645 0.27996 -0.10182 -0.02276 0.00554  563 VAL A CA  
2864 C C   . VAL A 360 ? 0.34963 0.30085 0.33661 -0.08595 -0.02412 0.01046  563 VAL A C   
2865 O O   . VAL A 360 ? 0.38465 0.31427 0.35517 -0.08220 -0.02245 0.01420  563 VAL A O   
2866 C CB  . VAL A 360 ? 0.32291 0.27655 0.31097 -0.10178 -0.02773 0.00098  563 VAL A CB  
2867 C CG1 . VAL A 360 ? 0.35097 0.31596 0.34535 -0.11784 -0.02776 -0.00580 563 VAL A CG1 
2868 C CG2 . VAL A 360 ? 0.31598 0.23566 0.28066 -0.09707 -0.02795 0.00232  563 VAL A CG2 
2869 N N   . THR A 361 ? 0.28513 0.25599 0.28704 -0.07664 -0.02723 0.00997  564 THR A N   
2870 C CA  . THR A 361 ? 0.27960 0.25025 0.28201 -0.06345 -0.02818 0.01256  564 THR A CA  
2871 C C   . THR A 361 ? 0.34396 0.30758 0.34190 -0.05581 -0.03106 0.01076  564 THR A C   
2872 O O   . THR A 361 ? 0.31306 0.28221 0.31436 -0.05818 -0.03309 0.00790  564 THR A O   
2873 C CB  . THR A 361 ? 0.30385 0.29840 0.32392 -0.05976 -0.02769 0.01278  564 THR A CB  
2874 O OG1 . THR A 361 ? 0.27636 0.28206 0.30342 -0.06789 -0.02481 0.01270  564 THR A OG1 
2875 C CG2 . THR A 361 ? 0.28423 0.27894 0.30453 -0.05007 -0.02731 0.01456  564 THR A CG2 
2876 N N   . CYS A 362 ? 0.32271 0.27632 0.31345 -0.04581 -0.03139 0.01178  565 CYS A N   
2877 C CA  . CYS A 362 ? 0.33503 0.28429 0.32264 -0.03782 -0.03272 0.00923  565 CYS A CA  
2878 C C   . CYS A 362 ? 0.32655 0.29156 0.32566 -0.02874 -0.03180 0.00878  565 CYS A C   
2879 O O   . CYS A 362 ? 0.34588 0.31362 0.34642 -0.02409 -0.03178 0.00998  565 CYS A O   
2880 C CB  . CYS A 362 ? 0.33107 0.25435 0.29943 -0.03331 -0.03355 0.00880  565 CYS A CB  
2881 S SG  . CYS A 362 ? 0.38120 0.30142 0.34660 -0.02085 -0.03407 0.00469  565 CYS A SG  
2882 N N   . TRP A 363 ? 0.25004 0.22484 0.25598 -0.02708 -0.03077 0.00666  566 TRP A N   
2883 C CA  . TRP A 363 ? 0.21500 0.20432 0.23167 -0.02167 -0.02808 0.00535  566 TRP A CA  
2884 C C   . TRP A 363 ? 0.27944 0.26705 0.29351 -0.01422 -0.02632 0.00144  566 TRP A C   
2885 O O   . TRP A 363 ? 0.26539 0.26621 0.28891 -0.01091 -0.02301 -0.00108 566 TRP A O   
2886 C CB  . TRP A 363 ? 0.22918 0.22965 0.25397 -0.02580 -0.02631 0.00615  566 TRP A CB  
2887 C CG  . TRP A 363 ? 0.22650 0.23458 0.25812 -0.03064 -0.02696 0.00870  566 TRP A CG  
2888 C CD1 . TRP A 363 ? 0.25725 0.26802 0.29014 -0.03603 -0.02890 0.00968  566 TRP A CD1 
2889 C CD2 . TRP A 363 ? 0.21310 0.22886 0.25146 -0.03006 -0.02560 0.00945  566 TRP A CD2 
2890 N NE1 . TRP A 363 ? 0.22249 0.24235 0.26309 -0.03855 -0.02794 0.01103  566 TRP A NE1 
2891 C CE2 . TRP A 363 ? 0.22340 0.24482 0.26616 -0.03518 -0.02582 0.01121  566 TRP A CE2 
2892 C CE3 . TRP A 363 ? 0.25616 0.27642 0.29763 -0.02544 -0.02457 0.00786  566 TRP A CE3 
2893 C CZ2 . TRP A 363 ? 0.21921 0.24776 0.26737 -0.03603 -0.02424 0.01193  566 TRP A CZ2 
2894 C CZ3 . TRP A 363 ? 0.25049 0.27809 0.29702 -0.02658 -0.02407 0.00848  566 TRP A CZ3 
2895 C CH2 . TRP A 363 ? 0.25689 0.28712 0.30571 -0.03194 -0.02351 0.01078  566 TRP A CH2 
2896 N N   . GLY A 364 ? 0.25234 0.22459 0.25404 -0.01207 -0.02773 -0.00005 567 GLY A N   
2897 C CA  . GLY A 364 ? 0.27584 0.24728 0.27516 -0.00353 -0.02555 -0.00464 567 GLY A CA  
2898 C C   . GLY A 364 ? 0.33546 0.28606 0.31827 -0.00202 -0.02716 -0.00629 567 GLY A C   
2899 O O   . GLY A 364 ? 0.31591 0.25291 0.28935 -0.00925 -0.02994 -0.00421 567 GLY A O   
2900 N N   . ALA A 365 ? 0.30246 0.25175 0.28226 0.00698  -0.02481 -0.01117 568 ALA A N   
2901 C CA  . ALA A 365 ? 0.38567 0.31326 0.34820 0.01059  -0.02576 -0.01392 568 ALA A CA  
2902 C C   . ALA A 365 ? 0.37013 0.30353 0.33282 0.01634  -0.02060 -0.01977 568 ALA A C   
2903 O O   . ALA A 365 ? 0.31897 0.27279 0.29546 0.02074  -0.01616 -0.02277 568 ALA A O   
2904 C CB  . ALA A 365 ? 0.40023 0.31097 0.35206 0.01996  -0.02916 -0.01390 568 ALA A CB  
2905 N N   . ALA A 366 ? 0.37696 0.29241 0.32369 0.01500  -0.02060 -0.02211 569 ALA A N   
2906 C CA  . ALA A 366 ? 0.39711 0.31227 0.33843 0.02080  -0.01535 -0.02821 569 ALA A CA  
2907 C C   . ALA A 366 ? 0.41309 0.31224 0.34320 0.03351  -0.01595 -0.03309 569 ALA A C   
2908 O O   . ALA A 366 ? 0.42938 0.30600 0.34633 0.03448  -0.02091 -0.03118 569 ALA A O   
2909 C CB  . ALA A 366 ? 0.40528 0.30978 0.33330 0.01220  -0.01542 -0.02842 569 ALA A CB  
2910 N N   . TYR A 367 ? 0.35774 0.26785 0.29216 0.04341  -0.01012 -0.03980 570 TYR A N   
2911 C CA  . TYR A 367 ? 0.40396 0.30251 0.32945 0.05884  -0.01015 -0.04581 570 TYR A CA  
2912 C C   . TYR A 367 ? 0.46516 0.36121 0.38228 0.06216  -0.00318 -0.05315 570 TYR A C   
2913 O O   . TYR A 367 ? 0.40027 0.31494 0.32611 0.05649  0.00386  -0.05499 570 TYR A O   
2914 C CB  . TYR A 367 ? 0.39811 0.31996 0.34154 0.07231  -0.01011 -0.04923 570 TYR A CB  
2915 C CG  . TYR A 367 ? 0.41494 0.34095 0.36579 0.07161  -0.01679 -0.04302 570 TYR A CG  
2916 C CD1 . TYR A 367 ? 0.39103 0.33453 0.35640 0.05872  -0.01638 -0.03799 570 TYR A CD1 
2917 C CD2 . TYR A 367 ? 0.41156 0.32267 0.35281 0.08523  -0.02323 -0.04246 570 TYR A CD2 
2918 C CE1 . TYR A 367 ? 0.41390 0.36127 0.38499 0.05815  -0.02188 -0.03296 570 TYR A CE1 
2919 C CE2 . TYR A 367 ? 0.44598 0.35980 0.39116 0.08491  -0.02902 -0.03676 570 TYR A CE2 
2920 C CZ  . TYR A 367 ? 0.48035 0.41337 0.44117 0.07089  -0.02807 -0.03235 570 TYR A CZ  
2921 O OH  . TYR A 367 ? 0.50061 0.43608 0.46415 0.07043  -0.03322 -0.02726 570 TYR A OH  
2922 N N   . ASP A 368 ? 0.44552 0.31637 0.34358 0.07188  -0.00438 -0.05758 571 ASP A N   
2923 C CA  . ASP A 368 ? 0.47486 0.34336 0.36443 0.07859  0.00273  -0.06612 571 ASP A CA  
2924 C C   . ASP A 368 ? 0.54149 0.43300 0.44665 0.09638  0.00710  -0.07400 571 ASP A C   
2925 O O   . ASP A 368 ? 0.50345 0.41053 0.42393 0.10394  0.00306  -0.07281 571 ASP A O   
2926 C CB  . ASP A 368 ? 0.52491 0.35406 0.38513 0.08002  -0.00016 -0.06836 571 ASP A CB  
2927 C CG  . ASP A 368 ? 0.57517 0.38026 0.42349 0.09459  -0.00552 -0.06905 571 ASP A CG  
2928 O OD1 . ASP A 368 ? 0.57246 0.39366 0.43481 0.10834  -0.00695 -0.06972 571 ASP A OD1 
2929 O OD2 . ASP A 368 ? 0.61107 0.37877 0.43361 0.09222  -0.00859 -0.06918 571 ASP A OD2 
2930 N N   . GLU A 369 ? 0.50661 0.40115 0.40735 0.10378  0.01516  -0.08307 572 GLU A N   
2931 C CA  . GLU A 369 ? 0.52083 0.44367 0.43944 0.12006  0.02090  -0.09288 572 GLU A CA  
2932 C C   . GLU A 369 ? 0.52853 0.44025 0.44280 0.14155  0.01332  -0.09577 572 GLU A C   
2933 O O   . GLU A 369 ? 0.63037 0.57136 0.56411 0.15686  0.01491  -0.10349 572 GLU A O   
2934 C CB  . GLU A 369 ? 0.47586 0.40228 0.38803 0.12230  0.03253  -0.10240 572 GLU A CB  
2935 C CG  . GLU A 369 ? 0.52967 0.46656 0.44307 0.10327  0.04131  -0.10003 572 GLU A CG  
2936 C CD  . GLU A 369 ? 0.63016 0.55836 0.52655 0.10405  0.05172  -0.10775 572 GLU A CD  
2937 O OE1 . GLU A 369 ? 0.61228 0.56099 0.51889 0.11562  0.06107  -0.11869 572 GLU A OE1 
2938 O OE2 . GLU A 369 ? 0.61633 0.51857 0.48912 0.09336  0.05042  -0.10363 572 GLU A OE2 
2939 N N   . ASP A 370 ? 0.55353 0.42346 0.44169 0.14331  0.00538  -0.09045 573 ASP A N   
2940 C CA  . ASP A 370 ? 0.52678 0.37875 0.40532 0.16298  -0.00272 -0.09058 573 ASP A CA  
2941 C C   . ASP A 370 ? 0.57072 0.42789 0.45799 0.15945  -0.01126 -0.08138 573 ASP A C   
2942 O O   . ASP A 370 ? 0.53650 0.37603 0.41264 0.17506  -0.01883 -0.07968 573 ASP A O   
2943 C CB  . ASP A 370 ? 0.55212 0.35055 0.39367 0.16580  -0.00567 -0.08962 573 ASP A CB  
2944 C CG  . ASP A 370 ? 0.68525 0.47459 0.51460 0.17715  0.00158  -0.10073 573 ASP A CG  
2945 O OD1 . ASP A 370 ? 0.64540 0.47127 0.49561 0.18475  0.00919  -0.10951 573 ASP A OD1 
2946 O OD2 . ASP A 370 ? 0.71363 0.45867 0.51177 0.17766  0.00042  -0.10138 573 ASP A OD2 
2947 N N   . ASN A 371 ? 0.49923 0.37723 0.40312 0.14001  -0.01005 -0.07538 574 ASN A N   
2948 C CA  . ASN A 371 ? 0.54077 0.42600 0.45389 0.13349  -0.01672 -0.06685 574 ASN A CA  
2949 C C   . ASN A 371 ? 0.57884 0.42233 0.46631 0.12555  -0.02309 -0.05757 574 ASN A C   
2950 O O   . ASN A 371 ? 0.52541 0.36602 0.41309 0.12578  -0.02923 -0.05111 574 ASN A O   
