data_9C0V
# 
_entry.id   9C0V 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9C0V         pdb_00009c0v 10.2210/pdb9c0v/pdb 
WWPDB D_1000284396 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-01-29 ? 
2 'Structure model' 1 1 2025-05-28 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.journal_volume'          
7  2 'Structure model' '_citation.page_first'              
8  2 'Structure model' '_citation.page_last'               
9  2 'Structure model' '_citation.pdbx_database_id_DOI'    
10 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
11 2 'Structure model' '_citation.title'                   
12 2 'Structure model' '_citation.year'                    
# 
_database_PDB_caveat.id     1 
_database_PDB_caveat.text   'NAG S 2 HAS WRONG CHIRALITY AT ATOM C1' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9C0V 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              kimyen@snu.ac.kr 
_pdbx_contact_author.name_first         Wilson 
_pdbx_contact_author.name_last          Ian 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6469-2419 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Nguyen, T.K.Y.' 1 ? 
'Wilson, I.A.'   2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_id_ASTM           PNASA6 
_citation.journal_id_CSD            0040 
_citation.journal_id_ISSN           1091-6490 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            122 
_citation.language                  ? 
_citation.page_first                e2416628122 
_citation.page_last                 e2416628122 
_citation.title                     
'Structural characterization of influenza group 1 chimeric hemagglutinins as broad vaccine immunogens.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.2416628122 
_citation.pdbx_database_id_PubMed   39937865 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Nguyen, Y.T.K.'  1  0000-0001-6424-4168 
primary 'Zhu, X.'         2  0000-0002-6021-3740 
primary 'Han, J.'         3  0000-0002-3402-2609 
primary 'Rodriguez, A.J.' 4  0009-0009-6510-7558 
primary 'Sun, W.'         5  0000-0002-2435-5047 
primary 'Yu, W.'          6  0000-0002-4025-2646 
primary 'Palese, P.'      7  0000-0002-0337-5823 
primary 'Krammer, F.'     8  0000-0003-4121-776X 
primary 'Ward, A.B.'      9  0000-0001-7153-3769 
primary 'Wilson, I.A.'    10 0000-0002-6469-2419 
# 
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 Hemagglutinin 60956.332 2 ? ? ? ? 
2 polymer     man 'Antibody 3E1 Fab heavy chain' 23871.846 1 ? ? ? ? 
3 polymer     man 'Antibody 3E1 Fab light chain' 23483.084 1 ? ? ? ? 
4 branched    man 
'beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 586.542   2 ? 
? ? ? 
5 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   1 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;GDTLCIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDKHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYI
VEKANPVNDLCYPGDFNDYEELKHLLSRINHFEKIQIIPKSSWSSHEASLGVSSACPYQGKSSFFRNVVWLIKKNSTYPT
IKRSYNNTNQEDLLVLWGIHHPNDAAEQTKLYQNPTTYISVGTSTLNQRLVPRIATRSKVNGQSGRMEFFWTILKPNDAI
NFESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTTCQTPKGAINTSLPFQNIHPITIGKCPKYVKSTKLRLATGLRN
VPSIQSRGLFGAIAGFIEGGWTGMVDGWYGYHHQNEQGSGYAADLKSTQNAIDGITNKVNSVIEKMNTQFTAVGKEFNHL
EKRIENLNKKVDDGFLDIWTYNAELLVLLENERTLDYHDSNVKNLYEKVRSQLKNNAKEIGNGCFEFYHKCDNTCMESVK
NGTYDYPKYSEEAKLNREEIDSGRLVPRGSPGSGYIPEAPRDGQAYVRKDGEWVLLSTFLG
;
;GDTLCIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDKHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYI
VEKANPVNDLCYPGDFNDYEELKHLLSRINHFEKIQIIPKSSWSSHEASLGVSSACPYQGKSSFFRNVVWLIKKNSTYPT
IKRSYNNTNQEDLLVLWGIHHPNDAAEQTKLYQNPTTYISVGTSTLNQRLVPRIATRSKVNGQSGRMEFFWTILKPNDAI
NFESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTTCQTPKGAINTSLPFQNIHPITIGKCPKYVKSTKLRLATGLRN
VPSIQSRGLFGAIAGFIEGGWTGMVDGWYGYHHQNEQGSGYAADLKSTQNAIDGITNKVNSVIEKMNTQFTAVGKEFNHL
EKRIENLNKKVDDGFLDIWTYNAELLVLLENERTLDYHDSNVKNLYEKVRSQLKNNAKEIGNGCFEFYHKCDNTCMESVK
NGTYDYPKYSEEAKLNREEIDSGRLVPRGSPGSGYIPEAPRDGQAYVRKDGEWVLLSTFLG
;
A,B ? 
2 'polypeptide(L)' no no 
;QVQLQESGPGLVKPSETLSLTCSVSGASISSYYWIWIRQPAGKGLEWIGRFYTSGSPNYNPSLRSRVTMSVDTSKNQFSL
KLTSVTAADTAVYYCAREEHITFGGVIVRYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTV
SWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSC
;
;QVQLQESGPGLVKPSETLSLTCSVSGASISSYYWIWIRQPAGKGLEWIGRFYTSGSPNYNPSLRSRVTMSVDTSKNQFSL
KLTSVTAADTAVYYCAREEHITFGGVIVRYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTV
SWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSC
;
H   ? 
3 'polypeptide(L)' no no 
;DIQMTQSPATLSASVGDRVSITCRASQSISSWLAWYQQKPGKAPKLLIYKASSLESGVPSRFSGSGSGSEFTLTISSLQP
DDFAIYYCQQYNSYPWTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQ
ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
;DIQMTQSPATLSASVGDRVSITCRASQSISSWLAWYQQKPGKAPKLLIYKASSLESGVPSRFSGSGSGSEFTLTISSLQP
DDFAIYYCQQYNSYPWTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQ
ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
L   ? 
# 
_pdbx_entity_nonpoly.entity_id   5 
_pdbx_entity_nonpoly.name        2-acetamido-2-deoxy-beta-D-glucopyranose 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ASP n 
1 3   THR n 
1 4   LEU n 
1 5   CYS n 
1 6   ILE n 
1 7   GLY n 
1 8   TYR n 
1 9   HIS n 
1 10  ALA n 
1 11  ASN n 
1 12  ASN n 
1 13  SER n 
1 14  THR n 
1 15  ASP n 
1 16  THR n 
1 17  VAL n 
1 18  ASP n 
1 19  THR n 
1 20  VAL n 
1 21  LEU n 
1 22  GLU n 
1 23  LYS n 
1 24  ASN n 
1 25  VAL n 
1 26  THR n 
1 27  VAL n 
1 28  THR n 
1 29  HIS n 
1 30  SER n 
1 31  VAL n 
1 32  ASN n 
1 33  LEU n 
1 34  LEU n 
1 35  GLU n 
1 36  ASP n 
1 37  LYS n 
1 38  HIS n 
1 39  ASN n 
1 40  GLY n 
1 41  LYS n 
1 42  LEU n 
1 43  CYS n 
1 44  ASP n 
1 45  LEU n 
1 46  ASP n 
1 47  GLY n 
1 48  VAL n 
1 49  LYS n 
1 50  PRO n 
1 51  LEU n 
1 52  ILE n 
1 53  LEU n 
1 54  ARG n 
1 55  ASP n 
1 56  CYS n 
1 57  SER n 
1 58  VAL n 
1 59  ALA n 
1 60  GLY n 
1 61  TRP n 
1 62  LEU n 
1 63  LEU n 
1 64  GLY n 
1 65  ASN n 
1 66  PRO n 
1 67  MET n 
1 68  CYS n 
1 69  ASP n 
1 70  GLU n 
1 71  PHE n 
1 72  ILE n 
1 73  ASN n 
1 74  VAL n 
1 75  PRO n 
1 76  GLU n 
1 77  TRP n 
1 78  SER n 
1 79  TYR n 
1 80  ILE n 
1 81  VAL n 
1 82  GLU n 
1 83  LYS n 
1 84  ALA n 
1 85  ASN n 
1 86  PRO n 
1 87  VAL n 
1 88  ASN n 
1 89  ASP n 
1 90  LEU n 
1 91  CYS n 
1 92  TYR n 
1 93  PRO n 
1 94  GLY n 
1 95  ASP n 
1 96  PHE n 
1 97  ASN n 
1 98  ASP n 
1 99  TYR n 
1 100 GLU n 
1 101 GLU n 
1 102 LEU n 
1 103 LYS n 
1 104 HIS n 
1 105 LEU n 
1 106 LEU n 
1 107 SER n 
1 108 ARG n 
1 109 ILE n 
1 110 ASN n 
1 111 HIS n 
1 112 PHE n 
1 113 GLU n 
1 114 LYS n 
1 115 ILE n 
1 116 GLN n 
1 117 ILE n 
1 118 ILE n 
1 119 PRO n 
1 120 LYS n 
1 121 SER n 
1 122 SER n 
1 123 TRP n 
1 124 SER n 
1 125 SER n 
1 126 HIS n 
1 127 GLU n 
1 128 ALA n 
1 129 SER n 
1 130 LEU n 
1 131 GLY n 
1 132 VAL n 
1 133 SER n 
1 134 SER n 
1 135 ALA n 
1 136 CYS n 
1 137 PRO n 
1 138 TYR n 
1 139 GLN n 
1 140 GLY n 
1 141 LYS n 
1 142 SER n 
1 143 SER n 
1 144 PHE n 
1 145 PHE n 
1 146 ARG n 
1 147 ASN n 
1 148 VAL n 
1 149 VAL n 
1 150 TRP n 
1 151 LEU n 
1 152 ILE n 
1 153 LYS n 
1 154 LYS n 
1 155 ASN n 
1 156 SER n 
1 157 THR n 
1 158 TYR n 
1 159 PRO n 
1 160 THR n 
1 161 ILE n 
1 162 LYS n 
1 163 ARG n 
1 164 SER n 
1 165 TYR n 
1 166 ASN n 
1 167 ASN n 
1 168 THR n 
1 169 ASN n 
1 170 GLN n 
1 171 GLU n 
1 172 ASP n 
1 173 LEU n 
1 174 LEU n 
1 175 VAL n 
1 176 LEU n 
1 177 TRP n 
1 178 GLY n 
1 179 ILE n 
1 180 HIS n 
1 181 HIS n 
1 182 PRO n 
1 183 ASN n 
1 184 ASP n 
1 185 ALA n 
1 186 ALA n 
1 187 GLU n 
1 188 GLN n 
1 189 THR n 
1 190 LYS n 
1 191 LEU n 
1 192 TYR n 
1 193 GLN n 
1 194 ASN n 
1 195 PRO n 
1 196 THR n 
1 197 THR n 
1 198 TYR n 
1 199 ILE n 
1 200 SER n 
1 201 VAL n 
1 202 GLY n 
1 203 THR n 
1 204 SER n 
1 205 THR n 
1 206 LEU n 
1 207 ASN n 
1 208 GLN n 
1 209 ARG n 
1 210 LEU n 
1 211 VAL n 
1 212 PRO n 
1 213 ARG n 
1 214 ILE n 
1 215 ALA n 
1 216 THR n 
1 217 ARG n 
1 218 SER n 
1 219 LYS n 
1 220 VAL n 
1 221 ASN n 
1 222 GLY n 
1 223 GLN n 
1 224 SER n 
1 225 GLY n 
1 226 ARG n 
1 227 MET n 
1 228 GLU n 
1 229 PHE n 
1 230 PHE n 
1 231 TRP n 
1 232 THR n 
1 233 ILE n 
1 234 LEU n 
1 235 LYS n 
1 236 PRO n 
1 237 ASN n 
1 238 ASP n 
1 239 ALA n 
1 240 ILE n 
1 241 ASN n 
1 242 PHE n 
1 243 GLU n 
1 244 SER n 
1 245 ASN n 
1 246 GLY n 
1 247 ASN n 
1 248 PHE n 
1 249 ILE n 
1 250 ALA n 
1 251 PRO n 
1 252 GLU n 
1 253 TYR n 
1 254 ALA n 
1 255 TYR n 
1 256 LYS n 
1 257 ILE n 
1 258 VAL n 
1 259 LYS n 
1 260 LYS n 
1 261 GLY n 
1 262 ASP n 
1 263 SER n 
1 264 THR n 
1 265 ILE n 
1 266 MET n 
1 267 LYS n 
1 268 SER n 
1 269 GLU n 
1 270 LEU n 
1 271 GLU n 
1 272 TYR n 
1 273 GLY n 
1 274 ASN n 
1 275 CYS n 
1 276 ASN n 
1 277 THR n 
1 278 THR n 
1 279 CYS n 
1 280 GLN n 
1 281 THR n 
1 282 PRO n 
1 283 LYS n 
1 284 GLY n 
1 285 ALA n 
1 286 ILE n 
1 287 ASN n 
1 288 THR n 
1 289 SER n 
1 290 LEU n 
1 291 PRO n 
1 292 PHE n 
1 293 GLN n 
1 294 ASN n 
1 295 ILE n 
1 296 HIS n 
1 297 PRO n 
1 298 ILE n 
1 299 THR n 
1 300 ILE n 
1 301 GLY n 
1 302 LYS n 
1 303 CYS n 
1 304 PRO n 
1 305 LYS n 
1 306 TYR n 
1 307 VAL n 
1 308 LYS n 
1 309 SER n 
1 310 THR n 
1 311 LYS n 
1 312 LEU n 
1 313 ARG n 
1 314 LEU n 
1 315 ALA n 
1 316 THR n 
1 317 GLY n 
1 318 LEU n 
1 319 ARG n 
1 320 ASN n 
1 321 VAL n 
1 322 PRO n 
1 323 SER n 
1 324 ILE n 
1 325 GLN n 
1 326 SER n 
1 327 ARG n 
1 328 GLY n 
1 329 LEU n 
1 330 PHE n 
1 331 GLY n 
1 332 ALA n 
1 333 ILE n 
1 334 ALA n 
1 335 GLY n 
1 336 PHE n 
1 337 ILE n 
1 338 GLU n 
1 339 GLY n 
1 340 GLY n 
1 341 TRP n 
1 342 THR n 
1 343 GLY n 
1 344 MET n 
1 345 VAL n 
1 346 ASP n 
1 347 GLY n 
1 348 TRP n 
1 349 TYR n 
1 350 GLY n 
1 351 TYR n 
1 352 HIS n 
1 353 HIS n 
1 354 GLN n 
1 355 ASN n 
1 356 GLU n 
1 357 GLN n 
1 358 GLY n 
1 359 SER n 
1 360 GLY n 
1 361 TYR n 
1 362 ALA n 
1 363 ALA n 
1 364 ASP n 
1 365 LEU n 
1 366 LYS n 
1 367 SER n 
1 368 THR n 
1 369 GLN n 
1 370 ASN n 
1 371 ALA n 
1 372 ILE n 
1 373 ASP n 
1 374 GLY n 
1 375 ILE n 
1 376 THR n 
1 377 ASN n 
1 378 LYS n 
1 379 VAL n 
1 380 ASN n 
1 381 SER n 
1 382 VAL n 
1 383 ILE n 
1 384 GLU n 
1 385 LYS n 
1 386 MET n 
1 387 ASN n 
1 388 THR n 
1 389 GLN n 
1 390 PHE n 
1 391 THR n 
1 392 ALA n 
1 393 VAL n 
1 394 GLY n 
1 395 LYS n 
1 396 GLU n 
1 397 PHE n 
1 398 ASN n 
1 399 HIS n 
1 400 LEU n 
1 401 GLU n 
1 402 LYS n 
1 403 ARG n 
1 404 ILE n 
1 405 GLU n 
1 406 ASN n 
1 407 LEU n 
1 408 ASN n 
1 409 LYS n 
1 410 LYS n 
1 411 VAL n 
1 412 ASP n 
1 413 ASP n 
1 414 GLY n 
1 415 PHE n 
1 416 LEU n 
1 417 ASP n 
1 418 ILE n 
1 419 TRP n 
1 420 THR n 
1 421 TYR n 
1 422 ASN n 
1 423 ALA n 
1 424 GLU n 
1 425 LEU n 
1 426 LEU n 
1 427 VAL n 
1 428 LEU n 
1 429 LEU n 
1 430 GLU n 
1 431 ASN n 
1 432 GLU n 
1 433 ARG n 
1 434 THR n 
1 435 LEU n 
1 436 ASP n 
1 437 TYR n 
1 438 HIS n 
1 439 ASP n 
1 440 SER n 
1 441 ASN n 
1 442 VAL n 
1 443 LYS n 
1 444 ASN n 
1 445 LEU n 
1 446 TYR n 
1 447 GLU n 
1 448 LYS n 
1 449 VAL n 
1 450 ARG n 
1 451 SER n 
1 452 GLN n 
1 453 LEU n 
1 454 LYS n 
1 455 ASN n 
1 456 ASN n 
1 457 ALA n 
1 458 LYS n 
1 459 GLU n 
1 460 ILE n 
1 461 GLY n 
1 462 ASN n 
1 463 GLY n 
1 464 CYS n 
1 465 PHE n 
1 466 GLU n 
1 467 PHE n 
1 468 TYR n 
1 469 HIS n 
1 470 LYS n 
1 471 CYS n 
1 472 ASP n 
1 473 ASN n 
1 474 THR n 
1 475 CYS n 
1 476 MET n 
1 477 GLU n 
1 478 SER n 
1 479 VAL n 
1 480 LYS n 
1 481 ASN n 
1 482 GLY n 
1 483 THR n 
1 484 TYR n 
1 485 ASP n 
1 486 TYR n 
1 487 PRO n 
1 488 LYS n 
1 489 TYR n 
1 490 SER n 
1 491 GLU n 
1 492 GLU n 
1 493 ALA n 
1 494 LYS n 
1 495 LEU n 
1 496 ASN n 
1 497 ARG n 
1 498 GLU n 
1 499 GLU n 
1 500 ILE n 
1 501 ASP n 
1 502 SER n 
1 503 GLY n 
1 504 ARG n 
1 505 LEU n 
1 506 VAL n 
1 507 PRO n 
1 508 ARG n 
1 509 GLY n 
1 510 SER n 
1 511 PRO n 
1 512 GLY n 
1 513 SER n 
1 514 GLY n 
1 515 TYR n 
1 516 ILE n 
1 517 PRO n 
1 518 GLU n 
1 519 ALA n 
1 520 PRO n 
1 521 ARG n 
1 522 ASP n 
1 523 GLY n 
1 524 GLN n 
1 525 ALA n 
1 526 TYR n 
1 527 VAL n 
1 528 ARG n 
1 529 LYS n 
1 530 ASP n 
1 531 GLY n 
1 532 GLU n 
1 533 TRP n 
1 534 VAL n 
1 535 LEU n 
1 536 LEU n 
1 537 SER n 
1 538 THR n 
1 539 PHE n 
1 540 LEU n 
1 541 GLY n 
2 1   GLN n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   GLN n 
2 6   GLU n 
2 7   SER n 
2 8   GLY n 
2 9   PRO n 
2 10  GLY n 
2 11  LEU n 
2 12  VAL n 
2 13  LYS n 
2 14  PRO n 
2 15  SER n 
2 16  GLU n 
2 17  THR n 
2 18  LEU n 
2 19  SER n 
2 20  LEU n 
2 21  THR n 
2 22  CYS n 
2 23  SER n 
2 24  VAL n 
2 25  SER n 
2 26  GLY n 
2 27  ALA n 
2 28  SER n 
2 29  ILE n 
2 30  SER n 
2 31  SER n 
2 32  TYR n 
2 33  TYR n 
2 34  TRP n 
2 35  ILE n 
2 36  TRP n 
2 37  ILE n 
2 38  ARG n 
2 39  GLN n 
2 40  PRO n 
2 41  ALA n 
2 42  GLY n 
2 43  LYS n 
2 44  GLY n 
2 45  LEU n 
2 46  GLU n 
2 47  TRP n 
2 48  ILE n 
2 49  GLY n 
2 50  ARG n 
2 51  PHE n 
2 52  TYR n 
2 53  THR n 
2 54  SER n 
2 55  GLY n 
2 56  SER n 
2 57  PRO n 
2 58  ASN n 
2 59  TYR n 
2 60  ASN n 
2 61  PRO n 
2 62  SER n 
2 63  LEU n 
2 64  ARG n 
2 65  SER n 
2 66  ARG n 
2 67  VAL n 
2 68  THR n 
2 69  MET n 
2 70  SER n 
2 71  VAL n 
2 72  ASP n 
2 73  THR n 
2 74  SER n 
2 75  LYS n 
2 76  ASN n 
2 77  GLN n 
2 78  PHE n 
2 79  SER n 
2 80  LEU n 
2 81  LYS n 
2 82  LEU n 
2 83  THR n 
2 84  SER n 
2 85  VAL n 
2 86  THR n 
2 87  ALA n 
2 88  ALA n 
2 89  ASP n 
2 90  THR n 
2 91  ALA n 
2 92  VAL n 
2 93  TYR n 
2 94  TYR n 
2 95  CYS n 
2 96  ALA n 
2 97  ARG n 
2 98  GLU n 
2 99  GLU n 
2 100 HIS n 
2 101 ILE n 
2 102 THR n 
2 103 PHE n 
2 104 GLY n 
2 105 GLY n 
2 106 VAL n 
2 107 ILE n 
2 108 VAL n 
2 109 ARG n 
2 110 TYR n 
2 111 TRP n 
2 112 GLY n 
2 113 GLN n 
2 114 GLY n 
2 115 THR n 
2 116 LEU n 
2 117 VAL n 
2 118 THR n 
2 119 VAL n 
2 120 SER n 
2 121 SER n 
2 122 ALA n 
2 123 SER n 
2 124 THR n 
2 125 LYS n 
2 126 GLY n 
2 127 PRO n 
2 128 SER n 
2 129 VAL n 
2 130 PHE n 
2 131 PRO n 
2 132 LEU n 
2 133 ALA n 
2 134 PRO n 
2 135 SER n 
2 136 SER n 
2 137 LYS n 
2 138 SER n 
2 139 THR n 
2 140 SER n 
2 141 GLY n 
2 142 GLY n 
2 143 THR n 
2 144 ALA n 
2 145 ALA n 
2 146 LEU n 
2 147 GLY n 
2 148 CYS n 
2 149 LEU n 
2 150 VAL n 
2 151 LYS n 
2 152 ASP n 
2 153 TYR n 
2 154 PHE n 
2 155 PRO n 
2 156 GLU n 
2 157 PRO n 
2 158 VAL n 
2 159 THR n 
2 160 VAL n 
2 161 SER n 
2 162 TRP n 
2 163 ASN n 
2 164 SER n 
2 165 GLY n 
2 166 ALA n 
2 167 LEU n 
2 168 THR n 
2 169 SER n 
2 170 GLY n 
2 171 VAL n 
2 172 HIS n 
2 173 THR n 
2 174 PHE n 
2 175 PRO n 
2 176 ALA n 
2 177 VAL n 
2 178 LEU n 
2 179 GLN n 
2 180 SER n 
2 181 SER n 
2 182 GLY n 
2 183 LEU n 
2 184 TYR n 
2 185 SER n 
2 186 LEU n 
2 187 SER n 
2 188 SER n 
2 189 VAL n 
2 190 VAL n 
2 191 THR n 
2 192 VAL n 
2 193 PRO n 
2 194 SER n 
2 195 SER n 
2 196 SER n 
2 197 LEU n 
2 198 GLY n 
2 199 THR n 
2 200 GLN n 
2 201 THR n 
2 202 TYR n 
2 203 ILE n 
2 204 CYS n 
2 205 ASN n 
2 206 VAL n 
2 207 ASN n 
2 208 HIS n 
2 209 LYS n 
2 210 PRO n 
2 211 SER n 
2 212 ASN n 
2 213 THR n 
2 214 LYS n 
2 215 VAL n 
2 216 ASP n 
2 217 LYS n 
2 218 ARG n 
2 219 VAL n 
2 220 GLU n 
2 221 PRO n 
2 222 LYS n 
2 223 SER n 
2 224 CYS n 
3 1   ASP n 
3 2   ILE n 
3 3   GLN n 
3 4   MET n 
3 5   THR n 
3 6   GLN n 
3 7   SER n 
3 8   PRO n 
3 9   ALA n 
3 10  THR n 
3 11  LEU n 
3 12  SER n 
3 13  ALA n 
3 14  SER n 
3 15  VAL n 
3 16  GLY n 
3 17  ASP n 
3 18  ARG n 
3 19  VAL n 
3 20  SER n 
3 21  ILE n 
3 22  THR n 
3 23  CYS n 
3 24  ARG n 
3 25  ALA n 
3 26  SER n 
3 27  GLN n 
3 28  SER n 
3 29  ILE n 
3 30  SER n 
3 31  SER n 
3 32  TRP n 
3 33  LEU n 
3 34  ALA n 
3 35  TRP n 
3 36  TYR n 
3 37  GLN n 
3 38  GLN n 
3 39  LYS n 
3 40  PRO n 
3 41  GLY n 
3 42  LYS n 
3 43  ALA n 
3 44  PRO n 
3 45  LYS n 
3 46  LEU n 
3 47  LEU n 
3 48  ILE n 
3 49  TYR n 
3 50  LYS n 
3 51  ALA n 
3 52  SER n 
3 53  SER n 
3 54  LEU n 
3 55  GLU n 
3 56  SER n 
3 57  GLY n 
3 58  VAL n 
3 59  PRO n 
3 60  SER n 
3 61  ARG n 
3 62  PHE n 
3 63  SER n 
3 64  GLY n 
3 65  SER n 
3 66  GLY n 
3 67  SER n 
3 68  GLY n 
3 69  SER n 
3 70  GLU n 
3 71  PHE n 
3 72  THR n 
3 73  LEU n 
3 74  THR n 
3 75  ILE n 
3 76  SER n 
3 77  SER n 
3 78  LEU n 
3 79  GLN n 
3 80  PRO n 
3 81  ASP n 
3 82  ASP n 
3 83  PHE n 
3 84  ALA n 
3 85  ILE n 
3 86  TYR n 
3 87  TYR n 
3 88  CYS n 
3 89  GLN n 
3 90  GLN n 
3 91  TYR n 
3 92  ASN n 
3 93  SER n 
3 94  TYR n 
3 95  PRO n 
3 96  TRP n 
3 97  THR n 
3 98  PHE n 
3 99  GLY n 
3 100 GLN n 
3 101 GLY n 
3 102 THR n 
3 103 LYS n 
3 104 VAL n 
3 105 GLU n 
3 106 ILE n 
3 107 LYS n 
3 108 ARG n 
3 109 THR n 
3 110 VAL n 
3 111 ALA n 
3 112 ALA n 
3 113 PRO n 
3 114 SER n 
3 115 VAL n 
3 116 PHE n 
3 117 ILE n 
3 118 PHE n 
3 119 PRO n 
3 120 PRO n 
3 121 SER n 
3 122 ASP n 
3 123 GLU n 
3 124 GLN n 
3 125 LEU n 
3 126 LYS n 
3 127 SER n 
3 128 GLY n 
3 129 THR n 
3 130 ALA n 
3 131 SER n 
3 132 VAL n 
3 133 VAL n 
3 134 CYS n 
3 135 LEU n 
3 136 LEU n 
3 137 ASN n 
3 138 ASN n 
3 139 PHE n 
3 140 TYR n 
3 141 PRO n 
3 142 ARG n 
3 143 GLU n 
3 144 ALA n 
3 145 LYS n 
3 146 VAL n 
3 147 GLN n 
3 148 TRP n 
3 149 LYS n 
3 150 VAL n 
3 151 ASP n 
3 152 ASN n 
3 153 ALA n 
3 154 LEU n 
3 155 GLN n 
3 156 SER n 
3 157 GLY n 
3 158 ASN n 
3 159 SER n 
3 160 GLN n 
3 161 GLU n 
3 162 SER n 
3 163 VAL n 
3 164 THR n 
3 165 GLU n 
3 166 GLN n 
3 167 ASP n 
3 168 SER n 
3 169 LYS n 
3 170 ASP n 
3 171 SER n 
3 172 THR n 
3 173 TYR n 
3 174 SER n 
3 175 LEU n 
3 176 SER n 
3 177 SER n 
3 178 THR n 
3 179 LEU n 
3 180 THR n 
3 181 LEU n 
3 182 SER n 
3 183 LYS n 
3 184 ALA n 
3 185 ASP n 
3 186 TYR n 
3 187 GLU n 
3 188 LYS n 
3 189 HIS n 
3 190 LYS n 
3 191 VAL n 
3 192 TYR n 
3 193 ALA n 
3 194 CYS n 
3 195 GLU n 
3 196 VAL n 
3 197 THR n 
3 198 HIS n 
3 199 GLN n 
3 200 GLY n 
3 201 LEU n 
3 202 SER n 
3 203 SER n 
3 204 PRO n 
3 205 VAL n 
3 206 THR n 
3 207 LYS n 
3 208 SER n 
3 209 PHE n 
3 210 ASN n 
3 211 ARG n 
3 212 GLY n 
3 213 GLU n 
3 214 CYS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 541 ?     ? HA ? ? ? ? ? ? 'Influenza A virus' 11320 ? ? ? ? ? ? ? 'cabbage looper'  
'Trichoplusia ni'    7111  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 224 human ? ?  ? ? ? ? ? ? 'Homo sapiens'      9606  ? ? ? ? ? ? ? 'Chinese hamster' 
'Cricetulus griseus' 10029 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 214 human ? ?  ? ? ? ? ? ? 'Homo sapiens'      9606  ? ? ? ? ? ? ? 'Chinese hamster' 
'Cricetulus griseus' 10029 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_pdbx_entity_branch.entity_id   4 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 4 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH                                          'Glycam Condensed Sequence' GMML       1.0   
2 4 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1' WURCS                       PDB2Glycan 1.1.0 
3 4 '[][D-1-deoxy-GlcpNAc]{[(4+1)][a-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}'           LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 4 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
# 
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 
BMA 'D-saccharide, beta linking' . beta-D-mannopyranose                     'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6'      
180.156 
CYS 'L-peptide linking'          y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking'          y GLUTAMINE                                ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE                                  ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'          y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking'          y ISOLEUCINE                               ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'          y LEUCINE                                  ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'          y LYSINE                                   ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'          y METHIONINE                               ? 'C5 H11 N O2 S'  149.211 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   10   10  GLY GLY A . n 
A 1 2   ASP 2   11   11  ASP ASP A . n 
A 1 3   THR 3   12   12  THR THR A . n 
A 1 4   LEU 4   13   13  LEU LEU A . n 
A 1 5   CYS 5   14   14  CYS CYS A . n 
A 1 6   ILE 6   15   15  ILE ILE A . n 
A 1 7   GLY 7   16   16  GLY GLY A . n 
A 1 8   TYR 8   17   17  TYR TYR A . n 
A 1 9   HIS 9   18   18  HIS HIS A . n 
A 1 10  ALA 10  19   19  ALA ALA A . n 
A 1 11  ASN 11  20   20  ASN ASN A . n 
A 1 12  ASN 12  21   21  ASN ASN A . n 
A 1 13  SER 13  22   22  SER SER A . n 
A 1 14  THR 14  23   23  THR THR A . n 
A 1 15  ASP 15  24   24  ASP ASP A . n 
A 1 16  THR 16  25   25  THR THR A . n 
A 1 17  VAL 17  26   26  VAL VAL A . n 
A 1 18  ASP 18  27   27  ASP ASP A . n 
A 1 19  THR 19  28   28  THR THR A . n 
A 1 20  VAL 20  29   29  VAL VAL A . n 
A 1 21  LEU 21  30   30  LEU LEU A . n 
A 1 22  GLU 22  31   31  GLU GLU A . n 
A 1 23  LYS 23  32   32  LYS LYS A . n 
A 1 24  ASN 24  33   33  ASN ASN A . n 
A 1 25  VAL 25  34   34  VAL VAL A . n 
A 1 26  THR 26  35   35  THR THR A . n 
A 1 27  VAL 27  36   36  VAL VAL A . n 
A 1 28  THR 28  37   37  THR THR A . n 
A 1 29  HIS 29  38   38  HIS HIS A . n 
A 1 30  SER 30  39   39  SER SER A . n 
A 1 31  VAL 31  40   40  VAL VAL A . n 
A 1 32  ASN 32  41   41  ASN ASN A . n 
A 1 33  LEU 33  42   42  LEU LEU A . n 
A 1 34  LEU 34  43   43  LEU LEU A . n 
A 1 35  GLU 35  44   44  GLU GLU A . n 
A 1 36  ASP 36  45   45  ASP ASP A . n 
A 1 37  LYS 37  46   46  LYS LYS A . n 
A 1 38  HIS 38  47   47  HIS HIS A . n 
A 1 39  ASN 39  48   48  ASN ASN A . n 
A 1 40  GLY 40  49   49  GLY GLY A . n 
A 1 41  LYS 41  50   50  LYS LYS A . n 
A 1 42  LEU 42  51   51  LEU LEU A . n 
A 1 43  CYS 43  52   52  CYS CYS A . n 
A 1 44  ASP 44  53   53  ASP ASP A . n 
A 1 45  LEU 45  54   54  LEU LEU A . n 
A 1 46  ASP 46  55   55  ASP ASP A . n 
A 1 47  GLY 47  55   55  GLY GLY A a n 
A 1 48  VAL 48  56   56  VAL VAL A . n 
A 1 49  LYS 49  57   57  LYS LYS A . n 
A 1 50  PRO 50  58   58  PRO PRO A . n 
A 1 51  LEU 51  59   59  LEU LEU A . n 
A 1 52  ILE 52  60   60  ILE ILE A . n 
A 1 53  LEU 53  61   61  LEU LEU A . n 
A 1 54  ARG 54  62   62  ARG ARG A . n 
A 1 55  ASP 55  63   63  ASP ASP A . n 
A 1 56  CYS 56  64   64  CYS CYS A . n 
A 1 57  SER 57  65   65  SER SER A . n 
A 1 58  VAL 58  66   66  VAL VAL A . n 
A 1 59  ALA 59  67   67  ALA ALA A . n 
A 1 60  GLY 60  68   68  GLY GLY A . n 
A 1 61  TRP 61  69   69  TRP TRP A . n 
A 1 62  LEU 62  70   70  LEU LEU A . n 
A 1 63  LEU 63  71   71  LEU LEU A . n 
A 1 64  GLY 64  72   72  GLY GLY A . n 
A 1 65  ASN 65  73   73  ASN ASN A . n 
A 1 66  PRO 66  74   74  PRO PRO A . n 
A 1 67  MET 67  75   75  MET MET A . n 
A 1 68  CYS 68  76   76  CYS CYS A . n 
A 1 69  ASP 69  77   77  ASP ASP A . n 
A 1 70  GLU 70  78   78  GLU GLU A . n 
A 1 71  PHE 71  79   79  PHE PHE A . n 
A 1 72  ILE 72  80   80  ILE ILE A . n 
A 1 73  ASN 73  81   81  ASN ASN A . n 
A 1 74  VAL 74  82   82  VAL VAL A . n 
A 1 75  PRO 75  83   83  PRO PRO A . n 
A 1 76  GLU 76  83   83  GLU GLU A a n 
A 1 77  TRP 77  84   84  TRP TRP A . n 
A 1 78  SER 78  85   85  SER SER A . n 
A 1 79  TYR 79  86   86  TYR TYR A . n 
A 1 80  ILE 80  87   87  ILE ILE A . n 
A 1 81  VAL 81  88   88  VAL VAL A . n 
A 1 82  GLU 82  89   89  GLU GLU A . n 
A 1 83  LYS 83  90   90  LYS LYS A . n 
A 1 84  ALA 84  91   91  ALA ALA A . n 
A 1 85  ASN 85  92   92  ASN ASN A . n 
A 1 86  PRO 86  93   93  PRO PRO A . n 
A 1 87  VAL 87  94   94  VAL VAL A . n 
A 1 88  ASN 88  95   95  ASN ASN A . n 
A 1 89  ASP 89  96   96  ASP ASP A . n 
A 1 90  LEU 90  96   96  LEU LEU A a n 
A 1 91  CYS 91  97   97  CYS CYS A . n 
A 1 92  TYR 92  98   98  TYR TYR A . n 
A 1 93  PRO 93  99   99  PRO PRO A . n 
A 1 94  GLY 94  100  100 GLY GLY A . n 
A 1 95  ASP 95  101  101 ASP ASP A . n 
A 1 96  PHE 96  102  102 PHE PHE A . n 
A 1 97  ASN 97  103  103 ASN ASN A . n 
A 1 98  ASP 98  104  104 ASP ASP A . n 
A 1 99  TYR 99  105  105 TYR TYR A . n 
A 1 100 GLU 100 106  106 GLU GLU A . n 
A 1 101 GLU 101 107  107 GLU GLU A . n 
A 1 102 LEU 102 108  108 LEU LEU A . n 
A 1 103 LYS 103 109  109 LYS LYS A . n 
A 1 104 HIS 104 110  110 HIS HIS A . n 
A 1 105 LEU 105 111  111 LEU LEU A . n 
A 1 106 LEU 106 112  112 LEU LEU A . n 
A 1 107 SER 107 113  113 SER SER A . n 
A 1 108 ARG 108 114  114 ARG ARG A . n 
A 1 109 ILE 109 115  115 ILE ILE A . n 
A 1 110 ASN 110 116  116 ASN ASN A . n 
A 1 111 HIS 111 117  117 HIS HIS A . n 
A 1 112 PHE 112 118  118 PHE PHE A . n 
A 1 113 GLU 113 119  119 GLU GLU A . n 
A 1 114 LYS 114 120  120 LYS LYS A . n 
A 1 115 ILE 115 121  121 ILE ILE A . n 
A 1 116 GLN 116 122  122 GLN GLN A . n 
A 1 117 ILE 117 123  123 ILE ILE A . n 
A 1 118 ILE 118 124  124 ILE ILE A . n 
A 1 119 PRO 119 125  125 PRO PRO A . n 
A 1 120 LYS 120 125  125 LYS LYS A a n 
A 1 121 SER 121 125  125 SER SER A b n 
A 1 122 SER 122 126  126 SER SER A . n 
A 1 123 TRP 123 127  127 TRP TRP A . n 
A 1 124 SER 124 128  128 SER SER A . n 
A 1 125 SER 125 129  129 SER SER A . n 
A 1 126 HIS 126 130  130 HIS HIS A . n 
A 1 127 GLU 127 131  131 GLU GLU A . n 
A 1 128 ALA 128 132  132 ALA ALA A . n 
A 1 129 SER 129 133  133 SER SER A . n 
A 1 130 LEU 130 133  133 LEU LEU A a n 
A 1 131 GLY 131 134  134 GLY GLY A . n 
A 1 132 VAL 132 135  135 VAL VAL A . n 
A 1 133 SER 133 136  136 SER SER A . n 
A 1 134 SER 134 137  137 SER SER A . n 
A 1 135 ALA 135 138  138 ALA ALA A . n 
A 1 136 CYS 136 139  139 CYS CYS A . n 
A 1 137 PRO 137 140  140 PRO PRO A . n 
A 1 138 TYR 138 141  141 TYR TYR A . n 
A 1 139 GLN 139 142  142 GLN GLN A . n 
A 1 140 GLY 140 143  143 GLY GLY A . n 
A 1 141 LYS 141 144  144 LYS LYS A . n 
A 1 142 SER 142 145  145 SER SER A . n 
A 1 143 SER 143 146  146 SER SER A . n 
A 1 144 PHE 144 147  147 PHE PHE A . n 
A 1 145 PHE 145 148  148 PHE PHE A . n 
A 1 146 ARG 146 149  149 ARG ARG A . n 
A 1 147 ASN 147 150  150 ASN ASN A . n 
A 1 148 VAL 148 151  151 VAL VAL A . n 
A 1 149 VAL 149 152  152 VAL VAL A . n 
A 1 150 TRP 150 153  153 TRP TRP A . n 
A 1 151 LEU 151 154  154 LEU LEU A . n 
A 1 152 ILE 152 155  155 ILE ILE A . n 
A 1 153 LYS 153 156  156 LYS LYS A . n 
A 1 154 LYS 154 157  157 LYS LYS A . n 
A 1 155 ASN 155 158  158 ASN ASN A . n 
A 1 156 SER 156 159  159 SER SER A . n 
A 1 157 THR 157 160  160 THR THR A . n 
A 1 158 TYR 158 161  161 TYR TYR A . n 
A 1 159 PRO 159 162  162 PRO PRO A . n 
A 1 160 THR 160 163  163 THR THR A . n 
A 1 161 ILE 161 164  164 ILE ILE A . n 
A 1 162 LYS 162 165  165 LYS LYS A . n 
A 1 163 ARG 163 166  166 ARG ARG A . n 
A 1 164 SER 164 167  167 SER SER A . n 
A 1 165 TYR 165 168  168 TYR TYR A . n 
A 1 166 ASN 166 169  169 ASN ASN A . n 
A 1 167 ASN 167 170  170 ASN ASN A . n 
A 1 168 THR 168 171  171 THR THR A . n 
A 1 169 ASN 169 172  172 ASN ASN A . n 
A 1 170 GLN 170 173  173 GLN GLN A . n 
A 1 171 GLU 171 174  174 GLU GLU A . n 
A 1 172 ASP 172 175  175 ASP ASP A . n 
A 1 173 LEU 173 176  176 LEU LEU A . n 
A 1 174 LEU 174 177  177 LEU LEU A . n 
A 1 175 VAL 175 178  178 VAL VAL A . n 
A 1 176 LEU 176 179  179 LEU LEU A . n 
A 1 177 TRP 177 180  180 TRP TRP A . n 
A 1 178 GLY 178 181  181 GLY GLY A . n 
A 1 179 ILE 179 182  182 ILE ILE A . n 
A 1 180 HIS 180 183  183 HIS HIS A . n 
A 1 181 HIS 181 184  184 HIS HIS A . n 
A 1 182 PRO 182 185  185 PRO PRO A . n 
A 1 183 ASN 183 186  186 ASN ASN A . n 
A 1 184 ASP 184 187  187 ASP ASP A . n 
A 1 185 ALA 185 188  188 ALA ALA A . n 
A 1 186 ALA 186 189  189 ALA ALA A . n 
A 1 187 GLU 187 190  190 GLU GLU A . n 
A 1 188 GLN 188 191  191 GLN GLN A . n 
A 1 189 THR 189 192  192 THR THR A . n 
A 1 190 LYS 190 193  193 LYS LYS A . n 
A 1 191 LEU 191 194  194 LEU LEU A . n 
A 1 192 TYR 192 195  195 TYR TYR A . n 
A 1 193 GLN 193 196  196 GLN GLN A . n 
A 1 194 ASN 194 197  197 ASN ASN A . n 
A 1 195 PRO 195 198  198 PRO PRO A . n 
A 1 196 THR 196 199  199 THR THR A . n 
A 1 197 THR 197 200  200 THR THR A . n 
A 1 198 TYR 198 201  201 TYR TYR A . n 
A 1 199 ILE 199 202  202 ILE ILE A . n 
A 1 200 SER 200 203  203 SER SER A . n 
A 1 201 VAL 201 204  204 VAL VAL A . n 
A 1 202 GLY 202 205  205 GLY GLY A . n 
A 1 203 THR 203 206  206 THR THR A . n 
A 1 204 SER 204 207  207 SER SER A . n 
A 1 205 THR 205 208  208 THR THR A . n 
A 1 206 LEU 206 209  209 LEU LEU A . n 
A 1 207 ASN 207 210  210 ASN ASN A . n 
A 1 208 GLN 208 211  211 GLN GLN A . n 
A 1 209 ARG 209 212  212 ARG ARG A . n 
A 1 210 LEU 210 213  213 LEU LEU A . n 
A 1 211 VAL 211 214  214 VAL VAL A . n 
A 1 212 PRO 212 215  215 PRO PRO A . n 
A 1 213 ARG 213 216  216 ARG ARG A . n 
A 1 214 ILE 214 217  217 ILE ILE A . n 
A 1 215 ALA 215 218  218 ALA ALA A . n 
A 1 216 THR 216 219  219 THR THR A . n 
A 1 217 ARG 217 220  220 ARG ARG A . n 
A 1 218 SER 218 221  221 SER SER A . n 
A 1 219 LYS 219 222  222 LYS LYS A . n 
A 1 220 VAL 220 223  223 VAL VAL A . n 
A 1 221 ASN 221 224  224 ASN ASN A . n 
A 1 222 GLY 222 225  225 GLY GLY A . n 
A 1 223 GLN 223 226  226 GLN GLN A . n 
A 1 224 SER 224 227  227 SER SER A . n 
A 1 225 GLY 225 228  228 GLY GLY A . n 
A 1 226 ARG 226 229  229 ARG ARG A . n 
A 1 227 MET 227 230  230 MET MET A . n 
A 1 228 GLU 228 231  231 GLU GLU A . n 
A 1 229 PHE 229 232  232 PHE PHE A . n 
A 1 230 PHE 230 233  233 PHE PHE A . n 
A 1 231 TRP 231 234  234 TRP TRP A . n 
A 1 232 THR 232 235  235 THR THR A . n 
A 1 233 ILE 233 236  236 ILE ILE A . n 
A 1 234 LEU 234 237  237 LEU LEU A . n 
A 1 235 LYS 235 238  238 LYS LYS A . n 
A 1 236 PRO 236 239  239 PRO PRO A . n 
A 1 237 ASN 237 240  240 ASN ASN A . n 
A 1 238 ASP 238 241  241 ASP ASP A . n 
A 1 239 ALA 239 242  242 ALA ALA A . n 
A 1 240 ILE 240 243  243 ILE ILE A . n 
A 1 241 ASN 241 244  244 ASN ASN A . n 
A 1 242 PHE 242 245  245 PHE PHE A . n 
A 1 243 GLU 243 246  246 GLU GLU A . n 
A 1 244 SER 244 247  247 SER SER A . n 
A 1 245 ASN 245 248  248 ASN ASN A . n 
A 1 246 GLY 246 249  249 GLY GLY A . n 
A 1 247 ASN 247 250  250 ASN ASN A . n 
A 1 248 PHE 248 251  251 PHE PHE A . n 
A 1 249 ILE 249 252  252 ILE ILE A . n 
A 1 250 ALA 250 253  253 ALA ALA A . n 
A 1 251 PRO 251 254  254 PRO PRO A . n 
A 1 252 GLU 252 255  255 GLU GLU A . n 
A 1 253 TYR 253 256  256 TYR TYR A . n 
A 1 254 ALA 254 257  257 ALA ALA A . n 
A 1 255 TYR 255 258  258 TYR TYR A . n 
A 1 256 LYS 256 259  259 LYS LYS A . n 
A 1 257 ILE 257 260  260 ILE ILE A . n 
A 1 258 VAL 258 260  260 VAL VAL A a n 
A 1 259 LYS 259 261  261 LYS LYS A . n 
A 1 260 LYS 260 262  262 LYS LYS A . n 
A 1 261 GLY 261 263  263 GLY GLY A . n 
A 1 262 ASP 262 264  264 ASP ASP A . n 
A 1 263 SER 263 265  265 SER SER A . n 
A 1 264 THR 264 266  266 THR THR A . n 
A 1 265 ILE 265 267  267 ILE ILE A . n 
A 1 266 MET 266 268  268 MET MET A . n 
A 1 267 LYS 267 269  269 LYS LYS A . n 
A 1 268 SER 268 270  270 SER SER A . n 
A 1 269 GLU 269 271  271 GLU GLU A . n 
A 1 270 LEU 270 272  272 LEU LEU A . n 
A 1 271 GLU 271 273  273 GLU GLU A . n 
A 1 272 TYR 272 274  274 TYR TYR A . n 
A 1 273 GLY 273 275  275 GLY GLY A . n 
A 1 274 ASN 274 276  276 ASN ASN A . n 
A 1 275 CYS 275 277  277 CYS CYS A . n 
A 1 276 ASN 276 278  278 ASN ASN A . n 
A 1 277 THR 277 279  279 THR THR A . n 
A 1 278 THR 278 280  280 THR THR A . n 
A 1 279 CYS 279 281  281 CYS CYS A . n 
A 1 280 GLN 280 282  282 GLN GLN A . n 
A 1 281 THR 281 283  283 THR THR A . n 
A 1 282 PRO 282 284  284 PRO PRO A . n 
A 1 283 LYS 283 285  285 LYS LYS A . n 
A 1 284 GLY 284 286  286 GLY GLY A . n 
A 1 285 ALA 285 287  287 ALA ALA A . n 
A 1 286 ILE 286 288  288 ILE ILE A . n 
A 1 287 ASN 287 289  289 ASN ASN A . n 
A 1 288 THR 288 290  290 THR THR A . n 
A 1 289 SER 289 291  291 SER SER A . n 
A 1 290 LEU 290 292  292 LEU LEU A . n 
A 1 291 PRO 291 293  293 PRO PRO A . n 
A 1 292 PHE 292 294  294 PHE PHE A . n 
A 1 293 GLN 293 295  295 GLN GLN A . n 
A 1 294 ASN 294 296  296 ASN ASN A . n 
A 1 295 ILE 295 297  297 ILE ILE A . n 
A 1 296 HIS 296 298  298 HIS HIS A . n 
A 1 297 PRO 297 299  299 PRO PRO A . n 
A 1 298 ILE 298 300  300 ILE ILE A . n 
A 1 299 THR 299 301  301 THR THR A . n 
A 1 300 ILE 300 302  302 ILE ILE A . n 
A 1 301 GLY 301 303  303 GLY GLY A . n 
A 1 302 LYS 302 304  304 LYS LYS A . n 
A 1 303 CYS 303 305  305 CYS CYS A . n 
A 1 304 PRO 304 306  306 PRO PRO A . n 
A 1 305 LYS 305 307  307 LYS LYS A . n 
A 1 306 TYR 306 308  308 TYR TYR A . n 
A 1 307 VAL 307 309  309 VAL VAL A . n 
A 1 308 LYS 308 310  310 LYS LYS A . n 
A 1 309 SER 309 311  311 SER SER A . n 
A 1 310 THR 310 312  312 THR THR A . n 
A 1 311 LYS 311 313  313 LYS LYS A . n 
A 1 312 LEU 312 314  314 LEU LEU A . n 
A 1 313 ARG 313 315  315 ARG ARG A . n 
A 1 314 LEU 314 316  316 LEU LEU A . n 
A 1 315 ALA 315 317  317 ALA ALA A . n 
A 1 316 THR 316 318  318 THR THR A . n 
A 1 317 GLY 317 319  319 GLY GLY A . n 
A 1 318 LEU 318 320  320 LEU LEU A . n 
A 1 319 ARG 319 321  321 ARG ARG A . n 
A 1 320 ASN 320 322  322 ASN ASN A . n 
A 1 321 VAL 321 323  323 VAL VAL A . n 
A 1 322 PRO 322 324  324 PRO PRO A . n 
A 1 323 SER 323 325  325 SER SER A . n 
A 1 324 ILE 324 326  ?   ?   ?   A . n 
A 1 325 GLN 325 327  ?   ?   ?   A . n 
A 1 326 SER 326 328  ?   ?   ?   A . n 
A 1 327 ARG 327 329  ?   ?   ?   A . n 
A 1 328 GLY 328 330  ?   ?   ?   A . n 
A 1 329 LEU 329 331  ?   ?   ?   A . n 
A 1 330 PHE 330 332  ?   ?   ?   A . n 
A 1 331 GLY 331 333  ?   ?   ?   A . n 
A 1 332 ALA 332 334  ?   ?   ?   A . n 
A 1 333 ILE 333 335  ?   ?   ?   A . n 
A 1 334 ALA 334 336  ?   ?   ?   A . n 
A 1 335 GLY 335 337  ?   ?   ?   A . n 
A 1 336 PHE 336 338  ?   ?   ?   A . n 
A 1 337 ILE 337 339  ?   ?   ?   A . n 
A 1 338 GLU 338 340  ?   ?   ?   A . n 
A 1 339 GLY 339 341  ?   ?   ?   A . n 
A 1 340 GLY 340 342  ?   ?   ?   A . n 
A 1 341 TRP 341 343  ?   ?   ?   A . n 
A 1 342 THR 342 344  ?   ?   ?   A . n 
A 1 343 GLY 343 345  ?   ?   ?   A . n 
A 1 344 MET 344 346  ?   ?   ?   A . n 
A 1 345 VAL 345 347  ?   ?   ?   A . n 
A 1 346 ASP 346 348  ?   ?   ?   A . n 
A 1 347 GLY 347 349  ?   ?   ?   A . n 
A 1 348 TRP 348 350  ?   ?   ?   A . n 
A 1 349 TYR 349 351  ?   ?   ?   A . n 
A 1 350 GLY 350 352  ?   ?   ?   A . n 
A 1 351 TYR 351 353  ?   ?   ?   A . n 
A 1 352 HIS 352 354  ?   ?   ?   A . n 
A 1 353 HIS 353 355  ?   ?   ?   A . n 
A 1 354 GLN 354 356  ?   ?   ?   A . n 
A 1 355 ASN 355 357  ?   ?   ?   A . n 
A 1 356 GLU 356 358  ?   ?   ?   A . n 
A 1 357 GLN 357 359  ?   ?   ?   A . n 
A 1 358 GLY 358 360  ?   ?   ?   A . n 
A 1 359 SER 359 361  ?   ?   ?   A . n 
A 1 360 GLY 360 362  ?   ?   ?   A . n 
A 1 361 TYR 361 363  ?   ?   ?   A . n 
A 1 362 ALA 362 364  ?   ?   ?   A . n 
A 1 363 ALA 363 365  ?   ?   ?   A . n 
A 1 364 ASP 364 366  ?   ?   ?   A . n 
A 1 365 LEU 365 367  ?   ?   ?   A . n 
A 1 366 LYS 366 368  ?   ?   ?   A . n 
A 1 367 SER 367 369  ?   ?   ?   A . n 
A 1 368 THR 368 370  ?   ?   ?   A . n 
A 1 369 GLN 369 371  ?   ?   ?   A . n 
A 1 370 ASN 370 372  ?   ?   ?   A . n 
A 1 371 ALA 371 373  ?   ?   ?   A . n 
A 1 372 ILE 372 374  ?   ?   ?   A . n 
A 1 373 ASP 373 375  ?   ?   ?   A . n 
A 1 374 GLY 374 376  ?   ?   ?   A . n 
A 1 375 ILE 375 377  ?   ?   ?   A . n 
A 1 376 THR 376 378  ?   ?   ?   A . n 
A 1 377 ASN 377 379  ?   ?   ?   A . n 
A 1 378 LYS 378 380  ?   ?   ?   A . n 
A 1 379 VAL 379 381  ?   ?   ?   A . n 
A 1 380 ASN 380 382  ?   ?   ?   A . n 
A 1 381 SER 381 383  ?   ?   ?   A . n 
A 1 382 VAL 382 384  ?   ?   ?   A . n 
A 1 383 ILE 383 385  ?   ?   ?   A . n 
A 1 384 GLU 384 386  ?   ?   ?   A . n 
A 1 385 LYS 385 387  ?   ?   ?   A . n 
A 1 386 MET 386 388  ?   ?   ?   A . n 
A 1 387 ASN 387 389  ?   ?   ?   A . n 
A 1 388 THR 388 390  ?   ?   ?   A . n 
A 1 389 GLN 389 391  ?   ?   ?   A . n 
A 1 390 PHE 390 392  ?   ?   ?   A . n 
A 1 391 THR 391 393  ?   ?   ?   A . n 
A 1 392 ALA 392 394  ?   ?   ?   A . n 
A 1 393 VAL 393 395  ?   ?   ?   A . n 
A 1 394 GLY 394 396  ?   ?   ?   A . n 
A 1 395 LYS 395 397  ?   ?   ?   A . n 
A 1 396 GLU 396 398  ?   ?   ?   A . n 
A 1 397 PHE 397 399  ?   ?   ?   A . n 
A 1 398 ASN 398 400  ?   ?   ?   A . n 
A 1 399 HIS 399 401  ?   ?   ?   A . n 
A 1 400 LEU 400 402  ?   ?   ?   A . n 
A 1 401 GLU 401 403  ?   ?   ?   A . n 
A 1 402 LYS 402 404  ?   ?   ?   A . n 
A 1 403 ARG 403 405  ?   ?   ?   A . n 
A 1 404 ILE 404 406  ?   ?   ?   A . n 
A 1 405 GLU 405 407  ?   ?   ?   A . n 
A 1 406 ASN 406 408  ?   ?   ?   A . n 
A 1 407 LEU 407 409  ?   ?   ?   A . n 
A 1 408 ASN 408 410  ?   ?   ?   A . n 
A 1 409 LYS 409 411  ?   ?   ?   A . n 
A 1 410 LYS 410 412  ?   ?   ?   A . n 
A 1 411 VAL 411 413  ?   ?   ?   A . n 
A 1 412 ASP 412 414  ?   ?   ?   A . n 
A 1 413 ASP 413 415  ?   ?   ?   A . n 
A 1 414 GLY 414 416  ?   ?   ?   A . n 
A 1 415 PHE 415 417  ?   ?   ?   A . n 
A 1 416 LEU 416 418  ?   ?   ?   A . n 
A 1 417 ASP 417 419  ?   ?   ?   A . n 
A 1 418 ILE 418 420  ?   ?   ?   A . n 
A 1 419 TRP 419 421  ?   ?   ?   A . n 
A 1 420 THR 420 422  ?   ?   ?   A . n 
A 1 421 TYR 421 423  ?   ?   ?   A . n 
A 1 422 ASN 422 424  ?   ?   ?   A . n 
A 1 423 ALA 423 425  ?   ?   ?   A . n 
A 1 424 GLU 424 426  ?   ?   ?   A . n 
A 1 425 LEU 425 427  ?   ?   ?   A . n 
A 1 426 LEU 426 428  ?   ?   ?   A . n 
A 1 427 VAL 427 429  ?   ?   ?   A . n 
A 1 428 LEU 428 430  ?   ?   ?   A . n 
A 1 429 LEU 429 431  ?   ?   ?   A . n 
A 1 430 GLU 430 432  ?   ?   ?   A . n 
A 1 431 ASN 431 433  ?   ?   ?   A . n 
A 1 432 GLU 432 434  ?   ?   ?   A . n 
A 1 433 ARG 433 435  ?   ?   ?   A . n 
A 1 434 THR 434 436  ?   ?   ?   A . n 
A 1 435 LEU 435 437  ?   ?   ?   A . n 
A 1 436 ASP 436 438  ?   ?   ?   A . n 
A 1 437 TYR 437 439  ?   ?   ?   A . n 
A 1 438 HIS 438 440  ?   ?   ?   A . n 
A 1 439 ASP 439 441  ?   ?   ?   A . n 
A 1 440 SER 440 442  ?   ?   ?   A . n 
A 1 441 ASN 441 443  ?   ?   ?   A . n 
A 1 442 VAL 442 444  ?   ?   ?   A . n 
A 1 443 LYS 443 445  ?   ?   ?   A . n 
A 1 444 ASN 444 446  ?   ?   ?   A . n 
A 1 445 LEU 445 447  ?   ?   ?   A . n 
A 1 446 TYR 446 448  ?   ?   ?   A . n 
A 1 447 GLU 447 449  ?   ?   ?   A . n 
A 1 448 LYS 448 450  ?   ?   ?   A . n 
A 1 449 VAL 449 451  ?   ?   ?   A . n 
A 1 450 ARG 450 452  ?   ?   ?   A . n 
A 1 451 SER 451 453  ?   ?   ?   A . n 
A 1 452 GLN 452 454  ?   ?   ?   A . n 
A 1 453 LEU 453 455  ?   ?   ?   A . n 
A 1 454 LYS 454 456  ?   ?   ?   A . n 
A 1 455 ASN 455 457  ?   ?   ?   A . n 
A 1 456 ASN 456 458  ?   ?   ?   A . n 
A 1 457 ALA 457 459  ?   ?   ?   A . n 
A 1 458 LYS 458 460  ?   ?   ?   A . n 
A 1 459 GLU 459 461  ?   ?   ?   A . n 
A 1 460 ILE 460 462  ?   ?   ?   A . n 
A 1 461 GLY 461 463  ?   ?   ?   A . n 
A 1 462 ASN 462 464  ?   ?   ?   A . n 
A 1 463 GLY 463 465  ?   ?   ?   A . n 
A 1 464 CYS 464 466  ?   ?   ?   A . n 
A 1 465 PHE 465 467  ?   ?   ?   A . n 
A 1 466 GLU 466 468  ?   ?   ?   A . n 
A 1 467 PHE 467 469  ?   ?   ?   A . n 
A 1 468 TYR 468 470  ?   ?   ?   A . n 
A 1 469 HIS 469 471  ?   ?   ?   A . n 
A 1 470 LYS 470 472  ?   ?   ?   A . n 
A 1 471 CYS 471 473  ?   ?   ?   A . n 
A 1 472 ASP 472 474  ?   ?   ?   A . n 
A 1 473 ASN 473 475  ?   ?   ?   A . n 
A 1 474 THR 474 476  ?   ?   ?   A . n 
A 1 475 CYS 475 477  ?   ?   ?   A . n 
A 1 476 MET 476 478  ?   ?   ?   A . n 
A 1 477 GLU 477 479  ?   ?   ?   A . n 
A 1 478 SER 478 480  ?   ?   ?   A . n 
A 1 479 VAL 479 481  ?   ?   ?   A . n 
A 1 480 LYS 480 482  ?   ?   ?   A . n 
A 1 481 ASN 481 483  ?   ?   ?   A . n 
A 1 482 GLY 482 484  ?   ?   ?   A . n 
A 1 483 THR 483 485  ?   ?   ?   A . n 
A 1 484 TYR 484 486  ?   ?   ?   A . n 
A 1 485 ASP 485 487  ?   ?   ?   A . n 
A 1 486 TYR 486 488  ?   ?   ?   A . n 
A 1 487 PRO 487 489  ?   ?   ?   A . n 
A 1 488 LYS 488 490  ?   ?   ?   A . n 
A 1 489 TYR 489 491  ?   ?   ?   A . n 
A 1 490 SER 490 492  ?   ?   ?   A . n 
A 1 491 GLU 491 493  ?   ?   ?   A . n 
A 1 492 GLU 492 494  ?   ?   ?   A . n 
A 1 493 ALA 493 495  ?   ?   ?   A . n 
A 1 494 LYS 494 496  ?   ?   ?   A . n 
A 1 495 LEU 495 497  ?   ?   ?   A . n 
A 1 496 ASN 496 498  ?   ?   ?   A . n 
A 1 497 ARG 497 499  ?   ?   ?   A . n 
A 1 498 GLU 498 500  ?   ?   ?   A . n 
A 1 499 GLU 499 501  ?   ?   ?   A . n 
A 1 500 ILE 500 502  ?   ?   ?   A . n 
A 1 501 ASP 501 503  ?   ?   ?   A . n 
A 1 502 SER 502 504  ?   ?   ?   A . n 
A 1 503 GLY 503 505  ?   ?   ?   A . n 
A 1 504 ARG 504 506  ?   ?   ?   A . n 
A 1 505 LEU 505 507  ?   ?   ?   A . n 
A 1 506 VAL 506 508  ?   ?   ?   A . n 
A 1 507 PRO 507 509  ?   ?   ?   A . n 
A 1 508 ARG 508 510  ?   ?   ?   A . n 
A 1 509 GLY 509 511  ?   ?   ?   A . n 
A 1 510 SER 510 512  ?   ?   ?   A . n 
A 1 511 PRO 511 513  ?   ?   ?   A . n 
A 1 512 GLY 512 514  ?   ?   ?   A . n 
A 1 513 SER 513 515  ?   ?   ?   A . n 
A 1 514 GLY 514 516  ?   ?   ?   A . n 
A 1 515 TYR 515 517  ?   ?   ?   A . n 
A 1 516 ILE 516 518  ?   ?   ?   A . n 
A 1 517 PRO 517 519  ?   ?   ?   A . n 
A 1 518 GLU 518 520  ?   ?   ?   A . n 
A 1 519 ALA 519 521  ?   ?   ?   A . n 
A 1 520 PRO 520 522  ?   ?   ?   A . n 
A 1 521 ARG 521 523  ?   ?   ?   A . n 
A 1 522 ASP 522 524  ?   ?   ?   A . n 
A 1 523 GLY 523 525  ?   ?   ?   A . n 
A 1 524 GLN 524 526  ?   ?   ?   A . n 
A 1 525 ALA 525 527  ?   ?   ?   A . n 
A 1 526 TYR 526 528  ?   ?   ?   A . n 
A 1 527 VAL 527 529  ?   ?   ?   A . n 
A 1 528 ARG 528 530  ?   ?   ?   A . n 
A 1 529 LYS 529 531  ?   ?   ?   A . n 
A 1 530 ASP 530 532  ?   ?   ?   A . n 
A 1 531 GLY 531 533  ?   ?   ?   A . n 
A 1 532 GLU 532 534  ?   ?   ?   A . n 
A 1 533 TRP 533 535  ?   ?   ?   A . n 
A 1 534 VAL 534 536  ?   ?   ?   A . n 
A 1 535 LEU 535 537  ?   ?   ?   A . n 
A 1 536 LEU 536 538  ?   ?   ?   A . n 
A 1 537 SER 537 539  ?   ?   ?   A . n 
A 1 538 THR 538 540  ?   ?   ?   A . n 
A 1 539 PHE 539 541  ?   ?   ?   A . n 
A 1 540 LEU 540 542  ?   ?   ?   A . n 
A 1 541 GLY 541 543  ?   ?   ?   A . n 
B 1 1   GLY 1   -326 ?   ?   ?   B . n 
B 1 2   ASP 2   -325 ?   ?   ?   B . n 
B 1 3   THR 3   -324 ?   ?   ?   B . n 
B 1 4   LEU 4   -323 ?   ?   ?   B . n 
B 1 5   CYS 5   -322 ?   ?   ?   B . n 
B 1 6   ILE 6   -321 ?   ?   ?   B . n 
B 1 7   GLY 7   -320 ?   ?   ?   B . n 
B 1 8   TYR 8   -319 ?   ?   ?   B . n 
B 1 9   HIS 9   -318 ?   ?   ?   B . n 
B 1 10  ALA 10  -317 ?   ?   ?   B . n 
B 1 11  ASN 11  -316 ?   ?   ?   B . n 
B 1 12  ASN 12  -315 ?   ?   ?   B . n 
B 1 13  SER 13  -314 ?   ?   ?   B . n 
B 1 14  THR 14  -313 ?   ?   ?   B . n 
B 1 15  ASP 15  -312 ?   ?   ?   B . n 
B 1 16  THR 16  -311 ?   ?   ?   B . n 
B 1 17  VAL 17  -310 ?   ?   ?   B . n 
B 1 18  ASP 18  -309 ?   ?   ?   B . n 
B 1 19  THR 19  -308 ?   ?   ?   B . n 
B 1 20  VAL 20  -307 ?   ?   ?   B . n 
B 1 21  LEU 21  -306 ?   ?   ?   B . n 
B 1 22  GLU 22  -305 ?   ?   ?   B . n 
B 1 23  LYS 23  -304 ?   ?   ?   B . n 
B 1 24  ASN 24  -303 ?   ?   ?   B . n 
B 1 25  VAL 25  -302 ?   ?   ?   B . n 
B 1 26  THR 26  -301 ?   ?   ?   B . n 
B 1 27  VAL 27  -300 ?   ?   ?   B . n 
B 1 28  THR 28  -299 ?   ?   ?   B . n 
B 1 29  HIS 29  -298 ?   ?   ?   B . n 
B 1 30  SER 30  -297 ?   ?   ?   B . n 
B 1 31  VAL 31  -296 ?   ?   ?   B . n 
B 1 32  ASN 32  -295 ?   ?   ?   B . n 
B 1 33  LEU 33  -294 ?   ?   ?   B . n 
B 1 34  LEU 34  -293 ?   ?   ?   B . n 
B 1 35  GLU 35  -292 ?   ?   ?   B . n 
B 1 36  ASP 36  -291 ?   ?   ?   B . n 
B 1 37  LYS 37  -290 ?   ?   ?   B . n 
B 1 38  HIS 38  -289 ?   ?   ?   B . n 
B 1 39  ASN 39  -288 ?   ?   ?   B . n 
B 1 40  GLY 40  -287 ?   ?   ?   B . n 
B 1 41  LYS 41  -286 ?   ?   ?   B . n 
B 1 42  LEU 42  -285 ?   ?   ?   B . n 
B 1 43  CYS 43  -284 ?   ?   ?   B . n 
B 1 44  ASP 44  -283 ?   ?   ?   B . n 
B 1 45  LEU 45  -282 ?   ?   ?   B . n 
B 1 46  ASP 46  -281 ?   ?   ?   B . n 
B 1 47  GLY 47  -280 ?   ?   ?   B . n 
B 1 48  VAL 48  -279 ?   ?   ?   B . n 
B 1 49  LYS 49  -278 ?   ?   ?   B . n 
B 1 50  PRO 50  -277 ?   ?   ?   B . n 
B 1 51  LEU 51  -276 ?   ?   ?   B . n 
B 1 52  ILE 52  -275 ?   ?   ?   B . n 
B 1 53  LEU 53  -274 ?   ?   ?   B . n 
B 1 54  ARG 54  -273 ?   ?   ?   B . n 
B 1 55  ASP 55  -272 ?   ?   ?   B . n 
B 1 56  CYS 56  -271 ?   ?   ?   B . n 
B 1 57  SER 57  -270 ?   ?   ?   B . n 
B 1 58  VAL 58  -269 ?   ?   ?   B . n 
B 1 59  ALA 59  -268 ?   ?   ?   B . n 
B 1 60  GLY 60  -267 ?   ?   ?   B . n 
B 1 61  TRP 61  -266 ?   ?   ?   B . n 
B 1 62  LEU 62  -265 ?   ?   ?   B . n 
B 1 63  LEU 63  -264 ?   ?   ?   B . n 
B 1 64  GLY 64  -263 ?   ?   ?   B . n 
B 1 65  ASN 65  -262 ?   ?   ?   B . n 
B 1 66  PRO 66  -261 ?   ?   ?   B . n 
B 1 67  MET 67  -260 ?   ?   ?   B . n 
B 1 68  CYS 68  -259 ?   ?   ?   B . n 
B 1 69  ASP 69  -258 ?   ?   ?   B . n 
B 1 70  GLU 70  -257 ?   ?   ?   B . n 
B 1 71  PHE 71  -256 ?   ?   ?   B . n 
B 1 72  ILE 72  -255 ?   ?   ?   B . n 
B 1 73  ASN 73  -254 ?   ?   ?   B . n 
B 1 74  VAL 74  -253 ?   ?   ?   B . n 
B 1 75  PRO 75  -252 ?   ?   ?   B . n 
B 1 76  GLU 76  -251 ?   ?   ?   B . n 
B 1 77  TRP 77  -250 ?   ?   ?   B . n 
B 1 78  SER 78  -249 ?   ?   ?   B . n 
B 1 79  TYR 79  -248 ?   ?   ?   B . n 
B 1 80  ILE 80  -247 ?   ?   ?   B . n 
B 1 81  VAL 81  -246 ?   ?   ?   B . n 
B 1 82  GLU 82  -245 ?   ?   ?   B . n 
B 1 83  LYS 83  -244 ?   ?   ?   B . n 
B 1 84  ALA 84  -243 ?   ?   ?   B . n 
B 1 85  ASN 85  -242 ?   ?   ?   B . n 
B 1 86  PRO 86  -241 ?   ?   ?   B . n 
B 1 87  VAL 87  -240 ?   ?   ?   B . n 
B 1 88  ASN 88  -239 ?   ?   ?   B . n 
B 1 89  ASP 89  -238 ?   ?   ?   B . n 
B 1 90  LEU 90  -237 ?   ?   ?   B . n 
B 1 91  CYS 91  -236 ?   ?   ?   B . n 
B 1 92  TYR 92  -235 ?   ?   ?   B . n 
B 1 93  PRO 93  -234 ?   ?   ?   B . n 
B 1 94  GLY 94  -233 ?   ?   ?   B . n 
B 1 95  ASP 95  -232 ?   ?   ?   B . n 
B 1 96  PHE 96  -231 ?   ?   ?   B . n 
B 1 97  ASN 97  -230 ?   ?   ?   B . n 
B 1 98  ASP 98  -229 ?   ?   ?   B . n 
B 1 99  TYR 99  -228 ?   ?   ?   B . n 
B 1 100 GLU 100 -227 ?   ?   ?   B . n 
B 1 101 GLU 101 -226 ?   ?   ?   B . n 
B 1 102 LEU 102 -225 ?   ?   ?   B . n 
B 1 103 LYS 103 -224 ?   ?   ?   B . n 
B 1 104 HIS 104 -223 ?   ?   ?   B . n 
B 1 105 LEU 105 -222 ?   ?   ?   B . n 
B 1 106 LEU 106 -221 ?   ?   ?   B . n 
B 1 107 SER 107 -220 ?   ?   ?   B . n 
B 1 108 ARG 108 -219 ?   ?   ?   B . n 
B 1 109 ILE 109 -218 ?   ?   ?   B . n 
B 1 110 ASN 110 -217 ?   ?   ?   B . n 
B 1 111 HIS 111 -216 ?   ?   ?   B . n 
B 1 112 PHE 112 -215 ?   ?   ?   B . n 
B 1 113 GLU 113 -214 ?   ?   ?   B . n 
B 1 114 LYS 114 -213 ?   ?   ?   B . n 
B 1 115 ILE 115 -212 ?   ?   ?   B . n 
B 1 116 GLN 116 -211 ?   ?   ?   B . n 
B 1 117 ILE 117 -210 ?   ?   ?   B . n 
B 1 118 ILE 118 -209 ?   ?   ?   B . n 
B 1 119 PRO 119 -208 ?   ?   ?   B . n 
B 1 120 LYS 120 -207 ?   ?   ?   B . n 
B 1 121 SER 121 -206 ?   ?   ?   B . n 
B 1 122 SER 122 -205 ?   ?   ?   B . n 
B 1 123 TRP 123 -204 ?   ?   ?   B . n 
B 1 124 SER 124 -203 ?   ?   ?   B . n 
B 1 125 SER 125 -202 ?   ?   ?   B . n 
B 1 126 HIS 126 -201 ?   ?   ?   B . n 
B 1 127 GLU 127 -200 ?   ?   ?   B . n 
B 1 128 ALA 128 -199 ?   ?   ?   B . n 
B 1 129 SER 129 -198 ?   ?   ?   B . n 
B 1 130 LEU 130 -197 ?   ?   ?   B . n 
B 1 131 GLY 131 -196 ?   ?   ?   B . n 
B 1 132 VAL 132 -195 ?   ?   ?   B . n 
B 1 133 SER 133 -194 ?   ?   ?   B . n 
B 1 134 SER 134 -193 ?   ?   ?   B . n 
B 1 135 ALA 135 -192 ?   ?   ?   B . n 
B 1 136 CYS 136 -191 ?   ?   ?   B . n 
B 1 137 PRO 137 -190 ?   ?   ?   B . n 
B 1 138 TYR 138 -189 ?   ?   ?   B . n 
B 1 139 GLN 139 -188 ?   ?   ?   B . n 
B 1 140 GLY 140 -187 ?   ?   ?   B . n 
B 1 141 LYS 141 -186 ?   ?   ?   B . n 
B 1 142 SER 142 -185 ?   ?   ?   B . n 
B 1 143 SER 143 -184 ?   ?   ?   B . n 
B 1 144 PHE 144 -183 ?   ?   ?   B . n 
B 1 145 PHE 145 -182 ?   ?   ?   B . n 
B 1 146 ARG 146 -181 ?   ?   ?   B . n 
B 1 147 ASN 147 -180 ?   ?   ?   B . n 
B 1 148 VAL 148 -179 ?   ?   ?   B . n 
B 1 149 VAL 149 -178 ?   ?   ?   B . n 
B 1 150 TRP 150 -177 ?   ?   ?   B . n 
B 1 151 LEU 151 -176 ?   ?   ?   B . n 
B 1 152 ILE 152 -175 ?   ?   ?   B . n 
B 1 153 LYS 153 -174 ?   ?   ?   B . n 
B 1 154 LYS 154 -173 ?   ?   ?   B . n 
B 1 155 ASN 155 -172 ?   ?   ?   B . n 
B 1 156 SER 156 -171 ?   ?   ?   B . n 
B 1 157 THR 157 -170 ?   ?   ?   B . n 
B 1 158 TYR 158 -169 ?   ?   ?   B . n 
B 1 159 PRO 159 -168 ?   ?   ?   B . n 
B 1 160 THR 160 -167 ?   ?   ?   B . n 
B 1 161 ILE 161 -166 ?   ?   ?   B . n 
B 1 162 LYS 162 -165 ?   ?   ?   B . n 
B 1 163 ARG 163 -164 ?   ?   ?   B . n 
B 1 164 SER 164 -163 ?   ?   ?   B . n 
B 1 165 TYR 165 -162 ?   ?   ?   B . n 
B 1 166 ASN 166 -161 ?   ?   ?   B . n 
B 1 167 ASN 167 -160 ?   ?   ?   B . n 
B 1 168 THR 168 -159 ?   ?   ?   B . n 
B 1 169 ASN 169 -158 ?   ?   ?   B . n 
B 1 170 GLN 170 -157 ?   ?   ?   B . n 
B 1 171 GLU 171 -156 ?   ?   ?   B . n 
B 1 172 ASP 172 -155 ?   ?   ?   B . n 
B 1 173 LEU 173 -154 ?   ?   ?   B . n 
B 1 174 LEU 174 -153 ?   ?   ?   B . n 
B 1 175 VAL 175 -152 ?   ?   ?   B . n 
B 1 176 LEU 176 -151 ?   ?   ?   B . n 
B 1 177 TRP 177 -150 ?   ?   ?   B . n 
B 1 178 GLY 178 -149 ?   ?   ?   B . n 
B 1 179 ILE 179 -148 ?   ?   ?   B . n 
B 1 180 HIS 180 -147 ?   ?   ?   B . n 
B 1 181 HIS 181 -146 ?   ?   ?   B . n 
B 1 182 PRO 182 -145 ?   ?   ?   B . n 
B 1 183 ASN 183 -144 ?   ?   ?   B . n 
B 1 184 ASP 184 -143 ?   ?   ?   B . n 
B 1 185 ALA 185 -142 ?   ?   ?   B . n 
B 1 186 ALA 186 -141 ?   ?   ?   B . n 
B 1 187 GLU 187 -140 ?   ?   ?   B . n 
B 1 188 GLN 188 -139 ?   ?   ?   B . n 
B 1 189 THR 189 -138 ?   ?   ?   B . n 
B 1 190 LYS 190 -137 ?   ?   ?   B . n 
B 1 191 LEU 191 -136 ?   ?   ?   B . n 
B 1 192 TYR 192 -135 ?   ?   ?   B . n 
B 1 193 GLN 193 -134 ?   ?   ?   B . n 
B 1 194 ASN 194 -133 ?   ?   ?   B . n 
B 1 195 PRO 195 -132 ?   ?   ?   B . n 
B 1 196 THR 196 -131 ?   ?   ?   B . n 
B 1 197 THR 197 -130 ?   ?   ?   B . n 
B 1 198 TYR 198 -129 ?   ?   ?   B . n 
B 1 199 ILE 199 -128 ?   ?   ?   B . n 
B 1 200 SER 200 -127 ?   ?   ?   B . n 
B 1 201 VAL 201 -126 ?   ?   ?   B . n 
B 1 202 GLY 202 -125 ?   ?   ?   B . n 
B 1 203 THR 203 -124 ?   ?   ?   B . n 
B 1 204 SER 204 -123 ?   ?   ?   B . n 
B 1 205 THR 205 -122 ?   ?   ?   B . n 
B 1 206 LEU 206 -121 ?   ?   ?   B . n 
B 1 207 ASN 207 -120 ?   ?   ?   B . n 
B 1 208 GLN 208 -119 ?   ?   ?   B . n 
B 1 209 ARG 209 -118 ?   ?   ?   B . n 
B 1 210 LEU 210 -117 ?   ?   ?   B . n 
B 1 211 VAL 211 -116 ?   ?   ?   B . n 
B 1 212 PRO 212 -115 ?   ?   ?   B . n 
B 1 213 ARG 213 -114 ?   ?   ?   B . n 
B 1 214 ILE 214 -113 ?   ?   ?   B . n 
B 1 215 ALA 215 -112 ?   ?   ?   B . n 
B 1 216 THR 216 -111 ?   ?   ?   B . n 
B 1 217 ARG 217 -110 ?   ?   ?   B . n 
B 1 218 SER 218 -109 ?   ?   ?   B . n 
B 1 219 LYS 219 -108 ?   ?   ?   B . n 
B 1 220 VAL 220 -107 ?   ?   ?   B . n 
B 1 221 ASN 221 -106 ?   ?   ?   B . n 
B 1 222 GLY 222 -105 ?   ?   ?   B . n 
B 1 223 GLN 223 -104 ?   ?   ?   B . n 
B 1 224 SER 224 -103 ?   ?   ?   B . n 
B 1 225 GLY 225 -102 ?   ?   ?   B . n 
B 1 226 ARG 226 -101 ?   ?   ?   B . n 
B 1 227 MET 227 -100 ?   ?   ?   B . n 
B 1 228 GLU 228 -99  ?   ?   ?   B . n 
B 1 229 PHE 229 -98  ?   ?   ?   B . n 
B 1 230 PHE 230 -97  ?   ?   ?   B . n 
B 1 231 TRP 231 -96  ?   ?   ?   B . n 
B 1 232 THR 232 -95  ?   ?   ?   B . n 
B 1 233 ILE 233 -94  ?   ?   ?   B . n 
B 1 234 LEU 234 -93  ?   ?   ?   B . n 
B 1 235 LYS 235 -92  ?   ?   ?   B . n 
B 1 236 PRO 236 -91  ?   ?   ?   B . n 
B 1 237 ASN 237 -90  ?   ?   ?   B . n 
B 1 238 ASP 238 -89  ?   ?   ?   B . n 
B 1 239 ALA 239 -88  ?   ?   ?   B . n 
B 1 240 ILE 240 -87  ?   ?   ?   B . n 
B 1 241 ASN 241 -86  ?   ?   ?   B . n 
B 1 242 PHE 242 -85  ?   ?   ?   B . n 
B 1 243 GLU 243 -84  ?   ?   ?   B . n 
B 1 244 SER 244 -83  ?   ?   ?   B . n 
B 1 245 ASN 245 -82  ?   ?   ?   B . n 
B 1 246 GLY 246 -81  ?   ?   ?   B . n 
B 1 247 ASN 247 -80  ?   ?   ?   B . n 
B 1 248 PHE 248 -79  ?   ?   ?   B . n 
B 1 249 ILE 249 -78  ?   ?   ?   B . n 
B 1 250 ALA 250 -77  ?   ?   ?   B . n 
B 1 251 PRO 251 -76  ?   ?   ?   B . n 
B 1 252 GLU 252 -75  ?   ?   ?   B . n 
B 1 253 TYR 253 -74  ?   ?   ?   B . n 
B 1 254 ALA 254 -73  ?   ?   ?   B . n 
B 1 255 TYR 255 -72  ?   ?   ?   B . n 
B 1 256 LYS 256 -71  ?   ?   ?   B . n 
B 1 257 ILE 257 -70  ?   ?   ?   B . n 
B 1 258 VAL 258 -69  ?   ?   ?   B . n 
B 1 259 LYS 259 -68  ?   ?   ?   B . n 
B 1 260 LYS 260 -67  ?   ?   ?   B . n 
B 1 261 GLY 261 -66  ?   ?   ?   B . n 
B 1 262 ASP 262 -65  ?   ?   ?   B . n 
B 1 263 SER 263 -64  ?   ?   ?   B . n 
B 1 264 THR 264 -63  ?   ?   ?   B . n 
B 1 265 ILE 265 -62  ?   ?   ?   B . n 
B 1 266 MET 266 -61  ?   ?   ?   B . n 
B 1 267 LYS 267 -60  ?   ?   ?   B . n 
B 1 268 SER 268 -59  ?   ?   ?   B . n 
B 1 269 GLU 269 -58  ?   ?   ?   B . n 
B 1 270 LEU 270 -57  ?   ?   ?   B . n 
B 1 271 GLU 271 -56  ?   ?   ?   B . n 
B 1 272 TYR 272 -55  ?   ?   ?   B . n 
B 1 273 GLY 273 -54  ?   ?   ?   B . n 
B 1 274 ASN 274 -53  ?   ?   ?   B . n 
B 1 275 CYS 275 -52  ?   ?   ?   B . n 
B 1 276 ASN 276 -51  ?   ?   ?   B . n 
B 1 277 THR 277 -50  ?   ?   ?   B . n 
B 1 278 THR 278 -49  ?   ?   ?   B . n 
B 1 279 CYS 279 -48  ?   ?   ?   B . n 
B 1 280 GLN 280 -47  ?   ?   ?   B . n 
B 1 281 THR 281 -46  ?   ?   ?   B . n 
B 1 282 PRO 282 -45  ?   ?   ?   B . n 
B 1 283 LYS 283 -44  ?   ?   ?   B . n 
B 1 284 GLY 284 -43  ?   ?   ?   B . n 
B 1 285 ALA 285 -42  ?   ?   ?   B . n 
B 1 286 ILE 286 -41  ?   ?   ?   B . n 
B 1 287 ASN 287 -40  ?   ?   ?   B . n 
B 1 288 THR 288 -39  ?   ?   ?   B . n 
B 1 289 SER 289 -38  ?   ?   ?   B . n 
B 1 290 LEU 290 -37  ?   ?   ?   B . n 
B 1 291 PRO 291 -36  ?   ?   ?   B . n 
B 1 292 PHE 292 -35  ?   ?   ?   B . n 
B 1 293 GLN 293 -34  ?   ?   ?   B . n 
B 1 294 ASN 294 -33  ?   ?   ?   B . n 
B 1 295 ILE 295 -32  ?   ?   ?   B . n 
B 1 296 HIS 296 -31  ?   ?   ?   B . n 
B 1 297 PRO 297 -30  ?   ?   ?   B . n 
B 1 298 ILE 298 -29  ?   ?   ?   B . n 
B 1 299 THR 299 -28  ?   ?   ?   B . n 
B 1 300 ILE 300 -27  ?   ?   ?   B . n 
B 1 301 GLY 301 -26  ?   ?   ?   B . n 
B 1 302 LYS 302 -25  ?   ?   ?   B . n 
B 1 303 CYS 303 -24  ?   ?   ?   B . n 
B 1 304 PRO 304 -23  ?   ?   ?   B . n 
B 1 305 LYS 305 -22  ?   ?   ?   B . n 
B 1 306 TYR 306 -21  ?   ?   ?   B . n 
B 1 307 VAL 307 -20  ?   ?   ?   B . n 
B 1 308 LYS 308 -19  ?   ?   ?   B . n 
B 1 309 SER 309 -18  ?   ?   ?   B . n 
B 1 310 THR 310 -17  ?   ?   ?   B . n 
B 1 311 LYS 311 -16  ?   ?   ?   B . n 
B 1 312 LEU 312 -15  ?   ?   ?   B . n 
B 1 313 ARG 313 -14  ?   ?   ?   B . n 
B 1 314 LEU 314 -13  ?   ?   ?   B . n 
B 1 315 ALA 315 -12  ?   ?   ?   B . n 
B 1 316 THR 316 -11  ?   ?   ?   B . n 
B 1 317 GLY 317 -10  ?   ?   ?   B . n 
B 1 318 LEU 318 -9   ?   ?   ?   B . n 
B 1 319 ARG 319 -8   ?   ?   ?   B . n 
B 1 320 ASN 320 -7   ?   ?   ?   B . n 
B 1 321 VAL 321 -6   ?   ?   ?   B . n 
B 1 322 PRO 322 -5   ?   ?   ?   B . n 
B 1 323 SER 323 -4   ?   ?   ?   B . n 
B 1 324 ILE 324 -3   ?   ?   ?   B . n 
B 1 325 GLN 325 -2   ?   ?   ?   B . n 
B 1 326 SER 326 -1   ?   ?   ?   B . n 
B 1 327 ARG 327 0    ?   ?   ?   B . n 
B 1 328 GLY 328 1    ?   ?   ?   B . n 
B 1 329 LEU 329 2    ?   ?   ?   B . n 
B 1 330 PHE 330 3    ?   ?   ?   B . n 
B 1 331 GLY 331 4    ?   ?   ?   B . n 
B 1 332 ALA 332 5    ?   ?   ?   B . n 
B 1 333 ILE 333 6    ?   ?   ?   B . n 
B 1 334 ALA 334 7    ?   ?   ?   B . n 
B 1 335 GLY 335 8    ?   ?   ?   B . n 
B 1 336 PHE 336 9    ?   ?   ?   B . n 
B 1 337 ILE 337 10   10  ILE ILE B . n 
B 1 338 GLU 338 11   11  GLU GLU B . n 
B 1 339 GLY 339 12   12  GLY GLY B . n 
B 1 340 GLY 340 13   13  GLY GLY B . n 
B 1 341 TRP 341 14   14  TRP TRP B . n 
B 1 342 THR 342 15   15  THR THR B . n 
B 1 343 GLY 343 16   16  GLY GLY B . n 
B 1 344 MET 344 17   17  MET MET B . n 
B 1 345 VAL 345 18   18  VAL VAL B . n 
B 1 346 ASP 346 19   19  ASP ASP B . n 
B 1 347 GLY 347 20   20  GLY GLY B . n 
B 1 348 TRP 348 21   21  TRP TRP B . n 
B 1 349 TYR 349 22   22  TYR TYR B . n 
B 1 350 GLY 350 23   23  GLY GLY B . n 
B 1 351 TYR 351 24   24  TYR TYR B . n 
B 1 352 HIS 352 25   25  HIS HIS B . n 
B 1 353 HIS 353 26   26  HIS HIS B . n 
B 1 354 GLN 354 27   27  GLN GLN B . n 
B 1 355 ASN 355 28   28  ASN ASN B . n 
B 1 356 GLU 356 29   29  GLU GLU B . n 
B 1 357 GLN 357 30   30  GLN GLN B . n 
B 1 358 GLY 358 31   31  GLY GLY B . n 
B 1 359 SER 359 32   32  SER SER B . n 
B 1 360 GLY 360 33   33  GLY GLY B . n 
B 1 361 TYR 361 34   34  TYR TYR B . n 
B 1 362 ALA 362 35   35  ALA ALA B . n 
B 1 363 ALA 363 36   36  ALA ALA B . n 
B 1 364 ASP 364 37   37  ASP ASP B . n 
B 1 365 LEU 365 38   38  LEU LEU B . n 
B 1 366 LYS 366 39   39  LYS LYS B . n 
B 1 367 SER 367 40   40  SER SER B . n 
B 1 368 THR 368 41   41  THR THR B . n 
B 1 369 GLN 369 42   42  GLN GLN B . n 
B 1 370 ASN 370 43   43  ASN ASN B . n 
B 1 371 ALA 371 44   44  ALA ALA B . n 
B 1 372 ILE 372 45   45  ILE ILE B . n 
B 1 373 ASP 373 46   46  ASP ASP B . n 
B 1 374 GLY 374 47   47  GLY GLY B . n 
B 1 375 ILE 375 48   48  ILE ILE B . n 
B 1 376 THR 376 49   49  THR THR B . n 
B 1 377 ASN 377 50   50  ASN ASN B . n 
B 1 378 LYS 378 51   51  LYS LYS B . n 
B 1 379 VAL 379 52   52  VAL VAL B . n 
B 1 380 ASN 380 53   53  ASN ASN B . n 
B 1 381 SER 381 54   54  SER SER B . n 
B 1 382 VAL 382 55   55  VAL VAL B . n 
B 1 383 ILE 383 56   56  ILE ILE B . n 
B 1 384 GLU 384 57   57  GLU GLU B . n 
B 1 385 LYS 385 58   58  LYS LYS B . n 
B 1 386 MET 386 59   59  MET MET B . n 
B 1 387 ASN 387 60   60  ASN ASN B . n 
B 1 388 THR 388 61   61  THR THR B . n 
B 1 389 GLN 389 62   62  GLN GLN B . n 
B 1 390 PHE 390 63   63  PHE PHE B . n 
B 1 391 THR 391 64   64  THR THR B . n 
B 1 392 ALA 392 65   65  ALA ALA B . n 
B 1 393 VAL 393 66   66  VAL VAL B . n 
B 1 394 GLY 394 67   ?   ?   ?   B . n 
B 1 395 LYS 395 68   ?   ?   ?   B . n 
B 1 396 GLU 396 69   ?   ?   ?   B . n 
B 1 397 PHE 397 70   ?   ?   ?   B . n 
B 1 398 ASN 398 71   ?   ?   ?   B . n 
B 1 399 HIS 399 72   ?   ?   ?   B . n 
B 1 400 LEU 400 73   ?   ?   ?   B . n 
B 1 401 GLU 401 74   ?   ?   ?   B . n 
B 1 402 LYS 402 75   ?   ?   ?   B . n 
B 1 403 ARG 403 76   76  ARG ARG B . n 
B 1 404 ILE 404 77   77  ILE ILE B . n 
B 1 405 GLU 405 78   78  GLU GLU B . n 
B 1 406 ASN 406 79   79  ASN ASN B . n 
B 1 407 LEU 407 80   80  LEU LEU B . n 
B 1 408 ASN 408 81   81  ASN ASN B . n 
B 1 409 LYS 409 82   82  LYS LYS B . n 
B 1 410 LYS 410 83   83  LYS LYS B . n 
B 1 411 VAL 411 84   84  VAL VAL B . n 
B 1 412 ASP 412 85   85  ASP ASP B . n 
B 1 413 ASP 413 86   86  ASP ASP B . n 
B 1 414 GLY 414 87   87  GLY GLY B . n 
B 1 415 PHE 415 88   88  PHE PHE B . n 
B 1 416 LEU 416 89   89  LEU LEU B . n 
B 1 417 ASP 417 90   90  ASP ASP B . n 
B 1 418 ILE 418 91   91  ILE ILE B . n 
B 1 419 TRP 419 92   92  TRP TRP B . n 
B 1 420 THR 420 93   93  THR THR B . n 
B 1 421 TYR 421 94   94  TYR TYR B . n 
B 1 422 ASN 422 95   95  ASN ASN B . n 
B 1 423 ALA 423 96   96  ALA ALA B . n 
B 1 424 GLU 424 97   97  GLU GLU B . n 
B 1 425 LEU 425 98   98  LEU LEU B . n 
B 1 426 LEU 426 99   99  LEU LEU B . n 
B 1 427 VAL 427 100  100 VAL VAL B . n 
B 1 428 LEU 428 101  101 LEU LEU B . n 
B 1 429 LEU 429 102  102 LEU LEU B . n 
B 1 430 GLU 430 103  103 GLU GLU B . n 
B 1 431 ASN 431 104  104 ASN ASN B . n 
B 1 432 GLU 432 105  105 GLU GLU B . n 
B 1 433 ARG 433 106  106 ARG ARG B . n 
B 1 434 THR 434 107  107 THR THR B . n 
B 1 435 LEU 435 108  108 LEU LEU B . n 
B 1 436 ASP 436 109  109 ASP ASP B . n 
B 1 437 TYR 437 110  110 TYR TYR B . n 
B 1 438 HIS 438 111  111 HIS HIS B . n 
B 1 439 ASP 439 112  112 ASP ASP B . n 
B 1 440 SER 440 113  113 SER SER B . n 
B 1 441 ASN 441 114  114 ASN ASN B . n 
B 1 442 VAL 442 115  115 VAL VAL B . n 
B 1 443 LYS 443 116  116 LYS LYS B . n 
B 1 444 ASN 444 117  117 ASN ASN B . n 
B 1 445 LEU 445 118  118 LEU LEU B . n 
B 1 446 TYR 446 119  119 TYR TYR B . n 
B 1 447 GLU 447 120  120 GLU GLU B . n 
B 1 448 LYS 448 121  121 LYS LYS B . n 
B 1 449 VAL 449 122  122 VAL VAL B . n 
B 1 450 ARG 450 123  123 ARG ARG B . n 
B 1 451 SER 451 124  124 SER SER B . n 
B 1 452 GLN 452 125  125 GLN GLN B . n 
B 1 453 LEU 453 126  126 LEU LEU B . n 
B 1 454 LYS 454 127  127 LYS LYS B . n 
B 1 455 ASN 455 128  128 ASN ASN B . n 
B 1 456 ASN 456 129  129 ASN ASN B . n 
B 1 457 ALA 457 130  130 ALA ALA B . n 
B 1 458 LYS 458 131  131 LYS LYS B . n 
B 1 459 GLU 459 132  132 GLU GLU B . n 
B 1 460 ILE 460 133  133 ILE ILE B . n 
B 1 461 GLY 461 134  134 GLY GLY B . n 
B 1 462 ASN 462 135  135 ASN ASN B . n 
B 1 463 GLY 463 136  136 GLY GLY B . n 
B 1 464 CYS 464 137  137 CYS CYS B . n 
B 1 465 PHE 465 138  138 PHE PHE B . n 
B 1 466 GLU 466 139  139 GLU GLU B . n 
B 1 467 PHE 467 140  140 PHE PHE B . n 
B 1 468 TYR 468 141  141 TYR TYR B . n 
B 1 469 HIS 469 142  142 HIS HIS B . n 
B 1 470 LYS 470 143  143 LYS LYS B . n 
B 1 471 CYS 471 144  144 CYS CYS B . n 
B 1 472 ASP 472 145  145 ASP ASP B . n 
B 1 473 ASN 473 146  146 ASN ASN B . n 
B 1 474 THR 474 147  147 THR THR B . n 
B 1 475 CYS 475 148  148 CYS CYS B . n 
B 1 476 MET 476 149  149 MET MET B . n 
B 1 477 GLU 477 150  150 GLU GLU B . n 
B 1 478 SER 478 151  151 SER SER B . n 
B 1 479 VAL 479 152  152 VAL VAL B . n 
B 1 480 LYS 480 153  153 LYS LYS B . n 
B 1 481 ASN 481 154  154 ASN ASN B . n 
B 1 482 GLY 482 155  155 GLY GLY B . n 
B 1 483 THR 483 156  156 THR THR B . n 
B 1 484 TYR 484 157  157 TYR TYR B . n 
B 1 485 ASP 485 158  158 ASP ASP B . n 
B 1 486 TYR 486 159  159 TYR TYR B . n 
B 1 487 PRO 487 160  160 PRO PRO B . n 
B 1 488 LYS 488 161  161 LYS LYS B . n 
B 1 489 TYR 489 162  162 TYR TYR B . n 
B 1 490 SER 490 163  163 SER SER B . n 
B 1 491 GLU 491 164  164 GLU GLU B . n 
B 1 492 GLU 492 165  165 GLU GLU B . n 
B 1 493 ALA 493 166  166 ALA ALA B . n 
B 1 494 LYS 494 167  167 LYS LYS B . n 
B 1 495 LEU 495 168  168 LEU LEU B . n 
B 1 496 ASN 496 169  169 ASN ASN B . n 
B 1 497 ARG 497 170  170 ARG ARG B . n 
B 1 498 GLU 498 171  171 GLU GLU B . n 
B 1 499 GLU 499 172  172 GLU GLU B . n 
B 1 500 ILE 500 173  173 ILE ILE B . n 
B 1 501 ASP 501 174  174 ASP ASP B . n 
B 1 502 SER 502 175  175 SER SER B . n 
B 1 503 GLY 503 176  ?   ?   ?   B . n 
B 1 504 ARG 504 177  ?   ?   ?   B . n 
B 1 505 LEU 505 178  ?   ?   ?   B . n 
B 1 506 VAL 506 179  ?   ?   ?   B . n 
B 1 507 PRO 507 180  ?   ?   ?   B . n 
B 1 508 ARG 508 181  ?   ?   ?   B . n 
B 1 509 GLY 509 182  ?   ?   ?   B . n 
B 1 510 SER 510 183  ?   ?   ?   B . n 
B 1 511 PRO 511 184  ?   ?   ?   B . n 
B 1 512 GLY 512 185  ?   ?   ?   B . n 
B 1 513 SER 513 186  ?   ?   ?   B . n 
B 1 514 GLY 514 187  ?   ?   ?   B . n 
B 1 515 TYR 515 188  ?   ?   ?   B . n 
B 1 516 ILE 516 189  ?   ?   ?   B . n 
B 1 517 PRO 517 190  ?   ?   ?   B . n 
B 1 518 GLU 518 191  ?   ?   ?   B . n 
B 1 519 ALA 519 192  ?   ?   ?   B . n 
B 1 520 PRO 520 193  ?   ?   ?   B . n 
B 1 521 ARG 521 194  ?   ?   ?   B . n 
B 1 522 ASP 522 195  ?   ?   ?   B . n 
B 1 523 GLY 523 196  ?   ?   ?   B . n 
B 1 524 GLN 524 197  ?   ?   ?   B . n 
B 1 525 ALA 525 198  ?   ?   ?   B . n 
B 1 526 TYR 526 199  ?   ?   ?   B . n 
B 1 527 VAL 527 200  ?   ?   ?   B . n 
B 1 528 ARG 528 201  ?   ?   ?   B . n 
B 1 529 LYS 529 202  ?   ?   ?   B . n 
B 1 530 ASP 530 203  ?   ?   ?   B . n 
B 1 531 GLY 531 204  ?   ?   ?   B . n 
B 1 532 GLU 532 205  ?   ?   ?   B . n 
B 1 533 TRP 533 206  ?   ?   ?   B . n 
B 1 534 VAL 534 207  ?   ?   ?   B . n 
B 1 535 LEU 535 208  ?   ?   ?   B . n 
B 1 536 LEU 536 209  ?   ?   ?   B . n 
B 1 537 SER 537 210  ?   ?   ?   B . n 
B 1 538 THR 538 211  ?   ?   ?   B . n 
B 1 539 PHE 539 212  ?   ?   ?   B . n 
B 1 540 LEU 540 213  ?   ?   ?   B . n 
B 1 541 GLY 541 214  ?   ?   ?   B . n 
C 2 1   GLN 1   1    1   GLN GLN H . n 
C 2 2   VAL 2   2    2   VAL VAL H . n 
C 2 3   GLN 3   3    3   GLN GLN H . n 
C 2 4   LEU 4   4    4   LEU LEU H . n 
C 2 5   GLN 5   5    5   GLN GLN H . n 
C 2 6   GLU 6   6    6   GLU GLU H . n 
C 2 7   SER 7   7    7   SER SER H . n 
C 2 8   GLY 8   8    8   GLY GLY H . n 
C 2 9   PRO 9   9    9   PRO PRO H . n 
C 2 10  GLY 10  10   10  GLY GLY H . n 
C 2 11  LEU 11  11   11  LEU LEU H . n 
C 2 12  VAL 12  12   12  VAL VAL H . n 
C 2 13  LYS 13  13   13  LYS LYS H . n 
C 2 14  PRO 14  14   14  PRO PRO H . n 
C 2 15  SER 15  15   15  SER SER H . n 
C 2 16  GLU 16  16   16  GLU GLU H . n 
C 2 17  THR 17  17   17  THR THR H . n 
C 2 18  LEU 18  18   18  LEU LEU H . n 
C 2 19  SER 19  19   19  SER SER H . n 
C 2 20  LEU 20  20   20  LEU LEU H . n 
C 2 21  THR 21  21   21  THR THR H . n 
C 2 22  CYS 22  22   22  CYS CYS H . n 
C 2 23  SER 23  23   23  SER SER H . n 
C 2 24  VAL 24  24   24  VAL VAL H . n 
C 2 25  SER 25  25   25  SER SER H . n 
C 2 26  GLY 26  26   26  GLY GLY H . n 
C 2 27  ALA 27  27   27  ALA ALA H . n 
C 2 28  SER 28  28   28  SER SER H . n 
C 2 29  ILE 29  29   29  ILE ILE H . n 
C 2 30  SER 30  30   30  SER SER H . n 
C 2 31  SER 31  31   31  SER SER H . n 
C 2 32  TYR 32  32   32  TYR TYR H . n 
C 2 33  TYR 33  33   33  TYR TYR H . n 
C 2 34  TRP 34  34   34  TRP TRP H . n 
C 2 35  ILE 35  35   35  ILE ILE H . n 
C 2 36  TRP 36  36   36  TRP TRP H . n 
C 2 37  ILE 37  37   37  ILE ILE H . n 
C 2 38  ARG 38  38   38  ARG ARG H . n 
C 2 39  GLN 39  39   39  GLN GLN H . n 
C 2 40  PRO 40  40   40  PRO PRO H . n 
C 2 41  ALA 41  41   41  ALA ALA H . n 
C 2 42  GLY 42  42   42  GLY GLY H . n 
C 2 43  LYS 43  43   43  LYS LYS H . n 
C 2 44  GLY 44  44   44  GLY GLY H . n 
C 2 45  LEU 45  45   45  LEU LEU H . n 
C 2 46  GLU 46  46   46  GLU GLU H . n 
C 2 47  TRP 47  47   47  TRP TRP H . n 
C 2 48  ILE 48  48   48  ILE ILE H . n 
C 2 49  GLY 49  49   49  GLY GLY H . n 
C 2 50  ARG 50  50   50  ARG ARG H . n 
C 2 51  PHE 51  51   51  PHE PHE H . n 
C 2 52  TYR 52  52   52  TYR TYR H . n 
C 2 53  THR 53  53   53  THR THR H . n 
C 2 54  SER 54  54   54  SER SER H . n 
C 2 55  GLY 55  55   55  GLY GLY H . n 
C 2 56  SER 56  56   56  SER SER H . n 
C 2 57  PRO 57  57   57  PRO PRO H . n 
C 2 58  ASN 58  58   58  ASN ASN H . n 
C 2 59  TYR 59  59   59  TYR TYR H . n 
C 2 60  ASN 60  60   60  ASN ASN H . n 
C 2 61  PRO 61  61   61  PRO PRO H . n 
C 2 62  SER 62  62   62  SER SER H . n 
C 2 63  LEU 63  63   63  LEU LEU H . n 
C 2 64  ARG 64  64   64  ARG ARG H . n 
C 2 65  SER 65  65   65  SER SER H . n 
C 2 66  ARG 66  66   66  ARG ARG H . n 
C 2 67  VAL 67  67   67  VAL VAL H . n 
C 2 68  THR 68  68   68  THR THR H . n 
C 2 69  MET 69  69   69  MET MET H . n 
C 2 70  SER 70  70   70  SER SER H . n 
C 2 71  VAL 71  71   71  VAL VAL H . n 
C 2 72  ASP 72  72   72  ASP ASP H . n 
C 2 73  THR 73  73   73  THR THR H . n 
C 2 74  SER 74  74   74  SER SER H . n 
C 2 75  LYS 75  75   75  LYS LYS H . n 
C 2 76  ASN 76  76   76  ASN ASN H . n 
C 2 77  GLN 77  77   77  GLN GLN H . n 
C 2 78  PHE 78  78   78  PHE PHE H . n 
C 2 79  SER 79  79   79  SER SER H . n 
C 2 80  LEU 80  80   80  LEU LEU H . n 
C 2 81  LYS 81  81   81  LYS LYS H . n 
C 2 82  LEU 82  82   82  LEU LEU H . n 
C 2 83  THR 83  83   83  THR THR H . n 
C 2 84  SER 84  84   84  SER SER H . n 
C 2 85  VAL 85  85   85  VAL VAL H . n 
C 2 86  THR 86  86   86  THR THR H . n 
C 2 87  ALA 87  87   87  ALA ALA H . n 
C 2 88  ALA 88  88   88  ALA ALA H . n 
C 2 89  ASP 89  89   89  ASP ASP H . n 
C 2 90  THR 90  90   90  THR THR H . n 
C 2 91  ALA 91  91   91  ALA ALA H . n 
C 2 92  VAL 92  92   92  VAL VAL H . n 
C 2 93  TYR 93  93   93  TYR TYR H . n 
C 2 94  TYR 94  94   94  TYR TYR H . n 
C 2 95  CYS 95  95   95  CYS CYS H . n 
C 2 96  ALA 96  96   96  ALA ALA H . n 
C 2 97  ARG 97  97   97  ARG ARG H . n 
C 2 98  GLU 98  98   98  GLU GLU H . n 
C 2 99  GLU 99  99   99  GLU GLU H . n 
C 2 100 HIS 100 100  100 HIS HIS H . n 
C 2 101 ILE 101 101  101 ILE ILE H . n 
C 2 102 THR 102 102  102 THR THR H . n 
C 2 103 PHE 103 103  103 PHE PHE H . n 
C 2 104 GLY 104 104  104 GLY GLY H . n 
C 2 105 GLY 105 105  105 GLY GLY H . n 
C 2 106 VAL 106 106  106 VAL VAL H . n 
C 2 107 ILE 107 107  107 ILE ILE H . n 
C 2 108 VAL 108 108  108 VAL VAL H . n 
C 2 109 ARG 109 109  109 ARG ARG H . n 
C 2 110 TYR 110 110  110 TYR TYR H . n 
C 2 111 TRP 111 111  111 TRP TRP H . n 
C 2 112 GLY 112 112  112 GLY GLY H . n 
C 2 113 GLN 113 113  113 GLN GLN H . n 
C 2 114 GLY 114 114  114 GLY GLY H . n 
C 2 115 THR 115 115  115 THR THR H . n 
C 2 116 LEU 116 116  116 LEU LEU H . n 
C 2 117 VAL 117 117  117 VAL VAL H . n 
C 2 118 THR 118 118  118 THR THR H . n 
C 2 119 VAL 119 119  119 VAL VAL H . n 
C 2 120 SER 120 120  120 SER SER H . n 
C 2 121 SER 121 121  121 SER SER H . n 
C 2 122 ALA 122 122  122 ALA ALA H . n 
C 2 123 SER 123 123  123 SER SER H . n 
C 2 124 THR 124 124  124 THR THR H . n 
C 2 125 LYS 125 125  125 LYS LYS H . n 
C 2 126 GLY 126 126  126 GLY GLY H . n 
C 2 127 PRO 127 127  127 PRO PRO H . n 
C 2 128 SER 128 128  128 SER SER H . n 
C 2 129 VAL 129 129  129 VAL VAL H . n 
C 2 130 PHE 130 130  130 PHE PHE H . n 
C 2 131 PRO 131 131  131 PRO PRO H . n 
C 2 132 LEU 132 132  132 LEU LEU H . n 
C 2 133 ALA 133 133  133 ALA ALA H . n 
C 2 134 PRO 134 134  134 PRO PRO H . n 
C 2 135 SER 135 135  135 SER SER H . n 
C 2 136 SER 136 136  136 SER SER H . n 
C 2 137 LYS 137 137  137 LYS LYS H . n 
C 2 138 SER 138 138  138 SER SER H . n 
C 2 139 THR 139 139  139 THR THR H . n 
C 2 140 SER 140 140  140 SER SER H . n 
C 2 141 GLY 141 141  141 GLY GLY H . n 
C 2 142 GLY 142 142  142 GLY GLY H . n 
C 2 143 THR 143 143  143 THR THR H . n 
C 2 144 ALA 144 144  144 ALA ALA H . n 
C 2 145 ALA 145 145  145 ALA ALA H . n 
C 2 146 LEU 146 146  146 LEU LEU H . n 
C 2 147 GLY 147 147  147 GLY GLY H . n 
C 2 148 CYS 148 148  148 CYS CYS H . n 
C 2 149 LEU 149 149  149 LEU LEU H . n 
C 2 150 VAL 150 150  150 VAL VAL H . n 
C 2 151 LYS 151 151  151 LYS LYS H . n 
C 2 152 ASP 152 152  152 ASP ASP H . n 
C 2 153 TYR 153 153  153 TYR TYR H . n 
C 2 154 PHE 154 154  154 PHE PHE H . n 
C 2 155 PRO 155 155  155 PRO PRO H . n 
C 2 156 GLU 156 156  156 GLU GLU H . n 
C 2 157 PRO 157 157  157 PRO PRO H . n 
C 2 158 VAL 158 158  158 VAL VAL H . n 
C 2 159 THR 159 159  159 THR THR H . n 
C 2 160 VAL 160 160  160 VAL VAL H . n 
C 2 161 SER 161 161  161 SER SER H . n 
C 2 162 TRP 162 162  162 TRP TRP H . n 
C 2 163 ASN 163 163  163 ASN ASN H . n 
C 2 164 SER 164 164  164 SER SER H . n 
C 2 165 GLY 165 165  165 GLY GLY H . n 
C 2 166 ALA 166 166  166 ALA ALA H . n 
C 2 167 LEU 167 167  167 LEU LEU H . n 
C 2 168 THR 168 168  168 THR THR H . n 
C 2 169 SER 169 169  169 SER SER H . n 
C 2 170 GLY 170 170  170 GLY GLY H . n 
C 2 171 VAL 171 171  171 VAL VAL H . n 
C 2 172 HIS 172 172  172 HIS HIS H . n 
C 2 173 THR 173 173  173 THR THR H . n 
C 2 174 PHE 174 174  174 PHE PHE H . n 
C 2 175 PRO 175 175  175 PRO PRO H . n 
C 2 176 ALA 176 176  176 ALA ALA H . n 
C 2 177 VAL 177 177  177 VAL VAL H . n 
C 2 178 LEU 178 178  178 LEU LEU H . n 
C 2 179 GLN 179 179  179 GLN GLN H . n 
C 2 180 SER 180 180  180 SER SER H . n 
C 2 181 SER 181 181  181 SER SER H . n 
C 2 182 GLY 182 182  182 GLY GLY H . n 
C 2 183 LEU 183 183  183 LEU LEU H . n 
C 2 184 TYR 184 184  184 TYR TYR H . n 
C 2 185 SER 185 185  185 SER SER H . n 
C 2 186 LEU 186 186  186 LEU LEU H . n 
C 2 187 SER 187 187  187 SER SER H . n 
C 2 188 SER 188 188  188 SER SER H . n 
C 2 189 VAL 189 189  189 VAL VAL H . n 
C 2 190 VAL 190 190  190 VAL VAL H . n 
C 2 191 THR 191 191  191 THR THR H . n 
C 2 192 VAL 192 192  192 VAL VAL H . n 
C 2 193 PRO 193 193  193 PRO PRO H . n 
C 2 194 SER 194 194  194 SER SER H . n 
C 2 195 SER 195 195  195 SER SER H . n 
C 2 196 SER 196 196  196 SER SER H . n 
C 2 197 LEU 197 197  197 LEU LEU H . n 
C 2 198 GLY 198 198  198 GLY GLY H . n 
C 2 199 THR 199 199  199 THR THR H . n 
C 2 200 GLN 200 200  200 GLN GLN H . n 
C 2 201 THR 201 201  201 THR THR H . n 
C 2 202 TYR 202 202  202 TYR TYR H . n 
C 2 203 ILE 203 203  203 ILE ILE H . n 
C 2 204 CYS 204 204  204 CYS CYS H . n 
C 2 205 ASN 205 205  205 ASN ASN H . n 
C 2 206 VAL 206 206  206 VAL VAL H . n 
C 2 207 ASN 207 207  207 ASN ASN H . n 
C 2 208 HIS 208 208  208 HIS HIS H . n 
C 2 209 LYS 209 209  209 LYS LYS H . n 
C 2 210 PRO 210 210  210 PRO PRO H . n 
C 2 211 SER 211 211  211 SER SER H . n 
C 2 212 ASN 212 212  212 ASN ASN H . n 
C 2 213 THR 213 213  213 THR THR H . n 
C 2 214 LYS 214 214  214 LYS LYS H . n 
C 2 215 VAL 215 215  215 VAL VAL H . n 
C 2 216 ASP 216 216  216 ASP ASP H . n 
C 2 217 LYS 217 217  217 LYS LYS H . n 
C 2 218 ARG 218 218  218 ARG ARG H . n 
C 2 219 VAL 219 219  219 VAL VAL H . n 
C 2 220 GLU 220 220  220 GLU GLU H . n 
C 2 221 PRO 221 221  221 PRO PRO H . n 
C 2 222 LYS 222 222  ?   ?   ?   H . n 
C 2 223 SER 223 223  ?   ?   ?   H . n 
C 2 224 CYS 224 224  ?   ?   ?   H . n 
D 3 1   ASP 1   1    1   ASP ASP L . n 
D 3 2   ILE 2   2    2   ILE ILE L . n 
D 3 3   GLN 3   3    3   GLN GLN L . n 
D 3 4   MET 4   4    4   MET MET L . n 
D 3 5   THR 5   5    5   THR THR L . n 
D 3 6   GLN 6   6    6   GLN GLN L . n 
D 3 7   SER 7   7    7   SER SER L . n 
D 3 8   PRO 8   8    8   PRO PRO L . n 
D 3 9   ALA 9   9    9   ALA ALA L . n 
D 3 10  THR 10  10   10  THR THR L . n 
D 3 11  LEU 11  11   11  LEU LEU L . n 
D 3 12  SER 12  12   12  SER SER L . n 
D 3 13  ALA 13  13   13  ALA ALA L . n 
D 3 14  SER 14  14   14  SER SER L . n 
D 3 15  VAL 15  15   15  VAL VAL L . n 
D 3 16  GLY 16  16   16  GLY GLY L . n 
D 3 17  ASP 17  17   17  ASP ASP L . n 
D 3 18  ARG 18  18   18  ARG ARG L . n 
D 3 19  VAL 19  19   19  VAL VAL L . n 
D 3 20  SER 20  20   20  SER SER L . n 
D 3 21  ILE 21  21   21  ILE ILE L . n 
D 3 22  THR 22  22   22  THR THR L . n 
D 3 23  CYS 23  23   23  CYS CYS L . n 
D 3 24  ARG 24  24   24  ARG ARG L . n 
D 3 25  ALA 25  25   25  ALA ALA L . n 
D 3 26  SER 26  26   26  SER SER L . n 
D 3 27  GLN 27  27   27  GLN GLN L . n 
D 3 28  SER 28  28   28  SER SER L . n 
D 3 29  ILE 29  29   29  ILE ILE L . n 
D 3 30  SER 30  30   30  SER SER L . n 
D 3 31  SER 31  31   31  SER SER L . n 
D 3 32  TRP 32  32   32  TRP TRP L . n 
D 3 33  LEU 33  33   33  LEU LEU L . n 
D 3 34  ALA 34  34   34  ALA ALA L . n 
D 3 35  TRP 35  35   35  TRP TRP L . n 
D 3 36  TYR 36  36   36  TYR TYR L . n 
D 3 37  GLN 37  37   37  GLN GLN L . n 
D 3 38  GLN 38  38   38  GLN GLN L . n 
D 3 39  LYS 39  39   39  LYS LYS L . n 
D 3 40  PRO 40  40   40  PRO PRO L . n 
D 3 41  GLY 41  41   41  GLY GLY L . n 
D 3 42  LYS 42  42   42  LYS LYS L . n 
D 3 43  ALA 43  43   43  ALA ALA L . n 
D 3 44  PRO 44  44   44  PRO PRO L . n 
D 3 45  LYS 45  45   45  LYS LYS L . n 
D 3 46  LEU 46  46   46  LEU LEU L . n 
D 3 47  LEU 47  47   47  LEU LEU L . n 
D 3 48  ILE 48  48   48  ILE ILE L . n 
D 3 49  TYR 49  49   49  TYR TYR L . n 
D 3 50  LYS 50  50   50  LYS LYS L . n 
D 3 51  ALA 51  51   51  ALA ALA L . n 
D 3 52  SER 52  52   52  SER SER L . n 
D 3 53  SER 53  53   53  SER SER L . n 
D 3 54  LEU 54  54   54  LEU LEU L . n 
D 3 55  GLU 55  55   55  GLU GLU L . n 
D 3 56  SER 56  56   56  SER SER L . n 
D 3 57  GLY 57  57   57  GLY GLY L . n 
D 3 58  VAL 58  58   58  VAL VAL L . n 
D 3 59  PRO 59  59   59  PRO PRO L . n 
D 3 60  SER 60  60   60  SER SER L . n 
D 3 61  ARG 61  61   61  ARG ARG L . n 
D 3 62  PHE 62  62   62  PHE PHE L . n 
D 3 63  SER 63  63   63  SER SER L . n 
D 3 64  GLY 64  64   64  GLY GLY L . n 
D 3 65  SER 65  65   65  SER SER L . n 
D 3 66  GLY 66  66   66  GLY GLY L . n 
D 3 67  SER 67  67   67  SER SER L . n 
D 3 68  GLY 68  68   68  GLY GLY L . n 
D 3 69  SER 69  69   69  SER SER L . n 
D 3 70  GLU 70  70   70  GLU GLU L . n 
D 3 71  PHE 71  71   71  PHE PHE L . n 
D 3 72  THR 72  72   72  THR THR L . n 
D 3 73  LEU 73  73   73  LEU LEU L . n 
D 3 74  THR 74  74   74  THR THR L . n 
D 3 75  ILE 75  75   75  ILE ILE L . n 
D 3 76  SER 76  76   76  SER SER L . n 
D 3 77  SER 77  77   77  SER SER L . n 
D 3 78  LEU 78  78   78  LEU LEU L . n 
D 3 79  GLN 79  79   79  GLN GLN L . n 
D 3 80  PRO 80  80   80  PRO PRO L . n 
D 3 81  ASP 81  81   81  ASP ASP L . n 
D 3 82  ASP 82  82   82  ASP ASP L . n 
D 3 83  PHE 83  83   83  PHE PHE L . n 
D 3 84  ALA 84  84   84  ALA ALA L . n 
D 3 85  ILE 85  85   85  ILE ILE L . n 
D 3 86  TYR 86  86   86  TYR TYR L . n 
D 3 87  TYR 87  87   87  TYR TYR L . n 
D 3 88  CYS 88  88   88  CYS CYS L . n 
D 3 89  GLN 89  89   89  GLN GLN L . n 
D 3 90  GLN 90  90   90  GLN GLN L . n 
D 3 91  TYR 91  91   91  TYR TYR L . n 
D 3 92  ASN 92  92   92  ASN ASN L . n 
D 3 93  SER 93  93   93  SER SER L . n 
D 3 94  TYR 94  94   94  TYR TYR L . n 
D 3 95  PRO 95  95   95  PRO PRO L . n 
D 3 96  TRP 96  96   96  TRP TRP L . n 
D 3 97  THR 97  97   97  THR THR L . n 
D 3 98  PHE 98  98   98  PHE PHE L . n 
D 3 99  GLY 99  99   99  GLY GLY L . n 
D 3 100 GLN 100 100  100 GLN GLN L . n 
D 3 101 GLY 101 101  101 GLY GLY L . n 
D 3 102 THR 102 102  102 THR THR L . n 
D 3 103 LYS 103 103  103 LYS LYS L . n 
D 3 104 VAL 104 104  104 VAL VAL L . n 
D 3 105 GLU 105 105  105 GLU GLU L . n 
D 3 106 ILE 106 106  106 ILE ILE L . n 
D 3 107 LYS 107 107  107 LYS LYS L . n 
D 3 108 ARG 108 108  108 ARG ARG L . n 
D 3 109 THR 109 109  109 THR THR L . n 
D 3 110 VAL 110 110  110 VAL VAL L . n 
D 3 111 ALA 111 111  111 ALA ALA L . n 
D 3 112 ALA 112 112  112 ALA ALA L . n 
D 3 113 PRO 113 113  113 PRO PRO L . n 
D 3 114 SER 114 114  114 SER SER L . n 
D 3 115 VAL 115 115  115 VAL VAL L . n 
D 3 116 PHE 116 116  116 PHE PHE L . n 
D 3 117 ILE 117 117  117 ILE ILE L . n 
D 3 118 PHE 118 118  118 PHE PHE L . n 
D 3 119 PRO 119 119  119 PRO PRO L . n 
D 3 120 PRO 120 120  120 PRO PRO L . n 
D 3 121 SER 121 121  121 SER SER L . n 
D 3 122 ASP 122 122  122 ASP ASP L . n 
D 3 123 GLU 123 123  123 GLU GLU L . n 
D 3 124 GLN 124 124  124 GLN GLN L . n 
D 3 125 LEU 125 125  125 LEU LEU L . n 
D 3 126 LYS 126 126  126 LYS LYS L . n 
D 3 127 SER 127 127  127 SER SER L . n 
D 3 128 GLY 128 128  128 GLY GLY L . n 
D 3 129 THR 129 129  129 THR THR L . n 
D 3 130 ALA 130 130  130 ALA ALA L . n 
D 3 131 SER 131 131  131 SER SER L . n 
D 3 132 VAL 132 132  132 VAL VAL L . n 
D 3 133 VAL 133 133  133 VAL VAL L . n 
D 3 134 CYS 134 134  134 CYS CYS L . n 
D 3 135 LEU 135 135  135 LEU LEU L . n 
D 3 136 LEU 136 136  136 LEU LEU L . n 
D 3 137 ASN 137 137  137 ASN ASN L . n 
D 3 138 ASN 138 138  138 ASN ASN L . n 
D 3 139 PHE 139 139  139 PHE PHE L . n 
D 3 140 TYR 140 140  140 TYR TYR L . n 
D 3 141 PRO 141 141  141 PRO PRO L . n 
D 3 142 ARG 142 142  142 ARG ARG L . n 
D 3 143 GLU 143 143  143 GLU GLU L . n 
D 3 144 ALA 144 144  144 ALA ALA L . n 
D 3 145 LYS 145 145  145 LYS LYS L . n 
D 3 146 VAL 146 146  146 VAL VAL L . n 
D 3 147 GLN 147 147  147 GLN GLN L . n 
D 3 148 TRP 148 148  148 TRP TRP L . n 
D 3 149 LYS 149 149  149 LYS LYS L . n 
D 3 150 VAL 150 150  150 VAL VAL L . n 
D 3 151 ASP 151 151  151 ASP ASP L . n 
D 3 152 ASN 152 152  152 ASN ASN L . n 
D 3 153 ALA 153 153  153 ALA ALA L . n 
D 3 154 LEU 154 154  154 LEU LEU L . n 
D 3 155 GLN 155 155  155 GLN GLN L . n 
D 3 156 SER 156 156  156 SER SER L . n 
D 3 157 GLY 157 157  157 GLY GLY L . n 
D 3 158 ASN 158 158  158 ASN ASN L . n 
D 3 159 SER 159 159  159 SER SER L . n 
D 3 160 GLN 160 160  160 GLN GLN L . n 
D 3 161 GLU 161 161  161 GLU GLU L . n 
D 3 162 SER 162 162  162 SER SER L . n 
D 3 163 VAL 163 163  163 VAL VAL L . n 
D 3 164 THR 164 164  164 THR THR L . n 
D 3 165 GLU 165 165  165 GLU GLU L . n 
D 3 166 GLN 166 166  166 GLN GLN L . n 
D 3 167 ASP 167 167  167 ASP ASP L . n 
D 3 168 SER 168 168  168 SER SER L . n 
D 3 169 LYS 169 169  169 LYS LYS L . n 
D 3 170 ASP 170 170  170 ASP ASP L . n 
D 3 171 SER 171 171  171 SER SER L . n 
D 3 172 THR 172 172  172 THR THR L . n 
D 3 173 TYR 173 173  173 TYR TYR L . n 
D 3 174 SER 174 174  174 SER SER L . n 
D 3 175 LEU 175 175  175 LEU LEU L . n 
D 3 176 SER 176 176  176 SER SER L . n 
D 3 177 SER 177 177  177 SER SER L . n 
D 3 178 THR 178 178  178 THR THR L . n 
D 3 179 LEU 179 179  179 LEU LEU L . n 
D 3 180 THR 180 180  180 THR THR L . n 
D 3 181 LEU 181 181  181 LEU LEU L . n 
D 3 182 SER 182 182  182 SER SER L . n 
D 3 183 LYS 183 183  183 LYS LYS L . n 
D 3 184 ALA 184 184  184 ALA ALA L . n 
D 3 185 ASP 185 185  185 ASP ASP L . n 
D 3 186 TYR 186 186  186 TYR TYR L . n 
D 3 187 GLU 187 187  187 GLU GLU L . n 
D 3 188 LYS 188 188  188 LYS LYS L . n 
D 3 189 HIS 189 189  189 HIS HIS L . n 
D 3 190 LYS 190 190  190 LYS LYS L . n 
D 3 191 VAL 191 191  191 VAL VAL L . n 
D 3 192 TYR 192 192  192 TYR TYR L . n 
D 3 193 ALA 193 193  193 ALA ALA L . n 
D 3 194 CYS 194 194  194 CYS CYS L . n 
D 3 195 GLU 195 195  195 GLU GLU L . n 
D 3 196 VAL 196 196  196 VAL VAL L . n 
D 3 197 THR 197 197  197 THR THR L . n 
D 3 198 HIS 198 198  198 HIS HIS L . n 
D 3 199 GLN 199 199  199 GLN GLN L . n 
D 3 200 GLY 200 200  200 GLY GLY L . n 
D 3 201 LEU 201 201  201 LEU LEU L . n 
D 3 202 SER 202 202  202 SER SER L . n 
D 3 203 SER 203 203  203 SER SER L . n 
D 3 204 PRO 204 204  204 PRO PRO L . n 
D 3 205 VAL 205 205  205 VAL VAL L . n 
D 3 206 THR 206 206  206 THR THR L . n 
D 3 207 LYS 207 207  207 LYS LYS L . n 
D 3 208 SER 208 208  208 SER SER L . n 
D 3 209 PHE 209 209  209 PHE PHE L . n 
D 3 210 ASN 210 210  210 ASN ASN L . n 
D 3 211 ARG 211 211  211 ARG ARG L . n 
D 3 212 GLY 212 212  212 GLY GLY L . n 
D 3 213 GLU 213 213  ?   ?   ?   L . n 
D 3 214 CYS 214 214  ?   ?   ?   L . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
E 4 NAG 1 S NAG 1 S NAG 1 n 
E 4 NAG 2 S NAG 2 S NAG 2 n 
E 4 BMA 3 S BMA 3 S BMA 3 n 
F 4 NAG 1 C NAG 1 C NAG 1 n 
F 4 NAG 2 C NAG 2 C NAG 2 n 
F 4 BMA 3 C BMA 3 C BMA 3 n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 BMA ? ? BMA ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NAG ? ? NAG ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
_pdbx_nonpoly_scheme.asym_id         G 
_pdbx_nonpoly_scheme.entity_id       5 
_pdbx_nonpoly_scheme.mon_id          NAG 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     601 
_pdbx_nonpoly_scheme.auth_seq_num    326 
_pdbx_nonpoly_scheme.pdb_mon_id      NAG 
_pdbx_nonpoly_scheme.auth_mon_id     NAG 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
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 N 1 C NAG 1   ? O1 ? F NAG 1 O1 
2 1 N 1 A NAG 601 ? O1 ? G NAG 1 O1 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.19.2_4158: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9C0V 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     241.491 
_cell.length_a_esd                 ? 
_cell.length_b                     241.491 
_cell.length_b_esd                 ? 
_cell.length_c                     241.491 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        48 
_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                         9C0V 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                199 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 21 3' 
_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                   9C0V 
_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             3.47 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          64.52 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M sodium cacodylate, pH 6.5, 0.8 M sodium citrate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_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         2022-07-24 
_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   0.979 
_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 BL12-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-1 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9C0V 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.50 
_reflns.d_resolution_low                               40.28 
_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                                     29612 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                41.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.3 
_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                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.50 
_reflns_shell.d_res_low                                     3.56 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1459 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.776 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9C0V 
_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                            3.50 
_refine.ls_d_res_low                             40.25 
_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                     28704 
_refine.ls_number_reflns_R_free                  1371 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.97 
_refine.ls_percent_reflns_R_free                 4.78 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2937 
_refine.ls_R_factor_R_free                       0.3214 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2923 
_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                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 43.46 
_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                            0.88 
_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                       3.50 
_refine_hist.d_res_low                        40.25 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               7207 
_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        7115 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         92 
_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' ? 0.009  ? 7371  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.494  ? 10017 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.866 ? 2690  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.171  ? 1134  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.019  ? 1273  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.50 3.62  . . 152 2615 95.00  . . . . 0.4746 . . . . . . . . . . . 0.4734 
'X-RAY DIFFRACTION' 3.63 3.77  . . 123 2481 89.00  . . . . 0.5823 . . . . . . . . . . . 0.6020 
'X-RAY DIFFRACTION' 3.77 3.94  . . 133 2476 88.00  . . . . 0.5696 . . . . . . . . . . . 0.5998 
'X-RAY DIFFRACTION' 3.94 4.15  . . 130 2753 99.00  . . . . 0.3303 . . . . . . . . . . . 0.3496 
'X-RAY DIFFRACTION' 4.15 4.41  . . 144 2817 100.00 . . . . 0.2698 . . . . . . . . . . . 0.2947 
'X-RAY DIFFRACTION' 4.41 4.75  . . 133 2823 100.00 . . . . 0.2432 . . . . . . . . . . . 0.2577 
'X-RAY DIFFRACTION' 4.75 5.23  . . 144 2800 100.00 . . . . 0.2323 . . . . . . . . . . . 0.2703 
'X-RAY DIFFRACTION' 5.23 5.98  . . 147 2825 100.00 . . . . 0.2611 . . . . . . . . . . . 0.3031 
'X-RAY DIFFRACTION' 5.98 7.52  . . 122 2854 100.00 . . . . 0.2631 . . . . . . . . . . . 0.3076 
'X-RAY DIFFRACTION' 7.53 40.25 . . 143 2889 99.00  . . . . 0.2198 . . . . . . . . . . . 0.2359 
# 
_struct.entry_id                     9C0V 
_struct.title                        
'Crystal structure of chimeric hemagglutinin cH5/1 in complex with broad protective antibody 3E1' 
_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        9C0V 
_struct_keywords.text            'immune system, VIRAL PROTEIN-IMMUNE SYSTEM complex' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN/IMMUNE SYSTEM' 
# 
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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 PDB 9C0V 9C0V ? 1 ? 1 
2 PDB 9C0V 9C0V ? 2 ? 1 
3 PDB 9C0V 9C0V ? 3 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9C0V A 1 ? 541 ? 9C0V 10   ? 543 ? 10   543 
2 1 9C0V B 1 ? 541 ? 9C0V -326 ? 214 ? -326 214 
3 2 9C0V H 1 ? 224 ? 9C0V 1    ? 224 ? 1    224 
4 3 9C0V L 1 ? 214 ? 9C0V 1    ? 214 ? 1    214 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dodecameric 
_pdbx_struct_assembly.oligomeric_count     12 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 35840  ? 
1 MORE         -142   ? 
1 'SSA (A^2)'  126330 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1,2,3 A,B,E,F,G 
1 4,5,6 C,D       
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z       1.0000000000  0.0000000000 0.0000000000  0.0000000000   0.0000000000  
1.0000000000 0.0000000000  0.0000000000   0.0000000000  0.0000000000 1.0000000000  0.0000000000   
2 'crystal symmetry operation' 5_555  z,x,y       0.0000000000  0.0000000000 1.0000000000  0.0000000000   1.0000000000  
0.0000000000 0.0000000000  0.0000000000   0.0000000000  1.0000000000 0.0000000000  0.0000000000   
3 'crystal symmetry operation' 9_555  y,z,x       0.0000000000  1.0000000000 0.0000000000  0.0000000000   0.0000000000  
0.0000000000 1.0000000000  0.0000000000   1.0000000000  0.0000000000 0.0000000000  0.0000000000   
4 'crystal symmetry operation' 15_555 -x+1/2,y,-z -1.0000000000 0.0000000000 0.0000000000  120.7455000000 0.0000000000  
1.0000000000 0.0000000000  0.0000000000   0.0000000000  0.0000000000 -1.0000000000 0.0000000000   
5 'crystal symmetry operation' 19_555 -z,-x+1/2,y 0.0000000000  0.0000000000 -1.0000000000 0.0000000000   -1.0000000000 
0.0000000000 0.0000000000  120.7455000000 0.0000000000  1.0000000000 0.0000000000  0.0000000000   
6 'crystal symmetry operation' 23_555 y,-z,-x+1/2 0.0000000000  1.0000000000 0.0000000000  0.0000000000   0.0000000000  
0.0000000000 -1.0000000000 0.0000000000   -1.0000000000 0.0000000000 0.0000000000  120.7455000000 
# 
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 SER A 57  ? GLY A 64  ? SER A 65  GLY A 72  1 ? 8  
HELX_P HELX_P2  AA2 CYS A 68  ? ILE A 72  ? CYS A 76  ILE A 80  5 ? 5  
HELX_P HELX_P3  AA3 ASP A 98  ? ILE A 109 ? ASP A 104 ILE A 115 1 ? 12 
HELX_P HELX_P4  AA4 ASP A 184 ? TYR A 192 ? ASP A 187 TYR A 195 1 ? 9  
HELX_P HELX_P5  AA5 ASP B 364 ? GLU B 384 ? ASP B 37  GLU B 57  1 ? 21 
HELX_P HELX_P6  AA6 ILE B 404 ? LYS B 454 ? ILE B 77  LYS B 127 1 ? 51 
HELX_P HELX_P7  AA7 ASP B 472 ? GLY B 482 ? ASP B 145 GLY B 155 1 ? 11 
HELX_P HELX_P8  AA8 TYR B 486 ? LYS B 488 ? TYR B 159 LYS B 161 5 ? 3  
HELX_P HELX_P9  AA9 TYR B 489 ? SER B 502 ? TYR B 162 SER B 175 1 ? 14 
HELX_P HELX_P10 AB1 SER C 28  ? TYR C 32  ? SER H 28  TYR H 32  5 ? 5  
HELX_P HELX_P11 AB2 SER C 195 ? GLY C 198 ? SER H 195 GLY H 198 5 ? 4  
HELX_P HELX_P12 AB3 GLN D 79  ? PHE D 83  ? GLN L 79  PHE L 83  5 ? 5  
HELX_P HELX_P13 AB4 SER D 121 ? GLY D 128 ? SER L 121 GLY L 128 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?    ? A CYS 5   SG  ? ? ? 1_555 B CYS 464 SG ? ? A CYS 14  B CYS 137 1_555 ? ? ? ? ? ? ? 2.042 ? ?               
disulf2 disulf ?    ? A CYS 91  SG  ? ? ? 1_555 A CYS 136 SG ? ? A CYS 97  A CYS 139 1_555 ? ? ? ? ? ? ? 2.027 ? ?               
disulf3 disulf ?    ? C CYS 22  SG  ? ? ? 1_555 C CYS 95  SG ? ? H CYS 22  H CYS 95  1_555 ? ? ? ? ? ? ? 2.034 ? ?               
disulf4 disulf ?    ? C CYS 148 SG  ? ? ? 1_555 C CYS 204 SG ? ? H CYS 148 H CYS 204 1_555 ? ? ? ? ? ? ? 2.024 ? ?               
disulf5 disulf ?    ? D CYS 23  SG  ? ? ? 1_555 D CYS 88  SG ? ? L CYS 23  L CYS 88  1_555 ? ? ? ? ? ? ? 2.039 ? ?               
disulf6 disulf ?    ? D CYS 134 SG  ? ? ? 1_555 D CYS 194 SG ? ? L CYS 134 L CYS 194 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
covale1 covale one  ? A ASN 166 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 169 S NAG 1   1_555 ? ? ? ? ? ? ? 1.488 ? N-Glycosylation 
covale2 covale both ? E NAG .   O4  ? ? ? 1_555 E NAG .   C1 ? ? S NAG 1   S NAG 2   1_555 ? ? ? ? ? ? ? 1.434 ? ?               
covale3 covale both ? E NAG .   O4  ? ? ? 1_555 E BMA .   C1 ? ? S NAG 2   S BMA 3   1_555 ? ? ? ? ? ? ? 1.439 ? ?               
covale4 covale both ? F NAG .   O4  ? ? ? 1_555 F NAG .   C1 ? ? C NAG 1   C NAG 2   1_555 ? ? ? ? ? ? ? 1.440 ? ?               
covale5 covale both ? F NAG .   O4  ? ? ? 1_555 F BMA .   C1 ? ? C NAG 2   C BMA 3   1_555 ? ? ? ? ? ? ? 1.437 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG E .   ? ASN A 166 ? NAG S 1   ? 1_555 ASN A 169 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 CYS A 5   ? CYS B 464 ? CYS A 14  ? 1_555 CYS B 137 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
3 CYS A 91  ? CYS A 136 ? CYS A 97  ? 1_555 CYS A 139 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
4 CYS C 22  ? CYS C 95  ? CYS H 22  ? 1_555 CYS H 95  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
5 CYS C 148 ? CYS C 204 ? CYS H 148 ? 1_555 CYS H 204 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
6 CYS D 23  ? CYS D 88  ? CYS L 23  ? 1_555 CYS L 88  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
7 CYS D 134 ? CYS D 194 ? CYS L 134 ? 1_555 CYS L 194 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 7  D . ? SER 7  L PRO 8  D ? PRO 8  L 1 -28.89 
2 TYR 94 D . ? TYR 94 L PRO 95 D ? PRO 95 L 1 2.75   
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 5 ? 
AB4 ? 5 ? 
AB5 ? 4 ? 
AB6 ? 4 ? 
AB7 ? 3 ? 
AB8 ? 4 ? 
AB9 ? 6 ? 
AC1 ? 4 ? 
AC2 ? 4 ? 
