data_8Y20
# 
_entry.id   8Y20 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8Y20         pdb_00008y20 10.2210/pdb8y20/pdb 
WWPDB D_1300044688 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-01-29 
2 'Structure model' 1 1 2025-02-19 
# 
_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 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8Y20 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 yonghenc@163.com   Yongheng Chen ? 'principal investigator/group leader' 0000-0001-8139-6892 
3 hudiewei18@163.com Hudie    Wei  ? 'principal investigator/group leader' 0000-0003-2072-2169 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wang, H.' 1 ? 
'Guo, M.'  2 ? 
'Wei, H.'  3 ? 
'Chen, Y.' 4 ? 
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? UK ? ? primary 'Cell Death Differ.' ? ? 1350-9047 ? ? ? ? ? ? 
'Deciphering molecular specificity in MCL-1/BAK interaction and its implications for designing potent MCL-1 inhibitors.' 2025 ? 
10.1038/s41418-025-01454-2  39901037 ? ? 
? ? ? ? ? ? ? US ? ? 1       'Res Sq'             ? ? 2693-5015 ? ? ? ? ? ? 
'Deciphering Molecular Specificity in MCL-1/BAK Interaction and Its Implications for Designing Potent MCL-1 Inhibitors'  2024 ? 
10.21203/rs.3.rs-4708498/v1 ?        ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wei, H.'   1  0000-0003-2072-2169 
primary 'Wang, H.'  2  ?                   
primary 'Xiang, S.' 3  0009-0006-6885-9390 
primary 'Wang, J.'  4  ?                   
primary 'Qu, L.'    5  ?                   
primary 'Chen, X.'  6  ?                   
primary 'Guo, M.'   7  0000-0002-7100-8443 
primary 'Lu, X.'    8  0000-0001-7931-6873 
primary 'Chen, Y.'  9  0000-0001-8139-6892 
1       'Chen, Y.'  10 ?                   
1       'Wei, H.'   11 ?                   
1       'Wang, H.'  12 ?                   
1       'Xiang, S.' 13 ?                   
1       'Wang, J.'  14 ?                   
1       'Qu, L.'    15 ?                   
1       'Chen, X.'  16 ?                   
1       'Guo, M.'   17 ?                   
1       'Lu, X.'    18 ?                   
# 
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 'Maltose/maltodextrin-binding periplasmic protein,Induced myeloid leukemia cell differentiation protein Mcl-1' 
57225.867 1   ? E173A,N174A,K240A,K391A,K394A,R398A ? ? 
2 branched    man 'alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose'                                                            
342.297   1   ? ?                                   ? ? 
3 non-polymer syn A-1210477                                                                                                      
850.037   1   ? ?                                   ? ? 
4 water       nat water                                                                                                          
18.015    142 ? ?                                   ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'MMBP,Maltodextrin-binding protein,Maltose-binding protein,MBP,Bcl-2-like protein 3,Bcl2-L-3,Bcl-2-related protein EAT/mcl1,mcl1/EAT' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEI
TPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWP
LIAADGGYAFKYAAGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA
VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAA
TMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTGSELYRQSLEIISRYLREQATGAADTAPMGASG
ATSRKALETLRRVGDGVQRNHETAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQ
ESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEI
TPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWP
LIAADGGYAFKYAAGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA
VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAA
TMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTGSELYRQSLEIISRYLREQATGAADTAPMGASG
ATSRKALETLRRVGDGVQRNHETAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQ
ESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHV
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 A-1210477 A1LXV 
4 water     HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   ILE n 
1 4   GLU n 
1 5   GLU n 
1 6   GLY n 
1 7   LYS n 
1 8   LEU n 
1 9   VAL n 
1 10  ILE n 
1 11  TRP n 
1 12  ILE n 
1 13  ASN n 
1 14  GLY n 
1 15  ASP n 
1 16  LYS n 
1 17  GLY n 
1 18  TYR n 
1 19  ASN n 
1 20  GLY n 
1 21  LEU n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  GLY n 
1 26  LYS n 
1 27  LYS n 
1 28  PHE n 
1 29  GLU n 
1 30  LYS n 
1 31  ASP n 
1 32  THR n 
1 33  GLY n 
1 34  ILE n 
1 35  LYS n 
1 36  VAL n 
1 37  THR n 
1 38  VAL n 
1 39  GLU n 
1 40  HIS n 
1 41  PRO n 
1 42  ASP n 
1 43  LYS n 
1 44  LEU n 
1 45  GLU n 
1 46  GLU n 
1 47  LYS n 
1 48  PHE n 
1 49  PRO n 
1 50  GLN n 
1 51  VAL n 
1 52  ALA n 
1 53  ALA n 
1 54  THR n 
1 55  GLY n 
1 56  ASP n 
1 57  GLY n 
1 58  PRO n 
1 59  ASP n 
1 60  ILE n 
1 61  ILE n 
1 62  PHE n 
1 63  TRP n 
1 64  ALA n 
1 65  HIS n 
1 66  ASP n 
1 67  ARG n 
1 68  PHE n 
1 69  GLY n 
1 70  GLY n 
1 71  TYR n 
1 72  ALA n 
1 73  GLN n 
1 74  SER n 
1 75  GLY n 
1 76  LEU n 
1 77  LEU n 
1 78  ALA n 
1 79  GLU n 
1 80  ILE n 
1 81  THR n 
1 82  PRO n 
1 83  ASP n 
1 84  LYS n 
1 85  ALA n 
1 86  PHE n 
1 87  GLN n 
1 88  ASP n 
1 89  LYS n 
1 90  LEU n 
1 91  TYR n 
1 92  PRO n 
1 93  PHE n 
1 94  THR n 
1 95  TRP n 
1 96  ASP n 
1 97  ALA n 
1 98  VAL n 
1 99  ARG n 
1 100 TYR n 
1 101 ASN n 
1 102 GLY n 
1 103 LYS n 
1 104 LEU n 
1 105 ILE n 
1 106 ALA n 
1 107 TYR n 
1 108 PRO n 
1 109 ILE n 
1 110 ALA n 
1 111 VAL n 
1 112 GLU n 
1 113 ALA n 
1 114 LEU n 
1 115 SER n 
1 116 LEU n 
1 117 ILE n 
1 118 TYR n 
1 119 ASN n 
1 120 LYS n 
1 121 ASP n 
1 122 LEU n 
1 123 LEU n 
1 124 PRO n 
1 125 ASN n 
1 126 PRO n 
1 127 PRO n 
1 128 LYS n 
1 129 THR n 
1 130 TRP n 
1 131 GLU n 
1 132 GLU n 
1 133 ILE n 
1 134 PRO n 
1 135 ALA n 
1 136 LEU n 
1 137 ASP n 
1 138 LYS n 
1 139 GLU n 
1 140 LEU n 
1 141 LYS n 
1 142 ALA n 
1 143 LYS n 
1 144 GLY n 
1 145 LYS n 
1 146 SER n 
1 147 ALA n 
1 148 LEU n 
1 149 MET n 
1 150 PHE n 
1 151 ASN n 
1 152 LEU n 
1 153 GLN n 
1 154 GLU n 
1 155 PRO n 
1 156 TYR n 
1 157 PHE n 
1 158 THR n 
1 159 TRP n 
1 160 PRO n 
1 161 LEU n 
1 162 ILE n 
1 163 ALA n 
1 164 ALA n 
1 165 ASP n 
1 166 GLY n 
1 167 GLY n 
1 168 TYR n 
1 169 ALA n 
1 170 PHE n 
1 171 LYS n 
1 172 TYR n 
1 173 ALA n 
1 174 ALA n 
1 175 GLY n 
1 176 LYS n 
1 177 TYR n 
1 178 ASP n 
1 179 ILE n 
1 180 LYS n 
1 181 ASP n 
1 182 VAL n 
1 183 GLY n 
1 184 VAL n 
1 185 ASP n 
1 186 ASN n 
1 187 ALA n 
1 188 GLY n 
1 189 ALA n 
1 190 LYS n 
1 191 ALA n 
1 192 GLY n 
1 193 LEU n 
1 194 THR n 
1 195 PHE n 
1 196 LEU n 
1 197 VAL n 
1 198 ASP n 
1 199 LEU n 
1 200 ILE n 
1 201 LYS n 
1 202 ASN n 
1 203 LYS n 
1 204 HIS n 
1 205 MET n 
1 206 ASN n 
1 207 ALA n 
1 208 ASP n 
1 209 THR n 
1 210 ASP n 
1 211 TYR n 
1 212 SER n 
1 213 ILE n 
1 214 ALA n 
1 215 GLU n 
1 216 ALA n 
1 217 ALA n 
1 218 PHE n 
1 219 ASN n 
1 220 LYS n 
1 221 GLY n 
1 222 GLU n 
1 223 THR n 
1 224 ALA n 
1 225 MET n 
1 226 THR n 
1 227 ILE n 
1 228 ASN n 
1 229 GLY n 
1 230 PRO n 
1 231 TRP n 
1 232 ALA n 
1 233 TRP n 
1 234 SER n 
1 235 ASN n 
1 236 ILE n 
1 237 ASP n 
1 238 THR n 
1 239 SER n 
1 240 ALA n 
1 241 VAL n 
1 242 ASN n 
1 243 TYR n 
1 244 GLY n 
1 245 VAL n 
1 246 THR n 
1 247 VAL n 
1 248 LEU n 
1 249 PRO n 
1 250 THR n 
1 251 PHE n 
1 252 LYS n 
1 253 GLY n 
1 254 GLN n 
1 255 PRO n 
1 256 SER n 
1 257 LYS n 
1 258 PRO n 
1 259 PHE n 
1 260 VAL n 
1 261 GLY n 
1 262 VAL n 
1 263 LEU n 
1 264 SER n 
1 265 ALA n 
1 266 GLY n 
1 267 ILE n 
1 268 ASN n 
1 269 ALA n 
1 270 ALA n 
1 271 SER n 
1 272 PRO n 
1 273 ASN n 
1 274 LYS n 
1 275 GLU n 
1 276 LEU n 
1 277 ALA n 
1 278 LYS n 
1 279 GLU n 
1 280 PHE n 
1 281 LEU n 
1 282 GLU n 
1 283 ASN n 
1 284 TYR n 
1 285 LEU n 
1 286 LEU n 
1 287 THR n 
1 288 ASP n 
1 289 GLU n 
1 290 GLY n 
1 291 LEU n 
1 292 GLU n 
1 293 ALA n 
1 294 VAL n 
1 295 ASN n 
1 296 LYS n 
1 297 ASP n 
1 298 LYS n 
1 299 PRO n 
1 300 LEU n 
1 301 GLY n 
1 302 ALA n 
1 303 VAL n 
1 304 ALA n 
1 305 LEU n 
1 306 LYS n 
1 307 SER n 
1 308 TYR n 
1 309 GLU n 
1 310 GLU n 
1 311 GLU n 
1 312 LEU n 
1 313 ALA n 
1 314 LYS n 
1 315 ASP n 
1 316 PRO n 
1 317 ARG n 
1 318 ILE n 
1 319 ALA n 
1 320 ALA n 
1 321 THR n 
1 322 MET n 
1 323 GLU n 
1 324 ASN n 
1 325 ALA n 
1 326 GLN n 
1 327 LYS n 
1 328 GLY n 
1 329 GLU n 
1 330 ILE n 
1 331 MET n 
1 332 PRO n 
1 333 ASN n 
1 334 ILE n 
1 335 PRO n 
1 336 GLN n 
1 337 MET n 
1 338 SER n 
1 339 ALA n 
1 340 PHE n 
1 341 TRP n 
1 342 TYR n 
1 343 ALA n 
1 344 VAL n 
1 345 ARG n 
1 346 THR n 
1 347 ALA n 
1 348 VAL n 
1 349 ILE n 
1 350 ASN n 
1 351 ALA n 
1 352 ALA n 
1 353 SER n 
1 354 GLY n 
1 355 ARG n 
1 356 GLN n 
1 357 THR n 
1 358 VAL n 
1 359 ASP n 
1 360 GLU n 
1 361 ALA n 
1 362 LEU n 
1 363 LYS n 
1 364 ASP n 
1 365 ALA n 
1 366 GLN n 
1 367 THR n 
1 368 GLY n 
1 369 SER n 
1 370 GLU n 
1 371 LEU n 
1 372 TYR n 
1 373 ARG n 
1 374 GLN n 
1 375 SER n 
1 376 LEU n 
1 377 GLU n 
1 378 ILE n 
1 379 ILE n 
1 380 SER n 
1 381 ARG n 
1 382 TYR n 
1 383 LEU n 
1 384 ARG n 
1 385 GLU n 
1 386 GLN n 
1 387 ALA n 
1 388 THR n 
1 389 GLY n 
1 390 ALA n 
1 391 ALA n 
1 392 ASP n 
1 393 THR n 
1 394 ALA n 
1 395 PRO n 
1 396 MET n 
1 397 GLY n 
1 398 ALA n 
1 399 SER n 
1 400 GLY n 
1 401 ALA n 
1 402 THR n 
1 403 SER n 
1 404 ARG n 
1 405 LYS n 
1 406 ALA n 
1 407 LEU n 
1 408 GLU n 
1 409 THR n 
1 410 LEU n 
1 411 ARG n 
1 412 ARG n 
1 413 VAL n 
1 414 GLY n 
1 415 ASP n 
1 416 GLY n 
1 417 VAL n 
1 418 GLN n 
1 419 ARG n 
1 420 ASN n 
1 421 HIS n 
1 422 GLU n 
1 423 THR n 
1 424 ALA n 
1 425 PHE n 
1 426 GLN n 
1 427 GLY n 
1 428 MET n 
1 429 LEU n 
1 430 ARG n 
1 431 LYS n 
1 432 LEU n 
1 433 ASP n 
1 434 ILE n 
1 435 LYS n 
1 436 ASN n 
1 437 GLU n 
1 438 ASP n 
1 439 ASP n 
1 440 VAL n 
1 441 LYS n 
1 442 SER n 
1 443 LEU n 
1 444 SER n 
1 445 ARG n 
1 446 VAL n 
1 447 MET n 
1 448 ILE n 
1 449 HIS n 
1 450 VAL n 
1 451 PHE n 
1 452 SER n 
1 453 ASP n 
1 454 GLY n 
1 455 VAL n 
1 456 THR n 
1 457 ASN n 
1 458 TRP n 
1 459 GLY n 
1 460 ARG n 
1 461 ILE n 
1 462 VAL n 
1 463 THR n 
1 464 LEU n 
1 465 ILE n 
1 466 SER n 
1 467 PHE n 
1 468 GLY n 
1 469 ALA n 
1 470 PHE n 
1 471 VAL n 
1 472 ALA n 
1 473 LYS n 
1 474 HIS n 
1 475 LEU n 
1 476 LYS n 
1 477 THR n 
1 478 ILE n 
1 479 ASN n 
1 480 GLN n 
1 481 GLU n 
1 482 SER n 
1 483 CYS n 
1 484 ILE n 
1 485 GLU n 
1 486 PRO n 
1 487 LEU n 
1 488 ALA n 
1 489 GLU n 
1 490 SER n 
1 491 ILE n 
1 492 THR n 
1 493 ASP n 
1 494 VAL n 
1 495 LEU n 
1 496 VAL n 
1 497 ARG n 
1 498 THR n 
1 499 LYS n 
1 500 ARG n 
1 501 ASP n 
1 502 TRP n 
1 503 LEU n 
1 504 VAL n 
1 505 LYS n 
1 506 GLN n 
1 507 ARG n 
1 508 GLY n 
1 509 TRP n 
1 510 ASP n 
1 511 GLY n 
1 512 PHE n 
1 513 VAL n 
1 514 GLU n 
1 515 PHE n 
1 516 PHE n 
1 517 HIS n 
1 518 VAL 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   367 ?     ? 'malE, Z5632, ECs5017' ? ? ? ? ? ? 'Escherichia coli O157:H7' 83334 ? ? ? ? ? ? ? 
? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 368 518 human ? 'MCL1, BCL2L3'         ? ? ? ? ? ? 'Homo sapiens'             9606  ? ? ? ? ? ? ? 
? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_pdbx_entity_branch.entity_id   2 
_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 2 DGlcpa1-4DGlcpa1-ROH                        'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/1,2,1/[a2122h-1a_1-5]/1-1/a4-b1' WURCS                       PDB2Glycan 1.1.0 
3 2 '[][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}'         LINUCS                      PDB-CARE   ?     
# 
_pdbx_entity_branch_link.link_id                    1 
_pdbx_entity_branch_link.entity_id                  2 
_pdbx_entity_branch_link.entity_branch_list_num_1   2 
_pdbx_entity_branch_link.comp_id_1                  GLC 
_pdbx_entity_branch_link.atom_id_1                  C1 
_pdbx_entity_branch_link.leaving_atom_id_1          O1 
_pdbx_entity_branch_link.entity_branch_list_num_2   1 
_pdbx_entity_branch_link.comp_id_2                  GLC 
_pdbx_entity_branch_link.atom_id_2                  O4 
_pdbx_entity_branch_link.leaving_atom_id_2          HO4 
_pdbx_entity_branch_link.value_order                sing 
_pdbx_entity_branch_link.details                    ? 
# 
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 
A1LXV non-polymer                   . A-1210477             1668553-26-1                          'C46 H55 N7 O7 S' 850.037 
ALA   'L-peptide linking'           y ALANINE               ?                                     'C3 H7 N O2'      89.093  
ARG   'L-peptide linking'           y ARGININE              ?                                     'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking'           y ASPARAGINE            ?                                     'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking'           y 'ASPARTIC ACID'       ?                                     'C4 H7 N O4'      133.103 
CYS   'L-peptide linking'           y CYSTEINE              ?                                     'C3 H7 N O2 S'    121.158 
GLC   'D-saccharide, alpha linking' . alpha-D-glucopyranose 'alpha-D-glucose; D-glucose; glucose' 'C6 H12 O6'       180.156 
GLN   'L-peptide linking'           y GLUTAMINE             ?                                     'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking'           y 'GLUTAMIC ACID'       ?                                     'C5 H9 N O4'      147.129 
GLY   'peptide linking'             y GLYCINE               ?                                     'C2 H5 N O2'      75.067  
HIS   'L-peptide linking'           y HISTIDINE             ?                                     'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer                   . WATER                 ?                                     'H2 O'            18.015  
ILE   'L-peptide linking'           y ISOLEUCINE            ?                                     'C6 H13 N O2'     131.173 
LEU   'L-peptide linking'           y LEUCINE               ?                                     'C6 H13 N O2'     131.173 
LYS   'L-peptide linking'           y LYSINE                ?                                     'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking'           y METHIONINE            ?                                     'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking'           y PHENYLALANINE         ?                                     'C9 H11 N O2'     165.189 
PRO   'L-peptide linking'           y PROLINE               ?                                     'C5 H9 N O2'      115.130 
SER   'L-peptide linking'           y SERINE                ?                                     'C3 H7 N O3'      105.093 
THR   'L-peptide linking'           y THREONINE             ?                                     'C4 H9 N O3'      119.119 
TRP   'L-peptide linking'           y TRYPTOPHAN            ?                                     'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking'           y TYROSINE              ?                                     'C9 H11 N O3'     181.189 
VAL   'L-peptide linking'           y VALINE                ?                                     'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_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 
GLC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpa            
GLC 'COMMON NAME'                         GMML     1.0 a-D-glucopyranose 
GLC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Glcp          
GLC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Glc               
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -196 ?    ?   ?   A . n 
A 1 2   LYS 2   -195 -195 LYS LYS A . n 
A 1 3   ILE 3   -194 -194 ILE ILE A . n 
A 1 4   GLU 4   -193 -193 GLU GLU A . n 
A 1 5   GLU 5   -192 -192 GLU GLU A . n 
A 1 6   GLY 6   -191 -191 GLY GLY A . n 
A 1 7   LYS 7   -190 -190 LYS LYS A . n 
A 1 8   LEU 8   -189 -189 LEU LEU A . n 
A 1 9   VAL 9   -188 -188 VAL VAL A . n 
A 1 10  ILE 10  -187 -187 ILE ILE A . n 
A 1 11  TRP 11  -186 -186 TRP TRP A . n 
A 1 12  ILE 12  -185 -185 ILE ILE A . n 
A 1 13  ASN 13  -184 -184 ASN ASN A . n 
A 1 14  GLY 14  -183 -183 GLY GLY A . n 
A 1 15  ASP 15  -182 -182 ASP ASP A . n 
A 1 16  LYS 16  -181 -181 LYS LYS A . n 
A 1 17  GLY 17  -180 -180 GLY GLY A . n 
A 1 18  TYR 18  -179 -179 TYR TYR A . n 
A 1 19  ASN 19  -178 -178 ASN ASN A . n 
A 1 20  GLY 20  -177 -177 GLY GLY A . n 
A 1 21  LEU 21  -176 -176 LEU LEU A . n 
A 1 22  ALA 22  -175 -175 ALA ALA A . n 
A 1 23  GLU 23  -174 -174 GLU GLU A . n 
A 1 24  VAL 24  -173 -173 VAL VAL A . n 
A 1 25  GLY 25  -172 -172 GLY GLY A . n 
A 1 26  LYS 26  -171 -171 LYS LYS A . n 
A 1 27  LYS 27  -170 -170 LYS LYS A . n 
A 1 28  PHE 28  -169 -169 PHE PHE A . n 
A 1 29  GLU 29  -168 -168 GLU GLU A . n 
A 1 30  LYS 30  -167 -167 LYS LYS A . n 
A 1 31  ASP 31  -166 -166 ASP ASP A . n 
A 1 32  THR 32  -165 -165 THR THR A . n 
A 1 33  GLY 33  -164 -164 GLY GLY A . n 
A 1 34  ILE 34  -163 -163 ILE ILE A . n 
A 1 35  LYS 35  -162 -162 LYS LYS A . n 
A 1 36  VAL 36  -161 -161 VAL VAL A . n 
A 1 37  THR 37  -160 -160 THR THR A . n 
A 1 38  VAL 38  -159 -159 VAL VAL A . n 
A 1 39  GLU 39  -158 -158 GLU GLU A . n 
A 1 40  HIS 40  -157 -157 HIS HIS A . n 
A 1 41  PRO 41  -156 -156 PRO PRO A . n 
A 1 42  ASP 42  -155 -155 ASP ASP A . n 
A 1 43  LYS 43  -154 -154 LYS LYS A . n 
A 1 44  LEU 44  -153 -153 LEU LEU A . n 
A 1 45  GLU 45  -152 -152 GLU GLU A . n 
A 1 46  GLU 46  -151 -151 GLU GLU A . n 
A 1 47  LYS 47  -150 -150 LYS LYS A . n 
A 1 48  PHE 48  -149 -149 PHE PHE A . n 
A 1 49  PRO 49  -148 -148 PRO PRO A . n 
A 1 50  GLN 50  -147 -147 GLN GLN A . n 
A 1 51  VAL 51  -146 -146 VAL VAL A . n 
A 1 52  ALA 52  -145 -145 ALA ALA A . n 
A 1 53  ALA 53  -144 -144 ALA ALA A . n 
A 1 54  THR 54  -143 -143 THR THR A . n 
A 1 55  GLY 55  -142 -142 GLY GLY A . n 
A 1 56  ASP 56  -141 -141 ASP ASP A . n 
A 1 57  GLY 57  -140 -140 GLY GLY A . n 
A 1 58  PRO 58  -139 -139 PRO PRO A . n 
A 1 59  ASP 59  -138 -138 ASP ASP A . n 
A 1 60  ILE 60  -137 -137 ILE ILE A . n 
A 1 61  ILE 61  -136 -136 ILE ILE A . n 
A 1 62  PHE 62  -135 -135 PHE PHE A . n 
A 1 63  TRP 63  -134 -134 TRP TRP A . n 
A 1 64  ALA 64  -133 -133 ALA ALA A . n 
A 1 65  HIS 65  -132 -132 HIS HIS A . n 
A 1 66  ASP 66  -131 -131 ASP ASP A . n 
A 1 67  ARG 67  -130 -130 ARG ARG A . n 
A 1 68  PHE 68  -129 -129 PHE PHE A . n 
A 1 69  GLY 69  -128 -128 GLY GLY A . n 
A 1 70  GLY 70  -127 -127 GLY GLY A . n 
A 1 71  TYR 71  -126 -126 TYR TYR A . n 
A 1 72  ALA 72  -125 -125 ALA ALA A . n 
A 1 73  GLN 73  -124 -124 GLN GLN A . n 
A 1 74  SER 74  -123 -123 SER SER A . n 
A 1 75  GLY 75  -122 -122 GLY GLY A . n 
A 1 76  LEU 76  -121 -121 LEU LEU A . n 
A 1 77  LEU 77  -120 -120 LEU LEU A . n 
A 1 78  ALA 78  -119 -119 ALA ALA A . n 
A 1 79  GLU 79  -118 -118 GLU GLU A . n 
A 1 80  ILE 80  -117 -117 ILE ILE A . n 
A 1 81  THR 81  -116 -116 THR THR A . n 
A 1 82  PRO 82  -115 -115 PRO PRO A . n 
A 1 83  ASP 83  -114 -114 ASP ASP A . n 
A 1 84  LYS 84  -113 -113 LYS LYS A . n 
A 1 85  ALA 85  -112 -112 ALA ALA A . n 
A 1 86  PHE 86  -111 -111 PHE PHE A . n 
A 1 87  GLN 87  -110 -110 GLN GLN A . n 
A 1 88  ASP 88  -109 -109 ASP ASP A . n 
A 1 89  LYS 89  -108 -108 LYS LYS A . n 
A 1 90  LEU 90  -107 -107 LEU LEU A . n 
A 1 91  TYR 91  -106 -106 TYR TYR A . n 
A 1 92  PRO 92  -105 -105 PRO PRO A . n 
A 1 93  PHE 93  -104 -104 PHE PHE A . n 
A 1 94  THR 94  -103 -103 THR THR A . n 
A 1 95  TRP 95  -102 -102 TRP TRP A . n 
A 1 96  ASP 96  -101 -101 ASP ASP A . n 
A 1 97  ALA 97  -100 -100 ALA ALA A . n 
A 1 98  VAL 98  -99  -99  VAL VAL A . n 
A 1 99  ARG 99  -98  -98  ARG ARG A . n 
A 1 100 TYR 100 -97  -97  TYR TYR A . n 
A 1 101 ASN 101 -96  -96  ASN ASN A . n 
A 1 102 GLY 102 -95  -95  GLY GLY A . n 
A 1 103 LYS 103 -94  -94  LYS LYS A . n 
A 1 104 LEU 104 -93  -93  LEU LEU A . n 
A 1 105 ILE 105 -92  -92  ILE ILE A . n 
A 1 106 ALA 106 -91  -91  ALA ALA A . n 
A 1 107 TYR 107 -90  -90  TYR TYR A . n 
A 1 108 PRO 108 -89  -89  PRO PRO A . n 
A 1 109 ILE 109 -88  -88  ILE ILE A . n 
A 1 110 ALA 110 -87  -87  ALA ALA A . n 
A 1 111 VAL 111 -86  -86  VAL VAL A . n 
A 1 112 GLU 112 -85  -85  GLU GLU A . n 
A 1 113 ALA 113 -84  -84  ALA ALA A . n 
A 1 114 LEU 114 -83  -83  LEU LEU A . n 
A 1 115 SER 115 -82  -82  SER SER A . n 
A 1 116 LEU 116 -81  -81  LEU LEU A . n 
A 1 117 ILE 117 -80  -80  ILE ILE A . n 
A 1 118 TYR 118 -79  -79  TYR TYR A . n 
A 1 119 ASN 119 -78  -78  ASN ASN A . n 
A 1 120 LYS 120 -77  -77  LYS LYS A . n 
A 1 121 ASP 121 -76  -76  ASP ASP A . n 
A 1 122 LEU 122 -75  -75  LEU LEU A . n 
A 1 123 LEU 123 -74  -74  LEU LEU A . n 
A 1 124 PRO 124 -73  -73  PRO PRO A . n 
A 1 125 ASN 125 -72  -72  ASN ASN A . n 
A 1 126 PRO 126 -71  -71  PRO PRO A . n 
A 1 127 PRO 127 -70  -70  PRO PRO A . n 
A 1 128 LYS 128 -69  -69  LYS LYS A . n 
A 1 129 THR 129 -68  -68  THR THR A . n 
A 1 130 TRP 130 -67  -67  TRP TRP A . n 
A 1 131 GLU 131 -66  -66  GLU GLU A . n 
A 1 132 GLU 132 -65  -65  GLU GLU A . n 
A 1 133 ILE 133 -64  -64  ILE ILE A . n 
A 1 134 PRO 134 -63  -63  PRO PRO A . n 
A 1 135 ALA 135 -62  -62  ALA ALA A . n 
A 1 136 LEU 136 -61  -61  LEU LEU A . n 
A 1 137 ASP 137 -60  -60  ASP ASP A . n 
A 1 138 LYS 138 -59  -59  LYS LYS A . n 
A 1 139 GLU 139 -58  -58  GLU GLU A . n 
A 1 140 LEU 140 -57  -57  LEU LEU A . n 
A 1 141 LYS 141 -56  -56  LYS LYS A . n 
A 1 142 ALA 142 -55  -55  ALA ALA A . n 
A 1 143 LYS 143 -54  -54  LYS LYS A . n 
A 1 144 GLY 144 -53  -53  GLY GLY A . n 
A 1 145 LYS 145 -52  -52  LYS LYS A . n 
A 1 146 SER 146 -51  -51  SER SER A . n 
A 1 147 ALA 147 -50  -50  ALA ALA A . n 
A 1 148 LEU 148 -49  -49  LEU LEU A . n 
A 1 149 MET 149 -48  -48  MET MET A . n 
A 1 150 PHE 150 -47  -47  PHE PHE A . n 
A 1 151 ASN 151 -46  -46  ASN ASN A . n 
A 1 152 LEU 152 -45  -45  LEU LEU A . n 
A 1 153 GLN 153 -44  -44  GLN GLN A . n 
A 1 154 GLU 154 -43  -43  GLU GLU A . n 
A 1 155 PRO 155 -42  -42  PRO PRO A . n 
A 1 156 TYR 156 -41  -41  TYR TYR A . n 
A 1 157 PHE 157 -40  -40  PHE PHE A . n 
A 1 158 THR 158 -39  -39  THR THR A . n 
A 1 159 TRP 159 -38  -38  TRP TRP A . n 
A 1 160 PRO 160 -37  -37  PRO PRO A . n 
A 1 161 LEU 161 -36  -36  LEU LEU A . n 
A 1 162 ILE 162 -35  -35  ILE ILE A . n 
A 1 163 ALA 163 -34  -34  ALA ALA A . n 
A 1 164 ALA 164 -33  -33  ALA ALA A . n 
A 1 165 ASP 165 -32  -32  ASP ASP A . n 
A 1 166 GLY 166 -31  -31  GLY GLY A . n 
A 1 167 GLY 167 -30  -30  GLY GLY A . n 
A 1 168 TYR 168 -29  -29  TYR TYR A . n 
A 1 169 ALA 169 -28  -28  ALA ALA A . n 
A 1 170 PHE 170 -27  -27  PHE PHE A . n 
A 1 171 LYS 171 -26  -26  LYS LYS A . n 
A 1 172 TYR 172 -25  -25  TYR TYR A . n 
A 1 173 ALA 173 -24  ?    ?   ?   A . n 
A 1 174 ALA 174 -23  ?    ?   ?   A . n 
A 1 175 GLY 175 -22  ?    ?   ?   A . n 
A 1 176 LYS 176 -21  -21  LYS LYS A . n 
A 1 177 TYR 177 -20  -20  TYR TYR A . n 
A 1 178 ASP 178 -19  -19  ASP ASP A . n 
A 1 179 ILE 179 -18  -18  ILE ILE A . n 
A 1 180 LYS 180 -17  -17  LYS LYS A . n 
A 1 181 ASP 181 -16  -16  ASP ASP A . n 
A 1 182 VAL 182 -15  -15  VAL VAL A . n 
A 1 183 GLY 183 -14  -14  GLY GLY A . n 
A 1 184 VAL 184 -13  -13  VAL VAL A . n 
A 1 185 ASP 185 -12  -12  ASP ASP A . n 
A 1 186 ASN 186 -11  -11  ASN ASN A . n 
A 1 187 ALA 187 -10  -10  ALA ALA A . n 
A 1 188 GLY 188 -9   -9   GLY GLY A . n 
A 1 189 ALA 189 -8   -8   ALA ALA A . n 
A 1 190 LYS 190 -7   -7   LYS LYS A . n 
A 1 191 ALA 191 -6   -6   ALA ALA A . n 
A 1 192 GLY 192 -5   -5   GLY GLY A . n 
A 1 193 LEU 193 -4   -4   LEU LEU A . n 
A 1 194 THR 194 -3   -3   THR THR A . n 
A 1 195 PHE 195 -2   -2   PHE PHE A . n 
A 1 196 LEU 196 -1   -1   LEU LEU A . n 
A 1 197 VAL 197 0    0    VAL VAL A . n 
A 1 198 ASP 198 1    1    ASP ASP A . n 
A 1 199 LEU 199 2    2    LEU LEU A . n 
A 1 200 ILE 200 3    3    ILE ILE A . n 
A 1 201 LYS 201 4    4    LYS LYS A . n 
A 1 202 ASN 202 5    5    ASN ASN A . n 
A 1 203 LYS 203 6    6    LYS LYS A . n 
A 1 204 HIS 204 7    7    HIS HIS A . n 
A 1 205 MET 205 8    8    MET MET A . n 
A 1 206 ASN 206 9    9    ASN ASN A . n 
A 1 207 ALA 207 10   10   ALA ALA A . n 
A 1 208 ASP 208 11   11   ASP ASP A . n 
A 1 209 THR 209 12   12   THR THR A . n 
A 1 210 ASP 210 13   13   ASP ASP A . n 
A 1 211 TYR 211 14   14   TYR TYR A . n 
A 1 212 SER 212 15   15   SER SER A . n 
A 1 213 ILE 213 16   16   ILE ILE A . n 
A 1 214 ALA 214 17   17   ALA ALA A . n 
A 1 215 GLU 215 18   18   GLU GLU A . n 
A 1 216 ALA 216 19   19   ALA ALA A . n 
A 1 217 ALA 217 20   20   ALA ALA A . n 
A 1 218 PHE 218 21   21   PHE PHE A . n 
A 1 219 ASN 219 22   22   ASN ASN A . n 
A 1 220 LYS 220 23   23   LYS LYS A . n 
A 1 221 GLY 221 24   24   GLY GLY A . n 
A 1 222 GLU 222 25   25   GLU GLU A . n 
A 1 223 THR 223 26   26   THR THR A . n 
A 1 224 ALA 224 27   27   ALA ALA A . n 
A 1 225 MET 225 28   28   MET MET A . n 
A 1 226 THR 226 29   29   THR THR A . n 
A 1 227 ILE 227 30   30   ILE ILE A . n 
A 1 228 ASN 228 31   31   ASN ASN A . n 
A 1 229 GLY 229 32   32   GLY GLY A . n 
A 1 230 PRO 230 33   33   PRO PRO A . n 
A 1 231 TRP 231 34   34   TRP TRP A . n 
A 1 232 ALA 232 35   35   ALA ALA A . n 
A 1 233 TRP 233 36   36   TRP TRP A . n 
A 1 234 SER 234 37   37   SER SER A . n 
A 1 235 ASN 235 38   38   ASN ASN A . n 
A 1 236 ILE 236 39   39   ILE ILE A . n 
A 1 237 ASP 237 40   40   ASP ASP A . n 
A 1 238 THR 238 41   41   THR THR A . n 
A 1 239 SER 239 42   42   SER SER A . n 
A 1 240 ALA 240 43   43   ALA ALA A . n 
A 1 241 VAL 241 44   44   VAL VAL A . n 
A 1 242 ASN 242 45   45   ASN ASN A . n 
A 1 243 TYR 243 46   46   TYR TYR A . n 
A 1 244 GLY 244 47   47   GLY GLY A . n 
A 1 245 VAL 245 48   48   VAL VAL A . n 
A 1 246 THR 246 49   49   THR THR A . n 
A 1 247 VAL 247 50   50   VAL VAL A . n 
A 1 248 LEU 248 51   51   LEU LEU A . n 
A 1 249 PRO 249 52   52   PRO PRO A . n 
A 1 250 THR 250 53   53   THR THR A . n 
A 1 251 PHE 251 54   54   PHE PHE A . n 
A 1 252 LYS 252 55   55   LYS LYS A . n 
A 1 253 GLY 253 56   56   GLY GLY A . n 
A 1 254 GLN 254 57   57   GLN GLN A . n 
A 1 255 PRO 255 58   58   PRO PRO A . n 
A 1 256 SER 256 59   59   SER SER A . n 
A 1 257 LYS 257 60   60   LYS LYS A . n 
A 1 258 PRO 258 61   61   PRO PRO A . n 
A 1 259 PHE 259 62   62   PHE PHE A . n 
A 1 260 VAL 260 63   63   VAL VAL A . n 
A 1 261 GLY 261 64   64   GLY GLY A . n 
A 1 262 VAL 262 65   65   VAL VAL A . n 
A 1 263 LEU 263 66   66   LEU LEU A . n 
A 1 264 SER 264 67   67   SER SER A . n 
A 1 265 ALA 265 68   68   ALA ALA A . n 
A 1 266 GLY 266 69   69   GLY GLY A . n 
A 1 267 ILE 267 70   70   ILE ILE A . n 
A 1 268 ASN 268 71   71   ASN ASN A . n 
A 1 269 ALA 269 72   72   ALA ALA A . n 
A 1 270 ALA 270 73   73   ALA ALA A . n 
A 1 271 SER 271 74   74   SER SER A . n 
A 1 272 PRO 272 75   75   PRO PRO A . n 
A 1 273 ASN 273 76   76   ASN ASN A . n 
A 1 274 LYS 274 77   77   LYS LYS A . n 
A 1 275 GLU 275 78   78   GLU GLU A . n 
A 1 276 LEU 276 79   79   LEU LEU A . n 
A 1 277 ALA 277 80   80   ALA ALA A . n 
A 1 278 LYS 278 81   81   LYS LYS A . n 
A 1 279 GLU 279 82   82   GLU GLU A . n 
A 1 280 PHE 280 83   83   PHE PHE A . n 
A 1 281 LEU 281 84   84   LEU LEU A . n 
A 1 282 GLU 282 85   85   GLU GLU A . n 
A 1 283 ASN 283 86   86   ASN ASN A . n 
A 1 284 TYR 284 87   87   TYR TYR A . n 
A 1 285 LEU 285 88   88   LEU LEU A . n 
A 1 286 LEU 286 89   89   LEU LEU A . n 
A 1 287 THR 287 90   90   THR THR A . n 
A 1 288 ASP 288 91   91   ASP ASP A . n 
A 1 289 GLU 289 92   92   GLU GLU A . n 
A 1 290 GLY 290 93   93   GLY GLY A . n 
A 1 291 LEU 291 94   94   LEU LEU A . n 
A 1 292 GLU 292 95   95   GLU GLU A . n 
A 1 293 ALA 293 96   96   ALA ALA A . n 
A 1 294 VAL 294 97   97   VAL VAL A . n 
A 1 295 ASN 295 98   98   ASN ASN A . n 
A 1 296 LYS 296 99   99   LYS LYS A . n 
A 1 297 ASP 297 100  100  ASP ASP A . n 
A 1 298 LYS 298 101  101  LYS LYS A . n 
A 1 299 PRO 299 102  102  PRO PRO A . n 
A 1 300 LEU 300 103  103  LEU LEU A . n 
A 1 301 GLY 301 104  104  GLY GLY A . n 
A 1 302 ALA 302 105  105  ALA ALA A . n 
A 1 303 VAL 303 106  106  VAL VAL A . n 
A 1 304 ALA 304 107  107  ALA ALA A . n 
A 1 305 LEU 305 108  108  LEU LEU A . n 
A 1 306 LYS 306 109  109  LYS LYS A . n 
A 1 307 SER 307 110  110  SER SER A . n 
A 1 308 TYR 308 111  111  TYR TYR A . n 
A 1 309 GLU 309 112  112  GLU GLU A . n 
A 1 310 GLU 310 113  113  GLU GLU A . n 
A 1 311 GLU 311 114  114  GLU GLU A . n 
A 1 312 LEU 312 115  115  LEU LEU A . n 
A 1 313 ALA 313 116  116  ALA ALA A . n 
A 1 314 LYS 314 117  117  LYS LYS A . n 
A 1 315 ASP 315 118  118  ASP ASP A . n 
A 1 316 PRO 316 119  119  PRO PRO A . n 
A 1 317 ARG 317 120  120  ARG ARG A . n 
A 1 318 ILE 318 121  121  ILE ILE A . n 
A 1 319 ALA 319 122  122  ALA ALA A . n 
A 1 320 ALA 320 123  123  ALA ALA A . n 
A 1 321 THR 321 124  124  THR THR A . n 
A 1 322 MET 322 125  125  MET MET A . n 
A 1 323 GLU 323 126  126  GLU GLU A . n 
A 1 324 ASN 324 127  127  ASN ASN A . n 
A 1 325 ALA 325 128  128  ALA ALA A . n 
A 1 326 GLN 326 129  129  GLN GLN A . n 
A 1 327 LYS 327 130  130  LYS LYS A . n 
A 1 328 GLY 328 131  131  GLY GLY A . n 
A 1 329 GLU 329 132  132  GLU GLU A . n 
A 1 330 ILE 330 133  133  ILE ILE A . n 
A 1 331 MET 331 134  134  MET MET A . n 
A 1 332 PRO 332 135  135  PRO PRO A . n 
A 1 333 ASN 333 136  136  ASN ASN A . n 
A 1 334 ILE 334 137  137  ILE ILE A . n 
A 1 335 PRO 335 138  138  PRO PRO A . n 
A 1 336 GLN 336 139  139  GLN GLN A . n 
A 1 337 MET 337 140  140  MET MET A . n 
A 1 338 SER 338 141  141  SER SER A . n 
A 1 339 ALA 339 142  142  ALA ALA A . n 
A 1 340 PHE 340 143  143  PHE PHE A . n 
A 1 341 TRP 341 144  144  TRP TRP A . n 
A 1 342 TYR 342 145  145  TYR TYR A . n 
A 1 343 ALA 343 146  146  ALA ALA A . n 
A 1 344 VAL 344 147  147  VAL VAL A . n 
A 1 345 ARG 345 148  148  ARG ARG A . n 
A 1 346 THR 346 149  149  THR THR A . n 
A 1 347 ALA 347 150  150  ALA ALA A . n 
A 1 348 VAL 348 151  151  VAL VAL A . n 
A 1 349 ILE 349 152  152  ILE ILE A . n 
A 1 350 ASN 350 153  153  ASN ASN A . n 
A 1 351 ALA 351 154  154  ALA ALA A . n 
A 1 352 ALA 352 155  155  ALA ALA A . n 
A 1 353 SER 353 156  156  SER SER A . n 
A 1 354 GLY 354 157  157  GLY GLY A . n 
A 1 355 ARG 355 158  158  ARG ARG A . n 
A 1 356 GLN 356 159  159  GLN GLN A . n 
A 1 357 THR 357 160  160  THR THR A . n 
A 1 358 VAL 358 161  161  VAL VAL A . n 
A 1 359 ASP 359 162  162  ASP ASP A . n 
A 1 360 GLU 360 163  163  GLU GLU A . n 
A 1 361 ALA 361 164  164  ALA ALA A . n 
A 1 362 LEU 362 165  165  LEU LEU A . n 
A 1 363 LYS 363 166  166  LYS LYS A . n 
A 1 364 ASP 364 167  167  ASP ASP A . n 
A 1 365 ALA 365 168  168  ALA ALA A . n 
A 1 366 GLN 366 169  169  GLN GLN A . n 
A 1 367 THR 367 170  170  THR THR A . n 
A 1 368 GLY 368 171  171  GLY GLY A . n 
A 1 369 SER 369 172  172  SER SER A . n 
A 1 370 GLU 370 173  173  GLU GLU A . n 
A 1 371 LEU 371 174  174  LEU LEU A . n 
A 1 372 TYR 372 175  175  TYR TYR A . n 
A 1 373 ARG 373 176  176  ARG ARG A . n 
A 1 374 GLN 374 177  177  GLN GLN A . n 
A 1 375 SER 375 178  178  SER SER A . n 
A 1 376 LEU 376 179  179  LEU LEU A . n 
A 1 377 GLU 377 180  180  GLU GLU A . n 
A 1 378 ILE 378 181  181  ILE ILE A . n 
A 1 379 ILE 379 182  182  ILE ILE A . n 
A 1 380 SER 380 183  183  SER SER A . n 
A 1 381 ARG 381 184  184  ARG ARG A . n 
A 1 382 TYR 382 185  185  TYR TYR A . n 
A 1 383 LEU 383 186  186  LEU LEU A . n 
A 1 384 ARG 384 187  187  ARG ARG A . n 
A 1 385 GLU 385 188  188  GLU GLU A . n 
A 1 386 GLN 386 189  189  GLN GLN A . n 
A 1 387 ALA 387 190  190  ALA ALA A . n 
A 1 388 THR 388 191  191  THR THR A . n 
A 1 389 GLY 389 192  192  GLY GLY A . n 
A 1 390 ALA 390 193  193  ALA ALA A . n 
A 1 391 ALA 391 194  194  ALA ALA A . n 
A 1 392 ASP 392 195  195  ASP ASP A . n 
A 1 393 THR 393 196  196  THR THR A . n 
A 1 394 ALA 394 197  197  ALA ALA A . n 
A 1 395 PRO 395 198  198  PRO PRO A . n 
A 1 396 MET 396 199  199  MET MET A . n 
A 1 397 GLY 397 200  200  GLY GLY A . n 
A 1 398 ALA 398 201  201  ALA ALA A . n 
A 1 399 SER 399 202  202  SER SER A . n 
A 1 400 GLY 400 203  203  GLY GLY A . n 
A 1 401 ALA 401 204  204  ALA ALA A . n 
A 1 402 THR 402 205  205  THR THR A . n 
A 1 403 SER 403 206  206  SER SER A . n 
A 1 404 ARG 404 207  207  ARG ARG A . n 
A 1 405 LYS 405 208  208  LYS LYS A . n 
A 1 406 ALA 406 209  209  ALA ALA A . n 
A 1 407 LEU 407 210  210  LEU LEU A . n 
A 1 408 GLU 408 211  211  GLU GLU A . n 
A 1 409 THR 409 212  212  THR THR A . n 
A 1 410 LEU 410 213  213  LEU LEU A . n 
A 1 411 ARG 411 214  214  ARG ARG A . n 
A 1 412 ARG 412 215  215  ARG ARG A . n 
A 1 413 VAL 413 216  216  VAL VAL A . n 
A 1 414 GLY 414 217  217  GLY GLY A . n 
A 1 415 ASP 415 218  218  ASP ASP A . n 
A 1 416 GLY 416 219  219  GLY GLY A . n 
A 1 417 VAL 417 220  220  VAL VAL A . n 
A 1 418 GLN 418 221  221  GLN GLN A . n 
A 1 419 ARG 419 222  222  ARG ARG A . n 
A 1 420 ASN 420 223  223  ASN ASN A . n 
A 1 421 HIS 421 224  224  HIS HIS A . n 
A 1 422 GLU 422 225  225  GLU GLU A . n 
A 1 423 THR 423 226  226  THR THR A . n 
A 1 424 ALA 424 227  227  ALA ALA A . n 
A 1 425 PHE 425 228  228  PHE PHE A . n 
A 1 426 GLN 426 229  229  GLN GLN A . n 
A 1 427 GLY 427 230  230  GLY GLY A . n 
A 1 428 MET 428 231  231  MET MET A . n 
A 1 429 LEU 429 232  232  LEU LEU A . n 
A 1 430 ARG 430 233  233  ARG ARG A . n 
A 1 431 LYS 431 234  234  LYS LYS A . n 
A 1 432 LEU 432 235  235  LEU LEU A . n 
A 1 433 ASP 433 236  236  ASP ASP A . n 
A 1 434 ILE 434 237  237  ILE ILE A . n 
A 1 435 LYS 435 238  238  LYS LYS A . n 
A 1 436 ASN 436 239  239  ASN ASN A . n 
A 1 437 GLU 437 240  240  GLU GLU A . n 
A 1 438 ASP 438 241  241  ASP ASP A . n 
A 1 439 ASP 439 242  242  ASP ASP A . n 
A 1 440 VAL 440 243  243  VAL VAL A . n 
A 1 441 LYS 441 244  244  LYS LYS A . n 
A 1 442 SER 442 245  245  SER SER A . n 
A 1 443 LEU 443 246  246  LEU LEU A . n 
A 1 444 SER 444 247  247  SER SER A . n 
A 1 445 ARG 445 248  248  ARG ARG A . n 
A 1 446 VAL 446 249  249  VAL VAL A . n 
A 1 447 MET 447 250  250  MET MET A . n 
A 1 448 ILE 448 251  251  ILE ILE A . n 
A 1 449 HIS 449 252  252  HIS HIS A . n 
A 1 450 VAL 450 253  253  VAL VAL A . n 
A 1 451 PHE 451 254  254  PHE PHE A . n 
A 1 452 SER 452 255  255  SER SER A . n 
A 1 453 ASP 453 256  256  ASP ASP A . n 
A 1 454 GLY 454 257  257  GLY GLY A . n 
A 1 455 VAL 455 258  258  VAL VAL A . n 
A 1 456 THR 456 259  259  THR THR A . n 
A 1 457 ASN 457 260  260  ASN ASN A . n 
A 1 458 TRP 458 261  261  TRP TRP A . n 
A 1 459 GLY 459 262  262  GLY GLY A . n 
A 1 460 ARG 460 263  263  ARG ARG A . n 
A 1 461 ILE 461 264  264  ILE ILE A . n 
A 1 462 VAL 462 265  265  VAL VAL A . n 
A 1 463 THR 463 266  266  THR THR A . n 
A 1 464 LEU 464 267  267  LEU LEU A . n 
A 1 465 ILE 465 268  268  ILE ILE A . n 
A 1 466 SER 466 269  269  SER SER A . n 
A 1 467 PHE 467 270  270  PHE PHE A . n 
A 1 468 GLY 468 271  271  GLY GLY A . n 
A 1 469 ALA 469 272  272  ALA ALA A . n 
A 1 470 PHE 470 273  273  PHE PHE A . n 
A 1 471 VAL 471 274  274  VAL VAL A . n 
A 1 472 ALA 472 275  275  ALA ALA A . n 
A 1 473 LYS 473 276  276  LYS LYS A . n 
A 1 474 HIS 474 277  277  HIS HIS A . n 
A 1 475 LEU 475 278  278  LEU LEU A . n 
A 1 476 LYS 476 279  279  LYS LYS A . n 
A 1 477 THR 477 280  280  THR THR A . n 
A 1 478 ILE 478 281  281  ILE ILE A . n 
A 1 479 ASN 479 282  282  ASN ASN A . n 
A 1 480 GLN 480 283  283  GLN GLN A . n 
A 1 481 GLU 481 284  284  GLU GLU A . n 
A 1 482 SER 482 285  285  SER SER A . n 
A 1 483 CYS 483 286  286  CYS CYS A . n 
A 1 484 ILE 484 287  287  ILE ILE A . n 
A 1 485 GLU 485 288  288  GLU GLU A . n 
A 1 486 PRO 486 289  289  PRO PRO A . n 
A 1 487 LEU 487 290  290  LEU LEU A . n 
A 1 488 ALA 488 291  291  ALA ALA A . n 
A 1 489 GLU 489 292  292  GLU GLU A . n 
A 1 490 SER 490 293  293  SER SER A . n 
A 1 491 ILE 491 294  294  ILE ILE A . n 
A 1 492 THR 492 295  295  THR THR A . n 
A 1 493 ASP 493 296  296  ASP ASP A . n 
A 1 494 VAL 494 297  297  VAL VAL A . n 
A 1 495 LEU 495 298  298  LEU LEU A . n 
A 1 496 VAL 496 299  299  VAL VAL A . n 
A 1 497 ARG 497 300  300  ARG ARG A . n 
A 1 498 THR 498 301  301  THR THR A . n 
A 1 499 LYS 499 302  302  LYS LYS A . n 
A 1 500 ARG 500 303  303  ARG ARG A . n 
A 1 501 ASP 501 304  304  ASP ASP A . n 
A 1 502 TRP 502 305  305  TRP TRP A . n 
A 1 503 LEU 503 306  306  LEU LEU A . n 
A 1 504 VAL 504 307  307  VAL VAL A . n 
A 1 505 LYS 505 308  308  LYS LYS A . n 
A 1 506 GLN 506 309  309  GLN GLN A . n 
A 1 507 ARG 507 310  310  ARG ARG A . n 
A 1 508 GLY 508 311  311  GLY GLY A . n 
A 1 509 TRP 509 312  312  TRP TRP A . n 
A 1 510 ASP 510 313  313  ASP ASP A . n 
A 1 511 GLY 511 314  314  GLY GLY A . n 
A 1 512 PHE 512 315  315  PHE PHE A . n 
A 1 513 VAL 513 316  316  VAL VAL A . n 
A 1 514 GLU 514 317  317  GLU GLU A . n 
A 1 515 PHE 515 318  318  PHE PHE A . n 
A 1 516 PHE 516 319  319  PHE PHE A . n 
A 1 517 HIS 517 320  320  HIS HIS A . n 
A 1 518 VAL 518 321  321  VAL VAL A . 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 
B 2 GLC 1 B GLC 1 B MAL 1 n 
B 2 GLC 2 B GLC 2 B MAL 1 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 GLC   ? ? GLC   ? ? 'SUBJECT OF INVESTIGATION' ? 
2 A1LXV ? ? A1LXV ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 A1LXV 1   401 401 A1LXV UNL A . 
D 4 HOH   1   501 103 HOH   HOH A . 