2951 C CB  . ASN A 371 ? 0.52905 0.43858 0.45806 0.15242  -0.02163 -0.07054 574 ASN A CB  
2952 C CG  . ASN A 371 ? 0.53469 0.49314 0.49491 0.15562  -0.01479 -0.08030 574 ASN A CG  
2953 O OD1 . ASN A 371 ? 0.57541 0.55312 0.54923 0.13849  -0.00704 -0.08036 574 ASN A OD1 
2954 N ND2 . ASN A 371 ? 0.57747 0.55608 0.54834 0.17771  -0.01735 -0.08917 574 ASN A ND2 
2955 N N   . ASN A 372 ? 0.54919 0.36057 0.41397 0.11741  -0.02127 -0.05743 575 ASN A N   
2956 C CA  . ASN A 372 ? 0.57049 0.34821 0.41511 0.10331  -0.02540 -0.04960 575 ASN A CA  
2957 C C   . ASN A 372 ? 0.53660 0.33553 0.39795 0.08229  -0.02503 -0.04361 575 ASN A C   
2958 O O   . ASN A 372 ? 0.51564 0.34015 0.39257 0.07535  -0.02047 -0.04593 575 ASN A O   
2959 C CB  . ASN A 372 ? 0.65225 0.39246 0.46928 0.09862  -0.02357 -0.05296 575 ASN A CB  
2960 C CG  . ASN A 372 ? 0.65176 0.36713 0.44941 0.12039  -0.02320 -0.05964 575 ASN A CG  
2961 O OD1 . ASN A 372 ? 0.65871 0.35010 0.44111 0.13330  -0.02773 -0.05708 575 ASN A OD1 
2962 N ND2 . ASN A 372 ? 0.66370 0.38210 0.45904 0.12538  -0.01761 -0.06831 575 ASN A ND2 
2963 N N   . ILE A 373 ? 0.50902 0.29614 0.36560 0.07261  -0.02929 -0.03595 576 ILE A N   
2964 C CA  . ILE A 373 ? 0.45936 0.26425 0.33009 0.05347  -0.02923 -0.03080 576 ILE A CA  
2965 C C   . ILE A 373 ? 0.47055 0.25703 0.32728 0.03810  -0.02859 -0.03177 576 ILE A C   
2966 O O   . ILE A 373 ? 0.48160 0.23377 0.31524 0.03452  -0.03005 -0.03192 576 ILE A O   
2967 C CB  . ILE A 373 ? 0.53353 0.33644 0.40605 0.04891  -0.03312 -0.02327 576 ILE A CB  
2968 C CG1 . ILE A 373 ? 0.50263 0.32894 0.39079 0.06386  -0.03484 -0.02338 576 ILE A CG1 
2969 C CG2 . ILE A 373 ? 0.44860 0.26741 0.33396 0.02955  -0.03287 -0.01889 576 ILE A CG2 
2970 C CD1 . ILE A 373 ? 0.55051 0.37286 0.43682 0.06215  -0.03896 -0.01634 576 ILE A CD1 
2971 N N   . ILE A 374 ? 0.46542 0.27336 0.33427 0.02901  -0.02647 -0.03293 577 ILE A N   
2972 C CA  . ILE A 374 ? 0.43275 0.22780 0.28888 0.01672  -0.02698 -0.03554 577 ILE A CA  
2973 C C   . ILE A 374 ? 0.51022 0.32033 0.37700 0.00020  -0.02987 -0.03129 577 ILE A C   
2974 O O   . ILE A 374 ? 0.45473 0.25355 0.31088 -0.01165 -0.03247 -0.03346 577 ILE A O   
2975 C CB  . ILE A 374 ? 0.46258 0.26399 0.31609 0.02239  -0.02254 -0.04195 577 ILE A CB  
2976 C CG1 . ILE A 374 ? 0.45449 0.28981 0.32920 0.02200  -0.01894 -0.04029 577 ILE A CG1 
2977 C CG2 . ILE A 374 ? 0.48168 0.27047 0.32585 0.03988  -0.01931 -0.04765 577 ILE A CG2 
2978 C CD1 . ILE A 374 ? 0.46369 0.30344 0.33329 0.02700  -0.01266 -0.04645 577 ILE A CD1 
2979 N N   . CYS A 375 ? 0.41039 0.24611 0.29770 -0.00075 -0.02985 -0.02626 578 CYS A N   
2980 C CA  . CYS A 375 ? 0.39770 0.24887 0.29575 -0.01382 -0.03259 -0.02267 578 CYS A CA  
2981 C C   . CYS A 375 ? 0.44585 0.31459 0.36136 -0.01300 -0.03250 -0.01698 578 CYS A C   
2982 O O   . CYS A 375 ? 0.42973 0.30850 0.35377 -0.00253 -0.02999 -0.01658 578 CYS A O   
2983 C CB  . CYS A 375 ? 0.41152 0.27818 0.31347 -0.01553 -0.03170 -0.02436 578 CYS A CB  
2984 S SG  . CYS A 375 ? 0.42314 0.30412 0.33187 -0.02905 -0.03729 -0.02219 578 CYS A SG  
2985 N N   . LEU A 376 ? 0.46146 0.33533 0.38255 -0.02436 -0.03520 -0.01367 579 LEU A N   
2986 C CA  . LEU A 376 ? 0.38545 0.27691 0.32255 -0.02551 -0.03503 -0.00868 579 LEU A CA  
2987 C C   . LEU A 376 ? 0.35865 0.27189 0.30906 -0.03215 -0.03621 -0.00752 579 LEU A C   
2988 O O   . LEU A 376 ? 0.34648 0.25918 0.29242 -0.03875 -0.03899 -0.01003 579 LEU A O   
2989 C CB  . LEU A 376 ? 0.34735 0.22536 0.27833 -0.03239 -0.03604 -0.00582 579 LEU A CB  
2990 C CG  . LEU A 376 ? 0.45784 0.30826 0.37053 -0.02452 -0.03545 -0.00579 579 LEU A CG  
2991 C CD1 . LEU A 376 ? 0.45936 0.29305 0.36209 -0.03323 -0.03515 -0.00211 579 LEU A CD1 
2992 C CD2 . LEU A 376 ? 0.41264 0.27305 0.33241 -0.00844 -0.03480 -0.00528 579 LEU A CD2 
2993 N N   . TYR A 377 ? 0.32610 0.25778 0.29166 -0.02968 -0.03462 -0.00418 580 TYR A N   
2994 C CA  . TYR A 377 ? 0.31792 0.26770 0.29452 -0.03348 -0.03552 -0.00256 580 TYR A CA  
2995 C C   . TYR A 377 ? 0.31489 0.27381 0.30171 -0.03923 -0.03646 0.00048  580 TYR A C   
2996 O O   . TYR A 377 ? 0.29631 0.25874 0.28901 -0.03597 -0.03425 0.00286  580 TYR A O   
2997 C CB  . TYR A 377 ? 0.27040 0.23055 0.25297 -0.02658 -0.03132 -0.00210 580 TYR A CB  
2998 C CG  . TYR A 377 ? 0.29009 0.24060 0.26067 -0.02243 -0.02935 -0.00578 580 TYR A CG  
2999 C CD1 . TYR A 377 ? 0.28273 0.23067 0.24430 -0.02474 -0.03140 -0.00694 580 TYR A CD1 
3000 C CD2 . TYR A 377 ? 0.33260 0.27604 0.29922 -0.01544 -0.02613 -0.00875 580 TYR A CD2 
3001 C CE1 . TYR A 377 ? 0.34157 0.27897 0.28944 -0.02129 -0.02913 -0.01067 580 TYR A CE1 
3002 C CE2 . TYR A 377 ? 0.33422 0.26879 0.28929 -0.01143 -0.02352 -0.01302 580 TYR A CE2 
3003 C CZ  . TYR A 377 ? 0.36660 0.29739 0.31171 -0.01506 -0.02457 -0.01382 580 TYR A CZ  
3004 O OH  . TYR A 377 ? 0.35016 0.27090 0.28162 -0.01130 -0.02148 -0.01834 580 TYR A OH  
3005 N N   . ILE A 378 ? 0.28715 0.25152 0.27617 -0.04776 -0.03977 -0.00052 581 ILE A N   
3006 C CA  . ILE A 378 ? 0.27911 0.24834 0.27420 -0.05619 -0.03980 0.00048  581 ILE A CA  
3007 C C   . ILE A 378 ? 0.32100 0.31342 0.33145 -0.05741 -0.04126 0.00103  581 ILE A C   
3008 O O   . ILE A 378 ? 0.27834 0.27972 0.29054 -0.05692 -0.04520 -0.00124 581 ILE A O   
3009 C CB  . ILE A 378 ? 0.32989 0.28707 0.31525 -0.06721 -0.04150 -0.00330 581 ILE A CB  
3010 C CG1 . ILE A 378 ? 0.30041 0.22921 0.26683 -0.06490 -0.03987 -0.00387 581 ILE A CG1 
3011 C CG2 . ILE A 378 ? 0.28143 0.24777 0.27477 -0.07863 -0.04010 -0.00341 581 ILE A CG2 
3012 C CD1 . ILE A 378 ? 0.32760 0.24473 0.28922 -0.05927 -0.03655 0.00044  581 ILE A CD1 
3013 N N   . ALA A 379 ? 0.24812 0.24940 0.26801 -0.05812 -0.03853 0.00368  582 ALA A N   
3014 C CA  . ALA A 379 ? 0.22259 0.24470 0.25638 -0.06078 -0.03960 0.00299  582 ALA A CA  
3015 C C   . ALA A 379 ? 0.29827 0.32369 0.33394 -0.07338 -0.03948 -0.00018 582 ALA A C   
3016 O O   . ALA A 379 ? 0.29881 0.31388 0.32938 -0.07919 -0.03522 0.00141  582 ALA A O   
3017 C CB  . ALA A 379 ? 0.25357 0.28359 0.29590 -0.05595 -0.03593 0.00630  582 ALA A CB  
3018 N N   . GLU A 380 ? 0.30279 0.34249 0.34465 -0.07789 -0.04398 -0.00509 583 GLU A N   
3019 C CA  . GLU A 380 ? 0.31268 0.35812 0.35732 -0.09234 -0.04381 -0.01047 583 GLU A CA  
3020 C C   . GLU A 380 ? 0.32418 0.40123 0.38911 -0.09363 -0.04506 -0.01387 583 GLU A C   
3021 O O   . GLU A 380 ? 0.36796 0.46307 0.44080 -0.08823 -0.05182 -0.01748 583 GLU A O   
3022 C CB  . GLU A 380 ? 0.30434 0.34275 0.33986 -0.09706 -0.04899 -0.01583 583 GLU A CB  
3023 C CG  . GLU A 380 ? 0.36859 0.38974 0.39304 -0.11285 -0.04578 -0.01964 583 GLU A CG  
3024 C CD  . GLU A 380 ? 0.42907 0.46902 0.46642 -0.12857 -0.04263 -0.02493 583 GLU A CD  
3025 O OE1 . GLU A 380 ? 0.42132 0.47922 0.47264 -0.12715 -0.03929 -0.02295 583 GLU A OE1 
3026 O OE2 . GLU A 380 ? 0.50290 0.53958 0.53607 -0.14349 -0.04267 -0.03193 583 GLU A OE2 
3027 N N   . SER A 381 ? 0.32022 0.40392 0.39237 -0.09966 -0.03873 -0.01306 584 SER A N   
3028 C CA  . SER A 381 ? 0.29582 0.41025 0.38800 -0.09799 -0.03881 -0.01625 584 SER A CA  
3029 C C   . SER A 381 ? 0.35961 0.50026 0.46539 -0.10666 -0.04325 -0.02572 584 SER A C   
3030 O O   . SER A 381 ? 0.27356 0.44414 0.39760 -0.10177 -0.04582 -0.02991 584 SER A O   
3031 C CB  . SER A 381 ? 0.25917 0.37392 0.35409 -0.10389 -0.02983 -0.01402 584 SER A CB  
3032 O OG  . SER A 381 ? 0.31962 0.42843 0.40979 -0.12166 -0.02424 -0.01726 584 SER A OG  
3033 N N   . ASN A 382 ? 0.32810 0.45884 0.42548 -0.11924 -0.04428 -0.03008 585 ASN A N   
3034 C CA  . ASN A 382 ? 0.32470 0.48144 0.43480 -0.12866 -0.04962 -0.04075 585 ASN A CA  
3035 C C   . ASN A 382 ? 0.35701 0.52166 0.46615 -0.11668 -0.06156 -0.04329 585 ASN A C   
3036 O O   . ASN A 382 ? 0.32133 0.51487 0.44409 -0.11982 -0.06860 -0.05270 585 ASN A O   
3037 C CB  . ASN A 382 ? 0.35479 0.49464 0.45389 -0.14941 -0.04489 -0.04531 585 ASN A CB  