AC3 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB3 4 5 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AB9 4 5 ? anti-parallel 
AB9 5 6 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 340 ? TRP B 341 ? GLY B 13  TRP B 14  
AA1 2 THR A 3   ? HIS A 9   ? THR A 12  HIS A 18  
AA1 3 TYR B 349 ? GLN B 354 ? TYR B 22  GLN B 27  
AA1 4 SER B 359 ? ALA B 363 ? SER B 32  ALA B 36  
AA2 1 GLY B 340 ? TRP B 341 ? GLY B 13  TRP B 14  
AA2 2 THR A 3   ? HIS A 9   ? THR A 12  HIS A 18  
AA2 3 CYS B 464 ? PHE B 467 ? CYS B 137 PHE B 140 
AA2 4 ALA B 457 ? GLY B 461 ? ALA B 130 GLY B 134 
AA3 1 THR A 16  ? VAL A 17  ? THR A 25  VAL A 26  
AA3 2 VAL A 25  ? THR A 26  ? VAL A 34  THR A 35  
AA4 1 SER A 30  ? ASN A 32  ? SER A 39  ASN A 41  
AA4 2 ARG A 313 ? ALA A 315 ? ARG A 315 ALA A 317 
AA5 1 LEU A 34  ? GLU A 35  ? LEU A 43  GLU A 44  
AA5 2 PHE A 292 ? GLN A 293 ? PHE A 294 GLN A 295 
AA5 3 LYS A 305 ? TYR A 306 ? LYS A 307 TYR A 308 
AA6 1 GLY A 94  ? PHE A 96  ? GLY A 100 PHE A 102 
AA6 2 ARG A 226 ? LEU A 234 ? ARG A 229 LEU A 237 
AA6 3 LEU A 173 ? HIS A 181 ? LEU A 176 HIS A 184 
AA6 4 PHE A 248 ? ILE A 249 ? PHE A 251 ILE A 252 
AA7 1 HIS A 111 ? LYS A 114 ? HIS A 117 LYS A 120 
AA7 2 TYR A 255 ? LYS A 259 ? TYR A 258 LYS A 261 
AA8 1 PRO A 137 ? TYR A 138 ? PRO A 140 TYR A 141 
AA8 2 LYS A 141 ? SER A 142 ? LYS A 144 SER A 145 
AA9 1 SER A 164 ? ASN A 166 ? SER A 167 ASN A 169 
AA9 2 ALA A 239 ? SER A 244 ? ALA A 242 SER A 247 
AA9 3 ILE A 199 ? THR A 203 ? ILE A 202 THR A 206 
AA9 4 ASN A 207 ? LEU A 210 ? ASN A 210 LEU A 213 
AB1 1 GLN C 3   ? SER C 7   ? GLN H 3   SER H 7   
AB1 2 LEU C 18  ? SER C 25  ? LEU H 18  SER H 25  
AB1 3 GLN C 77  ? LEU C 82  ? GLN H 77  LEU H 82  
AB1 4 VAL C 67  ? THR C 68  ? VAL H 67  THR H 68  
AB2 1 GLN C 3   ? SER C 7   ? GLN H 3   SER H 7   
AB2 2 LEU C 18  ? SER C 25  ? LEU H 18  SER H 25  
AB2 3 GLN C 77  ? LEU C 82  ? GLN H 77  LEU H 82  
AB2 4 VAL C 71  ? ASP C 72  ? VAL H 71  ASP H 72  
AB3 1 GLY C 55  ? TYR C 59  ? GLY H 55  TYR H 59  
AB3 2 GLU C 46  ? TYR C 52  ? GLU H 46  TYR H 52  
AB3 3 TYR C 33  ? GLN C 39  ? TYR H 33  GLN H 39  
AB3 4 ALA C 91  ? GLU C 98  ? ALA H 91  GLU H 98  
AB3 5 TYR C 110 ? TRP C 111 ? TYR H 110 TRP H 111 
AB4 1 GLY C 55  ? TYR C 59  ? GLY H 55  TYR H 59  
AB4 2 GLU C 46  ? TYR C 52  ? GLU H 46  TYR H 52  
AB4 3 TYR C 33  ? GLN C 39  ? TYR H 33  GLN H 39  
AB4 4 ALA C 91  ? GLU C 98  ? ALA H 91  GLU H 98  
AB4 5 THR C 115 ? VAL C 117 ? THR H 115 VAL H 117 
AB5 1 SER C 128 ? LEU C 132 ? SER H 128 LEU H 132 
AB5 2 THR C 143 ? TYR C 153 ? THR H 143 TYR H 153 
AB5 3 SER C 188 ? PRO C 193 ? SER H 188 PRO H 193 
AB5 4 VAL C 171 ? THR C 173 ? VAL H 171 THR H 173 
AB6 1 SER C 128 ? LEU C 132 ? SER H 128 LEU H 132 
AB6 2 THR C 143 ? TYR C 153 ? THR H 143 TYR H 153 
AB6 3 TYR C 184 ? LEU C 186 ? TYR H 184 LEU H 186 
AB6 4 VAL C 177 ? LEU C 178 ? VAL H 177 LEU H 178 
AB7 1 VAL C 160 ? TRP C 162 ? VAL H 160 TRP H 162 
AB7 2 ILE C 203 ? HIS C 208 ? ILE H 203 HIS H 208 
AB7 3 THR C 213 ? ARG C 218 ? THR H 213 ARG H 218 
AB8 1 MET D 4   ? SER D 7   ? MET L 4   SER L 7   
AB8 2 VAL D 19  ? ALA D 25  ? VAL L 19  ALA L 25  
AB8 3 GLU D 70  ? ILE D 75  ? GLU L 70  ILE L 75  
AB8 4 PHE D 62  ? SER D 67  ? PHE L 62  SER L 67  
AB9 1 THR D 10  ? SER D 14  ? THR L 10  SER L 14  
AB9 2 THR D 102 ? LYS D 107 ? THR L 102 LYS L 107 
AB9 3 ALA D 84  ? GLN D 90  ? ALA L 84  GLN L 90  
AB9 4 LEU D 33  ? GLN D 38  ? LEU L 33  GLN L 38  
AB9 5 PRO D 44  ? TYR D 49  ? PRO L 44  TYR L 49  
AB9 6 SER D 53  ? LEU D 54  ? SER L 53  LEU L 54  
AC1 1 THR D 10  ? SER D 14  ? THR L 10  SER L 14  
AC1 2 THR D 102 ? LYS D 107 ? THR L 102 LYS L 107 
AC1 3 ALA D 84  ? GLN D 90  ? ALA L 84  GLN L 90  
AC1 4 THR D 97  ? PHE D 98  ? THR L 97  PHE L 98  
AC2 1 SER D 114 ? PHE D 118 ? SER L 114 PHE L 118 
AC2 2 SER D 131 ? PHE D 139 ? SER L 131 PHE L 139 
AC2 3 TYR D 173 ? THR D 180 ? TYR L 173 THR L 180 
AC2 4 SER D 159 ? VAL D 163 ? SER L 159 VAL L 163 
AC3 1 LYS D 145 ? VAL D 150 ? LYS L 145 VAL L 150 
AC3 2 TYR D 192 ? THR D 197 ? TYR L 192 THR L 197 
AC3 3 VAL D 205 ? PHE D 209 ? VAL L 205 PHE L 209 
# 
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 O TRP B 341 ? O TRP B 14  N TYR A 8   ? N TYR A 17  
AA1 2 3 N GLY A 7   ? N GLY A 16  O GLY B 350 ? O GLY B 23  
AA1 3 4 N TYR B 351 ? N TYR B 24  O ALA B 362 ? O ALA B 35  
AA2 1 2 O TRP B 341 ? O TRP B 14  N TYR A 8   ? N TYR A 17  
AA2 2 3 N LEU A 4   ? N LEU A 13  O PHE B 465 ? O PHE B 138 
AA2 3 4 O GLU B 466 ? O GLU B 139 N LYS B 458 ? N LYS B 131 
AA3 1 2 N VAL A 17  ? N VAL A 26  O VAL A 25  ? O VAL A 34  
AA4 1 2 N VAL A 31  ? N VAL A 40  O LEU A 314 ? O LEU A 316 
AA5 1 2 N GLU A 35  ? N GLU A 44  O PHE A 292 ? O PHE A 294 
AA5 2 3 N GLN A 293 ? N GLN A 295 O LYS A 305 ? O LYS A 307 
AA6 1 2 N ASP A 95  ? N ASP A 101 O PHE A 229 ? O PHE A 232 
AA6 2 3 O ARG A 226 ? O ARG A 229 N HIS A 181 ? N HIS A 184 
AA6 3 4 N GLY A 178 ? N GLY A 181 O ILE A 249 ? O ILE A 252 
AA7 1 2 N GLU A 113 ? N GLU A 119 O LYS A 256 ? O LYS A 259 
AA8 1 2 N TYR A 138 ? N TYR A 141 O LYS A 141 ? O LYS A 144 
AA9 1 2 N TYR A 165 ? N TYR A 168 O ILE A 240 ? O ILE A 243 
AA9 2 3 O ASN A 241 ? O ASN A 244 N GLY A 202 ? N GLY A 205 
AA9 3 4 N ILE A 199 ? N ILE A 202 O LEU A 210 ? O LEU A 213 
AB1 1 2 N GLN C 3   ? N GLN H 3   O SER C 25  ? O SER H 25  
AB1 2 3 N CYS C 22  ? N CYS H 22  O PHE C 78  ? O PHE H 78  
AB1 3 4 O LYS C 81  ? O LYS H 81  N THR C 68  ? N THR H 68  
AB2 1 2 N GLN C 3   ? N GLN H 3   O SER C 25  ? O SER H 25  
AB2 2 3 N CYS C 22  ? N CYS H 22  O PHE C 78  ? O PHE H 78  
AB2 3 4 O GLN C 77  ? O GLN H 77  N ASP C 72  ? N ASP H 72  
AB3 1 2 O ASN C 58  ? O ASN H 58  N ARG C 50  ? N ARG H 50  
AB3 2 3 O GLU C 46  ? O GLU H 46  N ARG C 38  ? N ARG H 38  
AB3 3 4 N GLN C 39  ? N GLN H 39  O VAL C 92  ? O VAL H 92  
AB3 4 5 N ARG C 97  ? N ARG H 97  O TYR C 110 ? O TYR H 110 
AB4 1 2 O ASN C 58  ? O ASN H 58  N ARG C 50  ? N ARG H 50  
AB4 2 3 O GLU C 46  ? O GLU H 46  N ARG C 38  ? N ARG H 38  
AB4 3 4 N GLN C 39  ? N GLN H 39  O VAL C 92  ? O VAL H 92  
AB4 4 5 N ALA C 91  ? N ALA H 91  O VAL C 117 ? O VAL H 117 
AB5 1 2 N SER C 128 ? N SER H 128 O LYS C 151 ? O LYS H 151 
AB5 2 3 N ALA C 144 ? N ALA H 144 O VAL C 192 ? O VAL H 192 
AB5 3 4 O VAL C 189 ? O VAL H 189 N HIS C 172 ? N HIS H 172 
AB6 1 2 N SER C 128 ? N SER H 128 O LYS C 151 ? O LYS H 151 
AB6 2 3 N TYR C 153 ? N TYR H 153 O TYR C 184 ? O TYR H 184 
AB6 3 4 O SER C 185 ? O SER H 185 N VAL C 177 ? N VAL H 177 
AB7 1 2 N SER C 161 ? N SER H 161 O ASN C 205 ? O ASN H 205 
AB7 2 3 N CYS C 204 ? N CYS H 204 O LYS C 217 ? O LYS H 217 
AB8 1 2 N THR D 5   ? N THR L 5   O ARG D 24  ? O ARG L 24  
AB8 2 3 N VAL D 19  ? N VAL L 19  O ILE D 75  ? O ILE L 75  
AB8 3 4 O THR D 72  ? O THR L 72  N SER D 65  ? N SER L 65  
AB9 1 2 N LEU D 11  ? N LEU L 11  O LYS D 103 ? O LYS L 103 
AB9 2 3 O VAL D 104 ? O VAL L 104 N ALA D 84  ? N ALA L 84  
AB9 3 4 O ILE D 85  ? O ILE L 85  N GLN D 38  ? N GLN L 38  
AB9 4 5 N TRP D 35  ? N TRP L 35  O LEU D 47  ? O LEU L 47  
AB9 5 6 N TYR D 49  ? N TYR L 49  O SER D 53  ? O SER L 53  
AC1 1 2 N LEU D 11  ? N LEU L 11  O LYS D 103 ? O LYS L 103 
AC1 2 3 O VAL D 104 ? O VAL L 104 N ALA D 84  ? N ALA L 84  
AC1 3 4 N GLN D 90  ? N GLN L 90  O THR D 97  ? O THR L 97  
AC2 1 2 N SER D 114 ? N SER L 114 O ASN D 137 ? O ASN L 137 
AC2 2 3 N LEU D 136 ? N LEU L 136 O LEU D 175 ? O LEU L 175 
AC2 3 4 O THR D 178 ? O THR L 178 N GLN D 160 ? N GLN L 160 
AC3 1 2 N LYS D 145 ? N LYS L 145 O THR D 197 ? O THR L 197 
AC3 2 3 N VAL D 196 ? N VAL L 196 O VAL D 205 ? O VAL L 205 
# 
_pdbx_entry_details.entry_id                   9C0V 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 ND2 A ASN 169 ? ? O5  S NAG 1   ? ? 1.09 
2 1 ND2 A ASN 289 ? ? C1  A NAG 601 ? ? 1.65 
3 1 CE1 A HIS 130 ? ? CE1 A TYR 161 ? ? 2.04 
4 1 OD1 A ASN 289 ? ? O7  A NAG 601 ? ? 2.11 
5 1 NE2 A HIS 130 ? ? CE1 A TYR 161 ? ? 2.19 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_1             324 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            N 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_2             324 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.385 
_pdbx_validate_rmsd_bond.bond_target_value         1.474 
_pdbx_validate_rmsd_bond.bond_deviation            -0.089 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.014 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A ASN 276 ? ? CA A ASN 276 ? ? C  A ASN 276 ? ? 81.02  110.40 -29.38 2.00 N 
2 1 N  A ASN 276 ? ? CA A ASN 276 ? ? C  A ASN 276 ? ? 150.12 111.00 39.12  2.70 N 
3 1 N  A CYS 277 ? ? CA A CYS 277 ? ? CB A CYS 277 ? ? 92.52  110.60 -18.08 1.80 N 
4 1 CA L CYS 88  ? ? CB L CYS 88  ? ? SG L CYS 88  ? ? 120.99 114.20 6.79   1.10 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 ASN A 33  ? ? 61.18   70.35   
2  1 HIS A 47  ? ? -95.97  52.43   
3  1 ASP A 53  ? ? -79.02  -169.92 
4  1 ARG A 62  ? ? 42.37   -120.61 
5  1 ASN A 92  ? ? 62.01   74.28   
6  1 ASP A 96  ? ? -117.75 -115.80 
7  1 CYS A 97  ? ? -30.63  -79.26  
8  1 GLN A 122 ? ? 49.31   24.66   
9  1 ILE A 124 ? ? -38.24  128.38  
10 1 PRO A 125 ? ? 4.75    -109.93 
11 1 LYS A 125 a ? 164.67  169.64  
12 1 SER A 128 ? ? -148.82 27.52   
13 1 LEU A 133 a ? -153.34 71.50   
14 1 ALA A 138 ? ? -108.25 -158.70 
15 1 LYS A 165 ? ? -101.83 50.09   
16 1 THR A 199 ? ? 39.38   64.65   
17 1 ARG A 220 ? ? -127.63 -157.05 
18 1 LYS A 262 ? ? -117.43 65.61   
19 1 MET A 268 ? ? -39.77  122.44  
20 1 CYS A 277 ? ? -109.38 -158.56 
21 1 ASN A 278 ? ? -165.83 104.62  
22 1 ASN A 289 ? ? -121.41 -59.38  
23 1 SER A 291 ? ? -114.04 79.23   
24 1 LYS A 310 ? ? -93.53  35.88   
25 1 GLN B 62  ? ? -38.39  115.97  
26 1 LYS B 127 ? ? 54.03   -132.39 
27 1 ASN B 135 ? ? 45.08   -126.72 
28 1 GLU H 16  ? ? -113.28 -160.69 
29 1 ALA H 41  ? ? 51.60   -127.23 
30 1 THR H 86  ? ? -102.47 -164.47 
31 1 SER H 140 ? ? 32.74   56.44   
32 1 HIS H 208 ? ? -68.56  96.41   
33 1 ALA L 9   ? ? -69.69  7.23    
34 1 SER L 30  ? ? 50.94   -127.43 
35 1 SER L 31  ? ? -113.55 57.23   
36 1 LYS L 50  ? ? 55.81   12.56   
37 1 ALA L 51  ? ? 71.84   -4.05   
38 1 SER L 52  ? ? -147.69 -5.17   
39 1 TYR L 91  ? ? -98.92  41.64   
40 1 PRO L 141 ? ? -55.51  106.28  
41 1 SER L 182 ? ? -150.48 25.79   
42 1 ASP L 185 ? ? 47.00   -117.77 
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    C1 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    S 
_pdbx_validate_chiral.auth_comp_id    NAG 
_pdbx_validate_chiral.auth_seq_id     2 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         'WRONG HAND' 
_pdbx_validate_chiral.omega           . 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 166 ? ? 0.078 'SIDE CHAIN' 
2 1 ARG H 50  ? ? 0.146 'SIDE CHAIN' 
3 1 ARG L 142 ? ? 0.152 'SIDE CHAIN' 
# 
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 ILE 326  ? A ILE 324 
2   1 Y 1 A GLN 327  ? A GLN 325 
3   1 Y 1 A SER 328  ? A SER 326 
4   1 Y 1 A ARG 329  ? A ARG 327 
5   1 Y 1 A GLY 330  ? A GLY 328 
6   1 Y 1 A LEU 331  ? A LEU 329 
7   1 Y 1 A PHE 332  ? A PHE 330 
8   1 Y 1 A GLY 333  ? A GLY 331 
9   1 Y 1 A ALA 334  ? A ALA 332 
10  1 Y 1 A ILE 335  ? A ILE 333 
11  1 Y 1 A ALA 336  ? A ALA 334 
12  1 Y 1 A GLY 337  ? A GLY 335 
13  1 Y 1 A PHE 338  ? A PHE 336 
14  1 Y 1 A ILE 339  ? A ILE 337 
15  1 Y 1 A GLU 340  ? A GLU 338 
16  1 Y 1 A GLY 341  ? A GLY 339 
17  1 Y 1 A GLY 342  ? A GLY 340 
18  1 Y 1 A TRP 343  ? A TRP 341 
19  1 Y 1 A THR 344  ? A THR 342 
20  1 Y 1 A GLY 345  ? A GLY 343 
21  1 Y 1 A MET 346  ? A MET 344 
22  1 Y 1 A VAL 347  ? A VAL 345 
23  1 Y 1 A ASP 348  ? A ASP 346 
24  1 Y 1 A GLY 349  ? A GLY 347 
25  1 Y 1 A TRP 350  ? A TRP 348 
26  1 Y 1 A TYR 351  ? A TYR 349 
27  1 Y 1 A GLY 352  ? A GLY 350 
28  1 Y 1 A TYR 353  ? A TYR 351 
29  1 Y 1 A HIS 354  ? A HIS 352 
30  1 Y 1 A HIS 355  ? A HIS 353 
31  1 Y 1 A GLN 356  ? A GLN 354 
32  1 Y 1 A ASN 357  ? A ASN 355 
33  1 Y 1 A GLU 358  ? A GLU 356 
34  1 Y 1 A GLN 359  ? A GLN 357 
35  1 Y 1 A GLY 360  ? A GLY 358 
36  1 Y 1 A SER 361  ? A SER 359 
37  1 Y 1 A GLY 362  ? A GLY 360 
38  1 Y 1 A TYR 363  ? A TYR 361 
39  1 Y 1 A ALA 364  ? A ALA 362 
40  1 Y 1 A ALA 365  ? A ALA 363 
41  1 Y 1 A ASP 366  ? A ASP 364 
42  1 Y 1 A LEU 367  ? A LEU 365 
43  1 Y 1 A LYS 368  ? A LYS 366 
44  1 Y 1 A SER 369  ? A SER 367 
45  1 Y 1 A THR 370  ? A THR 368 
46  1 Y 1 A GLN 371  ? A GLN 369 
47  1 Y 1 A ASN 372  ? A ASN 370 
48  1 Y 1 A ALA 373  ? A ALA 371 
49  1 Y 1 A ILE 374  ? A ILE 372 
50  1 Y 1 A ASP 375  ? A ASP 373 
51  1 Y 1 A GLY 376  ? A GLY 374 
52  1 Y 1 A ILE 377  ? A ILE 375 
53  1 Y 1 A THR 378  ? A THR 376 
54  1 Y 1 A ASN 379  ? A ASN 377 
55  1 Y 1 A LYS 380  ? A LYS 378 
56  1 Y 1 A VAL 381  ? A VAL 379 
57  1 Y 1 A ASN 382  ? A ASN 380 
58  1 Y 1 A SER 383  ? A SER 381 
59  1 Y 1 A VAL 384  ? A VAL 382 
60  1 Y 1 A ILE 385  ? A ILE 383 
61  1 Y 1 A GLU 386  ? A GLU 384 
62  1 Y 1 A LYS 387  ? A LYS 385 
63  1 Y 1 A MET 388  ? A MET 386 
64  1 Y 1 A ASN 389  ? A ASN 387 
65  1 Y 1 A THR 390  ? A THR 388 
66  1 Y 1 A GLN 391  ? A GLN 389 
67  1 Y 1 A PHE 392  ? A PHE 390 
68  1 Y 1 A THR 393  ? A THR 391 
69  1 Y 1 A ALA 394  ? A ALA 392 
70  1 Y 1 A VAL 395  ? A VAL 393 
71  1 Y 1 A GLY 396  ? A GLY 394 
72  1 Y 1 A LYS 397  ? A LYS 395 
73  1 Y 1 A GLU 398  ? A GLU 396 
74  1 Y 1 A PHE 399  ? A PHE 397 
75  1 Y 1 A ASN 400  ? A ASN 398 
76  1 Y 1 A HIS 401  ? A HIS 399 
77  1 Y 1 A LEU 402  ? A LEU 400 
78  1 Y 1 A GLU 403  ? A GLU 401 
79  1 Y 1 A LYS 404  ? A LYS 402 
80  1 Y 1 A ARG 405  ? A ARG 403 
81  1 Y 1 A ILE 406  ? A ILE 404 
82  1 Y 1 A GLU 407  ? A GLU 405 
83  1 Y 1 A ASN 408  ? A ASN 406 
84  1 Y 1 A LEU 409  ? A LEU 407 
85  1 Y 1 A ASN 410  ? A ASN 408 
86  1 Y 1 A LYS 411  ? A LYS 409 
87  1 Y 1 A LYS 412  ? A LYS 410 
88  1 Y 1 A VAL 413  ? A VAL 411 
89  1 Y 1 A ASP 414  ? A ASP 412 
90  1 Y 1 A ASP 415  ? A ASP 413 
91  1 Y 1 A GLY 416  ? A GLY 414 
92  1 Y 1 A PHE 417  ? A PHE 415 
93  1 Y 1 A LEU 418  ? A LEU 416 
94  1 Y 1 A ASP 419  ? A ASP 417 
95  1 Y 1 A ILE 420  ? A ILE 418 
96  1 Y 1 A TRP 421  ? A TRP 419 
97  1 Y 1 A THR 422  ? A THR 420 
98  1 Y 1 A TYR 423  ? A TYR 421 
99  1 Y 1 A ASN 424  ? A ASN 422 
100 1 Y 1 A ALA 425  ? A ALA 423 
101 1 Y 1 A GLU 426  ? A GLU 424 
102 1 Y 1 A LEU 427  ? A LEU 425 
103 1 Y 1 A LEU 428  ? A LEU 426 
104 1 Y 1 A VAL 429  ? A VAL 427 
105 1 Y 1 A LEU 430  ? A LEU 428 
106 1 Y 1 A LEU 431  ? A LEU 429 
107 1 Y 1 A GLU 432  ? A GLU 430 
108 1 Y 1 A ASN 433  ? A ASN 431 
109 1 Y 1 A GLU 434  ? A GLU 432 
110 1 Y 1 A ARG 435  ? A ARG 433 
111 1 Y 1 A THR 436  ? A THR 434 
112 1 Y 1 A LEU 437  ? A LEU 435 
113 1 Y 1 A ASP 438  ? A ASP 436 
114 1 Y 1 A TYR 439  ? A TYR 437 
115 1 Y 1 A HIS 440  ? A HIS 438 
116 1 Y 1 A ASP 441  ? A ASP 439 
117 1 Y 1 A SER 442  ? A SER 440 
118 1 Y 1 A ASN 443  ? A ASN 441 
119 1 Y 1 A VAL 444  ? A VAL 442 
120 1 Y 1 A LYS 445  ? A LYS 443 
121 1 Y 1 A ASN 446  ? A ASN 444 
122 1 Y 1 A LEU 447  ? A LEU 445 
123 1 Y 1 A TYR 448  ? A TYR 446 
124 1 Y 1 A GLU 449  ? A GLU 447 
125 1 Y 1 A LYS 450  ? A LYS 448 
126 1 Y 1 A VAL 451  ? A VAL 449 
127 1 Y 1 A ARG 452  ? A ARG 450 
128 1 Y 1 A SER 453  ? A SER 451 
129 1 Y 1 A GLN 454  ? A GLN 452 
130 1 Y 1 A LEU 455  ? A LEU 453 
131 1 Y 1 A LYS 456  ? A LYS 454 
132 1 Y 1 A ASN 457  ? A ASN 455 
133 1 Y 1 A ASN 458  ? A ASN 456 
134 1 Y 1 A ALA 459  ? A ALA 457 
135 1 Y 1 A LYS 460  ? A LYS 458 
136 1 Y 1 A GLU 461  ? A GLU 459 
137 1 Y 1 A ILE 462  ? A ILE 460 
138 1 Y 1 A GLY 463  ? A GLY 461 
139 1 Y 1 A ASN 464  ? A ASN 462 
140 1 Y 1 A GLY 465  ? A GLY 463 
141 1 Y 1 A CYS 466  ? A CYS 464 
142 1 Y 1 A PHE 467  ? A PHE 465 
143 1 Y 1 A GLU 468  ? A GLU 466 
144 1 Y 1 A PHE 469  ? A PHE 467 
145 1 Y 1 A TYR 470  ? A TYR 468 
146 1 Y 1 A HIS 471  ? A HIS 469 
147 1 Y 1 A LYS 472  ? A LYS 470 
148 1 Y 1 A CYS 473  ? A CYS 471 
149 1 Y 1 A ASP 474  ? A ASP 472 
150 1 Y 1 A ASN 475  ? A ASN 473 
151 1 Y 1 A THR 476  ? A THR 474 
152 1 Y 1 A CYS 477  ? A CYS 475 
153 1 Y 1 A MET 478  ? A MET 476 
154 1 Y 1 A GLU 479  ? A GLU 477 
155 1 Y 1 A SER 480  ? A SER 478 
156 1 Y 1 A VAL 481  ? A VAL 479 
157 1 Y 1 A LYS 482  ? A LYS 480 
158 1 Y 1 A ASN 483  ? A ASN 481 
159 1 Y 1 A GLY 484  ? A GLY 482 
160 1 Y 1 A THR 485  ? A THR 483 
161 1 Y 1 A TYR 486  ? A TYR 484 
162 1 Y 1 A ASP 487  ? A ASP 485 
163 1 Y 1 A TYR 488  ? A TYR 486 
164 1 Y 1 A PRO 489  ? A PRO 487 
165 1 Y 1 A LYS 490  ? A LYS 488 
166 1 Y 1 A TYR 491  ? A TYR 489 
167 1 Y 1 A SER 492  ? A SER 490 
168 1 Y 1 A GLU 493  ? A GLU 491 
169 1 Y 1 A GLU 494  ? A GLU 492 
170 1 Y 1 A ALA 495  ? A ALA 493 
171 1 Y 1 A LYS 496  ? A LYS 494 
172 1 Y 1 A LEU 497  ? A LEU 495 
173 1 Y 1 A ASN 498  ? A ASN 496 
174 1 Y 1 A ARG 499  ? A ARG 497 
175 1 Y 1 A GLU 500  ? A GLU 498 
176 1 Y 1 A GLU 501  ? A GLU 499 
177 1 Y 1 A ILE 502  ? A ILE 500 
178 1 Y 1 A ASP 503  ? A ASP 501 
179 1 Y 1 A SER 504  ? A SER 502 
180 1 Y 1 A GLY 505  ? A GLY 503 
181 1 Y 1 A ARG 506  ? A ARG 504 
182 1 Y 1 A LEU 507  ? A LEU 505 
183 1 Y 1 A VAL 508  ? A VAL 506 
184 1 Y 1 A PRO 509  ? A PRO 507 
185 1 Y 1 A ARG 510  ? A ARG 508 
186 1 Y 1 A GLY 511  ? A GLY 509 
187 1 Y 1 A SER 512  ? A SER 510 
188 1 Y 1 A PRO 513  ? A PRO 511 
189 1 Y 1 A GLY 514  ? A GLY 512 
190 1 Y 1 A SER 515  ? A SER 513 
191 1 Y 1 A GLY 516  ? A GLY 514 
192 1 Y 1 A TYR 517  ? A TYR 515 
193 1 Y 1 A ILE 518  ? A ILE 516 
194 1 Y 1 A PRO 519  ? A PRO 517 
195 1 Y 1 A GLU 520  ? A GLU 518 
196 1 Y 1 A ALA 521  ? A ALA 519 
197 1 Y 1 A PRO 522  ? A PRO 520 
198 1 Y 1 A ARG 523  ? A ARG 521 
199 1 Y 1 A ASP 524  ? A ASP 522 
200 1 Y 1 A GLY 525  ? A GLY 523 
201 1 Y 1 A GLN 526  ? A GLN 524 
202 1 Y 1 A ALA 527  ? A ALA 525 
203 1 Y 1 A TYR 528  ? A TYR 526 
204 1 Y 1 A VAL 529  ? A VAL 527 
205 1 Y 1 A ARG 530  ? A ARG 528 
206 1 Y 1 A LYS 531  ? A LYS 529 
207 1 Y 1 A ASP 532  ? A ASP 530 
208 1 Y 1 A GLY 533  ? A GLY 531 
209 1 Y 1 A GLU 534  ? A GLU 532 
210 1 Y 1 A TRP 535  ? A TRP 533 
211 1 Y 1 A VAL 536  ? A VAL 534 
212 1 Y 1 A LEU 537  ? A LEU 535 
213 1 Y 1 A LEU 538  ? A LEU 536 
214 1 Y 1 A SER 539  ? A SER 537 
215 1 Y 1 A THR 540  ? A THR 538 
216 1 Y 1 A PHE 541  ? A PHE 539 
217 1 Y 1 A LEU 542  ? A LEU 540 
218 1 Y 1 A GLY 543  ? A GLY 541 
219 1 Y 1 B GLY -326 ? B GLY 1   
220 1 Y 1 B ASP -325 ? B ASP 2   
221 1 Y 1 B THR -324 ? B THR 3   
222 1 Y 1 B LEU -323 ? B LEU 4   
223 1 Y 1 B CYS -322 ? B CYS 5   
224 1 Y 1 B ILE -321 ? B ILE 6   
225 1 Y 1 B GLY -320 ? B GLY 7   
226 1 Y 1 B TYR -319 ? B TYR 8   
227 1 Y 1 B HIS -318 ? B HIS 9   
228 1 Y 1 B ALA -317 ? B ALA 10  
229 1 Y 1 B ASN -316 ? B ASN 11  
230 1 Y 1 B ASN -315 ? B ASN 12  
231 1 Y 1 B SER -314 ? B SER 13  
232 1 Y 1 B THR -313 ? B THR 14  
233 1 Y 1 B ASP -312 ? B ASP 15  
234 1 Y 1 B THR -311 ? B THR 16  
235 1 Y 1 B VAL -310 ? B VAL 17  
236 1 Y 1 B ASP -309 ? B ASP 18  
237 1 Y 1 B THR -308 ? B THR 19  
238 1 Y 1 B VAL -307 ? B VAL 20  
239 1 Y 1 B LEU -306 ? B LEU 21  
240 1 Y 1 B GLU -305 ? B GLU 22  
241 1 Y 1 B LYS -304 ? B LYS 23  
242 1 Y 1 B ASN -303 ? B ASN 24  
243 1 Y 1 B VAL -302 ? B VAL 25  
244 1 Y 1 B THR -301 ? B THR 26  
245 1 Y 1 B VAL -300 ? B VAL 27  
246 1 Y 1 B THR -299 ? B THR 28  
247 1 Y 1 B HIS -298 ? B HIS 29  
248 1 Y 1 B SER -297 ? B SER 30  
249 1 Y 1 B VAL -296 ? B VAL 31  
250 1 Y 1 B ASN -295 ? B ASN 32  
251 1 Y 1 B LEU -294 ? B LEU 33  
252 1 Y 1 B LEU -293 ? B LEU 34  
253 1 Y 1 B GLU -292 ? B GLU 35  
254 1 Y 1 B ASP -291 ? B ASP 36  
255 1 Y 1 B LYS -290 ? B LYS 37  
256 1 Y 1 B HIS -289 ? B HIS 38  
257 1 Y 1 B ASN -288 ? B ASN 39  
258 1 Y 1 B GLY -287 ? B GLY 40  
259 1 Y 1 B LYS -286 ? B LYS 41  
260 1 Y 1 B LEU -285 ? B LEU 42  
261 1 Y 1 B CYS -284 ? B CYS 43  
262 1 Y 1 B ASP -283 ? B ASP 44  
263 1 Y 1 B LEU -282 ? B LEU 45  
264 1 Y 1 B ASP -281 ? B ASP 46  
265 1 Y 1 B GLY -280 ? B GLY 47  
266 1 Y 1 B VAL -279 ? B VAL 48  
267 1 Y 1 B LYS -278 ? B LYS 49  
268 1 Y 1 B PRO -277 ? B PRO 50  
269 1 Y 1 B LEU -276 ? B LEU 51  
270 1 Y 1 B ILE -275 ? B ILE 52  
271 1 Y 1 B LEU -274 ? B LEU 53  
272 1 Y 1 B ARG -273 ? B ARG 54  
273 1 Y 1 B ASP -272 ? B ASP 55  
274 1 Y 1 B CYS -271 ? B CYS 56  
275 1 Y 1 B SER -270 ? B SER 57  
276 1 Y 1 B VAL -269 ? B VAL 58  
277 1 Y 1 B ALA -268 ? B ALA 59  
278 1 Y 1 B GLY -267 ? B GLY 60  
279 1 Y 1 B TRP -266 ? B TRP 61  
280 1 Y 1 B LEU -265 ? B LEU 62  
281 1 Y 1 B LEU -264 ? B LEU 63  
282 1 Y 1 B GLY -263 ? B GLY 64  
283 1 Y 1 B ASN -262 ? B ASN 65  
284 1 Y 1 B PRO -261 ? B PRO 66  
285 1 Y 1 B MET -260 ? B MET 67  
286 1 Y 1 B CYS -259 ? B CYS 68  
287 1 Y 1 B ASP -258 ? B ASP 69  
288 1 Y 1 B GLU -257 ? B GLU 70  
289 1 Y 1 B PHE -256 ? B PHE 71  
290 1 Y 1 B ILE -255 ? B ILE 72  
291 1 Y 1 B ASN -254 ? B ASN 73  
292 1 Y 1 B VAL -253 ? B VAL 74  
293 1 Y 1 B PRO -252 ? B PRO 75  
294 1 Y 1 B GLU -251 ? B GLU 76  
295 1 Y 1 B TRP -250 ? B TRP 77  
296 1 Y 1 B SER -249 ? B SER 78  
297 1 Y 1 B TYR -248 ? B TYR 79  
298 1 Y 1 B ILE -247 ? B ILE 80  
299 1 Y 1 B VAL -246 ? B VAL 81  
300 1 Y 1 B GLU -245 ? B GLU 82  
301 1 Y 1 B LYS -244 ? B LYS 83  
302 1 Y 1 B ALA -243 ? B ALA 84  
303 1 Y 1 B ASN -242 ? B ASN 85  
304 1 Y 1 B PRO -241 ? B PRO 86  
305 1 Y 1 B VAL -240 ? B VAL 87  
306 1 Y 1 B ASN -239 ? B ASN 88  
307 1 Y 1 B ASP -238 ? B ASP 89  
308 1 Y 1 B LEU -237 ? B LEU 90  
309 1 Y 1 B CYS -236 ? B CYS 91  
310 1 Y 1 B TYR -235 ? B TYR 92  
311 1 Y 1 B PRO -234 ? B PRO 93  
312 1 Y 1 B GLY -233 ? B GLY 94  
313 1 Y 1 B ASP -232 ? B ASP 95  
314 1 Y 1 B PHE -231 ? B PHE 96  
315 1 Y 1 B ASN -230 ? B ASN 97  
316 1 Y 1 B ASP -229 ? B ASP 98  
317 1 Y 1 B TYR -228 ? B TYR 99  
318 1 Y 1 B GLU -227 ? B GLU 100 
319 1 Y 1 B GLU -226 ? B GLU 101 
320 1 Y 1 B LEU -225 ? B LEU 102 
321 1 Y 1 B LYS -224 ? B LYS 103 
322 1 Y 1 B HIS -223 ? B HIS 104 
323 1 Y 1 B LEU -222 ? B LEU 105 
324 1 Y 1 B LEU -221 ? B LEU 106 
325 1 Y 1 B SER -220 ? B SER 107 
326 1 Y 1 B ARG -219 ? B ARG 108 
327 1 Y 1 B ILE -218 ? B ILE 109 
328 1 Y 1 B ASN -217 ? B ASN 110 
329 1 Y 1 B HIS -216 ? B HIS 111 
330 1 Y 1 B PHE -215 ? B PHE 112 
331 1 Y 1 B GLU -214 ? B GLU 113 
332 1 Y 1 B LYS -213 ? B LYS 114 
333 1 Y 1 B ILE -212 ? B ILE 115 
334 1 Y 1 B GLN -211 ? B GLN 116 
335 1 Y 1 B ILE -210 ? B ILE 117 
336 1 Y 1 B ILE -209 ? B ILE 118 
337 1 Y 1 B PRO -208 ? B PRO 119 
338 1 Y 1 B LYS -207 ? B LYS 120 
339 1 Y 1 B SER -206 ? B SER 121 
340 1 Y 1 B SER -205 ? B SER 122 
341 1 Y 1 B TRP -204 ? B TRP 123 
342 1 Y 1 B SER -203 ? B SER 124 
343 1 Y 1 B SER -202 ? B SER 125 
344 1 Y 1 B HIS -201 ? B HIS 126 
345 1 Y 1 B GLU -200 ? B GLU 127 
346 1 Y 1 B ALA -199 ? B ALA 128 
347 1 Y 1 B SER -198 ? B SER 129 
348 1 Y 1 B LEU -197 ? B LEU 130 
349 1 Y 1 B GLY -196 ? B GLY 131 
350 1 Y 1 B VAL -195 ? B VAL 132 
351 1 Y 1 B SER -194 ? B SER 133 
352 1 Y 1 B SER -193 ? B SER 134 
353 1 Y 1 B ALA -192 ? B ALA 135 
354 1 Y 1 B CYS -191 ? B CYS 136 
355 1 Y 1 B PRO -190 ? B PRO 137 
356 1 Y 1 B TYR -189 ? B TYR 138 
357 1 Y 1 B GLN -188 ? B GLN 139 
358 1 Y 1 B GLY -187 ? B GLY 140 
359 1 Y 1 B LYS -186 ? B LYS 141 
360 1 Y 1 B SER -185 ? B SER 142 
361 1 Y 1 B SER -184 ? B SER 143 
362 1 Y 1 B PHE -183 ? B PHE 144 
363 1 Y 1 B PHE -182 ? B PHE 145 
364 1 Y 1 B ARG -181 ? B ARG 146 
365 1 Y 1 B ASN -180 ? B ASN 147 
366 1 Y 1 B VAL -179 ? B VAL 148 
367 1 Y 1 B VAL -178 ? B VAL 149 
368 1 Y 1 B TRP -177 ? B TRP 150 
369 1 Y 1 B LEU -176 ? B LEU 151 
370 1 Y 1 B ILE -175 ? B ILE 152 
371 1 Y 1 B LYS -174 ? B LYS 153 
372 1 Y 1 B LYS -173 ? B LYS 154 
373 1 Y 1 B ASN -172 ? B ASN 155 
374 1 Y 1 B SER -171 ? B SER 156 
375 1 Y 1 B THR -170 ? B THR 157 
376 1 Y 1 B TYR -169 ? B TYR 158 
377 1 Y 1 B PRO -168 ? B PRO 159 
378 1 Y 1 B THR -167 ? B THR 160 
379 1 Y 1 B ILE -166 ? B ILE 161 
380 1 Y 1 B LYS -165 ? B LYS 162 
381 1 Y 1 B ARG -164 ? B ARG 163 
382 1 Y 1 B SER -163 ? B SER 164 
383 1 Y 1 B TYR -162 ? B TYR 165 
384 1 Y 1 B ASN -161 ? B ASN 166 
385 1 Y 1 B ASN -160 ? B ASN 167 
386 1 Y 1 B THR -159 ? B THR 168 
387 1 Y 1 B ASN -158 ? B ASN 169 
388 1 Y 1 B GLN -157 ? B GLN 170 
389 1 Y 1 B GLU -156 ? B GLU 171 
390 1 Y 1 B ASP -155 ? B ASP 172 
391 1 Y 1 B LEU -154 ? B LEU 173 
392 1 Y 1 B LEU -153 ? B LEU 174 
393 1 Y 1 B VAL -152 ? B VAL 175 
394 1 Y 1 B LEU -151 ? B LEU 176 
395 1 Y 1 B TRP -150 ? B TRP 177 
396 1 Y 1 B GLY -149 ? B GLY 178 
397 1 Y 1 B ILE -148 ? B ILE 179 
398 1 Y 1 B HIS -147 ? B HIS 180 
399 1 Y 1 B HIS -146 ? B HIS 181 
400 1 Y 1 B PRO -145 ? B PRO 182 
401 1 Y 1 B ASN -144 ? B ASN 183 
402 1 Y 1 B ASP -143 ? B ASP 184 
403 1 Y 1 B ALA -142 ? B ALA 185 
404 1 Y 1 B ALA -141 ? B ALA 186 
405 1 Y 1 B GLU -140 ? B GLU 187 
406 1 Y 1 B GLN -139 ? B GLN 188 
407 1 Y 1 B THR -138 ? B THR 189 
408 1 Y 1 B LYS -137 ? B LYS 190 
409 1 Y 1 B LEU -136 ? B LEU 191 
410 1 Y 1 B TYR -135 ? B TYR 192 
411 1 Y 1 B GLN -134 ? B GLN 193 
412 1 Y 1 B ASN -133 ? B ASN 194 
413 1 Y 1 B PRO -132 ? B PRO 195 
414 1 Y 1 B THR -131 ? B THR 196 
415 1 Y 1 B THR -130 ? B THR 197 
416 1 Y 1 B TYR -129 ? B TYR 198 
417 1 Y 1 B ILE -128 ? B ILE 199 
418 1 Y 1 B SER -127 ? B SER 200 
419 1 Y 1 B VAL -126 ? B VAL 201 
420 1 Y 1 B GLY -125 ? B GLY 202 
421 1 Y 1 B THR -124 ? B THR 203 
422 1 Y 1 B SER -123 ? B SER 204 
423 1 Y 1 B THR -122 ? B THR 205 
424 1 Y 1 B LEU -121 ? B LEU 206 
425 1 Y 1 B ASN -120 ? B ASN 207 
426 1 Y 1 B GLN -119 ? B GLN 208 
427 1 Y 1 B ARG -118 ? B ARG 209 
428 1 Y 1 B LEU -117 ? B LEU 210 
429 1 Y 1 B VAL -116 ? B VAL 211 
430 1 Y 1 B PRO -115 ? B PRO 212 
431 1 Y 1 B ARG -114 ? B ARG 213 
432 1 Y 1 B ILE -113 ? B ILE 214 
433 1 Y 1 B ALA -112 ? B ALA 215 
434 1 Y 1 B THR -111 ? B THR 216 
435 1 Y 1 B ARG -110 ? B ARG 217 
436 1 Y 1 B SER -109 ? B SER 218 
437 1 Y 1 B LYS -108 ? B LYS 219 
438 1 Y 1 B VAL -107 ? B VAL 220 
439 1 Y 1 B ASN -106 ? B ASN 221 
440 1 Y 1 B GLY -105 ? B GLY 222 
441 1 Y 1 B GLN -104 ? B GLN 223 
442 1 Y 1 B SER -103 ? B SER 224 
443 1 Y 1 B GLY -102 ? B GLY 225 
444 1 Y 1 B ARG -101 ? B ARG 226 
445 1 Y 1 B MET -100 ? B MET 227 
446 1 Y 1 B GLU -99  ? B GLU 228 
447 1 Y 1 B PHE -98  ? B PHE 229 
448 1 Y 1 B PHE -97  ? B PHE 230 
449 1 Y 1 B TRP -96  ? B TRP 231 
450 1 Y 1 B THR -95  ? B THR 232 
451 1 Y 1 B ILE -94  ? B ILE 233 
452 1 Y 1 B LEU -93  ? B LEU 234 
453 1 Y 1 B LYS -92  ? B LYS 235 
454 1 Y 1 B PRO -91  ? B PRO 236 
455 1 Y 1 B ASN -90  ? B ASN 237 
456 1 Y 1 B ASP -89  ? B ASP 238 
457 1 Y 1 B ALA -88  ? B ALA 239 
458 1 Y 1 B ILE -87  ? B ILE 240 
459 1 Y 1 B ASN -86  ? B ASN 241 
460 1 Y 1 B PHE -85  ? B PHE 242 
461 1 Y 1 B GLU -84  ? B GLU 243 
462 1 Y 1 B SER -83  ? B SER 244 
463 1 Y 1 B ASN -82  ? B ASN 245 
464 1 Y 1 B GLY -81  ? B GLY 246 
465 1 Y 1 B ASN -80  ? B ASN 247 
466 1 Y 1 B PHE -79  ? B PHE 248 
467 1 Y 1 B ILE -78  ? B ILE 249 
468 1 Y 1 B ALA -77  ? B ALA 250 
469 1 Y 1 B PRO -76  ? B PRO 251 
470 1 Y 1 B GLU -75  ? B GLU 252 
471 1 Y 1 B TYR -74  ? B TYR 253 
472 1 Y 1 B ALA -73  ? B ALA 254 
473 1 Y 1 B TYR -72  ? B TYR 255 
474 1 Y 1 B LYS -71  ? B LYS 256 
475 1 Y 1 B ILE -70  ? B ILE 257 
476 1 Y 1 B VAL -69  ? B VAL 258 
477 1 Y 1 B LYS -68  ? B LYS 259 
478 1 Y 1 B LYS -67  ? B LYS 260 
479 1 Y 1 B GLY -66  ? B GLY 261 
480 1 Y 1 B ASP -65  ? B ASP 262 
481 1 Y 1 B SER -64  ? B SER 263 
482 1 Y 1 B THR -63  ? B THR 264 
483 1 Y 1 B ILE -62  ? B ILE 265 
484 1 Y 1 B MET -61  ? B MET 266 
485 1 Y 1 B LYS -60  ? B LYS 267 
486 1 Y 1 B SER -59  ? B SER 268 
487 1 Y 1 B GLU -58  ? B GLU 269 
488 1 Y 1 B LEU -57  ? B LEU 270 
489 1 Y 1 B GLU -56  ? B GLU 271 
490 1 Y 1 B TYR -55  ? B TYR 272 
491 1 Y 1 B GLY -54  ? B GLY 273 
492 1 Y 1 B ASN -53  ? B ASN 274 
493 1 Y 1 B CYS -52  ? B CYS 275 
494 1 Y 1 B ASN -51  ? B ASN 276 
495 1 Y 1 B THR -50  ? B THR 277 
496 1 Y 1 B THR -49  ? B THR 278 
497 1 Y 1 B CYS -48  ? B CYS 279 
498 1 Y 1 B GLN -47  ? B GLN 280 
499 1 Y 1 B THR -46  ? B THR 281 
500 1 Y 1 B PRO -45  ? B PRO 282 
501 1 Y 1 B LYS -44  ? B LYS 283 
502 1 Y 1 B GLY -43  ? B GLY 284 
503 1 Y 1 B ALA -42  ? B ALA 285 
504 1 Y 1 B ILE -41  ? B ILE 286 
505 1 Y 1 B ASN -40  ? B ASN 287 
506 1 Y 1 B THR -39  ? B THR 288 
507 1 Y 1 B SER -38  ? B SER 289 
508 1 Y 1 B LEU -37  ? B LEU 290 
509 1 Y 1 B PRO -36  ? B PRO 291 
510 1 Y 1 B PHE -35  ? B PHE 292 
511 1 Y 1 B GLN -34  ? B GLN 293 
512 1 Y 1 B ASN -33  ? B ASN 294 
513 1 Y 1 B ILE -32  ? B ILE 295 
514 1 Y 1 B HIS -31  ? B HIS 296 
515 1 Y 1 B PRO -30  ? B PRO 297 
516 1 Y 1 B ILE -29  ? B ILE 298 
517 1 Y 1 B THR -28  ? B THR 299 
518 1 Y 1 B ILE -27  ? B ILE 300 
519 1 Y 1 B GLY -26  ? B GLY 301 
520 1 Y 1 B LYS -25  ? B LYS 302 
521 1 Y 1 B CYS -24  ? B CYS 303 
522 1 Y 1 B PRO -23  ? B PRO 304 
523 1 Y 1 B LYS -22  ? B LYS 305 
524 1 Y 1 B TYR -21  ? B TYR 306 
525 1 Y 1 B VAL -20  ? B VAL 307 
526 1 Y 1 B LYS -19  ? B LYS 308 
527 1 Y 1 B SER -18  ? B SER 309 
528 1 Y 1 B THR -17  ? B THR 310 
529 1 Y 1 B LYS -16  ? B LYS 311 
530 1 Y 1 B LEU -15  ? B LEU 312 
531 1 Y 1 B ARG -14  ? B ARG 313 
532 1 Y 1 B LEU -13  ? B LEU 314 
533 1 Y 1 B ALA -12  ? B ALA 315 
534 1 Y 1 B THR -11  ? B THR 316 
535 1 Y 1 B GLY -10  ? B GLY 317 
536 1 Y 1 B LEU -9   ? B LEU 318 
537 1 Y 1 B ARG -8   ? B ARG 319 
538 1 Y 1 B ASN -7   ? B ASN 320 
539 1 Y 1 B VAL -6   ? B VAL 321 
540 1 Y 1 B PRO -5   ? B PRO 322 
541 1 Y 1 B SER -4   ? B SER 323 
542 1 Y 1 B ILE -3   ? B ILE 324 
543 1 Y 1 B GLN -2   ? B GLN 325 
544 1 Y 1 B SER -1   ? B SER 326 
545 1 Y 1 B ARG 0    ? B ARG 327 
546 1 Y 1 B GLY 1    ? B GLY 328 
547 1 Y 1 B LEU 2    ? B LEU 329 
548 1 Y 1 B PHE 3    ? B PHE 330 
549 1 Y 1 B GLY 4    ? B GLY 331 
550 1 Y 1 B ALA 5    ? B ALA 332 
551 1 Y 1 B ILE 6    ? B ILE 333 
552 1 Y 1 B ALA 7    ? B ALA 334 
553 1 Y 1 B GLY 8    ? B GLY 335 
554 1 Y 1 B PHE 9    ? B PHE 336 
555 1 Y 1 B GLY 67   ? B GLY 394 
556 1 Y 1 B LYS 68   ? B LYS 395 
557 1 Y 1 B GLU 69   ? B GLU 396 
558 1 Y 1 B PHE 70   ? B PHE 397 
559 1 Y 1 B ASN 71   ? B ASN 398 
560 1 Y 1 B HIS 72   ? B HIS 399 
561 1 Y 1 B LEU 73   ? B LEU 400 
562 1 Y 1 B GLU 74   ? B GLU 401 
563 1 Y 1 B LYS 75   ? B LYS 402 
564 1 Y 1 B GLY 176  ? B GLY 503 
565 1 Y 1 B ARG 177  ? B ARG 504 
566 1 Y 1 B LEU 178  ? B LEU 505 
567 1 Y 1 B VAL 179  ? B VAL 506 
568 1 Y 1 B PRO 180  ? B PRO 507 
569 1 Y 1 B ARG 181  ? B ARG 508 
570 1 Y 1 B GLY 182  ? B GLY 509 
571 1 Y 1 B SER 183  ? B SER 510 
572 1 Y 1 B PRO 184  ? B PRO 511 
573 1 Y 1 B GLY 185  ? B GLY 512 
574 1 Y 1 B SER 186  ? B SER 513 
575 1 Y 1 B GLY 187  ? B GLY 514 
576 1 Y 1 B TYR 188  ? B TYR 515 
577 1 Y 1 B ILE 189  ? B ILE 516 
578 1 Y 1 B PRO 190  ? B PRO 517 
579 1 Y 1 B GLU 191  ? B GLU 518 
580 1 Y 1 B ALA 192  ? B ALA 519 
581 1 Y 1 B PRO 193  ? B PRO 520 
582 1 Y 1 B ARG 194  ? B ARG 521 
583 1 Y 1 B ASP 195  ? B ASP 522 
584 1 Y 1 B GLY 196  ? B GLY 523 
585 1 Y 1 B GLN 197  ? B GLN 524 
586 1 Y 1 B ALA 198  ? B ALA 525 
587 1 Y 1 B TYR 199  ? B TYR 526 
588 1 Y 1 B VAL 200  ? B VAL 527 
589 1 Y 1 B ARG 201  ? B ARG 528 
590 1 Y 1 B LYS 202  ? B LYS 529 
591 1 Y 1 B ASP 203  ? B ASP 530 
592 1 Y 1 B GLY 204  ? B GLY 531 
593 1 Y 1 B GLU 205  ? B GLU 532 
594 1 Y 1 B TRP 206  ? B TRP 533 
595 1 Y 1 B VAL 207  ? B VAL 534 
596 1 Y 1 B LEU 208  ? B LEU 535 
597 1 Y 1 B LEU 209  ? B LEU 536 
598 1 Y 1 B SER 210  ? B SER 537 
599 1 Y 1 B THR 211  ? B THR 538 
600 1 Y 1 B PHE 212  ? B PHE 539 
601 1 Y 1 B LEU 213  ? B LEU 540 
602 1 Y 1 B GLY 214  ? B GLY 541 
603 1 Y 1 H LYS 222  ? C LYS 222 
604 1 Y 1 H SER 223  ? C SER 223 
605 1 Y 1 H CYS 224  ? C CYS 224 
606 1 Y 1 L GLU 213  ? D GLU 213 
607 1 Y 1 L CYS 214  ? D CYS 214 
# 
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  
BMA C1   C N R 74  
BMA C2   C N S 75  
BMA C3   C N S 76  
BMA C4   C N S 77  
BMA C5   C N R 78  
BMA C6   C N N 79  
BMA O1   O N N 80  
BMA O2   O N N 81  
BMA O3   O N N 82  
BMA O4   O N N 83  
BMA O5   O N N 84  
BMA O6   O N N 85  
BMA H1   H N N 86  
BMA H2   H N N 87  
BMA H3   H N N 88  
BMA H4   H N N 89  
BMA H5   H N N 90  
BMA H61  H N N 91  
BMA H62  H N N 92  
BMA HO1  H N N 93  
BMA HO2  H N N 94  
BMA HO3  H N N 95  
BMA HO4  H N N 96  
BMA HO6  H N N 97  
CYS N    N N N 98  
CYS CA   C N R 99  
CYS C    C N N 100 
CYS O    O N N 101 
CYS CB   C N N 102 
CYS SG   S N N 103 
CYS OXT  O N N 104 
CYS H    H N N 105 
CYS H2   H N N 106 
CYS HA   H N N 107 
CYS HB2  H N N 108 
CYS HB3  H N N 109 
CYS HG   H N N 110 
CYS HXT  H N N 111 
GLN N    N N N 112 
GLN CA   C N S 113 
GLN C    C N N 114 
GLN O    O N N 115 
GLN CB   C N N 116 
GLN CG   C N N 117 
GLN CD   C N N 118 
GLN OE1  O N N 119 
GLN NE2  N N N 120 
GLN OXT  O N N 121 
GLN H    H N N 122 
GLN H2   H N N 123 
GLN HA   H N N 124 
GLN HB2  H N N 125 
GLN HB3  H N N 126 
GLN HG2  H N N 127 
GLN HG3  H N N 128 
GLN HE21 H N N 129 
GLN HE22 H N N 130 
GLN HXT  H N N 131 
GLU N    N N N 132 
GLU CA   C N S 133 
GLU C    C N N 134 
GLU O    O N N 135 
GLU CB   C N N 136 
GLU CG   C N N 137 
GLU CD   C N N 138 
GLU OE1  O N N 139 
GLU OE2  O N N 140 
GLU OXT  O N N 141 
GLU H    H N N 142 
GLU H2   H N N 143 
GLU HA   H N N 144 
GLU HB2  H N N 145 
GLU HB3  H N N 146 
GLU HG2  H N N 147 
GLU HG3  H N N 148 
GLU HE2  H N N 149 
GLU HXT  H N N 150 
GLY N    N N N 151 
GLY CA   C N N 152 
GLY C    C N N 153 
GLY O    O N N 154 
GLY OXT  O N N 155 
GLY H    H N N 156 
GLY H2   H N N 157 
GLY HA2  H N N 158 
GLY HA3  H N N 159 
GLY HXT  H N N 160 
HIS N    N N N 161 
HIS CA   C N S 162 
HIS C    C N N 163 
HIS O    O N N 164 
HIS CB   C N N 165 
HIS CG   C Y N 166 
HIS ND1  N Y N 167 
HIS CD2  C Y N 168 
HIS CE1  C Y N 169 
HIS NE2  N Y N 170 
HIS OXT  O N N 171 
HIS H    H N N 172 
HIS H2   H N N 173 
HIS HA   H N N 174 
HIS HB2  H N N 175 
HIS HB3  H N N 176 
HIS HD1  H N N 177 
HIS HD2  H N N 178 
HIS HE1  H N N 179 
HIS HE2  H N N 180 
HIS HXT  H N N 181 
ILE N    N N N 182 
ILE CA   C N S 183 
ILE C    C N N 184 
ILE O    O N N 185 
ILE CB   C N S 186 
ILE CG1  C N N 187 
ILE CG2  C N N 188 
ILE CD1  C N N 189 
ILE OXT  O N N 190 
ILE H    H N N 191 
ILE H2   H N N 192 
ILE HA   H N N 193 
ILE HB   H N N 194 
ILE HG12 H N N 195 
ILE HG13 H N N 196 
ILE HG21 H N N 197 
ILE HG22 H N N 198 
ILE HG23 H N N 199 
ILE HD11 H N N 200 
ILE HD12 H N N 201 
ILE HD13 H N N 202 
ILE HXT  H N N 203 
LEU N    N N N 204 
LEU CA   C N S 205 
LEU C    C N N 206 
LEU O    O N N 207 
LEU CB   C N N 208 
LEU CG   C N N 209 
LEU CD1  C N N 210 
LEU CD2  C N N 211 
LEU OXT  O N N 212 
LEU H    H N N 213 
LEU H2   H N N 214 
LEU HA   H N N 215 
LEU HB2  H N N 216 
LEU HB3  H N N 217 
LEU HG   H N N 218 
LEU HD11 H N N 219 
LEU HD12 H N N 220 
LEU HD13 H N N 221 
LEU HD21 H N N 222 
LEU HD22 H N N 223 
LEU HD23 H N N 224 
LEU HXT  H N N 225 
LYS N    N N N 226 
LYS CA   C N S 227 
LYS C    C N N 228 
LYS O    O N N 229 
LYS CB   C N N 230 
LYS CG   C N N 231 
LYS CD   C N N 232 
LYS CE   C N N 233 
LYS NZ   N N N 234 
LYS OXT  O N N 235 
LYS H    H N N 236 
LYS H2   H N N 237 
LYS HA   H N N 238 
LYS HB2  H N N 239 
LYS HB3  H N N 240 
LYS HG2  H N N 241 
LYS HG3  H N N 242 
LYS HD2  H N N 243 
LYS HD3  H N N 244 
LYS HE2  H N N 245 
LYS HE3  H N N 246 
LYS HZ1  H N N 247 
LYS HZ2  H N N 248 
LYS HZ3  H N N 249 
LYS HXT  H N N 250 
MET N    N N N 251 
MET CA   C N S 252 
MET C    C N N 253 
MET O    O N N 254 
MET CB   C N N 255 
MET CG   C N N 256 
MET SD   S N N 257 
MET CE   C N N 258 
MET OXT  O N N 259 
MET H    H N N 260 
MET H2   H N N 261 
MET HA   H N N 262 
MET HB2  H N N 263 
MET HB3  H N N 264 
MET HG2  H N N 265 
MET HG3  H N N 266 
MET HE1  H N N 267 
MET HE2  H N N 268 
MET HE3  H N N 269 
MET HXT  H N N 270 
NAG C1   C N R 271 
NAG C2   C N R 272 
NAG C3   C N R 273 
NAG C4   C N S 274 
NAG C5   C N R 275 
NAG C6   C N N 276 
NAG C7   C N N 277 
NAG C8   C N N 278 
NAG N2   N N N 279 
NAG O1   O N N 280 
NAG O3   O N N 281 
NAG O4   O N N 282 
NAG O5   O N N 283 
NAG O6   O N N 284 
NAG O7   O N N 285 
NAG H1   H N N 286 
NAG H2   H N N 287 
NAG H3   H N N 288 
NAG H4   H N N 289 
NAG H5   H N N 290 
NAG H61  H N N 291 
NAG H62  H N N 292 
NAG H81  H N N 293 
NAG H82  H N N 294 
NAG H83  H N N 295 
NAG HN2  H N N 296 
NAG HO1  H N N 297 
NAG HO3  H N N 298 
NAG HO4  H N N 299 
NAG HO6  H N N 300 
PHE N    N N N 301 
PHE CA   C N S 302 
PHE C    C N N 303 
PHE O    O N N 304 
PHE CB   C N N 305 
PHE CG   C Y N 306 
PHE CD1  C Y N 307 
PHE CD2  C Y N 308 
PHE CE1  C Y N 309 
PHE CE2  C Y N 310 
PHE CZ   C Y N 311 
PHE OXT  O N N 312 
PHE H    H N N 313 
PHE H2   H N N 314 
PHE HA   H N N 315 
PHE HB2  H N N 316 
PHE HB3  H N N 317 
PHE HD1  H N N 318 
PHE HD2  H N N 319 
PHE HE1  H N N 320 
PHE HE2  H N N 321 
PHE HZ   H N N 322 
PHE HXT  H N N 323 
PRO N    N N N 324 
PRO CA   C N S 325 
PRO C    C N N 326 
PRO O    O N N 327 
PRO CB   C N N 328 
PRO CG   C N N 329 
PRO CD   C N N 330 
PRO OXT  O N N 331 
PRO H    H N N 332 
PRO HA   H N N 333 
PRO HB2  H N N 334 
PRO HB3  H N N 335 
PRO HG2  H N N 336 
PRO HG3  H N N 337 
PRO HD2  H N N 338 
PRO HD3  H N N 339 
PRO HXT  H N N 340 
SER N    N N N 341 
SER CA   C N S 342 
SER C    C N N 343 
SER O    O N N 344 
SER CB   C N N 345 
SER OG   O N N 346 
SER OXT  O N N 347 
SER H    H N N 348 
SER H2   H N N 349 
SER HA   H N N 350 
SER HB2  H N N 351 
SER HB3  H N N 352 
SER HG   H N N 353 
SER HXT  H N N 354 
THR N    N N N 355 
THR CA   C N S 356 
THR C    C N N 357 
THR O    O N N 358 
THR CB   C N R 359 
THR OG1  O N N 360 
THR CG2  C N N 361 
THR OXT  O N N 362 
THR H    H N N 363 
THR H2   H N N 364 
THR HA   H N N 365 
THR HB   H N N 366 
THR HG1  H N N 367 
THR HG21 H N N 368 
THR HG22 H N N 369 
THR HG23 H N N 370 
THR HXT  H N N 371 
TRP N    N N N 372 
TRP CA   C N S 373 
TRP C    C N N 374 
TRP O    O N N 375 
TRP CB   C N N 376 
TRP CG   C Y N 377 
TRP CD1  C Y N 378 
TRP CD2  C Y N 379 
TRP NE1  N Y N 380 
TRP CE2  C Y N 381 
TRP CE3  C Y N 382 
TRP CZ2  C Y N 383 
TRP CZ3  C Y N 384 
TRP CH2  C Y N 385 
TRP OXT  O N N 386 
TRP H    H N N 387 
TRP H2   H N N 388 
TRP HA   H N N 389 
TRP HB2  H N N 390 
TRP HB3  H N N 391 
TRP HD1  H N N 392 
TRP HE1  H N N 393 
TRP HE3  H N N 394 
TRP HZ2  H N N 395 
TRP HZ3  H N N 396 
TRP HH2  H N N 397 
TRP HXT  H N N 398 
TYR N    N N N 399 
TYR CA   C N S 400 
TYR C    C N N 401 
TYR O    O N N 402 
TYR CB   C N N 403 
TYR CG   C Y N 404 
TYR CD1  C Y N 405 
TYR CD2  C Y N 406 
TYR CE1  C Y N 407 
TYR CE2  C Y N 408 
TYR CZ   C Y N 409 
TYR OH   O N N 410 
TYR OXT  O N N 411 
TYR H    H N N 412 
TYR H2   H N N 413 
TYR HA   H N N 414 
TYR HB2  H N N 415 
TYR HB3  H N N 416 
TYR HD1  H N N 417 
TYR HD2  H N N 418 
TYR HE1  H N N 419 
TYR HE2  H N N 420 
TYR HH   H N N 421 
TYR HXT  H N N 422 
VAL N    N N N 423 
VAL CA   C N S 424 
VAL C    C N N 425 
VAL O    O N N 426 
VAL CB   C N N 427 
VAL CG1  C N N 428 
VAL CG2  C N N 429 
VAL OXT  O N N 430 
VAL H    H N N 431 
VAL H2   H N N 432 
VAL HA   H N N 433 
VAL HB   H N N 434 
VAL HG11 H N N 435 
VAL HG12 H N N 436 
VAL HG13 H N N 437 
VAL HG21 H N N 438 
VAL HG22 H N N 439 
VAL HG23 H N N 440 
VAL HXT  H N N 441 
# 
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  
BMA C1  C2   sing N N 70  
BMA C1  O1   sing N N 71  
BMA C1  O5   sing N N 72  
BMA C1  H1   sing N N 73  
BMA C2  C3   sing N N 74  
BMA C2  O2   sing N N 75  
BMA C2  H2   sing N N 76  
BMA C3  C4   sing N N 77  
BMA C3  O3   sing N N 78  
BMA C3  H3   sing N N 79  
BMA C4  C5   sing N N 80  
BMA C4  O4   sing N N 81  
BMA C4  H4   sing N N 82  
BMA C5  C6   sing N N 83  
BMA C5  O5   sing N N 84  
BMA C5  H5   sing N N 85  
BMA C6  O6   sing N N 86  
BMA C6  H61  sing N N 87  
BMA C6  H62  sing N N 88  
BMA O1  HO1  sing N N 89  
BMA O2  HO2  sing N N 90  
BMA O3  HO3  sing N N 91  
BMA O4  HO4  sing N N 92  
BMA O6  HO6  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
GLN N   CA   sing N N 107 
GLN N   H    sing N N 108 
GLN N   H2   sing N N 109 
GLN CA  C    sing N N 110 
GLN CA  CB   sing N N 111 
GLN CA  HA   sing N N 112 
GLN C   O    doub N N 113 
GLN C   OXT  sing N N 114 
GLN CB  CG   sing N N 115 
GLN CB  HB2  sing N N 116 
GLN CB  HB3  sing N N 117 
GLN CG  CD   sing N N 118 
GLN CG  HG2  sing N N 119 
GLN CG  HG3  sing N N 120 
GLN CD  OE1  doub N N 121 
GLN CD  NE2  sing N N 122 
GLN NE2 HE21 sing N N 123 
GLN NE2 HE22 sing N N 124 
GLN OXT HXT  sing N N 125 
GLU N   CA   sing N N 126 
GLU N   H    sing N N 127 
GLU N   H2   sing N N 128 
GLU CA  C    sing N N 129 
GLU CA  CB   sing N N 130 
GLU CA  HA   sing N N 131 
GLU C   O    doub N N 132 
GLU C   OXT  sing N N 133 
GLU CB  CG   sing N N 134 
GLU CB  HB2  sing N N 135 
GLU CB  HB3  sing N N 136 
GLU CG  CD   sing N N 137 
GLU CG  HG2  sing N N 138 
GLU CG  HG3  sing N N 139 
GLU CD  OE1  doub N N 140 
GLU CD  OE2  sing N N 141 
GLU OE2 HE2  sing N N 142 
GLU OXT HXT  sing N N 143 
GLY N   CA   sing N N 144 
GLY N   H    sing N N 145 
GLY N   H2   sing N N 146 
GLY CA  C    sing N N 147 
GLY CA  HA2  sing N N 148 
GLY CA  HA3  sing N N 149 
GLY C   O    doub N N 150 
GLY C   OXT  sing N N 151 
GLY OXT HXT  sing N N 152 
HIS N   CA   sing N N 153 
HIS N   H    sing N N 154 
HIS N   H2   sing N N 155 
HIS CA  C    sing N N 156 
HIS CA  CB   sing N N 157 
HIS CA  HA   sing N N 158 
HIS C   O    doub N N 159 
HIS C   OXT  sing N N 160 
HIS CB  CG   sing N N 161 
HIS CB  HB2  sing N N 162 
HIS CB  HB3  sing N N 163 
HIS CG  ND1  sing Y N 164 
HIS CG  CD2  doub Y N 165 
HIS ND1 CE1  doub Y N 166 
HIS ND1 HD1  sing N N 167 
HIS CD2 NE2  sing Y N 168 
HIS CD2 HD2  sing N N 169 
HIS CE1 NE2  sing Y N 170 
HIS CE1 HE1  sing N N 171 
HIS NE2 HE2  sing N N 172 
HIS OXT HXT  sing N N 173 
ILE N   CA   sing N N 174 
ILE N   H    sing N N 175 
ILE N   H2   sing N N 176 
ILE CA  C    sing N N 177 
ILE CA  CB   sing N N 178 
ILE CA  HA   sing N N 179 
ILE C   O    doub N N 180 
ILE C   OXT  sing N N 181 
ILE CB  CG1  sing N N 182 
ILE CB  CG2  sing N N 183 
ILE CB  HB   sing N N 184 
ILE CG1 CD1  sing N N 185 
ILE CG1 HG12 sing N N 186 
ILE CG1 HG13 sing N N 187 
ILE CG2 HG21 sing N N 188 
ILE CG2 HG22 sing N N 189 
ILE CG2 HG23 sing N N 190 
ILE CD1 HD11 sing N N 191 
ILE CD1 HD12 sing N N 192 
ILE CD1 HD13 sing N N 193 
ILE OXT HXT  sing N N 194 
LEU N   CA   sing N N 195 
LEU N   H    sing N N 196 
LEU N   H2   sing N N 197 
LEU CA  C    sing N N 198 
LEU CA  CB   sing N N 199 
LEU CA  HA   sing N N 200 
LEU C   O    doub N N 201 
LEU C   OXT  sing N N 202 
LEU CB  CG   sing N N 203 
LEU CB  HB2  sing N N 204 
LEU CB  HB3  sing N N 205 
LEU CG  CD1  sing N N 206 
LEU CG  CD2  sing N N 207 
LEU CG  HG   sing N N 208 
LEU CD1 HD11 sing N N 209 
LEU CD1 HD12 sing N N 210 
LEU CD1 HD13 sing N N 211 
LEU CD2 HD21 sing N N 212 
LEU CD2 HD22 sing N N 213 
LEU CD2 HD23 sing N N 214 
LEU OXT HXT  sing N N 215 
LYS N   CA   sing N N 216 
LYS N   H    sing N N 217 
LYS N   H2   sing N N 218 
LYS CA  C    sing N N 219 
LYS CA  CB   sing N N 220 
LYS CA  HA   sing N N 221 
LYS C   O    doub N N 222 
LYS C   OXT  sing N N 223 
LYS CB  CG   sing N N 224 
LYS CB  HB2  sing N N 225 
LYS CB  HB3  sing N N 226 
LYS CG  CD   sing N N 227 
LYS CG  HG2  sing N N 228 
LYS CG  HG3  sing N N 229 
LYS CD  CE   sing N N 230 
LYS CD  HD2  sing N N 231 
LYS CD  HD3  sing N N 232 
LYS CE  NZ   sing N N 233 
LYS CE  HE2  sing N N 234 
LYS CE  HE3  sing N N 235 
LYS NZ  HZ1  sing N N 236 
LYS NZ  HZ2  sing N N 237 
LYS NZ  HZ3  sing N N 238 
LYS OXT HXT  sing N N 239 
MET N   CA   sing N N 240 
MET N   H    sing N N 241 
MET N   H2   sing N N 242 
MET CA  C    sing N N 243 
MET CA  CB   sing N N 244 
MET CA  HA   sing N N 245 
MET C   O    doub N N 246 
MET C   OXT  sing N N 247 
MET CB  CG   sing N N 248 
MET CB  HB2  sing N N 249 
MET CB  HB3  sing N N 250 
MET CG  SD   sing N N 251 
MET CG  HG2  sing N N 252 
MET CG  HG3  sing N N 253 
MET SD  CE   sing N N 254 
MET CE  HE1  sing N N 255 
MET CE  HE2  sing N N 256 
MET CE  HE3  sing N N 257 
MET OXT HXT  sing N N 258 
NAG C1  C2   sing N N 259 
NAG C1  O1   sing N N 260 
NAG C1  O5   sing N N 261 
NAG C1  H1   sing N N 262 
NAG C2  C3   sing N N 263 
NAG C2  N2   sing N N 264 
NAG C2  H2   sing N N 265 
NAG C3  C4   sing N N 266 
NAG C3  O3   sing N N 267 
NAG C3  H3   sing N N 268 
NAG C4  C5   sing N N 269 
NAG C4  O4   sing N N 270 
NAG C4  H4   sing N N 271 
NAG C5  C6   sing N N 272 
NAG C5  O5   sing N N 273 
NAG C5  H5   sing N N 274 
NAG C6  O6   sing N N 275 
NAG C6  H61  sing N N 276 
NAG C6  H62  sing N N 277 
NAG C7  C8   sing N N 278 
NAG C7  N2   sing N N 279 
NAG C7  O7   doub N N 280 
NAG C8  H81  sing N N 281 
NAG C8  H82  sing N N 282 
NAG C8  H83  sing N N 283 
NAG N2  HN2  sing N N 284 
NAG O1  HO1  sing N N 285 
NAG O3  HO3  sing N N 286 
NAG O4  HO4  sing N N 287 
NAG O6  HO6  sing N N 288 
PHE N   CA   sing N N 289 
PHE N   H    sing N N 290 
PHE N   H2   sing N N 291 
PHE CA  C    sing N N 292 
PHE CA  CB   sing N N 293 
PHE CA  HA   sing N N 294 
PHE C   O    doub N N 295 
PHE C   OXT  sing N N 296 
PHE CB  CG   sing N N 297 
PHE CB  HB2  sing N N 298 
PHE CB  HB3  sing N N 299 
PHE CG  CD1  doub Y N 300 
PHE CG  CD2  sing Y N 301 
PHE CD1 CE1  sing Y N 302 
PHE CD1 HD1  sing N N 303 
PHE CD2 CE2  doub Y N 304 
PHE CD2 HD2  sing N N 305 
PHE CE1 CZ   doub Y N 306 
PHE CE1 HE1  sing N N 307 
PHE CE2 CZ   sing Y N 308 
PHE CE2 HE2  sing N N 309 
PHE CZ  HZ   sing N N 310 
PHE OXT HXT  sing N N 311 
PRO N   CA   sing N N 312 
PRO N   CD   sing N N 313 
PRO N   H    sing N N 314 
PRO CA  C    sing N N 315 
PRO CA  CB   sing N N 316 
PRO CA  HA   sing N N 317 
PRO C   O    doub N N 318 
PRO C   OXT  sing N N 319 
PRO CB  CG   sing N N 320 
PRO CB  HB2  sing N N 321 
PRO CB  HB3  sing N N 322 
PRO CG  CD   sing N N 323 
PRO CG  HG2  sing N N 324 
PRO CG  HG3  sing N N 325 
PRO CD  HD2  sing N N 326 
PRO CD  HD3  sing N N 327 
PRO OXT HXT  sing N N 328 
SER N   CA   sing N N 329 
SER N   H    sing N N 330 
SER N   H2   sing N N 331 
SER CA  C    sing N N 332 
SER CA  CB   sing N N 333 
SER CA  HA   sing N N 334 
SER C   O    doub N N 335 
SER C   OXT  sing N N 336 
SER CB  OG   sing N N 337 
SER CB  HB2  sing N N 338 
SER CB  HB3  sing N N 339 
SER OG  HG   sing N N 340 
SER OXT HXT  sing N N 341 
THR N   CA   sing N N 342 
THR N   H    sing N N 343 
THR N   H2   sing N N 344 
THR CA  C    sing N N 345 
THR CA  CB   sing N N 346 
THR CA  HA   sing N N 347 
THR C   O    doub N N 348 
THR C   OXT  sing N N 349 
THR CB  OG1  sing N N 350 
THR CB  CG2  sing N N 351 
THR CB  HB   sing N N 352 
THR OG1 HG1  sing N N 353 
THR CG2 HG21 sing N N 354 
THR CG2 HG22 sing N N 355 
THR CG2 HG23 sing N N 356 
THR OXT HXT  sing N N 357 
TRP N   CA   sing N N 358 
TRP N   H    sing N N 359 
TRP N   H2   sing N N 360 
TRP CA  C    sing N N 361 
TRP CA  CB   sing N N 362 
TRP CA  HA   sing N N 363 
TRP C   O    doub N N 364 
TRP C   OXT  sing N N 365 
TRP CB  CG   sing N N 366 
TRP CB  HB2  sing N N 367 
TRP CB  HB3  sing N N 368 
TRP CG  CD1  doub Y N 369 
TRP CG  CD2  sing Y N 370 
TRP CD1 NE1  sing Y N 371 
TRP CD1 HD1  sing N N 372 
TRP CD2 CE2  doub Y N 373 
TRP CD2 CE3  sing Y N 374 
TRP NE1 CE2  sing Y N 375 
TRP NE1 HE1  sing N N 376 
TRP CE2 CZ2  sing Y N 377 
TRP CE3 CZ3  doub Y N 378 
TRP CE3 HE3  sing N N 379 
TRP CZ2 CH2  doub Y N 380 
TRP CZ2 HZ2  sing N N 381 
TRP CZ3 CH2  sing Y N 382 
TRP CZ3 HZ3  sing N N 383 
TRP CH2 HH2  sing N N 384 
TRP OXT HXT  sing N N 385 
TYR N   CA   sing N N 386 
TYR N   H    sing N N 387 
TYR N   H2   sing N N 388 
TYR CA  C    sing N N 389 
TYR CA  CB   sing N N 390 
TYR CA  HA   sing N N 391 
TYR C   O    doub N N 392 
TYR C   OXT  sing N N 393 
TYR CB  CG   sing N N 394 
TYR CB  HB2  sing N N 395 
TYR CB  HB3  sing N N 396 
TYR CG  CD1  doub Y N 397 
TYR CG  CD2  sing Y N 398 
TYR CD1 CE1  sing Y N 399 
TYR CD1 HD1  sing N N 400 
TYR CD2 CE2  doub Y N 401 
TYR CD2 HD2  sing N N 402 
TYR CE1 CZ   doub Y N 403 
TYR CE1 HE1  sing N N 404 
TYR CE2 CZ   sing Y N 405 
TYR CE2 HE2  sing N N 406 
TYR CZ  OH   sing N N 407 
TYR OH  HH   sing N N 408 
TYR OXT HXT  sing N N 409 
VAL N   CA   sing N N 410 
VAL N   H    sing N N 411 
VAL N   H2   sing N N 412 
VAL CA  C    sing N N 413 
VAL CA  CB   sing N N 414 
VAL CA  HA   sing N N 415 
VAL C   O    doub N N 416 
VAL C   OXT  sing N N 417 
VAL CB  CG1  sing N N 418 
VAL CB  CG2  sing N N 419 
VAL CB  HB   sing N N 420 
VAL CG1 HG11 sing N N 421 
VAL CG1 HG12 sing N N 422 
VAL CG1 HG13 sing N N 423 
VAL CG2 HG21 sing N N 424 
VAL CG2 HG22 sing N N 425 
VAL CG2 HG23 sing N N 426 
VAL OXT HXT  sing N N 427 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           75N93109C00051 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
4 NAG 1 n 
4 NAG 2 n 
4 BMA 3 n 
# 
_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   4M4Y 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9C0V 
_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]   0.004141 
_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]   0.004141 
_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]   0.004141 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLY A 1 1   ? -1.929  10.580 -14.325 1.00 116.78 ? 10  GLY A N   1 
ATOM   2    C CA  . GLY A 1 1   ? -2.703  11.592 -13.625 1.00 133.51 ? 10  GLY A CA  1 
ATOM   3    C C   . GLY A 1 1   ? -1.895  12.823 -13.256 1.00 144.15 ? 10  GLY A C   1 
ATOM   4    O O   . GLY A 1 1   ? -0.705  12.722 -12.960 1.00 148.53 ? 10  GLY A O   1 
ATOM   5    N N   . ASP A 1 2   ? -2.547  13.986 -13.277 1.00 143.54 ? 11  ASP A N   1 
ATOM   6    C CA  . ASP A 1 2   ? -1.870  15.236 -12.948 1.00 139.27 ? 11  ASP A CA  1 
ATOM   7    C C   . ASP A 1 2   ? -1.388  15.224 -11.504 1.00 136.39 ? 11  ASP A C   1 
ATOM   8    O O   . ASP A 1 2   ? -2.081  14.742 -10.605 1.00 143.17 ? 11  ASP A O   1 
ATOM   9    C CB  . ASP A 1 2   ? -2.805  16.425 -13.172 1.00 138.92 ? 11  ASP A CB  1 
ATOM   10   C CG  . ASP A 1 2   ? -3.113  16.657 -14.633 1.00 138.43 ? 11  ASP A CG  1 
ATOM   11   O OD1 . ASP A 1 2   ? -2.657  15.853 -15.473 1.00 137.04 ? 11  ASP A OD1 1 
ATOM   12   O OD2 . ASP A 1 2   ? -3.813  17.644 -14.943 1.00 134.79 ? 11  ASP A OD2 1 
ATOM   13   N N   . THR A 1 3   ? -0.192  15.765 -11.281 1.00 136.99 ? 12  THR A N   1 
ATOM   14   C CA  . THR A 1 3   ? 0.404   15.791 -9.954  1.00 131.49 ? 12  THR A CA  1 
ATOM   15   C C   . THR A 1 3   ? 0.870   17.196 -9.597  1.00 123.67 ? 12  THR A C   1 
ATOM   16   O O   . THR A 1 3   ? 1.170   18.021 -10.463 1.00 120.79 ? 12  THR A O   1 
ATOM   17   C CB  . THR A 1 3   ? 1.594   14.823 -9.831  1.00 135.56 ? 12  THR A CB  1 
ATOM   18   O OG1 . THR A 1 3   ? 2.709   15.328 -10.578 1.00 130.39 ? 12  THR A OG1 1 
ATOM   19   C CG2 . THR A 1 3   ? 1.224   13.433 -10.332 1.00 139.46 ? 12  THR A CG2 1 
ATOM   20   N N   . LEU A 1 4   ? 0.927   17.450 -8.292  1.00 122.30 ? 13  LEU A N   1 
ATOM   21   C CA  . LEU A 1 4   ? 1.498   18.666 -7.732  1.00 119.76 ? 13  LEU A CA  1 
ATOM   22   C C   . LEU A 1 4   ? 2.431   18.284 -6.592  1.00 121.24 ? 13  LEU A C   1 
ATOM   23   O O   . LEU A 1 4   ? 2.074   17.459 -5.745  1.00 128.96 ? 13  LEU A O   1 
ATOM   24   C CB  . LEU A 1 4   ? 0.411   19.619 -7.224  1.00 115.09 ? 13  LEU A CB  1 
ATOM   25   C CG  . LEU A 1 4   ? 0.936   20.772 -6.365  1.00 100.89 ? 13  LEU A CG  1 
ATOM   26   C CD1 . LEU A 1 4   ? 1.761   21.740 -7.202  1.00 111.40 ? 13  LEU A CD1 1 
ATOM   27   C CD2 . LEU A 1 4   ? -0.207  21.488 -5.669  1.00 105.80 ? 13  LEU A CD2 1 
ATOM   28   N N   . CYS A 1 5   ? 3.622   18.874 -6.574  1.00 113.47 ? 14  CYS A N   1 
ATOM   29   C CA  . CYS A 1 5   ? 4.623   18.574 -5.563  1.00 112.10 ? 14  CYS A CA  1 
ATOM   30   C C   . CYS A 1 5   ? 5.009   19.838 -4.809  1.00 105.07 ? 14  CYS A C   1 
ATOM   31   O O   . CYS A 1 5   ? 4.842   20.957 -5.297  1.00 106.00 ? 14  CYS A O   1 
ATOM   32   C CB  . CYS A 1 5   ? 5.872   17.935 -6.186  1.00 118.25 ? 14  CYS A CB  1 
ATOM   33   S SG  . CYS A 1 5   ? 5.574   16.323 -6.950  1.00 155.30 ? 14  CYS A SG  1 
ATOM   34   N N   . ILE A 1 6   ? 5.530   19.641 -3.602  1.00 101.63 ? 15  ILE A N   1 
ATOM   35   C CA  . ILE A 1 6   ? 5.971   20.725 -2.735  1.00 94.26  ? 15  ILE A CA  1 
ATOM   36   C C   . ILE A 1 6   ? 7.445   20.519 -2.417  1.00 93.03  ? 15  ILE A C   1 
ATOM   37   O O   . ILE A 1 6   ? 7.875   19.398 -2.123  1.00 106.37 ? 15  ILE A O   1 
ATOM   38   C CB  . ILE A 1 6   ? 5.129   20.789 -1.445  1.00 94.39  ? 15  ILE A CB  1 
ATOM   39   C CG1 . ILE A 1 6   ? 3.703   21.216 -1.782  1.00 95.27  ? 15  ILE A CG1 1 
ATOM   40   C CG2 . ILE A 1 6   ? 5.744   21.747 -0.435  1.00 92.60  ? 15  ILE A CG2 1 
ATOM   41   C CD1 . ILE A 1 6   ? 2.804   21.272 -0.592  1.00 99.84  ? 15  ILE A CD1 1 
ATOM   42   N N   . GLY A 1 7   ? 8.220   21.596 -2.489  1.00 83.59  ? 16  GLY A N   1 
ATOM   43   C CA  . GLY A 1 7   ? 9.640   21.480 -2.233  1.00 84.95  ? 16  GLY A CA  1 
ATOM   44   C C   . GLY A 1 7   ? 10.235  22.814 -1.845  1.00 77.28  ? 16  GLY A C   1 
ATOM   45   O O   . GLY A 1 7   ? 9.548   23.834 -1.773  1.00 71.37  ? 16  GLY A O   1 
ATOM   46   N N   . TYR A 1 8   ? 11.539  22.791 -1.606  1.00 77.28  ? 17  TYR A N   1 
ATOM   47   C CA  . TYR A 1 8   ? 12.256  23.959 -1.134  1.00 75.38  ? 17  TYR A CA  1 
ATOM   48   C C   . TYR A 1 8   ? 13.409  24.304 -2.069  1.00 78.76  ? 17  TYR A C   1 
ATOM   49   O O   . TYR A 1 8   ? 13.826  23.505 -2.912  1.00 85.73  ? 17  TYR A O   1 
ATOM   50   C CB  . TYR A 1 8   ? 12.748  23.749 0.308   1.00 82.32  ? 17  TYR A CB  1 
ATOM   51   C CG  . TYR A 1 8   ? 13.501  22.459 0.569   1.00 91.41  ? 17  TYR A CG  1 
ATOM   52   C CD1 . TYR A 1 8   ? 14.858  22.350 0.296   1.00 94.08  ? 17  TYR A CD1 1 
ATOM   53   C CD2 . TYR A 1 8   ? 12.854  21.357 1.115   1.00 96.36  ? 17  TYR A CD2 1 
ATOM   54   C CE1 . TYR A 1 8   ? 15.546  21.178 0.549   1.00 102.50 ? 17  TYR A CE1 1 
ATOM   55   C CE2 . TYR A 1 8   ? 13.534  20.179 1.368   1.00 107.38 ? 17  TYR A CE2 1 
ATOM   56   C CZ  . TYR A 1 8   ? 14.881  20.095 1.081   1.00 107.54 ? 17  TYR A CZ  1 
ATOM   57   O OH  . TYR A 1 8   ? 15.564  18.925 1.331   1.00 119.61 ? 17  TYR A OH  1 
ATOM   58   N N   . HIS A 1 9   ? 13.902  25.527 -1.909  1.00 78.00  ? 18  HIS A N   1 
ATOM   59   C CA  . HIS A 1 9   ? 14.948  26.075 -2.759  1.00 78.59  ? 18  HIS A CA  1 
ATOM   60   C C   . HIS A 1 9   ? 16.286  25.369 -2.545  1.00 80.57  ? 18  HIS A C   1 
ATOM   61   O O   . HIS A 1 9   ? 16.582  24.846 -1.465  1.00 83.45  ? 18  HIS A O   1 
ATOM   62   C CB  . HIS A 1 9   ? 15.084  27.575 -2.487  1.00 76.22  ? 18  HIS A CB  1 
ATOM   63   C CG  . HIS A 1 9   ? 16.122  28.260 -3.319  1.00 75.27  ? 18  HIS A CG  1 
ATOM   64   N ND1 . HIS A 1 9   ? 16.135  28.209 -4.695  1.00 76.73  ? 18  HIS A ND1 1 
ATOM   65   C CD2 . HIS A 1 9   ? 17.166  29.047 -2.963  1.00 79.20  ? 18  HIS A CD2 1 
ATOM   66   C CE1 . HIS A 1 9   ? 17.157  28.913 -5.151  1.00 79.48  ? 18  HIS A CE1 1 
ATOM   67   N NE2 . HIS A 1 9   ? 17.794  29.438 -4.120  1.00 81.98  ? 18  HIS A NE2 1 
ATOM   68   N N   . ALA A 1 10  ? 17.130  25.398 -3.582  1.00 82.59  ? 19  ALA A N   1 
ATOM   69   C CA  . ALA A 1 10  ? 18.496  24.832 -3.476  1.00 82.76  ? 19  ALA A CA  1 
ATOM   70   C C   . ALA A 1 10  ? 19.375  25.558 -4.498  1.00 79.84  ? 19  ALA A C   1 
ATOM   71   O O   . ALA A 1 10  ? 19.028  25.520 -5.690  1.00 75.30  ? 19  ALA A O   1 
ATOM   72   C CB  . ALA A 1 10  ? 18.476  23.346 -3.721  1.00 89.20  ? 19  ALA A CB  1 
ATOM   73   N N   . ASN A 1 11  ? 20.477  26.168 -4.053  1.00 71.21  ? 20  ASN A N   1 
ATOM   74   C CA  . ASN A 1 11  ? 21.314  26.968 -4.984  1.00 73.79  ? 20  ASN A CA  1 
ATOM   75   C C   . ASN A 1 11  ? 22.790  26.593 -4.843  1.00 78.05  ? 20  ASN A C   1 
ATOM   76   O O   . ASN A 1 11  ? 23.170  26.078 -3.786  1.00 81.50  ? 20  ASN A O   1 
ATOM   77   C CB  . ASN A 1 11  ? 21.130  28.469 -4.763  1.00 81.19  ? 20  ASN A CB  1 
ATOM   78   C CG  . ASN A 1 11  ? 21.376  28.895 -3.332  1.00 86.88  ? 20  ASN A CG  1 
ATOM   79   O OD1 . ASN A 1 11  ? 22.472  28.731 -2.805  1.00 149.29 ? 20  ASN A OD1 1 
ATOM   80   N ND2 . ASN A 1 11  ? 20.362  29.455 -2.697  1.00 88.61  ? 20  ASN A ND2 1 
ATOM   81   N N   . ASN A 1 12  ? 23.590  26.897 -5.864  1.00 79.60  ? 21  ASN A N   1 
ATOM   82   C CA  . ASN A 1 12  ? 25.034  26.559 -5.836  1.00 86.54  ? 21  ASN A CA  1 
ATOM   83   C C   . ASN A 1 12  ? 25.744  27.518 -4.883  1.00 85.35  ? 21  ASN A C   1 
ATOM   84   O O   . ASN A 1 12  ? 26.363  28.479 -5.370  1.00 87.35  ? 21  ASN A O   1 
ATOM   85   C CB  . ASN A 1 12  ? 25.649  26.631 -7.234  1.00 106.85 ? 21  ASN A CB  1 
ATOM   86   C CG  . ASN A 1 12  ? 27.034  26.023 -7.313  1.00 143.89 ? 21  ASN A CG  1 
ATOM   87   O OD1 . ASN A 1 12  ? 27.345  25.084 -6.583  1.00 191.49 ? 21  ASN A OD1 1 
ATOM   88   N ND2 . ASN A 1 12  ? 27.873  26.546 -8.191  1.00 175.55 ? 21  ASN A ND2 1 
ATOM   89   N N   . SER A 1 13  ? 25.657  27.255 -3.578  1.00 89.81  ? 22  SER A N   1 
ATOM   90   C CA  . SER A 1 13  ? 26.333  28.118 -2.580  1.00 86.94  ? 22  SER A CA  1 
ATOM   91   C C   . SER A 1 13  ? 27.225  27.268 -1.679  1.00 81.51  ? 22  SER A C   1 
ATOM   92   O O   . SER A 1 13  ? 26.710  26.316 -1.073  1.00 86.04  ? 22  SER A O   1 
ATOM   93   C CB  . SER A 1 13  ? 25.334  28.879 -1.764  1.00 92.41  ? 22  SER A CB  1 
ATOM   94   O OG  . SER A 1 13  ? 24.486  27.989 -1.056  1.00 94.69  ? 22  SER A OG  1 
ATOM   95   N N   . THR A 1 14  ? 28.509  27.607 -1.602  1.00 85.82  ? 23  THR A N   1 
ATOM   96   C CA  . THR A 1 14  ? 29.415  26.891 -0.715  1.00 97.31  ? 23  THR A CA  1 
ATOM   97   C C   . THR A 1 14  ? 29.432  27.457 0.699   1.00 102.35 ? 23  THR A C   1 
ATOM   98   O O   . THR A 1 14  ? 30.344  27.134 1.468   1.00 108.14 ? 23  THR A O   1 
ATOM   99   C CB  . THR A 1 14  ? 30.836  26.893 -1.283  1.00 102.67 ? 23  THR A CB  1 
ATOM   100  O OG1 . THR A 1 14  ? 31.377  28.216 -1.210  1.00 107.15 ? 23  THR A OG1 1 
ATOM   101  C CG2 . THR A 1 14  ? 30.830  26.431 -2.733  1.00 102.07 ? 23  THR A CG2 1 
ATOM   102  N N   . ASP A 1 15  ? 28.461  28.298 1.051   1.00 101.57 ? 24  ASP A N   1 
ATOM   103  C CA  . ASP A 1 15  ? 28.370  28.812 2.412   1.00 96.71  ? 24  ASP A CA  1 
ATOM   104  C C   . ASP A 1 15  ? 28.222  27.656 3.395   1.00 100.00 ? 24  ASP A C   1 
ATOM   105  O O   . ASP A 1 15  ? 27.431  26.738 3.170   1.00 100.20 ? 24  ASP A O   1 
ATOM   106  C CB  . ASP A 1 15  ? 27.180  29.767 2.533   1.00 93.91  ? 24  ASP A CB  1 
ATOM   107  C CG  . ASP A 1 15  ? 27.311  30.991 1.639   1.00 101.47 ? 24  ASP A CG  1 
ATOM   108  O OD1 . ASP A 1 15  ? 28.400  31.202 1.064   1.00 121.08 ? 24  ASP A OD1 1 
ATOM   109  O OD2 . ASP A 1 15  ? 26.318  31.740 1.506   1.00 99.33  ? 24  ASP A OD2 1 
ATOM   110  N N   . THR A 1 16  ? 28.994  27.692 4.483   1.00 97.52  ? 25  THR A N   1 
ATOM   111  C CA  . THR A 1 16  ? 28.945  26.660 5.514   1.00 89.36  ? 25  THR A CA  1 
ATOM   112  C C   . THR A 1 16  ? 28.694  27.311 6.866   1.00 82.59  ? 25  THR A C   1 
ATOM   113  O O   . THR A 1 16  ? 29.405  28.244 7.252   1.00 86.32  ? 25  THR A O   1 
ATOM   114  C CB  . THR A 1 16  ? 30.240  25.838 5.564   1.00 104.62 ? 25  THR A CB  1 
ATOM   115  O OG1 . THR A 1 16  ? 31.352  26.696 5.849   1.00 106.92 ? 25  THR A OG1 1 
ATOM   116  C CG2 . THR A 1 16  ? 30.478  25.129 4.239   1.00 110.24 ? 25  THR A CG2 1 
ATOM   117  N N   . VAL A 1 17  ? 27.688  26.813 7.581   1.00 78.28  ? 26  VAL A N   1 
ATOM   118  C CA  . VAL A 1 17  ? 27.270  27.363 8.862   1.00 75.94  ? 26  VAL A CA  1 
ATOM   119  C C   . VAL A 1 17  ? 27.129  26.202 9.840   1.00 76.36  ? 26  VAL A C   1 
ATOM   120  O O   . VAL A 1 17  ? 26.778  25.084 9.450   1.00 78.11  ? 26  VAL A O   1 
ATOM   121  C CB  . VAL A 1 17  ? 25.952  28.164 8.722   1.00 73.26  ? 26  VAL A CB  1 
ATOM   122  C CG1 . VAL A 1 17  ? 25.541  28.759 10.031  1.00 74.50  ? 26  VAL A CG1 1 
ATOM   123  C CG2 . VAL A 1 17  ? 26.103  29.261 7.676   1.00 82.55  ? 26  VAL A CG2 1 
ATOM   124  N N   . ASP A 1 18  ? 27.418  26.464 11.115  1.00 70.91  ? 27  ASP A N   1 
ATOM   125  C CA  . ASP A 1 18  ? 27.551  25.416 12.123  1.00 70.60  ? 27  ASP A CA  1 
ATOM   126  C C   . ASP A 1 18  ? 26.303  25.333 12.996  1.00 68.18  ? 27  ASP A C   1 
ATOM   127  O O   . ASP A 1 18  ? 25.998  26.270 13.740  1.00 73.03  ? 27  ASP A O   1 
ATOM   128  C CB  . ASP A 1 18  ? 28.793  25.654 12.980  1.00 67.55  ? 27  ASP A CB  1 
ATOM   129  C CG  . ASP A 1 18  ? 30.053  25.118 12.343  1.00 75.39  ? 27  ASP A CG  1 
ATOM   130  O OD1 . ASP A 1 18  ? 29.986  24.646 11.188  1.00 81.73  ? 27  ASP A OD1 1 
ATOM   131  O OD2 . ASP A 1 18  ? 31.114  25.178 12.999  1.00 80.85  ? 27  ASP A OD2 1 
ATOM   132  N N   . THR A 1 19  ? 25.595  24.211 12.914  1.00 66.54  ? 28  THR A N   1 
ATOM   133  C CA  . THR A 1 19  ? 24.478  23.944 13.803  1.00 68.78  ? 28  THR A CA  1 
ATOM   134  C C   . THR A 1 19  ? 24.982  23.320 15.100  1.00 72.48  ? 28  THR A C   1 
ATOM   135  O O   . THR A 1 19  ? 26.184  23.187 15.332  1.00 72.98  ? 28  THR A O   1 
ATOM   136  C CB  . THR A 1 19  ? 23.462  23.022 13.134  1.00 73.91  ? 28  THR A CB  1 
ATOM   137  O OG1 . THR A 1 19  ? 24.094  21.785 12.788  1.00 78.41  ? 28  THR A OG1 1 
ATOM   138  C CG2 . THR A 1 19  ? 22.909  23.664 11.880  1.00 76.55  ? 28  THR A CG2 1 
ATOM   139  N N   . VAL A 1 20  ? 24.053  22.923 15.961  1.00 74.53  ? 29  VAL A N   1 
ATOM   140  C CA  . VAL A 1 20  ? 24.434  22.169 17.151  1.00 76.91  ? 29  VAL A CA  1 
ATOM   141  C C   . VAL A 1 20  ? 24.710  20.721 16.762  1.00 75.80  ? 29  VAL A C   1 
ATOM   142  O O   . VAL A 1 20  ? 25.800  20.194 17.011  1.00 80.80  ? 29  VAL A O   1 
ATOM   143  C CB  . VAL A 1 20  ? 23.359  22.272 18.244  1.00 81.28  ? 29  VAL A CB  1 
ATOM   144  C CG1 . VAL A 1 20  ? 23.562  21.186 19.277  1.00 79.21  ? 29  VAL A CG1 1 
ATOM   145  C CG2 . VAL A 1 20  ? 23.430  23.632 18.898  1.00 76.81  ? 29  VAL A CG2 1 
ATOM   146  N N   . LEU A 1 21  ? 23.739  20.065 16.123  1.00 71.41  ? 30  LEU A N   1 
ATOM   147  C CA  . LEU A 1 21  ? 23.879  18.638 15.842  1.00 77.06  ? 30  LEU A CA  1 
ATOM   148  C C   . LEU A 1 21  ? 24.913  18.356 14.762  1.00 86.93  ? 30  LEU A C   1 
ATOM   149  O O   . LEU A 1 21  ? 25.466  17.251 14.710  1.00 86.05  ? 30  LEU A O   1 
ATOM   150  C CB  . LEU A 1 21  ? 22.536  18.048 15.431  1.00 81.35  ? 30  LEU A CB  1 
ATOM   151  C CG  . LEU A 1 21  ? 21.337  18.302 16.336  1.00 85.32  ? 30  LEU A CG  1 
ATOM   152  C CD1 . LEU A 1 21  ? 20.227  17.347 15.958  1.00 87.93  ? 30  LEU A CD1 1 
ATOM   153  C CD2 . LEU A 1 21  ? 21.715  18.140 17.794  1.00 87.40  ? 30  LEU A CD2 1 
ATOM   154  N N   . GLU A 1 22  ? 25.183  19.323 13.892  1.00 91.27  ? 31  GLU A N   1 
ATOM   155  C CA  . GLU A 1 22  ? 26.064  19.090 12.760  1.00 84.84  ? 31  GLU A CA  1 
ATOM   156  C C   . GLU A 1 22  ? 26.903  20.335 12.520  1.00 81.63  ? 31  GLU A C   1 
ATOM   157  O O   . GLU A 1 22  ? 26.434  21.464 12.684  1.00 83.85  ? 31  GLU A O   1 
ATOM   158  C CB  . GLU A 1 22  ? 25.264  18.743 11.495  1.00 88.22  ? 31  GLU A CB  1 
ATOM   159  C CG  . GLU A 1 22  ? 26.100  18.183 10.358  1.00 98.67  ? 31  GLU A CG  1 
ATOM   160  C CD  . GLU A 1 22  ? 25.271  17.863 9.132   1.00 99.31  ? 31  GLU A CD  1 
ATOM   161  O OE1 . GLU A 1 22  ? 24.040  18.067 9.178   1.00 97.77  ? 31  GLU A OE1 1 
ATOM   162  O OE2 . GLU A 1 22  ? 25.849  17.388 8.132   1.00 100.11 ? 31  GLU A OE2 1 
ATOM   163  N N   . LYS A 1 23  ? 28.174  20.134 12.172  1.00 77.10  ? 32  LYS A N   1 
ATOM   164  C CA  . LYS A 1 23  ? 29.060  21.294 11.894  1.00 83.54  ? 32  LYS A CA  1 
ATOM   165  C C   . LYS A 1 23  ? 29.369  21.336 10.396  1.00 88.86  ? 32  LYS A C   1 
ATOM   166  O O   . LYS A 1 23  ? 29.399  20.253 9.778   1.00 95.10  ? 32  LYS A O   1 
ATOM   167  C CB  . LYS A 1 23  ? 30.343  21.205 12.726  1.00 92.35  ? 32  LYS A CB  1 
ATOM   168  C CG  . LYS A 1 23  ? 30.146  21.320 14.232  1.00 98.11  ? 32  LYS A CG  1 
ATOM   169  C CD  . LYS A 1 23  ? 31.448  21.361 14.999  1.00 121.49 ? 32  LYS A CD  1 
ATOM   170  C CE  . LYS A 1 23  ? 32.332  20.163 14.726  1.00 157.26 ? 32  LYS A CE  1 
ATOM   171  N NZ  . LYS A 1 23  ? 33.606  20.238 15.479  1.00 183.51 ? 32  LYS A NZ  1 
ATOM   172  N N   . ASN A 1 24  ? 29.568  22.535 9.844   1.00 91.29  ? 33  ASN A N   1 
ATOM   173  C CA  . ASN A 1 24  ? 29.951  22.654 8.412   1.00 94.76  ? 33  ASN A CA  1 
ATOM   174  C C   . ASN A 1 24  ? 28.839  22.053 7.543   1.00 95.48  ? 33  ASN A C   1 
ATOM   175  O O   . ASN A 1 24  ? 29.051  20.965 6.969   1.00 98.65  ? 33  ASN A O   1 
ATOM   176  C CB  . ASN A 1 24  ? 31.329  22.028 8.184   1.00 114.43 ? 33  ASN A CB  1 
ATOM   177  C CG  . ASN A 1 24  ? 31.873  22.227 6.788   1.00 129.12 ? 33  ASN A CG  1 
ATOM   178  O OD1 . ASN A 1 24  ? 31.124  22.505 5.855   1.00 135.42 ? 33  ASN A OD1 1 
ATOM   179  N ND2 . ASN A 1 24  ? 33.182  22.101 6.647   1.00 144.78 ? 33  ASN A ND2 1 
ATOM   180  N N   . VAL A 1 25  ? 27.682  22.722 7.471   1.00 91.14  ? 34  VAL A N   1 
ATOM   181  C CA  . VAL A 1 25  ? 26.578  22.240 6.586   1.00 84.01  ? 34  VAL A CA  1 
ATOM   182  C C   . VAL A 1 25  ? 26.309  23.309 5.520   1.00 87.72  ? 34  VAL A C   1 
ATOM   183  O O   . VAL A 1 25  ? 26.234  24.501 5.881   1.00 95.97  ? 34  VAL A O   1 
ATOM   184  C CB  . VAL A 1 25  ? 25.308  21.876 7.383   1.00 73.50  ? 34  VAL A CB  1 
ATOM   185  C CG1 . VAL A 1 25  ? 24.821  23.018 8.261   1.00 81.23  ? 34  VAL A CG1 1 
ATOM   186  C CG2 . VAL A 1 25  ? 24.190  21.381 6.478   1.00 82.96  ? 34  VAL A CG2 1 
ATOM   187  N N   . THR A 1 26  ? 26.193  22.897 4.253   1.00 92.53  ? 35  THR A N   1 
ATOM   188  C CA  . THR A 1 26  ? 25.978  23.864 3.143   1.00 93.31  ? 35  THR A CA  1 
ATOM   189  C C   . THR A 1 26  ? 24.619  24.551 3.309   1.00 92.93  ? 35  THR A C   1 
ATOM   190  O O   . THR A 1 26  ? 23.600  23.833 3.351   1.00 94.38  ? 35  THR A O   1 
ATOM   191  C CB  . THR A 1 26  ? 26.083  23.171 1.779   1.00 105.04 ? 35  THR A CB  1 
ATOM   192  O OG1 . THR A 1 26  ? 25.050  22.189 1.703   1.00 110.65 ? 35  THR A OG1 1 
ATOM   193  C CG2 . THR A 1 26  ? 27.430  22.520 1.555   1.00 105.40 ? 35  THR A CG2 1 
ATOM   194  N N   . VAL A 1 27  ? 24.610  25.884 3.398   1.00 79.98  ? 36  VAL A N   1 
ATOM   195  C CA  . VAL A 1 27  ? 23.356  26.618 3.512   1.00 76.14  ? 36  VAL A CA  1 
ATOM   196  C C   . VAL A 1 27  ? 23.214  27.538 2.306   1.00 81.53  ? 36  VAL A C   1 
ATOM   197  O O   . VAL A 1 27  ? 24.205  28.094 1.819   1.00 86.79  ? 36  VAL A O   1 
ATOM   198  C CB  . VAL A 1 27  ? 23.303  27.416 4.835   1.00 67.04  ? 36  VAL A CB  1 
ATOM   199  C CG1 . VAL A 1 27  ? 22.095  28.344 4.880   1.00 77.89  ? 36  VAL A CG1 1 
ATOM   200  C CG2 . VAL A 1 27  ? 23.291  26.463 6.022   1.00 71.77  ? 36  VAL A CG2 1 
ATOM   201  N N   . THR A 1 28  ? 21.975  27.691 1.825   1.00 80.89  ? 37  THR A N   1 
ATOM   202  C CA  . THR A 1 28  ? 21.697  28.513 0.650   1.00 72.29  ? 37  THR A CA  1 
ATOM   203  C C   . THR A 1 28  ? 22.221  29.937 0.820   1.00 76.60  ? 37  THR A C   1 
ATOM   204  O O   . THR A 1 28  ? 23.003  30.430 -0.001  1.00 86.48  ? 37  THR A O   1 
ATOM   205  C CB  . THR A 1 28  ? 20.190  28.516 0.359   1.00 67.27  ? 37  THR A CB  1 
ATOM   206  O OG1 . THR A 1 28  ? 19.471  28.995 1.504   1.00 69.82  ? 37  THR A OG1 1 
ATOM   207  C CG2 . THR A 1 28  ? 19.708  27.112 -0.005  1.00 75.12  ? 37  THR A CG2 1 
ATOM   208  N N   . HIS A 1 29  ? 21.802  30.610 1.891   1.00 72.17  ? 38  HIS A N   1 
ATOM   209  C CA  . HIS A 1 29  ? 22.142  32.006 2.133   1.00 70.93  ? 38  HIS A CA  1 
ATOM   210  C C   . HIS A 1 29  ? 22.531  32.180 3.592   1.00 72.85  ? 38  HIS A C   1 
ATOM   211  O O   . HIS A 1 29  ? 21.797  31.748 4.486   1.00 77.23  ? 38  HIS A O   1 
ATOM   212  C CB  . HIS A 1 29  ? 20.968  32.927 1.789   1.00 70.23  ? 38  HIS A CB  1 
ATOM   213  C CG  . HIS A 1 29  ? 20.275  32.567 0.510   1.00 66.64  ? 38  HIS A CG  1 
ATOM   214  N ND1 . HIS A 1 29  ? 20.892  32.658 -0.720  1.00 80.26  ? 38  HIS A ND1 1 
ATOM   215  C CD2 . HIS A 1 29  ? 19.023  32.111 0.270   1.00 63.04  ? 38  HIS A CD2 1 
ATOM   216  C CE1 . HIS A 1 29  ? 20.050  32.274 -1.663  1.00 81.84  ? 38  HIS A CE1 1 
ATOM   217  N NE2 . HIS A 1 29  ? 18.908  31.937 -1.089  1.00 74.83  ? 38  HIS A NE2 1 
ATOM   218  N N   . SER A 1 30  ? 23.676  32.817 3.828   1.00 66.78  ? 39  SER A N   1 
ATOM   219  C CA  . SER A 1 30  ? 24.170  33.089 5.169   1.00 66.35  ? 39  SER A CA  1 
ATOM   220  C C   . SER A 1 30  ? 24.484  34.574 5.291   1.00 73.80  ? 39  SER A C   1 
ATOM   221  O O   . SER A 1 30  ? 24.471  35.321 4.309   1.00 80.60  ? 39  SER A O   1 
ATOM   222  C CB  . SER A 1 30  ? 25.416  32.249 5.492   1.00 69.62  ? 39  SER A CB  1 
ATOM   223  O OG  . SER A 1 30  ? 26.570  32.765 4.848   1.00 75.93  ? 39  SER A OG  1 
ATOM   224  N N   . VAL A 1 31  ? 24.763  34.999 6.521   1.00 66.01  ? 40  VAL A N   1 
ATOM   225  C CA  . VAL A 1 31  ? 25.144  36.378 6.805   1.00 62.68  ? 40  VAL A CA  1 
ATOM   226  C C   . VAL A 1 31  ? 26.314  36.342 7.778   1.00 65.11  ? 40  VAL A C   1 
ATOM   227  O O   . VAL A 1 31  ? 26.222  35.716 8.839   1.00 74.10  ? 40  VAL A O   1 
ATOM   228  C CB  . VAL A 1 31  ? 23.972  37.198 7.378   1.00 70.70  ? 40  VAL A CB  1 
ATOM   229  C CG1 . VAL A 1 31  ? 24.477  38.420 8.119   1.00 77.02  ? 40  VAL A CG1 1 
ATOM   230  C CG2 . VAL A 1 31  ? 23.025  37.611 6.258   1.00 100.81 ? 40  VAL A CG2 1 
ATOM   231  N N   . ASN A 1 32  ? 27.421  36.978 7.407   1.00 72.82  ? 41  ASN A N   1 
ATOM   232  C CA  . ASN A 1 32  ? 28.609  37.004 8.248   1.00 82.31  ? 41  ASN A CA  1 
ATOM   233  C C   . ASN A 1 32  ? 28.541  38.160 9.237   1.00 86.52  ? 41  ASN A C   1 
ATOM   234  O O   . ASN A 1 32  ? 27.975  39.218 8.950   1.00 96.11  ? 41  ASN A O   1 
ATOM   235  C CB  . ASN A 1 32  ? 29.878  37.124 7.401   1.00 94.36  ? 41  ASN A CB  1 
ATOM   236  C CG  . ASN A 1 32  ? 31.137  37.269 8.245   1.00 97.29  ? 41  ASN A CG  1 
ATOM   237  O OD1 . ASN A 1 32  ? 31.318  36.566 9.241   1.00 94.05  ? 41  ASN A OD1 1 
ATOM   238  N ND2 . ASN A 1 32  ? 32.007  38.193 7.854   1.00 103.58 ? 41  ASN A ND2 1 
ATOM   239  N N   . LEU A 1 33  ? 29.135  37.948 10.412  1.00 79.94  ? 42  LEU A N   1 
ATOM   240  C CA  . LEU A 1 33  ? 29.172  38.960 11.457  1.00 80.02  ? 42  LEU A CA  1 
ATOM   241  C C   . LEU A 1 33  ? 30.578  39.383 11.856  1.00 88.19  ? 42  LEU A C   1 
ATOM   242  O O   . LEU A 1 33  ? 30.722  40.368 12.589  1.00 89.81  ? 42  LEU A O   1 
ATOM   243  C CB  . LEU A 1 33  ? 28.428  38.465 12.708  1.00 80.25  ? 42  LEU A CB  1 
ATOM   244  C CG  . LEU A 1 33  ? 26.961  38.087 12.507  1.00 63.83  ? 42  LEU A CG  1 
ATOM   245  C CD1 . LEU A 1 33  ? 26.331  37.702 13.834  1.00 65.17  ? 42  LEU A CD1 1 
ATOM   246  C CD2 . LEU A 1 33  ? 26.188  39.226 11.852  1.00 86.98  ? 42  LEU A CD2 1 
ATOM   247  N N   . LEU A 1 34  ? 31.599  38.683 11.352  1.00 84.48  ? 43  LEU A N   1 
ATOM   248  C CA  . LEU A 1 34  ? 33.000  38.980 11.756  1.00 85.46  ? 43  LEU A CA  1 
ATOM   249  C C   . LEU A 1 34  ? 33.707  39.772 10.657  1.00 93.63  ? 43  LEU A C   1 
ATOM   250  O O   . LEU A 1 34  ? 33.432  39.508 9.477   1.00 96.18  ? 43  LEU A O   1 
ATOM   251  C CB  . LEU A 1 34  ? 33.734  37.662 12.012  1.00 80.61  ? 43  LEU A CB  1 
ATOM   252  C CG  . LEU A 1 34  ? 34.082  37.377 13.469  1.00 80.53  ? 43  LEU A CG  1 
ATOM   253  C CD1 . LEU A 1 34  ? 35.006  36.177 13.570  1.00 91.72  ? 43  LEU A CD1 1 
ATOM   254  C CD2 . LEU A 1 34  ? 34.724  38.593 14.115  1.00 102.37 ? 43  LEU A CD2 1 
ATOM   255  N N   . GLU A 1 35  ? 34.605  40.685 11.041  1.00 96.20  ? 44  GLU A N   1 
ATOM   256  C CA  . GLU A 1 35  ? 35.356  41.499 10.050  1.00 105.10 ? 44  GLU A CA  1 
ATOM   257  C C   . GLU A 1 35  ? 36.845  41.497 10.390  1.00 106.26 ? 44  GLU A C   1 
ATOM   258  O O   . GLU A 1 35  ? 37.235  42.215 11.321  1.00 102.56 ? 44  GLU A O   1 
ATOM   259  C CB  . GLU A 1 35  ? 34.865  42.942 10.032  1.00 103.90 ? 44  GLU A CB  1 
ATOM   260  C CG  . GLU A 1 35  ? 35.545  43.779 8.973   1.00 116.86 ? 44  GLU A CG  1 
ATOM   261  C CD  . GLU A 1 35  ? 34.881  45.124 8.757   1.00 140.99 ? 44  GLU A CD  1 
ATOM   262  O OE1 . GLU A 1 35  ? 33.911  45.426 9.477   1.00 133.52 ? 44  GLU A OE1 1 
ATOM   263  O OE2 . GLU A 1 35  ? 35.321  45.851 7.853   1.00 186.56 ? 44  GLU A OE2 1 
ATOM   264  N N   . ASP A 1 36  ? 37.631  40.717 9.655   1.00 114.01 ? 45  ASP A N   1 
ATOM   265  C CA  . ASP A 1 36  ? 39.095  40.683 9.866   1.00 117.68 ? 45  ASP A CA  1 
ATOM   266  C C   . ASP A 1 36  ? 39.747  41.360 8.672   1.00 123.44 ? 45  ASP A C   1 
ATOM   267  O O   . ASP A 1 36  ? 40.849  41.906 8.827   1.00 131.82 ? 45  ASP A O   1 
ATOM   268  C CB  . ASP A 1 36  ? 39.595  39.246 9.912   1.00 128.06 ? 45  ASP A CB  1 
ATOM   269  C CG  . ASP A 1 36  ? 39.320  38.495 8.621   1.00 141.39 ? 45  ASP A CG  1 
ATOM   270  O OD1 . ASP A 1 36  ? 38.139  38.413 8.233   1.00 157.90 ? 45  ASP A OD1 1 
ATOM   271  O OD2 . ASP A 1 36  ? 40.290  38.021 8.002   1.00 136.80 ? 45  ASP A OD2 1 
ATOM   272  N N   . LYS A 1 37  ? 39.065  41.336 7.529   1.00 139.82 ? 46  LYS A N   1 
ATOM   273  C CA  . LYS A 1 37  ? 39.652  41.886 6.282   1.00 146.84 ? 46  LYS A CA  1 
ATOM   274  C C   . LYS A 1 37  ? 40.181  43.310 6.400   1.00 157.73 ? 46  LYS A C   1 
ATOM   275  O O   . LYS A 1 37  ? 41.124  43.645 5.668   1.00 172.22 ? 46  LYS A O   1 
ATOM   276  C CB  . LYS A 1 37  ? 38.843  41.410 5.071   1.00 145.09 ? 46  LYS A CB  1 
ATOM   277  C CG  . LYS A 1 37  ? 38.910  39.916 4.775   1.00 154.07 ? 46  LYS A CG  1 
ATOM   278  C CD  . LYS A 1 37  ? 38.079  39.477 3.586   1.00 159.29 ? 46  LYS A CD  1 
ATOM   279  C CE  . LYS A 1 37  ? 38.182  37.995 3.300   1.00 161.54 ? 46  LYS A CE  1 
ATOM   280  N NZ  . LYS A 1 37  ? 37.339  37.600 2.147   1.00 165.41 ? 46  LYS A NZ  1 
ATOM   281  N N   . HIS A 1 38  ? 39.633  44.116 7.310   1.00 135.27 ? 47  HIS A N   1 
ATOM   282  C CA  . HIS A 1 38  ? 40.077  45.536 7.371   1.00 141.87 ? 47  HIS A CA  1 
ATOM   283  C C   . HIS A 1 38  ? 41.162  45.705 8.440   1.00 131.22 ? 47  HIS A C   1 
ATOM   284  O O   . HIS A 1 38  ? 41.039  46.613 9.291   1.00 126.65 ? 47  HIS A O   1 
ATOM   285  C CB  . HIS A 1 38  ? 38.881  46.474 7.560   1.00 152.42 ? 47  HIS A CB  1 
ATOM   286  C CG  . HIS A 1 38  ? 38.491  47.115 6.276   1.00 189.75 ? 47  HIS A CG  1 
ATOM   287  N ND1 . HIS A 1 38  ? 39.377  47.876 5.546   1.00 200.22 ? 47  HIS A ND1 1 
ATOM   288  C CD2 . HIS A 1 38  ? 37.356  47.091 5.577   1.00 199.58 ? 47  HIS A CD2 1 
ATOM   289  C CE1 . HIS A 1 38  ? 38.778  48.304 4.446   1.00 169.22 ? 47  HIS A CE1 1 
ATOM   290  N NE2 . HIS A 1 38  ? 37.548  47.838 4.445   1.00 178.57 ? 47  HIS A NE2 1 
ATOM   291  N N   . ASN A 1 39  ? 42.214  44.884 8.372   1.00 117.13 ? 48  ASN A N   1 
ATOM   292  C CA  . ASN A 1 39  ? 43.342  45.013 9.333   1.00 115.57 ? 48  ASN A CA  1 
ATOM   293  C C   . ASN A 1 39  ? 43.864  46.451 9.273   1.00 132.03 ? 48  ASN A C   1 
ATOM   294  O O   . ASN A 1 39  ? 44.263  46.971 10.331  1.00 142.50 ? 48  ASN A O   1 
ATOM   295  C CB  . ASN A 1 39  ? 44.453  43.999 9.050   1.00 122.32 ? 48  ASN A CB  1 
ATOM   296  C CG  . ASN A 1 39  ? 45.486  43.941 10.154  1.00 133.56 ? 48  ASN A CG  1 
ATOM   297  O OD1 . ASN A 1 39  ? 45.164  43.608 11.292  1.00 135.17 ? 48  ASN A OD1 1 
ATOM   298  N ND2 . ASN A 1 39  ? 46.727  44.262 9.830   1.00 130.52 ? 48  ASN A ND2 1 
ATOM   299  N N   . GLY A 1 40  ? 43.855  47.063 8.084   1.00 124.77 ? 49  GLY A N   1 
ATOM   300  C CA  . GLY A 1 40  ? 44.277  48.470 7.937   1.00 130.97 ? 49  GLY A CA  1 
ATOM   301  C C   . GLY A 1 40  ? 45.751  48.610 7.602   1.00 124.54 ? 49  GLY A C   1 
ATOM   302  O O   . GLY A 1 40  ? 46.043  48.984 6.449   1.00 137.58 ? 49  GLY A O   1 
ATOM   303  N N   . LYS A 1 41  ? 46.643  48.322 8.557   1.00 166.18 ? 50  LYS A N   1 
ATOM   304  C CA  . LYS A 1 41  ? 48.109  48.499 8.350   1.00 152.65 ? 50  LYS A CA  1 
ATOM   305  C C   . LYS A 1 41  ? 48.424  49.995 8.217   1.00 146.35 ? 50  LYS A C   1 
ATOM   306  O O   . LYS A 1 41  ? 49.508  50.320 7.695   1.00 161.63 ? 50  LYS A O   1 
ATOM   307  C CB  . LYS A 1 41  ? 48.608  47.689 7.147   1.00 140.06 ? 50  LYS A CB  1 
ATOM   308  C CG  . LYS A 1 41  ? 48.646  46.182 7.358   1.00 144.45 ? 50  LYS A CG  1 
ATOM   309  C CD  . LYS A 1 41  ? 49.470  45.776 8.561   1.00 145.94 ? 50  LYS A CD  1 
ATOM   310  C CE  . LYS A 1 41  ? 50.911  46.232 8.478   1.00 141.61 ? 50  LYS A CE  1 
ATOM   311  N NZ  . LYS A 1 41  ? 51.661  45.909 9.714   1.00 150.42 ? 50  LYS A NZ  1 
ATOM   312  N N   . LEU A 1 42  ? 47.515  50.862 8.678   1.00 134.24 ? 51  LEU A N   1 
ATOM   313  C CA  . LEU A 1 42  ? 47.744  52.333 8.639   1.00 134.83 ? 51  LEU A CA  1 
ATOM   314  C C   . LEU A 1 42  ? 46.894  52.997 9.728   1.00 137.79 ? 51  LEU A C   1 
ATOM   315  O O   . LEU A 1 42  ? 45.761  52.532 9.959   1.00 154.55 ? 51  LEU A O   1 
ATOM   316  C CB  . LEU A 1 42  ? 47.392  52.876 7.249   1.00 144.12 ? 51  LEU A CB  1 
ATOM   317  C CG  . LEU A 1 42  ? 48.265  52.389 6.093   1.00 143.94 ? 51  LEU A CG  1 
ATOM   318  C CD1 . LEU A 1 42  ? 47.737  52.872 4.751   1.00 141.89 ? 51  LEU A CD1 1 
ATOM   319  C CD2 . LEU A 1 42  ? 49.710  52.821 6.285   1.00 137.40 ? 51  LEU A CD2 1 
ATOM   320  N N   . CYS A 1 43  ? 47.424  54.040 10.373  1.00 119.80 ? 52  CYS A N   1 
ATOM   321  C CA  . CYS A 1 43  ? 46.685  54.703 11.477  1.00 155.96 ? 52  CYS A CA  1 
ATOM   322  C C   . CYS A 1 43  ? 46.161  56.047 10.970  1.00 148.46 ? 52  CYS A C   1 
ATOM   323  O O   . CYS A 1 43  ? 46.881  57.044 11.112  1.00 239.98 ? 52  CYS A O   1 
ATOM   324  C CB  . CYS A 1 43  ? 47.587  54.900 12.687  1.00 148.45 ? 52  CYS A CB  1 
ATOM   325  S SG  . CYS A 1 43  ? 49.224  55.547 12.264  1.00 146.74 ? 52  CYS A SG  1 
ATOM   326  N N   . ASP A 1 44  ? 44.945  56.045 10.419  1.00 141.72 ? 53  ASP A N   1 
ATOM   327  C CA  . ASP A 1 44  ? 44.325  57.275 9.866   1.00 148.07 ? 53  ASP A CA  1 
ATOM   328  C C   . ASP A 1 44  ? 43.758  58.130 11.001  1.00 161.65 ? 53  ASP A C   1 
ATOM   329  O O   . ASP A 1 44  ? 44.056  57.834 12.175  1.00 161.12 ? 53  ASP A O   1 
ATOM   330  C CB  . ASP A 1 44  ? 43.213  56.885 8.894   1.00 151.26 ? 53  ASP A CB  1 
ATOM   331  C CG  . ASP A 1 44  ? 43.640  55.827 7.893   1.00 161.75 ? 53  ASP A CG  1 
ATOM   332  O OD1 . ASP A 1 44  ? 44.838  55.483 7.883   1.00 183.49 ? 53  ASP A OD1 1 
ATOM   333  O OD2 . ASP A 1 44  ? 42.768  55.343 7.146   1.00 179.09 ? 53  ASP A OD2 1 
ATOM   334  N N   . LEU A 1 45  ? 42.992  59.158 10.637  1.00 164.46 ? 54  LEU A N   1 
ATOM   335  C CA  . LEU A 1 45  ? 42.370  60.044 11.650  1.00 165.02 ? 54  LEU A CA  1 
ATOM   336  C C   . LEU A 1 45  ? 41.100  59.365 12.150  1.00 159.76 ? 54  LEU A C   1 
ATOM   337  O O   . LEU A 1 45  ? 40.484  58.619 11.371  1.00 159.80 ? 54  LEU A O   1 
ATOM   338  C CB  . LEU A 1 45  ? 42.023  61.380 10.990  1.00 164.45 ? 54  LEU A CB  1 
ATOM   339  C CG  . LEU A 1 45  ? 43.143  62.036 10.188  1.00 164.89 ? 54  LEU A CG  1 
ATOM   340  C CD1 . LEU A 1 45  ? 42.774  63.464 9.818   1.00 159.46 ? 54  LEU A CD1 1 
ATOM   341  C CD2 . LEU A 1 45  ? 44.441  62.014 10.971  1.00 177.78 ? 54  LEU A CD2 1 
ATOM   342  N N   . ASP A 1 46  ? 40.723  59.620 13.399  1.00 171.68 ? 55  ASP A N   1 
ATOM   343  C CA  . ASP A 1 46  ? 39.448  59.060 13.907  1.00 175.65 ? 55  ASP A CA  1 
ATOM   344  C C   . ASP A 1 46  ? 38.524  60.231 14.228  1.00 176.71 ? 55  ASP A C   1 
ATOM   345  O O   . ASP A 1 46  ? 38.487  60.631 15.412  1.00 183.00 ? 55  ASP A O   1 
ATOM   346  C CB  . ASP A 1 46  ? 39.669  58.140 15.108  1.00 168.77 ? 55  ASP A CB  1 
ATOM   347  C CG  . ASP A 1 46  ? 38.623  57.043 15.217  1.00 167.61 ? 55  ASP A CG  1 
ATOM   348  O OD1 . ASP A 1 46  ? 37.433  57.379 15.367  1.00 158.35 ? 55  ASP A OD1 1 
ATOM   349  O OD2 . ASP A 1 46  ? 39.008  55.862 15.140  1.00 183.45 ? 55  ASP A OD2 1 
ATOM   350  N N   . GLY A 1 47  a 37.842  60.763 13.207  1.00 167.07 ? 55  GLY A N   1 
ATOM   351  C CA  . GLY A 1 47  a 36.931  61.908 13.401  1.00 175.46 ? 55  GLY A CA  1 
ATOM   352  C C   . GLY A 1 47  a 37.723  63.199 13.512  1.00 170.42 ? 55  GLY A C   1 
ATOM   353  O O   . GLY A 1 47  a 37.110  64.276 13.371  1.00 159.55 ? 55  GLY A O   1 
ATOM   354  N N   . VAL A 1 48  ? 39.038  63.092 13.736  1.00 160.46 ? 56  VAL A N   1 
ATOM   355  C CA  . VAL A 1 48  ? 39.924  64.287 13.862  1.00 188.55 ? 56  VAL A CA  1 
ATOM   356  C C   . VAL A 1 48  ? 41.371  63.788 13.938  1.00 168.33 ? 56  VAL A C   1 
ATOM   357  O O   . VAL A 1 48  ? 41.559  62.563 14.089  1.00 195.65 ? 56  VAL A O   1 
ATOM   358  C CB  . VAL A 1 48  ? 39.549  65.142 15.088  1.00 198.33 ? 56  VAL A CB  1 
ATOM   359  C CG1 . VAL A 1 48  ? 40.116  64.577 16.382  1.00 188.00 ? 56  VAL A CG1 1 
ATOM   360  C CG2 . VAL A 1 48  ? 39.935  66.601 14.908  1.00 186.46 ? 56  VAL A CG2 1 
ATOM   361  N N   . LYS A 1 49  ? 42.353  64.690 13.839  1.00 194.02 ? 57  LYS A N   1 
ATOM   362  C CA  . LYS A 1 49  ? 43.780  64.263 13.831  1.00 183.69 ? 57  LYS A CA  1 
ATOM   363  C C   . LYS A 1 49  ? 44.152  63.538 15.124  1.00 172.75 ? 57  LYS A C   1 
ATOM   364  O O   . LYS A 1 49  ? 43.492  63.784 16.150  1.00 167.62 ? 57  LYS A O   1 
ATOM   365  C CB  . LYS A 1 49  ? 44.671  65.501 13.692  1.00 188.49 ? 57  LYS A CB  1 
ATOM   366  C CG  . LYS A 1 49  ? 46.083  65.266 13.170  1.00 178.07 ? 57  LYS A CG  1 
ATOM   367  C CD  . LYS A 1 49  ? 46.140  65.008 11.678  1.00 171.84 ? 57  LYS A CD  1 
ATOM   368  C CE  . LYS A 1 49  ? 47.525  64.654 11.181  1.00 162.91 ? 57  LYS A CE  1 
ATOM   369  N NZ  . LYS A 1 49  ? 47.999  63.363 11.734  1.00 174.80 ? 57  LYS A NZ  1 
ATOM   370  N N   . PRO A 1 50  ? 45.161  62.638 15.120  1.00 164.83 ? 58  PRO A N   1 
ATOM   371  C CA  . PRO A 1 50  ? 45.637  62.007 16.342  1.00 157.89 ? 58  PRO A CA  1 
ATOM   372  C C   . PRO A 1 50  ? 46.891  62.702 16.861  1.00 150.79 ? 58  PRO A C   1 
ATOM   373  O O   . PRO A 1 50  ? 47.256  63.724 16.316  1.00 144.92 ? 58  PRO A O   1 
ATOM   374  C CB  . PRO A 1 50  ? 46.167  60.675 15.822  1.00 153.25 ? 58  PRO A CB  1 
ATOM   375  C CG  . PRO A 1 50  ? 46.764  61.029 14.485  1.00 165.33 ? 58  PRO A CG  1 
ATOM   376  C CD  . PRO A 1 50  ? 45.844  62.102 13.940  1.00 168.41 ? 58  PRO A CD  1 
ATOM   377  N N   . LEU A 1 51  ? 47.508  62.143 17.897  1.00 142.77 ? 59  LEU A N   1 
ATOM   378  C CA  . LEU A 1 51  ? 48.805  62.691 18.360  1.00 140.45 ? 59  LEU A CA  1 
ATOM   379  C C   . LEU A 1 51  ? 49.873  61.760 17.801  1.00 135.84 ? 59  LEU A C   1 
ATOM   380  O O   . LEU A 1 51  ? 49.640  60.543 17.832  1.00 136.87 ? 59  LEU A O   1 
ATOM   381  C CB  . LEU A 1 51  ? 48.840  62.679 19.887  1.00 141.85 ? 59  LEU A CB  1 
ATOM   382  C CG  . LEU A 1 51  ? 50.177  63.070 20.512  1.00 157.15 ? 59  LEU A CG  1 
ATOM   383  C CD1 . LEU A 1 51  ? 50.439  64.557 20.335  1.00 167.34 ? 59  LEU A CD1 1 
ATOM   384  C CD2 . LEU A 1 51  ? 50.211  62.696 21.984  1.00 172.13 ? 59  LEU A CD2 1 
ATOM   385  N N   . ILE A 1 52  ? 50.974  62.290 17.272  1.00 165.27 ? 60  ILE A N   1 
ATOM   386  C CA  . ILE A 1 52  ? 52.006  61.306 16.825  1.00 147.63 ? 60  ILE A CA  1 
ATOM   387  C C   . ILE A 1 52  ? 53.107  61.535 17.867  1.00 138.47 ? 60  ILE A C   1 
ATOM   388  O O   . ILE A 1 52  ? 53.325  62.702 18.246  1.00 149.09 ? 60  ILE A O   1 
ATOM   389  C CB  . ILE A 1 52  ? 52.468  61.701 15.408  1.00 149.19 ? 60  ILE A CB  1 
ATOM   390  C CG1 . ILE A 1 52  ? 51.339  61.554 14.385  1.00 159.26 ? 60  ILE A CG1 1 
ATOM   391  C CG2 . ILE A 1 52  ? 53.704  60.914 15.001  1.00 134.05 ? 60  ILE A CG2 1 
ATOM   392  C CD1 . ILE A 1 52  ? 51.717  61.992 12.989  1.00 169.73 ? 60  ILE A CD1 1 
ATOM   393  N N   . LEU A 1 53  ? 53.770  60.460 18.306  1.00 132.71 ? 61  LEU A N   1 
ATOM   394  C CA  . LEU A 1 53  ? 54.843  60.580 19.327  1.00 129.03 ? 61  LEU A CA  1 
ATOM   395  C C   . LEU A 1 53  ? 56.171  60.083 18.748  1.00 119.59 ? 61  LEU A C   1 
ATOM   396  O O   . LEU A 1 53  ? 57.177  60.115 19.483  1.00 117.09 ? 61  LEU A O   1 
ATOM   397  C CB  . LEU A 1 53  ? 54.436  59.748 20.547  1.00 130.91 ? 61  LEU A CB  1 
ATOM   398  C CG  . LEU A 1 53  ? 53.455  60.419 21.506  1.00 135.70 ? 61  LEU A CG  1 
ATOM   399  C CD1 . LEU A 1 53  ? 53.429  59.697 22.844  1.00 133.72 ? 61  LEU A CD1 1 
ATOM   400  C CD2 . LEU A 1 53  ? 53.807  61.886 21.700  1.00 134.45 ? 61  LEU A CD2 1 
ATOM   401  N N   . ARG A 1 54  ? 56.168  59.645 17.483  1.00 121.44 ? 62  ARG A N   1 
ATOM   402  C CA  . ARG A 1 54  ? 57.433  59.203 16.847  1.00 116.10 ? 62  ARG A CA  1 
ATOM   403  C C   . ARG A 1 54  ? 58.240  58.365 17.836  1.00 118.66 ? 62  ARG A C   1 
ATOM   404  O O   . ARG A 1 54  ? 57.721  57.333 18.290  1.00 120.16 ? 62  ARG A O   1 
ATOM   405  C CB  . ARG A 1 54  ? 58.265  60.407 16.407  1.00 115.81 ? 62  ARG A CB  1 
ATOM   406  C CG  . ARG A 1 54  ? 57.735  61.114 15.169  1.00 122.24 ? 62  ARG A CG  1 
ATOM   407  C CD  . ARG A 1 54  ? 58.631  62.277 14.794  1.00 131.44 ? 62  ARG A CD  1 
ATOM   408  N NE  . ARG A 1 54  ? 58.251  62.902 13.537  1.00 146.37 ? 62  ARG A NE  1 
ATOM   409  C CZ  . ARG A 1 54  ? 58.873  63.946 13.005  1.00 168.15 ? 62  ARG A CZ  1 
ATOM   410  N NH1 . ARG A 1 54  ? 59.799  64.584 13.699  1.00 167.95 ? 62  ARG A NH1 1 
ATOM   411  N NH2 . ARG A 1 54  ? 58.568  64.351 11.784  1.00 223.17 ? 62  ARG A NH2 1 
ATOM   412  N N   . ASP A 1 55  ? 59.459  58.800 18.154  1.00 127.18 ? 63  ASP A N   1 
ATOM   413  C CA  . ASP A 1 55  ? 60.346  57.987 19.026  1.00 123.13 ? 63  ASP A CA  1 
ATOM   414  C C   . ASP A 1 55  ? 60.474  58.627 20.409  1.00 123.86 ? 63  ASP A C   1 
ATOM   415  O O   . ASP A 1 55  ? 61.538  58.470 21.029  1.00 131.11 ? 63  ASP A O   1 
ATOM   416  C CB  . ASP A 1 55  ? 61.724  57.815 18.387  1.00 127.45 ? 63  ASP A CB  1 
ATOM   417  C CG  . ASP A 1 55  ? 61.680  57.132 17.033  1.00 129.59 ? 63  ASP A CG  1 
ATOM   418  O OD1 . ASP A 1 55  ? 61.016  57.671 16.129  1.00 135.83 ? 63  ASP A OD1 1 
ATOM   419  O OD2 . ASP A 1 55  ? 62.313  56.069 16.893  1.00 127.43 ? 63  ASP A OD2 1 
ATOM   420  N N   . CYS A 1 56  ? 59.424  59.301 20.876  1.00 121.60 ? 64  CYS A N   1 
ATOM   421  C CA  . CYS A 1 56  ? 59.467  59.904 22.233  1.00 126.07 ? 64  CYS A CA  1 
ATOM   422  C C   . CYS A 1 56  ? 58.446  59.213 23.136  1.00 124.04 ? 64  CYS A C   1 
ATOM   423  O O   . CYS A 1 56  ? 57.327  58.957 22.672  1.00 121.56 ? 64  CYS A O   1 
ATOM   424  C CB  . CYS A 1 56  ? 59.186  61.400 22.190  1.00 126.23 ? 64  CYS A CB  1 
ATOM   425  S SG  . CYS A 1 56  ? 59.746  62.292 23.664  1.00 135.21 ? 64  CYS A SG  1 
ATOM   426  N N   . SER A 1 57  ? 58.835  58.929 24.379  1.00 124.12 ? 65  SER A N   1 
ATOM   427  C CA  . SER A 1 57  ? 57.908  58.310 25.353  1.00 116.60 ? 65  SER A CA  1 
ATOM   428  C C   . SER A 1 57  ? 56.888  59.351 25.795  1.00 117.79 ? 65  SER A C   1 
ATOM   429  O O   . SER A 1 57  ? 57.145  60.547 25.598  1.00 125.25 ? 65  SER A O   1 
ATOM   430  C CB  . SER A 1 57  ? 58.659  57.799 26.543  1.00 117.96 ? 65  SER A CB  1 
ATOM   431  O OG  . SER A 1 57  ? 58.951  58.855 27.446  1.00 114.27 ? 65  SER A OG  1 
ATOM   432  N N   . VAL A 1 58  ? 55.774  58.906 26.371  1.00 121.36 ? 66  VAL A N   1 
ATOM   433  C CA  . VAL A 1 58  ? 54.801  59.886 26.924  1.00 123.24 ? 66  VAL A CA  1 
ATOM   434  C C   . VAL A 1 58  ? 55.545  60.696 27.982  1.00 120.70 ? 66  VAL A C   1 
ATOM   435  O O   . VAL A 1 58  ? 55.383  61.922 28.014  1.00 123.57 ? 66  VAL A O   1 
ATOM   436  C CB  . VAL A 1 58  ? 53.585  59.171 27.535  1.00 127.24 ? 66  VAL A CB  1 
ATOM   437  C CG1 . VAL A 1 58  ? 52.677  60.139 28.278  1.00 124.80 ? 66  VAL A CG1 1 
ATOM   438  C CG2 . VAL A 1 58  ? 52.797  58.397 26.488  1.00 133.15 ? 66  VAL A CG2 1 
ATOM   439  N N   . ALA A 1 59  ? 56.350  60.020 28.797  1.00 114.43 ? 67  ALA A N   1 
ATOM   440  C CA  . ALA A 1 59  ? 57.065  60.721 29.884  1.00 114.37 ? 67  ALA A CA  1 
ATOM   441  C C   . ALA A 1 59  ? 57.932  61.817 29.275  1.00 108.50 ? 67  ALA A C   1 
ATOM   442  O O   . ALA A 1 59  ? 58.004  62.913 29.841  1.00 109.22 ? 67  ALA A O   1 
ATOM   443  C CB  . ALA A 1 59  ? 57.903  59.736 30.648  1.00 118.51 ? 67  ALA A CB  1 
ATOM   444  N N   . GLY A 1 60  ? 58.589  61.503 28.168  1.00 109.61 ? 68  GLY A N   1 
ATOM   445  C CA  . GLY A 1 60  ? 59.487  62.499 27.560  1.00 110.03 ? 68  GLY A CA  1 
ATOM   446  C C   . GLY A 1 60  ? 58.685  63.660 27.025  1.00 111.33 ? 68  GLY A C   1 
ATOM   447  O O   . GLY A 1 60  ? 59.130  64.808 27.162  1.00 118.89 ? 68  GLY A O   1 
ATOM   448  N N   . TRP A 1 61  ? 57.540  63.358 26.423  1.00 111.35 ? 69  TRP A N   1 
ATOM   449  C CA  . TRP A 1 61  ? 56.706  64.419 25.814  1.00 117.99 ? 69  TRP A CA  1 
ATOM   450  C C   . TRP A 1 61  ? 56.179  65.342 26.911  1.00 120.21 ? 69  TRP A C   1 
ATOM   451  O O   . TRP A 1 61  ? 56.028  66.539 26.651  1.00 120.13 ? 69  TRP A O   1 
ATOM   452  C CB  . TRP A 1 61  ? 55.570  63.778 25.024  1.00 121.87 ? 69  TRP A CB  1 
ATOM   453  C CG  . TRP A 1 61  ? 54.384  64.664 24.827  1.00 133.06 ? 69  TRP A CG  1 
ATOM   454  C CD1 . TRP A 1 61  ? 54.348  65.862 24.178  1.00 138.05 ? 69  TRP A CD1 1 
ATOM   455  C CD2 . TRP A 1 61  ? 53.045  64.419 25.291  1.00 131.37 ? 69  TRP A CD2 1 
ATOM   456  N NE1 . TRP A 1 61  ? 53.083  66.378 24.201  1.00 148.03 ? 69  TRP A NE1 1 
ATOM   457  C CE2 . TRP A 1 61  ? 52.262  65.514 24.876  1.00 136.09 ? 69  TRP A CE2 1 
ATOM   458  C CE3 . TRP A 1 61  ? 52.437  63.384 26.007  1.00 129.54 ? 69  TRP A CE3 1 
ATOM   459  C CZ2 . TRP A 1 61  ? 50.900  65.602 25.157  1.00 141.49 ? 69  TRP A CZ2 1 
ATOM   460  C CZ3 . TRP A 1 61  ? 51.092  63.472 26.285  1.00 141.70 ? 69  TRP A CZ3 1 
ATOM   461  C CH2 . TRP A 1 61  ? 50.338  64.565 25.865  1.00 142.57 ? 69  TRP A CH2 1 
ATOM   462  N N   . LEU A 1 62  ? 55.902  64.784 28.087  1.00 117.67 ? 70  LEU A N   1 
ATOM   463  C CA  . LEU A 1 62  ? 55.326  65.599 29.185  1.00 111.39 ? 70  LEU A CA  1 
ATOM   464  C C   . LEU A 1 62  ? 56.450  66.275 29.970  1.00 113.08 ? 70  LEU A C   1 
ATOM   465  O O   . LEU A 1 62  ? 56.228  67.383 30.472  1.00 125.48 ? 70  LEU A O   1 
ATOM   466  C CB  . LEU A 1 62  ? 54.510  64.678 30.090  1.00 109.88 ? 70  LEU A CB  1 
ATOM   467  C CG  . LEU A 1 62  ? 53.216  64.147 29.480  1.00 111.03 ? 70  LEU A CG  1 
ATOM   468  C CD1 . LEU A 1 62  ? 52.474  63.292 30.490  1.00 112.94 ? 70  LEU A CD1 1 
ATOM   469  C CD2 . LEU A 1 62  ? 52.339  65.296 29.013  1.00 119.50 ? 70  LEU A CD2 1 
ATOM   470  N N   . LEU A 1 63  ? 57.609  65.623 30.069  1.00 103.45 ? 71  LEU A N   1 
ATOM   471  C CA  . LEU A 1 63  ? 58.725  66.183 30.871  1.00 100.60 ? 71  LEU A CA  1 
ATOM   472  C C   . LEU A 1 63  ? 59.591  67.076 29.980  1.00 107.96 ? 71  LEU A C   1 
ATOM   473  O O   . LEU A 1 63  ? 60.540  67.673 30.496  1.00 115.00 ? 71  LEU A O   1 
ATOM   474  C CB  . LEU A 1 63  ? 59.551  65.029 31.434  1.00 99.71  ? 71  LEU A CB  1 
ATOM   475  C CG  . LEU A 1 63  ? 59.000  64.381 32.699  1.00 105.70 ? 71  LEU A CG  1 
ATOM   476  C CD1 . LEU A 1 63  ? 59.931  63.283 33.188  1.00 112.87 ? 71  LEU A CD1 1 
ATOM   477  C CD2 . LEU A 1 63  ? 58.801  65.426 33.783  1.00 108.47 ? 71  LEU A CD2 1 
ATOM   478  N N   . GLY A 1 64  ? 59.261  67.168 28.693  1.00 105.38 ? 72  GLY A N   1 
ATOM   479  C CA  . GLY A 1 64  ? 60.011  68.066 27.794  1.00 108.07 ? 72  GLY A CA  1 
ATOM   480  C C   . GLY A 1 64  ? 61.445  67.612 27.611  1.00 115.56 ? 72  GLY A C   1 
ATOM   481  O O   . GLY A 1 64  ? 62.350  68.408 27.884  1.00 120.32 ? 72  GLY A O   1 
ATOM   482  N N   . ASN A 1 65  ? 61.639  66.369 27.166  1.00 121.63 ? 73  ASN A N   1 
ATOM   483  C CA  . ASN A 1 65  ? 63.009  65.870 26.883  1.00 127.95 ? 73  ASN A CA  1 
ATOM   484  C C   . ASN A 1 65  ? 63.568  66.673 25.713  1.00 137.84 ? 73  ASN A C   1 
ATOM   485  O O   . ASN A 1 65  ? 62.853  66.840 24.719  1.00 140.58 ? 73  ASN A O   1 
ATOM   486  C CB  . ASN A 1 65  ? 63.027  64.376 26.573  1.00 126.14 ? 73  ASN A CB  1 
ATOM   487  C CG  . ASN A 1 65  ? 64.422  63.816 26.434  1.00 128.98 ? 73  ASN A CG  1 
ATOM   488  O OD1 . ASN A 1 65  ? 65.108  64.064 25.445  1.00 134.84 ? 73  ASN A OD1 1 
ATOM   489  N ND2 . ASN A 1 65  ? 64.840  63.031 27.410  1.00 129.63 ? 73  ASN A ND2 1 
ATOM   490  N N   . PRO A 1 66  ? 64.817  67.158 25.785  1.00 141.57 ? 74  PRO A N   1 
ATOM   491  C CA  . PRO A 1 66  ? 65.350  68.005 24.729  1.00 145.29 ? 74  PRO A CA  1 
ATOM   492  C C   . PRO A 1 66  ? 65.086  67.377 23.356  1.00 148.78 ? 74  PRO A C   1 
ATOM   493  O O   . PRO A 1 66  ? 64.849  68.108 22.412  1.00 146.71 ? 74  PRO A O   1 
ATOM   494  C CB  . PRO A 1 66  ? 66.844  67.970 25.051  1.00 150.92 ? 74  PRO A CB  1 
ATOM   495  C CG  . PRO A 1 66  ? 66.886  67.865 26.555  1.00 146.07 ? 74  PRO A CG  1 
ATOM   496  C CD  . PRO A 1 66  ? 65.750  66.920 26.880  1.00 140.86 ? 74  PRO A CD  1 
ATOM   497  N N   . MET A 1 67  ? 65.162  66.050 23.278  1.00 143.23 ? 75  MET A N   1 
ATOM   498  C CA  . MET A 1 67  ? 64.866  65.369 21.993  1.00 142.15 ? 75  MET A CA  1 
ATOM   499  C C   . MET A 1 67  ? 63.351  65.292 21.844  1.00 140.90 ? 75  MET A C   1 
ATOM   500  O O   . MET A 1 67  ? 62.667  65.011 22.848  1.00 137.98 ? 75  MET A O   1 
ATOM   501  C CB  . MET A 1 67  ? 65.440  63.951 21.954  1.00 142.70 ? 75  MET A CB  1 
ATOM   502  C CG  . MET A 1 67  ? 66.944  63.934 21.875  1.00 141.92 ? 75  MET A CG  1 
ATOM   503  S SD  . MET A 1 67  ? 67.583  64.929 20.500  1.00 152.19 ? 75  MET A SD  1 
ATOM   504  C CE  . MET A 1 67  ? 66.739  64.177 19.110  1.00 136.20 ? 75  MET A CE  1 
ATOM   505  N N   . CYS A 1 68  ? 62.866  65.530 20.633  1.00 138.10 ? 76  CYS A N   1 
ATOM   506  C CA  . CYS A 1 68  ? 61.408  65.469 20.393  1.00 142.34 ? 76  CYS A CA  1 
ATOM   507  C C   . CYS A 1 68  ? 60.753  66.614 21.157  1.00 140.46 ? 76  CYS A C   1 
ATOM   508  O O   . CYS A 1 68  ? 59.628  66.420 21.645  1.00 135.19 ? 76  CYS A O   1 
ATOM   509  C CB  . CYS A 1 68  ? 60.832  64.128 20.821  1.00 157.11 ? 76  CYS A CB  1 
ATOM   510  S SG  . CYS A 1 68  ? 61.344  62.747 19.764  1.00 189.88 ? 76  CYS A SG  1 
ATOM   511  N N   . ASP A 1 69  ? 61.444  67.749 21.272  1.00 138.35 ? 77  ASP A N   1 
ATOM   512  C CA  . ASP A 1 69  ? 60.789  68.948 21.853  1.00 135.69 ? 77  ASP A CA  1 
ATOM   513  C C   . ASP A 1 69  ? 59.858  69.465 20.756  1.00 137.12 ? 77  ASP A C   1 
ATOM   514  O O   . ASP A 1 69  ? 59.234  70.506 20.971  1.00 133.30 ? 77  ASP A O   1 
ATOM   515  C CB  . ASP A 1 69  ? 61.809  69.971 22.350  1.00 141.16 ? 77  ASP A CB  1 
ATOM   516  C CG  . ASP A 1 69  ? 62.182  69.784 23.810  1.00 146.74 ? 77  ASP A CG  1 
ATOM   517  O OD1 . ASP A 1 69  ? 61.375  69.197 24.546  1.00 157.64 ? 77  ASP A OD1 1 
ATOM   518  O OD2 . ASP A 1 69  ? 63.292  70.212 24.193  1.00 170.94 ? 77  ASP A OD2 1 
ATOM   519  N N   . GLU A 1 70  ? 59.790  68.757 19.626  1.00 134.22 ? 78  GLU A N   1 
ATOM   520  C CA  . GLU A 1 70  ? 58.846  69.109 18.534  1.00 130.67 ? 78  GLU A CA  1 
ATOM   521  C C   . GLU A 1 70  ? 57.418  68.870 19.025  1.00 130.93 ? 78  GLU A C   1 
ATOM   522  O O   . GLU A 1 70  ? 56.463  69.126 18.263  1.00 133.32 ? 78  GLU A O   1 
ATOM   523  C CB  . GLU A 1 70  ? 59.138  68.222 17.329  1.00 132.36 ? 78  GLU A CB  1 
ATOM   524  C CG  . GLU A 1 70  ? 60.535  68.431 16.778  1.00 149.79 ? 78  GLU A CG  1 
ATOM   525  C CD  . GLU A 1 70  ? 60.906  67.527 15.611  1.00 170.44 ? 78  GLU A CD  1 
ATOM   526  O OE1 . GLU A 1 70  ? 60.111  66.622 15.301  1.00 170.76 ? 78  GLU A OE1 1 
ATOM   527  O OE2 . GLU A 1 70  ? 61.974  67.752 15.000  1.00 172.24 ? 78  GLU A OE2 1 
ATOM   528  N N   . PHE A 1 71  ? 57.280  68.362 20.249  1.00 129.89 ? 79  PHE A N   1 
ATOM   529  C CA  . PHE A 1 71  ? 55.940  68.054 20.811  1.00 129.94 ? 79  PHE A CA  1 
ATOM   530  C C   . PHE A 1 71  ? 55.645  68.979 21.996  1.00 133.71 ? 79  PHE A C   1 
ATOM   531  O O   . PHE A 1 71  ? 55.131  68.495 23.019  1.00 130.22 ? 79  PHE A O   1 
ATOM   532  C CB  . PHE A 1 71  ? 55.839  66.572 21.192  1.00 132.67 ? 79  PHE A CB  1 
ATOM   533  C CG  . PHE A 1 71  ? 56.196  65.596 20.099  1.00 136.55 ? 79  PHE A CG  1 
ATOM   534  C CD1 . PHE A 1 71  ? 55.821  65.823 18.783  1.00 133.30 ? 79  PHE A CD1 1 
ATOM   535  C CD2 . PHE A 1 71  ? 56.876  64.425 20.391  1.00 136.52 ? 79  PHE A CD2 1 
ATOM   536  C CE1 . PHE A 1 71  ? 56.152  64.921 17.784  1.00 128.03 ? 79  PHE A CE1 1 
ATOM   537  C CE2 . PHE A 1 71  ? 57.199  63.521 19.394  1.00 130.52 ? 79  PHE A CE2 1 
ATOM   538  C CZ  . PHE A 1 71  ? 56.837  63.770 18.092  1.00 127.19 ? 79  PHE A CZ  1 
ATOM   539  N N   . ILE A 1 72  ? 56.025  70.252 21.884  1.00 130.67 ? 80  ILE A N   1 
ATOM   540  C CA  . ILE A 1 72  ? 55.753  71.232 22.974  1.00 129.35 ? 80  ILE A CA  1 
ATOM   541  C C   . ILE A 1 72  ? 54.477  71.985 22.605  1.00 135.27 ? 80  ILE A C   1 
ATOM   542  O O   . ILE A 1 72  ? 53.645  72.213 23.500  1.00 131.61 ? 80  ILE A O   1 
ATOM   543  C CB  . ILE A 1 72  ? 56.953  72.175 23.173  1.00 122.01 ? 80  ILE A CB  1 
ATOM   544  C CG1 . ILE A 1 72  ? 58.126  71.450 23.836  1.00 126.11 ? 80  ILE A CG1 1 
ATOM   545  C CG2 . ILE A 1 72  ? 56.549  73.413 23.955  1.00 128.88 ? 80  ILE A CG2 1 
ATOM   546  C CD1 . ILE A 1 72  ? 59.286  72.352 24.180  1.00 135.21 ? 80  ILE A CD1 1 
ATOM   547  N N   . ASN A 1 73  ? 54.328  72.335 21.328  1.00 142.97 ? 81  ASN A N   1 
ATOM   548  C CA  . ASN A 1 73  ? 53.078  72.991 20.866  1.00 152.01 ? 81  ASN A CA  1 
ATOM   549  C C   . ASN A 1 73  ? 52.044  71.889 20.631  1.00 160.53 ? 81  ASN A C   1 
ATOM   550  O O   . ASN A 1 73  ? 51.678  71.654 19.463  1.00 162.34 ? 81  ASN A O   1 
ATOM   551  C CB  . ASN A 1 73  ? 53.322  73.845 19.621  1.00 159.13 ? 81  ASN A CB  1 
ATOM   552  C CG  . ASN A 1 73  ? 54.149  73.133 18.572  1.00 163.18 ? 81  ASN A CG  1 
ATOM   553  O OD1 . ASN A 1 73  ? 55.284  72.739 18.831  1.00 175.40 ? 81  ASN A OD1 1 
ATOM   554  N ND2 . ASN A 1 73  ? 53.587  72.958 17.387  1.00 156.63 ? 81  ASN A ND2 1 