D 4 HOH   2   502 142 HOH   HOH A . 
D 4 HOH   3   503 107 HOH   HOH A . 
D 4 HOH   4   504 44  HOH   HOH A . 
D 4 HOH   5   505 6   HOH   HOH A . 
D 4 HOH   6   506 110 HOH   HOH A . 
D 4 HOH   7   507 57  HOH   HOH A . 
D 4 HOH   8   508 78  HOH   HOH A . 
D 4 HOH   9   509 16  HOH   HOH A . 
D 4 HOH   10  510 95  HOH   HOH A . 
D 4 HOH   11  511 3   HOH   HOH A . 
D 4 HOH   12  512 37  HOH   HOH A . 
D 4 HOH   13  513 39  HOH   HOH A . 
D 4 HOH   14  514 98  HOH   HOH A . 
D 4 HOH   15  515 125 HOH   HOH A . 
D 4 HOH   16  516 108 HOH   HOH A . 
D 4 HOH   17  517 19  HOH   HOH A . 
D 4 HOH   18  518 66  HOH   HOH A . 
D 4 HOH   19  519 41  HOH   HOH A . 
D 4 HOH   20  520 9   HOH   HOH A . 
D 4 HOH   21  521 87  HOH   HOH A . 
D 4 HOH   22  522 8   HOH   HOH A . 
D 4 HOH   23  523 89  HOH   HOH A . 
D 4 HOH   24  524 65  HOH   HOH A . 
D 4 HOH   25  525 77  HOH   HOH A . 
D 4 HOH   26  526 12  HOH   HOH A . 
D 4 HOH   27  527 38  HOH   HOH A . 
D 4 HOH   28  528 60  HOH   HOH A . 
D 4 HOH   29  529 2   HOH   HOH A . 
D 4 HOH   30  530 11  HOH   HOH A . 
D 4 HOH   31  531 101 HOH   HOH A . 
D 4 HOH   32  532 67  HOH   HOH A . 
D 4 HOH   33  533 150 HOH   HOH A . 
D 4 HOH   34  534 129 HOH   HOH A . 
D 4 HOH   35  535 130 HOH   HOH A . 
D 4 HOH   36  536 45  HOH   HOH A . 
D 4 HOH   37  537 76  HOH   HOH A . 
D 4 HOH   38  538 138 HOH   HOH A . 
D 4 HOH   39  539 100 HOH   HOH A . 
D 4 HOH   40  540 29  HOH   HOH A . 
D 4 HOH   41  541 68  HOH   HOH A . 
D 4 HOH   42  542 32  HOH   HOH A . 
D 4 HOH   43  543 25  HOH   HOH A . 
D 4 HOH   44  544 106 HOH   HOH A . 
D 4 HOH   45  545 28  HOH   HOH A . 
D 4 HOH   46  546 26  HOH   HOH A . 
D 4 HOH   47  547 79  HOH   HOH A . 
D 4 HOH   48  548 55  HOH   HOH A . 
D 4 HOH   49  549 33  HOH   HOH A . 
D 4 HOH   50  550 62  HOH   HOH A . 
D 4 HOH   51  551 90  HOH   HOH A . 
D 4 HOH   52  552 140 HOH   HOH A . 
D 4 HOH   53  553 31  HOH   HOH A . 
D 4 HOH   54  554 73  HOH   HOH A . 
D 4 HOH   55  555 86  HOH   HOH A . 
D 4 HOH   56  556 40  HOH   HOH A . 
D 4 HOH   57  557 113 HOH   HOH A . 
D 4 HOH   58  558 53  HOH   HOH A . 
D 4 HOH   59  559 114 HOH   HOH A . 
D 4 HOH   60  560 58  HOH   HOH A . 
D 4 HOH   61  561 134 HOH   HOH A . 
D 4 HOH   62  562 21  HOH   HOH A . 
D 4 HOH   63  563 52  HOH   HOH A . 
D 4 HOH   64  564 49  HOH   HOH A . 
D 4 HOH   65  565 83  HOH   HOH A . 
D 4 HOH   66  566 97  HOH   HOH A . 
D 4 HOH   67  567 15  HOH   HOH A . 
D 4 HOH   68  568 69  HOH   HOH A . 
D 4 HOH   69  569 5   HOH   HOH A . 
D 4 HOH   70  570 146 HOH   HOH A . 
D 4 HOH   71  571 46  HOH   HOH A . 
D 4 HOH   72  572 153 HOH   HOH A . 
D 4 HOH   73  573 59  HOH   HOH A . 
D 4 HOH   74  574 18  HOH   HOH A . 
D 4 HOH   75  575 72  HOH   HOH A . 
D 4 HOH   76  576 1   HOH   HOH A . 
D 4 HOH   77  577 70  HOH   HOH A . 
D 4 HOH   78  578 82  HOH   HOH A . 
D 4 HOH   79  579 137 HOH   HOH A . 
D 4 HOH   80  580 81  HOH   HOH A . 
D 4 HOH   81  581 121 HOH   HOH A . 
D 4 HOH   82  582 7   HOH   HOH A . 
D 4 HOH   83  583 22  HOH   HOH A . 
D 4 HOH   84  584 35  HOH   HOH A . 
D 4 HOH   85  585 71  HOH   HOH A . 
D 4 HOH   86  586 34  HOH   HOH A . 
D 4 HOH   87  587 51  HOH   HOH A . 
D 4 HOH   88  588 13  HOH   HOH A . 
D 4 HOH   89  589 99  HOH   HOH A . 
D 4 HOH   90  590 64  HOH   HOH A . 
D 4 HOH   91  591 80  HOH   HOH A . 
D 4 HOH   92  592 50  HOH   HOH A . 
D 4 HOH   93  593 96  HOH   HOH A . 
D 4 HOH   94  594 74  HOH   HOH A . 
D 4 HOH   95  595 144 HOH   HOH A . 
D 4 HOH   96  596 94  HOH   HOH A . 
D 4 HOH   97  597 119 HOH   HOH A . 
D 4 HOH   98  598 117 HOH   HOH A . 
D 4 HOH   99  599 23  HOH   HOH A . 
D 4 HOH   100 600 30  HOH   HOH A . 
D 4 HOH   101 601 54  HOH   HOH A . 
D 4 HOH   102 602 127 HOH   HOH A . 
D 4 HOH   103 603 36  HOH   HOH A . 
D 4 HOH   104 604 111 HOH   HOH A . 
D 4 HOH   105 605 75  HOH   HOH A . 
D 4 HOH   106 606 131 HOH   HOH A . 
D 4 HOH   107 607 133 HOH   HOH A . 
D 4 HOH   108 608 42  HOH   HOH A . 
D 4 HOH   109 609 93  HOH   HOH A . 
D 4 HOH   110 610 92  HOH   HOH A . 
D 4 HOH   111 611 154 HOH   HOH A . 
D 4 HOH   112 612 135 HOH   HOH A . 
D 4 HOH   113 613 10  HOH   HOH A . 
D 4 HOH   114 614 124 HOH   HOH A . 
D 4 HOH   115 615 61  HOH   HOH A . 
D 4 HOH   116 616 122 HOH   HOH A . 
D 4 HOH   117 617 120 HOH   HOH A . 
D 4 HOH   118 618 85  HOH   HOH A . 
D 4 HOH   119 619 14  HOH   HOH A . 
D 4 HOH   120 620 27  HOH   HOH A . 
D 4 HOH   121 621 109 HOH   HOH A . 
D 4 HOH   122 622 115 HOH   HOH A . 
D 4 HOH   123 623 128 HOH   HOH A . 
D 4 HOH   124 624 102 HOH   HOH A . 
D 4 HOH   125 625 47  HOH   HOH A . 
D 4 HOH   126 626 112 HOH   HOH A . 
D 4 HOH   127 627 105 HOH   HOH A . 
D 4 HOH   128 628 24  HOH   HOH A . 
D 4 HOH   129 629 43  HOH   HOH A . 
D 4 HOH   130 630 132 HOH   HOH A . 
D 4 HOH   131 631 147 HOH   HOH A . 
D 4 HOH   132 632 143 HOH   HOH A . 
D 4 HOH   133 633 148 HOH   HOH A . 
D 4 HOH   134 634 152 HOH   HOH A . 
D 4 HOH   135 635 155 HOH   HOH A . 
D 4 HOH   136 636 104 HOH   HOH A . 
D 4 HOH   137 637 141 HOH   HOH A . 
D 4 HOH   138 638 20  HOH   HOH A . 
D 4 HOH   139 639 84  HOH   HOH A . 
D 4 HOH   140 640 151 HOH   HOH A . 
D 4 HOH   141 641 136 HOH   HOH A . 
D 4 HOH   142 642 149 HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU -193 ? CG  ? A GLU 4   CG  
2  1 Y 1 A GLU -193 ? CD  ? A GLU 4   CD  
3  1 Y 1 A GLU -193 ? OE1 ? A GLU 4   OE1 
4  1 Y 1 A GLU -193 ? OE2 ? A GLU 4   OE2 
5  1 Y 1 A LYS -26  ? CG  ? A LYS 171 CG  
6  1 Y 1 A LYS -26  ? CD  ? A LYS 171 CD  
7  1 Y 1 A LYS -26  ? CE  ? A LYS 171 CE  
8  1 Y 1 A LYS -26  ? NZ  ? A LYS 171 NZ  
9  1 Y 1 A TYR -25  ? CG  ? A TYR 172 CG  
10 1 Y 1 A TYR -25  ? CD1 ? A TYR 172 CD1 
11 1 Y 1 A TYR -25  ? CD2 ? A TYR 172 CD2 
12 1 Y 1 A TYR -25  ? CE1 ? A TYR 172 CE1 
13 1 Y 1 A TYR -25  ? CE2 ? A TYR 172 CE2 
14 1 Y 1 A TYR -25  ? CZ  ? A TYR 172 CZ  
15 1 Y 1 A TYR -25  ? OH  ? A TYR 172 OH  
16 1 Y 1 A LYS -21  ? CG  ? A LYS 176 CG  
17 1 Y 1 A LYS -21  ? CD  ? A LYS 176 CD  
18 1 Y 1 A LYS -21  ? CE  ? A LYS 176 CE  
19 1 Y 1 A LYS -21  ? NZ  ? A LYS 176 NZ  
20 1 Y 1 A LYS -17  ? CG  ? A LYS 180 CG  
21 1 Y 1 A LYS -17  ? CD  ? A LYS 180 CD  
22 1 Y 1 A LYS -17  ? CE  ? A LYS 180 CE  
23 1 Y 1 A LYS -17  ? NZ  ? A LYS 180 NZ  
24 1 Y 1 A LYS -7   ? CG  ? A LYS 190 CG  
25 1 Y 1 A LYS -7   ? CD  ? A LYS 190 CD  
26 1 Y 1 A LYS -7   ? CE  ? A LYS 190 CE  
27 1 Y 1 A LYS -7   ? NZ  ? A LYS 190 NZ  
28 1 Y 1 A ARG 158  ? CG  ? A ARG 355 CG  
29 1 Y 1 A ARG 158  ? CD  ? A ARG 355 CD  
30 1 Y 1 A ARG 158  ? NE  ? A ARG 355 NE  
31 1 Y 1 A ARG 158  ? CZ  ? A ARG 355 CZ  
32 1 Y 1 A ARG 158  ? NH1 ? A ARG 355 NH1 
33 1 Y 1 A ARG 158  ? NH2 ? A ARG 355 NH2 
34 1 Y 1 A LYS 166  ? CG  ? A LYS 363 CG  
35 1 Y 1 A LYS 166  ? CD  ? A LYS 363 CD  
36 1 Y 1 A LYS 166  ? CE  ? A LYS 363 CE  
37 1 Y 1 A LYS 166  ? NZ  ? A LYS 363 NZ  
38 1 Y 1 A ARG 233  ? CG  ? A ARG 430 CG  
39 1 Y 1 A ARG 233  ? CD  ? A ARG 430 CD  
40 1 Y 1 A ARG 233  ? NE  ? A ARG 430 NE  
41 1 Y 1 A ARG 233  ? CZ  ? A ARG 430 CZ  
42 1 Y 1 A ARG 233  ? NH1 ? A ARG 430 NH1 
43 1 Y 1 A ARG 233  ? NH2 ? A ARG 430 NH2 
44 1 Y 1 A LYS 234  ? CG  ? A LYS 431 CG  
45 1 Y 1 A LYS 234  ? CD  ? A LYS 431 CD  
46 1 Y 1 A LYS 234  ? CE  ? A LYS 431 CE  
47 1 Y 1 A LYS 234  ? NZ  ? A LYS 431 NZ  
48 1 Y 1 A LYS 238  ? CG  ? A LYS 435 CG  
49 1 Y 1 A LYS 238  ? CD  ? A LYS 435 CD  
50 1 Y 1 A LYS 238  ? CE  ? A LYS 435 CE  
51 1 Y 1 A LYS 238  ? NZ  ? A LYS 435 NZ  
52 1 Y 1 A LYS 244  ? CG  ? A LYS 441 CG  
53 1 Y 1 A LYS 244  ? CD  ? A LYS 441 CD  
54 1 Y 1 A LYS 244  ? CE  ? A LYS 441 CE  
55 1 Y 1 A LYS 244  ? NZ  ? A LYS 441 NZ  
56 1 Y 1 A ARG 248  ? CG  ? A ARG 445 CG  
57 1 Y 1 A ARG 248  ? CD  ? A ARG 445 CD  
58 1 Y 1 A ARG 248  ? NE  ? A ARG 445 NE  
59 1 Y 1 A ARG 248  ? CZ  ? A ARG 445 CZ  
60 1 Y 1 A ARG 248  ? NH1 ? A ARG 445 NH1 
61 1 Y 1 A ARG 248  ? NH2 ? A ARG 445 NH2 
# 
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 ? ? ? '(1.15.2_3472: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                    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                     8Y20 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     100.100 
_cell.length_a_esd                 ? 
_cell.length_b                     137.280 
_cell.length_b_esd                 ? 
_cell.length_c                     38.660 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8Y20 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8Y20 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.32 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.00 
_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, HANGING 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    '25% PEG 3350, 0.2M Magnesium Formate, 1mM Maltose' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-09-24 
_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   0.97923 
_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                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97923 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Y20 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.23 
_reflns.d_resolution_low                               38.66 
_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                                     27170 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.78 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.60 
_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                                0.1239 
_reflns.pdbx_Rpim_I_all                                0.03452 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1189 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.23 
_reflns_shell.d_res_low                                     2.31 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.32 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2601 
_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                               13.3 
_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                               1.341 
_reflns_shell.pdbx_Rpim_I_all                               0.3645 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.89 
_reflns_shell.pdbx_CC_star                                  0.971 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.42 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.289 
_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                                 8Y20 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.23 
_refine.ls_d_res_low                             38.660 
_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                     27170 
_refine.ls_number_reflns_R_free                  1997 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.80 
_refine.ls_percent_reflns_R_free                 7.35 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1912 
_refine.ls_R_factor_R_free                       0.2431 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1871 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       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                 26.66 
_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                            0.27 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3952 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         84 
_refine_hist.number_atoms_solvent             142 
_refine_hist.number_atoms_total               4178 
_refine_hist.d_res_high                       2.23 
_refine_hist.d_res_low                        38.660 
# 
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' ? 0.013 ? 4136 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.884 ? 5627 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 9.186 ? 2437 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.066 ? 620  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006 ? 721  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.23   2.2755 . . 141 1784 99.00  . . . . 0.2650 . . . . . . . . . . . 0.3056 
'X-RAY DIFFRACTION' 2.2755 2.3370 . . 137 1731 99.00  . . . . 0.2442 . . . . . . . . . . . 0.2744 
'X-RAY DIFFRACTION' 2.3370 2.4058 . . 140 1760 100.00 . . . . 0.2381 . . . . . . . . . . . 0.3321 
'X-RAY DIFFRACTION' 2.4058 2.4834 . . 138 1751 100.00 . . . . 0.2350 . . . . . . . . . . . 0.2744 
'X-RAY DIFFRACTION' 2.4834 2.5722 . . 143 1798 100.00 . . . . 0.2263 . . . . . . . . . . . 0.2876 
'X-RAY DIFFRACTION' 2.5722 2.6752 . . 139 1753 100.00 . . . . 0.2130 . . . . . . . . . . . 0.3013 
'X-RAY DIFFRACTION' 2.6752 2.7969 . . 143 1794 100.00 . . . . 0.2120 . . . . . . . . . . . 0.2889 
'X-RAY DIFFRACTION' 2.7969 2.9443 . . 141 1784 100.00 . . . . 0.2171 . . . . . . . . . . . 0.2753 
'X-RAY DIFFRACTION' 2.9443 3.1287 . . 142 1782 100.00 . . . . 0.2302 . . . . . . . . . . . 0.3088 
'X-RAY DIFFRACTION' 3.1287 3.3701 . . 142 1791 100.00 . . . . 0.2039 . . . . . . . . . . . 0.2777 
'X-RAY DIFFRACTION' 3.3701 3.7090 . . 144 1816 100.00 . . . . 0.1835 . . . . . . . . . . . 0.2263 
'X-RAY DIFFRACTION' 3.7090 4.2451 . . 145 1832 100.00 . . . . 0.1606 . . . . . . . . . . . 0.2197 
'X-RAY DIFFRACTION' 4.2451 5.3462 . . 147 1843 100.00 . . . . 0.1431 . . . . . . . . . . . 0.1813 
'X-RAY DIFFRACTION' 5.3462 38.66  . . 155 1954 99.00  . . . . 0.1612 . . . . . . . . . . . 0.2082 
# 
_struct.entry_id                     8Y20 
_struct.title                        'Crystal structure of the Mcl-1 in complex with A-1210477' 
_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        8Y20 
_struct_keywords.text            'MCL-1, BAK, BH3, APOPTOSIS' 
_struct_keywords.pdbx_keywords   APOPTOSIS 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP MALE_ECO57 P0AEY0 ? 1 
;KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT
PDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPL
IAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV
NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAAT
MENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQT
;
27  
2 UNP MCL1_HUMAN Q07820 ? 1 
;ELYRQSLEIISRYLREQATGAKDTKPMGRSGATSRKALETLRRVGDGVQRNHETAFQGMLRKLDIKNEDDVKSLSRVMIH
VFSDGVTNWGRIVTLISFGAFVAKHLKTINQESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHV
;
173 
# 
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 8Y20 A 2   ? 367 ? P0AEY0 27  ? 392 ? -195 170 
2 2 8Y20 A 370 ? 518 ? Q07820 173 ? 321 ? 173  321 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8Y20 MET A 1   ? UNP P0AEY0 ?   ?   'initiating methionine' -196 1 
1 8Y20 ALA A 173 ? UNP P0AEY0 GLU 198 'engineered mutation'   -24  2 
1 8Y20 ALA A 174 ? UNP P0AEY0 ASN 199 'engineered mutation'   -23  3 
1 8Y20 ALA A 240 ? UNP P0AEY0 LYS 265 'engineered mutation'   43   4 
1 8Y20 GLY A 368 ? UNP P0AEY0 ?   ?   linker                  171  5 
1 8Y20 SER A 369 ? UNP P0AEY0 ?   ?   linker                  172  6 
2 8Y20 ALA A 391 ? UNP Q07820 LYS 194 'engineered mutation'   194  7 
2 8Y20 ALA A 394 ? UNP Q07820 LYS 197 'engineered mutation'   197  8 
2 8Y20 ALA A 398 ? UNP Q07820 ARG 201 'engineered mutation'   201  9 
# 
_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   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 810   ? 
1 MORE         8     ? 
1 'SSA (A^2)'  21590 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'isothermal titration calorimetry' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 17  ? GLY A 33  ? GLY A -180 GLY A -164 1 ? 17 
HELX_P HELX_P2  AA2 LYS A 43  ? THR A 54  ? LYS A -154 THR A -143 1 ? 12 
HELX_P HELX_P3  AA3 ARG A 67  ? SER A 74  ? ARG A -130 SER A -123 1 ? 8  
HELX_P HELX_P4  AA4 ASP A 83  ? ASP A 88  ? ASP A -114 ASP A -109 1 ? 6  
HELX_P HELX_P5  AA5 TYR A 91  ? VAL A 98  ? TYR A -106 VAL A -99  1 ? 8  
HELX_P HELX_P6  AA6 THR A 129 ? GLU A 131 ? THR A -68  GLU A -66  5 ? 3  
HELX_P HELX_P7  AA7 GLU A 132 ? ALA A 142 ? GLU A -65  ALA A -55  1 ? 11 
HELX_P HELX_P8  AA8 GLU A 154 ? ASP A 165 ? GLU A -43  ASP A -32  1 ? 12 
HELX_P HELX_P9  AA9 ASN A 186 ? ASN A 202 ? ASN A -11  ASN A 5    1 ? 17 
HELX_P HELX_P10 AB1 ASP A 210 ? LYS A 220 ? ASP A 13   LYS A 23   1 ? 11 
HELX_P HELX_P11 AB2 GLY A 229 ? TRP A 231 ? GLY A 32   TRP A 34   5 ? 3  
HELX_P HELX_P12 AB3 ALA A 232 ? SER A 239 ? ALA A 35   SER A 42   1 ? 8  
HELX_P HELX_P13 AB4 ASN A 273 ? TYR A 284 ? ASN A 76   TYR A 87   1 ? 12 
HELX_P HELX_P14 AB5 THR A 287 ? LYS A 298 ? THR A 90   LYS A 101  1 ? 12 
HELX_P HELX_P15 AB6 LEU A 305 ? ALA A 313 ? LEU A 108  ALA A 116  1 ? 9  
HELX_P HELX_P16 AB7 ASP A 315 ? GLY A 328 ? ASP A 118  GLY A 131  1 ? 14 
HELX_P HELX_P17 AB8 GLN A 336 ? GLY A 354 ? GLN A 139  GLY A 157  1 ? 19 
HELX_P HELX_P18 AB9 THR A 357 ? GLY A 389 ? THR A 160  GLY A 192  1 ? 33 
HELX_P HELX_P19 AC1 SER A 399 ? HIS A 421 ? SER A 202  HIS A 224  1 ? 23 
HELX_P HELX_P20 AC2 HIS A 421 ? LEU A 432 ? HIS A 224  LEU A 235  1 ? 12 
HELX_P HELX_P21 AC3 ASN A 436 ? ASP A 453 ? ASN A 239  ASP A 256  1 ? 18 
HELX_P HELX_P22 AC4 ASN A 457 ? ILE A 478 ? ASN A 260  ILE A 281  1 ? 22 
HELX_P HELX_P23 AC5 GLN A 480 ? SER A 482 ? GLN A 283  SER A 285  5 ? 3  
HELX_P HELX_P24 AC6 CYS A 483 ? GLN A 506 ? CYS A 286  GLN A 309  1 ? 24 
HELX_P HELX_P25 AC7 ARG A 507 ? PHE A 516 ? ARG A 310  PHE A 319  1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        both 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           B 
_struct_conn.ptnr1_label_comp_id           GLC 
_struct_conn.ptnr1_label_seq_id            . 
_struct_conn.ptnr1_label_atom_id           O4 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           GLC 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C1 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            B 
_struct_conn.ptnr1_auth_comp_id            GLC 
_struct_conn.ptnr1_auth_seq_id             1 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            GLC 
_struct_conn.ptnr2_auth_seq_id             2 
_struct_conn.ptnr2_symmetry                1_555 
_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               1.414 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LYS A 35  ? GLU A 39  ? LYS A -162 GLU A -158 
AA1 2 LYS A 7   ? TRP A 11  ? LYS A -190 TRP A -186 
AA1 3 ILE A 60  ? ALA A 64  ? ILE A -137 ALA A -133 
AA1 4 PHE A 259 ? ILE A 267 ? PHE A 62   ILE A 70   
AA1 5 TYR A 107 ? GLU A 112 ? TYR A -90  GLU A -85  
AA1 6 ALA A 302 ? VAL A 303 ? ALA A 105  VAL A 106  
AA2 1 LYS A 35  ? GLU A 39  ? LYS A -162 GLU A -158 
AA2 2 LYS A 7   ? TRP A 11  ? LYS A -190 TRP A -186 
AA2 3 ILE A 60  ? ALA A 64  ? ILE A -137 ALA A -133 
AA2 4 PHE A 259 ? ILE A 267 ? PHE A 62   ILE A 70   
AA2 5 GLU A 329 ? ILE A 330 ? GLU A 132  ILE A 133  
AA3 1 ARG A 99  ? TYR A 100 ? ARG A -98  TYR A -97  
AA3 2 LYS A 103 ? LEU A 104 ? LYS A -94  LEU A -93  
AA4 1 SER A 146 ? LEU A 148 ? SER A -51  LEU A -49  
AA4 2 THR A 223 ? ASN A 228 ? THR A 26   ASN A 31   
AA4 3 SER A 115 ? ASN A 119 ? SER A -82  ASN A -78  
AA4 4 TYR A 243 ? THR A 246 ? TYR A 46   THR A 49   
AA5 1 TYR A 168 ? LYS A 171 ? TYR A -29  LYS A -26  
AA5 2 ASP A 178 ? GLY A 183 ? ASP A -19  GLY A -14  
# 
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 GLU A 39  ? O GLU A -158 N ILE A 10  ? N ILE A -187 
AA1 2 3 N TRP A 11  ? N TRP A -186 O PHE A 62  ? O PHE A -135 
AA1 3 4 N TRP A 63  ? N TRP A -134 O SER A 264 ? O SER A 67   
AA1 4 5 O GLY A 261 ? O GLY A 64   N GLU A 112 ? N GLU A -85  
AA1 5 6 N VAL A 111 ? N VAL A -86  O ALA A 302 ? O ALA A 105  
AA2 1 2 O GLU A 39  ? O GLU A -158 N ILE A 10  ? N ILE A -187 
AA2 2 3 N TRP A 11  ? N TRP A -186 O PHE A 62  ? O PHE A -135 
AA2 3 4 N TRP A 63  ? N TRP A -134 O SER A 264 ? O SER A 67   
AA2 4 5 N VAL A 260 ? N VAL A 63   O GLU A 329 ? O GLU A 132  
AA3 1 2 N TYR A 100 ? N TYR A -97  O LYS A 103 ? O LYS A -94  
AA4 1 2 N SER A 146 ? N SER A -51  O ALA A 224 ? O ALA A 27   
AA4 2 3 O THR A 226 ? O THR A 29   N ILE A 117 ? N ILE A -80  
AA4 3 4 N LEU A 116 ? N LEU A -81  O THR A 246 ? O THR A 49   
AA5 1 2 N TYR A 168 ? N TYR A -29  O GLY A 183 ? O GLY A -14  
# 
_pdbx_entry_details.entry_id                   8Y20 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   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 ALA A -28 ? ? -86.78  -78.26  
2 1 ILE A -18 ? ? -58.94  -9.61   
3 1 ASP A 13  ? ? -119.61 -167.64 
4 1 TYR A 87  ? ? -122.44 -53.79  
5 1 PRO A 198 ? ? -47.08  150.42  
# 
_pdbx_molecule_features.prd_id    PRD_900001 
_pdbx_molecule_features.name      alpha-maltose 
_pdbx_molecule_features.type      Oligosaccharide 
_pdbx_molecule_features.class     Nutrient 
_pdbx_molecule_features.details   oligosaccharide 
# 
_pdbx_molecule.instance_id   1 
_pdbx_molecule.prd_id        PRD_900001 
_pdbx_molecule.asym_id       B 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -10.7668 48.8034 16.5846 0.4014 ? 0.0276  ? 0.0240  ? 0.2801 ? 0.0038  ? 0.2515 ? 3.2059 ? -0.8717 
? 0.3367 ? 1.2333 ? 0.1865 ? 0.7009 ? -0.0573 ? -0.1434 ? -0.0811 ? 0.0375  ? 0.1115 ? -0.0294 ? 0.0084  ? 0.0985 ? -0.0472 ? 
2 'X-RAY DIFFRACTION' ? refined -17.5110 14.8090 6.7727  0.2325 ? -0.0384 ? -0.0080 ? 0.2617 ? -0.0037 ? 0.3108 ? 1.3819 ? -0.6932 
? 0.2359 ? 5.9701 ? 0.4219 ? 3.3601 ? -0.0276 ? 0.1109  ? 0.0160  ? -0.4193 ? 0.0254 ? -0.0473 ? -0.1914 ? 0.1962 ? -0.0145 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid -195 through 160 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 161 through 321 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET -196 ? A MET 1   
2 1 Y 1 A ALA -24  ? A ALA 173 
3 1 Y 1 A ALA -23  ? A ALA 174 
4 1 Y 1 A GLY -22  ? A GLY 175 
# 
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 
A1LXV C1   C Y N 1   
A1LXV C10  C Y N 2   
A1LXV C11  C Y N 3   
A1LXV C12  C N N 4   
A1LXV C13  C Y N 5   
A1LXV C14  C Y N 6   
A1LXV C15  C Y N 7   
A1LXV C16  C Y N 8   
A1LXV C17  C Y N 9   
A1LXV C18  C Y N 10  
A1LXV C19  C N N 11  
A1LXV C2   C Y N 12  
A1LXV C20  C N N 13  
A1LXV C21  C N N 14  
A1LXV C22  C N N 15  
A1LXV C23  C N N 16  
A1LXV C24  C N N 17  
A1LXV C25  C N N 18  
A1LXV C26  C N N 19  
A1LXV C27  C N N 20  
A1LXV C28  C N N 21  
A1LXV C29  C N N 22  
A1LXV C3   C Y N 23  
A1LXV C30  C N N 24  
A1LXV C31  C N N 25  
A1LXV C32  C N N 26  
A1LXV C33  C N N 27  
A1LXV C34  C N N 28  
A1LXV C35  C N N 29  
A1LXV C36  C Y N 30  
A1LXV C37  C Y N 31  
A1LXV C38  C Y N 32  
A1LXV C39  C Y N 33  
A1LXV C4   C Y N 34  
A1LXV C40  C Y N 35  
A1LXV C41  C Y N 36  
A1LXV C42  C Y N 37  
A1LXV C43  C Y N 38  
A1LXV C44  C Y N 39  
A1LXV C45  C Y N 40  
A1LXV C46  C N N 41  
A1LXV C5   C Y N 42  
A1LXV C6   C Y N 43  
A1LXV C7   C Y N 44  
A1LXV C8   C Y N 45  
A1LXV C9   C Y N 46  
A1LXV N1   N Y N 47  
A1LXV N2   N Y N 48  
A1LXV N3   N Y N 49  
A1LXV N4   N N N 50  
A1LXV N5   N N N 51  
A1LXV N6   N N N 52  
A1LXV N7   N N N 53  
A1LXV O1   O N N 54  
A1LXV O2   O N N 55  
A1LXV O3   O N N 56  
A1LXV O4   O N N 57  
A1LXV O5   O N N 58  
A1LXV O6   O N N 59  
A1LXV O7   O N N 60  
A1LXV S1   S N N 61  
A1LXV H1   H N N 62  
A1LXV H5   H N N 63  
A1LXV H6   H N N 64  
A1LXV H4   H N N 65  
A1LXV H7   H N N 66  
A1LXV H8   H N N 67  
A1LXV H9   H N N 68  
A1LXV H10  H N N 69  
A1LXV H12  H N N 70  
A1LXV H11  H N N 71  
A1LXV H2   H N N 72  
A1LXV H13  H N N 73  
A1LXV H14  H N N 74  
A1LXV H16  H N N 75  
A1LXV H15  H N N 76  
A1LXV H17  H N N 77  
A1LXV H18  H N N 78  
A1LXV H20  H N N 79  
A1LXV H19  H N N 80  
A1LXV H21  H N N 81  
A1LXV H22  H N N 82  
A1LXV H24  H N N 83  
A1LXV H23  H N N 84  
A1LXV H25  H N N 85  
A1LXV H26  H N N 86  
A1LXV H27  H N N 87  
A1LXV H29  H N N 88  
A1LXV H28  H N N 89  
A1LXV H31  H N N 90  
A1LXV H30  H N N 91  
A1LXV H33  H N N 92  
A1LXV H32  H N N 93  
A1LXV H35  H N N 94  
A1LXV H34  H N N 95  
A1LXV H3   H N N 96  
A1LXV H37  H N N 97  
A1LXV H36  H N N 98  
A1LXV H38  H N N 99  
A1LXV H39  H N N 100 
A1LXV H41  H N N 101 
A1LXV H40  H N N 102 
A1LXV H43  H N N 103 
A1LXV H42  H N N 104 
A1LXV H44  H N N 105 
A1LXV H45  H N N 106 
A1LXV H46  H N N 107 
A1LXV H47  H N N 108 
A1LXV H48  H N N 109 
A1LXV H49  H N N 110 
A1LXV H50  H N N 111 
A1LXV H51  H N N 112 
A1LXV H52  H N N 113 
A1LXV H53  H N N 114 
A1LXV H54  H N N 115 
A1LXV H56  H N N 116 
ALA   N    N N N 117 
ALA   CA   C N S 118 
ALA   C    C N N 119 
ALA   O    O N N 120 
ALA   CB   C N N 121 
ALA   OXT  O N N 122 
ALA   H    H N N 123 
ALA   H2   H N N 124 
ALA   HA   H N N 125 
ALA   HB1  H N N 126 
ALA   HB2  H N N 127 
ALA   HB3  H N N 128 
ALA   HXT  H N N 129 
ARG   N    N N N 130 
ARG   CA   C N S 131 
ARG   C    C N N 132 
ARG   O    O N N 133 
ARG   CB   C N N 134 
ARG   CG   C N N 135 
ARG   CD   C N N 136 
ARG   NE   N N N 137 
ARG   CZ   C N N 138 
ARG   NH1  N N N 139 
ARG   NH2  N N N 140 
ARG   OXT  O N N 141 
ARG   H    H N N 142 
ARG   H2   H N N 143 
ARG   HA   H N N 144 
ARG   HB2  H N N 145 
ARG   HB3  H N N 146 
ARG   HG2  H N N 147 
ARG   HG3  H N N 148 
ARG   HD2  H N N 149 
ARG   HD3  H N N 150 
ARG   HE   H N N 151 
ARG   HH11 H N N 152 
ARG   HH12 H N N 153 
ARG   HH21 H N N 154 
ARG   HH22 H N N 155 
ARG   HXT  H N N 156 
ASN   N    N N N 157 
ASN   CA   C N S 158 
ASN   C    C N N 159 
ASN   O    O N N 160 
ASN   CB   C N N 161 
ASN   CG   C N N 162 
ASN   OD1  O N N 163 
ASN   ND2  N N N 164 
ASN   OXT  O N N 165 
ASN   H    H N N 166 
ASN   H2   H N N 167 
ASN   HA   H N N 168 
ASN   HB2  H N N 169 
ASN   HB3  H N N 170 
ASN   HD21 H N N 171 
ASN   HD22 H N N 172 
ASN   HXT  H N N 173 
ASP   N    N N N 174 
ASP   CA   C N S 175 
ASP   C    C N N 176 
ASP   O    O N N 177 
ASP   CB   C N N 178 
ASP   CG   C N N 179 
ASP   OD1  O N N 180 
ASP   OD2  O N N 181 
ASP   OXT  O N N 182 
ASP   H    H N N 183 
ASP   H2   H N N 184 
ASP   HA   H N N 185 
ASP   HB2  H N N 186 
ASP   HB3  H N N 187 
ASP   HD2  H N N 188 
ASP   HXT  H N N 189 
CYS   N    N N N 190 
CYS   CA   C N R 191 
CYS   C    C N N 192 
CYS   O    O N N 193 
CYS   CB   C N N 194 
CYS   SG   S N N 195 
CYS   OXT  O N N 196 
CYS   H    H N N 197 
CYS   H2   H N N 198 
CYS   HA   H N N 199 
CYS   HB2  H N N 200 
CYS   HB3  H N N 201 
CYS   HG   H N N 202 
CYS   HXT  H N N 203 
GLC   C1   C N S 204 
GLC   C2   C N R 205 
GLC   C3   C N S 206 
GLC   C4   C N S 207 
GLC   C5   C N R 208 
GLC   C6   C N N 209 
GLC   O1   O N N 210 
GLC   O2   O N N 211 
GLC   O3   O N N 212 
GLC   O4   O N N 213 
GLC   O5   O N N 214 
GLC   O6   O N N 215 
GLC   H1   H N N 216 
GLC   H2   H N N 217 
GLC   H3   H N N 218 
GLC   H4   H N N 219 
GLC   H5   H N N 220 
GLC   H61  H N N 221 
GLC   H62  H N N 222 
GLC   HO1  H N N 223 
GLC   HO2  H N N 224 
GLC   HO3  H N N 225 
GLC   HO4  H N N 226 
GLC   HO6  H N N 227 
GLN   N    N N N 228 
GLN   CA   C N S 229 
GLN   C    C N N 230 
GLN   O    O N N 231 
GLN   CB   C N N 232 
GLN   CG   C N N 233 
GLN   CD   C N N 234 
GLN   OE1  O N N 235 
GLN   NE2  N N N 236 
GLN   OXT  O N N 237 
GLN   H    H N N 238 
GLN   H2   H N N 239 
GLN   HA   H N N 240 
GLN   HB2  H N N 241 
GLN   HB3  H N N 242 
GLN   HG2  H N N 243 
GLN   HG3  H N N 244 
GLN   HE21 H N N 245 
GLN   HE22 H N N 246 
GLN   HXT  H N N 247 
GLU   N    N N N 248 
GLU   CA   C N S 249 
GLU   C    C N N 250 
GLU   O    O N N 251 
GLU   CB   C N N 252 
GLU   CG   C N N 253 
GLU   CD   C N N 254 
GLU   OE1  O N N 255 
GLU   OE2  O N N 256 
GLU   OXT  O N N 257 
GLU   H    H N N 258 
GLU   H2   H N N 259 
GLU   HA   H N N 260 
GLU   HB2  H N N 261 
GLU   HB3  H N N 262 
GLU   HG2  H N N 263 
GLU   HG3  H N N 264 
GLU   HE2  H N N 265 
GLU   HXT  H N N 266 
GLY   N    N N N 267 
GLY   CA   C N N 268 
GLY   C    C N N 269 
GLY   O    O N N 270 
GLY   OXT  O N N 271 
GLY   H    H N N 272 
GLY   H2   H N N 273 
GLY   HA2  H N N 274 
GLY   HA3  H N N 275 
GLY   HXT  H N N 276 
HIS   N    N N N 277 
HIS   CA   C N S 278 
HIS   C    C N N 279 
HIS   O    O N N 280 
HIS   CB   C N N 281 
HIS   CG   C Y N 282 
HIS   ND1  N Y N 283 
HIS   CD2  C Y N 284 
HIS   CE1  C Y N 285 
HIS   NE2  N Y N 286 
HIS   OXT  O N N 287 
HIS   H    H N N 288 
HIS   H2   H N N 289 
HIS   HA   H N N 290 
HIS   HB2  H N N 291 
HIS   HB3  H N N 292 
HIS   HD1  H N N 293 
HIS   HD2  H N N 294 
HIS   HE1  H N N 295 
HIS   HE2  H N N 296 
HIS   HXT  H N N 297 
HOH   O    O N N 298 
HOH   H1   H N N 299 
HOH   H2   H N N 300 
ILE   N    N N N 301 
ILE   CA   C N S 302 
ILE   C    C N N 303 
ILE   O    O N N 304 
ILE   CB   C N S 305 
ILE   CG1  C N N 306 
ILE   CG2  C N N 307 
ILE   CD1  C N N 308 
ILE   OXT  O N N 309 
ILE   H    H N N 310 
ILE   H2   H N N 311 
ILE   HA   H N N 312 
ILE   HB   H N N 313 
ILE   HG12 H N N 314 
ILE   HG13 H N N 315 
ILE   HG21 H N N 316 
ILE   HG22 H N N 317 
ILE   HG23 H N N 318 
ILE   HD11 H N N 319 
ILE   HD12 H N N 320 
ILE   HD13 H N N 321 
ILE   HXT  H N N 322 
LEU   N    N N N 323 
LEU   CA   C N S 324 
LEU   C    C N N 325 
LEU   O    O N N 326 
LEU   CB   C N N 327 
LEU   CG   C N N 328 
LEU   CD1  C N N 329 
LEU   CD2  C N N 330 
LEU   OXT  O N N 331 
LEU   H    H N N 332 
LEU   H2   H N N 333 
LEU   HA   H N N 334 
LEU   HB2  H N N 335 
LEU   HB3  H N N 336 
LEU   HG   H N N 337 
LEU   HD11 H N N 338 
LEU   HD12 H N N 339 
LEU   HD13 H N N 340 
LEU   HD21 H N N 341 
LEU   HD22 H N N 342 
LEU   HD23 H N N 343 
LEU   HXT  H N N 344 
LYS   N    N N N 345 
LYS   CA   C N S 346 
LYS   C    C N N 347 
LYS   O    O N N 348 
LYS   CB   C N N 349 
LYS   CG   C N N 350 
LYS   CD   C N N 351 
LYS   CE   C N N 352 
LYS   NZ   N N N 353 
LYS   OXT  O N N 354 
LYS   H    H N N 355 
LYS   H2   H N N 356 
LYS   HA   H N N 357 
LYS   HB2  H N N 358 
LYS   HB3  H N N 359 
LYS   HG2  H N N 360 
LYS   HG3  H N N 361 
LYS   HD2  H N N 362 
LYS   HD3  H N N 363 
LYS   HE2  H N N 364 
LYS   HE3  H N N 365 
LYS   HZ1  H N N 366 
LYS   HZ2  H N N 367 
LYS   HZ3  H N N 368 
LYS   HXT  H N N 369 
MET   N    N N N 370 
MET   CA   C N S 371 
MET   C    C N N 372 
MET   O    O N N 373 
MET   CB   C N N 374 
MET   CG   C N N 375 
MET   SD   S N N 376 
MET   CE   C N N 377 
MET   OXT  O N N 378 
MET   H    H N N 379 
MET   H2   H N N 380 
MET   HA   H N N 381 
MET   HB2  H N N 382 
MET   HB3  H N N 383 
MET   HG2  H N N 384 
MET   HG3  H N N 385 
MET   HE1  H N N 386 
MET   HE2  H N N 387 
MET   HE3  H N N 388 
MET   HXT  H N N 389 
PHE   N    N N N 390 
PHE   CA   C N S 391 
PHE   C    C N N 392 
PHE   O    O N N 393 
PHE   CB   C N N 394 
PHE   CG   C Y N 395 
PHE   CD1  C Y N 396 
PHE   CD2  C Y N 397 
PHE   CE1  C Y N 398 
PHE   CE2  C Y N 399 
PHE   CZ   C Y N 400 
PHE   OXT  O N N 401 
PHE   H    H N N 402 
PHE   H2   H N N 403 
PHE   HA   H N N 404 
PHE   HB2  H N N 405 
PHE   HB3  H N N 406 
PHE   HD1  H N N 407 
PHE   HD2  H N N 408 
PHE   HE1  H N N 409 
PHE   HE2  H N N 410 
PHE   HZ   H N N 411 
PHE   HXT  H N N 412 
PRO   N    N N N 413 
PRO   CA   C N S 414 
PRO   C    C N N 415 
PRO   O    O N N 416 
PRO   CB   C N N 417 
PRO   CG   C N N 418 
PRO   CD   C N N 419 
PRO   OXT  O N N 420 
PRO   H    H N N 421 
PRO   HA   H N N 422 
PRO   HB2  H N N 423 
PRO   HB3  H N N 424 
PRO   HG2  H N N 425 
PRO   HG3  H N N 426 
PRO   HD2  H N N 427 
PRO   HD3  H N N 428 
PRO   HXT  H N N 429 
SER   N    N N N 430 
SER   CA   C N S 431 
SER   C    C N N 432 
SER   O    O N N 433 
SER   CB   C N N 434 
SER   OG   O N N 435 
SER   OXT  O N N 436 
SER   H    H N N 437 
SER   H2   H N N 438 
SER   HA   H N N 439 
SER   HB2  H N N 440 
SER   HB3  H N N 441 
SER   HG   H N N 442 
SER   HXT  H N N 443 
THR   N    N N N 444 
THR   CA   C N S 445 
THR   C    C N N 446 
THR   O    O N N 447 
THR   CB   C N R 448 
THR   OG1  O N N 449 
THR   CG2  C N N 450 
THR   OXT  O N N 451 
THR   H    H N N 452 
THR   H2   H N N 453 
THR   HA   H N N 454 
THR   HB   H N N 455 
THR   HG1  H N N 456 
THR   HG21 H N N 457 
THR   HG22 H N N 458 
THR   HG23 H N N 459 
THR   HXT  H N N 460 
TRP   N    N N N 461 
TRP   CA   C N S 462 
TRP   C    C N N 463 
TRP   O    O N N 464 
TRP   CB   C N N 465 
TRP   CG   C Y N 466 
TRP   CD1  C Y N 467 
TRP   CD2  C Y N 468 
TRP   NE1  N Y N 469 
TRP   CE2  C Y N 470 
TRP   CE3  C Y N 471 
TRP   CZ2  C Y N 472 
TRP   CZ3  C Y N 473 
TRP   CH2  C Y N 474 
TRP   OXT  O N N 475 
TRP   H    H N N 476 
TRP   H2   H N N 477 
TRP   HA   H N N 478 
TRP   HB2  H N N 479 
TRP   HB3  H N N 480 
TRP   HD1  H N N 481 
TRP   HE1  H N N 482 
TRP   HE3  H N N 483 
TRP   HZ2  H N N 484 
TRP   HZ3  H N N 485 
TRP   HH2  H N N 486 
TRP   HXT  H N N 487 
TYR   N    N N N 488 
TYR   CA   C N S 489 
TYR   C    C N N 490 
TYR   O    O N N 491 
TYR   CB   C N N 492 
TYR   CG   C Y N 493 
TYR   CD1  C Y N 494 
TYR   CD2  C Y N 495 
TYR   CE1  C Y N 496 
TYR   CE2  C Y N 497 
TYR   CZ   C Y N 498 
TYR   OH   O N N 499 
TYR   OXT  O N N 500 
TYR   H    H N N 501 
TYR   H2   H N N 502 
TYR   HA   H N N 503 
TYR   HB2  H N N 504 
TYR   HB3  H N N 505 
TYR   HD1  H N N 506 
TYR   HD2  H N N 507 
TYR   HE1  H N N 508 
TYR   HE2  H N N 509 
TYR   HH   H N N 510 
TYR   HXT  H N N 511 
VAL   N    N N N 512 
VAL   CA   C N S 513 
VAL   C    C N N 514 
VAL   O    O N N 515 
VAL   CB   C N N 516 
VAL   CG1  C N N 517 
VAL   CG2  C N N 518 
VAL   OXT  O N N 519 
VAL   H    H N N 520 
VAL   H2   H N N 521 
VAL   HA   H N N 522 
VAL   HB   H N N 523 
VAL   HG11 H N N 524 
VAL   HG12 H N N 525 
VAL   HG13 H N N 526 
VAL   HG21 H N N 527 
VAL   HG22 H N N 528 
VAL   HG23 H N N 529 
VAL   HXT  H N N 530 
# 
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 
A1LXV O3  C30  sing N N 1   
A1LXV O3  C29  sing N N 2   
A1LXV C30 C31  sing N N 3   
A1LXV C29 C28  sing N N 4   
A1LXV C31 N7   sing N N 5   
A1LXV C28 N7   sing N N 6   
A1LXV C23 N3   sing N N 7   
A1LXV N7  C27  sing N N 8   
A1LXV N2  N3   sing Y N 9   
A1LXV N2  C10  doub Y N 10  
A1LXV N3  C11  sing Y N 11  
A1LXV C27 C26  sing N N 12  
A1LXV C18 C17  doub Y N 13  
A1LXV C18 C13  sing Y N 14  
A1LXV C10 C12  sing N N 15  
A1LXV C10 C9   sing Y N 16  
A1LXV O7  C13  sing N N 17  
A1LXV O7  C46  sing N N 18  
A1LXV C17 C16  sing Y N 19  
A1LXV C11 C9   doub Y N 20  
A1LXV C11 C46  sing N N 21  
A1LXV C26 N1   sing N N 22  
A1LXV C13 C14  doub Y N 23  
A1LXV C9  C6   sing N N 24  
A1LXV C16 N4   sing N N 25  
A1LXV C16 C15  doub Y N 26  
A1LXV C20 C19  sing N N 27  
A1LXV C20 N5   sing N N 28  
A1LXV C19 N4   sing N N 29  
A1LXV O4  C32  doub N N 30  
A1LXV N1  C5   sing Y N 31  
A1LXV N1  C8   sing Y N 32  
A1LXV N4  C22  sing N N 33  
A1LXV C14 C15  sing Y N 34  
A1LXV C32 O5   sing N N 35  
A1LXV C32 C8   sing N N 36  
A1LXV C6  C5   doub Y N 37  
A1LXV C6  C1   sing Y N 38  
A1LXV O1  S1   doub N N 39  
A1LXV C5  C4   sing Y N 40  
A1LXV C8  C7   doub Y N 41  
A1LXV C22 C21  sing N N 42  
A1LXV N5  S1   sing N N 43  
A1LXV N5  C21  sing N N 44  
A1LXV C1  C2   doub Y N 45  
A1LXV S1  O2   doub N N 46  
A1LXV S1  N6   sing N N 47  
A1LXV C7  C4   sing Y N 48  
A1LXV C7  C33  sing N N 49  
A1LXV C4  C3   doub Y N 50  
A1LXV C2  C3   sing Y N 51  
A1LXV C34 C33  sing N N 52  
A1LXV C34 C35  sing N N 53  