3038 C CG  . ASN A 382 ? 0.51467 0.66891 0.62484 -0.16714 -0.03554 -0.05023 585 ASN A CG  
3039 O OD1 . ASN A 382 ? 0.58824 0.77923 0.72125 -0.16778 -0.03666 -0.05739 585 ASN A OD1 
3040 N ND2 . ASN A 382 ? 0.67431 0.79688 0.76612 -0.17880 -0.02553 -0.04579 585 ASN A ND2 
3041 N N   . LEU A 383 ? 0.33320 0.47435 0.42638 -0.10392 -0.06380 -0.03606 586 LEU A N   
3042 C CA  . LEU A 383 ? 0.27896 0.42431 0.36689 -0.09413 -0.07427 -0.03855 586 LEU A CA  
3043 C C   . LEU A 383 ? 0.33097 0.49327 0.42697 -0.07577 -0.07937 -0.03582 586 LEU A C   
3044 O O   . LEU A 383 ? 0.33310 0.49346 0.43329 -0.06893 -0.07370 -0.02985 586 LEU A O   
3045 C CB  . LEU A 383 ? 0.34399 0.45460 0.40819 -0.09046 -0.07356 -0.03337 586 LEU A CB  
3046 C CG  . LEU A 383 ? 0.39680 0.48599 0.44895 -0.10639 -0.06941 -0.03647 586 LEU A CG  
3047 C CD1 . LEU A 383 ? 0.38058 0.43713 0.41014 -0.10018 -0.06857 -0.03212 586 LEU A CD1 
3048 C CD2 . LEU A 383 ? 0.39795 0.50501 0.45635 -0.11999 -0.07508 -0.04791 586 LEU A CD2 
3049 N N   . PRO A 384 ? 0.36641 0.54404 0.46277 -0.06705 -0.09038 -0.04041 587 PRO A N   
3050 C CA  . PRO A 384 ? 0.29273 0.48956 0.39768 -0.04976 -0.09599 -0.03952 587 PRO A CA  
3051 C C   . PRO A 384 ? 0.29886 0.47047 0.38642 -0.03326 -0.09448 -0.02930 587 PRO A C   
3052 O O   . PRO A 384 ? 0.33381 0.51137 0.42689 -0.02158 -0.09344 -0.02607 587 PRO A O   
3053 C CB  . PRO A 384 ? 0.33057 0.55180 0.43936 -0.04656 -0.10947 -0.04890 587 PRO A CB  
3054 C CG  . PRO A 384 ? 0.37309 0.57339 0.46428 -0.05641 -0.11093 -0.05051 587 PRO A CG  
3055 C CD  . PRO A 384 ? 0.29703 0.47829 0.38704 -0.07343 -0.09879 -0.04829 587 PRO A CD  
3056 N N   . GLU A 385 ? 0.29736 0.44067 0.36349 -0.03245 -0.09362 -0.02486 588 GLU A N   
3057 C CA  . GLU A 385 ? 0.25544 0.37689 0.30424 -0.01819 -0.09207 -0.01670 588 GLU A CA  
3058 C C   . GLU A 385 ? 0.30305 0.40893 0.35266 -0.01908 -0.08056 -0.00974 588 GLU A C   
3059 O O   . GLU A 385 ? 0.30093 0.40235 0.35589 -0.03046 -0.07383 -0.00964 588 GLU A O   
3060 C CB  . GLU A 385 ? 0.33921 0.43818 0.36490 -0.01735 -0.09421 -0.01548 588 GLU A CB  
3061 C CG  . GLU A 385 ? 0.39111 0.50258 0.41038 -0.01193 -0.10716 -0.02148 588 GLU A CG  
3062 C CD  . GLU A 385 ? 0.51086 0.59919 0.50512 -0.01179 -0.10877 -0.02092 588 GLU A CD  
3063 O OE1 . GLU A 385 ? 0.53976 0.60242 0.51605 -0.00564 -0.10216 -0.01360 588 GLU A OE1 
3064 O OE2 . GLU A 385 ? 0.63539 0.73192 0.62795 -0.01869 -0.11610 -0.02868 588 GLU A OE2 
3065 N N   . ALA A 386 ? 0.27671 0.37266 0.31879 -0.00667 -0.07860 -0.00415 589 ALA A N   
3066 C CA  . ALA A 386 ? 0.27708 0.35864 0.31867 -0.00669 -0.06832 0.00155  589 ALA A CA  
3067 C C   . ALA A 386 ? 0.31661 0.37284 0.34151 -0.00928 -0.06256 0.00533  589 ALA A C   
3068 O O   . ALA A 386 ? 0.30744 0.34627 0.31840 -0.00269 -0.05860 0.00974  589 ALA A O   
3069 C CB  . ALA A 386 ? 0.31652 0.39645 0.35570 0.00647  -0.06812 0.00470  589 ALA A CB  
3070 N N   . VAL A 387 ? 0.28067 0.33443 0.30627 -0.01932 -0.06154 0.00290  590 VAL A N   
3071 C CA  . VAL A 387 ? 0.28609 0.31972 0.29787 -0.02132 -0.05677 0.00460  590 VAL A CA  
3072 C C   . VAL A 387 ? 0.27400 0.30607 0.29251 -0.03101 -0.05296 0.00308  590 VAL A C   
3073 O O   . VAL A 387 ? 0.26709 0.31101 0.29695 -0.03783 -0.05456 0.00054  590 VAL A O   
3074 C CB  . VAL A 387 ? 0.31208 0.33815 0.30760 -0.01944 -0.06253 0.00227  590 VAL A CB  
3075 C CG1 . VAL A 387 ? 0.27507 0.30216 0.26043 -0.00843 -0.06867 0.00365  590 VAL A CG1 
3076 C CG2 . VAL A 387 ? 0.29277 0.32837 0.29346 -0.02851 -0.06854 -0.00403 590 VAL A CG2 
3077 N N   . LEU A 388 ? 0.28926 0.30600 0.29932 -0.03130 -0.04765 0.00428  591 LEU A N   
3078 C CA  . LEU A 388 ? 0.27120 0.28050 0.27995 -0.03779 -0.04623 0.00225  591 LEU A CA  
3079 C C   . LEU A 388 ? 0.32107 0.32154 0.31704 -0.04001 -0.05043 -0.00166 591 LEU A C   
3080 O O   . LEU A 388 ? 0.32346 0.31725 0.30780 -0.03476 -0.05097 -0.00168 591 LEU A O   
3081 C CB  . LEU A 388 ? 0.26698 0.26671 0.27395 -0.03484 -0.03938 0.00416  591 LEU A CB  
3082 C CG  . LEU A 388 ? 0.29472 0.30220 0.31247 -0.03271 -0.03507 0.00704  591 LEU A CG  
3083 C CD1 . LEU A 388 ? 0.26823 0.26993 0.28536 -0.03034 -0.02987 0.00684  591 LEU A CD1 
3084 C CD2 . LEU A 388 ? 0.24561 0.26344 0.27416 -0.03768 -0.03673 0.00737  591 LEU A CD2 
3085 N N   . TYR A 389 ? 0.31814 0.31636 0.31401 -0.04861 -0.05266 -0.00521 592 TYR A N   
3086 C CA  . TYR A 389 ? 0.29875 0.28754 0.28179 -0.05240 -0.05678 -0.01023 592 TYR A CA  
3087 C C   . TYR A 389 ? 0.32730 0.29385 0.29783 -0.05230 -0.05228 -0.01089 592 TYR A C   
3088 O O   . TYR A 389 ? 0.30893 0.26894 0.28222 -0.05306 -0.04798 -0.00865 592 TYR A O   
3089 C CB  . TYR A 389 ? 0.30423 0.30318 0.29339 -0.06381 -0.06175 -0.01551 592 TYR A CB  
3090 C CG  . TYR A 389 ? 0.31451 0.33895 0.31584 -0.06320 -0.06848 -0.01784 592 TYR A CG  
3091 C CD1 . TYR A 389 ? 0.33268 0.37473 0.35043 -0.06093 -0.06706 -0.01503 592 TYR A CD1 
3092 C CD2 . TYR A 389 ? 0.35369 0.38552 0.34990 -0.06434 -0.07686 -0.02385 592 TYR A CD2 
3093 C CE1 . TYR A 389 ? 0.25814 0.32468 0.28749 -0.05828 -0.07362 -0.01804 592 TYR A CE1 
3094 C CE2 . TYR A 389 ? 0.36607 0.42389 0.37403 -0.06179 -0.08451 -0.02702 592 TYR A CE2 
3095 C CZ  . TYR A 389 ? 0.34110 0.41630 0.36594 -0.05808 -0.08276 -0.02406 592 TYR A CZ  
3096 O OH  . TYR A 389 ? 0.36388 0.46595 0.40062 -0.05315 -0.09077 -0.02793 592 TYR A OH  
3097 N N   . PRO A 390 ? 0.32111 0.27491 0.27632 -0.05022 -0.05338 -0.01423 593 PRO A N   
3098 C CA  . PRO A 390 ? 0.33604 0.26822 0.27876 -0.04867 -0.04930 -0.01596 593 PRO A CA  
3099 C C   . PRO A 390 ? 0.32229 0.24109 0.25750 -0.05924 -0.05148 -0.02029 593 PRO A C   
3100 O O   . PRO A 390 ? 0.37111 0.29457 0.30454 -0.06794 -0.05683 -0.02511 593 PRO A O   
3101 C CB  . PRO A 390 ? 0.33408 0.25883 0.26262 -0.04237 -0.04881 -0.01844 593 PRO A CB  
3102 C CG  . PRO A 390 ? 0.35520 0.29155 0.28264 -0.04537 -0.05598 -0.02023 593 PRO A CG  
3103 C CD  . PRO A 390 ? 0.33490 0.29221 0.28130 -0.04753 -0.05841 -0.01668 593 PRO A CD  
3104 N N   . PHE A 391 ? 0.38599 0.28773 0.31598 -0.05860 -0.04731 -0.01890 594 PHE A N   
3105 C CA  . PHE A 391 ? 0.42766 0.30753 0.34455 -0.06827 -0.04725 -0.02234 594 PHE A CA  
3106 C C   . PHE A 391 ? 0.43483 0.28774 0.33300 -0.05946 -0.04430 -0.02410 594 PHE A C   
3107 O O   . PHE A 391 ? 0.38704 0.23430 0.28530 -0.04879 -0.04080 -0.02048 594 PHE A O   
3108 C CB  . PHE A 391 ? 0.41202 0.29027 0.33440 -0.07477 -0.04457 -0.01849 594 PHE A CB  
3109 C CG  . PHE A 391 ? 0.39085 0.29127 0.32816 -0.08754 -0.04681 -0.01981 594 PHE A CG  
3110 C CD1 . PHE A 391 ? 0.37320 0.30345 0.32927 -0.08350 -0.04951 -0.01807 594 PHE A CD1 
3111 C CD2 . PHE A 391 ? 0.43915 0.33034 0.37126 -0.10357 -0.04555 -0.02339 594 PHE A CD2 
3112 C CE1 . PHE A 391 ? 0.35909 0.31230 0.33020 -0.09297 -0.05186 -0.02027 594 PHE A CE1 
3113 C CE2 . PHE A 391 ? 0.42836 0.34479 0.37713 -0.11560 -0.04691 -0.02617 594 PHE A CE2 
3114 C CZ  . PHE A 391 ? 0.48819 0.43729 0.45753 -0.10916 -0.05056 -0.02479 594 PHE A CZ  
3115 N N   . GLY A 392 ? 0.42543 0.26309 0.30777 -0.06313 -0.04611 -0.03050 595 GLY A N   
3116 C CA  . GLY A 392 ? 0.51880 0.32915 0.38181 -0.05422 -0.04306 -0.03331 595 GLY A CA  
3117 C C   . GLY A 392 ? 0.54707 0.32987 0.39764 -0.05456 -0.04022 -0.03148 595 GLY A C   
3118 O O   . GLY A 392 ? 0.53611 0.31238 0.38518 -0.06784 -0.04037 -0.03070 595 GLY A O   
3119 N N   . VAL A 393 ? 0.48037 0.24697 0.32114 -0.03925 -0.03726 -0.03095 596 VAL A N   
3120 C CA  . VAL A 393 ? 0.54216 0.27857 0.36660 -0.03489 -0.03526 -0.02861 596 VAL A CA  
3121 C C   . VAL A 393 ? 0.55649 0.25662 0.35376 -0.03107 -0.03402 -0.03483 596 VAL A C   
3122 O O   . VAL A 393 ? 0.61578 0.31853 0.41072 -0.02085 -0.03331 -0.03952 596 VAL A O   
3123 C CB  . VAL A 393 ? 0.49810 0.24468 0.33209 -0.01753 -0.03420 -0.02359 596 VAL A CB  
3124 C CG1 . VAL A 393 ? 0.55611 0.26790 0.36845 -0.01130 -0.03347 -0.02086 596 VAL A CG1 
3125 C CG2 . VAL A 393 ? 0.50218 0.28249 0.36139 -0.02198 -0.03502 -0.01816 596 VAL A CG2 