ATOM   555  N N   . VAL A 1 74  ? 51.592  71.243 21.705  1.00 157.29 ? 82  VAL A N   1 
ATOM   556  C CA  . VAL A 1 74  ? 50.661  70.087 21.560  1.00 163.80 ? 82  VAL A CA  1 
ATOM   557  C C   . VAL A 1 74  ? 49.431  70.512 20.758  1.00 169.62 ? 82  VAL A C   1 
ATOM   558  O O   . VAL A 1 74  ? 48.843  71.564 21.072  1.00 162.98 ? 82  VAL A O   1 
ATOM   559  C CB  . VAL A 1 74  ? 50.272  69.521 22.939  1.00 160.98 ? 82  VAL A CB  1 
ATOM   560  C CG1 . VAL A 1 74  ? 51.501  69.078 23.714  1.00 153.97 ? 82  VAL A CG1 1 
ATOM   561  C CG2 . VAL A 1 74  ? 49.466  70.511 23.766  1.00 149.94 ? 82  VAL A CG2 1 
ATOM   562  N N   . PRO A 1 75  ? 49.005  69.765 19.712  1.00 151.96 ? 83  PRO A N   1 
ATOM   563  C CA  . PRO A 1 75  ? 47.771  70.100 19.007  1.00 165.67 ? 83  PRO A CA  1 
ATOM   564  C C   . PRO A 1 75  ? 46.592  69.910 19.966  1.00 166.82 ? 83  PRO A C   1 
ATOM   565  O O   . PRO A 1 75  ? 46.771  69.264 20.976  1.00 165.30 ? 83  PRO A O   1 
ATOM   566  C CB  . PRO A 1 75  ? 47.688  69.072 17.872  1.00 167.32 ? 83  PRO A CB  1 
ATOM   567  C CG  . PRO A 1 75  ? 49.106  68.583 17.707  1.00 164.63 ? 83  PRO A CG  1 
ATOM   568  C CD  . PRO A 1 75  ? 49.667  68.597 19.111  1.00 157.90 ? 83  PRO A CD  1 
ATOM   569  N N   . GLU A 1 76  a 45.419  70.428 19.606  1.00 177.75 ? 83  GLU A N   1 
ATOM   570  C CA  . GLU A 1 76  a 44.228  70.346 20.497  1.00 184.19 ? 83  GLU A CA  1 
ATOM   571  C C   . GLU A 1 76  a 43.634  68.932 20.479  1.00 181.05 ? 83  GLU A C   1 
ATOM   572  O O   . GLU A 1 76  a 42.620  68.717 21.168  1.00 188.11 ? 83  GLU A O   1 
ATOM   573  C CB  . GLU A 1 76  a 43.197  71.398 20.081  1.00 193.10 ? 83  GLU A CB  1 
ATOM   574  C CG  . GLU A 1 76  a 42.804  71.296 18.620  1.00 194.79 ? 83  GLU A CG  1 
ATOM   575  C CD  . GLU A 1 76  a 41.695  72.236 18.184  1.00 204.72 ? 83  GLU A CD  1 
ATOM   576  O OE1 . GLU A 1 76  a 40.594  72.157 18.764  1.00 204.06 ? 83  GLU A OE1 1 
ATOM   577  O OE2 . GLU A 1 76  a 41.934  73.044 17.266  1.00 211.28 ? 83  GLU A OE2 1 
ATOM   578  N N   . TRP A 1 77  ? 44.240  68.007 19.732  1.00 161.98 ? 84  TRP A N   1 
ATOM   579  C CA  . TRP A 1 77  ? 43.671  66.640 19.610  1.00 165.59 ? 84  TRP A CA  1 
ATOM   580  C C   . TRP A 1 77  ? 44.750  65.597 19.902  1.00 151.32 ? 84  TRP A C   1 
ATOM   581  O O   . TRP A 1 77  ? 45.903  65.834 19.505  1.00 172.09 ? 84  TRP A O   1 
ATOM   582  C CB  . TRP A 1 77  ? 43.083  66.461 18.212  1.00 189.26 ? 84  TRP A CB  1 
ATOM   583  C CG  . TRP A 1 77  ? 42.052  67.489 17.865  1.00 212.38 ? 84  TRP A CG  1 
ATOM   584  C CD1 . TRP A 1 77  ? 42.109  68.404 16.855  1.00 204.47 ? 84  TRP A CD1 1 
ATOM   585  C CD2 . TRP A 1 77  ? 40.795  67.706 18.532  1.00 203.16 ? 84  TRP A CD2 1 
ATOM   586  N NE1 . TRP A 1 77  ? 40.976  69.174 16.846  1.00 193.67 ? 84  TRP A NE1 1 
ATOM   587  C CE2 . TRP A 1 77  ? 40.153  68.769 17.864  1.00 203.59 ? 84  TRP A CE2 1 
ATOM   588  C CE3 . TRP A 1 77  ? 40.152  67.108 19.621  1.00 197.11 ? 84  TRP A CE3 1 
ATOM   589  C CZ2 . TRP A 1 77  ? 38.901  69.242 18.251  1.00 201.49 ? 84  TRP A CZ2 1 
ATOM   590  C CZ3 . TRP A 1 77  ? 38.917  67.578 20.005  1.00 193.73 ? 84  TRP A CZ3 1 
ATOM   591  C CH2 . TRP A 1 77  ? 38.301  68.628 19.326  1.00 193.02 ? 84  TRP A CH2 1 
ATOM   592  N N   . SER A 1 78  ? 44.388  64.484 20.547  1.00 123.31 ? 85  SER A N   1 
ATOM   593  C CA  . SER A 1 78  ? 45.443  63.513 20.934  1.00 131.20 ? 85  SER A CA  1 
ATOM   594  C C   . SER A 1 78  ? 44.897  62.104 21.191  1.00 141.54 ? 85  SER A C   1 
ATOM   595  O O   . SER A 1 78  ? 44.353  61.895 22.289  1.00 208.03 ? 85  SER A O   1 
ATOM   596  C CB  . SER A 1 78  ? 46.159  64.020 22.155  1.00 126.47 ? 85  SER A CB  1 
ATOM   597  O OG  . SER A 1 78  ? 45.299  64.010 23.283  1.00 112.03 ? 85  SER A OG  1 
ATOM   598  N N   . TYR A 1 79  ? 45.020  61.201 20.213  1.00 132.94 ? 86  TYR A N   1 
ATOM   599  C CA  . TYR A 1 79  ? 44.728  59.766 20.482  1.00 121.35 ? 86  TYR A CA  1 
ATOM   600  C C   . TYR A 1 79  ? 46.143  59.175 20.524  1.00 125.54 ? 86  TYR A C   1 
ATOM   601  O O   . TYR A 1 79  ? 46.824  59.181 19.479  1.00 147.07 ? 86  TYR A O   1 
ATOM   602  C CB  . TYR A 1 79  ? 43.641  59.198 19.552  1.00 122.49 ? 86  TYR A CB  1 
ATOM   603  C CG  . TYR A 1 79  ? 44.030  58.605 18.220  1.00 129.44 ? 86  TYR A CG  1 
ATOM   604  C CD1 . TYR A 1 79  ? 44.888  57.521 18.125  1.00 142.08 ? 86  TYR A CD1 1 
ATOM   605  C CD2 . TYR A 1 79  ? 43.457  59.075 17.049  1.00 131.51 ? 86  TYR A CD2 1 
ATOM   606  C CE1 . TYR A 1 79  ? 45.221  56.967 16.900  1.00 131.97 ? 86  TYR A CE1 1 
ATOM   607  C CE2 . TYR A 1 79  ? 43.769  58.526 15.817  1.00 166.22 ? 86  TYR A CE2 1 
ATOM   608  C CZ  . TYR A 1 79  ? 44.659  57.471 15.741  1.00 153.09 ? 86  TYR A CZ  1 
ATOM   609  O OH  . TYR A 1 79  ? 44.978  56.927 14.520  1.00 168.79 ? 86  TYR A OH  1 
ATOM   610  N N   . ILE A 1 80  ? 46.609  58.765 21.705  1.00 125.95 ? 87  ILE A N   1 
ATOM   611  C CA  . ILE A 1 80  ? 48.044  58.371 21.868  1.00 130.77 ? 87  ILE A CA  1 
ATOM   612  C C   . ILE A 1 80  ? 48.529  57.335 20.849  1.00 130.24 ? 87  ILE A C   1 
ATOM   613  O O   . ILE A 1 80  ? 47.905  56.259 20.757  1.00 234.11 ? 87  ILE A O   1 
ATOM   614  C CB  . ILE A 1 80  ? 48.311  57.901 23.314  1.00 126.43 ? 87  ILE A CB  1 
ATOM   615  C CG1 . ILE A 1 80  ? 47.822  58.927 24.339  1.00 133.18 ? 87  ILE A CG1 1 
ATOM   616  C CG2 . ILE A 1 80  ? 49.781  57.562 23.510  1.00 160.89 ? 87  ILE A CG2 1 
ATOM   617  C CD1 . ILE A 1 80  ? 48.491  60.276 24.225  1.00 133.06 ? 87  ILE A CD1 1 
ATOM   618  N N   . VAL A 1 81  ? 49.602  57.658 20.117  1.00 134.91 ? 88  VAL A N   1 
ATOM   619  C CA  . VAL A 1 81  ? 50.268  56.676 19.210  1.00 137.96 ? 88  VAL A CA  1 
ATOM   620  C C   . VAL A 1 81  ? 51.692  56.616 19.761  1.00 137.03 ? 88  VAL A C   1 
ATOM   621  O O   . VAL A 1 81  ? 52.484  57.515 19.419  1.00 135.30 ? 88  VAL A O   1 
ATOM   622  C CB  . VAL A 1 81  ? 50.231  57.115 17.735  1.00 144.96 ? 88  VAL A CB  1 
ATOM   623  C CG1 . VAL A 1 81  ? 50.952  56.122 16.836  1.00 145.51 ? 88  VAL A CG1 1 
ATOM   624  C CG2 . VAL A 1 81  ? 48.808  57.338 17.249  1.00 155.60 ? 88  VAL A CG2 1 
ATOM   625  N N   . GLU A 1 82  ? 52.010  55.614 20.584  1.00 147.72 ? 89  GLU A N   1 
ATOM   626  C CA  . GLU A 1 82  ? 53.311  55.621 21.305  1.00 136.66 ? 89  GLU A CA  1 
ATOM   627  C C   . GLU A 1 82  ? 53.865  54.315 20.737  1.00 128.65 ? 89  GLU A C   1 
ATOM   628  O O   . GLU A 1 82  ? 53.072  53.522 20.210  1.00 135.45 ? 89  GLU A O   1 
ATOM   629  C CB  . GLU A 1 82  ? 53.312  55.554 22.832  1.00 134.90 ? 89  GLU A CB  1 
ATOM   630  C CG  . GLU A 1 82  ? 54.688  55.684 23.458  1.00 129.54 ? 89  GLU A CG  1 
ATOM   631  C CD  . GLU A 1 82  ? 54.744  55.328 24.934  1.00 124.13 ? 89  GLU A CD  1 
ATOM   632  O OE1 . GLU A 1 82  ? 53.699  54.934 25.484  1.00 126.54 ? 89  GLU A OE1 1 
ATOM   633  O OE2 . GLU A 1 82  ? 55.834  55.437 25.527  1.00 129.63 ? 89  GLU A OE2 1 
ATOM   634  N N   . LYS A 1 83  ? 55.177  54.110 20.825  1.00 128.83 ? 90  LYS A N   1 
ATOM   635  C CA  . LYS A 1 83  ? 55.762  52.819 20.387  1.00 129.07 ? 90  LYS A CA  1 
ATOM   636  C C   . LYS A 1 83  ? 56.385  52.148 21.610  1.00 135.82 ? 90  LYS A C   1 
ATOM   637  O O   . LYS A 1 83  ? 56.693  52.860 22.580  1.00 137.90 ? 90  LYS A O   1 
ATOM   638  C CB  . LYS A 1 83  ? 56.807  53.044 19.295  1.00 126.21 ? 90  LYS A CB  1 
ATOM   639  C CG  . LYS A 1 83  ? 56.315  53.831 18.088  1.00 135.31 ? 90  LYS A CG  1 
ATOM   640  C CD  . LYS A 1 83  ? 57.329  53.920 16.971  1.00 129.18 ? 90  LYS A CD  1 
ATOM   641  C CE  . LYS A 1 83  ? 56.860  54.799 15.832  1.00 132.84 ? 90  LYS A CE  1 
ATOM   642  N NZ  . LYS A 1 83  ? 55.509  54.411 15.361  1.00 141.61 ? 90  LYS A NZ  1 
ATOM   643  N N   . ALA A 1 84  ? 56.551  50.830 21.563  1.00 132.87 ? 91  ALA A N   1 
ATOM   644  C CA  . ALA A 1 84  ? 57.126  50.093 22.706  1.00 142.52 ? 91  ALA A CA  1 
ATOM   645  C C   . ALA A 1 84  ? 58.624  50.369 22.692  1.00 151.06 ? 91  ALA A C   1 
ATOM   646  O O   . ALA A 1 84  ? 59.242  50.249 21.618  1.00 146.43 ? 91  ALA A O   1 
ATOM   647  C CB  . ALA A 1 84  ? 56.854  48.621 22.580  1.00 137.81 ? 91  ALA A CB  1 
ATOM   648  N N   . ASN A 1 85  ? 59.173  50.761 23.840  1.00 157.79 ? 92  ASN A N   1 
ATOM   649  C CA  . ASN A 1 85  ? 60.620  51.077 23.908  1.00 157.53 ? 92  ASN A CA  1 
ATOM   650  C C   . ASN A 1 85  ? 60.932  52.256 22.977  1.00 155.70 ? 92  ASN A C   1 
ATOM   651  O O   . ASN A 1 85  ? 61.588  52.036 21.945  1.00 156.62 ? 92  ASN A O   1 
ATOM   652  C CB  . ASN A 1 85  ? 61.452  49.844 23.568  1.00 162.40 ? 92  ASN A CB  1 
ATOM   653  C CG  . ASN A 1 85  ? 60.993  48.612 24.314  1.00 169.25 ? 92  ASN A CG  1 
ATOM   654  O OD1 . ASN A 1 85  ? 61.022  48.576 25.540  1.00 166.52 ? 92  ASN A OD1 1 
ATOM   655  N ND2 . ASN A 1 85  ? 60.562  47.597 23.584  1.00 209.67 ? 92  ASN A ND2 1 
ATOM   656  N N   . PRO A 1 86  ? 60.564  53.513 23.333  1.00 148.89 ? 93  PRO A N   1 
ATOM   657  C CA  . PRO A 1 86  ? 60.922  54.673 22.522  1.00 137.30 ? 93  PRO A CA  1 
ATOM   658  C C   . PRO A 1 86  ? 62.405  55.011 22.697  1.00 132.54 ? 93  PRO A C   1 
ATOM   659  O O   . PRO A 1 86  ? 62.952  54.715 23.739  1.00 131.70 ? 93  PRO A O   1 
ATOM   660  C CB  . PRO A 1 86  ? 60.078  55.800 23.120  1.00 129.68 ? 93  PRO A CB  1 
ATOM   661  C CG  . PRO A 1 86  ? 59.950  55.416 24.566  1.00 132.69 ? 93  PRO A CG  1 
ATOM   662  C CD  . PRO A 1 86  ? 59.787  53.914 24.521  1.00 142.83 ? 93  PRO A CD  1 
ATOM   663  N N   . VAL A 1 87  ? 63.010  55.618 21.678  1.00 127.80 ? 94  VAL A N   1 
ATOM   664  C CA  . VAL A 1 87  ? 64.464  55.936 21.734  1.00 124.39 ? 94  VAL A CA  1 
ATOM   665  C C   . VAL A 1 87  ? 64.688  57.029 22.777  1.00 127.64 ? 94  VAL A C   1 
ATOM   666  O O   . VAL A 1 87  ? 65.574  56.857 23.630  1.00 125.26 ? 94  VAL A O   1 
ATOM   667  C CB  . VAL A 1 87  ? 64.979  56.378 20.354  1.00 124.39 ? 94  VAL A CB  1 
ATOM   668  C CG1 . VAL A 1 87  ? 66.466  56.689 20.380  1.00 133.32 ? 94  VAL A CG1 1 
ATOM   669  C CG2 . VAL A 1 87  ? 64.666  55.345 19.284  1.00 127.19 ? 94  VAL A CG2 1 
ATOM   670  N N   . ASN A 1 88  ? 63.902  58.102 22.712  1.00 125.11 ? 95  ASN A N   1 
ATOM   671  C CA  . ASN A 1 88  ? 64.111  59.242 23.637  1.00 119.30 ? 95  ASN A CA  1 
ATOM   672  C C   . ASN A 1 88  ? 63.031  59.218 24.719  1.00 123.99 ? 95  ASN A C   1 
ATOM   673  O O   . ASN A 1 88  ? 61.902  59.642 24.427  1.00 132.99 ? 95  ASN A O   1 
ATOM   674  C CB  . ASN A 1 88  ? 64.106  60.566 22.877  1.00 126.07 ? 95  ASN A CB  1 
ATOM   675  C CG  . ASN A 1 88  ? 64.901  60.510 21.590  1.00 127.35 ? 95  ASN A CG  1 
ATOM   676  O OD1 . ASN A 1 88  ? 64.364  60.757 20.513  1.00 136.75 ? 95  ASN A OD1 1 
ATOM   677  N ND2 . ASN A 1 88  ? 66.181  60.195 21.693  1.00 130.55 ? 95  ASN A ND2 1 
ATOM   678  N N   . ASP A 1 89  ? 63.375  58.748 25.918  1.00 124.21 ? 96  ASP A N   1 
ATOM   679  C CA  . ASP A 1 89  ? 62.401  58.668 27.037  1.00 131.28 ? 96  ASP A CA  1 
ATOM   680  C C   . ASP A 1 89  ? 62.895  59.570 28.169  1.00 122.76 ? 96  ASP A C   1 
ATOM   681  O O   . ASP A 1 89  ? 62.964  60.792 27.957  1.00 116.17 ? 96  ASP A O   1 
ATOM   682  C CB  . ASP A 1 89  ? 62.232  57.217 27.492  1.00 135.72 ? 96  ASP A CB  1 
ATOM   683  C CG  . ASP A 1 89  ? 61.212  57.001 28.597  1.00 139.52 ? 96  ASP A CG  1 
ATOM   684  O OD1 . ASP A 1 89  ? 60.623  57.996 29.059  1.00 141.55 ? 96  ASP A OD1 1 
ATOM   685  O OD2 . ASP A 1 89  ? 61.018  55.835 28.989  1.00 149.22 ? 96  ASP A OD2 1 
ATOM   686  N N   . LEU A 1 90  a 63.225  58.981 29.319  1.00 128.68 ? 96  LEU A N   1 
ATOM   687  C CA  . LEU A 1 90  a 63.742  59.762 30.469  1.00 121.73 ? 96  LEU A CA  1 
ATOM   688  C C   . LEU A 1 90  a 65.266  59.789 30.383  1.00 123.60 ? 96  LEU A C   1 
ATOM   689  O O   . LEU A 1 90  a 65.902  59.089 31.181  1.00 127.78 ? 96  LEU A O   1 
ATOM   690  C CB  . LEU A 1 90  a 63.290  59.087 31.764  1.00 119.25 ? 96  LEU A CB  1 
ATOM   691  C CG  . LEU A 1 90  a 62.533  59.981 32.742  1.00 117.70 ? 96  LEU A CG  1 
ATOM   692  C CD1 . LEU A 1 90  a 61.039  59.922 32.476  1.00 123.49 ? 96  LEU A CD1 1 
ATOM   693  C CD2 . LEU A 1 90  a 62.835  59.586 34.177  1.00 121.96 ? 96  LEU A CD2 1 
ATOM   694  N N   . CYS A 1 91  ? 65.812  60.561 29.446  1.00 131.90 ? 97  CYS A N   1 
ATOM   695  C CA  . CYS A 1 91  ? 67.282  60.638 29.262  1.00 139.57 ? 97  CYS A CA  1 
ATOM   696  C C   . CYS A 1 91  ? 67.983  60.418 30.603  1.00 140.73 ? 97  CYS A C   1 
ATOM   697  O O   . CYS A 1 91  ? 68.516  59.316 30.815  1.00 165.23 ? 97  CYS A O   1 
ATOM   698  C CB  . CYS A 1 91  ? 67.682  62.005 28.733  1.00 144.42 ? 97  CYS A CB  1 
ATOM   699  S SG  . CYS A 1 91  ? 66.808  63.362 29.553  1.00 167.93 ? 97  CYS A SG  1 
ATOM   700  N N   . TYR A 1 92  ? 68.034  61.449 31.444  1.00 130.56 ? 98  TYR A N   1 
ATOM   701  C CA  . TYR A 1 92  ? 68.769  61.277 32.716  1.00 132.54 ? 98  TYR A CA  1 
ATOM   702  C C   . TYR A 1 92  ? 68.147  60.064 33.396  1.00 138.61 ? 98  TYR A C   1 
ATOM   703  O O   . TYR A 1 92  ? 66.940  60.082 33.680  1.00 135.47 ? 98  TYR A O   1 
ATOM   704  C CB  . TYR A 1 92  ? 68.711  62.525 33.595  1.00 130.12 ? 98  TYR A CB  1 
ATOM   705  C CG  . TYR A 1 92  ? 69.706  62.520 34.727  1.00 136.34 ? 98  TYR A CG  1 
ATOM   706  C CD1 . TYR A 1 92  ? 69.627  61.588 35.748  1.00 150.04 ? 98  TYR A CD1 1 
ATOM   707  C CD2 . TYR A 1 92  ? 70.747  63.430 34.763  1.00 134.77 ? 98  TYR A CD2 1 
ATOM   708  C CE1 . TYR A 1 92  ? 70.545  61.570 36.783  1.00 146.46 ? 98  TYR A CE1 1 
ATOM   709  C CE2 . TYR A 1 92  ? 71.674  63.426 35.791  1.00 145.15 ? 98  TYR A CE2 1 
ATOM   710  C CZ  . TYR A 1 92  ? 71.574  62.492 36.804  1.00 141.33 ? 98  TYR A CZ  1 
ATOM   711  O OH  . TYR A 1 92  ? 72.495  62.484 37.820  1.00 145.69 ? 98  TYR A OH  1 
ATOM   712  N N   . PRO A 1 93  ? 68.925  59.004 33.665  1.00 148.99 ? 99  PRO A N   1 
ATOM   713  C CA  . PRO A 1 93  ? 68.371  57.777 34.220  1.00 151.05 ? 99  PRO A CA  1 
ATOM   714  C C   . PRO A 1 93  ? 67.330  58.052 35.310  1.00 143.77 ? 99  PRO A C   1 
ATOM   715  O O   . PRO A 1 93  ? 67.616  58.812 36.215  1.00 149.11 ? 99  PRO A O   1 
ATOM   716  C CB  . PRO A 1 93  ? 69.595  57.090 34.841  1.00 151.51 ? 99  PRO A CB  1 
ATOM   717  C CG  . PRO A 1 93  ? 70.741  58.075 34.693  1.00 156.85 ? 99  PRO A CG  1 
ATOM   718  C CD  . PRO A 1 93  ? 70.375  58.955 33.520  1.00 144.80 ? 99  PRO A CD  1 
ATOM   719  N N   . GLY A 1 94  ? 66.158  57.421 35.201  1.00 138.81 ? 100 GLY A N   1 
ATOM   720  C CA  . GLY A 1 94  ? 65.123  57.588 36.238  1.00 140.10 ? 100 GLY A CA  1 
ATOM   721  C C   . GLY A 1 94  ? 63.847  56.832 35.923  1.00 142.04 ? 100 GLY A C   1 
ATOM   722  O O   . GLY A 1 94  ? 63.764  56.252 34.825  1.00 141.92 ? 100 GLY A O   1 
ATOM   723  N N   . ASP A 1 95  ? 62.884  56.846 36.850  1.00 128.80 ? 101 ASP A N   1 
ATOM   724  C CA  . ASP A 1 95  ? 61.575  56.178 36.630  1.00 140.59 ? 101 ASP A CA  1 
ATOM   725  C C   . ASP A 1 95  ? 60.463  57.147 37.031  1.00 140.73 ? 101 ASP A C   1 
ATOM   726  O O   . ASP A 1 95  ? 60.741  58.045 37.844  1.00 145.15 ? 101 ASP A O   1 
ATOM   727  C CB  . ASP A 1 95  ? 61.472  54.879 37.427  1.00 153.10 ? 101 ASP A CB  1 
ATOM   728  C CG  . ASP A 1 95  ? 62.060  53.674 36.715  1.00 162.99 ? 101 ASP A CG  1 
ATOM   729  O OD1 . ASP A 1 95  ? 62.523  53.838 35.571  1.00 161.10 ? 101 ASP A OD1 1 
ATOM   730  O OD2 . ASP A 1 95  ? 62.052  52.582 37.313  1.00 167.12 ? 101 ASP A OD2 1 
ATOM   731  N N   . PHE A 1 96  ? 59.257  56.962 36.487  1.00 143.64 ? 102 PHE A N   1 
ATOM   732  C CA  . PHE A 1 96  ? 58.127  57.874 36.799  1.00 141.62 ? 102 PHE A CA  1 
ATOM   733  C C   . PHE A 1 96  ? 57.169  57.184 37.775  1.00 150.94 ? 102 PHE A C   1 
ATOM   734  O O   . PHE A 1 96  ? 56.650  56.099 37.454  1.00 154.39 ? 102 PHE A O   1 
ATOM   735  C CB  . PHE A 1 96  ? 57.399  58.301 35.523  1.00 136.88 ? 102 PHE A CB  1 
ATOM   736  C CG  . PHE A 1 96  ? 56.806  59.686 35.569  1.00 131.28 ? 102 PHE A CG  1 
ATOM   737  C CD1 . PHE A 1 96  ? 55.889  60.036 36.545  1.00 132.39 ? 102 PHE A CD1 1 
ATOM   738  C CD2 . PHE A 1 96  ? 57.165  60.640 34.632  1.00 119.85 ? 102 PHE A CD2 1 
ATOM   739  C CE1 . PHE A 1 96  ? 55.352  61.312 36.589  1.00 141.70 ? 102 PHE A CE1 1 
ATOM   740  C CE2 . PHE A 1 96  ? 56.625  61.914 34.675  1.00 118.51 ? 102 PHE A CE2 1 
ATOM   741  C CZ  . PHE A 1 96  ? 55.720  62.248 35.652  1.00 136.54 ? 102 PHE A CZ  1 
ATOM   742  N N   . ASN A 1 97  ? 56.942  57.806 38.934  1.00 143.80 ? 103 ASN A N   1 
ATOM   743  C CA  . ASN A 1 97  ? 56.035  57.216 39.949  1.00 150.60 ? 103 ASN A CA  1 
ATOM   744  C C   . ASN A 1 97  ? 54.627  57.116 39.356  1.00 151.06 ? 103 ASN A C   1 
ATOM   745  O O   . ASN A 1 97  ? 54.198  58.070 38.690  1.00 147.56 ? 103 ASN A O   1 
ATOM   746  C CB  . ASN A 1 97  ? 56.059  58.019 41.249  1.00 141.22 ? 103 ASN A CB  1 
ATOM   747  C CG  . ASN A 1 97  ? 55.191  57.410 42.330  1.00 148.06 ? 103 ASN A CG  1 
ATOM   748  O OD1 . ASN A 1 97  ? 55.326  56.232 42.651  1.00 179.77 ? 103 ASN A OD1 1 
ATOM   749  N ND2 . ASN A 1 97  ? 54.287  58.200 42.885  1.00 143.95 ? 103 ASN A ND2 1 
ATOM   750  N N   . ASP A 1 98  ? 53.950  55.991 39.583  1.00 143.11 ? 104 ASP A N   1 
ATOM   751  C CA  . ASP A 1 98  ? 52.562  55.821 39.086  1.00 152.55 ? 104 ASP A CA  1 
ATOM   752  C C   . ASP A 1 98  ? 52.524  56.212 37.610  1.00 145.94 ? 104 ASP A C   1 
ATOM   753  O O   . ASP A 1 98  ? 51.617  56.970 37.223  1.00 139.42 ? 104 ASP A O   1 
ATOM   754  C CB  . ASP A 1 98  ? 51.579  56.654 39.906  1.00 153.62 ? 104 ASP A CB  1 
ATOM   755  C CG  . ASP A 1 98  ? 51.748  56.473 41.403  1.00 161.44 ? 104 ASP A CG  1 
ATOM   756  O OD1 . ASP A 1 98  ? 51.684  55.316 41.858  1.00 182.53 ? 104 ASP A OD1 1 
ATOM   757  O OD2 . ASP A 1 98  ? 51.929  57.487 42.099  1.00 158.84 ? 104 ASP A OD2 1 
ATOM   758  N N   . TYR A 1 99  ? 53.464  55.699 36.822  1.00 145.50 ? 105 TYR A N   1 
ATOM   759  C CA  . TYR A 1 99  ? 53.549  56.098 35.397  1.00 145.02 ? 105 TYR A CA  1 
ATOM   760  C C   . TYR A 1 99  ? 52.275  55.691 34.658  1.00 147.72 ? 105 TYR A C   1 
ATOM   761  O O   . TYR A 1 99  ? 51.743  56.513 33.889  1.00 143.64 ? 105 TYR A O   1 
ATOM   762  C CB  . TYR A 1 99  ? 54.775  55.458 34.747  1.00 138.25 ? 105 TYR A CB  1 
ATOM   763  C CG  . TYR A 1 99  ? 54.991  55.841 33.306  1.00 130.74 ? 105 TYR A CG  1 
ATOM   764  C CD1 . TYR A 1 99  ? 55.042  57.170 32.923  1.00 134.61 ? 105 TYR A CD1 1 
ATOM   765  C CD2 . TYR A 1 99  ? 55.172  54.877 32.330  1.00 126.45 ? 105 TYR A CD2 1 
ATOM   766  C CE1 . TYR A 1 99  ? 55.245  57.533 31.603  1.00 127.83 ? 105 TYR A CE1 1 
ATOM   767  C CE2 . TYR A 1 99  ? 55.382  55.224 31.007  1.00 126.08 ? 105 TYR A CE2 1 
ATOM   768  C CZ  . TYR A 1 99  ? 55.417  56.556 30.641  1.00 125.05 ? 105 TYR A CZ  1 
ATOM   769  O OH  . TYR A 1 99  ? 55.623  56.894 29.326  1.00 112.83 ? 105 TYR A OH  1 
ATOM   770  N N   . GLU A 1 100 ? 51.791  54.471 34.890  1.00 153.04 ? 106 GLU A N   1 
ATOM   771  C CA  . GLU A 1 100 ? 50.627  53.977 34.101  1.00 155.90 ? 106 GLU A CA  1 
ATOM   772  C C   . GLU A 1 100 ? 49.336  54.668 34.555  1.00 160.87 ? 106 GLU A C   1 
ATOM   773  O O   . GLU A 1 100 ? 48.430  54.820 33.719  1.00 156.19 ? 106 GLU A O   1 
ATOM   774  C CB  . GLU A 1 100 ? 50.566  52.449 34.164  1.00 158.49 ? 106 GLU A CB  1 
ATOM   775  C CG  . GLU A 1 100 ? 51.779  51.802 33.517  1.00 151.79 ? 106 GLU A CG  1 
ATOM   776  C CD  . GLU A 1 100 ? 51.468  50.729 32.489  1.00 146.34 ? 106 GLU A CD  1 
ATOM   777  O OE1 . GLU A 1 100 ? 50.280  50.386 32.337  1.00 154.71 ? 106 GLU A OE1 1 
ATOM   778  O OE2 . GLU A 1 100 ? 52.414  50.255 31.826  1.00 136.18 ? 106 GLU A OE2 1 
ATOM   779  N N   . GLU A 1 101 ? 49.258  55.075 35.823  1.00 158.02 ? 107 GLU A N   1 
ATOM   780  C CA  . GLU A 1 101 ? 48.061  55.822 36.282  1.00 158.21 ? 107 GLU A CA  1 
ATOM   781  C C   . GLU A 1 101 ? 47.950  57.092 35.443  1.00 145.18 ? 107 GLU A C   1 
ATOM   782  O O   . GLU A 1 101 ? 46.851  57.376 34.934  1.00 137.44 ? 107 GLU A O   1 
ATOM   783  C CB  . GLU A 1 101 ? 48.192  56.193 37.756  1.00 170.01 ? 107 GLU A CB  1 
ATOM   784  C CG  . GLU A 1 101 ? 48.353  54.997 38.671  1.00 193.02 ? 107 GLU A CG  1 
ATOM   785  C CD  . GLU A 1 101 ? 48.331  55.359 40.145  1.00 202.35 ? 107 GLU A CD  1 
ATOM   786  O OE1 . GLU A 1 101 ? 48.162  56.557 40.452  1.00 187.79 ? 107 GLU A OE1 1 
ATOM   787  O OE2 . GLU A 1 101 ? 48.490  54.449 40.982  1.00 220.92 ? 107 GLU A OE2 1 
ATOM   788  N N   . LEU A 1 102 ? 49.064  57.809 35.299  1.00 143.37 ? 108 LEU A N   1 
ATOM   789  C CA  . LEU A 1 102 ? 49.061  59.029 34.459  1.00 138.64 ? 108 LEU A CA  1 
ATOM   790  C C   . LEU A 1 102 ? 48.560  58.623 33.080  1.00 135.19 ? 108 LEU A C   1 
ATOM   791  O O   . LEU A 1 102 ? 47.687  59.315 32.538  1.00 134.81 ? 108 LEU A O   1 
ATOM   792  C CB  . LEU A 1 102 ? 50.487  59.562 34.367  1.00 130.15 ? 108 LEU A CB  1 
ATOM   793  C CG  . LEU A 1 102 ? 50.710  60.930 35.003  1.00 135.23 ? 108 LEU A CG  1 
ATOM   794  C CD1 . LEU A 1 102 ? 52.123  61.423 34.734  1.00 136.96 ? 108 LEU A CD1 1 
ATOM   795  C CD2 . LEU A 1 102 ? 49.689  61.930 34.492  1.00 135.07 ? 108 LEU A CD2 1 
ATOM   796  N N   . LYS A 1 103 ? 49.079  57.511 32.567  1.00 133.24 ? 109 LYS A N   1 
ATOM   797  C CA  . LYS A 1 103 ? 48.669  57.041 31.224  1.00 134.84 ? 109 LYS A CA  1 
ATOM   798  C C   . LYS A 1 103 ? 47.151  56.876 31.193  1.00 142.21 ? 109 LYS A C   1 
ATOM   799  O O   . LYS A 1 103 ? 46.536  57.268 30.186  1.00 140.66 ? 109 LYS A O   1 
ATOM   800  C CB  . LYS A 1 103 ? 49.340  55.704 30.915  1.00 135.88 ? 109 LYS A CB  1 
ATOM   801  C CG  . LYS A 1 103 ? 50.818  55.780 30.563  1.00 140.12 ? 109 LYS A CG  1 
ATOM   802  C CD  . LYS A 1 103 ? 51.391  54.437 30.174  1.00 139.94 ? 109 LYS A CD  1 
ATOM   803  C CE  . LYS A 1 103 ? 52.568  54.544 29.228  1.00 138.64 ? 109 LYS A CE  1 
ATOM   804  N NZ  . LYS A 1 103 ? 53.113  53.211 28.880  1.00 141.18 ? 109 LYS A NZ  1 
ATOM   805  N N   . HIS A 1 104 ? 46.576  56.309 32.252  1.00 145.35 ? 110 HIS A N   1 
ATOM   806  C CA  . HIS A 1 104 ? 45.116  56.034 32.246  1.00 145.55 ? 110 HIS A CA  1 
ATOM   807  C C   . HIS A 1 104 ? 44.334  57.348 32.213  1.00 137.74 ? 110 HIS A C   1 
ATOM   808  O O   . HIS A 1 104 ? 43.337  57.465 31.474  1.00 142.78 ? 110 HIS A O   1 
ATOM   809  C CB  . HIS A 1 104 ? 44.720  55.194 33.462  1.00 161.29 ? 110 HIS A CB  1 
ATOM   810  C CG  . HIS A 1 104 ? 45.285  53.814 33.453  1.00 176.28 ? 110 HIS A CG  1 
ATOM   811  N ND1 . HIS A 1 104 ? 46.080  53.329 34.468  1.00 190.45 ? 110 HIS A ND1 1 
ATOM   812  C CD2 . HIS A 1 104 ? 45.161  52.818 32.569  1.00 210.87 ? 110 HIS A CD2 1 
ATOM   813  C CE1 . HIS A 1 104 ? 46.427  52.081 34.191  1.00 197.69 ? 110 HIS A CE1 1 
ATOM   814  N NE2 . HIS A 1 104 ? 45.880  51.750 33.043  1.00 197.93 ? 110 HIS A NE2 1 
ATOM   815  N N   . LEU A 1 105 ? 44.771  58.324 33.006  1.00 142.21 ? 111 LEU A N   1 
ATOM   816  C CA  . LEU A 1 105 ? 44.087  59.641 32.988  1.00 137.02 ? 111 LEU A CA  1 
ATOM   817  C C   . LEU A 1 105 ? 44.159  60.196 31.565  1.00 134.05 ? 111 LEU A C   1 
ATOM   818  O O   . LEU A 1 105 ? 43.152  60.748 31.089  1.00 133.29 ? 111 LEU A O   1 
ATOM   819  C CB  . LEU A 1 105 ? 44.775  60.577 33.980  1.00 140.14 ? 111 LEU A CB  1 
ATOM   820  C CG  . LEU A 1 105 ? 44.829  60.072 35.421  1.00 142.47 ? 111 LEU A CG  1 
ATOM   821  C CD1 . LEU A 1 105 ? 45.140  61.210 36.380  1.00 141.63 ? 111 LEU A CD1 1 
ATOM   822  C CD2 . LEU A 1 105 ? 43.524  59.396 35.808  1.00 143.90 ? 111 LEU A CD2 1 
ATOM   823  N N   . LEU A 1 106 ? 45.303  60.018 30.908  1.00 137.13 ? 112 LEU A N   1 
ATOM   824  C CA  . LEU A 1 106 ? 45.480  60.545 29.533  1.00 129.35 ? 112 LEU A CA  1 
ATOM   825  C C   . LEU A 1 106 ? 44.443  59.902 28.613  1.00 126.90 ? 112 LEU A C   1 
ATOM   826  O O   . LEU A 1 106 ? 44.100  60.516 27.595  1.00 126.68 ? 112 LEU A O   1 
ATOM   827  C CB  . LEU A 1 106 ? 46.895  60.219 29.056  1.00 132.64 ? 112 LEU A CB  1 
ATOM   828  C CG  . LEU A 1 106 ? 48.025  60.829 29.881  1.00 133.29 ? 112 LEU A CG  1 
ATOM   829  C CD1 . LEU A 1 106 ? 49.362  60.633 29.191  1.00 136.15 ? 112 LEU A CD1 1 
ATOM   830  C CD2 . LEU A 1 106 ? 47.773  62.304 30.141  1.00 134.09 ? 112 LEU A CD2 1 
ATOM   831  N N   . SER A 1 107 ? 43.971  58.707 28.962  1.00 128.44 ? 113 SER A N   1 
ATOM   832  C CA  . SER A 1 107 ? 42.914  58.078 28.137  1.00 135.54 ? 113 SER A CA  1 
ATOM   833  C C   . SER A 1 107 ? 41.720  59.029 28.067  1.00 135.30 ? 113 SER A C   1 
ATOM   834  O O   . SER A 1 107 ? 41.168  59.217 26.980  1.00 136.79 ? 113 SER A O   1 
ATOM   835  C CB  . SER A 1 107 ? 42.498  56.755 28.689  1.00 136.39 ? 113 SER A CB  1 
ATOM   836  O OG  . SER A 1 107 ? 41.562  56.930 29.740  1.00 148.95 ? 113 SER A OG  1 
ATOM   837  N N   . ARG A 1 108 ? 41.349  59.621 29.198  1.00 145.50 ? 114 ARG A N   1 
ATOM   838  C CA  . ARG A 1 108 ? 40.233  60.604 29.176  1.00 143.94 ? 114 ARG A CA  1 
ATOM   839  C C   . ARG A 1 108 ? 40.693  61.925 28.545  1.00 147.32 ? 114 ARG A C   1 
ATOM   840  O O   . ARG A 1 108 ? 39.983  62.427 27.662  1.00 147.52 ? 114 ARG A O   1 
ATOM   841  C CB  . ARG A 1 108 ? 39.687  60.799 30.592  1.00 145.43 ? 114 ARG A CB  1 
ATOM   842  C CG  . ARG A 1 108 ? 39.061  59.540 31.171  1.00 146.25 ? 114 ARG A CG  1 
ATOM   843  C CD  . ARG A 1 108 ? 38.332  59.782 32.478  1.00 153.16 ? 114 ARG A CD  1 
ATOM   844  N NE  . ARG A 1 108 ? 39.252  60.097 33.559  1.00 155.86 ? 114 ARG A NE  1 
ATOM   845  C CZ  . ARG A 1 108 ? 39.401  59.360 34.652  1.00 158.65 ? 114 ARG A CZ  1 
ATOM   846  N NH1 . ARG A 1 108 ? 38.713  58.241 34.792  1.00 171.65 ? 114 ARG A NH1 1 
ATOM   847  N NH2 . ARG A 1 108 ? 40.239  59.741 35.600  1.00 153.61 ? 114 ARG A NH2 1 
ATOM   848  N N   . ILE A 1 109 ? 41.853  62.450 28.943  1.00 132.17 ? 115 ILE A N   1 
ATOM   849  C CA  . ILE A 1 109 ? 42.287  63.791 28.450  1.00 129.35 ? 115 ILE A CA  1 
ATOM   850  C C   . ILE A 1 109 ? 42.510  63.754 26.935  1.00 128.82 ? 115 ILE A C   1 
ATOM   851  O O   . ILE A 1 109 ? 42.882  62.690 26.420  1.00 128.97 ? 115 ILE A O   1 
ATOM   852  C CB  . ILE A 1 109 ? 43.539  64.242 29.221  1.00 127.35 ? 115 ILE A CB  1 
ATOM   853  C CG1 . ILE A 1 109 ? 43.389  63.956 30.717  1.00 129.80 ? 115 ILE A CG1 1 
ATOM   854  C CG2 . ILE A 1 109 ? 43.847  65.705 28.953  1.00 132.98 ? 115 ILE A CG2 1 
ATOM   855  C CD1 . ILE A 1 109 ? 44.541  64.439 31.562  1.00 127.26 ? 115 ILE A CD1 1 
ATOM   856  N N   . ASN A 1 110 ? 42.276  64.880 26.253  1.00 129.90 ? 116 ASN A N   1 
ATOM   857  C CA  . ASN A 1 110 ? 42.454  64.951 24.777  1.00 135.83 ? 116 ASN A CA  1 
ATOM   858  C C   . ASN A 1 110 ? 43.294  66.174 24.387  1.00 141.23 ? 116 ASN A C   1 
ATOM   859  O O   . ASN A 1 110 ? 43.842  66.161 23.270  1.00 148.84 ? 116 ASN A O   1 
ATOM   860  C CB  . ASN A 1 110 ? 41.117  64.974 24.036  1.00 134.25 ? 116 ASN A CB  1 
ATOM   861  C CG  . ASN A 1 110 ? 40.826  63.686 23.301  1.00 140.30 ? 116 ASN A CG  1 
ATOM   862  O OD1 . ASN A 1 110 ? 41.572  63.296 22.407  1.00 148.38 ? 116 ASN A OD1 1 
ATOM   863  N ND2 . ASN A 1 110 ? 39.741  63.026 23.664  1.00 143.12 ? 116 ASN A ND2 1 
ATOM   864  N N   . HIS A 1 111 ? 43.378  67.192 25.251  1.00 151.17 ? 117 HIS A N   1 
ATOM   865  C CA  . HIS A 1 111 ? 44.255  68.363 24.958  1.00 155.87 ? 117 HIS A CA  1 
ATOM   866  C C   . HIS A 1 111 ? 44.768  68.983 26.263  1.00 155.75 ? 117 HIS A C   1 
ATOM   867  O O   . HIS A 1 111 ? 44.118  68.807 27.316  1.00 151.69 ? 117 HIS A O   1 
ATOM   868  C CB  . HIS A 1 111 ? 43.537  69.393 24.079  1.00 161.61 ? 117 HIS A CB  1 
ATOM   869  C CG  . HIS A 1 111 ? 44.349  70.611 23.800  1.00 160.79 ? 117 HIS A CG  1 
ATOM   870  N ND1 . HIS A 1 111 ? 45.618  70.563 23.265  1.00 159.33 ? 117 HIS A ND1 1 
ATOM   871  C CD2 . HIS A 1 111 ? 44.085  71.903 24.005  1.00 159.13 ? 117 HIS A CD2 1 
ATOM   872  C CE1 . HIS A 1 111 ? 46.085  71.796 23.139  1.00 162.06 ? 117 HIS A CE1 1 
ATOM   873  N NE2 . HIS A 1 111 ? 45.169  72.625 23.586  1.00 161.98 ? 117 HIS A NE2 1 
ATOM   874  N N   . PHE A 1 112 ? 45.894  69.699 26.194  1.00 160.51 ? 118 PHE A N   1 
ATOM   875  C CA  . PHE A 1 112 ? 46.515  70.273 27.414  1.00 153.72 ? 118 PHE A CA  1 
ATOM   876  C C   . PHE A 1 112 ? 46.925  71.724 27.169  1.00 151.79 ? 118 PHE A C   1 
ATOM   877  O O   . PHE A 1 112 ? 46.961  72.141 25.999  1.00 150.01 ? 118 PHE A O   1 
ATOM   878  C CB  . PHE A 1 112 ? 47.792  69.515 27.774  1.00 144.05 ? 118 PHE A CB  1 
ATOM   879  C CG  . PHE A 1 112 ? 47.613  68.188 28.463  1.00 144.50 ? 118 PHE A CG  1 
ATOM   880  C CD1 . PHE A 1 112 ? 47.020  68.109 29.711  1.00 138.49 ? 118 PHE A CD1 1 
ATOM   881  C CD2 . PHE A 1 112 ? 48.063  67.020 27.870  1.00 150.35 ? 118 PHE A CD2 1 
ATOM   882  C CE1 . PHE A 1 112 ? 46.874  66.887 30.348  1.00 143.00 ? 118 PHE A CE1 1 
ATOM   883  C CE2 . PHE A 1 112 ? 47.912  65.799 28.505  1.00 150.05 ? 118 PHE A CE2 1 
ATOM   884  C CZ  . PHE A 1 112 ? 47.319  65.736 29.743  1.00 150.12 ? 118 PHE A CZ  1 
ATOM   885  N N   . GLU A 1 113 ? 47.229  72.461 28.242  1.00 149.69 ? 119 GLU A N   1 
ATOM   886  C CA  . GLU A 1 113 ? 47.730  73.850 28.089  1.00 151.41 ? 119 GLU A CA  1 
ATOM   887  C C   . GLU A 1 113 ? 48.866  74.066 29.092  1.00 152.65 ? 119 GLU A C   1 
ATOM   888  O O   . GLU A 1 113 ? 48.585  74.080 30.301  1.00 156.93 ? 119 GLU A O   1 
ATOM   889  C CB  . GLU A 1 113 ? 46.609  74.859 28.325  1.00 149.24 ? 119 GLU A CB  1 
ATOM   890  C CG  . GLU A 1 113 ? 47.078  76.301 28.263  1.00 157.36 ? 119 GLU A CG  1 
ATOM   891  C CD  . GLU A 1 113 ? 45.985  77.326 28.511  1.00 164.05 ? 119 GLU A CD  1 
ATOM   892  O OE1 . GLU A 1 113 ? 44.827  76.913 28.713  1.00 169.70 ? 119 GLU A OE1 1 
ATOM   893  O OE2 . GLU A 1 113 ? 46.297  78.532 28.508  1.00 165.63 ? 119 GLU A OE2 1 
ATOM   894  N N   . LYS A 1 114 ? 50.100  74.223 28.610  1.00 148.92 ? 120 LYS A N   1 
ATOM   895  C CA  . LYS A 1 114 ? 51.225  74.514 29.533  1.00 145.05 ? 120 LYS A CA  1 
ATOM   896  C C   . LYS A 1 114 ? 50.933  75.837 30.240  1.00 152.52 ? 120 LYS A C   1 
ATOM   897  O O   . LYS A 1 114 ? 50.752  76.851 29.543  1.00 158.96 ? 120 LYS A O   1 
ATOM   898  C CB  . LYS A 1 114 ? 52.550  74.605 28.775  1.00 143.36 ? 120 LYS A CB  1 
ATOM   899  C CG  . LYS A 1 114 ? 53.225  73.275 28.469  1.00 141.83 ? 120 LYS A CG  1 
ATOM   900  C CD  . LYS A 1 114 ? 54.640  73.439 27.955  1.00 140.41 ? 120 LYS A CD  1 
ATOM   901  C CE  . LYS A 1 114 ? 55.373  72.127 27.776  1.00 147.04 ? 120 LYS A CE  1 
ATOM   902  N NZ  . LYS A 1 114 ? 56.809  72.338 27.477  1.00 143.11 ? 120 LYS A NZ  1 
ATOM   903  N N   . ILE A 1 115 ? 50.910  75.819 31.572  1.00 164.60 ? 121 ILE A N   1 
ATOM   904  C CA  . ILE A 1 115 ? 50.642  77.059 32.355  1.00 173.91 ? 121 ILE A CA  1 
ATOM   905  C C   . ILE A 1 115 ? 51.751  78.077 32.079  1.00 176.36 ? 121 ILE A C   1 
ATOM   906  O O   . ILE A 1 115 ? 51.417  79.274 31.999  1.00 185.44 ? 121 ILE A O   1 
ATOM   907  C CB  . ILE A 1 115 ? 50.523  76.750 33.860  1.00 179.79 ? 121 ILE A CB  1 
ATOM   908  C CG1 . ILE A 1 115 ? 49.986  77.947 34.640  1.00 178.64 ? 121 ILE A CG1 1 
ATOM   909  C CG2 . ILE A 1 115 ? 51.845  76.285 34.441  1.00 185.90 ? 121 ILE A CG2 1 
ATOM   910  C CD1 . ILE A 1 115 ? 48.571  78.309 34.303  1.00 196.05 ? 121 ILE A CD1 1 
ATOM   911  N N   . GLN A 1 116 ? 52.998  77.630 31.904  1.00 176.15 ? 122 GLN A N   1 
ATOM   912  C CA  . GLN A 1 116 ? 54.125  78.588 31.747  1.00 179.95 ? 122 GLN A CA  1 
ATOM   913  C C   . GLN A 1 116 ? 54.039  79.623 32.873  1.00 187.80 ? 122 GLN A C   1 
ATOM   914  O O   . GLN A 1 116 ? 54.565  80.737 32.686  1.00 192.55 ? 122 GLN A O   1 
ATOM   915  C CB  . GLN A 1 116 ? 54.064  79.273 30.380  1.00 182.21 ? 122 GLN A CB  1 
ATOM   916  C CG  . GLN A 1 116 ? 54.314  78.329 29.212  1.00 181.92 ? 122 GLN A CG  1 
ATOM   917  C CD  . GLN A 1 116 ? 54.177  79.016 27.877  1.00 185.31 ? 122 GLN A CD  1 
ATOM   918  O OE1 . GLN A 1 116 ? 53.482  80.021 27.743  1.00 186.48 ? 122 GLN A OE1 1 
ATOM   919  N NE2 . GLN A 1 116 ? 54.841  78.472 26.870  1.00 191.48 ? 122 GLN A NE2 1 
ATOM   920  N N   . ILE A 1 117 ? 53.409  79.270 33.999  1.00 187.87 ? 123 ILE A N   1 
ATOM   921  C CA  . ILE A 1 117 ? 53.251  80.229 35.138  1.00 197.31 ? 123 ILE A CA  1 
ATOM   922  C C   . ILE A 1 117 ? 53.914  79.646 36.394  1.00 196.87 ? 123 ILE A C   1 
ATOM   923  O O   . ILE A 1 117 ? 54.387  80.446 37.227  1.00 208.53 ? 123 ILE A O   1 
ATOM   924  C CB  . ILE A 1 117 ? 51.768  80.591 35.363  1.00 198.45 ? 123 ILE A CB  1 
ATOM   925  C CG1 . ILE A 1 117 ? 51.237  81.503 34.254  1.00 194.26 ? 123 ILE A CG1 1 
ATOM   926  C CG2 . ILE A 1 117 ? 51.544  81.203 36.738  1.00 196.19 ? 123 ILE A CG2 1 
ATOM   927  C CD1 . ILE A 1 117 ? 49.801  81.930 34.447  1.00 189.81 ? 123 ILE A CD1 1 
ATOM   928  N N   . ILE A 1 118 ? 53.984  78.315 36.513  1.00 175.38 ? 124 ILE A N   1 
ATOM   929  C CA  . ILE A 1 118 ? 54.709  77.712 37.672  1.00 177.85 ? 124 ILE A CA  1 
ATOM   930  C C   . ILE A 1 118 ? 55.939  78.586 37.921  1.00 180.53 ? 124 ILE A C   1 
ATOM   931  O O   . ILE A 1 118 ? 56.724  78.746 36.964  1.00 240.13 ? 124 ILE A O   1 
ATOM   932  C CB  . ILE A 1 118 ? 55.081  76.242 37.396  1.00 170.50 ? 124 ILE A CB  1 
ATOM   933  C CG1 . ILE A 1 118 ? 53.841  75.379 37.151  1.00 169.68 ? 124 ILE A CG1 1 
ATOM   934  C CG2 . ILE A 1 118 ? 55.941  75.675 38.514  1.00 161.03 ? 124 ILE A CG2 1 
ATOM   935  C CD1 . ILE A 1 118 ? 52.909  75.296 38.335  1.00 176.35 ? 124 ILE A CD1 1 
ATOM   936  N N   . PRO A 1 119 ? 56.208  79.075 39.154  1.00 190.49 ? 125 PRO A N   1 
ATOM   937  C CA  . PRO A 1 119 ? 57.281  80.037 39.424  1.00 192.72 ? 125 PRO A CA  1 
ATOM   938  C C   . PRO A 1 119 ? 57.987  80.516 38.147  1.00 190.78 ? 125 PRO A C   1 
ATOM   939  O O   . PRO A 1 119 ? 57.354  81.269 37.422  1.00 198.49 ? 125 PRO A O   1 
ATOM   940  C CB  . PRO A 1 119 ? 58.118  79.150 40.353  1.00 183.72 ? 125 PRO A CB  1 
ATOM   941  C CG  . PRO A 1 119 ? 57.055  78.451 41.204  1.00 182.47 ? 125 PRO A CG  1 
ATOM   942  C CD  . PRO A 1 119 ? 55.746  78.556 40.436  1.00 190.75 ? 125 PRO A CD  1 
ATOM   943  N N   . LYS A 1 120 a 59.246  80.113 37.929  1.00 174.13 ? 125 LYS A N   1 
ATOM   944  C CA  . LYS A 1 120 a 60.001  80.479 36.697  1.00 177.40 ? 125 LYS A CA  1 
ATOM   945  C C   . LYS A 1 120 a 61.491  80.204 36.914  1.00 174.13 ? 125 LYS A C   1 
ATOM   946  O O   . LYS A 1 120 a 61.878  79.939 38.069  1.00 175.62 ? 125 LYS A O   1 
ATOM   947  C CB  . LYS A 1 120 a 59.827  81.957 36.331  1.00 179.09 ? 125 LYS A CB  1 
ATOM   948  C CG  . LYS A 1 120 a 60.042  82.299 34.863  1.00 185.76 ? 125 LYS A CG  1 
ATOM   949  C CD  . LYS A 1 120 a 59.347  81.342 33.915  1.00 184.89 ? 125 LYS A CD  1 
ATOM   950  C CE  . LYS A 1 120 a 57.842  81.309 34.077  1.00 189.88 ? 125 LYS A CE  1 
ATOM   951  N NZ  . LYS A 1 120 a 57.233  80.214 33.287  1.00 189.89 ? 125 LYS A NZ  1 
ATOM   952  N N   . SER A 1 121 b 62.290  80.273 35.846  1.00 185.85 ? 125 SER A N   1 
ATOM   953  C CA  . SER A 1 121 b 63.759  80.108 35.986  1.00 184.75 ? 125 SER A CA  1 
ATOM   954  C C   . SER A 1 121 b 64.354  81.413 36.523  1.00 185.72 ? 125 SER A C   1 
ATOM   955  O O   . SER A 1 121 b 65.372  81.348 37.238  1.00 193.19 ? 125 SER A O   1 
ATOM   956  C CB  . SER A 1 121 b 64.388  79.716 34.677  1.00 200.92 ? 125 SER A CB  1 
ATOM   957  O OG  . SER A 1 121 b 64.125  80.693 33.681  1.00 186.63 ? 125 SER A OG  1 
ATOM   958  N N   . SER A 1 122 ? 63.731  82.551 36.195  1.00 182.88 ? 126 SER A N   1 
ATOM   959  C CA  . SER A 1 122 ? 64.219  83.852 36.711  1.00 184.92 ? 126 SER A CA  1 
ATOM   960  C C   . SER A 1 122 ? 64.362  83.758 38.231  1.00 184.75 ? 126 SER A C   1 
ATOM   961  O O   . SER A 1 122 ? 65.425  84.143 38.749  1.00 189.34 ? 126 SER A O   1 
ATOM   962  C CB  . SER A 1 122 ? 63.284  84.959 36.316  1.00 182.20 ? 126 SER A CB  1 
ATOM   963  O OG  . SER A 1 122 ? 62.024  84.798 36.946  1.00 183.06 ? 126 SER A OG  1 
ATOM   964  N N   . TRP A 1 123 ? 63.348  83.211 38.906  1.00 187.86 ? 127 TRP A N   1 
ATOM   965  C CA  . TRP A 1 123 ? 63.478  83.001 40.370  1.00 186.32 ? 127 TRP A CA  1 
ATOM   966  C C   . TRP A 1 123 ? 64.900  82.452 40.492  1.00 190.48 ? 127 TRP A C   1 
ATOM   967  O O   . TRP A 1 123 ? 65.204  81.444 39.827  1.00 194.01 ? 127 TRP A O   1 
ATOM   968  C CB  . TRP A 1 123 ? 62.337  82.138 40.918  1.00 184.63 ? 127 TRP A CB  1 
ATOM   969  C CG  . TRP A 1 123 ? 62.745  81.288 42.082  1.00 193.84 ? 127 TRP A CG  1 
ATOM   970  C CD1 . TRP A 1 123 ? 63.343  81.704 43.237  1.00 198.02 ? 127 TRP A CD1 1 
ATOM   971  C CD2 . TRP A 1 123 ? 62.591  79.863 42.206  1.00 212.73 ? 127 TRP A CD2 1 
ATOM   972  N NE1 . TRP A 1 123 ? 63.573  80.640 44.065  1.00 204.74 ? 127 TRP A NE1 1 
ATOM   973  C CE2 . TRP A 1 123 ? 63.119  79.497 43.462  1.00 213.46 ? 127 TRP A CE2 1 
ATOM   974  C CE3 . TRP A 1 123 ? 62.057  78.864 41.384  1.00 189.24 ? 127 TRP A CE3 1 
ATOM   975  C CZ2 . TRP A 1 123 ? 63.124  78.179 43.913  1.00 202.99 ? 127 TRP A CZ2 1 
ATOM   976  C CZ3 . TRP A 1 123 ? 62.065  77.561 41.829  1.00 182.90 ? 127 TRP A CZ3 1 
ATOM   977  C CH2 . TRP A 1 123 ? 62.591  77.226 43.076  1.00 190.91 ? 127 TRP A CH2 1 
ATOM   978  N N   . SER A 1 124 ? 65.742  83.112 41.286  1.00 196.89 ? 128 SER A N   1 
ATOM   979  C CA  . SER A 1 124 ? 67.123  82.620 41.514  1.00 197.30 ? 128 SER A CA  1 
ATOM   980  C C   . SER A 1 124 ? 67.455  83.070 42.935  1.00 196.71 ? 128 SER A C   1 
ATOM   981  O O   . SER A 1 124 ? 68.645  83.281 43.230  1.00 197.61 ? 128 SER A O   1 
ATOM   982  C CB  . SER A 1 124 ? 68.168  83.073 40.536  1.00 199.10 ? 128 SER A CB  1 
ATOM   983  O OG  . SER A 1 124 ? 69.417  82.458 40.814  1.00 201.32 ? 128 SER A OG  1 
ATOM   984  N N   . SER A 1 125 ? 66.432  83.216 43.776  1.00 177.64 ? 129 SER A N   1 
ATOM   985  C CA  . SER A 1 125 ? 66.662  83.739 45.144  1.00 181.51 ? 129 SER A CA  1 
ATOM   986  C C   . SER A 1 125 ? 67.623  82.830 45.912  1.00 192.18 ? 129 SER A C   1 
ATOM   987  O O   . SER A 1 125 ? 68.592  83.361 46.484  1.00 186.16 ? 129 SER A O   1 
ATOM   988  C CB  . SER A 1 125 ? 65.354  83.880 45.868  1.00 180.68 ? 129 SER A CB  1 
ATOM   989  O OG  . SER A 1 125 ? 64.716  82.619 45.999  1.00 166.95 ? 129 SER A OG  1 
ATOM   990  N N   . HIS A 1 126 ? 67.383  81.516 45.909  1.00 178.90 ? 130 HIS A N   1 
ATOM   991  C CA  . HIS A 1 126 ? 68.214  80.606 46.742  1.00 185.17 ? 130 HIS A CA  1 
ATOM   992  C C   . HIS A 1 126 ? 68.996  79.602 45.898  1.00 191.86 ? 130 HIS A C   1 
ATOM   993  O O   . HIS A 1 126 ? 69.908  78.941 46.434  1.00 194.88 ? 130 HIS A O   1 
ATOM   994  C CB  . HIS A 1 126 ? 67.333  79.772 47.673  1.00 187.30 ? 130 HIS A CB  1 
ATOM   995  C CG  . HIS A 1 126 ? 67.362  78.312 47.356  1.00 189.13 ? 130 HIS A CG  1 
ATOM   996  N ND1 . HIS A 1 126 ? 68.040  77.412 48.147  1.00 190.33 ? 130 HIS A ND1 1 
ATOM   997  C CD2 . HIS A 1 126 ? 66.865  77.600 46.333  1.00 190.43 ? 130 HIS A CD2 1 
ATOM   998  C CE1 . HIS A 1 126 ? 67.926  76.198 47.629  1.00 190.28 ? 130 HIS A CE1 1 
ATOM   999  N NE2 . HIS A 1 126 ? 67.215  76.289 46.527  1.00 190.47 ? 130 HIS A NE2 1 
ATOM   1000 N N   . GLU A 1 127 ? 68.646  79.456 44.623  1.00 182.91 ? 131 GLU A N   1 
ATOM   1001 C CA  . GLU A 1 127 ? 69.308  78.388 43.835  1.00 176.17 ? 131 GLU A CA  1 
ATOM   1002 C C   . GLU A 1 127 ? 69.864  78.942 42.527  1.00 164.81 ? 131 GLU A C   1 
ATOM   1003 O O   . GLU A 1 127 ? 69.573  80.110 42.206  1.00 153.47 ? 131 GLU A O   1 
ATOM   1004 C CB  . GLU A 1 127 ? 68.299  77.293 43.497  1.00 183.14 ? 131 GLU A CB  1 
ATOM   1005 C CG  . GLU A 1 127 ? 67.552  77.550 42.199  1.00 203.11 ? 131 GLU A CG  1 
ATOM   1006 C CD  . GLU A 1 127 ? 66.427  78.571 42.249  1.00 266.56 ? 131 GLU A CD  1 
ATOM   1007 O OE1 . GLU A 1 127 ? 66.657  79.689 42.749  1.00 323.29 ? 131 GLU A OE1 1 
ATOM   1008 O OE2 . GLU A 1 127 ? 65.334  78.258 41.745  1.00 306.27 ? 131 GLU A OE2 1 
ATOM   1009 N N   . ALA A 1 128 ? 70.642  78.126 41.811  1.00 167.24 ? 132 ALA A N   1 
ATOM   1010 C CA  . ALA A 1 128 ? 71.129  78.554 40.484  1.00 153.39 ? 132 ALA A CA  1 
ATOM   1011 C C   . ALA A 1 128 ? 70.252  77.894 39.418  1.00 139.15 ? 132 ALA A C   1 
ATOM   1012 O O   . ALA A 1 128 ? 70.094  76.661 39.462  1.00 145.27 ? 132 ALA A O   1 
ATOM   1013 C CB  . ALA A 1 128 ? 72.581  78.193 40.321  1.00 146.61 ? 132 ALA A CB  1 
ATOM   1014 N N   . SER A 1 129 ? 69.681  78.697 38.522  1.00 142.91 ? 133 SER A N   1 
ATOM   1015 C CA  . SER A 1 129 ? 68.854  78.153 37.419  1.00 139.61 ? 133 SER A CA  1 
ATOM   1016 C C   . SER A 1 129 ? 69.766  77.862 36.227  1.00 131.28 ? 133 SER A C   1 
ATOM   1017 O O   . SER A 1 129 ? 69.469  78.376 35.127  1.00 163.47 ? 133 SER A O   1 
ATOM   1018 C CB  . SER A 1 129 ? 67.771  79.118 37.065  1.00 152.88 ? 133 SER A CB  1 
ATOM   1019 O OG  . SER A 1 129 ? 68.322  80.379 36.715  1.00 155.08 ? 133 SER A OG  1 
ATOM   1020 N N   . LEU A 1 130 a 70.839  77.098 36.452  1.00 133.54 ? 133 LEU A N   1 
ATOM   1021 C CA  . LEU A 1 130 a 71.805  76.726 35.389  1.00 130.59 ? 133 LEU A CA  1 
ATOM   1022 C C   . LEU A 1 130 a 72.455  75.397 35.788  1.00 129.86 ? 133 LEU A C   1 
ATOM   1023 O O   . LEU A 1 130 a 73.641  75.407 36.168  1.00 119.18 ? 133 LEU A O   1 
ATOM   1024 C CB  . LEU A 1 130 a 72.843  77.842 35.265  1.00 130.72 ? 133 LEU A CB  1 
ATOM   1025 C CG  . LEU A 1 130 a 73.690  77.824 33.994  1.00 134.95 ? 133 LEU A CG  1 
ATOM   1026 C CD1 . LEU A 1 130 a 72.862  78.249 32.789  1.00 127.86 ? 133 LEU A CD1 1 
ATOM   1027 C CD2 . LEU A 1 130 a 74.900  78.731 34.151  1.00 126.61 ? 133 LEU A CD2 1 
ATOM   1028 N N   . GLY A 1 131 ? 71.691  74.305 35.718  1.00 134.50 ? 134 GLY A N   1 
ATOM   1029 C CA  . GLY A 1 131 ? 72.221  72.984 36.102  1.00 138.49 ? 134 GLY A CA  1 
ATOM   1030 C C   . GLY A 1 131 ? 72.046  71.942 35.013  1.00 144.75 ? 134 GLY A C   1 
ATOM   1031 O O   . GLY A 1 131 ? 71.855  70.768 35.357  1.00 146.97 ? 134 GLY A O   1 
ATOM   1032 N N   . VAL A 1 132 ? 72.158  72.338 33.744  1.00 149.79 ? 135 VAL A N   1 
ATOM   1033 C CA  . VAL A 1 132 ? 71.934  71.386 32.617  1.00 143.51 ? 135 VAL A CA  1 
ATOM   1034 C C   . VAL A 1 132 ? 72.864  70.186 32.800  1.00 139.74 ? 135 VAL A C   1 
ATOM   1035 O O   . VAL A 1 132 ? 73.934  70.348 33.411  1.00 134.35 ? 135 VAL A O   1 
ATOM   1036 C CB  . VAL A 1 132 ? 72.150  72.066 31.256  1.00 139.32 ? 135 VAL A CB  1 
ATOM   1037 C CG1 . VAL A 1 132 ? 70.900  72.795 30.791  1.00 137.29 ? 135 VAL A CG1 1 
ATOM   1038 C CG2 . VAL A 1 132 ? 73.341  73.008 31.290  1.00 141.41 ? 135 VAL A CG2 1 
ATOM   1039 N N   . SER A 1 133 ? 72.476  69.028 32.266  1.00 140.72 ? 136 SER A N   1 
ATOM   1040 C CA  . SER A 1 133 ? 73.279  67.799 32.495  1.00 137.78 ? 136 SER A CA  1 
ATOM   1041 C C   . SER A 1 133 ? 73.991  67.376 31.211  1.00 136.87 ? 136 SER A C   1 
ATOM   1042 O O   . SER A 1 133 ? 73.522  67.758 30.126  1.00 139.56 ? 136 SER A O   1 
ATOM   1043 C CB  . SER A 1 133 ? 72.423  66.686 33.015  1.00 141.89 ? 136 SER A CB  1 
ATOM   1044 O OG  . SER A 1 133 ? 71.463  66.296 32.041  1.00 154.79 ? 136 SER A OG  1 
ATOM   1045 N N   . SER A 1 134 ? 75.056  66.578 31.338  1.00 136.01 ? 137 SER A N   1 
ATOM   1046 C CA  . SER A 1 134 ? 75.771  66.039 30.141  1.00 131.80 ? 137 SER A CA  1 
ATOM   1047 C C   . SER A 1 134 ? 74.940  65.003 29.410  1.00 130.43 ? 137 SER A C   1 
ATOM   1048 O O   . SER A 1 134 ? 75.409  64.500 28.371  1.00 116.42 ? 137 SER A O   1 
ATOM   1049 C CB  . SER A 1 134 ? 77.015  65.312 30.548  1.00 131.08 ? 137 SER A CB  1 
ATOM   1050 O OG  . SER A 1 134 ? 76.689  64.208 31.381  1.00 136.14 ? 137 SER A OG  1 
ATOM   1051 N N   . ALA A 1 135 ? 73.751  64.685 29.935  1.00 136.85 ? 138 ALA A N   1 
ATOM   1052 C CA  . ALA A 1 135 ? 72.859  63.673 29.284  1.00 139.46 ? 138 ALA A CA  1 
ATOM   1053 C C   . ALA A 1 135 ? 71.732  64.558 28.718  1.00 148.18 ? 138 ALA A C   1 
ATOM   1054 O O   . ALA A 1 135 ? 71.959  65.768 28.521  1.00 146.96 ? 138 ALA A O   1 
ATOM   1055 C CB  . ALA A 1 135 ? 72.325  62.641 30.225  1.00 142.60 ? 138 ALA A CB  1 
ATOM   1056 N N   . CYS A 1 136 ? 70.567  63.953 28.461  1.00 167.97 ? 139 CYS A N   1 
ATOM   1057 C CA  . CYS A 1 136 ? 69.426  64.708 27.879  1.00 166.44 ? 139 CYS A CA  1 
ATOM   1058 C C   . CYS A 1 136 ? 69.960  65.625 26.784  1.00 174.11 ? 139 CYS A C   1 
ATOM   1059 O O   . CYS A 1 136 ? 69.825  66.853 26.925  1.00 175.68 ? 139 CYS A O   1 
ATOM   1060 C CB  . CYS A 1 136 ? 68.756  65.540 28.961  1.00 159.85 ? 139 CYS A CB  1 
ATOM   1061 S SG  . CYS A 1 136 ? 68.255  64.523 30.369  1.00 157.19 ? 139 CYS A SG  1 
ATOM   1062 N N   . PRO A 1 137 ? 70.562  65.096 25.699  1.00 167.56 ? 140 PRO A N   1 
ATOM   1063 C CA  . PRO A 1 137 ? 71.201  65.970 24.712  1.00 171.39 ? 140 PRO A CA  1 
ATOM   1064 C C   . PRO A 1 137 ? 70.178  66.593 23.752  1.00 184.63 ? 140 PRO A C   1 
ATOM   1065 O O   . PRO A 1 137 ? 69.388  65.863 23.183  1.00 187.07 ? 140 PRO A O   1 
ATOM   1066 C CB  . PRO A 1 137 ? 72.139  65.019 23.955  1.00 172.72 ? 140 PRO A CB  1 
ATOM   1067 C CG  . PRO A 1 137 ? 71.471  63.664 24.068  1.00 176.41 ? 140 PRO A CG  1 
ATOM   1068 C CD  . PRO A 1 137 ? 70.752  63.674 25.401  1.00 171.94 ? 140 PRO A CD  1 
ATOM   1069 N N   . TYR A 1 138 ? 70.210  67.920 23.603  1.00 189.12 ? 141 TYR A N   1 
ATOM   1070 C CA  . TYR A 1 138 ? 69.302  68.599 22.642  1.00 191.52 ? 141 TYR A CA  1 
ATOM   1071 C C   . TYR A 1 138 ? 69.963  68.598 21.262  1.00 198.49 ? 141 TYR A C   1 
ATOM   1072 O O   . TYR A 1 138 ? 70.866  69.425 21.037  1.00 189.89 ? 141 TYR A O   1 
ATOM   1073 C CB  . TYR A 1 138 ? 68.998  70.027 23.096  1.00 178.35 ? 141 TYR A CB  1 
ATOM   1074 C CG  . TYR A 1 138 ? 68.161  70.818 22.123  1.00 186.32 ? 141 TYR A CG  1 
ATOM   1075 C CD1 . TYR A 1 138 ? 66.897  70.389 21.756  1.00 185.85 ? 141 TYR A CD1 1 
ATOM   1076 C CD2 . TYR A 1 138 ? 68.635  71.991 21.559  1.00 179.51 ? 141 TYR A CD2 1 
ATOM   1077 C CE1 . TYR A 1 138 ? 66.122  71.105 20.860  1.00 186.90 ? 141 TYR A CE1 1 
ATOM   1078 C CE2 . TYR A 1 138 ? 67.873  72.720 20.662  1.00 182.84 ? 141 TYR A CE2 1 
ATOM   1079 C CZ  . TYR A 1 138 ? 66.611  72.276 20.312  1.00 188.57 ? 141 TYR A CZ  1 
ATOM   1080 O OH  . TYR A 1 138 ? 65.849  72.992 19.421  1.00 198.06 ? 141 TYR A OH  1 
ATOM   1081 N N   . GLN A 1 139 ? 69.537  67.689 20.381  1.00 212.21 ? 142 GLN A N   1 
ATOM   1082 C CA  . GLN A 1 139 ? 70.166  67.579 19.038  1.00 209.61 ? 142 GLN A CA  1 
ATOM   1083 C C   . GLN A 1 139 ? 71.678  67.412 19.218  1.00 213.60 ? 142 GLN A C   1 
ATOM   1084 O O   . GLN A 1 139 ? 72.433  67.998 18.418  1.00 215.65 ? 142 GLN A O   1 
ATOM   1085 C CB  . GLN A 1 139 ? 69.830  68.810 18.193  1.00 211.88 ? 142 GLN A CB  1 
ATOM   1086 C CG  . GLN A 1 139 ? 68.337  69.087 18.095  1.00 207.12 ? 142 GLN A CG  1 
ATOM   1087 C CD  . GLN A 1 139 ? 68.046  70.459 17.537  1.00 205.58 ? 142 GLN A CD  1 
ATOM   1088 O OE1 . GLN A 1 139 ? 68.952  71.233 17.235  1.00 201.65 ? 142 GLN A OE1 1 
ATOM   1089 N NE2 . GLN A 1 139 ? 66.768  70.772 17.401  1.00 203.48 ? 142 GLN A NE2 1 
ATOM   1090 N N   . GLY A 1 140 ? 72.098  66.649 20.233  1.00 208.93 ? 143 GLY A N   1 
ATOM   1091 C CA  . GLY A 1 140 ? 73.534  66.404 20.470  1.00 208.23 ? 143 GLY A CA  1 
ATOM   1092 C C   . GLY A 1 140 ? 74.160  67.440 21.390  1.00 205.12 ? 143 GLY A C   1 
ATOM   1093 O O   . GLY A 1 140 ? 75.397  67.419 21.540  1.00 208.31 ? 143 GLY A O   1 
ATOM   1094 N N   . LYS A 1 141 ? 73.343  68.316 21.984  1.00 189.92 ? 144 LYS A N   1 
ATOM   1095 C CA  . LYS A 1 141 ? 73.865  69.374 22.893  1.00 182.09 ? 144 LYS A CA  1 
ATOM   1096 C C   . LYS A 1 141 ? 73.364  69.108 24.316  1.00 178.57 ? 144 LYS A C   1 
ATOM   1097 O O   . LYS A 1 141 ? 72.139  69.159 24.525  1.00 177.90 ? 144 LYS A O   1 
ATOM   1098 C CB  . LYS A 1 141 ? 73.436  70.760 22.404  1.00 168.28 ? 144 LYS A CB  1 
ATOM   1099 C CG  . LYS A 1 141 ? 73.726  71.040 20.935  1.00 179.13 ? 144 LYS A CG  1 
ATOM   1100 C CD  . LYS A 1 141 ? 75.179  70.835 20.567  1.00 190.58 ? 144 LYS A CD  1 
ATOM   1101 C CE  . LYS A 1 141 ? 75.396  70.700 19.075  1.00 189.03 ? 144 LYS A CE  1 
ATOM   1102 N NZ  . LYS A 1 141 ? 74.670  69.533 18.521  1.00 187.97 ? 144 LYS A NZ  1 
ATOM   1103 N N   . SER A 1 142 ? 74.280  68.868 25.260  1.00 165.70 ? 145 SER A N   1 
ATOM   1104 C CA  . SER A 1 142 ? 73.877  68.533 26.651  1.00 157.36 ? 145 SER A CA  1 
ATOM   1105 C C   . SER A 1 142 ? 72.803  69.512 27.136  1.00 149.94 ? 145 SER A C   1 
ATOM   1106 O O   . SER A 1 142 ? 73.063  70.732 27.114  1.00 136.64 ? 145 SER A O   1 
ATOM   1107 C CB  . SER A 1 142 ? 75.070  68.533 27.570  1.00 142.89 ? 145 SER A CB  1 
ATOM   1108 O OG  . SER A 1 142 ? 75.653  69.826 27.640  1.00 117.31 ? 145 SER A OG  1 
ATOM   1109 N N   . SER A 1 143 ? 71.650  68.992 27.568  1.00 153.74 ? 146 SER A N   1 
ATOM   1110 C CA  . SER A 1 143 ? 70.543  69.853 28.060  1.00 146.88 ? 146 SER A CA  1 
ATOM   1111 C C   . SER A 1 143 ? 69.758  69.097 29.139  1.00 144.07 ? 146 SER A C   1 
ATOM   1112 O O   . SER A 1 143 ? 70.268  68.075 29.628  1.00 148.84 ? 146 SER A O   1 
ATOM   1113 C CB  . SER A 1 143 ? 69.649  70.285 26.927  1.00 152.71 ? 146 SER A CB  1 
ATOM   1114 O OG  . SER A 1 143 ? 68.613  71.135 27.395  1.00 148.95 ? 146 SER A OG  1 
ATOM   1115 N N   . PHE A 1 144 ? 68.568  69.588 29.493  1.00 131.69 ? 147 PHE A N   1 
ATOM   1116 C CA  . PHE A 1 144 ? 67.746  68.930 30.542  1.00 132.63 ? 147 PHE A CA  1 
ATOM   1117 C C   . PHE A 1 144 ? 66.258  69.146 30.251  1.00 132.47 ? 147 PHE A C   1 
ATOM   1118 O O   . PHE A 1 144 ? 65.927  70.024 29.430  1.00 135.24 ? 147 PHE A O   1 
ATOM   1119 C CB  . PHE A 1 144 ? 68.120  69.465 31.927  1.00 129.79 ? 147 PHE A CB  1 
ATOM   1120 C CG  . PHE A 1 144 ? 67.277  68.949 33.065  1.00 126.90 ? 147 PHE A CG  1 
ATOM   1121 C CD1 . PHE A 1 144 ? 67.240  67.597 33.366  1.00 124.90 ? 147 PHE A CD1 1 
ATOM   1122 C CD2 . PHE A 1 144 ? 66.510  69.814 33.829  1.00 137.90 ? 147 PHE A CD2 1 
ATOM   1123 C CE1 . PHE A 1 144 ? 66.463  67.124 34.411  1.00 123.90 ? 147 PHE A CE1 1 
ATOM   1124 C CE2 . PHE A 1 144 ? 65.732  69.340 34.873  1.00 135.51 ? 147 PHE A CE2 1 
ATOM   1125 C CZ  . PHE A 1 144 ? 65.709  67.996 35.161  1.00 130.29 ? 147 PHE A CZ  1 
ATOM   1126 N N   . PHE A 1 145 ? 65.394  68.365 30.904  1.00 126.41 ? 148 PHE A N   1 
ATOM   1127 C CA  . PHE A 1 145 ? 63.928  68.526 30.736  1.00 120.34 ? 148 PHE A CA  1 
ATOM   1128 C C   . PHE A 1 145 ? 63.561  69.999 30.927  1.00 121.77 ? 148 PHE A C   1 
ATOM   1129 O O   . PHE A 1 145 ? 63.935  70.575 31.965  1.00 129.39 ? 148 PHE A O   1 
ATOM   1130 C CB  . PHE A 1 145 ? 63.208  67.617 31.733  1.00 123.32 ? 148 PHE A CB  1 
ATOM   1131 C CG  . PHE A 1 145 ? 63.541  66.158 31.561  1.00 118.74 ? 148 PHE A CG  1 
ATOM   1132 C CD1 . PHE A 1 145 ? 63.241  65.500 30.380  1.00 121.05 ? 148 PHE A CD1 1 
ATOM   1133 C CD2 . PHE A 1 145 ? 64.182  65.451 32.565  1.00 116.33 ? 148 PHE A CD2 1 
ATOM   1134 C CE1 . PHE A 1 145 ? 63.557  64.161 30.214  1.00 121.45 ? 148 PHE A CE1 1 
ATOM   1135 C CE2 . PHE A 1 145 ? 64.500  64.113 32.397  1.00 111.97 ? 148 PHE A CE2 1 
ATOM   1136 C CZ  . PHE A 1 145 ? 64.189  63.472 31.222  1.00 117.19 ? 148 PHE A CZ  1 
ATOM   1137 N N   . ARG A 1 146 ? 62.858  70.587 29.955  1.00 119.26 ? 149 ARG A N   1 
ATOM   1138 C CA  . ARG A 1 146 ? 62.519  72.035 30.022  1.00 121.64 ? 149 ARG A CA  1 
ATOM   1139 C C   . ARG A 1 146 ? 61.475  72.284 31.116  1.00 118.52 ? 149 ARG A C   1 
ATOM   1140 O O   . ARG A 1 146 ? 61.617  73.286 31.843  1.00 128.90 ? 149 ARG A O   1 
ATOM   1141 C CB  . ARG A 1 146 ? 62.014  72.517 28.658  1.00 121.79 ? 149 ARG A CB  1 
ATOM   1142 C CG  . ARG A 1 146 ? 62.991  72.265 27.518  1.00 126.23 ? 149 ARG A CG  1 
ATOM   1143 C CD  . ARG A 1 146 ? 62.568  72.925 26.220  1.00 142.67 ? 149 ARG A CD  1 
ATOM   1144 N NE  . ARG A 1 146 ? 63.562  72.738 25.173  1.00 153.10 ? 149 ARG A NE  1 
ATOM   1145 C CZ  . ARG A 1 146 ? 63.460  73.221 23.939  1.00 163.46 ? 149 ARG A CZ  1 
ATOM   1146 N NH1 . ARG A 1 146 ? 62.435  73.986 23.610  1.00 181.64 ? 149 ARG A NH1 1 
ATOM   1147 N NH2 . ARG A 1 146 ? 64.384  72.933 23.039  1.00 162.43 ? 149 ARG A NH2 1 
ATOM   1148 N N   . ASN A 1 147 ? 60.470  71.410 31.227  1.00 108.23 ? 150 ASN A N   1 
ATOM   1149 C CA  . ASN A 1 147 ? 59.374  71.627 32.211  1.00 119.39 ? 150 ASN A CA  1 
ATOM   1150 C C   . ASN A 1 147 ? 59.857  71.659 33.666  1.00 125.86 ? 150 ASN A C   1 
ATOM   1151 O O   . ASN A 1 147 ? 59.399  72.542 34.416  1.00 131.99 ? 150 ASN A O   1 
ATOM   1152 C CB  . ASN A 1 147 ? 58.236  70.622 32.014  1.00 123.07 ? 150 ASN A CB  1 
ATOM   1153 C CG  . ASN A 1 147 ? 57.623  70.708 30.632  1.00 117.95 ? 150 ASN A CG  1 
ATOM   1154 O OD1 . ASN A 1 147 ? 58.061  71.501 29.802  1.00 113.57 ? 150 ASN A OD1 1 
ATOM   1155 N ND2 . ASN A 1 147 ? 56.611  69.896 30.376  1.00 129.99 ? 150 ASN A ND2 1 
ATOM   1156 N N   . VAL A 1 148 ? 60.740  70.731 34.045  1.00 114.53 ? 151 VAL A N   1 
ATOM   1157 C CA  . VAL A 1 148 ? 61.294  70.710 35.436  1.00 117.67 ? 151 VAL A CA  1 
ATOM   1158 C C   . VAL A 1 148 ? 62.594  71.512 35.431  1.00 121.45 ? 151 VAL A C   1 
ATOM   1159 O O   . VAL A 1 148 ? 63.045  71.873 34.328  1.00 122.75 ? 151 VAL A O   1 
ATOM   1160 C CB  . VAL A 1 148 ? 61.493  69.270 35.947  1.00 111.86 ? 151 VAL A CB  1 
ATOM   1161 C CG1 . VAL A 1 148 ? 62.191  69.249 37.298  1.00 118.88 ? 151 VAL A CG1 1 
ATOM   1162 C CG2 . VAL A 1 148 ? 60.171  68.523 36.021  1.00 111.10 ? 151 VAL A CG2 1 
ATOM   1163 N N   . VAL A 1 149 ? 63.164  71.798 36.605  1.00 119.27 ? 152 VAL A N   1 
ATOM   1164 C CA  . VAL A 1 149 ? 64.392  72.649 36.673  1.00 122.09 ? 152 VAL A CA  1 
ATOM   1165 C C   . VAL A 1 149 ? 65.479  72.001 37.537  1.00 128.06 ? 152 VAL A C   1 
ATOM   1166 O O   . VAL A 1 149 ? 65.140  71.493 38.623  1.00 128.91 ? 152 VAL A O   1 
ATOM   1167 C CB  . VAL A 1 149 ? 63.945  73.999 37.267  1.00 128.57 ? 152 VAL A CB  1 
ATOM   1168 C CG1 . VAL A 1 149 ? 65.131  74.888 37.602  1.00 139.03 ? 152 VAL A CG1 1 
ATOM   1169 C CG2 . VAL A 1 149 ? 62.971  74.727 36.355  1.00 135.15 ? 152 VAL A CG2 1 
ATOM   1170 N N   . TRP A 1 150 ? 66.735  72.040 37.080  1.00 130.93 ? 153 TRP A N   1 
ATOM   1171 C CA  . TRP A 1 150 ? 67.867  71.498 37.878  1.00 133.69 ? 153 TRP A CA  1 
ATOM   1172 C C   . TRP A 1 150 ? 68.236  72.505 38.971  1.00 148.48 ? 153 TRP A C   1 
ATOM   1173 O O   . TRP A 1 150 ? 69.205  73.263 38.770  1.00 153.73 ? 153 TRP A O   1 
ATOM   1174 C CB  . TRP A 1 150 ? 69.074  71.213 36.976  1.00 149.43 ? 153 TRP A CB  1 
ATOM   1175 C CG  . TRP A 1 150 ? 69.329  69.764 36.702  1.00 151.19 ? 153 TRP A CG  1 
ATOM   1176 C CD1 . TRP A 1 150 ? 69.330  69.150 35.484  1.00 166.30 ? 153 TRP A CD1 1 
ATOM   1177 C CD2 . TRP A 1 150 ? 69.654  68.744 37.663  1.00 149.69 ? 153 TRP A CD2 1 
ATOM   1178 N NE1 . TRP A 1 150 ? 69.614  67.818 35.621  1.00 165.93 ? 153 TRP A NE1 1 
ATOM   1179 C CE2 . TRP A 1 150 ? 69.820  67.540 36.946  1.00 156.70 ? 153 TRP A CE2 1 
ATOM   1180 C CE3 . TRP A 1 150 ? 69.815  68.727 39.053  1.00 145.66 ? 153 TRP A CE3 1 
ATOM   1181 C CZ2 . TRP A 1 150 ? 70.137  66.337 37.573  1.00 159.73 ? 153 TRP A CZ2 1 
ATOM   1182 C CZ3 . TRP A 1 150 ? 70.129  67.538 39.672  1.00 146.77 ? 153 TRP A CZ3 1 
ATOM   1183 C CH2 . TRP A 1 150 ? 70.287  66.361 38.940  1.00 154.39 ? 153 TRP A CH2 1 
ATOM   1184 N N   . LEU A 1 151 ? 67.529  72.500 40.103  1.00 129.57 ? 154 LEU A N   1 
ATOM   1185 C CA  . LEU A 1 151 ? 67.893  73.401 41.232  1.00 138.00 ? 154 LEU A CA  1 
ATOM   1186 C C   . LEU A 1 151 ? 69.275  73.016 41.763  1.00 151.24 ? 154 LEU A C   1 
ATOM   1187 O O   . LEU A 1 151 ? 69.561  71.808 41.804  1.00 150.63 ? 154 LEU A O   1 
ATOM   1188 C CB  . LEU A 1 151 ? 66.853  73.261 42.343  1.00 143.13 ? 154 LEU A CB  1 
ATOM   1189 C CG  . LEU A 1 151 ? 65.413  73.566 41.942  1.00 141.66 ? 154 LEU A CG  1 
ATOM   1190 C CD1 . LEU A 1 151 ? 64.522  73.615 43.171  1.00 155.40 ? 154 LEU A CD1 1 
ATOM   1191 C CD2 . LEU A 1 151 ? 65.331  74.875 41.174  1.00 142.99 ? 154 LEU A CD2 1 
ATOM   1192 N N   . ILE A 1 152 ? 70.085  73.999 42.165  1.00 141.06 ? 155 ILE A N   1 
ATOM   1193 C CA  . ILE A 1 152 ? 71.462  73.714 42.669  1.00 139.13 ? 155 ILE A CA  1 
ATOM   1194 C C   . ILE A 1 152 ? 71.844  74.792 43.690  1.00 142.48 ? 155 ILE A C   1 
ATOM   1195 O O   . ILE A 1 152 ? 71.336  75.917 43.571  1.00 154.44 ? 155 ILE A O   1 
ATOM   1196 C CB  . ILE A 1 152 ? 72.461  73.631 41.495  1.00 145.83 ? 155 ILE A CB  1 
ATOM   1197 C CG1 . ILE A 1 152 ? 73.393  72.424 41.626  1.00 182.34 ? 155 ILE A CG1 1 
ATOM   1198 C CG2 . ILE A 1 152 ? 73.233  74.931 41.326  1.00 141.62 ? 155 ILE A CG2 1 
ATOM   1199 C CD1 . ILE A 1 152 ? 72.712  71.102 41.368  1.00 235.80 ? 155 ILE A CD1 1 
ATOM   1200 N N   . LYS A 1 153 ? 72.708  74.459 44.653  1.00 145.11 ? 156 LYS A N   1 
ATOM   1201 C CA  . LYS A 1 153 ? 73.084  75.433 45.714  1.00 146.68 ? 156 LYS A CA  1 
ATOM   1202 C C   . LYS A 1 153 ? 73.617  76.709 45.054  1.00 146.67 ? 156 LYS A C   1 
ATOM   1203 O O   . LYS A 1 153 ? 74.215  76.609 43.963  1.00 148.70 ? 156 LYS A O   1 
ATOM   1204 C CB  . LYS A 1 153 ? 74.143  74.837 46.646  1.00 133.28 ? 156 LYS A CB  1 
ATOM   1205 C CG  . LYS A 1 153 ? 75.569  74.902 46.118  1.00 139.11 ? 156 LYS A CG  1 
ATOM   1206 C CD  . LYS A 1 153 ? 76.531  73.975 46.820  1.00 140.75 ? 156 LYS A CD  1 
ATOM   1207 C CE  . LYS A 1 153 ? 77.962  74.177 46.368  1.00 134.01 ? 156 LYS A CE  1 
ATOM   1208 N NZ  . LYS A 1 153 ? 78.851  73.096 46.855  1.00 129.43 ? 156 LYS A NZ  1 
ATOM   1209 N N   . LYS A 1 154 ? 73.408  77.863 45.692  1.00 155.79 ? 157 LYS A N   1 
ATOM   1210 C CA  . LYS A 1 154 ? 73.949  79.137 45.145  1.00 154.86 ? 157 LYS A CA  1 
ATOM   1211 C C   . LYS A 1 154 ? 75.360  79.643 45.468  1.00 156.58 ? 157 LYS A C   1 
ATOM   1212 O O   . LYS A 1 154 ? 76.194  79.687 44.542  1.00 163.59 ? 157 LYS A O   1 
ATOM   1213 C CB  . LYS A 1 154 ? 73.036  80.313 45.510  1.00 160.25 ? 157 LYS A CB  1 
ATOM   1214 C CG  . LYS A 1 154 ? 72.468  80.297 46.923  1.00 165.94 ? 157 LYS A CG  1 
ATOM   1215 C CD  . LYS A 1 154 ? 71.685  81.545 47.262  1.00 175.81 ? 157 LYS A CD  1 
ATOM   1216 C CE  . LYS A 1 154 ? 71.131  81.532 48.671  1.00 183.50 ? 157 LYS A CE  1 
ATOM   1217 N NZ  . LYS A 1 154 ? 72.207  81.405 49.682  1.00 180.62 ? 157 LYS A NZ  1 
ATOM   1218 N N   . ASN A 1 155 ? 75.616  80.003 46.728  1.00 155.17 ? 158 ASN A N   1 
ATOM   1219 C CA  . ASN A 1 155 ? 76.950  80.522 47.130  1.00 150.46 ? 158 ASN A CA  1 
ATOM   1220 C C   . ASN A 1 155 ? 77.243  79.513 48.246  1.00 153.08 ? 158 ASN A C   1 
ATOM   1221 O O   . ASN A 1 155 ? 77.097  79.888 49.425  1.00 157.09 ? 158 ASN A O   1 
ATOM   1222 C CB  . ASN A 1 155 ? 77.092  81.968 47.613  1.00 149.99 ? 158 ASN A CB  1 
ATOM   1223 C CG  . ASN A 1 155 ? 78.532  82.399 47.805  1.00 166.38 ? 158 ASN A CG  1 
ATOM   1224 O OD1 . ASN A 1 155 ? 79.003  83.315 47.135  1.00 173.72 ? 158 ASN A OD1 1 
ATOM   1225 N ND2 . ASN A 1 155 ? 79.240  81.747 48.713  1.00 168.40 ? 158 ASN A ND2 1 
ATOM   1226 N N   . SER A 1 156 ? 77.644  78.290 47.881  1.00 153.30 ? 159 SER A N   1 
ATOM   1227 C CA  . SER A 1 156 ? 77.982  77.257 48.895  1.00 152.21 ? 159 SER A CA  1 
ATOM   1228 C C   . SER A 1 156 ? 76.916  77.260 49.992  1.00 154.38 ? 159 SER A C   1 
ATOM   1229 O O   . SER A 1 156 ? 77.270  76.972 51.152  1.00 153.35 ? 159 SER A O   1 
ATOM   1230 C CB  . SER A 1 156 ? 79.353  77.506 49.464  1.00 148.51 ? 159 SER A CB  1 
ATOM   1231 O OG  . SER A 1 156 ? 80.341  77.426 48.447  1.00 140.85 ? 159 SER A OG  1 
ATOM   1232 N N   . THR A 1 157 ? 75.662  77.554 49.635  1.00 149.74 ? 160 THR A N   1 
ATOM   1233 C CA  . THR A 1 157 ? 74.574  77.678 50.637  1.00 162.15 ? 160 THR A CA  1 
ATOM   1234 C C   . THR A 1 157 ? 73.287  77.285 49.910  1.00 165.00 ? 160 THR A C   1 
ATOM   1235 O O   . THR A 1 157 ? 72.992  77.906 48.870  1.00 172.65 ? 160 THR A O   1 
ATOM   1236 C CB  . THR A 1 157 ? 74.396  79.024 51.346  1.00 163.55 ? 160 THR A CB  1 
ATOM   1237 O OG1 . THR A 1 157 ? 74.374  80.037 50.340  1.00 166.09 ? 160 THR A OG1 1 
ATOM   1238 C CG2 . THR A 1 157 ? 75.494  79.321 52.343  1.00 160.65 ? 160 THR A CG2 1 
ATOM   1239 N N   . TYR A 1 158 ? 72.552  76.302 50.439  1.00 165.71 ? 161 TYR A N   1 
ATOM   1240 C CA  . TYR A 1 158 ? 71.249  75.918 49.837  1.00 158.81 ? 161 TYR A CA  1 
ATOM   1241 C C   . TYR A 1 158 ? 70.152  76.049 50.895  1.00 161.56 ? 161 TYR A C   1 
ATOM   1242 O O   . TYR A 1 158 ? 69.782  75.035 51.513  1.00 155.20 ? 161 TYR A O   1 
ATOM   1243 C CB  . TYR A 1 158 ? 71.295  74.500 49.264  1.00 157.63 ? 161 TYR A CB  1 
ATOM   1244 C CG  . TYR A 1 158 ? 70.095  74.153 48.421  1.00 162.59 ? 161 TYR A CG  1 
ATOM   1245 C CD1 . TYR A 1 158 ? 69.745  74.928 47.329  1.00 172.76 ? 161 TYR A CD1 1 
ATOM   1246 C CD2 . TYR A 1 158 ? 69.304  73.058 48.714  1.00 158.52 ? 161 TYR A CD2 1 
ATOM   1247 C CE1 . TYR A 1 158 ? 68.641  74.624 46.551  1.00 183.75 ? 161 TYR A CE1 1 
ATOM   1248 C CE2 . TYR A 1 158 ? 68.195  72.741 47.948  1.00 160.59 ? 161 TYR A CE2 1 
ATOM   1249 C CZ  . TYR A 1 158 ? 67.862  73.525 46.861  1.00 168.68 ? 161 TYR A CZ  1 
ATOM   1250 O OH  . TYR A 1 158 ? 66.766  73.208 46.099  1.00 168.22 ? 161 TYR A OH  1 
ATOM   1251 N N   . PRO A 1 159 ? 69.631  77.268 51.140  1.00 163.03 ? 162 PRO A N   1 
ATOM   1252 C CA  . PRO A 1 159 ? 68.587  77.475 52.143  1.00 164.33 ? 162 PRO A CA  1 
ATOM   1253 C C   . PRO A 1 159 ? 67.265  76.818 51.723  1.00 162.99 ? 162 PRO A C   1 
ATOM   1254 O O   . PRO A 1 159 ? 66.892  76.959 50.576  1.00 164.55 ? 162 PRO A O   1 
ATOM   1255 C CB  . PRO A 1 159 ? 68.445  79.001 52.197  1.00 170.68 ? 162 PRO A CB  1 
ATOM   1256 C CG  . PRO A 1 159 ? 69.721  79.524 51.577  1.00 167.12 ? 162 PRO A CG  1 
ATOM   1257 C CD  . PRO A 1 159 ? 70.046  78.513 50.501  1.00 166.79 ? 162 PRO A CD  1 
ATOM   1258 N N   . THR A 1 160 ? 66.590  76.139 52.655  1.00 157.92 ? 163 THR A N   1 
ATOM   1259 C CA  . THR A 1 160 ? 65.338  75.405 52.328  1.00 160.01 ? 163 THR A CA  1 
ATOM   1260 C C   . THR A 1 160 ? 64.322  76.352 51.692  1.00 156.13 ? 163 THR A C   1 
ATOM   1261 O O   . THR A 1 160 ? 64.130  77.448 52.243  1.00 153.92 ? 163 THR A O   1 
ATOM   1262 C CB  . THR A 1 160 ? 64.729  74.789 53.590  1.00 157.99 ? 163 THR A CB  1 
ATOM   1263 O OG1 . THR A 1 160 ? 65.731  73.982 54.208  1.00 169.26 ? 163 THR A OG1 1 
ATOM   1264 C CG2 . THR A 1 160 ? 63.499  73.956 53.305  1.00 158.17 ? 163 THR A CG2 1 
ATOM   1265 N N   . ILE A 1 161 ? 63.693  75.950 50.584  1.00 159.33 ? 164 ILE A N   1 
ATOM   1266 C CA  . ILE A 1 161 ? 62.767  76.926 49.934  1.00 160.36 ? 164 ILE A CA  1 
ATOM   1267 C C   . ILE A 1 161 ? 61.332  76.465 50.202  1.00 159.33 ? 164 ILE A C   1 
ATOM   1268 O O   . ILE A 1 161 ? 60.992  75.349 49.771  1.00 160.76 ? 164 ILE A O   1 
ATOM   1269 C CB  . ILE A 1 161 ? 63.052  77.038 48.423  1.00 177.35 ? 164 ILE A CB  1 
ATOM   1270 C CG1 . ILE A 1 161 ? 62.834  75.709 47.699  1.00 174.95 ? 164 ILE A CG1 1 
ATOM   1271 C CG2 . ILE A 1 161 ? 64.448  77.589 48.176  1.00 191.23 ? 164 ILE A CG2 1 
ATOM   1272 C CD1 . ILE A 1 161 ? 61.508  75.616 46.982  1.00 167.00 ? 164 ILE A CD1 1 
ATOM   1273 N N   . LYS A 1 162 ? 60.512  77.322 50.814  1.00 167.78 ? 165 LYS A N   1 
ATOM   1274 C CA  . LYS A 1 162 ? 59.086  76.980 51.053  1.00 164.17 ? 165 LYS A CA  1 
ATOM   1275 C C   . LYS A 1 162 ? 58.216  77.689 50.015  1.00 160.53 ? 165 LYS A C   1 
ATOM   1276 O O   . LYS A 1 162 ? 57.237  78.339 50.416  1.00 163.58 ? 165 LYS A O   1 
ATOM   1277 C CB  . LYS A 1 162 ? 58.644  77.420 52.451  1.00 168.36 ? 165 LYS A CB  1 
ATOM   1278 C CG  . LYS A 1 162 ? 58.888  76.422 53.574  1.00 169.91 ? 165 LYS A CG  1 
ATOM   1279 C CD  . LYS A 1 162 ? 60.297  76.437 54.124  1.00 167.79 ? 165 LYS A CD  1 
ATOM   1280 C CE  . LYS A 1 162 ? 60.506  75.414 55.221  1.00 163.17 ? 165 LYS A CE  1 
ATOM   1281 N NZ  . LYS A 1 162 ? 59.488  75.539 56.290  1.00 154.39 ? 165 LYS A NZ  1 
ATOM   1282 N N   . ARG A 1 163 ? 58.558  77.573 48.734  1.00 153.27 ? 166 ARG A N   1 
ATOM   1283 C CA  . ARG A 1 163 ? 57.689  78.174 47.692  1.00 147.15 ? 166 ARG A CA  1 
ATOM   1284 C C   . ARG A 1 163 ? 56.415  77.339 47.575  1.00 149.49 ? 166 ARG A C   1 
ATOM   1285 O O   . ARG A 1 163 ? 56.481  76.125 47.841  1.00 150.19 ? 166 ARG A O   1 
ATOM   1286 C CB  . ARG A 1 163 ? 58.411  78.253 46.346  1.00 147.09 ? 166 ARG A CB  1 
ATOM   1287 C CG  . ARG A 1 163 ? 59.335  79.452 46.199  1.00 152.27 ? 166 ARG A CG  1 
ATOM   1288 C CD  . ARG A 1 163 ? 59.805  79.581 44.764  1.00 162.93 ? 166 ARG A CD  1 
ATOM   1289 N NE  . ARG A 1 163 ? 60.570  80.796 44.527  1.00 175.05 ? 166 ARG A NE  1 
ATOM   1290 C CZ  . ARG A 1 163 ? 60.089  82.028 44.642  1.00 179.59 ? 166 ARG A CZ  1 
ATOM   1291 N NH1 . ARG A 1 163 ? 58.783  82.230 44.666  1.00 167.45 ? 166 ARG A NH1 1 
ATOM   1292 N NH2 . ARG A 1 163 ? 60.917  83.056 44.715  1.00 179.05 ? 166 ARG A NH2 1 
ATOM   1293 N N   . SER A 1 164 ? 55.315  77.967 47.159  1.00 141.06 ? 167 SER A N   1 
ATOM   1294 C CA  . SER A 1 164 ? 54.028  77.244 47.008  1.00 145.81 ? 167 SER A CA  1 
ATOM   1295 C C   . SER A 1 164 ? 53.186  77.925 45.927  1.00 147.03 ? 167 SER A C   1 
ATOM   1296 O O   . SER A 1 164 ? 53.375  79.137 45.717  1.00 142.47 ? 167 SER A O   1 
ATOM   1297 C CB  . SER A 1 164 ? 53.296  77.204 48.313  1.00 154.50 ? 167 SER A CB  1 
ATOM   1298 O OG  . SER A 1 164 ? 53.025  78.518 48.774  1.00 165.05 ? 167 SER A OG  1 
ATOM   1299 N N   . TYR A 1 165 ? 52.300  77.171 45.271  1.00 122.89 ? 168 TYR A N   1 
ATOM   1300 C CA  . TYR A 1 165 ? 51.504  77.759 44.166  1.00 130.99 ? 168 TYR A CA  1 
ATOM   1301 C C   . TYR A 1 165 ? 50.084  77.198 44.182  1.00 140.44 ? 168 TYR A C   1 
ATOM   1302 O O   . TYR A 1 165 ? 49.926  75.982 44.387  1.00 136.87 ? 168 TYR A O   1 
ATOM   1303 C CB  . TYR A 1 165 ? 52.117  77.441 42.802  1.00 135.81 ? 168 TYR A CB  1 
ATOM   1304 C CG  . TYR A 1 165 ? 51.303  77.939 41.635  1.00 164.17 ? 168 TYR A CG  1 
ATOM   1305 C CD1 . TYR A 1 165 ? 51.045  79.290 41.468  1.00 145.09 ? 168 TYR A CD1 1 
ATOM   1306 C CD2 . TYR A 1 165 ? 50.771  77.062 40.706  1.00 211.93 ? 168 TYR A CD2 1 
ATOM   1307 C CE1 . TYR A 1 165 ? 50.292  79.756 40.404  1.00 147.62 ? 168 TYR A CE1 1 
ATOM   1308 C CE2 . TYR A 1 165 ? 50.017  77.511 39.636  1.00 174.82 ? 168 TYR A CE2 1 
ATOM   1309 C CZ  . TYR A 1 165 ? 49.777  78.863 39.483  1.00 148.40 ? 168 TYR A CZ  1 
ATOM   1310 O OH  . TYR A 1 165 ? 49.028  79.315 38.424  1.00 147.78 ? 168 TYR A OH  1 
ATOM   1311 N N   . ASN A 1 166 ? 49.091  78.064 43.976  1.00 169.54 ? 169 ASN A N   1 
ATOM   1312 C CA  . ASN A 1 166 ? 47.684  77.606 43.854  1.00 172.37 ? 169 ASN A CA  1 
ATOM   1313 C C   . ASN A 1 166 ? 47.194  78.178 42.528  1.00 173.24 ? 169 ASN A C   1 
ATOM   1314 O O   . ASN A 1 166 ? 47.115  79.416 42.418  1.00 175.63 ? 169 ASN A O   1 
ATOM   1315 C CB  . ASN A 1 166 ? 46.803  78.070 45.009  1.00 168.17 ? 169 ASN A CB  1 
ATOM   1316 C CG  . ASN A 1 166 ? 46.678  79.576 45.086  1.00 180.01 ? 169 ASN A CG  1 
ATOM   1317 O OD1 . ASN A 1 166 ? 47.422  80.308 44.438  1.00 193.22 ? 169 ASN A OD1 1 
ATOM   1318 N ND2 . ASN A 1 166 ? 45.746  80.044 45.899  1.00 182.64 ? 169 ASN A ND2 1 
ATOM   1319 N N   . ASN A 1 167 ? 46.868  77.317 41.569  1.00 165.44 ? 170 ASN A N   1 
ATOM   1320 C CA  . ASN A 1 167 ? 46.521  77.836 40.224  1.00 175.07 ? 170 ASN A CA  1 
ATOM   1321 C C   . ASN A 1 167 ? 45.426  78.897 40.302  1.00 167.97 ? 170 ASN A C   1 
ATOM   1322 O O   . ASN A 1 167 ? 45.582  79.937 39.637  1.00 168.31 ? 170 ASN A O   1 
ATOM   1323 C CB  . ASN A 1 167 ? 46.058  76.696 39.321  1.00 169.42 ? 170 ASN A CB  1 
ATOM   1324 C CG  . ASN A 1 167 ? 44.748  76.082 39.761  1.00 175.50 ? 170 ASN A CG  1 
ATOM   1325 O OD1 . ASN A 1 167 ? 43.750  76.190 39.055  1.00 198.87 ? 170 ASN A OD1 1 
ATOM   1326 N ND2 . ASN A 1 167 ? 44.740  75.450 40.923  1.00 168.25 ? 170 ASN A ND2 1 
ATOM   1327 N N   . THR A 1 168 ? 44.352  78.628 41.047  1.00 177.18 ? 171 THR A N   1 
ATOM   1328 C CA  . THR A 1 168 ? 43.202  79.570 41.065  1.00 178.67 ? 171 THR A CA  1 
ATOM   1329 C C   . THR A 1 168 ? 42.658  79.658 39.636  1.00 175.92 ? 171 THR A C   1 
ATOM   1330 O O   . THR A 1 168 ? 41.789  80.510 39.386  1.00 173.97 ? 171 THR A O   1 
ATOM   1331 C CB  . THR A 1 168 ? 43.598  80.933 41.649  1.00 180.30 ? 171 THR A CB  1 
ATOM   1332 O OG1 . THR A 1 168 ? 44.573  80.709 42.667  1.00 184.88 ? 171 THR A OG1 1 
ATOM   1333 C CG2 . THR A 1 168 ? 42.423  81.700 42.216  1.00 173.92 ? 171 THR A CG2 1 
ATOM   1334 N N   . ASN A 1 169 ? 43.147  78.796 38.741  1.00 168.83 ? 172 ASN A N   1 
ATOM   1335 C CA  . ASN A 1 169 ? 42.649  78.773 37.343  1.00 167.01 ? 172 ASN A CA  1 
ATOM   1336 C C   . ASN A 1 169 ? 41.312  78.030 37.336  1.00 166.87 ? 172 ASN A C   1 
ATOM   1337 O O   . ASN A 1 169 ? 40.815  77.710 38.429  1.00 168.30 ? 172 ASN A O   1 
ATOM   1338 C CB  . ASN A 1 169 ? 43.664  78.143 36.388  1.00 159.50 ? 172 ASN A CB  1 
ATOM   1339 C CG  . ASN A 1 169 ? 44.910  78.983 36.210  1.00 159.05 ? 172 ASN A CG  1 
ATOM   1340 O OD1 . ASN A 1 169 ? 44.834  80.129 35.776  1.00 156.91 ? 172 ASN A OD1 1 
ATOM   1341 N ND2 . ASN A 1 169 ? 46.061  78.419 36.536  1.00 155.76 ? 172 ASN A ND2 1 
ATOM   1342 N N   . GLN A 1 170 ? 40.743  77.785 36.154  1.00 165.41 ? 173 GLN A N   1 
ATOM   1343 C CA  . GLN A 1 170 ? 39.405  77.141 36.088  1.00 155.55 ? 173 GLN A CA  1 
ATOM   1344 C C   . GLN A 1 170 ? 39.582  75.675 35.688  1.00 145.70 ? 173 GLN A C   1 
ATOM   1345 O O   . GLN A 1 170 ? 38.595  74.921 35.759  1.00 141.19 ? 173 GLN A O   1 
ATOM   1346 C CB  . GLN A 1 170 ? 38.510  77.894 35.103  1.00 158.76 ? 173 GLN A CB  1 
ATOM   1347 C CG  . GLN A 1 170 ? 37.025  77.763 35.406  1.00 163.31 ? 173 GLN A CG  1 
ATOM   1348 C CD  . GLN A 1 170 ? 36.179  78.616 34.492  1.00 171.78 ? 173 GLN A CD  1 
ATOM   1349 O OE1 . GLN A 1 170 ? 36.685  79.306 33.610  1.00 166.81 ? 173 GLN A OE1 1 
ATOM   1350 N NE2 . GLN A 1 170 ? 34.873  78.574 34.699  1.00 182.48 ? 173 GLN A NE2 1 
ATOM   1351 N N   . GLU A 1 171 ? 40.797  75.296 35.291  1.00 159.33 ? 174 GLU A N   1 
ATOM   1352 C CA  . GLU A 1 171 ? 41.055  73.902 34.846  1.00 157.32 ? 174 GLU A CA  1 
ATOM   1353 C C   . GLU A 1 171 ? 41.996  73.222 35.845  1.00 159.00 ? 174 GLU A C   1 
ATOM   1354 O O   . GLU A 1 171 ? 42.666  73.943 36.605  1.00 158.02 ? 174 GLU A O   1 
ATOM   1355 C CB  . GLU A 1 171 ? 41.646  73.904 33.437  1.00 151.38 ? 174 GLU A CB  1 
ATOM   1356 C CG  . GLU A 1 171 ? 40.711  74.479 32.391  1.00 151.46 ? 174 GLU A CG  1 
ATOM   1357 C CD  . GLU A 1 171 ? 41.268  74.444 30.980  1.00 156.85 ? 174 GLU A CD  1 
ATOM   1358 O OE1 . GLU A 1 171 ? 42.411  73.979 30.811  1.00 156.71 ? 174 GLU A OE1 1 
ATOM   1359 O OE2 . GLU A 1 171 ? 40.556  74.875 30.054  1.00 164.88 ? 174 GLU A OE2 1 
ATOM   1360 N N   . ASP A 1 172 ? 42.029  71.886 35.844  1.00 155.34 ? 175 ASP A N   1 
ATOM   1361 C CA  . ASP A 1 172 ? 42.896  71.143 36.793  1.00 156.07 ? 175 ASP A CA  1 
ATOM   1362 C C   . ASP A 1 172 ? 44.338  71.208 36.295  1.00 147.16 ? 175 ASP A C   1 
ATOM   1363 O O   . ASP A 1 172 ? 44.547  71.666 35.158  1.00 143.08 ? 175 ASP A O   1 
ATOM   1364 C CB  . ASP A 1 172 ? 42.422  69.702 36.971  1.00 159.72 ? 175 ASP A CB  1 
ATOM   1365 C CG  . ASP A 1 172 ? 40.963  69.599 37.377  1.00 168.82 ? 175 ASP A CG  1 
ATOM   1366 O OD1 . ASP A 1 172 ? 40.314  70.656 37.492  1.00 172.68 ? 175 ASP A OD1 1 
ATOM   1367 O OD2 . ASP A 1 172 ? 40.491  68.464 37.576  1.00 171.87 ? 175 ASP A OD2 1 
ATOM   1368 N N   . LEU A 1 173 ? 45.292  70.756 37.109  1.00 147.08 ? 176 LEU A N   1 
ATOM   1369 C CA  . LEU A 1 173 ? 46.720  70.892 36.724  1.00 140.01 ? 176 LEU A CA  1 
ATOM   1370 C C   . LEU A 1 173 ? 47.410  69.529 36.763  1.00 138.32 ? 176 LEU A C   1 
ATOM   1371 O O   . LEU A 1 173 ? 46.926  68.649 37.491  1.00 140.67 ? 176 LEU A O   1 
ATOM   1372 C CB  . LEU A 1 173 ? 47.394  71.851 37.707  1.00 143.94 ? 176 LEU A CB  1 
ATOM   1373 C CG  . LEU A 1 173 ? 47.163  73.342 37.472  1.00 155.66 ? 176 LEU A CG  1 
ATOM   1374 C CD1 . LEU A 1 173 ? 45.770  73.765 37.912  1.00 160.78 ? 176 LEU A CD1 1 
ATOM   1375 C CD2 . LEU A 1 173 ? 48.217  74.162 38.198  1.00 163.47 ? 176 LEU A CD2 1 
ATOM   1376 N N   . LEU A 1 174 ? 48.504  69.376 36.014  1.00 132.15 ? 177 LEU A N   1 
ATOM   1377 C CA  . LEU A 1 174 ? 49.290  68.117 36.044  1.00 125.11 ? 177 LEU A CA  1 
ATOM   1378 C C   . LEU A 1 174 ? 50.706  68.484 36.479  1.00 124.49 ? 177 LEU A C   1 
ATOM   1379 O O   . LEU A 1 174 ? 51.628  68.315 35.669  1.00 123.84 ? 177 LEU A O   1 
ATOM   1380 C CB  . LEU A 1 174 ? 49.295  67.504 34.642  1.00 115.83 ? 177 LEU A CB  1 
ATOM   1381 C CG  . LEU A 1 174 ? 49.195  65.982 34.581  1.00 114.26 ? 177 LEU A CG  1 
ATOM   1382 C CD1 . LEU A 1 174 ? 49.653  65.469 33.226  1.00 114.33 ? 177 LEU A CD1 1 
ATOM   1383 C CD2 . LEU A 1 174 ? 49.997  65.335 35.698  1.00 128.06 ? 177 LEU A CD2 1 
ATOM   1384 N N   . VAL A 1 175 ? 50.860  68.983 37.704  1.00 127.98 ? 178 VAL A N   1 
ATOM   1385 C CA  . VAL A 1 175 ? 52.196  69.435 38.188  1.00 125.80 ? 178 VAL A CA  1 
ATOM   1386 C C   . VAL A 1 175 ? 53.154  68.242 38.181  1.00 125.28 ? 178 VAL A C   1 
ATOM   1387 O O   . VAL A 1 175 ? 52.694  67.119 38.458  1.00 133.59 ? 178 VAL A O   1 
ATOM   1388 C CB  . VAL A 1 175 ? 52.090  70.059 39.590  1.00 128.80 ? 178 VAL A CB  1 
ATOM   1389 C CG1 . VAL A 1 175 ? 53.436  70.546 40.102  1.00 125.31 ? 178 VAL A CG1 1 
ATOM   1390 C CG2 . VAL A 1 175 ? 51.065  71.181 39.626  1.00 131.53 ? 178 VAL A CG2 1 
ATOM   1391 N N   . LEU A 1 176 ? 54.432  68.483 37.880  1.00 113.77 ? 179 LEU A N   1 
ATOM   1392 C CA  . LEU A 1 176 ? 55.443  67.398 37.852  1.00 111.77 ? 179 LEU A CA  1 
ATOM   1393 C C   . LEU A 1 176 ? 56.685  67.872 38.608  1.00 116.18 ? 179 LEU A C   1 
ATOM   1394 O O   . LEU A 1 176 ? 56.978  69.070 38.529  1.00 111.84 ? 179 LEU A O   1 
ATOM   1395 C CB  . LEU A 1 176 ? 55.785  67.115 36.390  1.00 110.35 ? 179 LEU A CB  1 
ATOM   1396 C CG  . LEU A 1 176 ? 54.599  66.896 35.452  1.00 107.44 ? 179 LEU A CG  1 
ATOM   1397 C CD1 . LEU A 1 176 ? 55.056  66.857 34.003  1.00 104.75 ? 179 LEU A CD1 1 
ATOM   1398 C CD2 . LEU A 1 176 ? 53.862  65.615 35.802  1.00 118.15 ? 179 LEU A CD2 1 
ATOM   1399 N N   . TRP A 1 177 ? 57.380  66.976 39.317  1.00 121.68 ? 180 TRP A N   1 
ATOM   1400 C CA  . TRP A 1 177 ? 58.651  67.357 39.987  1.00 118.43 ? 180 TRP A CA  1 
ATOM   1401 C C   . TRP A 1 177 ? 59.541  66.116 40.073  1.00 118.71 ? 180 TRP A C   1 
ATOM   1402 O O   . TRP A 1 177 ? 59.139  65.062 39.538  1.00 120.94 ? 180 TRP A O   1 
ATOM   1403 C CB  . TRP A 1 177 ? 58.412  67.987 41.361  1.00 123.61 ? 180 TRP A CB  1 
ATOM   1404 C CG  . TRP A 1 177 ? 57.687  67.100 42.328  1.00 127.69 ? 180 TRP A CG  1 
ATOM   1405 C CD1 . TRP A 1 177 ? 58.235  66.359 43.332  1.00 128.01 ? 180 TRP A CD1 1 
ATOM   1406 C CD2 . TRP A 1 177 ? 56.269  66.895 42.401  1.00 129.83 ? 180 TRP A CD2 1 
ATOM   1407 N NE1 . TRP A 1 177 ? 57.258  65.683 44.007  1.00 133.91 ? 180 TRP A NE1 1 
ATOM   1408 C CE2 . TRP A 1 177 ? 56.040  65.994 43.464  1.00 133.89 ? 180 TRP A CE2 1 
ATOM   1409 C CE3 . TRP A 1 177 ? 55.175  67.372 41.674  1.00 128.83 ? 180 TRP A CE3 1 
ATOM   1410 C CZ2 . TRP A 1 177 ? 54.763  65.562 43.807  1.00 137.69 ? 180 TRP A CZ2 1 
ATOM   1411 C CZ3 . TRP A 1 177 ? 53.914  66.943 42.015  1.00 134.07 ? 180 TRP A CZ3 1 
ATOM   1412 C CH2 . TRP A 1 177 ? 53.714  66.050 43.067  1.00 138.70 ? 180 TRP A CH2 1 
ATOM   1413 N N   . GLY A 1 178 ? 60.717  66.241 40.694  1.00 110.37 ? 181 GLY A N   1 
ATOM   1414 C CA  . GLY A 1 178 ? 61.647  65.099 40.734  1.00 109.24 ? 181 GLY A CA  1 
ATOM   1415 C C   . GLY A 1 178 ? 62.609  65.130 41.906  1.00 107.80 ? 181 GLY A C   1 
ATOM   1416 O O   . GLY A 1 178 ? 62.727  66.193 42.540  1.00 107.16 ? 181 GLY A O   1 
ATOM   1417 N N   . ILE A 1 179 ? 63.266  64.002 42.191  1.00 113.32 ? 182 ILE A N   1 
ATOM   1418 C CA  . ILE A 1 179 ? 64.302  63.934 43.266  1.00 119.37 ? 182 ILE A CA  1 
ATOM   1419 C C   . ILE A 1 179 ? 65.593  63.431 42.623  1.00 126.14 ? 182 ILE A C   1 
ATOM   1420 O O   . ILE A 1 179 ? 65.530  62.434 41.882  1.00 132.80 ? 182 ILE A O   1 
ATOM   1421 C CB  . ILE A 1 179 ? 63.881  62.969 44.389  1.00 123.55 ? 182 ILE A CB  1 
ATOM   1422 C CG1 . ILE A 1 179 ? 62.469  63.261 44.901  1.00 157.33 ? 182 ILE A CG1 1 
ATOM   1423 C CG2 . ILE A 1 179 ? 64.900  62.959 45.520  1.00 124.41 ? 182 ILE A CG2 1 
ATOM   1424 C CD1 . ILE A 1 179 ? 61.972  62.211 45.851  1.00 197.01 ? 182 ILE A CD1 1 
ATOM   1425 N N   . HIS A 1 180 ? 66.720  64.078 42.908  1.00 137.99 ? 183 HIS A N   1 
ATOM   1426 C CA  . HIS A 1 180 ? 68.006  63.557 42.368  1.00 137.08 ? 183 HIS A CA  1 
ATOM   1427 C C   . HIS A 1 180 ? 68.642  62.616 43.392  1.00 138.41 ? 183 HIS A C   1 
ATOM   1428 O O   . HIS A 1 180 ? 68.890  63.031 44.545  1.00 136.67 ? 183 HIS A O   1 
ATOM   1429 C CB  . HIS A 1 180 ? 68.948  64.697 41.968  1.00 137.90 ? 183 HIS A CB  1 
ATOM   1430 C CG  . HIS A 1 180 ? 70.322  64.223 41.633  1.00 137.77 ? 183 HIS A CG  1 
ATOM   1431 N ND1 . HIS A 1 180 ? 70.558  63.265 40.673  1.00 143.08 ? 183 HIS A ND1 1 
ATOM   1432 C CD2 . HIS A 1 180 ? 71.518  64.549 42.134  1.00 138.28 ? 183 HIS A CD2 1 
ATOM   1433 C CE1 . HIS A 1 180 ? 71.861  63.036 40.598  1.00 146.98 ? 183 HIS A CE1 1 
ATOM   1434 N NE2 . HIS A 1 180 ? 72.462  63.807 41.475  1.00 146.41 ? 183 HIS A NE2 1 
ATOM   1435 N N   . HIS A 1 181 ? 68.865  61.363 42.992  1.00 140.95 ? 184 HIS A N   1 
ATOM   1436 C CA  . HIS A 1 181 ? 69.549  60.398 43.895  1.00 142.06 ? 184 HIS A CA  1 
ATOM   1437 C C   . HIS A 1 181 ? 71.020  60.348 43.484  1.00 143.09 ? 184 HIS A C   1 
ATOM   1438 O O   . HIS A 1 181 ? 71.370  59.622 42.532  1.00 142.55 ? 184 HIS A O   1 
ATOM   1439 C CB  . HIS A 1 181 ? 68.889  59.016 43.818  1.00 140.27 ? 184 HIS A CB  1 
ATOM   1440 C CG  . HIS A 1 181 ? 67.415  59.043 44.032  1.00 141.21 ? 184 HIS A CG  1 
ATOM   1441 N ND1 . HIS A 1 181 ? 66.831  58.893 45.269  1.00 146.09 ? 184 HIS A ND1 1 
ATOM   1442 C CD2 . HIS A 1 181 ? 66.412  59.212 43.166  1.00 142.85 ? 184 HIS A CD2 1 
ATOM   1443 C CE1 . HIS A 1 181 ? 65.515  58.968 45.140  1.00 145.61 ? 184 HIS A CE1 1 
ATOM   1444 N NE2 . HIS A 1 181 ? 65.241  59.163 43.871  1.00 143.56 ? 184 HIS A NE2 1 
ATOM   1445 N N   . PRO A 1 182 ? 71.922  61.069 44.184  1.00 143.16 ? 185 PRO A N   1 
ATOM   1446 C CA  . PRO A 1 182 ? 73.322  61.137 43.768  1.00 143.86 ? 185 PRO A CA  1 
ATOM   1447 C C   . PRO A 1 182 ? 74.062  59.817 44.006  1.00 145.54 ? 185 PRO A C   1 
ATOM   1448 O O   . PRO A 1 182 ? 73.467  58.898 44.513  1.00 143.93 ? 185 PRO A O   1 
ATOM   1449 C CB  . PRO A 1 182 ? 73.891  62.249 44.661  1.00 145.65 ? 185 PRO A CB  1 
ATOM   1450 C CG  . PRO A 1 182 ? 73.019  62.235 45.894  1.00 137.01 ? 185 PRO A CG  1 
ATOM   1451 C CD  . PRO A 1 182 ? 71.644  61.827 45.403  1.00 137.89 ? 185 PRO A CD  1 
ATOM   1452 N N   . ASN A 1 183 ? 75.333  59.754 43.612  1.00 135.34 ? 186 ASN A N   1 
ATOM   1453 C CA  . ASN A 1 183 ? 76.135  58.527 43.840  1.00 142.57 ? 186 ASN A CA  1 
ATOM   1454 C C   . ASN A 1 183 ? 76.985  58.709 45.099  1.00 150.54 ? 186 ASN A C   1 
ATOM   1455 O O   . ASN A 1 183 ? 77.133  57.726 45.844  1.00 149.34 ? 186 ASN A O   1 
ATOM   1456 C CB  . ASN A 1 183 ? 77.000  58.196 42.626  1.00 142.51 ? 186 ASN A CB  1 
ATOM   1457 C CG  . ASN A 1 183 ? 76.171  58.042 41.371  1.00 157.31 ? 186 ASN A CG  1 
ATOM   1458 O OD1 . ASN A 1 183 ? 75.288  57.192 41.312  1.00 184.05 ? 186 ASN A OD1 1 
ATOM   1459 N ND2 . ASN A 1 183 ? 76.442  58.862 40.371  1.00 182.05 ? 186 ASN A ND2 1 
ATOM   1460 N N   . ASP A 1 184 ? 77.517  59.915 45.326  1.00 143.28 ? 187 ASP A N   1 
ATOM   1461 C CA  . ASP A 1 184 ? 78.406  60.145 46.494  1.00 141.80 ? 187 ASP A CA  1 
ATOM   1462 C C   . ASP A 1 184 ? 77.841  61.248 47.384  1.00 141.12 ? 187 ASP A C   1 
ATOM   1463 O O   . ASP A 1 184 ? 77.124  62.114 46.856  1.00 142.10 ? 187 ASP A O   1 
ATOM   1464 C CB  . ASP A 1 184 ? 79.812  60.560 46.064  1.00 142.59 ? 187 ASP A CB  1 
ATOM   1465 C CG  . ASP A 1 184 ? 80.566  59.527 45.245  1.00 150.12 ? 187 ASP A CG  1 
ATOM   1466 O OD1 . ASP A 1 184 ? 79.961  58.492 44.900  1.00 170.79 ? 187 ASP A OD1 1 
ATOM   1467 O OD2 . ASP A 1 184 ? 81.760  59.757 44.977  1.00 177.33 ? 187 ASP A OD2 1 
ATOM   1468 N N   . ALA A 1 185 ? 78.134  61.211 48.686  1.00 143.15 ? 188 ALA A N   1 
ATOM   1469 C CA  . ALA A 1 185 ? 77.738  62.335 49.562  1.00 142.70 ? 188 ALA A CA  1 
ATOM   1470 C C   . ALA A 1 185 ? 78.507  63.556 49.084  1.00 147.71 ? 188 ALA A C   1 
ATOM   1471 O O   . ALA A 1 185 ? 77.980  64.671 49.174  1.00 160.78 ? 188 ALA A O   1 
ATOM   1472 C CB  . ALA A 1 185 ? 78.104  62.029 50.980  1.00 144.44 ? 188 ALA A CB  1 
ATOM   1473 N N   . ALA A 1 186 ? 79.735  63.326 48.625  1.00 144.49 ? 189 ALA A N   1 
ATOM   1474 C CA  . ALA A 1 186 ? 80.547  64.428 48.079  1.00 147.65 ? 189 ALA A CA  1 
ATOM   1475 C C   . ALA A 1 186 ? 79.774  65.060 46.928  1.00 158.46 ? 189 ALA A C   1 
ATOM   1476 O O   . ALA A 1 186 ? 79.655  66.296 46.886  1.00 165.08 ? 189 ALA A O   1 
ATOM   1477 C CB  . ALA A 1 186 ? 81.854  63.871 47.593  1.00 148.70 ? 189 ALA A CB  1 
ATOM   1478 N N   . GLU A 1 187 ? 79.261  64.217 46.035  1.00 151.71 ? 190 GLU A N   1 
ATOM   1479 C CA  . GLU A 1 187 ? 78.453  64.737 44.908  1.00 153.29 ? 190 GLU A CA  1 
ATOM   1480 C C   . GLU A 1 187 ? 77.286  65.524 45.502  1.00 157.12 ? 190 GLU A C   1 
ATOM   1481 O O   . GLU A 1 187 ? 77.045  66.654 45.058  1.00 160.74 ? 190 GLU A O   1 
ATOM   1482 C CB  . GLU A 1 187 ? 77.964  63.586 44.032  1.00 148.69 ? 190 GLU A CB  1 
ATOM   1483 C CG  . GLU A 1 187 ? 77.115  64.033 42.856  1.00 144.13 ? 190 GLU A CG  1 
ATOM   1484 C CD  . GLU A 1 187 ? 76.862  62.934 41.838  1.00 139.99 ? 190 GLU A CD  1 
ATOM   1485 O OE1 . GLU A 1 187 ? 77.378  61.819 42.044  1.00 147.07 ? 190 GLU A OE1 1 
ATOM   1486 O OE2 . GLU A 1 187 ? 76.153  63.195 40.850  1.00 129.98 ? 190 GLU A OE2 1 
ATOM   1487 N N   . GLN A 1 188 ? 76.612  64.942 46.490  1.00 152.43 ? 191 GLN A N   1 
ATOM   1488 C CA  . GLN A 1 188 ? 75.433  65.628 47.073  1.00 153.70 ? 191 GLN A CA  1 
ATOM   1489 C C   . GLN A 1 188 ? 75.872  67.011 47.560  1.00 159.49 ? 191 GLN A C   1 
ATOM   1490 O O   . GLN A 1 188 ? 75.174  67.985 47.265  1.00 162.34 ? 191 GLN A O   1 
ATOM   1491 C CB  . GLN A 1 188 ? 74.848  64.818 48.226  1.00 157.58 ? 191 GLN A CB  1 
ATOM   1492 C CG  . GLN A 1 188 ? 73.767  65.556 48.997  1.00 162.77 ? 191 GLN A CG  1 
ATOM   1493 C CD  . GLN A 1 188 ? 73.430  64.818 50.266  1.00 173.69 ? 191 GLN A CD  1 
ATOM   1494 O OE1 . GLN A 1 188 ? 74.311  64.458 51.043  1.00 174.22 ? 191 GLN A OE1 1 
ATOM   1495 N NE2 . GLN A 1 188 ? 72.150  64.555 50.468  1.00 211.74 ? 191 GLN A NE2 1 
ATOM   1496 N N   . THR A 1 189 ? 76.999  67.077 48.264  1.00 157.72 ? 192 THR A N   1 
ATOM   1497 C CA  . THR A 1 189 ? 77.450  68.374 48.822  1.00 159.81 ? 192 THR A CA  1 
ATOM   1498 C C   . THR A 1 189 ? 77.785  69.332 47.677  1.00 162.43 ? 192 THR A C   1 
ATOM   1499 O O   . THR A 1 189 ? 77.509  70.533 47.821  1.00 170.98 ? 192 THR A O   1 
ATOM   1500 C CB  . THR A 1 189 ? 78.632  68.174 49.770  1.00 153.58 ? 192 THR A CB  1 
ATOM   1501 O OG1 . THR A 1 189 ? 79.679  67.551 49.030  1.00 154.62 ? 192 THR A OG1 1 
ATOM   1502 C CG2 . THR A 1 189 ? 78.266  67.323 50.965  1.00 150.72 ? 192 THR A CG2 1 
ATOM   1503 N N   . LYS A 1 190 ? 78.357  68.812 46.592  1.00 160.11 ? 193 LYS A N   1 
ATOM   1504 C CA  . LYS A 1 190 ? 78.747  69.675 45.448  1.00 156.29 ? 193 LYS A CA  1 
ATOM   1505 C C   . LYS A 1 190 ? 77.497  70.373 44.921  1.00 155.03 ? 193 LYS A C   1 
ATOM   1506 O O   . LYS A 1 190 ? 77.578  71.562 44.578  1.00 151.79 ? 193 LYS A O   1 
ATOM   1507 C CB  . LYS A 1 190 ? 79.360  68.830 44.334  1.00 156.35 ? 193 LYS A CB  1 
ATOM   1508 C CG  . LYS A 1 190 ? 80.772  68.327 44.600  1.00 161.27 ? 193 LYS A CG  1 
ATOM   1509 C CD  . LYS A 1 190 ? 81.205  67.191 43.700  1.00 180.00 ? 193 LYS A CD  1 
ATOM   1510 C CE  . LYS A 1 190 ? 82.382  66.429 44.276  1.00 157.78 ? 193 LYS A CE  1 
ATOM   1511 N NZ  . LYS A 1 190 ? 82.483  65.050 43.743  1.00 141.14 ? 193 LYS A NZ  1 
ATOM   1512 N N   . LEU A 1 191 ? 76.400  69.626 44.834  1.00 149.51 ? 194 LEU A N   1 
ATOM   1513 C CA  . LEU A 1 191 ? 75.136  70.196 44.310  1.00 151.76 ? 194 LEU A CA  1 
ATOM   1514 C C   . LEU A 1 191 ? 74.398  70.897 45.450  1.00 151.67 ? 194 LEU A C   1 
ATOM   1515 O O   . LEU A 1 191 ? 73.937  72.031 45.239  1.00 149.11 ? 194 LEU A O   1 
ATOM   1516 C CB  . LEU A 1 191 ? 74.309  69.033 43.766  1.00 150.63 ? 194 LEU A CB  1 
ATOM   1517 C CG  . LEU A 1 191 ? 75.057  68.055 42.861  1.00 142.20 ? 194 LEU A CG  1 
ATOM   1518 C CD1 . LEU A 1 191 ? 74.176  66.865 42.518  1.00 133.20 ? 194 LEU A CD1 1 
ATOM   1519 C CD2 . LEU A 1 191 ? 75.519  68.751 41.592  1.00 141.68 ? 194 LEU A CD2 1 
ATOM   1520 N N   . TYR A 1 192 ? 74.299  70.244 46.607  1.00 150.61 ? 195 TYR A N   1 
ATOM   1521 C CA  . TYR A 1 192 ? 73.559  70.802 47.765  1.00 152.14 ? 195 TYR A CA  1 
ATOM   1522 C C   . TYR A 1 192 ? 74.408  70.557 49.008  1.00 161.26 ? 195 TYR A C   1 
ATOM   1523 O O   . TYR A 1 192 ? 74.401  69.418 49.499  1.00 221.56 ? 195 TYR A O   1 
ATOM   1524 C CB  . TYR A 1 192 ? 72.214  70.089 47.874  1.00 150.71 ? 195 TYR A CB  1 
ATOM   1525 C CG  . TYR A 1 192 ? 71.613  69.749 46.538  1.00 147.80 ? 195 TYR A CG  1 
ATOM   1526 C CD1 . TYR A 1 192 ? 71.083  70.738 45.732  1.00 155.32 ? 195 TYR A CD1 1 
ATOM   1527 C CD2 . TYR A 1 192 ? 71.638  68.455 46.045  1.00 146.56 ? 195 TYR A CD2 1 
ATOM   1528 C CE1 . TYR A 1 192 ? 70.553  70.447 44.489  1.00 145.63 ? 195 TYR A CE1 1 
ATOM   1529 C CE2 . TYR A 1 192 ? 71.116  68.147 44.800  1.00 141.37 ? 195 TYR A CE2 1 
ATOM   1530 C CZ  . TYR A 1 192 ? 70.570  69.148 44.016  1.00 143.01 ? 195 TYR A CZ  1 
ATOM   1531 O OH  . TYR A 1 192 ? 70.046  68.872 42.778  1.00 137.40 ? 195 TYR A OH  1 
ATOM   1532 N N   . GLN A 1 193 ? 75.069  71.591 49.535  1.00 162.15 ? 196 GLN A N   1 
ATOM   1533 C CA  . GLN A 1 193 ? 76.026  71.383 50.660  1.00 163.80 ? 196 GLN A CA  1 
ATOM   1534 C C   . GLN A 1 193 ? 75.327  70.781 51.883  1.00 164.06 ? 196 GLN A C   1 
ATOM   1535 O O   . GLN A 1 193 ? 76.035  70.315 52.785  1.00 170.37 ? 196 GLN A O   1 
ATOM   1536 C CB  . GLN A 1 193 ? 76.729  72.696 51.006  1.00 164.59 ? 196 GLN A CB  1 
ATOM   1537 C CG  . GLN A 1 193 ? 77.694  73.165 49.929  1.00 170.35 ? 196 GLN A CG  1 
ATOM   1538 C CD  . GLN A 1 193 ? 78.825  73.988 50.495  1.00 175.67 ? 196 GLN A CD  1 
ATOM   1539 O OE1 . GLN A 1 193 ? 79.671  74.501 49.767  1.00 159.10 ? 196 GLN A OE1 1 
ATOM   1540 N NE2 . GLN A 1 193 ? 78.838  74.128 51.809  1.00 166.87 ? 196 GLN A NE2 1 
ATOM   1541 N N   . ASN A 1 194 ? 74.000  70.790 51.910  1.00 158.60 ? 197 ASN A N   1 
ATOM   1542 C CA  . ASN A 1 194 ? 73.276  70.148 53.032  1.00 160.53 ? 197 ASN A CA  1 
ATOM   1543 C C   . ASN A 1 194 ? 73.242  68.631 52.796  1.00 162.23 ? 197 ASN A C   1 
ATOM   1544 O O   . ASN A 1 194 ? 72.775  68.224 51.722  1.00 165.62 ? 197 ASN A O   1 
ATOM   1545 C CB  . ASN A 1 194 ? 71.880  70.753 53.185  1.00 161.16 ? 197 ASN A CB  1 
ATOM   1546 C CG  . ASN A 1 194 ? 71.883  72.265 53.289  1.00 156.01 ? 197 ASN A CG  1 
ATOM   1547 O OD1 . ASN A 1 194 ? 72.383  72.955 52.404  1.00 158.16 ? 197 ASN A OD1 1 
ATOM   1548 N ND2 . ASN A 1 194 ? 71.322  72.789 54.366  1.00 156.44 ? 197 ASN A ND2 1 
ATOM   1549 N N   . PRO A 1 195 ? 73.686  67.760 53.737  1.00 160.50 ? 198 PRO A N   1 
ATOM   1550 C CA  . PRO A 1 195 ? 73.562  66.309 53.554  1.00 162.32 ? 198 PRO A CA  1 
ATOM   1551 C C   . PRO A 1 195 ? 72.211  65.786 54.064  1.00 161.42 ? 198 PRO A C   1 
ATOM   1552 O O   . PRO A 1 195 ? 71.464  66.572 54.620  1.00 161.64 ? 198 PRO A O   1 
ATOM   1553 C CB  . PRO A 1 195 ? 74.696  65.768 54.432  1.00 148.49 ? 198 PRO A CB  1 
ATOM   1554 C CG  . PRO A 1 195 ? 74.731  66.729 55.597  1.00 156.54 ? 198 PRO A CG  1 
ATOM   1555 C CD  . PRO A 1 195 ? 74.361  68.076 55.009  1.00 157.93 ? 198 PRO A CD  1 
ATOM   1556 N N   . THR A 1 196 ? 71.928  64.494 53.859  1.00 165.64 ? 199 THR A N   1 
ATOM   1557 C CA  . THR A 1 196 ? 70.664  63.885 54.360  1.00 171.45 ? 199 THR A CA  1 
ATOM   1558 C C   . THR A 1 196 ? 69.518  64.883 54.171  1.00 170.62 ? 199 THR A C   1 
ATOM   1559 O O   . THR A 1 196 ? 68.946  65.319 55.190  1.00 172.09 ? 199 THR A O   1 
ATOM   1560 C CB  . THR A 1 196 ? 70.806  63.432 55.819  1.00 164.28 ? 199 THR A CB  1 
ATOM   1561 O OG1 . THR A 1 196 ? 71.003  64.586 56.637  1.00 163.62 ? 199 THR A OG1 1 
ATOM   1562 C CG2 . THR A 1 196 ? 71.950  62.463 56.022  1.00 150.94 ? 199 THR A CG2 1 
ATOM   1563 N N   . THR A 1 197 ? 69.187  65.217 52.921  1.00 167.87 ? 200 THR A N   1 
ATOM   1564 C CA  . THR A 1 197 ? 68.159  66.262 52.662  1.00 162.00 ? 200 THR A CA  1 
ATOM   1565 C C   . THR A 1 197 ? 66.744  65.676 52.672  1.00 156.10 ? 200 THR A C   1 
ATOM   1566 O O   . THR A 1 197 ? 66.617  64.436 52.645  1.00 151.73 ? 200 THR A O   1 
ATOM   1567 C CB  . THR A 1 197 ? 68.424  66.956 51.322  1.00 159.45 ? 200 THR A CB  1 
ATOM   1568 O OG1 . THR A 1 197 ? 68.114  66.037 50.275  1.00 164.35 ? 200 THR A OG1 1 
ATOM   1569 C CG2 . THR A 1 197 ? 69.854  67.430 51.184  1.00 158.84 ? 200 THR A CG2 1 
ATOM   1570 N N   . TYR A 1 198 ? 65.729  66.544 52.710  1.00 152.27 ? 201 TYR A N   1 
ATOM   1571 C CA  . TYR A 1 198 ? 64.311  66.099 52.674  1.00 145.81 ? 201 TYR A CA  1 
ATOM   1572 C C   . TYR A 1 198 ? 63.562  66.907 51.614  1.00 146.18 ? 201 TYR A C   1 
ATOM   1573 O O   . TYR A 1 198 ? 64.011  68.009 51.281  1.00 151.10 ? 201 TYR A O   1 
ATOM   1574 C CB  . TYR A 1 198 ? 63.643  66.265 54.041  1.00 146.97 ? 201 TYR A CB  1 
ATOM   1575 C CG  . TYR A 1 198 ? 63.225  67.672 54.391  1.00 152.76 ? 201 TYR A CG  1 
ATOM   1576 C CD1 . TYR A 1 198 ? 62.004  68.186 53.985  1.00 154.31 ? 201 TYR A CD1 1 
ATOM   1577 C CD2 . TYR A 1 198 ? 64.055  68.499 55.128  1.00 160.72 ? 201 TYR A CD2 1 
ATOM   1578 C CE1 . TYR A 1 198 ? 61.620  69.480 54.295  1.00 156.49 ? 201 TYR A CE1 1 
ATOM   1579 C CE2 . TYR A 1 198 ? 63.690  69.796 55.449  1.00 159.81 ? 201 TYR A CE2 1 
ATOM   1580 C CZ  . TYR A 1 198 ? 62.467  70.289 55.030  1.00 157.64 ? 201 TYR A CZ  1 
ATOM   1581 O OH  . TYR A 1 198 ? 62.090  71.569 55.342  1.00 159.52 ? 201 TYR A OH  1 
ATOM   1582 N N   . ILE A 1 199 ? 62.470  66.357 51.085  1.00 148.87 ? 202 ILE A N   1 
ATOM   1583 C CA  . ILE A 1 199 ? 61.636  67.074 50.076  1.00 151.85 ? 202 ILE A CA  1 
ATOM   1584 C C   . ILE A 1 199 ? 60.175  66.918 50.497  1.00 156.36 ? 202 ILE A C   1 
ATOM   1585 O O   . ILE A 1 199 ? 59.695  65.770 50.561  1.00 158.29 ? 202 ILE A O   1 
ATOM   1586 C CB  . ILE A 1 199 ? 61.872  66.511 48.664  1.00 146.17 ? 202 ILE A CB  1 
ATOM   1587 C CG1 . ILE A 1 199 ? 63.292  66.809 48.178  1.00 144.51 ? 202 ILE A CG1 1 
ATOM   1588 C CG2 . ILE A 1 199 ? 60.821  67.018 47.687  1.00 146.21 ? 202 ILE A CG2 1 
ATOM   1589 C CD1 . ILE A 1 199 ? 63.691  66.018 46.965  1.00 145.09 ? 202 ILE A CD1 1 
ATOM   1590 N N   . SER A 1 200 ? 59.498  68.023 50.802  1.00 149.02 ? 203 SER A N   1 
ATOM   1591 C CA  . SER A 1 200 ? 58.116  67.878 51.308  1.00 150.67 ? 203 SER A CA  1 
ATOM   1592 C C   . SER A 1 200 ? 57.133  68.383 50.257  1.00 151.79 ? 203 SER A C   1 
ATOM   1593 O O   . SER A 1 200 ? 57.206  69.578 49.908  1.00 148.48 ? 203 SER A O   1 
ATOM   1594 C CB  . SER A 1 200 ? 57.928  68.603 52.611  1.00 163.03 ? 203 SER A CB  1 
ATOM   1595 O OG  . SER A 1 200 ? 57.509  69.938 52.377  1.00 193.47 ? 203 SER A OG  1 
ATOM   1596 N N   . VAL A 1 201 ? 56.213  67.526 49.806  1.00 145.71 ? 204 VAL A N   1 
ATOM   1597 C CA  . VAL A 1 201 ? 55.158  67.977 48.849  1.00 144.75 ? 204 VAL A CA  1 
ATOM   1598 C C   . VAL A 1 201 ? 53.856  68.164 49.632  1.00 157.69 ? 204 VAL A C   1 
ATOM   1599 O O   . VAL A 1 201 ? 53.292  67.146 50.078  1.00 171.85 ? 204 VAL A O   1 
ATOM   1600 C CB  . VAL A 1 201 ? 54.978  66.977 47.692  1.00 146.68 ? 204 VAL A CB  1 
ATOM   1601 C CG1 . VAL A 1 201 ? 53.934  67.458 46.695  1.00 145.95 ? 204 VAL A CG1 1 
ATOM   1602 C CG2 . VAL A 1 201 ? 56.298  66.690 46.994  1.00 152.94 ? 204 VAL A CG2 1 
ATOM   1603 N N   . GLY A 1 202 ? 53.402  69.411 49.796  1.00 152.71 ? 205 GLY A N   1 
ATOM   1604 C CA  . GLY A 1 202 ? 52.191  69.677 50.598  1.00 168.66 ? 205 GLY A CA  1 
ATOM   1605 C C   . GLY A 1 202 ? 51.021  70.142 49.748  1.00 172.65 ? 205 GLY A C   1 
ATOM   1606 O O   . GLY A 1 202 ? 51.003  71.330 49.375  1.00 179.36 ? 205 GLY A O   1 
ATOM   1607 N N   . THR A 1 203 ? 50.069  69.247 49.466  1.00 182.84 ? 206 THR A N   1 
ATOM   1608 C CA  . THR A 1 203 ? 48.856  69.631 48.695  1.00 179.65 ? 206 THR A CA  1 
ATOM   1609 C C   . THR A 1 203 ? 47.631  69.573 49.616  1.00 185.79 ? 206 THR A C   1 
ATOM   1610 O O   . THR A 1 203 ? 47.813  69.320 50.822  1.00 184.37 ? 206 THR A O   1 
ATOM   1611 C CB  . THR A 1 203 ? 48.677  68.745 47.455  1.00 176.62 ? 206 THR A CB  1 
ATOM   1612 O OG1 . THR A 1 203 ? 48.133  67.493 47.871  1.00 186.90 ? 206 THR A OG1 1 
ATOM   1613 C CG2 . THR A 1 203 ? 49.970  68.523 46.700  1.00 171.54 ? 206 THR A CG2 1 
ATOM   1614 N N   . SER A 1 204 ? 46.436  69.811 49.067  1.00 185.11 ? 207 SER A N   1 
ATOM   1615 C CA  . SER A 1 204 ? 45.191  69.756 49.877  1.00 186.81 ? 207 SER A CA  1 
ATOM   1616 C C   . SER A 1 204 ? 44.816  68.296 50.147  1.00 185.74 ? 207 SER A C   1 
ATOM   1617 O O   . SER A 1 204 ? 44.237  68.025 51.217  1.00 185.59 ? 207 SER A O   1 
ATOM   1618 C CB  . SER A 1 204 ? 44.067  70.477 49.188  1.00 185.95 ? 207 SER A CB  1 
ATOM   1619 O OG  . SER A 1 204 ? 43.622  69.742 48.057  1.00 187.17 ? 207 SER A OG  1 
ATOM   1620 N N   . THR A 1 205 ? 45.130  67.397 49.210  1.00 204.46 ? 208 THR A N   1 
ATOM   1621 C CA  . THR A 1 205 ? 44.749  65.968 49.361  1.00 192.09 ? 208 THR A CA  1 
ATOM   1622 C C   . THR A 1 205 ? 45.962  65.083 49.667  1.00 189.85 ? 208 THR A C   1 
ATOM   1623 O O   . THR A 1 205 ? 45.814  64.183 50.513  1.00 184.75 ? 208 THR A O   1 
ATOM   1624 C CB  . THR A 1 205 ? 44.090  65.463 48.074  1.00 190.57 ? 208 THR A CB  1 
ATOM   1625 O OG1 . THR A 1 205 ? 45.118  65.342 47.090  1.00 190.14 ? 208 THR A OG1 1 
ATOM   1626 C CG2 . THR A 1 205 ? 43.002  66.385 47.565  1.00 182.28 ? 208 THR A CG2 1 
ATOM   1627 N N   . LEU A 1 206 ? 47.106  65.311 49.015  1.00 190.10 ? 209 LEU A N   1 
ATOM   1628 C CA  . LEU A 1 206 ? 48.256  64.380 49.201  1.00 189.18 ? 209 LEU A CA  1 
ATOM   1629 C C   . LEU A 1 206 ? 49.478  65.098 49.779  1.00 189.04 ? 209 LEU A C   1 
ATOM   1630 O O   . LEU A 1 206 ? 49.906  66.099 49.178  1.00 187.25 ? 209 LEU A O   1 
ATOM   1631 C CB  . LEU A 1 206 ? 48.587  63.758 47.840  1.00 191.72 ? 209 LEU A CB  1 
ATOM   1632 C CG  . LEU A 1 206 ? 47.493  62.870 47.246  1.00 188.49 ? 209 LEU A CG  1 
ATOM   1633 C CD1 . LEU A 1 206 ? 47.899  62.325 45.885  1.00 180.70 ? 209 LEU A CD1 1 
ATOM   1634 C CD2 . LEU A 1 206 ? 47.143  61.728 48.189  1.00 183.23 ? 209 LEU A CD2 1 
ATOM   1635 N N   . ASN A 1 207 ? 50.029  64.585 50.884  1.00 187.42 ? 210 ASN A N   1 
ATOM   1636 C CA  . ASN A 1 207 ? 51.284  65.160 51.446  1.00 188.40 ? 210 ASN A CA  1 
ATOM   1637 C C   . ASN A 1 207 ? 52.317  64.043 51.599  1.00 183.87 ? 210 ASN A C   1 
ATOM   1638 O O   . ASN A 1 207 ? 52.109  63.158 52.454  1.00 179.65 ? 210 ASN A O   1 
ATOM   1639 C CB  . ASN A 1 207 ? 51.080  65.896 52.770  1.00 189.15 ? 210 ASN A CB  1 
ATOM   1640 C CG  . ASN A 1 207 ? 50.442  67.258 52.603  1.00 191.97 ? 210 ASN A CG  1 
ATOM   1641 O OD1 . ASN A 1 207 ? 49.916  67.573 51.541  1.00 197.42 ? 210 ASN A OD1 1 
ATOM   1642 N ND2 . ASN A 1 207 ? 50.454  68.058 53.657  1.00 202.33 ? 210 ASN A ND2 1 
ATOM   1643 N N   . GLN A 1 208 ? 53.384  64.098 50.799  1.00 174.05 ? 211 GLN A N   1 
ATOM   1644 C CA  . GLN A 1 208 ? 54.420  63.033 50.833  1.00 164.80 ? 211 GLN A CA  1 
ATOM   1645 C C   . GLN A 1 208 ? 55.789  63.671 51.062  1.00 149.55 ? 211 GLN A C   1 
ATOM   1646 O O   . GLN A 1 208 ? 56.162  64.568 50.281  1.00 154.47 ? 211 GLN A O   1 
ATOM   1647 C CB  . GLN A 1 208 ? 54.451  62.272 49.508  1.00 164.80 ? 211 GLN A CB  1 
ATOM   1648 C CG  . GLN A 1 208 ? 53.274  61.332 49.280  1.00 182.78 ? 211 GLN A CG  1 
ATOM   1649 C CD  . GLN A 1 208 ? 51.944  62.038 49.180  1.00 194.42 ? 211 GLN A CD  1 
ATOM   1650 O OE1 . GLN A 1 208 ? 51.800  63.041 48.484  1.00 238.90 ? 211 GLN A OE1 1 
ATOM   1651 N NE2 . GLN A 1 208 ? 50.965  61.538 49.915  1.00 190.00 ? 211 GLN A NE2 1 
ATOM   1652 N N   . ARG A 1 209 ? 56.502  63.224 52.094  1.00 169.60 ? 212 ARG A N   1 
ATOM   1653 C CA  . ARG A 1 209 ? 57.883  63.726 52.320  1.00 163.06 ? 212 ARG A CA  1 
ATOM   1654 C C   . ARG A 1 209 ? 58.843  62.689 51.743  1.00 167.72 ? 212 ARG A C   1 
ATOM   1655 O O   . ARG A 1 209 ? 58.667  61.494 52.065  1.00 165.70 ? 212 ARG A O   1 
ATOM   1656 C CB  . ARG A 1 209 ? 58.151  63.963 53.807  1.00 166.32 ? 212 ARG A CB  1 
ATOM   1657 C CG  . ARG A 1 209 ? 57.552  65.262 54.328  1.00 169.60 ? 212 ARG A CG  1 
ATOM   1658 C CD  . ARG A 1 209 ? 57.932  65.541 55.766  1.00 176.26 ? 212 ARG A CD  1 
ATOM   1659 N NE  . ARG A 1 209 ? 56.887  66.284 56.453  1.00 187.49 ? 212 ARG A NE  1 
ATOM   1660 C CZ  . ARG A 1 209 ? 56.907  66.600 57.742  1.00 184.85 ? 212 ARG A CZ  1 
ATOM   1661 N NH1 . ARG A 1 209 ? 57.942  66.263 58.491  1.00 181.03 ? 212 ARG A NH1 1 
ATOM   1662 N NH2 . ARG A 1 209 ? 55.887  67.246 58.282  1.00 182.24 ? 212 ARG A NH2 1 
ATOM   1663 N N   . LEU A 1 210 ? 59.791  63.117 50.906  1.00 157.56 ? 213 LEU A N   1 