A1LXV C25 N6   sing N N 54  
A1LXV N6  C24  sing N N 55  
A1LXV C35 O6   sing N N 56  
A1LXV C41 C40  doub Y N 57  
A1LXV C41 C36  sing Y N 58  
A1LXV O6  C36  sing N N 59  
A1LXV C40 C39  sing Y N 60  
A1LXV C36 C37  doub Y N 61  
A1LXV C37 C38  sing Y N 62  
A1LXV C37 C42  sing Y N 63  
A1LXV C39 C38  doub Y N 64  
A1LXV C38 C45  sing Y N 65  
A1LXV C42 C43  doub Y N 66  
A1LXV C43 C44  sing Y N 67  
A1LXV C45 C44  doub Y N 68  
A1LXV C1  H1   sing N N 69  
A1LXV C12 H5   sing N N 70  
A1LXV C12 H6   sing N N 71  
A1LXV C12 H4   sing N N 72  
A1LXV C14 H7   sing N N 73  
A1LXV C15 H8   sing N N 74  
A1LXV C17 H9   sing N N 75  
A1LXV C18 H10  sing N N 76  
A1LXV C19 H12  sing N N 77  
A1LXV C19 H11  sing N N 78  
A1LXV C2  H2   sing N N 79  
A1LXV C20 H13  sing N N 80  
A1LXV C20 H14  sing N N 81  
A1LXV C21 H16  sing N N 82  
A1LXV C21 H15  sing N N 83  
A1LXV C22 H17  sing N N 84  
A1LXV C22 H18  sing N N 85  
A1LXV C23 H20  sing N N 86  
A1LXV C23 H19  sing N N 87  
A1LXV C23 H21  sing N N 88  
A1LXV C24 H22  sing N N 89  
A1LXV C24 H24  sing N N 90  
A1LXV C24 H23  sing N N 91  
A1LXV C25 H25  sing N N 92  
A1LXV C25 H26  sing N N 93  
A1LXV C25 H27  sing N N 94  
A1LXV C26 H29  sing N N 95  
A1LXV C26 H28  sing N N 96  
A1LXV C27 H31  sing N N 97  
A1LXV C27 H30  sing N N 98  
A1LXV C28 H33  sing N N 99  
A1LXV C28 H32  sing N N 100 
A1LXV C29 H35  sing N N 101 
A1LXV C29 H34  sing N N 102 
A1LXV C3  H3   sing N N 103 
A1LXV C30 H37  sing N N 104 
A1LXV C30 H36  sing N N 105 
A1LXV C31 H38  sing N N 106 
A1LXV C31 H39  sing N N 107 
A1LXV C33 H41  sing N N 108 
A1LXV C33 H40  sing N N 109 
A1LXV C34 H43  sing N N 110 
A1LXV C34 H42  sing N N 111 
A1LXV C35 H44  sing N N 112 
A1LXV C35 H45  sing N N 113 
A1LXV C39 H46  sing N N 114 
A1LXV C40 H47  sing N N 115 
A1LXV C41 H48  sing N N 116 
A1LXV C42 H49  sing N N 117 
A1LXV C43 H50  sing N N 118 
A1LXV C44 H51  sing N N 119 
A1LXV C45 H52  sing N N 120 
A1LXV C46 H53  sing N N 121 
A1LXV C46 H54  sing N N 122 
A1LXV O5  H56  sing N N 123 
ALA   N   CA   sing N N 124 
ALA   N   H    sing N N 125 
ALA   N   H2   sing N N 126 
ALA   CA  C    sing N N 127 
ALA   CA  CB   sing N N 128 
ALA   CA  HA   sing N N 129 
ALA   C   O    doub N N 130 
ALA   C   OXT  sing N N 131 
ALA   CB  HB1  sing N N 132 
ALA   CB  HB2  sing N N 133 
ALA   CB  HB3  sing N N 134 
ALA   OXT HXT  sing N N 135 
ARG   N   CA   sing N N 136 
ARG   N   H    sing N N 137 
ARG   N   H2   sing N N 138 
ARG   CA  C    sing N N 139 
ARG   CA  CB   sing N N 140 
ARG   CA  HA   sing N N 141 
ARG   C   O    doub N N 142 
ARG   C   OXT  sing N N 143 
ARG   CB  CG   sing N N 144 
ARG   CB  HB2  sing N N 145 
ARG   CB  HB3  sing N N 146 
ARG   CG  CD   sing N N 147 
ARG   CG  HG2  sing N N 148 
ARG   CG  HG3  sing N N 149 
ARG   CD  NE   sing N N 150 
ARG   CD  HD2  sing N N 151 
ARG   CD  HD3  sing N N 152 
ARG   NE  CZ   sing N N 153 
ARG   NE  HE   sing N N 154 
ARG   CZ  NH1  sing N N 155 
ARG   CZ  NH2  doub N N 156 
ARG   NH1 HH11 sing N N 157 
ARG   NH1 HH12 sing N N 158 
ARG   NH2 HH21 sing N N 159 
ARG   NH2 HH22 sing N N 160 
ARG   OXT HXT  sing N N 161 
ASN   N   CA   sing N N 162 
ASN   N   H    sing N N 163 
ASN   N   H2   sing N N 164 
ASN   CA  C    sing N N 165 
ASN   CA  CB   sing N N 166 
ASN   CA  HA   sing N N 167 
ASN   C   O    doub N N 168 
ASN   C   OXT  sing N N 169 
ASN   CB  CG   sing N N 170 
ASN   CB  HB2  sing N N 171 
ASN   CB  HB3  sing N N 172 
ASN   CG  OD1  doub N N 173 
ASN   CG  ND2  sing N N 174 
ASN   ND2 HD21 sing N N 175 
ASN   ND2 HD22 sing N N 176 
ASN   OXT HXT  sing N N 177 
ASP   N   CA   sing N N 178 
ASP   N   H    sing N N 179 
ASP   N   H2   sing N N 180 
ASP   CA  C    sing N N 181 
ASP   CA  CB   sing N N 182 
ASP   CA  HA   sing N N 183 
ASP   C   O    doub N N 184 
ASP   C   OXT  sing N N 185 
ASP   CB  CG   sing N N 186 
ASP   CB  HB2  sing N N 187 
ASP   CB  HB3  sing N N 188 
ASP   CG  OD1  doub N N 189 
ASP   CG  OD2  sing N N 190 
ASP   OD2 HD2  sing N N 191 
ASP   OXT HXT  sing N N 192 
CYS   N   CA   sing N N 193 
CYS   N   H    sing N N 194 
CYS   N   H2   sing N N 195 
CYS   CA  C    sing N N 196 
CYS   CA  CB   sing N N 197 
CYS   CA  HA   sing N N 198 
CYS   C   O    doub N N 199 
CYS   C   OXT  sing N N 200 
CYS   CB  SG   sing N N 201 
CYS   CB  HB2  sing N N 202 
CYS   CB  HB3  sing N N 203 
CYS   SG  HG   sing N N 204 
CYS   OXT HXT  sing N N 205 
GLC   C1  C2   sing N N 206 
GLC   C1  O1   sing N N 207 
GLC   C1  O5   sing N N 208 
GLC   C1  H1   sing N N 209 
GLC   C2  C3   sing N N 210 
GLC   C2  O2   sing N N 211 
GLC   C2  H2   sing N N 212 
GLC   C3  C4   sing N N 213 
GLC   C3  O3   sing N N 214 
GLC   C3  H3   sing N N 215 
GLC   C4  C5   sing N N 216 
GLC   C4  O4   sing N N 217 
GLC   C4  H4   sing N N 218 
GLC   C5  C6   sing N N 219 
GLC   C5  O5   sing N N 220 
GLC   C5  H5   sing N N 221 
GLC   C6  O6   sing N N 222 
GLC   C6  H61  sing N N 223 
GLC   C6  H62  sing N N 224 
GLC   O1  HO1  sing N N 225 
GLC   O2  HO2  sing N N 226 
GLC   O3  HO3  sing N N 227 
GLC   O4  HO4  sing N N 228 
GLC   O6  HO6  sing N N 229 
GLN   N   CA   sing N N 230 
GLN   N   H    sing N N 231 
GLN   N   H2   sing N N 232 
GLN   CA  C    sing N N 233 
GLN   CA  CB   sing N N 234 
GLN   CA  HA   sing N N 235 
GLN   C   O    doub N N 236 
GLN   C   OXT  sing N N 237 
GLN   CB  CG   sing N N 238 
GLN   CB  HB2  sing N N 239 
GLN   CB  HB3  sing N N 240 
GLN   CG  CD   sing N N 241 
GLN   CG  HG2  sing N N 242 
GLN   CG  HG3  sing N N 243 
GLN   CD  OE1  doub N N 244 
GLN   CD  NE2  sing N N 245 
GLN   NE2 HE21 sing N N 246 
GLN   NE2 HE22 sing N N 247 
GLN   OXT HXT  sing N N 248 
GLU   N   CA   sing N N 249 
GLU   N   H    sing N N 250 
GLU   N   H2   sing N N 251 
GLU   CA  C    sing N N 252 
GLU   CA  CB   sing N N 253 
GLU   CA  HA   sing N N 254 
GLU   C   O    doub N N 255 
GLU   C   OXT  sing N N 256 
GLU   CB  CG   sing N N 257 
GLU   CB  HB2  sing N N 258 
GLU   CB  HB3  sing N N 259 
GLU   CG  CD   sing N N 260 
GLU   CG  HG2  sing N N 261 
GLU   CG  HG3  sing N N 262 
GLU   CD  OE1  doub N N 263 
GLU   CD  OE2  sing N N 264 
GLU   OE2 HE2  sing N N 265 
GLU   OXT HXT  sing N N 266 
GLY   N   CA   sing N N 267 
GLY   N   H    sing N N 268 
GLY   N   H2   sing N N 269 
GLY   CA  C    sing N N 270 
GLY   CA  HA2  sing N N 271 
GLY   CA  HA3  sing N N 272 
GLY   C   O    doub N N 273 
GLY   C   OXT  sing N N 274 
GLY   OXT HXT  sing N N 275 
HIS   N   CA   sing N N 276 
HIS   N   H    sing N N 277 
HIS   N   H2   sing N N 278 
HIS   CA  C    sing N N 279 
HIS   CA  CB   sing N N 280 
HIS   CA  HA   sing N N 281 
HIS   C   O    doub N N 282 
HIS   C   OXT  sing N N 283 
HIS   CB  CG   sing N N 284 
HIS   CB  HB2  sing N N 285 
HIS   CB  HB3  sing N N 286 
HIS   CG  ND1  sing Y N 287 
HIS   CG  CD2  doub Y N 288 
HIS   ND1 CE1  doub Y N 289 
HIS   ND1 HD1  sing N N 290 
HIS   CD2 NE2  sing Y N 291 
HIS   CD2 HD2  sing N N 292 
HIS   CE1 NE2  sing Y N 293 
HIS   CE1 HE1  sing N N 294 
HIS   NE2 HE2  sing N N 295 
HIS   OXT HXT  sing N N 296 
HOH   O   H1   sing N N 297 
HOH   O   H2   sing N N 298 
ILE   N   CA   sing N N 299 
ILE   N   H    sing N N 300 
ILE   N   H2   sing N N 301 
ILE   CA  C    sing N N 302 
ILE   CA  CB   sing N N 303 
ILE   CA  HA   sing N N 304 
ILE   C   O    doub N N 305 
ILE   C   OXT  sing N N 306 
ILE   CB  CG1  sing N N 307 
ILE   CB  CG2  sing N N 308 
ILE   CB  HB   sing N N 309 
ILE   CG1 CD1  sing N N 310 
ILE   CG1 HG12 sing N N 311 
ILE   CG1 HG13 sing N N 312 
ILE   CG2 HG21 sing N N 313 
ILE   CG2 HG22 sing N N 314 
ILE   CG2 HG23 sing N N 315 
ILE   CD1 HD11 sing N N 316 
ILE   CD1 HD12 sing N N 317 
ILE   CD1 HD13 sing N N 318 
ILE   OXT HXT  sing N N 319 
LEU   N   CA   sing N N 320 
LEU   N   H    sing N N 321 
LEU   N   H2   sing N N 322 
LEU   CA  C    sing N N 323 
LEU   CA  CB   sing N N 324 
LEU   CA  HA   sing N N 325 
LEU   C   O    doub N N 326 
LEU   C   OXT  sing N N 327 
LEU   CB  CG   sing N N 328 
LEU   CB  HB2  sing N N 329 
LEU   CB  HB3  sing N N 330 
LEU   CG  CD1  sing N N 331 
LEU   CG  CD2  sing N N 332 
LEU   CG  HG   sing N N 333 
LEU   CD1 HD11 sing N N 334 
LEU   CD1 HD12 sing N N 335 
LEU   CD1 HD13 sing N N 336 
LEU   CD2 HD21 sing N N 337 
LEU   CD2 HD22 sing N N 338 
LEU   CD2 HD23 sing N N 339 
LEU   OXT HXT  sing N N 340 
LYS   N   CA   sing N N 341 
LYS   N   H    sing N N 342 
LYS   N   H2   sing N N 343 
LYS   CA  C    sing N N 344 
LYS   CA  CB   sing N N 345 
LYS   CA  HA   sing N N 346 
LYS   C   O    doub N N 347 
LYS   C   OXT  sing N N 348 
LYS   CB  CG   sing N N 349 
LYS   CB  HB2  sing N N 350 
LYS   CB  HB3  sing N N 351 
LYS   CG  CD   sing N N 352 
LYS   CG  HG2  sing N N 353 
LYS   CG  HG3  sing N N 354 
LYS   CD  CE   sing N N 355 
LYS   CD  HD2  sing N N 356 
LYS   CD  HD3  sing N N 357 
LYS   CE  NZ   sing N N 358 
LYS   CE  HE2  sing N N 359 
LYS   CE  HE3  sing N N 360 
LYS   NZ  HZ1  sing N N 361 
LYS   NZ  HZ2  sing N N 362 
LYS   NZ  HZ3  sing N N 363 
LYS   OXT HXT  sing N N 364 
MET   N   CA   sing N N 365 
MET   N   H    sing N N 366 
MET   N   H2   sing N N 367 
MET   CA  C    sing N N 368 
MET   CA  CB   sing N N 369 
MET   CA  HA   sing N N 370 
MET   C   O    doub N N 371 
MET   C   OXT  sing N N 372 
MET   CB  CG   sing N N 373 
MET   CB  HB2  sing N N 374 
MET   CB  HB3  sing N N 375 
MET   CG  SD   sing N N 376 
MET   CG  HG2  sing N N 377 
MET   CG  HG3  sing N N 378 
MET   SD  CE   sing N N 379 
MET   CE  HE1  sing N N 380 
MET   CE  HE2  sing N N 381 
MET   CE  HE3  sing N N 382 
MET   OXT HXT  sing N N 383 
PHE   N   CA   sing N N 384 
PHE   N   H    sing N N 385 
PHE   N   H2   sing N N 386 
PHE   CA  C    sing N N 387 
PHE   CA  CB   sing N N 388 
PHE   CA  HA   sing N N 389 
PHE   C   O    doub N N 390 
PHE   C   OXT  sing N N 391 
PHE   CB  CG   sing N N 392 
PHE   CB  HB2  sing N N 393 
PHE   CB  HB3  sing N N 394 
PHE   CG  CD1  doub Y N 395 
PHE   CG  CD2  sing Y N 396 
PHE   CD1 CE1  sing Y N 397 
PHE   CD1 HD1  sing N N 398 
PHE   CD2 CE2  doub Y N 399 
PHE   CD2 HD2  sing N N 400 
PHE   CE1 CZ   doub Y N 401 
PHE   CE1 HE1  sing N N 402 
PHE   CE2 CZ   sing Y N 403 
PHE   CE2 HE2  sing N N 404 
PHE   CZ  HZ   sing N N 405 
PHE   OXT HXT  sing N N 406 
PRO   N   CA   sing N N 407 
PRO   N   CD   sing N N 408 
PRO   N   H    sing N N 409 
PRO   CA  C    sing N N 410 
PRO   CA  CB   sing N N 411 
PRO   CA  HA   sing N N 412 
PRO   C   O    doub N N 413 
PRO   C   OXT  sing N N 414 
PRO   CB  CG   sing N N 415 
PRO   CB  HB2  sing N N 416 
PRO   CB  HB3  sing N N 417 
PRO   CG  CD   sing N N 418 
PRO   CG  HG2  sing N N 419 
PRO   CG  HG3  sing N N 420 
PRO   CD  HD2  sing N N 421 
PRO   CD  HD3  sing N N 422 
PRO   OXT HXT  sing N N 423 
SER   N   CA   sing N N 424 
SER   N   H    sing N N 425 
SER   N   H2   sing N N 426 
SER   CA  C    sing N N 427 
SER   CA  CB   sing N N 428 
SER   CA  HA   sing N N 429 
SER   C   O    doub N N 430 
SER   C   OXT  sing N N 431 
SER   CB  OG   sing N N 432 
SER   CB  HB2  sing N N 433 
SER   CB  HB3  sing N N 434 
SER   OG  HG   sing N N 435 
SER   OXT HXT  sing N N 436 
THR   N   CA   sing N N 437 
THR   N   H    sing N N 438 
THR   N   H2   sing N N 439 
THR   CA  C    sing N N 440 
THR   CA  CB   sing N N 441 
THR   CA  HA   sing N N 442 
THR   C   O    doub N N 443 
THR   C   OXT  sing N N 444 
THR   CB  OG1  sing N N 445 
THR   CB  CG2  sing N N 446 
THR   CB  HB   sing N N 447 
THR   OG1 HG1  sing N N 448 
THR   CG2 HG21 sing N N 449 
THR   CG2 HG22 sing N N 450 
THR   CG2 HG23 sing N N 451 
THR   OXT HXT  sing N N 452 
TRP   N   CA   sing N N 453 
TRP   N   H    sing N N 454 
TRP   N   H2   sing N N 455 
TRP   CA  C    sing N N 456 
TRP   CA  CB   sing N N 457 
TRP   CA  HA   sing N N 458 
TRP   C   O    doub N N 459 
TRP   C   OXT  sing N N 460 
TRP   CB  CG   sing N N 461 
TRP   CB  HB2  sing N N 462 
TRP   CB  HB3  sing N N 463 
TRP   CG  CD1  doub Y N 464 
TRP   CG  CD2  sing Y N 465 
TRP   CD1 NE1  sing Y N 466 
TRP   CD1 HD1  sing N N 467 
TRP   CD2 CE2  doub Y N 468 
TRP   CD2 CE3  sing Y N 469 
TRP   NE1 CE2  sing Y N 470 
TRP   NE1 HE1  sing N N 471 
TRP   CE2 CZ2  sing Y N 472 
TRP   CE3 CZ3  doub Y N 473 
TRP   CE3 HE3  sing N N 474 
TRP   CZ2 CH2  doub Y N 475 
TRP   CZ2 HZ2  sing N N 476 
TRP   CZ3 CH2  sing Y N 477 
TRP   CZ3 HZ3  sing N N 478 
TRP   CH2 HH2  sing N N 479 
TRP   OXT HXT  sing N N 480 
TYR   N   CA   sing N N 481 
TYR   N   H    sing N N 482 
TYR   N   H2   sing N N 483 
TYR   CA  C    sing N N 484 
TYR   CA  CB   sing N N 485 
TYR   CA  HA   sing N N 486 
TYR   C   O    doub N N 487 
TYR   C   OXT  sing N N 488 
TYR   CB  CG   sing N N 489 
TYR   CB  HB2  sing N N 490 
TYR   CB  HB3  sing N N 491 
TYR   CG  CD1  doub Y N 492 
TYR   CG  CD2  sing Y N 493 
TYR   CD1 CE1  sing Y N 494 
TYR   CD1 HD1  sing N N 495 
TYR   CD2 CE2  doub Y N 496 
TYR   CD2 HD2  sing N N 497 
TYR   CE1 CZ   doub Y N 498 
TYR   CE1 HE1  sing N N 499 
TYR   CE2 CZ   sing Y N 500 
TYR   CE2 HE2  sing N N 501 
TYR   CZ  OH   sing N N 502 
TYR   OH  HH   sing N N 503 
TYR   OXT HXT  sing N N 504 
VAL   N   CA   sing N N 505 
VAL   N   H    sing N N 506 
VAL   N   H2   sing N N 507 
VAL   CA  C    sing N N 508 
VAL   CA  CB   sing N N 509 
VAL   CA  HA   sing N N 510 
VAL   C   O    doub N N 511 
VAL   C   OXT  sing N N 512 
VAL   CB  CG1  sing N N 513 
VAL   CB  CG2  sing N N 514 
VAL   CB  HB   sing N N 515 
VAL   CG1 HG11 sing N N 516 
VAL   CG1 HG12 sing N N 517 
VAL   CG1 HG13 sing N N 518 
VAL   CG2 HG21 sing N N 519 
VAL   CG2 HG22 sing N N 520 
VAL   CG2 HG23 sing N N 521 
VAL   OXT HXT  sing N N 522 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Natural Science Foundation of China (NSFC)' China 31900880  1 
'National Natural Science Foundation of China (NSFC)' China 82273496  2 
'National Natural Science Foundation of China (NSFC)' China 819740748 3 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 GLC 1 n 
2 GLC 2 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   5LOF 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8Y20 
_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]   0.009990 
_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]   0.007284 
_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]   0.025867 
_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 
H 
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   . LYS   A 1 2   ? 10.706  33.672 1.038   1.00 69.12  ? -195 LYS   A N   1 
ATOM   2    C CA  . LYS   A 1 2   ? 10.124  34.683 0.184   1.00 69.97  ? -195 LYS   A CA  1 
ATOM   3    C C   . LYS   A 1 2   ? 10.346  36.084 0.756   1.00 70.37  ? -195 LYS   A C   1 
ATOM   4    O O   . LYS   A 1 2   ? 10.536  37.061 0.009   1.00 72.74  ? -195 LYS   A O   1 
ATOM   5    C CB  . LYS   A 1 2   ? 8.642   34.426 -0.006  1.00 70.93  ? -195 LYS   A CB  1 
ATOM   6    C CG  . LYS   A 1 2   ? 8.339   33.142 -0.782  1.00 75.90  ? -195 LYS   A CG  1 
ATOM   7    C CD  . LYS   A 1 2   ? 6.870   33.079 -1.221  1.00 77.12  ? -195 LYS   A CD  1 
ATOM   8    C CE  . LYS   A 1 2   ? 6.723   32.493 -2.618  1.00 80.46  ? -195 LYS   A CE  1 
ATOM   9    N NZ  . LYS   A 1 2   ? 7.297   33.381 -3.666  1.00 81.41  ? -195 LYS   A NZ  1 
ATOM   10   N N   . ILE   A 1 3   ? 10.333  36.189 2.084   1.00 66.36  ? -194 ILE   A N   1 
ATOM   11   C CA  . ILE   A 1 3   ? 10.495  37.480 2.748   1.00 61.23  ? -194 ILE   A CA  1 
ATOM   12   C C   . ILE   A 1 3   ? 11.971  37.834 2.780   1.00 61.21  ? -194 ILE   A C   1 
ATOM   13   O O   . ILE   A 1 3   ? 12.809  37.005 3.134   1.00 61.36  ? -194 ILE   A O   1 
ATOM   14   C CB  . ILE   A 1 3   ? 9.893   37.434 4.159   1.00 56.18  ? -194 ILE   A CB  1 
ATOM   15   C CG1 . ILE   A 1 3   ? 8.371   37.294 4.066   1.00 54.82  ? -194 ILE   A CG1 1 
ATOM   16   C CG2 . ILE   A 1 3   ? 10.284  38.688 4.973   1.00 52.42  ? -194 ILE   A CG2 1 
ATOM   17   C CD1 . ILE   A 1 3   ? 7.690   37.044 5.380   1.00 53.50  ? -194 ILE   A CD1 1 
ATOM   18   N N   . GLU   A 1 4   ? 12.305  39.052 2.427   1.00 62.65  ? -193 GLU   A N   1 
ATOM   19   C CA  . GLU   A 1 4   ? 13.673  39.492 2.399   1.00 66.40  ? -193 GLU   A CA  1 
ATOM   20   C C   . GLU   A 1 4   ? 14.259  39.774 3.745   1.00 63.76  ? -193 GLU   A C   1 
ATOM   21   O O   . GLU   A 1 4   ? 13.666  40.408 4.548   1.00 61.43  ? -193 GLU   A O   1 
ATOM   22   C CB  . GLU   A 1 4   ? 13.810  40.724 1.526   1.00 73.51  ? -193 GLU   A CB  1 
ATOM   23   N N   . GLU   A 1 5   ? 15.469  39.314 3.960   1.00 65.95  ? -192 GLU   A N   1 
ATOM   24   C CA  . GLU   A 1 5   ? 16.150  39.501 5.220   1.00 68.85  ? -192 GLU   A CA  1 
ATOM   25   C C   . GLU   A 1 5   ? 16.918  40.816 5.235   1.00 70.21  ? -192 GLU   A C   1 
ATOM   26   O O   . GLU   A 1 5   ? 17.309  41.345 4.187   1.00 71.25  ? -192 GLU   A O   1 
ATOM   27   C CB  . GLU   A 1 5   ? 17.106  38.336 5.484   1.00 72.24  ? -192 GLU   A CB  1 
ATOM   28   C CG  . GLU   A 1 5   ? 17.859  38.436 6.801   1.00 74.12  ? -192 GLU   A CG  1 
ATOM   29   C CD  . GLU   A 1 5   ? 18.892  37.342 6.934   1.00 78.05  ? -192 GLU   A CD  1 
ATOM   30   O OE1 . GLU   A 1 5   ? 19.975  37.606 7.496   1.00 79.64  ? -192 GLU   A OE1 1 
ATOM   31   O OE2 . GLU   A 1 5   ? 18.624  36.220 6.464   1.00 79.60  ? -192 GLU   A OE2 1 
ATOM   32   N N   . GLY   A 1 6   ? 17.129  41.344 6.432   1.00 70.34  ? -191 GLY   A N   1 
ATOM   33   C CA  . GLY   A 1 6   ? 17.844  42.595 6.588   1.00 70.25  ? -191 GLY   A CA  1 
ATOM   34   C C   . GLY   A 1 6   ? 16.990  43.839 6.516   1.00 67.90  ? -191 GLY   A C   1 
ATOM   35   O O   . GLY   A 1 6   ? 17.527  44.926 6.277   1.00 65.88  ? -191 GLY   A O   1 
ATOM   36   N N   . LYS   A 1 7   ? 15.680  43.712 6.703   1.00 65.59  ? -190 LYS   A N   1 
ATOM   37   C CA  . LYS   A 1 7   ? 14.780  44.855 6.722   1.00 62.72  ? -190 LYS   A CA  1 
ATOM   38   C C   . LYS   A 1 7   ? 13.497  44.414 7.422   1.00 57.28  ? -190 LYS   A C   1 
ATOM   39   O O   . LYS   A 1 7   ? 13.370  43.261 7.844   1.00 56.06  ? -190 LYS   A O   1 
ATOM   40   C CB  . LYS   A 1 7   ? 14.510  45.374 5.309   1.00 64.11  ? -190 LYS   A CB  1 
ATOM   41   C CG  . LYS   A 1 7   ? 13.792  44.405 4.407   1.00 65.79  ? -190 LYS   A CG  1 
ATOM   42   C CD  . LYS   A 1 7   ? 13.545  45.018 3.029   1.00 70.71  ? -190 LYS   A CD  1 
ATOM   43   C CE  . LYS   A 1 7   ? 12.818  44.054 2.098   1.00 74.35  ? -190 LYS   A CE  1 
ATOM   44   N NZ  . LYS   A 1 7   ? 12.576  44.654 0.747   1.00 77.26  ? -190 LYS   A NZ  1 
ATOM   45   N N   . LEU   A 1 8   ? 12.539  45.341 7.537   1.00 51.67  ? -189 LEU   A N   1 
ATOM   46   C CA  . LEU   A 1 8   ? 11.264  45.064 8.172   1.00 47.40  ? -189 LEU   A CA  1 
ATOM   47   C C   . LEU   A 1 8   ? 10.143  45.678 7.338   1.00 50.48  ? -189 LEU   A C   1 
ATOM   48   O O   . LEU   A 1 8   ? 10.167  46.892 7.037   1.00 54.53  ? -189 LEU   A O   1 
ATOM   49   C CB  . LEU   A 1 8   ? 11.231  45.623 9.594   1.00 43.58  ? -189 LEU   A CB  1 
ATOM   50   C CG  . LEU   A 1 8   ? 11.976  44.825 10.683  1.00 43.11  ? -189 LEU   A CG  1 
ATOM   51   C CD1 . LEU   A 1 8   ? 11.857  45.506 12.059  1.00 40.22  ? -189 LEU   A CD1 1 
ATOM   52   C CD2 . LEU   A 1 8   ? 11.439  43.412 10.755  1.00 40.84  ? -189 LEU   A CD2 1 
ATOM   53   N N   . VAL   A 1 9   ? 9.167   44.845 6.962   1.00 48.38  ? -188 VAL   A N   1 
ATOM   54   C CA  . VAL   A 1 9   ? 7.931   45.300 6.329   1.00 44.73  ? -188 VAL   A CA  1 
ATOM   55   C C   . VAL   A 1 9   ? 6.797   45.125 7.341   1.00 42.47  ? -188 VAL   A C   1 
ATOM   56   O O   . VAL   A 1 9   ? 6.651   44.044 7.930   1.00 40.90  ? -188 VAL   A O   1 
ATOM   57   C CB  . VAL   A 1 9   ? 7.660   44.514 5.035   1.00 44.34  ? -188 VAL   A CB  1 
ATOM   58   C CG1 . VAL   A 1 9   ? 6.386   45.012 4.321   1.00 40.44  ? -188 VAL   A CG1 1 
ATOM   59   C CG2 . VAL   A 1 9   ? 8.884   44.609 4.098   1.00 46.22  ? -188 VAL   A CG2 1 
ATOM   60   N N   . ILE   A 1 10  ? 5.995   46.179 7.534   1.00 40.55  ? -187 ILE   A N   1 
ATOM   61   C CA  . ILE   A 1 10  ? 4.916   46.182 8.502   1.00 41.60  ? -187 ILE   A CA  1 
ATOM   62   C C   . ILE   A 1 10  ? 3.620   46.511 7.776   1.00 41.85  ? -187 ILE   A C   1 
ATOM   63   O O   . ILE   A 1 10  ? 3.572   47.459 6.970   1.00 43.15  ? -187 ILE   A O   1 
ATOM   64   C CB  . ILE   A 1 10  ? 5.170   47.208 9.635   1.00 42.98  ? -187 ILE   A CB  1 
ATOM   65   C CG1 . ILE   A 1 10  ? 6.514   46.940 10.310  1.00 45.81  ? -187 ILE   A CG1 1 
ATOM   66   C CG2 . ILE   A 1 10  ? 4.061   47.170 10.665  1.00 40.33  ? -187 ILE   A CG2 1 
ATOM   67   C CD1 . ILE   A 1 10  ? 6.940   48.122 11.252  1.00 45.59  ? -187 ILE   A CD1 1 
ATOM   68   N N   . TRP   A 1 11  ? 2.560   45.766 8.098   1.00 40.27  ? -186 TRP   A N   1 
ATOM   69   C CA  . TRP   A 1 11  ? 1.211   46.042 7.615   1.00 38.22  ? -186 TRP   A CA  1 
ATOM   70   C C   . TRP   A 1 11  ? 0.388   46.575 8.763   1.00 36.93  ? -186 TRP   A C   1 
ATOM   71   O O   . TRP   A 1 11  ? 0.411   46.014 9.854   1.00 36.67  ? -186 TRP   A O   1 
ATOM   72   C CB  . TRP   A 1 11  ? 0.541   44.806 7.032   1.00 40.66  ? -186 TRP   A CB  1 
ATOM   73   C CG  . TRP   A 1 11  ? 1.028   44.427 5.684   1.00 43.56  ? -186 TRP   A CG  1 
ATOM   74   C CD1 . TRP   A 1 11  ? 2.055   45.002 4.985   1.00 44.60  ? -186 TRP   A CD1 1 
ATOM   75   C CD2 . TRP   A 1 11  ? 0.518   43.378 4.850   1.00 44.71  ? -186 TRP   A CD2 1 
ATOM   76   N NE1 . TRP   A 1 11  ? 2.205   44.388 3.768   1.00 45.79  ? -186 TRP   A NE1 1 
ATOM   77   C CE2 . TRP   A 1 11  ? 1.280   43.377 3.667   1.00 46.53  ? -186 TRP   A CE2 1 
ATOM   78   C CE3 . TRP   A 1 11  ? -0.497  42.422 5.000   1.00 43.75  ? -186 TRP   A CE3 1 
ATOM   79   C CZ2 . TRP   A 1 11  ? 1.057   42.446 2.623   1.00 46.72  ? -186 TRP   A CZ2 1 
ATOM   80   C CZ3 . TRP   A 1 11  ? -0.724  41.526 3.974   1.00 42.88  ? -186 TRP   A CZ3 1 
ATOM   81   C CH2 . TRP   A 1 11  ? 0.046   41.543 2.801   1.00 44.27  ? -186 TRP   A CH2 1 
ATOM   82   N N   . ILE   A 1 12  ? -0.318  47.685 8.527   1.00 38.21  ? -185 ILE   A N   1 
ATOM   83   C CA  . ILE   A 1 12  ? -1.258  48.230 9.496   1.00 36.14  ? -185 ILE   A CA  1 
ATOM   84   C C   . ILE   A 1 12  ? -2.403  48.839 8.703   1.00 37.50  ? -185 ILE   A C   1 
ATOM   85   O O   . ILE   A 1 12  ? -2.221  49.224 7.536   1.00 37.76  ? -185 ILE   A O   1 
ATOM   86   C CB  . ILE   A 1 12  ? -0.581  49.260 10.424  1.00 35.41  ? -185 ILE   A CB  1 
ATOM   87   C CG1 . ILE   A 1 12  ? -1.486  49.557 11.602  1.00 35.71  ? -185 ILE   A CG1 1 
ATOM   88   C CG2 . ILE   A 1 12  ? -0.275  50.536 9.672   1.00 36.19  ? -185 ILE   A CG2 1 
ATOM   89   C CD1 . ILE   A 1 12  ? -0.796  50.452 12.630  1.00 37.93  ? -185 ILE   A CD1 1 
ATOM   90   N N   . ASN   A 1 13  ? -3.584  48.880 9.322   1.00 39.56  ? -184 ASN   A N   1 
ATOM   91   C CA  . ASN   A 1 13  ? -4.805  49.310 8.653   1.00 39.68  ? -184 ASN   A CA  1 
ATOM   92   C C   . ASN   A 1 13  ? -4.792  50.809 8.365   1.00 39.38  ? -184 ASN   A C   1 
ATOM   93   O O   . ASN   A 1 13  ? -4.214  51.602 9.115   1.00 39.34  ? -184 ASN   A O   1 
ATOM   94   C CB  . ASN   A 1 13  ? -6.017  48.961 9.509   1.00 39.93  ? -184 ASN   A CB  1 
ATOM   95   C CG  . ASN   A 1 13  ? -7.284  48.829 8.672   1.00 42.05  ? -184 ASN   A CG  1 
ATOM   96   O OD1 . ASN   A 1 13  ? -7.296  48.180 7.616   1.00 42.28  ? -184 ASN   A OD1 1 
ATOM   97   N ND2 . ASN   A 1 13  ? -8.364  49.453 9.153   1.00 41.18  ? -184 ASN   A ND2 1 
ATOM   98   N N   . GLY   A 1 14  ? -5.485  51.200 7.301   1.00 38.48  ? -183 GLY   A N   1 
ATOM   99   C CA  . GLY   A 1 14  ? -5.442  52.566 6.789   1.00 40.15  ? -183 GLY   A CA  1 
ATOM   100  C C   . GLY   A 1 14  ? -6.091  53.604 7.676   1.00 43.04  ? -183 GLY   A C   1 
ATOM   101  O O   . GLY   A 1 14  ? -5.891  54.796 7.417   1.00 46.54  ? -183 GLY   A O   1 
ATOM   102  N N   . ASP   A 1 15  ? -6.849  53.207 8.689   1.00 41.67  ? -182 ASP   A N   1 
ATOM   103  C CA  . ASP   A 1 15  ? -7.432  54.167 9.609   1.00 39.65  ? -182 ASP   A CA  1 
ATOM   104  C C   . ASP   A 1 15  ? -6.555  54.408 10.812  1.00 37.04  ? -182 ASP   A C   1 
ATOM   105  O O   . ASP   A 1 15  ? -6.955  55.160 11.706  1.00 40.77  ? -182 ASP   A O   1 
ATOM   106  C CB  . ASP   A 1 15  ? -8.823  53.714 10.060  1.00 40.53  ? -182 ASP   A CB  1 
ATOM   107  C CG  . ASP   A 1 15  ? -8.826  52.272 10.606  1.00 44.97  ? -182 ASP   A CG  1 
ATOM   108  O OD1 . ASP   A 1 15  ? -7.744  51.632 10.683  1.00 46.63  ? -182 ASP   A OD1 1 
ATOM   109  O OD2 . ASP   A 1 15  ? -9.916  51.781 10.974  1.00 45.06  ? -182 ASP   A OD2 1 
ATOM   110  N N   . LYS   A 1 16  ? -5.371  53.817 10.856  1.00 35.02  ? -181 LYS   A N   1 
ATOM   111  C CA  . LYS   A 1 16  ? -4.468  53.980 11.990  1.00 37.50  ? -181 LYS   A CA  1 
ATOM   112  C C   . LYS   A 1 16  ? -3.339  54.929 11.609  1.00 38.79  ? -181 LYS   A C   1 
ATOM   113  O O   . LYS   A 1 16  ? -3.185  55.319 10.454  1.00 38.23  ? -181 LYS   A O   1 
ATOM   114  C CB  . LYS   A 1 16  ? -3.897  52.617 12.466  1.00 37.07  ? -181 LYS   A CB  1 
ATOM   115  C CG  . LYS   A 1 16  ? -4.949  51.573 12.900  1.00 35.93  ? -181 LYS   A CG  1 
ATOM   116  C CD  . LYS   A 1 16  ? -6.051  52.229 13.745  1.00 34.58  ? -181 LYS   A CD  1 
ATOM   117  C CE  . LYS   A 1 16  ? -6.802  51.199 14.592  1.00 34.34  ? -181 LYS   A CE  1 
ATOM   118  N NZ  . LYS   A 1 16  ? -7.649  50.242 13.787  1.00 32.62  ? -181 LYS   A NZ  1 
ATOM   119  N N   . GLY   A 1 17  ? -2.520  55.272 12.607  1.00 41.08  ? -180 GLY   A N   1 
ATOM   120  C CA  . GLY   A 1 17  ? -1.448  56.224 12.407  1.00 39.37  ? -180 GLY   A CA  1 
ATOM   121  C C   . GLY   A 1 17  ? -0.205  55.639 11.794  1.00 39.76  ? -180 GLY   A C   1 
ATOM   122  O O   . GLY   A 1 17  ? 0.839   55.583 12.455  1.00 40.83  ? -180 GLY   A O   1 
ATOM   123  N N   . TYR   A 1 18  ? -0.274  55.269 10.506  1.00 40.65  ? -179 TYR   A N   1 
ATOM   124  C CA  . TYR   A 1 18  ? 0.867   54.608 9.862   1.00 40.35  ? -179 TYR   A CA  1 
ATOM   125  C C   . TYR   A 1 18  ? 2.002   55.588 9.544   1.00 40.36  ? -179 TYR   A C   1 
ATOM   126  O O   . TYR   A 1 18  ? 3.181   55.184 9.456   1.00 37.77  ? -179 TYR   A O   1 
ATOM   127  C CB  . TYR   A 1 18  ? 0.410   53.905 8.596   1.00 42.22  ? -179 TYR   A CB  1 
ATOM   128  C CG  . TYR   A 1 18  ? -0.402  54.742 7.633   1.00 45.51  ? -179 TYR   A CG  1 
ATOM   129  C CD1 . TYR   A 1 18  ? 0.218   55.578 6.691   1.00 46.54  ? -179 TYR   A CD1 1 
ATOM   130  C CD2 . TYR   A 1 18  ? -1.802  54.672 7.635   1.00 46.76  ? -179 TYR   A CD2 1 
ATOM   131  C CE1 . TYR   A 1 18  ? -0.543  56.339 5.787   1.00 45.86  ? -179 TYR   A CE1 1 
ATOM   132  C CE2 . TYR   A 1 18  ? -2.561  55.459 6.749   1.00 46.33  ? -179 TYR   A CE2 1 
ATOM   133  C CZ  . TYR   A 1 18  ? -1.923  56.256 5.831   1.00 45.85  ? -179 TYR   A CZ  1 
ATOM   134  O OH  . TYR   A 1 18  ? -2.687  56.966 4.947   1.00 49.07  ? -179 TYR   A OH  1 
ATOM   135  N N   . ASN   A 1 19  ? 1.680   56.863 9.318   1.00 40.40  ? -178 ASN   A N   1 
ATOM   136  C CA  . ASN   A 1 19  ? 2.753   57.851 9.198   1.00 44.83  ? -178 ASN   A CA  1 
ATOM   137  C C   . ASN   A 1 19  ? 3.517   57.947 10.530  1.00 43.61  ? -178 ASN   A C   1 
ATOM   138  O O   . ASN   A 1 19  ? 4.745   57.922 10.564  1.00 43.82  ? -178 ASN   A O   1 
ATOM   139  C CB  . ASN   A 1 19  ? 2.194   59.228 8.782   1.00 46.36  ? -178 ASN   A CB  1 
ATOM   140  C CG  . ASN   A 1 19  ? 1.664   59.221 7.366   1.00 46.67  ? -178 ASN   A CG  1 
ATOM   141  O OD1 . ASN   A 1 19  ? 2.301   58.668 6.468   1.00 48.73  ? -178 ASN   A OD1 1 
ATOM   142  N ND2 . ASN   A 1 19  ? 0.495   59.832 7.149   1.00 45.01  ? -178 ASN   A ND2 1 
ATOM   143  N N   . GLY   A 1 20  ? 2.782   58.033 11.647  1.00 41.20  ? -177 GLY   A N   1 
ATOM   144  C CA  . GLY   A 1 20  ? 3.409   57.967 12.952  1.00 37.67  ? -177 GLY   A CA  1 
ATOM   145  C C   . GLY   A 1 20  ? 4.225   56.703 13.115  1.00 40.23  ? -177 GLY   A C   1 
ATOM   146  O O   . GLY   A 1 20  ? 5.367   56.733 13.575  1.00 41.31  ? -177 GLY   A O   1 
ATOM   147  N N   . LEU   A 1 21  ? 3.637   55.541 12.732  1.00 40.05  ? -176 LEU   A N   1 
ATOM   148  C CA  . LEU   A 1 21  ? 4.403   54.302 12.808  1.00 38.69  ? -176 LEU   A CA  1 
ATOM   149  C C   . LEU   A 1 21  ? 5.666   54.362 11.964  1.00 39.02  ? -176 LEU   A C   1 
ATOM   150  O O   . LEU   A 1 21  ? 6.732   53.892 12.390  1.00 39.58  ? -176 LEU   A O   1 
ATOM   151  C CB  . LEU   A 1 21  ? 3.543   53.118 12.371  1.00 39.72  ? -176 LEU   A CB  1 
ATOM   152  C CG  . LEU   A 1 21  ? 4.195   51.796 12.657  1.00 36.45  ? -176 LEU   A CG  1 
ATOM   153  C CD1 . LEU   A 1 21  ? 4.537   51.723 14.157  1.00 33.81  ? -176 LEU   A CD1 1 
ATOM   154  C CD2 . LEU   A 1 21  ? 3.253   50.632 12.236  1.00 35.87  ? -176 LEU   A CD2 1 
ATOM   155  N N   . ALA   A 1 22  ? 5.584   54.947 10.760  1.00 39.40  ? -175 ALA   A N   1 
ATOM   156  C CA  . ALA   A 1 22  ? 6.792   55.033 9.940   1.00 42.71  ? -175 ALA   A CA  1 
ATOM   157  C C   . ALA   A 1 22  ? 7.865   55.888 10.611  1.00 47.91  ? -175 ALA   A C   1 
ATOM   158  O O   . ALA   A 1 22  ? 9.063   55.608 10.438  1.00 50.19  ? -175 ALA   A O   1 
ATOM   159  C CB  . ALA   A 1 22  ? 6.448   55.590 8.567   1.00 42.24  ? -175 ALA   A CB  1 
ATOM   160  N N   . GLU   A 1 23  ? 7.461   56.929 11.362  1.00 45.77  ? -174 GLU   A N   1 
ATOM   161  C CA  . GLU   A 1 23  ? 8.434   57.760 12.068  1.00 46.38  ? -174 GLU   A CA  1 
ATOM   162  C C   . GLU   A 1 23  ? 9.236   56.930 13.076  1.00 45.83  ? -174 GLU   A C   1 
ATOM   163  O O   . GLU   A 1 23  ? 10.469  57.062 13.182  1.00 47.23  ? -174 GLU   A O   1 
ATOM   164  C CB  . GLU   A 1 23  ? 7.713   58.899 12.774  1.00 48.33  ? -174 GLU   A CB  1 
ATOM   165  C CG  . GLU   A 1 23  ? 7.247   60.012 11.839  1.00 54.63  ? -174 GLU   A CG  1 
ATOM   166  C CD  . GLU   A 1 23  ? 6.589   61.191 12.601  1.00 55.80  ? -174 GLU   A CD  1 
ATOM   167  O OE1 . GLU   A 1 23  ? 6.775   61.284 13.850  1.00 53.72  ? -174 GLU   A OE1 1 
ATOM   168  O OE2 . GLU   A 1 23  ? 5.878   61.986 11.931  1.00 55.65  ? -174 GLU   A OE2 1 
ATOM   169  N N   . VAL   A 1 24  ? 8.548   56.076 13.848  1.00 41.82  ? -173 VAL   A N   1 
ATOM   170  C CA  . VAL   A 1 24  ? 9.263   55.192 14.739  1.00 40.56  ? -173 VAL   A CA  1 
ATOM   171  C C   . VAL   A 1 24  ? 10.193  54.320 13.926  1.00 42.83  ? -173 VAL   A C   1 
ATOM   172  O O   . VAL   A 1 24  ? 11.331  54.048 14.334  1.00 43.86  ? -173 VAL   A O   1 
ATOM   173  C CB  . VAL   A 1 24  ? 8.273   54.368 15.566  1.00 39.17  ? -173 VAL   A CB  1 
ATOM   174  C CG1 . VAL   A 1 24  ? 9.016   53.456 16.577  1.00 40.78  ? -173 VAL   A CG1 1 
ATOM   175  C CG2 . VAL   A 1 24  ? 7.275   55.274 16.295  1.00 36.34  ? -173 VAL   A CG2 1 
ATOM   176  N N   . GLY   A 1 25  ? 9.746   53.914 12.730  1.00 43.79  ? -172 GLY   A N   1 
ATOM   177  C CA  . GLY   A 1 25  ? 10.612  53.114 11.871  1.00 46.10  ? -172 GLY   A CA  1 
ATOM   178  C C   . GLY   A 1 25  ? 11.903  53.831 11.510  1.00 47.86  ? -172 GLY   A C   1 
ATOM   179  O O   . GLY   A 1 25  ? 12.991  53.228 11.523  1.00 48.84  ? -172 GLY   A O   1 
ATOM   180  N N   . LYS   A 1 26  ? 11.830  55.111 11.210  1.00 48.38  ? -171 LYS   A N   1 
ATOM   181  C CA  . LYS   A 1 26  ? 13.031  55.805 10.790  1.00 52.23  ? -171 LYS   A CA  1 
ATOM   182  C C   . LYS   A 1 26  ? 14.012  55.932 11.956  1.00 50.27  ? -171 LYS   A C   1 
ATOM   183  O O   . LYS   A 1 26  ? 15.227  55.827 11.761  1.00 51.67  ? -171 LYS   A O   1 
ATOM   184  C CB  . LYS   A 1 26  ? 12.699  57.143 10.143  1.00 57.69  ? -171 LYS   A CB  1 
ATOM   185  C CG  . LYS   A 1 26  ? 12.168  56.999 8.696   1.00 63.17  ? -171 LYS   A CG  1 
ATOM   186  C CD  . LYS   A 1 26  ? 13.195  57.447 7.642   1.00 68.35  ? -171 LYS   A CD  1 
ATOM   187  C CE  . LYS   A 1 26  ? 13.152  56.530 6.387   1.00 69.04  ? -171 LYS   A CE  1 
ATOM   188  N NZ  . LYS   A 1 26  ? 14.451  56.569 5.598   1.00 70.00  ? -171 LYS   A NZ  1 
ATOM   189  N N   . LYS   A 1 27  ? 13.490  56.115 13.169  1.00 47.58  ? -170 LYS   A N   1 
ATOM   190  C CA  . LYS   A 1 27  ? 14.392  56.143 14.322  1.00 48.10  ? -170 LYS   A CA  1 
ATOM   191  C C   . LYS   A 1 27  ? 15.074  54.792 14.514  1.00 47.65  ? -170 LYS   A C   1 
ATOM   192  O O   . LYS   A 1 27  ? 16.270  54.722 14.841  1.00 48.25  ? -170 LYS   A O   1 
ATOM   193  C CB  . LYS   A 1 27  ? 13.652  56.554 15.588  1.00 50.38  ? -170 LYS   A CB  1 
ATOM   194  C CG  . LYS   A 1 27  ? 14.565  56.679 16.806  1.00 56.47  ? -170 LYS   A CG  1 
ATOM   195  C CD  . LYS   A 1 27  ? 14.167  57.873 17.682  1.00 62.65  ? -170 LYS   A CD  1 
ATOM   196  C CE  . LYS   A 1 27  ? 14.079  57.458 19.159  1.00 65.19  ? -170 LYS   A CE  1 
ATOM   197  N NZ  . LYS   A 1 27  ? 13.587  58.593 20.046  1.00 66.85  ? -170 LYS   A NZ  1 
ATOM   198  N N   . PHE   A 1 28  ? 14.317  53.705 14.317  1.00 45.13  ? -169 PHE   A N   1 
ATOM   199  C CA  . PHE   A 1 28  ? 14.943  52.384 14.295  1.00 42.54  ? -169 PHE   A CA  1 
ATOM   200  C C   . PHE   A 1 28  ? 16.040  52.309 13.236  1.00 45.42  ? -169 PHE   A C   1 
ATOM   201  O O   . PHE   A 1 28  ? 17.120  51.787 13.490  1.00 47.67  ? -169 PHE   A O   1 
ATOM   202  C CB  . PHE   A 1 28  ? 13.880  51.324 14.031  1.00 40.92  ? -169 PHE   A CB  1 
ATOM   203  C CG  . PHE   A 1 28  ? 14.400  49.925 14.097  1.00 42.95  ? -169 PHE   A CG  1 
ATOM   204  C CD1 . PHE   A 1 28  ? 14.486  49.243 15.321  1.00 41.53  ? -169 PHE   A CD1 1 
ATOM   205  C CD2 . PHE   A 1 28  ? 14.755  49.246 12.924  1.00 46.83  ? -169 PHE   A CD2 1 
ATOM   206  C CE1 . PHE   A 1 28  ? 14.917  47.907 15.348  1.00 42.34  ? -169 PHE   A CE1 1 
ATOM   207  C CE2 . PHE   A 1 28  ? 15.184  47.898 12.959  1.00 45.37  ? -169 PHE   A CE2 1 
ATOM   208  C CZ  . PHE   A 1 28  ? 15.270  47.250 14.177  1.00 42.68  ? -169 PHE   A CZ  1 
ATOM   209  N N   . GLU   A 1 29  ? 15.784  52.851 12.041  1.00 48.98  ? -168 GLU   A N   1 
ATOM   210  C CA  . GLU   A 1 29  ? 16.776  52.858 10.970  1.00 50.32  ? -168 GLU   A CA  1 
ATOM   211  C C   . GLU   A 1 29  ? 18.016  53.647 11.371  1.00 53.37  ? -168 GLU   A C   1 
ATOM   212  O O   . GLU   A 1 29  ? 19.157  53.177 11.194  1.00 53.90  ? -168 GLU   A O   1 
ATOM   213  C CB  . GLU   A 1 29  ? 16.170  53.432 9.692   1.00 50.08  ? -168 GLU   A CB  1 
ATOM   214  C CG  . GLU   A 1 29  ? 16.980  53.211 8.451   1.00 52.82  ? -168 GLU   A CG  1 
ATOM   215  C CD  . GLU   A 1 29  ? 16.517  54.085 7.287   1.00 56.89  ? -168 GLU   A CD  1 
ATOM   216  O OE1 . GLU   A 1 29  ? 17.348  54.399 6.396   1.00 60.16  ? -168 GLU   A OE1 1 
ATOM   217  O OE2 . GLU   A 1 29  ? 15.334  54.473 7.256   1.00 57.07  ? -168 GLU   A OE2 1 
ATOM   218  N N   . LYS   A 1 30  ? 17.826  54.850 11.936  1.00 54.34  ? -167 LYS   A N   1 
ATOM   219  C CA  . LYS   A 1 30  ? 18.966  55.686 12.320  1.00 58.09  ? -167 LYS   A CA  1 