3126 N N   . ARG A 394 ? 0.59013 0.25479 0.36525 -0.04005 -0.03283 -0.03524 597 ARG A N   
3127 C CA  . ARG A 394 ? 0.64161 0.26450 0.38659 -0.03684 -0.03110 -0.04107 597 ARG A CA  
3128 C C   . ARG A 394 ? 0.70070 0.28249 0.42114 -0.03430 -0.02858 -0.03680 597 ARG A C   
3129 O O   . ARG A 394 ? 0.70675 0.29232 0.43249 -0.04012 -0.02797 -0.02999 597 ARG A O   
3130 C CB  . ARG A 394 ? 0.70016 0.31583 0.43663 -0.05641 -0.03213 -0.04900 597 ARG A CB  
3131 C CG  . ARG A 394 ? 0.67176 0.31252 0.41878 -0.05175 -0.03449 -0.05423 597 ARG A CG  
3132 C CD  . ARG A 394 ? 0.81354 0.45287 0.55380 -0.06983 -0.03742 -0.06254 597 ARG A CD  
3133 N NE  . ARG A 394 ? 0.77328 0.44280 0.52600 -0.06492 -0.04048 -0.06529 597 ARG A NE  
3134 C CZ  . ARG A 394 ? 0.77851 0.45623 0.52859 -0.07692 -0.04500 -0.07242 597 ARG A CZ  
3135 N NH1 . ARG A 394 ? 0.83525 0.49653 0.57354 -0.09581 -0.04697 -0.07903 597 ARG A NH1 
3136 N NH2 . ARG A 394 ? 0.71254 0.41516 0.47078 -0.07031 -0.04752 -0.07334 597 ARG A NH2 
3137 N N   . TYR A 395 ? 0.72317 0.26337 0.41418 -0.02449 -0.02682 -0.04074 598 TYR A N   
3138 C CA  . TYR A 395 ? 0.80919 0.30343 0.47068 -0.01809 -0.02457 -0.03631 598 TYR A CA  
3139 C C   . TYR A 395 ? 0.88740 0.32940 0.51271 -0.02892 -0.02116 -0.04264 598 TYR A C   
3140 O O   . TYR A 395 ? 0.85474 0.29022 0.47297 -0.02611 -0.02127 -0.05104 598 TYR A O   
3141 C CB  . TYR A 395 ? 0.71796 0.21064 0.37731 0.01281  -0.02641 -0.03379 598 TYR A CB  
3142 C CG  . TYR A 395 ? 0.80402 0.35130 0.50071 0.02245  -0.02937 -0.03018 598 TYR A CG  
3143 C CD1 . TYR A 395 ? 0.68871 0.24965 0.39597 0.02266  -0.03086 -0.02193 598 TYR A CD1 
3144 C CD2 . TYR A 395 ? 0.70518 0.28828 0.42443 0.03022  -0.02984 -0.03542 598 TYR A CD2 
3145 C CE1 . TYR A 395 ? 0.60907 0.21824 0.34939 0.03014  -0.03323 -0.01966 598 TYR A CE1 
3146 C CE2 . TYR A 395 ? 0.63035 0.26019 0.38174 0.03676  -0.03127 -0.03272 598 TYR A CE2 
3147 C CZ  . TYR A 395 ? 0.66502 0.30775 0.42723 0.03678  -0.03320 -0.02518 598 TYR A CZ  
3148 O OH  . TYR A 395 ? 0.60473 0.29271 0.39809 0.04235  -0.03428 -0.02358 598 TYR A OH  
3149 N N   . LYS A 396 ? 0.90453 0.31615 0.50970 -0.04189 -0.01710 -0.03817 599 LYS A N   
3150 C CA  . LYS A 396 ? 0.95701 0.33816 0.53775 -0.05366 -0.01211 -0.04194 599 LYS A CA  
3151 C C   . LYS A 396 ? 1.01028 0.35879 0.56527 -0.02906 -0.01162 -0.04295 599 LYS A C   
3152 O O   . LYS A 396 ? 1.00481 0.34294 0.55156 -0.00624 -0.01314 -0.03676 599 LYS A O   
3153 C CB  . LYS A 396 ? 0.93125 0.29690 0.50027 -0.07175 -0.00629 -0.03583 599 LYS A CB  
3154 N N   . GLY A 397 ? 0.92805 0.26298 0.47124 -0.03284 -0.01007 -0.05130 600 GLY A N   
3155 C CA  . GLY A 397 ? 1.04321 0.34473 0.55978 -0.01219 -0.00862 -0.05287 600 GLY A CA  
3156 C C   . GLY A 397 ? 1.01158 0.32759 0.53739 0.01530  -0.01227 -0.05717 600 GLY A C   
3157 O O   . GLY A 397 ? 1.13497 0.48281 0.68361 0.01361  -0.01479 -0.06270 600 GLY A O   
3158 N N   . ASN A 398 ? 0.97180 0.26618 0.47978 0.04109  -0.01235 -0.05500 601 ASN A N   
3159 C CA  . ASN A 398 ? 1.07945 0.38479 0.59291 0.06840  -0.01415 -0.06081 601 ASN A CA  
3160 C C   . ASN A 398 ? 1.01681 0.34421 0.54597 0.09293  -0.01858 -0.05541 601 ASN A C   
3161 O O   . ASN A 398 ? 1.06462 0.37254 0.57689 0.10959  -0.02002 -0.04977 601 ASN A O   
3162 C CB  . ASN A 398 ? 1.08305 0.34959 0.56513 0.07928  -0.01117 -0.06411 601 ASN A CB  
3163 C CG  . ASN A 398 ? 1.07593 0.35523 0.56417 0.10131  -0.01117 -0.07306 601 ASN A CG  
3164 O OD1 . ASN A 398 ? 1.10235 0.41334 0.61247 0.12202  -0.01383 -0.07404 601 ASN A OD1 
3165 N ND2 . ASN A 398 ? 1.06038 0.31677 0.53002 0.09639  -0.00756 -0.08035 601 ASN A ND2 
3166 N N   . ILE A 399 ? 0.92884 0.29734 0.48930 0.09563  -0.02099 -0.05780 602 ILE A N   
3167 C CA  . ILE A 399 ? 0.94558 0.34112 0.52563 0.11550  -0.02540 -0.05337 602 ILE A CA  
3168 C C   . ILE A 399 ? 0.89842 0.30015 0.47801 0.14840  -0.02715 -0.05676 602 ILE A C   
3169 O O   . ILE A 399 ? 0.96218 0.38943 0.55858 0.16682  -0.03155 -0.05417 602 ILE A O   
3170 C CB  . ILE A 399 ? 0.88877 0.33543 0.50670 0.10977  -0.02658 -0.05528 602 ILE A CB  
3171 C CG1 . ILE A 399 ? 0.83708 0.31010 0.46953 0.11630  -0.02355 -0.06540 602 ILE A CG1 
3172 C CG2 . ILE A 399 ? 0.78687 0.24548 0.41571 0.07736  -0.02598 -0.05078 602 ILE A CG2 
3173 C CD1 . ILE A 399 ? 0.81955 0.35370 0.49323 0.10685  -0.02326 -0.06452 602 ILE A CD1 
3174 N N   . TYR A 400 ? 0.99809 0.38074 0.56086 0.15621  -0.02409 -0.06324 603 TYR A N   
3175 C CA  . TYR A 400 ? 1.03838 0.42839 0.60120 0.18716  -0.02557 -0.06739 603 TYR A CA  
3176 C C   . TYR A 400 ? 1.12316 0.47116 0.65176 0.19812  -0.02724 -0.06214 603 TYR A C   
3177 O O   . TYR A 400 ? 1.22185 0.57653 0.74974 0.22550  -0.03043 -0.06411 603 TYR A O   
3178 C CB  . TYR A 400 ? 0.92344 0.32389 0.49160 0.19238  -0.02060 -0.07916 603 TYR A CB  
3179 C CG  . TYR A 400 ? 0.87171 0.31558 0.47158 0.18596  -0.01824 -0.08535 603 TYR A CG  
3180 C CD1 . TYR A 400 ? 0.83831 0.32828 0.46880 0.20522  -0.01899 -0.08923 603 TYR A CD1 
3181 C CD2 . TYR A 400 ? 0.85880 0.29861 0.45715 0.16003  -0.01527 -0.08776 603 TYR A CD2 
3182 C CE1 . TYR A 400 ? 0.80757 0.33521 0.46403 0.19841  -0.01543 -0.09485 603 TYR A CE1 
3183 C CE2 . TYR A 400 ? 0.81716 0.29349 0.43962 0.15416  -0.01311 -0.09285 603 TYR A CE2 
3184 C CZ  . TYR A 400 ? 0.79062 0.31726 0.44601 0.17037  -0.01249 -0.09422 603 TYR A CZ  
3185 O OH  . TYR A 400 ? 0.73913 0.31475 0.42538 0.15851  -0.00903 -0.09536 603 TYR A OH  
3186 N N   . GLU A 401 ? 1.12142 0.42809 0.62178 0.17734  -0.02494 -0.05611 604 GLU A N   
3187 C CA  . GLU A 401 ? 1.17785 0.43866 0.64009 0.18574  -0.02506 -0.05132 604 GLU A CA  
3188 C C   . GLU A 401 ? 1.15681 0.41155 0.61073 0.19072  -0.02954 -0.04081 604 GLU A C   
3189 O O   . GLU A 401 ? 1.13243 0.40286 0.60105 0.17446  -0.03011 -0.03541 604 GLU A O   
3190 C CB  . GLU A 401 ? 1.19386 0.41145 0.62715 0.15992  -0.01860 -0.05173 604 GLU A CB  
3191 N N   . GLU A 404 ? 1.36962 0.55287 0.77019 0.13035  -0.02122 -0.01649 607 GLU A N   
3192 C CA  . GLU A 404 ? 1.15229 0.34851 0.56921 0.09722  -0.01657 -0.01557 607 GLU A CA  
3193 C C   . GLU A 404 ? 1.25230 0.49109 0.70226 0.09897  -0.02145 -0.01154 607 GLU A C   
3194 O O   . GLU A 404 ? 1.30742 0.58058 0.78324 0.11903  -0.02738 -0.01477 607 GLU A O   
3195 C CB  . GLU A 404 ? 1.33206 0.53978 0.76422 0.08147  -0.01346 -0.02502 607 GLU A CB  
3196 C CG  . GLU A 404 ? 1.28625 0.45737 0.68994 0.08423  -0.00971 -0.03091 607 GLU A CG  
3197 C CD  . GLU A 404 ? 1.41789 0.59982 0.83467 0.06455  -0.00657 -0.04041 607 GLU A CD  
3198 O OE1 . GLU A 404 ? 1.22375 0.43455 0.66588 0.04285  -0.00629 -0.04163 607 GLU A OE1 
3199 O OE2 . GLU A 404 ? 1.45732 0.61906 0.85818 0.07120  -0.00473 -0.04703 607 GLU A OE2 
3200 N N   . LYS A 405 ? 1.23879 0.47619 0.68822 0.07733  -0.01825 -0.00508 608 LYS A N   
3201 C CA  . LYS A 405 ? 1.17198 0.44528 0.64886 0.07777  -0.02239 -0.00024 608 LYS A CA  
3202 C C   . LYS A 405 ? 1.11465 0.42929 0.63057 0.06532  -0.02336 -0.00541 608 LYS A C   
3203 O O   . LYS A 405 ? 1.06218 0.41160 0.60493 0.07713  -0.02891 -0.00451 608 LYS A O   
3204 C CB  . LYS A 405 ? 1.10778 0.36479 0.56937 0.05826  -0.01749 0.00784  608 LYS A CB  
3205 C CG  . LYS A 405 ? 1.09179 0.31156 0.51507 0.07420  -0.01787 0.01403  608 LYS A CG  
3206 C CD  . LYS A 405 ? 1.32401 0.53073 0.73332 0.05503  -0.01222 0.02155  608 LYS A CD  
3207 N N   . ASN A 406 ? 1.07990 0.39144 0.59834 0.04193  -0.01838 -0.01131 609 ASN A N   
3208 C CA  . ASN A 406 ? 0.96538 0.31206 0.51577 0.02871  -0.01939 -0.01740 609 ASN A CA  
3209 C C   . ASN A 406 ? 0.96165 0.33519 0.53448 0.01186  -0.01972 -0.01224 609 ASN A C   
3210 O O   . ASN A 406 ? 0.90731 0.31090 0.50414 0.02294  -0.02477 -0.01083 609 ASN A O   
3211 C CB  . ASN A 406 ? 0.92301 0.29395 0.49190 0.05355  -0.02464 -0.02334 609 ASN A CB  
3212 C CG  . ASN A 406 ? 1.06648 0.41440 0.61474 0.07348  -0.02421 -0.02847 609 ASN A CG  