ATOM   1664 C CA  . LEU A 1 210 ? 60.663  62.120 50.232  1.00 149.78 ? 213 LEU A CA  1 
ATOM   1665 C C   . LEU A 1 210 ? 62.132  62.383 50.572  1.00 147.37 ? 213 LEU A C   1 
ATOM   1666 O O   . LEU A 1 210 ? 62.501  63.560 50.748  1.00 140.03 ? 213 LEU A O   1 
ATOM   1667 C CB  . LEU A 1 210 ? 60.376  62.189 48.731  1.00 145.36 ? 213 LEU A CB  1 
ATOM   1668 C CG  . LEU A 1 210 ? 58.890  62.171 48.358  1.00 156.13 ? 213 LEU A CG  1 
ATOM   1669 C CD1 . LEU A 1 210 ? 58.626  62.892 47.043  1.00 155.61 ? 213 LEU A CD1 1 
ATOM   1670 C CD2 . LEU A 1 210 ? 58.339  60.752 48.315  1.00 162.87 ? 213 LEU A CD2 1 
ATOM   1671 N N   . VAL A 1 211 ? 62.924  61.314 50.695  1.00 152.64 ? 214 VAL A N   1 
ATOM   1672 C CA  . VAL A 1 211 ? 64.364  61.434 51.055  1.00 147.23 ? 214 VAL A CA  1 
ATOM   1673 C C   . VAL A 1 211 ? 65.178  60.733 49.963  1.00 150.86 ? 214 VAL A C   1 
ATOM   1674 O O   . VAL A 1 211 ? 64.844  59.582 49.612  1.00 151.44 ? 214 VAL A O   1 
ATOM   1675 C CB  . VAL A 1 211 ? 64.627  60.831 52.446  1.00 142.93 ? 214 VAL A CB  1 
ATOM   1676 C CG1 . VAL A 1 211 ? 66.111  60.630 52.720  1.00 146.56 ? 214 VAL A CG1 1 
ATOM   1677 C CG2 . VAL A 1 211 ? 63.983  61.656 53.549  1.00 144.18 ? 214 VAL A CG2 1 
ATOM   1678 N N   . PRO A 1 212 ? 66.212  61.380 49.387  1.00 151.41 ? 215 PRO A N   1 
ATOM   1679 C CA  . PRO A 1 212 ? 66.993  60.790 48.297  1.00 144.55 ? 215 PRO A CA  1 
ATOM   1680 C C   . PRO A 1 212 ? 67.870  59.622 48.753  1.00 140.27 ? 215 PRO A C   1 
ATOM   1681 O O   . PRO A 1 212 ? 68.480  59.742 49.788  1.00 140.67 ? 215 PRO A O   1 
ATOM   1682 C CB  . PRO A 1 212 ? 67.930  61.921 47.853  1.00 142.36 ? 215 PRO A CB  1 
ATOM   1683 C CG  . PRO A 1 212 ? 68.002  62.856 49.036  1.00 149.64 ? 215 PRO A CG  1 
ATOM   1684 C CD  . PRO A 1 212 ? 66.666  62.723 49.740  1.00 150.33 ? 215 PRO A CD  1 
ATOM   1685 N N   . ARG A 1 213 ? 67.929  58.555 47.952  1.00 140.31 ? 216 ARG A N   1 
ATOM   1686 C CA  . ARG A 1 213 ? 68.778  57.386 48.291  1.00 141.49 ? 216 ARG A CA  1 
ATOM   1687 C C   . ARG A 1 213 ? 70.163  57.571 47.670  1.00 138.00 ? 216 ARG A C   1 
ATOM   1688 O O   . ARG A 1 213 ? 70.324  57.249 46.479  1.00 143.11 ? 216 ARG A O   1 
ATOM   1689 C CB  . ARG A 1 213 ? 68.151  56.092 47.771  1.00 154.92 ? 216 ARG A CB  1 
ATOM   1690 C CG  . ARG A 1 213 ? 66.791  55.762 48.366  1.00 170.75 ? 216 ARG A CG  1 
ATOM   1691 C CD  . ARG A 1 213 ? 66.223  54.478 47.789  1.00 177.79 ? 216 ARG A CD  1 
ATOM   1692 N NE  . ARG A 1 213 ? 66.031  54.583 46.350  1.00 167.75 ? 216 ARG A NE  1 
ATOM   1693 C CZ  . ARG A 1 213 ? 64.854  54.502 45.742  1.00 173.34 ? 216 ARG A CZ  1 
ATOM   1694 N NH1 . ARG A 1 213 ? 63.757  54.294 46.447  1.00 183.96 ? 216 ARG A NH1 1 
ATOM   1695 N NH2 . ARG A 1 213 ? 64.775  54.634 44.429  1.00 176.64 ? 216 ARG A NH2 1 
ATOM   1696 N N   . ILE A 1 214 ? 71.122  58.049 48.464  1.00 139.80 ? 217 ILE A N   1 
ATOM   1697 C CA  . ILE A 1 214 ? 72.510  58.265 47.967  1.00 141.45 ? 217 ILE A CA  1 
ATOM   1698 C C   . ILE A 1 214 ? 73.185  56.906 47.799  1.00 138.77 ? 217 ILE A C   1 
ATOM   1699 O O   . ILE A 1 214 ? 73.438  56.240 48.821  1.00 136.15 ? 217 ILE A O   1 
ATOM   1700 C CB  . ILE A 1 214 ? 73.293  59.152 48.947  1.00 141.08 ? 217 ILE A CB  1 
ATOM   1701 C CG1 . ILE A 1 214 ? 72.480  60.372 49.387  1.00 146.34 ? 217 ILE A CG1 1 
ATOM   1702 C CG2 . ILE A 1 214 ? 74.632  59.554 48.351  1.00 141.83 ? 217 ILE A CG2 1 
ATOM   1703 C CD1 . ILE A 1 214 ? 73.151  61.171 50.482  1.00 153.06 ? 217 ILE A CD1 1 
ATOM   1704 N N   . ALA A 1 215 ? 73.469  56.528 46.552  1.00 142.45 ? 218 ALA A N   1 
ATOM   1705 C CA  . ALA A 1 215 ? 74.126  55.234 46.274  1.00 140.85 ? 218 ALA A CA  1 
ATOM   1706 C C   . ALA A 1 215 ? 74.588  55.202 44.816  1.00 148.42 ? 218 ALA A C   1 
ATOM   1707 O O   . ALA A 1 215 ? 73.788  55.575 43.941  1.00 151.26 ? 218 ALA A O   1 
ATOM   1708 C CB  . ALA A 1 215 ? 73.160  54.120 46.563  1.00 139.53 ? 218 ALA A CB  1 
ATOM   1709 N N   . THR A 1 216 ? 75.826  54.772 44.570  1.00 149.23 ? 219 THR A N   1 
ATOM   1710 C CA  . THR A 1 216 ? 76.315  54.635 43.176  1.00 147.35 ? 219 THR A CA  1 
ATOM   1711 C C   . THR A 1 216 ? 75.601  53.453 42.521  1.00 143.30 ? 219 THR A C   1 
ATOM   1712 O O   . THR A 1 216 ? 75.460  52.416 43.190  1.00 137.32 ? 219 THR A O   1 
ATOM   1713 C CB  . THR A 1 216 ? 77.828  54.419 43.137  1.00 147.26 ? 219 THR A CB  1 
ATOM   1714 O OG1 . THR A 1 216 ? 78.075  53.045 43.437  1.00 159.02 ? 219 THR A OG1 1 
ATOM   1715 C CG2 . THR A 1 216 ? 78.578  55.296 44.114  1.00 148.85 ? 219 THR A CG2 1 
ATOM   1716 N N   . ARG A 1 217 ? 75.174  53.607 41.269  1.00 141.59 ? 220 ARG A N   1 
ATOM   1717 C CA  . ARG A 1 217 ? 74.489  52.507 40.544  1.00 141.43 ? 220 ARG A CA  1 
ATOM   1718 C C   . ARG A 1 217 ? 75.185  52.283 39.200  1.00 142.55 ? 220 ARG A C   1 
ATOM   1719 O O   . ARG A 1 217 ? 76.367  52.632 39.080  1.00 150.80 ? 220 ARG A O   1 
ATOM   1720 C CB  . ARG A 1 217 ? 73.014  52.854 40.355  1.00 145.99 ? 220 ARG A CB  1 
ATOM   1721 C CG  . ARG A 1 217 ? 72.379  53.477 41.590  1.00 142.34 ? 220 ARG A CG  1 
ATOM   1722 C CD  . ARG A 1 217 ? 70.868  53.587 41.579  1.00 151.02 ? 220 ARG A CD  1 
ATOM   1723 N NE  . ARG A 1 217 ? 70.426  54.272 42.785  1.00 152.20 ? 220 ARG A NE  1 
ATOM   1724 C CZ  . ARG A 1 217 ? 69.156  54.444 43.132  1.00 156.68 ? 220 ARG A CZ  1 
ATOM   1725 N NH1 . ARG A 1 217 ? 68.200  53.802 42.486  1.00 161.61 ? 220 ARG A NH1 1 
ATOM   1726 N NH2 . ARG A 1 217 ? 68.847  55.242 44.139  1.00 154.21 ? 220 ARG A NH2 1 
ATOM   1727 N N   . SER A 1 218 ? 74.476  51.701 38.235  1.00 139.59 ? 221 SER A N   1 
ATOM   1728 C CA  . SER A 1 218 ? 75.093  51.429 36.914  1.00 144.33 ? 221 SER A CA  1 
ATOM   1729 C C   . SER A 1 218 ? 75.193  52.729 36.120  1.00 146.67 ? 221 SER A C   1 
ATOM   1730 O O   . SER A 1 218 ? 74.339  53.614 36.321  1.00 144.88 ? 221 SER A O   1 
ATOM   1731 C CB  . SER A 1 218 ? 74.329  50.387 36.152  1.00 155.36 ? 221 SER A CB  1 
ATOM   1732 O OG  . SER A 1 218 ? 72.955  50.729 36.073  1.00 184.72 ? 221 SER A OG  1 
ATOM   1733 N N   . LYS A 1 219 ? 76.199  52.835 35.254  1.00 149.91 ? 222 LYS A N   1 
ATOM   1734 C CA  . LYS A 1 219 ? 76.399  54.076 34.461  1.00 148.72 ? 222 LYS A CA  1 
ATOM   1735 C C   . LYS A 1 219 ? 75.418  54.088 33.287  1.00 145.46 ? 222 LYS A C   1 
ATOM   1736 O O   . LYS A 1 219 ? 75.477  53.166 32.460  1.00 150.61 ? 222 LYS A O   1 
ATOM   1737 C CB  . LYS A 1 219 ? 77.844  54.146 33.970  1.00 152.53 ? 222 LYS A CB  1 
ATOM   1738 C CG  . LYS A 1 219 ? 78.892  54.196 35.075  1.00 160.97 ? 222 LYS A CG  1 
ATOM   1739 C CD  . LYS A 1 219 ? 80.319  54.073 34.574  1.00 171.33 ? 222 LYS A CD  1 
ATOM   1740 C CE  . LYS A 1 219 ? 81.337  54.120 35.696  1.00 179.42 ? 222 LYS A CE  1 
ATOM   1741 N NZ  . LYS A 1 219 ? 82.723  53.911 35.215  1.00 179.40 ? 222 LYS A NZ  1 
ATOM   1742 N N   . VAL A 1 220 ? 74.550  55.096 33.229  1.00 148.20 ? 223 VAL A N   1 
ATOM   1743 C CA  . VAL A 1 220 ? 73.602  55.227 32.087  1.00 148.18 ? 223 VAL A CA  1 
ATOM   1744 C C   . VAL A 1 220 ? 73.756  56.640 31.527  1.00 145.46 ? 223 VAL A C   1 
ATOM   1745 O O   . VAL A 1 220 ? 73.733  57.598 32.317  1.00 148.69 ? 223 VAL A O   1 
ATOM   1746 C CB  . VAL A 1 220 ? 72.153  54.969 32.526  1.00 148.10 ? 223 VAL A CB  1 
ATOM   1747 C CG1 . VAL A 1 220 ? 71.179  55.106 31.366  1.00 149.74 ? 223 VAL A CG1 1 
ATOM   1748 C CG2 . VAL A 1 220 ? 72.009  53.615 33.197  1.00 151.46 ? 223 VAL A CG2 1 
ATOM   1749 N N   . ASN A 1 221 ? 73.952  56.752 30.220  1.00 147.16 ? 224 ASN A N   1 
ATOM   1750 C CA  . ASN A 1 221 ? 74.163  58.099 29.644  1.00 141.25 ? 224 ASN A CA  1 
ATOM   1751 C C   . ASN A 1 221 ? 75.255  58.790 30.457  1.00 143.29 ? 224 ASN A C   1 
ATOM   1752 O O   . ASN A 1 221 ? 75.117  59.995 30.703  1.00 139.19 ? 224 ASN A O   1 
ATOM   1753 C CB  . ASN A 1 221 ? 72.865  58.890 29.624  1.00 141.57 ? 224 ASN A CB  1 
ATOM   1754 C CG  . ASN A 1 221 ? 71.830  58.238 28.739  1.00 144.78 ? 224 ASN A CG  1 
ATOM   1755 O OD1 . ASN A 1 221 ? 72.113  57.241 28.085  1.00 146.63 ? 224 ASN A OD1 1 
ATOM   1756 N ND2 . ASN A 1 221 ? 70.634  58.798 28.700  1.00 144.72 ? 224 ASN A ND2 1 
ATOM   1757 N N   . GLY A 1 222 ? 76.265  58.037 30.900  1.00 148.35 ? 225 GLY A N   1 
ATOM   1758 C CA  . GLY A 1 222 ? 77.423  58.633 31.597  1.00 151.81 ? 225 GLY A CA  1 
ATOM   1759 C C   . GLY A 1 222 ? 77.120  59.034 33.028  1.00 148.58 ? 225 GLY A C   1 
ATOM   1760 O O   . GLY A 1 222 ? 77.973  59.701 33.639  1.00 152.91 ? 225 GLY A O   1 
ATOM   1761 N N   . GLN A 1 223 ? 75.946  58.670 33.544  1.00 142.53 ? 226 GLN A N   1 
ATOM   1762 C CA  . GLN A 1 223 ? 75.603  59.124 34.913  1.00 146.88 ? 226 GLN A CA  1 
ATOM   1763 C C   . GLN A 1 223 ? 74.939  57.965 35.661  1.00 145.91 ? 226 GLN A C   1 
ATOM   1764 O O   . GLN A 1 223 ? 73.991  57.384 35.110  1.00 146.86 ? 226 GLN A O   1 
ATOM   1765 C CB  . GLN A 1 223 ? 74.740  60.386 34.827  1.00 143.80 ? 226 GLN A CB  1 
ATOM   1766 C CG  . GLN A 1 223 ? 75.470  61.583 34.234  1.00 145.68 ? 226 GLN A CG  1 
ATOM   1767 C CD  . GLN A 1 223 ? 74.547  62.744 33.963  1.00 145.12 ? 226 GLN A CD  1 
ATOM   1768 O OE1 . GLN A 1 223 ? 74.759  63.858 34.436  1.00 149.12 ? 226 GLN A OE1 1 
ATOM   1769 N NE2 . GLN A 1 223 ? 73.513  62.486 33.180  1.00 148.05 ? 226 GLN A NE2 1 
ATOM   1770 N N   . SER A 1 224 ? 75.449  57.621 36.848  1.00 145.69 ? 227 SER A N   1 
ATOM   1771 C CA  . SER A 1 224 ? 74.825  56.547 37.666  1.00 147.66 ? 227 SER A CA  1 
ATOM   1772 C C   . SER A 1 224 ? 73.855  57.158 38.675  1.00 148.23 ? 227 SER A C   1 
ATOM   1773 O O   . SER A 1 224 ? 73.171  56.392 39.366  1.00 150.02 ? 227 SER A O   1 
ATOM   1774 C CB  . SER A 1 224 ? 75.857  55.695 38.337  1.00 151.70 ? 227 SER A CB  1 
ATOM   1775 O OG  . SER A 1 224 ? 76.788  56.489 39.045  1.00 156.48 ? 227 SER A OG  1 
ATOM   1776 N N   . GLY A 1 225 ? 73.806  58.484 38.767  1.00 151.42 ? 228 GLY A N   1 
ATOM   1777 C CA  . GLY A 1 225 ? 72.789  59.106 39.635  1.00 150.47 ? 228 GLY A CA  1 
ATOM   1778 C C   . GLY A 1 225 ? 71.423  58.926 39.000  1.00 150.14 ? 228 GLY A C   1 
ATOM   1779 O O   . GLY A 1 225 ? 71.372  58.772 37.764  1.00 155.04 ? 228 GLY A O   1 
ATOM   1780 N N   . ARG A 1 226 ? 70.351  58.928 39.792  1.00 140.99 ? 229 ARG A N   1 
ATOM   1781 C CA  . ARG A 1 226 ? 69.013  58.646 39.215  1.00 139.45 ? 229 ARG A CA  1 
ATOM   1782 C C   . ARG A 1 226 ? 68.189  59.860 39.616  1.00 135.24 ? 229 ARG A C   1 
ATOM   1783 O O   . ARG A 1 226 ? 68.658  60.641 40.467  1.00 139.75 ? 229 ARG A O   1 
ATOM   1784 C CB  . ARG A 1 226 ? 68.413  57.376 39.817  1.00 144.88 ? 229 ARG A CB  1 
ATOM   1785 C CG  . ARG A 1 226 ? 69.145  56.097 39.446  1.00 147.04 ? 229 ARG A CG  1 
ATOM   1786 C CD  . ARG A 1 226 ? 69.112  55.832 37.955  1.00 143.97 ? 229 ARG A CD  1 
ATOM   1787 N NE  . ARG A 1 226 ? 69.816  54.597 37.648  1.00 141.91 ? 229 ARG A NE  1 
ATOM   1788 C CZ  . ARG A 1 226 ? 70.992  54.550 37.038  1.00 141.62 ? 229 ARG A CZ  1 
ATOM   1789 N NH1 . ARG A 1 226 ? 71.661  55.665 36.813  1.00 143.86 ? 229 ARG A NH1 1 
ATOM   1790 N NH2 . ARG A 1 226 ? 71.506  53.387 36.675  1.00 142.17 ? 229 ARG A NH2 1 
ATOM   1791 N N   . MET A 1 227 ? 67.007  59.999 39.014  1.00 133.17 ? 230 MET A N   1 
ATOM   1792 C CA  . MET A 1 227 ? 66.055  61.071 39.385  1.00 134.19 ? 230 MET A CA  1 
ATOM   1793 C C   . MET A 1 227 ? 64.646  60.482 39.348  1.00 131.73 ? 230 MET A C   1 
ATOM   1794 O O   . MET A 1 227 ? 64.263  59.928 38.304  1.00 129.00 ? 230 MET A O   1 
ATOM   1795 C CB  . MET A 1 227 ? 66.152  62.248 38.411  1.00 131.95 ? 230 MET A CB  1 
ATOM   1796 C CG  . MET A 1 227 ? 67.458  62.996 38.507  1.00 133.83 ? 230 MET A CG  1 
ATOM   1797 S SD  . MET A 1 227 ? 67.562  64.316 37.284  1.00 146.29 ? 230 MET A SD  1 
ATOM   1798 C CE  . MET A 1 227 ? 66.392  65.479 37.982  1.00 138.71 ? 230 MET A CE  1 
ATOM   1799 N N   . GLU A 1 228 ? 63.937  60.525 40.475  1.00 134.26 ? 231 GLU A N   1 
ATOM   1800 C CA  . GLU A 1 228 ? 62.559  59.975 40.477  1.00 135.09 ? 231 GLU A CA  1 
ATOM   1801 C C   . GLU A 1 228 ? 61.665  61.124 40.015  1.00 130.52 ? 231 GLU A C   1 
ATOM   1802 O O   . GLU A 1 228 ? 61.936  62.263 40.413  1.00 130.75 ? 231 GLU A O   1 
ATOM   1803 C CB  . GLU A 1 228 ? 62.243  59.618 41.928  1.00 142.08 ? 231 GLU A CB  1 
ATOM   1804 C CG  . GLU A 1 228 ? 62.685  58.226 42.330  1.00 148.53 ? 231 GLU A CG  1 
ATOM   1805 C CD  . GLU A 1 228 ? 62.308  57.860 43.757  1.00 163.20 ? 231 GLU A CD  1 
ATOM   1806 O OE1 . GLU A 1 228 ? 61.636  58.678 44.409  1.00 161.35 ? 231 GLU A OE1 1 
ATOM   1807 O OE2 . GLU A 1 228 ? 62.703  56.769 44.216  1.00 171.44 ? 231 GLU A OE2 1 
ATOM   1808 N N   . PHE A 1 229 ? 60.662  60.833 39.190  1.00 133.60 ? 232 PHE A N   1 
ATOM   1809 C CA  . PHE A 1 229 ? 59.721  61.894 38.761  1.00 128.62 ? 232 PHE A CA  1 
ATOM   1810 C C   . PHE A 1 229 ? 58.347  61.629 39.378  1.00 136.44 ? 232 PHE A C   1 
ATOM   1811 O O   . PHE A 1 229 ? 57.812  60.519 39.184  1.00 138.95 ? 232 PHE A O   1 
ATOM   1812 C CB  . PHE A 1 229 ? 59.709  61.984 37.234  1.00 129.19 ? 232 PHE A CB  1 
ATOM   1813 C CG  . PHE A 1 229 ? 60.787  62.877 36.676  1.00 120.24 ? 232 PHE A CG  1 
ATOM   1814 C CD1 . PHE A 1 229 ? 60.664  64.255 36.733  1.00 116.79 ? 232 PHE A CD1 1 
ATOM   1815 C CD2 . PHE A 1 229 ? 61.947  62.341 36.146  1.00 126.34 ? 232 PHE A CD2 1 
ATOM   1816 C CE1 . PHE A 1 229 ? 61.659  65.077 36.230  1.00 117.88 ? 232 PHE A CE1 1 
ATOM   1817 C CE2 . PHE A 1 229 ? 62.945  63.164 35.650  1.00 126.78 ? 232 PHE A CE2 1 
ATOM   1818 C CZ  . PHE A 1 229 ? 62.799  64.530 35.693  1.00 121.81 ? 232 PHE A CZ  1 
ATOM   1819 N N   . PHE A 1 230 ? 57.809  62.610 40.107  1.00 130.94 ? 233 PHE A N   1 
ATOM   1820 C CA  . PHE A 1 230 ? 56.475  62.465 40.737  1.00 132.99 ? 233 PHE A CA  1 
ATOM   1821 C C   . PHE A 1 230 ? 55.476  63.373 40.017  1.00 128.61 ? 233 PHE A C   1 
ATOM   1822 O O   . PHE A 1 230 ? 55.911  64.314 39.328  1.00 123.68 ? 233 PHE A O   1 
ATOM   1823 C CB  . PHE A 1 230 ? 56.534  62.840 42.218  1.00 137.24 ? 233 PHE A CB  1 
ATOM   1824 C CG  . PHE A 1 230 ? 57.376  61.949 43.092  1.00 138.93 ? 233 PHE A CG  1 
ATOM   1825 C CD1 . PHE A 1 230 ? 58.749  61.879 42.928  1.00 143.14 ? 233 PHE A CD1 1 
ATOM   1826 C CD2 . PHE A 1 230 ? 56.790  61.172 44.078  1.00 148.14 ? 233 PHE A CD2 1 
ATOM   1827 C CE1 . PHE A 1 230 ? 59.515  61.051 43.730  1.00 149.33 ? 233 PHE A CE1 1 
ATOM   1828 C CE2 . PHE A 1 230 ? 57.558  60.344 44.879  1.00 162.18 ? 233 PHE A CE2 1 
ATOM   1829 C CZ  . PHE A 1 230 ? 58.920  60.286 44.705  1.00 160.78 ? 233 PHE A CZ  1 
ATOM   1830 N N   . TRP A 1 231 ? 54.181  63.093 40.173  1.00 127.78 ? 234 TRP A N   1 
ATOM   1831 C CA  . TRP A 1 231 ? 53.127  63.931 39.551  1.00 131.86 ? 234 TRP A CA  1 
ATOM   1832 C C   . TRP A 1 231 ? 51.909  63.993 40.471  1.00 137.61 ? 234 TRP A C   1 
ATOM   1833 O O   . TRP A 1 231 ? 51.759  63.075 41.298  1.00 152.06 ? 234 TRP A O   1 
ATOM   1834 C CB  . TRP A 1 231 ? 52.718  63.351 38.202  1.00 135.48 ? 234 TRP A CB  1 
ATOM   1835 C CG  . TRP A 1 231 ? 52.062  62.014 38.346  1.00 142.09 ? 234 TRP A CG  1 
ATOM   1836 C CD1 . TRP A 1 231 ? 52.662  60.825 38.638  1.00 143.45 ? 234 TRP A CD1 1 
ATOM   1837 C CD2 . TRP A 1 231 ? 50.649  61.756 38.296  1.00 145.47 ? 234 TRP A CD2 1 
ATOM   1838 N NE1 . TRP A 1 231 ? 51.723  59.833 38.725  1.00 153.91 ? 234 TRP A NE1 1 
ATOM   1839 C CE2 . TRP A 1 231 ? 50.483  60.374 38.526  1.00 153.11 ? 234 TRP A CE2 1 
ATOM   1840 C CE3 . TRP A 1 231 ? 49.527  62.551 38.065  1.00 143.54 ? 234 TRP A CE3 1 
ATOM   1841 C CZ2 . TRP A 1 231 ? 49.224  59.775 38.526  1.00 159.91 ? 234 TRP A CZ2 1 
ATOM   1842 C CZ3 . TRP A 1 231 ? 48.285  61.957 38.062  1.00 144.60 ? 234 TRP A CZ3 1 
ATOM   1843 C CH2 . TRP A 1 231 ? 48.141  60.589 38.290  1.00 155.58 ? 234 TRP A CH2 1 
ATOM   1844 N N   . THR A 1 232 ? 51.086  65.036 40.347  1.00 143.35 ? 235 THR A N   1 
ATOM   1845 C CA  . THR A 1 232 ? 49.812  65.127 41.111  1.00 141.57 ? 235 THR A CA  1 
ATOM   1846 C C   . THR A 1 232 ? 48.829  65.961 40.285  1.00 143.40 ? 235 THR A C   1 
ATOM   1847 O O   . THR A 1 232 ? 49.292  66.766 39.458  1.00 143.11 ? 235 THR A O   1 
ATOM   1848 C CB  . THR A 1 232 ? 49.958  65.776 42.493  1.00 141.52 ? 235 THR A CB  1 
ATOM   1849 O OG1 . THR A 1 232 ? 50.910  66.831 42.392  1.00 146.49 ? 235 THR A OG1 1 
ATOM   1850 C CG2 . THR A 1 232 ? 50.366  64.802 43.576  1.00 141.03 ? 235 THR A CG2 1 
ATOM   1851 N N   . ILE A 1 233 ? 47.528  65.764 40.479  1.00 146.05 ? 236 ILE A N   1 
ATOM   1852 C CA  . ILE A 1 233 ? 46.538  66.613 39.760  1.00 148.35 ? 236 ILE A CA  1 
ATOM   1853 C C   . ILE A 1 233 ? 46.100  67.723 40.714  1.00 154.80 ? 236 ILE A C   1 
ATOM   1854 O O   . ILE A 1 233 ? 45.359  67.421 41.666  1.00 157.70 ? 236 ILE A O   1 
ATOM   1855 C CB  . ILE A 1 233 ? 45.345  65.773 39.272  1.00 150.17 ? 236 ILE A CB  1 
ATOM   1856 C CG1 . ILE A 1 233 ? 45.793  64.635 38.353  1.00 145.95 ? 236 ILE A CG1 1 
ATOM   1857 C CG2 . ILE A 1 233 ? 44.305  66.656 38.601  1.00 160.06 ? 236 ILE A CG2 1 
ATOM   1858 C CD1 . ILE A 1 233 ? 46.345  65.105 37.030  1.00 138.41 ? 236 ILE A CD1 1 
ATOM   1859 N N   . LEU A 1 234 ? 46.561  68.952 40.472  1.00 155.34 ? 237 LEU A N   1 
ATOM   1860 C CA  . LEU A 1 234 ? 46.165  70.096 41.333  1.00 155.46 ? 237 LEU A CA  1 
ATOM   1861 C C   . LEU A 1 234 ? 44.833  70.645 40.822  1.00 162.81 ? 237 LEU A C   1 
ATOM   1862 O O   . LEU A 1 234 ? 44.787  71.099 39.666  1.00 158.53 ? 237 LEU A O   1 
ATOM   1863 C CB  . LEU A 1 234 ? 47.252  71.170 41.288  1.00 155.67 ? 237 LEU A CB  1 
ATOM   1864 C CG  . LEU A 1 234 ? 47.183  72.209 42.404  1.00 163.33 ? 237 LEU A CG  1 
ATOM   1865 C CD1 . LEU A 1 234 ? 47.695  71.618 43.706  1.00 160.89 ? 237 LEU A CD1 1 
ATOM   1866 C CD2 . LEU A 1 234 ? 47.973  73.456 42.037  1.00 168.48 ? 237 LEU A CD2 1 
ATOM   1867 N N   . LYS A 1 235 ? 43.795  70.589 41.656  1.00 175.21 ? 238 LYS A N   1 
ATOM   1868 C CA  . LYS A 1 235 ? 42.450  71.057 41.238  1.00 175.30 ? 238 LYS A CA  1 
ATOM   1869 C C   . LYS A 1 235 ? 42.480  72.581 41.108  1.00 175.12 ? 238 LYS A C   1 
ATOM   1870 O O   . LYS A 1 235 ? 43.381  73.204 41.699  1.00 174.06 ? 238 LYS A O   1 
ATOM   1871 C CB  . LYS A 1 235 ? 41.412  70.600 42.264  1.00 181.28 ? 238 LYS A CB  1 
ATOM   1872 C CG  . LYS A 1 235 ? 41.397  69.103 42.543  1.00 174.95 ? 238 LYS A CG  1 
ATOM   1873 C CD  . LYS A 1 235 ? 41.162  68.250 41.312  1.00 166.01 ? 238 LYS A CD  1 
ATOM   1874 C CE  . LYS A 1 235 ? 39.704  68.127 40.920  1.00 165.19 ? 238 LYS A CE  1 
ATOM   1875 N NZ  . LYS A 1 235 ? 39.183  69.363 40.291  1.00 158.21 ? 238 LYS A NZ  1 
ATOM   1876 N N   . PRO A 1 236 ? 41.497  73.232 40.438  1.00 167.09 ? 239 PRO A N   1 
ATOM   1877 C CA  . PRO A 1 236 ? 41.438  74.689 40.419  1.00 171.69 ? 239 PRO A CA  1 
ATOM   1878 C C   . PRO A 1 236 ? 41.237  75.125 41.873  1.00 180.84 ? 239 PRO A C   1 
ATOM   1879 O O   . PRO A 1 236 ? 40.403  74.527 42.531  1.00 183.26 ? 239 PRO A O   1 
ATOM   1880 C CB  . PRO A 1 236 ? 40.186  75.018 39.599  1.00 167.41 ? 239 PRO A CB  1 
ATOM   1881 C CG  . PRO A 1 236 ? 39.952  73.783 38.768  1.00 163.32 ? 239 PRO A CG  1 
ATOM   1882 C CD  . PRO A 1 236 ? 40.386  72.649 39.670  1.00 165.46 ? 239 PRO A CD  1 
ATOM   1883 N N   . ASN A 1 237 ? 42.016  76.105 42.341  1.00 181.44 ? 240 ASN A N   1 
ATOM   1884 C CA  . ASN A 1 237 ? 41.887  76.623 43.732  1.00 178.09 ? 240 ASN A CA  1 
ATOM   1885 C C   . ASN A 1 237 ? 42.538  75.650 44.725  1.00 181.46 ? 240 ASN A C   1 
ATOM   1886 O O   . ASN A 1 237 ? 42.385  75.876 45.941  1.00 183.07 ? 240 ASN A O   1 
ATOM   1887 C CB  . ASN A 1 237 ? 40.437  76.971 44.092  1.00 181.68 ? 240 ASN A CB  1 
ATOM   1888 C CG  . ASN A 1 237 ? 39.880  78.089 43.237  1.00 182.47 ? 240 ASN A CG  1 
ATOM   1889 O OD1 . ASN A 1 237 ? 39.815  77.972 42.016  1.00 184.92 ? 240 ASN A OD1 1 
ATOM   1890 N ND2 . ASN A 1 237 ? 39.483  79.182 43.869  1.00 186.70 ? 240 ASN A ND2 1 
ATOM   1891 N N   . ASP A 1 238 ? 43.240  74.619 44.239  1.00 176.76 ? 241 ASP A N   1 
ATOM   1892 C CA  . ASP A 1 238 ? 43.990  73.717 45.159  1.00 172.44 ? 241 ASP A CA  1 
ATOM   1893 C C   . ASP A 1 238 ? 45.441  74.201 45.213  1.00 166.81 ? 241 ASP A C   1 
ATOM   1894 O O   . ASP A 1 238 ? 45.890  74.795 44.214  1.00 169.34 ? 241 ASP A O   1 
ATOM   1895 C CB  . ASP A 1 238 ? 43.883  72.246 44.750  1.00 175.01 ? 241 ASP A CB  1 
ATOM   1896 C CG  . ASP A 1 238 ? 42.774  71.507 45.477  1.00 208.04 ? 241 ASP A CG  1 
ATOM   1897 O OD1 . ASP A 1 238 ? 42.031  72.165 46.232  1.00 272.67 ? 241 ASP A OD1 1 
ATOM   1898 O OD2 . ASP A 1 238 ? 42.681  70.276 45.305  1.00 184.94 ? 241 ASP A OD2 1 
ATOM   1899 N N   . ALA A 1 239 ? 46.147  73.965 46.324  1.00 158.85 ? 242 ALA A N   1 
ATOM   1900 C CA  . ALA A 1 239 ? 47.509  74.533 46.439  1.00 155.92 ? 242 ALA A CA  1 
ATOM   1901 C C   . ALA A 1 239 ? 48.537  73.404 46.569  1.00 158.92 ? 242 ALA A C   1 
ATOM   1902 O O   . ALA A 1 239 ? 48.127  72.263 46.847  1.00 174.05 ? 242 ALA A O   1 
ATOM   1903 C CB  . ALA A 1 239 ? 47.571  75.465 47.618  1.00 156.93 ? 242 ALA A CB  1 
ATOM   1904 N N   . ILE A 1 240 ? 49.820  73.717 46.378  1.00 150.09 ? 243 ILE A N   1 
ATOM   1905 C CA  . ILE A 1 240 ? 50.897  72.697 46.503  1.00 149.96 ? 243 ILE A CA  1 
ATOM   1906 C C   . ILE A 1 240 ? 52.054  73.465 47.137  1.00 146.44 ? 243 ILE A C   1 
ATOM   1907 O O   . ILE A 1 240 ? 52.444  74.503 46.577  1.00 150.53 ? 243 ILE A O   1 
ATOM   1908 C CB  . ILE A 1 240 ? 51.282  72.062 45.156  1.00 145.04 ? 243 ILE A CB  1 
ATOM   1909 C CG1 . ILE A 1 240 ? 52.293  70.932 45.343  1.00 144.12 ? 243 ILE A CG1 1 
ATOM   1910 C CG2 . ILE A 1 240 ? 51.804  73.113 44.191  1.00 147.41 ? 243 ILE A CG2 1 
ATOM   1911 C CD1 . ILE A 1 240 ? 52.469  70.079 44.118  1.00 155.98 ? 243 ILE A CD1 1 
ATOM   1912 N N   . ASN A 1 241 ? 52.519  73.008 48.297  1.00 155.03 ? 244 ASN A N   1 
ATOM   1913 C CA  . ASN A 1 241 ? 53.664  73.684 48.960  1.00 147.84 ? 244 ASN A CA  1 
ATOM   1914 C C   . ASN A 1 241 ? 54.893  72.779 48.821  1.00 145.77 ? 244 ASN A C   1 
ATOM   1915 O O   . ASN A 1 241 ? 54.807  71.589 49.179  1.00 153.39 ? 244 ASN A O   1 
ATOM   1916 C CB  . ASN A 1 241 ? 53.326  73.974 50.422  1.00 150.75 ? 244 ASN A CB  1 
ATOM   1917 C CG  . ASN A 1 241 ? 51.963  74.603 50.607  1.00 151.61 ? 244 ASN A CG  1 
ATOM   1918 O OD1 . ASN A 1 241 ? 51.272  74.890 49.635  1.00 156.33 ? 244 ASN A OD1 1 
ATOM   1919 N ND2 . ASN A 1 241 ? 51.568  74.819 51.850  1.00 142.68 ? 244 ASN A ND2 1 
ATOM   1920 N N   . PHE A 1 242 ? 55.991  73.325 48.305  1.00 146.17 ? 245 PHE A N   1 
ATOM   1921 C CA  . PHE A 1 242 ? 57.233  72.526 48.204  1.00 145.08 ? 245 PHE A CA  1 
ATOM   1922 C C   . PHE A 1 242 ? 58.223  73.032 49.247  1.00 152.57 ? 245 PHE A C   1 
ATOM   1923 O O   . PHE A 1 242 ? 58.476  74.249 49.282  1.00 155.92 ? 245 PHE A O   1 
ATOM   1924 C CB  . PHE A 1 242 ? 57.819  72.628 46.796  1.00 143.31 ? 245 PHE A CB  1 
ATOM   1925 C CG  . PHE A 1 242 ? 57.072  71.859 45.738  1.00 138.84 ? 245 PHE A CG  1 
ATOM   1926 C CD1 . PHE A 1 242 ? 56.846  70.499 45.877  1.00 140.46 ? 245 PHE A CD1 1 
ATOM   1927 C CD2 . PHE A 1 242 ? 56.606  72.492 44.600  1.00 135.96 ? 245 PHE A CD2 1 
ATOM   1928 C CE1 . PHE A 1 242 ? 56.161  69.793 44.901  1.00 146.96 ? 245 PHE A CE1 1 
ATOM   1929 C CE2 . PHE A 1 242 ? 55.924  71.784 43.625  1.00 136.18 ? 245 PHE A CE2 1 
ATOM   1930 C CZ  . PHE A 1 242 ? 55.703  70.436 43.777  1.00 138.34 ? 245 PHE A CZ  1 
ATOM   1931 N N   . GLU A 1 243 ? 58.724  72.141 50.102  1.00 157.31 ? 246 GLU A N   1 
ATOM   1932 C CA  . GLU A 1 243 ? 59.768  72.544 51.080  1.00 159.59 ? 246 GLU A CA  1 
ATOM   1933 C C   . GLU A 1 243 ? 60.907  71.529 50.978  1.00 159.53 ? 246 GLU A C   1 
ATOM   1934 O O   . GLU A 1 243 ? 60.697  70.371 51.377  1.00 160.41 ? 246 GLU A O   1 
ATOM   1935 C CB  . GLU A 1 243 ? 59.217  72.593 52.505  1.00 161.59 ? 246 GLU A CB  1 
ATOM   1936 C CG  . GLU A 1 243 ? 57.821  73.179 52.595  1.00 164.94 ? 246 GLU A CG  1 
ATOM   1937 C CD  . GLU A 1 243 ? 57.275  73.337 54.006  1.00 170.17 ? 246 GLU A CD  1 
ATOM   1938 O OE1 . GLU A 1 243 ? 58.008  73.021 54.964  1.00 170.45 ? 246 GLU A OE1 1 
ATOM   1939 O OE2 . GLU A 1 243 ? 56.114  73.771 54.141  1.00 171.49 ? 246 GLU A OE2 1 
ATOM   1940 N N   . SER A 1 244 ? 62.066  71.935 50.454  1.00 154.82 ? 247 SER A N   1 
ATOM   1941 C CA  . SER A 1 244 ? 63.144  70.938 50.239  1.00 147.72 ? 247 SER A CA  1 
ATOM   1942 C C   . SER A 1 244 ? 64.480  71.274 50.902  1.00 153.88 ? 247 SER A C   1 
ATOM   1943 O O   . SER A 1 244 ? 65.011  72.374 50.656  1.00 165.02 ? 247 SER A O   1 
ATOM   1944 C CB  . SER A 1 244 ? 63.285  70.607 48.778  1.00 144.35 ? 247 SER A CB  1 
ATOM   1945 O OG  . SER A 1 244 ? 62.139  69.917 48.295  1.00 141.00 ? 247 SER A OG  1 
ATOM   1946 N N   . ASN A 1 245 ? 64.998  70.350 51.714  1.00 158.90 ? 248 ASN A N   1 
ATOM   1947 C CA  . ASN A 1 245 ? 66.362  70.531 52.283  1.00 160.97 ? 248 ASN A CA  1 
ATOM   1948 C C   . ASN A 1 245 ? 67.359  70.628 51.114  1.00 163.11 ? 248 ASN A C   1 
ATOM   1949 O O   . ASN A 1 245 ? 68.085  71.627 51.012  1.00 166.24 ? 248 ASN A O   1 
ATOM   1950 C CB  . ASN A 1 245 ? 66.690  69.425 53.288  1.00 155.55 ? 248 ASN A CB  1 
ATOM   1951 C CG  . ASN A 1 245 ? 67.975  69.670 54.048  1.00 154.03 ? 248 ASN A CG  1 
ATOM   1952 O OD1 . ASN A 1 245 ? 68.822  70.444 53.613  1.00 162.44 ? 248 ASN A OD1 1 
ATOM   1953 N ND2 . ASN A 1 245 ? 68.146  68.984 55.166  1.00 156.42 ? 248 ASN A ND2 1 
ATOM   1954 N N   . GLY A 1 246 ? 67.296  69.638 50.219  1.00 164.81 ? 249 GLY A N   1 
ATOM   1955 C CA  . GLY A 1 246 ? 68.143  69.648 49.011  1.00 160.57 ? 249 GLY A CA  1 
ATOM   1956 C C   . GLY A 1 246 ? 67.703  68.529 48.084  1.00 148.33 ? 249 GLY A C   1 
ATOM   1957 O O   . GLY A 1 246 ? 66.680  67.900 48.388  1.00 152.50 ? 249 GLY A O   1 
ATOM   1958 N N   . ASN A 1 247 ? 68.435  68.306 46.987  1.00 150.84 ? 250 ASN A N   1 
ATOM   1959 C CA  . ASN A 1 247 ? 68.120  67.220 46.019  1.00 137.76 ? 250 ASN A CA  1 
ATOM   1960 C C   . ASN A 1 247 ? 66.757  67.480 45.376  1.00 131.85 ? 250 ASN A C   1 
ATOM   1961 O O   . ASN A 1 247 ? 66.090  66.491 45.016  1.00 129.00 ? 250 ASN A O   1 
ATOM   1962 C CB  . ASN A 1 247 ? 68.225  65.833 46.656  1.00 139.23 ? 250 ASN A CB  1 
ATOM   1963 C CG  . ASN A 1 247 ? 69.619  65.544 47.168  1.00 145.95 ? 250 ASN A CG  1 
ATOM   1964 O OD1 . ASN A 1 247 ? 70.080  66.167 48.120  1.00 148.93 ? 250 ASN A OD1 1 
ATOM   1965 N ND2 . ASN A 1 247 ? 70.292  64.591 46.549  1.00 145.31 ? 250 ASN A ND2 1 
ATOM   1966 N N   . PHE A 1 248 ? 66.379  68.746 45.207  1.00 121.81 ? 251 PHE A N   1 
ATOM   1967 C CA  . PHE A 1 248 ? 65.027  69.031 44.676  1.00 125.30 ? 251 PHE A CA  1 
ATOM   1968 C C   . PHE A 1 248 ? 65.090  69.400 43.198  1.00 125.16 ? 251 PHE A C   1 
ATOM   1969 O O   . PHE A 1 248 ? 65.898  70.270 42.847  1.00 131.01 ? 251 PHE A O   1 
ATOM   1970 C CB  . PHE A 1 248 ? 64.377  70.202 45.408  1.00 134.94 ? 251 PHE A CB  1 
ATOM   1971 C CG  . PHE A 1 248 ? 62.916  70.408 45.099  1.00 134.71 ? 251 PHE A CG  1 
ATOM   1972 C CD1 . PHE A 1 248 ? 62.123  69.368 44.639  1.00 131.63 ? 251 PHE A CD1 1 
ATOM   1973 C CD2 . PHE A 1 248 ? 62.332  71.653 45.259  1.00 135.49 ? 251 PHE A CD2 1 
ATOM   1974 C CE1 . PHE A 1 248 ? 60.781  69.569 44.355  1.00 127.63 ? 251 PHE A CE1 1 
ATOM   1975 C CE2 . PHE A 1 248 ? 60.991  71.851 44.977  1.00 134.61 ? 251 PHE A CE2 1 
ATOM   1976 C CZ  . PHE A 1 248 ? 60.217  70.810 44.523  1.00 132.04 ? 251 PHE A CZ  1 
ATOM   1977 N N   . ILE A 1 249 ? 64.227  68.799 42.383  1.00 124.23 ? 252 ILE A N   1 
ATOM   1978 C CA  . ILE A 1 249 ? 64.155  69.209 40.953  1.00 118.31 ? 252 ILE A CA  1 
ATOM   1979 C C   . ILE A 1 249 ? 62.778  69.854 40.770  1.00 115.03 ? 252 ILE A C   1 
ATOM   1980 O O   . ILE A 1 249 ? 61.847  69.146 40.341  1.00 114.74 ? 252 ILE A O   1 
ATOM   1981 C CB  . ILE A 1 249 ? 64.406  67.999 40.034  1.00 112.29 ? 252 ILE A CB  1 
ATOM   1982 C CG1 . ILE A 1 249 ? 65.250  66.935 40.738  1.00 117.65 ? 252 ILE A CG1 1 
ATOM   1983 C CG2 . ILE A 1 249 ? 65.047  68.443 38.732  1.00 118.40 ? 252 ILE A CG2 1 
ATOM   1984 C CD1 . ILE A 1 249 ? 66.690  67.340 40.965  1.00 133.25 ? 252 ILE A CD1 1 
ATOM   1985 N N   . ALA A 1 250 ? 62.649  71.134 41.139  1.00 121.62 ? 253 ALA A N   1 
ATOM   1986 C CA  . ALA A 1 250 ? 61.338  71.824 41.077  1.00 121.13 ? 253 ALA A CA  1 
ATOM   1987 C C   . ALA A 1 250 ? 60.905  72.021 39.622  1.00 119.56 ? 253 ALA A C   1 
ATOM   1988 O O   . ALA A 1 250 ? 61.784  72.148 38.753  1.00 127.03 ? 253 ALA A O   1 
ATOM   1989 C CB  . ALA A 1 250 ? 61.419  73.148 41.797  1.00 132.50 ? 253 ALA A CB  1 
ATOM   1990 N N   . PRO A 1 251 ? 59.588  72.067 39.327  1.00 108.38 ? 254 PRO A N   1 
ATOM   1991 C CA  . PRO A 1 251 ? 59.110  72.307 37.968  1.00 116.08 ? 254 PRO A CA  1 
ATOM   1992 C C   . PRO A 1 251 ? 59.073  73.787 37.576  1.00 127.26 ? 254 PRO A C   1 
ATOM   1993 O O   . PRO A 1 251 ? 59.316  74.628 38.425  1.00 132.56 ? 254 PRO A O   1 
ATOM   1994 C CB  . PRO A 1 251 ? 57.650  71.849 38.039  1.00 116.50 ? 254 PRO A CB  1 
ATOM   1995 C CG  . PRO A 1 251 ? 57.248  72.158 39.464  1.00 117.88 ? 254 PRO A CG  1 
ATOM   1996 C CD  . PRO A 1 251 ? 58.491  71.869 40.280  1.00 111.61 ? 254 PRO A CD  1 
ATOM   1997 N N   . GLU A 1 252 ? 58.774  74.065 36.307  1.00 130.82 ? 255 GLU A N   1 
ATOM   1998 C CA  . GLU A 1 252 ? 58.626  75.467 35.839  1.00 147.90 ? 255 GLU A CA  1 
ATOM   1999 C C   . GLU A 1 252 ? 57.363  75.511 34.974  1.00 154.99 ? 255 GLU A C   1 
ATOM   2000 O O   . GLU A 1 252 ? 56.809  76.608 34.771  1.00 169.55 ? 255 GLU A O   1 
ATOM   2001 C CB  . GLU A 1 252 ? 59.867  75.908 35.062  1.00 146.14 ? 255 GLU A CB  1 
ATOM   2002 C CG  . GLU A 1 252 ? 59.704  77.247 34.369  1.00 156.90 ? 255 GLU A CG  1 
ATOM   2003 C CD  . GLU A 1 252 ? 60.872  77.657 33.491  1.00 165.54 ? 255 GLU A CD  1 
ATOM   2004 O OE1 . GLU A 1 252 ? 61.262  76.858 32.617  1.00 162.35 ? 255 GLU A OE1 1 
ATOM   2005 O OE2 . GLU A 1 252 ? 61.369  78.783 33.666  1.00 173.50 ? 255 GLU A OE2 1 
ATOM   2006 N N   . TYR A 1 253 ? 56.921  74.342 34.499  1.00 142.21 ? 256 TYR A N   1 
ATOM   2007 C CA  . TYR A 1 253 ? 55.689  74.289 33.678  1.00 149.40 ? 256 TYR A CA  1 
ATOM   2008 C C   . TYR A 1 253 ? 54.776  73.193 34.212  1.00 151.20 ? 256 TYR A C   1 
ATOM   2009 O O   . TYR A 1 253 ? 55.267  72.330 34.953  1.00 142.28 ? 256 TYR A O   1 
ATOM   2010 C CB  . TYR A 1 253 ? 56.008  73.962 32.221  1.00 140.42 ? 256 TYR A CB  1 
ATOM   2011 C CG  . TYR A 1 253 ? 56.628  75.084 31.441  1.00 137.73 ? 256 TYR A CG  1 
ATOM   2012 C CD1 . TYR A 1 253 ? 57.900  75.539 31.731  1.00 139.57 ? 256 TYR A CD1 1 
ATOM   2013 C CD2 . TYR A 1 253 ? 55.934  75.699 30.415  1.00 145.67 ? 256 TYR A CD2 1 
ATOM   2014 C CE1 . TYR A 1 253 ? 58.475  76.577 31.017  1.00 148.68 ? 256 TYR A CE1 1 
ATOM   2015 C CE2 . TYR A 1 253 ? 56.492  76.740 29.691  1.00 154.23 ? 256 TYR A CE2 1 
ATOM   2016 C CZ  . TYR A 1 253 ? 57.767  77.181 29.995  1.00 151.67 ? 256 TYR A CZ  1 
ATOM   2017 O OH  . TYR A 1 253 ? 58.325  78.210 29.282  1.00 149.48 ? 256 TYR A OH  1 
ATOM   2018 N N   . ALA A 1 254 ? 53.499  73.233 33.840  1.00 143.95 ? 257 ALA A N   1 
ATOM   2019 C CA  . ALA A 1 254 ? 52.518  72.218 34.268  1.00 132.73 ? 257 ALA A CA  1 
ATOM   2020 C C   . ALA A 1 254 ? 51.469  72.164 33.163  1.00 132.51 ? 257 ALA A C   1 
ATOM   2021 O O   . ALA A 1 254 ? 51.630  72.901 32.184  1.00 139.32 ? 257 ALA A O   1 
ATOM   2022 C CB  . ALA A 1 254 ? 51.928  72.603 35.592  1.00 138.04 ? 257 ALA A CB  1 
ATOM   2023 N N   . TYR A 1 255 ? 50.440  71.331 33.295  1.00 127.29 ? 258 TYR A N   1 
ATOM   2024 C CA  . TYR A 1 255 ? 49.505  71.215 32.148  1.00 128.44 ? 258 TYR A CA  1 
ATOM   2025 C C   . TYR A 1 255 ? 48.062  71.485 32.571  1.00 130.15 ? 258 TYR A C   1 
ATOM   2026 O O   . TYR A 1 255 ? 47.547  70.762 33.440  1.00 123.49 ? 258 TYR A O   1 
ATOM   2027 C CB  . TYR A 1 255 ? 49.637  69.843 31.483  1.00 125.81 ? 258 TYR A CB  1 
ATOM   2028 C CG  . TYR A 1 255 ? 50.949  69.619 30.774  1.00 126.44 ? 258 TYR A CG  1 
ATOM   2029 C CD1 . TYR A 1 255 ? 52.079  69.217 31.465  1.00 126.42 ? 258 TYR A CD1 1 
ATOM   2030 C CD2 . TYR A 1 255 ? 51.070  69.827 29.411  1.00 128.48 ? 258 TYR A CD2 1 
ATOM   2031 C CE1 . TYR A 1 255 ? 53.289  69.013 30.821  1.00 125.03 ? 258 TYR A CE1 1 
ATOM   2032 C CE2 . TYR A 1 255 ? 52.271  69.630 28.750  1.00 126.24 ? 258 TYR A CE2 1 
ATOM   2033 C CZ  . TYR A 1 255 ? 53.387  69.221 29.458  1.00 122.94 ? 258 TYR A CZ  1 
ATOM   2034 O OH  . TYR A 1 255 ? 54.580  69.024 28.812  1.00 123.90 ? 258 TYR A OH  1 
ATOM   2035 N N   . LYS A 1 256 ? 47.427  72.481 31.951  1.00 140.54 ? 259 LYS A N   1 
ATOM   2036 C CA  . LYS A 1 256 ? 45.989  72.718 32.226  1.00 141.65 ? 259 LYS A CA  1 
ATOM   2037 C C   . LYS A 1 256 ? 45.198  71.726 31.378  1.00 143.03 ? 259 LYS A C   1 
ATOM   2038 O O   . LYS A 1 256 ? 45.481  71.620 30.175  1.00 137.00 ? 259 LYS A O   1 
ATOM   2039 C CB  . LYS A 1 256 ? 45.563  74.135 31.836  1.00 150.07 ? 259 LYS A CB  1 
ATOM   2040 C CG  . LYS A 1 256 ? 46.256  75.277 32.564  1.00 162.94 ? 259 LYS A CG  1 
ATOM   2041 C CD  . LYS A 1 256 ? 45.818  76.635 32.066  1.00 169.88 ? 259 LYS A CD  1 
ATOM   2042 C CE  . LYS A 1 256 ? 46.595  77.773 32.689  1.00 179.38 ? 259 LYS A CE  1 
ATOM   2043 N NZ  . LYS A 1 256 ? 46.106  79.098 32.236  1.00 173.67 ? 259 LYS A NZ  1 
ATOM   2044 N N   . ILE A 1 257 ? 44.264  71.000 32.000  1.00 146.13 ? 260 ILE A N   1 
ATOM   2045 C CA  . ILE A 1 257 ? 43.439  70.002 31.255  1.00 147.22 ? 260 ILE A CA  1 
ATOM   2046 C C   . ILE A 1 257 ? 42.415  70.763 30.408  1.00 149.71 ? 260 ILE A C   1 
ATOM   2047 O O   . ILE A 1 257 ? 41.336  71.091 30.941  1.00 149.40 ? 260 ILE A O   1 
ATOM   2048 C CB  . ILE A 1 257 ? 42.766  69.007 32.222  1.00 142.45 ? 260 ILE A CB  1 
ATOM   2049 C CG1 . ILE A 1 257 ? 43.776  68.392 33.194  1.00 140.14 ? 260 ILE A CG1 1 
ATOM   2050 C CG2 . ILE A 1 257 ? 42.004  67.939 31.452  1.00 141.27 ? 260 ILE A CG2 1 
ATOM   2051 C CD1 . ILE A 1 257 ? 43.181  67.366 34.128  1.00 145.24 ? 260 ILE A CD1 1 
ATOM   2052 N N   . VAL A 1 258 a 42.758  71.051 29.149  1.00 155.03 ? 260 VAL A N   1 
ATOM   2053 C CA  . VAL A 1 258 a 41.838  71.805 28.246  1.00 157.76 ? 260 VAL A CA  1 
ATOM   2054 C C   . VAL A 1 258 a 40.641  70.915 27.901  1.00 161.04 ? 260 VAL A C   1 
ATOM   2055 O O   . VAL A 1 258 a 39.496  71.394 28.026  1.00 163.42 ? 260 VAL A O   1 
ATOM   2056 C CB  . VAL A 1 258 a 42.566  72.275 26.973  1.00 158.31 ? 260 VAL A CB  1 
ATOM   2057 C CG1 . VAL A 1 258 a 41.629  73.006 26.024  1.00 157.40 ? 260 VAL A CG1 1 
ATOM   2058 C CG2 . VAL A 1 258 a 43.771  73.138 27.304  1.00 160.26 ? 260 VAL A CG2 1 
ATOM   2059 N N   . LYS A 1 259 ? 40.898  69.670 27.490  1.00 164.16 ? 261 LYS A N   1 
ATOM   2060 C CA  . LYS A 1 259 ? 39.795  68.766 27.070  1.00 148.02 ? 261 LYS A CA  1 
ATOM   2061 C C   . LYS A 1 259 ? 39.966  67.393 27.724  1.00 149.95 ? 261 LYS A C   1 
ATOM   2062 O O   . LYS A 1 259 ? 41.082  66.846 27.648  1.00 155.13 ? 261 LYS A O   1 
ATOM   2063 C CB  . LYS A 1 259 ? 39.778  68.621 25.545  1.00 145.71 ? 261 LYS A CB  1 
ATOM   2064 C CG  . LYS A 1 259 ? 39.629  69.922 24.768  1.00 160.93 ? 261 LYS A CG  1 
ATOM   2065 C CD  . LYS A 1 259 ? 39.667  69.736 23.267  1.00 174.70 ? 261 LYS A CD  1 
ATOM   2066 C CE  . LYS A 1 259 ? 39.613  71.047 22.513  1.00 184.06 ? 261 LYS A CE  1 
ATOM   2067 N NZ  . LYS A 1 259 ? 39.580  70.838 21.046  1.00 204.58 ? 261 LYS A NZ  1 
ATOM   2068 N N   . LYS A 1 260 ? 38.907  66.866 28.346  1.00 144.28 ? 262 LYS A N   1 
ATOM   2069 C CA  . LYS A 1 260 ? 38.963  65.493 28.918  1.00 150.10 ? 262 LYS A CA  1 
ATOM   2070 C C   . LYS A 1 260 ? 37.923  64.650 28.175  1.00 152.82 ? 262 LYS A C   1 
ATOM   2071 O O   . LYS A 1 260 ? 36.942  64.224 28.817  1.00 155.40 ? 262 LYS A O   1 
ATOM   2072 C CB  . LYS A 1 260 ? 38.739  65.522 30.433  1.00 144.14 ? 262 LYS A CB  1 
ATOM   2073 C CG  . LYS A 1 260 ? 39.346  64.348 31.190  1.00 140.57 ? 262 LYS A CG  1 
ATOM   2074 C CD  . LYS A 1 260 ? 39.428  64.564 32.685  1.00 129.91 ? 262 LYS A CD  1 
ATOM   2075 C CE  . LYS A 1 260 ? 40.192  63.465 33.394  1.00 129.08 ? 262 LYS A CE  1 
ATOM   2076 N NZ  . LYS A 1 260 ? 40.260  63.696 34.856  1.00 126.29 ? 262 LYS A NZ  1 
ATOM   2077 N N   . GLY A 1 261 ? 38.131  64.428 26.874  1.00 149.15 ? 263 GLY A N   1 
ATOM   2078 C CA  . GLY A 1 261 ? 37.174  63.684 26.040  1.00 156.95 ? 263 GLY A CA  1 
ATOM   2079 C C   . GLY A 1 261 ? 37.373  62.185 26.157  1.00 165.43 ? 263 GLY A C   1 
ATOM   2080 O O   . GLY A 1 261 ? 37.405  61.682 27.297  1.00 166.14 ? 263 GLY A O   1 
ATOM   2081 N N   . ASP A 1 262 ? 37.479  61.494 25.019  1.00 162.93 ? 264 ASP A N   1 
ATOM   2082 C CA  . ASP A 1 262 ? 37.711  60.031 25.022  1.00 160.79 ? 264 ASP A CA  1 
ATOM   2083 C C   . ASP A 1 262 ? 38.928  59.718 24.145  1.00 157.24 ? 264 ASP A C   1 
ATOM   2084 O O   . ASP A 1 262 ? 38.865  60.004 22.936  1.00 166.51 ? 264 ASP A O   1 
ATOM   2085 C CB  . ASP A 1 262 ? 36.462  59.284 24.558  1.00 166.29 ? 264 ASP A CB  1 
ATOM   2086 C CG  . ASP A 1 262 ? 35.392  59.169 25.630  1.00 172.83 ? 264 ASP A CG  1 
ATOM   2087 O OD1 . ASP A 1 262 ? 35.678  59.537 26.786  1.00 174.30 ? 264 ASP A OD1 1 
ATOM   2088 O OD2 . ASP A 1 262 ? 34.271  58.740 25.293  1.00 177.76 ? 264 ASP A OD2 1 
ATOM   2089 N N   . SER A 1 263 ? 39.985  59.161 24.743  1.00 148.31 ? 265 SER A N   1 
ATOM   2090 C CA  . SER A 1 263 ? 41.208  58.804 23.979  1.00 146.25 ? 265 SER A CA  1 
ATOM   2091 C C   . SER A 1 263 ? 41.782  57.492 24.508  1.00 145.43 ? 265 SER A C   1 
ATOM   2092 O O   . SER A 1 263 ? 41.290  57.007 25.535  1.00 140.69 ? 265 SER A O   1 
ATOM   2093 C CB  . SER A 1 263 ? 42.249  59.886 24.067  1.00 146.34 ? 265 SER A CB  1 
ATOM   2094 O OG  . SER A 1 263 ? 42.863  59.891 25.348  1.00 139.08 ? 265 SER A OG  1 
ATOM   2095 N N   . THR A 1 264 ? 42.785  56.944 23.811  1.00 143.19 ? 266 THR A N   1 
ATOM   2096 C CA  . THR A 1 264 ? 43.478  55.721 24.293  1.00 145.92 ? 266 THR A CA  1 
ATOM   2097 C C   . THR A 1 264 ? 44.980  55.889 24.056  1.00 144.66 ? 266 THR A C   1 
ATOM   2098 O O   . THR A 1 264 ? 45.351  56.852 23.367  1.00 145.28 ? 266 THR A O   1 
ATOM   2099 C CB  . THR A 1 264 ? 42.999  54.450 23.586  1.00 141.49 ? 266 THR A CB  1 
ATOM   2100 O OG1 . THR A 1 264 ? 43.575  54.436 22.280  1.00 144.85 ? 266 THR A OG1 1 
ATOM   2101 C CG2 . THR A 1 264 ? 41.492  54.337 23.508  1.00 143.72 ? 266 THR A CG2 1 
ATOM   2102 N N   . ILE A 1 265 ? 45.796  54.979 24.590  1.00 149.88 ? 267 ILE A N   1 
ATOM   2103 C CA  . ILE A 1 265 ? 47.280  55.076 24.454  1.00 152.11 ? 267 ILE A CA  1 
ATOM   2104 C C   . ILE A 1 265 ? 47.770  53.957 23.533  1.00 149.55 ? 267 ILE A C   1 
ATOM   2105 O O   . ILE A 1 265 ? 48.921  53.519 23.702  1.00 149.32 ? 267 ILE A O   1 
ATOM   2106 C CB  . ILE A 1 265 ? 47.952  55.002 25.837  1.00 151.23 ? 267 ILE A CB  1 
ATOM   2107 C CG1 . ILE A 1 265 ? 47.621  53.687 26.545  1.00 154.60 ? 267 ILE A CG1 1 
ATOM   2108 C CG2 . ILE A 1 265 ? 47.577  56.204 26.689  1.00 158.15 ? 267 ILE A CG2 1 
ATOM   2109 C CD1 . ILE A 1 265 ? 48.261  53.541 27.904  1.00 147.02 ? 267 ILE A CD1 1 
ATOM   2110 N N   . MET A 1 266 ? 46.934  53.527 22.590  1.00 133.30 ? 268 MET A N   1 
ATOM   2111 C CA  . MET A 1 266 ? 47.296  52.379 21.719  1.00 139.67 ? 268 MET A CA  1 
ATOM   2112 C C   . MET A 1 266 ? 48.770  52.451 21.329  1.00 140.16 ? 268 MET A C   1 
ATOM   2113 O O   . MET A 1 266 ? 49.160  53.469 20.730  1.00 141.72 ? 268 MET A O   1 
ATOM   2114 C CB  . MET A 1 266 ? 46.468  52.395 20.431  1.00 128.15 ? 268 MET A CB  1 
ATOM   2115 C CG  . MET A 1 266 ? 46.014  53.769 20.002  1.00 138.13 ? 268 MET A CG  1 
ATOM   2116 S SD  . MET A 1 266 ? 45.330  53.700 18.333  1.00 194.56 ? 268 MET A SD  1 
ATOM   2117 C CE  . MET A 1 266 ? 43.828  52.774 18.641  1.00 150.70 ? 268 MET A CE  1 
ATOM   2118 N N   . LYS A 1 267 ? 49.559  51.413 21.636  1.00 129.42 ? 269 LYS A N   1 
ATOM   2119 C CA  . LYS A 1 267 ? 50.949  51.498 21.114  1.00 125.27 ? 269 LYS A CA  1 
ATOM   2120 C C   . LYS A 1 267 ? 50.987  50.944 19.687  1.00 135.01 ? 269 LYS A C   1 
ATOM   2121 O O   . LYS A 1 267 ? 50.515  49.809 19.484  1.00 121.94 ? 269 LYS A O   1 
ATOM   2122 C CB  . LYS A 1 267 ? 51.921  50.735 22.020  1.00 113.31 ? 269 LYS A CB  1 
ATOM   2123 C CG  . LYS A 1 267 ? 52.469  51.525 23.200  1.00 119.81 ? 269 LYS A CG  1 
ATOM   2124 C CD  . LYS A 1 267 ? 53.606  50.819 23.906  1.00 131.73 ? 269 LYS A CD  1 
ATOM   2125 C CE  . LYS A 1 267 ? 54.232  51.649 25.006  1.00 153.91 ? 269 LYS A CE  1 
ATOM   2126 N NZ  . LYS A 1 267 ? 55.377  50.953 25.637  1.00 179.56 ? 269 LYS A NZ  1 
ATOM   2127 N N   . SER A 1 268 ? 51.531  51.719 18.743  1.00 135.59 ? 270 SER A N   1 
ATOM   2128 C CA  . SER A 1 268 ? 51.596  51.278 17.325  1.00 141.78 ? 270 SER A CA  1 
ATOM   2129 C C   . SER A 1 268 ? 52.955  51.653 16.724  1.00 133.92 ? 270 SER A C   1 
ATOM   2130 O O   . SER A 1 268 ? 53.258  52.860 16.658  1.00 148.06 ? 270 SER A O   1 
ATOM   2131 C CB  . SER A 1 268 ? 50.463  51.866 16.527  1.00 154.90 ? 270 SER A CB  1 
ATOM   2132 O OG  . SER A 1 268 ? 50.467  51.363 15.200  1.00 153.29 ? 270 SER A OG  1 
ATOM   2133 N N   . GLU A 1 269 ? 53.736  50.653 16.305  1.00 138.99 ? 271 GLU A N   1 
ATOM   2134 C CA  . GLU A 1 269 ? 55.059  50.918 15.678  1.00 140.03 ? 271 GLU A CA  1 
ATOM   2135 C C   . GLU A 1 269 ? 54.821  51.462 14.266  1.00 142.01 ? 271 GLU A C   1 
ATOM   2136 O O   . GLU A 1 269 ? 55.804  51.871 13.618  1.00 138.84 ? 271 GLU A O   1 
ATOM   2137 C CB  . GLU A 1 269 ? 55.896  49.639 15.648  1.00 130.15 ? 271 GLU A CB  1 
ATOM   2138 C CG  . GLU A 1 269 ? 55.808  48.833 16.931  1.00 136.19 ? 271 GLU A CG  1 
ATOM   2139 C CD  . GLU A 1 269 ? 56.260  49.566 18.183  1.00 141.48 ? 271 GLU A CD  1 
ATOM   2140 O OE1 . GLU A 1 269 ? 57.442  49.960 18.241  1.00 133.35 ? 271 GLU A OE1 1 
ATOM   2141 O OE2 . GLU A 1 269 ? 55.429  49.741 19.095  1.00 154.15 ? 271 GLU A OE2 1 
ATOM   2142 N N   . LEU A 1 270 ? 53.562  51.467 13.818  1.00 132.11 ? 272 LEU A N   1 
ATOM   2143 C CA  . LEU A 1 270 ? 53.207  51.985 12.474  1.00 134.90 ? 272 LEU A CA  1 
ATOM   2144 C C   . LEU A 1 270 ? 53.410  53.500 12.455  1.00 143.95 ? 272 LEU A C   1 
ATOM   2145 O O   . LEU A 1 270 ? 53.367  54.108 13.537  1.00 154.28 ? 272 LEU A O   1 
ATOM   2146 C CB  . LEU A 1 270 ? 51.750  51.628 12.178  1.00 132.54 ? 272 LEU A CB  1 
ATOM   2147 C CG  . LEU A 1 270 ? 51.531  50.286 11.483  1.00 132.34 ? 272 LEU A CG  1 
ATOM   2148 C CD1 . LEU A 1 270 ? 52.523  50.102 10.346  1.00 143.01 ? 272 LEU A CD1 1 
ATOM   2149 C CD2 . LEU A 1 270 ? 51.634  49.134 12.471  1.00 131.20 ? 272 LEU A CD2 1 
ATOM   2150 N N   . GLU A 1 271 ? 53.631  54.076 11.272  1.00 146.33 ? 273 GLU A N   1 
ATOM   2151 C CA  . GLU A 1 271 ? 53.767  55.552 11.155  1.00 147.98 ? 273 GLU A CA  1 
ATOM   2152 C C   . GLU A 1 271 ? 52.498  56.097 10.495  1.00 154.19 ? 273 GLU A C   1 
ATOM   2153 O O   . GLU A 1 271 ? 51.766  55.293 9.893   1.00 154.45 ? 273 GLU A O   1 
ATOM   2154 C CB  . GLU A 1 271 ? 55.027  55.913 10.369  1.00 153.07 ? 273 GLU A CB  1 
ATOM   2155 C CG  . GLU A 1 271 ? 56.313  55.537 11.083  1.00 147.10 ? 273 GLU A CG  1 
ATOM   2156 C CD  . GLU A 1 271 ? 56.712  56.455 12.227  1.00 140.70 ? 273 GLU A CD  1 
ATOM   2157 O OE1 . GLU A 1 271 ? 55.980  57.428 12.487  1.00 143.64 ? 273 GLU A OE1 1 
ATOM   2158 O OE2 . GLU A 1 271 ? 57.759  56.197 12.850  1.00 131.35 ? 273 GLU A OE2 1 
ATOM   2159 N N   . TYR A 1 272 ? 52.241  57.403 10.601  1.00 136.33 ? 274 TYR A N   1 
ATOM   2160 C CA  . TYR A 1 272 ? 51.007  58.005 10.027  1.00 145.14 ? 274 TYR A CA  1 
ATOM   2161 C C   . TYR A 1 272 ? 50.974  57.774 8.511   1.00 147.76 ? 274 TYR A C   1 
ATOM   2162 O O   . TYR A 1 272 ? 52.046  57.573 7.912   1.00 147.31 ? 274 TYR A O   1 
ATOM   2163 C CB  . TYR A 1 272 ? 50.945  59.492 10.381  1.00 148.89 ? 274 TYR A CB  1 
ATOM   2164 C CG  . TYR A 1 272 ? 49.755  60.245 9.845   1.00 159.94 ? 274 TYR A CG  1 
ATOM   2165 C CD1 . TYR A 1 272 ? 48.464  59.888 10.192  1.00 169.36 ? 274 TYR A CD1 1 
ATOM   2166 C CD2 . TYR A 1 272 ? 49.922  61.328 8.999   1.00 159.90 ? 274 TYR A CD2 1 
ATOM   2167 C CE1 . TYR A 1 272 ? 47.369  60.581 9.706   1.00 180.24 ? 274 TYR A CE1 1 
ATOM   2168 C CE2 . TYR A 1 272 ? 48.838  62.033 8.505   1.00 168.13 ? 274 TYR A CE2 1 
ATOM   2169 C CZ  . TYR A 1 272 ? 47.556  61.660 8.862   1.00 175.63 ? 274 TYR A CZ  1 
ATOM   2170 O OH  . TYR A 1 272 ? 46.479  62.356 8.372   1.00 185.97 ? 274 TYR A OH  1 
ATOM   2171 N N   . GLY A 1 273 ? 49.780  57.803 7.911   1.00 141.12 ? 275 GLY A N   1 
ATOM   2172 C CA  . GLY A 1 273 ? 49.657  57.598 6.456   1.00 142.53 ? 275 GLY A CA  1 
ATOM   2173 C C   . GLY A 1 273 ? 48.457  58.313 5.858   1.00 160.00 ? 275 GLY A C   1 
ATOM   2174 O O   . GLY A 1 273 ? 48.042  57.915 4.753   1.00 175.29 ? 275 GLY A O   1 
ATOM   2175 N N   . ASN A 1 274 ? 47.904  59.308 6.559   1.00 168.81 ? 276 ASN A N   1 
ATOM   2176 C CA  . ASN A 1 274 ? 46.751  60.083 6.049   1.00 180.05 ? 276 ASN A CA  1 
ATOM   2177 C C   . ASN A 1 274 ? 45.288  60.141 5.563   1.00 186.42 ? 276 ASN A C   1 
ATOM   2178 O O   . ASN A 1 274 ? 44.944  61.118 4.873   1.00 196.16 ? 276 ASN A O   1 
ATOM   2179 C CB  . ASN A 1 274 ? 46.986  60.664 4.653   1.00 183.53 ? 276 ASN A CB  1 
ATOM   2180 C CG  . ASN A 1 274 ? 47.997  61.791 4.643   1.00 182.07 ? 276 ASN A CG  1 
ATOM   2181 O OD1 . ASN A 1 274 ? 47.664  62.925 4.305   1.00 181.87 ? 276 ASN A OD1 1 
ATOM   2182 N ND2 . ASN A 1 274 ? 49.230  61.495 5.020   1.00 185.98 ? 276 ASN A ND2 1 
ATOM   2183 N N   . CYS A 1 275 ? 44.493  59.108 5.870   1.00 180.77 ? 277 CYS A N   1 
ATOM   2184 C CA  . CYS A 1 275 ? 43.074  59.009 5.431   1.00 180.49 ? 277 CYS A CA  1 
ATOM   2185 C C   . CYS A 1 275 ? 42.354  59.223 6.783   1.00 176.91 ? 277 CYS A C   1 
ATOM   2186 O O   . CYS A 1 275 ? 42.989  59.790 7.693   1.00 178.88 ? 277 CYS A O   1 
ATOM   2187 C CB  . CYS A 1 275 ? 43.215  57.545 5.080   1.00 178.33 ? 277 CYS A CB  1 
ATOM   2188 S SG  . CYS A 1 275 ? 43.557  57.263 3.324   1.00 179.85 ? 277 CYS A SG  1 
ATOM   2189 N N   . ASN A 1 276 ? 41.092  58.785 6.913   1.00 181.22 ? 278 ASN A N   1 
ATOM   2190 C CA  . ASN A 1 276 ? 40.358  59.086 8.175   1.00 173.43 ? 278 ASN A CA  1 
ATOM   2191 C C   . ASN A 1 276 ? 39.077  58.263 8.359   1.00 166.34 ? 278 ASN A C   1 
ATOM   2192 O O   . ASN A 1 276 ? 38.093  58.558 7.659   1.00 164.57 ? 278 ASN A O   1 
ATOM   2193 C CB  . ASN A 1 276 ? 40.038  60.582 8.273   1.00 171.29 ? 278 ASN A CB  1 
ATOM   2194 C CG  . ASN A 1 276 ? 38.847  60.908 9.151   1.00 166.94 ? 278 ASN A CG  1 
ATOM   2195 O OD1 . ASN A 1 276 ? 37.877  61.504 8.688   1.00 163.39 ? 278 ASN A OD1 1 
ATOM   2196 N ND2 . ASN A 1 276 ? 38.909  60.531 10.417  1.00 164.16 ? 278 ASN A ND2 1 
ATOM   2197 N N   . THR A 1 277 ? 39.095  57.252 9.234   1.00 168.47 ? 279 THR A N   1 
ATOM   2198 C CA  . THR A 1 277 ? 37.850  56.529 9.630   1.00 155.50 ? 279 THR A CA  1 
ATOM   2199 C C   . THR A 1 277 ? 37.185  56.630 11.003  1.00 152.06 ? 279 THR A C   1 
ATOM   2200 O O   . THR A 1 277 ? 37.730  57.331 11.857  1.00 160.36 ? 279 THR A O   1 
ATOM   2201 C CB  . THR A 1 277 ? 38.308  55.068 9.648   1.00 150.13 ? 279 THR A CB  1 
ATOM   2202 O OG1 . THR A 1 277 ? 38.874  54.816 10.939  1.00 145.17 ? 279 THR A OG1 1 
ATOM   2203 C CG2 . THR A 1 277 ? 39.274  54.696 8.545   1.00 155.42 ? 279 THR A CG2 1 
ATOM   2204 N N   . THR A 1 278 ? 36.092  55.896 11.219  1.00 143.89 ? 280 THR A N   1 
ATOM   2205 C CA  . THR A 1 278 ? 35.430  55.881 12.546  1.00 147.04 ? 280 THR A CA  1 
ATOM   2206 C C   . THR A 1 278 ? 35.992  54.746 13.396  1.00 147.90 ? 280 THR A C   1 
ATOM   2207 O O   . THR A 1 278 ? 35.348  54.424 14.399  1.00 147.72 ? 280 THR A O   1 
ATOM   2208 C CB  . THR A 1 278 ? 33.930  55.629 12.419  1.00 141.23 ? 280 THR A CB  1 
ATOM   2209 O OG1 . THR A 1 278 ? 33.748  54.239 12.140  1.00 141.28 ? 280 THR A OG1 1 
ATOM   2210 C CG2 . THR A 1 278 ? 33.280  56.472 11.344  1.00 146.38 ? 280 THR A CG2 1 
ATOM   2211 N N   . CYS A 1 279 ? 37.106  54.138 12.982  1.00 147.30 ? 281 CYS A N   1 
ATOM   2212 C CA  . CYS A 1 279 ? 37.674  52.976 13.717  1.00 142.96 ? 281 CYS A CA  1 
ATOM   2213 C C   . CYS A 1 279 ? 39.196  53.008 13.662  1.00 139.70 ? 281 CYS A C   1 
ATOM   2214 O O   . CYS A 1 279 ? 39.728  53.167 12.555  1.00 142.53 ? 281 CYS A O   1 
ATOM   2215 C CB  . CYS A 1 279 ? 37.205  51.663 13.117  1.00 140.78 ? 281 CYS A CB  1 
ATOM   2216 S SG  . CYS A 1 279 ? 35.403  51.482 13.070  1.00 163.12 ? 281 CYS A SG  1 
ATOM   2217 N N   . GLN A 1 280 ? 39.873  52.812 14.791  1.00 133.71 ? 282 GLN A N   1 
ATOM   2218 C CA  . GLN A 1 280 ? 41.347  52.679 14.736  1.00 128.31 ? 282 GLN A CA  1 
ATOM   2219 C C   . GLN A 1 280 ? 41.933  51.595 15.637  1.00 120.62 ? 282 GLN A C   1 
ATOM   2220 O O   . GLN A 1 280 ? 41.407  51.415 16.754  1.00 122.26 ? 282 GLN A O   1 
ATOM   2221 C CB  . GLN A 1 280 ? 41.924  54.028 15.152  1.00 133.73 ? 282 GLN A CB  1 
ATOM   2222 C CG  . GLN A 1 280 ? 43.440  54.086 15.043  1.00 131.73 ? 282 GLN A CG  1 
ATOM   2223 C CD  . GLN A 1 280 ? 43.929  53.963 13.622  1.00 138.79 ? 282 GLN A CD  1 
ATOM   2224 O OE1 . GLN A 1 280 ? 44.355  52.898 13.184  1.00 137.02 ? 282 GLN A OE1 1 
ATOM   2225 N NE2 . GLN A 1 280 ? 43.871  55.060 12.886  1.00 156.18 ? 282 GLN A NE2 1 
ATOM   2226 N N   . THR A 1 281 ? 42.934  50.861 15.147  1.00 124.85 ? 283 THR A N   1 
ATOM   2227 C CA  . THR A 1 281 ? 43.573  49.773 15.925  1.00 113.10 ? 283 THR A CA  1 
ATOM   2228 C C   . THR A 1 281 ? 45.088  49.923 15.786  1.00 111.77 ? 283 THR A C   1 
ATOM   2229 O O   . THR A 1 281 ? 45.526  50.528 14.802  1.00 121.93 ? 283 THR A O   1 
ATOM   2230 C CB  . THR A 1 281 ? 43.150  48.371 15.495  1.00 105.72 ? 283 THR A CB  1 
ATOM   2231 O OG1 . THR A 1 281 ? 43.826  48.084 14.271  1.00 108.46 ? 283 THR A OG1 1 
ATOM   2232 C CG2 . THR A 1 281 ? 41.655  48.235 15.317  1.00 107.85 ? 283 THR A CG2 1 
ATOM   2233 N N   . PRO A 1 282 ? 45.919  49.402 16.705  1.00 114.56 ? 284 PRO A N   1 
ATOM   2234 C CA  . PRO A 1 282 ? 47.358  49.521 16.558  1.00 118.46 ? 284 PRO A CA  1 
ATOM   2235 C C   . PRO A 1 282 ? 47.795  48.815 15.273  1.00 117.84 ? 284 PRO A C   1 
ATOM   2236 O O   . PRO A 1 282 ? 48.886  49.062 14.819  1.00 121.13 ? 284 PRO A O   1 
ATOM   2237 C CB  . PRO A 1 282 ? 47.914  48.759 17.759  1.00 118.53 ? 284 PRO A CB  1 
ATOM   2238 C CG  . PRO A 1 282 ? 46.792  48.793 18.760  1.00 119.50 ? 284 PRO A CG  1 
ATOM   2239 C CD  . PRO A 1 282 ? 45.540  48.678 17.909  1.00 118.62 ? 284 PRO A CD  1 
ATOM   2240 N N   . LYS A 1 283 ? 46.946  47.940 14.741  1.00 115.78 ? 285 LYS A N   1 
ATOM   2241 C CA  . LYS A 1 283 ? 47.266  47.255 13.465  1.00 117.55 ? 285 LYS A CA  1 
ATOM   2242 C C   . LYS A 1 283 ? 46.756  48.106 12.304  1.00 120.39 ? 285 LYS A C   1 
ATOM   2243 O O   . LYS A 1 283 ? 47.402  48.102 11.256  1.00 127.32 ? 285 LYS A O   1 
ATOM   2244 C CB  . LYS A 1 283 ? 46.626  45.867 13.428  1.00 118.34 ? 285 LYS A CB  1 
ATOM   2245 C CG  . LYS A 1 283 ? 47.214  44.842 14.389  1.00 116.51 ? 285 LYS A CG  1 
ATOM   2246 C CD  . LYS A 1 283 ? 46.553  43.487 14.278  1.00 115.76 ? 285 LYS A CD  1 
ATOM   2247 C CE  . LYS A 1 283 ? 47.198  42.431 15.150  1.00 121.02 ? 285 LYS A CE  1 
ATOM   2248 N NZ  . LYS A 1 283 ? 46.552  41.107 14.989  1.00 136.30 ? 285 LYS A NZ  1 
ATOM   2249 N N   . GLY A 1 284 ? 45.641  48.814 12.492  1.00 117.57 ? 286 GLY A N   1 
ATOM   2250 C CA  . GLY A 1 284 ? 45.175  49.709 11.417  1.00 128.78 ? 286 GLY A CA  1 
ATOM   2251 C C   . GLY A 1 284 ? 43.802  50.315 11.641  1.00 126.38 ? 286 GLY A C   1 
ATOM   2252 O O   . GLY A 1 284 ? 43.455  50.552 12.800  1.00 123.89 ? 286 GLY A O   1 
ATOM   2253 N N   . ALA A 1 285 ? 43.048  50.551 10.569  1.00 123.37 ? 287 ALA A N   1 
ATOM   2254 C CA  . ALA A 1 285 ? 41.752  51.207 10.640  1.00 129.67 ? 287 ALA A CA  1 
ATOM   2255 C C   . ALA A 1 285 ? 40.758  50.434 9.784   1.00 134.34 ? 287 ALA A C   1 
ATOM   2256 O O   . ALA A 1 285 ? 41.118  49.885 8.739   1.00 137.73 ? 287 ALA A O   1 
ATOM   2257 C CB  . ALA A 1 285 ? 41.843  52.664 10.171  1.00 146.49 ? 287 ALA A CB  1 
ATOM   2258 N N   . ILE A 1 286 ? 39.560  50.266 10.340  1.00 136.48 ? 288 ILE A N   1 
ATOM   2259 C CA  . ILE A 1 286 ? 38.540  49.405 9.685   1.00 142.22 ? 288 ILE A CA  1 
ATOM   2260 C C   . ILE A 1 286 ? 37.607  50.287 8.866   1.00 147.16 ? 288 ILE A C   1 
ATOM   2261 O O   . ILE A 1 286 ? 37.504  51.486 9.177   1.00 140.32 ? 288 ILE A O   1 
ATOM   2262 C CB  . ILE A 1 286 ? 37.784  48.631 10.781  1.00 143.01 ? 288 ILE A CB  1 
ATOM   2263 C CG1 . ILE A 1 286 ? 38.755  47.936 11.737  1.00 133.43 ? 288 ILE A CG1 1 
ATOM   2264 C CG2 . ILE A 1 286 ? 36.780  47.651 10.201  1.00 147.49 ? 288 ILE A CG2 1 
ATOM   2265 C CD1 . ILE A 1 286 ? 38.994  48.694 13.018  1.00 124.38 ? 288 ILE A CD1 1 
ATOM   2266 N N   . ASN A 1 287 ? 36.952  49.700 7.870   1.00 162.08 ? 289 ASN A N   1 
ATOM   2267 C CA  . ASN A 1 287 ? 36.087  50.510 6.983   1.00 161.41 ? 289 ASN A CA  1 
ATOM   2268 C C   . ASN A 1 287 ? 34.659  49.972 7.033   1.00 161.77 ? 289 ASN A C   1 
ATOM   2269 O O   . ASN A 1 287 ? 33.760  50.748 7.395   1.00 159.35 ? 289 ASN A O   1 
ATOM   2270 C CB  . ASN A 1 287 ? 36.647  50.528 5.568   1.00 163.77 ? 289 ASN A CB  1 
ATOM   2271 C CG  . ASN A 1 287 ? 35.974  51.560 4.706   1.00 166.85 ? 289 ASN A CG  1 
ATOM   2272 O OD1 . ASN A 1 287 ? 35.539  52.601 5.192   1.00 165.59 ? 289 ASN A OD1 1 
ATOM   2273 N ND2 . ASN A 1 287 ? 35.901  51.272 3.418   1.00 164.09 ? 289 ASN A ND2 1 
ATOM   2274 N N   . THR A 1 288 ? 34.455  48.705 6.670   1.00 160.21 ? 290 THR A N   1 
ATOM   2275 C CA  . THR A 1 288 ? 33.053  48.210 6.626   1.00 158.22 ? 290 THR A CA  1 
ATOM   2276 C C   . THR A 1 288 ? 32.491  48.178 8.048   1.00 143.50 ? 290 THR A C   1 
ATOM   2277 O O   . THR A 1 288 ? 33.281  48.150 9.007   1.00 145.56 ? 290 THR A O   1 
ATOM   2278 C CB  . THR A 1 288 ? 32.893  46.870 5.892   1.00 164.40 ? 290 THR A CB  1 
ATOM   2279 O OG1 . THR A 1 288 ? 32.691  45.840 6.861   1.00 148.08 ? 290 THR A OG1 1 
ATOM   2280 C CG2 . THR A 1 288 ? 34.060  46.538 4.987   1.00 158.92 ? 290 THR A CG2 1 
ATOM   2281 N N   . SER A 1 289 ? 31.169  48.184 8.159   1.00 136.52 ? 291 SER A N   1 
ATOM   2282 C CA  . SER A 1 289 ? 30.529  48.247 9.495   1.00 126.91 ? 291 SER A CA  1 
ATOM   2283 C C   . SER A 1 289 ? 29.761  46.969 9.823   1.00 118.77 ? 291 SER A C   1 
ATOM   2284 O O   . SER A 1 289 ? 28.525  46.977 9.689   1.00 112.08 ? 291 SER A O   1 
ATOM   2285 C CB  . SER A 1 289 ? 29.627  49.440 9.561   1.00 132.29 ? 291 SER A CB  1 
ATOM   2286 O OG  . SER A 1 289 ? 28.673  49.399 8.511   1.00 143.83 ? 291 SER A OG  1 
ATOM   2287 N N   . LEU A 1 290 ? 30.466  45.918 10.239  1.00 123.73 ? 292 LEU A N   1 
ATOM   2288 C CA  . LEU A 1 290 ? 29.781  44.716 10.691  1.00 108.91 ? 292 LEU A CA  1 
ATOM   2289 C C   . LEU A 1 290 ? 29.732  44.783 12.214  1.00 101.90 ? 292 LEU A C   1 
ATOM   2290 O O   . LEU A 1 290 ? 30.302  45.716 12.797  1.00 107.38 ? 292 LEU A O   1 
ATOM   2291 C CB  . LEU A 1 290 ? 30.495  43.460 10.190  1.00 106.51 ? 292 LEU A CB  1 
ATOM   2292 C CG  . LEU A 1 290 ? 30.577  43.319 8.673   1.00 107.35 ? 292 LEU A CG  1 
ATOM   2293 C CD1 . LEU A 1 290 ? 31.498  42.169 8.300   1.00 107.84 ? 292 LEU A CD1 1 
ATOM   2294 C CD2 . LEU A 1 290 ? 29.187  43.127 8.089   1.00 109.53 ? 292 LEU A CD2 1 
ATOM   2295 N N   . PRO A 1 291 ? 29.056  43.862 12.909  1.00 95.78  ? 293 PRO A N   1 
ATOM   2296 C CA  . PRO A 1 291 ? 28.946  44.022 14.364  1.00 95.92  ? 293 PRO A CA  1 
ATOM   2297 C C   . PRO A 1 291 ? 30.138  43.513 15.155  1.00 95.10  ? 293 PRO A C   1 
ATOM   2298 O O   . PRO A 1 291 ? 30.259  43.871 16.336  1.00 93.04  ? 293 PRO A O   1 
ATOM   2299 C CB  . PRO A 1 291 ? 27.677  43.238 14.708  1.00 92.71  ? 293 PRO A CB  1 
ATOM   2300 C CG  . PRO A 1 291 ? 27.620  42.189 13.690  1.00 90.02  ? 293 PRO A CG  1 
ATOM   2301 C CD  . PRO A 1 291 ? 28.160  42.800 12.421  1.00 92.42  ? 293 PRO A CD  1 
ATOM   2302 N N   . PHE A 1 292 ? 31.038  42.724 14.563  1.00 98.44  ? 294 PHE A N   1 
ATOM   2303 C CA  . PHE A 1 292 ? 32.099  42.110 15.351  1.00 98.00  ? 294 PHE A CA  1 
ATOM   2304 C C   . PHE A 1 292 ? 33.422  42.101 14.596  1.00 100.65 ? 294 PHE A C   1 
ATOM   2305 O O   . PHE A 1 292 ? 33.475  42.198 13.367  1.00 102.10 ? 294 PHE A O   1 
ATOM   2306 C CB  . PHE A 1 292 ? 31.700  40.700 15.787  1.00 91.54  ? 294 PHE A CB  1 
ATOM   2307 C CG  . PHE A 1 292 ? 30.529  40.683 16.720  1.00 91.69  ? 294 PHE A CG  1 
ATOM   2308 C CD1 . PHE A 1 292 ? 30.680  41.073 18.039  1.00 94.60  ? 294 PHE A CD1 1 
ATOM   2309 C CD2 . PHE A 1 292 ? 29.273  40.309 16.277  1.00 95.87  ? 294 PHE A CD2 1 
ATOM   2310 C CE1 . PHE A 1 292 ? 29.604  41.072 18.906  1.00 107.12 ? 294 PHE A CE1 1 
ATOM   2311 C CE2 . PHE A 1 292 ? 28.191  40.306 17.140  1.00 96.55  ? 294 PHE A CE2 1 
ATOM   2312 C CZ  . PHE A 1 292 ? 28.358  40.690 18.455  1.00 101.15 ? 294 PHE A CZ  1 
ATOM   2313 N N   . GLN A 1 293 ? 34.494  41.954 15.371  1.00 96.01  ? 295 GLN A N   1 
ATOM   2314 C CA  . GLN A 1 293 ? 35.849  42.235 14.922  1.00 93.49  ? 295 GLN A CA  1 
ATOM   2315 C C   . GLN A 1 293 ? 36.822  41.274 15.586  1.00 99.64  ? 295 GLN A C   1 
ATOM   2316 O O   . GLN A 1 293 ? 36.773  41.084 16.805  1.00 105.39 ? 295 GLN A O   1 
ATOM   2317 C CB  . GLN A 1 293 ? 36.226  43.676 15.262  1.00 93.03  ? 295 GLN A CB  1 
ATOM   2318 C CG  . GLN A 1 293 ? 37.710  43.924 15.311  1.00 99.43  ? 295 GLN A CG  1 
ATOM   2319 C CD  . GLN A 1 293 ? 38.036  45.382 15.482  1.00 118.83 ? 295 GLN A CD  1 
ATOM   2320 O OE1 . GLN A 1 293 ? 37.676  45.996 16.484  1.00 131.98 ? 295 GLN A OE1 1 
ATOM   2321 N NE2 . GLN A 1 293 ? 38.720  45.953 14.498  1.00 148.25 ? 295 GLN A NE2 1 
ATOM   2322 N N   . ASN A 1 294 ? 37.703  40.669 14.784  1.00 85.26  ? 296 ASN A N   1 
ATOM   2323 C CA  . ASN A 1 294 ? 38.779  39.830 15.302  1.00 94.47  ? 296 ASN A CA  1 
ATOM   2324 C C   . ASN A 1 294 ? 40.142  40.405 14.923  1.00 96.14  ? 296 ASN A C   1 
ATOM   2325 O O   . ASN A 1 294 ? 41.112  39.655 14.767  1.00 103.47 ? 296 ASN A O   1 
ATOM   2326 C CB  . ASN A 1 294 ? 38.625  38.392 14.790  1.00 99.85  ? 296 ASN A CB  1 
ATOM   2327 C CG  . ASN A 1 294 ? 39.518  37.390 15.513  1.00 135.77 ? 296 ASN A CG  1 
ATOM   2328 O OD1 . ASN A 1 294 ? 40.223  37.732 16.463  1.00 215.78 ? 296 ASN A OD1 1 
ATOM   2329 N ND2 . ASN A 1 294 ? 39.522  36.152 15.030  1.00 170.85 ? 296 ASN A ND2 1 
ATOM   2330 N N   . ILE A 1 295 ? 40.232  41.726 14.756  1.00 103.48 ? 297 ILE A N   1 
ATOM   2331 C CA  . ILE A 1 295 ? 41.497  42.359 14.396  1.00 99.95  ? 297 ILE A CA  1 
ATOM   2332 C C   . ILE A 1 295 ? 42.290  42.680 15.657  1.00 96.78  ? 297 ILE A C   1 
ATOM   2333 O O   . ILE A 1 295 ? 43.391  42.154 15.852  1.00 98.69  ? 297 ILE A O   1 
ATOM   2334 C CB  . ILE A 1 295 ? 41.271  43.617 13.537  1.00 100.60 ? 297 ILE A CB  1 
ATOM   2335 C CG1 . ILE A 1 295 ? 40.714  43.226 12.167  1.00 109.41 ? 297 ILE A CG1 1 
ATOM   2336 C CG2 . ILE A 1 295 ? 42.572  44.384 13.367  1.00 100.91 ? 297 ILE A CG2 1 
ATOM   2337 C CD1 . ILE A 1 295 ? 40.166  44.388 11.366  1.00 120.71 ? 297 ILE A CD1 1 
ATOM   2338 N N   . HIS A 1 296 ? 41.748  43.530 16.527  1.00 102.37 ? 298 HIS A N   1 
ATOM   2339 C CA  . HIS A 1 296 ? 42.477  43.908 17.729  1.00 94.48  ? 298 HIS A CA  1 
ATOM   2340 C C   . HIS A 1 296 ? 41.490  44.287 18.820  1.00 97.38  ? 298 HIS A C   1 
ATOM   2341 O O   . HIS A 1 296 ? 40.400  44.786 18.516  1.00 99.93  ? 298 HIS A O   1 
ATOM   2342 C CB  . HIS A 1 296 ? 43.427  45.083 17.469  1.00 101.73 ? 298 HIS A CB  1 
ATOM   2343 C CG  . HIS A 1 296 ? 44.496  45.222 18.504  1.00 102.56 ? 298 HIS A CG  1 
ATOM   2344 N ND1 . HIS A 1 296 ? 44.441  46.164 19.509  1.00 102.13 ? 298 HIS A ND1 1 
ATOM   2345 C CD2 . HIS A 1 296 ? 45.646  44.535 18.695  1.00 106.74 ? 298 HIS A CD2 1 
ATOM   2346 C CE1 . HIS A 1 296 ? 45.514  46.055 20.272  1.00 102.32 ? 298 HIS A CE1 1 
ATOM   2347 N NE2 . HIS A 1 296 ? 46.262  45.075 19.798  1.00 108.24 ? 298 HIS A NE2 1 
ATOM   2348 N N   . PRO A 1 297 ? 41.832  44.066 20.096  1.00 99.86  ? 299 PRO A N   1 
ATOM   2349 C CA  . PRO A 1 297 ? 40.908  44.447 21.175  1.00 100.47 ? 299 PRO A CA  1 
ATOM   2350 C C   . PRO A 1 297 ? 40.925  45.928 21.530  1.00 104.06 ? 299 PRO A C   1 
ATOM   2351 O O   . PRO A 1 297 ? 39.982  46.392 22.188  1.00 106.08 ? 299 PRO A O   1 
ATOM   2352 C CB  . PRO A 1 297 ? 41.379  43.580 22.353  1.00 100.31 ? 299 PRO A CB  1 
ATOM   2353 C CG  . PRO A 1 297 ? 42.828  43.386 22.082  1.00 94.65  ? 299 PRO A CG  1 
ATOM   2354 C CD  . PRO A 1 297 ? 42.887  43.167 20.594  1.00 103.22 ? 299 PRO A CD  1 
ATOM   2355 N N   . ILE A 1 298 ? 41.946  46.656 21.087  1.00 101.97 ? 300 ILE A N   1 
ATOM   2356 C CA  . ILE A 1 298 ? 42.035  48.109 21.404  1.00 99.41  ? 300 ILE A CA  1 
ATOM   2357 C C   . ILE A 1 298 ? 41.462  48.898 20.225  1.00 105.35 ? 300 ILE A C   1 
ATOM   2358 O O   . ILE A 1 298 ? 42.115  48.930 19.169  1.00 106.50 ? 300 ILE A O   1 
ATOM   2359 C CB  . ILE A 1 298 ? 43.483  48.515 21.731  1.00 99.62  ? 300 ILE A CB  1 
ATOM   2360 C CG1 . ILE A 1 298 ? 44.072  47.658 22.853  1.00 94.79  ? 300 ILE A CG1 1 
ATOM   2361 C CG2 . ILE A 1 298 ? 43.560  49.994 22.066  1.00 113.99 ? 300 ILE A CG2 1 
ATOM   2362 C CD1 . ILE A 1 298 ? 45.455  48.083 23.282  1.00 83.30  ? 300 ILE A CD1 1 
ATOM   2363 N N   . THR A 1 299 ? 40.286  49.502 20.404  1.00 104.08 ? 301 THR A N   1 
ATOM   2364 C CA  . THR A 1 299 ? 39.627  50.242 19.297  1.00 107.56 ? 301 THR A CA  1 
ATOM   2365 C C   . THR A 1 299 ? 39.225  51.645 19.756  1.00 114.39 ? 301 THR A C   1 
ATOM   2366 O O   . THR A 1 299 ? 39.125  51.852 20.978  1.00 114.58 ? 301 THR A O   1 
ATOM   2367 C CB  . THR A 1 299 ? 38.379  49.505 18.814  1.00 96.59  ? 301 THR A CB  1 
ATOM   2368 O OG1 . THR A 1 299 ? 37.341  49.755 19.762  1.00 90.99  ? 301 THR A OG1 1 
ATOM   2369 C CG2 . THR A 1 299 ? 38.597  48.017 18.664  1.00 102.22 ? 301 THR A CG2 1 
ATOM   2370 N N   . ILE A 1 300 ? 39.026  52.565 18.804  1.00 111.37 ? 302 ILE A N   1 
ATOM   2371 C CA  . ILE A 1 300 ? 38.625  53.968 19.129  1.00 121.46 ? 302 ILE A CA  1 
ATOM   2372 C C   . ILE A 1 300 ? 37.465  54.368 18.211  1.00 135.29 ? 302 ILE A C   1 
ATOM   2373 O O   . ILE A 1 300 ? 37.597  54.182 16.985  1.00 143.45 ? 302 ILE A O   1 
ATOM   2374 C CB  . ILE A 1 300 ? 39.819  54.933 18.972  1.00 123.72 ? 302 ILE A CB  1 
ATOM   2375 C CG1 . ILE A 1 300 ? 40.826  54.791 20.115  1.00 126.72 ? 302 ILE A CG1 1 
ATOM   2376 C CG2 . ILE A 1 300 ? 39.341  56.370 18.831  1.00 141.74 ? 302 ILE A CG2 1 
ATOM   2377 C CD1 . ILE A 1 300 ? 41.873  55.881 20.138  1.00 157.88 ? 302 ILE A CD1 1 
ATOM   2378 N N   . GLY A 1 301 ? 36.378  54.897 18.781  1.00 129.14 ? 303 GLY A N   1 
ATOM   2379 C CA  . GLY A 1 301 ? 35.233  55.353 17.969  1.00 122.98 ? 303 GLY A CA  1 
ATOM   2380 C C   . GLY A 1 301 ? 34.225  54.243 17.729  1.00 129.78 ? 303 GLY A C   1 
ATOM   2381 O O   . GLY A 1 301 ? 34.213  53.277 18.517  1.00 126.90 ? 303 GLY A O   1 
ATOM   2382 N N   . LYS A 1 302 ? 33.412  54.369 16.675  1.00 129.58 ? 304 LYS A N   1 
ATOM   2383 C CA  . LYS A 1 302 ? 32.364  53.358 16.376  1.00 129.43 ? 304 LYS A CA  1 
ATOM   2384 C C   . LYS A 1 302 ? 33.033  52.113 15.790  1.00 131.84 ? 304 LYS A C   1 
ATOM   2385 O O   . LYS A 1 302 ? 33.152  52.045 14.553  1.00 140.77 ? 304 LYS A O   1 
ATOM   2386 C CB  . LYS A 1 302 ? 31.354  53.930 15.378  1.00 134.43 ? 304 LYS A CB  1 
ATOM   2387 C CG  . LYS A 1 302 ? 31.087  55.423 15.511  1.00 149.24 ? 304 LYS A CG  1 
ATOM   2388 C CD  . LYS A 1 302 ? 30.297  55.990 14.352  1.00 156.74 ? 304 LYS A CD  1 
ATOM   2389 C CE  . LYS A 1 302 ? 30.155  57.496 14.413  1.00 193.05 ? 304 LYS A CE  1 
ATOM   2390 N NZ  . LYS A 1 302 ? 29.425  58.025 13.237  1.00 218.86 ? 304 LYS A NZ  1 
ATOM   2391 N N   . CYS A 1 303 ? 33.441  51.168 16.642  1.00 128.65 ? 305 CYS A N   1 
ATOM   2392 C CA  . CYS A 1 303 ? 34.179  49.972 16.152  1.00 117.93 ? 305 CYS A CA  1 
ATOM   2393 C C   . CYS A 1 303 ? 33.412  48.694 16.503  1.00 108.84 ? 305 CYS A C   1 
ATOM   2394 O O   . CYS A 1 303 ? 32.770  48.661 17.571  1.00 110.30 ? 305 CYS A O   1 
ATOM   2395 C CB  . CYS A 1 303 ? 35.566  49.911 16.776  1.00 118.30 ? 305 CYS A CB  1 
ATOM   2396 S SG  . CYS A 1 303 ? 36.459  51.484 16.685  1.00 134.53 ? 305 CYS A SG  1 
ATOM   2397 N N   . PRO A 1 304 ? 33.459  47.642 15.655  1.00 105.40 ? 306 PRO A N   1 
ATOM   2398 C CA  . PRO A 1 304 ? 32.801  46.370 15.962  1.00 99.92  ? 306 PRO A CA  1 
ATOM   2399 C C   . PRO A 1 304 ? 33.389  45.743 17.234  1.00 99.80  ? 306 PRO A C   1 
ATOM   2400 O O   . PRO A 1 304 ? 34.594  45.792 17.401  1.00 105.90 ? 306 PRO A O   1 
ATOM   2401 C CB  . PRO A 1 304 ? 33.132  45.488 14.749  1.00 98.80  ? 306 PRO A CB  1 
ATOM   2402 C CG  . PRO A 1 304 ? 33.470  46.466 13.647  1.00 101.57 ? 306 PRO A CG  1 
ATOM   2403 C CD  . PRO A 1 304 ? 34.134  47.627 14.356  1.00 107.48 ? 306 PRO A CD  1 
ATOM   2404 N N   . LYS A 1 305 ? 32.533  45.173 18.088  1.00 105.53 ? 307 LYS A N   1 
ATOM   2405 C CA  . LYS A 1 305 ? 33.002  44.560 19.360  1.00 105.94 ? 307 LYS A CA  1 
ATOM   2406 C C   . LYS A 1 305 ? 34.083  43.518 19.053  1.00 99.00  ? 307 LYS A C   1 
ATOM   2407 O O   . LYS A 1 305 ? 33.868  42.697 18.140  1.00 99.47  ? 307 LYS A O   1 
ATOM   2408 C CB  . LYS A 1 305 ? 31.828  43.918 20.105  1.00 114.59 ? 307 LYS A CB  1 
ATOM   2409 C CG  . LYS A 1 305 ? 30.661  44.851 20.394  1.00 124.04 ? 307 LYS A CG  1 
ATOM   2410 C CD  . LYS A 1 305 ? 31.069  46.083 21.172  1.00 135.72 ? 307 LYS A CD  1 
ATOM   2411 C CE  . LYS A 1 305 ? 29.935  47.069 21.356  1.00 143.73 ? 307 LYS A CE  1 
ATOM   2412 N NZ  . LYS A 1 305 ? 30.389  48.304 22.037  1.00 160.42 ? 307 LYS A NZ  1 
ATOM   2413 N N   . TYR A 1 306 ? 35.197  43.550 19.792  1.00 94.37  ? 308 TYR A N   1 
ATOM   2414 C CA  . TYR A 1 306 ? 36.277  42.604 19.537  1.00 97.71  ? 308 TYR A CA  1 
ATOM   2415 C C   . TYR A 1 306 ? 35.892  41.195 19.972  1.00 97.23  ? 308 TYR A C   1 
ATOM   2416 O O   . TYR A 1 306 ? 35.322  41.001 21.048  1.00 103.07 ? 308 TYR A O   1 
ATOM   2417 C CB  . TYR A 1 306 ? 37.557  43.027 20.251  1.00 94.46  ? 308 TYR A CB  1 
ATOM   2418 C CG  . TYR A 1 306 ? 38.677  42.034 20.039  1.00 98.92  ? 308 TYR A CG  1 
ATOM   2419 C CD1 . TYR A 1 306 ? 39.252  41.871 18.786  1.00 104.08 ? 308 TYR A CD1 1 
ATOM   2420 C CD2 . TYR A 1 306 ? 39.143  41.243 21.081  1.00 99.42  ? 308 TYR A CD2 1 
ATOM   2421 C CE1 . TYR A 1 306 ? 40.269  40.959 18.582  1.00 107.13 ? 308 TYR A CE1 1 
ATOM   2422 C CE2 . TYR A 1 306 ? 40.162  40.330 20.887  1.00 98.10  ? 308 TYR A CE2 1 
ATOM   2423 C CZ  . TYR A 1 306 ? 40.721  40.191 19.634  1.00 102.72 ? 308 TYR A CZ  1 
ATOM   2424 O OH  . TYR A 1 306 ? 41.734  39.283 19.428  1.00 107.66 ? 308 TYR A OH  1 
ATOM   2425 N N   . VAL A 1 307 ? 36.226  40.208 19.139  1.00 95.05  ? 309 VAL A N   1 
ATOM   2426 C CA  . VAL A 1 307 ? 35.937  38.803 19.406  1.00 94.62  ? 309 VAL A CA  1 
ATOM   2427 C C   . VAL A 1 307 ? 37.174  37.979 19.064  1.00 105.82 ? 309 VAL A C   1 
ATOM   2428 O O   . VAL A 1 307 ? 37.879  38.280 18.095  1.00 114.15 ? 309 VAL A O   1 
ATOM   2429 C CB  . VAL A 1 307 ? 34.714  38.310 18.599  1.00 85.26  ? 309 VAL A CB  1 
ATOM   2430 C CG1 . VAL A 1 307 ? 34.449  36.840 18.871  1.00 94.67  ? 309 VAL A CG1 1 
ATOM   2431 C CG2 . VAL A 1 307 ? 33.482  39.140 18.919  1.00 89.25  ? 309 VAL A CG2 1 
ATOM   2432 N N   . LYS A 1 308 ? 37.439  36.938 19.859  1.00 104.92 ? 310 LYS A N   1 
ATOM   2433 C CA  . LYS A 1 308 ? 38.578  36.037 19.651  1.00 108.52 ? 310 LYS A CA  1 
ATOM   2434 C C   . LYS A 1 308 ? 38.236  34.797 18.827  1.00 110.99 ? 310 LYS A C   1 
ATOM   2435 O O   . LYS A 1 308 ? 38.783  33.723 19.101  1.00 112.47 ? 310 LYS A O   1 
ATOM   2436 C CB  . LYS A 1 308 ? 39.168  35.612 20.995  1.00 93.00  ? 310 LYS A CB  1 
ATOM   2437 C CG  . LYS A 1 308 ? 39.910  36.671 21.796  1.00 93.56  ? 310 LYS A CG  1 
ATOM   2438 C CD  . LYS A 1 308 ? 40.985  35.986 22.645  1.00 100.98 ? 310 LYS A CD  1 
ATOM   2439 C CE  . LYS A 1 308 ? 41.656  36.928 23.631  1.00 106.82 ? 310 LYS A CE  1 
ATOM   2440 N NZ  . LYS A 1 308 ? 41.199  36.663 25.022  1.00 112.22 ? 310 LYS A NZ  1 
ATOM   2441 N N   . SER A 1 309 ? 37.366  34.872 17.825  1.00 97.38  ? 311 SER A N   1 
ATOM   2442 C CA  . SER A 1 309 ? 37.020  33.687 17.050  1.00 97.81  ? 311 SER A CA  1 
ATOM   2443 C C   . SER A 1 309 ? 37.314  33.913 15.574  1.00 102.96 ? 311 SER A C   1 
ATOM   2444 O O   . SER A 1 309 ? 37.595  35.027 15.130  1.00 107.71 ? 311 SER A O   1 
ATOM   2445 C CB  . SER A 1 309 ? 35.547  33.305 17.241  1.00 88.14  ? 311 SER A CB  1 
ATOM   2446 O OG  . SER A 1 309 ? 34.704  34.407 16.983  1.00 99.29  ? 311 SER A OG  1 
ATOM   2447 N N   . THR A 1 310 ? 37.235  32.824 14.813  1.00 92.99  ? 312 THR A N   1 
ATOM   2448 C CA  . THR A 1 310 ? 37.578  32.825 13.398  1.00 89.10  ? 312 THR A CA  1 
ATOM   2449 C C   . THR A 1 310 ? 36.370  32.960 12.482  1.00 96.20  ? 312 THR A C   1 
ATOM   2450 O O   . THR A 1 310 ? 36.438  33.691 11.490  1.00 101.20 ? 312 THR A O   1 
ATOM   2451 C CB  . THR A 1 310 ? 38.342  31.547 13.045  1.00 99.36  ? 312 THR A CB  1 
ATOM   2452 O OG1 . THR A 1 310 ? 37.423  30.454 12.919  1.00 114.14 ? 312 THR A OG1 1 
ATOM   2453 C CG2 . THR A 1 310 ? 39.348  31.225 14.143  1.00 97.45  ? 312 THR A CG2 1 
ATOM   2454 N N   . LYS A 1 311 ? 35.261  32.284 12.781  1.00 100.33 ? 313 LYS A N   1 
ATOM   2455 C CA  . LYS A 1 311 ? 34.066  32.394 11.954  1.00 94.34  ? 313 LYS A CA  1 
ATOM   2456 C C   . LYS A 1 311 ? 32.824  32.529 12.823  1.00 85.96  ? 313 LYS A C   1 
ATOM   2457 O O   . LYS A 1 311 ? 32.722  31.902 13.882  1.00 87.16  ? 313 LYS A O   1 
ATOM   2458 C CB  . LYS A 1 311 ? 33.915  31.197 11.002  1.00 101.05 ? 313 LYS A CB  1 
ATOM   2459 C CG  . LYS A 1 311 ? 34.989  31.136 9.923   1.00 134.33 ? 313 LYS A CG  1 
ATOM   2460 C CD  . LYS A 1 311 ? 34.778  29.962 8.980   1.00 167.60 ? 313 LYS A CD  1 
ATOM   2461 C CE  . LYS A 1 311 ? 35.935  29.845 7.998   1.00 161.83 ? 313 LYS A CE  1 
ATOM   2462 N NZ  . LYS A 1 311 ? 35.826  28.645 7.122   1.00 161.10 ? 313 LYS A NZ  1 
ATOM   2463 N N   . LEU A 1 312 ? 31.881  33.359 12.355  1.00 82.73  ? 314 LEU A N   1 
ATOM   2464 C CA  . LEU A 1 312 ? 30.612  33.674 13.005  1.00 71.66  ? 314 LEU A CA  1 
ATOM   2465 C C   . LEU A 1 312 ? 29.575  33.980 11.918  1.00 67.95  ? 314 LEU A C   1 
ATOM   2466 O O   . LEU A 1 312 ? 29.182  35.124 11.693  1.00 70.79  ? 314 LEU A O   1 
ATOM   2467 C CB  . LEU A 1 312 ? 30.744  34.849 13.979  1.00 73.07  ? 314 LEU A CB  1 
ATOM   2468 C CG  . LEU A 1 312 ? 31.349  34.676 15.377  1.00 72.54  ? 314 LEU A CG  1 
ATOM   2469 C CD1 . LEU A 1 312 ? 31.122  35.926 16.225  1.00 58.07  ? 314 LEU A CD1 1 
ATOM   2470 C CD2 . LEU A 1 312 ? 30.763  33.460 16.070  1.00 85.95  ? 314 LEU A CD2 1 
ATOM   2471 N N   . ARG A 1 313 ? 29.114  32.942 11.222  1.00 68.74  ? 315 ARG A N   1 
ATOM   2472 C CA  . ARG A 1 313 ? 28.075  33.081 10.209  1.00 65.42  ? 315 ARG A CA  1 
ATOM   2473 C C   . ARG A 1 313 ? 26.742  32.617 10.769  1.00 58.30  ? 315 ARG A C   1 
ATOM   2474 O O   . ARG A 1 313 ? 26.660  31.569 11.417  1.00 61.52  ? 315 ARG A O   1 
ATOM   2475 C CB  . ARG A 1 313 ? 28.391  32.272 8.950   1.00 69.13  ? 315 ARG A CB  1 
ATOM   2476 C CG  . ARG A 1 313 ? 29.323  32.961 7.977   1.00 81.47  ? 315 ARG A CG  1 
ATOM   2477 C CD  . ARG A 1 313 ? 29.597  32.071 6.772   1.00 81.63  ? 315 ARG A CD  1 
ATOM   2478 N NE  . ARG A 1 313 ? 31.002  32.031 6.377   1.00 108.13 ? 315 ARG A NE  1 
ATOM   2479 C CZ  . ARG A 1 313 ? 31.749  33.079 6.054   1.00 127.33 ? 315 ARG A CZ  1 
ATOM   2480 N NH1 . ARG A 1 313 ? 31.242  34.297 5.969   1.00 122.05 ? 315 ARG A NH1 1 
ATOM   2481 N NH2 . ARG A 1 313 ? 33.038  32.897 5.791   1.00 162.81 ? 315 ARG A NH2 1 
ATOM   2482 N N   . LEU A 1 314 ? 25.699  33.397 10.509  1.00 63.08  ? 316 LEU A N   1 
ATOM   2483 C CA  . LEU A 1 314 ? 24.333  33.006 10.821  1.00 56.19  ? 316 LEU A CA  1 
ATOM   2484 C C   . LEU A 1 314 ? 23.671  32.476 9.560   1.00 53.25  ? 316 LEU A C   1 
ATOM   2485 O O   . LEU A 1 314 ? 23.702  33.133 8.511   1.00 62.41  ? 316 LEU A O   1 
ATOM   2486 C CB  . LEU A 1 314 ? 23.522  34.177 11.379  1.00 59.86  ? 316 LEU A CB  1 
ATOM   2487 C CG  . LEU A 1 314 ? 23.914  34.686 12.764  1.00 63.26  ? 316 LEU A CG  1 
ATOM   2488 C CD1 . LEU A 1 314 ? 23.277  36.038 13.035  1.00 63.53  ? 316 LEU A CD1 1 
ATOM   2489 C CD2 . LEU A 1 314 ? 23.532  33.675 13.847  1.00 63.19  ? 316 LEU A CD2 1 
ATOM   2490 N N   . ALA A 1 315 ? 23.092  31.284 9.664   1.00 55.35  ? 317 ALA A N   1 
ATOM   2491 C CA  . ALA A 1 315 ? 22.287  30.750 8.579   1.00 56.81  ? 317 ALA A CA  1 
ATOM   2492 C C   . ALA A 1 315 ? 21.044  31.604 8.396   1.00 64.24  ? 317 ALA A C   1 
ATOM   2493 O O   . ALA A 1 315 ? 20.277  31.814 9.338   1.00 75.74  ? 317 ALA A O   1 
ATOM   2494 C CB  . ALA A 1 315 ? 21.892  29.303 8.869   1.00 60.65  ? 317 ALA A CB  1 
ATOM   2495 N N   . THR A 1 316 ? 20.858  32.113 7.183   1.00 60.90  ? 318 THR A N   1 
ATOM   2496 C CA  . THR A 1 316 ? 19.656  32.852 6.840   1.00 57.91  ? 318 THR A CA  1 
ATOM   2497 C C   . THR A 1 316 ? 18.804  32.135 5.809   1.00 56.95  ? 318 THR A C   1 
ATOM   2498 O O   . THR A 1 316 ? 17.745  32.652 5.439   1.00 66.02  ? 318 THR A O   1 
ATOM   2499 C CB  . THR A 1 316 ? 20.015  34.249 6.325   1.00 66.32  ? 318 THR A CB  1 
ATOM   2500 O OG1 . THR A 1 316 ? 20.815  34.133 5.142   1.00 69.97  ? 318 THR A OG1 1 
ATOM   2501 C CG2 . THR A 1 316 ? 20.789  35.014 7.382   1.00 71.22  ? 318 THR A CG2 1 
ATOM   2502 N N   . GLY A 1 317 ? 19.221  30.960 5.345   1.00 57.84  ? 319 GLY A N   1 
ATOM   2503 C CA  . GLY A 1 317 ? 18.463  30.265 4.327   1.00 60.32  ? 319 GLY A CA  1 
ATOM   2504 C C   . GLY A 1 317 ? 18.287  28.785 4.586   1.00 59.74  ? 319 GLY A C   1 
ATOM   2505 O O   . GLY A 1 317 ? 18.382  28.319 5.724   1.00 66.45  ? 319 GLY A O   1 
ATOM   2506 N N   . LEU A 1 318 ? 18.031  28.041 3.520   1.00 60.86  ? 320 LEU A N   1 
ATOM   2507 C CA  . LEU A 1 318 ? 17.750  26.619 3.586   1.00 72.01  ? 320 LEU A CA  1 
ATOM   2508 C C   . LEU A 1 318 ? 19.042  25.811 3.652   1.00 75.97  ? 320 LEU A C   1 
ATOM   2509 O O   . LEU A 1 318 ? 20.118  26.274 3.266   1.00 79.83  ? 320 LEU A O   1 
ATOM   2510 C CB  . LEU A 1 318 ? 16.942  26.199 2.360   1.00 72.01  ? 320 LEU A CB  1 
ATOM   2511 C CG  . LEU A 1 318 ? 15.576  26.863 2.228   1.00 63.78  ? 320 LEU A CG  1 
ATOM   2512 C CD1 . LEU A 1 318 ? 14.899  26.387 0.985   1.00 70.56  ? 320 LEU A CD1 1 
ATOM   2513 C CD2 . LEU A 1 318 ? 14.745  26.476 3.417   1.00 84.99  ? 320 LEU A CD2 1 
ATOM   2514 N N   . ARG A 1 319 ? 18.929  24.585 4.153   1.00 81.03  ? 321 ARG A N   1 
ATOM   2515 C CA  . ARG A 1 319 ? 19.972  23.609 3.888   1.00 82.14  ? 321 ARG A CA  1 
ATOM   2516 C C   . ARG A 1 319 ? 20.045  23.397 2.386   1.00 86.61  ? 321 ARG A C   1 
ATOM   2517 O O   . ARG A 1 319 ? 19.069  22.960 1.767   1.00 81.78  ? 321 ARG A O   1 
ATOM   2518 C CB  . ARG A 1 319 ? 19.679  22.287 4.597   1.00 82.29  ? 321 ARG A CB  1 
ATOM   2519 C CG  . ARG A 1 319 ? 20.006  22.261 6.077   1.00 94.69  ? 321 ARG A CG  1 
ATOM   2520 C CD  . ARG A 1 319 ? 19.946  20.831 6.605   1.00 98.35  ? 321 ARG A CD  1 
ATOM   2521 N NE  . ARG A 1 319 ? 19.578  20.770 8.015   1.00 108.10 ? 321 ARG A NE  1 
ATOM   2522 C CZ  . ARG A 1 319 ? 20.400  20.408 8.991   1.00 115.69 ? 321 ARG A CZ  1 
ATOM   2523 N NH1 . ARG A 1 319 ? 21.649  20.046 8.745   1.00 117.49 ? 321 ARG A NH1 1 
ATOM   2524 N NH2 . ARG A 1 319 ? 19.958  20.411 10.247  1.00 114.91 ? 321 ARG A NH2 1 
ATOM   2525 N N   . ASN A 1 320 ? 21.179  23.742 1.788   1.00 86.33  ? 322 ASN A N   1 
ATOM   2526 C CA  . ASN A 1 320 ? 21.363  23.474 0.369   1.00 89.05  ? 322 ASN A CA  1 
ATOM   2527 C C   . ASN A 1 320 ? 21.633  21.983 0.230   1.00 102.77 ? 322 ASN A C   1 
ATOM   2528 O O   . ASN A 1 320 ? 22.646  21.478 0.723   1.00 110.67 ? 322 ASN A O   1 
ATOM   2529 C CB  . ASN A 1 320 ? 22.595  24.195 -0.164  1.00 83.87  ? 322 ASN A CB  1 
ATOM   2530 C CG  . ASN A 1 320 ? 22.660  24.179 -1.675  1.00 96.00  ? 322 ASN A CG  1 
ATOM   2531 O OD1 . ASN A 1 320 ? 21.630  24.171 -2.353  1.00 100.57 ? 322 ASN A OD1 1 
ATOM   2532 N ND2 . ASN A 1 320 ? 23.870  24.159 -2.213  1.00 104.92 ? 322 ASN A ND2 1 
ATOM   2533 N N   . VAL A 1 321 ? 20.718  21.268 -0.418  1.00 95.02  ? 323 VAL A N   1 
ATOM   2534 C CA  . VAL A 1 321 ? 20.886  19.851 -0.702  1.00 102.50 ? 323 VAL A CA  1 
ATOM   2535 C C   . VAL A 1 321 ? 20.298  19.664 -2.114  1.00 107.13 ? 323 VAL A C   1 
ATOM   2536 O O   . VAL A 1 321 ? 19.084  19.495 -2.296  1.00 104.54 ? 323 VAL A O   1 
ATOM   2537 C CB  . VAL A 1 321 ? 20.168  18.934 0.305   1.00 111.61 ? 323 VAL A CB  1 
ATOM   2538 C CG1 . VAL A 1 321 ? 20.763  19.100 1.695   1.00 102.88 ? 323 VAL A CG1 1 
ATOM   2539 C CG2 . VAL A 1 321 ? 18.675  19.222 0.318   1.00 114.74 ? 323 VAL A CG2 1 
ATOM   2540 N N   . PRO A 1 322 ? 21.129  19.802 -3.144  1.00 117.41 ? 324 PRO A N   1 
ATOM   2541 C CA  . PRO A 1 322 ? 20.639  19.653 -4.518  1.00 117.99 ? 324 PRO A CA  1 
ATOM   2542 C C   . PRO A 1 322 ? 20.470  18.165 -4.781  1.00 124.03 ? 324 PRO A C   1 
ATOM   2543 O O   . PRO A 1 322 ? 20.860  17.314 -3.980  1.00 119.64 ? 324 PRO A O   1 
ATOM   2544 C CB  . PRO A 1 322 ? 21.839  20.232 -5.280  1.00 113.10 ? 324 PRO A CB  1 
ATOM   2545 C CG  . PRO A 1 322 ? 22.487  21.180 -4.300  1.00 103.15 ? 324 PRO A CG  1 
ATOM   2546 C CD  . PRO A 1 322 ? 22.329  20.475 -2.989  1.00 111.20 ? 324 PRO A CD  1 
ATOM   2547 N N   . SER A 1 323 ? 19.881  17.876 -5.943  1.00 127.21 ? 325 SER A N   1 
ATOM   2548 C CA  . SER A 1 323 ? 19.479  16.534 -6.413  1.00 128.24 ? 325 SER A CA  1 
ATOM   2549 C C   . SER A 1 323 ? 19.759  15.360 -5.475  1.00 128.37 ? 325 SER A C   1 
ATOM   2550 O O   . SER A 1 323 ? 18.992  14.403 -5.423  1.00 121.06 ? 325 SER A O   1 
ATOM   2551 C CB  . SER A 1 323 ? 20.141  16.251 -7.765  1.00 122.48 ? 325 SER A CB  1 
ATOM   2552 O OG  . SER A 1 323 ? 21.549  16.166 -7.640  1.00 120.46 ? 325 SER A OG  1 
ATOM   2553 N N   . ILE B 1 337 ? 10.139  14.987 2.789   1.00 132.72 ? 10  ILE B N   1 
ATOM   2554 C CA  . ILE B 1 337 ? 10.788  15.713 1.705   1.00 145.06 ? 10  ILE B CA  1 
ATOM   2555 C C   . ILE B 1 337 ? 12.269  15.906 1.996   1.00 146.63 ? 10  ILE B C   1 
ATOM   2556 O O   . ILE B 1 337 ? 12.636  16.608 2.937   1.00 152.99 ? 10  ILE B O   1 
ATOM   2557 C CB  . ILE B 1 337 ? 10.124  17.078 1.466   1.00 140.15 ? 10  ILE B CB  1 
ATOM   2558 C CG1 . ILE B 1 337 ? 8.622   16.920 1.256   1.00 143.55 ? 10  ILE B CG1 1 
ATOM   2559 C CG2 . ILE B 1 337 ? 10.746  17.764 0.263   1.00 122.97 ? 10  ILE B CG2 1 
ATOM   2560 C CD1 . ILE B 1 337 ? 7.875   18.231 1.236   1.00 128.84 ? 10  ILE B CD1 1 
ATOM   2561 N N   . GLU B 1 338 ? 13.123  15.284 1.186   1.00 143.52 ? 11  GLU B N   1 
ATOM   2562 C CA  . GLU B 1 338 ? 14.565  15.501 1.257   1.00 145.17 ? 11  GLU B CA  1 
ATOM   2563 C C   . GLU B 1 338 ? 15.101  15.758 -0.152  1.00 135.25 ? 11  GLU B C   1 
ATOM   2564 O O   . GLU B 1 338 ? 15.968  15.053 -0.666  1.00 158.18 ? 11  GLU B O   1 
ATOM   2565 C CB  . GLU B 1 338 ? 15.280  14.331 1.933   1.00 160.79 ? 11  GLU B CB  1 
ATOM   2566 C CG  . GLU B 1 338 ? 15.004  14.233 3.432   1.00 174.13 ? 11  GLU B CG  1 
ATOM   2567 C CD  . GLU B 1 338 ? 15.893  13.221 4.130   1.00 177.80 ? 11  GLU B CD  1 
ATOM   2568 O OE1 . GLU B 1 338 ? 16.714  12.579 3.443   1.00 177.24 ? 11  GLU B OE1 1 
ATOM   2569 O OE2 . GLU B 1 338 ? 15.772  13.069 5.365   1.00 189.01 ? 11  GLU B OE2 1 
ATOM   2570 N N   . GLY B 1 339 ? 14.558  16.794 -0.782  1.00 131.12 ? 12  GLY B N   1 
ATOM   2571 C CA  . GLY B 1 339 ? 15.014  17.226 -2.085  1.00 120.25 ? 12  GLY B CA  1 
ATOM   2572 C C   . GLY B 1 339 ? 14.952  18.730 -2.234  1.00 107.56 ? 12  GLY B C   1 
ATOM   2573 O O   . GLY B 1 339 ? 13.886  19.336 -2.082  1.00 105.43 ? 12  GLY B O   1 
ATOM   2574 N N   . GLY B 1 340 ? 16.097  19.349 -2.513  1.00 102.01 ? 13  GLY B N   1 
ATOM   2575 C CA  . GLY B 1 340 ? 16.144  20.772 -2.772  1.00 98.58  ? 13  GLY B CA  1 
ATOM   2576 C C   . GLY B 1 340 ? 16.064  21.025 -4.261  1.00 98.48  ? 13  GLY B C   1 
ATOM   2577 O O   . GLY B 1 340 ? 16.793  20.413 -5.047  1.00 103.18 ? 13  GLY B O   1 
ATOM   2578 N N   . TRP B 1 341 ? 15.169  21.929 -4.649  1.00 89.42  ? 14  TRP B N   1 
ATOM   2579 C CA  . TRP B 1 341 ? 14.961  22.249 -6.052  1.00 80.53  ? 14  TRP B CA  1 
ATOM   2580 C C   . TRP B 1 341 ? 15.854  23.415 -6.450  1.00 79.54  ? 14  TRP B C   1 
ATOM   2581 O O   . TRP B 1 341 ? 15.762  24.505 -5.874  1.00 81.78  ? 14  TRP B O   1 
ATOM   2582 C CB  . TRP B 1 341 ? 13.494  22.573 -6.325  1.00 80.48  ? 14  TRP B CB  1 
ATOM   2583 C CG  . TRP B 1 341 ? 12.543  21.480 -5.925  1.00 84.74  ? 14  TRP B CG  1 
ATOM   2584 C CD1 . TRP B 1 341 ? 12.862  20.202 -5.562  1.00 94.67  ? 14  TRP B CD1 1 
ATOM   2585 C CD2 . TRP B 1 341 ? 11.113  21.560 -5.884  1.00 87.58  ? 14  TRP B CD2 1 
ATOM   2586 N NE1 . TRP B 1 341 ? 11.721  19.491 -5.277  1.00 104.22 ? 14  TRP B NE1 1 
ATOM   2587 C CE2 . TRP B 1 341 ? 10.634  20.301 -5.471  1.00 92.47  ? 14  TRP B CE2 1 
ATOM   2588 C CE3 . TRP B 1 341 ? 10.192  22.576 -6.149  1.00 92.75  ? 14  TRP B CE3 1 
ATOM   2589 C CZ2 . TRP B 1 341 ? 9.276   20.033 -5.320  1.00 95.19  ? 14  TRP B CZ2 1 
ATOM   2590 C CZ3 . TRP B 1 341 ? 8.845   22.308 -5.997  1.00 92.92  ? 14  TRP B CZ3 1 
ATOM   2591 C CH2 . TRP B 1 341 ? 8.400   21.048 -5.586  1.00 93.45  ? 14  TRP B CH2 1 
ATOM   2592 N N   . THR B 1 342 ? 16.724  23.179 -7.431  1.00 77.63  ? 15  THR B N   1 
ATOM   2593 C CA  . THR B 1 342 ? 17.493  24.273 -8.005  1.00 74.34  ? 15  THR B CA  1 
ATOM   2594 C C   . THR B 1 342 ? 16.647  25.110 -8.951  1.00 80.36  ? 15  THR B C   1 
ATOM   2595 O O   . THR B 1 342 ? 16.942  26.291 -9.159  1.00 79.83  ? 15  THR B O   1 
ATOM   2596 C CB  . THR B 1 342 ? 18.712  23.733 -8.746  1.00 77.04  ? 15  THR B CB  1 
ATOM   2597 O OG1 . THR B 1 342 ? 18.275  22.918 -9.840  1.00 86.83  ? 15  THR B OG1 1 
ATOM   2598 C CG2 . THR B 1 342 ? 19.559  22.898 -7.814  1.00 81.99  ? 15  THR B CG2 1 
ATOM   2599 N N   . GLY B 1 343 ? 15.554  24.533 -9.434  1.00 85.13  ? 16  GLY B N   1 
ATOM   2600 C CA  . GLY B 1 343 ? 14.669  25.267 -10.356 1.00 93.57  ? 16  GLY B CA  1 
ATOM   2601 C C   . GLY B 1 343 ? 13.901  26.383 -9.671  1.00 96.12  ? 16  GLY B C   1 
ATOM   2602 O O   . GLY B 1 343 ? 13.468  27.303 -10.381 1.00 98.44  ? 16  GLY B O   1 
ATOM   2603 N N   . MET B 1 344 ? 13.738  26.320 -8.349  1.00 93.33  ? 17  MET B N   1 
ATOM   2604 C CA  . MET B 1 344 ? 12.913  27.331 -7.659  1.00 85.21  ? 17  MET B CA  1 
ATOM   2605 C C   . MET B 1 344 ? 13.936  28.450 -7.745  1.00 89.05  ? 17  MET B C   1 
ATOM   2606 O O   . MET B 1 344 ? 15.028  28.282 -7.202  1.00 91.19  ? 17  MET B O   1 
ATOM   2607 C CB  . MET B 1 344 ? 12.486  26.848 -6.261  1.00 78.34  ? 17  MET B CB  1 
ATOM   2608 C CG  . MET B 1 344 ? 11.536  25.679 -6.286  1.00 91.37  ? 17  MET B CG  1 
ATOM   2609 S SD  . MET B 1 344 ? 9.847   26.194 -5.945  1.00 93.59  ? 17  MET B SD  1 
ATOM   2610 C CE  . MET B 1 344 ? 10.155  27.714 -5.052  1.00 84.63  ? 17  MET B CE  1 
ATOM   2611 N N   . VAL B 1 345 ? 13.578  29.557 -8.385  1.00 87.86  ? 18  VAL B N   1 
ATOM   2612 C CA  . VAL B 1 345 ? 14.515  30.714 -8.526  1.00 84.74  ? 18  VAL B CA  1 
ATOM   2613 C C   . VAL B 1 345 ? 13.621  31.769 -7.853  1.00 89.65  ? 18  VAL B C   1 
ATOM   2614 O O   . VAL B 1 345 ? 14.167  32.783 -7.395  1.00 89.06  ? 18  VAL B O   1 
ATOM   2615 C CB  . VAL B 1 345 ? 14.889  31.122 -9.947  1.00 90.47  ? 18  VAL B CB  1 
ATOM   2616 C CG1 . VAL B 1 345 ? 15.356  32.563 -10.064 1.00 95.72  ? 18  VAL B CG1 1 
ATOM   2617 C CG2 . VAL B 1 345 ? 15.888  30.158 -10.564 1.00 92.80  ? 18  VAL B CG2 1 
ATOM   2618 N N   . ASP B 1 346 ? 12.309  31.538 -7.780  1.00 87.37  ? 19  ASP B N   1 
ATOM   2619 C CA  . ASP B 1 346 ? 11.437  32.581 -7.240  1.00 85.85  ? 19  ASP B CA  1 
ATOM   2620 C C   . ASP B 1 346 ? 11.468  32.639 -5.714  1.00 80.84  ? 19  ASP B C   1 
ATOM   2621 O O   . ASP B 1 346 ? 11.543  33.729 -5.134  1.00 74.55  ? 19  ASP B O   1 
ATOM   2622 C CB  . ASP B 1 346 ? 9.984   32.373 -7.668  1.00 94.17  ? 19  ASP B CB  1 
ATOM   2623 C CG  . ASP B 1 346 ? 9.646   33.005 -8.994  1.00 117.68 ? 19  ASP B CG  1 
ATOM   2624 O OD1 . ASP B 1 346 ? 9.966   34.191 -9.210  1.00 150.64 ? 19  ASP B OD1 1 
ATOM   2625 O OD2 . ASP B 1 346 ? 8.954   32.333 -9.784  1.00 145.04 ? 19  ASP B OD2 1 
ATOM   2626 N N   . GLY B 1 347 ? 11.366  31.492 -5.043  1.00 95.02  ? 20  GLY B N   1 
ATOM   2627 C CA  . GLY B 1 347 ? 11.133  31.493 -3.608  1.00 93.21  ? 20  GLY B CA  1 
ATOM   2628 C C   . GLY B 1 347 ? 11.770  30.326 -2.880  1.00 83.67  ? 20  GLY B C   1 
ATOM   2629 O O   . GLY B 1 347 ? 12.157  29.319 -3.482  1.00 86.83  ? 20  GLY B O   1 
ATOM   2630 N N   . TRP B 1 348 ? 11.901  30.494 -1.559  1.00 71.91  ? 21  TRP B N   1 
ATOM   2631 C CA  . TRP B 1 348 ? 12.460  29.448 -0.707  1.00 64.20  ? 21  TRP B CA  1 
ATOM   2632 C C   . TRP B 1 348 ? 11.555  28.229 -0.650  1.00 70.52  ? 21  TRP B C   1 
ATOM   2633 O O   . TRP B 1 348 ? 12.031  27.116 -0.410  1.00 71.31  ? 21  TRP B O   1 
ATOM   2634 C CB  . TRP B 1 348 ? 12.672  29.993 0.705   1.00 64.73  ? 21  TRP B CB  1 
ATOM   2635 C CG  . TRP B 1 348 ? 13.931  30.763 0.874   1.00 61.93  ? 21  TRP B CG  1 
ATOM   2636 C CD1 . TRP B 1 348 ? 14.969  30.839 -0.005  1.00 68.49  ? 21  TRP B CD1 1 
ATOM   2637 C CD2 . TRP B 1 348 ? 14.265  31.624 1.967   1.00 58.77  ? 21  TRP B CD2 1 
ATOM   2638 N NE1 . TRP B 1 348 ? 15.945  31.672 0.485   1.00 70.49  ? 21  TRP B NE1 1 
ATOM   2639 C CE2 . TRP B 1 348 ? 15.536  32.170 1.694   1.00 65.22  ? 21  TRP B CE2 1 
ATOM   2640 C CE3 . TRP B 1 348 ? 13.620  31.976 3.154   1.00 60.55  ? 21  TRP B CE3 1 
ATOM   2641 C CZ2 . TRP B 1 348 ? 16.171  33.050 2.565   1.00 63.81  ? 21  TRP B CZ2 1 
ATOM   2642 C CZ3 . TRP B 1 348 ? 14.254  32.849 4.017   1.00 64.23  ? 21  TRP B CZ3 1 
ATOM   2643 C CH2 . TRP B 1 348 ? 15.511  33.379 3.716   1.00 62.96  ? 21  TRP B CH2 1 
ATOM   2644 N N   . TYR B 1 349 ? 10.253  28.422 -0.844  1.00 74.47  ? 22  TYR B N   1 
ATOM   2645 C CA  . TYR B 1 349 ? 9.266   27.367 -0.700  1.00 78.07  ? 22  TYR B CA  1 
ATOM   2646 C C   . TYR B 1 349 ? 8.352   27.451 -1.909  1.00 80.08  ? 22  TYR B C   1 
ATOM   2647 O O   . TYR B 1 349 ? 7.927   28.548 -2.283  1.00 81.68  ? 22  TYR B O   1 
ATOM   2648 C CB  . TYR B 1 349 ? 8.452   27.554 0.585   1.00 82.16  ? 22  TYR B CB  1 
ATOM   2649 C CG  . TYR B 1 349 ? 9.300   27.773 1.816   1.00 71.90  ? 22  TYR B CG  1 
ATOM   2650 C CD1 . TYR B 1 349 ? 9.822   26.710 2.536   1.00 76.44  ? 22  TYR B CD1 1 
ATOM   2651 C CD2 . TYR B 1 349 ? 9.550   29.059 2.274   1.00 75.02  ? 22  TYR B CD2 1 
ATOM   2652 C CE1 . TYR B 1 349 ? 10.593  26.925 3.663   1.00 79.65  ? 22  TYR B CE1 1 
ATOM   2653 C CE2 . TYR B 1 349 ? 10.315  29.281 3.400   1.00 69.23  ? 22  TYR B CE2 1 
ATOM   2654 C CZ  . TYR B 1 349 ? 10.835  28.209 4.092   1.00 73.99  ? 22  TYR B CZ  1 
ATOM   2655 O OH  . TYR B 1 349 ? 11.600  28.421 5.217   1.00 70.80  ? 22  TYR B OH  1 
ATOM   2656 N N   . GLY B 1 350 ? 8.046   26.320 -2.516  1.00 78.03  ? 23  GLY B N   1 
ATOM   2657 C CA  . GLY B 1 350 ? 7.189   26.361 -3.674  1.00 84.76  ? 23  GLY B CA  1 
ATOM   2658 C C   . GLY B 1 350 ? 6.635   25.029 -4.096  1.00 89.10  ? 23  GLY B C   1 
ATOM   2659 O O   . GLY B 1 350 ? 6.590   24.073 -3.320  1.00 98.10  ? 23  GLY B O   1 
ATOM   2660 N N   . TYR B 1 351 ? 6.227   24.981 -5.362  1.00 86.15  ? 24  TYR B N   1 
ATOM   2661 C CA  . TYR B 1 351 ? 5.383   23.934 -5.904  1.00 91.05  ? 24  TYR B CA  1 
ATOM   2662 C C   . TYR B 1 351 ? 5.967   23.505 -7.241  1.00 92.24  ? 24  TYR B C   1 
ATOM   2663 O O   . TYR B 1 351 ? 6.585   24.309 -7.943  1.00 93.71  ? 24  TYR B O   1 
ATOM   2664 C CB  . TYR B 1 351 ? 3.960   24.450 -6.127  1.00 92.47  ? 24  TYR B CB  1 
ATOM   2665 C CG  . TYR B 1 351 ? 3.272   24.944 -4.877  1.00 94.20  ? 24  TYR B CG  1 
ATOM   2666 C CD1 . TYR B 1 351 ? 2.770   24.063 -3.932  1.00 98.12  ? 24  TYR B CD1 1 
ATOM   2667 C CD2 . TYR B 1 351 ? 3.132   26.309 -4.644  1.00 95.79  ? 24  TYR B CD2 1 
ATOM   2668 C CE1 . TYR B 1 351 ? 2.141   24.524 -2.790  1.00 106.82 ? 24  TYR B CE1 1 
ATOM   2669 C CE2 . TYR B 1 351 ? 2.505   26.779 -3.505  1.00 100.24 ? 24  TYR B CE2 1 
ATOM   2670 C CZ  . TYR B 1 351 ? 2.011   25.880 -2.580  1.00 104.19 ? 24  TYR B CZ  1 
ATOM   2671 O OH  . TYR B 1 351 ? 1.382   26.332 -1.441  1.00 108.10 ? 24  TYR B OH  1 
ATOM   2672 N N   . HIS B 1 352 ? 5.769   22.240 -7.599  1.00 97.32  ? 25  HIS B N   1 
ATOM   2673 C CA  . HIS B 1 352 ? 6.134   21.755 -8.927  1.00 99.56  ? 25  HIS B CA  1 
ATOM   2674 C C   . HIS B 1 352 ? 4.943   21.008 -9.507  1.00 107.90 ? 25  HIS B C   1 
ATOM   2675 O O   . HIS B 1 352 ? 4.582   19.931 -9.021  1.00 113.53 ? 25  HIS B O   1 
ATOM   2676 C CB  . HIS B 1 352 ? 7.369   20.858 -8.887  1.00 98.49  ? 25  HIS B CB  1 
ATOM   2677 C CG  . HIS B 1 352 ? 7.783   20.354 -10.234 1.00 105.89 ? 25  HIS B CG  1 
ATOM   2678 N ND1 . HIS B 1 352 ? 8.109   21.197 -11.276 1.00 113.32 ? 25  HIS B ND1 1 
ATOM   2679 C CD2 . HIS B 1 352 ? 7.920   19.095 -10.712 1.00 107.26 ? 25  HIS B CD2 1 
ATOM   2680 C CE1 . HIS B 1 352 ? 8.431   20.478 -12.336 1.00 116.24 ? 25  HIS B CE1 1 
ATOM   2681 N NE2 . HIS B 1 352 ? 8.324   19.200 -12.021 1.00 108.48 ? 25  HIS B NE2 1 
ATOM   2682 N N   . HIS B 1 353 ? 4.343   21.569 -10.548 1.00 112.64 ? 26  HIS B N   1 
ATOM   2683 C CA  . HIS B 1 353 ? 3.143   20.990 -11.132 1.00 118.49 ? 26  HIS B CA  1 
ATOM   2684 C C   . HIS B 1 353 ? 3.447   20.328 -12.470 1.00 122.11 ? 26  HIS B C   1 
ATOM   2685 O O   . HIS B 1 353 ? 4.303   20.790 -13.232 1.00 125.70 ? 26  HIS B O   1 
ATOM   2686 C CB  . HIS B 1 353 ? 2.050   22.051 -11.299 1.00 118.90 ? 26  HIS B CB  1 
ATOM   2687 C CG  . HIS B 1 353 ? 2.280   22.983 -12.447 1.00 119.25 ? 26  HIS B CG  1 
ATOM   2688 N ND1 . HIS B 1 353 ? 3.132   24.064 -12.366 1.00 113.32 ? 26  HIS B ND1 1 
ATOM   2689 C CD2 . HIS B 1 353 ? 1.759   23.007 -13.697 1.00 122.65 ? 26  HIS B CD2 1 
ATOM   2690 C CE1 . HIS B 1 353 ? 3.132   24.708 -13.520 1.00 117.58 ? 26  HIS B CE1 1 
ATOM   2691 N NE2 . HIS B 1 353 ? 2.308   24.087 -14.344 1.00 117.92 ? 26  HIS B NE2 1 
ATOM   2692 N N   . GLN B 1 354 ? 2.739   19.220 -12.733 1.00 123.35 ? 27  GLN B N   1 
ATOM   2693 C CA  . GLN B 1 354 ? 2.762   18.519 -14.023 1.00 130.61 ? 27  GLN B CA  1 
ATOM   2694 C C   . GLN B 1 354 ? 1.315   18.222 -14.413 1.00 132.92 ? 27  GLN B C   1 
ATOM   2695 O O   . GLN B 1 354 ? 0.755   17.202 -14.007 1.00 136.24 ? 27  GLN B O   1 
ATOM   2696 C CB  . GLN B 1 354 ? 3.579   17.235 -13.966 1.00 139.11 ? 27  GLN B CB  1 
ATOM   2697 C CG  . GLN B 1 354 ? 5.078   17.399 -13.938 1.00 140.91 ? 27  GLN B CG  1 
ATOM   2698 C CD  . GLN B 1 354 ? 5.788   16.057 -13.985 1.00 146.49 ? 27  GLN B CD  1 
ATOM   2699 O OE1 . GLN B 1 354 ? 5.145   15.008 -14.043 1.00 151.08 ? 27  GLN B OE1 1 
ATOM   2700 N NE2 . GLN B 1 354 ? 7.115   16.083 -13.969 1.00 146.46 ? 27  GLN B NE2 1 
ATOM   2701 N N   . ASN B 1 355 ? 0.720   19.095 -15.213 1.00 130.58 ? 28  ASN B N   1 
ATOM   2702 C CA  . ASN B 1 355 ? -0.613  18.839 -15.733 1.00 134.43 ? 28  ASN B CA  1 
ATOM   2703 C C   . ASN B 1 355 ? -0.548  18.757 -17.256 1.00 140.03 ? 28  ASN B C   1 
ATOM   2704 O O   . ASN B 1 355 ? 0.532   18.789 -17.855 1.00 135.23 ? 28  ASN B O   1 
ATOM   2705 C CB  . ASN B 1 355 ? -1.595  19.909 -15.256 1.00 137.09 ? 28  ASN B CB  1 
ATOM   2706 C CG  . ASN B 1 355 ? -1.303  21.275 -15.836 1.00 138.82 ? 28  ASN B CG  1 
ATOM   2707 O OD1 . ASN B 1 355 ? -0.203  21.539 -16.316 1.00 134.40 ? 28  ASN B OD1 1 
ATOM   2708 N ND2 . ASN B 1 355 ? -2.299  22.154 -15.801 1.00 144.12 ? 28  ASN B ND2 1 
ATOM   2709 N N   . GLU B 1 356 ? -1.721  18.648 -17.881 1.00 144.93 ? 29  GLU B N   1 
ATOM   2710 C CA  . GLU B 1 356 ? -1.780  18.620 -19.340 1.00 152.86 ? 29  GLU B CA  1 
ATOM   2711 C C   . GLU B 1 356 ? -1.150  19.868 -19.941 1.00 148.71 ? 29  GLU B C   1 
ATOM   2712 O O   . GLU B 1 356 ? -0.453  19.794 -20.961 1.00 156.58 ? 29  GLU B O   1 
ATOM   2713 C CB  . GLU B 1 356 ? -3.228  18.492 -19.803 1.00 160.46 ? 29  GLU B CB  1 
ATOM   2714 C CG  . GLU B 1 356 ? -3.841  17.133 -19.558 1.00 169.82 ? 29  GLU B CG  1 
ATOM   2715 C CD  . GLU B 1 356 ? -5.064  16.898 -20.413 1.00 190.11 ? 29  GLU B CD  1 
ATOM   2716 O OE1 . GLU B 1 356 ? -5.301  17.697 -21.345 1.00 189.59 ? 29  GLU B OE1 1 
ATOM   2717 O OE2 . GLU B 1 356 ? -5.796  15.924 -20.146 1.00 209.65 ? 29  GLU B OE2 1 
ATOM   2718 N N   . GLN B 1 357 ? -1.380  21.024 -19.314 1.00 142.36 ? 30  GLN B N   1 
ATOM   2719 C CA  . GLN B 1 357 ? -0.893  22.288 -19.860 1.00 142.66 ? 30  GLN B CA  1 
ATOM   2720 C C   . GLN B 1 357 ? 0.631   22.330 -19.896 1.00 146.24 ? 30  GLN B C   1 
ATOM   2721 O O   . GLN B 1 357 ? 1.233   22.713 -20.910 1.00 145.60 ? 30  GLN B O   1 
ATOM   2722 C CB  . GLN B 1 357 ? -1.459  23.451 -19.043 1.00 148.39 ? 30  GLN B CB  1 
ATOM   2723 C CG  . GLN B 1 357 ? -2.979  23.577 -19.154 1.00 145.51 ? 30  GLN B CG  1 
ATOM   2724 C CD  . GLN B 1 357 ? -3.550  24.634 -18.233 1.00 147.75 ? 30  GLN B CD  1 
ATOM   2725 O OE1 . GLN B 1 357 ? -2.911  25.027 -17.264 1.00 148.52 ? 30  GLN B OE1 1 
ATOM   2726 N NE2 . GLN B 1 357 ? -4.749  25.114 -18.543 1.00 146.89 ? 30  GLN B NE2 1 
ATOM   2727 N N   . GLY B 1 358 ? 1.273   21.930 -18.807 1.00 142.38 ? 31  GLY B N   1 
ATOM   2728 C CA  . GLY B 1 358 ? 2.720   21.916 -18.781 1.00 134.65 ? 31  GLY B CA  1 
ATOM   2729 C C   . GLY B 1 358 ? 3.242   21.432 -17.450 1.00 131.26 ? 31  GLY B C   1 
ATOM   2730 O O   . GLY B 1 358 ? 2.540   20.760 -16.691 1.00 132.71 ? 31  GLY B O   1 
ATOM   2731 N N   . SER B 1 359 ? 4.497   21.776 -17.182 1.00 129.47 ? 32  SER B N   1 
ATOM   2732 C CA  . SER B 1 359 ? 5.156   21.437 -15.933 1.00 130.67 ? 32  SER B CA  1 
ATOM   2733 C C   . SER B 1 359 ? 5.997   22.626 -15.501 1.00 126.81 ? 32  SER B C   1 
ATOM   2734 O O   . SER B 1 359 ? 6.781   23.159 -16.292 1.00 127.28 ? 32  SER B O   1 
ATOM   2735 C CB  . SER B 1 359 ? 6.033   20.198 -16.096 1.00 133.67 ? 32  SER B CB  1 
ATOM   2736 O OG  . SER B 1 359 ? 7.161   20.492 -16.897 1.00 168.13 ? 32  SER B OG  1 
ATOM   2737 N N   . GLY B 1 360 ? 5.840   23.027 -14.246 1.00 119.64 ? 33  GLY B N   1 
ATOM   2738 C CA  . GLY B 1 360 ? 6.512   24.217 -13.764 1.00 112.97 ? 33  GLY B CA  1 
ATOM   2739 C C   . GLY B 1 360 ? 6.862   24.280 -12.292 1.00 106.08 ? 33  GLY B C   1 
ATOM   2740 O O   . GLY B 1 360 ? 6.135   23.766 -11.430 1.00 107.62 ? 33  GLY B O   1 
ATOM   2741 N N   . TYR B 1 361 ? 8.006   24.912 -12.020 1.00 108.24 ? 34  TYR B N   1 
ATOM   2742 C CA  . TYR B 1 361 ? 8.389   25.325 -10.678 1.00 103.82 ? 34  TYR B CA  1 
ATOM   2743 C C   . TYR B 1 361 ? 7.786   26.699 -10.407 1.00 105.57 ? 34  TYR B C   1 
ATOM   2744 O O   . TYR B 1 361 ? 7.965   27.627 -11.202 1.00 115.14 ? 34  TYR B O   1 
ATOM   2745 C CB  . TYR B 1 361 ? 9.914   25.394 -10.557 1.00 100.68 ? 34  TYR B CB  1 
ATOM   2746 C CG  . TYR B 1 361 ? 10.643  24.075 -10.701 1.00 102.38 ? 34  TYR B CG  1 
ATOM   2747 C CD1 . TYR B 1 361 ? 10.731  23.181 -9.642  1.00 108.66 ? 34  TYR B CD1 1 
ATOM   2748 C CD2 . TYR B 1 361 ? 11.259  23.733 -11.898 1.00 113.05 ? 34  TYR B CD2 1 
ATOM   2749 C CE1 . TYR B 1 361 ? 11.406  21.977 -9.774  1.00 111.98 ? 34  TYR B CE1 1 
ATOM   2750 C CE2 . TYR B 1 361 ? 11.933  22.534 -12.040 1.00 120.77 ? 34  TYR B CE2 1 
ATOM   2751 C CZ  . TYR B 1 361 ? 12.005  21.659 -10.977 1.00 120.49 ? 34  TYR B CZ  1 
ATOM   2752 O OH  . TYR B 1 361 ? 12.678  20.466 -11.124 1.00 132.09 ? 34  TYR B OH  1 
ATOM   2753 N N   . ALA B 1 362 ? 7.074   26.836 -9.291  1.00 95.98  ? 35  ALA B N   1 
ATOM   2754 C CA  . ALA B 1 362 ? 6.378   28.079 -8.973  1.00 96.68  ? 35  ALA B CA  1 
ATOM   2755 C C   . ALA B 1 362 ? 6.478   28.335 -7.478  1.00 94.83  ? 35  ALA B C   1 
ATOM   2756 O O   . ALA B 1 362 ? 6.060   27.496 -6.680  1.00 101.19 ? 35  ALA B O   1 
ATOM   2757 C CB  . ALA B 1 362 ? 4.910   28.011 -9.406  1.00 100.65 ? 35  ALA B CB  1 
ATOM   2758 N N   . ALA B 1 363 ? 7.008   29.489 -7.089  1.00 92.30  ? 36  ALA B N   1 
ATOM   2759 C CA  . ALA B 1 363 ? 7.180   29.727 -5.665  1.00 89.05  ? 36  ALA B CA  1 
ATOM   2760 C C   . ALA B 1 363 ? 5.885   30.205 -5.022  1.00 93.20  ? 36  ALA B C   1 
ATOM   2761 O O   . ALA B 1 363 ? 4.890   30.501 -5.685  1.00 91.08  ? 36  ALA B O   1 
ATOM   2762 C CB  . ALA B 1 363 ? 8.265   30.757 -5.401  1.00 84.31  ? 36  ALA B CB  1 
ATOM   2763 N N   . ASP B 1 364 ? 5.921   30.287 -3.699  1.00 92.73  ? 37  ASP B N   1 
ATOM   2764 C CA  . ASP B 1 364 ? 4.837   30.829 -2.887  1.00 94.15  ? 37  ASP B CA  1 
ATOM   2765 C C   . ASP B 1 364 ? 5.410   32.066 -2.198  1.00 94.53  ? 37  ASP B C   1 
ATOM   2766 O O   . ASP B 1 364 ? 6.120   31.953 -1.193  1.00 88.98  ? 37  ASP B O   1 
ATOM   2767 C CB  . ASP B 1 364 ? 4.329   29.797 -1.882  1.00 86.13  ? 37  ASP B CB  1 
ATOM   2768 C CG  . ASP B 1 364 ? 3.127   30.284 -1.101  1.00 90.39  ? 37  ASP B CG  1 
ATOM   2769 O OD1 . ASP B 1 364 ? 2.266   30.959 -1.701  1.00 104.99 ? 37  ASP B OD1 1 
ATOM   2770 O OD2 . ASP B 1 364 ? 3.042   29.989 0.108   1.00 91.43  ? 37  ASP B OD2 1 
ATOM   2771 N N   . LEU B 1 365 ? 5.118   33.247 -2.753  1.00 97.46  ? 38  LEU B N   1 
ATOM   2772 C CA  . LEU B 1 365 ? 5.739   34.478 -2.266  1.00 94.54  ? 38  LEU B CA  1 