ATOM   220  C C   . LYS   A 1 30  ? 19.906  54.967 13.299  1.00 60.79  ? -167 LYS   A C   1 
ATOM   221  O O   . LYS   A 1 30  ? 21.110  55.254 13.325  1.00 61.62  ? -167 LYS   A O   1 
ATOM   222  C CB  . LYS   A 1 30  ? 18.471  57.007 12.893  1.00 59.29  ? -167 LYS   A CB  1 
ATOM   223  C CG  . LYS   A 1 30  ? 19.572  57.898 13.442  1.00 62.56  ? -167 LYS   A CG  1 
ATOM   224  C CD  . LYS   A 1 30  ? 18.970  59.058 14.260  1.00 63.79  ? -167 LYS   A CD  1 
ATOM   225  C CE  . LYS   A 1 30  ? 19.849  60.309 14.177  1.00 67.07  ? -167 LYS   A CE  1 
ATOM   226  N NZ  . LYS   A 1 30  ? 20.319  60.553 12.772  1.00 68.12  ? -167 LYS   A NZ  1 
ATOM   227  N N   . ASP   A 1 31  ? 19.375  54.028 14.086  1.00 62.32  ? -166 ASP   A N   1 
ATOM   228  C CA  . ASP   A 1 31  ? 20.216  53.286 15.027  1.00 64.04  ? -166 ASP   A CA  1 
ATOM   229  C C   . ASP   A 1 31  ? 20.899  52.071 14.412  1.00 64.28  ? -166 ASP   A C   1 
ATOM   230  O O   . ASP   A 1 31  ? 22.080  51.811 14.708  1.00 65.08  ? -166 ASP   A O   1 
ATOM   231  C CB  . ASP   A 1 31  ? 19.378  52.821 16.221  1.00 62.29  ? -166 ASP   A CB  1 
ATOM   232  C CG  . ASP   A 1 31  ? 19.313  53.860 17.335  1.00 60.47  ? -166 ASP   A CG  1 
ATOM   233  O OD1 . ASP   A 1 31  ? 20.129  54.814 17.305  1.00 63.28  ? -166 ASP   A OD1 1 
ATOM   234  O OD2 . ASP   A 1 31  ? 18.463  53.704 18.237  1.00 56.71  ? -166 ASP   A OD2 1 
ATOM   235  N N   . THR   A 1 32  ? 20.183  51.318 13.559  1.00 63.36  ? -165 THR   A N   1 
ATOM   236  C CA  . THR   A 1 32  ? 20.605  49.979 13.143  1.00 60.87  ? -165 THR   A CA  1 
ATOM   237  C C   . THR   A 1 32  ? 21.028  49.880 11.691  1.00 62.03  ? -165 THR   A C   1 
ATOM   238  O O   . THR   A 1 32  ? 21.680  48.891 11.329  1.00 62.62  ? -165 THR   A O   1 
ATOM   239  C CB  . THR   A 1 32  ? 19.460  48.974 13.357  1.00 56.65  ? -165 THR   A CB  1 
ATOM   240  O OG1 . THR   A 1 32  ? 18.372  49.308 12.470  1.00 53.25  ? -165 THR   A OG1 1 
ATOM   241  C CG2 . THR   A 1 32  ? 18.981  49.012 14.807  1.00 54.70  ? -165 THR   A CG2 1 
ATOM   242  N N   . GLY   A 1 33  ? 20.640  50.843 10.844  1.00 61.48  ? -164 GLY   A N   1 
ATOM   243  C CA  . GLY   A 1 33  ? 20.811  50.688 9.414   1.00 61.52  ? -164 GLY   A CA  1 
ATOM   244  C C   . GLY   A 1 33  ? 19.765  49.822 8.726   1.00 59.96  ? -164 GLY   A C   1 
ATOM   245  O O   . GLY   A 1 33  ? 19.874  49.590 7.514   1.00 62.03  ? -164 GLY   A O   1 
ATOM   246  N N   . ILE   A 1 34  ? 18.747  49.356 9.444   1.00 56.08  ? -163 ILE   A N   1 
ATOM   247  C CA  . ILE   A 1 34  ? 17.696  48.542 8.850   1.00 53.71  ? -163 ILE   A CA  1 
ATOM   248  C C   . ILE   A 1 34  ? 16.551  49.449 8.404   1.00 53.24  ? -163 ILE   A C   1 
ATOM   249  O O   . ILE   A 1 34  ? 16.061  50.268 9.181   1.00 50.45  ? -163 ILE   A O   1 
ATOM   250  C CB  . ILE   A 1 34  ? 17.195  47.478 9.844   1.00 49.83  ? -163 ILE   A CB  1 
ATOM   251  C CG1 . ILE   A 1 34  ? 18.357  46.684 10.447  1.00 47.28  ? -163 ILE   A CG1 1 
ATOM   252  C CG2 . ILE   A 1 34  ? 16.176  46.572 9.179   1.00 48.13  ? -163 ILE   A CG2 1 
ATOM   253  C CD1 . ILE   A 1 34  ? 19.252  46.083 9.438   1.00 46.34  ? -163 ILE   A CD1 1 
ATOM   254  N N   . LYS   A 1 35  ? 16.110  49.276 7.156   1.00 58.21  ? -162 LYS   A N   1 
ATOM   255  C CA  . LYS   A 1 35  ? 14.995  50.029 6.599   1.00 59.37  ? -162 LYS   A CA  1 
ATOM   256  C C   . LYS   A 1 35  ? 13.677  49.462 7.107   1.00 58.24  ? -162 LYS   A C   1 
ATOM   257  O O   . LYS   A 1 35  ? 13.505  48.239 7.230   1.00 60.05  ? -162 LYS   A O   1 
ATOM   258  C CB  . LYS   A 1 35  ? 15.034  49.988 5.071   1.00 64.35  ? -162 LYS   A CB  1 
ATOM   259  C CG  . LYS   A 1 35  ? 14.774  51.321 4.405   1.00 70.34  ? -162 LYS   A CG  1 
ATOM   260  C CD  . LYS   A 1 35  ? 16.034  52.178 4.350   1.00 76.12  ? -162 LYS   A CD  1 
ATOM   261  C CE  . LYS   A 1 35  ? 15.919  53.277 3.306   1.00 79.67  ? -162 LYS   A CE  1 
ATOM   262  N NZ  . LYS   A 1 35  ? 16.573  54.581 3.737   1.00 80.79  ? -162 LYS   A NZ  1 
ATOM   263  N N   . VAL   A 1 36  ? 12.730  50.351 7.370   1.00 54.34  ? -161 VAL   A N   1 
ATOM   264  C CA  . VAL   A 1 36  ? 11.416  49.978 7.873   1.00 52.32  ? -161 VAL   A CA  1 
ATOM   265  C C   . VAL   A 1 36  ? 10.377  50.534 6.926   1.00 51.88  ? -161 VAL   A C   1 
ATOM   266  O O   . VAL   A 1 36  ? 10.171  51.746 6.876   1.00 54.56  ? -161 VAL   A O   1 
ATOM   267  C CB  . VAL   A 1 36  ? 11.164  50.489 9.305   1.00 49.20  ? -161 VAL   A CB  1 
ATOM   268  C CG1 . VAL   A 1 36  ? 9.792   50.022 9.796   1.00 44.10  ? -161 VAL   A CG1 1 
ATOM   269  C CG2 . VAL   A 1 36  ? 12.270  49.979 10.237  1.00 49.73  ? -161 VAL   A CG2 1 
ATOM   270  N N   . THR   A 1 37  ? 9.696   49.648 6.202   1.00 50.83  ? -160 THR   A N   1 
ATOM   271  C CA  . THR   A 1 37  ? 8.629   50.022 5.273   1.00 47.76  ? -160 THR   A CA  1 
ATOM   272  C C   . THR   A 1 37  ? 7.293   49.733 5.934   1.00 46.47  ? -160 THR   A C   1 
ATOM   273  O O   . THR   A 1 37  ? 7.081   48.626 6.439   1.00 47.44  ? -160 THR   A O   1 
ATOM   274  C CB  . THR   A 1 37  ? 8.754   49.262 3.942   1.00 44.57  ? -160 THR   A CB  1 
ATOM   275  O OG1 . THR   A 1 37  ? 10.034  49.514 3.364   1.00 45.58  ? -160 THR   A OG1 1 
ATOM   276  C CG2 . THR   A 1 37  ? 7.669   49.700 2.962   1.00 40.52  ? -160 THR   A CG2 1 
ATOM   277  N N   . VAL   A 1 38  ? 6.409   50.739 5.964   1.00 45.80  ? -159 VAL   A N   1 
ATOM   278  C CA  . VAL   A 1 38  ? 5.078   50.609 6.525   1.00 43.75  ? -159 VAL   A CA  1 
ATOM   279  C C   . VAL   A 1 38  ? 4.103   50.676 5.369   1.00 45.05  ? -159 VAL   A C   1 
ATOM   280  O O   . VAL   A 1 38  ? 4.193   51.580 4.543   1.00 45.11  ? -159 VAL   A O   1 
ATOM   281  C CB  . VAL   A 1 38  ? 4.781   51.707 7.561   1.00 44.31  ? -159 VAL   A CB  1 
ATOM   282  C CG1 . VAL   A 1 38  ? 3.351   51.596 8.094   1.00 40.51  ? -159 VAL   A CG1 1 
ATOM   283  C CG2 . VAL   A 1 38  ? 5.778   51.648 8.709   1.00 44.48  ? -159 VAL   A CG2 1 
ATOM   284  N N   . GLU   A 1 39  ? 3.192   49.694 5.294   1.00 45.92  ? -158 GLU   A N   1 
ATOM   285  C CA  . GLU   A 1 39  ? 2.156   49.658 4.271   1.00 47.58  ? -158 GLU   A CA  1 
ATOM   286  C C   . GLU   A 1 39  ? 0.786   49.482 4.933   1.00 43.11  ? -158 GLU   A C   1 
ATOM   287  O O   . GLU   A 1 39  ? 0.670   48.909 6.022   1.00 41.70  ? -158 GLU   A O   1 
ATOM   288  C CB  . GLU   A 1 39  ? 2.418   48.534 3.256   1.00 50.84  ? -158 GLU   A CB  1 
ATOM   289  C CG  . GLU   A 1 39  ? 3.783   48.604 2.623   1.00 55.31  ? -158 GLU   A CG  1 
ATOM   290  C CD  . GLU   A 1 39  ? 4.086   47.426 1.708   1.00 58.29  ? -158 GLU   A CD  1 
ATOM   291  O OE1 . GLU   A 1 39  ? 3.428   46.362 1.830   1.00 59.94  ? -158 GLU   A OE1 1 
ATOM   292  O OE2 . GLU   A 1 39  ? 4.993   47.543 0.872   1.00 60.35  ? -158 GLU   A OE2 1 
ATOM   293  N N   . HIS   A 1 40  ? -0.251  49.973 4.263   1.00 41.81  ? -157 HIS   A N   1 
ATOM   294  C CA  . HIS   A 1 40  ? -1.635  49.875 4.743   1.00 40.73  ? -157 HIS   A CA  1 
ATOM   295  C C   . HIS   A 1 40  ? -2.528  49.380 3.613   1.00 40.27  ? -157 HIS   A C   1 
ATOM   296  O O   . HIS   A 1 40  ? -3.440  50.091 3.170   1.00 38.60  ? -157 HIS   A O   1 
ATOM   297  C CB  . HIS   A 1 40  ? -2.141  51.227 5.280   1.00 39.00  ? -157 HIS   A CB  1 
ATOM   298  C CG  . HIS   A 1 40  ? -1.846  52.388 4.373   1.00 41.12  ? -157 HIS   A CG  1 
ATOM   299  N ND1 . HIS   A 1 40  ? -2.813  52.959 3.558   1.00 41.98  ? -157 HIS   A ND1 1 
ATOM   300  C CD2 . HIS   A 1 40  ? -0.708  53.091 4.152   1.00 42.06  ? -157 HIS   A CD2 1 
ATOM   301  C CE1 . HIS   A 1 40  ? -2.283  53.951 2.872   1.00 42.98  ? -157 HIS   A CE1 1 
ATOM   302  N NE2 . HIS   A 1 40  ? -1.001  54.047 3.204   1.00 43.66  ? -157 HIS   A NE2 1 
ATOM   303  N N   . PRO   A 1 41  ? -2.336  48.134 3.172   1.00 43.67  ? -156 PRO   A N   1 
ATOM   304  C CA  . PRO   A 1 41  ? -3.091  47.643 2.006   1.00 46.09  ? -156 PRO   A CA  1 
ATOM   305  C C   . PRO   A 1 41  ? -4.550  47.409 2.340   1.00 43.81  ? -156 PRO   A C   1 
ATOM   306  O O   . PRO   A 1 41  ? -4.929  47.225 3.486   1.00 40.06  ? -156 PRO   A O   1 
ATOM   307  C CB  . PRO   A 1 41  ? -2.384  46.322 1.646   1.00 46.22  ? -156 PRO   A CB  1 
ATOM   308  C CG  . PRO   A 1 41  ? -1.838  45.858 2.921   1.00 44.49  ? -156 PRO   A CG  1 
ATOM   309  C CD  . PRO   A 1 41  ? -1.442  47.094 3.724   1.00 41.90  ? -156 PRO   A CD  1 
ATOM   310  N N   . ASP   A 1 42  ? -5.368  47.422 1.289   1.00 50.26  ? -155 ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 42  ? -6.788  47.121 1.417   1.00 54.91  ? -155 ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 42  ? -6.990  45.688 1.898   1.00 53.59  ? -155 ASP   A C   1 
ATOM   313  O O   . ASP   A 1 42  ? -6.310  44.768 1.447   1.00 51.32  ? -155 ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 42  ? -7.490  47.308 0.059   1.00 61.66  ? -155 ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 42  ? -7.877  48.768 -0.206  1.00 65.28  ? -155 ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 42  ? -8.218  49.493 0.760   1.00 65.00  ? -155 ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 42  ? -7.843  49.186 -1.396  1.00 67.00  ? -155 ASP   A OD2 1 
ATOM   318  N N   . LYS   A 1 43  ? -7.928  45.518 2.829   1.00 53.78  ? -154 LYS   A N   1 
ATOM   319  C CA  . LYS   A 1 43  ? -8.355  44.211 3.291   1.00 53.78  ? -154 LYS   A CA  1 
ATOM   320  C C   . LYS   A 1 43  ? -7.166  43.375 3.786   1.00 49.82  ? -154 LYS   A C   1 
ATOM   321  O O   . LYS   A 1 43  ? -7.078  42.152 3.533   1.00 49.83  ? -154 LYS   A O   1 
ATOM   322  C CB  . LYS   A 1 43  ? -9.108  43.483 2.174   1.00 61.46  ? -154 LYS   A CB  1 
ATOM   323  C CG  . LYS   A 1 43  ? -10.527 43.984 1.933   1.00 65.26  ? -154 LYS   A CG  1 
ATOM   324  C CD  . LYS   A 1 43  ? -11.421 42.834 1.467   1.00 68.84  ? -154 LYS   A CD  1 
ATOM   325  C CE  . LYS   A 1 43  ? -11.555 42.783 -0.055  1.00 70.94  ? -154 LYS   A CE  1 
ATOM   326  N NZ  . LYS   A 1 43  ? -12.378 43.911 -0.575  1.00 71.39  ? -154 LYS   A NZ  1 
ATOM   327  N N   . LEU   A 1 44  ? -6.249  44.019 4.504   1.00 44.05  ? -153 LEU   A N   1 
ATOM   328  C CA  . LEU   A 1 44  ? -5.012  43.351 4.902   1.00 42.97  ? -153 LEU   A CA  1 
ATOM   329  C C   . LEU   A 1 44  ? -5.255  42.166 5.854   1.00 44.61  ? -153 LEU   A C   1 
ATOM   330  O O   . LEU   A 1 44  ? -4.405  41.292 5.961   1.00 43.07  ? -153 LEU   A O   1 
ATOM   331  C CB  . LEU   A 1 44  ? -4.046  44.349 5.541   1.00 37.48  ? -153 LEU   A CB  1 
ATOM   332  C CG  . LEU   A 1 44  ? -4.335  44.697 6.980   1.00 33.93  ? -153 LEU   A CG  1 
ATOM   333  C CD1 . LEU   A 1 44  ? -3.621  43.761 7.905   1.00 30.34  ? -153 LEU   A CD1 1 
ATOM   334  C CD2 . LEU   A 1 44  ? -3.873  46.160 7.245   1.00 36.60  ? -153 LEU   A CD2 1 
ATOM   335  N N   . GLU   A 1 45  ? -6.384  42.136 6.562   1.00 44.72  ? -152 GLU   A N   1 
ATOM   336  C CA  . GLU   A 1 45  ? -6.688  41.046 7.467   1.00 43.22  ? -152 GLU   A CA  1 
ATOM   337  C C   . GLU   A 1 45  ? -7.101  39.779 6.717   1.00 44.92  ? -152 GLU   A C   1 
ATOM   338  O O   . GLU   A 1 45  ? -6.978  38.681 7.269   1.00 42.36  ? -152 GLU   A O   1 
ATOM   339  C CB  . GLU   A 1 45  ? -7.770  41.456 8.469   1.00 40.91  ? -152 GLU   A CB  1 
ATOM   340  C CG  . GLU   A 1 45  ? -9.194  41.373 7.929   1.00 45.56  ? -152 GLU   A CG  1 
ATOM   341  C CD  . GLU   A 1 45  ? -9.602  42.615 7.150   1.00 47.19  ? -152 GLU   A CD  1 
ATOM   342  O OE1 . GLU   A 1 45  ? -8.722  43.295 6.566   1.00 43.10  ? -152 GLU   A OE1 1 
ATOM   343  O OE2 . GLU   A 1 45  ? -10.823 42.894 7.111   1.00 52.15  ? -152 GLU   A OE2 1 
ATOM   344  N N   . GLU   A 1 46  ? -7.559  39.913 5.478   1.00 46.14  ? -151 GLU   A N   1 
ATOM   345  C CA  . GLU   A 1 46  ? -7.786  38.756 4.630   1.00 47.98  ? -151 GLU   A CA  1 
ATOM   346  C C   . GLU   A 1 46  ? -6.577  38.429 3.776   1.00 47.94  ? -151 GLU   A C   1 
ATOM   347  O O   . GLU   A 1 46  ? -6.371  37.253 3.435   1.00 52.11  ? -151 GLU   A O   1 
ATOM   348  C CB  . GLU   A 1 46  ? -8.993  38.970 3.720   1.00 51.51  ? -151 GLU   A CB  1 
ATOM   349  C CG  . GLU   A 1 46  ? -10.211 39.475 4.464   1.00 56.93  ? -151 GLU   A CG  1 
ATOM   350  C CD  . GLU   A 1 46  ? -11.425 39.577 3.572   1.00 63.66  ? -151 GLU   A CD  1 
ATOM   351  O OE1 . GLU   A 1 46  ? -11.252 39.639 2.330   1.00 65.28  ? -151 GLU   A OE1 1 
ATOM   352  O OE2 . GLU   A 1 46  ? -12.558 39.607 4.124   1.00 67.48  ? -151 GLU   A OE2 1 
ATOM   353  N N   . LYS   A 1 47  ? -5.763  39.420 3.428   1.00 42.85  ? -150 LYS   A N   1 
ATOM   354  C CA  . LYS   A 1 47  ? -4.608  39.112 2.608   1.00 46.21  ? -150 LYS   A CA  1 
ATOM   355  C C   . LYS   A 1 47  ? -3.510  38.442 3.418   1.00 45.25  ? -150 LYS   A C   1 
ATOM   356  O O   . LYS   A 1 47  ? -2.852  37.508 2.933   1.00 45.67  ? -150 LYS   A O   1 
ATOM   357  C CB  . LYS   A 1 47  ? -4.087  40.383 1.921   1.00 51.68  ? -150 LYS   A CB  1 
ATOM   358  C CG  . LYS   A 1 47  ? -4.988  40.819 0.742   1.00 53.45  ? -150 LYS   A CG  1 
ATOM   359  C CD  . LYS   A 1 47  ? -4.474  42.064 0.078   1.00 55.32  ? -150 LYS   A CD  1 
ATOM   360  C CE  . LYS   A 1 47  ? -5.584  42.768 -0.718  1.00 55.15  ? -150 LYS   A CE  1 
ATOM   361  N NZ  . LYS   A 1 47  ? -5.134  44.117 -1.200  1.00 56.10  ? -150 LYS   A NZ  1 
ATOM   362  N N   . PHE   A 1 48  ? -3.310  38.863 4.684   1.00 43.89  ? -149 PHE   A N   1 
ATOM   363  C CA  . PHE   A 1 48  ? -2.250  38.283 5.467   1.00 42.60  ? -149 PHE   A CA  1 
ATOM   364  C C   . PHE   A 1 48  ? -2.296  36.709 5.488   1.00 40.72  ? -149 PHE   A C   1 
ATOM   365  O O   . PHE   A 1 48  ? -1.325  36.075 5.150   1.00 40.36  ? -149 PHE   A O   1 
ATOM   366  C CB  . PHE   A 1 48  ? -2.248  38.783 6.906   1.00 41.43  ? -149 PHE   A CB  1 
ATOM   367  C CG  . PHE   A 1 48  ? -1.200  38.138 7.775   1.00 41.67  ? -149 PHE   A CG  1 
ATOM   368  C CD1 . PHE   A 1 48  ? 0.162   38.461 7.636   1.00 39.22  ? -149 PHE   A CD1 1 
ATOM   369  C CD2 . PHE   A 1 48  ? -1.572  37.170 8.713   1.00 41.93  ? -149 PHE   A CD2 1 
ATOM   370  C CE1 . PHE   A 1 48  ? 1.114   37.867 8.432   1.00 39.45  ? -149 PHE   A CE1 1 
ATOM   371  C CE2 . PHE   A 1 48  ? -0.630  36.573 9.501   1.00 41.90  ? -149 PHE   A CE2 1 
ATOM   372  C CZ  . PHE   A 1 48  ? 0.725   36.898 9.364   1.00 40.06  ? -149 PHE   A CZ  1 
ATOM   373  N N   . PRO   A 1 49  ? -3.419  36.111 5.909   1.00 42.91  ? -148 PRO   A N   1 
ATOM   374  C CA  . PRO   A 1 49  ? -3.424  34.617 5.979   1.00 45.45  ? -148 PRO   A CA  1 
ATOM   375  C C   . PRO   A 1 49  ? -3.179  33.974 4.644   1.00 50.70  ? -148 PRO   A C   1 
ATOM   376  O O   . PRO   A 1 49  ? -2.517  32.924 4.593   1.00 56.98  ? -148 PRO   A O   1 
ATOM   377  C CB  . PRO   A 1 49  ? -4.820  34.272 6.517   1.00 44.04  ? -148 PRO   A CB  1 
ATOM   378  C CG  . PRO   A 1 49  ? -5.635  35.563 6.384   1.00 45.67  ? -148 PRO   A CG  1 
ATOM   379  C CD  . PRO   A 1 49  ? -4.652  36.687 6.456   1.00 44.65  ? -148 PRO   A CD  1 
ATOM   380  N N   . GLN   A 1 50  ? -3.621  34.563 3.530   1.00 50.76  ? -147 GLN   A N   1 
ATOM   381  C CA  . GLN   A 1 50  ? -3.351  33.955 2.224   1.00 55.27  ? -147 GLN   A CA  1 
ATOM   382  C C   . GLN   A 1 50  ? -1.860  34.012 1.868   1.00 52.76  ? -147 GLN   A C   1 
ATOM   383  O O   . GLN   A 1 50  ? -1.282  33.026 1.446   1.00 51.94  ? -147 GLN   A O   1 
ATOM   384  C CB  . GLN   A 1 50  ? -4.208  34.609 1.152   1.00 60.72  ? -147 GLN   A CB  1 
ATOM   385  C CG  . GLN   A 1 50  ? -5.658  34.786 1.578   1.00 66.16  ? -147 GLN   A CG  1 
ATOM   386  C CD  . GLN   A 1 50  ? -6.458  35.581 0.542   1.00 71.70  ? -147 GLN   A CD  1 
ATOM   387  O OE1 . GLN   A 1 50  ? -5.957  36.577 -0.021  1.00 74.22  ? -147 GLN   A OE1 1 
ATOM   388  N NE2 . GLN   A 1 50  ? -7.701  35.151 0.280   1.00 71.78  ? -147 GLN   A NE2 1 
ATOM   389  N N   . VAL   A 1 51  ? -1.246  35.187 2.041   1.00 52.16  ? -146 VAL   A N   1 
ATOM   390  C CA  . VAL   A 1 51  ? 0.153   35.315 1.610   1.00 50.73  ? -146 VAL   A CA  1 
ATOM   391  C C   . VAL   A 1 51  ? 1.094   34.615 2.576   1.00 48.93  ? -146 VAL   A C   1 
ATOM   392  O O   . VAL   A 1 51  ? 2.098   34.034 2.155   1.00 48.81  ? -146 VAL   A O   1 
ATOM   393  C CB  . VAL   A 1 51  ? 0.524   36.815 1.480   1.00 47.91  ? -146 VAL   A CB  1 
ATOM   394  C CG1 . VAL   A 1 51  ? -0.007  37.369 0.179   1.00 46.36  ? -146 VAL   A CG1 1 
ATOM   395  C CG2 . VAL   A 1 51  ? -0.009  37.584 2.687   1.00 46.82  ? -146 VAL   A CG2 1 
ATOM   396  N N   . ALA   A 1 52  ? 0.806   34.679 3.883   1.00 48.31  ? -145 ALA   A N   1 
ATOM   397  C CA  . ALA   A 1 52  ? 1.691   34.123 4.892   1.00 47.65  ? -145 ALA   A CA  1 
ATOM   398  C C   . ALA   A 1 52  ? 1.661   32.602 4.856   1.00 51.26  ? -145 ALA   A C   1 
ATOM   399  O O   . ALA   A 1 52  ? 2.650   31.959 5.248   1.00 52.85  ? -145 ALA   A O   1 
ATOM   400  C CB  . ALA   A 1 52  ? 1.308   34.640 6.286   1.00 43.89  ? -145 ALA   A CB  1 
ATOM   401  N N   . ALA   A 1 53  ? 0.554   32.020 4.378   1.00 51.62  ? -144 ALA   A N   1 
ATOM   402  C CA  . ALA   A 1 53  ? 0.487   30.568 4.201   1.00 52.22  ? -144 ALA   A CA  1 
ATOM   403  C C   . ALA   A 1 53  ? 1.544   30.072 3.231   1.00 54.04  ? -144 ALA   A C   1 
ATOM   404  O O   . ALA   A 1 53  ? 2.009   28.927 3.351   1.00 58.40  ? -144 ALA   A O   1 
ATOM   405  C CB  . ALA   A 1 53  ? -0.903  30.143 3.728   1.00 51.44  ? -144 ALA   A CB  1 
ATOM   406  N N   . THR   A 1 54  ? 1.942   30.890 2.262   1.00 51.42  ? -143 THR   A N   1 
ATOM   407  C CA  . THR   A 1 54  ? 2.978   30.478 1.312   1.00 54.25  ? -143 THR   A CA  1 
ATOM   408  C C   . THR   A 1 54  ? 4.363   30.968 1.718   1.00 53.43  ? -143 THR   A C   1 
ATOM   409  O O   . THR   A 1 54  ? 5.283   30.962 0.907   1.00 49.06  ? -143 THR   A O   1 
ATOM   410  C CB  . THR   A 1 54  ? 2.621   30.955 -0.100  1.00 56.32  ? -143 THR   A CB  1 
ATOM   411  O OG1 . THR   A 1 54  ? 2.391   32.375 -0.101  1.00 55.49  ? -143 THR   A OG1 1 
ATOM   412  C CG2 . THR   A 1 54  ? 1.333   30.293 -0.553  1.00 57.06  ? -143 THR   A CG2 1 
ATOM   413  N N   . GLY   A 1 55  ? 4.508   31.438 2.962   1.00 57.40  ? -142 GLY   A N   1 
ATOM   414  C CA  . GLY   A 1 55  ? 5.794   31.927 3.423   1.00 59.81  ? -142 GLY   A CA  1 
ATOM   415  C C   . GLY   A 1 55  ? 6.115   33.362 3.050   1.00 60.21  ? -142 GLY   A C   1 
ATOM   416  O O   . GLY   A 1 55  ? 7.281   33.763 3.124   1.00 59.60  ? -142 GLY   A O   1 
ATOM   417  N N   . ASP   A 1 56  ? 5.111   34.139 2.633   1.00 60.28  ? -141 ASP   A N   1 
ATOM   418  C CA  . ASP   A 1 56  ? 5.291   35.491 2.141   1.00 61.92  ? -141 ASP   A CA  1 
ATOM   419  C C   . ASP   A 1 56  ? 4.629   36.496 3.088   1.00 57.18  ? -141 ASP   A C   1 
ATOM   420  O O   . ASP   A 1 56  ? 4.162   36.144 4.168   1.00 56.50  ? -141 ASP   A O   1 
ATOM   421  C CB  . ASP   A 1 56  ? 4.747   35.578 0.707   1.00 66.61  ? -141 ASP   A CB  1 
ATOM   422  C CG  . ASP   A 1 56  ? 5.350   36.749 -0.075  1.00 71.70  ? -141 ASP   A CG  1 
ATOM   423  O OD1 . ASP   A 1 56  ? 6.234   37.465 0.478   1.00 72.12  ? -141 ASP   A OD1 1 
ATOM   424  O OD2 . ASP   A 1 56  ? 4.936   36.964 -1.241  1.00 75.21  ? -141 ASP   A OD2 1 
ATOM   425  N N   . GLY   A 1 57  ? 4.603   37.768 2.683   1.00 55.22  ? -140 GLY   A N   1 
ATOM   426  C CA  . GLY   A 1 57  ? 3.887   38.784 3.423   1.00 50.85  ? -140 GLY   A CA  1 
ATOM   427  C C   . GLY   A 1 57  ? 4.795   39.690 4.222   1.00 48.17  ? -140 GLY   A C   1 
ATOM   428  O O   . GLY   A 1 57  ? 5.998   39.764 3.968   1.00 51.03  ? -140 GLY   A O   1 
ATOM   429  N N   . PRO   A 1 58  ? 4.239   40.408 5.205   1.00 43.42  ? -139 PRO   A N   1 
ATOM   430  C CA  . PRO   A 1 58  ? 5.054   41.294 6.038   1.00 40.40  ? -139 PRO   A CA  1 
ATOM   431  C C   . PRO   A 1 58  ? 5.690   40.568 7.219   1.00 45.01  ? -139 PRO   A C   1 
ATOM   432  O O   . PRO   A 1 58  ? 5.299   39.454 7.621   1.00 46.24  ? -139 PRO   A O   1 
ATOM   433  C CB  . PRO   A 1 58  ? 4.038   42.306 6.531   1.00 39.48  ? -139 PRO   A CB  1 
ATOM   434  C CG  . PRO   A 1 58  ? 2.780   41.489 6.713   1.00 38.54  ? -139 PRO   A CG  1 
ATOM   435  C CD  . PRO   A 1 58  ? 2.807   40.455 5.562   1.00 38.42  ? -139 PRO   A CD  1 
ATOM   436  N N   . ASP   A 1 59  ? 6.731   41.199 7.767   1.00 45.21  ? -138 ASP   A N   1 
ATOM   437  C CA  . ASP   A 1 59  ? 7.370   40.658 8.961   1.00 43.96  ? -138 ASP   A CA  1 
ATOM   438  C C   . ASP   A 1 59  ? 6.480   40.831 10.182  1.00 39.81  ? -138 ASP   A C   1 
ATOM   439  O O   . ASP   A 1 59  ? 6.456   39.940 11.062  1.00 38.96  ? -138 ASP   A O   1 
ATOM   440  C CB  . ASP   A 1 59  ? 8.711   41.352 9.201   1.00 46.05  ? -138 ASP   A CB  1 
ATOM   441  C CG  . ASP   A 1 59  ? 9.670   41.166 8.064   1.00 45.14  ? -138 ASP   A CG  1 
ATOM   442  O OD1 . ASP   A 1 59  ? 9.661   42.025 7.143   1.00 48.27  ? -138 ASP   A OD1 1 
ATOM   443  O OD2 . ASP   A 1 59  ? 10.464  40.227 8.128   1.00 41.40  ? -138 ASP   A OD2 1 
ATOM   444  N N   . ILE   A 1 60  ? 5.747   41.963 10.252  1.00 35.72  ? -137 ILE   A N   1 
ATOM   445  C CA  . ILE   A 1 60  ? 4.874   42.285 11.370  1.00 37.69  ? -137 ILE   A CA  1 
ATOM   446  C C   . ILE   A 1 60  ? 3.517   42.679 10.807  1.00 41.01  ? -137 ILE   A C   1 
ATOM   447  O O   . ILE   A 1 60  ? 3.436   43.514 9.896   1.00 42.71  ? -137 ILE   A O   1 
ATOM   448  C CB  . ILE   A 1 60  ? 5.445   43.449 12.213  1.00 38.32  ? -137 ILE   A CB  1 
ATOM   449  C CG1 . ILE   A 1 60  ? 6.811   43.082 12.787  1.00 38.66  ? -137 ILE   A CG1 1 
ATOM   450  C CG2 . ILE   A 1 60  ? 4.468   43.861 13.319  1.00 35.39  ? -137 ILE   A CG2 1 
ATOM   451  C CD1 . ILE   A 1 60  ? 7.570   44.327 13.346  1.00 38.94  ? -137 ILE   A CD1 1 
ATOM   452  N N   . ILE   A 1 61  ? 2.448   42.113 11.357  1.00 40.81  ? -136 ILE   A N   1 
ATOM   453  C CA  . ILE   A 1 61  ? 1.100   42.535 10.982  1.00 42.36  ? -136 ILE   A CA  1 
ATOM   454  C C   . ILE   A 1 61  ? 0.404   43.136 12.198  1.00 40.31  ? -136 ILE   A C   1 
ATOM   455  O O   . ILE   A 1 61  ? 0.482   42.571 13.305  1.00 39.39  ? -136 ILE   A O   1 
ATOM   456  C CB  . ILE   A 1 61  ? 0.274   41.341 10.412  1.00 44.33  ? -136 ILE   A CB  1 
ATOM   457  C CG1 . ILE   A 1 61  ? -1.215  41.742 10.348  1.00 45.44  ? -136 ILE   A CG1 1 
ATOM   458  C CG2 . ILE   A 1 61  ? 0.457   40.101 11.267  1.00 41.54  ? -136 ILE   A CG2 1 
ATOM   459  C CD1 . ILE   A 1 61  ? -2.037  40.967 9.370   1.00 48.41  ? -136 ILE   A CD1 1 
ATOM   460  N N   . PHE   A 1 62  ? -0.262  44.284 11.998  1.00 37.33  ? -135 PHE   A N   1 
ATOM   461  C CA  . PHE   A 1 62  ? -1.070  44.924 13.039  1.00 36.18  ? -135 PHE   A CA  1 
ATOM   462  C C   . PHE   A 1 62  ? -2.549  44.702 12.758  1.00 35.35  ? -135 PHE   A C   1 
ATOM   463  O O   . PHE   A 1 62  ? -2.999  44.834 11.612  1.00 37.70  ? -135 PHE   A O   1 
ATOM   464  C CB  . PHE   A 1 62  ? -0.833  46.443 13.101  1.00 37.28  ? -135 PHE   A CB  1 
ATOM   465  C CG  . PHE   A 1 62  ? 0.454   46.855 13.808  1.00 37.44  ? -135 PHE   A CG  1 
ATOM   466  C CD1 . PHE   A 1 62  ? 1.727   46.641 13.190  1.00 36.78  ? -135 PHE   A CD1 1 
ATOM   467  C CD2 . PHE   A 1 62  ? 0.411   47.481 15.048  1.00 33.42  ? -135 PHE   A CD2 1 
ATOM   468  C CE1 . PHE   A 1 62  ? 2.904   47.042 13.844  1.00 33.11  ? -135 PHE   A CE1 1 
ATOM   469  C CE2 . PHE   A 1 62  ? 1.583   47.877 15.693  1.00 31.63  ? -135 PHE   A CE2 1 
ATOM   470  C CZ  . PHE   A 1 62  ? 2.812   47.647 15.104  1.00 31.60  ? -135 PHE   A CZ  1 
ATOM   471  N N   . TRP   A 1 63  ? -3.314  44.392 13.810  1.00 33.81  ? -134 TRP   A N   1 
ATOM   472  C CA  . TRP   A 1 63  ? -4.767  44.244 13.735  1.00 29.75  ? -134 TRP   A CA  1 
ATOM   473  C C   . TRP   A 1 63  ? -5.266  44.109 15.148  1.00 31.10  ? -134 TRP   A C   1 
ATOM   474  O O   . TRP   A 1 63  ? -4.474  43.904 16.077  1.00 35.68  ? -134 TRP   A O   1 
ATOM   475  C CB  . TRP   A 1 63  ? -5.195  43.008 12.908  1.00 34.83  ? -134 TRP   A CB  1 
ATOM   476  C CG  . TRP   A 1 63  ? -6.626  43.110 12.469  1.00 35.24  ? -134 TRP   A CG  1 
ATOM   477  C CD1 . TRP   A 1 63  ? -7.699  42.504 13.038  1.00 35.00  ? -134 TRP   A CD1 1 
ATOM   478  C CD2 . TRP   A 1 63  ? -7.128  43.886 11.370  1.00 35.31  ? -134 TRP   A CD2 1 
ATOM   479  N NE1 . TRP   A 1 63  ? -8.862  42.822 12.345  1.00 36.02  ? -134 TRP   A NE1 1 
ATOM   480  C CE2 . TRP   A 1 63  ? -8.518  43.683 11.321  1.00 38.49  ? -134 TRP   A CE2 1 
ATOM   481  C CE3 . TRP   A 1 63  ? -6.530  44.723 10.417  1.00 33.32  ? -134 TRP   A CE3 1 
ATOM   482  C CZ2 . TRP   A 1 63  ? -9.328  44.300 10.358  1.00 40.82  ? -134 TRP   A CZ2 1 
ATOM   483  C CZ3 . TRP   A 1 63  ? -7.336  45.316 9.444   1.00 35.30  ? -134 TRP   A CZ3 1 
ATOM   484  C CH2 . TRP   A 1 63  ? -8.720  45.129 9.431   1.00 37.63  ? -134 TRP   A CH2 1 
ATOM   485  N N   . ALA   A 1 64  ? -6.569  44.278 15.334  1.00 28.13  ? -133 ALA   A N   1 
ATOM   486  C CA  . ALA   A 1 64  ? -7.135  43.969 16.630  1.00 30.48  ? -133 ALA   A CA  1 
ATOM   487  C C   . ALA   A 1 64  ? -6.945  42.466 16.914  1.00 34.35  ? -133 ALA   A C   1 
ATOM   488  O O   . ALA   A 1 64  ? -6.883  41.644 16.001  1.00 35.33  ? -133 ALA   A O   1 
ATOM   489  C CB  . ALA   A 1 64  ? -8.621  44.340 16.668  1.00 27.91  ? -133 ALA   A CB  1 
ATOM   490  N N   . HIS   A 1 65  ? -6.880  42.113 18.188  1.00 35.21  ? -132 HIS   A N   1 
ATOM   491  C CA  . HIS   A 1 65  ? -6.490  40.767 18.572  1.00 35.65  ? -132 HIS   A CA  1 
ATOM   492  C C   . HIS   A 1 65  ? -7.452  39.706 18.099  1.00 37.78  ? -132 HIS   A C   1 
ATOM   493  O O   . HIS   A 1 65  ? -7.057  38.513 18.042  1.00 41.03  ? -132 HIS   A O   1 
ATOM   494  C CB  . HIS   A 1 65  ? -6.359  40.674 20.087  1.00 34.18  ? -132 HIS   A CB  1 
ATOM   495  C CG  . HIS   A 1 65  ? -7.673  40.739 20.800  1.00 38.57  ? -132 HIS   A CG  1 
ATOM   496  N ND1 . HIS   A 1 65  ? -8.384  41.918 20.954  1.00 38.12  ? -132 HIS   A ND1 1 
ATOM   497  C CD2 . HIS   A 1 65  ? -8.409  39.769 21.396  1.00 40.00  ? -132 HIS   A CD2 1 
ATOM   498  C CE1 . HIS   A 1 65  ? -9.498  41.666 21.621  1.00 38.35  ? -132 HIS   A CE1 1 
ATOM   499  N NE2 . HIS   A 1 65  ? -9.538  40.372 21.905  1.00 40.38  ? -132 HIS   A NE2 1 
ATOM   500  N N   . ASP   A 1 66  ? -8.703  40.060 17.766  1.00 36.09  ? -131 ASP   A N   1 
ATOM   501  C CA  . ASP   A 1 66  ? -9.692  38.982 17.486  1.00 39.60  ? -131 ASP   A CA  1 
ATOM   502  C C   . ASP   A 1 66  ? -9.273  38.103 16.307  1.00 39.70  ? -131 ASP   A C   1 
ATOM   503  O O   . ASP   A 1 66  ? -9.617  36.919 16.259  1.00 41.73  ? -131 ASP   A O   1 
ATOM   504  C CB  . ASP   A 1 66  ? -11.109 39.567 17.241  1.00 37.25  ? -131 ASP   A CB  1 
ATOM   505  C CG  . ASP   A 1 66  ? -11.132 40.595 16.124  1.00 37.39  ? -131 ASP   A CG  1 
ATOM   506  O OD1 . ASP   A 1 66  ? -10.422 41.634 16.229  1.00 34.34  ? -131 ASP   A OD1 1 
ATOM   507  O OD2 . ASP   A 1 66  ? -11.869 40.359 15.117  1.00 37.64  ? -131 ASP   A OD2 1 
ATOM   508  N N   . ARG   A 1 67  ? -8.540  38.651 15.338  1.00 39.30  ? -130 ARG   A N   1 
ATOM   509  C CA  . ARG   A 1 67  ? -8.153  37.821 14.187  1.00 42.01  ? -130 ARG   A CA  1 
ATOM   510  C C   . ARG   A 1 67  ? -6.968  36.901 14.471  1.00 41.90  ? -130 ARG   A C   1 
ATOM   511  O O   . ARG   A 1 67  ? -6.697  36.016 13.666  1.00 44.27  ? -130 ARG   A O   1 
ATOM   512  C CB  . ARG   A 1 67  ? -7.791  38.715 12.991  1.00 45.41  ? -130 ARG   A CB  1 
ATOM   513  C CG  . ARG   A 1 67  ? -8.923  39.544 12.441  1.00 49.40  ? -130 ARG   A CG  1 
ATOM   514  C CD  . ARG   A 1 67  ? -9.620  38.837 11.324  1.00 54.42  ? -130 ARG   A CD  1 
ATOM   515  N NE  . ARG   A 1 67  ? -10.866 39.518 10.944  1.00 56.78  ? -130 ARG   A NE  1 
ATOM   516  C CZ  . ARG   A 1 67  ? -11.611 39.138 9.908   1.00 59.56  ? -130 ARG   A CZ  1 
ATOM   517  N NH1 . ARG   A 1 67  ? -11.212 38.089 9.147   1.00 59.10  ? -130 ARG   A NH1 1 
ATOM   518  N NH2 . ARG   A 1 67  ? -12.729 39.804 9.617   1.00 58.82  ? -130 ARG   A NH2 1 
ATOM   519  N N   . PHE   A 1 68  ? -6.251  37.079 15.577  1.00 39.39  ? -129 PHE   A N   1 
ATOM   520  C CA  . PHE   A 1 68  ? -4.952  36.439 15.696  1.00 39.66  ? -129 PHE   A CA  1 
ATOM   521  C C   . PHE   A 1 68  ? -5.051  34.956 16.104  1.00 39.61  ? -129 PHE   A C   1 
ATOM   522  O O   . PHE   A 1 68  ? -4.136  34.182 15.808  1.00 41.03  ? -129 PHE   A O   1 
ATOM   523  C CB  . PHE   A 1 68  ? -4.085  37.209 16.680  1.00 40.60  ? -129 PHE   A CB  1 
ATOM   524  C CG  . PHE   A 1 68  ? -3.407  38.433 16.069  1.00 43.29  ? -129 PHE   A CG  1 
ATOM   525  C CD1 . PHE   A 1 68  ? -4.142  39.387 15.443  1.00 48.55  ? -129 PHE   A CD1 1 
ATOM   526  C CD2 . PHE   A 1 68  ? -2.057  38.594 16.115  1.00 45.37  ? -129 PHE   A CD2 1 
ATOM   527  C CE1 . PHE   A 1 68  ? -3.545  40.497 14.892  1.00 51.65  ? -129 PHE   A CE1 1 
ATOM   528  C CE2 . PHE   A 1 68  ? -1.436  39.669 15.569  1.00 49.24  ? -129 PHE   A CE2 1 
ATOM   529  C CZ  . PHE   A 1 68  ? -2.162  40.644 14.942  1.00 51.36  ? -129 PHE   A CZ  1 
ATOM   530  N N   . GLY   A 1 69  ? -6.142  34.552 16.751  1.00 41.84  ? -128 GLY   A N   1 
ATOM   531  C CA  . GLY   A 1 69  ? -6.342  33.136 17.049  1.00 42.59  ? -128 GLY   A CA  1 
ATOM   532  C C   . GLY   A 1 69  ? -6.306  32.287 15.792  1.00 41.11  ? -128 GLY   A C   1 
ATOM   533  O O   . GLY   A 1 69  ? -5.533  31.318 15.721  1.00 42.22  ? -128 GLY   A O   1 
ATOM   534  N N   . GLY   A 1 70  ? -7.097  32.666 14.777  1.00 37.11  ? -127 GLY   A N   1 
ATOM   535  C CA  . GLY   A 1 70  ? -7.057  31.996 13.477  1.00 34.30  ? -127 GLY   A CA  1 
ATOM   536  C C   . GLY   A 1 70  ? -5.658  31.918 12.888  1.00 41.49  ? -127 GLY   A C   1 
ATOM   537  O O   . GLY   A 1 70  ? -5.209  30.857 12.450  1.00 40.50  ? -127 GLY   A O   1 
ATOM   538  N N   . TYR   A 1 71  ? -4.914  33.049 12.901  1.00 41.00  ? -126 TYR   A N   1 
ATOM   539  C CA  . TYR   A 1 71  ? -3.551  33.043 12.352  1.00 40.30  ? -126 TYR   A CA  1 
ATOM   540  C C   . TYR   A 1 71  ? -2.658  32.077 13.126  1.00 42.10  ? -126 TYR   A C   1 
ATOM   541  O O   . TYR   A 1 71  ? -1.909  31.308 12.542  1.00 44.68  ? -126 TYR   A O   1 
ATOM   542  C CB  . TYR   A 1 71  ? -2.952  34.457 12.423  1.00 42.42  ? -126 TYR   A CB  1 
ATOM   543  C CG  . TYR   A 1 71  ? -3.705  35.554 11.682  1.00 41.94  ? -126 TYR   A CG  1 
ATOM   544  C CD1 . TYR   A 1 71  ? -4.532  35.280 10.594  1.00 42.95  ? -126 TYR   A CD1 1 
ATOM   545  C CD2 . TYR   A 1 71  ? -3.572  36.888 12.070  1.00 41.11  ? -126 TYR   A CD2 1 
ATOM   546  C CE1 . TYR   A 1 71  ? -5.204  36.303 9.921   1.00 42.31  ? -126 TYR   A CE1 1 
ATOM   547  C CE2 . TYR   A 1 71  ? -4.242  37.887 11.417  1.00 41.01  ? -126 TYR   A CE2 1 
ATOM   548  C CZ  . TYR   A 1 71  ? -5.060  37.596 10.359  1.00 44.16  ? -126 TYR   A CZ  1 
ATOM   549  O OH  . TYR   A 1 71  ? -5.723  38.673 9.718   1.00 48.14  ? -126 TYR   A OH  1 
ATOM   550  N N   . ALA   A 1 72  ? -2.717  32.115 14.461  1.00 43.19  ? -125 ALA   A N   1 
ATOM   551  C CA  . ALA   A 1 72  ? -1.890  31.228 15.266  1.00 42.24  ? -125 ALA   A CA  1 
ATOM   552  C C   . ALA   A 1 72  ? -2.269  29.768 15.031  1.00 45.92  ? -125 ALA   A C   1 
ATOM   553  O O   . ALA   A 1 72  ? -1.390  28.907 14.922  1.00 46.13  ? -125 ALA   A O   1 
ATOM   554  C CB  . ALA   A 1 72  ? -2.014  31.576 16.750  1.00 38.84  ? -125 ALA   A CB  1 
ATOM   555  N N   . GLN   A 1 73  ? -3.576  29.475 14.921  1.00 46.26  ? -124 GLN   A N   1 
ATOM   556  C CA  . GLN   A 1 73  ? -4.009  28.098 14.671  1.00 47.07  ? -124 GLN   A CA  1 
ATOM   557  C C   . GLN   A 1 73  ? -3.455  27.585 13.358  1.00 44.63  ? -124 GLN   A C   1 
ATOM   558  O O   . GLN   A 1 73  ? -3.198  26.390 13.223  1.00 44.62  ? -124 GLN   A O   1 
ATOM   559  C CB  . GLN   A 1 73  ? -5.545  28.042 14.671  1.00 49.38  ? -124 GLN   A CB  1 
ATOM   560  C CG  . GLN   A 1 73  ? -6.146  26.659 14.563  1.00 53.01  ? -124 GLN   A CG  1 
ATOM   561  C CD  . GLN   A 1 73  ? -5.734  25.759 15.732  1.00 58.66  ? -124 GLN   A CD  1 
ATOM   562  O OE1 . GLN   A 1 73  ? -6.020  26.052 16.897  1.00 61.05  ? -124 GLN   A OE1 1 
ATOM   563  N NE2 . GLN   A 1 73  ? -5.066  24.653 15.420  1.00 60.70  ? -124 GLN   A NE2 1 
ATOM   564  N N   . SER   A 1 74  ? -3.317  28.461 12.365  1.00 43.01  ? -123 SER   A N   1 
ATOM   565  C CA  . SER   A 1 74  ? -2.798  28.119 11.049  1.00 42.88  ? -123 SER   A CA  1 
ATOM   566  C C   . SER   A 1 74  ? -1.289  28.120 10.991  1.00 44.53  ? -123 SER   A C   1 
ATOM   567  O O   . SER   A 1 74  ? -0.737  27.959 9.906   1.00 44.77  ? -123 SER   A O   1 
ATOM   568  C CB  . SER   A 1 74  ? -3.311  29.136 10.000  1.00 44.30  ? -123 SER   A CB  1 
ATOM   569  O OG  . SER   A 1 74  ? -4.714  29.072 9.873   1.00 44.50  ? -123 SER   A OG  1 
ATOM   570  N N   . GLY   A 1 75  ? -0.610  28.303 12.124  1.00 47.46  ? -122 GLY   A N   1 
ATOM   571  C CA  . GLY   A 1 75  ? 0.849   28.352 12.130  1.00 49.60  ? -122 GLY   A CA  1 
ATOM   572  C C   . GLY   A 1 75  ? 1.477   29.595 11.494  1.00 48.44  ? -122 GLY   A C   1 
ATOM   573  O O   . GLY   A 1 75  ? 2.637   29.524 11.041  1.00 50.19  ? -122 GLY   A O   1 
ATOM   574  N N   . LEU   A 1 76  ? 0.758   30.717 11.443  1.00 43.91  ? -121 LEU   A N   1 
ATOM   575  C CA  . LEU   A 1 76  ? 1.229   31.890 10.710  1.00 44.20  ? -121 LEU   A CA  1 
ATOM   576  C C   . LEU   A 1 76  ? 1.992   32.900 11.573  1.00 44.31  ? -121 LEU   A C   1 
ATOM   577  O O   . LEU   A 1 76  ? 2.597   33.833 11.031  1.00 44.42  ? -121 LEU   A O   1 
ATOM   578  C CB  . LEU   A 1 76  ? 0.043   32.627 10.049  1.00 43.96  ? -121 LEU   A CB  1 
ATOM   579  C CG  . LEU   A 1 76  ? -0.809  31.803 9.090   1.00 45.92  ? -121 LEU   A CG  1 
ATOM   580  C CD1 . LEU   A 1 76  ? -1.928  32.664 8.520   1.00 48.07  ? -121 LEU   A CD1 1 
ATOM   581  C CD2 . LEU   A 1 76  ? 0.043   31.221 7.985   1.00 47.34  ? -121 LEU   A CD2 1 
ATOM   582  N N   . LEU   A 1 77  ? 1.976   32.751 12.890  1.00 44.86  ? -120 LEU   A N   1 
ATOM   583  C CA  . LEU   A 1 77  ? 2.554   33.721 13.801  1.00 43.01  ? -120 LEU   A CA  1 
ATOM   584  C C   . LEU   A 1 77  ? 3.645   33.071 14.641  1.00 43.84  ? -120 LEU   A C   1 
ATOM   585  O O   . LEU   A 1 77  ? 3.499   31.935 15.070  1.00 45.96  ? -120 LEU   A O   1 
ATOM   586  C CB  . LEU   A 1 77  ? 1.465   34.300 14.711  1.00 42.48  ? -120 LEU   A CB  1 
ATOM   587  C CG  . LEU   A 1 77  ? 0.399   35.097 13.995  1.00 40.07  ? -120 LEU   A CG  1 
ATOM   588  C CD1 . LEU   A 1 77  ? -0.670  35.507 14.975  1.00 40.22  ? -120 LEU   A CD1 1 
ATOM   589  C CD2 . LEU   A 1 77  ? 1.068   36.324 13.372  1.00 39.21  ? -120 LEU   A CD2 1 
ATOM   590  N N   . ALA   A 1 78  ? 4.725   33.800 14.884  1.00 45.47  ? -119 ALA   A N   1 
ATOM   591  C CA  . ALA   A 1 78  ? 5.782   33.321 15.759  1.00 47.08  ? -119 ALA   A CA  1 
ATOM   592  C C   . ALA   A 1 78  ? 5.404   33.554 17.217  1.00 49.45  ? -119 ALA   A C   1 