3213 O OD1 . ASN A 406 ? 1.15730 0.50967 0.70494 0.10165  -0.02820 -0.02791 609 ASN A OD1 
3214 N ND2 . ASN A 406 ? 1.05864 0.38487 0.59141 0.05915  -0.01968 -0.03422 609 ASN A ND2 
3215 N N   . ARG A 407 ? 0.93375 0.29812 0.49964 -0.01513 -0.01383 -0.01014 610 ARG A N   
3216 C CA  . ARG A 407 ? 0.88803 0.27949 0.47566 -0.03393 -0.01284 -0.00622 610 ARG A CA  
3217 C C   . ARG A 407 ? 0.87941 0.31631 0.50406 -0.03868 -0.01726 -0.01136 610 ARG A C   
3218 O O   . ARG A 407 ? 0.86221 0.30797 0.49416 -0.04943 -0.01717 -0.01966 610 ARG A O   
3219 C CB  . ARG A 407 ? 0.95878 0.33958 0.53701 -0.06375 -0.00468 -0.00691 610 ARG A CB  
3220 C CG  . ARG A 407 ? 0.97981 0.38771 0.57806 -0.08271 -0.00203 -0.00285 610 ARG A CG  
3221 C CD  . ARG A 407 ? 0.94444 0.33515 0.52506 -0.07330 -0.00015 0.00704  610 ARG A CD  
3222 N NE  . ARG A 407 ? 1.05955 0.48248 0.66425 -0.08163 -0.00035 0.01153  610 ARG A NE  
3223 C CZ  . ARG A 407 ? 1.07461 0.50186 0.67909 -0.10194 0.00709  0.01403  610 ARG A CZ  
3224 N NH1 . ARG A 407 ? 1.10487 0.50640 0.68661 -0.11747 0.01564  0.01231  610 ARG A NH1 
3225 N NH2 . ARG A 407 ? 0.95542 0.41330 0.58237 -0.10665 0.00653  0.01796  610 ARG A NH2 
3226 N N   . THR A 408 ? 0.73712 0.21748 0.39108 -0.02969 -0.02087 -0.00626 611 THR A N   
3227 C CA  . THR A 408 ? 0.68662 0.22490 0.38186 -0.03252 -0.02408 -0.00963 611 THR A CA  
3228 C C   . THR A 408 ? 0.76413 0.32121 0.47403 -0.06125 -0.02139 -0.01213 611 THR A C   
3229 O O   . THR A 408 ? 0.81611 0.35835 0.51607 -0.07777 -0.01687 -0.00880 611 THR A O   
3230 C CB  . THR A 408 ? 0.68025 0.25537 0.39988 -0.01728 -0.02774 -0.00387 611 THR A CB  
3231 O OG1 . THR A 408 ? 0.78442 0.34623 0.49237 0.01000  -0.03104 -0.00324 611 THR A OG1 
3232 C CG2 . THR A 408 ? 0.61199 0.24107 0.37009 -0.01997 -0.03003 -0.00681 611 THR A CG2 
3233 N N   . TYR A 409 ? 0.64902 0.23827 0.38111 -0.06712 -0.02397 -0.01860 612 TYR A N   
3234 C CA  . TYR A 409 ? 0.65689 0.27648 0.41033 -0.08967 -0.02365 -0.02107 612 TYR A CA  
3235 C C   . TYR A 409 ? 0.67680 0.34352 0.46114 -0.08425 -0.02871 -0.02387 612 TYR A C   
3236 O O   . TYR A 409 ? 0.61706 0.28749 0.40223 -0.06802 -0.03098 -0.02584 612 TYR A O   
3237 C CB  . TYR A 409 ? 0.70291 0.29633 0.43811 -0.11310 -0.02033 -0.02839 612 TYR A CB  
3238 C CG  . TYR A 409 ? 0.73925 0.31892 0.46266 -0.11234 -0.02259 -0.03745 612 TYR A CG  
3239 C CD1 . TYR A 409 ? 0.72049 0.33668 0.46561 -0.11709 -0.02761 -0.04394 612 TYR A CD1 
3240 C CD2 . TYR A 409 ? 0.71267 0.23998 0.40016 -0.10705 -0.01963 -0.03977 612 TYR A CD2 
3241 C CE1 . TYR A 409 ? 0.76006 0.36306 0.49206 -0.11668 -0.02972 -0.05265 612 TYR A CE1 
3242 C CE2 . TYR A 409 ? 0.81454 0.32800 0.48971 -0.10648 -0.02122 -0.04886 612 TYR A CE2 
3243 C CZ  . TYR A 409 ? 0.81291 0.36518 0.51065 -0.11189 -0.02622 -0.05537 612 TYR A CZ  
3244 O OH  . TYR A 409 ? 0.84945 0.38750 0.53285 -0.11150 -0.02782 -0.06462 612 TYR A OH  
3245 N N   . MET A 410 ? 0.64087 0.34300 0.44961 -0.09733 -0.02983 -0.02392 613 MET A N   
3246 C CA  . MET A 410 ? 0.62773 0.37167 0.46288 -0.09331 -0.03452 -0.02573 613 MET A CA  
3247 C C   . MET A 410 ? 0.63080 0.39293 0.47586 -0.11316 -0.03683 -0.03243 613 MET A C   
3248 O O   . MET A 410 ? 0.66527 0.41405 0.50225 -0.13138 -0.03377 -0.03540 613 MET A O   
3249 C CB  . MET A 410 ? 0.46399 0.23854 0.32210 -0.08374 -0.03492 -0.01863 613 MET A CB  
3250 C CG  . MET A 410 ? 0.54431 0.33616 0.41601 -0.09777 -0.03322 -0.01621 613 MET A CG  
3251 S SD  . MET A 410 ? 0.61960 0.44204 0.51425 -0.08603 -0.03322 -0.00851 613 MET A SD  
3252 C CE  . MET A 410 ? 0.50013 0.33834 0.40644 -0.10560 -0.03000 -0.00814 613 MET A CE  
3253 N N   . PHE A 411 ? 0.60792 0.39986 0.46898 -0.10953 -0.04213 -0.03546 614 PHE A N   
3254 C CA  . PHE A 411 ? 0.58770 0.40021 0.45806 -0.12475 -0.04672 -0.04314 614 PHE A CA  
3255 C C   . PHE A 411 ? 0.56348 0.41541 0.45657 -0.11640 -0.05233 -0.04179 614 PHE A C   
3256 O O   . PHE A 411 ? 0.53144 0.38781 0.42679 -0.10007 -0.05235 -0.03714 614 PHE A O   
3257 C CB  . PHE A 411 ? 0.58910 0.37900 0.43882 -0.13060 -0.04877 -0.05212 614 PHE A CB  
3258 C CG  . PHE A 411 ? 0.63710 0.42284 0.47872 -0.11350 -0.05110 -0.05259 614 PHE A CG  
3259 C CD1 . PHE A 411 ? 0.65924 0.41262 0.48092 -0.10106 -0.04675 -0.05092 614 PHE A CD1 
3260 C CD2 . PHE A 411 ? 0.57260 0.38588 0.42479 -0.10949 -0.05729 -0.05516 614 PHE A CD2 
3261 C CE1 . PHE A 411 ? 0.62194 0.37365 0.43710 -0.08630 -0.04737 -0.05251 614 PHE A CE1 
3262 C CE2 . PHE A 411 ? 0.58988 0.39736 0.43192 -0.09541 -0.05770 -0.05577 614 PHE A CE2 
3263 C CZ  . PHE A 411 ? 0.59996 0.37824 0.42488 -0.08454 -0.05215 -0.05480 614 PHE A CZ  
3264 N N   . ASN A 412 ? 0.55898 0.43892 0.46780 -0.12793 -0.05688 -0.04667 615 ASN A N   
3265 C CA  . ASN A 412 ? 0.51786 0.43383 0.44679 -0.12002 -0.06266 -0.04526 615 ASN A CA  
3266 C C   . ASN A 412 ? 0.47376 0.39402 0.39477 -0.11551 -0.07004 -0.05097 615 ASN A C   
3267 O O   . ASN A 412 ? 0.51286 0.43944 0.43196 -0.12734 -0.07548 -0.06016 615 ASN A O   
3268 C CB  . ASN A 412 ? 0.50560 0.45168 0.45593 -0.13227 -0.06433 -0.04827 615 ASN A CB  
3269 C CG  . ASN A 412 ? 0.51563 0.49639 0.48580 -0.12145 -0.06992 -0.04585 615 ASN A CG  
3270 O OD1 . ASN A 412 ? 0.47756 0.45764 0.44342 -0.10642 -0.07227 -0.04174 615 ASN A OD1 
3271 N ND2 . ASN A 412 ? 0.53038 0.54021 0.52115 -0.12899 -0.07118 -0.04859 615 ASN A ND2 
3272 N N   . TYR A 413 ? 0.41137 0.32973 0.32770 -0.09909 -0.07003 -0.04604 616 TYR A N   
3273 C CA  . TYR A 413 ? 0.47885 0.40050 0.38495 -0.09333 -0.07633 -0.05018 616 TYR A CA  
3274 C C   . TYR A 413 ? 0.53576 0.48932 0.45502 -0.09594 -0.08598 -0.05413 616 TYR A C   
3275 O O   . TYR A 413 ? 0.49400 0.45081 0.40310 -0.09627 -0.09360 -0.06069 616 TYR A O   
3276 C CB  . TYR A 413 ? 0.44905 0.36522 0.34925 -0.07653 -0.07248 -0.04347 616 TYR A CB  
3277 C CG  . TYR A 413 ? 0.42284 0.30994 0.30464 -0.07101 -0.06596 -0.04390 616 TYR A CG  
3278 C CD1 . TYR A 413 ? 0.46315 0.33429 0.32446 -0.07141 -0.06798 -0.05070 616 TYR A CD1 
3279 C CD2 . TYR A 413 ? 0.42382 0.30111 0.30878 -0.06404 -0.05821 -0.03824 616 TYR A CD2 
3280 C CE1 . TYR A 413 ? 0.52904 0.37463 0.37391 -0.06481 -0.06162 -0.05193 616 TYR A CE1 
3281 C CE2 . TYR A 413 ? 0.44290 0.29684 0.31265 -0.05667 -0.05284 -0.03965 616 TYR A CE2 
3282 C CZ  . TYR A 413 ? 0.49247 0.33034 0.34235 -0.05685 -0.05414 -0.04653 616 TYR A CZ  
3283 O OH  . TYR A 413 ? 0.49964 0.31468 0.33431 -0.04824 -0.04842 -0.04888 616 TYR A OH  
3284 N N   . ALA A 414 ? 0.44041 0.41823 0.38135 -0.09632 -0.08634 -0.05071 617 ALA A N   
3285 C CA  . ALA A 414 ? 0.48396 0.49443 0.43875 -0.09532 -0.09600 -0.05460 617 ALA A CA  
3286 C C   . ALA A 414 ? 0.54402 0.56943 0.50422 -0.11170 -0.10267 -0.06680 617 ALA A C   
3287 O O   . ALA A 414 ? 0.60871 0.66423 0.58019 -0.11012 -0.11262 -0.07231 617 ALA A O   
3288 C CB  . ALA A 414 ? 0.42329 0.45493 0.39980 -0.09063 -0.09358 -0.04845 617 ALA A CB  
3289 N N   . LEU A 415 ? 0.49660 0.50188 0.44842 -0.12716 -0.09766 -0.07182 618 LEU A N   
3290 C CA  . LEU A 415 ? 0.53649 0.55489 0.49381 -0.14643 -0.10206 -0.08450 618 LEU A CA  
3291 C C   . LEU A 415 ? 0.65800 0.65328 0.59122 -0.15187 -0.10548 -0.09255 618 LEU A C   
3292 O O   . LEU A 415 ? 0.71706 0.67633 0.62859 -0.14684 -0.09933 -0.08830 618 LEU A O   
3293 C CB  . LEU A 415 ? 0.54764 0.55854 0.51218 -0.16424 -0.09212 -0.08525 618 LEU A CB  
3294 C CG  . LEU A 415 ? 0.59132 0.62517 0.57951 -0.16382 -0.08734 -0.07962 618 LEU A CG  
3295 C CD1 . LEU A 415 ? 0.60237 0.61511 0.58675 -0.18047 -0.07544 -0.07856 618 LEU A CD1 
3296 C CD2 . LEU A 415 ? 0.63076 0.71249 0.64471 -0.16725 -0.09605 -0.08821 618 LEU A CD2 
3297 N N   . SER A 416 ? 0.64010 0.65774 0.57757 -0.16162 -0.11560 -0.10515 619 SER A N   
3298 C CA  . SER A 416 ? 0.73536 0.73120 0.65192 -0.17437 -0.11745 -0.11589 619 SER A CA  
3299 C C   . SER A 416 ? 0.81823 0.79156 0.73192 -0.19589 -0.10670 -0.11945 619 SER A C   