ATOM   2773 C C   . LEU B 1 365 ? 5.426   34.732 -0.797  1.00 95.07  ? 38  LEU B C   1 
ATOM   2774 O O   . LEU B 1 365 ? 6.277   35.233 -0.055  1.00 97.15  ? 38  LEU B O   1 
ATOM   2775 C CB  . LEU B 1 365 ? 5.294   35.674 -3.110  1.00 99.89  ? 38  LEU B CB  1 
ATOM   2776 C CG  . LEU B 1 365 ? 6.067   35.983 -4.393  1.00 115.76 ? 38  LEU B CG  1 
ATOM   2777 C CD1 . LEU B 1 365 ? 5.667   37.358 -4.909  1.00 111.56 ? 38  LEU B CD1 1 
ATOM   2778 C CD2 . LEU B 1 365 ? 7.570   35.912 -4.159  1.00 119.81 ? 38  LEU B CD2 1 
ATOM   2779 N N   . LYS B 1 366 ? 4.212   34.394 -0.358  1.00 95.14  ? 39  LYS B N   1 
ATOM   2780 C CA  . LYS B 1 366 ? 3.798   34.696 1.010   1.00 94.22  ? 39  LYS B CA  1 
ATOM   2781 C C   . LYS B 1 366 ? 4.698   34.002 2.030   1.00 83.18  ? 39  LYS B C   1 
ATOM   2782 O O   . LYS B 1 366 ? 5.227   34.638 2.955   1.00 77.54  ? 39  LYS B O   1 
ATOM   2783 C CB  . LYS B 1 366 ? 2.338   34.280 1.195   1.00 105.58 ? 39  LYS B CB  1 
ATOM   2784 C CG  . LYS B 1 366 ? 1.353   35.107 0.370   1.00 118.69 ? 39  LYS B CG  1 
ATOM   2785 C CD  . LYS B 1 366 ? -0.051  34.530 0.457   1.00 135.08 ? 39  LYS B CD  1 
ATOM   2786 C CE  . LYS B 1 366 ? -1.045  35.353 -0.347  1.00 144.95 ? 39  LYS B CE  1 
ATOM   2787 N NZ  . LYS B 1 366 ? -2.420  34.786 -0.263  1.00 152.16 ? 39  LYS B NZ  1 
ATOM   2788 N N   . SER B 1 367 ? 4.881   32.690 1.870   1.00 85.61  ? 40  SER B N   1 
ATOM   2789 C CA  . SER B 1 367 ? 5.670   31.912 2.821   1.00 90.51  ? 40  SER B CA  1 
ATOM   2790 C C   . SER B 1 367 ? 7.114   32.402 2.885   1.00 88.09  ? 40  SER B C   1 
ATOM   2791 O O   . SER B 1 367 ? 7.658   32.630 3.973   1.00 87.00  ? 40  SER B O   1 
ATOM   2792 C CB  . SER B 1 367 ? 5.625   30.435 2.437   1.00 90.07  ? 40  SER B CB  1 
ATOM   2793 O OG  . SER B 1 367 ? 5.742   30.282 1.032   1.00 90.25  ? 40  SER B OG  1 
ATOM   2794 N N   . THR B 1 368 ? 7.757   32.560 1.726   1.00 79.65  ? 41  THR B N   1 
ATOM   2795 C CA  . THR B 1 368 ? 9.151   32.992 1.715   1.00 73.64  ? 41  THR B CA  1 
ATOM   2796 C C   . THR B 1 368 ? 9.302   34.427 2.213   1.00 77.26  ? 41  THR B C   1 
ATOM   2797 O O   . THR B 1 368 ? 10.304  34.750 2.860   1.00 81.43  ? 41  THR B O   1 
ATOM   2798 C CB  . THR B 1 368 ? 9.744   32.830 0.314   1.00 65.76  ? 41  THR B CB  1 
ATOM   2799 O OG1 . THR B 1 368 ? 9.385   33.947 -0.502  1.00 75.44  ? 41  THR B OG1 1 
ATOM   2800 C CG2 . THR B 1 368 ? 9.234   31.547 -0.324  1.00 71.13  ? 41  THR B CG2 1 
ATOM   2801 N N   . GLN B 1 369 ? 8.319   35.292 1.944   1.00 79.47  ? 42  GLN B N   1 
ATOM   2802 C CA  . GLN B 1 369 ? 8.358   36.657 2.460   1.00 78.79  ? 42  GLN B CA  1 
ATOM   2803 C C   . GLN B 1 369 ? 8.308   36.668 3.981   1.00 79.21  ? 42  GLN B C   1 
ATOM   2804 O O   . GLN B 1 369 ? 9.086   37.375 4.634   1.00 82.75  ? 42  GLN B O   1 
ATOM   2805 C CB  . GLN B 1 369 ? 7.197   37.472 1.891   1.00 86.74  ? 42  GLN B CB  1 
ATOM   2806 C CG  . GLN B 1 369 ? 7.475   38.106 0.548   1.00 92.86  ? 42  GLN B CG  1 
ATOM   2807 C CD  . GLN B 1 369 ? 6.217   38.631 -0.108  1.00 91.99  ? 42  GLN B CD  1 
ATOM   2808 O OE1 . GLN B 1 369 ? 5.123   38.108 0.118   1.00 93.42  ? 42  GLN B OE1 1 
ATOM   2809 N NE2 . GLN B 1 369 ? 6.362   39.657 -0.933  1.00 93.93  ? 42  GLN B NE2 1 
ATOM   2810 N N   . ASN B 1 370 ? 7.384   35.894 4.563   1.00 80.18  ? 43  ASN B N   1 
ATOM   2811 C CA  . ASN B 1 370 ? 7.307   35.824 6.021   1.00 77.41  ? 43  ASN B CA  1 
ATOM   2812 C C   . ASN B 1 370 ? 8.559   35.190 6.608   1.00 76.34  ? 43  ASN B C   1 
ATOM   2813 O O   . ASN B 1 370 ? 9.014   35.583 7.690   1.00 74.80  ? 43  ASN B O   1 
ATOM   2814 C CB  . ASN B 1 370 ? 6.064   35.052 6.460   1.00 73.11  ? 43  ASN B CB  1 
ATOM   2815 C CG  . ASN B 1 370 ? 4.780   35.694 5.983   1.00 76.84  ? 43  ASN B CG  1 
ATOM   2816 O OD1 . ASN B 1 370 ? 4.591   36.904 6.122   1.00 76.38  ? 43  ASN B OD1 1 
ATOM   2817 N ND2 . ASN B 1 370 ? 3.889   34.890 5.414   1.00 90.01  ? 43  ASN B ND2 1 
ATOM   2818 N N   . ALA B 1 371 ? 9.140   34.217 5.900   1.00 76.49  ? 44  ALA B N   1 
ATOM   2819 C CA  . ALA B 1 371 ? 10.389  33.615 6.351   1.00 72.29  ? 44  ALA B CA  1 
ATOM   2820 C C   . ALA B 1 371 ? 11.509  34.648 6.393   1.00 68.05  ? 44  ALA B C   1 
ATOM   2821 O O   . ALA B 1 371 ? 12.257  34.733 7.375   1.00 77.75  ? 44  ALA B O   1 
ATOM   2822 C CB  . ALA B 1 371 ? 10.765  32.443 5.442   1.00 73.49  ? 44  ALA B CB  1 
ATOM   2823 N N   . ILE B 1 372 ? 11.643  35.443 5.328   1.00 63.77  ? 45  ILE B N   1 
ATOM   2824 C CA  . ILE B 1 372 ? 12.698  36.451 5.295   1.00 63.21  ? 45  ILE B CA  1 
ATOM   2825 C C   . ILE B 1 372 ? 12.460  37.510 6.363   1.00 69.29  ? 45  ILE B C   1 
ATOM   2826 O O   . ILE B 1 372 ? 13.404  37.978 7.009   1.00 72.53  ? 45  ILE B O   1 
ATOM   2827 C CB  . ILE B 1 372 ? 12.827  37.077 3.893   1.00 70.81  ? 45  ILE B CB  1 
ATOM   2828 C CG1 . ILE B 1 372 ? 13.236  36.015 2.869   1.00 71.04  ? 45  ILE B CG1 1 
ATOM   2829 C CG2 . ILE B 1 372 ? 13.829  38.214 3.914   1.00 75.40  ? 45  ILE B CG2 1 
ATOM   2830 C CD1 . ILE B 1 372 ? 12.835  36.337 1.446   1.00 64.18  ? 45  ILE B CD1 1 
ATOM   2831 N N   . ASP B 1 373 ? 11.201  37.896 6.577   1.00 77.94  ? 46  ASP B N   1 
ATOM   2832 C CA  . ASP B 1 373 ? 10.904  38.872 7.622   1.00 78.63  ? 46  ASP B CA  1 
ATOM   2833 C C   . ASP B 1 373 ? 11.322  38.340 8.992   1.00 79.46  ? 46  ASP B C   1 
ATOM   2834 O O   . ASP B 1 373 ? 12.042  39.014 9.751   1.00 84.00  ? 46  ASP B O   1 
ATOM   2835 C CB  . ASP B 1 373 ? 9.414   39.221 7.593   1.00 86.77  ? 46  ASP B CB  1 
ATOM   2836 C CG  . ASP B 1 373 ? 9.073   40.230 6.502   1.00 91.55  ? 46  ASP B CG  1 
ATOM   2837 O OD1 . ASP B 1 373 ? 9.928   41.091 6.188   1.00 85.12  ? 46  ASP B OD1 1 
ATOM   2838 O OD2 . ASP B 1 373 ? 7.959   40.150 5.940   1.00 94.71  ? 46  ASP B OD2 1 
ATOM   2839 N N   . GLY B 1 374 ? 10.917  37.105 9.303   1.00 78.97  ? 47  GLY B N   1 
ATOM   2840 C CA  . GLY B 1 374 ? 11.236  36.533 10.601  1.00 78.82  ? 47  GLY B CA  1 
ATOM   2841 C C   . GLY B 1 374 ? 12.724  36.339 10.821  1.00 71.69  ? 47  GLY B C   1 
ATOM   2842 O O   . GLY B 1 374 ? 13.231  36.567 11.921  1.00 76.00  ? 47  GLY B O   1 
ATOM   2843 N N   . ILE B 1 375 ? 13.449  35.922 9.780   1.00 66.99  ? 48  ILE B N   1 
ATOM   2844 C CA  . ILE B 1 375 ? 14.885  35.719 9.953   1.00 67.21  ? 48  ILE B CA  1 
ATOM   2845 C C   . ILE B 1 375 ? 15.627  37.054 10.015  1.00 72.45  ? 48  ILE B C   1 
ATOM   2846 O O   . ILE B 1 375 ? 16.628  37.174 10.732  1.00 74.96  ? 48  ILE B O   1 
ATOM   2847 C CB  . ILE B 1 375 ? 15.436  34.787 8.856   1.00 58.98  ? 48  ILE B CB  1 
ATOM   2848 C CG1 . ILE B 1 375 ? 14.802  33.405 8.983   1.00 59.91  ? 48  ILE B CG1 1 
ATOM   2849 C CG2 . ILE B 1 375 ? 16.934  34.626 8.970   1.00 64.35  ? 48  ILE B CG2 1 
ATOM   2850 C CD1 . ILE B 1 375 ? 15.210  32.462 7.890   1.00 65.45  ? 48  ILE B CD1 1 
ATOM   2851 N N   . THR B 1 376 ? 15.163  38.080 9.292   1.00 71.99  ? 49  THR B N   1 
ATOM   2852 C CA  . THR B 1 376 ? 15.712  39.420 9.493   1.00 71.71  ? 49  THR B CA  1 
ATOM   2853 C C   . THR B 1 376 ? 15.607  39.824 10.959  1.00 79.82  ? 49  THR B C   1 
ATOM   2854 O O   . THR B 1 376 ? 16.594  40.249 11.581  1.00 87.89  ? 49  THR B O   1 
ATOM   2855 C CB  . THR B 1 376 ? 14.978  40.446 8.624   1.00 79.11  ? 49  THR B CB  1 
ATOM   2856 O OG1 . THR B 1 376 ? 13.591  40.114 8.564   1.00 85.18  ? 49  THR B OG1 1 
ATOM   2857 C CG2 . THR B 1 376 ? 15.527  40.494 7.217   1.00 74.50  ? 49  THR B CG2 1 
ATOM   2858 N N   . ASN B 1 377 ? 14.407  39.676 11.534  1.00 85.31  ? 50  ASN B N   1 
ATOM   2859 C CA  . ASN B 1 377 ? 14.219  40.056 12.933  1.00 86.59  ? 50  ASN B CA  1 
ATOM   2860 C C   . ASN B 1 377 ? 15.064  39.198 13.865  1.00 91.39  ? 50  ASN B C   1 
ATOM   2861 O O   . ASN B 1 377 ? 15.649  39.713 14.827  1.00 93.46  ? 50  ASN B O   1 
ATOM   2862 C CB  . ASN B 1 377 ? 12.745  39.980 13.318  1.00 91.32  ? 50  ASN B CB  1 
ATOM   2863 C CG  . ASN B 1 377 ? 11.897  40.918 12.505  1.00 101.91 ? 50  ASN B CG  1 
ATOM   2864 O OD1 . ASN B 1 377 ? 12.166  42.119 12.450  1.00 105.63 ? 50  ASN B OD1 1 
ATOM   2865 N ND2 . ASN B 1 377 ? 10.862  40.385 11.870  1.00 99.44  ? 50  ASN B ND2 1 
ATOM   2866 N N   . LYS B 1 378 ? 15.154  37.900 13.555  1.00 83.39  ? 51  LYS B N   1 
ATOM   2867 C CA  . LYS B 1 378 ? 16.025  37.000 14.355  1.00 80.55  ? 51  LYS B CA  1 
ATOM   2868 C C   . LYS B 1 378 ? 17.453  37.549 14.318  1.00 82.48  ? 51  LYS B C   1 
ATOM   2869 O O   . LYS B 1 378 ? 18.027  37.756 15.398  1.00 86.65  ? 51  LYS B O   1 
ATOM   2870 C CB  . LYS B 1 378 ? 16.008  35.578 13.790  1.00 78.40  ? 51  LYS B CB  1 
ATOM   2871 C CG  . LYS B 1 378 ? 14.741  34.774 14.046  1.00 105.32 ? 51  LYS B CG  1 
ATOM   2872 C CD  . LYS B 1 378 ? 14.821  33.370 13.487  1.00 100.46 ? 51  LYS B CD  1 
ATOM   2873 C CE  . LYS B 1 378 ? 13.598  32.530 13.788  1.00 87.23  ? 51  LYS B CE  1 
ATOM   2874 N NZ  . LYS B 1 378 ? 13.787  31.123 13.363  1.00 81.24  ? 51  LYS B NZ  1 
ATOM   2875 N N   . VAL B 1 379 ? 17.986  37.796 13.117  1.00 75.02  ? 52  VAL B N   1 
ATOM   2876 C CA  . VAL B 1 379 ? 19.395  38.272 12.983  1.00 72.76  ? 52  VAL B CA  1 
ATOM   2877 C C   . VAL B 1 379 ? 19.581  39.523 13.850  1.00 80.99  ? 52  VAL B C   1 
ATOM   2878 O O   . VAL B 1 379 ? 20.587  39.587 14.579  1.00 94.50  ? 52  VAL B O   1 
ATOM   2879 C CB  . VAL B 1 379 ? 19.762  38.545 11.511  1.00 71.34  ? 52  VAL B CB  1 
ATOM   2880 C CG1 . VAL B 1 379 ? 21.065  39.320 11.384  1.00 82.65  ? 52  VAL B CG1 1 
ATOM   2881 C CG2 . VAL B 1 379 ? 19.824  37.260 10.699  1.00 71.51  ? 52  VAL B CG2 1 
ATOM   2882 N N   . ASN B 1 380 ? 18.635  40.464 13.786  1.00 83.51  ? 53  ASN B N   1 
ATOM   2883 C CA  . ASN B 1 380 ? 18.750  41.723 14.570  1.00 87.76  ? 53  ASN B CA  1 
ATOM   2884 C C   . ASN B 1 380 ? 18.854  41.377 16.059  1.00 95.09  ? 53  ASN B C   1 
ATOM   2885 O O   . ASN B 1 380 ? 19.737  41.940 16.735  1.00 100.24 ? 53  ASN B O   1 
ATOM   2886 C CB  . ASN B 1 380 ? 17.581  42.673 14.300  1.00 94.96  ? 53  ASN B CB  1 
ATOM   2887 C CG  . ASN B 1 380 ? 17.476  43.076 12.845  1.00 99.26  ? 53  ASN B CG  1 
ATOM   2888 O OD1 . ASN B 1 380 ? 18.424  43.613 12.275  1.00 97.91  ? 53  ASN B OD1 1 
ATOM   2889 N ND2 . ASN B 1 380 ? 16.332  42.815 12.234  1.00 103.75 ? 53  ASN B ND2 1 
ATOM   2890 N N   . SER B 1 381 ? 17.992  40.476 16.541  1.00 87.23  ? 54  SER B N   1 
ATOM   2891 C CA  . SER B 1 381 ? 18.020  40.066 17.969  1.00 95.74  ? 54  SER B CA  1 
ATOM   2892 C C   . SER B 1 381 ? 19.361  39.395 18.289  1.00 99.39  ? 54  SER B C   1 
ATOM   2893 O O   . SER B 1 381 ? 19.899  39.648 19.383  1.00 95.00  ? 54  SER B O   1 
ATOM   2894 C CB  . SER B 1 381 ? 16.861  39.162 18.299  1.00 98.19  ? 54  SER B CB  1 
ATOM   2895 O OG  . SER B 1 381 ? 17.007  37.901 17.664  1.00 118.95 ? 54  SER B OG  1 
ATOM   2896 N N   . VAL B 1 382 ? 19.875  38.575 17.367  1.00 98.17  ? 55  VAL B N   1 
ATOM   2897 C CA  . VAL B 1 382 ? 21.203  37.926 17.578  1.00 91.49  ? 55  VAL B CA  1 
ATOM   2898 C C   . VAL B 1 382 ? 22.241  39.032 17.783  1.00 95.01  ? 55  VAL B C   1 
ATOM   2899 O O   . VAL B 1 382 ? 22.958  38.982 18.796  1.00 94.90  ? 55  VAL B O   1 
ATOM   2900 C CB  . VAL B 1 382 ? 21.602  37.030 16.390  1.00 93.20  ? 55  VAL B CB  1 
ATOM   2901 C CG1 . VAL B 1 382 ? 22.858  36.228 16.690  1.00 98.19  ? 55  VAL B CG1 1 
ATOM   2902 C CG2 . VAL B 1 382 ? 20.473  36.111 15.956  1.00 88.70  ? 55  VAL B CG2 1 
ATOM   2903 N N   . ILE B 1 383 ? 22.292  40.000 16.865  1.00 91.30  ? 56  ILE B N   1 
ATOM   2904 C CA  . ILE B 1 383 ? 23.316  41.087 16.916  1.00 87.61  ? 56  ILE B CA  1 
ATOM   2905 C C   . ILE B 1 383 ? 23.261  41.765 18.324  1.00 99.13  ? 56  ILE B C   1 
ATOM   2906 O O   . ILE B 1 383 ? 24.261  42.414 18.690  1.00 100.68 ? 56  ILE B O   1 
ATOM   2907 C CB  . ILE B 1 383 ? 23.047  42.148 15.852  1.00 87.80  ? 56  ILE B CB  1 
ATOM   2908 C CG1 . ILE B 1 383 ? 23.039  41.521 14.456  1.00 84.28  ? 56  ILE B CG1 1 
ATOM   2909 C CG2 . ILE B 1 383 ? 24.045  43.293 15.943  1.00 98.73  ? 56  ILE B CG2 1 
ATOM   2910 C CD1 . ILE B 1 383 ? 22.684  42.488 13.352  1.00 90.70  ? 56  ILE B CD1 1 
ATOM   2911 N N   . GLU B 1 384 ? 22.167  41.547 19.059  1.00 99.85  ? 57  GLU B N   1 
ATOM   2912 C CA  . GLU B 1 384 ? 22.012  42.177 20.397  1.00 104.11 ? 57  GLU B CA  1 
ATOM   2913 C C   . GLU B 1 384 ? 22.860  41.412 21.408  1.00 101.34 ? 57  GLU B C   1 
ATOM   2914 O O   . GLU B 1 384 ? 22.319  40.973 22.435  1.00 87.38  ? 57  GLU B O   1 
ATOM   2915 C CB  . GLU B 1 384 ? 20.545  42.244 20.811  1.00 103.76 ? 57  GLU B CB  1 
ATOM   2916 C CG  . GLU B 1 384 ? 19.751  43.218 19.966  1.00 115.55 ? 57  GLU B CG  1 
ATOM   2917 C CD  . GLU B 1 384 ? 20.501  44.509 19.688  1.00 124.86 ? 57  GLU B CD  1 
ATOM   2918 O OE1 . GLU B 1 384 ? 20.856  45.204 20.659  1.00 121.72 ? 57  GLU B OE1 1 
ATOM   2919 O OE2 . GLU B 1 384 ? 20.736  44.809 18.501  1.00 166.16 ? 57  GLU B OE2 1 
ATOM   2920 N N   . LYS B 1 385 ? 24.137  41.238 21.091  1.00 98.39  ? 58  LYS B N   1 
ATOM   2921 C CA  . LYS B 1 385 ? 25.058  40.618 22.068  1.00 100.72 ? 58  LYS B CA  1 
ATOM   2922 C C   . LYS B 1 385 ? 25.457  41.934 22.730  1.00 111.71 ? 58  LYS B C   1 
ATOM   2923 O O   . LYS B 1 385 ? 25.698  42.911 22.003  1.00 103.48 ? 58  LYS B O   1 
ATOM   2924 C CB  . LYS B 1 385 ? 26.088  39.746 21.351  1.00 88.88  ? 58  LYS B CB  1 
ATOM   2925 C CG  . LYS B 1 385 ? 25.509  38.610 20.521  1.00 82.90  ? 58  LYS B CG  1 
ATOM   2926 C CD  . LYS B 1 385 ? 26.535  37.926 19.651  1.00 67.77  ? 58  LYS B CD  1 
ATOM   2927 C CE  . LYS B 1 385 ? 25.925  36.902 18.719  1.00 62.84  ? 58  LYS B CE  1 
ATOM   2928 N NZ  . LYS B 1 385 ? 26.924  36.372 17.763  1.00 56.28  ? 58  LYS B NZ  1 
ATOM   2929 N N   . MET B 1 386 ? 25.522  41.953 24.065  1.00 108.03 ? 59  MET B N   1 
ATOM   2930 C CA  . MET B 1 386 ? 25.861  43.198 24.807  1.00 110.22 ? 59  MET B CA  1 
ATOM   2931 C C   . MET B 1 386 ? 27.341  42.925 25.095  1.00 128.96 ? 59  MET B C   1 
ATOM   2932 O O   . MET B 1 386 ? 27.635  42.300 26.134  1.00 119.57 ? 59  MET B O   1 
ATOM   2933 C CB  . MET B 1 386 ? 25.103  43.388 26.124  1.00 109.39 ? 59  MET B CB  1 
ATOM   2934 C CG  . MET B 1 386 ? 23.603  43.550 25.949  1.00 110.02 ? 59  MET B CG  1 
ATOM   2935 S SD  . MET B 1 386 ? 23.142  45.027 25.005  1.00 140.12 ? 59  MET B SD  1 
ATOM   2936 C CE  . MET B 1 386 ? 22.745  44.300 23.415  1.00 106.83 ? 59  MET B CE  1 
ATOM   2937 N N   . ASN B 1 387 ? 28.233  43.375 24.208  1.00 143.51 ? 60  ASN B N   1 
ATOM   2938 C CA  . ASN B 1 387 ? 29.694  43.199 24.425  1.00 147.52 ? 60  ASN B CA  1 
ATOM   2939 C C   . ASN B 1 387 ? 30.310  44.575 24.701  1.00 165.08 ? 60  ASN B C   1 
ATOM   2940 O O   . ASN B 1 387 ? 31.548  44.696 24.610  1.00 166.67 ? 60  ASN B O   1 
ATOM   2941 C CB  . ASN B 1 387 ? 30.356  42.487 23.243  1.00 134.07 ? 60  ASN B CB  1 
ATOM   2942 C CG  . ASN B 1 387 ? 29.854  41.070 23.066  1.00 130.30 ? 60  ASN B CG  1 
ATOM   2943 O OD1 . ASN B 1 387 ? 29.299  40.727 22.024  1.00 120.60 ? 60  ASN B OD1 1 
ATOM   2944 N ND2 . ASN B 1 387 ? 30.037  40.241 24.081  1.00 134.87 ? 60  ASN B ND2 1 
ATOM   2945 N N   . THR B 1 388 ? 29.474  45.565 25.030  1.00 159.09 ? 61  THR B N   1 
ATOM   2946 C CA  . THR B 1 388 ? 29.967  46.936 25.332  1.00 167.64 ? 61  THR B CA  1 
ATOM   2947 C C   . THR B 1 388 ? 30.681  46.927 26.689  1.00 184.77 ? 61  THR B C   1 
ATOM   2948 O O   . THR B 1 388 ? 31.415  47.893 26.974  1.00 218.76 ? 61  THR B O   1 
ATOM   2949 C CB  . THR B 1 388 ? 28.811  47.944 25.299  1.00 163.63 ? 61  THR B CB  1 
ATOM   2950 O OG1 . THR B 1 388 ? 28.023  47.670 24.139  1.00 156.52 ? 61  THR B OG1 1 
ATOM   2951 C CG2 . THR B 1 388 ? 29.273  49.384 25.274  1.00 166.72 ? 61  THR B CG2 1 
ATOM   2952 N N   . GLN B 1 389 ? 30.482  45.870 27.483  1.00 150.28 ? 62  GLN B N   1 
ATOM   2953 C CA  . GLN B 1 389 ? 31.102  45.779 28.833  1.00 163.26 ? 62  GLN B CA  1 
ATOM   2954 C C   . GLN B 1 389 ? 32.524  46.353 28.790  1.00 169.41 ? 62  GLN B C   1 
ATOM   2955 O O   . GLN B 1 389 ? 33.375  45.774 28.086  1.00 166.51 ? 62  GLN B O   1 
ATOM   2956 C CB  . GLN B 1 389 ? 31.099  44.324 29.307  1.00 177.02 ? 62  GLN B CB  1 
ATOM   2957 C CG  . GLN B 1 389 ? 31.396  43.323 28.198  1.00 188.05 ? 62  GLN B CG  1 
ATOM   2958 C CD  . GLN B 1 389 ? 31.403  41.898 28.694  1.00 196.08 ? 62  GLN B CD  1 
ATOM   2959 O OE1 . GLN B 1 389 ? 32.409  41.197 28.610  1.00 210.48 ? 62  GLN B OE1 1 
ATOM   2960 N NE2 . GLN B 1 389 ? 30.272  41.458 29.220  1.00 185.55 ? 62  GLN B NE2 1 
ATOM   2961 N N   . PHE B 1 390 ? 32.764  47.447 29.522  1.00 197.52 ? 63  PHE B N   1 
ATOM   2962 C CA  . PHE B 1 390 ? 34.112  48.075 29.565  1.00 201.29 ? 63  PHE B CA  1 
ATOM   2963 C C   . PHE B 1 390 ? 34.218  48.974 30.801  1.00 209.80 ? 63  PHE B C   1 
ATOM   2964 O O   . PHE B 1 390 ? 33.186  49.533 31.221  1.00 208.61 ? 63  PHE B O   1 
ATOM   2965 C CB  . PHE B 1 390 ? 34.371  48.887 28.293  1.00 207.71 ? 63  PHE B CB  1 
ATOM   2966 C CG  . PHE B 1 390 ? 35.618  49.734 28.333  1.00 217.35 ? 63  PHE B CG  1 
ATOM   2967 C CD1 . PHE B 1 390 ? 36.870  49.152 28.451  1.00 218.54 ? 63  PHE B CD1 1 
ATOM   2968 C CD2 . PHE B 1 390 ? 35.538  51.116 28.274  1.00 223.38 ? 63  PHE B CD2 1 
ATOM   2969 C CE1 . PHE B 1 390 ? 38.014  49.932 28.495  1.00 222.10 ? 63  PHE B CE1 1 
ATOM   2970 C CE2 . PHE B 1 390 ? 36.683  51.895 28.318  1.00 223.76 ? 63  PHE B CE2 1 
ATOM   2971 C CZ  . PHE B 1 390 ? 37.919  51.302 28.428  1.00 223.77 ? 63  PHE B CZ  1 
ATOM   2972 N N   . THR B 1 391 ? 35.424  49.112 31.359  1.00 216.34 ? 64  THR B N   1 
ATOM   2973 C CA  . THR B 1 391 ? 35.632  50.018 32.520  1.00 218.54 ? 64  THR B CA  1 
ATOM   2974 C C   . THR B 1 391 ? 36.534  51.180 32.091  1.00 232.55 ? 64  THR B C   1 
ATOM   2975 O O   . THR B 1 391 ? 37.703  50.918 31.746  1.00 283.03 ? 64  THR B O   1 
ATOM   2976 C CB  . THR B 1 391 ? 36.225  49.262 33.715  1.00 207.18 ? 64  THR B CB  1 
ATOM   2977 O OG1 . THR B 1 391 ? 37.513  48.776 33.335  1.00 211.40 ? 64  THR B OG1 1 
ATOM   2978 C CG2 . THR B 1 391 ? 35.356  48.111 34.173  1.00 193.87 ? 64  THR B CG2 1 
ATOM   2979 N N   . ALA B 1 392 ? 36.009  52.408 32.116  1.00 229.74 ? 65  ALA B N   1 
ATOM   2980 C CA  . ALA B 1 392 ? 36.799  53.592 31.704  1.00 227.71 ? 65  ALA B CA  1 
ATOM   2981 C C   . ALA B 1 392 ? 38.021  53.731 32.618  1.00 226.60 ? 65  ALA B C   1 
ATOM   2982 O O   . ALA B 1 392 ? 39.129  53.957 32.093  1.00 250.00 ? 65  ALA B O   1 
ATOM   2983 C CB  . ALA B 1 392 ? 35.935  54.827 31.745  1.00 219.67 ? 65  ALA B CB  1 
ATOM   2984 N N   . VAL B 1 393 ? 37.881  53.356 33.901  1.00 219.99 ? 66  VAL B N   1 
ATOM   2985 C CA  . VAL B 1 393 ? 39.009  53.471 34.881  1.00 208.75 ? 66  VAL B CA  1 
ATOM   2986 C C   . VAL B 1 393 ? 39.355  52.125 35.533  1.00 210.31 ? 66  VAL B C   1 
ATOM   2987 O O   . VAL B 1 393 ? 38.477  51.245 35.545  1.00 211.49 ? 66  VAL B O   1 
ATOM   2988 C CB  . VAL B 1 393 ? 38.680  54.499 35.980  1.00 190.21 ? 66  VAL B CB  1 
ATOM   2989 C CG1 . VAL B 1 393 ? 39.834  55.459 36.222  1.00 169.92 ? 66  VAL B CG1 1 
ATOM   2990 C CG2 . VAL B 1 393 ? 37.386  55.249 35.704  1.00 187.19 ? 66  VAL B CG2 1 
ATOM   2991 N N   . ARG B 1 403 ? 50.039  43.468 42.284  1.00 191.64 ? 76  ARG B N   1 
ATOM   2992 C CA  . ARG B 1 403 ? 49.722  42.421 41.259  1.00 170.69 ? 76  ARG B CA  1 
ATOM   2993 C C   . ARG B 1 403 ? 48.418  42.782 40.503  1.00 158.95 ? 76  ARG B C   1 
ATOM   2994 O O   . ARG B 1 403 ? 47.918  41.960 39.718  1.00 156.11 ? 76  ARG B O   1 
ATOM   2995 C CB  . ARG B 1 403 ? 49.851  41.030 41.837  1.00 165.92 ? 76  ARG B CB  1 
ATOM   2996 C CG  . ARG B 1 403 ? 51.240  40.698 42.360  1.00 171.29 ? 76  ARG B CG  1 
ATOM   2997 C CD  . ARG B 1 403 ? 52.245  40.499 41.241  1.00 175.07 ? 76  ARG B CD  1 
ATOM   2998 N NE  . ARG B 1 403 ? 53.561  40.136 41.747  1.00 173.69 ? 76  ARG B NE  1 
ATOM   2999 C CZ  . ARG B 1 403 ? 54.524  41.005 42.027  1.00 173.50 ? 76  ARG B CZ  1 
ATOM   3000 N NH1 . ARG B 1 403 ? 54.280  42.302 41.981  1.00 196.44 ? 76  ARG B NH1 1 
ATOM   3001 N NH2 . ARG B 1 403 ? 55.729  40.573 42.359  1.00 165.68 ? 76  ARG B NH2 1 
ATOM   3002 N N   . ILE B 1 404 ? 47.896  43.974 40.776  1.00 160.54 ? 77  ILE B N   1 
ATOM   3003 C CA  . ILE B 1 404 ? 46.597  44.334 40.245  1.00 151.48 ? 77  ILE B CA  1 
ATOM   3004 C C   . ILE B 1 404 ? 46.581  44.341 38.712  1.00 147.42 ? 77  ILE B C   1 
ATOM   3005 O O   . ILE B 1 404 ? 45.713  43.688 38.112  1.00 138.19 ? 77  ILE B O   1 
ATOM   3006 C CB  . ILE B 1 404 ? 46.004  45.636 40.810  1.00 155.63 ? 77  ILE B CB  1 
ATOM   3007 C CG1 . ILE B 1 404 ? 45.923  45.597 42.337  1.00 163.43 ? 77  ILE B CG1 1 
ATOM   3008 C CG2 . ILE B 1 404 ? 44.661  45.973 40.185  1.00 143.09 ? 77  ILE B CG2 1 
ATOM   3009 C CD1 . ILE B 1 404 ? 45.302  46.830 42.948  1.00 175.84 ? 77  ILE B CD1 1 
ATOM   3010 N N   . GLU B 1 405 ? 47.521  45.058 38.088  1.00 165.87 ? 78  GLU B N   1 
ATOM   3011 C CA  . GLU B 1 405 ? 47.396  45.122 36.636  1.00 161.24 ? 78  GLU B CA  1 
ATOM   3012 C C   . GLU B 1 405 ? 47.356  43.724 36.037  1.00 144.36 ? 78  GLU B C   1 
ATOM   3013 O O   . GLU B 1 405 ? 46.590  43.454 35.102  1.00 138.58 ? 78  GLU B O   1 
ATOM   3014 C CB  . GLU B 1 405 ? 48.559  45.928 36.057  1.00 177.91 ? 78  GLU B CB  1 
ATOM   3015 C CG  . GLU B 1 405 ? 48.389  46.357 34.613  1.00 178.40 ? 78  GLU B CG  1 
ATOM   3016 C CD  . GLU B 1 405 ? 49.617  47.078 34.100  1.00 173.04 ? 78  GLU B CD  1 
ATOM   3017 O OE1 . GLU B 1 405 ? 50.496  47.381 34.929  1.00 177.33 ? 78  GLU B OE1 1 
ATOM   3018 O OE2 . GLU B 1 405 ? 49.721  47.319 32.880  1.00 162.85 ? 78  GLU B OE2 1 
ATOM   3019 N N   . ASN B 1 406 ? 48.149  42.809 36.600  1.00 160.89 ? 79  ASN B N   1 
ATOM   3020 C CA  . ASN B 1 406 ? 48.099  41.417 36.175  1.00 150.81 ? 79  ASN B CA  1 
ATOM   3021 C C   . ASN B 1 406 ? 46.723  40.810 36.424  1.00 144.91 ? 79  ASN B C   1 
ATOM   3022 O O   . ASN B 1 406 ? 46.236  40.025 35.607  1.00 137.49 ? 79  ASN B O   1 
ATOM   3023 C CB  . ASN B 1 406 ? 49.181  40.613 36.891  1.00 156.68 ? 79  ASN B CB  1 
ATOM   3024 C CG  . ASN B 1 406 ? 50.573  41.045 36.499  1.00 156.79 ? 79  ASN B CG  1 
ATOM   3025 O OD1 . ASN B 1 406 ? 50.745  41.956 35.690  1.00 159.31 ? 79  ASN B OD1 1 
ATOM   3026 N ND2 . ASN B 1 406 ? 51.578  40.391 37.066  1.00 156.73 ? 79  ASN B ND2 1 
ATOM   3027 N N   . LEU B 1 407 ? 46.074  41.163 37.542  1.00 155.47 ? 80  LEU B N   1 
ATOM   3028 C CA  . LEU B 1 407 ? 44.727  40.646 37.784  1.00 145.42 ? 80  LEU B CA  1 
ATOM   3029 C C   . LEU B 1 407 ? 43.719  41.204 36.789  1.00 132.02 ? 80  LEU B C   1 
ATOM   3030 O O   . LEU B 1 407 ? 42.852  40.467 36.302  1.00 121.68 ? 80  LEU B O   1 
ATOM   3031 C CB  . LEU B 1 407 ? 44.252  40.941 39.204  1.00 145.52 ? 80  LEU B CB  1 
ATOM   3032 C CG  . LEU B 1 407 ? 44.780  40.093 40.350  1.00 139.47 ? 80  LEU B CG  1 
ATOM   3033 C CD1 . LEU B 1 407 ? 44.215  40.625 41.654  1.00 150.74 ? 80  LEU B CD1 1 
ATOM   3034 C CD2 . LEU B 1 407 ? 44.359  38.657 40.125  1.00 134.94 ? 80  LEU B CD2 1 
ATOM   3035 N N   . ASN B 1 408 ? 43.790  42.506 36.498  1.00 127.32 ? 81  ASN B N   1 
ATOM   3036 C CA  . ASN B 1 408 ? 42.872  43.072 35.514  1.00 122.13 ? 81  ASN B CA  1 
ATOM   3037 C C   . ASN B 1 408 ? 43.176  42.397 34.182  1.00 118.87 ? 81  ASN B C   1 
ATOM   3038 O O   . ASN B 1 408 ? 42.261  42.096 33.408  1.00 114.26 ? 81  ASN B O   1 
ATOM   3039 C CB  . ASN B 1 408 ? 43.052  44.591 35.416  1.00 142.87 ? 81  ASN B CB  1 
ATOM   3040 C CG  . ASN B 1 408 ? 41.762  45.318 35.016  1.00 153.82 ? 81  ASN B CG  1 
ATOM   3041 O OD1 . ASN B 1 408 ? 40.789  45.352 35.771  1.00 151.44 ? 81  ASN B OD1 1 
ATOM   3042 N ND2 . ASN B 1 408 ? 41.763  45.911 33.827  1.00 157.81 ? 81  ASN B ND2 1 
ATOM   3043 N N   . LYS B 1 409 ? 44.463  42.153 33.918  1.00 129.71 ? 82  LYS B N   1 
ATOM   3044 C CA  . LYS B 1 409 ? 44.864  41.492 32.647  1.00 122.91 ? 82  LYS B CA  1 
ATOM   3045 C C   . LYS B 1 409 ? 44.205  40.111 32.573  1.00 116.61 ? 82  LYS B C   1 
ATOM   3046 O O   . LYS B 1 409 ? 43.432  39.878 31.622  1.00 110.00 ? 82  LYS B O   1 
ATOM   3047 C CB  . LYS B 1 409 ? 46.388  41.374 32.561  1.00 132.51 ? 82  LYS B CB  1 
ATOM   3048 C CG  . LYS B 1 409 ? 46.917  40.778 31.264  1.00 128.72 ? 82  LYS B CG  1 
ATOM   3049 C CD  . LYS B 1 409 ? 46.489  41.557 30.039  1.00 128.88 ? 82  LYS B CD  1 
ATOM   3050 C CE  . LYS B 1 409 ? 47.049  40.991 28.751  1.00 134.20 ? 82  LYS B CE  1 
ATOM   3051 N NZ  . LYS B 1 409 ? 48.530  40.956 28.768  1.00 123.58 ? 82  LYS B NZ  1 
ATOM   3052 N N   . LYS B 1 410 ? 44.486  39.244 33.550  1.00 130.77 ? 83  LYS B N   1 
ATOM   3053 C CA  . LYS B 1 410 ? 43.935  37.862 33.536  1.00 127.09 ? 83  LYS B CA  1 
ATOM   3054 C C   . LYS B 1 410 ? 42.409  37.927 33.429  1.00 118.86 ? 83  LYS B C   1 
ATOM   3055 O O   . LYS B 1 410 ? 41.845  37.179 32.608  1.00 118.56 ? 83  LYS B O   1 
ATOM   3056 C CB  . LYS B 1 410 ? 44.336  37.118 34.812  1.00 130.70 ? 83  LYS B CB  1 
ATOM   3057 C CG  . LYS B 1 410 ? 45.834  37.019 35.067  1.00 155.01 ? 83  LYS B CG  1 
ATOM   3058 C CD  . LYS B 1 410 ? 46.173  36.851 36.532  1.00 170.32 ? 83  LYS B CD  1 
ATOM   3059 C CE  . LYS B 1 410 ? 47.646  37.044 36.825  1.00 178.91 ? 83  LYS B CE  1 
ATOM   3060 N NZ  . LYS B 1 410 ? 47.916  37.071 38.281  1.00 184.22 ? 83  LYS B NZ  1 
ATOM   3061 N N   . VAL B 1 411 ? 41.775  38.790 34.229  1.00 115.17 ? 84  VAL B N   1 
ATOM   3062 C CA  . VAL B 1 411 ? 40.285  38.886 34.230  1.00 103.83 ? 84  VAL B CA  1 
ATOM   3063 C C   . VAL B 1 411 ? 39.811  39.208 32.810  1.00 106.18 ? 84  VAL B C   1 
ATOM   3064 O O   . VAL B 1 411 ? 39.138  38.352 32.208  1.00 104.08 ? 84  VAL B O   1 
ATOM   3065 C CB  . VAL B 1 411 ? 39.798  39.938 35.246  1.00 101.73 ? 84  VAL B CB  1 
ATOM   3066 C CG1 . VAL B 1 411 ? 38.425  40.493 34.898  1.00 104.92 ? 84  VAL B CG1 1 
ATOM   3067 C CG2 . VAL B 1 411 ? 39.818  39.401 36.669  1.00 91.34  ? 84  VAL B CG2 1 
ATOM   3068 N N   . ASP B 1 412 ? 40.193  40.371 32.276  1.00 112.23 ? 85  ASP B N   1 
ATOM   3069 C CA  . ASP B 1 412 ? 39.687  40.782 30.940  1.00 105.93 ? 85  ASP B CA  1 
ATOM   3070 C C   . ASP B 1 412 ? 39.879  39.637 29.943  1.00 102.02 ? 85  ASP B C   1 
ATOM   3071 O O   . ASP B 1 412 ? 38.923  39.347 29.201  1.00 104.50 ? 85  ASP B O   1 
ATOM   3072 C CB  . ASP B 1 412 ? 40.360  42.069 30.456  1.00 119.62 ? 85  ASP B CB  1 
ATOM   3073 C CG  . ASP B 1 412 ? 39.970  43.293 31.267  1.00 133.94 ? 85  ASP B CG  1 
ATOM   3074 O OD1 . ASP B 1 412 ? 38.758  43.571 31.358  1.00 132.69 ? 85  ASP B OD1 1 
ATOM   3075 O OD2 . ASP B 1 412 ? 40.881  43.965 31.789  1.00 144.55 ? 85  ASP B OD2 1 
ATOM   3076 N N   . ASP B 1 413 ? 41.048  38.992 29.950  1.00 101.75 ? 86  ASP B N   1 
ATOM   3077 C CA  . ASP B 1 413 ? 41.336  37.962 28.955  1.00 97.07  ? 86  ASP B CA  1 
ATOM   3078 C C   . ASP B 1 413 ? 40.411  36.755 29.120  1.00 91.31  ? 86  ASP B C   1 
ATOM   3079 O O   . ASP B 1 413 ? 39.826  36.256 28.140  1.00 92.14  ? 86  ASP B O   1 
ATOM   3080 C CB  . ASP B 1 413 ? 42.801  37.536 29.072  1.00 105.06 ? 86  ASP B CB  1 
ATOM   3081 C CG  . ASP B 1 413 ? 43.766  38.581 28.529  1.00 113.60 ? 86  ASP B CG  1 
ATOM   3082 O OD1 . ASP B 1 413 ? 43.304  39.612 27.988  1.00 111.76 ? 86  ASP B OD1 1 
ATOM   3083 O OD2 . ASP B 1 413 ? 44.991  38.374 28.657  1.00 129.85 ? 86  ASP B OD2 1 
ATOM   3084 N N   . GLY B 1 414 ? 40.266  36.272 30.362  1.00 91.64  ? 87  GLY B N   1 
ATOM   3085 C CA  . GLY B 1 414 ? 39.426  35.109 30.602  1.00 94.60  ? 87  GLY B CA  1 
ATOM   3086 C C   . GLY B 1 414 ? 37.970  35.363 30.259  1.00 93.37  ? 87  GLY B C   1 
ATOM   3087 O O   . GLY B 1 414 ? 37.316  34.529 29.627  1.00 96.03  ? 87  GLY B O   1 
ATOM   3088 N N   . PHE B 1 415 ? 37.445  36.519 30.681  1.00 88.26  ? 88  PHE B N   1 
ATOM   3089 C CA  . PHE B 1 415 ? 36.088  36.907 30.295  1.00 84.52  ? 88  PHE B CA  1 
ATOM   3090 C C   . PHE B 1 415 ? 35.938  36.987 28.782  1.00 87.92  ? 88  PHE B C   1 
ATOM   3091 O O   . PHE B 1 415 ? 34.897  36.600 28.239  1.00 88.59  ? 88  PHE B O   1 
ATOM   3092 C CB  . PHE B 1 415 ? 35.701  38.242 30.933  1.00 92.69  ? 88  PHE B CB  1 
ATOM   3093 C CG  . PHE B 1 415 ? 35.457  38.168 32.414  1.00 96.26  ? 88  PHE B CG  1 
ATOM   3094 C CD1 . PHE B 1 415 ? 36.489  37.919 33.298  1.00 102.36 ? 88  PHE B CD1 1 
ATOM   3095 C CD2 . PHE B 1 415 ? 34.182  38.360 32.919  1.00 89.28  ? 88  PHE B CD2 1 
ATOM   3096 C CE1 . PHE B 1 415 ? 36.254  37.861 34.653  1.00 106.25 ? 88  PHE B CE1 1 
ATOM   3097 C CE2 . PHE B 1 415 ? 33.942  38.302 34.274  1.00 91.43  ? 88  PHE B CE2 1 
ATOM   3098 C CZ  . PHE B 1 415 ? 34.983  38.054 35.142  1.00 100.53 ? 88  PHE B CZ  1 
ATOM   3099 N N   . LEU B 1 416 ? 36.959  37.489 28.081  1.00 96.37  ? 89  LEU B N   1 
ATOM   3100 C CA  . LEU B 1 416 ? 36.910  37.505 26.622  1.00 88.25  ? 89  LEU B CA  1 
ATOM   3101 C C   . LEU B 1 416 ? 36.706  36.103 26.065  1.00 86.89  ? 89  LEU B C   1 
ATOM   3102 O O   . LEU B 1 416 ? 35.817  35.879 25.239  1.00 85.42  ? 89  LEU B O   1 
ATOM   3103 C CB  . LEU B 1 416 ? 38.184  38.125 26.048  1.00 88.62  ? 89  LEU B CB  1 
ATOM   3104 C CG  . LEU B 1 416 ? 38.349  39.639 26.154  1.00 92.24  ? 89  LEU B CG  1 
ATOM   3105 C CD1 . LEU B 1 416 ? 39.746  40.039 25.711  1.00 98.69  ? 89  LEU B CD1 1 
ATOM   3106 C CD2 . LEU B 1 416 ? 37.295  40.349 25.320  1.00 91.10  ? 89  LEU B CD2 1 
ATOM   3107 N N   . ASP B 1 417 ? 37.530  35.147 26.500  1.00 96.68  ? 90  ASP B N   1 
ATOM   3108 C CA  . ASP B 1 417 ? 37.379  33.786 25.979  1.00 95.99  ? 90  ASP B CA  1 
ATOM   3109 C C   . ASP B 1 417 ? 36.021  33.192 26.342  1.00 93.99  ? 90  ASP B C   1 
ATOM   3110 O O   . ASP B 1 417 ? 35.370  32.548 25.503  1.00 93.86  ? 90  ASP B O   1 
ATOM   3111 C CB  . ASP B 1 417 ? 38.514  32.887 26.466  1.00 96.39  ? 90  ASP B CB  1 
ATOM   3112 C CG  . ASP B 1 417 ? 39.856  33.292 25.895  1.00 104.62 ? 90  ASP B CG  1 
ATOM   3113 O OD1 . ASP B 1 417 ? 40.120  32.948 24.723  1.00 111.95 ? 90  ASP B OD1 1 
ATOM   3114 O OD2 . ASP B 1 417 ? 40.642  33.947 26.607  1.00 106.73 ? 90  ASP B OD2 1 
ATOM   3115 N N   . ILE B 1 418 ? 35.575  33.403 27.584  1.00 91.08  ? 91  ILE B N   1 
ATOM   3116 C CA  . ILE B 1 418 ? 34.267  32.906 28.011  1.00 86.87  ? 91  ILE B CA  1 
ATOM   3117 C C   . ILE B 1 418 ? 33.169  33.436 27.095  1.00 84.62  ? 91  ILE B C   1 
ATOM   3118 O O   . ILE B 1 418 ? 32.310  32.682 26.619  1.00 84.03  ? 91  ILE B O   1 
ATOM   3119 C CB  . ILE B 1 418 ? 34.003  33.280 29.481  1.00 84.89  ? 91  ILE B CB  1 
ATOM   3120 C CG1 . ILE B 1 418 ? 35.042  32.633 30.396  1.00 94.99  ? 91  ILE B CG1 1 
ATOM   3121 C CG2 . ILE B 1 418 ? 32.608  32.860 29.903  1.00 74.09  ? 91  ILE B CG2 1 
ATOM   3122 C CD1 . ILE B 1 418 ? 35.048  33.209 31.783  1.00 98.68  ? 91  ILE B CD1 1 
ATOM   3123 N N   . TRP B 1 419 ? 33.194  34.741 26.812  1.00 89.54  ? 92  TRP B N   1 
ATOM   3124 C CA  . TRP B 1 419 ? 32.121  35.328 26.019  1.00 86.70  ? 92  TRP B CA  1 
ATOM   3125 C C   . TRP B 1 419 ? 32.224  34.955 24.546  1.00 81.32  ? 92  TRP B C   1 
ATOM   3126 O O   . TRP B 1 419 ? 31.194  34.833 23.880  1.00 79.75  ? 92  TRP B O   1 
ATOM   3127 C CB  . TRP B 1 419 ? 32.084  36.845 26.191  1.00 88.83  ? 92  TRP B CB  1 
ATOM   3128 C CG  . TRP B 1 419 ? 31.553  37.268 27.524  1.00 102.06 ? 92  TRP B CG  1 
ATOM   3129 C CD1 . TRP B 1 419 ? 32.210  37.989 28.478  1.00 106.85 ? 92  TRP B CD1 1 
ATOM   3130 C CD2 . TRP B 1 419 ? 30.247  36.994 28.055  1.00 101.63 ? 92  TRP B CD2 1 
ATOM   3131 N NE1 . TRP B 1 419 ? 31.397  38.182 29.568  1.00 108.63 ? 92  TRP B NE1 1 
ATOM   3132 C CE2 . TRP B 1 419 ? 30.187  37.582 29.333  1.00 111.69 ? 92  TRP B CE2 1 
ATOM   3133 C CE3 . TRP B 1 419 ? 29.124  36.310 27.572  1.00 92.16  ? 92  TRP B CE3 1 
ATOM   3134 C CZ2 . TRP B 1 419 ? 29.048  37.508 30.136  1.00 111.17 ? 92  TRP B CZ2 1 
ATOM   3135 C CZ3 . TRP B 1 419 ? 27.996  36.236 28.370  1.00 89.59  ? 92  TRP B CZ3 1 
ATOM   3136 C CH2 . TRP B 1 419 ? 27.965  36.832 29.637  1.00 94.23  ? 92  TRP B CH2 1 
ATOM   3137 N N   . THR B 1 420 ? 33.433  34.760 24.013  1.00 79.41  ? 93  THR B N   1 
ATOM   3138 C CA  . THR B 1 420 ? 33.537  34.252 22.646  1.00 80.20  ? 93  THR B CA  1 
ATOM   3139 C C   . THR B 1 420 ? 32.947  32.854 22.533  1.00 84.10  ? 93  THR B C   1 
ATOM   3140 O O   . THR B 1 420 ? 32.240  32.547 21.562  1.00 86.09  ? 93  THR B O   1 
ATOM   3141 C CB  . THR B 1 420 ? 34.991  34.253 22.167  1.00 87.22  ? 93  THR B CB  1 
ATOM   3142 O OG1 . THR B 1 420 ? 35.754  33.278 22.897  1.00 108.33 ? 93  THR B OG1 1 
ATOM   3143 C CG2 . THR B 1 420 ? 35.619  35.637 22.275  1.00 84.55  ? 93  THR B CG2 1 
ATOM   3144 N N   . TYR B 1 421 ? 33.225  31.991 23.513  1.00 87.50  ? 94  TYR B N   1 
ATOM   3145 C CA  . TYR B 1 421 ? 32.601  30.674 23.508  1.00 83.74  ? 94  TYR B CA  1 
ATOM   3146 C C   . TYR B 1 421 ? 31.082  30.804 23.568  1.00 80.86  ? 94  TYR B C   1 
ATOM   3147 O O   . TYR B 1 421 ? 30.357  30.148 22.809  1.00 79.97  ? 94  TYR B O   1 
ATOM   3148 C CB  . TYR B 1 421 ? 33.120  29.836 24.677  1.00 83.98  ? 94  TYR B CB  1 
ATOM   3149 C CG  . TYR B 1 421 ? 32.431  28.499 24.801  1.00 87.45  ? 94  TYR B CG  1 
ATOM   3150 C CD1 . TYR B 1 421 ? 32.461  27.586 23.754  1.00 91.88  ? 94  TYR B CD1 1 
ATOM   3151 C CD2 . TYR B 1 421 ? 31.723  28.159 25.945  1.00 93.00  ? 94  TYR B CD2 1 
ATOM   3152 C CE1 . TYR B 1 421 ? 31.822  26.366 23.852  1.00 86.59  ? 94  TYR B CE1 1 
ATOM   3153 C CE2 . TYR B 1 421 ? 31.077  26.941 26.049  1.00 84.89  ? 94  TYR B CE2 1 
ATOM   3154 C CZ  . TYR B 1 421 ? 31.133  26.047 25.002  1.00 87.68  ? 94  TYR B CZ  1 
ATOM   3155 O OH  . TYR B 1 421 ? 30.495  24.830 25.099  1.00 89.69  ? 94  TYR B OH  1 
ATOM   3156 N N   . ASN B 1 422 ? 30.587  31.680 24.449  1.00 76.85  ? 95  ASN B N   1 
ATOM   3157 C CA  . ASN B 1 422 ? 29.144  31.856 24.595  1.00 77.78  ? 95  ASN B CA  1 
ATOM   3158 C C   . ASN B 1 422 ? 28.505  32.402 23.323  1.00 76.26  ? 95  ASN B C   1 
ATOM   3159 O O   . ASN B 1 422 ? 27.372  32.033 22.981  1.00 77.56  ? 95  ASN B O   1 
ATOM   3160 C CB  . ASN B 1 422 ? 28.843  32.778 25.777  1.00 83.13  ? 95  ASN B CB  1 
ATOM   3161 C CG  . ASN B 1 422 ? 29.121  32.118 27.113  1.00 86.10  ? 95  ASN B CG  1 
ATOM   3162 O OD1 . ASN B 1 422 ? 29.149  30.892 27.220  1.00 91.21  ? 95  ASN B OD1 1 
ATOM   3163 N ND2 . ASN B 1 422 ? 29.316  32.930 28.143  1.00 86.59  ? 95  ASN B ND2 1 
ATOM   3164 N N   . ALA B 1 423 ? 29.218  33.269 22.605  1.00 70.19  ? 96  ALA B N   1 
ATOM   3165 C CA  . ALA B 1 423 ? 28.684  33.847 21.377  1.00 61.21  ? 96  ALA B CA  1 
ATOM   3166 C C   . ALA B 1 423 ? 28.631  32.808 20.267  1.00 60.85  ? 96  ALA B C   1 
ATOM   3167 O O   . ALA B 1 423 ? 27.638  32.717 19.532  1.00 63.58  ? 96  ALA B O   1 
ATOM   3168 C CB  . ALA B 1 423 ? 29.531  35.045 20.953  1.00 54.13  ? 96  ALA B CB  1 
ATOM   3169 N N   . GLU B 1 424 ? 29.699  32.016 20.124  1.00 69.28  ? 97  GLU B N   1 
ATOM   3170 C CA  . GLU B 1 424 ? 29.644  30.902 19.184  1.00 67.41  ? 97  GLU B CA  1 
ATOM   3171 C C   . GLU B 1 424 ? 28.528  29.930 19.554  1.00 70.75  ? 97  GLU B C   1 
ATOM   3172 O O   . GLU B 1 424 ? 27.906  29.338 18.666  1.00 73.42  ? 97  GLU B O   1 
ATOM   3173 C CB  . GLU B 1 424 ? 31.000  30.191 19.121  1.00 80.96  ? 97  GLU B CB  1 
ATOM   3174 C CG  . GLU B 1 424 ? 32.102  31.042 18.477  1.00 87.01  ? 97  GLU B CG  1 
ATOM   3175 C CD  . GLU B 1 424 ? 33.491  30.430 18.597  1.00 96.35  ? 97  GLU B CD  1 
ATOM   3176 O OE1 . GLU B 1 424 ? 33.904  30.098 19.729  1.00 79.78  ? 97  GLU B OE1 1 
ATOM   3177 O OE2 . GLU B 1 424 ? 34.179  30.308 17.559  1.00 90.00  ? 97  GLU B OE2 1 
ATOM   3178 N N   . LEU B 1 425 ? 28.234  29.783 20.852  1.00 69.13  ? 98  LEU B N   1 
ATOM   3179 C CA  . LEU B 1 425 ? 27.087  28.979 21.273  1.00 70.93  ? 98  LEU B CA  1 
ATOM   3180 C C   . LEU B 1 425 ? 25.775  29.559 20.764  1.00 71.24  ? 98  LEU B C   1 
ATOM   3181 O O   . LEU B 1 425 ? 24.935  28.831 20.223  1.00 72.62  ? 98  LEU B O   1 
ATOM   3182 C CB  . LEU B 1 425 ? 27.045  28.854 22.794  1.00 67.48  ? 98  LEU B CB  1 
ATOM   3183 C CG  . LEU B 1 425 ? 27.507  27.530 23.388  1.00 66.98  ? 98  LEU B CG  1 
ATOM   3184 C CD1 . LEU B 1 425 ? 27.283  27.575 24.878  1.00 72.14  ? 98  LEU B CD1 1 
ATOM   3185 C CD2 . LEU B 1 425 ? 26.709  26.401 22.766  1.00 54.01  ? 98  LEU B CD2 1 
ATOM   3186 N N   . LEU B 1 426 ? 25.553  30.858 20.991  1.00 72.05  ? 99  LEU B N   1 
ATOM   3187 C CA  . LEU B 1 426 ? 24.348  31.504 20.467  1.00 72.51  ? 99  LEU B CA  1 
ATOM   3188 C C   . LEU B 1 426 ? 24.224  31.292 18.966  1.00 67.53  ? 99  LEU B C   1 
ATOM   3189 O O   . LEU B 1 426 ? 23.129  31.028 18.446  1.00 67.16  ? 99  LEU B O   1 
ATOM   3190 C CB  . LEU B 1 426 ? 24.356  33.000 20.779  1.00 74.20  ? 99  LEU B CB  1 
ATOM   3191 C CG  . LEU B 1 426 ? 24.290  33.433 22.238  1.00 83.22  ? 99  LEU B CG  1 
ATOM   3192 C CD1 . LEU B 1 426 ? 24.528  34.931 22.336  1.00 102.58 ? 99  LEU B CD1 1 
ATOM   3193 C CD2 . LEU B 1 426 ? 22.941  33.051 22.822  1.00 111.34 ? 99  LEU B CD2 1 
ATOM   3194 N N   . VAL B 1 427 ? 25.349  31.398 18.256  1.00 66.38  ? 100 VAL B N   1 
ATOM   3195 C CA  . VAL B 1 427 ? 25.343  31.223 16.808  1.00 62.21  ? 100 VAL B CA  1 
ATOM   3196 C C   . VAL B 1 427 ? 24.922  29.808 16.444  1.00 70.10  ? 100 VAL B C   1 
ATOM   3197 O O   . VAL B 1 427 ? 24.063  29.607 15.583  1.00 76.30  ? 100 VAL B O   1 
ATOM   3198 C CB  . VAL B 1 427 ? 26.719  31.571 16.217  1.00 63.59  ? 100 VAL B CB  1 
ATOM   3199 C CG1 . VAL B 1 427 ? 26.733  31.294 14.728  1.00 68.71  ? 100 VAL B CG1 1 
ATOM   3200 C CG2 . VAL B 1 427 ? 27.030  33.029 16.461  1.00 69.74  ? 100 VAL B CG2 1 
ATOM   3201 N N   . LEU B 1 428 ? 25.532  28.807 17.084  1.00 70.87  ? 101 LEU B N   1 
ATOM   3202 C CA  . LEU B 1 428 ? 25.163  27.416 16.824  1.00 65.22  ? 101 LEU B CA  1 
ATOM   3203 C C   . LEU B 1 428 ? 23.674  27.203 17.056  1.00 72.41  ? 101 LEU B C   1 
ATOM   3204 O O   . LEU B 1 428 ? 22.953  26.671 16.191  1.00 76.95  ? 101 LEU B O   1 
ATOM   3205 C CB  . LEU B 1 428 ? 25.962  26.485 17.737  1.00 62.84  ? 101 LEU B CB  1 
ATOM   3206 C CG  . LEU B 1 428 ? 27.486  26.449 17.654  1.00 66.53  ? 101 LEU B CG  1 
ATOM   3207 C CD1 . LEU B 1 428 ? 28.072  25.583 18.766  1.00 71.73  ? 101 LEU B CD1 1 
ATOM   3208 C CD2 . LEU B 1 428 ? 27.946  25.984 16.303  1.00 74.03  ? 101 LEU B CD2 1 
ATOM   3209 N N   . LEU B 1 429 ? 23.208  27.613 18.239  1.00 76.67  ? 102 LEU B N   1 
ATOM   3210 C CA  . LEU B 1 429 ? 21.817  27.448 18.633  1.00 71.50  ? 102 LEU B CA  1 
ATOM   3211 C C   . LEU B 1 429 ? 20.885  28.005 17.570  1.00 74.23  ? 102 LEU B C   1 
ATOM   3212 O O   . LEU B 1 429 ? 20.066  27.281 16.997  1.00 80.87  ? 102 LEU B O   1 
ATOM   3213 C CB  . LEU B 1 429 ? 21.571  28.147 19.973  1.00 67.77  ? 102 LEU B CB  1 
ATOM   3214 C CG  . LEU B 1 429 ? 22.208  27.537 21.220  1.00 73.01  ? 102 LEU B CG  1 
ATOM   3215 C CD1 . LEU B 1 429 ? 22.005  28.443 22.432  1.00 73.63  ? 102 LEU B CD1 1 
ATOM   3216 C CD2 . LEU B 1 429 ? 21.670  26.140 21.487  1.00 80.16  ? 102 LEU B CD2 1 
ATOM   3217 N N   . GLU B 1 430 ? 21.022  29.297 17.267  1.00 68.03  ? 103 GLU B N   1 
ATOM   3218 C CA  . GLU B 1 430 ? 20.070  29.924 16.362  1.00 75.89  ? 103 GLU B CA  1 
ATOM   3219 C C   . GLU B 1 430 ? 20.297  29.546 14.904  1.00 74.44  ? 103 GLU B C   1 
ATOM   3220 O O   . GLU B 1 430 ? 19.372  29.679 14.100  1.00 78.12  ? 103 GLU B O   1 
ATOM   3221 C CB  . GLU B 1 430 ? 20.091  31.432 16.564  1.00 79.87  ? 103 GLU B CB  1 
ATOM   3222 C CG  . GLU B 1 430 ? 19.173  31.831 17.706  1.00 94.72  ? 103 GLU B CG  1 
ATOM   3223 C CD  . GLU B 1 430 ? 19.415  33.232 18.176  1.00 123.38 ? 103 GLU B CD  1 
ATOM   3224 O OE1 . GLU B 1 430 ? 20.489  33.764 17.853  1.00 174.22 ? 103 GLU B OE1 1 
ATOM   3225 O OE2 . GLU B 1 430 ? 18.528  33.805 18.846  1.00 128.80 ? 103 GLU B OE2 1 
ATOM   3226 N N   . ASN B 1 431 ? 21.467  29.020 14.545  1.00 73.55  ? 104 ASN B N   1 
ATOM   3227 C CA  . ASN B 1 431 ? 21.601  28.396 13.236  1.00 68.05  ? 104 ASN B CA  1 
ATOM   3228 C C   . ASN B 1 431 ? 20.672  27.198 13.130  1.00 69.08  ? 104 ASN B C   1 
ATOM   3229 O O   . ASN B 1 431 ? 19.866  27.093 12.192  1.00 74.03  ? 104 ASN B O   1 
ATOM   3230 C CB  . ASN B 1 431 ? 23.053  27.990 13.010  1.00 64.28  ? 104 ASN B CB  1 
ATOM   3231 C CG  . ASN B 1 431 ? 23.950  29.177 12.779  1.00 64.93  ? 104 ASN B CG  1 
ATOM   3232 O OD1 . ASN B 1 431 ? 23.508  30.230 12.321  1.00 69.30  ? 104 ASN B OD1 1 
ATOM   3233 N ND2 . ASN B 1 431 ? 25.219  29.027 13.134  1.00 75.89  ? 104 ASN B ND2 1 
ATOM   3234 N N   . GLU B 1 432 ? 20.743  26.296 14.113  1.00 69.38  ? 105 GLU B N   1 
ATOM   3235 C CA  . GLU B 1 432 ? 19.780  25.201 14.127  1.00 69.28  ? 105 GLU B CA  1 
ATOM   3236 C C   . GLU B 1 432 ? 18.349  25.720 14.185  1.00 70.98  ? 105 GLU B C   1 
ATOM   3237 O O   . GLU B 1 432 ? 17.454  25.152 13.552  1.00 76.43  ? 105 GLU B O   1 
ATOM   3238 C CB  . GLU B 1 432 ? 20.042  24.242 15.281  1.00 66.47  ? 105 GLU B CB  1 
ATOM   3239 C CG  . GLU B 1 432 ? 19.389  22.899 15.006  1.00 76.01  ? 105 GLU B CG  1 
ATOM   3240 C CD  . GLU B 1 432 ? 20.173  21.735 15.536  1.00 87.49  ? 105 GLU B CD  1 
ATOM   3241 O OE1 . GLU B 1 432 ? 21.134  21.972 16.276  1.00 89.47  ? 105 GLU B OE1 1 
ATOM   3242 O OE2 . GLU B 1 432 ? 19.831  20.586 15.198  1.00 99.27  ? 105 GLU B OE2 1 
ATOM   3243 N N   . ARG B 1 433 ? 18.114  26.806 14.925  1.00 68.51  ? 106 ARG B N   1 
ATOM   3244 C CA  . ARG B 1 433 ? 16.744  27.284 15.102  1.00 74.42  ? 106 ARG B CA  1 
ATOM   3245 C C   . ARG B 1 433 ? 16.162  27.817 13.797  1.00 76.28  ? 106 ARG B C   1 
ATOM   3246 O O   . ARG B 1 433 ? 15.005  27.529 13.472  1.00 78.07  ? 106 ARG B O   1 
ATOM   3247 C CB  . ARG B 1 433 ? 16.698  28.336 16.207  1.00 79.17  ? 106 ARG B CB  1 
ATOM   3248 C CG  . ARG B 1 433 ? 17.115  27.772 17.554  1.00 80.83  ? 106 ARG B CG  1 
ATOM   3249 C CD  . ARG B 1 433 ? 17.074  28.798 18.666  1.00 83.40  ? 106 ARG B CD  1 
ATOM   3250 N NE  . ARG B 1 433 ? 17.699  28.268 19.873  1.00 84.67  ? 106 ARG B NE  1 
ATOM   3251 C CZ  . ARG B 1 433 ? 18.239  29.015 20.827  1.00 94.61  ? 106 ARG B CZ  1 
ATOM   3252 N NH1 . ARG B 1 433 ? 18.264  30.336 20.739  1.00 100.49 ? 106 ARG B NH1 1 
ATOM   3253 N NH2 . ARG B 1 433 ? 18.754  28.423 21.901  1.00 89.58  ? 106 ARG B NH2 1 
ATOM   3254 N N   . THR B 1 434 ? 16.949  28.568 13.022  1.00 75.62  ? 107 THR B N   1 
ATOM   3255 C CA  . THR B 1 434 ? 16.474  29.011 11.715  1.00 75.16  ? 107 THR B CA  1 
ATOM   3256 C C   . THR B 1 434 ? 16.310  27.841 10.751  1.00 68.36  ? 107 THR B C   1 
ATOM   3257 O O   . THR B 1 434 ? 15.355  27.812 9.967   1.00 86.03  ? 107 THR B O   1 
ATOM   3258 C CB  . THR B 1 434 ? 17.405  30.078 11.131  1.00 65.35  ? 107 THR B CB  1 
ATOM   3259 O OG1 . THR B 1 434 ? 18.624  29.475 10.668  1.00 68.57  ? 107 THR B OG1 1 
ATOM   3260 C CG2 . THR B 1 434 ? 17.685  31.188 12.146  1.00 60.05  ? 107 THR B CG2 1 
ATOM   3261 N N   . LEU B 1 435 ? 17.211  26.856 10.792  1.00 70.67  ? 108 LEU B N   1 
ATOM   3262 C CA  . LEU B 1 435 ? 17.042  25.717 9.889   1.00 74.53  ? 108 LEU B CA  1 
ATOM   3263 C C   . LEU B 1 435 ? 15.768  24.938 10.222  1.00 80.48  ? 108 LEU B C   1 
ATOM   3264 O O   . LEU B 1 435 ? 15.020  24.519 9.322   1.00 86.89  ? 108 LEU B O   1 
ATOM   3265 C CB  . LEU B 1 435 ? 18.279  24.824 9.952   1.00 74.16  ? 108 LEU B CB  1 
ATOM   3266 C CG  . LEU B 1 435 ? 19.478  25.397 9.191   1.00 63.32  ? 108 LEU B CG  1 
ATOM   3267 C CD1 . LEU B 1 435 ? 20.669  24.468 9.276   1.00 65.74  ? 108 LEU B CD1 1 
ATOM   3268 C CD2 . LEU B 1 435 ? 19.129  25.683 7.726   1.00 75.28  ? 108 LEU B CD2 1 
ATOM   3269 N N   . ASP B 1 436 ? 15.483  24.774 11.516  1.00 81.87  ? 109 ASP B N   1 
ATOM   3270 C CA  . ASP B 1 436 ? 14.264  24.098 11.953  1.00 90.68  ? 109 ASP B CA  1 
ATOM   3271 C C   . ASP B 1 436 ? 13.037  24.916 11.565  1.00 94.88  ? 109 ASP B C   1 
ATOM   3272 O O   . ASP B 1 436 ? 12.015  24.356 11.142  1.00 95.99  ? 109 ASP B O   1 
ATOM   3273 C CB  . ASP B 1 436 ? 14.359  23.858 13.471  1.00 95.56  ? 109 ASP B CB  1 
ATOM   3274 C CG  . ASP B 1 436 ? 13.032  23.445 14.140  1.00 109.31 ? 109 ASP B CG  1 
ATOM   3275 O OD1 . ASP B 1 436 ? 11.951  23.404 13.522  1.00 135.13 ? 109 ASP B OD1 1 
ATOM   3276 O OD2 . ASP B 1 436 ? 13.083  23.174 15.357  1.00 113.06 ? 109 ASP B OD2 1 
ATOM   3277 N N   . TYR B 1 437 ? 13.131  26.242 11.697  1.00 89.86  ? 110 TYR B N   1 
ATOM   3278 C CA  . TYR B 1 437 ? 12.077  27.138 11.235  1.00 90.05  ? 110 TYR B CA  1 
ATOM   3279 C C   . TYR B 1 437 ? 11.763  26.897 9.765   1.00 83.18  ? 110 TYR B C   1 
ATOM   3280 O O   . TYR B 1 437 ? 10.592  26.829 9.366   1.00 92.72  ? 110 TYR B O   1 
ATOM   3281 C CB  . TYR B 1 437 ? 12.516  28.588 11.479  1.00 87.17  ? 110 TYR B CB  1 
ATOM   3282 C CG  . TYR B 1 437 ? 11.578  29.666 10.975  1.00 92.13  ? 110 TYR B CG  1 
ATOM   3283 C CD1 . TYR B 1 437 ? 10.202  29.536 11.099  1.00 101.78 ? 110 TYR B CD1 1 
ATOM   3284 C CD2 . TYR B 1 437 ? 12.076  30.827 10.390  1.00 85.73  ? 110 TYR B CD2 1 
ATOM   3285 C CE1 . TYR B 1 437 ? 9.347   30.522 10.643  1.00 102.58 ? 110 TYR B CE1 1 
ATOM   3286 C CE2 . TYR B 1 437 ? 11.226  31.820 9.930   1.00 93.54  ? 110 TYR B CE2 1 
ATOM   3287 C CZ  . TYR B 1 437 ? 9.861   31.660 10.061  1.00 100.62 ? 110 TYR B CZ  1 
ATOM   3288 O OH  . TYR B 1 437 ? 9.003   32.635 9.610   1.00 94.53  ? 110 TYR B OH  1 
ATOM   3289 N N   . HIS B 1 438 ? 12.805  26.753 8.946   1.00 76.52  ? 111 HIS B N   1 
ATOM   3290 C CA  . HIS B 1 438 ? 12.606  26.476 7.525   1.00 78.04  ? 111 HIS B CA  1 
ATOM   3291 C C   . HIS B 1 438 ? 11.857  25.164 7.325   1.00 90.62  ? 111 HIS B C   1 
ATOM   3292 O O   . HIS B 1 438 ? 10.901  25.081 6.534   1.00 89.96  ? 111 HIS B O   1 
ATOM   3293 C CB  . HIS B 1 438 ? 13.954  26.420 6.810   1.00 74.24  ? 111 HIS B CB  1 
ATOM   3294 C CG  . HIS B 1 438 ? 14.567  27.763 6.572   1.00 72.40  ? 111 HIS B CG  1 
ATOM   3295 N ND1 . HIS B 1 438 ? 14.028  28.679 5.695   1.00 70.96  ? 111 HIS B ND1 1 
ATOM   3296 C CD2 . HIS B 1 438 ? 15.687  28.336 7.074   1.00 73.59  ? 111 HIS B CD2 1 
ATOM   3297 C CE1 . HIS B 1 438 ? 14.781  29.764 5.677   1.00 71.88  ? 111 HIS B CE1 1 
ATOM   3298 N NE2 . HIS B 1 438 ? 15.795  29.581 6.505   1.00 69.08  ? 111 HIS B NE2 1 
ATOM   3299 N N   . ASP B 1 439 ? 12.305  24.118 8.026   1.00 91.41  ? 112 ASP B N   1 
ATOM   3300 C CA  . ASP B 1 439 ? 11.603  22.834 7.997   1.00 94.96  ? 112 ASP B CA  1 
ATOM   3301 C C   . ASP B 1 439 ? 10.115  23.004 8.296   1.00 92.16  ? 112 ASP B C   1 
ATOM   3302 O O   . ASP B 1 439 ? 9.252   22.497 7.565   1.00 93.87  ? 112 ASP B O   1 
ATOM   3303 C CB  . ASP B 1 439 ? 12.235  21.862 8.999   1.00 100.95 ? 112 ASP B CB  1 
ATOM   3304 C CG  . ASP B 1 439 ? 13.582  21.334 8.540   1.00 104.06 ? 112 ASP B CG  1 
ATOM   3305 O OD1 . ASP B 1 439 ? 14.008  21.662 7.407   1.00 110.32 ? 112 ASP B OD1 1 
ATOM   3306 O OD2 . ASP B 1 439 ? 14.207  20.572 9.306   1.00 100.05 ? 112 ASP B OD2 1 
ATOM   3307 N N   . SER B 1 440 ? 9.801   23.715 9.381   1.00 85.95  ? 113 SER B N   1 
ATOM   3308 C CA  . SER B 1 440 ? 8.408   23.890 9.782   1.00 88.78  ? 113 SER B CA  1 
ATOM   3309 C C   . SER B 1 440 ? 7.613   24.648 8.724   1.00 91.87  ? 113 SER B C   1 
ATOM   3310 O O   . SER B 1 440 ? 6.424   24.376 8.516   1.00 99.96  ? 113 SER B O   1 
ATOM   3311 C CB  . SER B 1 440 ? 8.337   24.612 11.126  1.00 98.55  ? 113 SER B CB  1 
ATOM   3312 O OG  . SER B 1 440 ? 8.452   26.013 10.953  1.00 103.22 ? 113 SER B OG  1 
ATOM   3313 N N   . ASN B 1 441 ? 8.250   25.607 8.047   1.00 89.32  ? 114 ASN B N   1 
ATOM   3314 C CA  . ASN B 1 441 ? 7.555   26.326 6.982   1.00 84.10  ? 114 ASN B CA  1 
ATOM   3315 C C   . ASN B 1 441 ? 7.168   25.387 5.847   1.00 83.67  ? 114 ASN B C   1 
ATOM   3316 O O   . ASN B 1 441 ? 6.043   25.449 5.326   1.00 96.10  ? 114 ASN B O   1 
ATOM   3317 C CB  . ASN B 1 441 ? 8.412   27.478 6.460   1.00 84.44  ? 114 ASN B CB  1 
ATOM   3318 C CG  . ASN B 1 441 ? 8.629   28.557 7.494   1.00 87.33  ? 114 ASN B CG  1 
ATOM   3319 O OD1 . ASN B 1 441 ? 9.759   28.957 7.766   1.00 89.19  ? 114 ASN B OD1 1 
ATOM   3320 N ND2 . ASN B 1 441 ? 7.538   29.035 8.080   1.00 89.24  ? 114 ASN B ND2 1 
ATOM   3321 N N   . VAL B 1 442 ? 8.092   24.508 5.444   1.00 79.39  ? 115 VAL B N   1 
ATOM   3322 C CA  . VAL B 1 442 ? 7.743   23.542 4.398   1.00 83.30  ? 115 VAL B CA  1 
ATOM   3323 C C   . VAL B 1 442 ? 6.591   22.654 4.860   1.00 90.46  ? 115 VAL B C   1 
ATOM   3324 O O   . VAL B 1 442 ? 5.655   22.364 4.095   1.00 92.36  ? 115 VAL B O   1 
ATOM   3325 C CB  . VAL B 1 442 ? 8.962   22.698 3.983   1.00 80.25  ? 115 VAL B CB  1 
ATOM   3326 C CG1 . VAL B 1 442 ? 8.704   22.055 2.622   1.00 71.21  ? 115 VAL B CG1 1 
ATOM   3327 C CG2 . VAL B 1 442 ? 10.219  23.537 3.941   1.00 82.38  ? 115 VAL B CG2 1 
ATOM   3328 N N   . LYS B 1 443 ? 6.649   22.203 6.118   1.00 90.38  ? 116 LYS B N   1 
ATOM   3329 C CA  . LYS B 1 443 ? 5.570   21.387 6.669   1.00 88.70  ? 116 LYS B CA  1 
ATOM   3330 C C   . LYS B 1 443 ? 4.226   22.101 6.561   1.00 98.13  ? 116 LYS B C   1 
ATOM   3331 O O   . LYS B 1 443 ? 3.217   21.498 6.170   1.00 105.42 ? 116 LYS B O   1 
ATOM   3332 C CB  . LYS B 1 443 ? 5.869   21.049 8.129   1.00 97.43  ? 116 LYS B CB  1 
ATOM   3333 C CG  . LYS B 1 443 ? 7.204   20.356 8.362   1.00 111.50 ? 116 LYS B CG  1 
ATOM   3334 C CD  . LYS B 1 443 ? 7.472   20.216 9.857   1.00 143.83 ? 116 LYS B CD  1 
ATOM   3335 C CE  . LYS B 1 443 ? 8.906   19.799 10.142  1.00 151.06 ? 116 LYS B CE  1 
ATOM   3336 N NZ  . LYS B 1 443 ? 9.357   20.202 11.503  1.00 159.73 ? 116 LYS B NZ  1 
ATOM   3337 N N   . ASN B 1 444 ? 4.196   23.387 6.917   1.00 103.87 ? 117 ASN B N   1 
ATOM   3338 C CA  . ASN B 1 444 ? 2.940   24.132 6.910   1.00 101.56 ? 117 ASN B CA  1 
ATOM   3339 C C   . ASN B 1 444 ? 2.406   24.305 5.496   1.00 104.13 ? 117 ASN B C   1 
ATOM   3340 O O   . ASN B 1 444 ? 1.191   24.230 5.271   1.00 113.59 ? 117 ASN B O   1 
ATOM   3341 C CB  . ASN B 1 444 ? 3.128   25.489 7.584   1.00 105.16 ? 117 ASN B CB  1 
ATOM   3342 C CG  . ASN B 1 444 ? 3.594   25.363 9.020   1.00 110.89 ? 117 ASN B CG  1 
ATOM   3343 O OD1 . ASN B 1 444 ? 3.722   24.255 9.547   1.00 110.52 ? 117 ASN B OD1 1 
ATOM   3344 N ND2 . ASN B 1 444 ? 3.864   26.495 9.656   1.00 127.15 ? 117 ASN B ND2 1 
ATOM   3345 N N   . LEU B 1 445 ? 3.293   24.541 4.529   1.00 96.33  ? 118 LEU B N   1 
ATOM   3346 C CA  . LEU B 1 445 ? 2.849   24.578 3.137   1.00 97.17  ? 118 LEU B CA  1 
ATOM   3347 C C   . LEU B 1 445 ? 2.203   23.253 2.742   1.00 102.30 ? 118 LEU B C   1 
ATOM   3348 O O   . LEU B 1 445 ? 1.136   23.218 2.098   1.00 110.95 ? 118 LEU B O   1 
ATOM   3349 C CB  . LEU B 1 445 ? 4.036   24.892 2.226   1.00 91.65  ? 118 LEU B CB  1 
ATOM   3350 C CG  . LEU B 1 445 ? 3.730   25.443 0.836   1.00 91.48  ? 118 LEU B CG  1 
ATOM   3351 C CD1 . LEU B 1 445 ? 3.342   26.903 0.950   1.00 95.69  ? 118 LEU B CD1 1 
ATOM   3352 C CD2 . LEU B 1 445 ? 4.931   25.273 -0.085  1.00 90.41  ? 118 LEU B CD2 1 
ATOM   3353 N N   . TYR B 1 446 ? 2.829   22.149 3.151   1.00 94.03  ? 119 TYR B N   1 
ATOM   3354 C CA  . TYR B 1 446 ? 2.302   20.831 2.819   1.00 99.14  ? 119 TYR B CA  1 
ATOM   3355 C C   . TYR B 1 446 ? 0.925   20.605 3.435   1.00 109.16 ? 119 TYR B C   1 
ATOM   3356 O O   . TYR B 1 446 ? 0.035   20.020 2.801   1.00 117.75 ? 119 TYR B O   1 
ATOM   3357 C CB  . TYR B 1 446 ? 3.299   19.768 3.270   1.00 105.84 ? 119 TYR B CB  1 
ATOM   3358 C CG  . TYR B 1 446 ? 2.995   18.387 2.772   1.00 120.78 ? 119 TYR B CG  1 
ATOM   3359 C CD1 . TYR B 1 446 ? 3.225   18.041 1.452   1.00 124.97 ? 119 TYR B CD1 1 
ATOM   3360 C CD2 . TYR B 1 446 ? 2.541   17.406 3.638   1.00 135.41 ? 119 TYR B CD2 1 
ATOM   3361 C CE1 . TYR B 1 446 ? 2.962   16.772 0.998   1.00 137.78 ? 119 TYR B CE1 1 
ATOM   3362 C CE2 . TYR B 1 446 ? 2.290   16.135 3.192   1.00 150.04 ? 119 TYR B CE2 1 
ATOM   3363 C CZ  . TYR B 1 446 ? 2.498   15.821 1.870   1.00 148.37 ? 119 TYR B CZ  1 
ATOM   3364 O OH  . TYR B 1 446 ? 2.240   14.546 1.425   1.00 151.25 ? 119 TYR B OH  1 
ATOM   3365 N N   . GLU B 1 447 ? 0.725   21.078 4.666   1.00 112.15 ? 120 GLU B N   1 
ATOM   3366 C CA  . GLU B 1 447 ? -0.586  20.939 5.296   1.00 118.35 ? 120 GLU B CA  1 
ATOM   3367 C C   . GLU B 1 447 ? -1.629  21.815 4.610   1.00 120.03 ? 120 GLU B C   1 
ATOM   3368 O O   . GLU B 1 447 ? -2.791  21.411 4.467   1.00 118.74 ? 120 GLU B O   1 
ATOM   3369 C CB  . GLU B 1 447 ? -0.498  21.271 6.785   1.00 122.35 ? 120 GLU B CB  1 
ATOM   3370 C CG  . GLU B 1 447 ? 0.341   20.285 7.577   1.00 137.72 ? 120 GLU B CG  1 
ATOM   3371 C CD  . GLU B 1 447 ? 0.384   20.610 9.056   1.00 162.74 ? 120 GLU B CD  1 
ATOM   3372 O OE1 . GLU B 1 447 ? -0.413  21.463 9.501   1.00 206.30 ? 120 GLU B OE1 1 
ATOM   3373 O OE2 . GLU B 1 447 ? 1.211   20.009 9.774   1.00 159.65 ? 120 GLU B OE2 1 
ATOM   3374 N N   . LYS B 1 448 ? -1.236  23.022 4.190   1.00 122.21 ? 121 LYS B N   1 
ATOM   3375 C CA  . LYS B 1 448 ? -2.145  23.873 3.426   1.00 120.87 ? 121 LYS B CA  1 
ATOM   3376 C C   . LYS B 1 448 ? -2.637  23.163 2.172   1.00 121.20 ? 121 LYS B C   1 
ATOM   3377 O O   . LYS B 1 448 ? -3.801  23.314 1.777   1.00 122.02 ? 121 LYS B O   1 
ATOM   3378 C CB  . LYS B 1 448 ? -1.462  25.190 3.047   1.00 117.56 ? 121 LYS B CB  1 
ATOM   3379 C CG  . LYS B 1 448 ? -1.347  26.204 4.174   1.00 118.88 ? 121 LYS B CG  1 
ATOM   3380 C CD  . LYS B 1 448 ? -0.532  27.408 3.726   1.00 124.00 ? 121 LYS B CD  1 
ATOM   3381 C CE  . LYS B 1 448 ? -0.042  28.221 4.912   1.00 120.19 ? 121 LYS B CE  1 
ATOM   3382 N NZ  . LYS B 1 448 ? 0.889   29.310 4.499   1.00 133.61 ? 121 LYS B NZ  1 
ATOM   3383 N N   . VAL B 1 449 ? -1.765  22.384 1.530   1.00 117.70 ? 122 VAL B N   1 
ATOM   3384 C CA  . VAL B 1 449 ? -2.201  21.691 0.316   1.00 116.28 ? 122 VAL B CA  1 
ATOM   3385 C C   . VAL B 1 449 ? -3.065  20.472 0.649   1.00 120.98 ? 122 VAL B C   1 
ATOM   3386 O O   . VAL B 1 449 ? -4.101  20.237 0.004   1.00 123.31 ? 122 VAL B O   1 
ATOM   3387 C CB  . VAL B 1 449 ? -0.990  21.319 -0.555  1.00 112.14 ? 122 VAL B CB  1 
ATOM   3388 C CG1 . VAL B 1 449 ? -1.408  20.356 -1.642  1.00 115.24 ? 122 VAL B CG1 1 
ATOM   3389 C CG2 . VAL B 1 449 ? -0.400  22.573 -1.170  1.00 103.22 ? 122 VAL B CG2 1 
ATOM   3390 N N   . ARG B 1 450 ? -2.659  19.678 1.649   1.00 113.19 ? 123 ARG B N   1 
ATOM   3391 C CA  . ARG B 1 450 ? -3.471  18.530 2.054   1.00 120.74 ? 123 ARG B CA  1 
ATOM   3392 C C   . ARG B 1 450 ? -4.893  18.940 2.417   1.00 121.71 ? 123 ARG B C   1 
ATOM   3393 O O   . ARG B 1 450 ? -5.858  18.273 2.019   1.00 123.87 ? 123 ARG B O   1 
ATOM   3394 C CB  . ARG B 1 450 ? -2.841  17.789 3.237   1.00 126.93 ? 123 ARG B CB  1 
ATOM   3395 C CG  . ARG B 1 450 ? -1.791  16.755 2.884   1.00 138.32 ? 123 ARG B CG  1 
ATOM   3396 C CD  . ARG B 1 450 ? -1.457  15.880 4.089   1.00 160.28 ? 123 ARG B CD  1 
ATOM   3397 N NE  . ARG B 1 450 ? -0.421  14.900 3.786   1.00 197.02 ? 123 ARG B NE  1 
ATOM   3398 C CZ  . ARG B 1 450 ? 0.220   14.175 4.693   1.00 234.09 ? 123 ARG B CZ  1 
ATOM   3399 N NH1 . ARG B 1 450 ? -0.044  14.291 5.984   1.00 223.63 ? 123 ARG B NH1 1 
ATOM   3400 N NH2 . ARG B 1 450 ? 1.144   13.305 4.294   1.00 279.44 ? 123 ARG B NH2 1 
ATOM   3401 N N   . SER B 1 451 ? -5.039  20.009 3.205   1.00 124.14 ? 124 SER B N   1 
ATOM   3402 C CA  . SER B 1 451 ? -6.355  20.451 3.657   1.00 122.79 ? 124 SER B CA  1 
ATOM   3403 C C   . SER B 1 451 ? -7.316  20.633 2.488   1.00 129.43 ? 124 SER B C   1 
ATOM   3404 O O   . SER B 1 451 ? -8.424  20.086 2.480   1.00 139.77 ? 124 SER B O   1 
ATOM   3405 C CB  . SER B 1 451 ? -6.221  21.756 4.445   1.00 123.99 ? 124 SER B CB  1 
ATOM   3406 O OG  . SER B 1 451 ? -6.423  22.875 3.598   1.00 119.45 ? 124 SER B OG  1 
ATOM   3407 N N   . GLN B 1 452 ? -6.897  21.402 1.483   1.00 131.12 ? 125 GLN B N   1 
ATOM   3408 C CA  . GLN B 1 452 ? -7.776  21.668 0.353   1.00 130.39 ? 125 GLN B CA  1 
ATOM   3409 C C   . GLN B 1 452 ? -8.014  20.417 -0.475  1.00 130.46 ? 125 GLN B C   1 
ATOM   3410 O O   . GLN B 1 452 ? -9.145  20.161 -0.904  1.00 131.42 ? 125 GLN B O   1 
ATOM   3411 C CB  . GLN B 1 452 ? -7.196  22.771 -0.522  1.00 130.59 ? 125 GLN B CB  1 
ATOM   3412 C CG  . GLN B 1 452 ? -7.050  24.081 0.193   1.00 131.65 ? 125 GLN B CG  1 
ATOM   3413 C CD  . GLN B 1 452 ? -6.564  25.165 -0.726  1.00 137.38 ? 125 GLN B CD  1 
ATOM   3414 O OE1 . GLN B 1 452 ? -7.222  26.186 -0.882  1.00 147.88 ? 125 GLN B OE1 1 
ATOM   3415 N NE2 . GLN B 1 452 ? -5.412  24.950 -1.347  1.00 133.66 ? 125 GLN B NE2 1 
ATOM   3416 N N   . LEU B 1 453 ? -6.970  19.620 -0.715  1.00 129.53 ? 126 LEU B N   1 
ATOM   3417 C CA  . LEU B 1 453 ? -7.151  18.520 -1.656  1.00 130.95 ? 126 LEU B CA  1 
ATOM   3418 C C   . LEU B 1 453 ? -8.034  17.421 -1.079  1.00 140.19 ? 126 LEU B C   1 
ATOM   3419 O O   . LEU B 1 453 ? -8.886  16.879 -1.793  1.00 148.77 ? 126 LEU B O   1 
ATOM   3420 C CB  . LEU B 1 453 ? -5.803  17.961 -2.107  1.00 128.89 ? 126 LEU B CB  1 
ATOM   3421 C CG  . LEU B 1 453 ? -4.971  18.981 -2.883  1.00 124.68 ? 126 LEU B CG  1 
ATOM   3422 C CD1 . LEU B 1 453 ? -3.689  18.350 -3.400  1.00 125.65 ? 126 LEU B CD1 1 
ATOM   3423 C CD2 . LEU B 1 453 ? -5.776  19.626 -4.005  1.00 129.03 ? 126 LEU B CD2 1 
ATOM   3424 N N   . LYS B 1 454 ? -7.867  17.091 0.204   1.00 140.07 ? 127 LYS B N   1 
ATOM   3425 C CA  . LYS B 1 454 ? -8.617  15.997 0.849   1.00 142.51 ? 127 LYS B CA  1 
ATOM   3426 C C   . LYS B 1 454 ? -8.417  14.731 0.014   1.00 148.42 ? 127 LYS B C   1 
ATOM   3427 O O   . LYS B 1 454 ? -7.276  14.421 -0.358  1.00 144.75 ? 127 LYS B O   1 
ATOM   3428 C CB  . LYS B 1 454 ? -10.073 16.391 1.068   1.00 140.21 ? 127 LYS B CB  1 
ATOM   3429 C CG  . LYS B 1 454 ? -10.319 17.616 1.916   1.00 139.24 ? 127 LYS B CG  1 
ATOM   3430 C CD  . LYS B 1 454 ? -11.815 17.892 1.999   1.00 145.46 ? 127 LYS B CD  1 
ATOM   3431 C CE  . LYS B 1 454 ? -12.126 19.030 2.952   1.00 137.40 ? 127 LYS B CE  1 
ATOM   3432 N NZ  . LYS B 1 454 ? -13.591 19.278 3.053   1.00 140.89 ? 127 LYS B NZ  1 
ATOM   3433 N N   . ASN B 1 455 ? -9.475  13.990 -0.310  1.00 161.09 ? 128 ASN B N   1 
ATOM   3434 C CA  . ASN B 1 455 ? -9.366  12.728 -1.027  1.00 167.10 ? 128 ASN B CA  1 
ATOM   3435 C C   . ASN B 1 455 ? -9.449  12.886 -2.538  1.00 159.47 ? 128 ASN B C   1 
ATOM   3436 O O   . ASN B 1 455 ? -9.432  11.878 -3.251  1.00 157.69 ? 128 ASN B O   1 
ATOM   3437 C CB  . ASN B 1 455 ? -10.450 11.757 -0.550  1.00 177.00 ? 128 ASN B CB  1 
ATOM   3438 C CG  . ASN B 1 455 ? -10.191 11.243 0.852   1.00 198.89 ? 128 ASN B CG  1 
ATOM   3439 O OD1 . ASN B 1 455 ? -9.117  11.452 1.414   1.00 193.25 ? 128 ASN B OD1 1 
ATOM   3440 N ND2 . ASN B 1 455 ? -11.184 10.577 1.430   1.00 222.44 ? 128 ASN B ND2 1 
ATOM   3441 N N   . ASN B 1 456 ? -9.539  14.118 -3.046  1.00 153.46 ? 129 ASN B N   1 
ATOM   3442 C CA  . ASN B 1 456 ? -9.388  14.346 -4.479  1.00 150.39 ? 129 ASN B CA  1 
ATOM   3443 C C   . ASN B 1 456 ? -7.969  14.091 -4.965  1.00 148.54 ? 129 ASN B C   1 
ATOM   3444 O O   . ASN B 1 456 ? -7.733  14.136 -6.177  1.00 142.72 ? 129 ASN B O   1 
ATOM   3445 C CB  . ASN B 1 456 ? -9.793  15.774 -4.840  1.00 151.70 ? 129 ASN B CB  1 
ATOM   3446 C CG  . ASN B 1 456 ? -11.280 16.009 -4.715  1.00 159.88 ? 129 ASN B CG  1 
ATOM   3447 O OD1 . ASN B 1 456 ? -12.051 15.070 -4.514  1.00 163.67 ? 129 ASN B OD1 1 
ATOM   3448 N ND2 . ASN B 1 456 ? -11.694 17.265 -4.817  1.00 160.79 ? 129 ASN B ND2 1 
ATOM   3449 N N   . ALA B 1 457 ? -7.027  13.826 -4.062  1.00 146.26 ? 130 ALA B N   1 
ATOM   3450 C CA  . ALA B 1 457 ? -5.636  13.608 -4.424  1.00 140.18 ? 130 ALA B CA  1 
ATOM   3451 C C   . ALA B 1 457 ? -5.059  12.483 -3.576  1.00 137.20 ? 130 ALA B C   1 
ATOM   3452 O O   . ALA B 1 457 ? -5.623  12.099 -2.548  1.00 136.59 ? 130 ALA B O   1 
ATOM   3453 C CB  . ALA B 1 457 ? -4.802  14.884 -4.251  1.00 133.05 ? 130 ALA B CB  1 
ATOM   3454 N N   . LYS B 1 458 ? -3.912  11.961 -4.019  1.00 139.72 ? 131 LYS B N   1 
ATOM   3455 C CA  . LYS B 1 458 ? -3.227  10.879 -3.266  1.00 142.82 ? 131 LYS B CA  1 
ATOM   3456 C C   . LYS B 1 458 ? -1.773  11.300 -3.038  1.00 141.72 ? 131 LYS B C   1 
ATOM   3457 O O   . LYS B 1 458 ? -1.097  11.641 -4.029  1.00 137.95 ? 131 LYS B O   1 
ATOM   3458 C CB  . LYS B 1 458 ? -3.283  9.571  -4.058  1.00 142.12 ? 131 LYS B CB  1 
ATOM   3459 C CG  . LYS B 1 458 ? -2.676  8.361  -3.361  1.00 143.89 ? 131 LYS B CG  1 
ATOM   3460 C CD  . LYS B 1 458 ? -2.792  7.075  -4.154  1.00 145.56 ? 131 LYS B CD  1 
ATOM   3461 C CE  . LYS B 1 458 ? -2.167  5.875  -3.473  1.00 148.63 ? 131 LYS B CE  1 
ATOM   3462 N NZ  . LYS B 1 458 ? -2.304  4.641  -4.282  1.00 154.74 ? 131 LYS B NZ  1 
ATOM   3463 N N   . GLU B 1 459 ? -1.317  11.276 -1.783  1.00 145.93 ? 132 GLU B N   1 
ATOM   3464 C CA  . GLU B 1 459 ? 0.077   11.686 -1.467  1.00 144.54 ? 132 GLU B CA  1 
ATOM   3465 C C   . GLU B 1 459 ? 1.032   10.644 -2.056  1.00 145.79 ? 132 GLU B C   1 
ATOM   3466 O O   . GLU B 1 459 ? 1.163   9.560  -1.456  1.00 138.33 ? 132 GLU B O   1 
ATOM   3467 C CB  . GLU B 1 459 ? 0.269   11.836 0.044   1.00 150.59 ? 132 GLU B CB  1 
ATOM   3468 C CG  . GLU B 1 459 ? -0.510  12.993 0.646   1.00 159.41 ? 132 GLU B CG  1 
ATOM   3469 C CD  . GLU B 1 459 ? -2.009  12.774 0.760   1.00 162.66 ? 132 GLU B CD  1 
ATOM   3470 O OE1 . GLU B 1 459 ? -2.414  11.825 1.460   1.00 161.16 ? 132 GLU B OE1 1 
ATOM   3471 O OE2 . GLU B 1 459 ? -2.767  13.549 0.145   1.00 164.07 ? 132 GLU B OE2 1 
ATOM   3472 N N   . ILE B 1 460 ? 1.666   10.964 -3.189  1.00 144.64 ? 133 ILE B N   1 
ATOM   3473 C CA  . ILE B 1 460 ? 2.576   9.994  -3.869  1.00 149.73 ? 133 ILE B CA  1 
ATOM   3474 C C   . ILE B 1 460 ? 3.746   9.676  -2.935  1.00 147.67 ? 133 ILE B C   1 
ATOM   3475 O O   . ILE B 1 460 ? 4.045   8.480  -2.751  1.00 152.99 ? 133 ILE B O   1 
ATOM   3476 C CB  . ILE B 1 460 ? 3.070   10.573 -5.208  1.00 150.16 ? 133 ILE B CB  1 
ATOM   3477 C CG1 . ILE B 1 460 ? 1.964   11.338 -5.939  1.00 150.25 ? 133 ILE B CG1 1 
ATOM   3478 C CG2 . ILE B 1 460 ? 3.678   9.483  -6.078  1.00 153.54 ? 133 ILE B CG2 1 
ATOM   3479 C CD1 . ILE B 1 460 ? 2.434   12.038 -7.190  1.00 152.99 ? 133 ILE B CD1 1 
ATOM   3480 N N   . GLY B 1 461 ? 4.380   10.710 -2.376  1.00 153.30 ? 134 GLY B N   1 
ATOM   3481 C CA  . GLY B 1 461 ? 5.533   10.510 -1.478  1.00 154.81 ? 134 GLY B CA  1 
ATOM   3482 C C   . GLY B 1 461 ? 6.204   11.832 -1.154  1.00 156.64 ? 134 GLY B C   1 
ATOM   3483 O O   . GLY B 1 461 ? 5.988   12.799 -1.911  1.00 152.56 ? 134 GLY B O   1 
ATOM   3484 N N   . ASN B 1 462 ? 6.981   11.877 -0.067  1.00 165.16 ? 135 ASN B N   1 
ATOM   3485 C CA  . ASN B 1 462 ? 7.636   13.144 0.356   1.00 165.16 ? 135 ASN B CA  1 
ATOM   3486 C C   . ASN B 1 462 ? 6.472   14.128 0.207   1.00 159.84 ? 135 ASN B C   1 
ATOM   3487 O O   . ASN B 1 462 ? 5.398   13.862 0.782   1.00 173.34 ? 135 ASN B O   1 
ATOM   3488 C CB  . ASN B 1 462 ? 8.828   13.500 -0.536  1.00 162.47 ? 135 ASN B CB  1 
ATOM   3489 C CG  . ASN B 1 462 ? 9.983   12.533 -0.391  1.00 171.25 ? 135 ASN B CG  1 
ATOM   3490 O OD1 . ASN B 1 462 ? 9.902   11.571 0.369   1.00 177.45 ? 135 ASN B OD1 1 
ATOM   3491 N ND2 . ASN B 1 462 ? 11.063  12.780 -1.114  1.00 169.93 ? 135 ASN B ND2 1 
ATOM   3492 N N   . GLY B 1 463 ? 6.683   15.219 -0.535  1.00 154.31 ? 136 GLY B N   1 
ATOM   3493 C CA  . GLY B 1 463 ? 5.630   16.239 -0.701  1.00 148.68 ? 136 GLY B CA  1 
ATOM   3494 C C   . GLY B 1 463 ? 4.852   16.285 -2.003  1.00 139.02 ? 136 GLY B C   1 
ATOM   3495 O O   . GLY B 1 463 ? 4.563   17.404 -2.467  1.00 132.59 ? 136 GLY B O   1 
ATOM   3496 N N   . CYS B 1 464 ? 4.510   15.124 -2.570  1.00 136.96 ? 137 CYS B N   1 
ATOM   3497 C CA  . CYS B 1 464 ? 3.834   15.121 -3.897  1.00 135.26 ? 137 CYS B CA  1 
ATOM   3498 C C   . CYS B 1 464 ? 2.372   14.678 -3.775  1.00 139.28 ? 137 CYS B C   1 
ATOM   3499 O O   . CYS B 1 464 ? 2.077   13.862 -2.881  1.00 143.80 ? 137 CYS B O   1 
ATOM   3500 C CB  . CYS B 1 464 ? 4.579   14.251 -4.906  1.00 148.08 ? 137 CYS B CB  1 
ATOM   3501 S SG  . CYS B 1 464 ? 6.124   14.991 -5.503  1.00 188.78 ? 137 CYS B SG  1 
ATOM   3502 N N   . PHE B 1 465 ? 1.502   15.200 -4.641  1.00 133.73 ? 138 PHE B N   1 
ATOM   3503 C CA  . PHE B 1 465 ? 0.079   14.891 -4.657  1.00 131.98 ? 138 PHE B CA  1 
ATOM   3504 C C   . PHE B 1 465 ? -0.274  14.528 -6.088  1.00 132.28 ? 138 PHE B C   1 
ATOM   3505 O O   . PHE B 1 465 ? 0.009   15.303 -7.005  1.00 131.39 ? 138 PHE B O   1 
ATOM   3506 C CB  . PHE B 1 465 ? -0.761  16.103 -4.244  1.00 123.17 ? 138 PHE B CB  1 
ATOM   3507 C CG  . PHE B 1 465 ? -0.609  16.489 -2.810  1.00 125.70 ? 138 PHE B CG  1 
ATOM   3508 C CD1 . PHE B 1 465 ? 0.448   17.282 -2.403  1.00 125.70 ? 138 PHE B CD1 1 
ATOM   3509 C CD2 . PHE B 1 465 ? -1.531  16.070 -1.868  1.00 136.87 ? 138 PHE B CD2 1 
ATOM   3510 C CE1 . PHE B 1 465 ? 0.586   17.644 -1.086  1.00 132.58 ? 138 PHE B CE1 1 
ATOM   3511 C CE2 . PHE B 1 465 ? -1.398  16.432 -0.550  1.00 141.60 ? 138 PHE B CE2 1 
ATOM   3512 C CZ  . PHE B 1 465 ? -0.338  17.219 -0.157  1.00 139.99 ? 138 PHE B CZ  1 
ATOM   3513 N N   . GLU B 1 466 ? -0.896  13.369 -6.286  1.00 136.90 ? 139 GLU B N   1 
ATOM   3514 C CA  . GLU B 1 466 ? -1.464  13.012 -7.587  1.00 135.49 ? 139 GLU B CA  1 
ATOM   3515 C C   . GLU B 1 466 ? -2.962  13.261 -7.484  1.00 136.67 ? 139 GLU B C   1 
ATOM   3516 O O   . GLU B 1 466 ? -3.679  12.529 -6.797  1.00 139.56 ? 139 GLU B O   1 
ATOM   3517 C CB  . GLU B 1 466 ? -1.163  11.568 -7.975  1.00 142.94 ? 139 GLU B CB  1 
ATOM   3518 C CG  . GLU B 1 466 ? -1.706  11.205 -9.356  1.00 148.98 ? 139 GLU B CG  1 
ATOM   3519 C CD  . GLU B 1 466 ? -1.374  9.787  -9.778  1.00 154.07 ? 139 GLU B CD  1 
ATOM   3520 O OE1 . GLU B 1 466 ? -0.747  9.060  -8.979  1.00 155.60 ? 139 GLU B OE1 1 
ATOM   3521 O OE2 . GLU B 1 466 ? -1.740  9.399  -10.908 1.00 150.27 ? 139 GLU B OE2 1 
ATOM   3522 N N   . PHE B 1 467 ? -3.433  14.305 -8.163  1.00 139.94 ? 140 PHE B N   1 
ATOM   3523 C CA  . PHE B 1 467 ? -4.868  14.515 -8.284  1.00 142.31 ? 140 PHE B CA  1 
ATOM   3524 C C   . PHE B 1 467 ? -5.541  13.308 -8.922  1.00 142.50 ? 140 PHE B C   1 
ATOM   3525 O O   . PHE B 1 467 ? -5.008  12.702 -9.855  1.00 141.80 ? 140 PHE B O   1 
ATOM   3526 C CB  . PHE B 1 467 ? -5.092  15.744 -9.168  1.00 143.04 ? 140 PHE B CB  1 
ATOM   3527 C CG  . PHE B 1 467 ? -4.527  17.017 -8.610  1.00 138.93 ? 140 PHE B CG  1 
ATOM   3528 C CD1 . PHE B 1 467 ? -5.172  17.685 -7.584  1.00 138.42 ? 140 PHE B CD1 1 
ATOM   3529 C CD2 . PHE B 1 467 ? -3.365  17.560 -9.130  1.00 131.87 ? 140 PHE B CD2 1 
ATOM   3530 C CE1 . PHE B 1 467 ? -4.660  18.862 -7.081  1.00 131.13 ? 140 PHE B CE1 1 
ATOM   3531 C CE2 . PHE B 1 467 ? -2.848  18.738 -8.626  1.00 136.82 ? 140 PHE B CE2 1 
ATOM   3532 C CZ  . PHE B 1 467 ? -3.498  19.390 -7.599  1.00 132.08 ? 140 PHE B CZ  1 
ATOM   3533 N N   . TYR B 1 468 ? -6.716  12.948 -8.406  1.00 144.02 ? 141 TYR B N   1 
ATOM   3534 C CA  . TYR B 1 468 ? -7.557  12.006 -9.129  1.00 148.39 ? 141 TYR B CA  1 
ATOM   3535 C C   . TYR B 1 468 ? -8.302  12.680 -10.270 1.00 149.48 ? 141 TYR B C   1 
ATOM   3536 O O   . TYR B 1 468 ? -8.690  12.004 -11.228 1.00 154.12 ? 141 TYR B O   1 
ATOM   3537 C CB  . TYR B 1 468 ? -8.565  11.345 -8.193  1.00 155.39 ? 141 TYR B CB  1 
ATOM   3538 C CG  . TYR B 1 468 ? -7.977  10.429 -7.149  1.00 154.41 ? 141 TYR B CG  1 
ATOM   3539 C CD1 . TYR B 1 468 ? -7.389  9.223  -7.505  1.00 155.59 ? 141 TYR B CD1 1 
ATOM   3540 C CD2 . TYR B 1 468 ? -8.031  10.760 -5.802  1.00 152.26 ? 141 TYR B CD2 1 
ATOM   3541 C CE1 . TYR B 1 468 ? -6.859  8.379  -6.548  1.00 152.28 ? 141 TYR B CE1 1 
ATOM   3542 C CE2 . TYR B 1 468 ? -7.504  9.923  -4.839  1.00 148.71 ? 141 TYR B CE2 1 
ATOM   3543 C CZ  . TYR B 1 468 ? -6.919  8.735  -5.216  1.00 148.64 ? 141 TYR B CZ  1 
ATOM   3544 O OH  . TYR B 1 468 ? -6.395  7.903  -4.254  1.00 151.44 ? 141 TYR B OH  1 
ATOM   3545 N N   . HIS B 1 469 ? -8.509  13.990 -10.182 1.00 145.23 ? 142 HIS B N   1 
ATOM   3546 C CA  . HIS B 1 469 ? -9.103  14.785 -11.243 1.00 146.79 ? 142 HIS B CA  1 
ATOM   3547 C C   . HIS B 1 469 ? -8.003  15.467 -12.055 1.00 148.06 ? 142 HIS B C   1 
ATOM   3548 O O   . HIS B 1 469 ? -6.809  15.241 -11.851 1.00 147.18 ? 142 HIS B O   1 
ATOM   3549 C CB  . HIS B 1 469 ? -10.081 15.804 -10.655 1.00 152.56 ? 142 HIS B CB  1 
ATOM   3550 C CG  . HIS B 1 469 ? -9.443  16.783 -9.717  1.00 155.36 ? 142 HIS B CG  1 
ATOM   3551 N ND1 . HIS B 1 469 ? -9.197  18.094 -10.062 1.00 161.55 ? 142 HIS B ND1 1 
ATOM   3552 C CD2 . HIS B 1 469 ? -9.013  16.644 -8.440  1.00 150.16 ? 142 HIS B CD2 1 
ATOM   3553 C CE1 . HIS B 1 469 ? -8.637  18.719 -9.041  1.00 161.25 ? 142 HIS B CE1 1 
ATOM   3554 N NE2 . HIS B 1 469 ? -8.514  17.861 -8.044  1.00 156.15 ? 142 HIS B NE2 1 
ATOM   3555 N N   . LYS B 1 470 ? -8.412  16.314 -12.995 1.00 143.81 ? 143 LYS B N   1 
ATOM   3556 C CA  . LYS B 1 470 ? -7.484  17.031 -13.858 1.00 144.44 ? 143 LYS B CA  1 
ATOM   3557 C C   . LYS B 1 470 ? -7.459  18.505 -13.480 1.00 141.48 ? 143 LYS B C   1 
ATOM   3558 O O   . LYS B 1 470 ? -8.508  19.117 -13.262 1.00 145.55 ? 143 LYS B O   1 
ATOM   3559 C CB  . LYS B 1 470 ? -7.867  16.865 -15.330 1.00 145.93 ? 143 LYS B CB  1 
ATOM   3560 C CG  . LYS B 1 470 ? -7.607  15.469 -15.859 1.00 153.03 ? 143 LYS B CG  1 
ATOM   3561 C CD  . LYS B 1 470 ? -8.053  15.323 -17.298 1.00 160.93 ? 143 LYS B CD  1 
ATOM   3562 C CE  . LYS B 1 470 ? -7.970  13.873 -17.739 1.00 171.95 ? 143 LYS B CE  1 
ATOM   3563 N NZ  . LYS B 1 470 ? -8.474  13.683 -19.125 1.00 180.37 ? 143 LYS B NZ  1 
ATOM   3564 N N   . CYS B 1 471 ? -6.256  19.069 -13.404 1.00 152.10 ? 144 CYS B N   1 
ATOM   3565 C CA  . CYS B 1 471 ? -6.049  20.439 -12.950 1.00 144.59 ? 144 CYS B CA  1 
ATOM   3566 C C   . CYS B 1 471 ? -5.439  21.259 -14.075 1.00 147.29 ? 144 CYS B C   1 
ATOM   3567 O O   . CYS B 1 471 ? -4.389  20.896 -14.611 1.00 138.28 ? 144 CYS B O   1 
ATOM   3568 C CB  . CYS B 1 471 ? -5.138  20.482 -11.719 1.00 139.75 ? 144 CYS B CB  1 
ATOM   3569 S SG  . CYS B 1 471 ? -5.981  20.575 -10.124 1.00 136.44 ? 144 CYS B SG  1 
ATOM   3570 N N   . ASP B 1 472 ? -6.097  22.357 -14.434 1.00 150.78 ? 145 ASP B N   1 
ATOM   3571 C CA  . ASP B 1 472 ? -5.448  23.370 -15.246 1.00 152.42 ? 145 ASP B CA  1 
ATOM   3572 C C   . ASP B 1 472 ? -4.441  24.128 -14.386 1.00 149.08 ? 145 ASP B C   1 
ATOM   3573 O O   . ASP B 1 472 ? -4.357  23.931 -13.170 1.00 156.31 ? 145 ASP B O   1 
ATOM   3574 C CB  . ASP B 1 472 ? -6.475  24.343 -15.821 1.00 150.90 ? 145 ASP B CB  1 
ATOM   3575 C CG  . ASP B 1 472 ? -7.529  23.657 -16.661 1.00 159.93 ? 145 ASP B CG  1 
ATOM   3576 O OD1 . ASP B 1 472 ? -7.436  22.429 -16.863 1.00 191.03 ? 145 ASP B OD1 1 
ATOM   3577 O OD2 . ASP B 1 472 ? -8.466  24.354 -17.110 1.00 163.37 ? 145 ASP B OD2 1 
ATOM   3578 N N   . ASN B 1 473 ? -3.674  25.021 -15.017 1.00 152.91 ? 146 ASN B N   1 
ATOM   3579 C CA  . ASN B 1 473 ? -2.935  25.978 -14.202 1.00 160.03 ? 146 ASN B CA  1 
ATOM   3580 C C   . ASN B 1 473 ? -3.892  26.929 -13.497 1.00 153.76 ? 146 ASN B C   1 
ATOM   3581 O O   . ASN B 1 473 ? -3.512  27.548 -12.499 1.00 157.37 ? 146 ASN B O   1 
ATOM   3582 C CB  . ASN B 1 473 ? -1.924  26.767 -15.037 1.00 155.97 ? 146 ASN B CB  1 
ATOM   3583 C CG  . ASN B 1 473 ? -0.932  27.540 -14.180 1.00 154.23 ? 146 ASN B CG  1 
ATOM   3584 O OD1 . ASN B 1 473 ? -0.193  26.956 -13.387 1.00 137.87 ? 146 ASN B OD1 1 
ATOM   3585 N ND2 . ASN B 1 473 ? -0.912  28.860 -14.338 1.00 184.36 ? 146 ASN B ND2 1 
ATOM   3586 N N   . THR B 1 474 ? -5.128  27.048 -13.988 1.00 143.40 ? 147 THR B N   1 
ATOM   3587 C CA  . THR B 1 474 ? -6.166  27.701 -13.204 1.00 144.59 ? 147 THR B CA  1 
ATOM   3588 C C   . THR B 1 474 ? -6.477  26.887 -11.954 1.00 149.63 ? 147 THR B C   1 
ATOM   3589 O O   . THR B 1 474 ? -6.482  27.421 -10.842 1.00 152.96 ? 147 THR B O   1 
ATOM   3590 C CB  . THR B 1 474 ? -7.424  27.900 -14.051 1.00 144.72 ? 147 THR B CB  1 
ATOM   3591 O OG1 . THR B 1 474 ? -7.975  26.629 -14.416 1.00 147.91 ? 147 THR B OG1 1 
ATOM   3592 C CG2 . THR B 1 474 ? -7.099  28.671 -15.321 1.00 145.60 ? 147 THR B CG2 1 
ATOM   3593 N N   . CYS B 1 475 ? -6.688  25.577 -12.111 1.00 146.45 ? 148 CYS B N   1 
ATOM   3594 C CA  . CYS B 1 475 ? -6.971  24.728 -10.958 1.00 147.91 ? 148 CYS B CA  1 
ATOM   3595 C C   . CYS B 1 475 ? -5.733  24.462 -10.108 1.00 145.51 ? 148 CYS B C   1 
ATOM   3596 O O   . CYS B 1 475 ? -5.872  24.051 -8.950  1.00 144.48 ? 148 CYS B O   1 
ATOM   3597 C CB  . CYS B 1 475 ? -7.592  23.406 -11.414 1.00 155.21 ? 148 CYS B CB  1 
ATOM   3598 S SG  . CYS B 1 475 ? -9.365  23.492 -11.761 1.00 192.35 ? 148 CYS B SG  1 
ATOM   3599 N N   . MET B 1 476 ? -4.533  24.680 -10.653 1.00 144.66 ? 149 MET B N   1 
ATOM   3600 C CA  . MET B 1 476 ? -3.307  24.613 -9.859  1.00 141.87 ? 149 MET B CA  1 
ATOM   3601 C C   . MET B 1 476 ? -3.131  25.878 -9.022  1.00 146.09 ? 149 MET B C   1 
ATOM   3602 O O   . MET B 1 476 ? -2.947  25.821 -7.797  1.00 149.37 ? 149 MET B O   1 
ATOM   3603 C CB  . MET B 1 476 ? -2.095  24.423 -10.779 1.00 142.28 ? 149 MET B CB  1 
ATOM   3604 C CG  . MET B 1 476 ? -1.942  23.044 -11.413 1.00 142.16 ? 149 MET B CG  1 
ATOM   3605 S SD  . MET B 1 476 ? -1.684  21.706 -10.238 1.00 134.60 ? 149 MET B SD  1 
ATOM   3606 C CE  . MET B 1 476 ? -1.282  20.363 -11.352 1.00 129.33 ? 149 MET B CE  1 
ATOM   3607 N N   . GLU B 1 477 ? -3.172  27.037 -9.680  1.00 146.03 ? 150 GLU B N   1 
ATOM   3608 C CA  . GLU B 1 477 ? -3.070  28.313 -8.992  1.00 141.38 ? 150 GLU B CA  1 
ATOM   3609 C C   . GLU B 1 477 ? -4.281  28.589 -8.112  1.00 142.83 ? 150 GLU B C   1 
ATOM   3610 O O   . GLU B 1 477 ? -4.242  29.530 -7.319  1.00 141.82 ? 150 GLU B O   1 
ATOM   3611 C CB  . GLU B 1 477 ? -2.864  29.420 -10.029 1.00 147.62 ? 150 GLU B CB  1 
ATOM   3612 C CG  . GLU B 1 477 ? -1.459  29.399 -10.640 1.00 152.06 ? 150 GLU B CG  1 
ATOM   3613 C CD  . GLU B 1 477 ? -1.183  30.564 -11.571 1.00 166.60 ? 150 GLU B CD  1 
ATOM   3614 O OE1 . GLU B 1 477 ? -2.069  31.428 -11.739 1.00 177.10 ? 150 GLU B OE1 1 
ATOM   3615 O OE2 . GLU B 1 477 ? -0.075  30.604 -12.149 1.00 157.23 ? 150 GLU B OE2 1 
ATOM   3616 N N   . SER B 1 478 ? -5.342  27.788 -8.226  1.00 145.92 ? 151 SER B N   1 
ATOM   3617 C CA  . SER B 1 478 ? -6.385  27.789 -7.207  1.00 153.56 ? 151 SER B CA  1 
ATOM   3618 C C   . SER B 1 478 ? -5.856  27.220 -5.898  1.00 152.58 ? 151 SER B C   1 
ATOM   3619 O O   . SER B 1 478 ? -6.025  27.825 -4.831  1.00 156.35 ? 151 SER B O   1 
ATOM   3620 C CB  . SER B 1 478 ? -7.591  26.983 -7.691  1.00 154.73 ? 151 SER B CB  1 
ATOM   3621 O OG  . SER B 1 478 ? -7.295  25.596 -7.733  1.00 153.63 ? 151 SER B OG  1 
ATOM   3622 N N   . VAL B 1 479 ? -5.212  26.051 -5.963  1.00 142.25 ? 152 VAL B N   1 
ATOM   3623 C CA  . VAL B 1 479 ? -4.613  25.460 -4.769  1.00 141.99 ? 152 VAL B CA  1 
ATOM   3624 C C   . VAL B 1 479 ? -3.573  26.406 -4.184  1.00 138.20 ? 152 VAL B C   1 
ATOM   3625 O O   . VAL B 1 479 ? -3.560  26.675 -2.977  1.00 135.86 ? 152 VAL B O   1 
ATOM   3626 C CB  . VAL B 1 479 ? -3.999  24.086 -5.097  1.00 137.03 ? 152 VAL B CB  1 
ATOM   3627 C CG1 . VAL B 1 479 ? -3.365  23.476 -3.851  1.00 133.82 ? 152 VAL B CG1 1 
ATOM   3628 C CG2 . VAL B 1 479 ? -5.048  23.150 -5.684  1.00 138.86 ? 152 VAL B CG2 1 
ATOM   3629 N N   . LYS B 1 480 ? -2.689  26.932 -5.039  1.00 137.78 ? 153 LYS B N   1 
ATOM   3630 C CA  . LYS B 1 480 ? -1.666  27.859 -4.550  1.00 128.25 ? 153 LYS B CA  1 
ATOM   3631 C C   . LYS B 1 480 ? -2.292  29.121 -3.967  1.00 135.31 ? 153 LYS B C   1 
ATOM   3632 O O   . LYS B 1 480 ? -1.886  29.590 -2.897  1.00 124.78 ? 153 LYS B O   1 
ATOM   3633 C CB  . LYS B 1 480 ? -0.674  28.232 -5.653  1.00 123.61 ? 153 LYS B CB  1 
ATOM   3634 C CG  . LYS B 1 480 ? -0.053  27.067 -6.404  1.00 119.88 ? 153 LYS B CG  1 
ATOM   3635 C CD  . LYS B 1 480 ? 0.840   27.590 -7.528  1.00 120.30 ? 153 LYS B CD  1 
ATOM   3636 C CE  . LYS B 1 480 ? 1.243   26.493 -8.503  1.00 118.52 ? 153 LYS B CE  1 
ATOM   3637 N NZ  . LYS B 1 480 ? 1.719   27.052 -9.804  1.00 113.86 ? 153 LYS B NZ  1 
ATOM   3638 N N   . ASN B 1 481 ? -3.285  29.683 -4.657  1.00 149.02 ? 154 ASN B N   1 
ATOM   3639 C CA  . ASN B 1 481 ? -4.033  30.843 -4.192  1.00 150.65 ? 154 ASN B CA  1 
ATOM   3640 C C   . ASN B 1 481 ? -4.893  30.538 -2.973  1.00 148.24 ? 154 ASN B C   1 
ATOM   3641 O O   . ASN B 1 481 ? -5.429  31.469 -2.362  1.00 151.58 ? 154 ASN B O   1 
ATOM   3642 C CB  . ASN B 1 481 ? -4.900  31.370 -5.343  1.00 151.80 ? 154 ASN B CB  1 
ATOM   3643 C CG  . ASN B 1 481 ? -5.530  32.715 -5.043  1.00 165.09 ? 154 ASN B CG  1 
ATOM   3644 O OD1 . ASN B 1 481 ? -4.924  33.572 -4.402  1.00 172.55 ? 154 ASN B OD1 1 
ATOM   3645 N ND2 . ASN B 1 481 ? -6.749  32.915 -5.531  1.00 159.59 ? 154 ASN B ND2 1 
ATOM   3646 N N   . GLY B 1 482 ? -5.028  29.269 -2.597  1.00 146.01 ? 155 GLY B N   1 
ATOM   3647 C CA  . GLY B 1 482 ? -5.852  28.918 -1.461  1.00 148.89 ? 155 GLY B CA  1 
ATOM   3648 C C   . GLY B 1 482 ? -7.331  28.901 -1.757  1.00 151.58 ? 155 GLY B C   1 
ATOM   3649 O O   . GLY B 1 482 ? -8.143  29.100 -0.845  1.00 155.66 ? 155 GLY B O   1 
ATOM   3650 N N   . THR B 1 483 ? -7.710  28.649 -3.012  1.00 159.36 ? 156 THR B N   1 
ATOM   3651 C CA  . THR B 1 483 ? -9.101  28.729 -3.439  1.00 154.54 ? 156 THR B CA  1 
ATOM   3652 C C   . THR B 1 483 ? -9.596  27.447 -4.104  1.00 160.63 ? 156 THR B C   1 
ATOM   3653 O O   . THR B 1 483 ? -10.611 27.475 -4.808  1.00 167.21 ? 156 THR B O   1 
ATOM   3654 C CB  . THR B 1 483 ? -9.296  29.918 -4.384  1.00 153.67 ? 156 THR B CB  1 
ATOM   3655 O OG1 . THR B 1 483 ? -8.533  29.715 -5.580  1.00 147.31 ? 156 THR B OG1 1 
ATOM   3656 C CG2 . THR B 1 483 ? -8.862  31.218 -3.716  1.00 154.21 ? 156 THR B CG2 1 
ATOM   3657 N N   . TYR B 1 484 ? -8.915  26.323 -3.898  1.00 148.00 ? 157 TYR B N   1 
ATOM   3658 C CA  . TYR B 1 484 ? -9.387  25.061 -4.454  1.00 153.56 ? 157 TYR B CA  1 
ATOM   3659 C C   . TYR B 1 484 ? -10.586 24.553 -3.662  1.00 159.90 ? 157 TYR B C   1 
ATOM   3660 O O   . TYR B 1 484 ? -10.563 24.530 -2.429  1.00 158.25 ? 157 TYR B O   1 
ATOM   3661 C CB  . TYR B 1 484 ? -8.267  24.023 -4.440  1.00 146.14 ? 157 TYR B CB  1 
ATOM   3662 C CG  . TYR B 1 484 ? -8.713  22.627 -4.811  1.00 152.34 ? 157 TYR B CG  1 
ATOM   3663 C CD1 . TYR B 1 484 ? -9.063  22.314 -6.118  1.00 152.86 ? 157 TYR B CD1 1 
ATOM   3664 C CD2 . TYR B 1 484 ? -8.783  21.622 -3.855  1.00 153.72 ? 157 TYR B CD2 1 
ATOM   3665 C CE1 . TYR B 1 484 ? -9.468  21.039 -6.461  1.00 150.77 ? 157 TYR B CE1 1 
ATOM   3666 C CE2 . TYR B 1 484 ? -9.189  20.345 -4.189  1.00 149.80 ? 157 TYR B CE2 1 
ATOM   3667 C CZ  . TYR B 1 484 ? -9.529  20.059 -5.494  1.00 148.97 ? 157 TYR B CZ  1 
ATOM   3668 O OH  . TYR B 1 484 ? -9.933  18.789 -5.835  1.00 153.22 ? 157 TYR B OH  1 
ATOM   3669 N N   . ASP B 1 485 ? -11.637 24.145 -4.370  1.00 167.97 ? 158 ASP B N   1 
ATOM   3670 C CA  . ASP B 1 485 ? -12.870 23.668 -3.753  1.00 171.04 ? 158 ASP B CA  1 
ATOM   3671 C C   . ASP B 1 485 ? -12.961 22.156 -3.901  1.00 169.79 ? 158 ASP B C   1 
ATOM   3672 O O   . ASP B 1 485 ? -12.875 21.630 -5.018  1.00 166.40 ? 158 ASP B O   1 
ATOM   3673 C CB  . ASP B 1 485 ? -14.095 24.337 -4.376  1.00 176.66 ? 158 ASP B CB  1 
ATOM   3674 C CG  . ASP B 1 485 ? -14.050 25.848 -4.275  1.00 183.79 ? 158 ASP B CG  1 
ATOM   3675 O OD1 . ASP B 1 485 ? -13.046 26.381 -3.761  1.00 193.00 ? 158 ASP B OD1 1 
ATOM   3676 O OD2 . ASP B 1 485 ? -15.018 26.507 -4.713  1.00 198.66 ? 158 ASP B OD2 1 
ATOM   3677 N N   . TYR B 1 486 ? -13.136 21.466 -2.772  1.00 165.30 ? 159 TYR B N   1 
ATOM   3678 C CA  . TYR B 1 486 ? -13.306 20.013 -2.800  1.00 165.17 ? 159 TYR B CA  1 
ATOM   3679 C C   . TYR B 1 486 ? -14.484 19.562 -3.659  1.00 174.33 ? 159 TYR B C   1 
ATOM   3680 O O   . TYR B 1 486 ? -14.294 18.645 -4.479  1.00 188.83 ? 159 TYR B O   1 
ATOM   3681 C CB  . TYR B 1 486 ? -13.436 19.476 -1.368  1.00 157.72 ? 159 TYR B CB  1 
ATOM   3682 C CG  . TYR B 1 486 ? -13.479 17.966 -1.294  1.00 160.77 ? 159 TYR B CG  1 
ATOM   3683 C CD1 . TYR B 1 486 ? -12.387 17.196 -1.677  1.00 153.62 ? 159 TYR B CD1 1 
ATOM   3684 C CD2 . TYR B 1 486 ? -14.637 17.307 -0.904  1.00 165.28 ? 159 TYR B CD2 1 
ATOM   3685 C CE1 . TYR B 1 486 ? -12.439 15.814 -1.627  1.00 158.30 ? 159 TYR B CE1 1 
ATOM   3686 C CE2 . TYR B 1 486 ? -14.699 15.928 -0.858  1.00 167.09 ? 159 TYR B CE2 1 
ATOM   3687 C CZ  . TYR B 1 486 ? -13.598 15.187 -1.222  1.00 162.64 ? 159 TYR B CZ  1 
ATOM   3688 O OH  . TYR B 1 486 ? -13.639 13.813 -1.184  1.00 163.36 ? 159 TYR B OH  1 
ATOM   3689 N N   . PRO B 1 487 ? -15.696 20.138 -3.551  1.00 179.32 ? 160 PRO B N   1 
ATOM   3690 C CA  . PRO B 1 487 ? -16.847 19.566 -4.279  1.00 178.53 ? 160 PRO B CA  1 
ATOM   3691 C C   . PRO B 1 487 ? -16.707 19.581 -5.791  1.00 176.80 ? 160 PRO B C   1 
ATOM   3692 O O   . PRO B 1 487 ? -17.170 18.636 -6.444  1.00 179.34 ? 160 PRO B O   1 
ATOM   3693 C CB  . PRO B 1 487 ? -18.029 20.442 -3.831  1.00 176.17 ? 160 PRO B CB  1 
ATOM   3694 C CG  . PRO B 1 487 ? -17.431 21.673 -3.290  1.00 171.08 ? 160 PRO B CG  1 
ATOM   3695 C CD  . PRO B 1 487 ? -16.120 21.258 -2.691  1.00 173.94 ? 160 PRO B CD  1 
ATOM   3696 N N   . LYS B 1 488 ? -16.087 20.618 -6.362  1.00 168.63 ? 161 LYS B N   1 
ATOM   3697 C CA  . LYS B 1 488 ? -15.945 20.765 -7.809  1.00 168.33 ? 161 LYS B CA  1 
ATOM   3698 C C   . LYS B 1 488 ? -15.562 19.466 -8.503  1.00 168.40 ? 161 LYS B C   1 
ATOM   3699 O O   . LYS B 1 488 ? -16.050 19.175 -9.599  1.00 164.63 ? 161 LYS B O   1 
ATOM   3700 C CB  . LYS B 1 488 ? -14.898 21.828 -8.149  1.00 163.08 ? 161 LYS B CB  1 
ATOM   3701 C CG  . LYS B 1 488 ? -15.293 23.253 -7.838  1.00 157.51 ? 161 LYS B CG  1 
ATOM   3702 C CD  . LYS B 1 488 ? -14.096 24.156 -8.059  1.00 169.79 ? 161 LYS B CD  1 
ATOM   3703 C CE  . LYS B 1 488 ? -14.396 25.599 -7.711  1.00 172.63 ? 161 LYS B CE  1 
ATOM   3704 N NZ  . LYS B 1 488 ? -13.139 26.337 -7.403  1.00 179.82 ? 161 LYS B NZ  1 
ATOM   3705 N N   . TYR B 1 489 ? -14.698 18.676 -7.866  1.00 172.96 ? 162 TYR B N   1 
ATOM   3706 C CA  . TYR B 1 489 ? -14.175 17.455 -8.462  1.00 174.01 ? 162 TYR B CA  1 
ATOM   3707 C C   . TYR B 1 489 ? -14.470 16.236 -7.599  1.00 176.66 ? 162 TYR B C   1 
ATOM   3708 O O   . TYR B 1 489 ? -13.975 15.142 -7.902  1.00 178.32 ? 162 TYR B O   1 
ATOM   3709 C CB  . TYR B 1 489 ? -12.664 17.597 -8.673  1.00 177.49 ? 162 TYR B CB  1 
ATOM   3710 C CG  . TYR B 1 489 ? -12.286 18.657 -9.687  1.00 176.14 ? 162 TYR B CG  1 
ATOM   3711 C CD1 . TYR B 1 489 ? -12.391 18.424 -11.050 1.00 185.84 ? 162 TYR B CD1 1 
ATOM   3712 C CD2 . TYR B 1 489 ? -11.836 19.907 -9.269  1.00 171.46 ? 162 TYR B CD2 1 
ATOM   3713 C CE1 . TYR B 1 489 ? -12.049 19.397 -11.970 1.00 179.99 ? 162 TYR B CE1 1 
ATOM   3714 C CE2 . TYR B 1 489 ? -11.493 20.888 -10.182 1.00 179.37 ? 162 TYR B CE2 1 
ATOM   3715 C CZ  . TYR B 1 489 ? -11.602 20.626 -11.532 1.00 184.22 ? 162 TYR B CZ  1 
ATOM   3716 O OH  . TYR B 1 489 ? -11.263 21.595 -12.448 1.00 223.50 ? 162 TYR B OH  1 
ATOM   3717 N N   . SER B 1 490 ? -15.276 16.400 -6.544  1.00 179.52 ? 163 SER B N   1 
ATOM   3718 C CA  . SER B 1 490 ? -15.372 15.390 -5.491  1.00 184.26 ? 163 SER B CA  1 
ATOM   3719 C C   . SER B 1 490 ? -15.745 14.022 -6.051  1.00 185.23 ? 163 SER B C   1 
ATOM   3720 O O   . SER B 1 490 ? -15.031 13.037 -5.832  1.00 186.93 ? 163 SER B O   1 
ATOM   3721 C CB  . SER B 1 490 ? -16.389 15.831 -4.439  1.00 176.40 ? 163 SER B CB  1 
ATOM   3722 O OG  . SER B 1 490 ? -17.487 16.490 -5.046  1.00 176.34 ? 163 SER B OG  1 
ATOM   3723 N N   . GLU B 1 491 ? -16.869 13.936 -6.766  1.00 208.69 ? 164 GLU B N   1 
ATOM   3724 C CA  . GLU B 1 491 ? -17.248 12.668 -7.378  1.00 187.90 ? 164 GLU B CA  1 
ATOM   3725 C C   . GLU B 1 491 ? -16.284 12.296 -8.497  1.00 184.06 ? 164 GLU B C   1 
ATOM   3726 O O   . GLU B 1 491 ? -15.974 11.114 -8.683  1.00 185.46 ? 164 GLU B O   1 
ATOM   3727 C CB  . GLU B 1 491 ? -18.680 12.748 -7.903  1.00 189.74 ? 164 GLU B CB  1 
ATOM   3728 C CG  . GLU B 1 491 ? -19.701 13.154 -6.859  1.00 186.56 ? 164 GLU B CG  1 
ATOM   3729 C CD  . GLU B 1 491 ? -20.023 12.038 -5.882  1.00 186.16 ? 164 GLU B CD  1 
ATOM   3730 O OE1 . GLU B 1 491 ? -20.210 10.884 -6.334  1.00 181.36 ? 164 GLU B OE1 1 
ATOM   3731 O OE2 . GLU B 1 491 ? -20.112 12.314 -4.665  1.00 188.46 ? 164 GLU B OE2 1 
ATOM   3732 N N   . GLU B 1 492 ? -15.789 13.298 -9.234  1.00 177.31 ? 165 GLU B N   1 
ATOM   3733 C CA  . GLU B 1 492 ? -14.876 13.050 -10.344 1.00 174.40 ? 165 GLU B CA  1 
ATOM   3734 C C   . GLU B 1 492 ? -13.683 12.223 -9.892  1.00 175.28 ? 165 GLU B C   1 
ATOM   3735 O O   . GLU B 1 492 ? -13.185 11.374 -10.640 1.00 169.58 ? 165 GLU B O   1 
ATOM   3736 C CB  . GLU B 1 492 ? -14.405 14.382 -10.933 1.00 173.23 ? 165 GLU B CB  1 
ATOM   3737 C CG  . GLU B 1 492 ? -15.533 15.332 -11.265 1.00 175.27 ? 165 GLU B CG  1 
ATOM   3738 C CD  . GLU B 1 492 ? -15.119 16.408 -12.244 1.00 176.27 ? 165 GLU B CD  1 
ATOM   3739 O OE1 . GLU B 1 492 ? -14.088 16.214 -12.919 1.00 167.74 ? 165 GLU B OE1 1 
ATOM   3740 O OE2 . GLU B 1 492 ? -15.805 17.452 -12.320 1.00 176.76 ? 165 GLU B OE2 1 
ATOM   3741 N N   . ALA B 1 493 ? -13.215 12.460 -8.664  1.00 179.00 ? 166 ALA B N   1 
ATOM   3742 C CA  . ALA B 1 493 ? -12.123 11.687 -8.093  1.00 174.69 ? 166 ALA B CA  1 
ATOM   3743 C C   . ALA B 1 493 ? -12.592 10.302 -7.664  1.00 180.26 ? 166 ALA B C   1 
ATOM   3744 O O   . ALA B 1 493 ? -11.917 9.299  -7.935  1.00 181.60 ? 166 ALA B O   1 
ATOM   3745 C CB  . ALA B 1 493 ? -11.525 12.449 -6.909  1.00 168.33 ? 166 ALA B CB  1 
ATOM   3746 N N   . LYS B 1 494 ? -13.749 10.242 -6.992  1.00 180.01 ? 167 LYS B N   1 
ATOM   3747 C CA  . LYS B 1 494 ? -14.289 8.982  -6.488  1.00 182.28 ? 167 LYS B CA  1 
ATOM   3748 C C   . LYS B 1 494 ? -14.341 7.939  -7.590  1.00 189.85 ? 167 LYS B C   1 
ATOM   3749 O O   . LYS B 1 494 ? -13.908 6.795  -7.409  1.00 190.18 ? 167 LYS B O   1 
ATOM   3750 C CB  . LYS B 1 494 ? -15.688 9.218  -5.917  1.00 181.53 ? 167 LYS B CB  1 
ATOM   3751 C CG  . LYS B 1 494 ? -15.715 10.018 -4.630  1.00 176.39 ? 167 LYS B CG  1 
ATOM   3752 C CD  . LYS B 1 494 ? -17.127 10.133 -4.100  1.00 176.70 ? 167 LYS B CD  1 
ATOM   3753 C CE  . LYS B 1 494 ? -17.171 10.917 -2.804  1.00 172.97 ? 167 LYS B CE  1 
ATOM   3754 N NZ  . LYS B 1 494 ? -18.548 10.975 -2.240  1.00 177.23 ? 167 LYS B NZ  1 
ATOM   3755 N N   . LEU B 1 495 ? -14.857 8.341  -8.753  1.00 195.06 ? 168 LEU B N   1 
ATOM   3756 C CA  . LEU B 1 495 ? -14.926 7.458  -9.908  1.00 197.07 ? 168 LEU B CA  1 
ATOM   3757 C C   . LEU B 1 495 ? -13.575 6.817  -10.174 1.00 200.10 ? 168 LEU B C   1 
ATOM   3758 O O   . LEU B 1 495 ? -13.456 5.588  -10.230 1.00 202.34 ? 168 LEU B O   1 
ATOM   3759 C CB  . LEU B 1 495 ? -15.393 8.254  -11.125 1.00 188.04 ? 168 LEU B CB  1 
ATOM   3760 C CG  . LEU B 1 495 ? -16.778 8.888  -10.987 1.00 185.15 ? 168 LEU B CG  1 
ATOM   3761 C CD1 . LEU B 1 495 ? -17.107 9.758  -12.186 1.00 177.86 ? 168 LEU B CD1 1 
ATOM   3762 C CD2 . LEU B 1 495 ? -17.848 7.824  -10.792 1.00 190.49 ? 168 LEU B CD2 1 
ATOM   3763 N N   . ASN B 1 496 ? -12.535 7.645  -10.297 1.00 192.68 ? 169 ASN B N   1 
ATOM   3764 C CA  . ASN B 1 496 ? -11.206 7.121  -10.572 1.00 192.32 ? 169 ASN B CA  1 
ATOM   3765 C C   . ASN B 1 496 ? -10.660 6.320  -9.399  1.00 195.54 ? 169 ASN B C   1 
ATOM   3766 O O   . ASN B 1 496 ? -9.870  5.391  -9.605  1.00 203.05 ? 169 ASN B O   1 
ATOM   3767 C CB  . ASN B 1 496 ? -10.271 8.269  -10.946 1.00 181.98 ? 169 ASN B CB  1 
ATOM   3768 C CG  . ASN B 1 496 ? -10.871 9.175  -12.008 1.00 181.82 ? 169 ASN B CG  1 
ATOM   3769 O OD1 . ASN B 1 496 ? -11.809 8.784  -12.705 1.00 182.37 ? 169 ASN B OD1 1 
ATOM   3770 N ND2 . ASN B 1 496 ? -10.338 10.380 -12.138 1.00 179.39 ? 169 ASN B ND2 1 
ATOM   3771 N N   . ARG B 1 497 ? -11.080 6.642  -8.171  1.00 189.70 ? 170 ARG B N   1 
ATOM   3772 C CA  . ARG B 1 497 ? -10.745 5.780  -7.042  1.00 193.87 ? 170 ARG B CA  1 
ATOM   3773 C C   . ARG B 1 497 ? -11.264 4.367  -7.272  1.00 204.53 ? 170 ARG B C   1 
ATOM   3774 O O   . ARG B 1 497 ? -10.587 3.386  -6.944  1.00 204.49 ? 170 ARG B O   1 
ATOM   3775 C CB  . ARG B 1 497 ? -11.310 6.354  -5.743  1.00 177.19 ? 170 ARG B CB  1 
ATOM   3776 C CG  . ARG B 1 497 ? -10.757 7.719  -5.366  1.00 169.82 ? 170 ARG B CG  1 
ATOM   3777 C CD  . ARG B 1 497 ? -11.496 8.286  -4.166  1.00 168.65 ? 170 ARG B CD  1 
ATOM   3778 N NE  . ARG B 1 497 ? -11.740 9.718  -4.285  1.00 169.61 ? 170 ARG B NE  1 
ATOM   3779 C CZ  . ARG B 1 497 ? -12.530 10.409 -3.475  1.00 169.02 ? 170 ARG B CZ  1 
ATOM   3780 N NH1 . ARG B 1 497 ? -13.166 9.830  -2.469  1.00 168.83 ? 170 ARG B NH1 1 
ATOM   3781 N NH2 . ARG B 1 497 ? -12.700 11.710 -3.690  1.00 167.65 ? 170 ARG B NH2 1 
ATOM   3782 N N   . GLU B 1 498 ? -12.452 4.247  -7.865  1.00 195.37 ? 171 GLU B N   1 
ATOM   3783 C CA  . GLU B 1 498 ? -13.014 2.946  -8.205  1.00 196.01 ? 171 GLU B CA  1 
ATOM   3784 C C   . GLU B 1 498 ? -12.221 2.224  -9.289  1.00 199.56 ? 171 GLU B C   1 
ATOM   3785 O O   . GLU B 1 498 ? -12.476 1.039  -9.530  1.00 196.55 ? 171 GLU B O   1 
ATOM   3786 C CB  . GLU B 1 498 ? -14.472 3.124  -8.629  1.00 190.99 ? 171 GLU B CB  1 
ATOM   3787 C CG  . GLU B 1 498 ? -15.339 3.675  -7.510  1.00 193.49 ? 171 GLU B CG  1 
ATOM   3788 C CD  . GLU B 1 498 ? -16.421 4.598  -8.022  1.00 201.97 ? 171 GLU B CD  1 
ATOM   3789 O OE1 . GLU B 1 498 ? -16.643 4.614  -9.249  1.00 205.23 ? 171 GLU B OE1 1 
ATOM   3790 O OE2 . GLU B 1 498 ? -17.033 5.318  -7.205  1.00 218.31 ? 171 GLU B OE2 1 
ATOM   3791 N N   . GLU B 1 499 ? -11.277 2.902  -9.945  1.00 205.25 ? 172 GLU B N   1 
ATOM   3792 C CA  . GLU B 1 499 ? -10.327 2.244  -10.833 1.00 210.54 ? 172 GLU B CA  1 
ATOM   3793 C C   . GLU B 1 499 ? -9.090  1.747  -10.094 1.00 214.59 ? 172 GLU B C   1 
ATOM   3794 O O   . GLU B 1 499 ? -8.421  0.825  -10.577 1.00 214.22 ? 172 GLU B O   1 
ATOM   3795 C CB  . GLU B 1 499 ? -9.922  3.200  -11.960 1.00 212.50 ? 172 GLU B CB  1 
ATOM   3796 C CG  . GLU B 1 499 ? -11.102 3.668  -12.809 1.00 208.01 ? 172 GLU B CG  1 
ATOM   3797 C CD  . GLU B 1 499 ? -10.815 4.957  -13.550 1.00 202.54 ? 172 GLU B CD  1 
ATOM   3798 O OE1 . GLU B 1 499 ? -9.766  5.574  -13.275 1.00 199.83 ? 172 GLU B OE1 1 
ATOM   3799 O OE2 . GLU B 1 499 ? -11.642 5.361  -14.396 1.00 200.37 ? 172 GLU B OE2 1 
ATOM   3800 N N   . ILE B 1 500 ? -8.779  2.332  -8.939  1.00 212.45 ? 173 ILE B N   1 
ATOM   3801 C CA  . ILE B 1 500 ? -7.747  1.793  -8.060  1.00 208.23 ? 173 ILE B CA  1 
ATOM   3802 C C   . ILE B 1 500 ? -8.325  0.734  -7.121  1.00 210.67 ? 173 ILE B C   1 
ATOM   3803 O O   . ILE B 1 500 ? -7.607  -0.178 -6.696  1.00 209.77 ? 173 ILE B O   1 
ATOM   3804 C CB  . ILE B 1 500 ? -7.080  2.942  -7.281  1.00 201.19 ? 173 ILE B CB  1 
ATOM   3805 C CG1 . ILE B 1 500 ? -6.360  3.873  -8.255  1.00 197.01 ? 173 ILE B CG1 1 
ATOM   3806 C CG2 . ILE B 1 500 ? -6.083  2.420  -6.254  1.00 192.36 ? 173 ILE B CG2 1 
ATOM   3807 C CD1 . ILE B 1 500 ? -5.864  5.142  -7.626  1.00 191.87 ? 173 ILE B CD1 1 
ATOM   3808 N N   . ASP B 1 501 ? -9.621  0.824  -6.812  1.00 214.02 ? 174 ASP B N   1 
ATOM   3809 C CA  . ASP B 1 501 ? -10.272 -0.185 -5.982  1.00 212.80 ? 174 ASP B CA  1 
ATOM   3810 C C   . ASP B 1 501 ? -10.244 -1.551 -6.660  1.00 214.47 ? 174 ASP B C   1 
ATOM   3811 O O   . ASP B 1 501 ? -9.740  -2.531 -6.098  1.00 221.40 ? 174 ASP B O   1 
ATOM   3812 C CB  . ASP B 1 501 ? -11.712 0.240  -5.682  1.00 206.11 ? 174 ASP B CB  1 
ATOM   3813 C CG  . ASP B 1 501 ? -11.785 1.522  -4.873  1.00 194.05 ? 174 ASP B CG  1 
ATOM   3814 O OD1 . ASP B 1 501 ? -10.750 1.927  -4.300  1.00 193.18 ? 174 ASP B OD1 1 
ATOM   3815 O OD2 . ASP B 1 501 ? -12.875 2.131  -4.822  1.00 187.82 ? 174 ASP B OD2 1 
ATOM   3816 N N   . SER B 1 502 ? -10.775 -1.631 -7.877  1.00 221.07 ? 175 SER B N   1 
ATOM   3817 C CA  . SER B 1 502 ? -10.799 -2.887 -8.623  1.00 199.67 ? 175 SER B CA  1 
ATOM   3818 C C   . SER B 1 502 ? -9.425  -3.213 -9.196  1.00 194.66 ? 175 SER B C   1 
ATOM   3819 O O   . SER B 1 502 ? -9.314  -3.752 -10.296 1.00 185.29 ? 175 SER B O   1 
ATOM   3820 C CB  . SER B 1 502 ? -11.829 -2.829 -9.755  1.00 186.37 ? 175 SER B CB  1 
ATOM   3821 O OG  . SER B 1 502 ? -11.416 -1.934 -10.773 1.00 184.64 ? 175 SER B OG  1 
ATOM   3822 N N   . GLN C 2 1   ? 29.089  39.717 -15.672 1.00 108.07 ? 1   GLN H N   1 
ATOM   3823 C CA  . GLN C 2 1   ? 28.956  40.501 -16.898 1.00 116.09 ? 1   GLN H CA  1 
ATOM   3824 C C   . GLN C 2 1   ? 27.796  40.033 -17.766 1.00 115.48 ? 1   GLN H C   1 
ATOM   3825 O O   . GLN C 2 1   ? 28.000  39.450 -18.833 1.00 115.96 ? 1   GLN H O   1 
ATOM   3826 C CB  . GLN C 2 1   ? 30.257  40.460 -17.703 1.00 115.10 ? 1   GLN H CB  1 
ATOM   3827 C CG  . GLN C 2 1   ? 30.610  41.783 -18.363 1.00 119.87 ? 1   GLN H CG  1 
ATOM   3828 C CD  . GLN C 2 1   ? 30.999  42.850 -17.361 1.00 138.53 ? 1   GLN H CD  1 
ATOM   3829 O OE1 . GLN C 2 1   ? 30.147  43.567 -16.839 1.00 156.04 ? 1   GLN H OE1 1 
ATOM   3830 N NE2 . GLN C 2 1   ? 32.295  42.962 -17.089 1.00 152.51 ? 1   GLN H NE2 1 
ATOM   3831 N N   . VAL C 2 2   ? 26.583  40.298 -17.311 1.00 115.10 ? 2   VAL H N   1 
ATOM   3832 C CA  . VAL C 2 2   ? 25.381  39.980 -18.070 1.00 107.39 ? 2   VAL H CA  1 
ATOM   3833 C C   . VAL C 2 2   ? 24.993  41.198 -18.896 1.00 108.74 ? 2   VAL H C   1 
ATOM   3834 O O   . VAL C 2 2   ? 25.029  42.334 -18.408 1.00 115.90 ? 2   VAL H O   1 
ATOM   3835 C CB  . VAL C 2 2   ? 24.239  39.546 -17.133 1.00 100.68 ? 2   VAL H CB  1 
ATOM   3836 C CG1 . VAL C 2 2   ? 23.027  39.107 -17.938 1.00 98.11  ? 2   VAL H CG1 1 
ATOM   3837 C CG2 . VAL C 2 2   ? 24.707  38.431 -16.208 1.00 102.62 ? 2   VAL H CG2 1 
ATOM   3838 N N   . GLN C 2 3   ? 24.631  40.964 -20.157 1.00 106.86 ? 3   GLN H N   1 
ATOM   3839 C CA  . GLN C 2 3   ? 24.234  42.013 -21.089 1.00 103.54 ? 3   GLN H CA  1 
ATOM   3840 C C   . GLN C 2 3   ? 22.857  41.699 -21.654 1.00 98.60  ? 3   GLN H C   1 
ATOM   3841 O O   . GLN C 2 3   ? 22.604  40.574 -22.100 1.00 100.82 ? 3   GLN H O   1 
ATOM   3842 C CB  . GLN C 2 3   ? 25.235  42.160 -22.242 1.00 107.72 ? 3   GLN H CB  1 
ATOM   3843 C CG  . GLN C 2 3   ? 26.692  42.223 -21.828 1.00 109.66 ? 3   GLN H CG  1 
ATOM   3844 C CD  . GLN C 2 3   ? 27.029  43.507 -21.106 1.00 115.89 ? 3   GLN H CD  1 
ATOM   3845 O OE1 . GLN C 2 3   ? 26.772  44.599 -21.611 1.00 116.09 ? 3   GLN H OE1 1 
ATOM   3846 N NE2 . GLN C 2 3   ? 27.613  43.385 -19.918 1.00 131.94 ? 3   GLN H NE2 1 
ATOM   3847 N N   . LEU C 2 4   ? 21.983  42.703 -21.653 1.00 94.69  ? 4   LEU H N   1 
ATOM   3848 C CA  . LEU C 2 4   ? 20.640  42.604 -22.205 1.00 95.14  ? 4   LEU H CA  1 
ATOM   3849 C C   . LEU C 2 4   ? 20.510  43.648 -23.303 1.00 100.61 ? 4   LEU H C   1 
ATOM   3850 O O   . LEU C 2 4   ? 20.915  44.797 -23.106 1.00 111.17 ? 4   LEU H O   1 
ATOM   3851 C CB  . LEU C 2 4   ? 19.590  42.849 -21.116 1.00 90.36  ? 4   LEU H CB  1 
ATOM   3852 C CG  . LEU C 2 4   ? 19.718  42.027 -19.828 1.00 82.54  ? 4   LEU H CG  1 
ATOM   3853 C CD1 . LEU C 2 4   ? 18.700  42.449 -18.778 1.00 77.07  ? 4   LEU H CD1 1 
ATOM   3854 C CD2 . LEU C 2 4   ? 19.606  40.549 -20.117 1.00 86.82  ? 4   LEU H CD2 1 
ATOM   3855 N N   . GLN C 2 5   ? 19.952  43.268 -24.452 1.00 94.49  ? 5   GLN H N   1 
ATOM   3856 C CA  . GLN C 2 5   ? 19.736  44.284 -25.475 1.00 100.03 ? 5   GLN H CA  1 
ATOM   3857 C C   . GLN C 2 5   ? 18.477  43.975 -26.270 1.00 93.24  ? 5   GLN H C   1 
ATOM   3858 O O   . GLN C 2 5   ? 18.258  42.837 -26.687 1.00 89.96  ? 5   GLN H O   1 
ATOM   3859 C CB  . GLN C 2 5   ? 20.935  44.411 -26.417 1.00 111.44 ? 5   GLN H CB  1 
ATOM   3860 C CG  . GLN C 2 5   ? 20.821  45.592 -27.365 1.00 131.69 ? 5   GLN H CG  1 
ATOM   3861 C CD  . GLN C 2 5   ? 21.931  45.630 -28.390 1.00 162.13 ? 5   GLN H CD  1 
ATOM   3862 O OE1 . GLN C 2 5   ? 22.979  45.012 -28.209 1.00 204.34 ? 5   GLN H OE1 1 
ATOM   3863 N NE2 . GLN C 2 5   ? 21.706  46.356 -29.480 1.00 193.71 ? 5   GLN H NE2 1 
ATOM   3864 N N   . GLU C 2 6   ? 17.669  45.004 -26.499 1.00 90.46  ? 6   GLU H N   1 
ATOM   3865 C CA  . GLU C 2 6   ? 16.363  44.843 -27.115 1.00 87.51  ? 6   GLU H CA  1 
ATOM   3866 C C   . GLU C 2 6   ? 16.417  45.150 -28.607 1.00 91.78  ? 6   GLU H C   1 
ATOM   3867 O O   . GLU C 2 6   ? 17.215  45.971 -29.067 1.00 98.83  ? 6   GLU H O   1 
ATOM   3868 C CB  . GLU C 2 6   ? 15.330  45.745 -26.434 1.00 85.18  ? 6   GLU H CB  1 
ATOM   3869 C CG  . GLU C 2 6   ? 15.052  45.388 -24.981 1.00 83.53  ? 6   GLU H CG  1 
ATOM   3870 C CD  . GLU C 2 6   ? 15.813  46.274 -24.013 1.00 79.36  ? 6   GLU H CD  1 
ATOM   3871 O OE1 . GLU C 2 6   ? 16.669  47.054 -24.482 1.00 78.69  ? 6   GLU H OE1 1 
ATOM   3872 O OE2 . GLU C 2 6   ? 15.559  46.197 -22.792 1.00 75.69  ? 6   GLU H OE2 1 
ATOM   3873 N N   . SER C 2 7   ? 15.554  44.469 -29.356 1.00 91.77  ? 7   SER H N   1 
ATOM   3874 C CA  . SER C 2 7   ? 15.358  44.684 -30.781 1.00 93.77  ? 7   SER H CA  1 
ATOM   3875 C C   . SER C 2 7   ? 13.872  44.876 -31.037 1.00 94.42  ? 7   SER H C   1 
ATOM   3876 O O   . SER C 2 7   ? 13.048  44.047 -30.617 1.00 92.00  ? 7   SER H O   1 
ATOM   3877 C CB  . SER C 2 7   ? 15.893  43.510 -31.609 1.00 106.57 ? 7   SER H CB  1 
ATOM   3878 O OG  . SER C 2 7   ? 17.276  43.655 -31.868 1.00 137.16 ? 7   SER H OG  1 
ATOM   3879 N N   . GLY C 2 8   ? 13.545  45.967 -31.731 1.00 102.57 ? 8   GLY H N   1 
ATOM   3880 C CA  . GLY C 2 8   ? 12.180  46.365 -31.969 1.00 125.04 ? 8   GLY H CA  1 
ATOM   3881 C C   . GLY C 2 8   ? 11.996  47.144 -33.259 1.00 111.18 ? 8   GLY H C   1 