ATOM   593  O O   . ALA   A 1 78  ? 4.778   34.563 17.571  1.00 47.76  ? -119 ALA   A O   1 
ATOM   594  C CB  . ALA   A 1 78  ? 7.100   34.031 15.438  1.00 44.98  ? -119 ALA   A CB  1 
ATOM   595  N N   . GLU   A 1 79  ? 5.787   32.625 18.078  1.00 49.82  ? -118 GLU   A N   1 
ATOM   596  C CA  . GLU   A 1 79  ? 5.563   32.849 19.501  1.00 52.15  ? -118 GLU   A CA  1 
ATOM   597  C C   . GLU   A 1 79  ? 6.457   33.994 19.988  1.00 51.10  ? -118 GLU   A C   1 
ATOM   598  O O   . GLU   A 1 79  ? 7.650   34.043 19.685  1.00 52.70  ? -118 GLU   A O   1 
ATOM   599  C CB  . GLU   A 1 79  ? 5.847   31.576 20.292  1.00 53.86  ? -118 GLU   A CB  1 
ATOM   600  C CG  . GLU   A 1 79  ? 5.507   31.662 21.768  1.00 56.68  ? -118 GLU   A CG  1 
ATOM   601  C CD  . GLU   A 1 79  ? 5.917   30.393 22.514  1.00 62.38  ? -118 GLU   A CD  1 
ATOM   602  O OE1 . GLU   A 1 79  ? 6.092   29.333 21.841  1.00 66.50  ? -118 GLU   A OE1 1 
ATOM   603  O OE2 . GLU   A 1 79  ? 6.072   30.448 23.754  1.00 62.17  ? -118 GLU   A OE2 1 
ATOM   604  N N   . ILE   A 1 80  ? 5.900   34.894 20.762  1.00 48.36  ? -117 ILE   A N   1 
ATOM   605  C CA  . ILE   A 1 80  ? 6.664   36.014 21.291  1.00 48.64  ? -117 ILE   A CA  1 
ATOM   606  C C   . ILE   A 1 80  ? 7.055   35.688 22.719  1.00 51.35  ? -117 ILE   A C   1 
ATOM   607  O O   . ILE   A 1 80  ? 6.259   35.111 23.483  1.00 51.39  ? -117 ILE   A O   1 
ATOM   608  C CB  . ILE   A 1 80  ? 5.863   37.327 21.209  1.00 47.51  ? -117 ILE   A CB  1 
ATOM   609  C CG1 . ILE   A 1 80  ? 4.720   37.310 22.183  1.00 48.72  ? -117 ILE   A CG1 1 
ATOM   610  C CG2 . ILE   A 1 80  ? 5.354   37.556 19.766  1.00 45.63  ? -117 ILE   A CG2 1 
ATOM   611  C CD1 . ILE   A 1 80  ? 4.158   38.675 22.432  1.00 53.07  ? -117 ILE   A CD1 1 
ATOM   612  N N   . THR   A 1 81  ? 8.281   36.056 23.089  1.00 53.13  ? -116 THR   A N   1 
ATOM   613  C CA  . THR   A 1 81  ? 8.892   35.611 24.344  1.00 56.60  ? -116 THR   A CA  1 
ATOM   614  C C   . THR   A 1 81  ? 9.568   36.795 25.028  1.00 56.63  ? -116 THR   A C   1 
ATOM   615  O O   . THR   A 1 81  ? 10.799  36.851 25.147  1.00 60.08  ? -116 THR   A O   1 
ATOM   616  C CB  . THR   A 1 81  ? 9.903   34.497 24.074  1.00 58.83  ? -116 THR   A CB  1 
ATOM   617  O OG1 . THR   A 1 81  ? 10.789  34.932 23.027  1.00 57.83  ? -116 THR   A OG1 1 
ATOM   618  C CG2 . THR   A 1 81  ? 9.183   33.219 23.646  1.00 59.88  ? -116 THR   A CG2 1 
ATOM   619  N N   . PRO   A 1 82  ? 8.787   37.764 25.492  1.00 52.23  ? -115 PRO   A N   1 
ATOM   620  C CA  . PRO   A 1 82  ? 9.378   38.837 26.296  1.00 51.01  ? -115 PRO   A CA  1 
ATOM   621  C C   . PRO   A 1 82  ? 9.745   38.328 27.678  1.00 49.26  ? -115 PRO   A C   1 
ATOM   622  O O   . PRO   A 1 82  ? 9.093   37.450 28.232  1.00 49.99  ? -115 PRO   A O   1 
ATOM   623  C CB  . PRO   A 1 82  ? 8.262   39.886 26.363  1.00 51.35  ? -115 PRO   A CB  1 
ATOM   624  C CG  . PRO   A 1 82  ? 7.007   39.077 26.227  1.00 51.49  ? -115 PRO   A CG  1 
ATOM   625  C CD  . PRO   A 1 82  ? 7.340   37.940 25.296  1.00 50.53  ? -115 PRO   A CD  1 
ATOM   626  N N   . ASP   A 1 83  ? 10.815  38.887 28.238  1.00 47.24  ? -114 ASP   A N   1 
ATOM   627  C CA  . ASP   A 1 83  ? 11.157  38.583 29.617  1.00 47.57  ? -114 ASP   A CA  1 
ATOM   628  C C   . ASP   A 1 83  ? 10.163  39.260 30.576  1.00 47.15  ? -114 ASP   A C   1 
ATOM   629  O O   . ASP   A 1 83  ? 9.308   40.052 30.173  1.00 44.37  ? -114 ASP   A O   1 
ATOM   630  C CB  . ASP   A 1 83  ? 12.596  39.006 29.909  1.00 47.90  ? -114 ASP   A CB  1 
ATOM   631  C CG  . ASP   A 1 83  ? 12.795  40.519 29.863  1.00 49.68  ? -114 ASP   A CG  1 
ATOM   632  O OD1 . ASP   A 1 83  ? 11.826  41.271 29.665  1.00 50.17  ? -114 ASP   A OD1 1 
ATOM   633  O OD2 . ASP   A 1 83  ? 13.927  40.965 30.051  1.00 52.27  ? -114 ASP   A OD2 1 
ATOM   634  N N   . LYS   A 1 84  ? 10.262  38.900 31.855  1.00 49.05  ? -113 LYS   A N   1 
ATOM   635  C CA  . LYS   A 1 84  ? 9.336   39.444 32.844  1.00 49.14  ? -113 LYS   A CA  1 
ATOM   636  C C   . LYS   A 1 84  ? 9.448   40.969 32.946  1.00 50.73  ? -113 LYS   A C   1 
ATOM   637  O O   . LYS   A 1 84  ? 8.437   41.673 33.129  1.00 48.61  ? -113 LYS   A O   1 
ATOM   638  C CB  . LYS   A 1 84  ? 9.587   38.797 34.211  1.00 48.10  ? -113 LYS   A CB  1 
ATOM   639  C CG  . LYS   A 1 84  ? 8.788   39.426 35.352  1.00 49.69  ? -113 LYS   A CG  1 
ATOM   640  C CD  . LYS   A 1 84  ? 9.137   38.803 36.691  1.00 54.44  ? -113 LYS   A CD  1 
ATOM   641  C CE  . LYS   A 1 84  ? 8.661   39.638 37.892  1.00 57.17  ? -113 LYS   A CE  1 
ATOM   642  N NZ  . LYS   A 1 84  ? 7.177   39.676 37.996  1.00 58.30  ? -113 LYS   A NZ  1 
ATOM   643  N N   . ALA   A 1 85  ? 10.667  41.504 32.849  1.00 52.74  ? -112 ALA   A N   1 
ATOM   644  C CA  . ALA   A 1 85  ? 10.834  42.957 32.898  1.00 51.39  ? -112 ALA   A CA  1 
ATOM   645  C C   . ALA   A 1 85  ? 9.968   43.647 31.851  1.00 50.30  ? -112 ALA   A C   1 
ATOM   646  O O   . ALA   A 1 85  ? 9.326   44.661 32.130  1.00 50.21  ? -112 ALA   A O   1 
ATOM   647  C CB  . ALA   A 1 85  ? 12.302  43.330 32.702  1.00 50.33  ? -112 ALA   A CB  1 
ATOM   648  N N   . PHE   A 1 86  ? 9.924   43.105 30.642  1.00 49.75  ? -111 PHE   A N   1 
ATOM   649  C CA  . PHE   A 1 86  ? 9.076   43.730 29.641  1.00 49.66  ? -111 PHE   A CA  1 
ATOM   650  C C   . PHE   A 1 86  ? 7.592   43.418 29.867  1.00 50.18  ? -111 PHE   A C   1 
ATOM   651  O O   . PHE   A 1 86  ? 6.735   44.317 29.720  1.00 50.36  ? -111 PHE   A O   1 
ATOM   652  C CB  . PHE   A 1 86  ? 9.483   43.311 28.223  1.00 46.79  ? -111 PHE   A CB  1 
ATOM   653  C CG  . PHE   A 1 86  ? 8.638   43.943 27.177  1.00 46.70  ? -111 PHE   A CG  1 
ATOM   654  C CD1 . PHE   A 1 86  ? 8.931   45.229 26.708  1.00 46.06  ? -111 PHE   A CD1 1 
ATOM   655  C CD2 . PHE   A 1 86  ? 7.527   43.291 26.681  1.00 48.85  ? -111 PHE   A CD2 1 
ATOM   656  C CE1 . PHE   A 1 86  ? 8.139   45.828 25.760  1.00 47.28  ? -111 PHE   A CE1 1 
ATOM   657  C CE2 . PHE   A 1 86  ? 6.714   43.883 25.719  1.00 49.83  ? -111 PHE   A CE2 1 
ATOM   658  C CZ  . PHE   A 1 86  ? 7.019   45.173 25.258  1.00 48.40  ? -111 PHE   A CZ  1 
ATOM   659  N N   . GLN   A 1 87  ? 7.259   42.164 30.218  1.00 46.64  ? -110 GLN   A N   1 
ATOM   660  C CA  . GLN   A 1 87  ? 5.849   41.836 30.406  1.00 45.69  ? -110 GLN   A CA  1 
ATOM   661  C C   . GLN   A 1 87  ? 5.222   42.660 31.526  1.00 46.54  ? -110 GLN   A C   1 
ATOM   662  O O   . GLN   A 1 87  ? 4.042   42.991 31.450  1.00 48.67  ? -110 GLN   A O   1 
ATOM   663  C CB  . GLN   A 1 87  ? 5.684   40.357 30.679  1.00 48.07  ? -110 GLN   A CB  1 
ATOM   664  C CG  . GLN   A 1 87  ? 5.900   39.474 29.447  1.00 50.03  ? -110 GLN   A CG  1 
ATOM   665  C CD  . GLN   A 1 87  ? 5.622   38.002 29.749  1.00 50.99  ? -110 GLN   A CD  1 
ATOM   666  O OE1 . GLN   A 1 87  ? 4.540   37.659 30.223  1.00 51.83  ? -110 GLN   A OE1 1 
ATOM   667  N NE2 . GLN   A 1 87  ? 6.602   37.142 29.498  1.00 49.69  ? -110 GLN   A NE2 1 
ATOM   668  N N   . ASP   A 1 88  ? 5.980   42.997 32.564  1.00 47.82  ? -109 ASP   A N   1 
ATOM   669  C CA  . ASP   A 1 88  ? 5.458   43.788 33.665  1.00 51.57  ? -109 ASP   A CA  1 
ATOM   670  C C   . ASP   A 1 88  ? 5.078   45.210 33.247  1.00 54.01  ? -109 ASP   A C   1 
ATOM   671  O O   . ASP   A 1 88  ? 4.312   45.865 33.966  1.00 54.86  ? -109 ASP   A O   1 
ATOM   672  C CB  . ASP   A 1 88  ? 6.477   43.852 34.799  1.00 54.40  ? -109 ASP   A CB  1 
ATOM   673  C CG  . ASP   A 1 88  ? 6.494   42.595 35.654  1.00 60.24  ? -109 ASP   A CG  1 
ATOM   674  O OD1 . ASP   A 1 88  ? 5.525   41.801 35.579  1.00 62.21  ? -109 ASP   A OD1 1 
ATOM   675  O OD2 . ASP   A 1 88  ? 7.489   42.378 36.384  1.00 62.33  ? -109 ASP   A OD2 1 
ATOM   676  N N   . LYS   A 1 89  ? 5.597   45.702 32.112  1.00 53.44  ? -108 LYS   A N   1 
ATOM   677  C CA  . LYS   A 1 89  ? 5.317   47.060 31.674  1.00 53.75  ? -108 LYS   A CA  1 
ATOM   678  C C   . LYS   A 1 89  ? 3.968   47.190 30.966  1.00 53.81  ? -108 LYS   A C   1 
ATOM   679  O O   . LYS   A 1 89  ? 3.502   48.329 30.751  1.00 53.07  ? -108 LYS   A O   1 
ATOM   680  C CB  . LYS   A 1 89  ? 6.424   47.566 30.745  1.00 53.69  ? -108 LYS   A CB  1 
ATOM   681  C CG  . LYS   A 1 89  ? 7.823   47.479 31.337  1.00 58.39  ? -108 LYS   A CG  1 
ATOM   682  C CD  . LYS   A 1 89  ? 8.882   47.770 30.273  1.00 62.13  ? -108 LYS   A CD  1 
ATOM   683  C CE  . LYS   A 1 89  ? 9.042   49.270 30.042  1.00 67.08  ? -108 LYS   A CE  1 
ATOM   684  N NZ  . LYS   A 1 89  ? 10.472  49.656 29.787  1.00 69.56  ? -108 LYS   A NZ  1 
ATOM   685  N N   . LEU   A 1 90  ? 3.340   46.077 30.569  1.00 51.25  ? -107 LEU   A N   1 
ATOM   686  C CA  . LEU   A 1 90  ? 2.018   46.150 29.949  1.00 47.49  ? -107 LEU   A CA  1 
ATOM   687  C C   . LEU   A 1 90  ? 0.980   45.626 30.933  1.00 46.64  ? -107 LEU   A C   1 
ATOM   688  O O   . LEU   A 1 90  ? 1.302   44.804 31.818  1.00 42.37  ? -107 LEU   A O   1 
ATOM   689  C CB  . LEU   A 1 90  ? 1.945   45.362 28.654  1.00 43.30  ? -107 LEU   A CB  1 
ATOM   690  C CG  . LEU   A 1 90  ? 3.013   45.587 27.577  1.00 43.67  ? -107 LEU   A CG  1 
ATOM   691  C CD1 . LEU   A 1 90  ? 2.468   45.075 26.226  1.00 43.83  ? -107 LEU   A CD1 1 
ATOM   692  C CD2 . LEU   A 1 90  ? 3.436   47.019 27.464  1.00 42.87  ? -107 LEU   A CD2 1 
ATOM   693  N N   . TYR   A 1 91  ? -0.269  46.123 30.769  1.00 45.94  ? -106 TYR   A N   1 
ATOM   694  C CA  . TYR   A 1 91  ? -1.353  45.699 31.640  1.00 45.52  ? -106 TYR   A CA  1 
ATOM   695  C C   . TYR   A 1 91  ? -1.620  44.201 31.475  1.00 43.76  ? -106 TYR   A C   1 
ATOM   696  O O   . TYR   A 1 91  ? -1.735  43.725 30.329  1.00 42.89  ? -106 TYR   A O   1 
ATOM   697  C CB  . TYR   A 1 91  ? -2.619  46.492 31.327  1.00 42.73  ? -106 TYR   A CB  1 
ATOM   698  C CG  . TYR   A 1 91  ? -2.557  47.911 31.806  1.00 43.68  ? -106 TYR   A CG  1 
ATOM   699  C CD1 . TYR   A 1 91  ? -2.634  48.211 33.178  1.00 47.44  ? -106 TYR   A CD1 1 
ATOM   700  C CD2 . TYR   A 1 91  ? -2.403  48.952 30.905  1.00 39.35  ? -106 TYR   A CD2 1 
ATOM   701  C CE1 . TYR   A 1 91  ? -2.575  49.543 33.620  1.00 50.48  ? -106 TYR   A CE1 1 
ATOM   702  C CE2 . TYR   A 1 91  ? -2.323  50.272 31.347  1.00 43.72  ? -106 TYR   A CE2 1 
ATOM   703  C CZ  . TYR   A 1 91  ? -2.424  50.570 32.684  1.00 49.03  ? -106 TYR   A CZ  1 
ATOM   704  O OH  . TYR   A 1 91  ? -2.346  51.898 33.099  1.00 54.78  ? -106 TYR   A OH  1 
ATOM   705  N N   . PRO   A 1 92  ? -1.732  43.430 32.572  1.00 44.30  ? -105 PRO   A N   1 
ATOM   706  C CA  . PRO   A 1 92  ? -1.996  41.985 32.427  1.00 47.77  ? -105 PRO   A CA  1 
ATOM   707  C C   . PRO   A 1 92  ? -3.128  41.655 31.463  1.00 49.73  ? -105 PRO   A C   1 
ATOM   708  O O   . PRO   A 1 92  ? -2.995  40.721 30.654  1.00 50.01  ? -105 PRO   A O   1 
ATOM   709  C CB  . PRO   A 1 92  ? -2.340  41.557 33.859  1.00 51.14  ? -105 PRO   A CB  1 
ATOM   710  C CG  . PRO   A 1 92  ? -1.558  42.510 34.724  1.00 50.49  ? -105 PRO   A CG  1 
ATOM   711  C CD  . PRO   A 1 92  ? -1.574  43.827 33.973  1.00 45.16  ? -105 PRO   A CD  1 
ATOM   712  N N   . PHE   A 1 93  ? -4.229  42.426 31.491  1.00 48.87  ? -104 PHE   A N   1 
ATOM   713  C CA  . PHE   A 1 93  ? -5.395  42.048 30.697  1.00 47.19  ? -104 PHE   A CA  1 
ATOM   714  C C   . PHE   A 1 93  ? -5.119  42.179 29.207  1.00 48.50  ? -104 PHE   A C   1 
ATOM   715  O O   . PHE   A 1 93  ? -5.721  41.440 28.405  1.00 50.06  ? -104 PHE   A O   1 
ATOM   716  C CB  . PHE   A 1 93  ? -6.637  42.867 31.105  1.00 45.50  ? -104 PHE   A CB  1 
ATOM   717  C CG  . PHE   A 1 93  ? -6.668  44.265 30.580  1.00 43.96  ? -104 PHE   A CG  1 
ATOM   718  C CD1 . PHE   A 1 93  ? -6.109  45.302 31.293  1.00 46.38  ? -104 PHE   A CD1 1 
ATOM   719  C CD2 . PHE   A 1 93  ? -7.302  44.555 29.376  1.00 43.81  ? -104 PHE   A CD2 1 
ATOM   720  C CE1 . PHE   A 1 93  ? -6.160  46.635 30.816  1.00 44.12  ? -104 PHE   A CE1 1 
ATOM   721  C CE2 . PHE   A 1 93  ? -7.366  45.866 28.895  1.00 43.15  ? -104 PHE   A CE2 1 
ATOM   722  C CZ  . PHE   A 1 93  ? -6.785  46.896 29.631  1.00 43.53  ? -104 PHE   A CZ  1 
ATOM   723  N N   . THR   A 1 94  ? -4.210  43.080 28.808  1.00 45.56  ? -103 THR   A N   1 
ATOM   724  C CA  . THR   A 1 94  ? -3.904  43.169 27.388  1.00 43.04  ? -103 THR   A CA  1 
ATOM   725  C C   . THR   A 1 94  ? -3.050  41.969 26.934  1.00 41.87  ? -103 THR   A C   1 
ATOM   726  O O   . THR   A 1 94  ? -3.196  41.495 25.786  1.00 40.26  ? -103 THR   A O   1 
ATOM   727  C CB  . THR   A 1 94  ? -3.237  44.517 27.056  1.00 39.57  ? -103 THR   A CB  1 
ATOM   728  O OG1 . THR   A 1 94  ? -1.908  44.560 27.566  1.00 40.68  ? -103 THR   A OG1 1 
ATOM   729  C CG2 . THR   A 1 94  ? -4.005  45.647 27.689  1.00 39.46  ? -103 THR   A CG2 1 
ATOM   730  N N   . TRP   A 1 95  ? -2.165  41.474 27.803  1.00 40.91  ? -102 TRP   A N   1 
ATOM   731  C CA  . TRP   A 1 95  ? -1.444  40.244 27.477  1.00 42.09  ? -102 TRP   A CA  1 
ATOM   732  C C   . TRP   A 1 95  ? -2.415  39.065 27.312  1.00 45.35  ? -102 TRP   A C   1 
ATOM   733  O O   . TRP   A 1 95  ? -2.242  38.219 26.421  1.00 46.99  ? -102 TRP   A O   1 
ATOM   734  C CB  . TRP   A 1 95  ? -0.406  39.921 28.577  1.00 40.45  ? -102 TRP   A CB  1 
ATOM   735  C CG  . TRP   A 1 95  ? 0.892   40.656 28.479  1.00 38.96  ? -102 TRP   A CG  1 
ATOM   736  C CD1 . TRP   A 1 95  ? 1.454   41.447 29.438  1.00 41.83  ? -102 TRP   A CD1 1 
ATOM   737  C CD2 . TRP   A 1 95  ? 1.792   40.670 27.372  1.00 39.59  ? -102 TRP   A CD2 1 
ATOM   738  N NE1 . TRP   A 1 95  ? 2.654   41.955 28.997  1.00 44.31  ? -102 TRP   A NE1 1 
ATOM   739  C CE2 . TRP   A 1 95  ? 2.891   41.489 27.735  1.00 42.72  ? -102 TRP   A CE2 1 
ATOM   740  C CE3 . TRP   A 1 95  ? 1.778   40.086 26.105  1.00 41.14  ? -102 TRP   A CE3 1 
ATOM   741  C CZ2 . TRP   A 1 95  ? 3.980   41.720 26.874  1.00 43.50  ? -102 TRP   A CZ2 1 
ATOM   742  C CZ3 . TRP   A 1 95  ? 2.855   40.323 25.232  1.00 43.08  ? -102 TRP   A CZ3 1 
ATOM   743  C CH2 . TRP   A 1 95  ? 3.934   41.135 25.622  1.00 43.54  ? -102 TRP   A CH2 1 
ATOM   744  N N   . ASP   A 1 96  ? -3.420  38.961 28.193  1.00 44.57  ? -101 ASP   A N   1 
ATOM   745  C CA  . ASP   A 1 96  ? -4.414  37.895 28.058  1.00 42.73  ? -101 ASP   A CA  1 
ATOM   746  C C   . ASP   A 1 96  ? -5.044  37.903 26.676  1.00 42.41  ? -101 ASP   A C   1 
ATOM   747  O O   . ASP   A 1 96  ? -5.321  36.834 26.113  1.00 40.39  ? -101 ASP   A O   1 
ATOM   748  C CB  . ASP   A 1 96  ? -5.517  38.059 29.112  1.00 44.23  ? -101 ASP   A CB  1 
ATOM   749  C CG  . ASP   A 1 96  ? -5.002  37.864 30.528  1.00 48.19  ? -101 ASP   A CG  1 
ATOM   750  O OD1 . ASP   A 1 96  ? -3.991  37.148 30.725  1.00 48.90  ? -101 ASP   A OD1 1 
ATOM   751  O OD2 . ASP   A 1 96  ? -5.591  38.469 31.451  1.00 50.80  ? -101 ASP   A OD2 1 
ATOM   752  N N   . ALA   A 1 97  ? -5.268  39.130 26.084  1.00 38.14  ? -100 ALA   A N   1 
ATOM   753  C CA  . ALA   A 1 97  ? -5.972  39.200 24.817  1.00 36.38  ? -100 ALA   A CA  1 
ATOM   754  C C   . ALA   A 1 97  ? -5.188  38.581 23.679  1.00 37.60  ? -100 ALA   A C   1 
ATOM   755  O O   . ALA   A 1 97  ? -5.783  38.234 22.643  1.00 39.09  ? -100 ALA   A O   1 
ATOM   756  C CB  . ALA   A 1 97  ? -6.309  40.648 24.477  1.00 35.54  ? -100 ALA   A CB  1 
ATOM   757  N N   . VAL   A 1 98  ? -3.873  38.440 23.825  1.00 36.81  ? -99  VAL   A N   1 
ATOM   758  C CA  . VAL   A 1 98  ? -3.031  37.934 22.766  1.00 37.75  ? -99  VAL   A CA  1 
ATOM   759  C C   . VAL   A 1 98  ? -2.414  36.601 23.181  1.00 42.77  ? -99  VAL   A C   1 
ATOM   760  O O   . VAL   A 1 98  ? -1.361  36.211 22.659  1.00 44.14  ? -99  VAL   A O   1 
ATOM   761  C CB  . VAL   A 1 98  ? -1.949  38.955 22.389  1.00 39.23  ? -99  VAL   A CB  1 
ATOM   762  C CG1 . VAL   A 1 98  ? -2.596  40.240 21.859  1.00 37.79  ? -99  VAL   A CG1 1 
ATOM   763  C CG2 . VAL   A 1 98  ? -1.090  39.265 23.637  1.00 38.54  ? -99  VAL   A CG2 1 
ATOM   764  N N   . ARG   A 1 99  ? -3.038  35.913 24.148  1.00 44.76  ? -98  ARG   A N   1 
ATOM   765  C CA  . ARG   A 1 99  ? -2.630  34.576 24.551  1.00 49.75  ? -98  ARG   A CA  1 
ATOM   766  C C   . ARG   A 1 99  ? -3.544  33.555 23.866  1.00 51.60  ? -98  ARG   A C   1 
ATOM   767  O O   . ARG   A 1 99  ? -4.769  33.651 23.990  1.00 54.51  ? -98  ARG   A O   1 
ATOM   768  C CB  . ARG   A 1 99  ? -2.675  34.425 26.066  1.00 50.66  ? -98  ARG   A CB  1 
ATOM   769  C CG  . ARG   A 1 99  ? -2.116  33.085 26.532  1.00 55.21  ? -98  ARG   A CG  1 
ATOM   770  C CD  . ARG   A 1 99  ? -2.083  33.016 28.068  1.00 59.22  ? -98  ARG   A CD  1 
ATOM   771  N NE  . ARG   A 1 99  ? -1.176  34.015 28.653  1.00 59.73  ? -98  ARG   A NE  1 
ATOM   772  C CZ  . ARG   A 1 99  ? -1.585  35.094 29.326  1.00 58.04  ? -98  ARG   A CZ  1 
ATOM   773  N NH1 . ARG   A 1 99  ? -2.893  35.317 29.510  1.00 57.06  ? -98  ARG   A NH1 1 
ATOM   774  N NH2 . ARG   A 1 99  ? -0.688  35.935 29.828  1.00 57.29  ? -98  ARG   A NH2 1 
ATOM   775  N N   . TYR   A 1 100 ? -2.957  32.613 23.126  1.00 48.93  ? -97  TYR   A N   1 
ATOM   776  C CA  . TYR   A 1 100 ? -3.718  31.610 22.407  1.00 49.19  ? -97  TYR   A CA  1 
ATOM   777  C C   . TYR   A 1 100 ? -3.132  30.242 22.733  1.00 53.56  ? -97  TYR   A C   1 
ATOM   778  O O   . TYR   A 1 100 ? -1.942  29.996 22.503  1.00 53.55  ? -97  TYR   A O   1 
ATOM   779  C CB  . TYR   A 1 100 ? -3.705  31.854 20.896  1.00 46.80  ? -97  TYR   A CB  1 
ATOM   780  C CG  . TYR   A 1 100 ? -4.571  30.884 20.130  1.00 46.21  ? -97  TYR   A CG  1 
ATOM   781  C CD1 . TYR   A 1 100 ? -5.949  30.930 20.214  1.00 44.63  ? -97  TYR   A CD1 1 
ATOM   782  C CD2 . TYR   A 1 100 ? -3.976  29.859 19.348  1.00 50.61  ? -97  TYR   A CD2 1 
ATOM   783  C CE1 . TYR   A 1 100 ? -6.747  29.999 19.537  1.00 47.48  ? -97  TYR   A CE1 1 
ATOM   784  C CE2 . TYR   A 1 100 ? -4.772  28.901 18.669  1.00 49.44  ? -97  TYR   A CE2 1 
ATOM   785  C CZ  . TYR   A 1 100 ? -6.149  28.997 18.770  1.00 50.06  ? -97  TYR   A CZ  1 
ATOM   786  O OH  . TYR   A 1 100 ? -6.930  28.078 18.095  1.00 53.78  ? -97  TYR   A OH  1 
ATOM   787  N N   . ASN   A 1 101 ? -3.971  29.363 23.275  1.00 58.24  ? -96  ASN   A N   1 
ATOM   788  C CA  . ASN   A 1 101 ? -3.545  28.026 23.662  1.00 62.84  ? -96  ASN   A CA  1 
ATOM   789  C C   . ASN   A 1 101 ? -2.296  28.101 24.527  1.00 60.39  ? -96  ASN   A C   1 
ATOM   790  O O   . ASN   A 1 101 ? -1.327  27.375 24.327  1.00 61.62  ? -96  ASN   A O   1 
ATOM   791  C CB  . ASN   A 1 101 ? -3.315  27.139 22.428  1.00 68.06  ? -96  ASN   A CB  1 
ATOM   792  C CG  . ASN   A 1 101 ? -4.617  26.653 21.812  1.00 72.58  ? -96  ASN   A CG  1 
ATOM   793  O OD1 . ASN   A 1 101 ? -5.635  26.543 22.496  1.00 73.78  ? -96  ASN   A OD1 1 
ATOM   794  N ND2 . ASN   A 1 101 ? -4.593  26.365 20.513  1.00 74.88  ? -96  ASN   A ND2 1 
ATOM   795  N N   . GLY   A 1 102 ? -2.330  28.998 25.497  1.00 56.17  ? -95  GLY   A N   1 
ATOM   796  C CA  . GLY   A 1 102 ? -1.271  29.129 26.469  1.00 56.63  ? -95  GLY   A CA  1 
ATOM   797  C C   . GLY   A 1 102 ? -0.025  29.863 26.009  1.00 56.96  ? -95  GLY   A C   1 
ATOM   798  O O   . GLY   A 1 102 ? 0.925   29.986 26.794  1.00 60.32  ? -95  GLY   A O   1 
ATOM   799  N N   . LYS   A 1 103 ? 0.039   30.355 24.774  1.00 54.37  ? -94  LYS   A N   1 
ATOM   800  C CA  . LYS   A 1 103 ? 1.221   31.061 24.303  1.00 52.28  ? -94  LYS   A CA  1 
ATOM   801  C C   . LYS   A 1 103 ? 0.872   32.464 23.847  1.00 50.59  ? -94  LYS   A C   1 
ATOM   802  O O   . LYS   A 1 103 ? -0.211  32.710 23.285  1.00 48.62  ? -94  LYS   A O   1 
ATOM   803  C CB  . LYS   A 1 103 ? 1.912   30.302 23.195  1.00 52.63  ? -94  LYS   A CB  1 
ATOM   804  C CG  . LYS   A 1 103 ? 2.055   28.790 23.525  1.00 55.40  ? -94  LYS   A CG  1 
ATOM   805  C CD  . LYS   A 1 103 ? 3.005   28.063 22.594  1.00 56.89  ? -94  LYS   A CD  1 
ATOM   806  C CE  . LYS   A 1 103 ? 3.643   26.854 23.301  1.00 61.05  ? -94  LYS   A CE  1 
ATOM   807  N NZ  . LYS   A 1 103 ? 5.129   26.901 23.200  1.00 63.35  ? -94  LYS   A NZ  1 
ATOM   808  N N   . LEU   A 1 104 ? 1.775   33.402 24.116  1.00 49.61  ? -93  LEU   A N   1 
ATOM   809  C CA  . LEU   A 1 104 ? 1.628   34.751 23.623  1.00 46.44  ? -93  LEU   A CA  1 
ATOM   810  C C   . LEU   A 1 104 ? 1.957   34.773 22.134  1.00 43.97  ? -93  LEU   A C   1 
ATOM   811  O O   . LEU   A 1 104 ? 3.030   34.313 21.706  1.00 42.71  ? -93  LEU   A O   1 
ATOM   812  C CB  . LEU   A 1 104 ? 2.550   35.689 24.398  1.00 46.20  ? -93  LEU   A CB  1 
ATOM   813  C CG  . LEU   A 1 104 ? 2.351   35.765 25.906  1.00 45.47  ? -93  LEU   A CG  1 
ATOM   814  C CD1 . LEU   A 1 104 ? 3.391   36.679 26.519  1.00 46.01  ? -93  LEU   A CD1 1 
ATOM   815  C CD2 . LEU   A 1 104 ? 0.959   36.266 26.232  1.00 44.44  ? -93  LEU   A CD2 1 
ATOM   816  N N   . ILE   A 1 105 ? 1.028   35.308 21.343  1.00 40.72  ? -92  ILE   A N   1 
ATOM   817  C CA  . ILE   A 1 105 ? 1.166   35.309 19.899  1.00 41.39  ? -92  ILE   A CA  1 
ATOM   818  C C   . ILE   A 1 105 ? 1.240   36.708 19.313  1.00 42.93  ? -92  ILE   A C   1 
ATOM   819  O O   . ILE   A 1 105 ? 1.298   36.859 18.093  1.00 42.40  ? -92  ILE   A O   1 
ATOM   820  C CB  . ILE   A 1 105 ? 0.020   34.510 19.228  1.00 43.78  ? -92  ILE   A CB  1 
ATOM   821  C CG1 . ILE   A 1 105 ? -1.322  35.062 19.690  1.00 46.51  ? -92  ILE   A CG1 1 
ATOM   822  C CG2 . ILE   A 1 105 ? 0.148   33.007 19.569  1.00 47.84  ? -92  ILE   A CG2 1 
ATOM   823  C CD1 . ILE   A 1 105 ? -2.372  35.201 18.563  1.00 50.36  ? -92  ILE   A CD1 1 
ATOM   824  N N   . ALA   A 1 106 ? 1.234   37.750 20.148  1.00 43.75  ? -91  ALA   A N   1 
ATOM   825  C CA  . ALA   A 1 106 ? 1.314   39.111 19.656  1.00 40.39  ? -91  ALA   A CA  1 
ATOM   826  C C   . ALA   A 1 106 ? 1.722   40.049 20.785  1.00 40.01  ? -91  ALA   A C   1 
ATOM   827  O O   . ALA   A 1 106 ? 1.532   39.756 21.964  1.00 39.86  ? -91  ALA   A O   1 
ATOM   828  C CB  . ALA   A 1 106 ? -0.025  39.547 19.053  1.00 38.22  ? -91  ALA   A CB  1 
ATOM   829  N N   . TYR   A 1 107 ? 2.268   41.202 20.399  1.00 37.37  ? -90  TYR   A N   1 
ATOM   830  C CA  . TYR   A 1 107 ? 2.480   42.273 21.364  1.00 40.84  ? -90  TYR   A CA  1 
ATOM   831  C C   . TYR   A 1 107 ? 1.231   43.146 21.411  1.00 40.46  ? -90  TYR   A C   1 
ATOM   832  O O   . TYR   A 1 107 ? 0.837   43.699 20.370  1.00 40.64  ? -90  TYR   A O   1 
ATOM   833  C CB  . TYR   A 1 107 ? 3.687   43.129 20.978  1.00 42.28  ? -90  TYR   A CB  1 
ATOM   834  C CG  . TYR   A 1 107 ? 5.014   42.443 21.184  1.00 42.17  ? -90  TYR   A CG  1 
ATOM   835  C CD1 . TYR   A 1 107 ? 5.654   42.507 22.416  1.00 42.89  ? -90  TYR   A CD1 1 
ATOM   836  C CD2 . TYR   A 1 107 ? 5.627   41.759 20.159  1.00 41.99  ? -90  TYR   A CD2 1 
ATOM   837  C CE1 . TYR   A 1 107 ? 6.884   41.901 22.610  1.00 44.31  ? -90  TYR   A CE1 1 
ATOM   838  C CE2 . TYR   A 1 107 ? 6.867   41.134 20.331  1.00 42.38  ? -90  TYR   A CE2 1 
ATOM   839  C CZ  . TYR   A 1 107 ? 7.483   41.216 21.553  1.00 44.59  ? -90  TYR   A CZ  1 
ATOM   840  O OH  . TYR   A 1 107 ? 8.693   40.610 21.742  1.00 46.69  ? -90  TYR   A OH  1 
ATOM   841  N N   . PRO   A 1 108 ? 0.594   43.322 22.570  1.00 38.93  ? -89  PRO   A N   1 
ATOM   842  C CA  . PRO   A 1 108 ? -0.545  44.224 22.634  1.00 36.29  ? -89  PRO   A CA  1 
ATOM   843  C C   . PRO   A 1 108 ? -0.078  45.682 22.572  1.00 38.56  ? -89  PRO   A C   1 
ATOM   844  O O   . PRO   A 1 108 ? 1.006   46.021 23.046  1.00 42.24  ? -89  PRO   A O   1 
ATOM   845  C CB  . PRO   A 1 108 ? -1.178  43.863 23.976  1.00 33.71  ? -89  PRO   A CB  1 
ATOM   846  C CG  . PRO   A 1 108 ? -0.052  43.425 24.782  1.00 37.33  ? -89  PRO   A CG  1 
ATOM   847  C CD  . PRO   A 1 108 ? 0.905   42.734 23.868  1.00 37.72  ? -89  PRO   A CD  1 
ATOM   848  N N   . ILE   A 1 109 ? -0.899  46.537 21.958  1.00 34.62  ? -88  ILE   A N   1 
ATOM   849  C CA  . ILE   A 1 109 ? -0.509  47.927 21.714  1.00 36.72  ? -88  ILE   A CA  1 
ATOM   850  C C   . ILE   A 1 109 ? -1.479  48.862 22.441  1.00 38.54  ? -88  ILE   A C   1 
ATOM   851  O O   . ILE   A 1 109 ? -1.079  49.610 23.353  1.00 39.85  ? -88  ILE   A O   1 
ATOM   852  C CB  . ILE   A 1 109 ? -0.491  48.245 20.213  1.00 38.56  ? -88  ILE   A CB  1 
ATOM   853  C CG1 . ILE   A 1 109 ? 0.290   47.165 19.428  1.00 41.57  ? -88  ILE   A CG1 1 
ATOM   854  C CG2 . ILE   A 1 109 ? 0.027   49.613 19.973  1.00 40.32  ? -88  ILE   A CG2 1 
ATOM   855  C CD1 . ILE   A 1 109 ? 1.763   47.049 19.797  1.00 42.22  ? -88  ILE   A CD1 1 
ATOM   856  N N   . ALA   A 1 110 ? -2.763  48.783 22.090  1.00 38.66  ? -87  ALA   A N   1 
ATOM   857  C CA  . ALA   A 1 110 ? -3.754  49.731 22.566  1.00 38.85  ? -87  ALA   A CA  1 
ATOM   858  C C   . ALA   A 1 110 ? -5.117  49.069 22.685  1.00 36.57  ? -87  ALA   A C   1 
ATOM   859  O O   . ALA   A 1 110 ? -5.431  48.162 21.937  1.00 37.17  ? -87  ALA   A O   1 
ATOM   860  C CB  . ALA   A 1 110 ? -3.817  50.943 21.627  1.00 38.53  ? -87  ALA   A CB  1 
ATOM   861  N N   . VAL   A 1 111 ? -5.928  49.561 23.607  1.00 36.35  ? -86  VAL   A N   1 
ATOM   862  C CA  . VAL   A 1 111 ? -7.282  49.072 23.821  1.00 36.17  ? -86  VAL   A CA  1 
ATOM   863  C C   . VAL   A 1 111 ? -8.253  50.034 23.107  1.00 36.91  ? -86  VAL   A C   1 
ATOM   864  O O   . VAL   A 1 111 ? -8.245  51.243 23.377  1.00 38.56  ? -86  VAL   A O   1 
ATOM   865  C CB  . VAL   A 1 111 ? -7.596  48.964 25.319  1.00 37.08  ? -86  VAL   A CB  1 
ATOM   866  C CG1 . VAL   A 1 111 ? -9.068  48.557 25.550  1.00 36.54  ? -86  VAL   A CG1 1 
ATOM   867  C CG2 . VAL   A 1 111 ? -6.648  47.991 25.985  1.00 38.57  ? -86  VAL   A CG2 1 
ATOM   868  N N   . GLU   A 1 112 ? -9.093  49.489 22.228  1.00 36.03  ? -85  GLU   A N   1 
ATOM   869  C CA  . GLU   A 1 112 ? -10.037 50.224 21.426  1.00 39.35  ? -85  GLU   A CA  1 
ATOM   870  C C   . GLU   A 1 112 ? -11.465 49.846 21.772  1.00 41.32  ? -85  GLU   A C   1 
ATOM   871  O O   . GLU   A 1 112 ? -11.798 48.641 21.828  1.00 43.92  ? -85  GLU   A O   1 
ATOM   872  C CB  . GLU   A 1 112 ? -9.837  49.963 19.931  1.00 42.13  ? -85  GLU   A CB  1 
ATOM   873  C CG  . GLU   A 1 112 ? -8.403  49.853 19.454  1.00 43.86  ? -85  GLU   A CG  1 
ATOM   874  C CD  . GLU   A 1 112 ? -8.338  49.539 17.976  1.00 40.92  ? -85  GLU   A CD  1 
ATOM   875  O OE1 . GLU   A 1 112 ? -9.298  48.935 17.467  1.00 38.97  ? -85  GLU   A OE1 1 
ATOM   876  O OE2 . GLU   A 1 112 ? -7.343  49.931 17.322  1.00 40.23  ? -85  GLU   A OE2 1 
ATOM   877  N N   . ALA   A 1 113 ? -12.312 50.856 21.968  1.00 37.42  ? -84  ALA   A N   1 
ATOM   878  C CA  . ALA   A 1 113 ? -13.743 50.657 22.153  1.00 35.49  ? -84  ALA   A CA  1 
ATOM   879  C C   . ALA   A 1 113 ? -14.479 51.807 21.468  1.00 37.39  ? -84  ALA   A C   1 
ATOM   880  O O   . ALA   A 1 113 ? -13.960 52.934 21.378  1.00 35.63  ? -84  ALA   A O   1 
ATOM   881  C CB  . ALA   A 1 113 ? -14.147 50.617 23.629  1.00 33.49  ? -84  ALA   A CB  1 
ATOM   882  N N   . LEU   A 1 114 ? -15.657 51.503 20.916  1.00 35.75  ? -83  LEU   A N   1 
ATOM   883  C CA  . LEU   A 1 114 ? -16.466 52.555 20.314  1.00 36.60  ? -83  LEU   A CA  1 
ATOM   884  C C   . LEU   A 1 114 ? -17.076 53.450 21.386  1.00 35.87  ? -83  LEU   A C   1 
ATOM   885  O O   . LEU   A 1 114 ? -17.431 52.988 22.481  1.00 35.37  ? -83  LEU   A O   1 
ATOM   886  C CB  . LEU   A 1 114 ? -17.575 51.940 19.470  1.00 34.85  ? -83  LEU   A CB  1 
ATOM   887  C CG  . LEU   A 1 114 ? -17.110 51.213 18.208  1.00 33.84  ? -83  LEU   A CG  1 
ATOM   888  C CD1 . LEU   A 1 114 ? -18.309 50.442 17.561  1.00 32.30  ? -83  LEU   A CD1 1 
ATOM   889  C CD2 . LEU   A 1 114 ? -16.509 52.224 17.244  1.00 32.86  ? -83  LEU   A CD2 1 
ATOM   890  N N   . SER   A 1 115 ? -17.229 54.748 21.041  1.00 34.40  ? -82  SER   A N   1 
ATOM   891  C CA  . SER   A 1 115 ? -17.972 55.675 21.868  1.00 31.90  ? -82  SER   A CA  1 
ATOM   892  C C   . SER   A 1 115 ? -18.987 56.434 21.020  1.00 32.97  ? -82  SER   A C   1 
ATOM   893  O O   . SER   A 1 115 ? -18.948 56.411 19.806  1.00 34.34  ? -82  SER   A O   1 
ATOM   894  C CB  . SER   A 1 115 ? -17.060 56.662 22.614  1.00 32.95  ? -82  SER   A CB  1 
ATOM   895  O OG  . SER   A 1 115 ? -15.920 56.056 23.178  1.00 36.62  ? -82  SER   A OG  1 
ATOM   896  N N   . LEU   A 1 116 ? -19.903 57.137 21.689  1.00 33.99  ? -81  LEU   A N   1 
ATOM   897  C CA  . LEU   A 1 116 ? -20.740 58.095 20.982  1.00 37.19  ? -81  LEU   A CA  1 
ATOM   898  C C   . LEU   A 1 116 ? -20.001 59.429 20.878  1.00 36.18  ? -81  LEU   A C   1 
ATOM   899  O O   . LEU   A 1 116 ? -19.576 59.959 21.883  1.00 41.82  ? -81  LEU   A O   1 
ATOM   900  C CB  . LEU   A 1 116 ? -22.056 58.274 21.721  1.00 35.95  ? -81  LEU   A CB  1 
ATOM   901  C CG  . LEU   A 1 116 ? -23.062 59.283 21.120  1.00 30.16  ? -81  LEU   A CG  1 
ATOM   902  C CD1 . LEU   A 1 116 ? -23.615 58.691 19.809  1.00 27.13  ? -81  LEU   A CD1 1 
ATOM   903  C CD2 . LEU   A 1 116 ? -24.190 59.570 22.135  1.00 29.30  ? -81  LEU   A CD2 1 
ATOM   904  N N   . ILE   A 1 117 ? -19.775 59.911 19.678  1.00 33.27  ? -80  ILE   A N   1 
ATOM   905  C CA  . ILE   A 1 117 ? -19.161 61.209 19.418  1.00 33.38  ? -80  ILE   A CA  1 
ATOM   906  C C   . ILE   A 1 117 ? -20.276 62.148 18.957  1.00 31.67  ? -80  ILE   A C   1 
ATOM   907  O O   . ILE   A 1 117 ? -21.062 61.786 18.068  1.00 30.57  ? -80  ILE   A O   1 
ATOM   908  C CB  . ILE   A 1 117 ? -18.076 61.113 18.333  1.00 34.26  ? -80  ILE   A CB  1 
ATOM   909  C CG1 . ILE   A 1 117 ? -16.986 60.150 18.747  1.00 32.89  ? -80  ILE   A CG1 1 
ATOM   910  C CG2 . ILE   A 1 117 ? -17.420 62.495 18.074  1.00 37.68  ? -80  ILE   A CG2 1 
ATOM   911  C CD1 . ILE   A 1 117 ? -16.021 59.792 17.581  1.00 30.38  ? -80  ILE   A CD1 1 
ATOM   912  N N   . TYR   A 1 118 ? -20.397 63.300 19.603  1.00 33.07  ? -79  TYR   A N   1 
ATOM   913  C CA  . TYR   A 1 118 ? -21.518 64.188 19.355  1.00 35.29  ? -79  TYR   A CA  1 
ATOM   914  C C   . TYR   A 1 118 ? -21.038 65.638 19.206  1.00 36.34  ? -79  TYR   A C   1 
ATOM   915  O O   . TYR   A 1 118 ? -20.030 66.035 19.772  1.00 38.44  ? -79  TYR   A O   1 
ATOM   916  C CB  . TYR   A 1 118 ? -22.564 64.088 20.469  1.00 35.16  ? -79  TYR   A CB  1 
ATOM   917  C CG  . TYR   A 1 118 ? -22.158 64.700 21.813  1.00 37.70  ? -79  TYR   A CG  1 
ATOM   918  C CD1 . TYR   A 1 118 ? -21.299 64.021 22.688  1.00 36.09  ? -79  TYR   A CD1 1 
ATOM   919  C CD2 . TYR   A 1 118 ? -22.651 65.934 22.203  1.00 40.26  ? -79  TYR   A CD2 1 
ATOM   920  C CE1 . TYR   A 1 118 ? -20.943 64.542 23.882  1.00 39.50  ? -79  TYR   A CE1 1 
ATOM   921  C CE2 . TYR   A 1 118 ? -22.283 66.491 23.420  1.00 43.82  ? -79  TYR   A CE2 1 
ATOM   922  C CZ  . TYR   A 1 118 ? -21.438 65.779 24.259  1.00 45.17  ? -79  TYR   A CZ  1 
ATOM   923  O OH  . TYR   A 1 118 ? -21.062 66.335 25.455  1.00 50.66  ? -79  TYR   A OH  1 
ATOM   924  N N   . ASN   A 1 119 ? -21.775 66.403 18.429  1.00 36.28  ? -78  ASN   A N   1 
ATOM   925  C CA  . ASN   A 1 119 ? -21.451 67.813 18.142  1.00 37.95  ? -78  ASN   A CA  1 
ATOM   926  C C   . ASN   A 1 119 ? -22.074 68.701 19.223  1.00 39.33  ? -78  ASN   A C   1 
ATOM   927  O O   . ASN   A 1 119 ? -23.304 68.813 19.331  1.00 38.93  ? -78  ASN   A O   1 
ATOM   928  C CB  . ASN   A 1 119 ? -21.942 68.179 16.746  1.00 36.45  ? -78  ASN   A CB  1 
ATOM   929  C CG  . ASN   A 1 119 ? -21.657 69.622 16.381  1.00 40.14  ? -78  ASN   A CG  1 
ATOM   930  O OD1 . ASN   A 1 119 ? -21.774 70.553 17.225  1.00 42.04  ? -78  ASN   A OD1 1 
ATOM   931  N ND2 . ASN   A 1 119 ? -21.347 69.852 15.117  1.00 33.92  ? -78  ASN   A ND2 1 
ATOM   932  N N   . LYS   A 1 120 ? -21.225 69.301 20.056  1.00 40.36  ? -77  LYS   A N   1 
ATOM   933  C CA  . LYS   A 1 120 ? -21.713 70.082 21.179  1.00 43.56  ? -77  LYS   A CA  1 
ATOM   934  C C   . LYS   A 1 120 ? -22.437 71.367 20.753  1.00 46.52  ? -77  LYS   A C   1 
ATOM   935  O O   . LYS   A 1 120 ? -23.125 71.977 21.587  1.00 49.77  ? -77  LYS   A O   1 
ATOM   936  C CB  . LYS   A 1 120 ? -20.546 70.451 22.111  1.00 46.94  ? -77  LYS   A CB  1 
ATOM   937  C CG  . LYS   A 1 120 ? -19.839 69.322 22.776  1.00 47.70  ? -77  LYS   A CG  1 
ATOM   938  C CD  . LYS   A 1 120 ? -18.767 69.878 23.719  1.00 53.17  ? -77  LYS   A CD  1 
ATOM   939  C CE  . LYS   A 1 120 ? -18.106 68.785 24.579  1.00 54.12  ? -77  LYS   A CE  1 
ATOM   940  N NZ  . LYS   A 1 120 ? -17.154 69.397 25.584  1.00 57.34  ? -77  LYS   A NZ  1 
ATOM   941  N N   . ASP   A 1 121 ? -22.293 71.797 19.493  1.00 42.88  ? -76  ASP   A N   1 
ATOM   942  C CA  . ASP   A 1 121 ? -23.007 72.990 19.066  1.00 45.89  ? -76  ASP   A CA  1 
ATOM   943  C C   . ASP   A 1 121 ? -24.434 72.682 18.623  1.00 48.35  ? -76  ASP   A C   1 
ATOM   944  O O   . ASP   A 1 121 ? -25.280 73.596 18.669  1.00 52.40  ? -76  ASP   A O   1 
ATOM   945  C CB  . ASP   A 1 121 ? -22.251 73.704 17.944  1.00 44.09  ? -76  ASP   A CB  1 
ATOM   946  C CG  . ASP   A 1 121 ? -20.991 74.392 18.445  1.00 47.30  ? -76  ASP   A CG  1 
ATOM   947  O OD1 . ASP   A 1 121 ? -20.860 74.629 19.664  1.00 49.09  ? -76  ASP   A OD1 1 
ATOM   948  O OD2 . ASP   A 1 121 ? -20.094 74.674 17.626  1.00 48.60  ? -76  ASP   A OD2 1 
ATOM   949  N N   . LEU   A 1 122 ? -24.714 71.448 18.203  1.00 43.98  ? -75  LEU   A N   1 
ATOM   950  C CA  . LEU   A 1 122 ? -26.065 71.016 17.853  1.00 42.70  ? -75  LEU   A CA  1 
ATOM   951  C C   . LEU   A 1 122 ? -26.792 70.338 18.996  1.00 45.07  ? -75  LEU   A C   1 
ATOM   952  O O   . LEU   A 1 122 ? -27.996 70.584 19.172  1.00 47.27  ? -75  LEU   A O   1 
ATOM   953  C CB  . LEU   A 1 122 ? -26.057 70.041 16.654  1.00 36.84  ? -75  LEU   A CB  1 
ATOM   954  C CG  . LEU   A 1 122 ? -25.301 70.439 15.399  1.00 39.94  ? -75  LEU   A CG  1 
ATOM   955  C CD1 . LEU   A 1 122 ? -25.332 69.269 14.368  1.00 41.61  ? -75  LEU   A CD1 1 
ATOM   956  C CD2 . LEU   A 1 122 ? -25.854 71.710 14.799  1.00 40.93  ? -75  LEU   A CD2 1 
ATOM   957  N N   . LEU   A 1 123 ? -26.091 69.468 19.753  1.00 43.01  ? -74  LEU   A N   1 
ATOM   958  C CA  . LEU   A 1 123 ? -26.642 68.730 20.876  1.00 40.47  ? -74  LEU   A CA  1 
ATOM   959  C C   . LEU   A 1 123 ? -25.758 68.972 22.095  1.00 39.77  ? -74  LEU   A C   1 
ATOM   960  O O   . LEU   A 1 123 ? -24.859 68.174 22.388  1.00 40.15  ? -74  LEU   A O   1 
ATOM   961  C CB  . LEU   A 1 123 ? -26.710 67.228 20.580  1.00 42.56  ? -74  LEU   A CB  1 
ATOM   962  C CG  . LEU   A 1 123 ? -27.692 66.632 19.566  1.00 42.30  ? -74  LEU   A CG  1 
ATOM   963  C CD1 . LEU   A 1 123 ? -27.326 65.170 19.325  1.00 41.38  ? -74  LEU   A CD1 1 
ATOM   964  C CD2 . LEU   A 1 123 ? -29.115 66.755 20.086  1.00 41.88  ? -74  LEU   A CD2 1 
ATOM   965  N N   . PRO   A 1 124 ? -25.991 70.035 22.846  1.00 40.45  ? -73  PRO   A N   1 