3300 O O   . SER A 416 ? 0.70998 0.70368 0.64675 -0.20418 -0.10166 -0.11934 619 SER A O   
3301 C CB  . SER A 416 ? 0.75978 0.78915 0.68364 -0.17965 -0.13175 -0.12955 619 SER A CB  
3302 O OG  . SER A 416 ? 0.83220 0.89892 0.78856 -0.18596 -0.13210 -0.13343 619 SER A OG  
3303 N N   . LYS A 417 ? 0.83828 0.76732 0.72411 -0.19912 -0.10070 -0.12024 620 LYS A N   
3304 C CA  . LYS A 417 ? 0.88527 0.78312 0.76316 -0.21178 -0.08787 -0.11954 620 LYS A CA  
3305 C C   . LYS A 417 ? 0.83847 0.73554 0.72758 -0.21199 -0.07921 -0.10913 620 LYS A C   
3306 O O   . LYS A 417 ? 0.80001 0.71521 0.70788 -0.22317 -0.07398 -0.11024 620 LYS A O   
3307 C CB  . LYS A 417 ? 0.76689 0.67957 0.65584 -0.22859 -0.08731 -0.13053 620 LYS A CB  
3308 N N   . PRO A 418 ? 0.75913 0.63913 0.64067 -0.19473 -0.07589 -0.09731 621 PRO A N   
3309 C CA  . PRO A 418 ? 0.70969 0.58704 0.60049 -0.19256 -0.06727 -0.08688 621 PRO A CA  
3310 C C   . PRO A 418 ? 0.78257 0.61783 0.65257 -0.20677 -0.05673 -0.08683 621 PRO A C   
3311 O O   . PRO A 418 ? 0.75653 0.55184 0.59901 -0.20697 -0.05430 -0.08926 621 PRO A O   
3312 C CB  . PRO A 418 ? 0.66937 0.54028 0.55719 -0.16716 -0.06673 -0.07525 621 PRO A CB  
3313 C CG  . PRO A 418 ? 0.71711 0.56850 0.58394 -0.15914 -0.07041 -0.07933 621 PRO A CG  
3314 C CD  . PRO A 418 ? 0.76834 0.63543 0.63584 -0.17337 -0.07865 -0.09237 621 PRO A CD  
3315 N N   . GLU A 419 ? 0.73265 0.57625 0.61482 -0.21647 -0.04962 -0.08340 622 GLU A N   
3316 C CA  . GLU A 419 ? 0.78086 0.58636 0.64374 -0.22379 -0.03773 -0.07947 622 GLU A CA  
3317 C C   . GLU A 419 ? 0.69566 0.46244 0.53673 -0.20925 -0.03454 -0.06896 622 GLU A C   
3318 O O   . GLU A 419 ? 0.63032 0.41751 0.48660 -0.19159 -0.03676 -0.06045 622 GLU A O   
3319 C CB  . GLU A 419 ? 0.75209 0.58013 0.63373 -0.23611 -0.03030 -0.07829 622 GLU A CB  
3320 N N   . ASN A 420 ? 0.65596 0.37551 0.46687 -0.20792 -0.02827 -0.06742 623 ASN A N   
3321 C CA  . ASN A 420 ? 0.69275 0.37484 0.48232 -0.19168 -0.02486 -0.05756 623 ASN A CA  
3322 C C   . ASN A 420 ? 0.73126 0.41739 0.52754 -0.19369 -0.01873 -0.04864 623 ASN A C   
3323 O O   . ASN A 420 ? 0.73262 0.41618 0.52705 -0.20811 -0.01091 -0.04884 623 ASN A O   
3324 C CB  . ASN A 420 ? 0.80061 0.43197 0.55551 -0.18940 -0.01952 -0.05844 623 ASN A CB  
3325 C CG  . ASN A 420 ? 0.87716 0.50011 0.62202 -0.18369 -0.02520 -0.06659 623 ASN A CG  
3326 O OD1 . ASN A 420 ? 0.83962 0.49232 0.60098 -0.17709 -0.03318 -0.06968 623 ASN A OD1 
3327 N ND2 . ASN A 420 ? 0.98072 0.56498 0.69824 -0.18382 -0.02057 -0.06919 623 ASN A ND2 
3328 N N   . ILE A 421 ? 0.68132 0.38438 0.49041 -0.17287 -0.02104 -0.03950 624 ILE A N   
3329 C CA  . ILE A 421 ? 0.72412 0.43390 0.54009 -0.17170 -0.01640 -0.03096 624 ILE A CA  
3330 C C   . ILE A 421 ? 0.71515 0.38333 0.50371 -0.15451 -0.01366 -0.02248 624 ILE A C   
3331 O O   . ILE A 421 ? 0.62452 0.29672 0.41576 -0.13187 -0.01837 -0.01897 624 ILE A O   
3332 C CB  . ILE A 421 ? 0.63361 0.39418 0.48420 -0.16125 -0.02146 -0.02784 624 ILE A CB  
3333 C CG1 . ILE A 421 ? 0.58918 0.39081 0.46546 -0.17562 -0.02538 -0.03652 624 ILE A CG1 
3334 C CG2 . ILE A 421 ? 0.65689 0.42145 0.51182 -0.15806 -0.01671 -0.01917 624 ILE A CG2 
3335 C CD1 . ILE A 421 ? 0.55443 0.40134 0.46049 -0.16162 -0.03197 -0.03420 624 ILE A CD1 
3336 N N   . TYR A 422 ? 0.69635 0.32475 0.45776 -0.16491 -0.00593 -0.01957 625 TYR A N   
3337 C CA  . TYR A 422 ? 0.79636 0.38180 0.52758 -0.14721 -0.00420 -0.01144 625 TYR A CA  
3338 C C   . TYR A 422 ? 0.75104 0.35517 0.49383 -0.13633 -0.00419 -0.00224 625 TYR A C   
3339 O O   . TYR A 422 ? 0.82548 0.42478 0.56339 -0.15001 0.00242  0.00121  625 TYR A O   
3340 C CB  . TYR A 422 ? 0.75473 0.29518 0.45189 -0.15749 0.00406  -0.01156 625 TYR A CB  
3341 C CG  . TYR A 422 ? 0.79372 0.31873 0.47974 -0.16112 0.00332  -0.02016 625 TYR A CG  
3342 C CD1 . TYR A 422 ? 0.88191 0.37652 0.54717 -0.14082 -0.00059 -0.02013 625 TYR A CD1 
3343 C CD2 . TYR A 422 ? 0.83147 0.37492 0.52900 -0.18369 0.00625  -0.02906 625 TYR A CD2 
3344 C CE1 . TYR A 422 ? 0.95630 0.43620 0.61021 -0.14391 -0.00087 -0.02833 625 TYR A CE1 
3345 C CE2 . TYR A 422 ? 1.00365 0.53265 0.69002 -0.18727 0.00520  -0.03729 625 TYR A CE2 
3346 C CZ  . TYR A 422 ? 0.96839 0.46451 0.63215 -0.16772 0.00190  -0.03664 625 TYR A CZ  
3347 O OH  . TYR A 422 ? 1.11302 0.59447 0.76485 -0.17101 0.00127  -0.04496 625 TYR A OH  
3348 N N   . ILE A 423 ? 0.65260 0.27884 0.41061 -0.11259 -0.01106 0.00085  626 ILE A N   
3349 C CA  . ILE A 423 ? 0.75845 0.40265 0.52703 -0.10001 -0.01231 0.00846  626 ILE A CA  
3350 C C   . ILE A 423 ? 0.80887 0.40841 0.54246 -0.09694 -0.00789 0.01572  626 ILE A C   
3351 O O   . ILE A 423 ? 0.82008 0.37617 0.52213 -0.08605 -0.00829 0.01696  626 ILE A O   
3352 C CB  . ILE A 423 ? 0.72589 0.39315 0.51075 -0.07536 -0.01971 0.00889  626 ILE A CB  
3353 C CG1 . ILE A 423 ? 0.60711 0.31431 0.42201 -0.07906 -0.02310 0.00271  626 ILE A CG1 
3354 C CG2 . ILE A 423 ? 0.73145 0.41702 0.52650 -0.06294 -0.02147 0.01542  626 ILE A CG2 
3355 C CD1 . ILE A 423 ? 0.69478 0.42400 0.52491 -0.05814 -0.02818 0.00233  626 ILE A CD1 
3356 N N   . ASP A 424 ? 0.79815 0.40612 0.53468 -0.10573 -0.00348 0.02055  627 ASP A N   
3357 C CA  . ASP A 424 ? 0.72861 0.29371 0.42917 -0.10138 0.00049  0.02846  627 ASP A CA  
3358 C C   . ASP A 424 ? 0.82006 0.39671 0.52392 -0.07536 -0.00664 0.03447  627 ASP A C   
3359 O O   . ASP A 424 ? 0.77145 0.30969 0.44288 -0.05919 -0.00860 0.03974  627 ASP A O   
3360 C CB  . ASP A 424 ? 0.85581 0.41719 0.55111 -0.12664 0.01088  0.03012  627 ASP A CB  
3361 C CG  . ASP A 424 ? 0.98702 0.52550 0.66633 -0.14776 0.01926  0.02435  627 ASP A CG  
3362 O OD1 . ASP A 424 ? 0.97885 0.48379 0.63421 -0.13947 0.01796  0.02297  627 ASP A OD1 
3363 O OD2 . ASP A 424 ? 1.00817 0.56940 0.70227 -0.16976 0.02688  0.02002  627 ASP A OD2 
3364 N N   . GLY A 425 ? 0.68658 0.31448 0.42774 -0.07012 -0.01105 0.03316  628 GLY A N   
3365 C CA  . GLY A 425 ? 0.63732 0.27883 0.38346 -0.04690 -0.01803 0.03690  628 GLY A CA  
3366 C C   . GLY A 425 ? 0.60741 0.30434 0.39535 -0.04526 -0.02138 0.03401  628 GLY A C   
3367 O O   . GLY A 425 ? 0.61515 0.33910 0.42742 -0.05925 -0.01926 0.02953  628 GLY A O   
3368 N N   . LEU A 426 ? 0.51319 0.22575 0.30773 -0.02731 -0.02705 0.03620  629 LEU A N   
3369 C CA  . LEU A 426 ? 0.49924 0.25936 0.32896 -0.02502 -0.02961 0.03391  629 LEU A CA  
3370 C C   . LEU A 426 ? 0.56941 0.33460 0.39548 -0.02516 -0.02868 0.03861  629 LEU A C   
3371 O O   . LEU A 426 ? 0.58281 0.32058 0.38126 -0.01517 -0.03059 0.04332  629 LEU A O   
3372 C CB  . LEU A 426 ? 0.48879 0.26907 0.33367 -0.00503 -0.03673 0.03001  629 LEU A CB  
3373 C CG  . LEU A 426 ? 0.55098 0.33990 0.40828 -0.00266 -0.03772 0.02402  629 LEU A CG  
3374 C CD1 . LEU A 426 ? 0.77082 0.51936 0.60039 -0.00304 -0.03646 0.02364  629 LEU A CD1 
3375 C CD2 . LEU A 426 ? 0.55456 0.36637 0.42695 0.01630  -0.04299 0.02016  629 LEU A CD2 
3376 N N   . THR A 427 ? 0.41695 0.21530 0.26847 -0.03541 -0.02595 0.03725  630 THR A N   
3377 C CA  . THR A 427 ? 0.47146 0.28347 0.32593 -0.03268 -0.02615 0.03988  630 THR A CA  
3378 C C   . THR A 427 ? 0.51318 0.36349 0.39749 -0.02248 -0.03144 0.03554  630 THR A C   
3379 O O   . THR A 427 ? 0.45235 0.32767 0.36184 -0.02881 -0.03009 0.03158  630 THR A O   
3380 C CB  . THR A 427 ? 0.50490 0.32386 0.36370 -0.05209 -0.01772 0.04096  630 THR A CB  
3381 O OG1 . THR A 427 ? 0.54099 0.32199 0.36901 -0.06314 -0.01127 0.04479  630 THR A OG1 
3382 C CG2 . THR A 427 ? 0.47544 0.31251 0.34022 -0.04855 -0.01789 0.04244  630 THR A CG2 
3383 N N   . THR A 428 ? 0.43428 0.28824 0.31431 -0.00688 -0.03748 0.03584  631 THR A N   
3384 C CA  . THR A 428 ? 0.41356 0.30119 0.31945 0.00281  -0.04226 0.03046  631 THR A CA  
3385 C C   . THR A 428 ? 0.48292 0.39016 0.39703 0.00219  -0.04262 0.03028  631 THR A C   
3386 O O   . THR A 428 ? 0.45542 0.34673 0.34914 0.00162  -0.04205 0.03465  631 THR A O   
3387 C CB  . THR A 428 ? 0.49650 0.37991 0.39589 0.02237  -0.04986 0.02788  631 THR A CB  