ATOM   3882 O O   . GLY C 2 8   ? 12.874  47.898 -33.694 1.00 94.51  ? 8   GLY H O   1 
ATOM   3883 N N   . PRO C 2 9   ? 10.830  46.973 -33.892 1.00 107.91 ? 9   PRO H N   1 
ATOM   3884 C CA  . PRO C 2 9   ? 10.596  47.606 -35.200 1.00 111.47 ? 9   PRO H CA  1 
ATOM   3885 C C   . PRO C 2 9   ? 10.527  49.120 -35.156 1.00 107.42 ? 9   PRO H C   1 
ATOM   3886 O O   . PRO C 2 9   ? 10.785  49.762 -36.177 1.00 108.10 ? 9   PRO H O   1 
ATOM   3887 C CB  . PRO C 2 9   ? 9.255   46.999 -35.638 1.00 102.57 ? 9   PRO H CB  1 
ATOM   3888 C CG  . PRO C 2 9   ? 8.587   46.634 -34.350 1.00 95.41  ? 9   PRO H CG  1 
ATOM   3889 C CD  . PRO C 2 9   ? 9.706   46.103 -33.505 1.00 96.62  ? 9   PRO H CD  1 
ATOM   3890 N N   . GLY C 2 10  ? 10.192  49.714 -34.026 1.00 103.10 ? 10  GLY H N   1 
ATOM   3891 C CA  . GLY C 2 10  ? 10.060  51.150 -33.977 1.00 93.52  ? 10  GLY H CA  1 
ATOM   3892 C C   . GLY C 2 10  ? 8.648   51.579 -34.304 1.00 94.00  ? 10  GLY H C   1 
ATOM   3893 O O   . GLY C 2 10  ? 8.106   52.474 -33.651 1.00 104.13 ? 10  GLY H O   1 
ATOM   3894 N N   . LEU C 2 11  ? 8.035   50.941 -35.302 1.00 79.16  ? 11  LEU H N   1 
ATOM   3895 C CA  . LEU C 2 11  ? 6.684   51.265 -35.737 1.00 75.30  ? 11  LEU H CA  1 
ATOM   3896 C C   . LEU C 2 11  ? 5.805   50.024 -35.731 1.00 74.59  ? 11  LEU H C   1 
ATOM   3897 O O   . LEU C 2 11  ? 6.239   48.937 -36.125 1.00 78.35  ? 11  LEU H O   1 
ATOM   3898 C CB  . LEU C 2 11  ? 6.681   51.883 -37.136 1.00 76.60  ? 11  LEU H CB  1 
ATOM   3899 C CG  . LEU C 2 11  ? 7.084   53.350 -37.243 1.00 76.70  ? 11  LEU H CG  1 
ATOM   3900 C CD1 . LEU C 2 11  ? 7.301   53.754 -38.682 1.00 85.87  ? 11  LEU H CD1 1 
ATOM   3901 C CD2 . LEU C 2 11  ? 5.985   54.202 -36.641 1.00 91.05  ? 11  LEU H CD2 1 
ATOM   3902 N N   . VAL C 2 12  ? 4.569   50.182 -35.264 1.00 79.41  ? 12  VAL H N   1 
ATOM   3903 C CA  . VAL C 2 12  ? 3.597   49.053 -35.300 1.00 84.22  ? 12  VAL H CA  1 
ATOM   3904 C C   . VAL C 2 12  ? 2.239   49.637 -35.679 1.00 93.16  ? 12  VAL H C   1 
ATOM   3905 O O   . VAL C 2 12  ? 1.680   50.397 -34.880 1.00 96.56  ? 12  VAL H O   1 
ATOM   3906 C CB  . VAL C 2 12  ? 3.518   48.303 -33.961 1.00 84.10  ? 12  VAL H CB  1 
ATOM   3907 C CG1 . VAL C 2 12  ? 2.225   47.515 -33.832 1.00 82.97  ? 12  VAL H CG1 1 
ATOM   3908 C CG2 . VAL C 2 12  ? 4.717   47.394 -33.757 1.00 91.08  ? 12  VAL H CG2 1 
ATOM   3909 N N   . LYS C 2 13  ? 1.741   49.286 -36.869 1.00 98.81  ? 13  LYS H N   1 
ATOM   3910 C CA  . LYS C 2 13  ? 0.402   49.759 -37.306 1.00 98.95  ? 13  LYS H CA  1 
ATOM   3911 C C   . LYS C 2 13  ? -0.587  49.524 -36.162 1.00 99.56  ? 13  LYS H C   1 
ATOM   3912 O O   . LYS C 2 13  ? -0.620  48.396 -35.639 1.00 102.87 ? 13  LYS H O   1 
ATOM   3913 C CB  . LYS C 2 13  ? -0.030  49.038 -38.586 1.00 103.64 ? 13  LYS H CB  1 
ATOM   3914 C CG  . LYS C 2 13  ? 0.932   49.182 -39.756 1.00 110.93 ? 13  LYS H CG  1 
ATOM   3915 C CD  . LYS C 2 13  ? 1.272   50.624 -40.068 1.00 114.94 ? 13  LYS H CD  1 
ATOM   3916 C CE  . LYS C 2 13  ? 2.319   50.765 -41.152 1.00 122.06 ? 13  LYS H CE  1 
ATOM   3917 N NZ  . LYS C 2 13  ? 2.662   52.185 -41.402 1.00 125.43 ? 13  LYS H NZ  1 
ATOM   3918 N N   . PRO C 2 14  ? -1.404  50.522 -35.739 1.00 90.31  ? 14  PRO H N   1 
ATOM   3919 C CA  . PRO C 2 14  ? -2.410  50.307 -34.691 1.00 94.19  ? 14  PRO H CA  1 
ATOM   3920 C C   . PRO C 2 14  ? -3.340  49.126 -35.000 1.00 95.18  ? 14  PRO H C   1 
ATOM   3921 O O   . PRO C 2 14  ? -3.476  48.793 -36.166 1.00 98.96  ? 14  PRO H O   1 
ATOM   3922 C CB  . PRO C 2 14  ? -3.238  51.601 -34.699 1.00 90.14  ? 14  PRO H CB  1 
ATOM   3923 C CG  . PRO C 2 14  ? -2.273  52.649 -35.193 1.00 88.75  ? 14  PRO H CG  1 
ATOM   3924 C CD  . PRO C 2 14  ? -1.419  51.921 -36.209 1.00 86.69  ? 14  PRO H CD  1 
ATOM   3925 N N   . SER C 2 15  ? -3.941  48.527 -33.965 1.00 104.16 ? 15  SER H N   1 
ATOM   3926 C CA  . SER C 2 15  ? -4.880  47.383 -34.140 1.00 111.27 ? 15  SER H CA  1 
ATOM   3927 C C   . SER C 2 15  ? -4.127  46.138 -34.626 1.00 102.68 ? 15  SER H C   1 
ATOM   3928 O O   . SER C 2 15  ? -4.797  45.144 -34.966 1.00 99.15  ? 15  SER H O   1 
ATOM   3929 C CB  . SER C 2 15  ? -6.041  47.732 -35.044 1.00 109.04 ? 15  SER H CB  1 
ATOM   3930 O OG  . SER C 2 15  ? -5.595  48.017 -36.361 1.00 111.99 ? 15  SER H OG  1 
ATOM   3931 N N   . GLU C 2 16  ? -2.792  46.190 -34.655 1.00 90.86  ? 16  GLU H N   1 
ATOM   3932 C CA  . GLU C 2 16  ? -1.988  44.997 -35.036 1.00 91.24  ? 16  GLU H CA  1 
ATOM   3933 C C   . GLU C 2 16  ? -1.192  44.514 -33.820 1.00 89.82  ? 16  GLU H C   1 
ATOM   3934 O O   . GLU C 2 16  ? -1.573  44.880 -32.690 1.00 92.93  ? 16  GLU H O   1 
ATOM   3935 C CB  . GLU C 2 16  ? -1.088  45.318 -36.230 1.00 94.44  ? 16  GLU H CB  1 
ATOM   3936 C CG  . GLU C 2 16  ? -1.832  45.305 -37.553 1.00 106.66 ? 16  GLU H CG  1 
ATOM   3937 C CD  . GLU C 2 16  ? -0.947  45.359 -38.786 1.00 111.63 ? 16  GLU H CD  1 
ATOM   3938 O OE1 . GLU C 2 16  ? -0.066  44.487 -38.917 1.00 119.42 ? 16  GLU H OE1 1 
ATOM   3939 O OE2 . GLU C 2 16  ? -1.155  46.259 -39.622 1.00 121.77 ? 16  GLU H OE2 1 
ATOM   3940 N N   . THR C 2 17  ? -0.135  43.726 -34.035 1.00 92.68  ? 17  THR H N   1 
ATOM   3941 C CA  . THR C 2 17  ? 0.587   43.183 -32.893 1.00 89.23  ? 17  THR H CA  1 
ATOM   3942 C C   . THR C 2 17  ? 1.995   43.765 -32.814 1.00 86.10  ? 17  THR H C   1 
ATOM   3943 O O   . THR C 2 17  ? 2.584   44.181 -33.815 1.00 94.10  ? 17  THR H O   1 
ATOM   3944 C CB  . THR C 2 17  ? 0.665   41.651 -32.965 1.00 89.68  ? 17  THR H CB  1 
ATOM   3945 O OG1 . THR C 2 17  ? 1.575   41.254 -34.001 1.00 104.51 ? 17  THR H OG1 1 
ATOM   3946 C CG2 . THR C 2 17  ? -0.707  41.055 -33.244 1.00 93.64  ? 17  THR H CG2 1 
ATOM   3947 N N   . LEU C 2 18  ? 2.526   43.794 -31.595 1.00 82.32  ? 18  LEU H N   1 
ATOM   3948 C CA  . LEU C 2 18  ? 3.882   44.248 -31.311 1.00 85.90  ? 18  LEU H CA  1 
ATOM   3949 C C   . LEU C 2 18  ? 4.745   43.049 -30.951 1.00 89.50  ? 18  LEU H C   1 
ATOM   3950 O O   . LEU C 2 18  ? 4.409   42.298 -30.031 1.00 95.66  ? 18  LEU H O   1 
ATOM   3951 C CB  . LEU C 2 18  ? 3.896   45.271 -30.174 1.00 82.40  ? 18  LEU H CB  1 
ATOM   3952 C CG  . LEU C 2 18  ? 5.291   45.677 -29.688 1.00 77.01  ? 18  LEU H CG  1 
ATOM   3953 C CD1 . LEU C 2 18  ? 6.086   46.387 -30.770 1.00 76.41  ? 18  LEU H CD1 1 
ATOM   3954 C CD2 . LEU C 2 18  ? 5.179   46.555 -28.464 1.00 67.40  ? 18  LEU H CD2 1 
ATOM   3955 N N   . SER C 2 19  ? 5.852   42.880 -31.668 1.00 83.53  ? 19  SER H N   1 
ATOM   3956 C CA  . SER C 2 19  ? 6.805   41.812 -31.404 1.00 87.40  ? 19  SER H CA  1 
ATOM   3957 C C   . SER C 2 19  ? 8.155   42.423 -31.061 1.00 88.21  ? 19  SER H C   1 
ATOM   3958 O O   . SER C 2 19  ? 8.694   43.225 -31.830 1.00 90.97  ? 19  SER H O   1 
ATOM   3959 C CB  . SER C 2 19  ? 6.932   40.875 -32.604 1.00 104.01 ? 19  SER H CB  1 
ATOM   3960 O OG  . SER C 2 19  ? 6.034   39.786 -32.490 1.00 123.04 ? 19  SER H OG  1 
ATOM   3961 N N   . LEU C 2 20  ? 8.695   42.045 -29.906 1.00 86.40  ? 20  LEU H N   1 
ATOM   3962 C CA  . LEU C 2 20  ? 9.963   42.571 -29.426 1.00 86.50  ? 20  LEU H CA  1 
ATOM   3963 C C   . LEU C 2 20  ? 10.834  41.418 -28.955 1.00 84.57  ? 20  LEU H C   1 
ATOM   3964 O O   . LEU C 2 20  ? 10.330  40.448 -28.381 1.00 83.32  ? 20  LEU H O   1 
ATOM   3965 C CB  . LEU C 2 20  ? 9.756   43.551 -28.271 1.00 88.67  ? 20  LEU H CB  1 
ATOM   3966 C CG  . LEU C 2 20  ? 9.064   44.872 -28.591 1.00 83.53  ? 20  LEU H CG  1 
ATOM   3967 C CD1 . LEU C 2 20  ? 8.994   45.721 -27.340 1.00 79.93  ? 20  LEU H CD1 1 
ATOM   3968 C CD2 . LEU C 2 20  ? 9.752   45.610 -29.712 1.00 82.57  ? 20  LEU H CD2 1 
ATOM   3969 N N   . THR C 2 21  ? 12.146  41.528 -29.179 1.00 83.26  ? 21  THR H N   1 
ATOM   3970 C CA  . THR C 2 21  ? 13.060  40.456 -28.786 1.00 82.50  ? 21  THR H CA  1 
ATOM   3971 C C   . THR C 2 21  ? 14.258  41.013 -28.030 1.00 81.95  ? 21  THR H C   1 
ATOM   3972 O O   . THR C 2 21  ? 15.034  41.799 -28.577 1.00 85.72  ? 21  THR H O   1 
ATOM   3973 C CB  . THR C 2 21  ? 13.526  39.644 -30.000 1.00 89.27  ? 21  THR H CB  1 
ATOM   3974 O OG1 . THR C 2 21  ? 13.954  40.527 -31.043 1.00 100.40 ? 21  THR H OG1 1 
ATOM   3975 C CG2 . THR C 2 21  ? 12.406  38.743 -30.511 1.00 89.72  ? 21  THR H CG2 1 
ATOM   3976 N N   . CYS C 2 22  ? 14.414  40.589 -26.781 1.00 82.86  ? 22  CYS H N   1 
ATOM   3977 C CA  . CYS C 2 22  ? 15.559  40.939 -25.949 1.00 87.75  ? 22  CYS H CA  1 
ATOM   3978 C C   . CYS C 2 22  ? 16.563  39.791 -26.014 1.00 95.31  ? 22  CYS H C   1 
ATOM   3979 O O   . CYS C 2 22  ? 16.289  38.693 -25.522 1.00 99.33  ? 22  CYS H O   1 
ATOM   3980 C CB  . CYS C 2 22  ? 15.109  41.211 -24.514 1.00 92.90  ? 22  CYS H CB  1 
ATOM   3981 S SG  . CYS C 2 22  ? 16.428  41.351 -23.281 1.00 114.54 ? 22  CYS H SG  1 
ATOM   3982 N N   . SER C 2 23  ? 17.710  40.039 -26.641 1.00 96.87  ? 23  SER H N   1 
ATOM   3983 C CA  . SER C 2 23  ? 18.794  39.070 -26.701 1.00 97.63  ? 23  SER H CA  1 
ATOM   3984 C C   . SER C 2 23  ? 19.694  39.234 -25.482 1.00 98.41  ? 23  SER H C   1 
ATOM   3985 O O   . SER C 2 23  ? 20.032  40.361 -25.091 1.00 103.73 ? 23  SER H O   1 
ATOM   3986 C CB  . SER C 2 23  ? 19.604  39.235 -27.987 1.00 100.51 ? 23  SER H CB  1 
ATOM   3987 O OG  . SER C 2 23  ? 19.966  40.589 -28.192 1.00 94.47  ? 23  SER H OG  1 
ATOM   3988 N N   . VAL C 2 24  ? 20.078  38.104 -24.891 1.00 94.55  ? 24  VAL H N   1 
ATOM   3989 C CA  . VAL C 2 24  ? 20.854  38.059 -23.659 1.00 97.54  ? 24  VAL H CA  1 
ATOM   3990 C C   . VAL C 2 24  ? 22.204  37.429 -23.957 1.00 99.89  ? 24  VAL H C   1 
ATOM   3991 O O   . VAL C 2 24  ? 22.276  36.356 -24.568 1.00 99.02  ? 24  VAL H O   1 
ATOM   3992 C CB  . VAL C 2 24  ? 20.122  37.263 -22.564 1.00 98.09  ? 24  VAL H CB  1 
ATOM   3993 C CG1 . VAL C 2 24  ? 20.984  37.154 -21.312 1.00 96.45  ? 24  VAL H CG1 1 
ATOM   3994 C CG2 . VAL C 2 24  ? 18.782  37.899 -22.253 1.00 96.34  ? 24  VAL H CG2 1 
ATOM   3995 N N   . SER C 2 25  ? 23.270  38.089 -23.520 1.00 99.27  ? 25  SER H N   1 
ATOM   3996 C CA  . SER C 2 25  ? 24.607  37.518 -23.553 1.00 94.90  ? 25  SER H CA  1 
ATOM   3997 C C   . SER C 2 25  ? 25.145  37.467 -22.131 1.00 100.96 ? 25  SER H C   1 
ATOM   3998 O O   . SER C 2 25  ? 24.875  38.362 -21.327 1.00 111.90 ? 25  SER H O   1 
ATOM   3999 C CB  . SER C 2 25  ? 25.538  38.331 -24.454 1.00 96.82  ? 25  SER H CB  1 
ATOM   4000 O OG  . SER C 2 25  ? 25.928  39.537 -23.824 1.00 107.33 ? 25  SER H OG  1 
ATOM   4001 N N   . GLY C 2 26  ? 25.885  36.412 -21.811 1.00 100.08 ? 26  GLY H N   1 
ATOM   4002 C CA  . GLY C 2 26  ? 26.456  36.280 -20.487 1.00 99.60  ? 26  GLY H CA  1 
ATOM   4003 C C   . GLY C 2 26  ? 25.590  35.572 -19.472 1.00 92.06  ? 26  GLY H C   1 
ATOM   4004 O O   . GLY C 2 26  ? 25.868  35.673 -18.270 1.00 92.39  ? 26  GLY H O   1 
ATOM   4005 N N   . ALA C 2 27  ? 24.553  34.865 -19.912 1.00 90.95  ? 27  ALA H N   1 
ATOM   4006 C CA  . ALA C 2 27  ? 23.697  34.095 -19.023 1.00 92.50  ? 27  ALA H CA  1 
ATOM   4007 C C   . ALA C 2 27  ? 22.831  33.179 -19.869 1.00 96.20  ? 27  ALA H C   1 
ATOM   4008 O O   . ALA C 2 27  ? 22.462  33.522 -20.996 1.00 99.09  ? 27  ALA H O   1 
ATOM   4009 C CB  . ALA C 2 27  ? 22.821  35.000 -18.144 1.00 103.46 ? 27  ALA H CB  1 
ATOM   4010 N N   . SER C 2 28  ? 22.525  32.010 -19.318 1.00 92.33  ? 28  SER H N   1 
ATOM   4011 C CA  . SER C 2 28  ? 21.608  31.082 -19.962 1.00 96.34  ? 28  SER H CA  1 
ATOM   4012 C C   . SER C 2 28  ? 20.180  31.525 -19.676 1.00 95.32  ? 28  SER H C   1 
ATOM   4013 O O   . SER C 2 28  ? 19.756  31.558 -18.514 1.00 99.52  ? 28  SER H O   1 
ATOM   4014 C CB  . SER C 2 28  ? 21.844  29.661 -19.458 1.00 102.13 ? 28  SER H CB  1 
ATOM   4015 O OG  . SER C 2 28  ? 20.906  29.310 -18.456 1.00 118.99 ? 28  SER H OG  1 
ATOM   4016 N N   . ILE C 2 29  ? 19.436  31.866 -20.730 1.00 92.45  ? 29  ILE H N   1 
ATOM   4017 C CA  . ILE C 2 29  ? 18.039  32.234 -20.563 1.00 96.11  ? 29  ILE H CA  1 
ATOM   4018 C C   . ILE C 2 29  ? 17.222  31.067 -20.013 1.00 95.37  ? 29  ILE H C   1 
ATOM   4019 O O   . ILE C 2 29  ? 16.106  31.263 -19.521 1.00 98.61  ? 29  ILE H O   1 
ATOM   4020 C CB  . ILE C 2 29  ? 17.485  32.769 -21.906 1.00 96.96  ? 29  ILE H CB  1 
ATOM   4021 C CG1 . ILE C 2 29  ? 18.133  34.105 -22.233 1.00 101.79 ? 29  ILE H CG1 1 
ATOM   4022 C CG2 . ILE C 2 29  ? 16.012  33.053 -21.829 1.00 98.90  ? 29  ILE H CG2 1 
ATOM   4023 C CD1 . ILE C 2 29  ? 17.433  34.847 -23.339 1.00 121.07 ? 29  ILE H CD1 1 
ATOM   4024 N N   . SER C 2 30  ? 17.781  29.855 -20.042 1.00 97.45  ? 30  SER H N   1 
ATOM   4025 C CA  . SER C 2 30  ? 17.110  28.707 -19.444 1.00 98.93  ? 30  SER H CA  1 
ATOM   4026 C C   . SER C 2 30  ? 16.952  28.862 -17.935 1.00 96.97  ? 30  SER H C   1 
ATOM   4027 O O   . SER C 2 30  ? 15.962  28.389 -17.365 1.00 96.89  ? 30  SER H O   1 
ATOM   4028 C CB  . SER C 2 30  ? 17.891  27.428 -19.752 1.00 102.48 ? 30  SER H CB  1 
ATOM   4029 O OG  . SER C 2 30  ? 18.294  27.386 -21.111 1.00 110.03 ? 30  SER H OG  1 
ATOM   4030 N N   . SER C 2 31  ? 17.903  29.527 -17.274 1.00 96.66  ? 31  SER H N   1 
ATOM   4031 C CA  . SER C 2 31  ? 18.027  29.469 -15.821 1.00 98.44  ? 31  SER H CA  1 
ATOM   4032 C C   . SER C 2 31  ? 17.722  30.796 -15.129 1.00 98.50  ? 31  SER H C   1 
ATOM   4033 O O   . SER C 2 31  ? 18.213  31.032 -14.021 1.00 99.55  ? 31  SER H O   1 
ATOM   4034 C CB  . SER C 2 31  ? 19.427  28.989 -15.434 1.00 105.54 ? 31  SER H CB  1 
ATOM   4035 O OG  . SER C 2 31  ? 20.429  29.639 -16.198 1.00 119.72 ? 31  SER H OG  1 
ATOM   4036 N N   . TYR C 2 32  ? 16.910  31.659 -15.738 1.00 97.78  ? 32  TYR H N   1 
ATOM   4037 C CA  . TYR C 2 32  ? 16.515  32.903 -15.091 1.00 89.76  ? 32  TYR H CA  1 
ATOM   4038 C C   . TYR C 2 32  ? 15.122  33.324 -15.545 1.00 92.18  ? 32  TYR H C   1 
ATOM   4039 O O   . TYR C 2 32  ? 14.695  33.031 -16.669 1.00 93.93  ? 32  TYR H O   1 
ATOM   4040 C CB  . TYR C 2 32  ? 17.508  34.040 -15.372 1.00 92.31  ? 32  TYR H CB  1 
ATOM   4041 C CG  . TYR C 2 32  ? 18.723  34.080 -14.463 1.00 95.39  ? 32  TYR H CG  1 
ATOM   4042 C CD1 . TYR C 2 32  ? 18.664  34.710 -13.226 1.00 99.13  ? 32  TYR H CD1 1 
ATOM   4043 C CD2 . TYR C 2 32  ? 19.935  33.517 -14.851 1.00 99.35  ? 32  TYR H CD2 1 
ATOM   4044 C CE1 . TYR C 2 32  ? 19.766  34.760 -12.393 1.00 118.08 ? 32  TYR H CE1 1 
ATOM   4045 C CE2 . TYR C 2 32  ? 21.044  33.563 -14.024 1.00 107.86 ? 32  TYR H CE2 1 
ATOM   4046 C CZ  . TYR C 2 32  ? 20.953  34.188 -12.799 1.00 110.93 ? 32  TYR H CZ  1 
ATOM   4047 O OH  . TYR C 2 32  ? 22.052  34.234 -11.973 1.00 124.13 ? 32  TYR H OH  1 
ATOM   4048 N N   . TYR C 2 33  ? 14.418  34.010 -14.643 1.00 87.90  ? 33  TYR H N   1 
ATOM   4049 C CA  . TYR C 2 33  ? 13.231  34.779 -14.994 1.00 86.81  ? 33  TYR H CA  1 
ATOM   4050 C C   . TYR C 2 33  ? 13.575  36.100 -15.657 1.00 78.69  ? 33  TYR H C   1 
ATOM   4051 O O   . TYR C 2 33  ? 14.555  36.770 -15.316 1.00 78.80  ? 33  TYR H O   1 
ATOM   4052 C CB  . TYR C 2 33  ? 12.382  35.059 -13.762 1.00 93.37  ? 33  TYR H CB  1 
ATOM   4053 C CG  . TYR C 2 33  ? 11.488  33.940 -13.319 1.00 105.03 ? 33  TYR H CG  1 
ATOM   4054 C CD1 . TYR C 2 33  ? 11.947  32.938 -12.479 1.00 114.72 ? 33  TYR H CD1 1 
ATOM   4055 C CD2 . TYR C 2 33  ? 10.134  33.947 -13.659 1.00 113.76 ? 33  TYR H CD2 1 
ATOM   4056 C CE1 . TYR C 2 33  ? 11.111  31.937 -12.058 1.00 120.43 ? 33  TYR H CE1 1 
ATOM   4057 C CE2 . TYR C 2 33  ? 9.285   32.949 -13.223 1.00 124.08 ? 33  TYR H CE2 1 
ATOM   4058 C CZ  . TYR C 2 33  ? 9.787   31.940 -12.430 1.00 125.88 ? 33  TYR H CZ  1 
ATOM   4059 O OH  . TYR C 2 33  ? 8.969   30.932 -11.984 1.00 135.21 ? 33  TYR H OH  1 
ATOM   4060 N N   . TRP C 2 34  ? 12.715  36.493 -16.582 1.00 78.85  ? 34  TRP H N   1 
ATOM   4061 C CA  . TRP C 2 34  ? 12.929  37.682 -17.380 1.00 82.76  ? 34  TRP H CA  1 
ATOM   4062 C C   . TRP C 2 34  ? 11.691  38.561 -17.303 1.00 79.83  ? 34  TRP H C   1 
ATOM   4063 O O   . TRP C 2 34  ? 10.565  38.069 -17.162 1.00 81.96  ? 34  TRP H O   1 
ATOM   4064 C CB  . TRP C 2 34  ? 13.255  37.307 -18.814 1.00 88.10  ? 34  TRP H CB  1 
ATOM   4065 C CG  . TRP C 2 34  ? 14.448  36.416 -18.896 1.00 88.96  ? 34  TRP H CG  1 
ATOM   4066 C CD1 . TRP C 2 34  ? 14.454  35.064 -19.088 1.00 92.76  ? 34  TRP H CD1 1 
ATOM   4067 C CD2 . TRP C 2 34  ? 15.815  36.806 -18.740 1.00 87.84  ? 34  TRP H CD2 1 
ATOM   4068 N NE1 . TRP C 2 34  ? 15.746  34.594 -19.087 1.00 95.72  ? 34  TRP H NE1 1 
ATOM   4069 C CE2 . TRP C 2 34  ? 16.600  35.645 -18.877 1.00 93.31  ? 34  TRP H CE2 1 
ATOM   4070 C CE3 . TRP C 2 34  ? 16.453  38.028 -18.511 1.00 83.66  ? 34  TRP H CE3 1 
ATOM   4071 C CZ2 . TRP C 2 34  ? 17.989  35.670 -18.791 1.00 89.43  ? 34  TRP H CZ2 1 
ATOM   4072 C CZ3 . TRP C 2 34  ? 17.832  38.050 -18.427 1.00 87.29  ? 34  TRP H CZ3 1 
ATOM   4073 C CH2 . TRP C 2 34  ? 18.585  36.879 -18.566 1.00 82.62  ? 34  TRP H CH2 1 
ATOM   4074 N N   . ILE C 2 35  ? 11.922  39.868 -17.393 1.00 68.54  ? 35  ILE H N   1 
ATOM   4075 C CA  . ILE C 2 35  ? 10.913  40.879 -17.125 1.00 64.90  ? 35  ILE H CA  1 
ATOM   4076 C C   . ILE C 2 35  ? 10.791  41.792 -18.332 1.00 70.65  ? 35  ILE H C   1 
ATOM   4077 O O   . ILE C 2 35  ? 11.803  42.201 -18.914 1.00 71.86  ? 35  ILE H O   1 
ATOM   4078 C CB  . ILE C 2 35  ? 11.280  41.705 -15.878 1.00 68.28  ? 35  ILE H CB  1 
ATOM   4079 C CG1 . ILE C 2 35  ? 11.050  40.894 -14.617 1.00 80.08  ? 35  ILE H CG1 1 
ATOM   4080 C CG2 . ILE C 2 35  ? 10.461  42.968 -15.810 1.00 69.72  ? 35  ILE H CG2 1 
ATOM   4081 C CD1 . ILE C 2 35  ? 11.406  41.651 -13.372 1.00 106.05 ? 35  ILE H CD1 1 
ATOM   4082 N N   . TRP C 2 36  ? 9.552   42.128 -18.687 1.00 69.61  ? 36  TRP H N   1 
ATOM   4083 C CA  . TRP C 2 36  ? 9.261   43.212 -19.618 1.00 67.81  ? 36  TRP H CA  1 
ATOM   4084 C C   . TRP C 2 36  ? 8.598   44.359 -18.866 1.00 67.02  ? 36  TRP H C   1 
ATOM   4085 O O   . TRP C 2 36  ? 7.660   44.129 -18.085 1.00 72.14  ? 36  TRP H O   1 
ATOM   4086 C CB  . TRP C 2 36  ? 8.360   42.734 -20.756 1.00 74.10  ? 36  TRP H CB  1 
ATOM   4087 C CG  . TRP C 2 36  ? 9.103   42.095 -21.889 1.00 70.47  ? 36  TRP H CG  1 
ATOM   4088 C CD1 . TRP C 2 36  ? 8.947   40.821 -22.345 1.00 73.18  ? 36  TRP H CD1 1 
ATOM   4089 C CD2 . TRP C 2 36  ? 10.088  42.706 -22.735 1.00 67.03  ? 36  TRP H CD2 1 
ATOM   4090 N NE1 . TRP C 2 36  ? 9.789   40.591 -23.406 1.00 75.98  ? 36  TRP H NE1 1 
ATOM   4091 C CE2 . TRP C 2 36  ? 10.496  41.734 -23.669 1.00 69.26  ? 36  TRP H CE2 1 
ATOM   4092 C CE3 . TRP C 2 36  ? 10.666  43.977 -22.792 1.00 70.12  ? 36  TRP H CE3 1 
ATOM   4093 C CZ2 . TRP C 2 36  ? 11.454  41.991 -24.643 1.00 72.62  ? 36  TRP H CZ2 1 
ATOM   4094 C CZ3 . TRP C 2 36  ? 11.621  44.229 -23.761 1.00 73.47  ? 36  TRP H CZ3 1 
ATOM   4095 C CH2 . TRP C 2 36  ? 12.004  43.241 -24.672 1.00 70.24  ? 36  TRP H CH2 1 
ATOM   4096 N N   . ILE C 2 37  ? 9.093   45.585 -19.108 1.00 68.72  ? 37  ILE H N   1 
ATOM   4097 C CA  . ILE C 2 37  ? 8.592   46.814 -18.495 1.00 71.62  ? 37  ILE H CA  1 
ATOM   4098 C C   . ILE C 2 37  ? 8.459   47.909 -19.553 1.00 70.83  ? 37  ILE H C   1 
ATOM   4099 O O   . ILE C 2 37  ? 9.200   47.945 -20.542 1.00 75.22  ? 37  ILE H O   1 
ATOM   4100 C CB  . ILE C 2 37  ? 9.498   47.275 -17.321 1.00 59.96  ? 37  ILE H CB  1 
ATOM   4101 C CG1 . ILE C 2 37  ? 9.393   46.296 -16.157 1.00 62.38  ? 37  ILE H CG1 1 
ATOM   4102 C CG2 . ILE C 2 37  ? 9.171   48.679 -16.837 1.00 61.94  ? 37  ILE H CG2 1 
ATOM   4103 C CD1 . ILE C 2 37  ? 10.523  46.407 -15.177 1.00 71.19  ? 37  ILE H CD1 1 
ATOM   4104 N N   . ARG C 2 38  ? 7.503   48.814 -19.326 1.00 66.74  ? 38  ARG H N   1 
ATOM   4105 C CA  . ARG C 2 38  ? 7.077   49.833 -20.278 1.00 62.25  ? 38  ARG H CA  1 
ATOM   4106 C C   . ARG C 2 38  ? 7.216   51.226 -19.670 1.00 68.30  ? 38  ARG H C   1 
ATOM   4107 O O   . ARG C 2 38  ? 6.997   51.414 -18.468 1.00 78.52  ? 38  ARG H O   1 
ATOM   4108 C CB  . ARG C 2 38  ? 5.617   49.567 -20.692 1.00 66.17  ? 38  ARG H CB  1 
ATOM   4109 C CG  . ARG C 2 38  ? 5.138   50.266 -21.944 1.00 72.24  ? 38  ARG H CG  1 
ATOM   4110 C CD  . ARG C 2 38  ? 4.116   49.402 -22.701 1.00 71.84  ? 38  ARG H CD  1 
ATOM   4111 N NE  . ARG C 2 38  ? 2.787   49.272 -22.106 1.00 67.10  ? 38  ARG H NE  1 
ATOM   4112 C CZ  . ARG C 2 38  ? 2.001   50.270 -21.721 1.00 79.84  ? 38  ARG H CZ  1 
ATOM   4113 N NH1 . ARG C 2 38  ? 2.349   51.535 -21.883 1.00 107.38 ? 38  ARG H NH1 1 
ATOM   4114 N NH2 . ARG C 2 38  ? 0.815   49.989 -21.185 1.00 81.78  ? 38  ARG H NH2 1 
ATOM   4115 N N   . GLN C 2 39  ? 7.584   52.202 -20.500 1.00 65.41  ? 39  GLN H N   1 
ATOM   4116 C CA  . GLN C 2 39  ? 7.637   53.607 -20.095 1.00 69.40  ? 39  GLN H CA  1 
ATOM   4117 C C   . GLN C 2 39  ? 7.123   54.484 -21.229 1.00 69.82  ? 39  GLN H C   1 
ATOM   4118 O O   . GLN C 2 39  ? 7.844   54.734 -22.208 1.00 70.13  ? 39  GLN H O   1 
ATOM   4119 C CB  . GLN C 2 39  ? 9.041   54.043 -19.690 1.00 64.85  ? 39  GLN H CB  1 
ATOM   4120 C CG  . GLN C 2 39  ? 9.026   55.353 -18.920 1.00 71.61  ? 39  GLN H CG  1 
ATOM   4121 C CD  . GLN C 2 39  ? 10.398  55.807 -18.478 1.00 74.78  ? 39  GLN H CD  1 
ATOM   4122 O OE1 . GLN C 2 39  ? 11.414  55.290 -18.940 1.00 77.43  ? 39  GLN H OE1 1 
ATOM   4123 N NE2 . GLN C 2 39  ? 10.435  56.785 -17.577 1.00 77.99  ? 39  GLN H NE2 1 
ATOM   4124 N N   . PRO C 2 40  ? 5.877   54.941 -21.151 1.00 73.39  ? 40  PRO H N   1 
ATOM   4125 C CA  . PRO C 2 40  ? 5.375   55.888 -22.156 1.00 76.71  ? 40  PRO H CA  1 
ATOM   4126 C C   . PRO C 2 40  ? 5.932   57.286 -21.928 1.00 83.27  ? 40  PRO H C   1 
ATOM   4127 O O   . PRO C 2 40  ? 5.830   57.838 -20.830 1.00 90.24  ? 40  PRO H O   1 
ATOM   4128 C CB  . PRO C 2 40  ? 3.853   55.847 -21.959 1.00 84.84  ? 40  PRO H CB  1 
ATOM   4129 C CG  . PRO C 2 40  ? 3.643   55.167 -20.631 1.00 84.66  ? 40  PRO H CG  1 
ATOM   4130 C CD  . PRO C 2 40  ? 4.787   54.245 -20.450 1.00 79.11  ? 40  PRO H CD  1 
ATOM   4131 N N   . ALA C 2 41  ? 6.515   57.856 -22.986 1.00 83.55  ? 41  ALA H N   1 
ATOM   4132 C CA  . ALA C 2 41  ? 6.973   59.254 -23.025 1.00 89.42  ? 41  ALA H CA  1 
ATOM   4133 C C   . ALA C 2 41  ? 7.857   59.503 -21.802 1.00 96.90  ? 41  ALA H C   1 
ATOM   4134 O O   . ALA C 2 41  ? 8.809   58.743 -21.578 1.00 96.79  ? 41  ALA H O   1 
ATOM   4135 C CB  . ALA C 2 41  ? 5.763   60.166 -23.157 1.00 83.76  ? 41  ALA H CB  1 
ATOM   4136 N N   . GLY C 2 42  ? 7.590   60.529 -20.999 1.00 94.18  ? 42  GLY H N   1 
ATOM   4137 C CA  . GLY C 2 42  ? 8.274   60.724 -19.742 1.00 94.62  ? 42  GLY H CA  1 
ATOM   4138 C C   . GLY C 2 42  ? 7.523   60.213 -18.537 1.00 104.96 ? 42  GLY H C   1 
ATOM   4139 O O   . GLY C 2 42  ? 8.019   60.344 -17.414 1.00 108.11 ? 42  GLY H O   1 
ATOM   4140 N N   . LYS C 2 43  ? 6.344   59.627 -18.736 1.00 97.56  ? 43  LYS H N   1 
ATOM   4141 C CA  . LYS C 2 43  ? 5.541   59.116 -17.638 1.00 96.53  ? 43  LYS H CA  1 
ATOM   4142 C C   . LYS C 2 43  ? 6.248   57.949 -16.947 1.00 87.62  ? 43  LYS H C   1 
ATOM   4143 O O   . LYS C 2 43  ? 7.327   57.503 -17.350 1.00 78.60  ? 43  LYS H O   1 
ATOM   4144 C CB  . LYS C 2 43  ? 4.162   58.694 -18.144 1.00 93.49  ? 43  LYS H CB  1 
ATOM   4145 C CG  . LYS C 2 43  ? 3.346   59.851 -18.704 1.00 97.81  ? 43  LYS H CG  1 
ATOM   4146 C CD  . LYS C 2 43  ? 2.148   59.377 -19.512 1.00 114.26 ? 43  LYS H CD  1 
ATOM   4147 C CE  . LYS C 2 43  ? 2.475   59.323 -20.996 1.00 147.06 ? 43  LYS H CE  1 
ATOM   4148 N NZ  . LYS C 2 43  ? 1.455   58.564 -21.771 1.00 167.38 ? 43  LYS H NZ  1 
ATOM   4149 N N   . GLY C 2 44  ? 5.614   57.448 -15.893 1.00 92.97  ? 44  GLY H N   1 
ATOM   4150 C CA  . GLY C 2 44  ? 6.222   56.452 -15.039 1.00 83.35  ? 44  GLY H CA  1 
ATOM   4151 C C   . GLY C 2 44  ? 6.412   55.106 -15.719 1.00 78.06  ? 44  GLY H C   1 
ATOM   4152 O O   . GLY C 2 44  ? 6.059   54.882 -16.878 1.00 77.51  ? 44  GLY H O   1 
ATOM   4153 N N   . LEU C 2 45  ? 6.999   54.189 -14.957 1.00 73.30  ? 45  LEU H N   1 
ATOM   4154 C CA  . LEU C 2 45  ? 7.260   52.832 -15.409 1.00 66.18  ? 45  LEU H CA  1 
ATOM   4155 C C   . LEU C 2 45  ? 6.039   51.953 -15.173 1.00 71.84  ? 45  LEU H C   1 
ATOM   4156 O O   . LEU C 2 45  ? 5.283   52.144 -14.216 1.00 77.86  ? 45  LEU H O   1 
ATOM   4157 C CB  . LEU C 2 45  ? 8.468   52.246 -14.677 1.00 69.08  ? 45  LEU H CB  1 
ATOM   4158 C CG  . LEU C 2 45  ? 9.787   52.998 -14.851 1.00 70.68  ? 45  LEU H CG  1 
ATOM   4159 C CD1 . LEU C 2 45  ? 10.903  52.305 -14.092 1.00 72.62  ? 45  LEU H CD1 1 
ATOM   4160 C CD2 . LEU C 2 45  ? 10.136  53.107 -16.323 1.00 82.42  ? 45  LEU H CD2 1 
ATOM   4161 N N   . GLU C 2 46  ? 5.849   50.981 -16.061 1.00 71.28  ? 46  GLU H N   1 
ATOM   4162 C CA  . GLU C 2 46  ? 4.771   50.009 -15.930 1.00 69.56  ? 46  GLU H CA  1 
ATOM   4163 C C   . GLU C 2 46  ? 5.331   48.619 -16.180 1.00 63.81  ? 46  GLU H C   1 
ATOM   4164 O O   . GLU C 2 46  ? 5.868   48.345 -17.258 1.00 70.66  ? 46  GLU H O   1 
ATOM   4165 C CB  . GLU C 2 46  ? 3.618   50.318 -16.890 1.00 66.81  ? 46  GLU H CB  1 
ATOM   4166 C CG  . GLU C 2 46  ? 2.526   49.261 -16.884 1.00 72.87  ? 46  GLU H CG  1 
ATOM   4167 C CD  . GLU C 2 46  ? 1.336   49.646 -17.736 1.00 83.11  ? 46  GLU H CD  1 
ATOM   4168 O OE1 . GLU C 2 46  ? 1.547   50.239 -18.815 1.00 89.71  ? 46  GLU H OE1 1 
ATOM   4169 O OE2 . GLU C 2 46  ? 0.193   49.343 -17.336 1.00 75.00  ? 46  GLU H OE2 1 
ATOM   4170 N N   . TRP C 2 47  ? 5.201   47.751 -15.184 1.00 59.47  ? 47  TRP H N   1 
ATOM   4171 C CA  . TRP C 2 47  ? 5.711   46.389 -15.258 1.00 64.17  ? 47  TRP H CA  1 
ATOM   4172 C C   . TRP C 2 47  ? 4.756   45.533 -16.081 1.00 65.52  ? 47  TRP H C   1 
ATOM   4173 O O   . TRP C 2 47  ? 3.585   45.375 -15.722 1.00 69.95  ? 47  TRP H O   1 
ATOM   4174 C CB  . TRP C 2 47  ? 5.911   45.856 -13.838 1.00 72.13  ? 47  TRP H CB  1 
ATOM   4175 C CG  . TRP C 2 47  ? 6.176   44.384 -13.672 1.00 72.58  ? 47  TRP H CG  1 
ATOM   4176 C CD1 . TRP C 2 47  ? 7.387   43.799 -13.454 1.00 71.06  ? 47  TRP H CD1 1 
ATOM   4177 C CD2 . TRP C 2 47  ? 5.199   43.335 -13.547 1.00 71.08  ? 47  TRP H CD2 1 
ATOM   4178 N NE1 . TRP C 2 47  ? 7.236   42.443 -13.287 1.00 75.57  ? 47  TRP H NE1 1 
ATOM   4179 C CE2 . TRP C 2 47  ? 5.902   42.135 -13.331 1.00 73.43  ? 47  TRP H CE2 1 
ATOM   4180 C CE3 . TRP C 2 47  ? 3.804   43.291 -13.631 1.00 72.70  ? 47  TRP H CE3 1 
ATOM   4181 C CZ2 . TRP C 2 47  ? 5.260   40.907 -13.200 1.00 75.88  ? 47  TRP H CZ2 1 
ATOM   4182 C CZ3 . TRP C 2 47  ? 3.169   42.069 -13.504 1.00 74.07  ? 47  TRP H CZ3 1 
ATOM   4183 C CH2 . TRP C 2 47  ? 3.897   40.895 -13.290 1.00 74.53  ? 47  TRP H CH2 1 
ATOM   4184 N N   . ILE C 2 48  ? 5.226   45.036 -17.227 1.00 68.89  ? 48  ILE H N   1 
ATOM   4185 C CA  . ILE C 2 48  ? 4.331   44.282 -18.156 1.00 70.05  ? 48  ILE H CA  1 
ATOM   4186 C C   . ILE C 2 48  ? 4.169   42.833 -17.691 1.00 78.34  ? 48  ILE H C   1 
ATOM   4187 O O   . ILE C 2 48  ? 3.015   42.394 -17.559 1.00 76.81  ? 48  ILE H O   1 
ATOM   4188 C CB  . ILE C 2 48  ? 4.870   44.347 -19.595 1.00 64.62  ? 48  ILE H CB  1 
ATOM   4189 C CG1 . ILE C 2 48  ? 5.234   45.776 -20.001 1.00 66.92  ? 48  ILE H CG1 1 
ATOM   4190 C CG2 . ILE C 2 48  ? 3.884   43.719 -20.566 1.00 67.99  ? 48  ILE H CG2 1 
ATOM   4191 C CD1 . ILE C 2 48  ? 5.878   45.873 -21.361 1.00 67.72  ? 48  ILE H CD1 1 
ATOM   4192 N N   . GLY C 2 49  ? 5.268   42.109 -17.466 1.00 74.34  ? 49  GLY H N   1 
ATOM   4193 C CA  . GLY C 2 49  ? 5.104   40.688 -17.104 1.00 77.64  ? 49  GLY H CA  1 
ATOM   4194 C C   . GLY C 2 49  ? 6.385   39.962 -16.741 1.00 80.87  ? 49  GLY H C   1 
ATOM   4195 O O   . GLY C 2 49  ? 7.462   40.568 -16.868 1.00 74.80  ? 49  GLY H O   1 
ATOM   4196 N N   . ARG C 2 50  ? 6.264   38.700 -16.319 1.00 70.52  ? 50  ARG H N   1 
ATOM   4197 C CA  . ARG C 2 50  ? 7.428   37.882 -15.904 1.00 68.42  ? 50  ARG H CA  1 
ATOM   4198 C C   . ARG C 2 50  ? 7.342   36.540 -16.628 1.00 71.44  ? 50  ARG H C   1 
ATOM   4199 O O   . ARG C 2 50  ? 6.215   36.067 -16.812 1.00 74.27  ? 50  ARG H O   1 
ATOM   4200 C CB  . ARG C 2 50  ? 7.322   37.641 -14.402 1.00 85.56  ? 50  ARG H CB  1 
ATOM   4201 C CG  . ARG C 2 50  ? 8.561   38.013 -13.603 1.00 96.18  ? 50  ARG H CG  1 
ATOM   4202 C CD  . ARG C 2 50  ? 8.201   38.280 -12.154 1.00 105.85 ? 50  ARG H CD  1 
ATOM   4203 N NE  . ARG C 2 50  ? 7.275   37.302 -11.599 1.00 158.18 ? 50  ARG H NE  1 
ATOM   4204 C CZ  . ARG C 2 50  ? 7.531   36.009 -11.442 1.00 178.76 ? 50  ARG H CZ  1 
ATOM   4205 N NH1 . ARG C 2 50  ? 8.760   35.602 -11.184 1.00 199.64 ? 50  ARG H NH1 1 
ATOM   4206 N NH2 . ARG C 2 50  ? 6.551   35.127 -11.525 1.00 148.41 ? 50  ARG H NH2 1 
ATOM   4207 N N   . PHE C 2 51  ? 8.475   35.941 -17.004 1.00 86.06  ? 51  PHE H N   1 
ATOM   4208 C CA  . PHE C 2 51  ? 8.417   34.596 -17.632 1.00 91.24  ? 51  PHE H CA  1 
ATOM   4209 C C   . PHE C 2 51  ? 9.624   33.745 -17.240 1.00 93.18  ? 51  PHE H C   1 
ATOM   4210 O O   . PHE C 2 51  ? 10.656  34.316 -16.857 1.00 91.20  ? 51  PHE H O   1 
ATOM   4211 C CB  . PHE C 2 51  ? 8.371   34.700 -19.154 1.00 91.93  ? 51  PHE H CB  1 
ATOM   4212 C CG  . PHE C 2 51  ? 8.062   33.402 -19.854 1.00 94.06  ? 51  PHE H CG  1 
ATOM   4213 C CD1 . PHE C 2 51  ? 6.877   32.731 -19.607 1.00 96.59  ? 51  PHE H CD1 1 
ATOM   4214 C CD2 . PHE C 2 51  ? 8.958   32.846 -20.749 1.00 98.58  ? 51  PHE H CD2 1 
ATOM   4215 C CE1 . PHE C 2 51  ? 6.591   31.535 -20.245 1.00 100.18 ? 51  PHE H CE1 1 
ATOM   4216 C CE2 . PHE C 2 51  ? 8.673   31.650 -21.387 1.00 100.66 ? 51  PHE H CE2 1 
ATOM   4217 C CZ  . PHE C 2 51  ? 7.490   30.997 -21.134 1.00 111.45 ? 51  PHE H CZ  1 
ATOM   4218 N N   . TYR C 2 52  ? 9.488   32.422 -17.353 1.00 100.77 ? 52  TYR H N   1 
ATOM   4219 C CA  . TYR C 2 52  ? 10.599  31.489 -17.031 1.00 105.85 ? 52  TYR H CA  1 
ATOM   4220 C C   . TYR C 2 52  ? 10.379  30.199 -17.816 1.00 113.04 ? 52  TYR H C   1 
ATOM   4221 O O   . TYR C 2 52  ? 9.255   29.669 -17.792 1.00 114.35 ? 52  TYR H O   1 
ATOM   4222 C CB  . TYR C 2 52  ? 10.661  31.216 -15.532 1.00 112.33 ? 52  TYR H CB  1 
ATOM   4223 C CG  . TYR C 2 52  ? 11.768  30.309 -15.060 1.00 115.08 ? 52  TYR H CG  1 
ATOM   4224 C CD1 . TYR C 2 52  ? 13.088  30.544 -15.404 1.00 108.32 ? 52  TYR H CD1 1 
ATOM   4225 C CD2 . TYR C 2 52  ? 11.501  29.248 -14.214 1.00 115.83 ? 52  TYR H CD2 1 
ATOM   4226 C CE1 . TYR C 2 52  ? 14.107  29.723 -14.953 1.00 109.79 ? 52  TYR H CE1 1 
ATOM   4227 C CE2 . TYR C 2 52  ? 12.508  28.420 -13.748 1.00 108.90 ? 52  TYR H CE2 1 
ATOM   4228 C CZ  . TYR C 2 52  ? 13.817  28.657 -14.122 1.00 107.97 ? 52  TYR H CZ  1 
ATOM   4229 O OH  . TYR C 2 52  ? 14.815  27.835 -13.664 1.00 109.28 ? 52  TYR H OH  1 
ATOM   4230 N N   . THR C 2 53  ? 11.422  29.709 -18.476 1.00 115.30 ? 53  THR H N   1 
ATOM   4231 C CA  . THR C 2 53  ? 11.286  28.541 -19.341 1.00 113.04 ? 53  THR H CA  1 
ATOM   4232 C C   . THR C 2 53  ? 10.615  27.390 -18.607 1.00 112.71 ? 53  THR H C   1 
ATOM   4233 O O   . THR C 2 53  ? 9.778   26.679 -19.176 1.00 106.27 ? 53  THR H O   1 
ATOM   4234 C CB  . THR C 2 53  ? 12.654  28.104 -19.856 1.00 106.65 ? 53  THR H CB  1 
ATOM   4235 O OG1 . THR C 2 53  ? 13.507  27.811 -18.744 1.00 113.73 ? 53  THR H OG1 1 
ATOM   4236 C CG2 . THR C 2 53  ? 13.282  29.208 -20.657 1.00 100.09 ? 53  THR H CG2 1 
ATOM   4237 N N   . SER C 2 54  ? 10.965  27.195 -17.343 1.00 116.36 ? 54  SER H N   1 
ATOM   4238 C CA  . SER C 2 54  ? 10.466  26.096 -16.531 1.00 115.99 ? 54  SER H CA  1 
ATOM   4239 C C   . SER C 2 54  ? 9.716   26.618 -15.311 1.00 114.11 ? 54  SER H C   1 
ATOM   4240 O O   . SER C 2 54  ? 9.887   26.131 -14.194 1.00 119.29 ? 54  SER H O   1 
ATOM   4241 C CB  . SER C 2 54  ? 11.610  25.173 -16.119 1.00 119.06 ? 54  SER H CB  1 
ATOM   4242 O OG  . SER C 2 54  ? 12.654  25.901 -15.495 1.00 123.86 ? 54  SER H OG  1 
ATOM   4243 N N   . GLY C 2 55  ? 8.872   27.624 -15.516 1.00 117.91 ? 55  GLY H N   1 
ATOM   4244 C CA  . GLY C 2 55  ? 8.100   28.207 -14.436 1.00 119.85 ? 55  GLY H CA  1 
ATOM   4245 C C   . GLY C 2 55  ? 6.939   29.031 -14.952 1.00 121.44 ? 55  GLY H C   1 
ATOM   4246 O O   . GLY C 2 55  ? 7.103   29.807 -15.899 1.00 122.48 ? 55  GLY H O   1 
ATOM   4247 N N   . SER C 2 56  ? 5.764   28.870 -14.346 1.00 117.06 ? 56  SER H N   1 
ATOM   4248 C CA  . SER C 2 56  ? 4.571   29.529 -14.856 1.00 115.77 ? 56  SER H CA  1 
ATOM   4249 C C   . SER C 2 56  ? 4.740   31.045 -14.800 1.00 115.94 ? 56  SER H C   1 
ATOM   4250 O O   . SER C 2 56  ? 5.348   31.572 -13.855 1.00 115.75 ? 56  SER H O   1 
ATOM   4251 C CB  . SER C 2 56  ? 3.336   29.106 -14.057 1.00 115.19 ? 56  SER H CB  1 
ATOM   4252 O OG  . SER C 2 56  ? 3.612   29.073 -12.669 1.00 118.75 ? 56  SER H OG  1 
ATOM   4253 N N   . PRO C 2 57  ? 4.209   31.804 -15.790 1.00 102.49 ? 57  PRO H N   1 
ATOM   4254 C CA  . PRO C 2 57  ? 4.419   33.242 -15.832 1.00 93.43  ? 57  PRO H CA  1 
ATOM   4255 C C   . PRO C 2 57  ? 3.300   34.071 -15.195 1.00 93.88  ? 57  PRO H C   1 
ATOM   4256 O O   . PRO C 2 57  ? 2.230   33.549 -14.981 1.00 99.52  ? 57  PRO H O   1 
ATOM   4257 C CB  . PRO C 2 57  ? 4.403   33.482 -17.342 1.00 88.81  ? 57  PRO H CB  1 
ATOM   4258 C CG  . PRO C 2 57  ? 3.321   32.565 -17.845 1.00 91.82  ? 57  PRO H CG  1 
ATOM   4259 C CD  . PRO C 2 57  ? 3.405   31.354 -16.942 1.00 100.54 ? 57  PRO H CD  1 
ATOM   4260 N N   . ASN C 2 58  ? 3.589   35.339 -14.905 1.00 95.70  ? 58  ASN H N   1 
ATOM   4261 C CA  . ASN C 2 58  ? 2.570   36.251 -14.330 1.00 97.18  ? 58  ASN H CA  1 
ATOM   4262 C C   . ASN C 2 58  ? 2.608   37.555 -15.126 1.00 93.35  ? 58  ASN H C   1 
ATOM   4263 O O   . ASN C 2 58  ? 3.684   38.169 -15.188 1.00 91.73  ? 58  ASN H O   1 
ATOM   4264 C CB  . ASN C 2 58  ? 2.810   36.491 -12.841 1.00 102.78 ? 58  ASN H CB  1 
ATOM   4265 C CG  . ASN C 2 58  ? 1.778   37.397 -12.203 1.00 109.17 ? 58  ASN H CG  1 
ATOM   4266 O OD1 . ASN C 2 58  ? 1.658   38.567 -12.562 1.00 101.95 ? 58  ASN H OD1 1 
ATOM   4267 N ND2 . ASN C 2 58  ? 1.037   36.871 -11.242 1.00 120.29 ? 58  ASN H ND2 1 
ATOM   4268 N N   . TYR C 2 59  ? 1.477   37.948 -15.712 1.00 93.94  ? 59  TYR H N   1 
ATOM   4269 C CA  . TYR C 2 59  ? 1.431   39.174 -16.545 1.00 90.84  ? 59  TYR H CA  1 
ATOM   4270 C C   . TYR C 2 59  ? 0.552   40.229 -15.872 1.00 91.87  ? 59  TYR H C   1 
ATOM   4271 O O   . TYR C 2 59  ? -0.367  39.858 -15.123 1.00 92.64  ? 59  TYR H O   1 
ATOM   4272 C CB  . TYR C 2 59  ? 0.903   38.850 -17.942 1.00 94.51  ? 59  TYR H CB  1 
ATOM   4273 C CG  . TYR C 2 59  ? 1.666   37.801 -18.708 1.00 93.19  ? 59  TYR H CG  1 
ATOM   4274 C CD1 . TYR C 2 59  ? 3.029   37.913 -18.918 1.00 93.07  ? 59  TYR H CD1 1 
ATOM   4275 C CD2 . TYR C 2 59  ? 1.015   36.712 -19.261 1.00 93.74  ? 59  TYR H CD2 1 
ATOM   4276 C CE1 . TYR C 2 59  ? 3.731   36.958 -19.634 1.00 87.27  ? 59  TYR H CE1 1 
ATOM   4277 C CE2 . TYR C 2 59  ? 1.700   35.749 -19.981 1.00 100.07 ? 59  TYR H CE2 1 
ATOM   4278 C CZ  . TYR C 2 59  ? 3.063   35.872 -20.168 1.00 91.02  ? 59  TYR H CZ  1 
ATOM   4279 O OH  . TYR C 2 59  ? 3.745   34.917 -20.881 1.00 92.86  ? 59  TYR H OH  1 
ATOM   4280 N N   . ASN C 2 60  ? 0.823   41.505 -16.140 1.00 87.47  ? 60  ASN H N   1 
ATOM   4281 C CA  . ASN C 2 60  ? 0.077   42.600 -15.536 1.00 87.08  ? 60  ASN H CA  1 
ATOM   4282 C C   . ASN C 2 60  ? -1.376  42.531 -15.999 1.00 95.29  ? 60  ASN H C   1 
ATOM   4283 O O   . ASN C 2 60  ? -1.631  42.438 -17.208 1.00 103.20 ? 60  ASN H O   1 
ATOM   4284 C CB  . ASN C 2 60  ? 0.719   43.936 -15.928 1.00 84.40  ? 60  ASN H CB  1 
ATOM   4285 C CG  . ASN C 2 60  ? 0.051   45.142 -15.276 1.00 90.57  ? 60  ASN H CG  1 
ATOM   4286 O OD1 . ASN C 2 60  ? -0.789  45.009 -14.390 1.00 96.51  ? 60  ASN H OD1 1 
ATOM   4287 N ND2 . ASN C 2 60  ? 0.436   46.335 -15.719 1.00 87.60  ? 60  ASN H ND2 1 
ATOM   4288 N N   . PRO C 2 61  ? -2.349  42.540 -15.080 1.00 96.44  ? 61  PRO H N   1 
ATOM   4289 C CA  . PRO C 2 61  ? -3.754  42.350 -15.491 1.00 99.45  ? 61  PRO H CA  1 
ATOM   4290 C C   . PRO C 2 61  ? -4.265  43.344 -16.526 1.00 95.63  ? 61  PRO H C   1 
ATOM   4291 O O   . PRO C 2 61  ? -5.159  42.990 -17.305 1.00 94.66  ? 61  PRO H O   1 
ATOM   4292 C CB  . PRO C 2 61  ? -4.512  42.480 -14.163 1.00 100.06 ? 61  PRO H CB  1 
ATOM   4293 C CG  . PRO C 2 61  ? -3.546  41.956 -13.157 1.00 102.62 ? 61  PRO H CG  1 
ATOM   4294 C CD  . PRO C 2 61  ? -2.195  42.450 -13.615 1.00 98.67  ? 61  PRO H CD  1 
ATOM   4295 N N   . SER C 2 62  ? -3.745  44.575 -16.560 1.00 94.50  ? 62  SER H N   1 
ATOM   4296 C CA  . SER C 2 62  ? -4.203  45.528 -17.569 1.00 94.07  ? 62  SER H CA  1 
ATOM   4297 C C   . SER C 2 62  ? -3.898  45.026 -18.974 1.00 98.41  ? 62  SER H C   1 
ATOM   4298 O O   . SER C 2 62  ? -4.691  45.220 -19.903 1.00 109.00 ? 62  SER H O   1 
ATOM   4299 C CB  . SER C 2 62  ? -3.554  46.895 -17.342 1.00 99.20  ? 62  SER H CB  1 
ATOM   4300 O OG  . SER C 2 62  ? -2.204  46.767 -16.925 1.00 104.92 ? 62  SER H OG  1 
ATOM   4301 N N   . LEU C 2 63  ? -2.757  44.360 -19.140 1.00 93.19  ? 63  LEU H N   1 
ATOM   4302 C CA  . LEU C 2 63  ? -2.276  43.929 -20.441 1.00 91.10  ? 63  LEU H CA  1 
ATOM   4303 C C   . LEU C 2 63  ? -2.368  42.422 -20.644 1.00 94.08  ? 63  LEU H C   1 
ATOM   4304 O O   . LEU C 2 63  ? -2.013  41.944 -21.726 1.00 97.20  ? 63  LEU H O   1 
ATOM   4305 C CB  . LEU C 2 63  ? -0.822  44.382 -20.626 1.00 81.20  ? 63  LEU H CB  1 
ATOM   4306 C CG  . LEU C 2 63  ? -0.564  45.889 -20.502 1.00 73.46  ? 63  LEU H CG  1 
ATOM   4307 C CD1 . LEU C 2 63  ? 0.873   46.245 -20.856 1.00 76.86  ? 63  LEU H CD1 1 
ATOM   4308 C CD2 . LEU C 2 63  ? -1.547  46.688 -21.342 1.00 91.19  ? 63  LEU H CD2 1 
ATOM   4309 N N   . ARG C 2 64  ? -2.847  41.673 -19.641 1.00 95.86  ? 64  ARG H N   1 
ATOM   4310 C CA  . ARG C 2 64  ? -2.805  40.211 -19.685 1.00 97.25  ? 64  ARG H CA  1 
ATOM   4311 C C   . ARG C 2 64  ? -3.386  39.651 -20.979 1.00 108.00 ? 64  ARG H C   1 
ATOM   4312 O O   . ARG C 2 64  ? -2.767  38.809 -21.640 1.00 114.00 ? 64  ARG H O   1 
ATOM   4313 C CB  . ARG C 2 64  ? -3.560  39.619 -18.493 1.00 98.98  ? 64  ARG H CB  1 
ATOM   4314 C CG  . ARG C 2 64  ? -2.717  39.216 -17.302 1.00 101.23 ? 64  ARG H CG  1 
ATOM   4315 C CD  . ARG C 2 64  ? -3.610  38.550 -16.265 1.00 108.73 ? 64  ARG H CD  1 
ATOM   4316 N NE  . ARG C 2 64  ? -2.902  38.221 -15.034 1.00 120.50 ? 64  ARG H NE  1 
ATOM   4317 C CZ  . ARG C 2 64  ? -3.480  38.091 -13.847 1.00 128.34 ? 64  ARG H CZ  1 
ATOM   4318 N NH1 . ARG C 2 64  ? -4.782  38.268 -13.687 1.00 133.65 ? 64  ARG H NH1 1 
ATOM   4319 N NH2 . ARG C 2 64  ? -2.731  37.782 -12.793 1.00 137.79 ? 64  ARG H NH2 1 
ATOM   4320 N N   . SER C 2 65  ? -4.589  40.105 -21.345 1.00 103.50 ? 65  SER H N   1 
ATOM   4321 C CA  . SER C 2 65  ? -5.292  39.555 -22.501 1.00 103.01 ? 65  SER H CA  1 
ATOM   4322 C C   . SER C 2 65  ? -4.455  39.610 -23.772 1.00 103.12 ? 65  SER H C   1 
ATOM   4323 O O   . SER C 2 65  ? -4.596  38.749 -24.649 1.00 108.90 ? 65  SER H O   1 
ATOM   4324 C CB  . SER C 2 65  ? -6.605  40.310 -22.710 1.00 110.97 ? 65  SER H CB  1 
ATOM   4325 O OG  . SER C 2 65  ? -6.395  41.705 -22.610 1.00 112.37 ? 65  SER H OG  1 
ATOM   4326 N N   . ARG C 2 66  ? -3.563  40.596 -23.875 1.00 93.45  ? 66  ARG H N   1 
ATOM   4327 C CA  . ARG C 2 66  ? -2.791  40.855 -25.082 1.00 88.86  ? 66  ARG H CA  1 
ATOM   4328 C C   . ARG C 2 66  ? -1.363  40.331 -25.017 1.00 87.81  ? 66  ARG H C   1 
ATOM   4329 O O   . ARG C 2 66  ? -0.755  40.114 -26.069 1.00 91.42  ? 66  ARG H O   1 
ATOM   4330 C CB  . ARG C 2 66  ? -2.758  42.367 -25.348 1.00 89.68  ? 66  ARG H CB  1 
ATOM   4331 C CG  . ARG C 2 66  ? -4.133  42.999 -25.180 1.00 90.62  ? 66  ARG H CG  1 
ATOM   4332 C CD  . ARG C 2 66  ? -4.251  44.380 -25.780 1.00 87.79  ? 66  ARG H CD  1 
ATOM   4333 N NE  . ARG C 2 66  ? -3.649  45.399 -24.931 1.00 78.97  ? 66  ARG H NE  1 
ATOM   4334 C CZ  . ARG C 2 66  ? -2.934  46.425 -25.371 1.00 85.81  ? 66  ARG H CZ  1 
ATOM   4335 N NH1 . ARG C 2 66  ? -2.688  46.596 -26.661 1.00 91.38  ? 66  ARG H NH1 1 
ATOM   4336 N NH2 . ARG C 2 66  ? -2.467  47.312 -24.496 1.00 90.93  ? 66  ARG H NH2 1 
ATOM   4337 N N   . VAL C 2 67  ? -0.824  40.101 -23.823 1.00 92.04  ? 67  VAL H N   1 
ATOM   4338 C CA  . VAL C 2 67  ? 0.592   39.790 -23.651 1.00 90.37  ? 67  VAL H CA  1 
ATOM   4339 C C   . VAL C 2 67  ? 0.804   38.286 -23.750 1.00 95.38  ? 67  VAL H C   1 
ATOM   4340 O O   . VAL C 2 67  ? 0.067   37.500 -23.143 1.00 98.09  ? 67  VAL H O   1 
ATOM   4341 C CB  . VAL C 2 67  ? 1.110   40.317 -22.302 1.00 89.42  ? 67  VAL H CB  1 
ATOM   4342 C CG1 . VAL C 2 67  ? 2.537   39.836 -22.049 1.00 84.38  ? 67  VAL H CG1 1 
ATOM   4343 C CG2 . VAL C 2 67  ? 1.047   41.824 -22.253 1.00 92.18  ? 67  VAL H CG2 1 
ATOM   4344 N N   . THR C 2 68  ? 1.823   37.888 -24.510 1.00 92.34  ? 68  THR H N   1 
ATOM   4345 C CA  . THR C 2 68  ? 2.383   36.543 -24.464 1.00 92.52  ? 68  THR H CA  1 
ATOM   4346 C C   . THR C 2 68  ? 3.899   36.666 -24.528 1.00 90.35  ? 68  THR H C   1 
ATOM   4347 O O   . THR C 2 68  ? 4.429   37.432 -25.337 1.00 94.02  ? 68  THR H O   1 
ATOM   4348 C CB  . THR C 2 68  ? 1.864   35.656 -25.607 1.00 94.83  ? 68  THR H CB  1 
ATOM   4349 O OG1 . THR C 2 68  ? 2.109   36.296 -26.866 1.00 107.49 ? 68  THR H OG1 1 
ATOM   4350 C CG2 . THR C 2 68  ? 0.370   35.368 -25.453 1.00 86.06  ? 68  THR H CG2 1 
ATOM   4351 N N   . MET C 2 69  ? 4.592   35.919 -23.672 1.00 86.52  ? 69  MET H N   1 
ATOM   4352 C CA  . MET C 2 69  ? 6.035   36.043 -23.511 1.00 83.28  ? 69  MET H CA  1 
ATOM   4353 C C   . MET C 2 69  ? 6.656   34.667 -23.697 1.00 94.73  ? 69  MET H C   1 
ATOM   4354 O O   . MET C 2 69  ? 6.313   33.730 -22.969 1.00 100.04 ? 69  MET H O   1 
ATOM   4355 C CB  . MET C 2 69  ? 6.375   36.602 -22.126 1.00 82.68  ? 69  MET H CB  1 
ATOM   4356 C CG  . MET C 2 69  ? 6.507   38.107 -22.055 1.00 83.42  ? 69  MET H CG  1 
ATOM   4357 S SD  . MET C 2 69  ? 6.889   38.633 -20.376 1.00 70.84  ? 69  MET H SD  1 
ATOM   4358 C CE  . MET C 2 69  ? 6.032   40.200 -20.307 1.00 74.95  ? 69  MET H CE  1 
ATOM   4359 N N   . SER C 2 70  ? 7.561   34.540 -24.664 1.00 95.13  ? 70  SER H N   1 
ATOM   4360 C CA  . SER C 2 70  ? 8.203   33.266 -24.953 1.00 98.80  ? 70  SER H CA  1 
ATOM   4361 C C   . SER C 2 70  ? 9.720   33.398 -24.871 1.00 98.63  ? 70  SER H C   1 
ATOM   4362 O O   . SER C 2 70  ? 10.271  34.493 -24.736 1.00 89.42  ? 70  SER H O   1 
ATOM   4363 C CB  . SER C 2 70  ? 7.799   32.740 -26.336 1.00 102.06 ? 70  SER H CB  1 
ATOM   4364 O OG  . SER C 2 70  ? 8.702   33.173 -27.339 1.00 113.61 ? 70  SER H OG  1 
ATOM   4365 N N   . VAL C 2 71  ? 10.388  32.251 -24.961 1.00 105.74 ? 71  VAL H N   1 
ATOM   4366 C CA  . VAL C 2 71  ? 11.836  32.148 -24.818 1.00 108.39 ? 71  VAL H CA  1 
ATOM   4367 C C   . VAL C 2 71  ? 12.383  31.181 -25.861 1.00 118.50 ? 71  VAL H C   1 
ATOM   4368 O O   . VAL C 2 71  ? 11.782  30.137 -26.134 1.00 115.59 ? 71  VAL H O   1 
ATOM   4369 C CB  . VAL C 2 71  ? 12.231  31.698 -23.397 1.00 104.48 ? 71  VAL H CB  1 
ATOM   4370 C CG1 . VAL C 2 71  ? 13.657  31.245 -23.381 1.00 110.16 ? 71  VAL H CG1 1 
ATOM   4371 C CG2 . VAL C 2 71  ? 12.052  32.842 -22.419 1.00 101.67 ? 71  VAL H CG2 1 
ATOM   4372 N N   . ASP C 2 72  ? 13.530  31.529 -26.440 1.00 121.38 ? 72  ASP H N   1 
ATOM   4373 C CA  . ASP C 2 72  ? 14.200  30.711 -27.447 1.00 119.46 ? 72  ASP H CA  1 
ATOM   4374 C C   . ASP C 2 72  ? 15.584  30.340 -26.913 1.00 119.53 ? 72  ASP H C   1 
ATOM   4375 O O   . ASP C 2 72  ? 16.533  31.119 -27.030 1.00 123.56 ? 72  ASP H O   1 
ATOM   4376 C CB  . ASP C 2 72  ? 14.281  31.462 -28.775 1.00 124.45 ? 72  ASP H CB  1 
ATOM   4377 C CG  . ASP C 2 72  ? 14.646  30.560 -29.932 1.00 137.46 ? 72  ASP H CG  1 
ATOM   4378 O OD1 . ASP C 2 72  ? 14.437  29.334 -29.816 1.00 136.65 ? 72  ASP H OD1 1 
ATOM   4379 O OD2 . ASP C 2 72  ? 15.137  31.073 -30.959 1.00 149.22 ? 72  ASP H OD2 1 
ATOM   4380 N N   . THR C 2 73  ? 15.693  29.142 -26.328 1.00 117.48 ? 73  THR H N   1 
ATOM   4381 C CA  . THR C 2 73  ? 16.962  28.692 -25.763 1.00 118.31 ? 73  THR H CA  1 
ATOM   4382 C C   . THR C 2 73  ? 18.056  28.554 -26.812 1.00 126.62 ? 73  THR H C   1 
ATOM   4383 O O   . THR C 2 73  ? 19.241  28.617 -26.467 1.00 131.10 ? 73  THR H O   1 
ATOM   4384 C CB  . THR C 2 73  ? 16.785  27.352 -25.046 1.00 115.64 ? 73  THR H CB  1 
ATOM   4385 O OG1 . THR C 2 73  ? 15.898  26.516 -25.801 1.00 111.65 ? 73  THR H OG1 1 
ATOM   4386 C CG2 . THR C 2 73  ? 16.224  27.559 -23.653 1.00 125.91 ? 73  THR H CG2 1 
ATOM   4387 N N   . SER C 2 74  ? 17.690  28.359 -28.078 1.00 127.50 ? 74  SER H N   1 
ATOM   4388 C CA  . SER C 2 74  ? 18.692  28.214 -29.128 1.00 126.07 ? 74  SER H CA  1 
ATOM   4389 C C   . SER C 2 74  ? 19.470  29.508 -29.330 1.00 133.57 ? 74  SER H C   1 
ATOM   4390 O O   . SER C 2 74  ? 20.706  29.504 -29.394 1.00 131.55 ? 74  SER H O   1 
ATOM   4391 C CB  . SER C 2 74  ? 18.012  27.780 -30.426 1.00 129.90 ? 74  SER H CB  1 
ATOM   4392 O OG  . SER C 2 74  ? 17.234  28.836 -30.971 1.00 145.89 ? 74  SER H OG  1 
ATOM   4393 N N   . LYS C 2 75  ? 18.743  30.624 -29.440 1.00 133.26 ? 75  LYS H N   1 
ATOM   4394 C CA  . LYS C 2 75  ? 19.407  31.925 -29.720 1.00 132.30 ? 75  LYS H CA  1 
ATOM   4395 C C   . LYS C 2 75  ? 19.296  32.843 -28.499 1.00 129.11 ? 75  LYS H C   1 
ATOM   4396 O O   . LYS C 2 75  ? 19.570  34.049 -28.651 1.00 138.25 ? 75  LYS H O   1 
ATOM   4397 C CB  . LYS C 2 75  ? 18.760  32.583 -30.941 1.00 131.88 ? 75  LYS H CB  1 
ATOM   4398 C CG  . LYS C 2 75  ? 18.584  31.672 -32.149 1.00 136.85 ? 75  LYS H CG  1 
ATOM   4399 C CD  . LYS C 2 75  ? 17.703  32.267 -33.224 1.00 143.24 ? 75  LYS H CD  1 
ATOM   4400 C CE  . LYS C 2 75  ? 17.441  31.313 -34.370 1.00 151.76 ? 75  LYS H CE  1 
ATOM   4401 N NZ  . LYS C 2 75  ? 16.554  31.914 -35.393 1.00 157.07 ? 75  LYS H NZ  1 
ATOM   4402 N N   . ASN C 2 76  ? 18.907  32.293 -27.345 1.00 131.56 ? 76  ASN H N   1 
ATOM   4403 C CA  . ASN C 2 76  ? 18.730  33.119 -26.119 1.00 129.02 ? 76  ASN H CA  1 
ATOM   4404 C C   . ASN C 2 76  ? 17.916  34.370 -26.470 1.00 123.04 ? 76  ASN H C   1 
ATOM   4405 O O   . ASN C 2 76  ? 18.483  35.480 -26.403 1.00 111.21 ? 76  ASN H O   1 
ATOM   4406 C CB  . ASN C 2 76  ? 20.067  33.462 -25.457 1.00 119.98 ? 76  ASN H CB  1 
ATOM   4407 C CG  . ASN C 2 76  ? 20.581  32.352 -24.565 1.00 120.68 ? 76  ASN H CG  1 
ATOM   4408 O OD1 . ASN C 2 76  ? 19.951  31.303 -24.447 1.00 125.58 ? 76  ASN H OD1 1 
ATOM   4409 N ND2 . ASN C 2 76  ? 21.721  32.574 -23.931 1.00 102.47 ? 76  ASN H ND2 1 
ATOM   4410 N N   . GLN C 2 77  ? 16.639  34.192 -26.824 1.00 126.11 ? 77  GLN H N   1 
ATOM   4411 C CA  . GLN C 2 77  ? 15.782  35.343 -27.218 1.00 116.21 ? 77  GLN H CA  1 
ATOM   4412 C C   . GLN C 2 77  ? 14.565  35.437 -26.293 1.00 111.22 ? 77  GLN H C   1 
ATOM   4413 O O   . GLN C 2 77  ? 13.835  34.433 -26.182 1.00 112.29 ? 77  GLN H O   1 
ATOM   4414 C CB  . GLN C 2 77  ? 15.340  35.199 -28.675 1.00 127.94 ? 77  GLN H CB  1 
ATOM   4415 C CG  . GLN C 2 77  ? 16.471  35.389 -29.674 1.00 135.00 ? 77  GLN H CG  1 
ATOM   4416 C CD  . GLN C 2 77  ? 16.015  35.171 -31.096 1.00 144.44 ? 77  GLN H CD  1 
ATOM   4417 O OE1 . GLN C 2 77  ? 14.866  34.821 -31.353 1.00 145.07 ? 77  GLN H OE1 1 
ATOM   4418 N NE2 . GLN C 2 77  ? 16.924  35.371 -32.036 1.00 145.12 ? 77  GLN H NE2 1 
ATOM   4419 N N   . PHE C 2 78  ? 14.356  36.596 -25.660 1.00 95.92  ? 78  PHE H N   1 
ATOM   4420 C CA  . PHE C 2 78  ? 13.190  36.799 -24.812 1.00 97.34  ? 78  PHE H CA  1 
ATOM   4421 C C   . PHE C 2 78  ? 12.156  37.575 -25.619 1.00 91.05  ? 78  PHE H C   1 
ATOM   4422 O O   . PHE C 2 78  ? 12.468  38.634 -26.165 1.00 89.15  ? 78  PHE H O   1 
ATOM   4423 C CB  . PHE C 2 78  ? 13.601  37.565 -23.547 1.00 90.47  ? 78  PHE H CB  1 
ATOM   4424 C CG  . PHE C 2 78  ? 12.491  37.784 -22.561 1.00 87.11  ? 78  PHE H CG  1 
ATOM   4425 C CD1 . PHE C 2 78  ? 11.549  36.802 -22.310 1.00 90.57  ? 78  PHE H CD1 1 
ATOM   4426 C CD2 . PHE C 2 78  ? 12.405  38.982 -21.868 1.00 79.86  ? 78  PHE H CD2 1 
ATOM   4427 C CE1 . PHE C 2 78  ? 10.536  37.017 -21.392 1.00 85.56  ? 78  PHE H CE1 1 
ATOM   4428 C CE2 . PHE C 2 78  ? 11.400  39.202 -20.955 1.00 80.44  ? 78  PHE H CE2 1 
ATOM   4429 C CZ  . PHE C 2 78  ? 10.462  38.219 -20.715 1.00 82.24  ? 78  PHE H CZ  1 
ATOM   4430 N N   . SER C 2 79  ? 10.938  37.054 -25.721 1.00 93.76  ? 79  SER H N   1 
ATOM   4431 C CA  . SER C 2 79  ? 9.968   37.624 -26.647 1.00 97.75  ? 79  SER H CA  1 
ATOM   4432 C C   . SER C 2 79  ? 8.829   38.324 -25.916 1.00 95.23  ? 79  SER H C   1 
ATOM   4433 O O   . SER C 2 79  ? 8.417   37.920 -24.826 1.00 94.39  ? 79  SER H O   1 
ATOM   4434 C CB  . SER C 2 79  ? 9.398   36.550 -27.578 1.00 107.69 ? 79  SER H CB  1 
ATOM   4435 O OG  . SER C 2 79  ? 10.200  36.419 -28.738 1.00 128.62 ? 79  SER H OG  1 
ATOM   4436 N N   . LEU C 2 80  ? 8.325   39.386 -26.543 1.00 95.86  ? 80  LEU H N   1 
ATOM   4437 C CA  . LEU C 2 80  ? 7.157   40.118 -26.070 1.00 92.92  ? 80  LEU H CA  1 
ATOM   4438 C C   . LEU C 2 80  ? 6.197   40.315 -27.232 1.00 99.62  ? 80  LEU H C   1 
ATOM   4439 O O   . LEU C 2 80  ? 6.608   40.778 -28.302 1.00 102.91 ? 80  LEU H O   1 
ATOM   4440 C CB  . LEU C 2 80  ? 7.551   41.476 -25.483 1.00 88.39  ? 80  LEU H CB  1 
ATOM   4441 C CG  . LEU C 2 80  ? 6.415   42.369 -24.985 1.00 84.75  ? 80  LEU H CG  1 
ATOM   4442 C CD1 . LEU C 2 80  ? 5.627   41.682 -23.880 1.00 89.88  ? 80  LEU H CD1 1 
ATOM   4443 C CD2 . LEU C 2 80  ? 6.977   43.694 -24.500 1.00 86.80  ? 80  LEU H CD2 1 
ATOM   4444 N N   . LYS C 2 81  ? 4.926   39.969 -27.024 1.00 101.90 ? 81  LYS H N   1 
ATOM   4445 C CA  . LYS C 2 81  ? 3.901   40.094 -28.057 1.00 100.18 ? 81  LYS H CA  1 
ATOM   4446 C C   . LYS C 2 81  ? 2.669   40.782 -27.487 1.00 100.82 ? 81  LYS H C   1 
ATOM   4447 O O   . LYS C 2 81  ? 2.011   40.248 -26.589 1.00 98.28  ? 81  LYS H O   1 
ATOM   4448 C CB  . LYS C 2 81  ? 3.534   38.726 -28.646 1.00 101.01 ? 81  LYS H CB  1 
ATOM   4449 C CG  . LYS C 2 81  ? 4.584   38.182 -29.610 1.00 110.71 ? 81  LYS H CG  1 
ATOM   4450 C CD  . LYS C 2 81  ? 4.117   36.907 -30.297 1.00 133.69 ? 81  LYS H CD  1 
ATOM   4451 C CE  . LYS C 2 81  ? 5.272   36.208 -31.001 1.00 154.25 ? 81  LYS H CE  1 
ATOM   4452 N NZ  . LYS C 2 81  ? 4.893   34.861 -31.514 1.00 163.96 ? 81  LYS H NZ  1 
ATOM   4453 N N   . LEU C 2 82  ? 2.356   41.955 -28.025 1.00 99.58  ? 82  LEU H N   1 
ATOM   4454 C CA  . LEU C 2 82  ? 1.201   42.763 -27.623 1.00 89.49  ? 82  LEU H CA  1 
ATOM   4455 C C   . LEU C 2 82  ? 0.175   42.770 -28.753 1.00 84.66  ? 82  LEU H C   1 
ATOM   4456 O O   . LEU C 2 82  ? 0.335   43.486 -29.745 1.00 86.74  ? 82  LEU H O   1 
ATOM   4457 C CB  . LEU C 2 82  ? 1.620   44.191 -27.278 1.00 89.42  ? 82  LEU H CB  1 
ATOM   4458 C CG  . LEU C 2 82  ? 2.358   44.502 -25.979 1.00 92.36  ? 82  LEU H CG  1 
ATOM   4459 C CD1 . LEU C 2 82  ? 2.690   45.979 -25.918 1.00 101.74 ? 82  LEU H CD1 1 
ATOM   4460 C CD2 . LEU C 2 82  ? 1.483   44.137 -24.812 1.00 107.14 ? 82  LEU H CD2 1 
ATOM   4461 N N   . THR C 2 83  ? -0.892  41.995 -28.593 1.00 87.52  ? 83  THR H N   1 
ATOM   4462 C CA  . THR C 2 83  ? -1.946  41.991 -29.597 1.00 86.34  ? 83  THR H CA  1 
ATOM   4463 C C   . THR C 2 83  ? -2.753  43.282 -29.526 1.00 89.51  ? 83  THR H C   1 
ATOM   4464 O O   . THR C 2 83  ? -2.837  43.929 -28.479 1.00 101.65 ? 83  THR H O   1 
ATOM   4465 C CB  . THR C 2 83  ? -2.885  40.802 -29.405 1.00 88.84  ? 83  THR H CB  1 
ATOM   4466 O OG1 . THR C 2 83  ? -3.783  41.073 -28.325 1.00 89.45  ? 83  THR H OG1 1 
ATOM   4467 C CG2 . THR C 2 83  ? -2.091  39.552 -29.081 1.00 101.78 ? 83  THR H CG2 1 
ATOM   4468 N N   . SER C 2 84  ? -3.402  43.623 -30.638 1.00 90.15  ? 84  SER H N   1 
ATOM   4469 C CA  . SER C 2 84  ? -4.272  44.825 -30.687 1.00 90.20  ? 84  SER H CA  1 
ATOM   4470 C C   . SER C 2 84  ? -3.601  46.012 -30.001 1.00 92.95  ? 84  SER H C   1 
ATOM   4471 O O   . SER C 2 84  ? -4.122  46.470 -28.975 1.00 97.00  ? 84  SER H O   1 
ATOM   4472 C CB  . SER C 2 84  ? -5.607  44.537 -30.078 1.00 103.10 ? 84  SER H CB  1 
ATOM   4473 O OG  . SER C 2 84  ? -6.425  45.696 -30.103 1.00 138.44 ? 84  SER H OG  1 
ATOM   4474 N N   . VAL C 2 85  ? -2.505  46.500 -30.574 1.00 90.07  ? 85  VAL H N   1 
ATOM   4475 C CA  . VAL C 2 85  ? -1.798  47.677 -30.000 1.00 83.57  ? 85  VAL H CA  1 
ATOM   4476 C C   . VAL C 2 85  ? -2.691  48.908 -30.143 1.00 86.43  ? 85  VAL H C   1 
ATOM   4477 O O   . VAL C 2 85  ? -3.346  49.040 -31.184 1.00 87.98  ? 85  VAL H O   1 
ATOM   4478 C CB  . VAL C 2 85  ? -0.440  47.881 -30.687 1.00 76.11  ? 85  VAL H CB  1 
ATOM   4479 C CG1 . VAL C 2 85  ? 0.262   49.131 -30.192 1.00 78.13  ? 85  VAL H CG1 1 
ATOM   4480 C CG2 . VAL C 2 85  ? 0.455   46.668 -30.509 1.00 85.49  ? 85  VAL H CG2 1 
ATOM   4481 N N   . THR C 2 86  ? -2.739  49.753 -29.115 1.00 84.21  ? 86  THR H N   1 
ATOM   4482 C CA  . THR C 2 86  ? -3.507  51.016 -29.202 1.00 82.98  ? 86  THR H CA  1 
ATOM   4483 C C   . THR C 2 86  ? -2.511  52.145 -29.429 1.00 81.97  ? 86  THR H C   1 
ATOM   4484 O O   . THR C 2 86  ? -1.366  51.847 -29.786 1.00 77.93  ? 86  THR H O   1 
ATOM   4485 C CB  . THR C 2 86  ? -4.259  51.305 -27.904 1.00 86.72  ? 86  THR H CB  1 
ATOM   4486 O OG1 . THR C 2 86  ? -3.307  51.814 -26.970 1.00 88.01  ? 86  THR H OG1 1 
ATOM   4487 C CG2 . THR C 2 86  ? -4.942  50.083 -27.333 1.00 92.19  ? 86  THR H CG2 1 
ATOM   4488 N N   . ALA C 2 87  ? -2.931  53.387 -29.226 1.00 78.08  ? 87  ALA H N   1 
ATOM   4489 C CA  . ALA C 2 87  ? -1.967  54.499 -29.331 1.00 74.97  ? 87  ALA H CA  1 
ATOM   4490 C C   . ALA C 2 87  ? -1.234  54.579 -27.999 1.00 78.55  ? 87  ALA H C   1 
ATOM   4491 O O   . ALA C 2 87  ? -0.053  54.953 -27.981 1.00 77.97  ? 87  ALA H O   1 
ATOM   4492 C CB  . ALA C 2 87  ? -2.701  55.772 -29.627 1.00 75.40  ? 87  ALA H CB  1 
ATOM   4493 N N   . ALA C 2 88  ? -1.933  54.222 -26.928 1.00 82.98  ? 88  ALA H N   1 
ATOM   4494 C CA  . ALA C 2 88  ? -1.326  54.261 -25.600 1.00 82.32  ? 88  ALA H CA  1 
ATOM   4495 C C   . ALA C 2 88  ? -0.095  53.373 -25.506 1.00 79.98  ? 88  ALA H C   1 
ATOM   4496 O O   . ALA C 2 88  ? 0.834   53.683 -24.752 1.00 82.09  ? 88  ALA H O   1 
ATOM   4497 C CB  . ALA C 2 88  ? -2.343  53.837 -24.544 1.00 85.82  ? 88  ALA H CB  1 
ATOM   4498 N N   . ASP C 2 89  ? -0.064  52.271 -26.255 1.00 75.35  ? 89  ASP H N   1 
ATOM   4499 C CA  . ASP C 2 89  ? 1.047   51.332 -26.170 1.00 70.70  ? 89  ASP H CA  1 
ATOM   4500 C C   . ASP C 2 89  ? 2.334   51.872 -26.782 1.00 69.18  ? 89  ASP H C   1 
ATOM   4501 O O   . ASP C 2 89  ? 3.350   51.170 -26.745 1.00 70.39  ? 89  ASP H O   1 
ATOM   4502 C CB  . ASP C 2 89  ? 0.657   50.011 -26.836 1.00 73.35  ? 89  ASP H CB  1 
ATOM   4503 C CG  . ASP C 2 89  ? -0.291  49.184 -25.983 1.00 76.80  ? 89  ASP H CG  1 
ATOM   4504 O OD1 . ASP C 2 89  ? 0.165   48.570 -24.995 1.00 78.96  ? 89  ASP H OD1 1 
ATOM   4505 O OD2 . ASP C 2 89  ? -1.501  49.171 -26.291 1.00 75.42  ? 89  ASP H OD2 1 
ATOM   4506 N N   . THR C 2 90  ? 2.316   53.081 -27.347 1.00 74.00  ? 90  THR H N   1 
ATOM   4507 C CA  . THR C 2 90  ? 3.534   53.765 -27.766 1.00 77.83  ? 90  THR H CA  1 
ATOM   4508 C C   . THR C 2 90  ? 4.409   54.064 -26.558 1.00 70.87  ? 90  THR H C   1 
ATOM   4509 O O   . THR C 2 90  ? 4.013   54.862 -25.701 1.00 70.85  ? 90  THR H O   1 
ATOM   4510 C CB  . THR C 2 90  ? 3.195   55.074 -28.487 1.00 76.99  ? 90  THR H CB  1 
ATOM   4511 O OG1 . THR C 2 90  ? 2.447   54.803 -29.677 1.00 81.82  ? 90  THR H OG1 1 
ATOM   4512 C CG2 . THR C 2 90  ? 4.461   55.840 -28.839 1.00 77.12  ? 90  THR H CG2 1 
ATOM   4513 N N   . ALA C 2 91  ? 5.596   53.462 -26.478 1.00 66.63  ? 91  ALA H N   1 
ATOM   4514 C CA  . ALA C 2 91  ? 6.405   53.620 -25.274 1.00 63.82  ? 91  ALA H CA  1 
ATOM   4515 C C   . ALA C 2 91  ? 7.797   53.047 -25.503 1.00 63.03  ? 91  ALA H C   1 
ATOM   4516 O O   . ALA C 2 91  ? 8.059   52.364 -26.496 1.00 72.68  ? 91  ALA H O   1 
ATOM   4517 C CB  . ALA C 2 91  ? 5.742   52.944 -24.073 1.00 72.03  ? 91  ALA H CB  1 
ATOM   4518 N N   . VAL C 2 92  ? 8.696   53.354 -24.571 1.00 67.17  ? 92  VAL H N   1 
ATOM   4519 C CA  . VAL C 2 92  ? 9.986   52.683 -24.496 1.00 54.03  ? 92  VAL H CA  1 
ATOM   4520 C C   . VAL C 2 92  ? 9.786   51.358 -23.781 1.00 60.94  ? 92  VAL H C   1 
ATOM   4521 O O   . VAL C 2 92  ? 9.035   51.270 -22.803 1.00 73.28  ? 92  VAL H O   1 
ATOM   4522 C CB  . VAL C 2 92  ? 11.017  53.566 -23.768 1.00 51.99  ? 92  VAL H CB  1 
ATOM   4523 C CG1 . VAL C 2 92  ? 12.381  52.903 -23.744 1.00 65.16  ? 92  VAL H CG1 1 
ATOM   4524 C CG2 . VAL C 2 92  ? 11.096  54.939 -24.417 1.00 62.67  ? 92  VAL H CG2 1 
ATOM   4525 N N   . TYR C 2 93  ? 10.434  50.311 -24.272 1.00 65.48  ? 93  TYR H N   1 
ATOM   4526 C CA  . TYR C 2 93  ? 10.343  48.999 -23.650 1.00 66.52  ? 93  TYR H CA  1 
ATOM   4527 C C   . TYR C 2 93  ? 11.716  48.550 -23.175 1.00 69.66  ? 93  TYR H C   1 
ATOM   4528 O O   . TYR C 2 93  ? 12.727  48.757 -23.860 1.00 73.00  ? 93  TYR H O   1 
ATOM   4529 C CB  . TYR C 2 93  ? 9.739   47.959 -24.599 1.00 65.04  ? 93  TYR H CB  1 
ATOM   4530 C CG  . TYR C 2 93  ? 8.284   48.200 -24.953 1.00 63.81  ? 93  TYR H CG  1 
ATOM   4531 C CD1 . TYR C 2 93  ? 7.883   49.357 -25.612 1.00 66.12  ? 93  TYR H CD1 1 
ATOM   4532 C CD2 . TYR C 2 93  ? 7.310   47.267 -24.623 1.00 63.69  ? 93  TYR H CD2 1 
ATOM   4533 C CE1 . TYR C 2 93  ? 6.560   49.575 -25.936 1.00 67.12  ? 93  TYR H CE1 1 
ATOM   4534 C CE2 . TYR C 2 93  ? 5.984   47.476 -24.946 1.00 61.96  ? 93  TYR H CE2 1 
ATOM   4535 C CZ  . TYR C 2 93  ? 5.615   48.631 -25.603 1.00 64.15  ? 93  TYR H CZ  1 
ATOM   4536 O OH  . TYR C 2 93  ? 4.294   48.845 -25.921 1.00 67.24  ? 93  TYR H OH  1 
ATOM   4537 N N   . TYR C 2 94  ? 11.727  47.940 -21.987 1.00 66.92  ? 94  TYR H N   1 
ATOM   4538 C CA  . TYR C 2 94  ? 12.925  47.476 -21.306 1.00 68.67  ? 94  TYR H CA  1 
ATOM   4539 C C   . TYR C 2 94  ? 12.759  46.008 -20.938 1.00 70.65  ? 94  TYR H C   1 
ATOM   4540 O O   . TYR C 2 94  ? 11.688  45.590 -20.483 1.00 70.39  ? 94  TYR H O   1 
ATOM   4541 C CB  . TYR C 2 94  ? 13.184  48.267 -20.020 1.00 70.85  ? 94  TYR H CB  1 
ATOM   4542 C CG  . TYR C 2 94  ? 13.554  49.724 -20.181 1.00 74.05  ? 94  TYR H CG  1 
ATOM   4543 C CD1 . TYR C 2 94  ? 14.878  50.115 -20.355 1.00 81.77  ? 94  TYR H CD1 1 
ATOM   4544 C CD2 . TYR C 2 94  ? 12.584  50.717 -20.108 1.00 72.67  ? 94  TYR H CD2 1 
ATOM   4545 C CE1 . TYR C 2 94  ? 15.220  51.455 -20.481 1.00 79.32  ? 94  TYR H CE1 1 
ATOM   4546 C CE2 . TYR C 2 94  ? 12.917  52.053 -20.234 1.00 73.87  ? 94  TYR H CE2 1 
ATOM   4547 C CZ  . TYR C 2 94  ? 14.233  52.417 -20.418 1.00 79.91  ? 94  TYR H CZ  1 
ATOM   4548 O OH  . TYR C 2 94  ? 14.553  53.751 -20.541 1.00 85.89  ? 94  TYR H OH  1 
ATOM   4549 N N   . CYS C 2 95  ? 13.824  45.234 -21.116 1.00 74.91  ? 95  CYS H N   1 
ATOM   4550 C CA  . CYS C 2 95  ? 13.905  43.885 -20.579 1.00 77.89  ? 95  CYS H CA  1 
ATOM   4551 C C   . CYS C 2 95  ? 14.876  43.862 -19.403 1.00 77.71  ? 95  CYS H C   1 
ATOM   4552 O O   . CYS C 2 95  ? 15.830  44.643 -19.350 1.00 81.67  ? 95  CYS H O   1 
ATOM   4553 C CB  . CYS C 2 95  ? 14.332  42.876 -21.658 1.00 84.31  ? 95  CYS H CB  1 
ATOM   4554 S SG  . CYS C 2 95  ? 16.021  43.077 -22.284 1.00 109.44 ? 95  CYS H SG  1 
ATOM   4555 N N   . ALA C 2 96  ? 14.610  42.975 -18.443 1.00 68.83  ? 96  ALA H N   1 
ATOM   4556 C CA  . ALA C 2 96  ? 15.416  42.929 -17.227 1.00 71.98  ? 96  ALA H CA  1 
ATOM   4557 C C   . ALA C 2 96  ? 15.498  41.501 -16.706 1.00 76.02  ? 96  ALA H C   1 
ATOM   4558 O O   . ALA C 2 96  ? 14.691  40.639 -17.065 1.00 74.48  ? 96  ALA H O   1 
ATOM   4559 C CB  . ALA C 2 96  ? 14.854  43.858 -16.143 1.00 75.58  ? 96  ALA H CB  1 
ATOM   4560 N N   . ARG C 2 97  ? 16.484  41.263 -15.839 1.00 82.56  ? 97  ARG H N   1 
ATOM   4561 C CA  . ARG C 2 97  ? 16.717  39.940 -15.261 1.00 81.94  ? 97  ARG H CA  1 
ATOM   4562 C C   . ARG C 2 97  ? 16.178  39.876 -13.836 1.00 81.81  ? 97  ARG H C   1 
ATOM   4563 O O   . ARG C 2 97  ? 16.624  40.636 -12.971 1.00 84.41  ? 97  ARG H O   1 
ATOM   4564 C CB  . ARG C 2 97  ? 18.205  39.586 -15.256 1.00 88.12  ? 97  ARG H CB  1 
ATOM   4565 C CG  . ARG C 2 97  ? 18.460  38.136 -14.867 1.00 93.17  ? 97  ARG H CG  1 
ATOM   4566 C CD  . ARG C 2 97  ? 19.834  37.652 -15.273 1.00 101.25 ? 97  ARG H CD  1 
ATOM   4567 N NE  . ARG C 2 97  ? 20.853  38.011 -14.295 1.00 107.88 ? 97  ARG H NE  1 
ATOM   4568 C CZ  . ARG C 2 97  ? 22.007  37.373 -14.158 1.00 115.97 ? 97  ARG H CZ  1 
ATOM   4569 N NH1 . ARG C 2 97  ? 22.324  36.347 -14.932 1.00 119.72 ? 97  ARG H NH1 1 
ATOM   4570 N NH2 . ARG C 2 97  ? 22.863  37.772 -13.222 1.00 115.08 ? 97  ARG H NH2 1 
ATOM   4571 N N   . GLU C 2 98  ? 15.242  38.959 -13.587 1.00 79.07  ? 98  GLU H N   1 
ATOM   4572 C CA  . GLU C 2 98  ? 14.804  38.648 -12.228 1.00 85.73  ? 98  GLU H CA  1 
ATOM   4573 C C   . GLU C 2 98  ? 15.835  37.725 -11.579 1.00 93.30  ? 98  GLU H C   1 
ATOM   4574 O O   . GLU C 2 98  ? 15.906  36.529 -11.886 1.00 97.84  ? 98  GLU H O   1 
ATOM   4575 C CB  . GLU C 2 98  ? 13.411  38.025 -12.243 1.00 94.33  ? 98  GLU H CB  1 
ATOM   4576 C CG  . GLU C 2 98  ? 12.877  37.707 -10.854 1.00 103.66 ? 98  GLU H CG  1 
ATOM   4577 C CD  . GLU C 2 98  ? 11.473  37.117 -10.827 1.00 121.80 ? 98  GLU H CD  1 
ATOM   4578 O OE1 . GLU C 2 98  ? 10.941  36.750 -11.890 1.00 127.16 ? 98  GLU H OE1 1 
ATOM   4579 O OE2 . GLU C 2 98  ? 10.900  37.002 -9.723  1.00 128.55 ? 98  GLU H OE2 1 
ATOM   4580 N N   . GLU C 2 99  ? 16.640  38.288 -10.675 1.00 85.63  ? 99  GLU H N   1 
ATOM   4581 C CA  . GLU C 2 99  ? 17.678  37.538 -9.982  1.00 82.80  ? 99  GLU H CA  1 
ATOM   4582 C C   . GLU C 2 99  ? 17.077  36.388 -9.182  1.00 83.67  ? 99  GLU H C   1 
ATOM   4583 O O   . GLU C 2 99  ? 15.874  36.346 -8.899  1.00 82.13  ? 99  GLU H O   1 
ATOM   4584 C CB  . GLU C 2 99  ? 18.465  38.451 -9.038  1.00 76.64  ? 99  GLU H CB  1 
ATOM   4585 C CG  . GLU C 2 99  ? 19.062  39.697 -9.680  1.00 80.93  ? 99  GLU H CG  1 
ATOM   4586 C CD  . GLU C 2 99  ? 20.018  39.380 -10.806 1.00 92.15  ? 99  GLU H CD  1 
ATOM   4587 O OE1 . GLU C 2 99  ? 21.020  38.686 -10.546 1.00 99.01  ? 99  GLU H OE1 1 
ATOM   4588 O OE2 . GLU C 2 99  ? 19.767  39.825 -11.947 1.00 92.88  ? 99  GLU H OE2 1 
ATOM   4589 N N   . HIS C 2 100 ? 17.937  35.439 -8.825  1.00 91.69  ? 100 HIS H N   1 
ATOM   4590 C CA  . HIS C 2 100 ? 17.529  34.399 -7.899  1.00 98.19  ? 100 HIS H CA  1 
ATOM   4591 C C   . HIS C 2 100 ? 17.175  35.017 -6.553  1.00 94.79  ? 100 HIS H C   1 
ATOM   4592 O O   . HIS C 2 100 ? 17.439  36.193 -6.287  1.00 98.55  ? 100 HIS H O   1 
ATOM   4593 C CB  . HIS C 2 100 ? 18.630  33.354 -7.714  1.00 101.83 ? 100 HIS H CB  1 
ATOM   4594 C CG  . HIS C 2 100 ? 19.142  32.766 -8.995  1.00 103.93 ? 100 HIS H CG  1 
ATOM   4595 N ND1 . HIS C 2 100 ? 18.353  32.018 -9.841  1.00 89.00  ? 100 HIS H ND1 1 
ATOM   4596 C CD2 . HIS C 2 100 ? 20.374  32.791 -9.560  1.00 106.05 ? 100 HIS H CD2 1 
ATOM   4597 C CE1 . HIS C 2 100 ? 19.071  31.614 -10.874 1.00 101.32 ? 100 HIS H CE1 1 
ATOM   4598 N NE2 . HIS C 2 100 ? 20.302  32.070 -10.727 1.00 106.92 ? 100 HIS H NE2 1 
ATOM   4599 N N   . ILE C 2 101 ? 16.546  34.201 -5.706  1.00 80.12  ? 101 ILE H N   1 
ATOM   4600 C CA  . ILE C 2 101 ? 16.223  34.634 -4.356  1.00 72.74  ? 101 ILE H CA  1 
ATOM   4601 C C   . ILE C 2 101 ? 17.501  35.059 -3.671  1.00 76.67  ? 101 ILE H C   1 
ATOM   4602 O O   . ILE C 2 101 ? 18.530  34.384 -3.771  1.00 86.19  ? 101 ILE H O   1 
ATOM   4603 C CB  . ILE C 2 101 ? 15.601  33.486 -3.553  1.00 71.22  ? 101 ILE H CB  1 
ATOM   4604 C CG1 . ILE C 2 101 ? 14.611  32.730 -4.408  1.00 82.51  ? 101 ILE H CG1 1 
ATOM   4605 C CG2 . ILE C 2 101 ? 14.862  34.035 -2.343  1.00 62.60  ? 101 ILE H CG2 1 
ATOM   4606 C CD1 . ILE C 2 101 ? 14.556  31.284 -4.057  1.00 89.08  ? 101 ILE H CD1 1 
ATOM   4607 N N   . THR C 2 102 ? 17.444  36.164 -2.957  1.00 71.06  ? 102 THR H N   1 
ATOM   4608 C CA  . THR C 2 102 ? 18.412  36.422 -1.910  1.00 75.71  ? 102 THR H CA  1 
ATOM   4609 C C   . THR C 2 102 ? 17.643  36.651 -0.618  1.00 73.10  ? 102 THR H C   1 
ATOM   4610 O O   . THR C 2 102 ? 16.410  36.631 -0.586  1.00 68.08  ? 102 THR H O   1 
ATOM   4611 C CB  . THR C 2 102 ? 19.316  37.617 -2.242  1.00 81.55  ? 102 THR H CB  1 
ATOM   4612 O OG1 . THR C 2 102 ? 18.703  38.836 -1.797  1.00 94.69  ? 102 THR H OG1 1 
ATOM   4613 C CG2 . THR C 2 102 ? 19.572  37.699 -3.738  1.00 79.00  ? 102 THR H CG2 1 
ATOM   4614 N N   . PHE C 2 103 ? 18.390  36.854 0.460   1.00 77.79  ? 103 PHE H N   1 
ATOM   4615 C CA  . PHE C 2 103 ? 17.797  37.254 1.725   1.00 77.55  ? 103 PHE H CA  1 
ATOM   4616 C C   . PHE C 2 103 ? 17.164  38.641 1.628   1.00 76.53  ? 103 PHE H C   1 
ATOM   4617 O O   . PHE C 2 103 ? 16.510  39.085 2.577   1.00 79.77  ? 103 PHE H O   1 
ATOM   4618 C CB  . PHE C 2 103 ? 18.893  37.168 2.793   1.00 81.52  ? 103 PHE H CB  1 
ATOM   4619 C CG  . PHE C 2 103 ? 18.451  37.507 4.177   1.00 85.11  ? 103 PHE H CG  1 
ATOM   4620 C CD1 . PHE C 2 103 ? 17.596  36.662 4.862   1.00 70.48  ? 103 PHE H CD1 1 
ATOM   4621 C CD2 . PHE C 2 103 ? 18.945  38.627 4.825   1.00 93.73  ? 103 PHE H CD2 1 
ATOM   4622 C CE1 . PHE C 2 103 ? 17.203  36.950 6.146   1.00 70.76  ? 103 PHE H CE1 1 
ATOM   4623 C CE2 . PHE C 2 103 ? 18.558  38.918 6.115   1.00 90.07  ? 103 PHE H CE2 1 
ATOM   4624 C CZ  . PHE C 2 103 ? 17.692  38.073 6.776   1.00 81.40  ? 103 PHE H CZ  1 
ATOM   4625 N N   . GLY C 2 104 ? 17.337  39.320 0.497   1.00 71.46  ? 104 GLY H N   1 
ATOM   4626 C CA  . GLY C 2 104 ? 16.650  40.525 0.092   1.00 71.00  ? 104 GLY H CA  1 
ATOM   4627 C C   . GLY C 2 104 ? 15.525  40.302 -0.887  1.00 72.62  ? 104 GLY H C   1 
ATOM   4628 O O   . GLY C 2 104 ? 15.038  41.266 -1.486  1.00 66.63  ? 104 GLY H O   1 
ATOM   4629 N N   . GLY C 2 105 ? 15.099  39.059 -1.072  1.00 79.19  ? 105 GLY H N   1 
ATOM   4630 C CA  . GLY C 2 105 ? 14.005  38.784 -1.965  1.00 73.42  ? 105 GLY H CA  1 
ATOM   4631 C C   . GLY C 2 105 ? 14.433  38.863 -3.420  1.00 72.08  ? 105 GLY H C   1 
ATOM   4632 O O   . GLY C 2 105 ? 15.614  38.768 -3.769  1.00 73.63  ? 105 GLY H O   1 
ATOM   4633 N N   . VAL C 2 106 ? 13.437  39.043 -4.276  1.00 76.00  ? 106 VAL H N   1 
ATOM   4634 C CA  . VAL C 2 106 ? 13.662  39.171 -5.710  1.00 81.54  ? 106 VAL H CA  1 
ATOM   4635 C C   . VAL C 2 106 ? 14.084  40.595 -6.047  1.00 83.53  ? 106 VAL H C   1 
ATOM   4636 O O   . VAL C 2 106 ? 13.438  41.567 -5.637  1.00 89.75  ? 106 VAL H O   1 
ATOM   4637 C CB  . VAL C 2 106 ? 12.406  38.761 -6.487  1.00 87.29  ? 106 VAL H CB  1 
ATOM   4638 C CG1 . VAL C 2 106 ? 12.554  39.161 -7.915  1.00 94.22  ? 106 VAL H CG1 1 
ATOM   4639 C CG2 . VAL C 2 106 ? 12.219  37.257 -6.401  1.00 92.76  ? 106 VAL H CG2 1 
ATOM   4640 N N   . ILE C 2 107 ? 15.166  40.716 -6.813  1.00 78.97  ? 107 ILE H N   1 
ATOM   4641 C CA  . ILE C 2 107 ? 15.777  41.988 -7.169  1.00 73.83  ? 107 ILE H CA  1 
ATOM   4642 C C   . ILE C 2 107 ? 16.032  42.000 -8.672  1.00 83.71  ? 107 ILE H C   1 
ATOM   4643 O O   . ILE C 2 107 ? 16.265  40.955 -9.286  1.00 88.48  ? 107 ILE H O   1 
ATOM   4644 C CB  . ILE C 2 107 ? 17.090  42.206 -6.382  1.00 74.41  ? 107 ILE H CB  1 
ATOM   4645 C CG1 . ILE C 2 107 ? 16.839  42.099 -4.880  1.00 81.03  ? 107 ILE H CG1 1 
ATOM   4646 C CG2 . ILE C 2 107 ? 17.699  43.540 -6.689  1.00 74.66  ? 107 ILE H CG2 1 
ATOM   4647 C CD1 . ILE C 2 107 ? 18.102  42.153 -4.058  1.00 91.93  ? 107 ILE H CD1 1 
ATOM   4648 N N   . VAL C 2 108 ? 15.970  43.188 -9.274  1.00 81.39  ? 108 VAL H N   1 
ATOM   4649 C CA  . VAL C 2 108 ? 16.324  43.365 -10.681 1.00 73.92  ? 108 VAL H CA  1 
ATOM   4650 C C   . VAL C 2 108 ? 17.481  44.355 -10.757 1.00 76.28  ? 108 VAL H C   1 
ATOM   4651 O O   . VAL C 2 108 ? 17.314  45.570 -10.590 1.00 80.15  ? 108 VAL H O   1 
ATOM   4652 C CB  . VAL C 2 108 ? 15.128  43.787 -11.544 1.00 67.01  ? 108 VAL H CB  1 
ATOM   4653 C CG1 . VAL C 2 108 ? 14.105  42.690 -11.527 1.00 78.45  ? 108 VAL H CG1 1 
ATOM   4654 C CG2 . VAL C 2 108 ? 14.476  45.053 -11.032 1.00 70.75  ? 108 VAL H CG2 1 
ATOM   4655 N N   . ARG C 2 109 ? 18.678  43.822 -10.990 1.00 80.51  ? 109 ARG H N   1 
ATOM   4656 C CA  . ARG C 2 109 ? 19.888  44.621 -11.106 1.00 84.76  ? 109 ARG H CA  1 
ATOM   4657 C C   . ARG C 2 109 ? 20.262  44.904 -12.548 1.00 89.58  ? 109 ARG H C   1 
ATOM   4658 O O   . ARG C 2 109 ? 20.951  45.895 -12.812 1.00 88.80  ? 109 ARG H O   1 
ATOM   4659 C CB  . ARG C 2 109 ? 21.057  43.897 -10.421 1.00 91.95  ? 109 ARG H CB  1 
ATOM   4660 C CG  . ARG C 2 109 ? 20.935  43.849 -8.911  1.00 98.85  ? 109 ARG H CG  1 
ATOM   4661 C CD  . ARG C 2 109 ? 22.155  43.228 -8.261  1.00 95.84  ? 109 ARG H CD  1 
ATOM   4662 N NE  . ARG C 2 109 ? 22.457  43.896 -7.003  1.00 108.55 ? 109 ARG H NE  1 
ATOM   4663 C CZ  . ARG C 2 109 ? 22.671  43.271 -5.855  1.00 138.31 ? 109 ARG H CZ  1 
ATOM   4664 N NH1 . ARG C 2 109 ? 22.636  41.951 -5.769  1.00 165.99 ? 109 ARG H NH1 1 
ATOM   4665 N NH2 . ARG C 2 109 ? 22.912  43.989 -4.763  1.00 159.91 ? 109 ARG H NH2 1 
ATOM   4666 N N   . TYR C 2 110 ? 19.795  44.078 -13.479 1.00 91.17  ? 110 TYR H N   1 
ATOM   4667 C CA  . TYR C 2 110 ? 20.293  44.060 -14.846 1.00 84.62  ? 110 TYR H CA  1 
ATOM   4668 C C   . TYR C 2 110 ? 19.155  44.422 -15.786 1.00 90.84  ? 110 TYR H C   1 
ATOM   4669 O O   . TYR C 2 110 ? 18.158  43.694 -15.878 1.00 90.56  ? 110 TYR H O   1 
ATOM   4670 C CB  . TYR C 2 110 ? 20.886  42.691 -15.174 1.00 81.22  ? 110 TYR H CB  1 
ATOM   4671 C CG  . TYR C 2 110 ? 22.071  42.387 -14.289 1.00 87.97  ? 110 TYR H CG  1 
ATOM   4672 C CD1 . TYR C 2 110 ? 23.079  43.325 -14.103 1.00 92.10  ? 110 TYR H CD1 1 
ATOM   4673 C CD2 . TYR C 2 110 ? 22.149  41.195 -13.581 1.00 94.67  ? 110 TYR H CD2 1 
ATOM   4674 C CE1 . TYR C 2 110 ? 24.153  43.067 -13.272 1.00 92.85  ? 110 TYR H CE1 1 
ATOM   4675 C CE2 . TYR C 2 110 ? 23.221  40.930 -12.743 1.00 97.53  ? 110 TYR H CE2 1 
ATOM   4676 C CZ  . TYR C 2 110 ? 24.219  41.870 -12.593 1.00 90.91  ? 110 TYR H CZ  1 
ATOM   4677 O OH  . TYR C 2 110 ? 25.288  41.618 -11.767 1.00 91.26  ? 110 TYR H OH  1 
ATOM   4678 N N   . TRP C 2 111 ? 19.313  45.547 -16.476 1.00 89.30  ? 111 TRP H N   1 
ATOM   4679 C CA  . TRP C 2 111 ? 18.307  46.150 -17.332 1.00 81.75  ? 111 TRP H CA  1 
ATOM   4680 C C   . TRP C 2 111 ? 18.829  46.203 -18.761 1.00 85.26  ? 111 TRP H C   1 
ATOM   4681 O O   . TRP C 2 111 ? 20.037  46.159 -19.005 1.00 91.93  ? 111 TRP H O   1 
ATOM   4682 C CB  . TRP C 2 111 ? 17.977  47.572 -16.857 1.00 87.51  ? 111 TRP H CB  1 
ATOM   4683 C CG  . TRP C 2 111 ? 17.082  47.655 -15.661 1.00 86.86  ? 111 TRP H CG  1 
ATOM   4684 C CD1 . TRP C 2 111 ? 17.437  47.474 -14.357 1.00 85.90  ? 111 TRP H CD1 1 
ATOM   4685 C CD2 . TRP C 2 111 ? 15.696  48.009 -15.654 1.00 79.68  ? 111 TRP H CD2 1 
ATOM   4686 N NE1 . TRP C 2 111 ? 16.349  47.657 -13.539 1.00 76.41  ? 111 TRP H NE1 1 
ATOM   4687 C CE2 . TRP C 2 111 ? 15.268  47.990 -14.312 1.00 71.40  ? 111 TRP H CE2 1 
ATOM   4688 C CE3 . TRP C 2 111 ? 14.771  48.326 -16.653 1.00 80.68  ? 111 TRP H CE3 1 
ATOM   4689 C CZ2 . TRP C 2 111 ? 13.958  48.277 -13.945 1.00 72.59  ? 111 TRP H CZ2 1 
ATOM   4690 C CZ3 . TRP C 2 111 ? 13.472  48.610 -16.286 1.00 80.23  ? 111 TRP H CZ3 1 
ATOM   4691 C CH2 . TRP C 2 111 ? 13.078  48.588 -14.945 1.00 74.32  ? 111 TRP H CH2 1 
ATOM   4692 N N   . GLY C 2 112 ? 17.911  46.304 -19.713 1.00 84.44  ? 112 GLY H N   1 
ATOM   4693 C CA  . GLY C 2 112 ? 18.281  46.534 -21.092 1.00 81.82  ? 112 GLY H CA  1 
ATOM   4694 C C   . GLY C 2 112 ? 18.605  47.994 -21.331 1.00 85.64  ? 112 GLY H C   1 
ATOM   4695 O O   . GLY C 2 112 ? 18.814  48.777 -20.404 1.00 91.77  ? 112 GLY H O   1 
ATOM   4696 N N   . GLN C 2 113 ? 18.648  48.364 -22.610 1.00 88.65  ? 113 GLN H N   1 
ATOM   4697 C CA  . GLN C 2 113 ? 18.788  49.764 -22.980 1.00 102.22 ? 113 GLN H CA  1 
ATOM   4698 C C   . GLN C 2 113 ? 17.465  50.419 -23.349 1.00 88.22  ? 113 GLN H C   1 
ATOM   4699 O O   . GLN C 2 113 ? 17.353  51.647 -23.257 1.00 79.00  ? 113 GLN H O   1 
ATOM   4700 C CB  . GLN C 2 113 ? 19.770  49.908 -24.147 1.00 114.84 ? 113 GLN H CB  1 
ATOM   4701 C CG  . GLN C 2 113 ? 21.220  49.626 -23.790 1.00 137.38 ? 113 GLN H CG  1 
ATOM   4702 C CD  . GLN C 2 113 ? 22.106  49.548 -25.014 1.00 176.89 ? 113 GLN H CD  1 
ATOM   4703 O OE1 . GLN C 2 113 ? 21.694  49.919 -26.112 1.00 200.75 ? 113 GLN H OE1 1 
ATOM   4704 N NE2 . GLN C 2 113 ? 23.327  49.055 -24.836 1.00 213.22 ? 113 GLN H NE2 1 
ATOM   4705 N N   . GLY C 2 114 ? 16.468  49.636 -23.749 1.00 87.59  ? 114 GLY H N   1 
ATOM   4706 C CA  . GLY C 2 114 ? 15.187  50.190 -24.132 1.00 82.91  ? 114 GLY H CA  1 
ATOM   4707 C C   . GLY C 2 114 ? 15.064  50.454 -25.618 1.00 87.62  ? 114 GLY H C   1 
ATOM   4708 O O   . GLY C 2 114 ? 15.994  50.973 -26.243 1.00 98.42  ? 114 GLY H O   1 
ATOM   4709 N N   . THR C 2 115 ? 13.924  50.088 -26.199 1.00 85.33  ? 115 THR H N   1 
ATOM   4710 C CA  . THR C 2 115 ? 13.618  50.391 -27.593 1.00 90.95  ? 115 THR H CA  1 
ATOM   4711 C C   . THR C 2 115 ? 12.304  51.154 -27.649 1.00 88.47  ? 115 THR H C   1 
ATOM   4712 O O   . THR C 2 115 ? 11.340  50.786 -26.971 1.00 86.20  ? 115 THR H O   1 
ATOM   4713 C CB  . THR C 2 115 ? 13.544  49.117 -28.450 1.00 93.13  ? 115 THR H CB  1 
ATOM   4714 O OG1 . THR C 2 115 ? 12.717  48.139 -27.805 1.00 94.67  ? 115 THR H OG1 1 
ATOM   4715 C CG2 . THR C 2 115 ? 14.936  48.544 -28.687 1.00 88.57  ? 115 THR H CG2 1 
ATOM   4716 N N   . LEU C 2 116 ? 12.274  52.229 -28.435 1.00 80.31  ? 116 LEU H N   1 
ATOM   4717 C CA  . LEU C 2 116 ? 11.096  53.087 -28.523 1.00 76.90  ? 116 LEU H CA  1 
ATOM   4718 C C   . LEU C 2 116 ? 10.181  52.568 -29.625 1.00 76.99  ? 116 LEU H C   1 
ATOM   4719 O O   . LEU C 2 116 ? 10.538  52.602 -30.808 1.00 81.45  ? 116 LEU H O   1 
ATOM   4720 C CB  . LEU C 2 116 ? 11.492  54.540 -28.779 1.00 76.52  ? 116 LEU H CB  1 
ATOM   4721 C CG  . LEU C 2 116 ? 10.302  55.486 -28.974 1.00 75.42  ? 116 LEU H CG  1 
ATOM   4722 C CD1 . LEU C 2 116 ? 9.465   55.593 -27.706 1.00 81.43  ? 116 LEU H CD1 1 
ATOM   4723 C CD2 . LEU C 2 116 ? 10.773  56.862 -29.415 1.00 83.52  ? 116 LEU H CD2 1 
ATOM   4724 N N   . VAL C 2 117 ? 9.003   52.088 -29.241 1.00 74.84  ? 117 VAL H N   1 
ATOM   4725 C CA  . VAL C 2 117 ? 7.994   51.642 -30.189 1.00 73.59  ? 117 VAL H CA  1 
ATOM   4726 C C   . VAL C 2 117 ? 6.938   52.735 -30.289 1.00 72.03  ? 117 VAL H C   1 
ATOM   4727 O O   . VAL C 2 117 ? 6.205   52.997 -29.327 1.00 79.44  ? 117 VAL H O   1 
ATOM   4728 C CB  . VAL C 2 117 ? 7.374   50.304 -29.772 1.00 71.75  ? 117 VAL H CB  1 
ATOM   4729 C CG1 . VAL C 2 117 ? 6.197   49.975 -30.672 1.00 67.49  ? 117 VAL H CG1 1 
ATOM   4730 C CG2 . VAL C 2 117 ? 8.415   49.198 -29.816 1.00 71.70  ? 117 VAL H CG2 1 
ATOM   4731 N N   . THR C 2 118 ? 6.881   53.389 -31.445 1.00 71.98  ? 118 THR H N   1 
ATOM   4732 C CA  . THR C 2 118 ? 5.794   54.297 -31.777 1.00 72.71  ? 118 THR H CA  1 
ATOM   4733 C C   . THR C 2 118 ? 4.725   53.545 -32.558 1.00 76.30  ? 118 THR H C   1 
ATOM   4734 O O   . THR C 2 118 ? 5.011   52.574 -33.264 1.00 81.79  ? 118 THR H O   1 
ATOM   4735 C CB  . THR C 2 118 ? 6.296   55.489 -32.594 1.00 72.68  ? 118 THR H CB  1 
ATOM   4736 O OG1 . THR C 2 118 ? 6.973   55.016 -33.763 1.00 80.53  ? 118 THR H OG1 1 
ATOM   4737 C CG2 . THR C 2 118 ? 7.250   56.343 -31.777 1.00 76.22  ? 118 THR H CG2 1 
ATOM   4738 N N   . VAL C 2 119 ? 3.485   53.997 -32.423 1.00 71.13  ? 119 VAL H N   1 
ATOM   4739 C CA  . VAL C 2 119 ? 2.331   53.314 -33.000 1.00 72.65  ? 119 VAL H CA  1 
ATOM   4740 C C   . VAL C 2 119 ? 1.669   54.291 -33.960 1.00 85.23  ? 119 VAL H C   1 
ATOM   4741 O O   . VAL C 2 119 ? 0.908   55.172 -33.539 1.00 89.47  ? 119 VAL H O   1 
ATOM   4742 C CB  . VAL C 2 119 ? 1.348   52.836 -31.928 1.00 67.85  ? 119 VAL H CB  1 
ATOM   4743 C CG1 . VAL C 2 119 ? 0.137   52.181 -32.569 1.00 70.36  ? 119 VAL H CG1 1 
ATOM   4744 C CG2 . VAL C 2 119 ? 2.047   51.892 -30.966 1.00 72.45  ? 119 VAL H CG2 1 
ATOM   4745 N N   . SER C 2 120 ? 1.931   54.127 -35.252 1.00 93.66  ? 120 SER H N   1 
ATOM   4746 C CA  . SER C 2 120 ? 1.445   55.071 -36.243 1.00 101.11 ? 120 SER H CA  1 
ATOM   4747 C C   . SER C 2 120 ? 1.181   54.322 -37.536 1.00 107.11 ? 120 SER H C   1 
ATOM   4748 O O   . SER C 2 120 ? 1.838   53.307 -37.808 1.00 98.91  ? 120 SER H O   1 
ATOM   4749 C CB  . SER C 2 120 ? 2.465   56.192 -36.485 1.00 104.22 ? 120 SER H CB  1 
ATOM   4750 O OG  . SER C 2 120 ? 1.953   57.174 -37.367 1.00 108.84 ? 120 SER H OG  1 
ATOM   4751 N N   . SER C 2 121 ? 0.230   54.787 -38.353 1.00 108.48 ? 121 SER H N   1 
ATOM   4752 C CA  . SER C 2 121 ? 0.138   54.287 -39.727 1.00 104.41 ? 121 SER H CA  1 
ATOM   4753 C C   . SER C 2 121 ? 1.119   54.959 -40.670 1.00 110.13 ? 121 SER H C   1 
ATOM   4754 O O   . SER C 2 121 ? 1.171   54.587 -41.852 1.00 108.52 ? 121 SER H O   1 
ATOM   4755 C CB  . SER C 2 121 ? -1.282  54.482 -40.264 1.00 115.98 ? 121 SER H CB  1 
ATOM   4756 O OG  . SER C 2 121 ? -1.611  55.858 -40.345 1.00 128.51 ? 121 SER H OG  1 
ATOM   4757 N N   . ALA C 2 122 ? 1.901   55.923 -40.180 1.00 118.72 ? 122 ALA H N   1 
ATOM   4758 C CA  . ALA C 2 122 ? 2.846   56.644 -41.016 1.00 118.29 ? 122 ALA H CA  1 
ATOM   4759 C C   . ALA C 2 122 ? 3.937   55.690 -41.496 1.00 109.60 ? 122 ALA H C   1 
ATOM   4760 O O   . ALA C 2 122 ? 4.029   54.535 -41.075 1.00 114.02 ? 122 ALA H O   1 
ATOM   4761 C CB  . ALA C 2 122 ? 3.461   57.818 -40.257 1.00 118.26 ? 122 ALA H CB  1 
ATOM   4762 N N   . SER C 2 123 ? 4.782   56.198 -42.385 1.00 105.12 ? 123 SER H N   1 
ATOM   4763 C CA  . SER C 2 123 ? 5.778   55.392 -43.074 1.00 104.11 ? 123 SER H CA  1 
ATOM   4764 C C   . SER C 2 123 ? 7.175   55.772 -42.608 1.00 103.83 ? 123 SER H C   1 
ATOM   4765 O O   . SER C 2 123 ? 7.487   56.961 -42.466 1.00 108.76 ? 123 SER H O   1 
ATOM   4766 C CB  . SER C 2 123 ? 5.660   55.570 -44.590 1.00 110.54 ? 123 SER H CB  1 
ATOM   4767 O OG  . SER C 2 123 ? 4.336   55.317 -45.026 1.00 104.73 ? 123 SER H OG  1 
ATOM   4768 N N   . THR C 2 124 ? 8.004   54.758 -42.366 1.00 98.10  ? 124 THR H N   1 
ATOM   4769 C CA  . THR C 2 124 ? 9.418   54.940 -42.071 1.00 98.09  ? 124 THR H CA  1 
ATOM   4770 C C   . THR C 2 124 ? 10.066  55.877 -43.077 1.00 102.73 ? 124 THR H C   1 
ATOM   4771 O O   . THR C 2 124 ? 10.014  55.640 -44.288 1.00 109.39 ? 124 THR H O   1 
ATOM   4772 C CB  . THR C 2 124 ? 10.134  53.586 -42.096 1.00 100.25 ? 124 THR H CB  1 
ATOM   4773 O OG1 . THR C 2 124 ? 9.825   52.903 -43.319 1.00 117.65 ? 124 THR H OG1 1 
ATOM   4774 C CG2 . THR C 2 124 ? 9.716   52.733 -40.914 1.00 93.78  ? 124 THR H CG2 1 
ATOM   4775 N N   . LYS C 2 125 ? 10.677  56.948 -42.577 1.00 92.03  ? 125 LYS H N   1 
ATOM   4776 C CA  . LYS C 2 125 ? 11.414  57.877 -43.421 1.00 93.55  ? 125 LYS H CA  1 
ATOM   4777 C C   . LYS C 2 125 ? 12.766  58.181 -42.802 1.00 89.91  ? 125 LYS H C   1 
ATOM   4778 O O   . LYS C 2 125 ? 12.858  58.493 -41.610 1.00 89.35  ? 125 LYS H O   1 
ATOM   4779 C CB  . LYS C 2 125 ? 10.629  59.171 -43.660 1.00 98.61  ? 125 LYS H CB  1 
ATOM   4780 C CG  . LYS C 2 125 ? 9.446   58.990 -44.600 1.00 118.15 ? 125 LYS H CG  1 
ATOM   4781 C CD  . LYS C 2 125 ? 8.490   60.172 -44.562 1.00 141.37 ? 125 LYS H CD  1 
ATOM   4782 C CE  . LYS C 2 125 ? 7.150   59.800 -45.181 1.00 155.64 ? 125 LYS H CE  1 
ATOM   4783 N NZ  . LYS C 2 125 ? 6.136   60.885 -45.080 1.00 201.08 ? 125 LYS H NZ  1 
ATOM   4784 N N   . GLY C 2 126 ? 13.804  58.099 -43.628 1.00 98.35  ? 126 GLY H N   1 
ATOM   4785 C CA  . GLY C 2 126 ? 15.161  58.303 -43.195 1.00 96.65  ? 126 GLY H CA  1 
ATOM   4786 C C   . GLY C 2 126 ? 15.530  59.764 -43.081 1.00 95.36  ? 126 GLY H C   1 
ATOM   4787 O O   . GLY C 2 126 ? 14.924  60.643 -43.701 1.00 100.45 ? 126 GLY H O   1 
ATOM   4788 N N   . PRO C 2 127 ? 16.550  60.046 -42.282 1.00 90.21  ? 127 PRO H N   1 
ATOM   4789 C CA  . PRO C 2 127 ? 16.910  61.438 -42.008 1.00 88.42  ? 127 PRO H CA  1 
ATOM   4790 C C   . PRO C 2 127 ? 17.629  62.073 -43.187 1.00 89.98  ? 127 PRO H C   1 
ATOM   4791 O O   . PRO C 2 127 ? 17.937  61.439 -44.198 1.00 96.50  ? 127 PRO H O   1 
ATOM   4792 C CB  . PRO C 2 127 ? 17.830  61.326 -40.791 1.00 83.91  ? 127 PRO H CB  1 
ATOM   4793 C CG  . PRO C 2 127 ? 18.408  59.962 -40.880 1.00 94.99  ? 127 PRO H CG  1 
ATOM   4794 C CD  . PRO C 2 127 ? 17.332  59.098 -41.471 1.00 94.91  ? 127 PRO H CD  1 
ATOM   4795 N N   . SER C 2 128 ? 17.886  63.368 -43.044 1.00 81.72  ? 128 SER H N   1 
ATOM   4796 C CA  . SER C 2 128 ? 18.779  64.089 -43.942 1.00 86.04  ? 128 SER H CA  1 
ATOM   4797 C C   . SER C 2 128 ? 19.762  64.860 -43.073 1.00 88.59  ? 128 SER H C   1 
ATOM   4798 O O   . SER C 2 128 ? 19.347  65.698 -42.266 1.00 95.19  ? 128 SER H O   1 
ATOM   4799 C CB  . SER C 2 128 ? 18.002  65.020 -44.882 1.00 98.81  ? 128 SER H CB  1 
ATOM   4800 O OG  . SER C 2 128 ? 17.066  64.286 -45.657 1.00 101.67 ? 128 SER H OG  1 
ATOM   4801 N N   . VAL C 2 129 ? 21.050  64.538 -43.195 1.00 85.07  ? 129 VAL H N   1 
ATOM   4802 C CA  . VAL C 2 129 ? 22.092  65.154 -42.380 1.00 89.79  ? 129 VAL H CA  1 
ATOM   4803 C C   . VAL C 2 129 ? 22.736  66.286 -43.164 1.00 97.95  ? 129 VAL H C   1 
ATOM   4804 O O   . VAL C 2 129 ? 23.134  66.110 -44.322 1.00 104.89 ? 129 VAL H O   1 
ATOM   4805 C CB  . VAL C 2 129 ? 23.147  64.121 -41.947 1.00 89.82  ? 129 VAL H CB  1 
ATOM   4806 C CG1 . VAL C 2 129 ? 24.179  64.772 -41.034 1.00 96.53  ? 129 VAL H CG1 1 
ATOM   4807 C CG2 . VAL C 2 129 ? 22.490  62.943 -41.245 1.00 93.71  ? 129 VAL H CG2 1 
ATOM   4808 N N   . PHE C 2 130 ? 22.857  67.444 -42.520 1.00 101.15 ? 130 PHE H N   1 
ATOM   4809 C CA  . PHE C 2 130 ? 23.453  68.642 -43.077 1.00 101.65 ? 130 PHE H CA  1 
ATOM   4810 C C   . PHE C 2 130 ? 24.340  69.270 -42.010 1.00 99.42  ? 130 PHE H C   1 
ATOM   4811 O O   . PHE C 2 130 ? 23.939  69.356 -40.840 1.00 99.76  ? 130 PHE H O   1 
ATOM   4812 C CB  . PHE C 2 130 ? 22.385  69.644 -43.529 1.00 101.20 ? 130 PHE H CB  1 
ATOM   4813 C CG  . PHE C 2 130 ? 21.345  69.061 -44.450 1.00 98.86  ? 130 PHE H CG  1 
ATOM   4814 C CD1 . PHE C 2 130 ? 21.713  68.451 -45.640 1.00 107.07 ? 130 PHE H CD1 1 
ATOM   4815 C CD2 . PHE C 2 130 ? 20.000  69.126 -44.127 1.00 105.01 ? 130 PHE H CD2 1 
ATOM   4816 C CE1 . PHE C 2 130 ? 20.756  67.920 -46.491 1.00 118.29 ? 130 PHE H CE1 1 
ATOM   4817 C CE2 . PHE C 2 130 ? 19.041  68.595 -44.973 1.00 104.30 ? 130 PHE H CE2 1 
ATOM   4818 C CZ  . PHE C 2 130 ? 19.419  67.993 -46.154 1.00 105.91 ? 130 PHE H CZ  1 
ATOM   4819 N N   . PRO C 2 131 ? 25.533  69.732 -42.373 1.00 106.25 ? 131 PRO H N   1 
ATOM   4820 C CA  . PRO C 2 131 ? 26.483  70.194 -41.361 1.00 104.19 ? 131 PRO H CA  1 
ATOM   4821 C C   . PRO C 2 131 ? 26.176  71.610 -40.892 1.00 105.51 ? 131 PRO H C   1 
ATOM   4822 O O   . PRO C 2 131 ? 25.518  72.402 -41.570 1.00 104.16 ? 131 PRO H O   1 
ATOM   4823 C CB  . PRO C 2 131 ? 27.825  70.137 -42.097 1.00 107.34 ? 131 PRO H CB  1 
ATOM   4824 C CG  . PRO C 2 131 ? 27.463  70.455 -43.507 1.00 113.96 ? 131 PRO H CG  1 
ATOM   4825 C CD  . PRO C 2 131 ? 26.072  69.884 -43.738 1.00 108.56 ? 131 PRO H CD  1 
ATOM   4826 N N   . LEU C 2 132 ? 26.706  71.926 -39.710 1.00 104.85 ? 132 LEU H N   1 
ATOM   4827 C CA  . LEU C 2 132 ? 26.605  73.308 -39.190 1.00 106.96 ? 132 LEU H CA  1 
ATOM   4828 C C   . LEU C 2 132 ? 28.049  73.779 -39.083 1.00 104.13 ? 132 LEU H C   1 
ATOM   4829 O O   . LEU C 2 132 ? 28.673  73.528 -38.043 1.00 105.04 ? 132 LEU H O   1 
ATOM   4830 C CB  . LEU C 2 132 ? 25.921  73.290 -37.827 1.00 109.33 ? 132 LEU H CB  1 
ATOM   4831 C CG  . LEU C 2 132 ? 24.404  73.138 -37.871 1.00 109.66 ? 132 LEU H CG  1 
ATOM   4832 C CD1 . LEU C 2 132 ? 23.785  73.536 -36.542 1.00 107.04 ? 132 LEU H CD1 1 
ATOM   4833 C CD2 . LEU C 2 132 ? 23.821  73.969 -39.003 1.00 106.27 ? 132 LEU H CD2 1 
ATOM   4834 N N   . ALA C 2 133 ? 28.559  74.406 -40.137 1.00 106.09 ? 133 ALA H N   1 
ATOM   4835 C CA  . ALA C 2 133 ? 29.988  74.777 -40.177 1.00 112.68 ? 133 ALA H CA  1 
ATOM   4836 C C   . ALA C 2 133 ? 30.343  75.771 -39.076 1.00 117.58 ? 133 ALA H C   1 
ATOM   4837 O O   . ALA C 2 133 ? 29.472  76.548 -38.662 1.00 117.48 ? 133 ALA H O   1 
ATOM   4838 C CB  . ALA C 2 133 ? 30.299  75.344 -41.533 1.00 116.22 ? 133 ALA H CB  1 
ATOM   4839 N N   . PRO C 2 134 ? 31.615  75.854 -38.619 1.00 114.45 ? 134 PRO H N   1 
ATOM   4840 C CA  . PRO C 2 134 ? 31.990  76.860 -37.634 1.00 125.40 ? 134 PRO H CA  1 
ATOM   4841 C C   . PRO C 2 134 ? 32.374  78.194 -38.282 1.00 145.35 ? 134 PRO H C   1 
ATOM   4842 O O   . PRO C 2 134 ? 33.070  78.181 -39.274 1.00 154.98 ? 134 PRO H O   1 
ATOM   4843 C CB  . PRO C 2 134 ? 33.239  76.247 -36.997 1.00 125.20 ? 134 PRO H CB  1 
ATOM   4844 C CG  . PRO C 2 134 ? 33.903  75.501 -38.127 1.00 117.65 ? 134 PRO H CG  1 
ATOM   4845 C CD  . PRO C 2 134 ? 32.758  74.997 -38.979 1.00 115.77 ? 134 PRO H CD  1 
ATOM   4846 N N   . SER C 2 135 ? 31.917  79.309 -37.709 1.00 156.39 ? 135 SER H N   1 
ATOM   4847 C CA  . SER C 2 135 ? 32.315  80.642 -38.231 1.00 168.58 ? 135 SER H CA  1 
ATOM   4848 C C   . SER C 2 135 ? 33.685  80.994 -37.652 1.00 188.60 ? 135 SER H C   1 
ATOM   4849 O O   . SER C 2 135 ? 33.738  81.857 -36.761 1.00 204.56 ? 135 SER H O   1 
ATOM   4850 C CB  . SER C 2 135 ? 31.291  81.683 -37.885 1.00 163.93 ? 135 SER H CB  1 
ATOM   4851 O OG  . SER C 2 135 ? 31.080  81.736 -36.482 1.00 165.57 ? 135 SER H OG  1 
ATOM   4852 N N   . SER C 2 136 ? 34.751  80.361 -38.151 1.00 202.93 ? 136 SER H N   1 
ATOM   4853 C CA  . SER C 2 136 ? 36.109  80.577 -37.581 1.00 205.86 ? 136 SER H CA  1 
ATOM   4854 C C   . SER C 2 136 ? 36.394  82.076 -37.456 1.00 220.57 ? 136 SER H C   1 
ATOM   4855 O O   . SER C 2 136 ? 37.127  82.462 -36.525 1.00 227.76 ? 136 SER H O   1 
ATOM   4856 C CB  . SER C 2 136 ? 37.162  79.900 -38.413 1.00 194.06 ? 136 SER H CB  1 
ATOM   4857 O OG  . SER C 2 136 ? 37.245  80.497 -39.697 1.00 196.08 ? 136 SER H OG  1 
ATOM   4858 N N   . LYS C 2 137 ? 35.830  82.881 -38.357 1.00 220.23 ? 137 LYS H N   1 
ATOM   4859 C CA  . LYS C 2 137 ? 36.044  84.349 -38.309 1.00 226.78 ? 137 LYS H CA  1 
ATOM   4860 C C   . LYS C 2 137 ? 35.662  84.865 -36.917 1.00 236.14 ? 137 LYS H C   1 
ATOM   4861 O O   . LYS C 2 137 ? 36.385  85.735 -36.393 1.00 261.37 ? 137 LYS H O   1 
ATOM   4862 C CB  . LYS C 2 137 ? 35.222  85.035 -39.404 1.00 220.53 ? 137 LYS H CB  1 
ATOM   4863 C CG  . LYS C 2 137 ? 35.416  86.541 -39.498 1.00 221.30 ? 137 LYS H CG  1 
ATOM   4864 C CD  . LYS C 2 137 ? 36.864  86.937 -39.686 1.00 217.83 ? 137 LYS H CD  1 
ATOM   4865 C CE  . LYS C 2 137 ? 37.169  88.325 -39.162 1.00 208.94 ? 137 LYS H CE  1 
ATOM   4866 N NZ  . LYS C 2 137 ? 36.911  88.425 -37.706 1.00 202.28 ? 137 LYS H NZ  1 
ATOM   4867 N N   . SER C 2 138 ? 34.581  84.336 -36.337 1.00 237.02 ? 138 SER H N   1 
ATOM   4868 C CA  . SER C 2 138 ? 34.109  84.815 -35.011 1.00 225.77 ? 138 SER H CA  1 
ATOM   4869 C C   . SER C 2 138 ? 35.247  84.747 -33.989 1.00 229.75 ? 138 SER H C   1 
ATOM   4870 O O   . SER C 2 138 ? 35.896  83.688 -33.904 1.00 228.43 ? 138 SER H O   1 
ATOM   4871 C CB  . SER C 2 138 ? 32.929  84.016 -34.535 1.00 211.86 ? 138 SER H CB  1 
ATOM   4872 O OG  . SER C 2 138 ? 33.321  82.690 -34.207 1.00 211.36 ? 138 SER H OG  1 
ATOM   4873 N N   . THR C 2 139 ? 35.461  85.828 -33.235 1.00 220.36 ? 139 THR H N   1 
ATOM   4874 C CA  . THR C 2 139 ? 36.499  85.827 -32.172 1.00 216.60 ? 139 THR H CA  1 
ATOM   4875 C C   . THR C 2 139 ? 36.145  84.755 -31.138 1.00 217.00 ? 139 THR H C   1 
ATOM   4876 O O   . THR C 2 139 ? 37.023  83.926 -30.840 1.00 228.09 ? 139 THR H O   1 
ATOM   4877 C CB  . THR C 2 139 ? 36.610  87.213 -31.529 1.00 211.24 ? 139 THR H CB  1 
ATOM   4878 O OG1 . THR C 2 139 ? 35.391  87.478 -30.835 1.00 212.58 ? 139 THR H OG1 1 
ATOM   4879 C CG2 . THR C 2 139 ? 36.870  88.308 -32.541 1.00 206.15 ? 139 THR H CG2 1 
ATOM   4880 N N   . SER C 2 140 ? 34.912  84.776 -30.618 1.00 221.37 ? 140 SER H N   1 
ATOM   4881 C CA  . SER C 2 140 ? 34.443  83.735 -29.662 1.00 206.50 ? 140 SER H CA  1 
ATOM   4882 C C   . SER C 2 140 ? 35.602  83.239 -28.793 1.00 199.60 ? 140 SER H C   1 
ATOM   4883 O O   . SER C 2 140 ? 35.854  82.018 -28.791 1.00 194.77 ? 140 SER H O   1 
ATOM   4884 C CB  . SER C 2 140 ? 33.775  82.596 -30.389 1.00 195.27 ? 140 SER H CB  1 
ATOM   4885 O OG  . SER C 2 140 ? 34.665  81.993 -31.315 1.00 196.24 ? 140 SER H OG  1 
ATOM   4886 N N   . GLY C 2 141 ? 36.277  84.151 -28.086 1.00 208.88 ? 141 GLY H N   1 
ATOM   4887 C CA  . GLY C 2 141 ? 37.373  83.744 -27.188 1.00 200.68 ? 141 GLY H CA  1 
ATOM   4888 C C   . GLY C 2 141 ? 38.234  82.679 -27.840 1.00 195.99 ? 141 GLY H C   1 
ATOM   4889 O O   . GLY C 2 141 ? 38.835  82.971 -28.893 1.00 197.88 ? 141 GLY H O   1 
ATOM   4890 N N   . GLY C 2 142 ? 38.299  81.488 -27.239 1.00 186.66 ? 142 GLY H N   1 
ATOM   4891 C CA  . GLY C 2 142 ? 39.082  80.378 -27.814 1.00 172.59 ? 142 GLY H CA  1 
ATOM   4892 C C   . GLY C 2 142 ? 38.213  79.164 -28.088 1.00 159.27 ? 142 GLY H C   1 
ATOM   4893 O O   . GLY C 2 142 ? 38.776  78.069 -28.275 1.00 155.29 ? 142 GLY H O   1 
ATOM   4894 N N   . THR C 2 143 ? 36.891  79.349 -28.120 1.00 153.51 ? 143 THR H N   1 
ATOM   4895 C CA  . THR C 2 143 ? 35.965  78.203 -28.317 1.00 139.53 ? 143 THR H CA  1 
ATOM   4896 C C   . THR C 2 143 ? 35.178  78.394 -29.615 1.00 132.60 ? 143 THR H C   1 
ATOM   4897 O O   . THR C 2 143 ? 35.071  79.545 -30.069 1.00 150.47 ? 143 THR H O   1 
ATOM   4898 C CB  . THR C 2 143 ? 35.059  78.027 -27.094 1.00 141.48 ? 143 THR H CB  1 
ATOM   4899 O OG1 . THR C 2 143 ? 34.575  79.318 -26.728 1.00 169.44 ? 143 THR H OG1 1 
ATOM   4900 C CG2 . THR C 2 143 ? 35.778  77.402 -25.918 1.00 129.50 ? 143 THR H CG2 1 
ATOM   4901 N N   . ALA C 2 144 ? 34.650  77.308 -30.180 1.00 117.71 ? 144 ALA H N   1 
ATOM   4902 C CA  . ALA C 2 144 ? 33.939  77.385 -31.447 1.00 107.97 ? 144 ALA H CA  1 
ATOM   4903 C C   . ALA C 2 144 ? 33.073  76.137 -31.556 1.00 101.73 ? 144 ALA H C   1 
ATOM   4904 O O   . ALA C 2 144 ? 33.468  75.067 -31.092 1.00 101.55 ? 144 ALA H O   1 
ATOM   4905 C CB  . ALA C 2 144 ? 34.906  77.485 -32.632 1.00 110.61 ? 144 ALA H CB  1 
ATOM   4906 N N   . ALA C 2 145 ? 31.894  76.270 -32.155 1.00 97.11  ? 145 ALA H N   1 
ATOM   4907 C CA  . ALA C 2 145 ? 30.894  75.211 -32.117 1.00 90.07  ? 145 ALA H CA  1 
ATOM   4908 C C   . ALA C 2 145 ? 30.661  74.610 -33.499 1.00 85.62  ? 145 ALA H C   1 
ATOM   4909 O O   . ALA C 2 145 ? 30.711  75.305 -34.516 1.00 95.01  ? 145 ALA H O   1 
ATOM   4910 C CB  . ALA C 2 145 ? 29.567  75.728 -31.546 1.00 96.55  ? 145 ALA H CB  1 
ATOM   4911 N N   . LEU C 2 146 ? 30.391  73.303 -33.512 1.00 88.40  ? 146 LEU H N   1 
ATOM   4912 C CA  . LEU C 2 146 ? 30.153  72.521 -34.719 1.00 88.04  ? 146 LEU H CA  1 
ATOM   4913 C C   . LEU C 2 146 ? 28.795  71.847 -34.605 1.00 89.11  ? 146 LEU H C   1 
ATOM   4914 O O   . LEU C 2 146 ? 28.323  71.581 -33.499 1.00 93.83  ? 146 LEU H O   1 
ATOM   4915 C CB  . LEU C 2 146 ? 31.218  71.452 -34.884 1.00 95.33  ? 146 LEU H CB  1 
ATOM   4916 C CG  . LEU C 2 146 ? 32.620  72.015 -35.008 1.00 106.46 ? 146 LEU H CG  1 
ATOM   4917 C CD1 . LEU C 2 146 ? 33.609  70.894 -34.958 1.00 106.32 ? 146 LEU H CD1 1 
ATOM   4918 C CD2 . LEU C 2 146 ? 32.720  72.743 -36.310 1.00 105.93 ? 146 LEU H CD2 1 
ATOM   4919 N N   . GLY C 2 147 ? 28.166  71.537 -35.736 1.00 87.89  ? 147 GLY H N   1 
ATOM   4920 C CA  . GLY C 2 147 ? 26.879  70.868 -35.638 1.00 84.48  ? 147 GLY H CA  1 
ATOM   4921 C C   . GLY C 2 147 ? 26.599  69.875 -36.743 1.00 91.27  ? 147 GLY H C   1 
ATOM   4922 O O   . GLY C 2 147 ? 27.251  69.869 -37.790 1.00 100.18 ? 147 GLY H O   1 
ATOM   4923 N N   . CYS C 2 148 ? 25.579  69.051 -36.508 1.00 88.38  ? 148 CYS H N   1 
ATOM   4924 C CA  . CYS C 2 148 ? 25.072  68.129 -37.530 1.00 90.74  ? 148 CYS H CA  1 
ATOM   4925 C C   . CYS C 2 148 ? 23.550  68.081 -37.423 1.00 92.63  ? 148 CYS H C   1 
ATOM   4926 O O   . CYS C 2 148 ? 22.991  67.275 -36.673 1.00 124.03 ? 148 CYS H O   1 
ATOM   4927 C CB  . CYS C 2 148 ? 25.687  66.747 -37.388 1.00 91.03  ? 148 CYS H CB  1 
ATOM   4928 S SG  . CYS C 2 148 ? 27.338  66.606 -38.061 1.00 110.83 ? 148 CYS H SG  1 
ATOM   4929 N N   . LEU C 2 149 ? 22.887  68.938 -38.194 1.00 84.76  ? 149 LEU H N   1 
ATOM   4930 C CA  . LEU C 2 149 ? 21.435  68.933 -38.235 1.00 88.84  ? 149 LEU H CA  1 
ATOM   4931 C C   . LEU C 2 149 ? 20.925  67.701 -38.962 1.00 86.18  ? 149 LEU H C   1 
ATOM   4932 O O   . LEU C 2 149 ? 21.487  67.271 -39.974 1.00 93.01  ? 149 LEU H O   1 
ATOM   4933 C CB  . LEU C 2 149 ? 20.909  70.191 -38.916 1.00 101.63 ? 149 LEU H CB  1 
ATOM   4934 C CG  . LEU C 2 149 ? 21.327  71.495 -38.254 1.00 122.32 ? 149 LEU H CG  1 
ATOM   4935 C CD1 . LEU C 2 149 ? 20.575  72.684 -38.831 1.00 156.00 ? 149 LEU H CD1 1 
ATOM   4936 C CD2 . LEU C 2 149 ? 21.086  71.385 -36.768 1.00 152.51 ? 149 LEU H CD2 1 
ATOM   4937 N N   . VAL C 2 150 ? 19.848  67.140 -38.428 1.00 76.69  ? 150 VAL H N   1 
ATOM   4938 C CA  . VAL C 2 150 ? 19.262  65.896 -38.895 1.00 71.78  ? 150 VAL H CA  1 
ATOM   4939 C C   . VAL C 2 150 ? 17.774  66.155 -39.046 1.00 78.39  ? 150 VAL H C   1 
ATOM   4940 O O   . VAL C 2 150 ? 17.064  66.271 -38.044 1.00 84.81  ? 150 VAL H O   1 
ATOM   4941 C CB  . VAL C 2 150 ? 19.520  64.748 -37.910 1.00 72.28  ? 150 VAL H CB  1 
ATOM   4942 C CG1 . VAL C 2 150 ? 18.941  63.470 -38.431 1.00 77.16  ? 150 VAL H CG1 1 
ATOM   4943 C CG2 . VAL C 2 150 ? 21.009  64.586 -37.656 1.00 77.63  ? 150 VAL H CG2 1 
ATOM   4944 N N   . LYS C 2 151 ? 17.288  66.294 -40.282 1.00 80.32  ? 151 LYS H N   1 
ATOM   4945 C CA  . LYS C 2 151 ? 15.865  66.701 -40.446 1.00 77.99  ? 151 LYS H CA  1 
ATOM   4946 C C   . LYS C 2 151 ? 15.043  65.653 -41.199 1.00 80.01  ? 151 LYS H C   1 
ATOM   4947 O O   . LYS C 2 151 ? 15.650  64.719 -41.761 1.00 83.48  ? 151 LYS H O   1 
ATOM   4948 C CB  . LYS C 2 151 ? 15.796  68.033 -41.199 1.00 78.52  ? 151 LYS H CB  1 
ATOM   4949 C CG  . LYS C 2 151 ? 16.609  69.167 -40.590 1.00 101.54 ? 151 LYS H CG  1 
ATOM   4950 C CD  . LYS C 2 151 ? 17.401  69.946 -41.617 1.00 140.97 ? 151 LYS H CD  1 
ATOM   4951 C CE  . LYS C 2 151 ? 18.157  71.111 -41.018 1.00 150.72 ? 151 LYS H CE  1 
ATOM   4952 N NZ  . LYS C 2 151 ? 19.117  71.698 -41.981 1.00 199.32 ? 151 LYS H NZ  1 
ATOM   4953 N N   . ASP C 2 152 ? 13.714  65.811 -41.198 1.00 89.84  ? 152 ASP H N   1 
ATOM   4954 C CA  . ASP C 2 152 ? 12.799  64.908 -41.969 1.00 87.96  ? 152 ASP H CA  1 
ATOM   4955 C C   . ASP C 2 152 ? 13.013  63.416 -41.640 1.00 92.01  ? 152 ASP H C   1 
ATOM   4956 O O   . ASP C 2 152 ? 13.297  62.653 -42.579 1.00 93.40  ? 152 ASP H O   1 
ATOM   4957 C CB  . ASP C 2 152 ? 12.933  65.146 -43.466 1.00 100.35 ? 152 ASP H CB  1 
ATOM   4958 C CG  . ASP C 2 152 ? 12.641  66.583 -43.863 1.00 115.38 ? 152 ASP H CG  1 
ATOM   4959 O OD1 . ASP C 2 152 ? 12.341  67.390 -42.961 1.00 97.20  ? 152 ASP H OD1 1 
ATOM   4960 O OD2 . ASP C 2 152 ? 12.717  66.882 -45.071 1.00 137.51 ? 152 ASP H OD2 1 
ATOM   4961 N N   . TYR C 2 153 ? 12.814  63.018 -40.384 1.00 90.06  ? 153 TYR H N   1 
ATOM   4962 C CA  . TYR C 2 153 ? 12.876  61.571 -40.046 1.00 89.87  ? 153 TYR H CA  1 
ATOM   4963 C C   . TYR C 2 153 ? 11.596  61.243 -39.269 1.00 90.09  ? 153 TYR H C   1 
ATOM   4964 O O   . TYR C 2 153 ? 11.216  62.050 -38.398 1.00 91.07  ? 153 TYR H O   1 
ATOM   4965 C CB  . TYR C 2 153 ? 14.183  61.245 -39.314 1.00 96.44  ? 153 TYR H CB  1 
ATOM   4966 C CG  . TYR C 2 153 ? 14.249  61.653 -37.864 1.00 91.14  ? 153 TYR H CG  1 
ATOM   4967 C CD1 . TYR C 2 153 ? 13.541  60.965 -36.893 1.00 99.40  ? 153 TYR H CD1 1 
ATOM   4968 C CD2 . TYR C 2 153 ? 15.019  62.731 -37.459 1.00 87.42  ? 153 TYR H CD2 1 
ATOM   4969 C CE1 . TYR C 2 153 ? 13.594  61.333 -35.561 1.00 104.84 ? 153 TYR H CE1 1 
ATOM   4970 C CE2 . TYR C 2 153 ? 15.086  63.112 -36.129 1.00 91.65  ? 153 TYR H CE2 1 
ATOM   4971 C CZ  . TYR C 2 153 ? 14.372  62.408 -35.176 1.00 102.16 ? 153 TYR H CZ  1 
ATOM   4972 O OH  . TYR C 2 153 ? 14.418  62.768 -33.852 1.00 101.43 ? 153 TYR H OH  1 
ATOM   4973 N N   . PHE C 2 154 ? 10.915  60.144 -39.604 1.00 92.19  ? 154 PHE H N   1 
ATOM   4974 C CA  . PHE C 2 154 ? 9.624   59.888 -38.910 1.00 96.96  ? 154 PHE H CA  1 
ATOM   4975 C C   . PHE C 2 154 ? 9.608   58.934 -37.707 1.00 106.28 ? 154 PHE H C   1 
ATOM   4976 O O   . PHE C 2 154 ? 8.699   59.073 -36.879 1.00 117.47 ? 154 PHE H O   1 
ATOM   4977 C CB  . PHE C 2 154 ? 8.576   59.227 -39.811 1.00 104.83 ? 154 PHE H CB  1 
ATOM   4978 C CG  . PHE C 2 154 ? 7.360   58.825 -39.019 1.00 101.29 ? 154 PHE H CG  1 
ATOM   4979 C CD1 . PHE C 2 154 ? 6.611   59.782 -38.353 1.00 95.80  ? 154 PHE H CD1 1 
ATOM   4980 C CD2 . PHE C 2 154 ? 7.008   57.494 -38.875 1.00 109.95 ? 154 PHE H CD2 1 
ATOM   4981 C CE1 . PHE C 2 154 ? 5.511   59.421 -37.594 1.00 102.96 ? 154 PHE H CE1 1 
ATOM   4982 C CE2 . PHE C 2 154 ? 5.908   57.135 -38.113 1.00 114.34 ? 154 PHE H CE2 1 
ATOM   4983 C CZ  . PHE C 2 154 ? 5.164   58.097 -37.472 1.00 118.38 ? 154 PHE H CZ  1 
ATOM   4984 N N   . PRO C 2 155 ? 10.372  57.821 -37.661 1.00 105.42 ? 155 PRO H N   1 
ATOM   4985 C CA  . PRO C 2 155 ? 10.467  57.032 -36.425 1.00 84.91  ? 155 PRO H CA  1 
ATOM   4986 C C   . PRO C 2 155 ? 11.376  57.843 -35.489 1.00 106.48 ? 155 PRO H C   1 
ATOM   4987 O O   . PRO C 2 155 ? 12.518  58.058 -35.842 1.00 173.98 ? 155 PRO H O   1 
ATOM   4988 C CB  . PRO C 2 155 ? 11.054  55.692 -36.875 1.00 86.92  ? 155 PRO H CB  1 
ATOM   4989 C CG  . PRO C 2 155 ? 10.730  55.643 -38.350 1.00 98.53  ? 155 PRO H CG  1 