ATOM   966  C CA  . PRO   A 1 124 ? -25.268 70.193 24.114  1.00 44.57  ? -73  PRO   A CA  1 
ATOM   967  C C   . PRO   A 1 124 ? -25.505 69.053 25.092  1.00 46.68  ? -73  PRO   A C   1 
ATOM   968  O O   . PRO   A 1 124 ? -24.700 68.869 26.026  1.00 46.01  ? -73  PRO   A O   1 
ATOM   969  C CB  . PRO   A 1 124 ? -25.809 71.507 24.674  1.00 42.51  ? -73  PRO   A CB  1 
ATOM   970  C CG  . PRO   A 1 124 ? -27.117 71.673 23.981  1.00 41.69  ? -73  PRO   A CG  1 
ATOM   971  C CD  . PRO   A 1 124 ? -26.938 71.136 22.614  1.00 39.62  ? -73  PRO   A CD  1 
ATOM   972  N N   . ASN   A 1 125 ? -26.594 68.301 24.919  1.00 49.49  ? -72  ASN   A N   1 
ATOM   973  C CA  . ASN   A 1 125 ? -26.910 67.161 25.788  1.00 51.53  ? -72  ASN   A CA  1 
ATOM   974  C C   . ASN   A 1 125 ? -27.184 65.944 24.932  1.00 49.35  ? -72  ASN   A C   1 
ATOM   975  O O   . ASN   A 1 125 ? -28.276 65.814 24.357  1.00 46.48  ? -72  ASN   A O   1 
ATOM   976  C CB  . ASN   A 1 125 ? -28.104 67.510 26.681  1.00 54.38  ? -72  ASN   A CB  1 
ATOM   977  C CG  . ASN   A 1 125 ? -27.705 68.393 27.829  1.00 55.71  ? -72  ASN   A CG  1 
ATOM   978  O OD1 . ASN   A 1 125 ? -26.735 68.088 28.538  1.00 56.06  ? -72  ASN   A OD1 1 
ATOM   979  N ND2 . ASN   A 1 125 ? -28.410 69.508 28.005  1.00 57.29  ? -72  ASN   A ND2 1 
ATOM   980  N N   . PRO   A 1 126 ? -26.216 65.036 24.818  1.00 53.77  ? -71  PRO   A N   1 
ATOM   981  C CA  . PRO   A 1 126 ? -26.418 63.860 23.983  1.00 52.43  ? -71  PRO   A CA  1 
ATOM   982  C C   . PRO   A 1 126 ? -27.467 62.920 24.567  1.00 48.55  ? -71  PRO   A C   1 
ATOM   983  O O   . PRO   A 1 126 ? -27.606 62.814 25.790  1.00 46.79  ? -71  PRO   A O   1 
ATOM   984  C CB  . PRO   A 1 126 ? -25.033 63.196 23.970  1.00 55.45  ? -71  PRO   A CB  1 
ATOM   985  C CG  . PRO   A 1 126 ? -24.406 63.642 25.253  1.00 57.25  ? -71  PRO   A CG  1 
ATOM   986  C CD  . PRO   A 1 126 ? -24.898 65.043 25.474  1.00 57.23  ? -71  PRO   A CD  1 
ATOM   987  N N   . PRO   A 1 127 ? -28.194 62.187 23.716  1.00 46.39  ? -70  PRO   A N   1 
ATOM   988  C CA  . PRO   A 1 127 ? -29.235 61.285 24.229  1.00 46.13  ? -70  PRO   A CA  1 
ATOM   989  C C   . PRO   A 1 127 ? -28.634 60.134 25.050  1.00 42.46  ? -70  PRO   A C   1 
ATOM   990  O O   . PRO   A 1 127 ? -27.568 59.601 24.736  1.00 40.89  ? -70  PRO   A O   1 
ATOM   991  C CB  . PRO   A 1 127 ? -29.912 60.758 22.955  1.00 46.67  ? -70  PRO   A CB  1 
ATOM   992  C CG  . PRO   A 1 127 ? -28.814 60.840 21.889  1.00 44.48  ? -70  PRO   A CG  1 
ATOM   993  C CD  . PRO   A 1 127 ? -28.010 62.071 22.256  1.00 45.05  ? -70  PRO   A CD  1 
ATOM   994  N N   . LYS   A 1 128 ? -29.319 59.765 26.103  1.00 40.67  ? -69  LYS   A N   1 
ATOM   995  C CA  . LYS   A 1 128 ? -28.881 58.650 26.894  1.00 45.12  ? -69  LYS   A CA  1 
ATOM   996  C C   . LYS   A 1 128 ? -29.449 57.318 26.380  1.00 41.56  ? -69  LYS   A C   1 
ATOM   997  O O   . LYS   A 1 128 ? -28.898 56.284 26.684  1.00 39.63  ? -69  LYS   A O   1 
ATOM   998  C CB  . LYS   A 1 128 ? -29.239 58.861 28.377  1.00 48.39  ? -69  LYS   A CB  1 
ATOM   999  C CG  . LYS   A 1 128 ? -28.136 59.634 29.118  1.00 54.69  ? -69  LYS   A CG  1 
ATOM   1000 C CD  . LYS   A 1 128 ? -28.655 60.203 30.419  1.00 59.78  ? -69  LYS   A CD  1 
ATOM   1001 C CE  . LYS   A 1 128 ? -27.806 61.363 30.894  1.00 62.83  ? -69  LYS   A CE  1 
ATOM   1002 N NZ  . LYS   A 1 128 ? -28.638 62.638 31.107  1.00 65.52  ? -69  LYS   A NZ  1 
ATOM   1003 N N   . THR   A 1 129 ? -30.529 57.364 25.611  1.00 42.56  ? -68  THR   A N   1 
ATOM   1004 C CA  . THR   A 1 129 ? -31.228 56.193 25.114  1.00 40.00  ? -68  THR   A CA  1 
ATOM   1005 C C   . THR   A 1 129 ? -31.255 56.219 23.598  1.00 39.05  ? -68  THR   A C   1 
ATOM   1006 O O   . THR   A 1 129 ? -31.380 57.298 22.979  1.00 38.36  ? -68  THR   A O   1 
ATOM   1007 C CB  . THR   A 1 129 ? -32.666 56.122 25.648  1.00 40.30  ? -68  THR   A CB  1 
ATOM   1008 O OG1 . THR   A 1 129 ? -33.492 57.031 24.905  1.00 40.90  ? -68  THR   A OG1 1 
ATOM   1009 C CG2 . THR   A 1 129 ? -32.720 56.449 27.122  1.00 39.96  ? -68  THR   A CG2 1 
ATOM   1010 N N   . TRP   A 1 130 ? -31.152 55.017 22.986  1.00 35.46  ? -67  TRP   A N   1 
ATOM   1011 C CA  . TRP   A 1 130 ? -31.404 54.894 21.555  1.00 32.24  ? -67  TRP   A CA  1 
ATOM   1012 C C   . TRP   A 1 130 ? -32.841 55.259 21.213  1.00 32.85  ? -67  TRP   A C   1 
ATOM   1013 O O   . TRP   A 1 130 ? -33.103 55.774 20.125  1.00 32.12  ? -67  TRP   A O   1 
ATOM   1014 C CB  . TRP   A 1 130 ? -31.141 53.446 21.098  1.00 31.40  ? -67  TRP   A CB  1 
ATOM   1015 C CG  . TRP   A 1 130 ? -29.713 53.085 20.856  1.00 30.84  ? -67  TRP   A CG  1 
ATOM   1016 C CD1 . TRP   A 1 130 ? -28.816 52.525 21.746  1.00 28.93  ? -67  TRP   A CD1 1 
ATOM   1017 C CD2 . TRP   A 1 130 ? -28.996 53.246 19.609  1.00 31.30  ? -67  TRP   A CD2 1 
ATOM   1018 N NE1 . TRP   A 1 130 ? -27.598 52.320 21.122  1.00 28.09  ? -67  TRP   A NE1 1 
ATOM   1019 C CE2 . TRP   A 1 130 ? -27.676 52.743 19.819  1.00 30.37  ? -67  TRP   A CE2 1 
ATOM   1020 C CE3 . TRP   A 1 130 ? -29.343 53.774 18.350  1.00 30.55  ? -67  TRP   A CE3 1 
ATOM   1021 C CZ2 . TRP   A 1 130 ? -26.717 52.753 18.819  1.00 31.46  ? -67  TRP   A CZ2 1 
ATOM   1022 C CZ3 . TRP   A 1 130 ? -28.388 53.776 17.347  1.00 30.38  ? -67  TRP   A CZ3 1 
ATOM   1023 C CH2 . TRP   A 1 130 ? -27.086 53.286 17.589  1.00 31.37  ? -67  TRP   A CH2 1 
ATOM   1024 N N   . GLU   A 1 131 ? -33.786 54.923 22.109  1.00 36.64  ? -66  GLU   A N   1 
ATOM   1025 C CA  . GLU   A 1 131 ? -35.227 55.131 21.864  1.00 42.10  ? -66  GLU   A CA  1 
ATOM   1026 C C   . GLU   A 1 131 ? -35.588 56.585 21.557  1.00 46.16  ? -66  GLU   A C   1 
ATOM   1027 O O   . GLU   A 1 131 ? -36.574 56.852 20.845  1.00 47.47  ? -66  GLU   A O   1 
ATOM   1028 C CB  . GLU   A 1 131 ? -36.038 54.671 23.089  1.00 43.59  ? -66  GLU   A CB  1 
ATOM   1029 C CG  . GLU   A 1 131 ? -36.193 53.155 23.168  1.00 44.42  ? -66  GLU   A CG  1 
ATOM   1030 C CD  . GLU   A 1 131 ? -35.045 52.471 23.880  1.00 43.47  ? -66  GLU   A CD  1 
ATOM   1031 O OE1 . GLU   A 1 131 ? -34.018 53.116 24.153  1.00 43.76  ? -66  GLU   A OE1 1 
ATOM   1032 O OE2 . GLU   A 1 131 ? -35.186 51.271 24.165  1.00 46.19  ? -66  GLU   A OE2 1 
ATOM   1033 N N   . GLU   A 1 132 ? -34.839 57.541 22.102  1.00 46.18  ? -65  GLU   A N   1 
ATOM   1034 C CA  . GLU   A 1 132 ? -35.162 58.953 21.899  1.00 42.24  ? -65  GLU   A CA  1 
ATOM   1035 C C   . GLU   A 1 132 ? -34.509 59.541 20.659  1.00 43.79  ? -65  GLU   A C   1 
ATOM   1036 O O   . GLU   A 1 132 ? -34.662 60.750 20.397  1.00 44.04  ? -65  GLU   A O   1 
ATOM   1037 C CB  . GLU   A 1 132 ? -34.744 59.764 23.137  1.00 38.91  ? -65  GLU   A CB  1 
ATOM   1038 C CG  . GLU   A 1 132 ? -33.264 59.952 23.265  1.00 37.70  ? -65  GLU   A CG  1 
ATOM   1039 C CD  . GLU   A 1 132 ? -32.877 60.299 24.679  1.00 43.00  ? -65  GLU   A CD  1 
ATOM   1040 O OE1 . GLU   A 1 132 ? -32.595 59.359 25.461  1.00 42.54  ? -65  GLU   A OE1 1 
ATOM   1041 O OE2 . GLU   A 1 132 ? -32.830 61.548 25.022  1.00 45.80  ? -65  GLU   A OE2 1 
ATOM   1042 N N   . ILE   A 1 133 ? -33.804 58.736 19.864  1.00 43.26  ? -64  ILE   A N   1 
ATOM   1043 C CA  . ILE   A 1 133 ? -33.082 59.299 18.728  1.00 42.64  ? -64  ILE   A CA  1 
ATOM   1044 C C   . ILE   A 1 133 ? -34.033 59.677 17.579  1.00 40.86  ? -64  ILE   A C   1 
ATOM   1045 O O   . ILE   A 1 133 ? -33.826 60.718 16.929  1.00 39.44  ? -64  ILE   A O   1 
ATOM   1046 C CB  . ILE   A 1 133 ? -31.983 58.340 18.264  1.00 43.93  ? -64  ILE   A CB  1 
ATOM   1047 C CG1 . ILE   A 1 133 ? -30.893 58.263 19.335  1.00 42.33  ? -64  ILE   A CG1 1 
ATOM   1048 C CG2 . ILE   A 1 133 ? -31.378 58.813 16.908  1.00 42.02  ? -64  ILE   A CG2 1 
ATOM   1049 C CD1 . ILE   A 1 133 ? -29.584 57.642 18.811  1.00 41.20  ? -64  ILE   A CD1 1 
ATOM   1050 N N   . PRO   A 1 134 ? -35.085 58.885 17.299  1.00 39.30  ? -63  PRO   A N   1 
ATOM   1051 C CA  . PRO   A 1 134 ? -36.042 59.302 16.258  1.00 40.17  ? -63  PRO   A CA  1 
ATOM   1052 C C   . PRO   A 1 134 ? -36.644 60.686 16.494  1.00 42.50  ? -63  PRO   A C   1 
ATOM   1053 O O   . PRO   A 1 134 ? -36.705 61.499 15.571  1.00 45.12  ? -63  PRO   A O   1 
ATOM   1054 C CB  . PRO   A 1 134 ? -37.102 58.186 16.303  1.00 40.25  ? -63  PRO   A CB  1 
ATOM   1055 C CG  . PRO   A 1 134 ? -36.330 56.990 16.708  1.00 40.55  ? -63  PRO   A CG  1 
ATOM   1056 C CD  . PRO   A 1 134 ? -35.277 57.481 17.690  1.00 40.90  ? -63  PRO   A CD  1 
ATOM   1057 N N   . ALA   A 1 135 ? -37.089 60.977 17.709  1.00 41.00  ? -62  ALA   A N   1 
ATOM   1058 C CA  . ALA   A 1 135 ? -37.684 62.273 17.974  1.00 38.64  ? -62  ALA   A CA  1 
ATOM   1059 C C   . ALA   A 1 135 ? -36.642 63.375 17.865  1.00 41.37  ? -62  ALA   A C   1 
ATOM   1060 O O   . ALA   A 1 135 ? -36.935 64.462 17.317  1.00 43.90  ? -62  ALA   A O   1 
ATOM   1061 C CB  . ALA   A 1 135 ? -38.337 62.291 19.348  1.00 38.87  ? -62  ALA   A CB  1 
ATOM   1062 N N   . LEU   A 1 136 ? -35.426 63.140 18.364  1.00 36.95  ? -61  LEU   A N   1 
ATOM   1063 C CA  . LEU   A 1 136 ? -34.354 64.096 18.166  1.00 36.40  ? -61  LEU   A CA  1 
ATOM   1064 C C   . LEU   A 1 136 ? -34.060 64.328 16.676  1.00 41.18  ? -61  LEU   A C   1 
ATOM   1065 O O   . LEU   A 1 136 ? -33.832 65.475 16.247  1.00 45.68  ? -61  LEU   A O   1 
ATOM   1066 C CB  . LEU   A 1 136 ? -33.117 63.663 18.907  1.00 37.06  ? -61  LEU   A CB  1 
ATOM   1067 C CG  . LEU   A 1 136 ? -31.978 64.675 18.822  1.00 45.03  ? -61  LEU   A CG  1 
ATOM   1068 C CD1 . LEU   A 1 136 ? -32.245 65.852 19.790  1.00 45.70  ? -61  LEU   A CD1 1 
ATOM   1069 C CD2 . LEU   A 1 136 ? -30.654 63.974 19.158  1.00 47.54  ? -61  LEU   A CD2 1 
ATOM   1070 N N   . ASP   A 1 137 ? -34.097 63.252 15.887  1.00 40.04  ? -60  ASP   A N   1 
ATOM   1071 C CA  . ASP   A 1 137 ? -33.871 63.427 14.458  1.00 40.09  ? -60  ASP   A CA  1 
ATOM   1072 C C   . ASP   A 1 137 ? -34.960 64.281 13.828  1.00 39.25  ? -60  ASP   A C   1 
ATOM   1073 O O   . ASP   A 1 137 ? -34.663 65.095 12.990  1.00 40.52  ? -60  ASP   A O   1 
ATOM   1074 C CB  . ASP   A 1 137 ? -33.796 62.068 13.741  1.00 38.98  ? -60  ASP   A CB  1 
ATOM   1075 C CG  . ASP   A 1 137 ? -33.383 62.217 12.286  1.00 39.16  ? -60  ASP   A CG  1 
ATOM   1076 O OD1 . ASP   A 1 137 ? -32.231 62.681 12.050  1.00 38.60  ? -60  ASP   A OD1 1 
ATOM   1077 O OD2 . ASP   A 1 137 ? -34.192 61.890 11.366  1.00 38.46  ? -60  ASP   A OD2 1 
ATOM   1078 N N   . LYS   A 1 138 ? -36.222 64.065 14.197  1.00 42.21  ? -59  LYS   A N   1 
ATOM   1079 C CA  . LYS   A 1 138 ? -37.305 64.949 13.741  1.00 44.92  ? -59  LYS   A CA  1 
ATOM   1080 C C   . LYS   A 1 138 ? -37.008 66.407 14.106  1.00 42.47  ? -59  LYS   A C   1 
ATOM   1081 O O   . LYS   A 1 138 ? -37.176 67.310 13.282  1.00 44.08  ? -59  LYS   A O   1 
ATOM   1082 C CB  . LYS   A 1 138 ? -38.641 64.523 14.374  1.00 49.17  ? -59  LYS   A CB  1 
ATOM   1083 C CG  . LYS   A 1 138 ? -39.373 63.446 13.624  1.00 54.22  ? -59  LYS   A CG  1 
ATOM   1084 C CD  . LYS   A 1 138 ? -40.498 62.840 14.479  1.00 57.46  ? -59  LYS   A CD  1 
ATOM   1085 C CE  . LYS   A 1 138 ? -40.579 61.287 14.314  1.00 56.10  ? -59  LYS   A CE  1 
ATOM   1086 N NZ  . LYS   A 1 138 ? -40.995 60.643 15.610  1.00 56.13  ? -59  LYS   A NZ  1 
ATOM   1087 N N   . GLU   A 1 139 ? -36.512 66.613 15.321  1.00 37.97  ? -58  GLU   A N   1 
ATOM   1088 C CA  . GLU   A 1 139 ? -36.170 67.947 15.798  1.00 40.72  ? -58  GLU   A CA  1 
ATOM   1089 C C   . GLU   A 1 139 ? -35.028 68.571 14.994  1.00 37.52  ? -58  GLU   A C   1 
ATOM   1090 O O   . GLU   A 1 139 ? -35.075 69.755 14.661  1.00 39.10  ? -58  GLU   A O   1 
ATOM   1091 C CB  . GLU   A 1 139 ? -35.805 67.907 17.283  1.00 43.00  ? -58  GLU   A CB  1 
ATOM   1092 C CG  . GLU   A 1 139 ? -35.861 69.260 17.973  1.00 44.90  ? -58  GLU   A CG  1 
ATOM   1093 C CD  . GLU   A 1 139 ? -37.240 69.886 17.917  1.00 45.95  ? -58  GLU   A CD  1 
ATOM   1094 O OE1 . GLU   A 1 139 ? -37.351 71.042 17.458  1.00 47.31  ? -58  GLU   A OE1 1 
ATOM   1095 O OE2 . GLU   A 1 139 ? -38.213 69.222 18.331  1.00 45.20  ? -58  GLU   A OE2 1 
ATOM   1096 N N   . LEU   A 1 140 ? -34.005 67.778 14.684  1.00 37.82  ? -57  LEU   A N   1 
ATOM   1097 C CA  . LEU   A 1 140 ? -32.868 68.286 13.927  1.00 36.83  ? -57  LEU   A CA  1 
ATOM   1098 C C   . LEU   A 1 140 ? -33.198 68.405 12.435  1.00 39.05  ? -57  LEU   A C   1 
ATOM   1099 O O   . LEU   A 1 140 ? -32.721 69.316 11.771  1.00 41.49  ? -57  LEU   A O   1 
ATOM   1100 C CB  . LEU   A 1 140 ? -31.647 67.376 14.151  1.00 33.26  ? -57  LEU   A CB  1 
ATOM   1101 C CG  . LEU   A 1 140 ? -30.992 67.536 15.518  1.00 34.46  ? -57  LEU   A CG  1 
ATOM   1102 C CD1 . LEU   A 1 140 ? -30.105 66.313 15.791  1.00 33.62  ? -57  LEU   A CD1 1 
ATOM   1103 C CD2 . LEU   A 1 140 ? -30.182 68.823 15.627  1.00 33.42  ? -57  LEU   A CD2 1 
ATOM   1104 N N   . LYS   A 1 141 ? -33.964 67.465 11.869  1.00 38.51  ? -56  LYS   A N   1 
ATOM   1105 C CA  . LYS   A 1 141 ? -34.313 67.570 10.459  1.00 40.66  ? -56  LYS   A CA  1 
ATOM   1106 C C   . LYS   A 1 141 ? -34.976 68.930 10.170  1.00 43.56  ? -56  LYS   A C   1 
ATOM   1107 O O   . LYS   A 1 141 ? -34.694 69.593 9.171   1.00 42.69  ? -56  LYS   A O   1 
ATOM   1108 C CB  . LYS   A 1 141 ? -35.239 66.418 10.055  1.00 39.11  ? -56  LYS   A CB  1 
ATOM   1109 C CG  . LYS   A 1 141 ? -34.534 65.045 9.893   1.00 37.49  ? -56  LYS   A CG  1 
ATOM   1110 C CD  . LYS   A 1 141 ? -34.035 64.837 8.458   1.00 38.29  ? -56  LYS   A CD  1 
ATOM   1111 C CE  . LYS   A 1 141 ? -32.954 63.757 8.398   1.00 39.25  ? -56  LYS   A CE  1 
ATOM   1112 N NZ  . LYS   A 1 141 ? -33.486 62.364 8.678   1.00 37.63  ? -56  LYS   A NZ  1 
ATOM   1113 N N   . ALA   A 1 142 ? -35.854 69.363 11.051  1.00 48.23  ? -55  ALA   A N   1 
ATOM   1114 C CA  . ALA   A 1 142 ? -36.527 70.648 10.862  1.00 48.96  ? -55  ALA   A CA  1 
ATOM   1115 C C   . ALA   A 1 142 ? -35.545 71.801 10.816  1.00 48.84  ? -55  ALA   A C   1 
ATOM   1116 O O   . ALA   A 1 142 ? -35.878 72.849 10.261  1.00 49.62  ? -55  ALA   A O   1 
ATOM   1117 C CB  . ALA   A 1 142 ? -37.546 70.861 11.970  1.00 48.74  ? -55  ALA   A CB  1 
ATOM   1118 N N   . LYS   A 1 143 ? -34.340 71.619 11.348  1.00 48.05  ? -54  LYS   A N   1 
ATOM   1119 C CA  . LYS   A 1 143 ? -33.275 72.610 11.255  1.00 51.80  ? -54  LYS   A CA  1 
ATOM   1120 C C   . LYS   A 1 143 ? -32.282 72.292 10.152  1.00 49.15  ? -54  LYS   A C   1 
ATOM   1121 O O   . LYS   A 1 143 ? -31.234 72.945 10.093  1.00 50.01  ? -54  LYS   A O   1 
ATOM   1122 C CB  . LYS   A 1 143 ? -32.498 72.708 12.599  1.00 53.63  ? -54  LYS   A CB  1 
ATOM   1123 C CG  . LYS   A 1 143 ? -33.339 72.920 13.843  1.00 52.79  ? -54  LYS   A CG  1 
ATOM   1124 C CD  . LYS   A 1 143 ? -32.493 72.623 15.074  1.00 51.11  ? -54  LYS   A CD  1 
ATOM   1125 C CE  . LYS   A 1 143 ? -33.293 72.793 16.353  1.00 53.29  ? -54  LYS   A CE  1 
ATOM   1126 N NZ  . LYS   A 1 143 ? -33.527 74.237 16.648  1.00 57.68  ? -54  LYS   A NZ  1 
ATOM   1127 N N   . GLY   A 1 144 ? -32.568 71.304 9.299   1.00 43.74  ? -53  GLY   A N   1 
ATOM   1128 C CA  . GLY   A 1 144 ? -31.664 70.988 8.208   1.00 41.94  ? -53  GLY   A CA  1 
ATOM   1129 C C   . GLY   A 1 144 ? -30.491 70.112 8.595   1.00 40.07  ? -53  GLY   A C   1 
ATOM   1130 O O   . GLY   A 1 144 ? -29.514 69.988 7.840   1.00 35.69  ? -53  GLY   A O   1 
ATOM   1131 N N   . LYS   A 1 145 ? -30.587 69.431 9.734   1.00 40.03  ? -52  LYS   A N   1 
ATOM   1132 C CA  . LYS   A 1 145 ? -29.561 68.524 10.216  1.00 38.24  ? -52  LYS   A CA  1 
ATOM   1133 C C   . LYS   A 1 145 ? -30.166 67.146 10.401  1.00 35.99  ? -52  LYS   A C   1 
ATOM   1134 O O   . LYS   A 1 145 ? -31.377 66.947 10.261  1.00 37.37  ? -52  LYS   A O   1 
ATOM   1135 C CB  . LYS   A 1 145 ? -28.929 69.043 11.525  1.00 36.47  ? -52  LYS   A CB  1 
ATOM   1136 C CG  . LYS   A 1 145 ? -28.424 70.496 11.427  1.00 36.75  ? -52  LYS   A CG  1 
ATOM   1137 C CD  . LYS   A 1 145 ? -27.024 70.527 10.784  1.00 36.81  ? -52  LYS   A CD  1 
ATOM   1138 C CE  . LYS   A 1 145 ? -26.601 72.056 10.543  1.00 40.12  ? -52  LYS   A CE  1 
ATOM   1139 N NZ  . LYS   A 1 145 ? -25.263 72.061 9.859   1.00 39.90  ? -52  LYS   A NZ  1 
ATOM   1140 N N   . SER   A 1 146 ? -29.318 66.197 10.813  1.00 33.92  ? -51  SER   A N   1 
ATOM   1141 C CA  . SER   A 1 146 ? -29.802 64.893 11.211  1.00 32.68  ? -51  SER   A CA  1 
ATOM   1142 C C   . SER   A 1 146 ? -29.165 64.520 12.549  1.00 35.05  ? -51  SER   A C   1 
ATOM   1143 O O   . SER   A 1 146 ? -28.142 65.108 12.967  1.00 36.52  ? -51  SER   A O   1 
ATOM   1144 C CB  . SER   A 1 146 ? -29.476 63.837 10.102  1.00 29.78  ? -51  SER   A CB  1 
ATOM   1145 O OG  . SER   A 1 146 ? -28.093 63.496 10.130  1.00 32.29  ? -51  SER   A OG  1 
ATOM   1146 N N   . ALA   A 1 147 ? -29.774 63.535 13.214  1.00 35.03  ? -50  ALA   A N   1 
ATOM   1147 C CA  . ALA   A 1 147 ? -29.337 63.151 14.559  1.00 33.91  ? -50  ALA   A CA  1 
ATOM   1148 C C   . ALA   A 1 147 ? -28.028 62.359 14.504  1.00 34.18  ? -50  ALA   A C   1 
ATOM   1149 O O   . ALA   A 1 147 ? -27.054 62.709 15.202  1.00 32.32  ? -50  ALA   A O   1 
ATOM   1150 C CB  . ALA   A 1 147 ? -30.429 62.325 15.252  1.00 30.89  ? -50  ALA   A CB  1 
ATOM   1151 N N   . LEU   A 1 148 ? -27.980 61.268 13.692  1.00 32.41  ? -49  LEU   A N   1 
ATOM   1152 C CA  . LEU   A 1 148 ? -26.905 60.285 13.851  1.00 35.56  ? -49  LEU   A CA  1 
ATOM   1153 C C   . LEU   A 1 148 ? -26.583 59.574 12.532  1.00 37.56  ? -49  LEU   A C   1 
ATOM   1154 O O   . LEU   A 1 148 ? -27.486 59.115 11.806  1.00 35.95  ? -49  LEU   A O   1 
ATOM   1155 C CB  . LEU   A 1 148 ? -27.315 59.210 14.888  1.00 35.63  ? -49  LEU   A CB  1 
ATOM   1156 C CG  . LEU   A 1 148 ? -26.488 57.894 14.919  1.00 31.61  ? -49  LEU   A CG  1 
ATOM   1157 C CD1 . LEU   A 1 148 ? -25.064 58.175 15.579  1.00 28.89  ? -49  LEU   A CD1 1 
ATOM   1158 C CD2 . LEU   A 1 148 ? -27.204 56.774 15.666  1.00 27.33  ? -49  LEU   A CD2 1 
ATOM   1159 N N   . MET   A 1 149 ? -25.282 59.484 12.221  1.00 38.36  ? -48  MET   A N   1 
ATOM   1160 C CA  . MET   A 1 149 ? -24.815 58.734 11.050  1.00 38.08  ? -48  MET   A CA  1 
ATOM   1161 C C   . MET   A 1 149 ? -23.559 57.969 11.452  1.00 38.79  ? -48  MET   A C   1 
ATOM   1162 O O   . MET   A 1 149 ? -22.641 58.559 12.034  1.00 37.76  ? -48  MET   A O   1 
ATOM   1163 C CB  . MET   A 1 149 ? -24.518 59.658 9.871   1.00 38.69  ? -48  MET   A CB  1 
ATOM   1164 C CG  . MET   A 1 149 ? -25.700 60.414 9.311   1.00 37.19  ? -48  MET   A CG  1 
ATOM   1165 S SD  . MET   A 1 149 ? -25.234 61.433 7.848   1.00 43.70  ? -48  MET   A SD  1 
ATOM   1166 C CE  . MET   A 1 149 ? -25.129 60.115 6.589   1.00 45.24  ? -48  MET   A CE  1 
ATOM   1167 N N   . PHE   A 1 150 ? -23.528 56.660 11.169  1.00 36.29  ? -47  PHE   A N   1 
ATOM   1168 C CA  . PHE   A 1 150 ? -22.347 55.853 11.386  1.00 33.80  ? -47  PHE   A CA  1 
ATOM   1169 C C   . PHE   A 1 150 ? -22.312 54.688 10.388  1.00 32.75  ? -47  PHE   A C   1 
ATOM   1170 O O   . PHE   A 1 150 ? -23.336 54.300 9.804   1.00 30.55  ? -47  PHE   A O   1 
ATOM   1171 C CB  . PHE   A 1 150 ? -22.284 55.337 12.839  1.00 30.47  ? -47  PHE   A CB  1 
ATOM   1172 C CG  . PHE   A 1 150 ? -23.360 54.309 13.201  1.00 33.15  ? -47  PHE   A CG  1 
ATOM   1173 C CD1 . PHE   A 1 150 ? -24.617 54.720 13.604  1.00 33.94  ? -47  PHE   A CD1 1 
ATOM   1174 C CD2 . PHE   A 1 150 ? -23.065 52.947 13.237  1.00 33.63  ? -47  PHE   A CD2 1 
ATOM   1175 C CE1 . PHE   A 1 150 ? -25.594 53.787 14.005  1.00 36.36  ? -47  PHE   A CE1 1 
ATOM   1176 C CE2 . PHE   A 1 150 ? -24.023 51.975 13.621  1.00 33.59  ? -47  PHE   A CE2 1 
ATOM   1177 C CZ  . PHE   A 1 150 ? -25.291 52.368 14.010  1.00 34.32  ? -47  PHE   A CZ  1 
ATOM   1178 N N   . ASN   A 1 151 ? -21.103 54.147 10.222  1.00 32.47  ? -46  ASN   A N   1 
ATOM   1179 C CA  . ASN   A 1 151 ? -20.812 53.085 9.248   1.00 34.93  ? -46  ASN   A CA  1 
ATOM   1180 C C   . ASN   A 1 151 ? -21.745 51.902 9.443   1.00 36.91  ? -46  ASN   A C   1 
ATOM   1181 O O   . ASN   A 1 151 ? -21.726 51.286 10.484  1.00 36.48  ? -46  ASN   A O   1 
ATOM   1182 C CB  . ASN   A 1 151 ? -19.350 52.619 9.404   1.00 31.36  ? -46  ASN   A CB  1 
ATOM   1183 C CG  . ASN   A 1 151 ? -18.910 51.700 8.303   1.00 34.83  ? -46  ASN   A CG  1 
ATOM   1184 O OD1 . ASN   A 1 151 ? -19.661 51.431 7.309   1.00 39.20  ? -46  ASN   A OD1 1 
ATOM   1185 N ND2 . ASN   A 1 151 ? -17.673 51.209 8.418   1.00 34.10  ? -46  ASN   A ND2 1 
ATOM   1186 N N   . LEU   A 1 152 ? -22.578 51.607 8.428   1.00 38.68  ? -45  LEU   A N   1 
ATOM   1187 C CA  . LEU   A 1 152 ? -23.494 50.465 8.519   1.00 38.22  ? -45  LEU   A CA  1 
ATOM   1188 C C   . LEU   A 1 152 ? -23.013 49.277 7.684   1.00 38.29  ? -45  LEU   A C   1 
ATOM   1189 O O   . LEU   A 1 152 ? -23.737 48.275 7.579   1.00 39.21  ? -45  LEU   A O   1 
ATOM   1190 C CB  . LEU   A 1 152 ? -24.922 50.868 8.119   1.00 35.47  ? -45  LEU   A CB  1 
ATOM   1191 C CG  . LEU   A 1 152 ? -25.555 52.061 8.890   1.00 35.11  ? -45  LEU   A CG  1 
ATOM   1192 C CD1 . LEU   A 1 152 ? -26.999 52.266 8.454   1.00 32.92  ? -45  LEU   A CD1 1 
ATOM   1193 C CD2 . LEU   A 1 152 ? -25.483 51.832 10.385  1.00 34.34  ? -45  LEU   A CD2 1 
ATOM   1194 N N   . GLN   A 1 153 ? -21.811 49.356 7.089   1.00 39.16  ? -44  GLN   A N   1 
ATOM   1195 C CA  . GLN   A 1 153 ? -21.304 48.249 6.263   1.00 40.76  ? -44  GLN   A CA  1 
ATOM   1196 C C   . GLN   A 1 153 ? -20.411 47.298 7.038   1.00 40.35  ? -44  GLN   A C   1 
ATOM   1197 O O   . GLN   A 1 153 ? -20.113 46.188 6.536   1.00 41.25  ? -44  GLN   A O   1 
ATOM   1198 C CB  . GLN   A 1 153 ? -20.508 48.758 5.062   1.00 39.77  ? -44  GLN   A CB  1 
ATOM   1199 C CG  . GLN   A 1 153 ? -21.217 49.859 4.261   1.00 40.73  ? -44  GLN   A CG  1 
ATOM   1200 C CD  . GLN   A 1 153 ? -22.620 49.500 3.874   1.00 41.06  ? -44  GLN   A CD  1 
ATOM   1201 O OE1 . GLN   A 1 153 ? -22.858 48.502 3.188   1.00 41.00  ? -44  GLN   A OE1 1 
ATOM   1202 N NE2 . GLN   A 1 153 ? -23.581 50.383 4.228   1.00 42.39  ? -44  GLN   A NE2 1 
ATOM   1203 N N   . GLU   A 1 154 ? -19.951 47.708 8.219   1.00 37.82  ? -43  GLU   A N   1 
ATOM   1204 C CA  . GLU   A 1 154 ? -19.060 46.878 9.044   1.00 35.34  ? -43  GLU   A CA  1 
ATOM   1205 C C   . GLU   A 1 154 ? -19.789 46.529 10.337  1.00 35.16  ? -43  GLU   A C   1 
ATOM   1206 O O   . GLU   A 1 154 ? -20.177 47.435 11.077  1.00 36.16  ? -43  GLU   A O   1 
ATOM   1207 C CB  . GLU   A 1 154 ? -17.736 47.587 9.336   1.00 32.22  ? -43  GLU   A CB  1 
ATOM   1208 C CG  . GLU   A 1 154 ? -16.748 47.476 8.215   1.00 34.57  ? -43  GLU   A CG  1 
ATOM   1209 C CD  . GLU   A 1 154 ? -16.397 45.995 7.904   1.00 41.26  ? -43  GLU   A CD  1 
ATOM   1210 O OE1 . GLU   A 1 154 ? -16.076 45.703 6.740   1.00 46.83  ? -43  GLU   A OE1 1 
ATOM   1211 O OE2 . GLU   A 1 154 ? -16.455 45.140 8.845   1.00 37.15  ? -43  GLU   A OE2 1 
ATOM   1212 N N   . PRO   A 1 155 ? -19.992 45.259 10.657  1.00 32.70  ? -42  PRO   A N   1 
ATOM   1213 C CA  . PRO   A 1 155 ? -20.794 44.918 11.851  1.00 31.32  ? -42  PRO   A CA  1 
ATOM   1214 C C   . PRO   A 1 155 ? -20.182 45.409 13.142  1.00 32.00  ? -42  PRO   A C   1 
ATOM   1215 O O   . PRO   A 1 155 ? -20.885 45.537 14.161  1.00 30.06  ? -42  PRO   A O   1 
ATOM   1216 C CB  . PRO   A 1 155 ? -20.870 43.356 11.800  1.00 30.23  ? -42  PRO   A CB  1 
ATOM   1217 C CG  . PRO   A 1 155 ? -19.794 42.915 10.840  1.00 26.91  ? -42  PRO   A CG  1 
ATOM   1218 C CD  . PRO   A 1 155 ? -19.588 44.082 9.855   1.00 31.91  ? -42  PRO   A CD  1 
ATOM   1219 N N   . TYR   A 1 156 ? -18.872 45.669 13.161  1.00 34.16  ? -41  TYR   A N   1 
ATOM   1220 C CA  . TYR   A 1 156 ? -18.233 46.232 14.372  1.00 34.91  ? -41  TYR   A CA  1 
ATOM   1221 C C   . TYR   A 1 156 ? -19.042 47.394 14.962  1.00 33.83  ? -41  TYR   A C   1 
ATOM   1222 O O   . TYR   A 1 156 ? -19.112 47.590 16.186  1.00 31.54  ? -41  TYR   A O   1 
ATOM   1223 C CB  . TYR   A 1 156 ? -16.824 46.713 13.999  1.00 33.65  ? -41  TYR   A CB  1 
ATOM   1224 C CG  . TYR   A 1 156 ? -15.990 47.280 15.090  1.00 35.23  ? -41  TYR   A CG  1 
ATOM   1225 C CD1 . TYR   A 1 156 ? -15.412 46.467 16.061  1.00 35.26  ? -41  TYR   A CD1 1 
ATOM   1226 C CD2 . TYR   A 1 156 ? -15.740 48.692 15.149  1.00 33.59  ? -41  TYR   A CD2 1 
ATOM   1227 C CE1 . TYR   A 1 156 ? -14.611 47.029 17.096  1.00 34.12  ? -41  TYR   A CE1 1 
ATOM   1228 C CE2 . TYR   A 1 156 ? -14.946 49.226 16.144  1.00 33.31  ? -41  TYR   A CE2 1 
ATOM   1229 C CZ  . TYR   A 1 156 ? -14.384 48.405 17.098  1.00 36.26  ? -41  TYR   A CZ  1 
ATOM   1230 O OH  . TYR   A 1 156 ? -13.597 48.954 18.083  1.00 37.17  ? -41  TYR   A OH  1 
ATOM   1231 N N   . PHE   A 1 157 ? -19.646 48.186 14.098  1.00 33.42  ? -40  PHE   A N   1 
ATOM   1232 C CA  . PHE   A 1 157 ? -20.286 49.446 14.555  1.00 32.02  ? -40  PHE   A CA  1 
ATOM   1233 C C   . PHE   A 1 157 ? -21.728 49.229 14.988  1.00 32.93  ? -40  PHE   A C   1 
ATOM   1234 O O   . PHE   A 1 157 ? -22.225 49.965 15.828  1.00 34.42  ? -40  PHE   A O   1 
ATOM   1235 C CB  . PHE   A 1 157 ? -20.246 50.471 13.434  1.00 28.87  ? -40  PHE   A CB  1 
ATOM   1236 C CG  . PHE   A 1 157 ? -18.854 50.896 13.064  1.00 30.17  ? -40  PHE   A CG  1 
ATOM   1237 C CD1 . PHE   A 1 157 ? -18.127 50.192 12.147  1.00 32.73  ? -40  PHE   A CD1 1 
ATOM   1238 C CD2 . PHE   A 1 157 ? -18.270 52.023 13.651  1.00 32.74  ? -40  PHE   A CD2 1 
ATOM   1239 C CE1 . PHE   A 1 157 ? -16.843 50.577 11.787  1.00 36.12  ? -40  PHE   A CE1 1 
ATOM   1240 C CE2 . PHE   A 1 157 ? -16.987 52.418 13.287  1.00 35.11  ? -40  PHE   A CE2 1 
ATOM   1241 C CZ  . PHE   A 1 157 ? -16.271 51.746 12.369  1.00 34.13  ? -40  PHE   A CZ  1 
ATOM   1242 N N   . THR   A 1 158 ? -22.387 48.184 14.453  1.00 33.68  ? -39  THR   A N   1 
ATOM   1243 C CA  . THR   A 1 158 ? -23.782 47.906 14.796  1.00 35.00  ? -39  THR   A CA  1 
ATOM   1244 C C   . THR   A 1 158 ? -23.901 46.917 15.945  1.00 36.03  ? -39  THR   A C   1 
ATOM   1245 O O   . THR   A 1 158 ? -24.950 46.886 16.615  1.00 35.30  ? -39  THR   A O   1 
ATOM   1246 C CB  . THR   A 1 158 ? -24.509 47.360 13.567  1.00 38.04  ? -39  THR   A CB  1 
ATOM   1247 O OG1 . THR   A 1 158 ? -24.715 48.462 12.635  1.00 40.82  ? -39  THR   A OG1 1 
ATOM   1248 C CG2 . THR   A 1 158 ? -25.858 46.799 13.920  1.00 42.45  ? -39  THR   A CG2 1 
ATOM   1249 N N   . TRP   A 1 159 ? -22.835 46.125 16.217  1.00 35.10  ? -38  TRP   A N   1 
ATOM   1250 C CA  . TRP   A 1 159 ? -22.831 45.141 17.289  1.00 33.58  ? -38  TRP   A CA  1 
ATOM   1251 C C   . TRP   A 1 159 ? -23.190 45.692 18.660  1.00 36.13  ? -38  TRP   A C   1 
ATOM   1252 O O   . TRP   A 1 159 ? -23.907 45.007 19.407  1.00 35.64  ? -38  TRP   A O   1 
ATOM   1253 C CB  . TRP   A 1 159 ? -21.442 44.521 17.386  1.00 33.70  ? -38  TRP   A CB  1 
ATOM   1254 C CG  . TRP   A 1 159 ? -21.472 43.346 18.310  1.00 37.42  ? -38  TRP   A CG  1 
ATOM   1255 C CD1 . TRP   A 1 159 ? -20.929 43.276 19.560  1.00 39.05  ? -38  TRP   A CD1 1 
ATOM   1256 C CD2 . TRP   A 1 159 ? -22.119 42.077 18.073  1.00 37.57  ? -38  TRP   A CD2 1 
ATOM   1257 N NE1 . TRP   A 1 159 ? -21.165 42.027 20.114  1.00 40.58  ? -38  TRP   A NE1 1 
ATOM   1258 C CE2 . TRP   A 1 159 ? -21.902 41.273 19.234  1.00 37.45  ? -38  TRP   A CE2 1 
ATOM   1259 C CE3 . TRP   A 1 159 ? -22.864 41.555 17.007  1.00 37.56  ? -38  TRP   A CE3 1 
ATOM   1260 C CZ2 . TRP   A 1 159 ? -22.402 40.003 19.365  1.00 37.12  ? -38  TRP   A CZ2 1 
ATOM   1261 C CZ3 . TRP   A 1 159 ? -23.343 40.269 17.122  1.00 41.59  ? -38  TRP   A CZ3 1 
ATOM   1262 C CH2 . TRP   A 1 159 ? -23.114 39.492 18.310  1.00 40.16  ? -38  TRP   A CH2 1 
ATOM   1263 N N   . PRO   A 1 160 ? -22.723 46.883 19.069  1.00 37.85  ? -37  PRO   A N   1 
ATOM   1264 C CA  . PRO   A 1 160 ? -23.107 47.376 20.426  1.00 38.38  ? -37  PRO   A CA  1 
ATOM   1265 C C   . PRO   A 1 160 ? -24.615 47.360 20.640  1.00 39.34  ? -37  PRO   A C   1 
ATOM   1266 O O   . PRO   A 1 160 ? -25.112 46.909 21.677  1.00 39.39  ? -37  PRO   A O   1 
ATOM   1267 C CB  . PRO   A 1 160 ? -22.522 48.805 20.437  1.00 35.16  ? -37  PRO   A CB  1 
ATOM   1268 C CG  . PRO   A 1 160 ? -21.400 48.790 19.426  1.00 32.31  ? -37  PRO   A CG  1 
ATOM   1269 C CD  . PRO   A 1 160 ? -21.839 47.836 18.339  1.00 31.53  ? -37  PRO   A CD  1 
ATOM   1270 N N   . LEU   A 1 161 ? -25.361 47.874 19.660  1.00 39.62  ? -36  LEU   A N   1 
ATOM   1271 C CA  . LEU   A 1 161 ? -26.819 47.859 19.770  1.00 38.38  ? -36  LEU   A CA  1 
ATOM   1272 C C   . LEU   A 1 161 ? -27.361 46.421 19.780  1.00 41.55  ? -36  LEU   A C   1 
ATOM   1273 O O   . LEU   A 1 161 ? -28.344 46.111 20.476  1.00 41.20  ? -36  LEU   A O   1 
ATOM   1274 C CB  . LEU   A 1 161 ? -27.424 48.667 18.636  1.00 32.17  ? -36  LEU   A CB  1 
ATOM   1275 C CG  . LEU   A 1 161 ? -28.937 48.633 18.500  1.00 32.21  ? -36  LEU   A CG  1 
ATOM   1276 C CD1 . LEU   A 1 161 ? -29.593 49.179 19.739  1.00 32.67  ? -36  LEU   A CD1 1 
ATOM   1277 C CD2 . LEU   A 1 161 ? -29.362 49.450 17.243  1.00 31.89  ? -36  LEU   A CD2 1 
ATOM   1278 N N   . ILE   A 1 162 ? -26.724 45.517 19.019  1.00 40.90  ? -35  ILE   A N   1 
ATOM   1279 C CA  . ILE   A 1 162 ? -27.241 44.162 18.875  1.00 39.30  ? -35  ILE   A CA  1 
ATOM   1280 C C   . ILE   A 1 162 ? -27.020 43.368 20.152  1.00 39.41  ? -35  ILE   A C   1 
ATOM   1281 O O   . ILE   A 1 162 ? -27.871 42.580 20.571  1.00 36.33  ? -35  ILE   A O   1 
ATOM   1282 C CB  . ILE   A 1 162 ? -26.569 43.475 17.656  1.00 38.75  ? -35  ILE   A CB  1 
ATOM   1283 C CG1 . ILE   A 1 162 ? -27.104 44.028 16.338  1.00 35.64  ? -35  ILE   A CG1 1 
ATOM   1284 C CG2 . ILE   A 1 162 ? -26.789 42.001 17.705  1.00 38.59  ? -35  ILE   A CG2 1 
ATOM   1285 C CD1 . ILE   A 1 162 ? -26.509 43.245 15.154  1.00 37.09  ? -35  ILE   A CD1 1 
ATOM   1286 N N   . ALA   A 1 163 ? -25.866 43.568 20.807  1.00 40.49  ? -34  ALA   A N   1 
ATOM   1287 C CA  . ALA   A 1 163 ? -25.612 42.850 22.049  1.00 41.39  ? -34  ALA   A CA  1 
ATOM   1288 C C   . ALA   A 1 163 ? -26.343 43.453 23.248  1.00 43.80  ? -34  ALA   A C   1 
ATOM   1289 O O   . ALA   A 1 163 ? -26.468 42.773 24.285  1.00 43.34  ? -34  ALA   A O   1 
ATOM   1290 C CB  . ALA   A 1 163 ? -24.113 42.834 22.342  1.00 39.23  ? -34  ALA   A CB  1 
ATOM   1291 N N   . ALA   A 1 164 ? -26.841 44.703 23.128  1.00 41.54  ? -33  ALA   A N   1 
ATOM   1292 C CA  . ALA   A 1 164 ? -27.357 45.412 24.303  1.00 40.40  ? -33  ALA   A CA  1 
ATOM   1293 C C   . ALA   A 1 164 ? -28.430 44.609 25.039  1.00 39.74  ? -33  ALA   A C   1 
ATOM   1294 O O   . ALA   A 1 164 ? -28.422 44.526 26.268  1.00 37.89  ? -33  ALA   A O   1 
ATOM   1295 C CB  . ALA   A 1 164 ? -27.928 46.800 23.905  1.00 37.23  ? -33  ALA   A CB  1 
ATOM   1296 N N   . ASP   A 1 165 ? -29.401 44.058 24.289  1.00 40.17  ? -32  ASP   A N   1 
ATOM   1297 C CA  . ASP   A 1 165 ? -30.537 43.353 24.885  1.00 42.16  ? -32  ASP   A CA  1 
ATOM   1298 C C   . ASP   A 1 165 ? -30.394 41.832 24.900  1.00 46.21  ? -32  ASP   A C   1 
ATOM   1299 O O   . ASP   A 1 165 ? -31.402 41.119 25.121  1.00 47.39  ? -32  ASP   A O   1 
ATOM   1300 C CB  . ASP   A 1 165 ? -31.821 43.720 24.148  1.00 41.44  ? -32  ASP   A CB  1 
ATOM   1301 C CG  . ASP   A 1 165 ? -33.056 43.373 24.954  1.00 44.68  ? -32  ASP   A CG  1 
ATOM   1302 O OD1 . ASP   A 1 165 ? -33.003 43.506 26.191  1.00 46.13  ? -32  ASP   A OD1 1 
ATOM   1303 O OD2 . ASP   A 1 165 ? -34.065 42.924 24.369  1.00 45.89  ? -32  ASP   A OD2 1 
ATOM   1304 N N   . GLY   A 1 166 ? -29.175 41.305 24.705  1.00 45.51  ? -31  GLY   A N   1 
ATOM   1305 C CA  . GLY   A 1 166 ? -29.008 39.864 24.909  1.00 43.61  ? -31  GLY   A CA  1 
ATOM   1306 C C   . GLY   A 1 166 ? -28.254 39.164 23.785  1.00 47.66  ? -31  GLY   A C   1 
ATOM   1307 O O   . GLY   A 1 166 ? -27.910 37.970 23.899  1.00 51.10  ? -31  GLY   A O   1 
ATOM   1308 N N   . GLY   A 1 167 ? -27.997 39.871 22.673  1.00 45.94  ? -30  GLY   A N   1 
ATOM   1309 C CA  . GLY   A 1 167 ? -27.235 39.269 21.587  1.00 42.04  ? -30  GLY   A CA  1 
ATOM   1310 C C   . GLY   A 1 167 ? -25.796 39.027 22.033  1.00 44.56  ? -30  GLY   A C   1 
ATOM   1311 O O   . GLY   A 1 167 ? -25.222 39.815 22.794  1.00 47.00  ? -30  GLY   A O   1 
ATOM   1312 N N   . TYR   A 1 168 ? -25.203 37.929 21.547  1.00 43.22  ? -29  TYR   A N   1 
ATOM   1313 C CA  . TYR   A 1 168 ? -23.812 37.670 21.851  1.00 41.69  ? -29  TYR   A CA  1 
ATOM   1314 C C   . TYR   A 1 168 ? -23.232 36.731 20.788  1.00 42.47  ? -29  TYR   A C   1 
ATOM   1315 O O   . TYR   A 1 168 ? -23.969 36.106 20.005  1.00 44.04  ? -29  TYR   A O   1 
ATOM   1316 C CB  . TYR   A 1 168 ? -23.670 37.098 23.259  1.00 45.00  ? -29  TYR   A CB  1 
ATOM   1317 C CG  . TYR   A 1 168 ? -24.421 35.755 23.501  1.00 48.81  ? -29  TYR   A CG  1 
ATOM   1318 C CD1 . TYR   A 1 168 ? -25.729 35.756 24.009  1.00 52.05  ? -29  TYR   A CD1 1 
ATOM   1319 C CD2 . TYR   A 1 168 ? -23.835 34.553 23.207  1.00 49.22  ? -29  TYR   A CD2 1 
ATOM   1320 C CE1 . TYR   A 1 168 ? -26.431 34.592 24.227  1.00 52.51  ? -29  TYR   A CE1 1 
ATOM   1321 C CE2 . TYR   A 1 168 ? -24.541 33.323 23.437  1.00 52.14  ? -29  TYR   A CE2 1 
ATOM   1322 C CZ  . TYR   A 1 168 ? -25.828 33.374 23.943  1.00 53.52  ? -29  TYR   A CZ  1 
ATOM   1323 O OH  . TYR   A 1 168 ? -26.512 32.212 24.170  1.00 53.79  ? -29  TYR   A OH  1 
ATOM   1324 N N   . ALA   A 1 169 ? -21.898 36.640 20.774  1.00 38.21  ? -28  ALA   A N   1 
ATOM   1325 C CA  . ALA   A 1 169 ? -21.216 35.805 19.814  1.00 39.83  ? -28  ALA   A CA  1 
ATOM   1326 C C   . ALA   A 1 169 ? -21.099 34.366 20.340  1.00 44.18  ? -28  ALA   A C   1 
ATOM   1327 O O   . ALA   A 1 169 ? -21.913 33.519 19.968  1.00 48.13  ? -28  ALA   A O   1 
ATOM   1328 C CB  . ALA   A 1 169 ? -19.838 36.379 19.500  1.00 39.71  ? -28  ALA   A CB  1 
ATOM   1329 N N   . PHE   A 1 170 ? -20.153 34.113 21.245  1.00 42.78  ? -27  PHE   A N   1 
ATOM   1330 C CA  . PHE   A 1 170 ? -19.990 32.833 21.892  1.00 48.12  ? -27  PHE   A CA  1 
ATOM   1331 C C   . PHE   A 1 170 ? -20.167 32.990 23.395  1.00 53.15  ? -27  PHE   A C   1 
ATOM   1332 O O   . PHE   A 1 170 ? -19.560 33.886 23.988  1.00 51.10  ? -27  PHE   A O   1 
ATOM   1333 C CB  . PHE   A 1 170 ? -18.622 32.260 21.552  1.00 48.04  ? -27  PHE   A CB  1 
ATOM   1334 C CG  . PHE   A 1 170 ? -18.323 32.269 20.071  1.00 46.60  ? -27  PHE   A CG  1 
ATOM   1335 C CD1 . PHE   A 1 170 ? -18.790 31.258 19.238  1.00 45.52  ? -27  PHE   A CD1 1 
ATOM   1336 C CD2 . PHE   A 1 170 ? -17.611 33.337 19.503  1.00 47.04  ? -27  PHE   A CD2 1 
ATOM   1337 C CE1 . PHE   A 1 170 ? -18.515 31.255 17.903  1.00 46.60  ? -27  PHE   A CE1 1 
ATOM   1338 C CE2 . PHE   A 1 170 ? -17.338 33.375 18.139  1.00 45.17  ? -27  PHE   A CE2 1 
ATOM   1339 C CZ  . PHE   A 1 170 ? -17.789 32.361 17.326  1.00 45.85  ? -27  PHE   A CZ  1 