3388 O OG1 . THR A 428 ? 0.52096 0.38651 0.39586 0.03355  -0.05476 0.03147  631 THR A OG1 
3389 C CG2 . THR A 428 ? 0.48638 0.34559 0.37315 0.02447  -0.04927 0.02787  631 THR A CG2 
3390 N N   . LEU A 429 ? 0.43879 0.37833 0.38054 0.00196  -0.04300 0.02500  632 LEU A N   
3391 C CA  . LEU A 429 ? 0.38822 0.34805 0.33998 0.00124  -0.04330 0.02306  632 LEU A CA  
3392 C C   . LEU A 429 ? 0.37404 0.35754 0.34170 0.01238  -0.04904 0.01626  632 LEU A C   
3393 O O   . LEU A 429 ? 0.38996 0.39005 0.37743 0.01102  -0.04745 0.01175  632 LEU A O   
3394 C CB  . LEU A 429 ? 0.33006 0.30523 0.29941 -0.01270 -0.03637 0.02239  632 LEU A CB  
3395 C CG  . LEU A 429 ? 0.35851 0.35187 0.33670 -0.01399 -0.03568 0.01984  632 LEU A CG  
3396 C CD1 . LEU A 429 ? 0.36335 0.34257 0.31864 -0.01132 -0.03718 0.02330  632 LEU A CD1 
3397 C CD2 . LEU A 429 ? 0.27637 0.28263 0.27070 -0.02537 -0.02887 0.01898  632 LEU A CD2 
3398 N N   . ASP A 430 ? 0.34634 0.33189 0.30460 0.02284  -0.05546 0.01499  633 ASP A N   
3399 C CA  . ASP A 430 ? 0.34579 0.35802 0.32026 0.03263  -0.06139 0.00679  633 ASP A CA  
3400 C C   . ASP A 430 ? 0.33986 0.37541 0.33096 0.02417  -0.05880 0.00234  633 ASP A C   
3401 O O   . ASP A 430 ? 0.32218 0.35038 0.30562 0.01590  -0.05496 0.00620  633 ASP A O   
3402 C CB  . ASP A 430 ? 0.36947 0.37287 0.32418 0.05003  -0.07131 0.00676  633 ASP A CB  
3403 C CG  . ASP A 430 ? 0.44594 0.48011 0.41894 0.06194  -0.07857 -0.00341 633 ASP A CG  
3404 O OD1 . ASP A 430 ? 0.43155 0.48556 0.41067 0.06323  -0.08273 -0.00851 633 ASP A OD1 
3405 O OD2 . ASP A 430 ? 0.45133 0.49086 0.43253 0.06977  -0.07993 -0.00718 633 ASP A OD2 
3406 N N   . LYS A 431 ? 0.29736 0.36057 0.31089 0.02549  -0.05992 -0.00652 634 LYS A N   
3407 C CA  . LYS A 431 ? 0.31939 0.40180 0.34696 0.01690  -0.05701 -0.01174 634 LYS A CA  
3408 C C   . LYS A 431 ? 0.29486 0.37780 0.30902 0.02137  -0.06288 -0.01244 634 LYS A C   
3409 O O   . LYS A 431 ? 0.27173 0.35968 0.28859 0.01279  -0.05918 -0.01380 634 LYS A O   
3410 C CB  . LYS A 431 ? 0.32274 0.43297 0.37446 0.01608  -0.05640 -0.02211 634 LYS A CB  
3411 C CG  . LYS A 431 ? 0.40022 0.51029 0.46468 0.00839  -0.04827 -0.02182 634 LYS A CG  
3412 C CD  . LYS A 431 ? 0.48983 0.62485 0.57429 0.00896  -0.04718 -0.03213 634 LYS A CD  
3413 C CE  . LYS A 431 ? 0.46955 0.59950 0.56050 0.00375  -0.03951 -0.03073 634 LYS A CE  
3414 N NZ  . LYS A 431 ? 0.49131 0.64484 0.60037 0.00315  -0.03649 -0.04100 634 LYS A NZ  
3415 N N   . GLY A 432 ? 0.28238 0.35905 0.28024 0.03581  -0.07224 -0.01178 635 GLY A N   
3416 C CA  . GLY A 432 ? 0.38908 0.46564 0.37067 0.04255  -0.07954 -0.01268 635 GLY A CA  
3417 C C   . GLY A 432 ? 0.41389 0.52415 0.41441 0.04316  -0.08436 -0.02490 635 GLY A C   
3418 O O   . GLY A 432 ? 0.30026 0.41441 0.29529 0.03891  -0.08506 -0.02701 635 GLY A O   
3419 N N   A GLU A 433 ? 0.35414 0.48953 0.37649 0.04781  -0.08735 -0.03398 636 GLU A N   
3420 N N   B GLU A 433 ? 0.35812 0.49327 0.38053 0.04773  -0.08722 -0.03388 636 GLU A N   
3421 C CA  A GLU A 433 ? 0.36131 0.53159 0.40583 0.04417  -0.08971 -0.04743 636 GLU A CA  
3422 C CA  B GLU A 433 ? 0.36125 0.53169 0.40581 0.04472  -0.08996 -0.04747 636 GLU A CA  
3423 C C   A GLU A 433 ? 0.38085 0.56270 0.41394 0.05640  -0.10273 -0.05287 636 GLU A C   
3424 C C   B GLU A 433 ? 0.38149 0.56268 0.41393 0.05705  -0.10299 -0.05260 636 GLU A C   
3425 O O   A GLU A 433 ? 0.36530 0.56405 0.40490 0.04926  -0.10365 -0.06067 636 GLU A O   
3426 O O   B GLU A 433 ? 0.36676 0.56414 0.40498 0.05001  -0.10396 -0.06010 636 GLU A O   
3427 C CB  A GLU A 433 ? 0.38148 0.57695 0.45202 0.04527  -0.08842 -0.05648 636 GLU A CB  
3428 C CB  B GLU A 433 ? 0.38159 0.57703 0.45152 0.04674  -0.08916 -0.05643 636 GLU A CB  
3429 C CG  A GLU A 433 ? 0.42956 0.61350 0.50911 0.03384  -0.07612 -0.05159 636 GLU A CG  
3430 C CG  B GLU A 433 ? 0.41702 0.64173 0.51414 0.03225  -0.08288 -0.06863 636 GLU A CG  
3431 C CD  A GLU A 433 ? 0.55427 0.76532 0.66157 0.02343  -0.06919 -0.06269 636 GLU A CD  
3432 C CD  B GLU A 433 ? 0.55041 0.76721 0.65921 0.01837  -0.06924 -0.06578 636 GLU A CD  
3433 O OE1 A GLU A 433 ? 0.58539 0.81090 0.70264 0.01245  -0.06635 -0.07005 636 GLU A OE1 
3434 O OE1 B GLU A 433 ? 0.56744 0.76407 0.66820 0.02213  -0.06653 -0.05682 636 GLU A OE1 
3435 O OE2 A GLU A 433 ? 0.49793 0.71425 0.61540 0.02558  -0.06585 -0.06443 636 GLU A OE2 
3436 O OE2 B GLU A 433 ? 0.60178 0.83050 0.72556 0.00378  -0.06130 -0.07262 636 GLU A OE2 
3437 N N   A ASP A 434 ? 0.36170 0.53336 0.37583 0.07552  -0.11332 -0.04929 637 ASP A N   
3438 N N   B ASP A 434 ? 0.36519 0.53609 0.37879 0.07621  -0.11350 -0.04900 637 ASP A N   
3439 C CA  A ASP A 434 ? 0.38967 0.57199 0.39021 0.08987  -0.12745 -0.05446 637 ASP A CA  
3440 C CA  B ASP A 434 ? 0.38985 0.56967 0.38843 0.09106  -0.12771 -0.05354 637 ASP A CA  
3441 C C   A ASP A 434 ? 0.38290 0.54416 0.35830 0.08367  -0.12617 -0.04803 637 ASP A C   
3442 C C   B ASP A 434 ? 0.38305 0.54406 0.35848 0.08391  -0.12618 -0.04791 637 ASP A C   
3443 O O   A ASP A 434 ? 0.36175 0.54083 0.33590 0.08503  -0.13340 -0.05608 637 ASP A O   
3444 O O   B ASP A 434 ? 0.36433 0.54455 0.34000 0.08491  -0.13327 -0.05643 637 ASP A O   
3445 C CB  A ASP A 434 ? 0.42400 0.59369 0.40455 0.11398  -0.13905 -0.05064 637 ASP A CB  
3446 C CB  B ASP A 434 ? 0.42858 0.59023 0.40376 0.11434  -0.13826 -0.04788 637 ASP A CB  
3447 C CG  A ASP A 434 ? 0.45380 0.65552 0.46171 0.12403  -0.14341 -0.06160 637 ASP A CG  
3448 C CG  B ASP A 434 ? 0.46940 0.62997 0.41911 0.13193  -0.15346 -0.04923 637 ASP A CG  
3449 O OD1 A ASP A 434 ? 0.43208 0.66112 0.47286 0.10948  -0.13501 -0.07035 637 ASP A OD1 
3450 O OD1 B ASP A 434 ? 0.49662 0.69622 0.46363 0.13977  -0.16425 -0.06321 637 ASP A OD1 
3451 O OD2 A ASP A 434 ? 0.49767 0.69623 0.49297 0.14673  -0.15463 -0.06167 637 ASP A OD2 
3452 O OD2 B ASP A 434 ? 0.56282 0.68345 0.47414 0.13753  -0.15449 -0.03672 637 ASP A OD2 
3453 N N   . GLN A 435 ? 0.36069 0.48587 0.31664 0.07597  -0.11654 -0.03464 638 GLN A N   
3454 C CA  . GLN A 435 ? 0.40778 0.51446 0.34164 0.06837  -0.11279 -0.02914 638 GLN A CA  
3455 C C   . GLN A 435 ? 0.36764 0.49572 0.32351 0.05146  -0.10561 -0.03753 638 GLN A C   
3456 O O   . GLN A 435 ? 0.35844 0.48947 0.30324 0.04967  -0.10828 -0.04101 638 GLN A O   
3457 C CB  . GLN A 435 ? 0.42086 0.48875 0.33368 0.06192  -0.10246 -0.01469 638 GLN A CB  
3458 C CG  . GLN A 435 ? 0.48762 0.52730 0.37528 0.07668  -0.10765 -0.00598 638 GLN A CG  
3459 C CD  . GLN A 435 ? 0.52287 0.56418 0.42974 0.07621  -0.10379 -0.00555 638 GLN A CD  
3460 O OE1 . GLN A 435 ? 0.41791 0.48959 0.35297 0.07931  -0.10712 -0.01522 638 GLN A OE1 
3461 N NE2 . GLN A 435 ? 0.49580 0.50458 0.38679 0.07119  -0.09607 0.00497  638 GLN A NE2 
3462 N N   . TRP A 436 ? 0.33269 0.47323 0.31700 0.03946  -0.09642 -0.04093 639 TRP A N   
3463 C CA  . TRP A 436 ? 0.35321 0.51051 0.35679 0.02420  -0.08925 -0.04925 639 TRP A CA  
3464 C C   . TRP A 436 ? 0.37646 0.56609 0.39210 0.02666  -0.09854 -0.06427 639 TRP A C   
3465 O O   . TRP A 436 ? 0.40090 0.59595 0.41369 0.01934  -0.09786 -0.07019 639 TRP A O   
3466 C CB  . TRP A 436 ? 0.28513 0.44626 0.31281 0.01328  -0.07853 -0.04949 639 TRP A CB  
3467 C CG  . TRP A 436 ? 0.26372 0.40049 0.28538 0.00403  -0.06706 -0.03909 639 TRP A CG  
3468 C CD1 . TRP A 436 ? 0.26410 0.38524 0.28550 0.00384  -0.06215 -0.03033 639 TRP A CD1 
3469 C CD2 . TRP A 436 ? 0.28652 0.41448 0.30299 -0.00600 -0.05930 -0.03775 639 TRP A CD2 
3470 N NE1 . TRP A 436 ? 0.28958 0.39553 0.30747 -0.00574 -0.05252 -0.02405 639 TRP A NE1 
3471 C CE2 . TRP A 436 ? 0.28867 0.39862 0.30381 -0.01121 -0.05035 -0.02836 639 TRP A CE2 
3472 C CE3 . TRP A 436 ? 0.30138 0.43578 0.31419 -0.01072 -0.05917 -0.04448 639 TRP A CE3 
3473 C CZ2 . TRP A 436 ? 0.28900 0.38968 0.30102 -0.01960 -0.04152 -0.02573 639 TRP A CZ2 
3474 C CZ3 . TRP A 436 ? 0.27544 0.39714 0.28307 -0.01920 -0.04961 -0.04133 639 TRP A CZ3 