ATOM   4990 C CD  . PRO C 2 155 ? 10.928  57.075 -38.798 1.00 78.88  ? 155 PRO H CD  1 
ATOM   4991 N N   . GLU C 2 156 ? 10.868  58.261 -34.326 1.00 98.66  ? 156 GLU H N   1 
ATOM   4992 C CA  . GLU C 2 156 ? 11.639  59.166 -33.422 1.00 105.96 ? 156 GLU H CA  1 
ATOM   4993 C C   . GLU C 2 156 ? 13.050  58.645 -33.105 1.00 108.77 ? 156 GLU H C   1 
ATOM   4994 O O   . GLU C 2 156 ? 13.996  59.444 -33.247 1.00 109.85 ? 156 GLU H O   1 
ATOM   4995 C CB  . GLU C 2 156 ? 10.844  59.421 -32.138 1.00 108.49 ? 156 GLU H CB  1 
ATOM   4996 C CG  . GLU C 2 156 ? 11.434  60.520 -31.275 1.00 107.72 ? 156 GLU H CG  1 
ATOM   4997 C CD  . GLU C 2 156 ? 10.593  60.888 -30.065 1.00 118.32 ? 156 GLU H CD  1 
ATOM   4998 O OE1 . GLU C 2 156 ? 9.521   60.276 -29.885 1.00 148.09 ? 156 GLU H OE1 1 
ATOM   4999 O OE2 . GLU C 2 156 ? 11.011  61.786 -29.308 1.00 116.59 ? 156 GLU H OE2 1 
ATOM   5000 N N   . PRO C 2 157 ? 13.272  57.383 -32.669 1.00 97.29  ? 157 PRO H N   1 
ATOM   5001 C CA  . PRO C 2 157 ? 14.616  56.933 -32.268 1.00 92.68  ? 157 PRO H CA  1 
ATOM   5002 C C   . PRO C 2 157 ? 15.701  57.340 -33.280 1.00 95.72  ? 157 PRO H C   1 
ATOM   5003 O O   . PRO C 2 157 ? 15.677  56.829 -34.387 1.00 98.44  ? 157 PRO H O   1 
ATOM   5004 C CB  . PRO C 2 157 ? 14.501  55.399 -32.206 1.00 91.05  ? 157 PRO H CB  1 
ATOM   5005 C CG  . PRO C 2 157 ? 13.151  55.080 -32.820 1.00 94.83  ? 157 PRO H CG  1 
ATOM   5006 C CD  . PRO C 2 157 ? 12.295  56.300 -32.559 1.00 94.58  ? 157 PRO H CD  1 
ATOM   5007 N N   . VAL C 2 158 ? 16.618  58.232 -32.879 1.00 93.11  ? 158 VAL H N   1 
ATOM   5008 C CA  . VAL C 2 158 ? 17.713  58.689 -33.801 1.00 89.32  ? 158 VAL H CA  1 
ATOM   5009 C C   . VAL C 2 158 ? 18.924  58.876 -32.875 1.00 93.43  ? 158 VAL H C   1 
ATOM   5010 O O   . VAL C 2 158 ? 18.785  59.614 -31.887 1.00 94.48  ? 158 VAL H O   1 
ATOM   5011 C CB  . VAL C 2 158 ? 17.514  59.895 -34.699 1.00 89.93  ? 158 VAL H CB  1 
ATOM   5012 C CG1 . VAL C 2 158 ? 18.832  60.395 -35.269 1.00 74.54  ? 158 VAL H CG1 1 
ATOM   5013 C CG2 . VAL C 2 158 ? 16.542  59.590 -35.824 1.00 104.54 ? 158 VAL H CG2 1 
ATOM   5014 N N   . THR C 2 159 ? 20.055  58.259 -33.202 1.00 94.83  ? 159 THR H N   1 
ATOM   5015 C CA  . THR C 2 159 ? 21.262  58.316 -32.391 1.00 90.03  ? 159 THR H CA  1 
ATOM   5016 C C   . THR C 2 159 ? 22.354  59.082 -33.130 1.00 83.70  ? 159 THR H C   1 
ATOM   5017 O O   . THR C 2 159 ? 22.541  58.904 -34.337 1.00 88.02  ? 159 THR H O   1 
ATOM   5018 C CB  . THR C 2 159 ? 21.756  56.906 -32.056 1.00 91.58  ? 159 THR H CB  1 
ATOM   5019 O OG1 . THR C 2 159 ? 22.024  56.192 -33.270 1.00 115.93 ? 159 THR H OG1 1 
ATOM   5020 C CG2 . THR C 2 159 ? 20.701  56.151 -31.267 1.00 89.23  ? 159 THR H CG2 1 
ATOM   5021 N N   . VAL C 2 160 ? 23.078  59.927 -32.399 1.00 87.05  ? 160 VAL H N   1 
ATOM   5022 C CA  . VAL C 2 160 ? 24.131  60.766 -32.963 1.00 86.44  ? 160 VAL H CA  1 
ATOM   5023 C C   . VAL C 2 160 ? 25.386  60.602 -32.115 1.00 98.86  ? 160 VAL H C   1 
ATOM   5024 O O   . VAL C 2 160 ? 25.358  60.857 -30.905 1.00 102.82 ? 160 VAL H O   1 
ATOM   5025 C CB  . VAL C 2 160 ? 23.718  62.246 -33.027 1.00 83.23  ? 160 VAL H CB  1 
ATOM   5026 C CG1 . VAL C 2 160 ? 24.877  63.093 -33.519 1.00 89.45  ? 160 VAL H CG1 1 
ATOM   5027 C CG2 . VAL C 2 160 ? 22.509  62.423 -33.928 1.00 86.57  ? 160 VAL H CG2 1 
ATOM   5028 N N   . SER C 2 161 ? 26.487  60.192 -32.748 1.00 106.32 ? 161 SER H N   1 
ATOM   5029 C CA  . SER C 2 161 ? 27.773  60.067 -32.071 1.00 104.04 ? 161 SER H CA  1 
ATOM   5030 C C   . SER C 2 161 ? 28.846  60.754 -32.902 1.00 104.00 ? 161 SER H C   1 
ATOM   5031 O O   . SER C 2 161 ? 28.822  60.691 -34.130 1.00 108.52 ? 161 SER H O   1 
ATOM   5032 C CB  . SER C 2 161 ? 28.147  58.598 -31.833 1.00 108.13 ? 161 SER H CB  1 
ATOM   5033 O OG  . SER C 2 161 ? 28.841  58.058 -32.942 1.00 120.38 ? 161 SER H OG  1 
ATOM   5034 N N   . TRP C 2 162 ? 29.792  61.410 -32.242 1.00 103.33 ? 162 TRP H N   1 
ATOM   5035 C CA  . TRP C 2 162 ? 30.774  62.227 -32.945 1.00 108.80 ? 162 TRP H CA  1 
ATOM   5036 C C   . TRP C 2 162 ? 32.123  61.521 -33.005 1.00 107.82 ? 162 TRP H C   1 
ATOM   5037 O O   . TRP C 2 162 ? 32.624  61.035 -31.985 1.00 109.68 ? 162 TRP H O   1 
ATOM   5038 C CB  . TRP C 2 162 ? 30.921  63.594 -32.279 1.00 108.73 ? 162 TRP H CB  1 
ATOM   5039 C CG  . TRP C 2 162 ? 29.783  64.514 -32.566 1.00 103.39 ? 162 TRP H CG  1 
ATOM   5040 C CD1 . TRP C 2 162 ? 28.501  64.395 -32.115 1.00 103.28 ? 162 TRP H CD1 1 
ATOM   5041 C CD2 . TRP C 2 162 ? 29.815  65.692 -33.380 1.00 99.52  ? 162 TRP H CD2 1 
ATOM   5042 N NE1 . TRP C 2 162 ? 27.734  65.431 -32.590 1.00 102.78 ? 162 TRP H NE1 1 
ATOM   5043 C CE2 . TRP C 2 162 ? 28.517  66.240 -33.371 1.00 101.42 ? 162 TRP H CE2 1 
ATOM   5044 C CE3 . TRP C 2 162 ? 30.817  66.342 -34.109 1.00 102.24 ? 162 TRP H CE3 1 
ATOM   5045 C CZ2 . TRP C 2 162 ? 28.195  67.408 -34.060 1.00 101.33 ? 162 TRP H CZ2 1 
ATOM   5046 C CZ3 . TRP C 2 162 ? 30.493  67.499 -34.798 1.00 103.32 ? 162 TRP H CZ3 1 
ATOM   5047 C CH2 . TRP C 2 162 ? 29.194  68.020 -34.768 1.00 103.00 ? 162 TRP H CH2 1 
ATOM   5048 N N   . ASN C 2 163 ? 32.704  61.482 -34.206 1.00 103.55 ? 163 ASN H N   1 
ATOM   5049 C CA  . ASN C 2 163 ? 34.012  60.875 -34.459 1.00 102.62 ? 163 ASN H CA  1 
ATOM   5050 C C   . ASN C 2 163 ? 34.089  59.451 -33.912 1.00 106.46 ? 163 ASN H C   1 
ATOM   5051 O O   . ASN C 2 163 ? 35.079  59.049 -33.297 1.00 108.38 ? 163 ASN H O   1 
ATOM   5052 C CB  . ASN C 2 163 ? 35.142  61.740 -33.893 1.00 103.39 ? 163 ASN H CB  1 
ATOM   5053 C CG  . ASN C 2 163 ? 35.361  63.019 -34.687 1.00 104.20 ? 163 ASN H CG  1 
ATOM   5054 O OD1 . ASN C 2 163 ? 34.677  63.278 -35.678 1.00 108.89 ? 163 ASN H OD1 1 
ATOM   5055 N ND2 . ASN C 2 163 ? 36.328  63.820 -34.258 1.00 101.06 ? 163 ASN H ND2 1 
ATOM   5056 N N   . SER C 2 164 ? 33.027  58.686 -34.154 1.00 114.64 ? 164 SER H N   1 
ATOM   5057 C CA  . SER C 2 164 ? 32.923  57.284 -33.744 1.00 117.67 ? 164 SER H CA  1 
ATOM   5058 C C   . SER C 2 164 ? 33.308  57.107 -32.275 1.00 120.07 ? 164 SER H C   1 
ATOM   5059 O O   . SER C 2 164 ? 34.231  56.374 -31.919 1.00 124.02 ? 164 SER H O   1 
ATOM   5060 C CB  . SER C 2 164 ? 33.763  56.384 -34.647 1.00 118.92 ? 164 SER H CB  1 
ATOM   5061 O OG  . SER C 2 164 ? 33.203  56.309 -35.948 1.00 117.99 ? 164 SER H OG  1 
ATOM   5062 N N   . GLY C 2 165 ? 32.575  57.817 -31.416 1.00 118.35 ? 165 GLY H N   1 
ATOM   5063 C CA  . GLY C 2 165 ? 32.758  57.728 -29.983 1.00 113.24 ? 165 GLY H CA  1 
ATOM   5064 C C   . GLY C 2 165 ? 33.934  58.493 -29.419 1.00 109.89 ? 165 GLY H C   1 
ATOM   5065 O O   . GLY C 2 165 ? 34.042  58.604 -28.190 1.00 111.76 ? 165 GLY H O   1 
ATOM   5066 N N   . ALA C 2 166 ? 34.821  59.027 -30.265 1.00 109.00 ? 166 ALA H N   1 
ATOM   5067 C CA  . ALA C 2 166 ? 35.992  59.731 -29.748 1.00 112.21 ? 166 ALA H CA  1 
ATOM   5068 C C   . ALA C 2 166 ? 35.616  61.055 -29.097 1.00 116.81 ? 166 ALA H C   1 
ATOM   5069 O O   . ALA C 2 166 ? 36.228  61.446 -28.097 1.00 121.20 ? 166 ALA H O   1 
ATOM   5070 C CB  . ALA C 2 166 ? 37.013  59.961 -30.862 1.00 116.42 ? 166 ALA H CB  1 
ATOM   5071 N N   . LEU C 2 167 ? 34.626  61.755 -29.642 1.00 124.08 ? 167 LEU H N   1 
ATOM   5072 C CA  . LEU C 2 167 ? 34.162  63.011 -29.067 1.00 119.83 ? 167 LEU H CA  1 
ATOM   5073 C C   . LEU C 2 167 ? 33.003  62.739 -28.120 1.00 119.32 ? 167 LEU H C   1 
ATOM   5074 O O   . LEU C 2 167 ? 31.970  62.197 -28.529 1.00 115.72 ? 167 LEU H O   1 
ATOM   5075 C CB  . LEU C 2 167 ? 33.737  63.992 -30.155 1.00 113.62 ? 167 LEU H CB  1 
ATOM   5076 C CG  . LEU C 2 167 ? 34.866  64.569 -30.997 1.00 120.86 ? 167 LEU H CG  1 
ATOM   5077 C CD1 . LEU C 2 167 ? 34.284  65.500 -32.040 1.00 115.31 ? 167 LEU H CD1 1 
ATOM   5078 C CD2 . LEU C 2 167 ? 35.859  65.293 -30.103 1.00 112.53 ? 167 LEU H CD2 1 
ATOM   5079 N N   . THR C 2 168 ? 33.176  63.126 -26.857 1.00 121.69 ? 168 THR H N   1 
ATOM   5080 C CA  . THR C 2 168 ? 32.141  62.961 -25.842 1.00 115.44 ? 168 THR H CA  1 
ATOM   5081 C C   . THR C 2 168 ? 31.974  64.161 -24.922 1.00 112.63 ? 168 THR H C   1 
ATOM   5082 O O   . THR C 2 168 ? 30.913  64.287 -24.301 1.00 112.14 ? 168 THR H O   1 
ATOM   5083 C CB  . THR C 2 168 ? 32.426  61.720 -24.987 1.00 120.09 ? 168 THR H CB  1 
ATOM   5084 O OG1 . THR C 2 168 ? 31.358  61.523 -24.054 1.00 131.84 ? 168 THR H OG1 1 
ATOM   5085 C CG2 . THR C 2 168 ? 33.738  61.882 -24.227 1.00 119.95 ? 168 THR H CG2 1 
ATOM   5086 N N   . SER C 2 169 ? 32.960  65.050 -24.817 1.00 111.63 ? 169 SER H N   1 
ATOM   5087 C CA  . SER C 2 169 ? 32.935  66.180 -23.897 1.00 111.49 ? 169 SER H CA  1 
ATOM   5088 C C   . SER C 2 169 ? 32.611  67.452 -24.672 1.00 105.29 ? 169 SER H C   1 
ATOM   5089 O O   . SER C 2 169 ? 33.337  67.820 -25.602 1.00 101.85 ? 169 SER H O   1 
ATOM   5090 C CB  . SER C 2 169 ? 34.273  66.306 -23.167 1.00 114.82 ? 169 SER H CB  1 
ATOM   5091 O OG  . SER C 2 169 ? 35.333  66.502 -24.086 1.00 127.61 ? 169 SER H OG  1 
ATOM   5092 N N   . GLY C 2 170 ? 31.525  68.120 -24.283 1.00 103.82 ? 170 GLY H N   1 
ATOM   5093 C CA  . GLY C 2 170 ? 31.030  69.284 -24.985 1.00 106.33 ? 170 GLY H CA  1 
ATOM   5094 C C   . GLY C 2 170 ? 29.894  69.005 -25.946 1.00 98.72  ? 170 GLY H C   1 
ATOM   5095 O O   . GLY C 2 170 ? 29.347  69.952 -26.526 1.00 93.95  ? 170 GLY H O   1 
ATOM   5096 N N   . VAL C 2 171 ? 29.520  67.744 -26.128 1.00 103.64 ? 171 VAL H N   1 
ATOM   5097 C CA  . VAL C 2 171 ? 28.478  67.387 -27.082 1.00 103.03 ? 171 VAL H CA  1 
ATOM   5098 C C   . VAL C 2 171 ? 27.114  67.599 -26.436 1.00 106.48 ? 171 VAL H C   1 
ATOM   5099 O O   . VAL C 2 171 ? 26.846  67.102 -25.336 1.00 110.49 ? 171 VAL H O   1 
ATOM   5100 C CB  . VAL C 2 171 ? 28.650  65.935 -27.558 1.00 104.24 ? 171 VAL H CB  1 
ATOM   5101 C CG1 . VAL C 2 171 ? 27.641  65.606 -28.653 1.00 96.76  ? 171 VAL H CG1 1 
ATOM   5102 C CG2 . VAL C 2 171 ? 30.075  65.695 -28.038 1.00 111.10 ? 171 VAL H CG2 1 
ATOM   5103 N N   . HIS C 2 172 ? 26.255  68.349 -27.116 1.00 106.22 ? 172 HIS H N   1 
ATOM   5104 C CA  . HIS C 2 172 ? 24.863  68.551 -26.728 1.00 94.86  ? 172 HIS H CA  1 
ATOM   5105 C C   . HIS C 2 172 ? 24.023  68.085 -27.913 1.00 96.65  ? 172 HIS H C   1 
ATOM   5106 O O   . HIS C 2 172 ? 23.937  68.780 -28.929 1.00 100.55 ? 172 HIS H O   1 
ATOM   5107 C CB  . HIS C 2 172 ? 24.593  70.015 -26.382 1.00 92.86  ? 172 HIS H CB  1 
ATOM   5108 C CG  . HIS C 2 172 ? 25.199  70.452 -25.084 1.00 105.22 ? 172 HIS H CG  1 
ATOM   5109 N ND1 . HIS C 2 172 ? 24.774  69.974 -23.863 1.00 110.22 ? 172 HIS H ND1 1 
ATOM   5110 C CD2 . HIS C 2 172 ? 26.199  71.325 -24.818 1.00 108.06 ? 172 HIS H CD2 1 
ATOM   5111 C CE1 . HIS C 2 172 ? 25.486  70.534 -22.902 1.00 109.94 ? 172 HIS H CE1 1 
ATOM   5112 N NE2 . HIS C 2 172 ? 26.359  71.357 -23.455 1.00 111.70 ? 172 HIS H NE2 1 
ATOM   5113 N N   . THR C 2 173 ? 23.446  66.893 -27.810 1.00 89.80  ? 173 THR H N   1 
ATOM   5114 C CA  . THR C 2 173 ? 22.559  66.361 -28.841 1.00 86.50  ? 173 THR H CA  1 
ATOM   5115 C C   . THR C 2 173 ? 21.126  66.637 -28.390 1.00 87.78  ? 173 THR H C   1 
ATOM   5116 O O   . THR C 2 173 ? 20.613  65.981 -27.477 1.00 91.01  ? 173 THR H O   1 
ATOM   5117 C CB  . THR C 2 173 ? 22.800  64.869 -29.075 1.00 85.83  ? 173 THR H CB  1 
ATOM   5118 O OG1 . THR C 2 173 ? 23.966  64.697 -29.893 1.00 88.01  ? 173 THR H OG1 1 
ATOM   5119 C CG2 . THR C 2 173 ? 21.617  64.239 -29.795 1.00 90.02  ? 173 THR H CG2 1 
ATOM   5120 N N   . PHE C 2 174 ? 20.492  67.621 -29.024 1.00 83.98  ? 174 PHE H N   1 
ATOM   5121 C CA  . PHE C 2 174 ? 19.236  68.175 -28.544 1.00 81.02  ? 174 PHE H CA  1 
ATOM   5122 C C   . PHE C 2 174 ? 18.093  67.178 -28.714 1.00 83.79  ? 174 PHE H C   1 
ATOM   5123 O O   . PHE C 2 174 ? 18.220  66.194 -29.444 1.00 86.92  ? 174 PHE H O   1 
ATOM   5124 C CB  . PHE C 2 174 ? 18.926  69.472 -29.291 1.00 83.82  ? 174 PHE H CB  1 
ATOM   5125 C CG  . PHE C 2 174 ? 19.703  70.656 -28.794 1.00 79.90  ? 174 PHE H CG  1 
ATOM   5126 C CD1 . PHE C 2 174 ? 19.228  71.425 -27.744 1.00 84.37  ? 174 PHE H CD1 1 
ATOM   5127 C CD2 . PHE C 2 174 ? 20.912  70.996 -29.376 1.00 83.99  ? 174 PHE H CD2 1 
ATOM   5128 C CE1 . PHE C 2 174 ? 19.948  72.513 -27.288 1.00 90.03  ? 174 PHE H CE1 1 
ATOM   5129 C CE2 . PHE C 2 174 ? 21.633  72.081 -28.925 1.00 83.13  ? 174 PHE H CE2 1 
ATOM   5130 C CZ  . PHE C 2 174 ? 21.148  72.842 -27.877 1.00 89.24  ? 174 PHE H CZ  1 
ATOM   5131 N N   . PRO C 2 175 ? 16.971  67.400 -28.033 1.00 87.71  ? 175 PRO H N   1 
ATOM   5132 C CA  . PRO C 2 175 ? 15.814  66.521 -28.218 1.00 87.68  ? 175 PRO H CA  1 
ATOM   5133 C C   . PRO C 2 175 ? 15.076  66.820 -29.515 1.00 86.31  ? 175 PRO H C   1 
ATOM   5134 O O   . PRO C 2 175 ? 15.240  67.870 -30.139 1.00 89.63  ? 175 PRO H O   1 
ATOM   5135 C CB  . PRO C 2 175 ? 14.928  66.807 -26.998 1.00 83.86  ? 175 PRO H CB  1 
ATOM   5136 C CG  . PRO C 2 175 ? 15.721  67.691 -26.099 1.00 80.87  ? 175 PRO H CG  1 
ATOM   5137 C CD  . PRO C 2 175 ? 16.790  68.331 -26.908 1.00 87.48  ? 175 PRO H CD  1 
ATOM   5138 N N   . ALA C 2 176 ? 14.255  65.853 -29.915 1.00 85.69  ? 176 ALA H N   1 
ATOM   5139 C CA  . ALA C 2 176 ? 13.557  65.941 -31.187 1.00 91.97  ? 176 ALA H CA  1 
ATOM   5140 C C   . ALA C 2 176 ? 12.511  67.045 -31.158 1.00 96.04  ? 176 ALA H C   1 
ATOM   5141 O O   . ALA C 2 176 ? 11.946  67.373 -30.113 1.00 105.64 ? 176 ALA H O   1 
ATOM   5142 C CB  . ALA C 2 176 ? 12.896  64.606 -31.529 1.00 105.35 ? 176 ALA H CB  1 
ATOM   5143 N N   . VAL C 2 177 ? 12.264  67.624 -32.328 1.00 90.98  ? 177 VAL H N   1 
ATOM   5144 C CA  . VAL C 2 177 ? 11.212  68.611 -32.528 1.00 88.08  ? 177 VAL H CA  1 
ATOM   5145 C C   . VAL C 2 177 ? 10.304  68.098 -33.634 1.00 89.01  ? 177 VAL H C   1 
ATOM   5146 O O   . VAL C 2 177 ? 10.776  67.789 -34.734 1.00 100.20 ? 177 VAL H O   1 
ATOM   5147 C CB  . VAL C 2 177 ? 11.785  69.994 -32.886 1.00 91.52  ? 177 VAL H CB  1 
ATOM   5148 C CG1 . VAL C 2 177 ? 10.656  70.959 -33.206 1.00 97.56  ? 177 VAL H CG1 1 
ATOM   5149 C CG2 . VAL C 2 177 ? 12.641  70.528 -31.750 1.00 88.50  ? 177 VAL H CG2 1 
ATOM   5150 N N   . LEU C 2 178 ? 9.011   67.997 -33.345 1.00 84.26  ? 178 LEU H N   1 
ATOM   5151 C CA  . LEU C 2 178 ? 8.041   67.529 -34.326 1.00 87.52  ? 178 LEU H CA  1 
ATOM   5152 C C   . LEU C 2 178 ? 7.597   68.709 -35.183 1.00 91.70  ? 178 LEU H C   1 
ATOM   5153 O O   . LEU C 2 178 ? 6.965   69.644 -34.680 1.00 94.74  ? 178 LEU H O   1 
ATOM   5154 C CB  . LEU C 2 178 ? 6.845   66.869 -33.643 1.00 82.89  ? 178 LEU H CB  1 
ATOM   5155 C CG  . LEU C 2 178 ? 5.785   66.281 -34.578 1.00 85.19  ? 178 LEU H CG  1 
ATOM   5156 C CD1 . LEU C 2 178 ? 6.349   65.098 -35.345 1.00 93.15  ? 178 LEU H CD1 1 
ATOM   5157 C CD2 . LEU C 2 178 ? 4.545   65.866 -33.799 1.00 81.21  ? 178 LEU H CD2 1 
ATOM   5158 N N   . GLN C 2 179 ? 7.935   68.667 -36.469 1.00 91.44  ? 179 GLN H N   1 
ATOM   5159 C CA  . GLN C 2 179 ? 7.624   69.762 -37.373 1.00 90.16  ? 179 GLN H CA  1 
ATOM   5160 C C   . GLN C 2 179 ? 6.193   69.641 -37.890 1.00 87.64  ? 179 GLN H C   1 
ATOM   5161 O O   . GLN C 2 179 ? 5.525   68.617 -37.718 1.00 87.13  ? 179 GLN H O   1 
ATOM   5162 C CB  . GLN C 2 179 ? 8.607   69.788 -38.541 1.00 87.88  ? 179 GLN H CB  1 
ATOM   5163 C CG  . GLN C 2 179 ? 10.058  69.813 -38.120 1.00 86.81  ? 179 GLN H CG  1 
ATOM   5164 C CD  . GLN C 2 179 ? 10.988  69.417 -39.242 1.00 90.40  ? 179 GLN H CD  1 
ATOM   5165 O OE1 . GLN C 2 179 ? 11.646  70.261 -39.850 1.00 107.72 ? 179 GLN H OE1 1 
ATOM   5166 N NE2 . GLN C 2 179 ? 11.049  68.121 -39.525 1.00 94.15  ? 179 GLN H NE2 1 
ATOM   5167 N N   . SER C 2 180 ? 5.728   70.712 -38.542 1.00 81.65  ? 180 SER H N   1 
ATOM   5168 C CA  . SER C 2 180 ? 4.389   70.712 -39.124 1.00 81.30  ? 180 SER H CA  1 
ATOM   5169 C C   . SER C 2 180 ? 4.219   69.605 -40.153 1.00 84.03  ? 180 SER H C   1 
ATOM   5170 O O   . SER C 2 180 ? 3.102   69.120 -40.366 1.00 85.09  ? 180 SER H O   1 
ATOM   5171 C CB  . SER C 2 180 ? 4.094   72.072 -39.758 1.00 81.95  ? 180 SER H CB  1 
ATOM   5172 O OG  . SER C 2 180 ? 5.192   72.512 -40.540 1.00 85.28  ? 180 SER H OG  1 
ATOM   5173 N N   . SER C 2 181 ? 5.309   69.184 -40.795 1.00 89.47  ? 181 SER H N   1 
ATOM   5174 C CA  . SER C 2 181 ? 5.228   68.108 -41.773 1.00 88.62  ? 181 SER H CA  1 
ATOM   5175 C C   . SER C 2 181 ? 4.848   66.776 -41.138 1.00 92.17  ? 181 SER H C   1 
ATOM   5176 O O   . SER C 2 181 ? 4.419   65.860 -41.850 1.00 97.94  ? 181 SER H O   1 
ATOM   5177 C CB  . SER C 2 181 ? 6.568   67.988 -42.495 1.00 92.39  ? 181 SER H CB  1 
ATOM   5178 O OG  . SER C 2 181 ? 7.636   68.115 -41.569 1.00 90.92  ? 181 SER H OG  1 
ATOM   5179 N N   . GLY C 2 182 ? 4.968   66.662 -39.817 1.00 91.48  ? 182 GLY H N   1 
ATOM   5180 C CA  . GLY C 2 182 ? 4.842   65.395 -39.133 1.00 86.53  ? 182 GLY H CA  1 
ATOM   5181 C C   . GLY C 2 182 ? 6.134   64.627 -39.010 1.00 90.66  ? 182 GLY H C   1 
ATOM   5182 O O   . GLY C 2 182 ? 6.102   63.448 -38.640 1.00 92.12  ? 182 GLY H O   1 
ATOM   5183 N N   . LEU C 2 183 ? 7.267   65.259 -39.304 1.00 89.83  ? 183 LEU H N   1 
ATOM   5184 C CA  . LEU C 2 183 ? 8.581   64.639 -39.265 1.00 91.12  ? 183 LEU H CA  1 
ATOM   5185 C C   . LEU C 2 183 ? 9.438   65.338 -38.216 1.00 91.75  ? 183 LEU H C   1 
ATOM   5186 O O   . LEU C 2 183 ? 9.225   66.512 -37.901 1.00 91.97  ? 183 LEU H O   1 
ATOM   5187 C CB  . LEU C 2 183 ? 9.262   64.720 -40.636 1.00 88.32  ? 183 LEU H CB  1 
ATOM   5188 C CG  . LEU C 2 183 ? 8.595   63.931 -41.761 1.00 96.42  ? 183 LEU H CG  1 
ATOM   5189 C CD1 . LEU C 2 183 ? 9.460   63.913 -43.016 1.00 104.26 ? 183 LEU H CD1 1 
ATOM   5190 C CD2 . LEU C 2 183 ? 8.250   62.523 -41.314 1.00 100.07 ? 183 LEU H CD2 1 
ATOM   5191 N N   . TYR C 2 184 ? 10.413  64.613 -37.680 1.00 89.72  ? 184 TYR H N   1 
ATOM   5192 C CA  . TYR C 2 184 ? 11.230  65.105 -36.581 1.00 89.99  ? 184 TYR H CA  1 
ATOM   5193 C C   . TYR C 2 184 ? 12.540  65.701 -37.094 1.00 85.47  ? 184 TYR H C   1 
ATOM   5194 O O   . TYR C 2 184 ? 13.002  65.406 -38.201 1.00 92.70  ? 184 TYR H O   1 
ATOM   5195 C CB  . TYR C 2 184 ? 11.529  63.983 -35.578 1.00 94.49  ? 184 TYR H CB  1 
ATOM   5196 C CG  . TYR C 2 184 ? 10.316  63.405 -34.872 1.00 96.69  ? 184 TYR H CG  1 
ATOM   5197 C CD1 . TYR C 2 184 ? 9.809   63.992 -33.718 1.00 94.01  ? 184 TYR H CD1 1 
ATOM   5198 C CD2 . TYR C 2 184 ? 9.694   62.255 -35.347 1.00 106.52 ? 184 TYR H CD2 1 
ATOM   5199 C CE1 . TYR C 2 184 ? 8.707   63.456 -33.066 1.00 101.02 ? 184 TYR H CE1 1 
ATOM   5200 C CE2 . TYR C 2 184 ? 8.593   61.714 -34.700 1.00 99.91  ? 184 TYR H CE2 1 
ATOM   5201 C CZ  . TYR C 2 184 ? 8.104   62.318 -33.561 1.00 102.47 ? 184 TYR H CZ  1 
ATOM   5202 O OH  . TYR C 2 184 ? 7.010   61.781 -32.920 1.00 99.42  ? 184 TYR H OH  1 
ATOM   5203 N N   . SER C 2 185 ? 13.142  66.546 -36.261 1.00 79.10  ? 185 SER H N   1 
ATOM   5204 C CA  . SER C 2 185 ? 14.405  67.188 -36.607 1.00 82.07  ? 185 SER H CA  1 
ATOM   5205 C C   . SER C 2 185 ? 15.227  67.368 -35.341 1.00 88.46  ? 185 SER H C   1 
ATOM   5206 O O   . SER C 2 185 ? 14.782  68.021 -34.392 1.00 94.52  ? 185 SER H O   1 
ATOM   5207 C CB  . SER C 2 185 ? 14.176  68.534 -37.299 1.00 87.23  ? 185 SER H CB  1 
ATOM   5208 O OG  . SER C 2 185 ? 14.023  69.579 -36.358 1.00 103.96 ? 185 SER H OG  1 
ATOM   5209 N N   . LEU C 2 186 ? 16.417  66.783 -35.335 1.00 93.03  ? 186 LEU H N   1 
ATOM   5210 C CA  . LEU C 2 186 ? 17.379  66.915 -34.256 1.00 91.53  ? 186 LEU H CA  1 
ATOM   5211 C C   . LEU C 2 186 ? 18.504  67.856 -34.657 1.00 93.75  ? 186 LEU H C   1 
ATOM   5212 O O   . LEU C 2 186 ? 18.820  68.019 -35.841 1.00 101.97 ? 186 LEU H O   1 
ATOM   5213 C CB  . LEU C 2 186 ? 17.986  65.564 -33.882 1.00 88.57  ? 186 LEU H CB  1 
ATOM   5214 C CG  . LEU C 2 186 ? 17.068  64.497 -33.309 1.00 94.40  ? 186 LEU H CG  1 
ATOM   5215 C CD1 . LEU C 2 186 ? 17.764  63.169 -33.390 1.00 99.78  ? 186 LEU H CD1 1 
ATOM   5216 C CD2 . LEU C 2 186 ? 16.786  64.829 -31.874 1.00 100.05 ? 186 LEU H CD2 1 
ATOM   5217 N N   . SER C 2 187 ? 19.110  68.465 -33.648 1.00 94.62  ? 187 SER H N   1 
ATOM   5218 C CA  . SER C 2 187 ? 20.360  69.189 -33.788 1.00 89.23  ? 187 SER H CA  1 
ATOM   5219 C C   . SER C 2 187 ? 21.354  68.614 -32.792 1.00 93.64  ? 187 SER H C   1 
ATOM   5220 O O   . SER C 2 187 ? 21.019  68.403 -31.623 1.00 100.05 ? 187 SER H O   1 
ATOM   5221 C CB  . SER C 2 187 ? 20.165  70.690 -33.544 1.00 93.64  ? 187 SER H CB  1 
ATOM   5222 O OG  . SER C 2 187 ? 19.381  70.934 -32.390 1.00 100.43 ? 187 SER H OG  1 
ATOM   5223 N N   . SER C 2 188 ? 22.566  68.332 -33.255 1.00 94.27  ? 188 SER H N   1 
ATOM   5224 C CA  . SER C 2 188 ? 23.646  67.933 -32.366 1.00 93.45  ? 188 SER H CA  1 
ATOM   5225 C C   . SER C 2 188 ? 24.786  68.926 -32.519 1.00 88.87  ? 188 SER H C   1 
ATOM   5226 O O   . SER C 2 188 ? 25.190  69.256 -33.639 1.00 92.11  ? 188 SER H O   1 
ATOM   5227 C CB  . SER C 2 188 ? 24.138  66.512 -32.649 1.00 90.72  ? 188 SER H CB  1 
ATOM   5228 O OG  . SER C 2 188 ? 25.060  66.494 -33.721 1.00 96.99  ? 188 SER H OG  1 
ATOM   5229 N N   . VAL C 2 189 ? 25.293  69.402 -31.388 1.00 80.64  ? 189 VAL H N   1 
ATOM   5230 C CA  . VAL C 2 189 ? 26.264  70.482 -31.348 1.00 85.44  ? 189 VAL H CA  1 
ATOM   5231 C C   . VAL C 2 189 ? 27.446  70.024 -30.509 1.00 94.27  ? 189 VAL H C   1 
ATOM   5232 O O   . VAL C 2 189 ? 27.301  69.208 -29.597 1.00 99.30  ? 189 VAL H O   1 
ATOM   5233 C CB  . VAL C 2 189 ? 25.633  71.766 -30.767 1.00 83.87  ? 189 VAL H CB  1 
ATOM   5234 C CG1 . VAL C 2 189 ? 26.689  72.807 -30.466 1.00 89.08  ? 189 VAL H CG1 1 
ATOM   5235 C CG2 . VAL C 2 189 ? 24.579  72.310 -31.713 1.00 88.10  ? 189 VAL H CG2 1 
ATOM   5236 N N   . VAL C 2 190 ? 28.631  70.532 -30.836 1.00 95.26  ? 190 VAL H N   1 
ATOM   5237 C CA  . VAL C 2 190 ? 29.832  70.254 -30.055 1.00 95.13  ? 190 VAL H CA  1 
ATOM   5238 C C   . VAL C 2 190 ? 30.616  71.548 -29.888 1.00 95.97  ? 190 VAL H C   1 
ATOM   5239 O O   . VAL C 2 190 ? 30.982  72.184 -30.883 1.00 96.79  ? 190 VAL H O   1 
ATOM   5240 C CB  . VAL C 2 190 ? 30.721  69.184 -30.709 1.00 94.75  ? 190 VAL H CB  1 
ATOM   5241 C CG1 . VAL C 2 190 ? 31.982  68.991 -29.902 1.00 95.08  ? 190 VAL H CG1 1 
ATOM   5242 C CG2 . VAL C 2 190 ? 29.977  67.880 -30.832 1.00 96.24  ? 190 VAL H CG2 1 
ATOM   5243 N N   . THR C 2 191 ? 30.885  71.933 -28.638 1.00 100.78 ? 191 THR H N   1 
ATOM   5244 C CA  . THR C 2 191 ? 31.821  73.017 -28.363 1.00 102.32 ? 191 THR H CA  1 
ATOM   5245 C C   . THR C 2 191 ? 33.246  72.476 -28.359 1.00 109.99 ? 191 THR H C   1 
ATOM   5246 O O   . THR C 2 191 ? 33.525  71.432 -27.762 1.00 112.47 ? 191 THR H O   1 
ATOM   5247 C CB  . THR C 2 191 ? 31.505  73.698 -27.031 1.00 109.69 ? 191 THR H CB  1 
ATOM   5248 O OG1 . THR C 2 191 ? 31.642  72.751 -25.962 1.00 113.92 ? 191 THR H OG1 1 
ATOM   5249 C CG2 . THR C 2 191 ? 30.097  74.276 -27.041 1.00 110.49 ? 191 THR H CG2 1 
ATOM   5250 N N   . VAL C 2 192 ? 34.147  73.201 -29.017 1.00 108.85 ? 192 VAL H N   1 
ATOM   5251 C CA  . VAL C 2 192 ? 35.491  72.724 -29.342 1.00 111.04 ? 192 VAL H CA  1 
ATOM   5252 C C   . VAL C 2 192 ? 36.465  73.870 -29.154 1.00 120.77 ? 192 VAL H C   1 
ATOM   5253 O O   . VAL C 2 192 ? 36.089  75.045 -29.271 1.00 122.94 ? 192 VAL H O   1 
ATOM   5254 C CB  . VAL C 2 192 ? 35.555  72.208 -30.806 1.00 108.42 ? 192 VAL H CB  1 
ATOM   5255 C CG1 . VAL C 2 192 ? 36.948  71.842 -31.245 1.00 110.01 ? 192 VAL H CG1 1 
ATOM   5256 C CG2 . VAL C 2 192 ? 34.648  71.016 -30.994 1.00 108.63 ? 192 VAL H CG2 1 
ATOM   5257 N N   . PRO C 2 193 ? 37.718  73.575 -28.805 1.00 126.37 ? 193 PRO H N   1 
ATOM   5258 C CA  . PRO C 2 193 ? 38.738  74.625 -28.893 1.00 130.95 ? 193 PRO H CA  1 
ATOM   5259 C C   . PRO C 2 193 ? 38.894  75.122 -30.323 1.00 132.43 ? 193 PRO H C   1 
ATOM   5260 O O   . PRO C 2 193 ? 38.938  74.336 -31.273 1.00 133.43 ? 193 PRO H O   1 
ATOM   5261 C CB  . PRO C 2 193 ? 40.008  73.946 -28.371 1.00 126.86 ? 193 PRO H CB  1 
ATOM   5262 C CG  . PRO C 2 193 ? 39.748  72.481 -28.444 1.00 128.06 ? 193 PRO H CG  1 
ATOM   5263 C CD  . PRO C 2 193 ? 38.266  72.324 -28.244 1.00 135.88 ? 193 PRO H CD  1 
ATOM   5264 N N   . SER C 2 194 ? 38.946  76.453 -30.470 1.00 133.35 ? 194 SER H N   1 
ATOM   5265 C CA  . SER C 2 194 ? 39.105  77.048 -31.795 1.00 130.56 ? 194 SER H CA  1 
ATOM   5266 C C   . SER C 2 194 ? 40.426  76.639 -32.427 1.00 120.67 ? 194 SER H C   1 
ATOM   5267 O O   . SER C 2 194 ? 40.565  76.666 -33.655 1.00 117.98 ? 194 SER H O   1 
ATOM   5268 C CB  . SER C 2 194 ? 39.012  78.574 -31.711 1.00 137.88 ? 194 SER H CB  1 
ATOM   5269 O OG  . SER C 2 194 ? 39.721  79.075 -30.590 1.00 146.86 ? 194 SER H OG  1 
ATOM   5270 N N   . SER C 2 195 ? 41.396  76.242 -31.605 1.00 124.74 ? 195 SER H N   1 
ATOM   5271 C CA  . SER C 2 195 ? 42.710  75.875 -32.118 1.00 127.76 ? 195 SER H CA  1 
ATOM   5272 C C   . SER C 2 195 ? 42.662  74.556 -32.884 1.00 121.73 ? 195 SER H C   1 
ATOM   5273 O O   . SER C 2 195 ? 43.215  74.448 -33.985 1.00 115.66 ? 195 SER H O   1 
ATOM   5274 C CB  . SER C 2 195 ? 43.704  75.803 -30.960 1.00 135.09 ? 195 SER H CB  1 
ATOM   5275 O OG  . SER C 2 195 ? 43.235  74.925 -29.953 1.00 136.60 ? 195 SER H OG  1 
ATOM   5276 N N   . SER C 2 196 ? 41.996  73.540 -32.322 1.00 125.94 ? 196 SER H N   1 
ATOM   5277 C CA  . SER C 2 196 ? 41.958  72.207 -32.934 1.00 119.79 ? 196 SER H CA  1 
ATOM   5278 C C   . SER C 2 196 ? 41.108  72.143 -34.200 1.00 120.03 ? 196 SER H C   1 
ATOM   5279 O O   . SER C 2 196 ? 40.889  71.029 -34.698 1.00 118.80 ? 196 SER H O   1 
ATOM   5280 C CB  . SER C 2 196 ? 41.450  71.175 -31.921 1.00 121.08 ? 196 SER H CB  1 
ATOM   5281 O OG  . SER C 2 196 ? 40.097  71.414 -31.567 1.00 128.54 ? 196 SER H OG  1 
ATOM   5282 N N   . LEU C 2 197 ? 40.634  73.273 -34.730 1.00 116.59 ? 197 LEU H N   1 
ATOM   5283 C CA  . LEU C 2 197 ? 39.814  73.241 -35.937 1.00 111.90 ? 197 LEU H CA  1 
ATOM   5284 C C   . LEU C 2 197 ? 40.649  72.916 -37.170 1.00 111.38 ? 197 LEU H C   1 
ATOM   5285 O O   . LEU C 2 197 ? 40.181  72.217 -38.076 1.00 115.15 ? 197 LEU H O   1 
ATOM   5286 C CB  . LEU C 2 197 ? 39.097  74.579 -36.118 1.00 104.91 ? 197 LEU H CB  1 
ATOM   5287 C CG  . LEU C 2 197 ? 37.829  74.827 -35.297 1.00 105.39 ? 197 LEU H CG  1 
ATOM   5288 C CD1 . LEU C 2 197 ? 37.170  76.133 -35.712 1.00 120.66 ? 197 LEU H CD1 1 
ATOM   5289 C CD2 . LEU C 2 197 ? 36.860  73.670 -35.455 1.00 109.92 ? 197 LEU H CD2 1 
ATOM   5290 N N   . GLY C 2 198 ? 41.882  73.411 -37.222 1.00 112.58 ? 198 GLY H N   1 
ATOM   5291 C CA  . GLY C 2 198 ? 42.703  73.272 -38.408 1.00 119.45 ? 198 GLY H CA  1 
ATOM   5292 C C   . GLY C 2 198 ? 43.306  71.897 -38.608 1.00 122.92 ? 198 GLY H C   1 
ATOM   5293 O O   . GLY C 2 198 ? 43.355  71.399 -39.737 1.00 128.03 ? 198 GLY H O   1 
ATOM   5294 N N   . THR C 2 199 ? 43.763  71.269 -37.526 1.00 118.91 ? 199 THR H N   1 
ATOM   5295 C CA  . THR C 2 199 ? 44.499  70.016 -37.649 1.00 123.45 ? 199 THR H CA  1 
ATOM   5296 C C   . THR C 2 199 ? 43.628  68.781 -37.475 1.00 122.92 ? 199 THR H C   1 
ATOM   5297 O O   . THR C 2 199 ? 43.935  67.734 -38.057 1.00 120.17 ? 199 THR H O   1 
ATOM   5298 C CB  . THR C 2 199 ? 45.640  69.972 -36.632 1.00 130.97 ? 199 THR H CB  1 
ATOM   5299 O OG1 . THR C 2 199 ? 45.103  69.964 -35.303 1.00 136.08 ? 199 THR H OG1 1 
ATOM   5300 C CG2 . THR C 2 199 ? 46.541  71.180 -36.803 1.00 141.07 ? 199 THR H CG2 1 
ATOM   5301 N N   . GLN C 2 200 ? 42.554  68.866 -36.698 1.00 118.27 ? 200 GLN H N   1 
ATOM   5302 C CA  . GLN C 2 200 ? 41.691  67.720 -36.456 1.00 117.15 ? 200 GLN H CA  1 
ATOM   5303 C C   . GLN C 2 200 ? 40.351  67.906 -37.155 1.00 118.06 ? 200 GLN H C   1 
ATOM   5304 O O   . GLN C 2 200 ? 39.782  69.002 -37.154 1.00 113.36 ? 200 GLN H O   1 
ATOM   5305 C CB  . GLN C 2 200 ? 41.476  67.495 -34.958 1.00 118.82 ? 200 GLN H CB  1 
ATOM   5306 C CG  . GLN C 2 200 ? 40.629  66.280 -34.655 1.00 113.01 ? 200 GLN H CG  1 
ATOM   5307 C CD  . GLN C 2 200 ? 40.588  65.942 -33.183 1.00 119.84 ? 200 GLN H CD  1 
ATOM   5308 O OE1 . GLN C 2 200 ? 41.146  66.658 -32.350 1.00 119.85 ? 200 GLN H OE1 1 
ATOM   5309 N NE2 . GLN C 2 200 ? 39.932  64.836 -32.853 1.00 128.13 ? 200 GLN H NE2 1 
ATOM   5310 N N   . THR C 2 201 ? 39.858  66.828 -37.755 1.00 117.24 ? 201 THR H N   1 
ATOM   5311 C CA  . THR C 2 201 ? 38.593  66.822 -38.470 1.00 118.26 ? 201 THR H CA  1 
ATOM   5312 C C   . THR C 2 201 ? 37.464  66.385 -37.540 1.00 120.84 ? 201 THR H C   1 
ATOM   5313 O O   . THR C 2 201 ? 37.690  65.881 -36.437 1.00 119.33 ? 201 THR H O   1 
ATOM   5314 C CB  . THR C 2 201 ? 38.678  65.901 -39.685 1.00 122.63 ? 201 THR H CB  1 
ATOM   5315 O OG1 . THR C 2 201 ? 38.532  64.537 -39.264 1.00 118.83 ? 201 THR H OG1 1 
ATOM   5316 C CG2 . THR C 2 201 ? 40.021  66.066 -40.368 1.00 125.83 ? 201 THR H CG2 1 
ATOM   5317 N N   . TYR C 2 202 ? 36.229  66.581 -38.003 1.00 117.38 ? 202 TYR H N   1 
ATOM   5318 C CA  . TYR C 2 202 ? 35.045  66.353 -37.182 1.00 111.39 ? 202 TYR H CA  1 
ATOM   5319 C C   . TYR C 2 202 ? 33.951  65.719 -38.028 1.00 107.79 ? 202 TYR H C   1 
ATOM   5320 O O   . TYR C 2 202 ? 33.636  66.214 -39.115 1.00 112.70 ? 202 TYR H O   1 
ATOM   5321 C CB  . TYR C 2 202 ? 34.569  67.669 -36.559 1.00 113.28 ? 202 TYR H CB  1 
ATOM   5322 C CG  . TYR C 2 202 ? 35.589  68.248 -35.605 1.00 114.06 ? 202 TYR H CG  1 
ATOM   5323 C CD1 . TYR C 2 202 ? 35.772  67.705 -34.339 1.00 113.93 ? 202 TYR H CD1 1 
ATOM   5324 C CD2 . TYR C 2 202 ? 36.408  69.305 -35.989 1.00 114.76 ? 202 TYR H CD2 1 
ATOM   5325 C CE1 . TYR C 2 202 ? 36.713  68.221 -33.470 1.00 109.80 ? 202 TYR H CE1 1 
ATOM   5326 C CE2 . TYR C 2 202 ? 37.352  69.825 -35.124 1.00 114.19 ? 202 TYR H CE2 1 
ATOM   5327 C CZ  . TYR C 2 202 ? 37.501  69.279 -33.868 1.00 109.11 ? 202 TYR H CZ  1 
ATOM   5328 O OH  . TYR C 2 202 ? 38.444  69.791 -33.010 1.00 106.35 ? 202 TYR H OH  1 
ATOM   5329 N N   . ILE C 2 203 ? 33.380  64.621 -37.523 1.00 102.67 ? 203 ILE H N   1 
ATOM   5330 C CA  . ILE C 2 203 ? 32.450  63.781 -38.268 1.00 102.84 ? 203 ILE H CA  1 
ATOM   5331 C C   . ILE C 2 203 ? 31.295  63.408 -37.343 1.00 99.98  ? 203 ILE H C   1 
ATOM   5332 O O   . ILE C 2 203 ? 31.434  63.379 -36.119 1.00 101.58 ? 203 ILE H O   1 
ATOM   5333 C CB  . ILE C 2 203 ? 33.153  62.511 -38.818 1.00 103.97 ? 203 ILE H CB  1 
ATOM   5334 C CG1 . ILE C 2 203 ? 34.316  62.891 -39.734 1.00 103.66 ? 203 ILE H CG1 1 
ATOM   5335 C CG2 . ILE C 2 203 ? 32.198  61.636 -39.616 1.00 105.26 ? 203 ILE H CG2 1 
ATOM   5336 C CD1 . ILE C 2 203 ? 35.032  61.703 -40.331 1.00 115.83 ? 203 ILE H CD1 1 
ATOM   5337 N N   . CYS C 2 204 ? 30.134  63.141 -37.944 1.00 100.32 ? 204 CYS H N   1 
ATOM   5338 C CA  . CYS C 2 204 ? 28.942  62.718 -37.218 1.00 97.91  ? 204 CYS H CA  1 
ATOM   5339 C C   . CYS C 2 204 ? 28.458  61.390 -37.773 1.00 104.79 ? 204 CYS H C   1 
ATOM   5340 O O   . CYS C 2 204 ? 28.309  61.245 -38.993 1.00 113.17 ? 204 CYS H O   1 
ATOM   5341 C CB  . CYS C 2 204 ? 27.817  63.748 -37.334 1.00 102.19 ? 204 CYS H CB  1 
ATOM   5342 S SG  . CYS C 2 204 ? 28.249  65.371 -36.741 1.00 141.05 ? 204 CYS H SG  1 
ATOM   5343 N N   . ASN C 2 205 ? 28.193  60.443 -36.873 1.00 101.71 ? 205 ASN H N   1 
ATOM   5344 C CA  . ASN C 2 205 ? 27.615  59.143 -37.182 1.00 104.93 ? 205 ASN H CA  1 
ATOM   5345 C C   . ASN C 2 205 ? 26.173  59.189 -36.693 1.00 102.38 ? 205 ASN H C   1 
ATOM   5346 O O   . ASN C 2 205 ? 25.930  59.268 -35.482 1.00 108.47 ? 205 ASN H O   1 
ATOM   5347 C CB  . ASN C 2 205 ? 28.396  58.021 -36.499 1.00 109.12 ? 205 ASN H CB  1 
ATOM   5348 C CG  . ASN C 2 205 ? 29.871  58.047 -36.842 1.00 119.43 ? 205 ASN H CG  1 
ATOM   5349 O OD1 . ASN C 2 205 ? 30.319  58.868 -37.638 1.00 117.60 ? 205 ASN H OD1 1 
ATOM   5350 N ND2 . ASN C 2 205 ? 30.634  57.140 -36.241 1.00 147.63 ? 205 ASN H ND2 1 
ATOM   5351 N N   . VAL C 2 206 ? 25.225  59.175 -37.627 1.00 93.18  ? 206 VAL H N   1 
ATOM   5352 C CA  . VAL C 2 206 ? 23.803  59.329 -37.331 1.00 86.33  ? 206 VAL H CA  1 
ATOM   5353 C C   . VAL C 2 206 ? 23.089  58.086 -37.842 1.00 86.86  ? 206 VAL H C   1 
ATOM   5354 O O   . VAL C 2 206 ? 23.111  57.810 -39.046 1.00 100.07 ? 206 VAL H O   1 
ATOM   5355 C CB  . VAL C 2 206 ? 23.223  60.601 -37.973 1.00 83.89  ? 206 VAL H CB  1 
ATOM   5356 C CG1 . VAL C 2 206 ? 21.766  60.793 -37.572 1.00 87.57  ? 206 VAL H CG1 1 
ATOM   5357 C CG2 . VAL C 2 206 ? 24.060  61.820 -37.604 1.00 87.18  ? 206 VAL H CG2 1 
ATOM   5358 N N   . ASN C 2 207 ? 22.446  57.335 -36.929 1.00 87.57  ? 207 ASN H N   1 
ATOM   5359 C CA  . ASN C 2 207 ? 21.966  55.971 -37.219 1.00 90.96  ? 207 ASN H CA  1 
ATOM   5360 C C   . ASN C 2 207 ? 20.473  55.833 -36.896 1.00 88.41  ? 207 ASN H C   1 
ATOM   5361 O O   . ASN C 2 207 ? 20.092  55.326 -35.837 1.00 86.80  ? 207 ASN H O   1 
ATOM   5362 C CB  . ASN C 2 207 ? 22.809  54.942 -36.455 1.00 109.60 ? 207 ASN H CB  1 
ATOM   5363 C CG  . ASN C 2 207 ? 24.222  54.828 -37.003 1.00 126.84 ? 207 ASN H CG  1 
ATOM   5364 O OD1 . ASN C 2 207 ? 24.621  55.587 -37.882 1.00 157.92 ? 207 ASN H OD1 1 
ATOM   5365 N ND2 . ASN C 2 207 ? 24.991  53.885 -36.470 1.00 161.22 ? 207 ASN H ND2 1 
ATOM   5366 N N   . HIS C 2 208 ? 19.629  56.264 -37.834 1.00 94.58  ? 208 HIS H N   1 
ATOM   5367 C CA  . HIS C 2 208 ? 18.190  56.051 -37.731 1.00 96.93  ? 208 HIS H CA  1 
ATOM   5368 C C   . HIS C 2 208 ? 17.878  54.568 -37.884 1.00 97.42  ? 208 HIS H C   1 
ATOM   5369 O O   . HIS C 2 208 ? 17.772  54.066 -39.008 1.00 99.69  ? 208 HIS H O   1 
ATOM   5370 C CB  . HIS C 2 208 ? 17.453  56.873 -38.793 1.00 96.45  ? 208 HIS H CB  1 
ATOM   5371 C CG  . HIS C 2 208 ? 15.969  56.970 -38.587 1.00 97.03  ? 208 HIS H CG  1 
ATOM   5372 N ND1 . HIS C 2 208 ? 15.143  55.867 -38.579 1.00 104.48 ? 208 HIS H ND1 1 
ATOM   5373 C CD2 . HIS C 2 208 ? 15.160  58.042 -38.413 1.00 95.32  ? 208 HIS H CD2 1 
ATOM   5374 C CE1 . HIS C 2 208 ? 13.894  56.252 -38.388 1.00 106.33 ? 208 HIS H CE1 1 
ATOM   5375 N NE2 . HIS C 2 208 ? 13.877  57.568 -38.281 1.00 102.19 ? 208 HIS H NE2 1 
ATOM   5376 N N   . LYS C 2 209 ? 17.729  53.860 -36.764 1.00 94.19  ? 209 LYS H N   1 
ATOM   5377 C CA  . LYS C 2 209 ? 17.556  52.411 -36.827 1.00 98.79  ? 209 LYS H CA  1 
ATOM   5378 C C   . LYS C 2 209 ? 16.341  51.957 -37.633 1.00 103.09 ? 209 LYS H C   1 
ATOM   5379 O O   . LYS C 2 209 ? 16.490  51.013 -38.429 1.00 109.41 ? 209 LYS H O   1 
ATOM   5380 C CB  . LYS C 2 209 ? 17.505  51.834 -35.407 1.00 107.85 ? 209 LYS H CB  1 
ATOM   5381 C CG  . LYS C 2 209 ? 18.832  51.863 -34.677 1.00 120.30 ? 209 LYS H CG  1 
ATOM   5382 C CD  . LYS C 2 209 ? 18.635  51.464 -33.230 1.00 120.13 ? 209 LYS H CD  1 
ATOM   5383 C CE  . LYS C 2 209 ? 19.918  51.578 -32.435 1.00 128.30 ? 209 LYS H CE  1 
ATOM   5384 N NZ  . LYS C 2 209 ? 19.686  51.203 -31.014 1.00 146.05 ? 209 LYS H NZ  1 
ATOM   5385 N N   . PRO C 2 210 ? 15.141  52.538 -37.485 1.00 106.16 ? 210 PRO H N   1 
ATOM   5386 C CA  . PRO C 2 210 ? 13.997  52.013 -38.256 1.00 105.95 ? 210 PRO H CA  1 
ATOM   5387 C C   . PRO C 2 210 ? 14.157  52.122 -39.766 1.00 107.28 ? 210 PRO H C   1 
ATOM   5388 O O   . PRO C 2 210 ? 13.739  51.209 -40.489 1.00 107.09 ? 210 PRO H O   1 
ATOM   5389 C CB  . PRO C 2 210 ? 12.817  52.849 -37.746 1.00 100.99 ? 210 PRO H CB  1 
ATOM   5390 C CG  . PRO C 2 210 ? 13.232  53.299 -36.393 1.00 111.99 ? 210 PRO H CG  1 
ATOM   5391 C CD  . PRO C 2 210 ? 14.707  53.528 -36.481 1.00 104.70 ? 210 PRO H CD  1 
ATOM   5392 N N   . SER C 2 211 ? 14.736  53.212 -40.271 1.00 104.67 ? 211 SER H N   1 
ATOM   5393 C CA  . SER C 2 211 ? 14.979  53.327 -41.705 1.00 100.00 ? 211 SER H CA  1 
ATOM   5394 C C   . SER C 2 211 ? 16.278  52.661 -42.139 1.00 106.67 ? 211 SER H C   1 
ATOM   5395 O O   . SER C 2 211 ? 16.525  52.551 -43.346 1.00 108.64 ? 211 SER H O   1 
ATOM   5396 C CB  . SER C 2 211 ? 15.000  54.799 -42.121 1.00 97.24  ? 211 SER H CB  1 
ATOM   5397 O OG  . SER C 2 211 ? 16.033  55.498 -41.449 1.00 98.92  ? 211 SER H OG  1 
ATOM   5398 N N   . ASN C 2 212 ? 17.098  52.212 -41.189 1.00 108.39 ? 212 ASN H N   1 
ATOM   5399 C CA  . ASN C 2 212 ? 18.405  51.618 -41.470 1.00 107.77 ? 212 ASN H CA  1 
ATOM   5400 C C   . ASN C 2 212 ? 19.268  52.572 -42.292 1.00 103.01 ? 212 ASN H C   1 
ATOM   5401 O O   . ASN C 2 212 ? 19.863  52.205 -43.308 1.00 112.51 ? 212 ASN H O   1 
ATOM   5402 C CB  . ASN C 2 212 ? 18.259  50.259 -42.159 1.00 115.28 ? 212 ASN H CB  1 
ATOM   5403 C CG  . ASN C 2 212 ? 17.874  49.156 -41.188 1.00 123.29 ? 212 ASN H CG  1 
ATOM   5404 O OD1 . ASN C 2 212 ? 18.734  48.468 -40.639 1.00 126.01 ? 212 ASN H OD1 1 
ATOM   5405 N ND2 . ASN C 2 212 ? 16.573  48.983 -40.974 1.00 150.07 ? 212 ASN H ND2 1 
ATOM   5406 N N   . THR C 2 213 ? 19.316  53.822 -41.838 1.00 102.58 ? 213 THR H N   1 
ATOM   5407 C CA  . THR C 2 213 ? 20.159  54.858 -42.415 1.00 96.98  ? 213 THR H CA  1 
ATOM   5408 C C   . THR C 2 213 ? 21.272  55.192 -41.432 1.00 96.60  ? 213 THR H C   1 
ATOM   5409 O O   . THR C 2 213 ? 21.039  55.273 -40.221 1.00 105.46 ? 213 THR H O   1 
ATOM   5410 C CB  . THR C 2 213 ? 19.352  56.118 -42.737 1.00 98.34  ? 213 THR H CB  1 
ATOM   5411 O OG1 . THR C 2 213 ? 18.063  55.746 -43.236 1.00 100.69 ? 213 THR H OG1 1 
ATOM   5412 C CG2 . THR C 2 213 ? 20.066  56.952 -43.786 1.00 98.88  ? 213 THR H CG2 1 
ATOM   5413 N N   . LYS C 2 214 ? 22.486  55.368 -41.951 1.00 88.98  ? 214 LYS H N   1 
ATOM   5414 C CA  . LYS C 2 214 ? 23.660  55.630 -41.124 1.00 93.11  ? 214 LYS H CA  1 
ATOM   5415 C C   . LYS C 2 214 ? 24.542  56.689 -41.792 1.00 88.22  ? 214 LYS H C   1 
ATOM   5416 O O   . LYS C 2 214 ? 25.718  56.479 -42.078 1.00 93.98  ? 214 LYS H O   1 
ATOM   5417 C CB  . LYS C 2 214 ? 24.431  54.338 -40.854 1.00 105.25 ? 214 LYS H CB  1 
ATOM   5418 C CG  . LYS C 2 214 ? 23.648  53.307 -40.047 1.00 104.67 ? 214 LYS H CG  1 
ATOM   5419 C CD  . LYS C 2 214 ? 24.555  52.254 -39.425 1.00 113.24 ? 214 LYS H CD  1 
ATOM   5420 C CE  . LYS C 2 214 ? 23.798  51.389 -38.429 1.00 131.13 ? 214 LYS H CE  1 
ATOM   5421 N NZ  . LYS C 2 214 ? 24.668  50.337 -37.832 1.00 130.74 ? 214 LYS H NZ  1 
ATOM   5422 N N   . VAL C 2 215 ? 23.962  57.867 -42.025 1.00 91.81  ? 215 VAL H N   1 
ATOM   5423 C CA  . VAL C 2 215 ? 24.674  58.947 -42.703 1.00 98.53  ? 215 VAL H CA  1 
ATOM   5424 C C   . VAL C 2 215 ? 25.748  59.512 -41.781 1.00 99.90  ? 215 VAL H C   1 
ATOM   5425 O O   . VAL C 2 215 ? 25.451  60.015 -40.691 1.00 98.86  ? 215 VAL H O   1 
ATOM   5426 C CB  . VAL C 2 215 ? 23.705  60.046 -43.157 1.00 102.69 ? 215 VAL H CB  1 
ATOM   5427 C CG1 . VAL C 2 215 ? 24.466  61.183 -43.819 1.00 125.20 ? 215 VAL H CG1 1 
ATOM   5428 C CG2 . VAL C 2 215 ? 22.668  59.477 -44.108 1.00 123.47 ? 215 VAL H CG2 1 
ATOM   5429 N N   . ASP C 2 216 ? 27.003  59.424 -42.215 1.00 107.16 ? 216 ASP H N   1 
ATOM   5430 C CA  . ASP C 2 216 ? 28.136  60.031 -41.528 1.00 108.11 ? 216 ASP H CA  1 
ATOM   5431 C C   . ASP C 2 216 ? 28.587  61.235 -42.341 1.00 112.52 ? 216 ASP H C   1 
ATOM   5432 O O   . ASP C 2 216 ? 28.919  61.100 -43.523 1.00 113.73 ? 216 ASP H O   1 
ATOM   5433 C CB  . ASP C 2 216 ? 29.285  59.036 -41.358 1.00 110.71 ? 216 ASP H CB  1 
ATOM   5434 C CG  . ASP C 2 216 ? 28.861  57.780 -40.630 1.00 110.83 ? 216 ASP H CG  1 
ATOM   5435 O OD1 . ASP C 2 216 ? 27.714  57.739 -40.140 1.00 125.43 ? 216 ASP H OD1 1 
ATOM   5436 O OD2 . ASP C 2 216 ? 29.677  56.838 -40.541 1.00 109.25 ? 216 ASP H OD2 1 
ATOM   5437 N N   . LYS C 2 217 ? 28.600  62.405 -41.717 1.00 105.06 ? 217 LYS H N   1 
ATOM   5438 C CA  . LYS C 2 217 ? 28.924  63.626 -42.448 1.00 102.01 ? 217 LYS H CA  1 
ATOM   5439 C C   . LYS C 2 217 ? 30.018  64.442 -41.773 1.00 98.32  ? 217 LYS H C   1 
ATOM   5440 O O   . LYS C 2 217 ? 30.108  64.490 -40.545 1.00 100.43 ? 217 LYS H O   1 
ATOM   5441 C CB  . LYS C 2 217 ? 27.679  64.499 -42.669 1.00 98.07  ? 217 LYS H CB  1 
ATOM   5442 C CG  . LYS C 2 217 ? 27.900  65.609 -43.685 1.00 112.46 ? 217 LYS H CG  1 
ATOM   5443 C CD  . LYS C 2 217 ? 26.593  66.102 -44.268 1.00 114.00 ? 217 LYS H CD  1 
ATOM   5444 C CE  . LYS C 2 217 ? 26.837  66.990 -45.474 1.00 128.57 ? 217 LYS H CE  1 
ATOM   5445 N NZ  . LYS C 2 217 ? 25.571  67.595 -45.976 1.00 152.76 ? 217 LYS H NZ  1 
ATOM   5446 N N   . ARG C 2 218 ? 30.859  65.069 -42.593 1.00 97.85  ? 218 ARG H N   1 
ATOM   5447 C CA  . ARG C 2 218 ? 31.959  65.899 -42.123 1.00 92.49  ? 218 ARG H CA  1 
ATOM   5448 C C   . ARG C 2 218 ? 31.531  67.346 -41.937 1.00 96.75  ? 218 ARG H C   1 
ATOM   5449 O O   . ARG C 2 218 ? 30.627  67.835 -42.618 1.00 102.85 ? 218 ARG H O   1 
ATOM   5450 C CB  . ARG C 2 218 ? 33.127  65.835 -43.110 1.00 120.60 ? 218 ARG H CB  1 
ATOM   5451 C CG  . ARG C 2 218 ? 33.786  64.469 -43.203 1.00 115.90 ? 218 ARG H CG  1 
ATOM   5452 C CD  . ARG C 2 218 ? 34.916  64.392 -44.218 1.00 114.18 ? 218 ARG H CD  1 
ATOM   5453 N NE  . ARG C 2 218 ? 35.531  63.068 -44.254 1.00 131.66 ? 218 ARG H NE  1 
ATOM   5454 C CZ  . ARG C 2 218 ? 35.052  62.043 -44.942 1.00 137.56 ? 218 ARG H CZ  1 
ATOM   5455 N NH1 . ARG C 2 218 ? 33.947  62.182 -45.663 1.00 137.45 ? 218 ARG H NH1 1 
ATOM   5456 N NH2 . ARG C 2 218 ? 35.678  60.873 -44.916 1.00 125.50 ? 218 ARG H NH2 1 
ATOM   5457 N N   . VAL C 2 219 ? 32.198  68.036 -41.018 1.00 108.41 ? 219 VAL H N   1 
ATOM   5458 C CA  . VAL C 2 219 ? 31.906  69.433 -40.711 1.00 113.18 ? 219 VAL H CA  1 
ATOM   5459 C C   . VAL C 2 219 ? 33.198  70.204 -40.949 1.00 121.92 ? 219 VAL H C   1 
ATOM   5460 O O   . VAL C 2 219 ? 34.053  70.295 -40.059 1.00 117.22 ? 219 VAL H O   1 
ATOM   5461 C CB  . VAL C 2 219 ? 31.367  69.670 -39.297 1.00 105.15 ? 219 VAL H CB  1 
ATOM   5462 C CG1 . VAL C 2 219 ? 31.038  71.143 -39.103 1.00 106.73 ? 219 VAL H CG1 1 
ATOM   5463 C CG2 . VAL C 2 219 ? 30.148  68.804 -39.044 1.00 107.44 ? 219 VAL H CG2 1 
ATOM   5464 N N   . GLU C 2 220 ? 33.341  70.774 -42.142 1.00 122.13 ? 220 GLU H N   1 
ATOM   5465 C CA  . GLU C 2 220 ? 34.555  71.474 -42.542 1.00 125.31 ? 220 GLU H CA  1 
ATOM   5466 C C   . GLU C 2 220 ? 34.224  72.946 -42.758 1.00 118.48 ? 220 GLU H C   1 
ATOM   5467 O O   . GLU C 2 220 ? 33.311  73.254 -43.544 1.00 119.56 ? 220 GLU H O   1 
ATOM   5468 C CB  . GLU C 2 220 ? 35.134  70.860 -43.820 1.00 128.96 ? 220 GLU H CB  1 
ATOM   5469 C CG  . GLU C 2 220 ? 35.610  69.415 -43.678 1.00 134.61 ? 220 GLU H CG  1 
ATOM   5470 C CD  . GLU C 2 220 ? 36.600  69.213 -42.546 1.00 154.37 ? 220 GLU H CD  1 
ATOM   5471 O OE1 . GLU C 2 220 ? 37.462  70.091 -42.340 1.00 142.04 ? 220 GLU H OE1 1 
ATOM   5472 O OE2 . GLU C 2 220 ? 36.517  68.166 -41.868 1.00 174.86 ? 220 GLU H OE2 1 
ATOM   5473 N N   . PRO C 2 221 ? 34.910  73.887 -42.081 1.00 116.66 ? 221 PRO H N   1 
ATOM   5474 C CA  . PRO C 2 221 ? 34.732  75.345 -42.150 1.00 113.07 ? 221 PRO H CA  1 
ATOM   5475 C C   . PRO C 2 221 ? 34.409  75.881 -43.544 1.00 101.13 ? 221 PRO H C   1 
ATOM   5476 O O   . PRO C 2 221 ? 33.809  76.952 -43.651 1.00 93.91  ? 221 PRO H O   1 
ATOM   5477 C CB  . PRO C 2 221 ? 36.090  75.863 -41.685 1.00 114.95 ? 221 PRO H CB  1 
ATOM   5478 C CG  . PRO C 2 221 ? 36.519  74.867 -40.663 1.00 113.15 ? 221 PRO H CG  1 
ATOM   5479 C CD  . PRO C 2 221 ? 35.889  73.527 -41.038 1.00 122.60 ? 221 PRO H CD  1 
ATOM   5480 N N   . ASP D 3 1   ? -2.909  46.715 -8.621  1.00 92.68  ? 1   ASP L N   1 
ATOM   5481 C CA  . ASP D 3 1   ? -3.726  46.579 -7.421  1.00 95.27  ? 1   ASP L CA  1 
ATOM   5482 C C   . ASP D 3 1   ? -3.317  47.547 -6.320  1.00 98.27  ? 1   ASP L C   1 
ATOM   5483 O O   . ASP D 3 1   ? -4.170  48.129 -5.651  1.00 97.95  ? 1   ASP L O   1 
ATOM   5484 C CB  . ASP D 3 1   ? -3.657  45.148 -6.880  1.00 102.85 ? 1   ASP L CB  1 
ATOM   5485 C CG  . ASP D 3 1   ? -4.258  44.136 -7.829  1.00 118.08 ? 1   ASP L CG  1 
ATOM   5486 O OD1 . ASP D 3 1   ? -4.901  44.556 -8.813  1.00 140.30 ? 1   ASP L OD1 1 
ATOM   5487 O OD2 . ASP D 3 1   ? -4.097  42.921 -7.587  1.00 127.09 ? 1   ASP L OD2 1 
ATOM   5488 N N   . ILE D 3 2   ? -2.012  47.715 -6.132  1.00 102.81 ? 2   ILE L N   1 
ATOM   5489 C CA  . ILE D 3 2   ? -1.468  48.436 -4.990  1.00 104.01 ? 2   ILE L CA  1 
ATOM   5490 C C   . ILE D 3 2   ? -0.818  49.640 -5.658  1.00 106.28 ? 2   ILE L C   1 
ATOM   5491 O O   . ILE D 3 2   ? 0.035   49.481 -6.539  1.00 108.69 ? 2   ILE L O   1 
ATOM   5492 C CB  . ILE D 3 2   ? -0.424  47.595 -4.244  1.00 96.34  ? 2   ILE L CB  1 
ATOM   5493 C CG1 . ILE D 3 2   ? -0.942  46.187 -3.991  1.00 102.89 ? 2   ILE L CG1 1 
ATOM   5494 C CG2 . ILE D 3 2   ? -0.176  48.177 -2.871  1.00 92.01  ? 2   ILE L CG2 1 
ATOM   5495 C CD1 . ILE D 3 2   ? 0.021   45.333 -3.194  1.00 93.59  ? 2   ILE L CD1 1 
ATOM   5496 N N   . GLN D 3 3   ? -1.215  50.838 -5.242  1.00 103.62 ? 3   GLN L N   1 
ATOM   5497 C CA  . GLN D 3 3   ? -0.644  52.050 -5.839  1.00 109.16 ? 3   GLN L CA  1 
ATOM   5498 C C   . GLN D 3 3   ? 0.560   52.508 -5.058  1.00 90.77  ? 3   GLN L C   1 
ATOM   5499 O O   . GLN D 3 3   ? 0.739   52.107 -3.908  1.00 82.70  ? 3   GLN L O   1 
ATOM   5500 C CB  . GLN D 3 3   ? -1.702  53.146 -5.893  1.00 117.15 ? 3   GLN L CB  1 
ATOM   5501 C CG  . GLN D 3 3   ? -2.824  52.818 -6.818  1.00 134.57 ? 3   GLN L CG  1 
ATOM   5502 C CD  . GLN D 3 3   ? -2.358  52.614 -8.226  1.00 154.66 ? 3   GLN L CD  1 
ATOM   5503 O OE1 . GLN D 3 3   ? -1.489  53.329 -8.729  1.00 183.28 ? 3   GLN L OE1 1 
ATOM   5504 N NE2 . GLN D 3 3   ? -2.958  51.645 -8.886  1.00 152.01 ? 3   GLN L NE2 1 
ATOM   5505 N N   . MET D 3 4   ? 1.402   53.335 -5.680  1.00 87.99  ? 4   MET L N   1 
ATOM   5506 C CA  . MET D 3 4   ? 2.609   53.842 -5.028  1.00 84.78  ? 4   MET L CA  1 
ATOM   5507 C C   . MET D 3 4   ? 2.636   55.344 -5.280  1.00 80.87  ? 4   MET L C   1 
ATOM   5508 O O   . MET D 3 4   ? 2.857   55.777 -6.412  1.00 87.11  ? 4   MET L O   1 
ATOM   5509 C CB  . MET D 3 4   ? 3.769   53.153 -5.740  1.00 82.48  ? 4   MET L CB  1 
ATOM   5510 C CG  . MET D 3 4   ? 3.954   51.729 -5.307  1.00 88.44  ? 4   MET L CG  1 
ATOM   5511 S SD  . MET D 3 4   ? 3.881   51.503 -3.522  1.00 90.84  ? 4   MET L SD  1 
ATOM   5512 C CE  . MET D 3 4   ? 5.331   52.347 -2.948  1.00 76.59  ? 4   MET L CE  1 
ATOM   5513 N N   . THR D 3 5   ? 2.417   56.130 -4.235  1.00 73.38  ? 5   THR L N   1 
ATOM   5514 C CA  . THR D 3 5   ? 2.363   57.595 -4.423  1.00 79.84  ? 5   THR L CA  1 
ATOM   5515 C C   . THR D 3 5   ? 3.653   58.204 -3.891  1.00 77.64  ? 5   THR L C   1 
ATOM   5516 O O   . THR D 3 5   ? 3.996   57.918 -2.738  1.00 86.70  ? 5   THR L O   1 
ATOM   5517 C CB  . THR D 3 5   ? 1.140   58.182 -3.716  1.00 96.60  ? 5   THR L CB  1 
ATOM   5518 O OG1 . THR D 3 5   ? 1.603   59.085 -2.712  1.00 157.54 ? 5   THR L OG1 1 
ATOM   5519 C CG2 . THR D 3 5   ? 0.260   57.124 -3.087  1.00 89.62  ? 5   THR L CG2 1 
ATOM   5520 N N   . GLN D 3 6   ? 4.323   59.012 -4.708  1.00 92.10  ? 6   GLN L N   1 
ATOM   5521 C CA  . GLN D 3 6   ? 5.618   59.598 -4.285  1.00 84.07  ? 6   GLN L CA  1 
ATOM   5522 C C   . GLN D 3 6   ? 5.435   61.085 -3.999  1.00 82.91  ? 6   GLN L C   1 
ATOM   5523 O O   . GLN D 3 6   ? 4.361   61.611 -4.314  1.00 89.08  ? 6   GLN L O   1 
ATOM   5524 C CB  . GLN D 3 6   ? 6.685   59.422 -5.364  1.00 80.34  ? 6   GLN L CB  1 
ATOM   5525 C CG  . GLN D 3 6   ? 7.161   57.991 -5.536  1.00 75.08  ? 6   GLN L CG  1 
ATOM   5526 C CD  . GLN D 3 6   ? 8.480   57.946 -6.264  1.00 71.09  ? 6   GLN L CD  1 
ATOM   5527 O OE1 . GLN D 3 6   ? 9.433   58.631 -5.902  1.00 72.22  ? 6   GLN L OE1 1 
ATOM   5528 N NE2 . GLN D 3 6   ? 8.542   57.137 -7.306  1.00 83.84  ? 6   GLN L NE2 1 
ATOM   5529 N N   . SER D 3 7   ? 6.461   61.720 -3.440  1.00 80.69  ? 7   SER L N   1 
ATOM   5530 C CA  . SER D 3 7   ? 6.414   63.172 -3.154  1.00 80.97  ? 7   SER L CA  1 
ATOM   5531 C C   . SER D 3 7   ? 7.845   63.644 -2.910  1.00 86.23  ? 7   SER L C   1 
ATOM   5532 O O   . SER D 3 7   ? 8.651   62.819 -2.470  1.00 89.49  ? 7   SER L O   1 
ATOM   5533 C CB  . SER D 3 7   ? 5.559   63.438 -1.963  1.00 86.41  ? 7   SER L CB  1 
ATOM   5534 O OG  . SER D 3 7   ? 6.356   63.770 -0.837  1.00 90.97  ? 7   SER L OG  1 
ATOM   5535 N N   . PRO D 3 8   ? 8.192   64.926 -3.125  1.00 88.52  ? 8   PRO L N   1 
ATOM   5536 C CA  . PRO D 3 8   ? 7.526   65.760 -4.112  1.00 85.48  ? 8   PRO L CA  1 
ATOM   5537 C C   . PRO D 3 8   ? 7.976   65.412 -5.531  1.00 85.85  ? 8   PRO L C   1 
ATOM   5538 O O   . PRO D 3 8   ? 9.151   65.240 -5.721  1.00 97.46  ? 8   PRO L O   1 
ATOM   5539 C CB  . PRO D 3 8   ? 8.059   67.160 -3.798  1.00 91.65  ? 8   PRO L CB  1 
ATOM   5540 C CG  . PRO D 3 8   ? 8.634   67.042 -2.409  1.00 96.39  ? 8   PRO L CG  1 
ATOM   5541 C CD  . PRO D 3 8   ? 9.218   65.650 -2.384  1.00 91.34  ? 8   PRO L CD  1 
ATOM   5542 N N   . ALA D 3 9   ? 7.043   65.358 -6.481  1.00 82.66  ? 9   ALA L N   1 
ATOM   5543 C CA  . ALA D 3 9   ? 7.393   64.953 -7.861  1.00 78.50  ? 9   ALA L CA  1 
ATOM   5544 C C   . ALA D 3 9   ? 8.238   66.038 -8.525  1.00 83.89  ? 9   ALA L C   1 
ATOM   5545 O O   . ALA D 3 9   ? 8.503   65.912 -9.729  1.00 86.47  ? 9   ALA L O   1 
ATOM   5546 C CB  . ALA D 3 9   ? 6.147   64.681 -8.652  1.00 70.36  ? 9   ALA L CB  1 
ATOM   5547 N N   . THR D 3 10  ? 8.645   67.054 -7.771  1.00 79.08  ? 10  THR L N   1 
ATOM   5548 C CA  . THR D 3 10  ? 9.537   68.104 -8.331  1.00 77.08  ? 10  THR L CA  1 
ATOM   5549 C C   . THR D 3 10  ? 10.380  68.715 -7.209  1.00 80.24  ? 10  THR L C   1 
ATOM   5550 O O   . THR D 3 10  ? 9.788   69.335 -6.304  1.00 82.77  ? 10  THR L O   1 
ATOM   5551 C CB  . THR D 3 10  ? 8.731   69.175 -9.075  1.00 92.01  ? 10  THR L CB  1 
ATOM   5552 O OG1 . THR D 3 10  ? 7.968   68.528 -10.094 1.00 95.89  ? 10  THR L OG1 1 
ATOM   5553 C CG2 . THR D 3 10  ? 9.604   70.246 -9.691  1.00 93.53  ? 10  THR L CG2 1 
ATOM   5554 N N   . LEU D 3 11  ? 11.704  68.541 -7.266  1.00 88.85  ? 11  LEU L N   1 
ATOM   5555 C CA  . LEU D 3 11  ? 12.585  69.122 -6.266  1.00 89.01  ? 11  LEU L CA  1 
ATOM   5556 C C   . LEU D 3 11  ? 13.663  69.945 -6.953  1.00 89.55  ? 11  LEU L C   1 
ATOM   5557 O O   . LEU D 3 11  ? 13.867  69.865 -8.168  1.00 91.89  ? 11  LEU L O   1 
ATOM   5558 C CB  . LEU D 3 11  ? 13.221  68.048 -5.378  1.00 87.78  ? 11  LEU L CB  1 
ATOM   5559 C CG  . LEU D 3 11  ? 12.258  67.374 -4.407  1.00 95.75  ? 11  LEU L CG  1 
ATOM   5560 C CD1 . LEU D 3 11  ? 12.962  66.272 -3.649  1.00 102.57 ? 11  LEU L CD1 1 
ATOM   5561 C CD2 . LEU D 3 11  ? 11.714  68.414 -3.452  1.00 102.39 ? 11  LEU L CD2 1 
ATOM   5562 N N   . SER D 3 12  ? 14.350  70.754 -6.150  1.00 79.63  ? 12  SER L N   1 
ATOM   5563 C CA  . SER D 3 12  ? 15.455  71.572 -6.629  1.00 85.26  ? 12  SER L CA  1 
ATOM   5564 C C   . SER D 3 12  ? 16.237  72.051 -5.415  1.00 94.18  ? 12  SER L C   1 
ATOM   5565 O O   . SER D 3 12  ? 15.669  72.669 -4.509  1.00 103.09 ? 12  SER L O   1 
ATOM   5566 C CB  . SER D 3 12  ? 14.948  72.757 -7.456  1.00 88.27  ? 12  SER L CB  1 
ATOM   5567 O OG  . SER D 3 12  ? 16.001  73.345 -8.198  1.00 94.68  ? 12  SER L OG  1 
ATOM   5568 N N   . ALA D 3 13  ? 17.529  71.743 -5.383  1.00 88.51  ? 13  ALA L N   1 
ATOM   5569 C CA  . ALA D 3 13  ? 18.365  72.104 -4.250  1.00 93.53  ? 13  ALA L CA  1 
ATOM   5570 C C   . ALA D 3 13  ? 19.793  72.286 -4.734  1.00 100.47 ? 13  ALA L C   1 
ATOM   5571 O O   . ALA D 3 13  ? 20.250  71.582 -5.639  1.00 104.01 ? 13  ALA L O   1 
ATOM   5572 C CB  . ALA D 3 13  ? 18.317  71.041 -3.147  1.00 98.16  ? 13  ALA L CB  1 
ATOM   5573 N N   . SER D 3 14  ? 20.494  73.238 -4.121  1.00 105.10 ? 14  SER L N   1 
ATOM   5574 C CA  . SER D 3 14  ? 21.891  73.465 -4.449  1.00 102.43 ? 14  SER L CA  1 
ATOM   5575 C C   . SER D 3 14  ? 22.753  72.306 -3.947  1.00 99.37  ? 14  SER L C   1 
ATOM   5576 O O   . SER D 3 14  ? 22.345  71.514 -3.091  1.00 98.29  ? 14  SER L O   1 
ATOM   5577 C CB  . SER D 3 14  ? 22.365  74.791 -3.856  1.00 102.03 ? 14  SER L CB  1 
ATOM   5578 O OG  . SER D 3 14  ? 21.943  74.926 -2.513  1.00 117.88 ? 14  SER L OG  1 
ATOM   5579 N N   . VAL D 3 15  ? 23.962  72.209 -4.508  1.00 95.83  ? 15  VAL L N   1 
ATOM   5580 C CA  . VAL D 3 15  ? 24.843  71.085 -4.209  1.00 93.56  ? 15  VAL L CA  1 
ATOM   5581 C C   . VAL D 3 15  ? 25.219  71.101 -2.735  1.00 98.66  ? 15  VAL L C   1 
ATOM   5582 O O   . VAL D 3 15  ? 25.598  72.142 -2.183  1.00 104.62 ? 15  VAL L O   1 
ATOM   5583 C CB  . VAL D 3 15  ? 26.089  71.132 -5.108  1.00 90.93  ? 15  VAL L CB  1 
ATOM   5584 C CG1 . VAL D 3 15  ? 27.196  70.260 -4.538  1.00 91.29  ? 15  VAL L CG1 1 
ATOM   5585 C CG2 . VAL D 3 15  ? 25.738  70.696 -6.523  1.00 96.02  ? 15  VAL L CG2 1 
ATOM   5586 N N   . GLY D 3 16  ? 25.111  69.940 -2.087  1.00 101.11 ? 16  GLY L N   1 
ATOM   5587 C CA  . GLY D 3 16  ? 25.429  69.791 -0.687  1.00 104.03 ? 16  GLY L CA  1 
ATOM   5588 C C   . GLY D 3 16  ? 24.226  69.678 0.226   1.00 100.21 ? 16  GLY L C   1 
ATOM   5589 O O   . GLY D 3 16  ? 24.372  69.206 1.360   1.00 96.64  ? 16  GLY L O   1 
ATOM   5590 N N   . ASP D 3 17  ? 23.049  70.096 -0.233  1.00 98.37  ? 17  ASP L N   1 
ATOM   5591 C CA  . ASP D 3 17  ? 21.849  69.988 0.584   1.00 97.73  ? 17  ASP L CA  1 
ATOM   5592 C C   . ASP D 3 17  ? 21.470  68.530 0.807   1.00 94.89  ? 17  ASP L C   1 
ATOM   5593 O O   . ASP D 3 17  ? 21.804  67.648 0.013   1.00 96.99  ? 17  ASP L O   1 
ATOM   5594 C CB  . ASP D 3 17  ? 20.676  70.712 -0.081  1.00 99.26  ? 17  ASP L CB  1 
ATOM   5595 C CG  . ASP D 3 17  ? 20.865  72.211 -0.130  1.00 108.37 ? 17  ASP L CG  1 
ATOM   5596 O OD1 . ASP D 3 17  ? 21.885  72.701 0.398   1.00 140.31 ? 17  ASP L OD1 1 
ATOM   5597 O OD2 . ASP D 3 17  ? 19.988  72.899 -0.699  1.00 112.11 ? 17  ASP L OD2 1 
ATOM   5598 N N   . ARG D 3 18  ? 20.758  68.287 1.902   1.00 87.70  ? 18  ARG L N   1 
ATOM   5599 C CA  . ARG D 3 18  ? 20.066  67.023 2.085   1.00 91.64  ? 18  ARG L CA  1 
ATOM   5600 C C   . ARG D 3 18  ? 18.786  67.020 1.263   1.00 91.43  ? 18  ARG L C   1 
ATOM   5601 O O   . ARG D 3 18  ? 18.088  68.035 1.172   1.00 93.10  ? 18  ARG L O   1 
ATOM   5602 C CB  . ARG D 3 18  ? 19.742  66.793 3.561   1.00 99.44  ? 18  ARG L CB  1 
ATOM   5603 C CG  . ARG D 3 18  ? 19.319  65.372 3.902   1.00 98.72  ? 18  ARG L CG  1 
ATOM   5604 C CD  . ARG D 3 18  ? 19.577  65.070 5.369   1.00 96.70  ? 18  ARG L CD  1 
ATOM   5605 N NE  . ARG D 3 18  ? 20.768  65.761 5.846   1.00 117.60 ? 18  ARG L NE  1 
ATOM   5606 C CZ  . ARG D 3 18  ? 21.911  65.159 6.142   1.00 137.98 ? 18  ARG L CZ  1 
ATOM   5607 N NH1 . ARG D 3 18  ? 22.045  63.847 6.046   1.00 138.68 ? 18  ARG L NH1 1 
ATOM   5608 N NH2 . ARG D 3 18  ? 22.947  65.891 6.539   1.00 165.38 ? 18  ARG L NH2 1 
ATOM   5609 N N   . VAL D 3 19  ? 18.484  65.879 0.649   1.00 96.62  ? 19  VAL L N   1 
ATOM   5610 C CA  . VAL D 3 19  ? 17.243  65.716 -0.099  1.00 93.58  ? 19  VAL L CA  1 
ATOM   5611 C C   . VAL D 3 19  ? 16.549  64.458 0.401   1.00 87.44  ? 19  VAL L C   1 
ATOM   5612 O O   . VAL D 3 19  ? 17.209  63.462 0.709   1.00 89.97  ? 19  VAL L O   1 
ATOM   5613 C CB  . VAL D 3 19  ? 17.499  65.649 -1.621  1.00 92.42  ? 19  VAL L CB  1 
ATOM   5614 C CG1 . VAL D 3 19  ? 16.205  65.383 -2.376  1.00 95.27  ? 19  VAL L CG1 1 
ATOM   5615 C CG2 . VAL D 3 19  ? 18.149  66.938 -2.112  1.00 97.55  ? 19  VAL L CG2 1 
ATOM   5616 N N   . SER D 3 20  ? 15.223  64.505 0.506   1.00 82.34  ? 20  SER L N   1 
ATOM   5617 C CA  . SER D 3 20  ? 14.466  63.340 0.939   1.00 77.56  ? 20  SER L CA  1 
ATOM   5618 C C   . SER D 3 20  ? 13.159  63.246 0.168   1.00 73.55  ? 20  SER L C   1 
ATOM   5619 O O   . SER D 3 20  ? 12.441  64.237 0.007   1.00 79.22  ? 20  SER L O   1 
ATOM   5620 C CB  . SER D 3 20  ? 14.197  63.373 2.450   1.00 87.65  ? 20  SER L CB  1 
ATOM   5621 O OG  . SER D 3 20  ? 13.982  64.692 2.911   1.00 146.74 ? 20  SER L OG  1 
ATOM   5622 N N   . ILE D 3 21  ? 12.861  62.032 -0.281  1.00 69.47  ? 21  ILE L N   1 
ATOM   5623 C CA  . ILE D 3 21  ? 11.742  61.725 -1.160  1.00 69.45  ? 21  ILE L CA  1 
ATOM   5624 C C   . ILE D 3 21  ? 10.901  60.656 -0.483  1.00 72.00  ? 21  ILE L C   1 
ATOM   5625 O O   . ILE D 3 21  ? 11.413  59.581 -0.146  1.00 79.27  ? 21  ILE L O   1 
ATOM   5626 C CB  . ILE D 3 21  ? 12.232  61.232 -2.533  1.00 72.54  ? 21  ILE L CB  1 
ATOM   5627 C CG1 . ILE D 3 21  ? 13.069  62.310 -3.226  1.00 74.06  ? 21  ILE L CG1 1 
ATOM   5628 C CG2 . ILE D 3 21  ? 11.061  60.790 -3.390  1.00 79.69  ? 21  ILE L CG2 1 
ATOM   5629 C CD1 . ILE D 3 21  ? 13.963  61.773 -4.327  1.00 68.82  ? 21  ILE L CD1 1 
ATOM   5630 N N   . THR D 3 22  ? 9.619   60.946 -0.288  1.00 66.35  ? 22  THR L N   1 
ATOM   5631 C CA  . THR D 3 22  ? 8.713   60.040 0.397   1.00 68.84  ? 22  THR L CA  1 
ATOM   5632 C C   . THR D 3 22  ? 7.907   59.228 -0.606  1.00 64.69  ? 22  THR L C   1 
ATOM   5633 O O   . THR D 3 22  ? 7.574   59.696 -1.700  1.00 72.56  ? 22  THR L O   1 
ATOM   5634 C CB  . THR D 3 22  ? 7.769   60.807 1.320   1.00 75.18  ? 22  THR L CB  1 
ATOM   5635 O OG1 . THR D 3 22  ? 6.771   61.474 0.537   1.00 132.16 ? 22  THR L OG1 1 
ATOM   5636 C CG2 . THR D 3 22  ? 8.547   61.831 2.122   1.00 72.90  ? 22  THR L CG2 1 
ATOM   5637 N N   . CYS D 3 23  ? 7.601   57.998 -0.206  1.00 62.70  ? 23  CYS L N   1 
ATOM   5638 C CA  . CYS D 3 23  ? 6.891   57.040 -1.040  1.00 68.72  ? 23  CYS L CA  1 
ATOM   5639 C C   . CYS D 3 23  ? 5.929   56.283 -0.137  1.00 71.84  ? 23  CYS L C   1 
ATOM   5640 O O   . CYS D 3 23  ? 6.362   55.603 0.800   1.00 80.96  ? 23  CYS L O   1 
ATOM   5641 C CB  . CYS D 3 23  ? 7.875   56.086 -1.734  1.00 76.35  ? 23  CYS L CB  1 
ATOM   5642 S SG  . CYS D 3 23  ? 7.169   55.059 -3.037  1.00 82.50  ? 23  CYS L SG  1 
ATOM   5643 N N   . ARG D 3 24  ? 4.632   56.429 -0.397  1.00 70.62  ? 24  ARG L N   1 
ATOM   5644 C CA  . ARG D 3 24  ? 3.576   55.801 0.383   1.00 69.75  ? 24  ARG L CA  1 
ATOM   5645 C C   . ARG D 3 24  ? 2.856   54.754 -0.457  1.00 65.90  ? 24  ARG L C   1 
ATOM   5646 O O   . ARG D 3 24  ? 2.899   54.771 -1.692  1.00 78.53  ? 24  ARG L O   1 
ATOM   5647 C CB  . ARG D 3 24  ? 2.586   56.852 0.903   1.00 88.21  ? 24  ARG L CB  1 
ATOM   5648 C CG  . ARG D 3 24  ? 3.232   57.906 1.782   1.00 100.61 ? 24  ARG L CG  1 
ATOM   5649 C CD  . ARG D 3 24  ? 2.216   58.881 2.351   1.00 113.21 ? 24  ARG L CD  1 
ATOM   5650 N NE  . ARG D 3 24  ? 2.846   59.834 3.257   1.00 125.97 ? 24  ARG L NE  1 
ATOM   5651 C CZ  . ARG D 3 24  ? 2.343   61.021 3.564   1.00 131.68 ? 24  ARG L CZ  1 
ATOM   5652 N NH1 . ARG D 3 24  ? 1.196   61.439 3.055   1.00 138.78 ? 24  ARG L NH1 1 
ATOM   5653 N NH2 . ARG D 3 24  ? 3.010   61.813 4.399   1.00 131.54 ? 24  ARG L NH2 1 
ATOM   5654 N N   . ALA D 3 25  ? 2.161   53.854 0.241   1.00 71.45  ? 25  ALA L N   1 
ATOM   5655 C CA  . ALA D 3 25  ? 1.625   52.641 -0.355  1.00 81.71  ? 25  ALA L CA  1 
ATOM   5656 C C   . ALA D 3 25  ? 0.170   52.437 0.033   1.00 80.97  ? 25  ALA L C   1 
ATOM   5657 O O   . ALA D 3 25  ? -0.215  52.682 1.179   1.00 88.75  ? 25  ALA L O   1 
ATOM   5658 C CB  . ALA D 3 25  ? 2.435   51.422 0.083   1.00 84.45  ? 25  ALA L CB  1 
ATOM   5659 N N   . SER D 3 26  ? -0.621  51.959 -0.931  1.00 81.62  ? 26  SER L N   1 
ATOM   5660 C CA  . SER D 3 26  ? -2.013  51.604 -0.672  1.00 90.10  ? 26  SER L CA  1 
ATOM   5661 C C   . SER D 3 26  ? -2.150  50.580 0.447   1.00 91.94  ? 26  SER L C   1 
ATOM   5662 O O   . SER D 3 26  ? -3.107  50.639 1.229   1.00 95.53  ? 26  SER L O   1 
ATOM   5663 C CB  . SER D 3 26  ? -2.651  51.068 -1.951  1.00 101.42 ? 26  SER L CB  1 
ATOM   5664 O OG  . SER D 3 26  ? -3.877  50.414 -1.677  1.00 96.63  ? 26  SER L OG  1 
ATOM   5665 N N   . GLN D 3 27  ? -1.217  49.640 0.540   1.00 91.24  ? 27  GLN L N   1 
ATOM   5666 C CA  . GLN D 3 27  ? -1.257  48.563 1.519   1.00 93.84  ? 27  GLN L CA  1 
ATOM   5667 C C   . GLN D 3 27  ? 0.102   48.480 2.206   1.00 93.84  ? 27  GLN L C   1 
ATOM   5668 O O   . GLN D 3 27  ? 1.035   49.213 1.867   1.00 89.38  ? 27  GLN L O   1 
ATOM   5669 C CB  . GLN D 3 27  ? -1.623  47.232 0.849   1.00 90.36  ? 27  GLN L CB  1 
ATOM   5670 C CG  . GLN D 3 27  ? -2.985  47.258 0.194   1.00 94.30  ? 27  GLN L CG  1 
ATOM   5671 C CD  . GLN D 3 27  ? -3.224  46.080 -0.718  1.00 99.68  ? 27  GLN L CD  1 
ATOM   5672 O OE1 . GLN D 3 27  ? -2.405  45.165 -0.803  1.00 98.44  ? 27  GLN L OE1 1 
ATOM   5673 N NE2 . GLN D 3 27  ? -4.345  46.107 -1.429  1.00 121.97 ? 27  GLN L NE2 1 
ATOM   5674 N N   . SER D 3 28  ? 0.224   47.588 3.185   1.00 98.66  ? 28  SER L N   1 
ATOM   5675 C CA  . SER D 3 28  ? 1.511   47.377 3.837   1.00 94.22  ? 28  SER L CA  1 
ATOM   5676 C C   . SER D 3 28  ? 2.406   46.523 2.946   1.00 91.37  ? 28  SER L C   1 
ATOM   5677 O O   . SER D 3 28  ? 1.973   45.512 2.390   1.00 90.73  ? 28  SER L O   1 
ATOM   5678 C CB  . SER D 3 28  ? 1.329   46.711 5.201   1.00 104.72 ? 28  SER L CB  1 
ATOM   5679 O OG  . SER D 3 28  ? 1.110   45.318 5.065   1.00 126.68 ? 28  SER L OG  1 
ATOM   5680 N N   . ILE D 3 29  ? 3.663   46.963 2.809   1.00 87.37  ? 29  ILE L N   1 
ATOM   5681 C CA  . ILE D 3 29  ? 4.655   46.247 1.955   1.00 84.97  ? 29  ILE L CA  1 
ATOM   5682 C C   . ILE D 3 29  ? 5.760   45.722 2.874   1.00 89.46  ? 29  ILE L C   1 
ATOM   5683 O O   . ILE D 3 29  ? 6.758   45.187 2.357   1.00 93.98  ? 29  ILE L O   1 
ATOM   5684 C CB  . ILE D 3 29  ? 5.217   47.226 0.904   1.00 79.17  ? 29  ILE L CB  1 
ATOM   5685 C CG1 . ILE D 3 29  ? 4.111   48.067 0.263   1.00 85.71  ? 29  ILE L CG1 1 
ATOM   5686 C CG2 . ILE D 3 29  ? 6.054   46.520 -0.152  1.00 88.72  ? 29  ILE L CG2 1 
ATOM   5687 C CD1 . ILE D 3 29  ? 4.621   49.022 -0.784  1.00 92.32  ? 29  ILE L CD1 1 
ATOM   5688 N N   . SER D 3 30  ? 5.594   45.883 4.191   1.00 90.23  ? 30  SER L N   1 
ATOM   5689 C CA  . SER D 3 30  ? 6.666   45.477 5.137   1.00 86.72  ? 30  SER L CA  1 
ATOM   5690 C C   . SER D 3 30  ? 7.900   46.168 4.549   1.00 83.25  ? 30  SER L C   1 
ATOM   5691 O O   . SER D 3 30  ? 7.831   47.388 4.311   1.00 89.18  ? 30  SER L O   1 
ATOM   5692 C CB  . SER D 3 30  ? 6.813   43.978 5.193   1.00 85.69  ? 30  SER L CB  1 
ATOM   5693 O OG  . SER D 3 30  ? 7.892   43.607 6.038   1.00 89.62  ? 30  SER L OG  1 
ATOM   5694 N N   . SER D 3 31  ? 8.978   45.415 4.316   1.00 73.33  ? 31  SER L N   1 
ATOM   5695 C CA  . SER D 3 31  ? 10.189  45.993 3.677   1.00 75.06  ? 31  SER L CA  1 
ATOM   5696 C C   . SER D 3 31  ? 10.494  45.437 2.282   1.00 75.31  ? 31  SER L C   1 
ATOM   5697 O O   . SER D 3 31  ? 11.589  44.871 2.100   1.00 84.93  ? 31  SER L O   1 
ATOM   5698 C CB  . SER D 3 31  ? 11.326  45.740 4.632   1.00 78.98  ? 31  SER L CB  1 
ATOM   5699 O OG  . SER D 3 31  ? 11.069  46.341 5.893   1.00 74.76  ? 31  SER L OG  1 
ATOM   5700 N N   . TRP D 3 32  ? 9.536   45.560 1.368   1.00 70.00  ? 32  TRP L N   1 
ATOM   5701 C CA  . TRP D 3 32  ? 9.712   45.015 0.003   1.00 71.07  ? 32  TRP L CA  1 
ATOM   5702 C C   . TRP D 3 32  ? 9.695   46.170 -0.994  1.00 73.61  ? 32  TRP L C   1 
ATOM   5703 O O   . TRP D 3 32  ? 9.114   46.006 -2.077  1.00 79.46  ? 32  TRP L O   1 
ATOM   5704 C CB  . TRP D 3 32  ? 8.619   43.988 -0.296  1.00 71.24  ? 32  TRP L CB  1 
ATOM   5705 C CG  . TRP D 3 32  ? 8.590   42.842 0.665   1.00 71.86  ? 32  TRP L CG  1 
ATOM   5706 C CD1 . TRP D 3 32  ? 7.532   42.426 1.418   1.00 81.22  ? 32  TRP L CD1 1 
ATOM   5707 C CD2 . TRP D 3 32  ? 9.683   41.968 0.992   1.00 72.49  ? 32  TRP L CD2 1 
ATOM   5708 N NE1 . TRP D 3 32  ? 7.889   41.350 2.185   1.00 83.57  ? 32  TRP L NE1 1 
ATOM   5709 C CE2 . TRP D 3 32  ? 9.202   41.049 1.946   1.00 78.10  ? 32  TRP L CE2 1 
ATOM   5710 C CE3 . TRP D 3 32  ? 11.013  41.872 0.575   1.00 72.17  ? 32  TRP L CE3 1 
ATOM   5711 C CZ2 . TRP D 3 32  ? 10.008  40.050 2.484   1.00 86.53  ? 32  TRP L CZ2 1 
ATOM   5712 C CZ3 . TRP D 3 32  ? 11.809  40.884 1.106   1.00 71.20  ? 32  TRP L CZ3 1 
ATOM   5713 C CH2 . TRP D 3 32  ? 11.310  39.986 2.048   1.00 82.76  ? 32  TRP L CH2 1 
ATOM   5714 N N   . LEU D 3 33  ? 10.313  47.291 -0.629  1.00 73.40  ? 33  LEU L N   1 
ATOM   5715 C CA  . LEU D 3 33  ? 10.380  48.449 -1.554  1.00 74.64  ? 33  LEU L CA  1 
ATOM   5716 C C   . LEU D 3 33  ? 11.780  48.535 -2.146  1.00 72.04  ? 33  LEU L C   1 
ATOM   5717 O O   . LEU D 3 33  ? 12.724  48.069 -1.495  1.00 76.79  ? 33  LEU L O   1 
ATOM   5718 C CB  . LEU D 3 33  ? 10.064  49.745 -0.808  1.00 74.41  ? 33  LEU L CB  1 
ATOM   5719 C CG  . LEU D 3 33  ? 8.584   50.097 -0.705  1.00 83.67  ? 33  LEU L CG  1 
ATOM   5720 C CD1 . LEU D 3 33  ? 8.389   51.596 -0.821  1.00 84.33  ? 33  LEU L CD1 1 
ATOM   5721 C CD2 . LEU D 3 33  ? 7.790   49.379 -1.779  1.00 85.53  ? 33  LEU L CD2 1 
ATOM   5722 N N   . ALA D 3 34  ? 11.887  49.124 -3.331  1.00 65.94  ? 34  ALA L N   1 
ATOM   5723 C CA  . ALA D 3 34  ? 13.198  49.295 -3.975  1.00 58.52  ? 34  ALA L CA  1 
ATOM   5724 C C   . ALA D 3 34  ? 13.203  50.662 -4.646  1.00 60.44  ? 34  ALA L C   1 
ATOM   5725 O O   . ALA D 3 34  ? 12.133  51.094 -5.098  1.00 62.61  ? 34  ALA L O   1 
ATOM   5726 C CB  . ALA D 3 34  ? 13.412  48.200 -4.973  1.00 60.76  ? 34  ALA L CB  1 
ATOM   5727 N N   . TRP D 3 35  ? 14.360  51.313 -4.679  1.00 59.91  ? 35  TRP L N   1 
ATOM   5728 C CA  . TRP D 3 35  ? 14.436  52.670 -5.268  1.00 54.72  ? 35  TRP L CA  1 
ATOM   5729 C C   . TRP D 3 35  ? 15.322  52.627 -6.508  1.00 75.25  ? 35  TRP L C   1 
ATOM   5730 O O   . TRP D 3 35  ? 16.319  51.896 -6.482  1.00 63.16  ? 35  TRP L O   1 
ATOM   5731 C CB  . TRP D 3 35  ? 14.955  53.684 -4.249  1.00 60.61  ? 35  TRP L CB  1 
ATOM   5732 C CG  . TRP D 3 35  ? 14.024  53.967 -3.112  1.00 67.42  ? 35  TRP L CG  1 
ATOM   5733 C CD1 . TRP D 3 35  ? 13.830  53.211 -1.993  1.00 73.96  ? 35  TRP L CD1 1 
ATOM   5734 C CD2 . TRP D 3 35  ? 13.140  55.093 -2.991  1.00 72.06  ? 35  TRP L CD2 1 
ATOM   5735 N NE1 . TRP D 3 35  ? 12.897  53.795 -1.181  1.00 76.18  ? 35  TRP L NE1 1 
ATOM   5736 C CE2 . TRP D 3 35  ? 12.454  54.949 -1.768  1.00 77.60  ? 35  TRP L CE2 1 
ATOM   5737 C CE3 . TRP D 3 35  ? 12.864  56.205 -3.793  1.00 74.28  ? 35  TRP L CE3 1 
ATOM   5738 C CZ2 . TRP D 3 35  ? 11.511  55.878 -1.333  1.00 77.70  ? 35  TRP L CZ2 1 
ATOM   5739 C CZ3 . TRP D 3 35  ? 11.933  57.122 -3.362  1.00 69.97  ? 35  TRP L CZ3 1 
ATOM   5740 C CH2 . TRP D 3 35  ? 11.268  56.958 -2.148  1.00 74.38  ? 35  TRP L CH2 1 
ATOM   5741 N N   . TYR D 3 36  ? 14.962  53.379 -7.542  1.00 44.97  ? 36  TYR L N   1 
ATOM   5742 C CA  . TYR D 3 36  ? 15.733  53.430 -8.775  1.00 47.75  ? 36  TYR L CA  1 
ATOM   5743 C C   . TYR D 3 36  ? 16.057  54.867 -9.145  1.00 60.91  ? 36  TYR L C   1 
ATOM   5744 O O   . TYR D 3 36  ? 15.296  55.793 -8.849  1.00 58.21  ? 36  TYR L O   1 
ATOM   5745 C CB  . TYR D 3 36  ? 15.008  52.783 -9.960  1.00 58.39  ? 36  TYR L CB  1 
ATOM   5746 C CG  . TYR D 3 36  ? 14.663  51.332 -9.768  1.00 53.97  ? 36  TYR L CG  1 
ATOM   5747 C CD1 . TYR D 3 36  ? 13.502  50.969 -9.109  1.00 61.87  ? 36  TYR L CD1 1 
ATOM   5748 C CD2 . TYR D 3 36  ? 15.489  50.325 -10.254 1.00 62.50  ? 36  TYR L CD2 1 
ATOM   5749 C CE1 . TYR D 3 36  ? 13.170  49.657 -8.935  1.00 66.86  ? 36  TYR L CE1 1 
ATOM   5750 C CE2 . TYR D 3 36  ? 15.161  48.993 -10.082 1.00 60.89  ? 36  TYR L CE2 1 
ATOM   5751 C CZ  . TYR D 3 36  ? 13.996  48.668 -9.420  1.00 64.96  ? 36  TYR L CZ  1 
ATOM   5752 O OH  . TYR D 3 36  ? 13.640  47.356 -9.224  1.00 73.12  ? 36  TYR L OH  1 
ATOM   5753 N N   . GLN D 3 37  ? 17.197  55.028 -9.812  1.00 56.77  ? 37  GLN L N   1 
ATOM   5754 C CA  . GLN D 3 37  ? 17.631  56.296 -10.385 1.00 62.08  ? 37  GLN L CA  1 
ATOM   5755 C C   . GLN D 3 37  ? 17.650  56.144 -11.898 1.00 71.11  ? 37  GLN L C   1 
ATOM   5756 O O   . GLN D 3 37  ? 18.497  55.430 -12.445 1.00 81.95  ? 37  GLN L O   1 
ATOM   5757 C CB  . GLN D 3 37  ? 19.011  56.693 -9.873  1.00 62.60  ? 37  GLN L CB  1 
ATOM   5758 C CG  . GLN D 3 37  ? 19.565  57.914 -10.588 1.00 64.08  ? 37  GLN L CG  1 
ATOM   5759 C CD  . GLN D 3 37  ? 21.001  58.214 -10.220 1.00 74.81  ? 37  GLN L CD  1 
ATOM   5760 O OE1 . GLN D 3 37  ? 21.933  57.618 -10.758 1.00 82.30  ? 37  GLN L OE1 1 
ATOM   5761 N NE2 . GLN D 3 37  ? 21.188  59.153 -9.298  1.00 71.93  ? 37  GLN L NE2 1 
ATOM   5762 N N   . GLN D 3 38  ? 16.722  56.810 -12.574 1.00 70.70  ? 38  GLN L N   1 
ATOM   5763 C CA  . GLN D 3 38  ? 16.693  56.855 -14.028 1.00 77.61  ? 38  GLN L CA  1 
ATOM   5764 C C   . GLN D 3 38  ? 17.270  58.205 -14.448 1.00 79.85  ? 38  GLN L C   1 
ATOM   5765 O O   . GLN D 3 38  ? 16.696  59.262 -14.147 1.00 83.41  ? 38  GLN L O   1 
ATOM   5766 C CB  . GLN D 3 38  ? 15.272  56.646 -14.549 1.00 73.84  ? 38  GLN L CB  1 
ATOM   5767 C CG  . GLN D 3 38  ? 15.186  56.324 -16.028 1.00 73.24  ? 38  GLN L CG  1 
ATOM   5768 C CD  . GLN D 3 38  ? 13.870  56.750 -16.651 1.00 77.89  ? 38  GLN L CD  1 
ATOM   5769 O OE1 . GLN D 3 38  ? 12.942  57.158 -15.955 1.00 76.35  ? 38  GLN L OE1 1 
ATOM   5770 N NE2 . GLN D 3 38  ? 13.779  56.642 -17.971 1.00 88.75  ? 38  GLN L NE2 1 
ATOM   5771 N N   . LYS D 3 39  ? 18.428  58.164 -15.093 1.00 84.92  ? 39  LYS L N   1 
ATOM   5772 C CA  . LYS D 3 39  ? 19.093  59.349 -15.620 1.00 91.16  ? 39  LYS L CA  1 
ATOM   5773 C C   . LYS D 3 39  ? 18.437  59.678 -16.960 1.00 96.66  ? 39  LYS L C   1 
ATOM   5774 O O   . LYS D 3 39  ? 17.588  58.928 -17.450 1.00 99.45  ? 39  LYS L O   1 
ATOM   5775 C CB  . LYS D 3 39  ? 20.596  59.079 -15.704 1.00 101.40 ? 39  LYS L CB  1 
ATOM   5776 C CG  . LYS D 3 39  ? 21.258  58.895 -14.340 1.00 105.53 ? 39  LYS L CG  1 
ATOM   5777 C CD  . LYS D 3 39  ? 21.714  60.215 -13.712 1.00 98.81  ? 39  LYS L CD  1 
ATOM   5778 C CE  . LYS D 3 39  ? 22.720  60.955 -14.585 1.00 104.11 ? 39  LYS L CE  1 
ATOM   5779 N NZ  . LYS D 3 39  ? 23.131  62.253 -13.975 1.00 97.07  ? 39  LYS L NZ  1 
ATOM   5780 N N   . PRO D 3 40  ? 18.769  60.815 -17.579 1.00 98.58  ? 40  PRO L N   1 
ATOM   5781 C CA  . PRO D 3 40  ? 18.126  61.142 -18.864 1.00 96.12  ? 40  PRO L CA  1 
ATOM   5782 C C   . PRO D 3 40  ? 18.449  60.113 -19.937 1.00 96.24  ? 40  PRO L C   1 
ATOM   5783 O O   . PRO D 3 40  ? 19.616  59.849 -20.243 1.00 101.23 ? 40  PRO L O   1 
ATOM   5784 C CB  . PRO D 3 40  ? 18.693  62.526 -19.206 1.00 106.67 ? 40  PRO L CB  1 
ATOM   5785 C CG  . PRO D 3 40  ? 19.228  63.060 -17.928 1.00 101.60 ? 40  PRO L CG  1 
ATOM   5786 C CD  . PRO D 3 40  ? 19.713  61.874 -17.172 1.00 105.21 ? 40  PRO L CD  1 
ATOM   5787 N N   . GLY D 3 41  ? 17.395  59.528 -20.503 1.00 93.51  ? 41  GLY L N   1 
ATOM   5788 C CA  . GLY D 3 41  ? 17.522  58.581 -21.593 1.00 102.69 ? 41  GLY L CA  1 
ATOM   5789 C C   . GLY D 3 41  ? 18.369  57.374 -21.256 1.00 100.09 ? 41  GLY L C   1 
ATOM   5790 O O   . GLY D 3 41  ? 19.231  56.970 -22.044 1.00 103.40 ? 41  GLY L O   1 
ATOM   5791 N N   . LYS D 3 42  ? 18.139  56.797 -20.079 1.00 93.51  ? 42  LYS L N   1 
ATOM   5792 C CA  . LYS D 3 42  ? 18.890  55.632 -19.642 1.00 96.72  ? 42  LYS L CA  1 
ATOM   5793 C C   . LYS D 3 42  ? 17.955  54.708 -18.879 1.00 92.52  ? 42  LYS L C   1 
ATOM   5794 O O   . LYS D 3 42  ? 16.892  55.118 -18.408 1.00 93.59  ? 42  LYS L O   1 
ATOM   5795 C CB  . LYS D 3 42  ? 20.091  56.026 -18.771 1.00 98.64  ? 42  LYS L CB  1 
ATOM   5796 C CG  . LYS D 3 42  ? 21.217  56.706 -19.536 1.00 109.89 ? 42  LYS L CG  1 
ATOM   5797 C CD  . LYS D 3 42  ? 22.371  57.088 -18.626 1.00 138.08 ? 42  LYS L CD  1 
ATOM   5798 C CE  . LYS D 3 42  ? 23.276  58.106 -19.300 1.00 153.86 ? 42  LYS L CE  1 
ATOM   5799 N NZ  . LYS D 3 42  ? 24.247  58.724 -18.358 1.00 169.08 ? 42  LYS L NZ  1 
ATOM   5800 N N   . ALA D 3 43  ? 18.360  53.447 -18.770 1.00 95.73  ? 43  ALA L N   1 
ATOM   5801 C CA  . ALA D 3 43  ? 17.614  52.501 -17.965 1.00 82.91  ? 43  ALA L CA  1 
ATOM   5802 C C   . ALA D 3 43  ? 17.725  52.882 -16.490 1.00 77.25  ? 43  ALA L C   1 
ATOM   5803 O O   . ALA D 3 43  ? 18.676  53.553 -16.084 1.00 85.33  ? 43  ALA L O   1 
ATOM   5804 C CB  . ALA D 3 43  ? 18.140  51.087 -18.193 1.00 85.98  ? 43  ALA L CB  1 
ATOM   5805 N N   . PRO D 3 44  ? 16.758  52.484 -15.666 1.00 68.63  ? 44  PRO L N   1 
ATOM   5806 C CA  . PRO D 3 44  ? 16.876  52.753 -14.229 1.00 73.85  ? 44  PRO L CA  1 
ATOM   5807 C C   . PRO D 3 44  ? 18.027  51.981 -13.610 1.00 79.92  ? 44  PRO L C   1 
ATOM   5808 O O   . PRO D 3 44  ? 18.346  50.858 -14.009 1.00 87.71  ? 44  PRO L O   1 
ATOM   5809 C CB  . PRO D 3 44  ? 15.528  52.283 -13.663 1.00 71.93  ? 44  PRO L CB  1 
ATOM   5810 C CG  . PRO D 3 44  ? 14.627  52.202 -14.853 1.00 71.48  ? 44  PRO L CG  1 
ATOM   5811 C CD  . PRO D 3 44  ? 15.519  51.749 -15.961 1.00 76.77  ? 44  PRO L CD  1 
ATOM   5812 N N   . LYS D 3 45  ? 18.655  52.605 -12.622 1.00 78.35  ? 45  LYS L N   1 
ATOM   5813 C CA  . LYS D 3 45  ? 19.735  51.990 -11.867 1.00 78.06  ? 45  LYS L CA  1 
ATOM   5814 C C   . LYS D 3 45  ? 19.271  51.794 -10.434 1.00 65.92  ? 45  LYS L C   1 
ATOM   5815 O O   . LYS D 3 45  ? 18.851  52.751 -9.776  1.00 70.47  ? 45  LYS L O   1 
ATOM   5816 C CB  . LYS D 3 45  ? 21.008  52.836 -11.933 1.00 87.08  ? 45  LYS L CB  1 
ATOM   5817 C CG  . LYS D 3 45  ? 21.364  53.265 -13.350 1.00 107.52 ? 45  LYS L CG  1 
ATOM   5818 C CD  . LYS D 3 45  ? 22.528  54.240 -13.372 1.00 134.82 ? 45  LYS L CD  1 
ATOM   5819 C CE  . LYS D 3 45  ? 23.001  54.482 -14.799 1.00 137.32 ? 45  LYS L CE  1 
ATOM   5820 N NZ  . LYS D 3 45  ? 24.255  55.287 -14.869 1.00 149.46 ? 45  LYS L NZ  1 
ATOM   5821 N N   . LEU D 3 46  ? 19.330  50.553 -9.966  1.00 62.82  ? 46  LEU L N   1 
ATOM   5822 C CA  . LEU D 3 46  ? 18.753  50.199 -8.678  1.00 61.50  ? 46  LEU L CA  1 
ATOM   5823 C C   . LEU D 3 46  ? 19.610  50.758 -7.552  1.00 59.70  ? 46  LEU L C   1 
ATOM   5824 O O   . LEU D 3 46  ? 20.793  50.420 -7.435  1.00 66.28  ? 46  LEU L O   1 
ATOM   5825 C CB  . LEU D 3 46  ? 18.628  48.687 -8.547  1.00 66.67  ? 46  LEU L CB  1 
ATOM   5826 C CG  . LEU D 3 46  ? 18.205  48.260 -7.148  1.00 66.52  ? 46  LEU L CG  1 
ATOM   5827 C CD1 . LEU D 3 46  ? 16.739  48.578 -6.898  1.00 69.04  ? 46  LEU L CD1 1 
ATOM   5828 C CD2 . LEU D 3 46  ? 18.488  46.802 -6.968  1.00 73.17  ? 46  LEU L CD2 1 
ATOM   5829 N N   . LEU D 3 47  ? 19.011  51.602 -6.715  1.00 61.50  ? 47  LEU L N   1 
ATOM   5830 C CA  . LEU D 3 47  ? 19.748  52.241 -5.634  1.00 60.35  ? 47  LEU L CA  1 
ATOM   5831 C C   . LEU D 3 47  ? 19.658  51.455 -4.332  1.00 69.16  ? 47  LEU L C   1 
ATOM   5832 O O   . LEU D 3 47  ? 20.674  51.232 -3.668  1.00 71.88  ? 47  LEU L O   1 
ATOM   5833 C CB  . LEU D 3 47  ? 19.229  53.665 -5.413  1.00 55.26  ? 47  LEU L CB  1 
ATOM   5834 C CG  . LEU D 3 47  ? 19.504  54.665 -6.532  1.00 50.86  ? 47  LEU L CG  1 
ATOM   5835 C CD1 . LEU D 3 47  ? 18.759  55.962 -6.273  1.00 52.72  ? 47  LEU L CD1 1 
ATOM   5836 C CD2 . LEU D 3 47  ? 20.998  54.909 -6.695  1.00 66.83  ? 47  LEU L CD2 1 
ATOM   5837 N N   . ILE D 3 48  ? 18.449  51.043 -3.948  1.00 71.22  ? 48  ILE L N   1 
ATOM   5838 C CA  . ILE D 3 48  ? 18.183  50.517 -2.612  1.00 67.38  ? 48  ILE L CA  1 
ATOM   5839 C C   . ILE D 3 48  ? 17.148  49.403 -2.700  1.00 65.88  ? 48  ILE L C   1 
ATOM   5840 O O   . ILE D 3 48  ? 16.150  49.525 -3.418  1.00 67.27  ? 48  ILE L O   1 
ATOM   5841 C CB  . ILE D 3 48  ? 17.698  51.635 -1.664  1.00 64.26  ? 48  ILE L CB  1 
ATOM   5842 C CG1 . ILE D 3 48  ? 18.770  52.710 -1.537  1.00 67.02  ? 48  ILE L CG1 1 
ATOM   5843 C CG2 . ILE D 3 48  ? 17.326  51.076 -0.296  1.00 70.97  ? 48  ILE L CG2 1 
ATOM   5844 C CD1 . ILE D 3 48  ? 18.494  53.720 -0.498  1.00 72.94  ? 48  ILE L CD1 1 
ATOM   5845 N N   . TYR D 3 49  ? 17.385  48.320 -1.957  1.00 65.77  ? 49  TYR L N   1 
ATOM   5846 C CA  . TYR D 3 49  ? 16.449  47.213 -1.807  1.00 66.41  ? 49  TYR L CA  1 
ATOM   5847 C C   . TYR D 3 49  ? 16.175  46.866 -0.346  1.00 76.36  ? 49  TYR L C   1 
ATOM   5848 O O   . TYR D 3 49  ? 16.810  47.394 0.570   1.00 81.51  ? 49  TYR L O   1 
ATOM   5849 C CB  . TYR D 3 49  ? 16.911  45.968 -2.577  1.00 63.11  ? 49  TYR L CB  1 
ATOM   5850 C CG  . TYR D 3 49  ? 18.234  45.401 -2.112  1.00 73.36  ? 49  TYR L CG  1 
ATOM   5851 C CD1 . TYR D 3 49  ? 19.432  45.987 -2.502  1.00 80.01  ? 49  TYR L CD1 1 
ATOM   5852 C CD2 . TYR D 3 49  ? 18.290  44.280 -1.293  1.00 79.60  ? 49  TYR L CD2 1 
ATOM   5853 C CE1 . TYR D 3 49  ? 20.644  45.476 -2.088  1.00 80.94  ? 49  TYR L CE1 1 
ATOM   5854 C CE2 . TYR D 3 49  ? 19.503  43.762 -0.872  1.00 76.25  ? 49  TYR L CE2 1 
ATOM   5855 C CZ  . TYR D 3 49  ? 20.676  44.365 -1.273  1.00 79.37  ? 49  TYR L CZ  1 
ATOM   5856 O OH  . TYR D 3 49  ? 21.891  43.864 -0.865  1.00 98.05  ? 49  TYR L OH  1 
ATOM   5857 N N   . LYS D 3 50  ? 15.186  46.001 -0.105  1.00 76.69  ? 50  LYS L N   1 
ATOM   5858 C CA  . LYS D 3 50  ? 14.785  45.732 1.304   1.00 73.12  ? 50  LYS L CA  1 
ATOM   5859 C C   . LYS D 3 50  ? 14.431  47.076 1.948   1.00 79.98  ? 50  LYS L C   1 
ATOM   5860 O O   . LYS D 3 50  ? 14.325  47.118 3.191   1.00 92.77  ? 50  LYS L O   1 
ATOM   5861 C CB  . LYS D 3 50  ? 15.895  45.023 2.087   1.00 78.13  ? 50  LYS L CB  1 
ATOM   5862 C CG  . LYS D 3 50  ? 16.344  43.683 1.525   1.00 93.49  ? 50  LYS L CG  1 
ATOM   5863 C CD  . LYS D 3 50  ? 17.409  43.017 2.368   1.00 111.32 ? 50  LYS L CD  1 
ATOM   5864 C CE  . LYS D 3 50  ? 16.919  42.642 3.750   1.00 120.66 ? 50  LYS L CE  1 
ATOM   5865 N NZ  . LYS D 3 50  ? 17.974  41.966 4.541   1.00 126.36 ? 50  LYS L NZ  1 
ATOM   5866 N N   . ALA D 3 51  ? 14.286  48.129 1.134   1.00 72.08  ? 51  ALA L N   1 
ATOM   5867 C CA  . ALA D 3 51  ? 13.919  49.477 1.637   1.00 68.20  ? 51  ALA L CA  1 
ATOM   5868 C C   . ALA D 3 51  ? 15.047  50.177 2.407   1.00 70.29  ? 51  ALA L C   1 
ATOM   5869 O O   . ALA D 3 51  ? 14.854  51.355 2.773   1.00 69.99  ? 51  ALA L O   1 
ATOM   5870 C CB  . ALA D 3 51  ? 12.539  49.446 2.253   1.00 73.53  ? 51  ALA L CB  1 
ATOM   5871 N N   . SER D 3 52  ? 16.179  49.493 2.615   1.00 72.46  ? 52  SER L N   1 
ATOM   5872 C CA  . SER D 3 52  ? 17.339  50.093 3.328   1.00 78.62  ? 52  SER L CA  1 
ATOM   5873 C C   . SER D 3 52  ? 18.692  49.577 2.829   1.00 74.35  ? 52  SER L C   1 
ATOM   5874 O O   . SER D 3 52  ? 19.712  50.234 3.114   1.00 74.06  ? 52  SER L O   1 
ATOM   5875 C CB  . SER D 3 52  ? 17.112  49.643 4.748   1.00 85.13  ? 52  SER L CB  1 
ATOM   5876 O OG  . SER D 3 52  ? 17.016  48.228 4.815   1.00 114.12 ? 52  SER L OG  1 
ATOM   5877 N N   . SER D 3 53  ? 18.758  48.638 1.952   1.00 72.31  ? 53  SER L N   1 
ATOM   5878 C CA  . SER D 3 53  ? 19.971  47.843 1.649   1.00 74.69  ? 53  SER L CA  1 
ATOM   5879 C C   . SER D 3 53  ? 20.510  48.582 0.426   1.00 72.97  ? 53  SER L C   1 
ATOM   5880 O O   . SER D 3 53  ? 19.850  48.524 -0.616  1.00 78.52  ? 53  SER L O   1 
ATOM   5881 C CB  . SER D 3 53  ? 19.776  46.388 1.373   1.00 75.10  ? 53  SER L CB  1 
ATOM   5882 O OG  . SER D 3 53  ? 19.608  45.670 2.585   1.00 68.80  ? 53  SER L OG  1 
ATOM   5883 N N   . LEU D 3 54  ? 21.655  49.257 0.558   1.00 72.76  ? 54  LEU L N   1 
ATOM   5884 C CA  . LEU D 3 54  ? 22.275  49.901 -0.594  1.00 73.71  ? 54  LEU L CA  1 
ATOM   5885 C C   . LEU D 3 54  ? 22.937  48.854 -1.477  1.00 78.51  ? 54  LEU L C   1 
ATOM   5886 O O   . LEU D 3 54  ? 23.688  48.005 -0.988  1.00 87.50  ? 54  LEU L O   1 
ATOM   5887 C CB  . LEU D 3 54  ? 23.314  50.929 -0.146  1.00 76.23  ? 54  LEU L CB  1 
ATOM   5888 C CG  . LEU D 3 54  ? 22.845  52.061 0.764   1.00 98.65  ? 54  LEU L CG  1 
ATOM   5889 C CD1 . LEU D 3 54  ? 24.025  52.795 1.382   1.00 118.65 ? 54  LEU L CD1 1 
ATOM   5890 C CD2 . LEU D 3 54  ? 21.995  53.019 -0.041  1.00 127.89 ? 54  LEU L CD2 1 
ATOM   5891 N N   . GLU D 3 55  ? 22.660  48.908 -2.775  1.00 85.14  ? 55  GLU L N   1 
ATOM   5892 C CA  . GLU D 3 55  ? 23.367  48.036 -3.699  1.00 84.17  ? 55  GLU L CA  1 
ATOM   5893 C C   . GLU D 3 55  ? 24.824  48.474 -3.818  1.00 86.42  ? 55  GLU L C   1 
ATOM   5894 O O   . GLU D 3 55  ? 25.157  49.651 -3.652  1.00 84.11  ? 55  GLU L O   1 
ATOM   5895 C CB  . GLU D 3 55  ? 22.693  48.041 -5.070  1.00 80.70  ? 55  GLU L CB  1 
ATOM   5896 C CG  . GLU D 3 55  ? 23.381  47.139 -6.072  1.00 95.03  ? 55  GLU L CG  1 
ATOM   5897 C CD  . GLU D 3 55  ? 22.646  47.030 -7.382  1.00 109.69 ? 55  GLU L CD  1 
ATOM   5898 O OE1 . GLU D 3 55  ? 21.674  47.784 -7.590  1.00 128.17 ? 55  GLU L OE1 1 
ATOM   5899 O OE2 . GLU D 3 55  ? 23.066  46.203 -8.219  1.00 116.82 ? 55  GLU L OE2 1 
ATOM   5900 N N   . SER D 3 56  ? 25.701  47.503 -4.075  1.00 91.77  ? 56  SER L N   1 
ATOM   5901 C CA  . SER D 3 56  ? 27.118  47.787 -4.254  1.00 93.29  ? 56  SER L CA  1 
ATOM   5902 C C   . SER D 3 56  ? 27.322  48.820 -5.354  1.00 95.76  ? 56  SER L C   1 
ATOM   5903 O O   . SER D 3 56  ? 26.620  48.818 -6.369  1.00 99.27  ? 56  SER L O   1 
ATOM   5904 C CB  . SER D 3 56  ? 27.869  46.499 -4.601  1.00 100.13 ? 56  SER L CB  1 
ATOM   5905 O OG  . SER D 3 56  ? 27.668  46.155 -5.961  1.00 103.33 ? 56  SER L OG  1 
ATOM   5906 N N   . GLY D 3 57  ? 28.284  49.713 -5.145  1.00 100.61 ? 57  GLY L N   1 
ATOM   5907 C CA  . GLY D 3 57  ? 28.579  50.728 -6.133  1.00 110.53 ? 57  GLY L CA  1 
ATOM   5908 C C   . GLY D 3 57  ? 27.722  51.971 -6.064  1.00 97.83  ? 57  GLY L C   1 
ATOM   5909 O O   . GLY D 3 57  ? 27.905  52.875 -6.886  1.00 94.01  ? 57  GLY L O   1 
ATOM   5910 N N   . VAL D 3 58  ? 26.790  52.042 -5.126  1.00 87.09  ? 58  VAL L N   1 
ATOM   5911 C CA  . VAL D 3 58  ? 25.997  53.244 -4.877  1.00 84.12  ? 58  VAL L CA  1 
ATOM   5912 C C   . VAL D 3 58  ? 26.684  54.040 -3.772  1.00 81.02  ? 58  VAL L C   1 
ATOM   5913 O O   . VAL D 3 58  ? 27.014  53.459 -2.727  1.00 81.36  ? 58  VAL L O   1 
ATOM   5914 C CB  . VAL D 3 58  ? 24.548  52.897 -4.486  1.00 74.10  ? 58  VAL L CB  1 
ATOM   5915 C CG1 . VAL D 3 58  ? 23.693  54.148 -4.444  1.00 62.03  ? 58  VAL L CG1 1 
ATOM   5916 C CG2 . VAL D 3 58  ? 23.957  51.901 -5.471  1.00 73.27  ? 58  VAL L CG2 1 
ATOM   5917 N N   . PRO D 3 59  ? 26.929  55.339 -3.961  1.00 79.55  ? 59  PRO L N   1 
ATOM   5918 C CA  . PRO D 3 59  ? 27.639  56.115 -2.935  1.00 84.86  ? 59  PRO L CA  1 
ATOM   5919 C C   . PRO D 3 59  ? 27.061  56.140 -1.527  1.00 83.04  ? 59  PRO L C   1 
ATOM   5920 O O   . PRO D 3 59  ? 25.864  55.932 -1.315  1.00 78.86  ? 59  PRO L O   1 
ATOM   5921 C CB  . PRO D 3 59  ? 27.662  57.533 -3.519  1.00 88.79  ? 59  PRO L CB  1 
ATOM   5922 C CG  . PRO D 3 59  ? 27.586  57.323 -4.993  1.00 81.48  ? 59  PRO L CG  1 
ATOM   5923 C CD  . PRO D 3 59  ? 26.669  56.142 -5.170  1.00 81.83  ? 59  PRO L CD  1 
ATOM   5924 N N   . SER D 3 60  ? 27.942  56.404 -0.557  1.00 94.90  ? 60  SER L N   1 
ATOM   5925 C CA  . SER D 3 60  ? 27.538  56.418 0.846   1.00 95.82  ? 60  SER L CA  1 
ATOM   5926 C C   . SER D 3 60  ? 26.339  57.352 1.152   1.00 88.55  ? 60  SER L C   1 
ATOM   5927 O O   . SER D 3 60  ? 25.475  57.063 1.989   1.00 87.86  ? 60  SER L O   1 
ATOM   5928 C CB  . SER D 3 60  ? 28.757  56.710 1.727   1.00 113.86 ? 60  SER L CB  1 
ATOM   5929 O OG  . SER D 3 60  ? 29.730  55.684 1.613   1.00 132.91 ? 60  SER L OG  1 
ATOM   5930 N N   . ARG D 3 61  ? 26.275  58.459 0.412   1.00 86.88  ? 61  ARG L N   1 
ATOM   5931 C CA  . ARG D 3 61  ? 25.206  59.432 0.603   1.00 82.93  ? 61  ARG L CA  1 
ATOM   5932 C C   . ARG D 3 61  ? 23.747  59.054 0.370   1.00 78.07  ? 61  ARG L C   1 
ATOM   5933 O O   . ARG D 3 61  ? 22.859  59.723 0.908   1.00 79.67  ? 61  ARG L O   1 
ATOM   5934 C CB  . ARG D 3 61  ? 25.590  60.641 -0.249  1.00 82.67  ? 61  ARG L CB  1 
ATOM   5935 C CG  . ARG D 3 61  ? 25.453  60.419 -1.740  1.00 79.30  ? 61  ARG L CG  1 
ATOM   5936 C CD  . ARG D 3 61  ? 25.461  61.736 -2.486  1.00 79.13  ? 61  ARG L CD  1 
ATOM   5937 N NE  . ARG D 3 61  ? 25.461  61.555 -3.932  1.00 83.33  ? 61  ARG L NE  1 
ATOM   5938 C CZ  . ARG D 3 61  ? 26.530  61.217 -4.641  1.00 85.12  ? 61  ARG L CZ  1 
ATOM   5939 N NH1 . ARG D 3 61  ? 27.707  61.025 -4.068  1.00 80.63  ? 61  ARG L NH1 1 
ATOM   5940 N NH2 . ARG D 3 61  ? 26.418  61.078 -5.959  1.00 88.95  ? 61  ARG L NH2 1 
ATOM   5941 N N   . PHE D 3 62  ? 23.474  58.010 -0.408  1.00 76.55  ? 62  PHE L N   1 
ATOM   5942 C CA  . PHE D 3 62  ? 22.112  57.514 -0.547  1.00 77.67  ? 62  PHE L CA  1 
ATOM   5943 C C   . PHE D 3 62  ? 21.759  56.621 0.633   1.00 84.53  ? 62  PHE L C   1 
ATOM   5944 O O   . PHE D 3 62  ? 22.593  55.852 1.118   1.00 93.73  ? 62  PHE L O   1 
ATOM   5945 C CB  . PHE D 3 62  ? 21.941  56.747 -1.857  1.00 76.33  ? 62  PHE L CB  1 
ATOM   5946 C CG  . PHE D 3 62  ? 22.034  57.608 -3.079  1.00 78.62  ? 62  PHE L CG  1 
ATOM   5947 C CD1 . PHE D 3 62  ? 23.255  57.859 -3.678  1.00 81.02  ? 62  PHE L CD1 1 
ATOM   5948 C CD2 . PHE D 3 62  ? 20.894  58.174 -3.624  1.00 74.31  ? 62  PHE L CD2 1 
ATOM   5949 C CE1 . PHE D 3 62  ? 23.338  58.656 -4.804  1.00 81.60  ? 62  PHE L CE1 1 
ATOM   5950 C CE2 . PHE D 3 62  ? 20.970  58.970 -4.747  1.00 80.78  ? 62  PHE L CE2 1 
ATOM   5951 C CZ  . PHE D 3 62  ? 22.194  59.212 -5.338  1.00 81.55  ? 62  PHE L CZ  1 
ATOM   5952 N N   . SER D 3 63  ? 20.518  56.734 1.104   1.00 81.51  ? 63  SER L N   1 
ATOM   5953 C CA  . SER D 3 63  ? 20.099  55.977 2.278   1.00 81.84  ? 63  SER L CA  1 
ATOM   5954 C C   . SER D 3 63  ? 18.583  55.860 2.299   1.00 77.50  ? 63  SER L C   1 
ATOM   5955 O O   . SER D 3 63  ? 17.879  56.869 2.210   1.00 82.30  ? 63  SER L O   1 
ATOM   5956 C CB  . SER D 3 63  ? 20.603  56.640 3.562   1.00 90.83  ? 63  SER L CB  1 
ATOM   5957 O OG  . SER D 3 63  ? 20.372  58.040 3.538   1.00 90.55  ? 63  SER L OG  1 
ATOM   5958 N N   . GLY D 3 64  ? 18.078  54.644 2.439   1.00 80.54  ? 64  GLY L N   1 
ATOM   5959 C CA  . GLY D 3 64  ? 16.650  54.395 2.384   1.00 81.00  ? 64  GLY L CA  1 
ATOM   5960 C C   . GLY D 3 64  ? 16.143  53.950 3.753   1.00 85.09  ? 64  GLY L C   1 
ATOM   5961 O O   . GLY D 3 64  ? 16.803  53.168 4.443   1.00 96.77  ? 64  GLY L O   1 
ATOM   5962 N N   . SER D 3 65  ? 14.960  54.430 4.109   1.00 82.55  ? 65  SER L N   1 
ATOM   5963 C CA  . SER D 3 65  ? 14.372  54.122 5.403   1.00 82.30  ? 65  SER L CA  1 
ATOM   5964 C C   . SER D 3 65  ? 12.887  53.840 5.233   1.00 77.44  ? 65  SER L C   1 
ATOM   5965 O O   . SER D 3 65  ? 12.279  54.174 4.213   1.00 82.86  ? 65  SER L O   1 
ATOM   5966 C CB  . SER D 3 65  ? 14.586  55.268 6.398   1.00 85.73  ? 65  SER L CB  1 
ATOM   5967 O OG  . SER D 3 65  ? 14.343  56.527 5.792   1.00 84.67  ? 65  SER L OG  1 
ATOM   5968 N N   . GLY D 3 66  ? 12.305  53.230 6.263   1.00 64.32  ? 66  GLY L N   1 
ATOM   5969 C CA  . GLY D 3 66  ? 10.874  53.018 6.316   1.00 66.16  ? 66  GLY L CA  1 
ATOM   5970 C C   . GLY D 3 66  ? 10.456  51.568 6.373   1.00 66.86  ? 66  GLY L C   1 
ATOM   5971 O O   . GLY D 3 66  ? 11.200  50.679 5.954   1.00 67.17  ? 66  GLY L O   1 
ATOM   5972 N N   . SER D 3 67  ? 9.256   51.328 6.894   1.00 71.92  ? 67  SER L N   1 
ATOM   5973 C CA  . SER D 3 67  ? 8.634   50.013 6.895   1.00 73.23  ? 67  SER L CA  1 
ATOM   5974 C C   . SER D 3 67  ? 7.130   50.187 6.754   1.00 76.18  ? 67  SER L C   1 
ATOM   5975 O O   . SER D 3 67  ? 6.584   51.254 7.038   1.00 85.94  ? 67  SER L O   1 
ATOM   5976 C CB  . SER D 3 67  ? 8.955   49.220 8.171   1.00 82.00  ? 67  SER L CB  1 
ATOM   5977 O OG  . SER D 3 67  ? 8.207   49.711 9.275   1.00 96.19  ? 67  SER L OG  1 
ATOM   5978 N N   . GLY D 3 68  ? 6.463   49.127 6.306   1.00 81.49  ? 68  GLY L N   1 
ATOM   5979 C CA  . GLY D 3 68  ? 5.013   49.124 6.233   1.00 91.02  ? 68  GLY L CA  1 
ATOM   5980 C C   . GLY D 3 68  ? 4.418   49.900 5.075   1.00 90.29  ? 68  GLY L C   1 
ATOM   5981 O O   . GLY D 3 68  ? 4.253   49.358 3.978   1.00 95.87  ? 68  GLY L O   1 
ATOM   5982 N N   . SER D 3 69  ? 4.088   51.173 5.308   1.00 81.69  ? 69  SER L N   1 
ATOM   5983 C CA  . SER D 3 69  ? 3.346   51.967 4.340   1.00 73.94  ? 69  SER L CA  1 
ATOM   5984 C C   . SER D 3 69  ? 4.052   53.235 3.869   1.00 79.99  ? 69  SER L C   1 
ATOM   5985 O O   . SER D 3 69  ? 3.700   53.740 2.796   1.00 91.37  ? 69  SER L O   1 
ATOM   5986 C CB  . SER D 3 69  ? 1.972   52.356 4.914   1.00 85.57  ? 69  SER L CB  1 
ATOM   5987 O OG  . SER D 3 69  ? 1.142   52.933 3.919   1.00 93.36  ? 69  SER L OG  1 
ATOM   5988 N N   . GLU D 3 70  ? 5.024   53.766 4.620   1.00 78.66  ? 70  GLU L N   1 
ATOM   5989 C CA  . GLU D 3 70  ? 5.742   54.976 4.231   1.00 84.89  ? 70  GLU L CA  1 
ATOM   5990 C C   . GLU D 3 70  ? 7.243   54.734 4.243   1.00 78.35  ? 70  GLU L C   1 
ATOM   5991 O O   . GLU D 3 70  ? 7.765   54.063 5.140   1.00 80.72  ? 70  GLU L O   1 
ATOM   5992 C CB  . GLU D 3 70  ? 5.423   56.153 5.155   1.00 99.48  ? 70  GLU L CB  1 
ATOM   5993 C CG  . GLU D 3 70  ? 3.961   56.540 5.215   1.00 110.32 ? 70  GLU L CG  1 
ATOM   5994 C CD  . GLU D 3 70  ? 3.732   57.746 6.100   1.00 128.08 ? 70  GLU L CD  1 
ATOM   5995 O OE1 . GLU D 3 70  ? 4.731   58.378 6.510   1.00 119.89 ? 70  GLU L OE1 1 
ATOM   5996 O OE2 . GLU D 3 70  ? 2.558   58.058 6.389   1.00 135.48 ? 70  GLU L OE2 1 
ATOM   5997 N N   . PHE D 3 71  ? 7.932   55.294 3.246   1.00 71.74  ? 71  PHE L N   1 
ATOM   5998 C CA  . PHE D 3 71  ? 9.353   55.045 3.040   1.00 71.34  ? 71  PHE L CA  1 
ATOM   5999 C C   . PHE D 3 71  ? 10.005  56.317 2.511   1.00 71.96  ? 71  PHE L C   1 
ATOM   6000 O O   . PHE D 3 71  ? 9.337   57.186 1.949   1.00 77.78  ? 71  PHE L O   1 
ATOM   6001 C CB  . PHE D 3 71  ? 9.561   53.868 2.075   1.00 69.57  ? 71  PHE L CB  1 
ATOM   6002 C CG  . PHE D 3 71  ? 8.860   52.596 2.501   1.00 74.07  ? 71  PHE L CG  1 
ATOM   6003 C CD1 . PHE D 3 71  ? 7.515   52.392 2.215   1.00 74.74  ? 71  PHE L CD1 1 
ATOM   6004 C CD2 . PHE D 3 71  ? 9.561   51.579 3.133   1.00 76.30  ? 71  PHE L CD2 1 
ATOM   6005 C CE1 . PHE D 3 71  ? 6.877   51.227 2.588   1.00 75.14  ? 71  PHE L CE1 1 
ATOM   6006 C CE2 . PHE D 3 71  ? 8.924   50.405 3.503   1.00 77.75  ? 71  PHE L CE2 1 
ATOM   6007 C CZ  . PHE D 3 71  ? 7.582   50.232 3.231   1.00 75.78  ? 71  PHE L CZ  1 
ATOM   6008 N N   . THR D 3 72  ? 11.320  56.427 2.704   1.00 79.07  ? 72  THR L N   1 
ATOM   6009 C CA  . THR D 3 72  ? 12.033  57.669 2.411   1.00 77.06  ? 72  THR L CA  1 
ATOM   6010 C C   . THR D 3 72  ? 13.417  57.387 1.846   1.00 76.01  ? 72  THR L C   1 
ATOM   6011 O O   . THR D 3 72  ? 14.228  56.703 2.480   1.00 79.28  ? 72  THR L O   1 
ATOM   6012 C CB  . THR D 3 72  ? 12.144  58.546 3.663   1.00 75.11  ? 72  THR L CB  1 
ATOM   6013 O OG1 . THR D 3 72  ? 10.879  58.583 4.334   1.00 72.26  ? 72  THR L OG1 1 
ATOM   6014 C CG2 . THR D 3 72  ? 12.558  59.962 3.288   1.00 74.68  ? 72  THR L CG2 1 
ATOM   6015 N N   . LEU D 3 73  ? 13.677  57.933 0.659   1.00 64.73  ? 73  LEU L N   1 
ATOM   6016 C CA  . LEU D 3 73  ? 15.013  57.984 0.080   1.00 65.87  ? 73  LEU L CA  1 
ATOM   6017 C C   . LEU D 3 73  ? 15.682  59.296 0.470   1.00 64.75  ? 73  LEU L C   1 
ATOM   6018 O O   . LEU D 3 73  ? 15.071  60.362 0.368   1.00 67.08  ? 73  LEU L O   1 
ATOM   6019 C CB  . LEU D 3 73  ? 14.945  57.863 -1.442  1.00 69.23  ? 73  LEU L CB  1 
ATOM   6020 C CG  . LEU D 3 73  ? 16.292  57.850 -2.166  1.00 66.76  ? 73  LEU L CG  1 
ATOM   6021 C CD1 . LEU D 3 73  ? 16.942  56.491 -2.048  1.00 68.51  ? 73  LEU L CD1 1 
ATOM   6022 C CD2 . LEU D 3 73  ? 16.125  58.237 -3.624  1.00 60.72  ? 73  LEU L CD2 1 
ATOM   6023 N N   . THR D 3 74  ? 16.928  59.229 0.931   1.00 70.17  ? 74  THR L N   1 
ATOM   6024 C CA  . THR D 3 74  ? 17.600  60.452 1.432   1.00 71.56  ? 74  THR L CA  1 
ATOM   6025 C C   . THR D 3 74  ? 18.994  60.588 0.833   1.00 72.52  ? 74  THR L C   1 
ATOM   6026 O O   . THR D 3 74  ? 19.732  59.594 0.851   1.00 80.43  ? 74  THR L O   1 
ATOM   6027 C CB  . THR D 3 74  ? 17.743  60.396 2.953   1.00 79.11  ? 74  THR L CB  1 
ATOM   6028 O OG1 . THR D 3 74  ? 16.429  60.366 3.510   1.00 81.30  ? 74  THR L OG1 1 
ATOM   6029 C CG2 . THR D 3 74  ? 18.515  61.566 3.519   1.00 84.63  ? 74  THR L CG2 1 
ATOM   6030 N N   . ILE D 3 75  ? 19.339  61.779 0.342   1.00 80.81  ? 75  ILE L N   1 
ATOM   6031 C CA  . ILE D 3 75  ? 20.703  62.032 -0.199  1.00 77.59  ? 75  ILE L CA  1 
ATOM   6032 C C   . ILE D 3 75  ? 21.400  63.002 0.752   1.00 80.40  ? 75  ILE L C   1 
ATOM   6033 O O   . ILE D 3 75  ? 20.889  64.115 0.921   1.00 83.14  ? 75  ILE L O   1 
ATOM   6034 C CB  . ILE D 3 75  ? 20.627  62.594 -1.628  1.00 75.63  ? 75  ILE L CB  1 
ATOM   6035 C CG1 . ILE D 3 75  ? 19.780  61.707 -2.542  1.00 73.04  ? 75  ILE L CG1 1 
ATOM   6036 C CG2 . ILE D 3 75  ? 22.019  62.818 -2.194  1.00 77.35  ? 75  ILE L CG2 1 
ATOM   6037 C CD1 . ILE D 3 75  ? 19.669  62.224 -3.953  1.00 70.36  ? 75  ILE L CD1 1 
ATOM   6038 N N   . SER D 3 76  ? 22.515  62.584 1.349   1.00 86.84  ? 76  SER L N   1 
ATOM   6039 C CA  . SER D 3 76  ? 23.214  63.433 2.344   1.00 92.06  ? 76  SER L CA  1 
ATOM   6040 C C   . SER D 3 76  ? 23.835  64.737 1.850   1.00 95.91  ? 76  SER L C   1 
ATOM   6041 O O   . SER D 3 76  ? 23.653  65.764 2.516   1.00 105.36 ? 76  SER L O   1 
ATOM   6042 C CB  . SER D 3 76  ? 24.392  62.713 2.912   1.00 92.86  ? 76  SER L CB  1 
ATOM   6043 O OG  . SER D 3 76  ? 24.015  61.422 3.363   1.00 119.30 ? 76  SER L OG  1 
ATOM   6044 N N   . SER D 3 77  ? 24.544  64.683 0.725   1.00 97.05  ? 77  SER L N   1 
ATOM   6045 C CA  . SER D 3 77  ? 25.176  65.898 0.160   1.00 100.26 ? 77  SER L CA  1 
ATOM   6046 C C   . SER D 3 77  ? 24.842  65.785 -1.323  1.00 96.88  ? 77  SER L C   1 
ATOM   6047 O O   . SER D 3 77  ? 25.579  65.091 -2.034  1.00 99.16  ? 77  SER L O   1 
ATOM   6048 C CB  . SER D 3 77  ? 26.646  66.054 0.364   1.00 106.45 ? 77  SER L CB  1 
ATOM   6049 O OG  . SER D 3 77  ? 27.343  64.926 -0.141  1.00 103.33 ? 77  SER L OG  1 
ATOM   6050 N N   . LEU D 3 78  ? 23.765  66.430 -1.767  1.00 89.68  ? 78  LEU L N   1 
ATOM   6051 C CA  . LEU D 3 78  ? 23.378  66.261 -3.160  1.00 88.04  ? 78  LEU L CA  1 
ATOM   6052 C C   . LEU D 3 78  ? 24.503  66.709 -4.085  1.00 90.87  ? 78  LEU L C   1 
ATOM   6053 O O   . LEU D 3 78  ? 25.003  67.832 -3.977  1.00 94.29  ? 78  LEU L O   1 
ATOM   6054 C CB  . LEU D 3 78  ? 22.103  67.049 -3.453  1.00 86.41  ? 78  LEU L CB  1 
ATOM   6055 C CG  . LEU D 3 78  ? 21.598  67.019 -4.896  1.00 82.55  ? 78  LEU L CG  1 
ATOM   6056 C CD1 . LEU D 3 78  ? 20.776  65.768 -5.153  1.00 85.62  ? 78  LEU L CD1 1 
ATOM   6057 C CD2 . LEU D 3 78  ? 20.783  68.264 -5.185  1.00 87.15  ? 78  LEU L CD2 1 
ATOM   6058 N N   . GLN D 3 79  ? 24.901  65.822 -5.001  1.00 87.04  ? 79  GLN L N   1 
ATOM   6059 C CA  . GLN D 3 79  ? 25.956  66.083 -5.968  1.00 85.68  ? 79  GLN L CA  1 
ATOM   6060 C C   . GLN D 3 79  ? 25.381  66.326 -7.357  1.00 92.99  ? 79  GLN L C   1 
ATOM   6061 O O   . GLN D 3 79  ? 24.214  66.021 -7.624  1.00 91.87  ? 79  GLN L O   1 
ATOM   6062 C CB  . GLN D 3 79  ? 26.945  64.911 -5.999  1.00 85.85  ? 79  GLN L CB  1 
ATOM   6063 C CG  . GLN D 3 79  ? 27.661  64.682 -4.679  1.00 95.11  ? 79  GLN L CG  1 
ATOM   6064 C CD  . GLN D 3 79  ? 28.355  65.936 -4.184  1.00 100.97 ? 79  GLN L CD  1 
ATOM   6065 O OE1 . GLN D 3 79  ? 27.990  66.496 -3.151  1.00 108.68 ? 79  GLN L OE1 1 
ATOM   6066 N NE2 . GLN D 3 79  ? 29.360  66.389 -4.928  1.00 98.53  ? 79  GLN L NE2 1 
ATOM   6067 N N   . PRO D 3 80  ? 26.175  66.897 -8.269  1.00 93.67  ? 80  PRO L N   1 
ATOM   6068 C CA  . PRO D 3 80  ? 25.623  67.242 -9.589  1.00 86.88  ? 80  PRO L CA  1 
ATOM   6069 C C   . PRO D 3 80  ? 25.161  66.043 -10.405 1.00 85.95  ? 80  PRO L C   1 
ATOM   6070 O O   . PRO D 3 80  ? 24.161  66.150 -11.125 1.00 89.20  ? 80  PRO L O   1 
ATOM   6071 C CB  . PRO D 3 80  ? 26.788  67.991 -10.253 1.00 98.40  ? 80  PRO L CB  1 
ATOM   6072 C CG  . PRO D 3 80  ? 27.522  68.590 -9.103  1.00 100.30 ? 80  PRO L CG  1 
ATOM   6073 C CD  . PRO D 3 80  ? 27.510  67.495 -8.079  1.00 96.27  ? 80  PRO L CD  1 
ATOM   6074 N N   . ASP D 3 81  ? 25.839  64.897 -10.307 1.00 86.47  ? 81  ASP L N   1 
ATOM   6075 C CA  . ASP D 3 81  ? 25.415  63.734 -11.081 1.00 93.53  ? 81  ASP L CA  1 
ATOM   6076 C C   . ASP D 3 81  ? 24.115  63.125 -10.558 1.00 89.72  ? 81  ASP L C   1 
ATOM   6077 O O   . ASP D 3 81  ? 23.550  62.241 -11.214 1.00 89.62  ? 81  ASP L O   1 
ATOM   6078 C CB  . ASP D 3 81  ? 26.535  62.687 -11.098 1.00 91.58  ? 81  ASP L CB  1 
ATOM   6079 C CG  . ASP D 3 81  ? 26.217  61.504 -11.992 1.00 103.32 ? 81  ASP L CG  1 
ATOM   6080 O OD1 . ASP D 3 81  ? 26.369  61.634 -13.226 1.00 109.49 ? 81  ASP L OD1 1 
ATOM   6081 O OD2 . ASP D 3 81  ? 25.819  60.446 -11.464 1.00 118.95 ? 81  ASP L OD2 1 
ATOM   6082 N N   . ASP D 3 82  ? 23.614  63.590 -9.415  1.00 83.73  ? 82  ASP L N   1 
ATOM   6083 C CA  . ASP D 3 82  ? 22.376  63.069 -8.850  1.00 81.22  ? 82  ASP L CA  1 
ATOM   6084 C C   . ASP D 3 82  ? 21.127  63.608 -9.533  1.00 79.89  ? 82  ASP L C   1 
ATOM   6085 O O   . ASP D 3 82  ? 20.026  63.165 -9.190  1.00 80.38  ? 82  ASP L O   1 
ATOM   6086 C CB  . ASP D 3 82  ? 22.301  63.376 -7.354  1.00 80.71  ? 82  ASP L CB  1 
ATOM   6087 C CG  . ASP D 3 82  ? 23.446  62.772 -6.581  1.00 84.31  ? 82  ASP L CG  1 
ATOM   6088 O OD1 . ASP D 3 82  ? 23.802  61.609 -6.867  1.00 83.70  ? 82  ASP L OD1 1 
ATOM   6089 O OD2 . ASP D 3 82  ? 23.982  63.455 -5.685  1.00 89.43  ? 82  ASP L OD2 1 
ATOM   6090 N N   . PHE D 3 83  ? 21.260  64.555 -10.462 1.00 74.99  ? 83  PHE L N   1 
ATOM   6091 C CA  . PHE D 3 83  ? 20.114  65.000 -11.247 1.00 78.49  ? 83  PHE L CA  1 
ATOM   6092 C C   . PHE D 3 83  ? 19.475  63.809 -11.939 1.00 77.77  ? 83  PHE L C   1 
ATOM   6093 O O   . PHE D 3 83  ? 20.112  63.170 -12.783 1.00 84.78  ? 83  PHE L O   1 
ATOM   6094 C CB  . PHE D 3 83  ? 20.543  66.024 -12.295 1.00 85.78  ? 83  PHE L CB  1 
ATOM   6095 C CG  . PHE D 3 83  ? 19.556  66.175 -13.426 1.00 92.78  ? 83  PHE L CG  1 
ATOM   6096 C CD1 . PHE D 3 83  ? 18.252  66.577 -13.182 1.00 94.95  ? 83  PHE L CD1 1 
ATOM   6097 C CD2 . PHE D 3 83  ? 19.919  65.861 -14.727 1.00 96.91  ? 83  PHE L CD2 1 
ATOM   6098 C CE1 . PHE D 3 83  ? 17.341  66.698 -14.217 1.00 101.07 ? 83  PHE L CE1 1 