ATOM   1340 N N   . LYS   A 1 171 ? -20.979 32.095 24.004  1.00 57.82  ? -26  LYS   A N   1 
ATOM   1341 C CA  . LYS   A 1 171 ? -21.371 32.238 25.403  1.00 61.99  ? -26  LYS   A CA  1 
ATOM   1342 C C   . LYS   A 1 171 ? -20.155 32.207 26.338  1.00 64.92  ? -26  LYS   A C   1 
ATOM   1343 O O   . LYS   A 1 171 ? -19.091 31.676 26.002  1.00 61.99  ? -26  LYS   A O   1 
ATOM   1344 C CB  . LYS   A 1 171 ? -22.354 31.124 25.807  1.00 65.29  ? -26  LYS   A CB  1 
ATOM   1345 N N   . TYR   A 1 172 ? -20.355 32.754 27.546  1.00 71.86  ? -25  TYR   A N   1 
ATOM   1346 C CA  . TYR   A 1 172 ? -19.315 32.905 28.582  1.00 76.85  ? -25  TYR   A CA  1 
ATOM   1347 C C   . TYR   A 1 172 ? -17.957 33.331 27.991  1.00 77.53  ? -25  TYR   A C   1 
ATOM   1348 O O   . TYR   A 1 172 ? -16.969 33.507 28.719  1.00 78.40  ? -25  TYR   A O   1 
ATOM   1349 C CB  . TYR   A 1 172 ? -19.153 31.608 29.381  1.00 80.11  ? -25  TYR   A CB  1 
ATOM   1350 N N   . LYS   A 1 176 ? -15.076 29.802 30.367  1.00 83.48  ? -21  LYS   A N   1 
ATOM   1351 C CA  . LYS   A 1 176 ? -14.516 29.909 29.016  1.00 83.33  ? -21  LYS   A CA  1 
ATOM   1352 C C   . LYS   A 1 176 ? -15.619 30.084 27.957  1.00 83.18  ? -21  LYS   A C   1 
ATOM   1353 O O   . LYS   A 1 176 ? -16.813 29.949 28.264  1.00 84.08  ? -21  LYS   A O   1 
ATOM   1354 C CB  . LYS   A 1 176 ? -13.668 28.681 28.692  1.00 85.28  ? -21  LYS   A CB  1 
ATOM   1355 N N   . TYR   A 1 177 ? -15.204 30.395 26.716  1.00 81.20  ? -20  TYR   A N   1 
ATOM   1356 C CA  . TYR   A 1 177 ? -16.138 30.517 25.590  1.00 77.67  ? -20  TYR   A CA  1 
ATOM   1357 C C   . TYR   A 1 177 ? -16.636 29.145 25.157  1.00 78.40  ? -20  TYR   A C   1 
ATOM   1358 O O   . TYR   A 1 177 ? -15.833 28.260 24.830  1.00 83.72  ? -20  TYR   A O   1 
ATOM   1359 C CB  . TYR   A 1 177 ? -15.455 31.195 24.416  1.00 74.95  ? -20  TYR   A CB  1 
ATOM   1360 C CG  . TYR   A 1 177 ? -15.000 32.602 24.667  1.00 73.75  ? -20  TYR   A CG  1 
ATOM   1361 C CD1 . TYR   A 1 177 ? -15.923 33.645 24.754  1.00 73.58  ? -20  TYR   A CD1 1 
ATOM   1362 C CD2 . TYR   A 1 177 ? -13.645 32.911 24.793  1.00 72.02  ? -20  TYR   A CD2 1 
ATOM   1363 C CE1 . TYR   A 1 177 ? -15.506 34.951 24.975  1.00 69.71  ? -20  TYR   A CE1 1 
ATOM   1364 C CE2 . TYR   A 1 177 ? -13.227 34.205 25.020  1.00 70.33  ? -20  TYR   A CE2 1 
ATOM   1365 C CZ  . TYR   A 1 177 ? -14.165 35.223 25.109  1.00 68.94  ? -20  TYR   A CZ  1 
ATOM   1366 O OH  . TYR   A 1 177 ? -13.754 36.507 25.335  1.00 68.35  ? -20  TYR   A OH  1 
ATOM   1367 N N   . ASP   A 1 178 ? -17.954 28.950 25.164  1.00 72.83  ? -19  ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 178 ? -18.567 27.739 24.623  1.00 69.50  ? -19  ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 178 ? -18.846 27.986 23.143  1.00 67.25  ? -19  ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 178 ? -19.874 28.580 22.785  1.00 67.34  ? -19  ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 178 ? -19.835 27.383 25.388  1.00 68.34  ? -19  ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 178 ? -20.535 26.161 24.821  1.00 67.24  ? -19  ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 178 ? -21.623 25.802 25.329  1.00 68.36  ? -19  ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 178 ? -20.020 25.558 23.854  1.00 66.12  ? -19  ASP   A OD2 1 
ATOM   1375 N N   . ILE   A 1 179 ? -17.923 27.540 22.275  1.00 64.73  ? -18  ILE   A N   1 
ATOM   1376 C CA  . ILE   A 1 179 ? -18.062 27.707 20.827  1.00 60.33  ? -18  ILE   A CA  1 
ATOM   1377 C C   . ILE   A 1 179 ? -19.331 27.050 20.289  1.00 58.20  ? -18  ILE   A C   1 
ATOM   1378 O O   . ILE   A 1 179 ? -19.687 27.267 19.125  1.00 56.12  ? -18  ILE   A O   1 
ATOM   1379 C CB  . ILE   A 1 179 ? -16.831 27.139 20.089  1.00 58.54  ? -18  ILE   A CB  1 
ATOM   1380 C CG1 . ILE   A 1 179 ? -16.784 25.604 20.264  1.00 63.11  ? -18  ILE   A CG1 1 
ATOM   1381 C CG2 . ILE   A 1 179 ? -15.557 27.770 20.616  1.00 55.25  ? -18  ILE   A CG2 1 
ATOM   1382 C CD1 . ILE   A 1 179 ? -15.603 24.944 19.555  1.00 63.37  ? -18  ILE   A CD1 1 
ATOM   1383 N N   . LYS   A 1 180 ? -20.028 26.266 21.112  1.00 58.86  ? -17  LYS   A N   1 
ATOM   1384 C CA  . LYS   A 1 180 ? -21.256 25.613 20.682  1.00 62.78  ? -17  LYS   A CA  1 
ATOM   1385 C C   . LYS   A 1 180 ? -22.497 26.436 20.996  1.00 66.60  ? -17  LYS   A C   1 
ATOM   1386 O O   . LYS   A 1 180 ? -23.578 26.118 20.491  1.00 71.13  ? -17  LYS   A O   1 
ATOM   1387 C CB  . LYS   A 1 180 ? -21.371 24.219 21.324  1.00 63.55  ? -17  LYS   A CB  1 
ATOM   1388 N N   . ASP   A 1 181 ? -22.372 27.485 21.811  1.00 65.56  ? -16  ASP   A N   1 
ATOM   1389 C CA  . ASP   A 1 181 ? -23.495 28.364 22.151  1.00 62.96  ? -16  ASP   A CA  1 
ATOM   1390 C C   . ASP   A 1 181 ? -23.295 29.682 21.419  1.00 58.60  ? -16  ASP   A C   1 
ATOM   1391 O O   . ASP   A 1 181 ? -22.477 30.524 21.819  1.00 57.15  ? -16  ASP   A O   1 
ATOM   1392 C CB  . ASP   A 1 181 ? -23.583 28.561 23.663  1.00 62.77  ? -16  ASP   A CB  1 
ATOM   1393 C CG  . ASP   A 1 181 ? -24.826 29.339 24.079  1.00 62.58  ? -16  ASP   A CG  1 
ATOM   1394 O OD1 . ASP   A 1 181 ? -25.544 29.891 23.192  1.00 59.54  ? -16  ASP   A OD1 1 
ATOM   1395 O OD2 . ASP   A 1 181 ? -25.094 29.383 25.298  1.00 64.86  ? -16  ASP   A OD2 1 
ATOM   1396 N N   . VAL   A 1 182 ? -24.071 29.883 20.356  1.00 58.45  ? -15  VAL   A N   1 
ATOM   1397 C CA  . VAL   A 1 182 ? -24.011 31.106 19.541  1.00 54.34  ? -15  VAL   A CA  1 
ATOM   1398 C C   . VAL   A 1 182 ? -25.288 31.907 19.768  1.00 53.55  ? -15  VAL   A C   1 
ATOM   1399 O O   . VAL   A 1 182 ? -26.398 31.362 19.700  1.00 54.58  ? -15  VAL   A O   1 
ATOM   1400 C CB  . VAL   A 1 182 ? -23.833 30.770 18.051  1.00 52.07  ? -15  VAL   A CB  1 
ATOM   1401 C CG1 . VAL   A 1 182 ? -24.048 32.015 17.179  1.00 45.65  ? -15  VAL   A CG1 1 
ATOM   1402 C CG2 . VAL   A 1 182 ? -22.458 30.147 17.814  1.00 53.28  ? -15  VAL   A CG2 1 
ATOM   1403 N N   . GLY   A 1 183 ? -25.137 33.196 20.007  1.00 53.00  ? -14  GLY   A N   1 
ATOM   1404 C CA  . GLY   A 1 183 ? -26.283 34.027 20.341  1.00 51.53  ? -14  GLY   A CA  1 
ATOM   1405 C C   . GLY   A 1 183 ? -26.550 35.106 19.302  1.00 48.54  ? -14  GLY   A C   1 
ATOM   1406 O O   . GLY   A 1 183 ? -26.747 36.285 19.634  1.00 44.55  ? -14  GLY   A O   1 
ATOM   1407 N N   . VAL   A 1 184 ? -26.556 34.705 18.035  1.00 47.74  ? -13  VAL   A N   1 
ATOM   1408 C CA  . VAL   A 1 184 ? -26.741 35.679 16.967  1.00 48.60  ? -13  VAL   A CA  1 
ATOM   1409 C C   . VAL   A 1 184 ? -28.199 35.820 16.551  1.00 47.96  ? -13  VAL   A C   1 
ATOM   1410 O O   . VAL   A 1 184 ? -28.579 36.863 16.017  1.00 44.32  ? -13  VAL   A O   1 
ATOM   1411 C CB  . VAL   A 1 184 ? -25.884 35.303 15.744  1.00 48.88  ? -13  VAL   A CB  1 
ATOM   1412 C CG1 . VAL   A 1 184 ? -26.304 36.153 14.540  1.00 47.86  ? -13  VAL   A CG1 1 
ATOM   1413 C CG2 . VAL   A 1 184 ? -24.407 35.512 16.077  1.00 48.01  ? -13  VAL   A CG2 1 
ATOM   1414 N N   . ASP   A 1 185 ? -29.042 34.801 16.787  1.00 49.95  ? -12  ASP   A N   1 
ATOM   1415 C CA  . ASP   A 1 185 ? -30.425 34.894 16.335  1.00 52.14  ? -12  ASP   A CA  1 
ATOM   1416 C C   . ASP   A 1 185 ? -31.421 34.780 17.481  1.00 51.77  ? -12  ASP   A C   1 
ATOM   1417 O O   . ASP   A 1 185 ? -32.600 34.470 17.239  1.00 54.51  ? -12  ASP   A O   1 
ATOM   1418 C CB  . ASP   A 1 185 ? -30.681 33.860 15.223  1.00 52.78  ? -12  ASP   A CB  1 
ATOM   1419 C CG  . ASP   A 1 185 ? -31.069 32.508 15.743  1.00 54.35  ? -12  ASP   A CG  1 
ATOM   1420 O OD1 . ASP   A 1 185 ? -30.387 32.012 16.669  1.00 54.01  ? -12  ASP   A OD1 1 
ATOM   1421 O OD2 . ASP   A 1 185 ? -32.056 31.961 15.201  1.00 56.72  ? -12  ASP   A OD2 1 
ATOM   1422 N N   . ASN   A 1 186 ? -30.995 35.071 18.713  1.00 48.71  ? -11  ASN   A N   1 
ATOM   1423 C CA  . ASN   A 1 186 ? -31.927 35.052 19.842  1.00 49.46  ? -11  ASN   A CA  1 
ATOM   1424 C C   . ASN   A 1 186 ? -32.682 36.391 19.923  1.00 48.59  ? -11  ASN   A C   1 
ATOM   1425 O O   . ASN   A 1 186 ? -32.439 37.343 19.164  1.00 42.88  ? -11  ASN   A O   1 
ATOM   1426 C CB  . ASN   A 1 186 ? -31.177 34.750 21.129  1.00 49.44  ? -11  ASN   A CB  1 
ATOM   1427 C CG  . ASN   A 1 186 ? -30.242 35.909 21.564  1.00 47.69  ? -11  ASN   A CG  1 
ATOM   1428 O OD1 . ASN   A 1 186 ? -30.532 37.119 21.348  1.00 40.35  ? -11  ASN   A OD1 1 
ATOM   1429 N ND2 . ASN   A 1 186 ? -29.136 35.524 22.243  1.00 50.10  ? -11  ASN   A ND2 1 
ATOM   1430 N N   . ALA   A 1 187 ? -33.632 36.456 20.865  1.00 52.04  ? -10  ALA   A N   1 
ATOM   1431 C CA  . ALA   A 1 187 ? -34.559 37.578 20.951  1.00 50.82  ? -10  ALA   A CA  1 
ATOM   1432 C C   . ALA   A 1 187 ? -33.838 38.916 21.152  1.00 48.23  ? -10  ALA   A C   1 
ATOM   1433 O O   . ALA   A 1 187 ? -34.321 39.954 20.656  1.00 45.25  ? -10  ALA   A O   1 
ATOM   1434 C CB  . ALA   A 1 187 ? -35.568 37.344 22.089  1.00 43.13  ? -10  ALA   A CB  1 
ATOM   1435 N N   . GLY   A 1 188 ? -32.720 38.911 21.886  1.00 47.67  ? -9   GLY   A N   1 
ATOM   1436 C CA  . GLY   A 1 188 ? -32.005 40.138 22.138  1.00 46.96  ? -9   GLY   A CA  1 
ATOM   1437 C C   . GLY   A 1 188 ? -31.375 40.684 20.859  1.00 48.03  ? -9   GLY   A C   1 
ATOM   1438 O O   . GLY   A 1 188 ? -31.594 41.851 20.488  1.00 47.30  ? -9   GLY   A O   1 
ATOM   1439 N N   . ALA   A 1 189 ? -30.594 39.843 20.157  1.00 46.57  ? -8   ALA   A N   1 
ATOM   1440 C CA  . ALA   A 1 189 ? -30.058 40.227 18.854  1.00 43.80  ? -8   ALA   A CA  1 
ATOM   1441 C C   . ALA   A 1 189 ? -31.168 40.764 17.956  1.00 42.78  ? -8   ALA   A C   1 
ATOM   1442 O O   . ALA   A 1 189 ? -31.012 41.797 17.308  1.00 39.12  ? -8   ALA   A O   1 
ATOM   1443 C CB  . ALA   A 1 189 ? -29.374 38.988 18.210  1.00 44.63  ? -8   ALA   A CB  1 
ATOM   1444 N N   . LYS   A 1 190 ? -32.307 40.042 17.888  1.00 43.12  ? -7   LYS   A N   1 
ATOM   1445 C CA  . LYS   A 1 190 ? -33.402 40.504 17.027  1.00 43.13  ? -7   LYS   A CA  1 
ATOM   1446 C C   . LYS   A 1 190 ? -33.867 41.896 17.434  1.00 43.53  ? -7   LYS   A C   1 
ATOM   1447 O O   . LYS   A 1 190 ? -34.143 42.733 16.585  1.00 43.25  ? -7   LYS   A O   1 
ATOM   1448 C CB  . LYS   A 1 190 ? -34.578 39.510 17.068  1.00 42.71  ? -7   LYS   A CB  1 
ATOM   1449 N N   . ALA   A 1 191 ? -34.024 42.128 18.742  1.00 44.52  ? -6   ALA   A N   1 
ATOM   1450 C CA  . ALA   A 1 191 ? -34.567 43.392 19.220  1.00 42.41  ? -6   ALA   A CA  1 
ATOM   1451 C C   . ALA   A 1 191 ? -33.660 44.544 18.812  1.00 41.35  ? -6   ALA   A C   1 
ATOM   1452 O O   . ALA   A 1 191 ? -34.146 45.573 18.331  1.00 41.26  ? -6   ALA   A O   1 
ATOM   1453 C CB  . ALA   A 1 191 ? -34.735 43.341 20.743  1.00 39.92  ? -6   ALA   A CB  1 
ATOM   1454 N N   . GLY   A 1 192 ? -32.343 44.373 18.966  1.00 40.76  ? -5   GLY   A N   1 
ATOM   1455 C CA  . GLY   A 1 192 ? -31.402 45.423 18.555  1.00 39.90  ? -5   GLY   A CA  1 
ATOM   1456 C C   . GLY   A 1 192 ? -31.392 45.645 17.048  1.00 39.01  ? -5   GLY   A C   1 
ATOM   1457 O O   . GLY   A 1 192 ? -31.504 46.772 16.574  1.00 36.68  ? -5   GLY   A O   1 
ATOM   1458 N N   . LEU   A 1 193 ? -31.279 44.565 16.275  1.00 37.04  ? -4   LEU   A N   1 
ATOM   1459 C CA  . LEU   A 1 193 ? -31.208 44.766 14.826  1.00 38.53  ? -4   LEU   A CA  1 
ATOM   1460 C C   . LEU   A 1 193 ? -32.517 45.301 14.283  1.00 39.93  ? -4   LEU   A C   1 
ATOM   1461 O O   . LEU   A 1 193 ? -32.508 46.014 13.269  1.00 41.15  ? -4   LEU   A O   1 
ATOM   1462 C CB  . LEU   A 1 193 ? -30.822 43.429 14.123  1.00 39.65  ? -4   LEU   A CB  1 
ATOM   1463 C CG  . LEU   A 1 193 ? -30.576 43.527 12.597  1.00 39.37  ? -4   LEU   A CG  1 
ATOM   1464 C CD1 . LEU   A 1 193 ? -29.655 44.705 12.280  1.00 43.19  ? -4   LEU   A CD1 1 
ATOM   1465 C CD2 . LEU   A 1 193 ? -29.954 42.266 12.071  1.00 35.01  ? -4   LEU   A CD2 1 
ATOM   1466 N N   . THR   A 1 194 ? -33.636 44.925 14.905  1.00 41.70  ? -3   THR   A N   1 
ATOM   1467 C CA  . THR   A 1 194 ? -34.920 45.482 14.507  1.00 41.29  ? -3   THR   A CA  1 
ATOM   1468 C C   . THR   A 1 194 ? -34.959 46.984 14.734  1.00 40.93  ? -3   THR   A C   1 
ATOM   1469 O O   . THR   A 1 194 ? -35.498 47.728 13.894  1.00 41.94  ? -3   THR   A O   1 
ATOM   1470 C CB  . THR   A 1 194 ? -36.066 44.817 15.285  1.00 38.86  ? -3   THR   A CB  1 
ATOM   1471 O OG1 . THR   A 1 194 ? -36.089 43.435 15.001  1.00 36.05  ? -3   THR   A OG1 1 
ATOM   1472 C CG2 . THR   A 1 194 ? -37.420 45.450 14.888  1.00 37.83  ? -3   THR   A CG2 1 
ATOM   1473 N N   . PHE   A 1 195 ? -34.449 47.451 15.888  1.00 40.62  ? -2   PHE   A N   1 
ATOM   1474 C CA  . PHE   A 1 195 ? -34.422 48.895 16.127  1.00 41.56  ? -2   PHE   A CA  1 
ATOM   1475 C C   . PHE   A 1 195 ? -33.590 49.609 15.057  1.00 41.36  ? -2   PHE   A C   1 
ATOM   1476 O O   . PHE   A 1 195 ? -33.974 50.686 14.571  1.00 40.84  ? -2   PHE   A O   1 
ATOM   1477 C CB  . PHE   A 1 195 ? -33.882 49.200 17.527  1.00 41.93  ? -2   PHE   A CB  1 
ATOM   1478 C CG  . PHE   A 1 195 ? -34.054 50.623 17.933  1.00 40.50  ? -2   PHE   A CG  1 
ATOM   1479 C CD1 . PHE   A 1 195 ? -35.237 51.049 18.483  1.00 42.35  ? -2   PHE   A CD1 1 
ATOM   1480 C CD2 . PHE   A 1 195 ? -33.028 51.545 17.745  1.00 39.51  ? -2   PHE   A CD2 1 
ATOM   1481 C CE1 . PHE   A 1 195 ? -35.426 52.413 18.856  1.00 43.91  ? -2   PHE   A CE1 1 
ATOM   1482 C CE2 . PHE   A 1 195 ? -33.193 52.899 18.088  1.00 40.96  ? -2   PHE   A CE2 1 
ATOM   1483 C CZ  . PHE   A 1 195 ? -34.383 53.327 18.638  1.00 43.46  ? -2   PHE   A CZ  1 
ATOM   1484 N N   . LEU   A 1 196 ? -32.462 49.009 14.653  1.00 40.41  ? -1   LEU   A N   1 
ATOM   1485 C CA  . LEU   A 1 196 ? -31.653 49.621 13.607  1.00 41.40  ? -1   LEU   A CA  1 
ATOM   1486 C C   . LEU   A 1 196 ? -32.417 49.668 12.285  1.00 42.73  ? -1   LEU   A C   1 
ATOM   1487 O O   . LEU   A 1 196 ? -32.437 50.702 11.599  1.00 44.28  ? -1   LEU   A O   1 
ATOM   1488 C CB  . LEU   A 1 196 ? -30.329 48.858 13.431  1.00 42.12  ? -1   LEU   A CB  1 
ATOM   1489 C CG  . LEU   A 1 196 ? -29.418 49.498 12.363  1.00 39.98  ? -1   LEU   A CG  1 
ATOM   1490 C CD1 . LEU   A 1 196 ? -28.312 50.303 13.032  1.00 40.36  ? -1   LEU   A CD1 1 
ATOM   1491 C CD2 . LEU   A 1 196 ? -28.809 48.509 11.391  1.00 38.94  ? -1   LEU   A CD2 1 
ATOM   1492 N N   . VAL   A 1 197 ? -33.055 48.561 11.908  1.00 40.34  ? 0    VAL   A N   1 
ATOM   1493 C CA  . VAL   A 1 197 ? -33.788 48.521 10.643  1.00 38.08  ? 0    VAL   A CA  1 
ATOM   1494 C C   . VAL   A 1 197 ? -34.916 49.552 10.654  1.00 38.59  ? 0    VAL   A C   1 
ATOM   1495 O O   . VAL   A 1 197 ? -35.148 50.282 9.647   1.00 37.26  ? 0    VAL   A O   1 
ATOM   1496 C CB  . VAL   A 1 197 ? -34.322 47.081 10.380  1.00 38.50  ? 0    VAL   A CB  1 
ATOM   1497 C CG1 . VAL   A 1 197 ? -35.397 47.114 9.295   1.00 41.21  ? 0    VAL   A CG1 1 
ATOM   1498 C CG2 . VAL   A 1 197 ? -33.179 46.140 9.965   1.00 33.82  ? 0    VAL   A CG2 1 
ATOM   1499 N N   . ASP   A 1 198 ? -35.627 49.660 11.802  1.00 39.64  ? 1    ASP   A N   1 
ATOM   1500 C CA  . ASP   A 1 198 ? -36.707 50.634 11.915  1.00 41.01  ? 1    ASP   A CA  1 
ATOM   1501 C C   . ASP   A 1 198 ? -36.164 52.054 11.751  1.00 42.84  ? 1    ASP   A C   1 
ATOM   1502 O O   . ASP   A 1 198 ? -36.802 52.891 11.105  1.00 45.93  ? 1    ASP   A O   1 
ATOM   1503 C CB  . ASP   A 1 198 ? -37.447 50.497 13.229  1.00 39.26  ? 1    ASP   A CB  1 
ATOM   1504 C CG  . ASP   A 1 198 ? -38.418 49.332 13.235  1.00 42.04  ? 1    ASP   A CG  1 
ATOM   1505 O OD1 . ASP   A 1 198 ? -38.917 48.924 12.165  1.00 43.60  ? 1    ASP   A OD1 1 
ATOM   1506 O OD2 . ASP   A 1 198 ? -38.694 48.801 14.326  1.00 43.19  ? 1    ASP   A OD2 1 
ATOM   1507 N N   . LEU   A 1 199 ? -34.986 52.338 12.315  1.00 41.26  ? 2    LEU   A N   1 
ATOM   1508 C CA  . LEU   A 1 199 ? -34.376 53.651 12.126  1.00 39.72  ? 2    LEU   A CA  1 
ATOM   1509 C C   . LEU   A 1 199 ? -34.221 53.953 10.644  1.00 42.56  ? 2    LEU   A C   1 
ATOM   1510 O O   . LEU   A 1 199 ? -34.494 55.086 10.209  1.00 47.49  ? 2    LEU   A O   1 
ATOM   1511 C CB  . LEU   A 1 199 ? -33.021 53.726 12.821  1.00 36.16  ? 2    LEU   A CB  1 
ATOM   1512 C CG  . LEU   A 1 199 ? -32.966 53.911 14.346  1.00 37.16  ? 2    LEU   A CG  1 
ATOM   1513 C CD1 . LEU   A 1 199 ? -31.535 53.827 14.842  1.00 34.83  ? 2    LEU   A CD1 1 
ATOM   1514 C CD2 . LEU   A 1 199 ? -33.595 55.239 14.770  1.00 36.72  ? 2    LEU   A CD2 1 
ATOM   1515 N N   . ILE   A 1 200 ? -33.801 52.959 9.851   1.00 35.08  ? 3    ILE   A N   1 
ATOM   1516 C CA  . ILE   A 1 200 ? -33.639 53.144 8.421   1.00 36.68  ? 3    ILE   A CA  1 
ATOM   1517 C C   . ILE   A 1 200 ? -34.996 53.328 7.745   1.00 40.08  ? 3    ILE   A C   1 
ATOM   1518 O O   . ILE   A 1 200 ? -35.163 54.183 6.841   1.00 40.25  ? 3    ILE   A O   1 
ATOM   1519 C CB  . ILE   A 1 200 ? -32.877 51.940 7.828   1.00 40.19  ? 3    ILE   A CB  1 
ATOM   1520 C CG1 . ILE   A 1 200 ? -31.425 51.935 8.352   1.00 38.16  ? 3    ILE   A CG1 1 
ATOM   1521 C CG2 . ILE   A 1 200 ? -32.943 51.949 6.306   1.00 41.93  ? 3    ILE   A CG2 1 
ATOM   1522 C CD1 . ILE   A 1 200 ? -30.732 50.621 8.188   1.00 32.47  ? 3    ILE   A CD1 1 
ATOM   1523 N N   . LYS   A 1 201 ? -35.991 52.523 8.154   1.00 41.99  ? 4    LYS   A N   1 
ATOM   1524 C CA  . LYS   A 1 201 ? -37.313 52.574 7.528   1.00 41.54  ? 4    LYS   A CA  1 
ATOM   1525 C C   . LYS   A 1 201 ? -37.952 53.959 7.708   1.00 42.22  ? 4    LYS   A C   1 
ATOM   1526 O O   . LYS   A 1 201 ? -38.658 54.433 6.819   1.00 41.46  ? 4    LYS   A O   1 
ATOM   1527 C CB  . LYS   A 1 201 ? -38.232 51.506 8.122   1.00 41.79  ? 4    LYS   A CB  1 
ATOM   1528 C CG  . LYS   A 1 201 ? -37.869 50.074 7.735   1.00 48.13  ? 4    LYS   A CG  1 
ATOM   1529 C CD  . LYS   A 1 201 ? -38.988 49.099 8.181   1.00 52.90  ? 4    LYS   A CD  1 
ATOM   1530 C CE  . LYS   A 1 201 ? -38.696 47.687 7.778   1.00 55.31  ? 4    LYS   A CE  1 
ATOM   1531 N NZ  . LYS   A 1 201 ? -39.729 46.767 8.344   1.00 56.66  ? 4    LYS   A NZ  1 
ATOM   1532 N N   . ASN   A 1 202 ? -37.771 54.574 8.879   1.00 42.96  ? 5    ASN   A N   1 
ATOM   1533 C CA  . ASN   A 1 202 ? -38.380 55.862 9.173   1.00 45.26  ? 5    ASN   A CA  1 
ATOM   1534 C C   . ASN   A 1 202 ? -37.529 57.039 8.690   1.00 44.39  ? 5    ASN   A C   1 
ATOM   1535 O O   . ASN   A 1 202 ? -37.765 58.157 9.102   1.00 44.98  ? 5    ASN   A O   1 
ATOM   1536 C CB  . ASN   A 1 202 ? -38.647 55.974 10.675  1.00 46.28  ? 5    ASN   A CB  1 
ATOM   1537 C CG  . ASN   A 1 202 ? -39.699 54.949 11.144  1.00 46.42  ? 5    ASN   A CG  1 
ATOM   1538 O OD1 . ASN   A 1 202 ? -40.721 54.789 10.474  1.00 49.41  ? 5    ASN   A OD1 1 
ATOM   1539 N ND2 . ASN   A 1 202 ? -39.464 54.291 12.294  1.00 40.44  ? 5    ASN   A ND2 1 
ATOM   1540 N N   . LYS   A 1 203 ? -36.555 56.792 7.829   1.00 45.64  ? 6    LYS   A N   1 
ATOM   1541 C CA  . LYS   A 1 203 ? -35.719 57.811 7.219   1.00 48.76  ? 6    LYS   A CA  1 
ATOM   1542 C C   . LYS   A 1 203 ? -34.788 58.487 8.219   1.00 44.79  ? 6    LYS   A C   1 
ATOM   1543 O O   . LYS   A 1 203 ? -34.223 59.544 7.928   1.00 44.31  ? 6    LYS   A O   1 
ATOM   1544 C CB  . LYS   A 1 203 ? -36.561 58.860 6.489   1.00 55.11  ? 6    LYS   A CB  1 
ATOM   1545 C CG  . LYS   A 1 203 ? -37.527 58.242 5.474   1.00 59.82  ? 6    LYS   A CG  1 
ATOM   1546 C CD  . LYS   A 1 203 ? -36.795 57.619 4.315   1.00 60.34  ? 6    LYS   A CD  1 
ATOM   1547 C CE  . LYS   A 1 203 ? -37.760 56.880 3.364   1.00 61.38  ? 6    LYS   A CE  1 
ATOM   1548 N NZ  . LYS   A 1 203 ? -38.577 57.800 2.528   1.00 61.33  ? 6    LYS   A NZ  1 
ATOM   1549 N N   . HIS   A 1 204 ? -34.608 57.897 9.386   1.00 39.97  ? 7    HIS   A N   1 
ATOM   1550 C CA  . HIS   A 1 204 ? -33.617 58.400 10.328  1.00 40.72  ? 7    HIS   A CA  1 
ATOM   1551 C C   . HIS   A 1 204 ? -32.175 58.012 9.949   1.00 41.91  ? 7    HIS   A C   1 
ATOM   1552 O O   . HIS   A 1 204 ? -31.221 58.684 10.371  1.00 42.47  ? 7    HIS   A O   1 
ATOM   1553 C CB  . HIS   A 1 204 ? -33.942 57.904 11.734  1.00 38.21  ? 7    HIS   A CB  1 
ATOM   1554 C CG  . HIS   A 1 204 ? -35.335 58.234 12.189  1.00 38.22  ? 7    HIS   A CG  1 
ATOM   1555 N ND1 . HIS   A 1 204 ? -35.865 59.542 12.110  1.00 38.06  ? 7    HIS   A ND1 1 
ATOM   1556 C CD2 . HIS   A 1 204 ? -36.308 57.456 12.727  1.00 34.80  ? 7    HIS   A CD2 1 
ATOM   1557 C CE1 . HIS   A 1 204 ? -37.106 59.526 12.591  1.00 36.75  ? 7    HIS   A CE1 1 
ATOM   1558 N NE2 . HIS   A 1 204 ? -37.389 58.277 12.980  1.00 39.09  ? 7    HIS   A NE2 1 
ATOM   1559 N N   . MET   A 1 205 ? -31.987 56.977 9.146   1.00 40.84  ? 8    MET   A N   1 
ATOM   1560 C CA  . MET   A 1 205 ? -30.662 56.548 8.713   1.00 39.62  ? 8    MET   A CA  1 
ATOM   1561 C C   . MET   A 1 205 ? -30.793 55.973 7.311   1.00 38.86  ? 8    MET   A C   1 
ATOM   1562 O O   . MET   A 1 205 ? -31.882 55.598 6.877   1.00 40.35  ? 8    MET   A O   1 
ATOM   1563 C CB  . MET   A 1 205 ? -30.032 55.497 9.664   1.00 38.29  ? 8    MET   A CB  1 
ATOM   1564 C CG  . MET   A 1 205 ? -29.602 56.020 11.030  1.00 41.78  ? 8    MET   A CG  1 
ATOM   1565 S SD  . MET   A 1 205 ? -28.294 55.012 11.850  1.00 42.34  ? 8    MET   A SD  1 
ATOM   1566 C CE  . MET   A 1 205 ? -29.147 53.431 11.966  1.00 47.50  ? 8    MET   A CE  1 
ATOM   1567 N N   . ASN   A 1 206 ? -29.672 55.898 6.614   1.00 38.85  ? 9    ASN   A N   1 
ATOM   1568 C CA  . ASN   A 1 206 ? -29.615 55.374 5.263   1.00 40.33  ? 9    ASN   A CA  1 
ATOM   1569 C C   . ASN   A 1 206 ? -28.806 54.087 5.248   1.00 42.79  ? 9    ASN   A C   1 
ATOM   1570 O O   . ASN   A 1 206 ? -27.670 54.068 5.728   1.00 41.77  ? 9    ASN   A O   1 
ATOM   1571 C CB  . ASN   A 1 206 ? -28.967 56.401 4.334   1.00 42.86  ? 9    ASN   A CB  1 
ATOM   1572 C CG  . ASN   A 1 206 ? -29.145 56.037 2.872   1.00 48.13  ? 9    ASN   A CG  1 
ATOM   1573 O OD1 . ASN   A 1 206 ? -28.609 55.055 2.388   1.00 47.82  ? 9    ASN   A OD1 1 
ATOM   1574 N ND2 . ASN   A 1 206 ? -29.906 56.869 2.142   1.00 53.75  ? 9    ASN   A ND2 1 
ATOM   1575 N N   . ALA   A 1 207 ? -29.390 52.998 4.706   1.00 45.20  ? 10   ALA   A N   1 
ATOM   1576 C CA  . ALA   A 1 207 ? -28.712 51.707 4.707   1.00 44.24  ? 10   ALA   A CA  1 
ATOM   1577 C C   . ALA   A 1 207 ? -27.371 51.770 3.993   1.00 45.06  ? 10   ALA   A C   1 
ATOM   1578 O O   . ALA   A 1 207 ? -26.520 50.905 4.242   1.00 43.12  ? 10   ALA   A O   1 
ATOM   1579 C CB  . ALA   A 1 207 ? -29.601 50.636 4.038   1.00 43.06  ? 10   ALA   A CB  1 
ATOM   1580 N N   . ASP   A 1 208 ? -27.160 52.760 3.118   1.00 42.48  ? 11   ASP   A N   1 
ATOM   1581 C CA  . ASP   A 1 208 ? -25.946 52.823 2.330   1.00 42.66  ? 11   ASP   A CA  1 
ATOM   1582 C C   . ASP   A 1 208 ? -24.822 53.574 3.042   1.00 43.06  ? 11   ASP   A C   1 
ATOM   1583 O O   . ASP   A 1 208 ? -23.709 53.646 2.521   1.00 47.28  ? 11   ASP   A O   1 
ATOM   1584 C CB  . ASP   A 1 208 ? -26.232 53.474 0.980   1.00 47.28  ? 11   ASP   A CB  1 
ATOM   1585 C CG  . ASP   A 1 208 ? -27.090 52.619 0.084   1.00 56.51  ? 11   ASP   A CG  1 
ATOM   1586 O OD1 . ASP   A 1 208 ? -26.919 51.354 0.065   1.00 58.81  ? 11   ASP   A OD1 1 
ATOM   1587 O OD2 . ASP   A 1 208 ? -27.935 53.196 -0.657  1.00 62.14  ? 11   ASP   A OD2 1 
ATOM   1588 N N   . THR   A 1 209 ? -25.074 54.172 4.196   1.00 40.53  ? 12   THR   A N   1 
ATOM   1589 C CA  . THR   A 1 209 ? -24.021 54.935 4.854   1.00 40.04  ? 12   THR   A CA  1 
ATOM   1590 C C   . THR   A 1 209 ? -22.848 54.034 5.252   1.00 38.29  ? 12   THR   A C   1 
ATOM   1591 O O   . THR   A 1 209 ? -23.052 52.957 5.817   1.00 39.47  ? 12   THR   A O   1 
ATOM   1592 C CB  . THR   A 1 209 ? -24.579 55.654 6.091   1.00 39.20  ? 12   THR   A CB  1 
ATOM   1593 O OG1 . THR   A 1 209 ? -25.655 56.536 5.708   1.00 36.86  ? 12   THR   A OG1 1 
ATOM   1594 C CG2 . THR   A 1 209 ? -23.465 56.489 6.779   1.00 38.54  ? 12   THR   A CG2 1 
ATOM   1595 N N   . ASP   A 1 210 ? -21.631 54.445 4.897   1.00 35.73  ? 13   ASP   A N   1 
ATOM   1596 C CA  . ASP   A 1 210 ? -20.415 53.730 5.267   1.00 38.20  ? 13   ASP   A CA  1 
ATOM   1597 C C   . ASP   A 1 210 ? -19.495 54.620 6.110   1.00 39.94  ? 13   ASP   A C   1 
ATOM   1598 O O   . ASP   A 1 210 ? -19.888 55.732 6.585   1.00 40.74  ? 13   ASP   A O   1 
ATOM   1599 C CB  . ASP   A 1 210 ? -19.698 53.210 4.019   1.00 40.82  ? 13   ASP   A CB  1 
ATOM   1600 C CG  . ASP   A 1 210 ? -19.333 54.336 3.052   1.00 45.53  ? 13   ASP   A CG  1 
ATOM   1601 O OD1 . ASP   A 1 210 ? -19.661 55.524 3.353   1.00 47.32  ? 13   ASP   A OD1 1 
ATOM   1602 O OD2 . ASP   A 1 210 ? -18.701 54.038 2.009   1.00 46.32  ? 13   ASP   A OD2 1 
ATOM   1603 N N   . TYR   A 1 211 ? -18.254 54.155 6.281   1.00 36.66  ? 14   TYR   A N   1 
ATOM   1604 C CA  . TYR   A 1 211 ? -17.304 54.913 7.082   1.00 36.84  ? 14   TYR   A CA  1 
ATOM   1605 C C   . TYR   A 1 211 ? -17.114 56.325 6.527   1.00 38.71  ? 14   TYR   A C   1 
ATOM   1606 O O   . TYR   A 1 211 ? -17.223 57.317 7.263   1.00 40.95  ? 14   TYR   A O   1 
ATOM   1607 C CB  . TYR   A 1 211 ? -15.959 54.216 7.160   1.00 35.78  ? 14   TYR   A CB  1 
ATOM   1608 C CG  . TYR   A 1 211 ? -15.038 54.805 8.207   1.00 32.92  ? 14   TYR   A CG  1 
ATOM   1609 C CD1 . TYR   A 1 211 ? -14.279 55.952 7.939   1.00 34.37  ? 14   TYR   A CD1 1 
ATOM   1610 C CD2 . TYR   A 1 211 ? -14.959 54.239 9.467   1.00 30.95  ? 14   TYR   A CD2 1 
ATOM   1611 C CE1 . TYR   A 1 211 ? -13.446 56.509 8.943   1.00 35.28  ? 14   TYR   A CE1 1 
ATOM   1612 C CE2 . TYR   A 1 211 ? -14.128 54.731 10.439  1.00 30.09  ? 14   TYR   A CE2 1 
ATOM   1613 C CZ  . TYR   A 1 211 ? -13.380 55.850 10.172  1.00 33.21  ? 14   TYR   A CZ  1 
ATOM   1614 O OH  . TYR   A 1 211 ? -12.564 56.330 11.212  1.00 33.64  ? 14   TYR   A OH  1 
ATOM   1615 N N   . SER   A 1 212 ? -16.805 56.470 5.265   1.00 41.74  ? 15   SER   A N   1 
ATOM   1616 C CA  . SER   A 1 212 ? -16.452 57.776 4.733   1.00 46.56  ? 15   SER   A CA  1 
ATOM   1617 C C   . SER   A 1 212 ? -17.661 58.731 4.723   1.00 45.97  ? 15   SER   A C   1 
ATOM   1618 O O   . SER   A 1 212 ? -17.516 59.866 5.112   1.00 48.38  ? 15   SER   A O   1 
ATOM   1619 C CB  . SER   A 1 212 ? -15.723 57.679 3.394   1.00 53.21  ? 15   SER   A CB  1 
ATOM   1620 O OG  . SER   A 1 212 ? -14.404 57.098 3.608   1.00 59.35  ? 15   SER   A OG  1 
ATOM   1621 N N   . ILE   A 1 213 ? -18.793 58.219 4.238   1.00 44.96  ? 16   ILE   A N   1 
ATOM   1622 C CA  . ILE   A 1 213 ? -19.977 59.106 4.251   1.00 42.72  ? 16   ILE   A CA  1 
ATOM   1623 C C   . ILE   A 1 213 ? -20.313 59.594 5.679   1.00 41.16  ? 16   ILE   A C   1 
ATOM   1624 O O   . ILE   A 1 213 ? -20.646 60.782 5.893   1.00 40.44  ? 16   ILE   A O   1 
ATOM   1625 C CB  . ILE   A 1 213 ? -21.191 58.397 3.623   1.00 44.75  ? 16   ILE   A CB  1 
ATOM   1626 C CG1 . ILE   A 1 213 ? -21.016 58.287 2.112   1.00 44.35  ? 16   ILE   A CG1 1 
ATOM   1627 C CG2 . ILE   A 1 213 ? -22.494 59.182 3.940   1.00 43.02  ? 16   ILE   A CG2 1 
ATOM   1628 C CD1 . ILE   A 1 213 ? -21.908 57.236 1.476   1.00 42.25  ? 16   ILE   A CD1 1 
ATOM   1629 N N   . ALA   A 1 214 ? -20.248 58.696 6.683   1.00 36.28  ? 17   ALA   A N   1 
ATOM   1630 C CA  . ALA   A 1 214 ? -20.602 59.111 8.037   1.00 34.82  ? 17   ALA   A CA  1 
ATOM   1631 C C   . ALA   A 1 214 ? -19.556 60.084 8.600   1.00 35.94  ? 17   ALA   A C   1 
ATOM   1632 O O   . ALA   A 1 214 ? -19.907 61.099 9.239   1.00 31.55  ? 17   ALA   A O   1 
ATOM   1633 C CB  . ALA   A 1 214 ? -20.755 57.903 8.956   1.00 32.28  ? 17   ALA   A CB  1 
ATOM   1634 N N   . GLU   A 1 215 ? -18.255 59.776 8.365   1.00 38.26  ? 18   GLU   A N   1 
ATOM   1635 C CA  . GLU   A 1 215 ? -17.195 60.654 8.874   1.00 40.09  ? 18   GLU   A CA  1 
ATOM   1636 C C   . GLU   A 1 215 ? -17.321 62.065 8.309   1.00 40.91  ? 18   GLU   A C   1 
ATOM   1637 O O   . GLU   A 1 215 ? -17.251 63.065 9.049   1.00 41.36  ? 18   GLU   A O   1 
ATOM   1638 C CB  . GLU   A 1 215 ? -15.824 60.051 8.573   1.00 38.66  ? 18   GLU   A CB  1 
ATOM   1639 C CG  . GLU   A 1 215 ? -14.664 61.016 8.917   1.00 40.58  ? 18   GLU   A CG  1 
ATOM   1640 C CD  . GLU   A 1 215 ? -13.307 60.417 8.632   1.00 39.70  ? 18   GLU   A CD  1 
ATOM   1641 O OE1 . GLU   A 1 215 ? -13.100 59.971 7.478   1.00 40.76  ? 18   GLU   A OE1 1 
ATOM   1642 O OE2 . GLU   A 1 215 ? -12.446 60.385 9.537   1.00 39.30  ? 18   GLU   A OE2 1 
ATOM   1643 N N   . ALA   A 1 216 ? -17.509 62.175 6.990   1.00 39.37  ? 19   ALA   A N   1 
ATOM   1644 C CA  . ALA   A 1 216 ? -17.599 63.496 6.362   1.00 37.36  ? 19   ALA   A CA  1 
ATOM   1645 C C   . ALA   A 1 216 ? -18.873 64.226 6.774   1.00 38.20  ? 19   ALA   A C   1 
ATOM   1646 O O   . ALA   A 1 216 ? -18.913 65.468 6.837   1.00 36.66  ? 19   ALA   A O   1 
ATOM   1647 C CB  . ALA   A 1 216 ? -17.539 63.360 4.836   1.00 36.53  ? 19   ALA   A CB  1 
ATOM   1648 N N   . ALA   A 1 217 ? -19.952 63.498 7.042   1.00 38.98  ? 20   ALA   A N   1 
ATOM   1649 C CA  . ALA   A 1 217 ? -21.181 64.184 7.437   1.00 38.26  ? 20   ALA   A CA  1 
ATOM   1650 C C   . ALA   A 1 217 ? -21.004 64.810 8.816   1.00 36.57  ? 20   ALA   A C   1 
ATOM   1651 O O   . ALA   A 1 217 ? -21.335 65.981 9.019   1.00 38.28  ? 20   ALA   A O   1 
ATOM   1652 C CB  . ALA   A 1 217 ? -22.372 63.223 7.431   1.00 36.90  ? 20   ALA   A CB  1 
ATOM   1653 N N   . PHE   A 1 218 ? -20.446 64.043 9.763   1.00 33.14  ? 21   PHE   A N   1 
ATOM   1654 C CA  . PHE   A 1 218 ? -20.224 64.591 11.101  1.00 36.79  ? 21   PHE   A CA  1 
ATOM   1655 C C   . PHE   A 1 218 ? -19.205 65.741 11.074  1.00 40.25  ? 21   PHE   A C   1 
ATOM   1656 O O   . PHE   A 1 218 ? -19.399 66.766 11.721  1.00 40.18  ? 21   PHE   A O   1 
ATOM   1657 C CB  . PHE   A 1 218 ? -19.776 63.497 12.082  1.00 31.85  ? 21   PHE   A CB  1 
ATOM   1658 C CG  . PHE   A 1 218 ? -19.696 63.963 13.484  1.00 34.30  ? 21   PHE   A CG  1 
ATOM   1659 C CD1 . PHE   A 1 218 ? -20.831 63.968 14.310  1.00 35.02  ? 21   PHE   A CD1 1 
ATOM   1660 C CD2 . PHE   A 1 218 ? -18.509 64.455 14.001  1.00 36.80  ? 21   PHE   A CD2 1 
ATOM   1661 C CE1 . PHE   A 1 218 ? -20.757 64.419 15.623  1.00 35.23  ? 21   PHE   A CE1 1 
ATOM   1662 C CE2 . PHE   A 1 218 ? -18.435 64.951 15.329  1.00 38.03  ? 21   PHE   A CE2 1 
ATOM   1663 C CZ  . PHE   A 1 218 ? -19.549 64.917 16.122  1.00 37.29  ? 21   PHE   A CZ  1 
ATOM   1664 N N   . ASN   A 1 219 ? -18.072 65.544 10.389  1.00 41.57  ? 22   ASN   A N   1 
ATOM   1665 C CA  . ASN   A 1 219 ? -16.971 66.492 10.389  1.00 42.37  ? 22   ASN   A CA  1 
ATOM   1666 C C   . ASN   A 1 219 ? -17.318 67.789 9.653   1.00 43.74  ? 22   ASN   A C   1 
ATOM   1667 O O   . ASN   A 1 219 ? -16.589 68.774 9.787   1.00 41.76  ? 22   ASN   A O   1 
ATOM   1668 C CB  . ASN   A 1 219 ? -15.726 65.852 9.779   1.00 39.82  ? 22   ASN   A CB  1 
ATOM   1669 C CG  . ASN   A 1 219 ? -15.169 64.707 10.645  1.00 39.54  ? 22   ASN   A CG  1 
ATOM   1670 O OD1 . ASN   A 1 219 ? -15.785 64.292 11.647  1.00 40.82  ? 22   ASN   A OD1 1 
ATOM   1671 N ND2 . ASN   A 1 219 ? -13.982 64.217 10.284  1.00 34.58  ? 22   ASN   A ND2 1 
ATOM   1672 N N   . LYS   A 1 220 ? -18.398 67.806 8.867   1.00 45.08  ? 23   LYS   A N   1 
ATOM   1673 C CA  . LYS   A 1 220 ? -18.916 69.014 8.248   1.00 45.46  ? 23   LYS   A CA  1 
ATOM   1674 C C   . LYS   A 1 220 ? -20.071 69.607 9.034   1.00 44.48  ? 23   LYS   A C   1 
ATOM   1675 O O   . LYS   A 1 220 ? -20.542 70.687 8.685   1.00 42.89  ? 23   LYS   A O   1 
ATOM   1676 C CB  . LYS   A 1 220 ? -19.398 68.748 6.803   1.00 45.68  ? 23   LYS   A CB  1 
ATOM   1677 C CG  . LYS   A 1 220 ? -18.255 68.581 5.811   1.00 50.43  ? 23   LYS   A CG  1 
ATOM   1678 C CD  . LYS   A 1 220 ? -18.731 67.845 4.540   1.00 54.72  ? 23   LYS   A CD  1 
ATOM   1679 C CE  . LYS   A 1 220 ? -20.169 68.244 4.168   1.00 56.85  ? 23   LYS   A CE  1 
ATOM   1680 N NZ  . LYS   A 1 220 ? -20.433 68.089 2.688   1.00 58.69  ? 23   LYS   A NZ  1 
ATOM   1681 N N   . GLY   A 1 221 ? -20.553 68.924 10.074  1.00 41.43  ? 24   GLY   A N   1 
ATOM   1682 C CA  . GLY   A 1 221 ? -21.602 69.480 10.890  1.00 41.91  ? 24   GLY   A CA  1 
ATOM   1683 C C   . GLY   A 1 221 ? -22.995 69.249 10.372  1.00 43.11  ? 24   GLY   A C   1 
ATOM   1684 O O   . GLY   A 1 221 ? -23.933 69.917 10.851  1.00 42.50  ? 24   GLY   A O   1 
ATOM   1685 N N   . GLU   A 1 222 ? -23.180 68.294 9.441   1.00 42.33  ? 25   GLU   A N   1 
ATOM   1686 C CA  . GLU   A 1 222 ? -24.521 68.003 8.947   1.00 43.25  ? 25   GLU   A CA  1 
ATOM   1687 C C   . GLU   A 1 222 ? -25.286 67.069 9.873   1.00 39.93  ? 25   GLU   A C   1 
ATOM   1688 O O   . GLU   A 1 222 ? -26.516 67.155 9.966   1.00 41.10  ? 25   GLU   A O   1 
ATOM   1689 C CB  . GLU   A 1 222 ? -24.441 67.380 7.543   1.00 47.30  ? 25   GLU   A CB  1 
ATOM   1690 C CG  . GLU   A 1 222 ? -23.805 68.284 6.498   1.00 49.01  ? 25   GLU   A CG  1 
ATOM   1691 C CD  . GLU   A 1 222 ? -23.844 67.688 5.109   1.00 51.67  ? 25   GLU   A CD  1 
ATOM   1692 O OE1 . GLU   A 1 222 ? -23.524 66.468 4.927   1.00 52.97  ? 25   GLU   A OE1 1 
ATOM   1693 O OE2 . GLU   A 1 222 ? -24.167 68.434 4.174   1.00 52.62  ? 25   GLU   A OE2 1 
ATOM   1694 N N   . THR   A 1 223 ? -24.602 66.168 10.562  1.00 37.65  ? 26   THR   A N   1 
ATOM   1695 C CA  . THR   A 1 223 ? -25.226 65.252 11.504  1.00 35.47  ? 26   THR   A CA  1 
ATOM   1696 C C   . THR   A 1 223 ? -24.686 65.536 12.894  1.00 34.96  ? 26   THR   A C   1 
ATOM   1697 O O   . THR   A 1 223 ? -23.493 65.837 13.047  1.00 35.94  ? 26   THR   A O   1 
ATOM   1698 C CB  . THR   A 1 223 ? -24.956 63.789 11.097  1.00 35.41  ? 26   THR   A CB  1 
ATOM   1699 O OG1 . THR   A 1 223 ? -25.878 62.921 11.740  1.00 36.36  ? 26   THR   A OG1 1 
ATOM   1700 C CG2 . THR   A 1 223 ? -23.531 63.351 11.429  1.00 32.84  ? 26   THR   A CG2 1 
ATOM   1701 N N   . ALA   A 1 224 ? -25.546 65.387 13.903  1.00 34.34  ? 27   ALA   A N   1 
ATOM   1702 C CA  . ALA   A 1 224 ? -25.210 65.718 15.289  1.00 34.34  ? 27   ALA   A CA  1 
ATOM   1703 C C   . ALA   A 1 224 ? -24.379 64.658 16.021  1.00 35.27  ? 27   ALA   A C   1 
ATOM   1704 O O   . ALA   A 1 224 ? -23.704 65.009 17.018  1.00 35.09  ? 27   ALA   A O   1 
ATOM   1705 C CB  . ALA   A 1 224 ? -26.494 65.965 16.068  1.00 33.96  ? 27   ALA   A CB  1 
ATOM   1706 N N   . MET   A 1 225 ? -24.431 63.383 15.585  1.00 31.39  ? 28   MET   A N   1 
ATOM   1707 C CA  . MET   A 1 225 ? -23.775 62.313 16.314  1.00 32.12  ? 28   MET   A CA  1 
ATOM   1708 C C   . MET   A 1 225 ? -23.160 61.313 15.351  1.00 32.73  ? 28   MET   A C   1 
ATOM   1709 O O   . MET   A 1 225 ? -23.658 61.077 14.231  1.00 32.99  ? 28   MET   A O   1 
ATOM   1710 C CB  . MET   A 1 225 ? -24.732 61.563 17.236  1.00 33.43  ? 28   MET   A CB  1 
ATOM   1711 C CG  . MET   A 1 225 ? -25.231 62.388 18.402  1.00 36.90  ? 28   MET   A CG  1 
ATOM   1712 S SD  . MET   A 1 225 ? -26.426 61.479 19.382  1.00 38.02  ? 28   MET   A SD  1 