3475 C CH2 . TRP A 436 ? 0.27314 0.37930 0.28119 -0.02294 -0.04097 -0.03210 639 TRP A CH2 
3476 N N   . LYS A 437 ? 0.30344 0.51652 0.33334 0.03684  -0.10723 -0.07175 640 LYS A N   
3477 C CA  . LYS A 437 ? 0.31414 0.56394 0.35905 0.03912  -0.11685 -0.08805 640 LYS A CA  
3478 C C   . LYS A 437 ? 0.38145 0.62886 0.40103 0.04911  -0.12884 -0.08922 640 LYS A C   
3479 O O   . LYS A 437 ? 0.32648 0.59486 0.35240 0.04275  -0.13230 -0.10129 640 LYS A O   
3480 C CB  . LYS A 437 ? 0.30088 0.57754 0.36441 0.05143  -0.12479 -0.09563 640 LYS A CB  
3481 C CG  . LYS A 437 ? 0.44507 0.73577 0.53862 0.03927  -0.11336 -0.10038 640 LYS A CG  
3482 C CD  . LYS A 437 ? 0.47949 0.78955 0.58557 0.05480  -0.12032 -0.10467 640 LYS A CD  
3483 C CE  . LYS A 437 ? 0.42941 0.74688 0.55964 0.04377  -0.10764 -0.10690 640 LYS A CE  
3484 N NZ  . LYS A 437 ? 0.44046 0.77244 0.57955 0.05945  -0.11233 -0.11052 640 LYS A NZ  
3485 N N   . LYS A 438 ? 0.33208 0.55217 0.32045 0.06440  -0.13510 -0.07710 641 LYS A N   
3486 C CA  . LYS A 438 ? 0.39549 0.60805 0.35378 0.07488  -0.14615 -0.07666 641 LYS A CA  
3487 C C   . LYS A 438 ? 0.34586 0.54343 0.29212 0.05943  -0.13675 -0.07459 641 LYS A C   
3488 O O   . LYS A 438 ? 0.37621 0.58430 0.31245 0.06031  -0.14397 -0.08248 641 LYS A O   
3489 C CB  . LYS A 438 ? 0.41394 0.59285 0.33680 0.09333  -0.15242 -0.06260 641 LYS A CB  
3490 C CG  . LYS A 438 ? 0.50497 0.69993 0.43127 0.11548  -0.16707 -0.06706 641 LYS A CG  
3491 C CD  . LYS A 438 ? 0.65097 0.80392 0.54219 0.13134  -0.16932 -0.05145 641 LYS A CD  
3492 N N   . TRP A 439 ? 0.35512 0.52898 0.30176 0.04615  -0.12108 -0.06469 642 TRP A N   
3493 C CA  . TRP A 439 ? 0.38090 0.54311 0.31978 0.03205  -0.11093 -0.06386 642 TRP A CA  
3494 C C   . TRP A 439 ? 0.42523 0.61599 0.38857 0.01993  -0.10958 -0.07964 642 TRP A C   
3495 O O   . TRP A 439 ? 0.39043 0.58355 0.34244 0.01623  -0.11134 -0.08591 642 TRP A O   
3496 C CB  . TRP A 439 ? 0.36296 0.50088 0.30346 0.02125  -0.09511 -0.05229 642 TRP A CB  
3497 C CG  . TRP A 439 ? 0.49232 0.61920 0.42484 0.00909  -0.08455 -0.05175 642 TRP A CG  
3498 C CD1 . TRP A 439 ? 0.46665 0.57144 0.36885 0.01014  -0.08197 -0.04479 642 TRP A CD1 
3499 C CD2 . TRP A 439 ? 0.42671 0.56294 0.38011 -0.00521 -0.07462 -0.05895 642 TRP A CD2 
3500 N NE1 . TRP A 439 ? 0.44632 0.54925 0.35180 -0.00205 -0.07111 -0.04788 642 TRP A NE1 
3501 C CE2 . TRP A 439 ? 0.46034 0.58098 0.39616 -0.01079 -0.06695 -0.05638 642 TRP A CE2 
3502 C CE3 . TRP A 439 ? 0.48206 0.63572 0.46501 -0.01373 -0.07062 -0.06715 642 TRP A CE3 
3503 C CZ2 . TRP A 439 ? 0.51079 0.63293 0.45800 -0.02261 -0.05657 -0.06208 642 TRP A CZ2 
3504 C CZ3 . TRP A 439 ? 0.42215 0.57374 0.41373 -0.02638 -0.06000 -0.07190 642 TRP A CZ3 
3505 C CH2 . TRP A 439 ? 0.43713 0.57317 0.41111 -0.02977 -0.05363 -0.06950 642 TRP A CH2 
3506 N N   . LEU A 440 ? 0.37825 0.58922 0.37330 0.01297  -0.10585 -0.08665 643 LEU A N   
3507 C CA  . LEU A 440 ? 0.34589 0.58085 0.36332 -0.00088 -0.10273 -0.10196 643 LEU A CA  
3508 C C   . LEU A 440 ? 0.42740 0.69204 0.44542 0.00535  -0.11771 -0.11671 643 LEU A C   
3509 O O   . LEU A 440 ? 0.45999 0.73276 0.47696 -0.00408 -0.11747 -0.12720 643 LEU A O   
3510 C CB  . LEU A 440 ? 0.40765 0.65570 0.45533 -0.00922 -0.09513 -0.10564 643 LEU A CB  
3511 C CG  . LEU A 440 ? 0.52138 0.77862 0.58761 -0.02835 -0.08480 -0.11686 643 LEU A CG  
3512 C CD1 . LEU A 440 ? 0.46365 0.69307 0.51389 -0.03681 -0.07450 -0.11090 643 LEU A CD1 
3513 C CD2 . LEU A 440 ? 0.52053 0.78114 0.60916 -0.03535 -0.07549 -0.11617 643 LEU A CD2 
3514 N N   . GLU A 441 ? 0.36570 0.64704 0.38468 0.02212  -0.13144 -0.11841 644 GLU A N   
3515 C CA  . GLU A 441 ? 0.37185 0.67837 0.39129 0.03046  -0.14467 -0.13026 644 GLU A CA  
3516 C C   . GLU A 441 ? 0.47192 0.76355 0.45777 0.03544  -0.15176 -0.12846 644 GLU A C   
3517 O O   . GLU A 441 ? 0.45455 0.76036 0.44204 0.03212  -0.15549 -0.13896 644 GLU A O   
3518 C CB  . GLU A 441 ? 0.41085 0.72582 0.43313 0.05035  -0.15412 -0.12747 644 GLU A CB  
3519 C CG  . GLU A 441 ? 0.46373 0.79678 0.48254 0.06236  -0.16607 -0.13579 644 GLU A CG  
3520 N N   . ALA A 442 ? 0.46557 0.72306 0.41939 0.04240  -0.15050 -0.11329 645 ALA A N   
3521 C CA  . ALA A 442 ? 0.51036 0.74961 0.42842 0.04653  -0.15487 -0.11042 645 ALA A CA  
3522 C C   . ALA A 442 ? 0.52249 0.76084 0.44441 0.02721  -0.14401 -0.11783 645 ALA A C   
3523 O O   . ALA A 442 ? 0.55196 0.79314 0.45517 0.02801  -0.15061 -0.12495 645 ALA A O   
3524 C CB  . ALA A 442 ? 0.40876 0.60478 0.29234 0.05453  -0.14983 -0.09036 645 ALA A CB  
3525 N N   . HIS A 443 ? 0.44029 0.67337 0.38435 0.01086  -0.12779 -0.11657 646 HIS A N   
3526 C CA  . HIS A 443 ? 0.53971 0.76818 0.48653 -0.00622 -0.11660 -0.12340 646 HIS A CA  
3527 C C   . HIS A 443 ? 0.56750 0.82943 0.53337 -0.01484 -0.12304 -0.14432 646 HIS A C   
3528 O O   . HIS A 443 ? 0.58098 0.84386 0.53344 -0.01988 -0.12504 -0.15335 646 HIS A O   
3529 C CB  . HIS A 443 ? 0.51595 0.72826 0.47925 -0.01855 -0.09881 -0.11606 646 HIS A CB  
3530 C CG  . HIS A 443 ? 0.63709 0.82423 0.58516 -0.02700 -0.08593 -0.11150 646 HIS A CG  
3531 N ND1 . HIS A 443 ? 0.60945 0.76943 0.53928 -0.02314 -0.07832 -0.09609 646 HIS A ND1 
3532 C CD2 . HIS A 443 ? 0.62427 0.80993 0.57237 -0.03887 -0.07905 -0.12135 646 HIS A CD2 
3533 C CE1 . HIS A 443 ? 0.63252 0.77845 0.55394 -0.03144 -0.06733 -0.09687 646 HIS A CE1 
3534 N NE2 . HIS A 443 ? 0.73182 0.89109 0.66285 -0.04027 -0.06771 -0.11173 646 HIS A NE2 
3535 N N   . GLN A 444 ? 0.50799 0.79835 0.50487 -0.01745 -0.12590 -0.15318 647 GLN A N   
3536 C CA  . GLN A 444 ? 0.58456 0.89758 0.60211 -0.02635 -0.12567 -0.16763 647 GLN A CA  
3537 C C   . GLN A 444 ? 0.67030 0.99563 0.67413 -0.01385 -0.14036 -0.17257 647 GLN A C   
3538 O O   . GLN A 444 ? 0.60729 0.94709 0.61900 -0.02266 -0.14067 -0.18535 647 GLN A O   
3539 C CB  . GLN A 444 ? 0.58418 0.91659 0.63504 -0.02986 -0.12087 -0.17072 647 GLN A CB  
3540 C CG  . GLN A 444 ? 0.69585 1.01661 0.76205 -0.04772 -0.10396 -0.16993 647 GLN A CG  
3541 C CD  . GLN A 444 ? 0.79867 1.12647 0.88625 -0.04575 -0.09944 -0.16508 647 GLN A CD  
3542 O OE1 . GLN A 444 ? 0.87013 1.21738 0.96774 -0.03397 -0.10709 -0.16632 647 GLN A OE1 
3543 N NE2 . GLN A 444 ? 0.65989 0.97089 0.75333 -0.05680 -0.08666 -0.15983 647 GLN A NE2 
3544 N N   . LYS A 445 ? 0.61285 0.93010 0.59392 0.00636  -0.15224 -0.16251 648 LYS A N   
3545 C CA  . LYS A 445 ? 0.61929 0.94246 0.58141 0.01929  -0.16620 -0.16564 648 LYS A CA  
3546 C C   . LYS A 445 ? 0.66446 0.96655 0.59384 0.01540  -0.16591 -0.16517 648 LYS A C   
3547 O O   . LYS A 445 ? 0.65492 0.96516 0.57404 0.01806  -0.17426 -0.17278 648 LYS A O   
3548 C CB  . LYS A 445 ? 0.60495 0.92123 0.55051 0.04306  -0.17791 -0.15421 648 LYS A CB  
3549 N N   . GLY A 446 ? 0.65021 0.92625 0.56236 0.00938  -0.15613 -0.15705 649 GLY A N   
3550 C CA  . GLY A 446 ? 0.72623 0.98228 0.60700 0.00504  -0.15326 -0.15754 649 GLY A CA  
3551 C C   . GLY A 446 ? 0.71458 0.97533 0.61031 -0.01582 -0.14216 -0.17087 649 GLY A C   
3552 O O   . GLY A 446 ? 0.72303 0.96510 0.59625 -0.02237 -0.13522 -0.17196 649 GLY A O   
3553 N N   . GLU A 447 ? 0.64078 0.92423 0.57262 -0.02623 -0.13916 -0.18096 650 GLU A N   
3554 C CA  . GLU A 447 ? 0.67861 0.96209 0.62592 -0.04691 -0.12658 -0.19248 650 GLU A CA  
3555 C C   . GLU A 447 ? 0.75416 1.03608 0.68443 -0.05154 -0.12981 -0.20304 650 GLU A C   
3556 O O   . GLU A 447 ? 0.75036 1.04416 0.66996 -0.04064 -0.14372 -0.20560 650 GLU A O   
3557 C CB  . GLU A 447 ? 0.61917 0.92637 0.60486 -0.05568 -0.12288 -0.20002 650 GLU A CB  
3558 C CG  . GLU A 447 ? 0.74852 1.04503 0.75087 -0.07571 -0.10519 -0.20417 650 GLU A CG  
3559 C CD  . GLU A 447 ? 0.78937 1.06757 0.79228 -0.07581 -0.09615 -0.19225 650 GLU A CD  
3560 O OE1 . GLU A 447 ? 0.79441 1.05118 0.77310 -0.07143 -0.09430 -0.18447 650 GLU A OE1 
3561 O OE2 . GLU A 447 ? 0.69718 0.98188 0.72404 -0.08042 -0.08990 -0.19042 650 GLU A OE2 
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