ATOM   6099 C CE2 . PHE D 3 83  ? 19.010  65.978 -15.766 1.00 97.57  ? 83  PHE L CE2 1 
ATOM   6100 C CZ  . PHE D 3 83  ? 17.721  66.397 -15.509 1.00 100.04 ? 83  PHE L CZ  1 
ATOM   6101 N N   . ALA D 3 84  ? 18.215  63.523 -11.609 1.00 75.60  ? 84  ALA L N   1 
ATOM   6102 C CA  . ALA D 3 84  ? 17.595  62.347 -12.223 1.00 71.26  ? 84  ALA L CA  1 
ATOM   6103 C C   . ALA D 3 84  ? 16.148  62.233 -11.774 1.00 67.94  ? 84  ALA L C   1 
ATOM   6104 O O   . ALA D 3 84  ? 15.691  62.952 -10.880 1.00 73.25  ? 84  ALA L O   1 
ATOM   6105 C CB  . ALA D 3 84  ? 18.324  61.045 -11.875 1.00 69.04  ? 84  ALA L CB  1 
ATOM   6106 N N   . ILE D 3 85  ? 15.434  61.293 -12.387 1.00 66.04  ? 85  ILE L N   1 
ATOM   6107 C CA  . ILE D 3 85  ? 14.125  60.902 -11.892 1.00 65.28  ? 85  ILE L CA  1 
ATOM   6108 C C   . ILE D 3 85  ? 14.326  59.706 -10.976 1.00 67.48  ? 85  ILE L C   1 
ATOM   6109 O O   . ILE D 3 85  ? 15.071  58.776 -11.300 1.00 67.09  ? 85  ILE L O   1 
ATOM   6110 C CB  . ILE D 3 85  ? 13.164  60.564 -13.040 1.00 60.73  ? 85  ILE L CB  1 
ATOM   6111 C CG1 . ILE D 3 85  ? 13.195  61.655 -14.104 1.00 73.92  ? 85  ILE L CG1 1 
ATOM   6112 C CG2 . ILE D 3 85  ? 11.754  60.491 -12.508 1.00 61.50  ? 85  ILE L CG2 1 
ATOM   6113 C CD1 . ILE D 3 85  ? 12.621  61.207 -15.432 1.00 92.51  ? 85  ILE L CD1 1 
ATOM   6114 N N   . TYR D 3 86  ? 13.690  59.739 -9.818  1.00 59.29  ? 86  TYR L N   1 
ATOM   6115 C CA  . TYR D 3 86  ? 13.836  58.697 -8.817  1.00 56.17  ? 86  TYR L CA  1 
ATOM   6116 C C   . TYR D 3 86  ? 12.499  57.993 -8.649  1.00 58.66  ? 86  TYR L C   1 
ATOM   6117 O O   . TYR D 3 86  ? 11.467  58.646 -8.454  1.00 70.08  ? 86  TYR L O   1 
ATOM   6118 C CB  . TYR D 3 86  ? 14.337  59.291 -7.503  1.00 52.10  ? 86  TYR L CB  1 
ATOM   6119 C CG  . TYR D 3 86  ? 15.767  59.775 -7.596  1.00 54.36  ? 86  TYR L CG  1 
ATOM   6120 C CD1 . TYR D 3 86  ? 16.821  58.873 -7.637  1.00 62.45  ? 86  TYR L CD1 1 
ATOM   6121 C CD2 . TYR D 3 86  ? 16.061  61.130 -7.680  1.00 60.32  ? 86  TYR L CD2 1 
ATOM   6122 C CE1 . TYR D 3 86  ? 18.129  59.306 -7.731  1.00 64.32  ? 86  TYR L CE1 1 
ATOM   6123 C CE2 . TYR D 3 86  ? 17.368  61.572 -7.776  1.00 64.51  ? 86  TYR L CE2 1 
ATOM   6124 C CZ  . TYR D 3 86  ? 18.398  60.655 -7.802  1.00 62.92  ? 86  TYR L CZ  1 
ATOM   6125 O OH  . TYR D 3 86  ? 19.704  61.080 -7.899  1.00 64.44  ? 86  TYR L OH  1 
ATOM   6126 N N   . TYR D 3 87  ? 12.521  56.667 -8.752  1.00 58.36  ? 87  TYR L N   1 
ATOM   6127 C CA  . TYR D 3 87  ? 11.327  55.836 -8.715  1.00 57.82  ? 87  TYR L CA  1 
ATOM   6128 C C   . TYR D 3 87  ? 11.372  54.892 -7.519  1.00 59.97  ? 87  TYR L C   1 
ATOM   6129 O O   . TYR D 3 87  ? 12.420  54.662 -6.911  1.00 66.14  ? 87  TYR L O   1 
ATOM   6130 C CB  . TYR D 3 87  ? 11.168  55.019 -10.003 1.00 65.62  ? 87  TYR L CB  1 
ATOM   6131 C CG  . TYR D 3 87  ? 10.706  55.796 -11.216 1.00 65.73  ? 87  TYR L CG  1 
ATOM   6132 C CD1 . TYR D 3 87  ? 11.596  56.566 -11.948 1.00 66.73  ? 87  TYR L CD1 1 
ATOM   6133 C CD2 . TYR D 3 87  ? 9.382   55.743 -11.639 1.00 66.36  ? 87  TYR L CD2 1 
ATOM   6134 C CE1 . TYR D 3 87  ? 11.183  57.263 -13.063 1.00 69.27  ? 87  TYR L CE1 1 
ATOM   6135 C CE2 . TYR D 3 87  ? 8.960   56.444 -12.755 1.00 68.88  ? 87  TYR L CE2 1 
ATOM   6136 C CZ  . TYR D 3 87  ? 9.865   57.205 -13.462 1.00 71.88  ? 87  TYR L CZ  1 
ATOM   6137 O OH  . TYR D 3 87  ? 9.463   57.910 -14.577 1.00 76.39  ? 87  TYR L OH  1 
ATOM   6138 N N   . CYS D 3 88  ? 10.216  54.285 -7.253  1.00 60.94  ? 88  CYS L N   1 
ATOM   6139 C CA  . CYS D 3 88  ? 9.934   53.494 -6.063  1.00 59.40  ? 88  CYS L CA  1 
ATOM   6140 C C   . CYS D 3 88  ? 9.074   52.305 -6.476  1.00 64.87  ? 88  CYS L C   1 
ATOM   6141 O O   . CYS D 3 88  ? 8.251   52.417 -7.387  1.00 68.91  ? 88  CYS L O   1 
ATOM   6142 C CB  . CYS D 3 88  ? 9.237   54.379 -5.025  1.00 65.12  ? 88  CYS L CB  1 
ATOM   6143 S SG  . CYS D 3 88  ? 8.605   53.688 -3.501  1.00 133.89 ? 88  CYS L SG  1 
ATOM   6144 N N   . GLN D 3 89  ? 9.271   51.160 -5.819  1.00 64.29  ? 89  GLN L N   1 
ATOM   6145 C CA  . GLN D 3 89  ? 8.705   49.923 -6.349  1.00 64.38  ? 89  GLN L CA  1 
ATOM   6146 C C   . GLN D 3 89  ? 8.330   48.919 -5.268  1.00 65.69  ? 89  GLN L C   1 
ATOM   6147 O O   . GLN D 3 89  ? 9.130   48.648 -4.371  1.00 74.37  ? 89  GLN L O   1 
ATOM   6148 C CB  . GLN D 3 89  ? 9.689   49.231 -7.273  1.00 67.44  ? 89  GLN L CB  1 
ATOM   6149 C CG  . GLN D 3 89  ? 9.175   47.892 -7.666  1.00 69.69  ? 89  GLN L CG  1 
ATOM   6150 C CD  . GLN D 3 89  ? 10.114  47.128 -8.515  1.00 76.22  ? 89  GLN L CD  1 
ATOM   6151 O OE1 . GLN D 3 89  ? 11.266  47.499 -8.697  1.00 81.13  ? 89  GLN L OE1 1 
ATOM   6152 N NE2 . GLN D 3 89  ? 9.619   46.066 -9.081  1.00 79.49  ? 89  GLN L NE2 1 
ATOM   6153 N N   . GLN D 3 90  ? 7.152   48.302 -5.429  1.00 62.88  ? 90  GLN L N   1 
ATOM   6154 C CA  . GLN D 3 90  ? 6.694   47.177 -4.609  1.00 66.35  ? 90  GLN L CA  1 
ATOM   6155 C C   . GLN D 3 90  ? 7.126   45.874 -5.254  1.00 76.85  ? 90  GLN L C   1 
ATOM   6156 O O   . GLN D 3 90  ? 6.518   45.438 -6.232  1.00 84.71  ? 90  GLN L O   1 
ATOM   6157 C CB  . GLN D 3 90  ? 5.179   47.123 -4.533  1.00 68.78  ? 90  GLN L CB  1 
ATOM   6158 C CG  . GLN D 3 90  ? 4.493   48.340 -4.142  1.00 96.60  ? 90  GLN L CG  1 
ATOM   6159 C CD  . GLN D 3 90  ? 3.029   48.182 -4.411  1.00 140.15 ? 90  GLN L CD  1 
ATOM   6160 O OE1 . GLN D 3 90  ? 2.575   47.086 -4.744  1.00 114.43 ? 90  GLN L OE1 1 
ATOM   6161 N NE2 . GLN D 3 90  ? 2.292   49.285 -4.376  1.00 186.94 ? 90  GLN L NE2 1 
ATOM   6162 N N   . TYR D 3 91  ? 8.110   45.202 -4.681  1.00 82.84  ? 91  TYR L N   1 
ATOM   6163 C CA  . TYR D 3 91  ? 8.172   43.775 -4.958  1.00 81.99  ? 91  TYR L CA  1 
ATOM   6164 C C   . TYR D 3 91  ? 7.558   42.977 -3.828  1.00 83.05  ? 91  TYR L C   1 
ATOM   6165 O O   . TYR D 3 91  ? 8.016   41.892 -3.469  1.00 87.60  ? 91  TYR L O   1 
ATOM   6166 C CB  . TYR D 3 91  ? 9.594   43.322 -5.267  1.00 80.93  ? 91  TYR L CB  1 
ATOM   6167 C CG  . TYR D 3 91  ? 10.665  43.606 -4.252  1.00 73.93  ? 91  TYR L CG  1 
ATOM   6168 C CD1 . TYR D 3 91  ? 11.249  44.858 -4.171  1.00 73.63  ? 91  TYR L CD1 1 
ATOM   6169 C CD2 . TYR D 3 91  ? 11.143  42.602 -3.418  1.00 80.22  ? 91  TYR L CD2 1 
ATOM   6170 C CE1 . TYR D 3 91  ? 12.248  45.117 -3.258  1.00 78.25  ? 91  TYR L CE1 1 
ATOM   6171 C CE2 . TYR D 3 91  ? 12.141  42.850 -2.503  1.00 78.93  ? 91  TYR L CE2 1 
ATOM   6172 C CZ  . TYR D 3 91  ? 12.691  44.108 -2.426  1.00 76.97  ? 91  TYR L CZ  1 
ATOM   6173 O OH  . TYR D 3 91  ? 13.688  44.352 -1.510  1.00 78.11  ? 91  TYR L OH  1 
ATOM   6174 N N   . ASN D 3 92  ? 6.433   43.476 -3.320  1.00 79.86  ? 92  ASN L N   1 
ATOM   6175 C CA  . ASN D 3 92  ? 5.700   42.682 -2.305  1.00 81.06  ? 92  ASN L CA  1 
ATOM   6176 C C   . ASN D 3 92  ? 4.773   41.742 -3.063  1.00 83.81  ? 92  ASN L C   1 
ATOM   6177 O O   . ASN D 3 92  ? 4.996   40.524 -3.010  1.00 88.89  ? 92  ASN L O   1 
ATOM   6178 C CB  . ASN D 3 92  ? 4.872   43.541 -1.356  1.00 75.87  ? 92  ASN L CB  1 
ATOM   6179 C CG  . ASN D 3 92  ? 4.022   42.733 -0.402  1.00 82.22  ? 92  ASN L CG  1 
ATOM   6180 O OD1 . ASN D 3 92  ? 4.452   41.698 0.098   1.00 100.99 ? 92  ASN L OD1 1 
ATOM   6181 N ND2 . ASN D 3 92  ? 2.813   43.202 -0.143  1.00 75.68  ? 92  ASN L ND2 1 
ATOM   6182 N N   . SER D 3 93  ? 3.792   42.301 -3.768  1.00 80.77  ? 93  SER L N   1 
ATOM   6183 C CA  . SER D 3 93  ? 2.801   41.433 -4.446  1.00 84.84  ? 93  SER L CA  1 
ATOM   6184 C C   . SER D 3 93  ? 2.650   41.814 -5.915  1.00 84.51  ? 93  SER L C   1 
ATOM   6185 O O   . SER D 3 93  ? 2.893   42.980 -6.252  1.00 78.35  ? 93  SER L O   1 
ATOM   6186 C CB  . SER D 3 93  ? 1.476   41.497 -3.751  1.00 86.80  ? 93  SER L CB  1 
ATOM   6187 O OG  . SER D 3 93  ? 1.641   41.688 -2.355  1.00 87.02  ? 93  SER L OG  1 
ATOM   6188 N N   . TYR D 3 94  ? 2.251   40.852 -6.744  1.00 90.20  ? 94  TYR L N   1 
ATOM   6189 C CA  . TYR D 3 94  ? 2.006   41.124 -8.179  1.00 97.11  ? 94  TYR L CA  1 
ATOM   6190 C C   . TYR D 3 94  ? 0.587   41.674 -8.328  1.00 100.07 ? 94  TYR L C   1 
ATOM   6191 O O   . TYR D 3 94  ? -0.287  41.247 -7.559  1.00 103.87 ? 94  TYR L O   1 
ATOM   6192 C CB  . TYR D 3 94  ? 2.184   39.833 -8.979  1.00 95.51  ? 94  TYR L CB  1 
ATOM   6193 C CG  . TYR D 3 94  ? 3.561   39.230 -8.889  1.00 96.95  ? 94  TYR L CG  1 
ATOM   6194 C CD1 . TYR D 3 94  ? 4.685   39.967 -9.218  1.00 100.67 ? 94  TYR L CD1 1 
ATOM   6195 C CD2 . TYR D 3 94  ? 3.742   37.924 -8.472  1.00 106.93 ? 94  TYR L CD2 1 
ATOM   6196 C CE1 . TYR D 3 94  ? 5.954   39.421 -9.138  1.00 111.68 ? 94  TYR L CE1 1 
ATOM   6197 C CE2 . TYR D 3 94  ? 5.003   37.363 -8.387  1.00 127.89 ? 94  TYR L CE2 1 
ATOM   6198 C CZ  . TYR D 3 94  ? 6.115   38.116 -8.714  1.00 125.58 ? 94  TYR L CZ  1 
ATOM   6199 O OH  . TYR D 3 94  ? 7.370   37.569 -8.626  1.00 129.87 ? 94  TYR L OH  1 
ATOM   6200 N N   . PRO D 3 95  ? 0.304   42.593 -9.274  1.00 87.89  ? 95  PRO L N   1 
ATOM   6201 C CA  . PRO D 3 95  ? 1.298   43.056 -10.221 1.00 78.62  ? 95  PRO L CA  1 
ATOM   6202 C C   . PRO D 3 95  ? 2.267   44.047 -9.579  1.00 78.84  ? 95  PRO L C   1 
ATOM   6203 O O   . PRO D 3 95  ? 1.882   44.759 -8.689  1.00 80.47  ? 95  PRO L O   1 
ATOM   6204 C CB  . PRO D 3 95  ? 0.465   43.779 -11.275 1.00 84.54  ? 95  PRO L CB  1 
ATOM   6205 C CG  . PRO D 3 95  ? -0.737  44.280 -10.517 1.00 98.30  ? 95  PRO L CG  1 
ATOM   6206 C CD  . PRO D 3 95  ? -1.005  43.210 -9.481  1.00 102.46 ? 95  PRO L CD  1 
ATOM   6207 N N   . TRP D 3 96  ? 3.513   44.030 -10.040 1.00 83.96  ? 96  TRP L N   1 
ATOM   6208 C CA  . TRP D 3 96  ? 4.524   44.966 -9.496  1.00 84.06  ? 96  TRP L CA  1 
ATOM   6209 C C   . TRP D 3 96  ? 4.133   46.373 -9.917  1.00 83.36  ? 96  TRP L C   1 
ATOM   6210 O O   . TRP D 3 96  ? 3.542   46.525 -10.993 1.00 86.41  ? 96  TRP L O   1 
ATOM   6211 C CB  . TRP D 3 96  ? 5.935   44.602 -9.955  1.00 80.60  ? 96  TRP L CB  1 
ATOM   6212 C CG  . TRP D 3 96  ? 6.573   43.537 -9.123  1.00 85.07  ? 96  TRP L CG  1 
ATOM   6213 C CD1 . TRP D 3 96  ? 6.037   42.912 -8.036  1.00 104.31 ? 96  TRP L CD1 1 
ATOM   6214 C CD2 . TRP D 3 96  ? 7.877   42.965 -9.312  1.00 89.02  ? 96  TRP L CD2 1 
ATOM   6215 N NE1 . TRP D 3 96  ? 6.919   41.994 -7.534  1.00 95.28  ? 96  TRP L NE1 1 
ATOM   6216 C CE2 . TRP D 3 96  ? 8.055   42.002 -8.298  1.00 89.23  ? 96  TRP L CE2 1 
ATOM   6217 C CE3 . TRP D 3 96  ? 8.906   43.168 -10.236 1.00 87.96  ? 96  TRP L CE3 1 
ATOM   6218 C CZ2 . TRP D 3 96  ? 9.220   41.249 -8.187  1.00 94.90  ? 96  TRP L CZ2 1 
ATOM   6219 C CZ3 . TRP D 3 96  ? 10.060  42.428 -10.121 1.00 79.81  ? 96  TRP L CZ3 1 
ATOM   6220 C CH2 . TRP D 3 96  ? 10.211  41.482 -9.111  1.00 87.48  ? 96  TRP L CH2 1 
ATOM   6221 N N   . THR D 3 97  ? 4.481   47.358 -9.109  1.00 80.88  ? 97  THR L N   1 
ATOM   6222 C CA  . THR D 3 97  ? 4.045   48.722 -9.347  1.00 78.71  ? 97  THR L CA  1 
ATOM   6223 C C   . THR D 3 97  ? 5.181   49.686 -9.052  1.00 76.74  ? 97  THR L C   1 
ATOM   6224 O O   . THR D 3 97  ? 6.087   49.382 -8.273  1.00 83.01  ? 97  THR L O   1 
ATOM   6225 C CB  . THR D 3 97  ? 2.846   49.083 -8.475  1.00 93.72  ? 97  THR L CB  1 
ATOM   6226 O OG1 . THR D 3 97  ? 3.244   49.043 -7.106  1.00 98.40  ? 97  THR L OG1 1 
ATOM   6227 C CG2 . THR D 3 97  ? 1.714   48.099 -8.689  1.00 100.13 ? 97  THR L CG2 1 
ATOM   6228 N N   . PHE D 3 98  ? 5.112   50.859 -9.671  1.00 75.23  ? 98  PHE L N   1 
ATOM   6229 C CA  . PHE D 3 98  ? 6.112   51.894 -9.487  1.00 73.99  ? 98  PHE L CA  1 
ATOM   6230 C C   . PHE D 3 98  ? 5.456   53.194 -9.049  1.00 69.57  ? 98  PHE L C   1 
ATOM   6231 O O   . PHE D 3 98  ? 4.254   53.403 -9.230  1.00 73.09  ? 98  PHE L O   1 
ATOM   6232 C CB  . PHE D 3 98  ? 6.913   52.132 -10.773 1.00 77.13  ? 98  PHE L CB  1 
ATOM   6233 C CG  . PHE D 3 98  ? 7.893   51.046 -11.080 1.00 70.36  ? 98  PHE L CG  1 
ATOM   6234 C CD1 . PHE D 3 98  ? 9.187   51.106 -10.593 1.00 69.58  ? 98  PHE L CD1 1 
ATOM   6235 C CD2 . PHE D 3 98  ? 7.521   49.962 -11.853 1.00 70.09  ? 98  PHE L CD2 1 
ATOM   6236 C CE1 . PHE D 3 98  ? 10.093  50.104 -10.875 1.00 75.59  ? 98  PHE L CE1 1 
ATOM   6237 C CE2 . PHE D 3 98  ? 8.421   48.957 -12.139 1.00 70.34  ? 98  PHE L CE2 1 
ATOM   6238 C CZ  . PHE D 3 98  ? 9.709   49.028 -11.650 1.00 74.46  ? 98  PHE L CZ  1 
ATOM   6239 N N   . GLY D 3 99  ? 6.266   54.065 -8.464  1.00 62.84  ? 99  GLY L N   1 
ATOM   6240 C CA  . GLY D 3 99  ? 5.825   55.413 -8.202  1.00 70.95  ? 99  GLY L CA  1 
ATOM   6241 C C   . GLY D 3 99  ? 5.805   56.237 -9.473  1.00 74.07  ? 99  GLY L C   1 
ATOM   6242 O O   . GLY D 3 99  ? 6.326   55.852 -10.521 1.00 68.81  ? 99  GLY L O   1 
ATOM   6243 N N   . GLN D 3 100 ? 5.175   57.407 -9.376  1.00 71.62  ? 100 GLN L N   1 
ATOM   6244 C CA  . GLN D 3 100 ? 5.158   58.326 -10.506 1.00 70.96  ? 100 GLN L CA  1 
ATOM   6245 C C   . GLN D 3 100 ? 6.515   58.967 -10.757 1.00 65.89  ? 100 GLN L C   1 
ATOM   6246 O O   . GLN D 3 100 ? 6.672   59.662 -11.766 1.00 71.13  ? 100 GLN L O   1 
ATOM   6247 C CB  . GLN D 3 100 ? 4.107   59.415 -10.287 1.00 87.58  ? 100 GLN L CB  1 
ATOM   6248 C CG  . GLN D 3 100 ? 4.464   60.401 -9.188  1.00 93.13  ? 100 GLN L CG  1 
ATOM   6249 C CD  . GLN D 3 100 ? 3.750   60.107 -7.885  1.00 129.96 ? 100 GLN L CD  1 
ATOM   6250 O OE1 . GLN D 3 100 ? 3.761   58.976 -7.395  1.00 118.93 ? 100 GLN L OE1 1 
ATOM   6251 N NE2 . GLN D 3 100 ? 3.117   61.127 -7.317  1.00 184.38 ? 100 GLN L NE2 1 
ATOM   6252 N N   . GLY D 3 101 ? 7.487   58.755 -9.874  1.00 62.43  ? 101 GLY L N   1 
ATOM   6253 C CA  . GLY D 3 101 ? 8.809   59.320 -10.049 1.00 60.24  ? 101 GLY L CA  1 
ATOM   6254 C C   . GLY D 3 101 ? 8.900   60.755 -9.583  1.00 59.65  ? 101 GLY L C   1 
ATOM   6255 O O   . GLY D 3 101 ? 7.938   61.515 -9.710  1.00 69.06  ? 101 GLY L O   1 
ATOM   6256 N N   . THR D 3 102 ? 10.044  61.138 -9.025  1.00 61.70  ? 102 THR L N   1 
ATOM   6257 C CA  . THR D 3 102 ? 10.313  62.518 -8.643  1.00 71.87  ? 102 THR L CA  1 
ATOM   6258 C C   . THR D 3 102 ? 11.580  63.006 -9.328  1.00 68.17  ? 102 THR L C   1 
ATOM   6259 O O   . THR D 3 102 ? 12.604  62.320 -9.314  1.00 75.53  ? 102 THR L O   1 
ATOM   6260 C CB  . THR D 3 102 ? 10.462  62.678 -7.122  1.00 71.76  ? 102 THR L CB  1 
ATOM   6261 O OG1 . THR D 3 102 ? 11.783  62.294 -6.718  1.00 68.59  ? 102 THR L OG1 1 
ATOM   6262 C CG2 . THR D 3 102 ? 9.414   61.874 -6.373  1.00 68.19  ? 102 THR L CG2 1 
ATOM   6263 N N   . LYS D 3 103 ? 11.508  64.189 -9.930  1.00 67.46  ? 103 LYS L N   1 
ATOM   6264 C CA  . LYS D 3 103 ? 12.629  64.754 -10.672 1.00 72.73  ? 103 LYS L CA  1 
ATOM   6265 C C   . LYS D 3 103 ? 13.443  65.646 -9.747  1.00 77.17  ? 103 LYS L C   1 
ATOM   6266 O O   . LYS D 3 103 ? 12.999  66.737 -9.373  1.00 85.73  ? 103 LYS L O   1 
ATOM   6267 C CB  . LYS D 3 103 ? 12.149  65.534 -11.893 1.00 87.79  ? 103 LYS L CB  1 
ATOM   6268 C CG  . LYS D 3 103 ? 11.355  64.708 -12.880 1.00 109.79 ? 103 LYS L CG  1 
ATOM   6269 C CD  . LYS D 3 103 ? 10.781  65.586 -13.976 1.00 118.85 ? 103 LYS L CD  1 
ATOM   6270 C CE  . LYS D 3 103 ? 9.998   64.768 -14.987 1.00 128.88 ? 103 LYS L CE  1 
ATOM   6271 N NZ  . LYS D 3 103 ? 9.639   65.566 -16.194 1.00 117.25 ? 103 LYS L NZ  1 
ATOM   6272 N N   . VAL D 3 104 ? 14.636  65.189 -9.386  1.00 72.19  ? 104 VAL L N   1 
ATOM   6273 C CA  . VAL D 3 104 ? 15.561  65.994 -8.602  1.00 74.55  ? 104 VAL L CA  1 
ATOM   6274 C C   . VAL D 3 104 ? 16.476  66.748 -9.557  1.00 84.56  ? 104 VAL L C   1 
ATOM   6275 O O   . VAL D 3 104 ? 17.244  66.134 -10.317 1.00 94.60  ? 104 VAL L O   1 
ATOM   6276 C CB  . VAL D 3 104 ? 16.370  65.135 -7.623  1.00 71.76  ? 104 VAL L CB  1 
ATOM   6277 C CG1 . VAL D 3 104 ? 17.449  65.982 -6.973  1.00 81.34  ? 104 VAL L CG1 1 
ATOM   6278 C CG2 . VAL D 3 104 ? 15.453  64.540 -6.571  1.00 76.07  ? 104 VAL L CG2 1 
ATOM   6279 N N   . GLU D 3 105 ? 16.364  68.078 -9.513  1.00 75.72  ? 105 GLU L N   1 
ATOM   6280 C CA  . GLU D 3 105 ? 17.139  69.069 -10.245 1.00 77.44  ? 105 GLU L CA  1 
ATOM   6281 C C   . GLU D 3 105 ? 18.052  69.800 -9.269  1.00 74.59  ? 105 GLU L C   1 
ATOM   6282 O O   . GLU D 3 105 ? 17.983  69.598 -8.055  1.00 82.71  ? 105 GLU L O   1 
ATOM   6283 C CB  . GLU D 3 105 ? 16.204  70.064 -10.944 1.00 87.31  ? 105 GLU L CB  1 
ATOM   6284 C CG  . GLU D 3 105 ? 15.298  69.413 -11.971 1.00 100.06 ? 105 GLU L CG  1 
ATOM   6285 C CD  . GLU D 3 105 ? 14.785  70.388 -13.010 1.00 116.34 ? 105 GLU L CD  1 
ATOM   6286 O OE1 . GLU D 3 105 ? 14.086  71.351 -12.625 1.00 123.87 ? 105 GLU L OE1 1 
ATOM   6287 O OE2 . GLU D 3 105 ? 15.075  70.190 -14.209 1.00 123.46 ? 105 GLU L OE2 1 
ATOM   6288 N N   . ILE D 3 106 ? 18.902  70.678 -9.799  1.00 77.36  ? 106 ILE L N   1 
ATOM   6289 C CA  . ILE D 3 106 ? 19.999  71.254 -9.025  1.00 81.92  ? 106 ILE L CA  1 
ATOM   6290 C C   . ILE D 3 106 ? 20.035  72.764 -9.218  1.00 89.89  ? 106 ILE L C   1 
ATOM   6291 O O   . ILE D 3 106 ? 20.147  73.250 -10.351 1.00 94.64  ? 106 ILE L O   1 
ATOM   6292 C CB  . ILE D 3 106 ? 21.346  70.629 -9.412  1.00 80.37  ? 106 ILE L CB  1 
ATOM   6293 C CG1 . ILE D 3 106 ? 21.292  69.137 -9.117  1.00 82.42  ? 106 ILE L CG1 1 
ATOM   6294 C CG2 . ILE D 3 106 ? 22.483  71.276 -8.641  1.00 82.30  ? 106 ILE L CG2 1 
ATOM   6295 C CD1 . ILE D 3 106 ? 22.433  68.388 -9.662  1.00 82.37  ? 106 ILE L CD1 1 
ATOM   6296 N N   . LYS D 3 107 ? 19.964  73.500 -8.109  1.00 87.68  ? 107 LYS L N   1 
ATOM   6297 C CA  . LYS D 3 107 ? 20.168  74.941 -8.133  1.00 86.16  ? 107 LYS L CA  1 
ATOM   6298 C C   . LYS D 3 107 ? 21.651  75.251 -8.297  1.00 93.74  ? 107 LYS L C   1 
ATOM   6299 O O   . LYS D 3 107 ? 22.511  74.592 -7.703  1.00 91.33  ? 107 LYS L O   1 
ATOM   6300 C CB  . LYS D 3 107 ? 19.634  75.571 -6.846  1.00 86.23  ? 107 LYS L CB  1 
ATOM   6301 C CG  . LYS D 3 107 ? 18.128  75.445 -6.660  1.00 92.68  ? 107 LYS L CG  1 
ATOM   6302 C CD  . LYS D 3 107 ? 17.666  76.159 -5.395  1.00 106.70 ? 107 LYS L CD  1 
ATOM   6303 C CE  . LYS D 3 107 ? 16.159  76.034 -5.203  1.00 140.04 ? 107 LYS L CE  1 
ATOM   6304 N NZ  . LYS D 3 107 ? 15.694  76.545 -3.880  1.00 174.37 ? 107 LYS L NZ  1 
ATOM   6305 N N   . ARG D 3 108 ? 21.949  76.265 -9.106  1.00 99.90  ? 108 ARG L N   1 
ATOM   6306 C CA  . ARG D 3 108 ? 23.318  76.588 -9.472  1.00 99.42  ? 108 ARG L CA  1 
ATOM   6307 C C   . ARG D 3 108 ? 23.483  78.103 -9.535  1.00 101.62 ? 108 ARG L C   1 
ATOM   6308 O O   . ARG D 3 108 ? 22.508  78.851 -9.651  1.00 102.93 ? 108 ARG L O   1 
ATOM   6309 C CB  . ARG D 3 108 ? 23.696  75.946 -10.823 1.00 107.07 ? 108 ARG L CB  1 
ATOM   6310 C CG  . ARG D 3 108 ? 25.029  76.398 -11.393 1.00 108.72 ? 108 ARG L CG  1 
ATOM   6311 C CD  . ARG D 3 108 ? 25.163  76.148 -12.875 1.00 105.63 ? 108 ARG L CD  1 
ATOM   6312 N NE  . ARG D 3 108 ? 26.420  76.695 -13.374 1.00 101.84 ? 108 ARG L NE  1 
ATOM   6313 C CZ  . ARG D 3 108 ? 27.502  75.978 -13.648 1.00 128.10 ? 108 ARG L CZ  1 
ATOM   6314 N NH1 . ARG D 3 108 ? 27.524  74.666 -13.483 1.00 175.21 ? 108 ARG L NH1 1 
ATOM   6315 N NH2 . ARG D 3 108 ? 28.593  76.595 -14.094 1.00 137.32 ? 108 ARG L NH2 1 
ATOM   6316 N N   . THR D 3 109 ? 24.736  78.546 -9.417  1.00 101.03 ? 109 THR L N   1 
ATOM   6317 C CA  . THR D 3 109 ? 25.111  79.903 -9.793  1.00 101.24 ? 109 THR L CA  1 
ATOM   6318 C C   . THR D 3 109 ? 24.572  80.242 -11.177 1.00 105.16 ? 109 THR L C   1 
ATOM   6319 O O   . THR D 3 109 ? 24.590  79.411 -12.088 1.00 108.76 ? 109 THR L O   1 
ATOM   6320 C CB  . THR D 3 109 ? 26.634  80.047 -9.789  1.00 100.70 ? 109 THR L CB  1 
ATOM   6321 O OG1 . THR D 3 109 ? 27.206  79.105 -10.706 1.00 103.94 ? 109 THR L OG1 1 
ATOM   6322 C CG2 . THR D 3 109 ? 27.192  79.792 -8.401  1.00 104.52 ? 109 THR L CG2 1 
ATOM   6323 N N   . VAL D 3 110 ? 24.093  81.479 -11.332 1.00 101.84 ? 110 VAL L N   1 
ATOM   6324 C CA  . VAL D 3 110 ? 23.594  81.915 -12.628 1.00 101.41 ? 110 VAL L CA  1 
ATOM   6325 C C   . VAL D 3 110 ? 24.729  81.876 -13.641 1.00 98.81  ? 110 VAL L C   1 
ATOM   6326 O O   . VAL D 3 110 ? 25.864  82.276 -13.349 1.00 104.50 ? 110 VAL L O   1 
ATOM   6327 C CB  . VAL D 3 110 ? 22.978  83.319 -12.520 1.00 111.59 ? 110 VAL L CB  1 
ATOM   6328 C CG1 . VAL D 3 110 ? 22.886  83.976 -13.891 1.00 109.40 ? 110 VAL L CG1 1 
ATOM   6329 C CG2 . VAL D 3 110 ? 21.605  83.241 -11.874 1.00 118.12 ? 110 VAL L CG2 1 
ATOM   6330 N N   . ALA D 3 111 ? 24.432  81.369 -14.836 1.00 97.81  ? 111 ALA L N   1 
ATOM   6331 C CA  . ALA D 3 111 ? 25.422  81.242 -15.897 1.00 100.55 ? 111 ALA L CA  1 
ATOM   6332 C C   . ALA D 3 111 ? 24.917  81.948 -17.145 1.00 94.42  ? 111 ALA L C   1 
ATOM   6333 O O   . ALA D 3 111 ? 23.781  81.722 -17.572 1.00 93.38  ? 111 ALA L O   1 
ATOM   6334 C CB  . ALA D 3 111 ? 25.721  79.772 -16.203 1.00 109.40 ? 111 ALA L CB  1 
ATOM   6335 N N   . ALA D 3 112 ? 25.758  82.806 -17.723 1.00 103.79 ? 112 ALA L N   1 
ATOM   6336 C CA  . ALA D 3 112 ? 25.391  83.447 -18.978 1.00 105.03 ? 112 ALA L CA  1 
ATOM   6337 C C   . ALA D 3 112 ? 25.619  82.485 -20.141 1.00 105.49 ? 112 ALA L C   1 
ATOM   6338 O O   . ALA D 3 112 ? 26.634  81.782 -20.175 1.00 111.04 ? 112 ALA L O   1 
ATOM   6339 C CB  . ALA D 3 112 ? 26.204  84.721 -19.194 1.00 115.16 ? 112 ALA L CB  1 
ATOM   6340 N N   . PRO D 3 113 ? 24.700  82.429 -21.101 1.00 100.42 ? 113 PRO L N   1 
ATOM   6341 C CA  . PRO D 3 113 ? 24.892  81.535 -22.245 1.00 103.56 ? 113 PRO L CA  1 
ATOM   6342 C C   . PRO D 3 113 ? 26.000  82.041 -23.154 1.00 107.15 ? 113 PRO L C   1 
ATOM   6343 O O   . PRO D 3 113 ? 26.408  83.204 -23.104 1.00 110.28 ? 113 PRO L O   1 
ATOM   6344 C CB  . PRO D 3 113 ? 23.538  81.570 -22.961 1.00 101.19 ? 113 PRO L CB  1 
ATOM   6345 C CG  . PRO D 3 113 ? 22.954  82.889 -22.591 1.00 96.80  ? 113 PRO L CG  1 
ATOM   6346 C CD  . PRO D 3 113 ? 23.468  83.230 -21.217 1.00 95.30  ? 113 PRO L CD  1 
ATOM   6347 N N   . SER D 3 114 ? 26.492  81.140 -23.996 1.00 105.99 ? 114 SER L N   1 
ATOM   6348 C CA  . SER D 3 114 ? 27.310  81.528 -25.136 1.00 105.80 ? 114 SER L CA  1 
ATOM   6349 C C   . SER D 3 114 ? 26.516  81.264 -26.409 1.00 112.06 ? 114 SER L C   1 
ATOM   6350 O O   . SER D 3 114 ? 26.000  80.158 -26.606 1.00 109.28 ? 114 SER L O   1 
ATOM   6351 C CB  . SER D 3 114 ? 28.654  80.790 -25.139 1.00 109.46 ? 114 SER L CB  1 
ATOM   6352 O OG  . SER D 3 114 ? 28.508  79.434 -24.753 1.00 120.45 ? 114 SER L OG  1 
ATOM   6353 N N   . VAL D 3 115 ? 26.386  82.293 -27.251 1.00 111.34 ? 115 VAL L N   1 
ATOM   6354 C CA  . VAL D 3 115 ? 25.521  82.244 -28.423 1.00 109.41 ? 115 VAL L CA  1 
ATOM   6355 C C   . VAL D 3 115 ? 26.359  81.934 -29.653 1.00 114.81 ? 115 VAL L C   1 
ATOM   6356 O O   . VAL D 3 115 ? 27.517  82.352 -29.778 1.00 112.67 ? 115 VAL L O   1 
ATOM   6357 C CB  . VAL D 3 115 ? 24.738  83.564 -28.607 1.00 111.49 ? 115 VAL L CB  1 
ATOM   6358 C CG1 . VAL D 3 115 ? 23.773  83.475 -29.795 1.00 111.43 ? 115 VAL L CG1 1 
ATOM   6359 C CG2 . VAL D 3 115 ? 24.001  83.938 -27.335 1.00 108.11 ? 115 VAL L CG2 1 
ATOM   6360 N N   . PHE D 3 116 ? 25.758  81.183 -30.569 1.00 120.18 ? 116 PHE L N   1 
ATOM   6361 C CA  . PHE D 3 116 ? 26.375  80.825 -31.834 1.00 120.17 ? 116 PHE L CA  1 
ATOM   6362 C C   . PHE D 3 116 ? 25.288  80.833 -32.896 1.00 117.10 ? 116 PHE L C   1 
ATOM   6363 O O   . PHE D 3 116 ? 24.149  80.458 -32.613 1.00 117.14 ? 116 PHE L O   1 
ATOM   6364 C CB  . PHE D 3 116 ? 27.024  79.440 -31.753 1.00 113.81 ? 116 PHE L CB  1 
ATOM   6365 C CG  . PHE D 3 116 ? 28.290  79.411 -30.946 1.00 120.04 ? 116 PHE L CG  1 
ATOM   6366 C CD1 . PHE D 3 116 ? 29.500  79.757 -31.519 1.00 126.33 ? 116 PHE L CD1 1 
ATOM   6367 C CD2 . PHE D 3 116 ? 28.268  79.036 -29.611 1.00 116.26 ? 116 PHE L CD2 1 
ATOM   6368 C CE1 . PHE D 3 116 ? 30.664  79.729 -30.778 1.00 127.42 ? 116 PHE L CE1 1 
ATOM   6369 C CE2 . PHE D 3 116 ? 29.429  79.007 -28.865 1.00 113.22 ? 116 PHE L CE2 1 
ATOM   6370 C CZ  . PHE D 3 116 ? 30.629  79.355 -29.451 1.00 124.17 ? 116 PHE L CZ  1 
ATOM   6371 N N   . ILE D 3 117 ? 25.623  81.263 -34.112 1.00 115.86 ? 117 ILE L N   1 
ATOM   6372 C CA  . ILE D 3 117 ? 24.701  81.163 -35.238 1.00 111.76 ? 117 ILE L CA  1 
ATOM   6373 C C   . ILE D 3 117 ? 25.292  80.257 -36.304 1.00 110.27 ? 117 ILE L C   1 
ATOM   6374 O O   . ILE D 3 117 ? 26.490  80.318 -36.607 1.00 109.98 ? 117 ILE L O   1 
ATOM   6375 C CB  . ILE D 3 117 ? 24.330  82.527 -35.851 1.00 109.76 ? 117 ILE L CB  1 
ATOM   6376 C CG1 . ILE D 3 117 ? 23.728  83.437 -34.802 1.00 114.24 ? 117 ILE L CG1 1 
ATOM   6377 C CG2 . ILE D 3 117 ? 23.347  82.364 -37.012 1.00 107.37 ? 117 ILE L CG2 1 
ATOM   6378 C CD1 . ILE D 3 117 ? 23.395  84.737 -35.384 1.00 116.28 ? 117 ILE L CD1 1 
ATOM   6379 N N   . PHE D 3 118 ? 24.432  79.423 -36.874 1.00 106.93 ? 118 PHE L N   1 
ATOM   6380 C CA  . PHE D 3 118 ? 24.789  78.513 -37.944 1.00 104.28 ? 118 PHE L CA  1 
ATOM   6381 C C   . PHE D 3 118 ? 23.935  78.813 -39.165 1.00 110.72 ? 118 PHE L C   1 
ATOM   6382 O O   . PHE D 3 118 ? 22.691  78.744 -39.086 1.00 109.90 ? 118 PHE L O   1 
ATOM   6383 C CB  . PHE D 3 118 ? 24.618  77.073 -37.485 1.00 101.56 ? 118 PHE L CB  1 
ATOM   6384 C CG  . PHE D 3 118 ? 25.617  76.669 -36.448 1.00 102.66 ? 118 PHE L CG  1 
ATOM   6385 C CD1 . PHE D 3 118 ? 26.974  76.719 -36.724 1.00 102.33 ? 118 PHE L CD1 1 
ATOM   6386 C CD2 . PHE D 3 118 ? 25.209  76.309 -35.178 1.00 104.24 ? 118 PHE L CD2 1 
ATOM   6387 C CE1 . PHE D 3 118 ? 27.901  76.367 -35.765 1.00 99.72  ? 118 PHE L CE1 1 
ATOM   6388 C CE2 . PHE D 3 118 ? 26.131  75.957 -34.216 1.00 103.72 ? 118 PHE L CE2 1 
ATOM   6389 C CZ  . PHE D 3 118 ? 27.479  75.987 -34.510 1.00 109.12 ? 118 PHE L CZ  1 
ATOM   6390 N N   . PRO D 3 119 ? 24.566  79.196 -40.271 1.00 112.39 ? 119 PRO L N   1 
ATOM   6391 C CA  . PRO D 3 119 ? 23.849  79.455 -41.515 1.00 108.24 ? 119 PRO L CA  1 
ATOM   6392 C C   . PRO D 3 119 ? 23.369  78.159 -42.141 1.00 101.83 ? 119 PRO L C   1 
ATOM   6393 O O   . PRO D 3 119 ? 23.884  77.077 -41.820 1.00 101.36 ? 119 PRO L O   1 
ATOM   6394 C CB  . PRO D 3 119 ? 24.910  80.139 -42.396 1.00 111.98 ? 119 PRO L CB  1 
ATOM   6395 C CG  . PRO D 3 119 ? 26.049  80.490 -41.463 1.00 113.56 ? 119 PRO L CG  1 
ATOM   6396 C CD  . PRO D 3 119 ? 26.007  79.458 -40.396 1.00 111.64 ? 119 PRO L CD  1 
ATOM   6397 N N   . PRO D 3 120 ? 22.395  78.224 -43.047 1.00 102.69 ? 120 PRO L N   1 
ATOM   6398 C CA  . PRO D 3 120 ? 21.877  76.993 -43.647 1.00 109.09 ? 120 PRO L CA  1 
ATOM   6399 C C   . PRO D 3 120 ? 22.909  76.322 -44.536 1.00 112.55 ? 120 PRO L C   1 
ATOM   6400 O O   . PRO D 3 120 ? 23.761  76.969 -45.151 1.00 112.16 ? 120 PRO L O   1 
ATOM   6401 C CB  . PRO D 3 120 ? 20.665  77.473 -44.451 1.00 108.28 ? 120 PRO L CB  1 
ATOM   6402 C CG  . PRO D 3 120 ? 20.980  78.879 -44.780 1.00 116.65 ? 120 PRO L CG  1 
ATOM   6403 C CD  . PRO D 3 120 ? 21.730  79.421 -43.591 1.00 110.50 ? 120 PRO L CD  1 
ATOM   6404 N N   . SER D 3 121 ? 22.830  74.996 -44.579 1.00 112.65 ? 121 SER L N   1 
ATOM   6405 C CA  . SER D 3 121 ? 23.756  74.195 -45.363 1.00 111.10 ? 121 SER L CA  1 
ATOM   6406 C C   . SER D 3 121 ? 23.396  74.275 -46.838 1.00 113.61 ? 121 SER L C   1 
ATOM   6407 O O   . SER D 3 121 ? 22.218  74.193 -47.203 1.00 118.85 ? 121 SER L O   1 
ATOM   6408 C CB  . SER D 3 121 ? 23.716  72.746 -44.893 1.00 115.35 ? 121 SER L CB  1 
ATOM   6409 O OG  . SER D 3 121 ? 22.396  72.257 -44.995 1.00 107.02 ? 121 SER L OG  1 
ATOM   6410 N N   . ASP D 3 122 ? 24.418  74.415 -47.684 1.00 111.68 ? 122 ASP L N   1 
ATOM   6411 C CA  . ASP D 3 122 ? 24.191  74.576 -49.116 1.00 115.00 ? 122 ASP L CA  1 
ATOM   6412 C C   . ASP D 3 122 ? 23.491  73.361 -49.707 1.00 119.72 ? 122 ASP L C   1 
ATOM   6413 O O   . ASP D 3 122 ? 22.675  73.488 -50.626 1.00 122.17 ? 122 ASP L O   1 
ATOM   6414 C CB  . ASP D 3 122 ? 25.522  74.826 -49.819 1.00 120.22 ? 122 ASP L CB  1 
ATOM   6415 C CG  . ASP D 3 122 ? 26.034  76.235 -49.606 1.00 126.07 ? 122 ASP L CG  1 
ATOM   6416 O OD1 . ASP D 3 122 ? 25.368  77.013 -48.888 1.00 123.92 ? 122 ASP L OD1 1 
ATOM   6417 O OD2 . ASP D 3 122 ? 27.105  76.567 -50.154 1.00 134.27 ? 122 ASP L OD2 1 
ATOM   6418 N N   . GLU D 3 123 ? 23.802  72.174 -49.189 1.00 118.14 ? 123 GLU L N   1 
ATOM   6419 C CA  . GLU D 3 123 ? 23.162  70.951 -49.661 1.00 119.94 ? 123 GLU L CA  1 
ATOM   6420 C C   . GLU D 3 123 ? 21.656  71.008 -49.416 1.00 118.09 ? 123 GLU L C   1 
ATOM   6421 O O   . GLU D 3 123 ? 20.843  70.755 -50.322 1.00 126.65 ? 123 GLU L O   1 
ATOM   6422 C CB  . GLU D 3 123 ? 23.805  69.762 -48.946 1.00 121.45 ? 123 GLU L CB  1 
ATOM   6423 C CG  . GLU D 3 123 ? 25.302  69.661 -49.238 1.00 132.30 ? 123 GLU L CG  1 
ATOM   6424 C CD  . GLU D 3 123 ? 25.900  68.325 -48.865 1.00 151.62 ? 123 GLU L CD  1 
ATOM   6425 O OE1 . GLU D 3 123 ? 25.165  67.316 -48.867 1.00 175.90 ? 123 GLU L OE1 1 
ATOM   6426 O OE2 . GLU D 3 123 ? 27.103  68.290 -48.530 1.00 165.70 ? 123 GLU L OE2 1 
ATOM   6427 N N   . GLN D 3 124 ? 21.268  71.387 -48.196 1.00 119.65 ? 124 GLN L N   1 
ATOM   6428 C CA  . GLN D 3 124 ? 19.859  71.611 -47.886 1.00 124.20 ? 124 GLN L CA  1 
ATOM   6429 C C   . GLN D 3 124 ? 19.258  72.690 -48.780 1.00 124.84 ? 124 GLN L C   1 
ATOM   6430 O O   . GLN D 3 124 ? 18.145  72.534 -49.298 1.00 129.34 ? 124 GLN L O   1 
ATOM   6431 C CB  . GLN D 3 124 ? 19.702  71.996 -46.416 1.00 123.04 ? 124 GLN L CB  1 
ATOM   6432 C CG  . GLN D 3 124 ? 18.273  72.150 -45.957 1.00 124.56 ? 124 GLN L CG  1 
ATOM   6433 C CD  . GLN D 3 124 ? 18.165  73.056 -44.754 1.00 122.14 ? 124 GLN L CD  1 
ATOM   6434 O OE1 . GLN D 3 124 ? 19.087  73.817 -44.458 1.00 118.27 ? 124 GLN L OE1 1 
ATOM   6435 N NE2 . GLN D 3 124 ? 17.043  72.974 -44.045 1.00 123.73 ? 124 GLN L NE2 1 
ATOM   6436 N N   . LEU D 3 125 ? 19.982  73.799 -48.963 1.00 121.14 ? 125 LEU L N   1 
ATOM   6437 C CA  . LEU D 3 125 ? 19.509  74.860 -49.848 1.00 122.07 ? 125 LEU L CA  1 
ATOM   6438 C C   . LEU D 3 125 ? 19.175  74.315 -51.229 1.00 123.72 ? 125 LEU L C   1 
ATOM   6439 O O   . LEU D 3 125 ? 18.165  74.697 -51.831 1.00 121.01 ? 125 LEU L O   1 
ATOM   6440 C CB  . LEU D 3 125 ? 20.560  75.967 -49.951 1.00 114.54 ? 125 LEU L CB  1 
ATOM   6441 C CG  . LEU D 3 125 ? 20.693  76.931 -48.771 1.00 106.61 ? 125 LEU L CG  1 
ATOM   6442 C CD1 . LEU D 3 125 ? 21.971  77.738 -48.900 1.00 110.30 ? 125 LEU L CD1 1 
ATOM   6443 C CD2 . LEU D 3 125 ? 19.492  77.856 -48.704 1.00 113.63 ? 125 LEU L CD2 1 
ATOM   6444 N N   . LYS D 3 126 ? 20.009  73.407 -51.738 1.00 128.45 ? 126 LYS L N   1 
ATOM   6445 C CA  . LYS D 3 126 ? 19.732  72.781 -53.025 1.00 130.82 ? 126 LYS L CA  1 
ATOM   6446 C C   . LYS D 3 126 ? 18.483  71.917 -52.951 1.00 130.37 ? 126 LYS L C   1 
ATOM   6447 O O   . LYS D 3 126 ? 17.708  71.849 -53.914 1.00 131.80 ? 126 LYS L O   1 
ATOM   6448 C CB  . LYS D 3 126 ? 20.934  71.952 -53.474 1.00 127.95 ? 126 LYS L CB  1 
ATOM   6449 C CG  . LYS D 3 126 ? 22.181  72.779 -53.725 1.00 134.18 ? 126 LYS L CG  1 
ATOM   6450 C CD  . LYS D 3 126 ? 23.231  71.997 -54.489 1.00 137.87 ? 126 LYS L CD  1 
ATOM   6451 C CE  . LYS D 3 126 ? 24.331  72.922 -54.984 1.00 146.98 ? 126 LYS L CE  1 
ATOM   6452 N NZ  . LYS D 3 126 ? 25.335  72.214 -55.824 1.00 145.20 ? 126 LYS L NZ  1 
ATOM   6453 N N   . SER D 3 127 ? 18.265  71.248 -51.814 1.00 133.15 ? 127 SER L N   1 
ATOM   6454 C CA  . SER D 3 127 ? 17.040  70.465 -51.672 1.00 136.99 ? 127 SER L CA  1 
ATOM   6455 C C   . SER D 3 127 ? 15.787  71.335 -51.721 1.00 132.87 ? 127 SER L C   1 
ATOM   6456 O O   . SER D 3 127 ? 14.719  70.842 -52.100 1.00 134.83 ? 127 SER L O   1 
ATOM   6457 C CB  . SER D 3 127 ? 17.059  69.655 -50.374 1.00 140.43 ? 127 SER L CB  1 
ATOM   6458 O OG  . SER D 3 127 ? 17.170  70.498 -49.242 1.00 137.56 ? 127 SER L OG  1 
ATOM   6459 N N   . GLY D 3 128 ? 15.886  72.606 -51.358 1.00 129.28 ? 128 GLY L N   1 
ATOM   6460 C CA  . GLY D 3 128 ? 14.773  73.522 -51.445 1.00 130.64 ? 128 GLY L CA  1 
ATOM   6461 C C   . GLY D 3 128 ? 14.268  74.108 -50.136 1.00 129.53 ? 128 GLY L C   1 
ATOM   6462 O O   . GLY D 3 128 ? 13.171  74.682 -50.124 1.00 132.10 ? 128 GLY L O   1 
ATOM   6463 N N   . THR D 3 129 ? 15.015  73.975 -49.045 1.00 132.12 ? 129 THR L N   1 
ATOM   6464 C CA  . THR D 3 129 ? 14.672  74.566 -47.760 1.00 120.61 ? 129 THR L CA  1 
ATOM   6465 C C   . THR D 3 129 ? 15.917  75.232 -47.182 1.00 121.31 ? 129 THR L C   1 
ATOM   6466 O O   . THR D 3 129 ? 17.000  75.189 -47.773 1.00 121.66 ? 129 THR L O   1 
ATOM   6467 C CB  . THR D 3 129 ? 14.102  73.515 -46.795 1.00 118.85 ? 129 THR L CB  1 
ATOM   6468 O OG1 . THR D 3 129 ? 15.093  72.515 -46.530 1.00 123.02 ? 129 THR L OG1 1 
ATOM   6469 C CG2 . THR D 3 129 ? 12.859  72.854 -47.381 1.00 113.94 ? 129 THR L CG2 1 
ATOM   6470 N N   . ALA D 3 130 ? 15.759  75.863 -46.020 1.00 112.51 ? 130 ALA L N   1 
ATOM   6471 C CA  . ALA D 3 130 ? 16.874  76.530 -45.361 1.00 111.47 ? 130 ALA L CA  1 
ATOM   6472 C C   . ALA D 3 130 ? 16.567  76.681 -43.878 1.00 109.40 ? 130 ALA L C   1 
ATOM   6473 O O   . ALA D 3 130 ? 15.423  76.940 -43.498 1.00 119.02 ? 130 ALA L O   1 
ATOM   6474 C CB  . ALA D 3 130 ? 17.160  77.903 -45.979 1.00 117.47 ? 130 ALA L CB  1 
ATOM   6475 N N   . SER D 3 131 ? 17.600  76.533 -43.052 1.00 103.11 ? 131 SER L N   1 
ATOM   6476 C CA  . SER D 3 131 ? 17.454  76.608 -41.605 1.00 96.76  ? 131 SER L CA  1 
ATOM   6477 C C   . SER D 3 131 ? 18.636  77.347 -40.998 1.00 93.82  ? 131 SER L C   1 
ATOM   6478 O O   . SER D 3 131 ? 19.792  77.039 -41.300 1.00 99.88  ? 131 SER L O   1 
ATOM   6479 C CB  . SER D 3 131 ? 17.340  75.211 -40.986 1.00 98.42  ? 131 SER L CB  1 
ATOM   6480 O OG  . SER D 3 131 ? 16.200  74.530 -41.477 1.00 91.14  ? 131 SER L OG  1 
ATOM   6481 N N   . VAL D 3 132 ? 18.337  78.313 -40.136 1.00 92.85  ? 132 VAL L N   1 
ATOM   6482 C CA  . VAL D 3 132 ? 19.342  79.032 -39.360 1.00 95.05  ? 132 VAL L CA  1 
ATOM   6483 C C   . VAL D 3 132 ? 19.200  78.588 -37.912 1.00 98.87  ? 132 VAL L C   1 
ATOM   6484 O O   . VAL D 3 132 ? 18.083  78.332 -37.446 1.00 105.13 ? 132 VAL L O   1 
ATOM   6485 C CB  . VAL D 3 132 ? 19.172  80.559 -39.491 1.00 97.59  ? 132 VAL L CB  1 
ATOM   6486 C CG1 . VAL D 3 132 ? 20.389  81.289 -38.931 1.00 96.57  ? 132 VAL L CG1 1 
ATOM   6487 C CG2 . VAL D 3 132 ? 18.910  80.942 -40.935 1.00 93.71  ? 132 VAL L CG2 1 
ATOM   6488 N N   . VAL D 3 133 ? 20.317  78.484 -37.194 1.00 98.22  ? 133 VAL L N   1 
ATOM   6489 C CA  . VAL D 3 133 ? 20.251  77.976 -35.823 1.00 93.99  ? 133 VAL L CA  1 
ATOM   6490 C C   . VAL D 3 133 ? 21.002  78.890 -34.864 1.00 98.54  ? 133 VAL L C   1 
ATOM   6491 O O   . VAL D 3 133 ? 22.188  79.170 -35.069 1.00 103.07 ? 133 VAL L O   1 
ATOM   6492 C CB  . VAL D 3 133 ? 20.789  76.537 -35.716 1.00 93.05  ? 133 VAL L CB  1 
ATOM   6493 C CG1 . VAL D 3 133 ? 20.831  76.105 -34.260 1.00 100.74 ? 133 VAL L CG1 1 
ATOM   6494 C CG2 . VAL D 3 133 ? 19.917  75.582 -36.514 1.00 89.11  ? 133 VAL L CG2 1 
ATOM   6495 N N   . CYS D 3 134 ? 20.310  79.339 -33.810 1.00 104.04 ? 134 CYS L N   1 
ATOM   6496 C CA  . CYS D 3 134 ? 20.966  79.867 -32.618 1.00 104.98 ? 134 CYS L CA  1 
ATOM   6497 C C   . CYS D 3 134 ? 21.234  78.726 -31.650 1.00 101.80 ? 134 CYS L C   1 
ATOM   6498 O O   . CYS D 3 134 ? 20.326  77.955 -31.316 1.00 99.97  ? 134 CYS L O   1 
ATOM   6499 C CB  . CYS D 3 134 ? 20.138  80.931 -31.888 1.00 106.01 ? 134 CYS L CB  1 
ATOM   6500 S SG  . CYS D 3 134 ? 19.173  82.102 -32.838 1.00 141.82 ? 134 CYS L SG  1 
ATOM   6501 N N   . LEU D 3 135 ? 22.476  78.639 -31.196 1.00 99.16  ? 135 LEU L N   1 
ATOM   6502 C CA  . LEU D 3 135 ? 22.897  77.758 -30.118 1.00 96.35  ? 135 LEU L CA  1 
ATOM   6503 C C   . LEU D 3 135 ? 23.188  78.620 -28.899 1.00 98.63  ? 135 LEU L C   1 
ATOM   6504 O O   . LEU D 3 135 ? 24.103  79.451 -28.928 1.00 100.14 ? 135 LEU L O   1 
ATOM   6505 C CB  . LEU D 3 135 ? 24.139  76.965 -30.503 1.00 99.78  ? 135 LEU L CB  1 
ATOM   6506 C CG  . LEU D 3 135 ? 24.736  76.208 -29.313 1.00 99.18  ? 135 LEU L CG  1 
ATOM   6507 C CD1 . LEU D 3 135 ? 24.030  74.872 -29.088 1.00 90.95  ? 135 LEU L CD1 1 
ATOM   6508 C CD2 . LEU D 3 135 ? 26.241  76.052 -29.453 1.00 105.96 ? 135 LEU L CD2 1 
ATOM   6509 N N   . LEU D 3 136 ? 22.408  78.433 -27.840 1.00 99.46  ? 136 LEU L N   1 
ATOM   6510 C CA  . LEU D 3 136 ? 22.713  78.992 -26.530 1.00 94.89  ? 136 LEU L CA  1 
ATOM   6511 C C   . LEU D 3 136 ? 23.361  77.904 -25.690 1.00 96.68  ? 136 LEU L C   1 
ATOM   6512 O O   . LEU D 3 136 ? 22.727  76.884 -25.407 1.00 97.20  ? 136 LEU L O   1 
ATOM   6513 C CB  . LEU D 3 136 ? 21.460  79.557 -25.864 1.00 92.22  ? 136 LEU L CB  1 
ATOM   6514 C CG  . LEU D 3 136 ? 20.913  80.882 -26.395 1.00 95.53  ? 136 LEU L CG  1 
ATOM   6515 C CD1 . LEU D 3 136 ? 20.162  80.687 -27.706 1.00 97.67  ? 136 LEU L CD1 1 
ATOM   6516 C CD2 . LEU D 3 136 ? 20.005  81.509 -25.352 1.00 105.12 ? 136 LEU L CD2 1 
ATOM   6517 N N   . ASN D 3 137 ? 24.630  78.092 -25.330 1.00 96.10  ? 137 ASN L N   1 
ATOM   6518 C CA  . ASN D 3 137 ? 25.342  76.985 -24.643 1.00 98.12  ? 137 ASN L CA  1 
ATOM   6519 C C   . ASN D 3 137 ? 25.577  77.192 -23.153 1.00 102.21 ? 137 ASN L C   1 
ATOM   6520 O O   . ASN D 3 137 ? 25.823  78.342 -22.768 1.00 107.52 ? 137 ASN L O   1 
ATOM   6521 C CB  . ASN D 3 137 ? 26.717  76.795 -25.280 1.00 104.19 ? 137 ASN L CB  1 
ATOM   6522 C CG  . ASN D 3 137 ? 27.384  75.504 -24.866 1.00 103.49 ? 137 ASN L CG  1 
ATOM   6523 O OD1 . ASN D 3 137 ? 26.708  74.513 -24.602 1.00 105.83 ? 137 ASN L OD1 1 
ATOM   6524 N ND2 . ASN D 3 137 ? 28.705  75.504 -24.813 1.00 104.79 ? 137 ASN L ND2 1 
ATOM   6525 N N   . ASN D 3 138 ? 25.404  76.141 -22.351 1.00 98.68  ? 138 ASN L N   1 
ATOM   6526 C CA  . ASN D 3 138 ? 25.709  76.195 -20.896 1.00 101.51 ? 138 ASN L CA  1 
ATOM   6527 C C   . ASN D 3 138 ? 25.243  77.327 -19.974 1.00 103.49 ? 138 ASN L C   1 
ATOM   6528 O O   . ASN D 3 138 ? 26.098  77.908 -19.282 1.00 105.96 ? 138 ASN L O   1 
ATOM   6529 C CB  . ASN D 3 138 ? 27.209  76.010 -20.666 1.00 108.40 ? 138 ASN L CB  1 
ATOM   6530 C CG  . ASN D 3 138 ? 27.706  74.668 -21.157 1.00 106.38 ? 138 ASN L CG  1 
ATOM   6531 O OD1 . ASN D 3 138 ? 28.564  74.600 -22.034 1.00 104.61 ? 138 ASN L OD1 1 
ATOM   6532 N ND2 . ASN D 3 138 ? 27.167  73.595 -20.604 1.00 101.87 ? 138 ASN L ND2 1 
ATOM   6533 N N   . PHE D 3 139 ? 23.934  77.585 -19.918 1.00 97.88  ? 139 PHE L N   1 
ATOM   6534 C CA  . PHE D 3 139 ? 23.382  78.588 -18.970 1.00 93.03  ? 139 PHE L CA  1 
ATOM   6535 C C   . PHE D 3 139 ? 22.496  78.027 -17.860 1.00 94.06  ? 139 PHE L C   1 
ATOM   6536 O O   . PHE D 3 139 ? 21.730  77.102 -18.161 1.00 103.17 ? 139 PHE L O   1 
ATOM   6537 C CB  . PHE D 3 139 ? 22.587  79.519 -19.883 1.00 97.38  ? 139 PHE L CB  1 
ATOM   6538 C CG  . PHE D 3 139 ? 21.393  78.906 -20.562 1.00 92.81  ? 139 PHE L CG  1 
ATOM   6539 C CD1 . PHE D 3 139 ? 21.547  78.026 -21.619 1.00 92.19  ? 139 PHE L CD1 1 
ATOM   6540 C CD2 . PHE D 3 139 ? 20.111  79.202 -20.133 1.00 99.91  ? 139 PHE L CD2 1 
ATOM   6541 C CE1 . PHE D 3 139 ? 20.444  77.464 -22.238 1.00 92.21  ? 139 PHE L CE1 1 
ATOM   6542 C CE2 . PHE D 3 139 ? 19.009  78.636 -20.750 1.00 105.69 ? 139 PHE L CE2 1 
ATOM   6543 C CZ  . PHE D 3 139 ? 19.178  77.767 -21.799 1.00 100.32 ? 139 PHE L CZ  1 
ATOM   6544 N N   . TYR D 3 140 ? 22.584  78.547 -16.633 1.00 96.17  ? 140 TYR L N   1 
ATOM   6545 C CA  . TYR D 3 140 ? 21.806  77.901 -15.538 1.00 107.00 ? 140 TYR L CA  1 
ATOM   6546 C C   . TYR D 3 140 ? 20.332  78.308 -15.568 1.00 112.45 ? 140 TYR L C   1 
ATOM   6547 O O   . TYR D 3 140 ? 19.495  77.417 -15.758 1.00 124.67 ? 140 TYR L O   1 
ATOM   6548 C CB  . TYR D 3 140 ? 22.354  78.158 -14.133 1.00 105.40 ? 140 TYR L CB  1 
ATOM   6549 C CG  . TYR D 3 140 ? 21.362  77.755 -13.074 1.00 105.16 ? 140 TYR L CG  1 
ATOM   6550 C CD1 . TYR D 3 140 ? 20.927  76.445 -12.972 1.00 105.00 ? 140 TYR L CD1 1 
ATOM   6551 C CD2 . TYR D 3 140 ? 20.803  78.690 -12.221 1.00 112.87 ? 140 TYR L CD2 1 
ATOM   6552 C CE1 . TYR D 3 140 ? 19.991  76.066 -12.026 1.00 106.47 ? 140 TYR L CE1 1 
ATOM   6553 C CE2 . TYR D 3 140 ? 19.866  78.329 -11.268 1.00 107.42 ? 140 TYR L CE2 1 
ATOM   6554 C CZ  . TYR D 3 140 ? 19.460  77.011 -11.169 1.00 108.30 ? 140 TYR L CZ  1 
ATOM   6555 O OH  . TYR D 3 140 ? 18.532  76.648 -10.227 1.00 106.55 ? 140 TYR L OH  1 
ATOM   6556 N N   . PRO D 3 141 ? 19.942  79.581 -15.365 1.00 93.96  ? 141 PRO L N   1 
ATOM   6557 C CA  . PRO D 3 141 ? 18.522  79.886 -15.334 1.00 89.65  ? 141 PRO L CA  1 
ATOM   6558 C C   . PRO D 3 141 ? 17.960  79.364 -16.657 1.00 141.35 ? 141 PRO L C   1 
ATOM   6559 O O   . PRO D 3 141 ? 18.201  79.988 -17.658 1.00 155.35 ? 141 PRO L O   1 
ATOM   6560 C CB  . PRO D 3 141 ? 18.497  81.409 -15.291 1.00 94.48  ? 141 PRO L CB  1 
ATOM   6561 C CG  . PRO D 3 141 ? 19.823  81.784 -14.671 1.00 100.05 ? 141 PRO L CG  1 
ATOM   6562 C CD  . PRO D 3 141 ? 20.798  80.754 -15.196 1.00 76.02  ? 141 PRO L CD  1 
ATOM   6563 N N   . ARG D 3 142 ? 17.224  78.254 -16.638 1.00 107.81 ? 142 ARG L N   1 
ATOM   6564 C CA  . ARG D 3 142 ? 16.758  77.654 -17.914 1.00 106.17 ? 142 ARG L CA  1 
ATOM   6565 C C   . ARG D 3 142 ? 15.979  78.705 -18.694 1.00 110.99 ? 142 ARG L C   1 
ATOM   6566 O O   . ARG D 3 142 ? 15.940  78.621 -19.930 1.00 111.20 ? 142 ARG L O   1 
ATOM   6567 C CB  . ARG D 3 142 ? 15.830  76.469 -17.652 1.00 121.67 ? 142 ARG L CB  1 
ATOM   6568 C CG  . ARG D 3 142 ? 15.408  75.722 -18.909 1.00 122.62 ? 142 ARG L CG  1 
ATOM   6569 C CD  . ARG D 3 142 ? 13.984  75.206 -18.824 1.00 126.87 ? 142 ARG L CD  1 
ATOM   6570 N NE  . ARG D 3 142 ? 13.794  74.268 -17.728 1.00 135.71 ? 142 ARG L NE  1 
ATOM   6571 C CZ  . ARG D 3 142 ? 14.400  73.091 -17.632 1.00 163.91 ? 142 ARG L CZ  1 
ATOM   6572 N NH1 . ARG D 3 142 ? 14.691  72.406 -18.723 1.00 173.76 ? 142 ARG L NH1 1 
ATOM   6573 N NH2 . ARG D 3 142 ? 14.700  72.597 -16.444 1.00 180.76 ? 142 ARG L NH2 1 
ATOM   6574 N N   . GLU D 3 143 ? 15.387  79.659 -17.984 1.00 126.45 ? 143 GLU L N   1 
ATOM   6575 C CA  . GLU D 3 143 ? 14.535  80.677 -18.648 1.00 130.78 ? 143 GLU L CA  1 
ATOM   6576 C C   . GLU D 3 143 ? 15.381  81.663 -19.457 1.00 120.41 ? 143 GLU L C   1 
ATOM   6577 O O   . GLU D 3 143 ? 16.242  82.328 -18.856 1.00 113.13 ? 143 GLU L O   1 
ATOM   6578 C CB  . GLU D 3 143 ? 13.677  81.390 -17.599 1.00 137.13 ? 143 GLU L CB  1 
ATOM   6579 C CG  . GLU D 3 143 ? 12.653  80.486 -16.934 1.00 129.78 ? 143 GLU L CG  1 
ATOM   6580 C CD  . GLU D 3 143 ? 13.182  79.503 -15.903 1.00 135.48 ? 143 GLU L CD  1 
ATOM   6581 O OE1 . GLU D 3 143 ? 14.402  79.507 -15.645 1.00 139.93 ? 143 GLU L OE1 1 
ATOM   6582 O OE2 . GLU D 3 143 ? 12.370  78.730 -15.360 1.00 143.10 ? 143 GLU L OE2 1 
ATOM   6583 N N   . ALA D 3 144 ? 15.143  81.744 -20.766 1.00 123.08 ? 144 ALA L N   1 
ATOM   6584 C CA  . ALA D 3 144 ? 15.807  82.705 -21.637 1.00 114.36 ? 144 ALA L CA  1 
ATOM   6585 C C   . ALA D 3 144 ? 14.918  82.907 -22.854 1.00 114.44 ? 144 ALA L C   1 
ATOM   6586 O O   . ALA D 3 144 ? 14.112  82.035 -23.190 1.00 116.39 ? 144 ALA L O   1 
ATOM   6587 C CB  . ALA D 3 144 ? 17.198  82.220 -22.062 1.00 110.80 ? 144 ALA L CB  1 
ATOM   6588 N N   . LYS D 3 145 ? 15.058  84.053 -23.516 1.00 113.14 ? 145 LYS L N   1 
ATOM   6589 C CA  . LYS D 3 145 ? 14.242  84.326 -24.695 1.00 116.04 ? 145 LYS L CA  1 
ATOM   6590 C C   . LYS D 3 145 ? 15.121  84.629 -25.900 1.00 115.35 ? 145 LYS L C   1 
ATOM   6591 O O   . LYS D 3 145 ? 16.090  85.383 -25.803 1.00 112.73 ? 145 LYS L O   1 
ATOM   6592 C CB  . LYS D 3 145 ? 13.265  85.479 -24.449 1.00 122.98 ? 145 LYS L CB  1 
ATOM   6593 C CG  . LYS D 3 145 ? 12.203  85.162 -23.405 1.00 144.73 ? 145 LYS L CG  1 
ATOM   6594 C CD  . LYS D 3 145 ? 11.395  86.397 -23.051 1.00 148.51 ? 145 LYS L CD  1 
ATOM   6595 C CE  . LYS D 3 145 ? 10.483  86.135 -21.865 1.00 145.97 ? 145 LYS L CE  1 
ATOM   6596 N NZ  . LYS D 3 145 ? 9.670   87.331 -21.509 1.00 146.29 ? 145 LYS L NZ  1 
ATOM   6597 N N   . VAL D 3 146 ? 14.779  84.036 -27.040 1.00 114.99 ? 146 VAL L N   1 
ATOM   6598 C CA  . VAL D 3 146 ? 15.565  84.174 -28.260 1.00 112.42 ? 146 VAL L CA  1 
ATOM   6599 C C   . VAL D 3 146 ? 14.648  84.668 -29.370 1.00 118.53 ? 146 VAL L C   1 
ATOM   6600 O O   . VAL D 3 146 ? 13.638  84.025 -29.681 1.00 114.37 ? 146 VAL L O   1 
ATOM   6601 C CB  . VAL D 3 146 ? 16.243  82.854 -28.661 1.00 115.90 ? 146 VAL L CB  1 
ATOM   6602 C CG1 . VAL D 3 146 ? 17.198  83.084 -29.823 1.00 117.74 ? 146 VAL L CG1 1 
ATOM   6603 C CG2 . VAL D 3 146 ? 16.973  82.256 -27.474 1.00 122.90 ? 146 VAL L CG2 1 
ATOM   6604 N N   . GLN D 3 147 ? 15.007  85.798 -29.973 1.00 124.00 ? 147 GLN L N   1 
ATOM   6605 C CA  . GLN D 3 147 ? 14.236  86.426 -31.034 1.00 121.04 ? 147 GLN L CA  1 
ATOM   6606 C C   . GLN D 3 147 ? 14.967  86.299 -32.365 1.00 113.46 ? 147 GLN L C   1 
ATOM   6607 O O   . GLN D 3 147 ? 16.199  86.295 -32.418 1.00 110.58 ? 147 GLN L O   1 
ATOM   6608 C CB  . GLN D 3 147 ? 13.987  87.904 -30.727 1.00 123.51 ? 147 GLN L CB  1 
ATOM   6609 C CG  . GLN D 3 147 ? 13.138  88.163 -29.495 1.00 126.26 ? 147 GLN L CG  1 
ATOM   6610 C CD  . GLN D 3 147 ? 13.079  89.637 -29.142 1.00 131.79 ? 147 GLN L CD  1 
ATOM   6611 O OE1 . GLN D 3 147 ? 14.037  90.198 -28.608 1.00 126.98 ? 147 GLN L OE1 1 
ATOM   6612 N NE2 . GLN D 3 147 ? 11.958  90.276 -29.455 1.00 133.76 ? 147 GLN L NE2 1 
ATOM   6613 N N   . TRP D 3 148 ? 14.188  86.231 -33.443 1.00 110.07 ? 148 TRP L N   1 
ATOM   6614 C CA  . TRP D 3 148 ? 14.686  86.019 -34.802 1.00 117.86 ? 148 TRP L CA  1 
ATOM   6615 C C   . TRP D 3 148 ? 14.454  87.286 -35.623 1.00 124.95 ? 148 TRP L C   1 
ATOM   6616 O O   . TRP D 3 148 ? 13.328  87.556 -36.052 1.00 129.98 ? 148 TRP L O   1 
ATOM   6617 C CB  . TRP D 3 148 ? 13.991  84.818 -35.435 1.00 113.32 ? 148 TRP L CB  1 
ATOM   6618 C CG  . TRP D 3 148 ? 14.720  83.522 -35.261 1.00 108.67 ? 148 TRP L CG  1 
ATOM   6619 C CD1 . TRP D 3 148 ? 14.210  82.360 -34.767 1.00 106.67 ? 148 TRP L CD1 1 
ATOM   6620 C CD2 . TRP D 3 148 ? 16.074  83.238 -35.638 1.00 108.71 ? 148 TRP L CD2 1 
ATOM   6621 N NE1 . TRP D 3 148 ? 15.171  81.378 -34.778 1.00 113.32 ? 148 TRP L NE1 1 
ATOM   6622 C CE2 . TRP D 3 148 ? 16.323  81.891 -35.311 1.00 108.25 ? 148 TRP L CE2 1 
ATOM   6623 C CE3 . TRP D 3 148 ? 17.101  83.995 -36.208 1.00 112.04 ? 148 TRP L CE3 1 
ATOM   6624 C CZ2 . TRP D 3 148 ? 17.551  81.283 -35.546 1.00 105.72 ? 148 TRP L CZ2 1 
ATOM   6625 C CZ3 . TRP D 3 148 ? 18.323  83.392 -36.431 1.00 112.77 ? 148 TRP L CZ3 1 
ATOM   6626 C CH2 . TRP D 3 148 ? 18.537  82.050 -36.101 1.00 107.48 ? 148 TRP L CH2 1 
ATOM   6627 N N   . LYS D 3 149 ? 15.513  88.059 -35.860 1.00 124.17 ? 149 LYS L N   1 
ATOM   6628 C CA  . LYS D 3 149 ? 15.408  89.297 -36.624 1.00 122.38 ? 149 LYS L CA  1 
ATOM   6629 C C   . LYS D 3 149 ? 15.949  89.077 -38.031 1.00 122.21 ? 149 LYS L C   1 
ATOM   6630 O O   . LYS D 3 149 ? 17.107  88.682 -38.204 1.00 126.11 ? 149 LYS L O   1 
ATOM   6631 C CB  . LYS D 3 149 ? 16.146  90.440 -35.927 1.00 123.86 ? 149 LYS L CB  1 
ATOM   6632 C CG  . LYS D 3 149 ? 15.467  90.863 -34.644 1.00 123.56 ? 149 LYS L CG  1 
ATOM   6633 C CD  . LYS D 3 149 ? 16.039  92.138 -34.071 1.00 130.35 ? 149 LYS L CD  1 
ATOM   6634 C CE  . LYS D 3 149 ? 15.168  92.618 -32.922 1.00 134.61 ? 149 LYS L CE  1 
ATOM   6635 N NZ  . LYS D 3 149 ? 15.675  93.871 -32.307 1.00 147.35 ? 149 LYS L NZ  1 
ATOM   6636 N N   . VAL D 3 150 ? 15.111  89.338 -39.028 1.00 125.99 ? 150 VAL L N   1 
ATOM   6637 C CA  . VAL D 3 150 ? 15.437  89.117 -40.434 1.00 127.70 ? 150 VAL L CA  1 
ATOM   6638 C C   . VAL D 3 150 ? 15.419  90.482 -41.112 1.00 128.11 ? 150 VAL L C   1 
ATOM   6639 O O   . VAL D 3 150 ? 14.360  90.954 -41.542 1.00 129.39 ? 150 VAL L O   1 
ATOM   6640 C CB  . VAL D 3 150 ? 14.455  88.149 -41.102 1.00 132.09 ? 150 VAL L CB  1 
ATOM   6641 C CG1 . VAL D 3 150 ? 14.831  87.936 -42.543 1.00 135.86 ? 150 VAL L CG1 1 
ATOM   6642 C CG2 . VAL D 3 150 ? 14.418  86.828 -40.356 1.00 132.75 ? 150 VAL L CG2 1 
ATOM   6643 N N   . ASP D 3 151 ? 16.591  91.105 -41.241 1.00 127.65 ? 151 ASP L N   1 
ATOM   6644 C CA  . ASP D 3 151 ? 16.693  92.524 -41.581 1.00 129.16 ? 151 ASP L CA  1 
ATOM   6645 C C   . ASP D 3 151 ? 15.866  93.364 -40.613 1.00 126.44 ? 151 ASP L C   1 
ATOM   6646 O O   . ASP D 3 151 ? 15.026  94.175 -41.010 1.00 123.17 ? 151 ASP L O   1 
ATOM   6647 C CB  . ASP D 3 151 ? 16.282  92.799 -43.029 1.00 133.42 ? 151 ASP L CB  1 
ATOM   6648 C CG  . ASP D 3 151 ? 17.363  92.437 -44.020 1.00 129.34 ? 151 ASP L CG  1 
ATOM   6649 O OD1 . ASP D 3 151 ? 18.515  92.887 -43.838 1.00 126.44 ? 151 ASP L OD1 1 
ATOM   6650 O OD2 . ASP D 3 151 ? 17.057  91.718 -44.989 1.00 123.20 ? 151 ASP L OD2 1 
ATOM   6651 N N   . ASN D 3 152 ? 16.109  93.144 -39.318 1.00 132.71 ? 152 ASN L N   1 
ATOM   6652 C CA  . ASN D 3 152 ? 15.424  93.860 -38.241 1.00 131.36 ? 152 ASN L CA  1 
ATOM   6653 C C   . ASN D 3 152 ? 13.914  93.654 -38.292 1.00 130.17 ? 152 ASN L C   1 
ATOM   6654 O O   . ASN D 3 152 ? 13.142  94.532 -37.900 1.00 131.50 ? 152 ASN L O   1 
ATOM   6655 C CB  . ASN D 3 152 ? 15.760  95.353 -38.264 1.00 128.99 ? 152 ASN L CB  1 
ATOM   6656 C CG  . ASN D 3 152 ? 17.236  95.611 -38.489 1.00 127.70 ? 152 ASN L CG  1 
ATOM   6657 O OD1 . ASN D 3 152 ? 18.050  94.688 -38.458 1.00 125.97 ? 152 ASN L OD1 1 
ATOM   6658 N ND2 . ASN D 3 152 ? 17.589  96.870 -38.717 1.00 127.61 ? 152 ASN L ND2 1 
ATOM   6659 N N   . ALA D 3 153 ? 13.481  92.494 -38.776 1.00 130.49 ? 153 ALA L N   1 
ATOM   6660 C CA  . ALA D 3 153 ? 12.065  92.143 -38.871 1.00 128.94 ? 153 ALA L CA  1 
ATOM   6661 C C   . ALA D 3 153 ? 11.829  90.878 -38.051 1.00 135.14 ? 153 ALA L C   1 
ATOM   6662 O O   . ALA D 3 153 ? 12.076  89.764 -38.524 1.00 132.79 ? 153 ALA L O   1 
ATOM   6663 C CB  . ALA D 3 153 ? 11.638  91.951 -40.324 1.00 130.68 ? 153 ALA L CB  1 
ATOM   6664 N N   . LEU D 3 154 ? 11.370  91.059 -36.815 1.00 135.55 ? 154 LEU L N   1 
ATOM   6665 C CA  . LEU D 3 154 ? 10.997  89.927 -35.978 1.00 134.81 ? 154 LEU L CA  1 
ATOM   6666 C C   . LEU D 3 154 ? 9.945   89.069 -36.667 1.00 134.61 ? 154 LEU L C   1 
ATOM   6667 O O   . LEU D 3 154 ? 9.026   89.579 -37.315 1.00 133.33 ? 154 LEU L O   1 
ATOM   6668 C CB  . LEU D 3 154 ? 10.473  90.419 -34.630 1.00 136.21 ? 154 LEU L CB  1 
ATOM   6669 C CG  . LEU D 3 154 ? 11.526  90.963 -33.669 1.00 141.68 ? 154 LEU L CG  1 
ATOM   6670 C CD1 . LEU D 3 154 ? 10.861  91.519 -32.432 1.00 152.78 ? 154 LEU L CD1 1 
ATOM   6671 C CD2 . LEU D 3 154 ? 12.450  89.830 -33.290 1.00 167.09 ? 154 LEU L CD2 1 
ATOM   6672 N N   . GLN D 3 155 ? 10.117  87.746 -36.562 1.00 133.26 ? 155 GLN L N   1 
ATOM   6673 C CA  . GLN D 3 155 ? 9.166   86.790 -37.190 1.00 137.93 ? 155 GLN L CA  1 
ATOM   6674 C C   . GLN D 3 155 ? 8.967   85.610 -36.234 1.00 147.70 ? 155 GLN L C   1 
ATOM   6675 O O   . GLN D 3 155 ? 9.802   84.684 -36.266 1.00 146.19 ? 155 GLN L O   1 
ATOM   6676 C CB  . GLN D 3 155 ? 9.710   86.291 -38.529 1.00 140.33 ? 155 GLN L CB  1 
ATOM   6677 C CG  . GLN D 3 155 ? 9.928   87.390 -39.559 1.00 139.94 ? 155 GLN L CG  1 
ATOM   6678 C CD  . GLN D 3 155 ? 10.676  86.894 -40.772 1.00 142.82 ? 155 GLN L CD  1 
ATOM   6679 O OE1 . GLN D 3 155 ? 11.043  85.725 -40.865 1.00 151.86 ? 155 GLN L OE1 1 
ATOM   6680 N NE2 . GLN D 3 155 ? 10.911  87.790 -41.717 1.00 139.38 ? 155 GLN L NE2 1 
ATOM   6681 N N   . SER D 3 156 ? 7.910   85.643 -35.417 1.00 142.52 ? 156 SER L N   1 
ATOM   6682 C CA  . SER D 3 156 ? 7.680   84.572 -34.410 1.00 154.62 ? 156 SER L CA  1 
ATOM   6683 C C   . SER D 3 156 ? 7.494   83.218 -35.103 1.00 159.47 ? 156 SER L C   1 
ATOM   6684 O O   . SER D 3 156 ? 8.005   82.213 -34.572 1.00 176.81 ? 156 SER L O   1 
ATOM   6685 C CB  . SER D 3 156 ? 6.498   84.903 -33.537 1.00 156.24 ? 156 SER L CB  1 
ATOM   6686 O OG  . SER D 3 156 ? 5.312   84.995 -34.312 1.00 170.43 ? 156 SER L OG  1 
ATOM   6687 N N   . GLY D 3 157 ? 6.794   83.195 -36.241 1.00 148.68 ? 157 GLY L N   1 
ATOM   6688 C CA  . GLY D 3 157 ? 6.515   81.926 -36.943 1.00 138.70 ? 157 GLY L CA  1 
ATOM   6689 C C   . GLY D 3 157 ? 7.758   81.327 -37.577 1.00 135.90 ? 157 GLY L C   1 
ATOM   6690 O O   . GLY D 3 157 ? 8.764   82.056 -37.700 1.00 133.55 ? 157 GLY L O   1 
ATOM   6691 N N   . ASN D 3 158 ? 7.697   80.045 -37.955 1.00 138.95 ? 158 ASN L N   1 
ATOM   6692 C CA  . ASN D 3 158 ? 8.842   79.368 -38.625 1.00 137.84 ? 158 ASN L CA  1 
ATOM   6693 C C   . ASN D 3 158 ? 10.036  79.319 -37.667 1.00 122.56 ? 158 ASN L C   1 
ATOM   6694 O O   . ASN D 3 158 ? 11.171  79.526 -38.134 1.00 120.57 ? 158 ASN L O   1 
ATOM   6695 C CB  . ASN D 3 158 ? 9.180   80.033 -39.962 1.00 147.94 ? 158 ASN L CB  1 
ATOM   6696 C CG  . ASN D 3 158 ? 8.012   80.019 -40.924 1.00 176.34 ? 158 ASN L CG  1 
ATOM   6697 O OD1 . ASN D 3 158 ? 7.553   78.956 -41.335 1.00 211.89 ? 158 ASN L OD1 1 
ATOM   6698 N ND2 . ASN D 3 158 ? 7.525   81.194 -41.290 1.00 186.31 ? 158 ASN L ND2 1 
ATOM   6699 N N   . SER D 3 159 ? 9.782   79.049 -36.384 1.00 119.34 ? 159 SER L N   1 
ATOM   6700 C CA  . SER D 3 159 ? 10.849  78.949 -35.394 1.00 112.09 ? 159 SER L CA  1 
ATOM   6701 C C   . SER D 3 159 ? 10.511  77.883 -34.362 1.00 111.59 ? 159 SER L C   1 
ATOM   6702 O O   . SER D 3 159 ? 9.402   77.880 -33.819 1.00 118.95 ? 159 SER L O   1 
ATOM   6703 C CB  . SER D 3 159 ? 11.088  80.297 -34.709 1.00 105.75 ? 159 SER L CB  1 
ATOM   6704 O OG  . SER D 3 159 ? 11.732  80.145 -33.454 1.00 97.85  ? 159 SER L OG  1 
ATOM   6705 N N   . GLN D 3 160 ? 11.440  76.968 -34.079 1.00 109.35 ? 160 GLN L N   1 
ATOM   6706 C CA  . GLN D 3 160 ? 11.220  75.981 -33.027 1.00 110.85 ? 160 GLN L CA  1 
ATOM   6707 C C   . GLN D 3 160 ? 12.429  75.906 -32.110 1.00 102.39 ? 160 GLN L C   1 
ATOM   6708 O O   . GLN D 3 160 ? 13.568  75.875 -32.575 1.00 95.70  ? 160 GLN L O   1 
ATOM   6709 C CB  . GLN D 3 160 ? 10.914  74.589 -33.598 1.00 103.27 ? 160 GLN L CB  1 
ATOM   6710 C CG  . GLN D 3 160 ? 9.772   74.548 -34.598 1.00 110.99 ? 160 GLN L CG  1 
ATOM   6711 C CD  . GLN D 3 160 ? 9.961   73.476 -35.650 1.00 111.27 ? 160 GLN L CD  1 
ATOM   6712 O OE1 . GLN D 3 160 ? 9.188   72.525 -35.723 1.00 107.42 ? 160 GLN L OE1 1 
ATOM   6713 N NE2 . GLN D 3 160 ? 10.991  73.629 -36.476 1.00 122.92 ? 160 GLN L NE2 1 
ATOM   6714 N N   . GLU D 3 161 ? 12.178  75.875 -30.807 1.00 107.24 ? 161 GLU L N   1 
ATOM   6715 C CA  . GLU D 3 161 ? 13.245  75.792 -29.826 1.00 99.70  ? 161 GLU L CA  1 
ATOM   6716 C C   . GLU D 3 161 ? 13.210  74.435 -29.141 1.00 95.01  ? 161 GLU L C   1 
ATOM   6717 O O   . GLU D 3 161 ? 12.140  73.862 -28.918 1.00 94.20  ? 161 GLU L O   1 
ATOM   6718 C CB  . GLU D 3 161 ? 13.131  76.903 -28.779 1.00 104.96 ? 161 GLU L CB  1 
ATOM   6719 C CG  . GLU D 3 161 ? 13.036  78.294 -29.366 1.00 118.54 ? 161 GLU L CG  1 
ATOM   6720 C CD  . GLU D 3 161 ? 12.897  79.365 -28.305 1.00 135.34 ? 161 GLU L CD  1 
ATOM   6721 O OE1 . GLU D 3 161 ? 12.716  79.015 -27.118 1.00 136.22 ? 161 GLU L OE1 1 
ATOM   6722 O OE2 . GLU D 3 161 ? 12.979  80.559 -28.661 1.00 139.19 ? 161 GLU L OE2 1 
ATOM   6723 N N   . SER D 3 162 ? 14.393  73.918 -28.817 1.00 96.76  ? 162 SER L N   1 
ATOM   6724 C CA  . SER D 3 162 ? 14.485  72.712 -28.003 1.00 91.35  ? 162 SER L CA  1 
ATOM   6725 C C   . SER D 3 162 ? 15.573  72.884 -26.951 1.00 91.75  ? 162 SER L C   1 
ATOM   6726 O O   . SER D 3 162 ? 16.564  73.591 -27.160 1.00 92.64  ? 162 SER L O   1 
ATOM   6727 C CB  . SER D 3 162 ? 14.750  71.454 -28.847 1.00 84.05  ? 162 SER L CB  1 
ATOM   6728 O OG  . SER D 3 162 ? 16.132  71.269 -29.093 1.00 91.34  ? 162 SER L OG  1 
ATOM   6729 N N   . VAL D 3 163 ? 15.369  72.221 -25.812 1.00 86.57  ? 163 VAL L N   1 
ATOM   6730 C CA  . VAL D 3 163 ? 16.156  72.431 -24.602 1.00 88.75  ? 163 VAL L CA  1 
ATOM   6731 C C   . VAL D 3 163 ? 16.832  71.125 -24.212 1.00 90.80  ? 163 VAL L C   1 
ATOM   6732 O O   . VAL D 3 163 ? 16.191  70.069 -24.203 1.00 86.54  ? 163 VAL L O   1 
ATOM   6733 C CB  . VAL D 3 163 ? 15.278  72.916 -23.428 1.00 90.57  ? 163 VAL L CB  1 
ATOM   6734 C CG1 . VAL D 3 163 ? 16.137  73.565 -22.341 1.00 98.71  ? 163 VAL L CG1 1 
ATOM   6735 C CG2 . VAL D 3 163 ? 14.135  73.809 -23.909 1.00 86.22  ? 163 VAL L CG2 1 
ATOM   6736 N N   . THR D 3 164 ? 18.108  71.202 -23.838 1.00 88.45  ? 164 THR L N   1 
ATOM   6737 C CA  . THR D 3 164 ? 18.747  70.051 -23.218 1.00 92.19  ? 164 THR L CA  1 
ATOM   6738 C C   . THR D 3 164 ? 18.267  69.898 -21.776 1.00 101.70 ? 164 THR L C   1 
ATOM   6739 O O   . THR D 3 164 ? 17.757  70.838 -21.159 1.00 102.33 ? 164 THR L O   1 
ATOM   6740 C CB  . THR D 3 164 ? 20.274  70.187 -23.235 1.00 89.28  ? 164 THR L CB  1 
ATOM   6741 O OG1 . THR D 3 164 ? 20.660  71.458 -22.693 1.00 93.05  ? 164 THR L OG1 1 
ATOM   6742 C CG2 . THR D 3 164 ? 20.815  70.055 -24.649 1.00 91.59  ? 164 THR L CG2 1 
ATOM   6743 N N   . GLU D 3 165 ? 18.418  68.689 -21.244 1.00 105.02 ? 165 GLU L N   1 
ATOM   6744 C CA  . GLU D 3 165 ? 18.245  68.512 -19.813 1.00 102.33 ? 165 GLU L CA  1 
ATOM   6745 C C   . GLU D 3 165 ? 19.551  68.869 -19.105 1.00 102.11 ? 165 GLU L C   1 
ATOM   6746 O O   . GLU D 3 165 ? 20.581  69.111 -19.740 1.00 99.92  ? 165 GLU L O   1 
ATOM   6747 C CB  . GLU D 3 165 ? 17.796  67.084 -19.495 1.00 102.80 ? 165 GLU L CB  1 
ATOM   6748 C CG  . GLU D 3 165 ? 16.305  66.852 -19.737 1.00 105.59 ? 165 GLU L CG  1 
ATOM   6749 C CD  . GLU D 3 165 ? 15.780  65.591 -19.074 1.00 116.50 ? 165 GLU L CD  1 
ATOM   6750 O OE1 . GLU D 3 165 ? 16.466  65.055 -18.179 1.00 145.44 ? 165 GLU L OE1 1 
ATOM   6751 O OE2 . GLU D 3 165 ? 14.679  65.135 -19.447 1.00 121.82 ? 165 GLU L OE2 1 
ATOM   6752 N N   . GLN D 3 166 ? 19.501  68.930 -17.774 1.00 102.60 ? 166 GLN L N   1 
ATOM   6753 C CA  . GLN D 3 166 ? 20.660  69.391 -17.020 1.00 93.98  ? 166 GLN L CA  1 
ATOM   6754 C C   . GLN D 3 166 ? 21.870  68.504 -17.271 1.00 96.48  ? 166 GLN L C   1 
ATOM   6755 O O   . GLN D 3 166 ? 21.776  67.274 -17.262 1.00 102.47 ? 166 GLN L O   1 
ATOM   6756 C CB  . GLN D 3 166 ? 20.362  69.431 -15.522 1.00 101.83 ? 166 GLN L CB  1 
ATOM   6757 C CG  . GLN D 3 166 ? 19.540  70.612 -15.096 1.00 97.54  ? 166 GLN L CG  1 
ATOM   6758 C CD  . GLN D 3 166 ? 19.645  70.895 -13.615 1.00 101.17 ? 166 GLN L CD  1 
ATOM   6759 O OE1 . GLN D 3 166 ? 20.454  70.291 -12.913 1.00 106.21 ? 166 GLN L OE1 1 
ATOM   6760 N NE2 . GLN D 3 166 ? 18.839  71.833 -13.133 1.00 104.51 ? 166 GLN L NE2 1 
ATOM   6761 N N   . ASP D 3 167 ? 23.010  69.144 -17.509 1.00 93.75  ? 167 ASP L N   1 
ATOM   6762 C CA  . ASP D 3 167 ? 24.265  68.421 -17.597 1.00 103.31 ? 167 ASP L CA  1 
ATOM   6763 C C   . ASP D 3 167 ? 24.600  67.805 -16.244 1.00 106.82 ? 167 ASP L C   1 
ATOM   6764 O O   . ASP D 3 167 ? 24.238  68.333 -15.189 1.00 106.19 ? 167 ASP L O   1 
ATOM   6765 C CB  . ASP D 3 167 ? 25.382  69.357 -18.056 1.00 105.11 ? 167 ASP L CB  1 
ATOM   6766 C CG  . ASP D 3 167 ? 26.648  68.616 -18.423 1.00 107.62 ? 167 ASP L CG  1 
ATOM   6767 O OD1 . ASP D 3 167 ? 26.594  67.760 -19.333 1.00 104.50 ? 167 ASP L OD1 1 
ATOM   6768 O OD2 . ASP D 3 167 ? 27.701  68.895 -17.816 1.00 114.02 ? 167 ASP L OD2 1 
ATOM   6769 N N   . SER D 3 168 ? 25.272  66.655 -16.279 1.00 110.34 ? 168 SER L N   1 
ATOM   6770 C CA  . SER D 3 168 ? 25.629  65.996 -15.028 1.00 101.94 ? 168 SER L CA  1 
ATOM   6771 C C   . SER D 3 168 ? 26.760  66.733 -14.320 1.00 102.96 ? 168 SER L C   1 
ATOM   6772 O O   . SER D 3 168 ? 26.765  66.832 -13.088 1.00 108.03 ? 168 SER L O   1 
ATOM   6773 C CB  . SER D 3 168 ? 26.005  64.537 -15.286 1.00 110.51 ? 168 SER L CB  1 
ATOM   6774 O OG  . SER D 3 168 ? 27.174  64.439 -16.076 1.00 137.99 ? 168 SER L OG  1 
ATOM   6775 N N   . LYS D 3 169 ? 27.718  67.268 -15.079 1.00 108.29 ? 169 LYS L N   1 
ATOM   6776 C CA  . LYS D 3 169 ? 28.824  68.010 -14.478 1.00 112.71 ? 169 LYS L CA  1 
ATOM   6777 C C   . LYS D 3 169 ? 28.416  69.440 -14.137 1.00 117.58 ? 169 LYS L C   1 
ATOM   6778 O O   . LYS D 3 169 ? 28.509  69.867 -12.981 1.00 118.21 ? 169 LYS L O   1 
ATOM   6779 C CB  . LYS D 3 169 ? 30.034  68.018 -15.417 1.00 123.69 ? 169 LYS L CB  1 
ATOM   6780 C CG  . LYS D 3 169 ? 30.725  66.678 -15.595 1.00 135.00 ? 169 LYS L CG  1 
ATOM   6781 C CD  . LYS D 3 169 ? 31.993  66.847 -16.423 1.00 153.96 ? 169 LYS L CD  1 
ATOM   6782 C CE  . LYS D 3 169 ? 32.790  65.553 -16.504 1.00 174.15 ? 169 LYS L CE  1 
ATOM   6783 N NZ  . LYS D 3 169 ? 34.113  65.733 -17.172 1.00 180.44 ? 169 LYS L NZ  1 
ATOM   6784 N N   . ASP D 3 170 ? 27.958  70.195 -15.139 1.00 118.01 ? 170 ASP L N   1 
ATOM   6785 C CA  . ASP D 3 170 ? 27.673  71.614 -14.948 1.00 111.86 ? 170 ASP L CA  1 
ATOM   6786 C C   . ASP D 3 170 ? 26.334  71.863 -14.268 1.00 106.09 ? 170 ASP L C   1 
ATOM   6787 O O   . ASP D 3 170 ? 26.187  72.863 -13.555 1.00 98.20  ? 170 ASP L O   1 
ATOM   6788 C CB  . ASP D 3 170 ? 27.679  72.338 -16.294 1.00 110.17 ? 170 ASP L CB  1 
ATOM   6789 C CG  . ASP D 3 170 ? 28.973  72.160 -17.049 1.00 113.36 ? 170 ASP L CG  1 
ATOM   6790 O OD1 . ASP D 3 170 ? 29.804  71.336 -16.613 1.00 157.42 ? 170 ASP L OD1 1 
ATOM   6791 O OD2 . ASP D 3 170 ? 29.158  72.836 -18.082 1.00 115.13 ? 170 ASP L OD2 1 
ATOM   6792 N N   . SER D 3 171 ? 25.359  70.978 -14.480 1.00 111.80 ? 171 SER L N   1 
ATOM   6793 C CA  . SER D 3 171 ? 23.960  71.254 -14.154 1.00 107.80 ? 171 SER L CA  1 
ATOM   6794 C C   . SER D 3 171 ? 23.482  72.517 -14.869 1.00 106.63 ? 171 SER L C   1 
ATOM   6795 O O   . SER D 3 171 ? 22.738  73.327 -14.311 1.00 107.23 ? 171 SER L O   1 
ATOM   6796 C CB  . SER D 3 171 ? 23.736  71.348 -12.641 1.00 104.74 ? 171 SER L CB  1 
ATOM   6797 O OG  . SER D 3 171 ? 24.239  70.200 -11.982 1.00 104.01 ? 171 SER L OG  1 
ATOM   6798 N N   . THR D 3 172 ? 23.914  72.682 -16.120 1.00 103.24 ? 172 THR L N   1 
ATOM   6799 C CA  . THR D 3 172 ? 23.527  73.796 -16.977 1.00 101.91 ? 172 THR L CA  1 
ATOM   6800 C C   . THR D 3 172 ? 22.695  73.287 -18.150 1.00 103.12 ? 172 THR L C   1 
ATOM   6801 O O   . THR D 3 172 ? 22.442  72.087 -18.296 1.00 108.46 ? 172 THR L O   1 
ATOM   6802 C CB  . THR D 3 172 ? 24.754  74.555 -17.484 1.00 102.24 ? 172 THR L CB  1 
ATOM   6803 O OG1 . THR D 3 172 ? 25.603  73.662 -18.216 1.00 100.36 ? 172 THR L OG1 1 
ATOM   6804 C CG2 . THR D 3 172 ? 25.523  75.150 -16.324 1.00 106.54 ? 172 THR L CG2 1 
ATOM   6805 N N   . TYR D 3 173 ? 22.289  74.221 -19.007 1.00 95.84  ? 173 TYR L N   1 
ATOM   6806 C CA  . TYR D 3 173 ? 21.318  73.952 -20.054 1.00 91.48  ? 173 TYR L CA  1 
ATOM   6807 C C   . TYR D 3 173 ? 21.838  74.451 -21.395 1.00 90.47  ? 173 TYR L C   1 
ATOM   6808 O O   . TYR D 3 173 ? 22.814  75.201 -21.480 1.00 90.82  ? 173 TYR L O   1 
ATOM   6809 C CB  . TYR D 3 173 ? 19.973  74.630 -19.753 1.00 97.53  ? 173 TYR L CB  1 
ATOM   6810 C CG  . TYR D 3 173 ? 19.274  74.113 -18.522 1.00 101.23 ? 173 TYR L CG  1 
ATOM   6811 C CD1 . TYR D 3 173 ? 18.542  72.934 -18.557 1.00 114.43 ? 173 TYR L CD1 1 
ATOM   6812 C CD2 . TYR D 3 173 ? 19.312  74.829 -17.334 1.00 103.71 ? 173 TYR L CD2 1 
ATOM   6813 C CE1 . TYR D 3 173 ? 17.894  72.465 -17.432 1.00 121.02 ? 173 TYR L CE1 1 
ATOM   6814 C CE2 . TYR D 3 173 ? 18.663  74.372 -16.205 1.00 107.04 ? 173 TYR L CE2 1 
ATOM   6815 C CZ  . TYR D 3 173 ? 17.952  73.191 -16.260 1.00 120.26 ? 173 TYR L CZ  1 
ATOM   6816 O OH  . TYR D 3 173 ? 17.302  72.733 -15.135 1.00 119.26 ? 173 TYR L OH  1 
ATOM   6817 N N   . SER D 3 174 ? 21.155  74.041 -22.458 1.00 90.16  ? 174 SER L N   1 
ATOM   6818 C CA  . SER D 3 174 ? 21.450  74.549 -23.786 1.00 89.03  ? 174 SER L CA  1 
ATOM   6819 C C   . SER D 3 174 ? 20.162  74.601 -24.595 1.00 89.25  ? 174 SER L C   1 
ATOM   6820 O O   . SER D 3 174 ? 19.272  73.764 -24.431 1.00 88.56  ? 174 SER L O   1 
ATOM   6821 C CB  . SER D 3 174 ? 22.504  73.697 -24.503 1.00 89.35  ? 174 SER L CB  1 
ATOM   6822 O OG  . SER D 3 174 ? 23.689  73.605 -23.734 1.00 92.76  ? 174 SER L OG  1 
ATOM   6823 N N   . LEU D 3 175 ? 20.075  75.605 -25.461 1.00 88.49  ? 175 LEU L N   1 
ATOM   6824 C CA  . LEU D 3 175 ? 18.925  75.838 -26.322 1.00 90.18  ? 175 LEU L CA  1 
ATOM   6825 C C   . LEU D 3 175 ? 19.340  75.834 -27.782 1.00 88.82  ? 175 LEU L C   1 
ATOM   6826 O O   . LEU D 3 175 ? 20.413  76.327 -28.145 1.00 89.93  ? 175 LEU L O   1 
ATOM   6827 C CB  . LEU D 3 175 ? 18.244  77.175 -26.019 1.00 96.94  ? 175 LEU L CB  1 
ATOM   6828 C CG  . LEU D 3 175 ? 17.536  77.294 -24.682 1.00 105.51 ? 175 LEU L CG  1 
ATOM   6829 C CD1 . LEU D 3 175 ? 17.036  78.708 -24.462 1.00 130.86 ? 175 LEU L CD1 1 
ATOM   6830 C CD2 . LEU D 3 175 ? 16.390  76.328 -24.701 1.00 123.80 ? 175 LEU L CD2 1 
ATOM   6831 N N   . SER D 3 176 ? 18.464  75.287 -28.619 1.00 89.98  ? 176 SER L N   1 
ATOM   6832 C CA  . SER D 3 176 ? 18.608  75.387 -30.067 1.00 84.59  ? 176 SER L CA  1 
ATOM   6833 C C   . SER D 3 176 ? 17.341  76.026 -30.607 1.00 91.37  ? 176 SER L C   1 
ATOM   6834 O O   . SER D 3 176 ? 16.251  75.454 -30.484 1.00 93.81  ? 176 SER L O   1 
ATOM   6835 C CB  . SER D 3 176 ? 18.851  74.026 -30.715 1.00 86.51  ? 176 SER L CB  1 
ATOM   6836 O OG  . SER D 3 176 ? 17.627  73.404 -31.059 1.00 85.54  ? 176 SER L OG  1 
ATOM   6837 N N   . SER D 3 177 ? 17.487  77.218 -31.176 1.00 96.66  ? 177 SER L N   1 
ATOM   6838 C CA  . SER D 3 177 ? 16.396  77.909 -31.846 1.00 96.81  ? 177 SER L CA  1 
ATOM   6839 C C   . SER D 3 177 ? 16.611  77.786 -33.347 1.00 95.07  ? 177 SER L C   1 
ATOM   6840 O O   . SER D 3 177 ? 17.599  78.300 -33.883 1.00 97.22  ? 177 SER L O   1 
ATOM   6841 C CB  . SER D 3 177 ? 16.330  79.375 -31.421 1.00 100.50 ? 177 SER L CB  1 
ATOM   6842 O OG  . SER D 3 177 ? 15.064  79.936 -31.719 1.00 96.42  ? 177 SER L OG  1 
ATOM   6843 N N   . THR D 3 178 ? 15.693  77.098 -34.017 1.00 91.94  ? 178 THR L N   1 
ATOM   6844 C CA  . THR D 3 178 ? 15.822  76.760 -35.429 1.00 94.86  ? 178 THR L CA  1 
ATOM   6845 C C   . THR D 3 178 ? 14.768  77.536 -36.209 1.00 101.92 ? 178 THR L C   1 
ATOM   6846 O O   . THR D 3 178 ? 13.565  77.271 -36.082 1.00 109.59 ? 178 THR L O   1 
ATOM   6847 C CB  . THR D 3 178 ? 15.683  75.251 -35.643 1.00 98.47  ? 178 THR L CB  1 
ATOM   6848 O OG1 . THR D 3 178 ? 16.605  74.560 -34.784 1.00 101.63 ? 178 THR L OG1 1 
ATOM   6849 C CG2 . THR D 3 178 ? 15.997  74.892 -37.085 1.00 99.43  ? 178 THR L CG2 1 
ATOM   6850 N N   . LEU D 3 179 ? 15.231  78.512 -36.985 1.00 101.57 ? 179 LEU L N   1 
ATOM   6851 C CA  . LEU D 3 179 ? 14.397  79.269 -37.908 1.00 103.58 ? 179 LEU L CA  1 
ATOM   6852 C C   . LEU D 3 179 ? 14.384  78.556 -39.255 1.00 106.43 ? 179 LEU L C   1 
ATOM   6853 O O   . LEU D 3 179 ? 15.420  78.466 -39.923 1.00 105.80 ? 179 LEU L O   1 
ATOM   6854 C CB  . LEU D 3 179 ? 14.944  80.688 -38.060 1.00 104.36 ? 179 LEU L CB  1 
ATOM   6855 C CG  . LEU D 3 179 ? 14.497  81.622 -39.185 1.00 109.57 ? 179 LEU L CG  1 
ATOM   6856 C CD1 . LEU D 3 179 ? 13.131  82.223 -38.905 1.00 114.94 ? 179 LEU L CD1 1 
ATOM   6857 C CD2 . LEU D 3 179 ? 15.528  82.716 -39.410 1.00 110.83 ? 179 LEU L CD2 1 
ATOM   6858 N N   . THR D 3 180 ? 13.217  78.063 -39.659 1.00 114.77 ? 180 THR L N   1 
ATOM   6859 C CA  . THR D 3 180 ? 13.070  77.246 -40.863 1.00 114.77 ? 180 THR L CA  1 
ATOM   6860 C C   . THR D 3 180 ? 12.275  78.030 -41.902 1.00 123.30 ? 180 THR L C   1 
ATOM   6861 O O   . THR D 3 180 ? 11.048  78.134 -41.812 1.00 133.39 ? 180 THR L O   1 
ATOM   6862 C CB  . THR D 3 180 ? 12.396  75.918 -40.525 1.00 116.36 ? 180 THR L CB  1 
ATOM   6863 O OG1 . THR D 3 180 ? 11.163  76.166 -39.834 1.00 122.35 ? 180 THR L OG1 1 
ATOM   6864 C CG2 . THR D 3 180 ? 13.302  75.073 -39.645 1.00 114.95 ? 180 THR L CG2 1 
ATOM   6865 N N   . LEU D 3 181 ? 12.975  78.572 -42.894 1.00 118.79 ? 181 LEU L N   1 
ATOM   6866 C CA  . LEU D 3 181 ? 12.360  79.388 -43.930 1.00 124.71 ? 181 LEU L CA  1 
ATOM   6867 C C   . LEU D 3 181 ? 12.848  78.969 -45.308 1.00 127.30 ? 181 LEU L C   1 
ATOM   6868 O O   . LEU D 3 181 ? 13.993  78.539 -45.482 1.00 129.36 ? 181 LEU L O   1 
ATOM   6869 C CB  . LEU D 3 181 ? 12.652  80.882 -43.724 1.00 127.65 ? 181 LEU L CB  1 
ATOM   6870 C CG  . LEU D 3 181 ? 11.950  81.585 -42.566 1.00 153.39 ? 181 LEU L CG  1 
ATOM   6871 C CD1 . LEU D 3 181 ? 12.396  83.029 -42.497 1.00 179.60 ? 181 LEU L CD1 1 
ATOM   6872 C CD2 . LEU D 3 181 ? 10.457  81.519 -42.796 1.00 177.47 ? 181 LEU L CD2 1 
ATOM   6873 N N   . SER D 3 182 ? 11.957  79.105 -46.298 1.00 134.07 ? 182 SER L N   1 
ATOM   6874 C CA  . SER D 3 182 ? 12.362  78.886 -47.681 1.00 133.30 ? 182 SER L CA  1 
ATOM   6875 C C   . SER D 3 182 ? 11.550  79.721 -48.670 1.00 138.32 ? 182 SER L C   1 
ATOM   6876 O O   . SER D 3 182 ? 11.436  79.343 -49.841 1.00 138.49 ? 182 SER L O   1 
ATOM   6877 C CB  . SER D 3 182 ? 12.285  77.398 -48.052 1.00 127.60 ? 182 SER L CB  1 
ATOM   6878 O OG  . SER D 3 182 ? 11.203  76.755 -47.403 1.00 131.58 ? 182 SER L OG  1 
ATOM   6879 N N   . LYS D 3 183 ? 11.002  80.858 -48.239 1.00 145.33 ? 183 LYS L N   1 
ATOM   6880 C CA  . LYS D 3 183 ? 10.368  81.798 -49.164 1.00 143.05 ? 183 LYS L CA  1 
ATOM   6881 C C   . LYS D 3 183 ? 11.465  82.556 -49.903 1.00 133.81 ? 183 LYS L C   1 
ATOM   6882 O O   . LYS D 3 183 ? 12.179  83.368 -49.303 1.00 133.85 ? 183 LYS L O   1 
ATOM   6883 C CB  . LYS D 3 183 ? 9.440   82.761 -48.427 1.00 134.95 ? 183 LYS L CB  1 
ATOM   6884 C CG  . LYS D 3 183 ? 8.142   82.142 -47.937 1.00 127.33 ? 183 LYS L CG  1 
ATOM   6885 C CD  . LYS D 3 183 ? 7.432   83.068 -46.960 1.00 128.92 ? 183 LYS L CD  1 
ATOM   6886 C CE  . LYS D 3 183 ? 6.586   82.291 -45.962 1.00 136.15 ? 183 LYS L CE  1 
ATOM   6887 N NZ  . LYS D 3 183 ? 6.544   82.967 -44.634 1.00 149.94 ? 183 LYS L NZ  1 
ATOM   6888 N N   . ALA D 3 184 ? 11.577  82.312 -51.214 1.00 138.15 ? 184 ALA L N   1 
ATOM   6889 C CA  . ALA D 3 184 ? 12.787  82.638 -51.969 1.00 134.83 ? 184 ALA L CA  1 
ATOM   6890 C C   . ALA D 3 184 ? 14.001  82.009 -51.292 1.00 134.53 ? 184 ALA L C   1 
ATOM   6891 O O   . ALA D 3 184 ? 15.075  82.602 -51.222 1.00 133.62 ? 184 ALA L O   1 
ATOM   6892 C CB  . ALA D 3 184 ? 12.964  84.152 -52.134 1.00 138.24 ? 184 ALA L CB  1 
ATOM   6893 N N   . ASP D 3 185 ? 13.823  80.780 -50.807 1.00 134.74 ? 185 ASP L N   1 
ATOM   6894 C CA  . ASP D 3 185 ? 14.686  80.218 -49.776 1.00 133.97 ? 185 ASP L CA  1 
ATOM   6895 C C   . ASP D 3 185 ? 14.839  81.269 -48.689 1.00 136.43 ? 185 ASP L C   1 
ATOM   6896 O O   . ASP D 3 185 ? 13.848  81.668 -48.070 1.00 141.37 ? 185 ASP L O   1 
ATOM   6897 C CB  . ASP D 3 185 ? 15.995  79.699 -50.354 1.00 137.45 ? 185 ASP L CB  1 
ATOM   6898 C CG  . ASP D 3 185 ? 15.828  78.340 -50.989 1.00 134.78 ? 185 ASP L CG  1 
ATOM   6899 O OD1 . ASP D 3 185 ? 14.775  77.709 -50.738 1.00 129.60 ? 185 ASP L OD1 1 
ATOM   6900 O OD2 . ASP D 3 185 ? 16.735  77.898 -51.719 1.00 127.63 ? 185 ASP L OD2 1 
ATOM   6901 N N   . TYR D 3 186 ? 16.048  81.752 -48.438 1.00 132.84 ? 186 TYR L N   1 
ATOM   6902 C CA  . TYR D 3 186 ? 16.166  82.854 -47.496 1.00 131.15 ? 186 TYR L CA  1 
ATOM   6903 C C   . TYR D 3 186 ? 16.580  84.110 -48.265 1.00 132.99 ? 186 TYR L C   1 
ATOM   6904 O O   . TYR D 3 186 ? 17.096  85.065 -47.674 1.00 135.75 ? 186 TYR L O   1 
ATOM   6905 C CB  . TYR D 3 186 ? 17.118  82.507 -46.342 1.00 131.97 ? 186 TYR L CB  1 
ATOM   6906 C CG  . TYR D 3 186 ? 18.572  82.216 -46.647 1.00 124.79 ? 186 TYR L CG  1 
ATOM   6907 C CD1 . TYR D 3 186 ? 19.520  83.230 -46.679 1.00 131.04 ? 186 TYR L CD1 1 
ATOM   6908 C CD2 . TYR D 3 186 ? 19.004  80.916 -46.857 1.00 121.77 ? 186 TYR L CD2 1 
ATOM   6909 C CE1 . TYR D 3 186 ? 20.850  82.961 -46.928 1.00 138.78 ? 186 TYR L CE1 1 
ATOM   6910 C CE2 . TYR D 3 186 ? 20.331  80.640 -47.112 1.00 128.03 ? 186 TYR L CE2 1 
ATOM   6911 C CZ  . TYR D 3 186 ? 21.250  81.660 -47.145 1.00 133.70 ? 186 TYR L CZ  1 
ATOM   6912 O OH  . TYR D 3 186 ? 22.567  81.368 -47.400 1.00 134.29 ? 186 TYR L OH  1 
ATOM   6913 N N   . GLU D 3 187 ? 16.299  84.138 -49.568 1.00 132.67 ? 187 GLU L N   1 
ATOM   6914 C CA  . GLU D 3 187 ? 16.452  85.362 -50.344 1.00 139.66 ? 187 GLU L CA  1 
ATOM   6915 C C   . GLU D 3 187 ? 15.449  86.389 -49.826 1.00 142.33 ? 187 GLU L C   1 
ATOM   6916 O O   . GLU D 3 187 ? 14.622  86.106 -48.955 1.00 140.00 ? 187 GLU L O   1 
ATOM   6917 C CB  . GLU D 3 187 ? 16.198  85.126 -51.831 1.00 143.70 ? 187 GLU L CB  1 
ATOM   6918 C CG  . GLU D 3 187 ? 17.260  84.298 -52.525 1.00 145.26 ? 187 GLU L CG  1 
ATOM   6919 C CD  . GLU D 3 187 ? 16.918  84.037 -53.974 1.00 157.38 ? 187 GLU L CD  1 
ATOM   6920 O OE1 . GLU D 3 187 ? 15.773  84.338 -54.372 1.00 153.82 ? 187 GLU L OE1 1 
ATOM   6921 O OE2 . GLU D 3 187 ? 17.782  83.516 -54.710 1.00 167.57 ? 187 GLU L OE2 1 
ATOM   6922 N N   . LYS D 3 188 ? 15.530  87.596 -50.391 1.00 147.24 ? 188 LYS L N   1 
ATOM   6923 C CA  . LYS D 3 188 ? 14.780  88.800 -50.013 1.00 148.86 ? 188 LYS L CA  1 
ATOM   6924 C C   . LYS D 3 188 ? 15.270  89.416 -48.711 1.00 152.44 ? 188 LYS L C   1 
ATOM   6925 O O   . LYS D 3 188 ? 14.623  90.339 -48.173 1.00 158.08 ? 188 LYS L O   1 
ATOM   6926 C CB  . LYS D 3 188 ? 13.286  88.486 -49.882 1.00 154.14 ? 188 LYS L CB  1 
ATOM   6927 C CG  . LYS D 3 188 ? 12.621  88.062 -51.180 1.00 166.36 ? 188 LYS L CG  1 
ATOM   6928 C CD  . LYS D 3 188 ? 11.101  88.089 -51.098 1.00 178.38 ? 188 LYS L CD  1 
ATOM   6929 C CE  . LYS D 3 188 ? 10.492  88.002 -52.487 1.00 186.23 ? 188 LYS L CE  1 
ATOM   6930 N NZ  . LYS D 3 188 ? 9.020   87.853 -52.415 1.00 195.01 ? 188 LYS L NZ  1 
ATOM   6931 N N   . HIS D 3 189 ? 16.392  88.932 -48.180 1.00 139.71 ? 189 HIS L N   1 
ATOM   6932 C CA  . HIS D 3 189 ? 16.862  89.325 -46.859 1.00 132.43 ? 189 HIS L CA  1 
ATOM   6933 C C   . HIS D 3 189 ? 18.379  89.257 -46.830 1.00 132.32 ? 189 HIS L C   1 
ATOM   6934 O O   . HIS D 3 189 ? 18.959  88.267 -47.285 1.00 130.02 ? 189 HIS L O   1 
ATOM   6935 C CB  . HIS D 3 189 ? 16.285  88.411 -45.776 1.00 136.47 ? 189 HIS L CB  1 
ATOM   6936 C CG  . HIS D 3 189 ? 14.797  88.257 -45.849 1.00 142.14 ? 189 HIS L CG  1 
ATOM   6937 N ND1 . HIS D 3 189 ? 13.924  89.263 -45.491 1.00 134.10 ? 189 HIS L ND1 1 
ATOM   6938 C CD2 . HIS D 3 189 ? 14.026  87.223 -46.263 1.00 145.83 ? 189 HIS L CD2 1 
ATOM   6939 C CE1 . HIS D 3 189 ? 12.682  88.848 -45.662 1.00 138.53 ? 189 HIS L CE1 1 
ATOM   6940 N NE2 . HIS D 3 189 ? 12.716  87.615 -46.134 1.00 143.68 ? 189 HIS L NE2 1 
ATOM   6941 N N   . LYS D 3 190 ? 19.014  90.287 -46.266 1.00 132.84 ? 190 LYS L N   1 
ATOM   6942 C CA  . LYS D 3 190 ? 20.472  90.337 -46.221 1.00 132.09 ? 190 LYS L CA  1 
ATOM   6943 C C   . LYS D 3 190 ? 21.049  89.804 -44.914 1.00 128.84 ? 190 LYS L C   1 
ATOM   6944 O O   . LYS D 3 190 ? 22.040  89.070 -44.939 1.00 129.95 ? 190 LYS L O   1 
ATOM   6945 C CB  . LYS D 3 190 ? 20.964  91.769 -46.450 1.00 139.58 ? 190 LYS L CB  1 
ATOM   6946 C CG  . LYS D 3 190 ? 21.013  92.185 -47.912 1.00 146.70 ? 190 LYS L CG  1 
ATOM   6947 C CD  . LYS D 3 190 ? 21.460  93.630 -48.063 1.00 153.23 ? 190 LYS L CD  1 
ATOM   6948 C CE  . LYS D 3 190 ? 21.310  94.101 -49.502 1.00 151.15 ? 190 LYS L CE  1 
ATOM   6949 N NZ  . LYS D 3 190 ? 21.538  95.567 -49.639 1.00 144.79 ? 190 LYS L NZ  1 
ATOM   6950 N N   . VAL D 3 191 ? 20.460  90.151 -43.774 1.00 125.60 ? 191 VAL L N   1 
ATOM   6951 C CA  . VAL D 3 191 ? 21.040  89.822 -42.477 1.00 124.35 ? 191 VAL L CA  1 
ATOM   6952 C C   . VAL D 3 191 ? 20.063  88.965 -41.680 1.00 128.48 ? 191 VAL L C   1 
ATOM   6953 O O   . VAL D 3 191 ? 18.843  89.041 -41.861 1.00 131.02 ? 191 VAL L O   1 
ATOM   6954 C CB  . VAL D 3 191 ? 21.422  91.101 -41.695 1.00 124.70 ? 191 VAL L CB  1 
ATOM   6955 C CG1 . VAL D 3 191 ? 20.181  91.778 -41.142 1.00 121.98 ? 191 VAL L CG1 1 
ATOM   6956 C CG2 . VAL D 3 191 ? 22.415  90.786 -40.586 1.00 129.03 ? 191 VAL L CG2 1 
ATOM   6957 N N   . TYR D 3 192 ? 20.618  88.130 -40.799 1.00 126.89 ? 192 TYR L N   1 
ATOM   6958 C CA  . TYR D 3 192 ? 19.851  87.340 -39.845 1.00 123.20 ? 192 TYR L CA  1 
ATOM   6959 C C   . TYR D 3 192 ? 20.495  87.467 -38.474 1.00 120.49 ? 192 TYR L C   1 
ATOM   6960 O O   . TYR D 3 192 ? 21.724  87.522 -38.366 1.00 123.16 ? 192 TYR L O   1 
ATOM   6961 C CB  . TYR D 3 192 ? 19.781  85.870 -40.269 1.00 126.14 ? 192 TYR L CB  1 
ATOM   6962 C CG  . TYR D 3 192 ? 19.214  85.694 -41.653 1.00 123.50 ? 192 TYR L CG  1 
ATOM   6963 C CD1 . TYR D 3 192 ? 17.845  85.717 -41.859 1.00 123.92 ? 192 TYR L CD1 1 
ATOM   6964 C CD2 . TYR D 3 192 ? 20.043  85.541 -42.756 1.00 122.32 ? 192 TYR L CD2 1 
ATOM   6965 C CE1 . TYR D 3 192 ? 17.313  85.571 -43.116 1.00 123.36 ? 192 TYR L CE1 1 
ATOM   6966 C CE2 . TYR D 3 192 ? 19.518  85.395 -44.024 1.00 130.09 ? 192 TYR L CE2 1 
ATOM   6967 C CZ  . TYR D 3 192 ? 18.149  85.413 -44.194 1.00 127.68 ? 192 TYR L CZ  1 
ATOM   6968 O OH  . TYR D 3 192 ? 17.598  85.275 -45.443 1.00 133.66 ? 192 TYR L OH  1 
ATOM   6969 N N   . ALA D 3 193 ? 19.669  87.525 -37.427 1.00 120.41 ? 193 ALA L N   1 
ATOM   6970 C CA  . ALA D 3 193 ? 20.187  87.788 -36.092 1.00 123.04 ? 193 ALA L CA  1 
ATOM   6971 C C   . ALA D 3 193 ? 19.371  87.078 -35.020 1.00 120.65 ? 193 ALA L C   1 
ATOM   6972 O O   . ALA D 3 193 ? 18.143  86.988 -35.107 1.00 119.31 ? 193 ALA L O   1 
ATOM   6973 C CB  . ALA D 3 193 ? 20.215  89.294 -35.803 1.00 125.93 ? 193 ALA L CB  1 
ATOM   6974 N N   . CYS D 3 194 ? 20.081  86.578 -34.012 1.00 121.65 ? 194 CYS L N   1 
ATOM   6975 C CA  . CYS D 3 194 ? 19.485  86.127 -32.762 1.00 118.08 ? 194 CYS L CA  1 
ATOM   6976 C C   . CYS D 3 194 ? 19.592  87.241 -31.732 1.00 122.51 ? 194 CYS L C   1 
ATOM   6977 O O   . CYS D 3 194 ? 20.691  87.747 -31.476 1.00 127.34 ? 194 CYS L O   1 
ATOM   6978 C CB  . CYS D 3 194 ? 20.185  84.882 -32.214 1.00 117.72 ? 194 CYS L CB  1 
ATOM   6979 S SG  . CYS D 3 194 ? 20.487  83.552 -33.382 1.00 143.53 ? 194 CYS L SG  1 
ATOM   6980 N N   . GLU D 3 195 ? 18.457  87.614 -31.146 1.00 112.54 ? 195 GLU L N   1 
ATOM   6981 C CA  . GLU D 3 195 ? 18.416  88.474 -29.963 1.00 116.26 ? 195 GLU L CA  1 
ATOM   6982 C C   . GLU D 3 195 ? 18.218  87.568 -28.756 1.00 115.30 ? 195 GLU L C   1 
ATOM   6983 O O   . GLU D 3 195 ? 17.106  87.105 -28.500 1.00 116.91 ? 195 GLU L O   1 
ATOM   6984 C CB  . GLU D 3 195 ? 17.295  89.503 -30.052 1.00 122.12 ? 195 GLU L CB  1 
ATOM   6985 C CG  . GLU D 3 195 ? 17.546  90.648 -31.005 1.00 137.28 ? 195 GLU L CG  1 
ATOM   6986 C CD  . GLU D 3 195 ? 17.506  91.992 -30.304 1.00 147.22 ? 195 GLU L CD  1 
ATOM   6987 O OE1 . GLU D 3 195 ? 16.944  92.064 -29.191 1.00 146.47 ? 195 GLU L OE1 1 
ATOM   6988 O OE2 . GLU D 3 195 ? 18.037  92.975 -30.863 1.00 180.61 ? 195 GLU L OE2 1 
ATOM   6989 N N   . VAL D 3 196 ? 19.292  87.310 -28.017 1.00 115.43 ? 196 VAL L N   1 
ATOM   6990 C CA  . VAL D 3 196 ? 19.265  86.407 -26.878 1.00 109.98 ? 196 VAL L CA  1 
ATOM   6991 C C   . VAL D 3 196 ? 19.217  87.244 -25.609 1.00 108.40 ? 196 VAL L C   1 
ATOM   6992 O O   . VAL D 3 196 ? 20.050  88.138 -25.409 1.00 115.21 ? 196 VAL L O   1 
ATOM   6993 C CB  . VAL D 3 196 ? 20.487  85.473 -26.893 1.00 107.84 ? 196 VAL L CB  1 
ATOM   6994 C CG1 . VAL D 3 196 ? 20.855  85.042 -25.482 1.00 107.40 ? 196 VAL L CG1 1 
ATOM   6995 C CG2 . VAL D 3 196 ? 20.211  84.276 -27.789 1.00 112.86 ? 196 VAL L CG2 1 
ATOM   6996 N N   . THR D 3 197 ? 18.232  86.963 -24.760 1.00 109.67 ? 197 THR L N   1 
ATOM   6997 C CA  . THR D 3 197 ? 17.983  87.719 -23.541 1.00 110.50 ? 197 THR L CA  1 
ATOM   6998 C C   . THR D 3 197 ? 17.991  86.750 -22.371 1.00 108.35 ? 197 THR L C   1 
ATOM   6999 O O   . THR D 3 197 ? 17.199  85.797 -22.344 1.00 114.32 ? 197 THR L O   1 
ATOM   7000 C CB  . THR D 3 197 ? 16.647  88.458 -23.616 1.00 111.75 ? 197 THR L CB  1 
ATOM   7001 O OG1 . THR D 3 197 ? 15.607  87.527 -23.927 1.00 119.47 ? 197 THR L OG1 1 
ATOM   7002 C CG2 . THR D 3 197 ? 16.687  89.497 -24.711 1.00 111.51 ? 197 THR L CG2 1 
ATOM   7003 N N   . HIS D 3 198 ? 18.879  87.001 -21.410 1.00 97.14  ? 198 HIS L N   1 
ATOM   7004 C CA  . HIS D 3 198 ? 19.072  86.114 -20.275 1.00 98.54  ? 198 HIS L CA  1 
ATOM   7005 C C   . HIS D 3 198 ? 19.616  86.919 -19.105 1.00 101.06 ? 198 HIS L C   1 
ATOM   7006 O O   . HIS D 3 198 ? 20.176  88.005 -19.281 1.00 105.29 ? 198 HIS L O   1 
ATOM   7007 C CB  . HIS D 3 198 ? 20.017  84.960 -20.627 1.00 103.37 ? 198 HIS L CB  1 
ATOM   7008 C CG  . HIS D 3 198 ? 20.087  83.896 -19.577 1.00 94.66  ? 198 HIS L CG  1 
ATOM   7009 N ND1 . HIS D 3 198 ? 21.225  83.658 -18.837 1.00 92.44  ? 198 HIS L ND1 1 
ATOM   7010 C CD2 . HIS D 3 198 ? 19.157  83.021 -19.128 1.00 93.98  ? 198 HIS L CD2 1 
ATOM   7011 C CE1 . HIS D 3 198 ? 20.997  82.673 -17.988 1.00 95.62  ? 198 HIS L CE1 1 
ATOM   7012 N NE2 . HIS D 3 198 ? 19.749  82.269 -18.143 1.00 98.56  ? 198 HIS L NE2 1 
ATOM   7013 N N   . GLN D 3 199 ? 19.448  86.364 -17.902 1.00 105.56 ? 199 GLN L N   1 
ATOM   7014 C CA  . GLN D 3 199 ? 19.831  87.077 -16.687 1.00 108.79 ? 199 GLN L CA  1 
ATOM   7015 C C   . GLN D 3 199 ? 21.334  87.308 -16.622 1.00 108.79 ? 199 GLN L C   1 
ATOM   7016 O O   . GLN D 3 199 ? 21.786  88.369 -16.182 1.00 110.98 ? 199 GLN L O   1 
ATOM   7017 C CB  . GLN D 3 199 ? 19.360  86.300 -15.460 1.00 103.04 ? 199 GLN L CB  1 
ATOM   7018 C CG  . GLN D 3 199 ? 17.875  85.998 -15.444 1.00 110.27 ? 199 GLN L CG  1 
ATOM   7019 C CD  . GLN D 3 199 ? 17.442  85.324 -14.164 1.00 125.76 ? 199 GLN L CD  1 
ATOM   7020 O OE1 . GLN D 3 199 ? 18.270  85.023 -13.306 1.00 121.82 ? 199 GLN L OE1 1 
ATOM   7021 N NE2 . GLN D 3 199 ? 16.144  85.055 -14.039 1.00 134.57 ? 199 GLN L NE2 1 
ATOM   7022 N N   . GLY D 3 200 ? 22.125  86.331 -17.055 1.00 107.67 ? 200 GLY L N   1 
ATOM   7023 C CA  . GLY D 3 200 ? 23.571  86.476 -17.041 1.00 111.09 ? 200 GLY L CA  1 
ATOM   7024 C C   . GLY D 3 200 ? 24.119  87.490 -18.017 1.00 114.64 ? 200 GLY L C   1 
ATOM   7025 O O   . GLY D 3 200 ? 25.339  87.648 -18.098 1.00 116.35 ? 200 GLY L O   1 
ATOM   7026 N N   . LEU D 3 201 ? 23.257  88.182 -18.759 1.00 113.85 ? 201 LEU L N   1 
ATOM   7027 C CA  . LEU D 3 201 ? 23.660  89.196 -19.726 1.00 117.76 ? 201 LEU L CA  1 
ATOM   7028 C C   . LEU D 3 201 ? 23.055  90.526 -19.302 1.00 118.00 ? 201 LEU L C   1 
ATOM   7029 O O   . LEU D 3 201 ? 21.835  90.626 -19.132 1.00 120.45 ? 201 LEU L O   1 
ATOM   7030 C CB  . LEU D 3 201 ? 23.193  88.816 -21.131 1.00 111.76 ? 201 LEU L CB  1 
ATOM   7031 C CG  . LEU D 3 201 ? 23.649  87.440 -21.617 1.00 104.18 ? 201 LEU L CG  1 
ATOM   7032 C CD1 . LEU D 3 201 ? 22.977  87.078 -22.931 1.00 99.78  ? 201 LEU L CD1 1 
ATOM   7033 C CD2 . LEU D 3 201 ? 25.162  87.386 -21.746 1.00 114.72 ? 201 LEU L CD2 1 
ATOM   7034 N N   . SER D 3 202 ? 23.906  91.541 -19.130 1.00 124.61 ? 202 SER L N   1 
ATOM   7035 C CA  . SER D 3 202 ? 23.420  92.861 -18.735 1.00 132.91 ? 202 SER L CA  1 
ATOM   7036 C C   . SER D 3 202 ? 22.417  93.394 -19.750 1.00 134.87 ? 202 SER L C   1 
ATOM   7037 O O   . SER D 3 202 ? 21.267  93.699 -19.415 1.00 140.44 ? 202 SER L O   1 
ATOM   7038 C CB  . SER D 3 202 ? 24.596  93.827 -18.576 1.00 139.88 ? 202 SER L CB  1 
ATOM   7039 O OG  . SER D 3 202 ? 25.436  93.803 -19.715 1.00 136.37 ? 202 SER L OG  1 
ATOM   7040 N N   . SER D 3 203 ? 22.839  93.511 -21.003 1.00 128.68 ? 203 SER L N   1 
ATOM   7041 C CA  . SER D 3 203 ? 21.949  93.864 -22.091 1.00 132.37 ? 203 SER L CA  1 
ATOM   7042 C C   . SER D 3 203 ? 21.924  92.734 -23.114 1.00 127.43 ? 203 SER L C   1 
ATOM   7043 O O   . SER D 3 203 ? 22.919  92.019 -23.274 1.00 125.14 ? 203 SER L O   1 
ATOM   7044 C CB  . SER D 3 203 ? 22.386  95.168 -22.768 1.00 140.68 ? 203 SER L CB  1 
ATOM   7045 O OG  . SER D 3 203 ? 23.643  95.014 -23.404 1.00 189.55 ? 203 SER L OG  1 
ATOM   7046 N N   . PRO D 3 204 ? 20.783  92.530 -23.798 1.00 124.24 ? 204 PRO L N   1 
ATOM   7047 C CA  . PRO D 3 204 ? 20.657  91.417 -24.751 1.00 121.34 ? 204 PRO L CA  1 
ATOM   7048 C C   . PRO D 3 204 ? 21.834  91.261 -25.695 1.00 126.76 ? 204 PRO L C   1 
ATOM   7049 O O   . PRO D 3 204 ? 22.390  92.249 -26.183 1.00 130.08 ? 204 PRO L O   1 
ATOM   7050 C CB  . PRO D 3 204 ? 19.392  91.785 -25.531 1.00 122.56 ? 204 PRO L CB  1 
ATOM   7051 C CG  . PRO D 3 204 ? 18.551  92.479 -24.526 1.00 125.42 ? 204 PRO L CG  1 
ATOM   7052 C CD  . PRO D 3 204 ? 19.485  93.185 -23.560 1.00 123.07 ? 204 PRO L CD  1 
ATOM   7053 N N   . VAL D 3 205 ? 22.217  90.021 -25.965 1.00 124.16 ? 205 VAL L N   1 
ATOM   7054 C CA  . VAL D 3 205 ? 23.294  89.729 -26.899 1.00 117.93 ? 205 VAL L CA  1 
ATOM   7055 C C   . VAL D 3 205 ? 22.662  89.298 -28.212 1.00 121.39 ? 205 VAL L C   1 
ATOM   7056 O O   . VAL D 3 205 ? 21.983  88.270 -28.284 1.00 123.48 ? 205 VAL L O   1 
ATOM   7057 C CB  . VAL D 3 205 ? 24.247  88.656 -26.358 1.00 117.27 ? 205 VAL L CB  1 
ATOM   7058 C CG1 . VAL D 3 205 ? 25.090  88.080 -27.486 1.00 115.01 ? 205 VAL L CG1 1 
ATOM   7059 C CG2 . VAL D 3 205 ? 25.138  89.247 -25.283 1.00 123.12 ? 205 VAL L CG2 1 
ATOM   7060 N N   . THR D 3 206 ? 22.850  90.095 -29.249 1.00 131.69 ? 206 THR L N   1 
ATOM   7061 C CA  . THR D 3 206 ? 22.510  89.643 -30.582 1.00 123.21 ? 206 THR L CA  1 
ATOM   7062 C C   . THR D 3 206 ? 23.759  89.090 -31.244 1.00 124.65 ? 206 THR L C   1 
ATOM   7063 O O   . THR D 3 206 ? 24.877  89.555 -31.010 1.00 120.56 ? 206 THR L O   1 
ATOM   7064 C CB  . THR D 3 206 ? 21.935  90.769 -31.438 1.00 121.51 ? 206 THR L CB  1 
ATOM   7065 O OG1 . THR D 3 206 ? 22.999  91.616 -31.884 1.00 134.60 ? 206 THR L OG1 1 
ATOM   7066 C CG2 . THR D 3 206 ? 20.954  91.589 -30.634 1.00 120.60 ? 206 THR L CG2 1 
ATOM   7067 N N   . LYS D 3 207 ? 23.562  88.061 -32.043 1.00 120.18 ? 207 LYS L N   1 
ATOM   7068 C CA  . LYS D 3 207 ? 24.591  87.622 -32.967 1.00 118.09 ? 207 LYS L CA  1 
ATOM   7069 C C   . LYS D 3 207 ? 23.971  87.640 -34.357 1.00 118.96 ? 207 LYS L C   1 
ATOM   7070 O O   . LYS D 3 207 ? 22.748  87.579 -34.503 1.00 121.31 ? 207 LYS L O   1 
ATOM   7071 C CB  . LYS D 3 207 ? 25.149  86.241 -32.571 1.00 116.49 ? 207 LYS L CB  1 
ATOM   7072 C CG  . LYS D 3 207 ? 26.449  85.858 -33.277 1.00 124.77 ? 207 LYS L CG  1 
ATOM   7073 C CD  . LYS D 3 207 ? 26.830  84.397 -33.023 1.00 133.11 ? 207 LYS L CD  1 
ATOM   7074 C CE  . LYS D 3 207 ? 27.767  83.860 -34.109 1.00 140.06 ? 207 LYS L CE  1 
ATOM   7075 N NZ  . LYS D 3 207 ? 28.448  82.620 -33.668 1.00 145.66 ? 207 LYS L NZ  1 
ATOM   7076 N N   . SER D 3 208 ? 24.797  87.791 -35.394 1.00 126.16 ? 208 SER L N   1 
ATOM   7077 C CA  . SER D 3 208 ? 24.187  87.961 -36.739 1.00 124.83 ? 208 SER L CA  1 
ATOM   7078 C C   . SER D 3 208 ? 25.104  87.539 -37.887 1.00 126.62 ? 208 SER L C   1 
ATOM   7079 O O   . SER D 3 208 ? 26.334  87.616 -37.723 1.00 127.31 ? 208 SER L O   1 
ATOM   7080 C CB  . SER D 3 208 ? 23.774  89.393 -36.918 1.00 123.58 ? 208 SER L CB  1 
ATOM   7081 O OG  . SER D 3 208 ? 24.883  90.259 -36.730 1.00 124.53 ? 208 SER L OG  1 
ATOM   7082 N N   . PHE D 3 209 ? 24.511  87.118 -39.008 1.00 125.33 ? 209 PHE L N   1 
ATOM   7083 C CA  . PHE D 3 209 ? 25.300  86.781 -40.222 1.00 133.27 ? 209 PHE L CA  1 
ATOM   7084 C C   . PHE D 3 209 ? 24.538  87.347 -41.421 1.00 137.13 ? 209 PHE L C   1 
ATOM   7085 O O   . PHE D 3 209 ? 23.295  87.355 -41.372 1.00 138.30 ? 209 PHE L O   1 
ATOM   7086 C CB  . PHE D 3 209 ? 25.534  85.274 -40.351 1.00 133.66 ? 209 PHE L CB  1 
ATOM   7087 C CG  . PHE D 3 209 ? 24.451  84.497 -41.053 1.00 131.13 ? 209 PHE L CG  1 
ATOM   7088 C CD1 . PHE D 3 209 ? 23.225  84.275 -40.450 1.00 131.39 ? 209 PHE L CD1 1 
ATOM   7089 C CD2 . PHE D 3 209 ? 24.656  83.996 -42.328 1.00 129.68 ? 209 PHE L CD2 1 
ATOM   7090 C CE1 . PHE D 3 209 ? 22.236  83.555 -41.101 1.00 127.91 ? 209 PHE L CE1 1 
ATOM   7091 C CE2 . PHE D 3 209 ? 23.663  83.284 -42.981 1.00 122.19 ? 209 PHE L CE2 1 
ATOM   7092 C CZ  . PHE D 3 209 ? 22.455  83.063 -42.365 1.00 120.91 ? 209 PHE L CZ  1 
ATOM   7093 N N   . ASN D 3 210 ? 25.268  87.823 -42.433 1.00 137.56 ? 210 ASN L N   1 
ATOM   7094 C CA  . ASN D 3 210 ? 24.621  88.448 -43.617 1.00 134.27 ? 210 ASN L CA  1 
ATOM   7095 C C   . ASN D 3 210 ? 24.987  87.656 -44.877 1.00 142.82 ? 210 ASN L C   1 
ATOM   7096 O O   . ASN D 3 210 ? 24.971  88.252 -45.973 1.00 155.32 ? 210 ASN L O   1 
ATOM   7097 C CB  . ASN D 3 210 ? 24.992  89.928 -43.746 1.00 142.78 ? 210 ASN L CB  1 
ATOM   7098 C CG  . ASN D 3 210 ? 26.483  90.178 -43.658 1.00 154.58 ? 210 ASN L CG  1 
ATOM   7099 O OD1 . ASN D 3 210 ? 27.267  89.248 -43.482 1.00 159.25 ? 210 ASN L OD1 1 
ATOM   7100 N ND2 . ASN D 3 210 ? 26.884  91.433 -43.774 1.00 154.39 ? 210 ASN L ND2 1 
ATOM   7101 N N   . ARG D 3 211 ? 25.291  86.365 -44.722 1.00 148.09 ? 211 ARG L N   1 
ATOM   7102 C CA  . ARG D 3 211 ? 25.627  85.511 -45.892 1.00 153.64 ? 211 ARG L CA  1 
ATOM   7103 C C   . ARG D 3 211 ? 24.326  85.114 -46.596 1.00 156.10 ? 211 ARG L C   1 
ATOM   7104 O O   . ARG D 3 211 ? 23.706  84.121 -46.171 1.00 163.88 ? 211 ARG L O   1 
ATOM   7105 C CB  . ARG D 3 211 ? 26.417  84.277 -45.445 1.00 149.46 ? 211 ARG L CB  1 
ATOM   7106 C CG  . ARG D 3 211 ? 26.882  83.388 -46.590 1.00 145.53 ? 211 ARG L CG  1 
ATOM   7107 C CD  . ARG D 3 211 ? 27.612  82.154 -46.094 1.00 157.68 ? 211 ARG L CD  1 
ATOM   7108 N NE  . ARG D 3 211 ? 28.063  81.304 -47.186 1.00 151.63 ? 211 ARG L NE  1 
ATOM   7109 C CZ  . ARG D 3 211 ? 29.332  80.992 -47.419 1.00 147.36 ? 211 ARG L CZ  1 
ATOM   7110 N NH1 . ARG D 3 211 ? 30.285  81.464 -46.636 1.00 139.79 ? 211 ARG L NH1 1 
ATOM   7111 N NH2 . ARG D 3 211 ? 29.644  80.207 -48.437 1.00 144.71 ? 211 ARG L NH2 1 
ATOM   7112 N N   . GLY D 3 212 ? 23.930  85.871 -47.624 1.00 139.54 ? 212 GLY L N   1 
ATOM   7113 C CA  . GLY D 3 212 ? 22.675  85.587 -48.347 1.00 131.80 ? 212 GLY L CA  1 
ATOM   7114 C C   . GLY D 3 212 ? 21.507  86.368 -47.770 1.00 132.01 ? 212 GLY L C   1 
ATOM   7115 O O   . GLY D 3 212 ? 21.440  86.458 -46.527 1.00 136.78 ? 212 GLY L O   1 
HETATM 7116 C C1  . NAG E 4 .   ? 44.692  81.092 45.839  1.00 190.71 ? 1   NAG S C1  1 
HETATM 7117 C C2  . NAG E 4 .   ? 43.208  81.466 45.747  1.00 187.28 ? 1   NAG S C2  1 
HETATM 7118 C C3  . NAG E 4 .   ? 42.285  80.297 46.113  1.00 191.33 ? 1   NAG S C3  1 
HETATM 7119 C C4  . NAG E 4 .   ? 42.724  79.490 47.334  1.00 191.66 ? 1   NAG S C4  1 
HETATM 7120 C C5  . NAG E 4 .   ? 44.108  79.920 47.805  1.00 196.91 ? 1   NAG S C5  1 
HETATM 7121 C C6  . NAG E 4 .   ? 44.725  78.946 48.777  1.00 183.62 ? 1   NAG S C6  1 
HETATM 7122 C C7  . NAG E 4 .   ? 42.008  83.566 46.097  1.00 176.48 ? 1   NAG S C7  1 
HETATM 7123 C C8  . NAG E 4 .   ? 41.797  84.740 47.003  1.00 161.71 ? 1   NAG S C8  1 
HETATM 7124 N N2  . NAG E 4 .   ? 42.890  82.657 46.512  1.00 175.28 ? 1   NAG S N2  1 
HETATM 7125 O O3  . NAG E 4 .   ? 42.185  79.450 44.977  1.00 209.83 ? 1   NAG S O3  1 
HETATM 7126 O O4  . NAG E 4 .   ? 41.808  79.632 48.421  1.00 189.32 ? 1   NAG S O4  1 
HETATM 7127 O O5  . NAG E 4 .   ? 44.972  79.973 46.658  1.00 225.88 ? 1   NAG S O5  1 
HETATM 7128 O O6  . NAG E 4 .   ? 43.732  78.114 49.371  1.00 171.54 ? 1   NAG S O6  1 
HETATM 7129 O O7  . NAG E 4 .   ? 41.402  83.448 45.037  1.00 162.57 ? 1   NAG S O7  1 
HETATM 7130 C C1  . NAG E 4 .   ? 40.858  80.690 48.234  1.00 211.06 ? 2   NAG S C1  1 
HETATM 7131 C C2  . NAG E 4 .   ? 41.099  81.785 49.273  1.00 214.58 ? 2   NAG S C2  1 
HETATM 7132 C C3  . NAG E 4 .   ? 39.761  82.317 49.769  1.00 213.35 ? 2   NAG S C3  1 
HETATM 7133 C C4  . NAG E 4 .   ? 38.814  82.549 48.598  1.00 208.26 ? 2   NAG S C4  1 
HETATM 7134 C C5  . NAG E 4 .   ? 38.557  81.223 47.887  1.00 215.11 ? 2   NAG S C5  1 
HETATM 7135 C C6  . NAG E 4 .   ? 38.681  81.305 46.382  1.00 205.05 ? 2   NAG S C6  1 
HETATM 7136 C C7  . NAG E 4 .   ? 42.914  82.060 50.889  1.00 212.84 ? 2   NAG S C7  1 
HETATM 7137 C C8  . NAG E 4 .   ? 43.556  83.041 49.958  1.00 201.28 ? 2   NAG S C8  1 
HETATM 7138 N N2  . NAG E 4 .   ? 41.915  81.335 50.382  1.00 212.33 ? 2   NAG S N2  1 
HETATM 7139 O O3  . NAG E 4 .   ? 40.000  83.508 50.505  1.00 213.44 ? 2   NAG S O3  1 
HETATM 7140 O O4  . NAG E 4 .   ? 37.563  83.042 49.071  1.00 209.63 ? 2   NAG S O4  1 
HETATM 7141 O O5  . NAG E 4 .   ? 39.516  80.241 48.328  1.00 211.70 ? 2   NAG S O5  1 
HETATM 7142 O O6  . NAG E 4 .   ? 38.991  82.621 45.939  1.00 193.96 ? 2   NAG S O6  1 
HETATM 7143 O O7  . NAG E 4 .   ? 43.282  81.932 52.052  1.00 200.97 ? 2   NAG S O7  1 
HETATM 7144 C C1  . BMA E 4 .   ? 37.519  84.480 49.048  1.00 206.02 ? 3   BMA S C1  1 
HETATM 7145 C C2  . BMA E 4 .   ? 37.730  85.030 47.657  1.00 197.83 ? 3   BMA S C2  1 
HETATM 7146 C C3  . BMA E 4 .   ? 37.728  86.544 47.666  1.00 195.27 ? 3   BMA S C3  1 
HETATM 7147 C C4  . BMA E 4 .   ? 36.491  87.069 48.374  1.00 192.45 ? 3   BMA S C4  1 
HETATM 7148 C C5  . BMA E 4 .   ? 36.380  86.453 49.762  1.00 189.43 ? 3   BMA S C5  1 
HETATM 7149 C C6  . BMA E 4 .   ? 35.127  86.868 50.495  1.00 175.41 ? 3   BMA S C6  1 
HETATM 7150 O O2  . BMA E 4 .   ? 36.733  84.520 46.777  1.00 201.42 ? 3   BMA S O2  1 
HETATM 7151 O O3  . BMA E 4 .   ? 37.772  87.026 46.325  1.00 199.55 ? 3   BMA S O3  1 
HETATM 7152 O O4  . BMA E 4 .   ? 36.565  88.485 48.501  1.00 186.70 ? 3   BMA S O4  1 
HETATM 7153 O O5  . BMA E 4 .   ? 36.335  85.024 49.632  1.00 199.80 ? 3   BMA S O5  1 
HETATM 7154 O O6  . BMA E 4 .   ? 35.443  87.536 51.714  1.00 148.46 ? 3   BMA S O6  1 
HETATM 7155 C C1  . NAG F 4 .   ? 31.334  18.727 5.804   1.00 178.34 ? 1   NAG C C1  1 
HETATM 7156 C C2  . NAG F 4 .   ? 32.850  18.544 5.716   1.00 178.34 ? 1   NAG C C2  1 
HETATM 7157 C C3  . NAG F 4 .   ? 33.481  19.538 4.745   1.00 178.34 ? 1   NAG C C3  1 
HETATM 7158 C C4  . NAG F 4 .   ? 32.696  19.657 3.446   1.00 178.34 ? 1   NAG C C4  1 
HETATM 7159 C C5  . NAG F 4 .   ? 31.229  19.925 3.759   1.00 178.34 ? 1   NAG C C5  1 
HETATM 7160 C C6  . NAG F 4 .   ? 30.356  20.033 2.532   1.00 178.34 ? 1   NAG C C6  1 
HETATM 7161 C C7  . NAG F 4 .   ? 34.447  17.955 7.477   1.00 178.34 ? 1   NAG C C7  1 
HETATM 7162 C C8  . NAG F 4 .   ? 34.448  16.523 7.040   1.00 178.34 ? 1   NAG C C8  1 
HETATM 7163 N N2  . NAG F 4 .   ? 33.439  18.702 7.028   1.00 178.34 ? 1   NAG C N2  1 
HETATM 7164 O O3  . NAG F 4 .   ? 34.821  19.138 4.494   1.00 178.34 ? 1   NAG C O3  1 
HETATM 7165 O O4  . NAG F 4 .   ? 33.226  20.757 2.713   1.00 178.34 ? 1   NAG C O4  1 
HETATM 7166 O O5  . NAG F 4 .   ? 30.718  18.825 4.532   1.00 178.34 ? 1   NAG C O5  1 
HETATM 7167 O O6  . NAG F 4 .   ? 30.586  21.261 1.849   1.00 178.34 ? 1   NAG C O6  1 
HETATM 7168 O O7  . NAG F 4 .   ? 35.320  18.417 8.203   1.00 178.34 ? 1   NAG C O7  1 
HETATM 7169 C C1  . NAG F 4 .   ? 33.686  20.343 1.413   1.00 190.29 ? 2   NAG C C1  1 
HETATM 7170 C C2  . NAG F 4 .   ? 35.205  20.281 1.272   1.00 190.29 ? 2   NAG C C2  1 
HETATM 7171 C C3  . NAG F 4 .   ? 35.565  20.110 -0.200  1.00 190.29 ? 2   NAG C C3  1 
HETATM 7172 C C4  . NAG F 4 .   ? 34.828  18.931 -0.825  1.00 190.29 ? 2   NAG C C4  1 
HETATM 7173 C C5  . NAG F 4 .   ? 33.339  18.988 -0.491  1.00 190.29 ? 2   NAG C C5  1 
HETATM 7174 C C6  . NAG F 4 .   ? 32.593  17.742 -0.903  1.00 190.29 ? 2   NAG C C6  1 
HETATM 7175 C C7  . NAG F 4 .   ? 36.275  21.501 3.092   1.00 190.29 ? 2   NAG C C7  1 
HETATM 7176 C C8  . NAG F 4 .   ? 35.898  22.730 3.860   1.00 190.29 ? 2   NAG C C8  1 
HETATM 7177 N N2  . NAG F 4 .   ? 35.852  21.449 1.829   1.00 190.29 ? 2   NAG C N2  1 
HETATM 7178 O O3  . NAG F 4 .   ? 36.972  19.948 -0.310  1.00 190.29 ? 2   NAG C O3  1 
HETATM 7179 O O4  . NAG F 4 .   ? 34.960  19.017 -2.240  1.00 190.29 ? 2   NAG C O4  1 
HETATM 7180 O O5  . NAG F 4 .   ? 33.158  19.122 0.931   1.00 190.29 ? 2   NAG C O5  1 
HETATM 7181 O O6  . NAG F 4 .   ? 33.379  16.575 -0.680  1.00 190.29 ? 2   NAG C O6  1 
HETATM 7182 O O7  . NAG F 4 .   ? 36.920  20.588 3.598   1.00 190.29 ? 2   NAG C O7  1 
HETATM 7183 C C1  . BMA F 4 .   ? 35.809  17.968 -2.734  1.00 210.45 ? 3   BMA C C1  1 
HETATM 7184 C C2  . BMA F 4 .   ? 35.059  17.229 -3.822  1.00 210.45 ? 3   BMA C C2  1 
HETATM 7185 C C3  . BMA F 4 .   ? 35.935  16.197 -4.503  1.00 210.45 ? 3   BMA C C3  1 
HETATM 7186 C C4  . BMA F 4 .   ? 37.244  16.820 -4.951  1.00 210.45 ? 3   BMA C C4  1 
HETATM 7187 C C5  . BMA F 4 .   ? 37.919  17.515 -3.778  1.00 210.45 ? 3   BMA C C5  1 
HETATM 7188 C C6  . BMA F 4 .   ? 39.187  18.234 -4.172  1.00 210.45 ? 3   BMA C C6  1 
HETATM 7189 O O2  . BMA F 4 .   ? 34.543  18.159 -4.770  1.00 210.45 ? 3   BMA C O2  1 
HETATM 7190 O O3  . BMA F 4 .   ? 35.242  15.649 -5.624  1.00 210.45 ? 3   BMA C O3  1 
HETATM 7191 O O4  . BMA F 4 .   ? 38.116  15.815 -5.459  1.00 210.45 ? 3   BMA C O4  1 
HETATM 7192 O O5  . BMA F 4 .   ? 37.027  18.508 -3.249  1.00 210.45 ? 3   BMA C O5  1 
HETATM 7193 O O6  . BMA F 4 .   ? 39.647  19.084 -3.124  1.00 210.45 ? 3   BMA C O6  1 
HETATM 7194 C C1  . NAG G 5 .   ? 34.878  51.762 2.218   1.00 160.04 ? 601 NAG A C1  1 
HETATM 7195 C C2  . NAG G 5 .   ? 35.380  53.088 1.642   1.00 161.42 ? 601 NAG A C2  1 
HETATM 7196 C C3  . NAG G 5 .   ? 34.896  53.226 0.204   1.00 163.60 ? 601 NAG A C3  1 
HETATM 7197 C C4  . NAG G 5 .   ? 35.396  52.058 -0.634  1.00 160.24 ? 601 NAG A C4  1 
HETATM 7198 C C5  . NAG G 5 .   ? 35.033  50.741 0.048   1.00 157.52 ? 601 NAG A C5  1 
HETATM 7199 C C6  . NAG G 5 .   ? 36.238  49.938 0.499   1.00 147.36 ? 601 NAG A C6  1 
HETATM 7200 C C7  . NAG G 5 .   ? 35.775  54.692 3.412   1.00 157.17 ? 601 NAG A C7  1 
HETATM 7201 C C8  . NAG G 5 .   ? 37.073  55.288 2.965   1.00 153.75 ? 601 NAG A C8  1 
HETATM 7202 N N2  . NAG G 5 .   ? 34.986  54.223 2.447   1.00 158.73 ? 601 NAG A N2  1 
HETATM 7203 O O3  . NAG G 5 .   ? 35.340  54.465 -0.331  1.00 155.25 ? 601 NAG A O3  1 
HETATM 7204 O O4  . NAG G 5 .   ? 34.773  52.104 -1.914  1.00 151.58 ? 601 NAG A O4  1 
HETATM 7205 O O5  . NAG G 5 .   ? 34.226  50.996 1.217   1.00 176.24 ? 601 NAG A O5  1 
HETATM 7206 O O6  . NAG G 5 .   ? 37.457  50.655 0.314   1.00 149.55 ? 601 NAG A O6  1 
HETATM 7207 O O7  . NAG G 5 .   ? 35.459  54.628 4.596   1.00 158.41 ? 601 NAG A O7  1 
# 