ATOM   1713 C CE  . MET   A 1 225 ? -27.885 61.522 18.296  1.00 35.08  ? 28   MET   A CE  1 
ATOM   1714 N N   . THR   A 1 226 ? -22.066 60.704 15.790  1.00 33.62  ? 29   THR   A N   1 
ATOM   1715 C CA  . THR   A 1 226 ? -21.539 59.549 15.077  1.00 34.14  ? 29   THR   A CA  1 
ATOM   1716 C C   . THR   A 1 226 ? -21.037 58.534 16.110  1.00 35.92  ? 29   THR   A C   1 
ATOM   1717 O O   . THR   A 1 226 ? -21.022 58.786 17.330  1.00 35.75  ? 29   THR   A O   1 
ATOM   1718 C CB  . THR   A 1 226 ? -20.451 59.961 14.064  1.00 35.05  ? 29   THR   A CB  1 
ATOM   1719 O OG1 . THR   A 1 226 ? -20.114 58.815 13.234  1.00 38.36  ? 29   THR   A OG1 1 
ATOM   1720 C CG2 . THR   A 1 226 ? -19.194 60.456 14.762  1.00 33.94  ? 29   THR   A CG2 1 
ATOM   1721 N N   . ILE   A 1 227 ? -20.694 57.340 15.629  1.00 34.49  ? 30   ILE   A N   1 
ATOM   1722 C CA  . ILE   A 1 227 ? -20.172 56.262 16.468  1.00 33.08  ? 30   ILE   A CA  1 
ATOM   1723 C C   . ILE   A 1 227 ? -18.840 55.830 15.856  1.00 32.32  ? 30   ILE   A C   1 
ATOM   1724 O O   . ILE   A 1 227 ? -18.802 55.378 14.721  1.00 32.47  ? 30   ILE   A O   1 
ATOM   1725 C CB  . ILE   A 1 227 ? -21.149 55.056 16.538  1.00 31.05  ? 30   ILE   A CB  1 
ATOM   1726 C CG1 . ILE   A 1 227 ? -22.424 55.455 17.287  1.00 27.09  ? 30   ILE   A CG1 1 
ATOM   1727 C CG2 . ILE   A 1 227 ? -20.461 53.849 17.207  1.00 28.78  ? 30   ILE   A CG2 1 
ATOM   1728 C CD1 . ILE   A 1 227 ? -23.447 54.260 17.254  1.00 29.02  ? 30   ILE   A CD1 1 
ATOM   1729 N N   . ASN   A 1 228 ? -17.755 55.988 16.601  1.00 35.31  ? 31   ASN   A N   1 
ATOM   1730 C CA  . ASN   A 1 228 ? -16.434 55.673 16.061  1.00 36.04  ? 31   ASN   A CA  1 
ATOM   1731 C C   . ASN   A 1 228 ? -15.457 55.488 17.210  1.00 33.87  ? 31   ASN   A C   1 
ATOM   1732 O O   . ASN   A 1 228 ? -15.814 55.608 18.376  1.00 32.86  ? 31   ASN   A O   1 
ATOM   1733 C CB  . ASN   A 1 228 ? -15.967 56.748 15.067  1.00 38.61  ? 31   ASN   A CB  1 
ATOM   1734 C CG  . ASN   A 1 228 ? -15.279 56.155 13.849  1.00 41.48  ? 31   ASN   A CG  1 
ATOM   1735 O OD1 . ASN   A 1 228 ? -14.579 55.153 13.949  1.00 44.81  ? 31   ASN   A OD1 1 
ATOM   1736 N ND2 . ASN   A 1 228 ? -15.518 56.715 12.706  1.00 42.76  ? 31   ASN   A ND2 1 
ATOM   1737 N N   . GLY   A 1 229 ? -14.222 55.120 16.853  1.00 36.03  ? 32   GLY   A N   1 
ATOM   1738 C CA  . GLY   A 1 229 ? -13.179 54.825 17.814  1.00 36.83  ? 32   GLY   A CA  1 
ATOM   1739 C C   . GLY   A 1 229 ? -12.178 55.979 17.916  1.00 39.63  ? 32   GLY   A C   1 
ATOM   1740 O O   . GLY   A 1 229 ? -12.314 57.021 17.251  1.00 36.60  ? 32   GLY   A O   1 
ATOM   1741 N N   . PRO   A 1 230 ? -11.168 55.810 18.781  1.00 40.75  ? 33   PRO   A N   1 
ATOM   1742 C CA  . PRO   A 1 230 ? -10.216 56.907 19.025  1.00 42.35  ? 33   PRO   A CA  1 
ATOM   1743 C C   . PRO   A 1 230 ? -9.436  57.329 17.774  1.00 42.64  ? 33   PRO   A C   1 
ATOM   1744 O O   . PRO   A 1 230 ? -9.055  58.526 17.672  1.00 40.67  ? 33   PRO   A O   1 
ATOM   1745 C CB  . PRO   A 1 230 ? -9.277  56.326 20.088  1.00 43.28  ? 33   PRO   A CB  1 
ATOM   1746 C CG  . PRO   A 1 230 ? -10.097 55.267 20.764  1.00 41.35  ? 33   PRO   A CG  1 
ATOM   1747 C CD  . PRO   A 1 230 ? -10.963 54.679 19.693  1.00 40.09  ? 33   PRO   A CD  1 
ATOM   1748 N N   . TRP   A 1 231 ? -9.207  56.396 16.819  1.00 37.71  ? 34   TRP   A N   1 
ATOM   1749 C CA  . TRP   A 1 231 ? -8.464  56.739 15.617  1.00 38.34  ? 34   TRP   A CA  1 
ATOM   1750 C C   . TRP   A 1 231 ? -9.131  57.849 14.801  1.00 38.66  ? 34   TRP   A C   1 
ATOM   1751 O O   . TRP   A 1 231 ? -8.475  58.485 13.980  1.00 39.66  ? 34   TRP   A O   1 
ATOM   1752 C CB  . TRP   A 1 231 ? -8.302  55.517 14.733  1.00 36.17  ? 34   TRP   A CB  1 
ATOM   1753 C CG  . TRP   A 1 231 ? -9.619  54.899 14.422  1.00 35.13  ? 34   TRP   A CG  1 
ATOM   1754 C CD1 . TRP   A 1 231 ? -10.461 55.217 13.398  1.00 34.72  ? 34   TRP   A CD1 1 
ATOM   1755 C CD2 . TRP   A 1 231 ? -10.246 53.845 15.155  1.00 33.83  ? 34   TRP   A CD2 1 
ATOM   1756 N NE1 . TRP   A 1 231 ? -11.580 54.390 13.450  1.00 35.04  ? 34   TRP   A NE1 1 
ATOM   1757 C CE2 . TRP   A 1 231 ? -11.467 53.567 14.532  1.00 33.02  ? 34   TRP   A CE2 1 
ATOM   1758 C CE3 . TRP   A 1 231 ? -9.896  53.134 16.310  1.00 35.40  ? 34   TRP   A CE3 1 
ATOM   1759 C CZ2 . TRP   A 1 231 ? -12.341 52.624 15.014  1.00 33.84  ? 34   TRP   A CZ2 1 
ATOM   1760 C CZ3 . TRP   A 1 231 ? -10.768 52.170 16.772  1.00 36.90  ? 34   TRP   A CZ3 1 
ATOM   1761 C CH2 . TRP   A 1 231 ? -11.979 51.925 16.105  1.00 34.67  ? 34   TRP   A CH2 1 
ATOM   1762 N N   . ALA   A 1 232 ? -10.421 58.062 14.974  1.00 39.51  ? 35   ALA   A N   1 
ATOM   1763 C CA  . ALA   A 1 232 ? -11.162 59.042 14.204  1.00 38.25  ? 35   ALA   A CA  1 
ATOM   1764 C C   . ALA   A 1 232 ? -11.057 60.444 14.791  1.00 40.19  ? 35   ALA   A C   1 
ATOM   1765 O O   . ALA   A 1 232 ? -11.526 61.387 14.155  1.00 43.44  ? 35   ALA   A O   1 
ATOM   1766 C CB  . ALA   A 1 232 ? -12.645 58.655 14.132  1.00 35.37  ? 35   ALA   A CB  1 
ATOM   1767 N N   . TRP   A 1 233 ? -10.467 60.608 15.972  1.00 42.09  ? 36   TRP   A N   1 
ATOM   1768 C CA  . TRP   A 1 233 ? -10.470 61.915 16.609  1.00 44.05  ? 36   TRP   A CA  1 
ATOM   1769 C C   . TRP   A 1 233 ? -9.633  62.908 15.832  1.00 47.25  ? 36   TRP   A C   1 
ATOM   1770 O O   . TRP   A 1 233 ? -9.948  64.103 15.812  1.00 48.79  ? 36   TRP   A O   1 
ATOM   1771 C CB  . TRP   A 1 233 ? -9.967  61.812 18.050  1.00 42.91  ? 36   TRP   A CB  1 
ATOM   1772 C CG  . TRP   A 1 233 ? -10.807 60.929 18.930  1.00 41.72  ? 36   TRP   A CG  1 
ATOM   1773 C CD1 . TRP   A 1 233 ? -12.080 60.495 18.686  1.00 40.67  ? 36   TRP   A CD1 1 
ATOM   1774 C CD2 . TRP   A 1 233 ? -10.439 60.385 20.202  1.00 40.82  ? 36   TRP   A CD2 1 
ATOM   1775 N NE1 . TRP   A 1 233 ? -12.536 59.750 19.728  1.00 41.04  ? 36   TRP   A NE1 1 
ATOM   1776 C CE2 . TRP   A 1 233 ? -11.540 59.622 20.658  1.00 41.68  ? 36   TRP   A CE2 1 
ATOM   1777 C CE3 . TRP   A 1 233 ? -9.288  60.454 20.986  1.00 40.36  ? 36   TRP   A CE3 1 
ATOM   1778 C CZ2 . TRP   A 1 233 ? -11.522 58.924 21.858  1.00 43.14  ? 36   TRP   A CZ2 1 
ATOM   1779 C CZ3 . TRP   A 1 233 ? -9.262  59.761 22.184  1.00 42.33  ? 36   TRP   A CZ3 1 
ATOM   1780 C CH2 . TRP   A 1 233 ? -10.378 59.010 22.615  1.00 44.56  ? 36   TRP   A CH2 1 
ATOM   1781 N N   . SER   A 1 234 ? -8.550  62.488 15.199  1.00 47.99  ? 37   SER   A N   1 
ATOM   1782 C CA  . SER   A 1 234 ? -7.672  63.438 14.539  1.00 50.62  ? 37   SER   A CA  1 
ATOM   1783 C C   . SER   A 1 234 ? -8.427  64.186 13.431  1.00 47.50  ? 37   SER   A C   1 
ATOM   1784 O O   . SER   A 1 234 ? -8.288  65.408 13.323  1.00 48.29  ? 37   SER   A O   1 
ATOM   1785 C CB  . SER   A 1 234 ? -6.389  62.767 14.041  1.00 56.07  ? 37   SER   A CB  1 
ATOM   1786 O OG  . SER   A 1 234 ? -5.489  62.569 15.127  1.00 60.20  ? 37   SER   A OG  1 
ATOM   1787 N N   . ASN   A 1 235 ? -9.181  63.413 12.638  1.00 41.80  ? 38   ASN   A N   1 
ATOM   1788 C CA  . ASN   A 1 235 ? -9.876  64.114 11.536  1.00 43.56  ? 38   ASN   A CA  1 
ATOM   1789 C C   . ASN   A 1 235 ? -10.965 65.079 12.047  1.00 45.13  ? 38   ASN   A C   1 
ATOM   1790 O O   . ASN   A 1 235 ? -11.199 66.135 11.436  1.00 47.33  ? 38   ASN   A O   1 
ATOM   1791 C CB  . ASN   A 1 235 ? -10.472 63.168 10.522  1.00 42.15  ? 38   ASN   A CB  1 
ATOM   1792 C CG  . ASN   A 1 235 ? -9.417  62.463 9.712   1.00 44.39  ? 38   ASN   A CG  1 
ATOM   1793 O OD1 . ASN   A 1 235 ? -8.269  62.874 9.713   1.00 43.46  ? 38   ASN   A OD1 1 
ATOM   1794 N ND2 . ASN   A 1 235 ? -9.800  61.357 9.034   1.00 45.70  ? 38   ASN   A ND2 1 
ATOM   1795 N N   . ILE   A 1 236 ? -11.611 64.752 13.157  1.00 42.49  ? 39   ILE   A N   1 
ATOM   1796 C CA  . ILE   A 1 236 ? -12.564 65.700 13.733  1.00 43.02  ? 39   ILE   A CA  1 
ATOM   1797 C C   . ILE   A 1 236 ? -11.843 66.936 14.248  1.00 41.26  ? 39   ILE   A C   1 
ATOM   1798 O O   . ILE   A 1 236 ? -12.314 68.051 14.049  1.00 41.72  ? 39   ILE   A O   1 
ATOM   1799 C CB  . ILE   A 1 236 ? -13.372 65.033 14.864  1.00 44.46  ? 39   ILE   A CB  1 
ATOM   1800 C CG1 . ILE   A 1 236 ? -13.775 63.597 14.477  1.00 40.11  ? 39   ILE   A CG1 1 
ATOM   1801 C CG2 . ILE   A 1 236 ? -14.569 65.919 15.183  1.00 44.46  ? 39   ILE   A CG2 1 
ATOM   1802 C CD1 . ILE   A 1 236 ? -14.700 62.973 15.454  1.00 39.72  ? 39   ILE   A CD1 1 
ATOM   1803 N N   . ASP   A 1 237 ? -10.689 66.758 14.893  1.00 42.83  ? 40   ASP   A N   1 
ATOM   1804 C CA  . ASP   A 1 237 ? -9.903  67.906 15.356  1.00 46.94  ? 40   ASP   A CA  1 
ATOM   1805 C C   . ASP   A 1 237 ? -9.659  68.897 14.218  1.00 48.87  ? 40   ASP   A C   1 
ATOM   1806 O O   . ASP   A 1 237 ? -9.884  70.109 14.373  1.00 47.99  ? 40   ASP   A O   1 
ATOM   1807 C CB  . ASP   A 1 237 ? -8.582  67.442 15.959  1.00 48.69  ? 40   ASP   A CB  1 
ATOM   1808 C CG  . ASP   A 1 237 ? -8.755  66.805 17.363  1.00 52.21  ? 40   ASP   A CG  1 
ATOM   1809 O OD1 . ASP   A 1 237 ? -9.786  67.066 18.046  1.00 53.24  ? 40   ASP   A OD1 1 
ATOM   1810 O OD2 . ASP   A 1 237 ? -7.853  66.053 17.787  1.00 52.20  ? 40   ASP   A OD2 1 
ATOM   1811 N N   . THR   A 1 238 ? -9.272  68.374 13.047  1.00 49.07  ? 41   THR   A N   1 
ATOM   1812 C CA  . THR   A 1 238 ? -8.970  69.214 11.904  1.00 50.79  ? 41   THR   A CA  1 
ATOM   1813 C C   . THR   A 1 238 ? -10.196 69.970 11.395  1.00 50.74  ? 41   THR   A C   1 
ATOM   1814 O O   . THR   A 1 238 ? -10.081 71.116 10.946  1.00 50.68  ? 41   THR   A O   1 
ATOM   1815 C CB  . THR   A 1 238 ? -8.370  68.361 10.789  1.00 48.89  ? 41   THR   A CB  1 
ATOM   1816 O OG1 . THR   A 1 238 ? -7.319  67.579 11.341  1.00 46.73  ? 41   THR   A OG1 1 
ATOM   1817 C CG2 . THR   A 1 238 ? -7.802  69.285 9.676   1.00 49.97  ? 41   THR   A CG2 1 
ATOM   1818 N N   . SER   A 1 239 ? -11.361 69.325 11.389  1.00 48.57  ? 42   SER   A N   1 
ATOM   1819 C CA  . SER   A 1 239 ? -12.582 70.036 10.976  1.00 48.35  ? 42   SER   A CA  1 
ATOM   1820 C C   . SER   A 1 239 ? -13.018 71.080 11.972  1.00 47.57  ? 42   SER   A C   1 
ATOM   1821 O O   . SER   A 1 239 ? -14.026 71.744 11.709  1.00 48.49  ? 42   SER   A O   1 
ATOM   1822 C CB  . SER   A 1 239 ? -13.716 69.031 10.797  1.00 48.92  ? 42   SER   A CB  1 
ATOM   1823 O OG  . SER   A 1 239 ? -14.092 68.544 12.077  1.00 48.24  ? 42   SER   A OG  1 
ATOM   1824 N N   . ALA   A 1 240 ? -12.338 71.187 13.126  1.00 44.02  ? 43   ALA   A N   1 
ATOM   1825 C CA  . ALA   A 1 240 ? -12.646 72.214 14.128  1.00 46.32  ? 43   ALA   A CA  1 
ATOM   1826 C C   . ALA   A 1 240 ? -14.055 72.063 14.693  1.00 49.90  ? 43   ALA   A C   1 
ATOM   1827 O O   . ALA   A 1 240 ? -14.564 72.962 15.329  1.00 51.71  ? 43   ALA   A O   1 
ATOM   1828 C CB  . ALA   A 1 240 ? -12.440 73.650 13.584  1.00 43.04  ? 43   ALA   A CB  1 
ATOM   1829 N N   . VAL   A 1 241 ? -14.694 70.914 14.497  1.00 49.39  ? 44   VAL   A N   1 
ATOM   1830 C CA  . VAL   A 1 241 ? -15.986 70.678 15.128  1.00 48.66  ? 44   VAL   A CA  1 
ATOM   1831 C C   . VAL   A 1 241 ? -15.815 70.592 16.651  1.00 47.83  ? 44   VAL   A C   1 
ATOM   1832 O O   . VAL   A 1 241 ? -14.800 70.095 17.193  1.00 46.06  ? 44   VAL   A O   1 
ATOM   1833 C CB  . VAL   A 1 241 ? -16.619 69.380 14.566  1.00 50.10  ? 44   VAL   A CB  1 
ATOM   1834 C CG1 . VAL   A 1 241 ? -17.743 68.885 15.494  1.00 49.35  ? 44   VAL   A CG1 1 
ATOM   1835 C CG2 . VAL   A 1 241 ? -17.183 69.642 13.154  1.00 50.01  ? 44   VAL   A CG2 1 
ATOM   1836 N N   . ASN   A 1 242 ? -16.828 71.079 17.347  1.00 49.15  ? 45   ASN   A N   1 
ATOM   1837 C CA  . ASN   A 1 242 ? -16.829 71.120 18.815  1.00 47.74  ? 45   ASN   A CA  1 
ATOM   1838 C C   . ASN   A 1 242 ? -17.483 69.837 19.333  1.00 42.70  ? 45   ASN   A C   1 
ATOM   1839 O O   . ASN   A 1 242 ? -18.682 69.776 19.569  1.00 42.26  ? 45   ASN   A O   1 
ATOM   1840 C CB  . ASN   A 1 242 ? -17.557 72.368 19.298  1.00 45.13  ? 45   ASN   A CB  1 
ATOM   1841 C CG  . ASN   A 1 242 ? -17.452 72.565 20.780  1.00 48.26  ? 45   ASN   A CG  1 
ATOM   1842 O OD1 . ASN   A 1 242 ? -16.566 72.026 21.431  1.00 48.41  ? 45   ASN   A OD1 1 
ATOM   1843 N ND2 . ASN   A 1 242 ? -18.363 73.380 21.337  1.00 52.32  ? 45   ASN   A ND2 1 
ATOM   1844 N N   . TYR   A 1 243 ? -16.683 68.825 19.549  1.00 40.77  ? 46   TYR   A N   1 
ATOM   1845 C CA  . TYR   A 1 243 ? -17.230 67.485 19.766  1.00 40.25  ? 46   TYR   A CA  1 
ATOM   1846 C C   . TYR   A 1 243 ? -16.920 67.011 21.177  1.00 41.46  ? 46   TYR   A C   1 
ATOM   1847 O O   . TYR   A 1 243 ? -15.925 67.443 21.797  1.00 43.29  ? 46   TYR   A O   1 
ATOM   1848 C CB  . TYR   A 1 243 ? -16.705 66.481 18.741  1.00 35.39  ? 46   TYR   A CB  1 
ATOM   1849 C CG  . TYR   A 1 243 ? -15.238 66.135 18.896  1.00 37.89  ? 46   TYR   A CG  1 
ATOM   1850 C CD1 . TYR   A 1 243 ? -14.244 67.012 18.487  1.00 38.38  ? 46   TYR   A CD1 1 
ATOM   1851 C CD2 . TYR   A 1 243 ? -14.853 64.885 19.413  1.00 40.20  ? 46   TYR   A CD2 1 
ATOM   1852 C CE1 . TYR   A 1 243 ? -12.911 66.715 18.616  1.00 39.51  ? 46   TYR   A CE1 1 
ATOM   1853 C CE2 . TYR   A 1 243 ? -13.492 64.520 19.533  1.00 41.65  ? 46   TYR   A CE2 1 
ATOM   1854 C CZ  . TYR   A 1 243 ? -12.525 65.452 19.129  1.00 41.05  ? 46   TYR   A CZ  1 
ATOM   1855 O OH  . TYR   A 1 243 ? -11.197 65.146 19.245  1.00 39.86  ? 46   TYR   A OH  1 
ATOM   1856 N N   . GLY   A 1 244 ? -17.817 66.177 21.690  1.00 38.31  ? 47   GLY   A N   1 
ATOM   1857 C CA  . GLY   A 1 244 ? -17.593 65.433 22.906  1.00 39.39  ? 47   GLY   A CA  1 
ATOM   1858 C C   . GLY   A 1 244 ? -17.579 63.949 22.611  1.00 39.81  ? 47   GLY   A C   1 
ATOM   1859 O O   . GLY   A 1 244 ? -18.067 63.506 21.553  1.00 36.45  ? 47   GLY   A O   1 
ATOM   1860 N N   . VAL   A 1 245 ? -16.969 63.175 23.509  1.00 44.03  ? 48   VAL   A N   1 
ATOM   1861 C CA  . VAL   A 1 245 ? -16.884 61.694 23.382  1.00 40.95  ? 48   VAL   A CA  1 
ATOM   1862 C C   . VAL   A 1 245 ? -17.499 61.144 24.664  1.00 39.27  ? 48   VAL   A C   1 
ATOM   1863 O O   . VAL   A 1 245 ? -17.063 61.516 25.756  1.00 38.19  ? 48   VAL   A O   1 
ATOM   1864 C CB  . VAL   A 1 245 ? -15.442 61.226 23.211  1.00 36.51  ? 48   VAL   A CB  1 
ATOM   1865 C CG1 . VAL   A 1 245 ? -15.365 59.659 23.274  1.00 33.85  ? 48   VAL   A CG1 1 
ATOM   1866 C CG2 . VAL   A 1 245 ? -14.856 61.781 21.950  1.00 34.48  ? 48   VAL   A CG2 1 
ATOM   1867 N N   . THR   A 1 246 ? -18.519 60.287 24.536  1.00 35.43  ? 49   THR   A N   1 
ATOM   1868 C CA  . THR   A 1 246 ? -19.314 59.971 25.721  1.00 36.34  ? 49   THR   A CA  1 
ATOM   1869 C C   . THR   A 1 246 ? -19.858 58.531 25.636  1.00 38.14  ? 49   THR   A C   1 
ATOM   1870 O O   . THR   A 1 246 ? -19.575 57.767 24.688  1.00 38.54  ? 49   THR   A O   1 
ATOM   1871 C CB  . THR   A 1 246 ? -20.450 60.989 25.895  1.00 34.22  ? 49   THR   A CB  1 
ATOM   1872 O OG1 . THR   A 1 246 ? -21.047 60.832 27.186  1.00 38.78  ? 49   THR   A OG1 1 
ATOM   1873 C CG2 . THR   A 1 246 ? -21.509 60.777 24.841  1.00 34.14  ? 49   THR   A CG2 1 
ATOM   1874 N N   . VAL   A 1 247 ? -20.638 58.172 26.660  1.00 39.06  ? 50   VAL   A N   1 
ATOM   1875 C CA  . VAL   A 1 247 ? -21.145 56.806 26.773  1.00 40.85  ? 50   VAL   A CA  1 
ATOM   1876 C C   . VAL   A 1 247 ? -22.167 56.577 25.665  1.00 42.01  ? 50   VAL   A C   1 
ATOM   1877 O O   . VAL   A 1 247 ? -22.981 57.464 25.364  1.00 42.67  ? 50   VAL   A O   1 
ATOM   1878 C CB  . VAL   A 1 247 ? -21.758 56.611 28.172  1.00 40.95  ? 50   VAL   A CB  1 
ATOM   1879 C CG1 . VAL   A 1 247 ? -22.763 57.735 28.444  1.00 42.22  ? 50   VAL   A CG1 1 
ATOM   1880 C CG2 . VAL   A 1 247 ? -22.411 55.233 28.320  1.00 37.36  ? 50   VAL   A CG2 1 
ATOM   1881 N N   . LEU   A 1 248 ? -22.114 55.364 25.062  1.00 40.93  ? 51   LEU   A N   1 
ATOM   1882 C CA  . LEU   A 1 248 ? -23.085 55.041 24.024  1.00 40.20  ? 51   LEU   A CA  1 
ATOM   1883 C C   . LEU   A 1 248 ? -24.500 55.012 24.610  1.00 43.54  ? 51   LEU   A C   1 
ATOM   1884 O O   . LEU   A 1 248 ? -24.679 54.879 25.813  1.00 44.24  ? 51   LEU   A O   1 
ATOM   1885 C CB  . LEU   A 1 248 ? -22.763 53.724 23.378  1.00 37.65  ? 51   LEU   A CB  1 
ATOM   1886 C CG  . LEU   A 1 248 ? -21.543 53.660 22.463  1.00 36.38  ? 51   LEU   A CG  1 
ATOM   1887 C CD1 . LEU   A 1 248 ? -20.970 52.199 22.502  1.00 37.87  ? 51   LEU   A CD1 1 
ATOM   1888 C CD2 . LEU   A 1 248 ? -21.850 54.057 21.040  1.00 29.99  ? 51   LEU   A CD2 1 
ATOM   1889 N N   . PRO   A 1 249 ? -25.524 55.177 23.772  1.00 46.49  ? 52   PRO   A N   1 
ATOM   1890 C CA  . PRO   A 1 249 ? -26.893 55.210 24.305  1.00 47.55  ? 52   PRO   A CA  1 
ATOM   1891 C C   . PRO   A 1 249 ? -27.303 53.826 24.775  1.00 49.07  ? 52   PRO   A C   1 
ATOM   1892 O O   . PRO   A 1 249 ? -26.839 52.809 24.257  1.00 49.96  ? 52   PRO   A O   1 
ATOM   1893 C CB  . PRO   A 1 249 ? -27.741 55.660 23.109  1.00 46.74  ? 52   PRO   A CB  1 
ATOM   1894 C CG  . PRO   A 1 249 ? -26.754 56.185 22.083  1.00 47.22  ? 52   PRO   A CG  1 
ATOM   1895 C CD  . PRO   A 1 249 ? -25.488 55.421 22.319  1.00 47.59  ? 52   PRO   A CD  1 
ATOM   1896 N N   . THR   A 1 250 ? -28.160 53.798 25.783  1.00 44.65  ? 53   THR   A N   1 
ATOM   1897 C CA  . THR   A 1 250 ? -28.701 52.540 26.196  1.00 43.00  ? 53   THR   A CA  1 
ATOM   1898 C C   . THR   A 1 250 ? -29.823 52.109 25.247  1.00 42.55  ? 53   THR   A C   1 
ATOM   1899 O O   . THR   A 1 250 ? -30.431 52.922 24.530  1.00 39.46  ? 53   THR   A O   1 
ATOM   1900 C CB  . THR   A 1 250 ? -29.232 52.605 27.631  1.00 44.05  ? 53   THR   A CB  1 
ATOM   1901 O OG1 . THR   A 1 250 ? -30.366 53.493 27.687  1.00 45.74  ? 53   THR   A OG1 1 
ATOM   1902 C CG2 . THR   A 1 250 ? -28.140 53.088 28.557  1.00 44.12  ? 53   THR   A CG2 1 
ATOM   1903 N N   . PHE   A 1 251 ? -30.114 50.797 25.278  1.00 41.18  ? 54   PHE   A N   1 
ATOM   1904 C CA  . PHE   A 1 251 ? -31.234 50.243 24.541  1.00 40.34  ? 54   PHE   A CA  1 
ATOM   1905 C C   . PHE   A 1 251 ? -32.054 49.420 25.513  1.00 40.88  ? 54   PHE   A C   1 
ATOM   1906 O O   . PHE   A 1 251 ? -31.506 48.562 26.210  1.00 39.21  ? 54   PHE   A O   1 
ATOM   1907 C CB  . PHE   A 1 251 ? -30.768 49.395 23.359  1.00 38.23  ? 54   PHE   A CB  1 
ATOM   1908 C CG  . PHE   A 1 251 ? -31.889 48.763 22.612  1.00 40.44  ? 54   PHE   A CG  1 
ATOM   1909 C CD1 . PHE   A 1 251 ? -32.864 49.543 22.012  1.00 42.13  ? 54   PHE   A CD1 1 
ATOM   1910 C CD2 . PHE   A 1 251 ? -31.955 47.369 22.455  1.00 40.75  ? 54   PHE   A CD2 1 
ATOM   1911 C CE1 . PHE   A 1 251 ? -33.921 48.947 21.293  1.00 43.79  ? 54   PHE   A CE1 1 
ATOM   1912 C CE2 . PHE   A 1 251 ? -32.993 46.782 21.735  1.00 41.27  ? 54   PHE   A CE2 1 
ATOM   1913 C CZ  . PHE   A 1 251 ? -33.979 47.574 21.169  1.00 43.00  ? 54   PHE   A CZ  1 
ATOM   1914 N N   . LYS   A 1 252 ? -33.362 49.699 25.569  1.00 43.81  ? 55   LYS   A N   1 
ATOM   1915 C CA  . LYS   A 1 252 ? -34.263 48.972 26.456  1.00 47.47  ? 55   LYS   A CA  1 
ATOM   1916 C C   . LYS   A 1 252 ? -33.725 48.965 27.889  1.00 48.23  ? 55   LYS   A C   1 
ATOM   1917 O O   . LYS   A 1 252 ? -33.768 47.942 28.592  1.00 50.05  ? 55   LYS   A O   1 
ATOM   1918 C CB  . LYS   A 1 252 ? -34.493 47.554 25.950  1.00 48.10  ? 55   LYS   A CB  1 
ATOM   1919 C CG  . LYS   A 1 252 ? -35.155 47.478 24.583  1.00 48.51  ? 55   LYS   A CG  1 
ATOM   1920 C CD  . LYS   A 1 252 ? -35.315 46.026 24.140  1.00 48.93  ? 55   LYS   A CD  1 
ATOM   1921 C CE  . LYS   A 1 252 ? -36.317 45.283 25.019  1.00 50.93  ? 55   LYS   A CE  1 
ATOM   1922 N NZ  . LYS   A 1 252 ? -36.568 43.908 24.466  1.00 51.88  ? 55   LYS   A NZ  1 
ATOM   1923 N N   . GLY   A 1 253 ? -33.164 50.104 28.307  1.00 44.17  ? 56   GLY   A N   1 
ATOM   1924 C CA  . GLY   A 1 253 ? -32.680 50.279 29.655  1.00 43.38  ? 56   GLY   A CA  1 
ATOM   1925 C C   . GLY   A 1 253 ? -31.292 49.757 29.917  1.00 46.64  ? 56   GLY   A C   1 
ATOM   1926 O O   . GLY   A 1 253 ? -30.752 49.998 31.018  1.00 50.77  ? 56   GLY   A O   1 
ATOM   1927 N N   . GLN   A 1 254 ? -30.679 49.036 28.980  1.00 47.73  ? 57   GLN   A N   1 
ATOM   1928 C CA  . GLN   A 1 254 ? -29.377 48.430 29.212  1.00 49.71  ? 57   GLN   A CA  1 
ATOM   1929 C C   . GLN   A 1 254 ? -28.297 49.053 28.354  1.00 45.57  ? 57   GLN   A C   1 
ATOM   1930 O O   . GLN   A 1 254 ? -28.576 49.677 27.319  1.00 43.11  ? 57   GLN   A O   1 
ATOM   1931 C CB  . GLN   A 1 254 ? -29.426 46.930 28.941  1.00 54.17  ? 57   GLN   A CB  1 
ATOM   1932 C CG  . GLN   A 1 254 ? -30.621 46.248 29.647  1.00 59.17  ? 57   GLN   A CG  1 
ATOM   1933 C CD  . GLN   A 1 254 ? -31.053 44.989 28.945  1.00 62.35  ? 57   GLN   A CD  1 
ATOM   1934 O OE1 . GLN   A 1 254 ? -31.751 45.038 27.924  1.00 62.49  ? 57   GLN   A OE1 1 
ATOM   1935 N NE2 . GLN   A 1 254 ? -30.637 43.841 29.484  1.00 66.00  ? 57   GLN   A NE2 1 
ATOM   1936 N N   . PRO   A 1 255 ? -27.040 48.929 28.760  1.00 46.11  ? 58   PRO   A N   1 
ATOM   1937 C CA  . PRO   A 1 255 ? -25.953 49.602 28.037  1.00 45.94  ? 58   PRO   A CA  1 
ATOM   1938 C C   . PRO   A 1 255 ? -25.704 48.966 26.683  1.00 47.06  ? 58   PRO   A C   1 
ATOM   1939 O O   . PRO   A 1 255 ? -25.882 47.754 26.480  1.00 46.24  ? 58   PRO   A O   1 
ATOM   1940 C CB  . PRO   A 1 255 ? -24.735 49.395 28.946  1.00 45.38  ? 58   PRO   A CB  1 
ATOM   1941 C CG  . PRO   A 1 255 ? -25.050 48.106 29.718  1.00 45.89  ? 58   PRO   A CG  1 
ATOM   1942 C CD  . PRO   A 1 255 ? -26.552 48.157 29.936  1.00 46.74  ? 58   PRO   A CD  1 
ATOM   1943 N N   . SER   A 1 256 ? -25.293 49.787 25.735  1.00 45.09  ? 59   SER   A N   1 
ATOM   1944 C CA  . SER   A 1 256 ? -24.710 49.256 24.516  1.00 43.84  ? 59   SER   A CA  1 
ATOM   1945 C C   . SER   A 1 256 ? -23.398 48.588 24.856  1.00 43.32  ? 59   SER   A C   1 
ATOM   1946 O O   . SER   A 1 256 ? -22.625 49.066 25.706  1.00 42.85  ? 59   SER   A O   1 
ATOM   1947 C CB  . SER   A 1 256 ? -24.504 50.352 23.479  1.00 43.64  ? 59   SER   A CB  1 
ATOM   1948 O OG  . SER   A 1 256 ? -25.641 50.507 22.627  1.00 43.61  ? 59   SER   A OG  1 
ATOM   1949 N N   . LYS   A 1 257 ? -23.115 47.448 24.231  1.00 43.03  ? 60   LYS   A N   1 
ATOM   1950 C CA  . LYS   A 1 257 ? -21.976 46.613 24.598  1.00 46.44  ? 60   LYS   A CA  1 
ATOM   1951 C C   . LYS   A 1 257 ? -21.083 46.441 23.380  1.00 45.18  ? 60   LYS   A C   1 
ATOM   1952 O O   . LYS   A 1 257 ? -21.252 45.498 22.600  1.00 48.36  ? 60   LYS   A O   1 
ATOM   1953 C CB  . LYS   A 1 257 ? -22.446 45.283 25.162  1.00 50.50  ? 60   LYS   A CB  1 
ATOM   1954 C CG  . LYS   A 1 257 ? -22.893 45.384 26.599  1.00 55.20  ? 60   LYS   A CG  1 
ATOM   1955 C CD  . LYS   A 1 257 ? -23.957 44.310 26.941  1.00 60.28  ? 60   LYS   A CD  1 
ATOM   1956 C CE  . LYS   A 1 257 ? -23.560 42.946 26.447  1.00 63.51  ? 60   LYS   A CE  1 
ATOM   1957 N NZ  . LYS   A 1 257 ? -22.349 42.413 27.145  1.00 67.15  ? 60   LYS   A NZ  1 
ATOM   1958 N N   . PRO   A 1 258 ? -20.119 47.303 23.202  1.00 41.05  ? 61   PRO   A N   1 
ATOM   1959 C CA  . PRO   A 1 258 ? -19.237 47.153 22.064  1.00 39.57  ? 61   PRO   A CA  1 
ATOM   1960 C C   . PRO   A 1 258 ? -18.190 46.070 22.247  1.00 43.66  ? 61   PRO   A C   1 
ATOM   1961 O O   . PRO   A 1 258 ? -17.759 45.849 23.325  1.00 46.20  ? 61   PRO   A O   1 
ATOM   1962 C CB  . PRO   A 1 258 ? -18.534 48.474 22.041  1.00 38.18  ? 61   PRO   A CB  1 
ATOM   1963 C CG  . PRO   A 1 258 ? -18.538 48.921 23.437  1.00 36.34  ? 61   PRO   A CG  1 
ATOM   1964 C CD  . PRO   A 1 258 ? -19.836 48.513 23.956  1.00 36.71  ? 61   PRO   A CD  1 
ATOM   1965 N N   . PHE   A 1 259 ? -17.819 45.400 21.184  1.00 42.55  ? 62   PHE   A N   1 
ATOM   1966 C CA  . PHE   A 1 259 ? -16.797 44.431 21.252  1.00 42.17  ? 62   PHE   A CA  1 
ATOM   1967 C C   . PHE   A 1 259 ? -15.509 45.180 21.357  1.00 42.31  ? 62   PHE   A C   1 
ATOM   1968 O O   . PHE   A 1 259 ? -15.182 45.930 20.508  1.00 40.78  ? 62   PHE   A O   1 
ATOM   1969 C CB  . PHE   A 1 259 ? -16.798 43.579 20.012  1.00 43.59  ? 62   PHE   A CB  1 
ATOM   1970 C CG  . PHE   A 1 259 ? -17.305 42.212 20.240  1.00 49.53  ? 62   PHE   A CG  1 
ATOM   1971 C CD1 . PHE   A 1 259 ? -17.110 41.595 21.426  1.00 52.56  ? 62   PHE   A CD1 1 
ATOM   1972 C CD2 . PHE   A 1 259 ? -17.995 41.570 19.289  1.00 52.53  ? 62   PHE   A CD2 1 
ATOM   1973 C CE1 . PHE   A 1 259 ? -17.569 40.338 21.652  1.00 56.26  ? 62   PHE   A CE1 1 
ATOM   1974 C CE2 . PHE   A 1 259 ? -18.487 40.329 19.501  1.00 58.45  ? 62   PHE   A CE2 1 
ATOM   1975 C CZ  . PHE   A 1 259 ? -18.266 39.704 20.683  1.00 60.11  ? 62   PHE   A CZ  1 
ATOM   1976 N N   . VAL   A 1 260 ? -14.782 44.979 22.425  1.00 41.00  ? 63   VAL   A N   1 
ATOM   1977 C CA  . VAL   A 1 260 ? -13.535 45.656 22.592  1.00 40.66  ? 63   VAL   A CA  1 
ATOM   1978 C C   . VAL   A 1 260 ? -12.405 44.912 21.907  1.00 41.39  ? 63   VAL   A C   1 
ATOM   1979 O O   . VAL   A 1 260 ? -12.328 43.718 21.978  1.00 42.45  ? 63   VAL   A O   1 
ATOM   1980 C CB  . VAL   A 1 260 ? -13.194 45.829 24.059  1.00 42.36  ? 63   VAL   A CB  1 
ATOM   1981 C CG1 . VAL   A 1 260 ? -11.934 46.596 24.219  1.00 40.53  ? 63   VAL   A CG1 1 
ATOM   1982 C CG2 . VAL   A 1 260 ? -14.314 46.457 24.822  1.00 40.74  ? 63   VAL   A CG2 1 
ATOM   1983 N N   . GLY   A 1 261 ? -11.553 45.641 21.224  1.00 40.05  ? 64   GLY   A N   1 
ATOM   1984 C CA  . GLY   A 1 261 ? -10.422 45.058 20.525  1.00 39.19  ? 64   GLY   A CA  1 
ATOM   1985 C C   . GLY   A 1 261 ? -9.125  45.647 21.054  1.00 40.28  ? 64   GLY   A C   1 
ATOM   1986 O O   . GLY   A 1 261 ? -9.080  46.821 21.476  1.00 41.58  ? 64   GLY   A O   1 
ATOM   1987 N N   . VAL   A 1 262 ? -8.080  44.811 21.087  1.00 37.79  ? 65   VAL   A N   1 
ATOM   1988 C CA  . VAL   A 1 262 ? -6.731  45.243 21.432  1.00 36.60  ? 65   VAL   A CA  1 
ATOM   1989 C C   . VAL   A 1 262 ? -5.907  45.239 20.157  1.00 36.79  ? 65   VAL   A C   1 
ATOM   1990 O O   . VAL   A 1 262 ? -5.626  44.175 19.578  1.00 33.11  ? 65   VAL   A O   1 
ATOM   1991 C CB  . VAL   A 1 262 ? -6.086  44.341 22.492  1.00 38.15  ? 65   VAL   A CB  1 
ATOM   1992 C CG1 . VAL   A 1 262 ? -4.685  44.812 22.788  1.00 38.07  ? 65   VAL   A CG1 1 
ATOM   1993 C CG2 . VAL   A 1 262 ? -6.931  44.279 23.778  1.00 37.51  ? 65   VAL   A CG2 1 
ATOM   1994 N N   . LEU   A 1 263 ? -5.585  46.435 19.652  1.00 36.16  ? 66   LEU   A N   1 
ATOM   1995 C CA  . LEU   A 1 263 ? -4.600  46.502 18.567  1.00 34.52  ? 66   LEU   A CA  1 
ATOM   1996 C C   . LEU   A 1 263 ? -3.316  45.765 18.964  1.00 34.69  ? 66   LEU   A C   1 
ATOM   1997 O O   . LEU   A 1 263 ? -2.739  46.016 20.035  1.00 38.87  ? 66   LEU   A O   1 
ATOM   1998 C CB  . LEU   A 1 263 ? -4.303  47.974 18.256  1.00 31.50  ? 66   LEU   A CB  1 
ATOM   1999 C CG  . LEU   A 1 263 ? -3.324  48.262 17.135  1.00 33.20  ? 66   LEU   A CG  1 
ATOM   2000 C CD1 . LEU   A 1 263 ? -3.886  47.805 15.826  1.00 33.13  ? 66   LEU   A CD1 1 
ATOM   2001 C CD2 . LEU   A 1 263 ? -3.037  49.811 17.108  1.00 33.78  ? 66   LEU   A CD2 1 
ATOM   2002 N N   . SER   A 1 264 ? -2.846  44.878 18.109  1.00 36.10  ? 67   SER   A N   1 
ATOM   2003 C CA  . SER   A 1 264 ? -1.706  44.054 18.481  1.00 38.70  ? 67   SER   A CA  1 
ATOM   2004 C C   . SER   A 1 264 ? -0.834  43.755 17.296  1.00 39.08  ? 67   SER   A C   1 
ATOM   2005 O O   . SER   A 1 264 ? -1.286  43.821 16.137  1.00 39.75  ? 67   SER   A O   1 
ATOM   2006 C CB  . SER   A 1 264 ? -2.125  42.718 19.110  1.00 40.38  ? 67   SER   A CB  1 
ATOM   2007 O OG  . SER   A 1 264 ? -3.257  42.872 19.957  1.00 40.16  ? 67   SER   A OG  1 
ATOM   2008 N N   . ALA   A 1 265 ? 0.458   43.492 17.549  1.00 34.34  ? 68   ALA   A N   1 
ATOM   2009 C CA  . ALA   A 1 265 ? 1.455   43.366 16.516  1.00 33.55  ? 68   ALA   A CA  1 
ATOM   2010 C C   . ALA   A 1 265 ? 2.021   41.950 16.551  1.00 37.73  ? 68   ALA   A C   1 
ATOM   2011 O O   . ALA   A 1 265 ? 2.622   41.538 17.562  1.00 39.42  ? 68   ALA   A O   1 
ATOM   2012 C CB  . ALA   A 1 265 ? 2.567   44.400 16.706  1.00 31.65  ? 68   ALA   A CB  1 
ATOM   2013 N N   . GLY   A 1 266 ? 1.801   41.202 15.475  1.00 37.16  ? 69   GLY   A N   1 
ATOM   2014 C CA  . GLY   A 1 266 ? 2.223   39.810 15.377  1.00 36.47  ? 69   GLY   A CA  1 
ATOM   2015 C C   . GLY   A 1 266 ? 3.410   39.692 14.449  1.00 38.26  ? 69   GLY   A C   1 
ATOM   2016 O O   . GLY   A 1 266 ? 3.559   40.479 13.497  1.00 42.29  ? 69   GLY   A O   1 
ATOM   2017 N N   . ILE   A 1 267 ? 4.283   38.743 14.745  1.00 38.70  ? 70   ILE   A N   1 
ATOM   2018 C CA  . ILE   A 1 267 ? 5.477   38.501 13.939  1.00 40.33  ? 70   ILE   A CA  1 
ATOM   2019 C C   . ILE   A 1 267 ? 5.230   37.289 13.056  1.00 41.70  ? 70   ILE   A C   1 
ATOM   2020 O O   . ILE   A 1 267 ? 4.865   36.232 13.561  1.00 45.03  ? 70   ILE   A O   1 
ATOM   2021 C CB  . ILE   A 1 267 ? 6.708   38.292 14.839  1.00 40.53  ? 70   ILE   A CB  1 
ATOM   2022 C CG1 . ILE   A 1 267 ? 7.054   39.603 15.548  1.00 40.63  ? 70   ILE   A CG1 1 
ATOM   2023 C CG2 . ILE   A 1 267 ? 7.894   37.776 14.010  1.00 38.79  ? 70   ILE   A CG2 1 
ATOM   2024 C CD1 . ILE   A 1 267 ? 8.005   39.447 16.712  1.00 42.32  ? 70   ILE   A CD1 1 
ATOM   2025 N N   . ASN   A 1 268 ? 5.428   37.451 11.754  1.00 41.58  ? 71   ASN   A N   1 
ATOM   2026 C CA  . ASN   A 1 268 ? 5.167   36.407 10.765  1.00 43.34  ? 71   ASN   A CA  1 
ATOM   2027 C C   . ASN   A 1 268 ? 6.030   35.163 11.040  1.00 43.84  ? 71   ASN   A C   1 
ATOM   2028 O O   . ASN   A 1 268 ? 7.254   35.246 11.200  1.00 45.86  ? 71   ASN   A O   1 
ATOM   2029 C CB  . ASN   A 1 268 ? 5.462   36.951 9.359   1.00 44.11  ? 71   ASN   A CB  1 
ATOM   2030 C CG  . ASN   A 1 268 ? 4.918   36.068 8.252   1.00 47.01  ? 71   ASN   A CG  1 
ATOM   2031 O OD1 . ASN   A 1 268 ? 5.010   34.843 8.301   1.00 50.32  ? 71   ASN   A OD1 1 
ATOM   2032 N ND2 . ASN   A 1 268 ? 4.379   36.686 7.234   1.00 46.78  ? 71   ASN   A ND2 1 
ATOM   2033 N N   . ALA   A 1 269 ? 5.391   34.012 11.105  1.00 42.56  ? 72   ALA   A N   1 
ATOM   2034 C CA  . ALA   A 1 269 ? 6.146   32.783 11.401  1.00 43.75  ? 72   ALA   A CA  1 
ATOM   2035 C C   . ALA   A 1 269 ? 7.216   32.492 10.348  1.00 45.61  ? 72   ALA   A C   1 
ATOM   2036 O O   . ALA   A 1 269 ? 8.211   31.810 10.646  1.00 44.72  ? 72   ALA   A O   1 
ATOM   2037 C CB  . ALA   A 1 269 ? 5.195   31.591 11.524  1.00 40.61  ? 72   ALA   A CB  1 
ATOM   2038 N N   . ALA   A 1 270 ? 7.069   33.034 9.136   1.00 48.14  ? 73   ALA   A N   1 
ATOM   2039 C CA  . ALA   A 1 270 ? 8.041   32.779 8.074   1.00 50.69  ? 73   ALA   A CA  1 
ATOM   2040 C C   . ALA   A 1 270 ? 9.034   33.918 7.903   1.00 48.51  ? 73   ALA   A C   1 
ATOM   2041 O O   . ALA   A 1 270 ? 9.805   33.903 6.940   1.00 47.80  ? 73   ALA   A O   1 
ATOM   2042 C CB  . ALA   A 1 270 ? 7.333   32.511 6.737   1.00 50.01  ? 73   ALA   A CB  1 
ATOM   2043 N N   . SER   A 1 271 ? 9.057   34.883 8.792   1.00 46.48  ? 74   SER   A N   1 
ATOM   2044 C CA  . SER   A 1 271 ? 9.942   36.013 8.616   1.00 47.01  ? 74   SER   A CA  1 
ATOM   2045 C C   . SER   A 1 271 ? 11.350  35.678 9.052   1.00 49.04  ? 74   SER   A C   1 
ATOM   2046 O O   . SER   A 1 271 ? 11.560  35.136 10.157  1.00 51.56  ? 74   SER   A O   1 
ATOM   2047 C CB  . SER   A 1 271 ? 9.462   37.237 9.381   1.00 46.88  ? 74   SER   A CB  1 
ATOM   2048 O OG  . SER   A 1 271 ? 10.547  38.101 9.715   1.00 46.33  ? 74   SER   A OG  1 
ATOM   2049 N N   . PRO   A 1 272 ? 12.393  35.971 8.279   1.00 50.31  ? 75   PRO   A N   1 
ATOM   2050 C CA  . PRO   A 1 272 ? 13.775  35.777 8.712   1.00 51.76  ? 75   PRO   A CA  1 
ATOM   2051 C C   . PRO   A 1 272 ? 14.293  36.848 9.652   1.00 50.86  ? 75   PRO   A C   1 
ATOM   2052 O O   . PRO   A 1 272 ? 15.432  36.734 10.112  1.00 50.19  ? 75   PRO   A O   1 
ATOM   2053 C CB  . PRO   A 1 272 ? 14.544  35.802 7.379   1.00 53.05  ? 75   PRO   A CB  1 
ATOM   2054 C CG  . PRO   A 1 272 ? 13.754  36.767 6.545   1.00 52.61  ? 75   PRO   A CG  1 
ATOM   2055 C CD  . PRO   A 1 272 ? 12.293  36.500 6.909   1.00 51.39  ? 75   PRO   A CD  1 
ATOM   2056 N N   . ASN   A 1 273 ? 13.494  37.874 9.965   1.00 49.84  ? 76   ASN   A N   1 
ATOM   2057 C CA  . ASN   A 1 273 ? 13.935  39.010 10.769  1.00 48.99  ? 76   ASN   A CA  1 
ATOM   2058 C C   . ASN   A 1 273 ? 13.220  39.075 12.121  1.00 47.30  ? 76   ASN   A C   1 
ATOM   2059 O O   . ASN   A 1 273 ? 12.836  40.152 12.560  1.00 46.69  ? 76   ASN   A O   1 
ATOM   2060 C CB  . ASN   A 1 273 ? 13.718  40.315 10.008  1.00 49.13  ? 76   ASN   A CB  1 
ATOM   2061 C CG  . ASN   A 1 273 ? 14.141  40.225 8.546   1.00 48.99  ? 76   ASN   A CG  1 
ATOM   2062 O OD1 . ASN   A 1 273 ? 15.343  40.128 8.236   1.00 52.91  ? 76   ASN   A OD1 1 
ATOM   2063 N ND2 . ASN   A 1 273 ? 13.166  40.265 7.643   1.00 44.44  ? 76   ASN   A ND2 1 
ATOM   2064 N N   . LYS   A 1 274 ? 13.050  37.932 12.799  1.00 46.16  ? 77   LYS   A N   1 
ATOM   2065 C CA  . LYS   A 1 274 ? 12.272  37.912 14.034  1.00 44.34  ? 77   LYS   A CA  1 
ATOM   2066 C C   . LYS   A 1 274 ? 12.986  38.636 15.171  1.00 45.68  ? 77   LYS   A C   1 
ATOM   2067 O O   . LYS   A 1 274 ? 12.326  39.279 16.000  1.00 44.22  ? 77   LYS   A O   1 
ATOM   2068 C CB  . LYS   A 1 274 ? 11.954  36.475 14.446  1.00 42.08  ? 77   LYS   A CB  1 
ATOM   2069 C CG  . LYS   A 1 274 ? 11.102  35.698 13.455  1.00 40.68  ? 77   LYS   A CG  1 
ATOM   2070 C CD  . LYS   A 1 274 ? 10.721  34.317 14.056  1.00 41.48  ? 77   LYS   A CD  1 
ATOM   2071 C CE  . LYS   A 1 274 ? 9.818   33.557 13.134  1.00 43.18  ? 77   LYS   A CE  1 
ATOM   2072 N NZ  . LYS   A 1 274 ? 10.491  33.223 11.826  1.00 45.16  ? 77   LYS   A NZ  1 
ATOM   2073 N N   . GLU   A 1 275 ? 14.331  38.538 15.243  1.00 47.57  ? 78   GLU   A N   1 
ATOM   2074 C CA  . GLU   A 1 275 ? 15.063  39.286 16.260  1.00 47.99  ? 78   GLU   A CA  1 
ATOM   2075 C C   . GLU   A 1 275 ? 14.965  40.790 16.012  1.00 48.30  ? 78   GLU   A C   1 
ATOM   2076 O O   . GLU   A 1 275 ? 14.823  41.569 16.964  1.00 50.52  ? 78   GLU   A O   1 
ATOM   2077 C CB  . GLU   A 1 275 ? 16.522  38.856 16.308  1.00 52.33  ? 78   GLU   A CB  1 
ATOM   2078 C CG  . GLU   A 1 275 ? 16.763  37.525 16.996  1.00 59.79  ? 78   GLU   A CG  1 
ATOM   2079 C CD  . GLU   A 1 275 ? 16.424  37.548 18.480  1.00 65.40  ? 78   GLU   A CD  1 
ATOM   2080 O OE1 . GLU   A 1 275 ? 16.951  38.413 19.214  1.00 66.14  ? 78   GLU   A OE1 1 
ATOM   2081 O OE2 . GLU   A 1 275 ? 15.635  36.672 18.920  1.00 68.60  ? 78   GLU   A OE2 1 
ATOM   2082 N N   . LEU   A 1 276 ? 15.060  41.221 14.751  1.00 46.24  ? 79   LEU   A N   1 
ATOM   2083 C CA  . LEU   A 1 276 ? 14.883  42.634 14.432  1.00 47.22  ? 79   LEU   A CA  1 
ATOM   2084 C C   . LEU   A 1 276 ? 13.493  43.113 14.844  1.00 45.54  ? 79   LEU   A C   1 
ATOM   2085 O O   . LEU   A 1 276 ? 13.341  44.153 15.479  1.00 44.72  ? 79   LEU   A O   1 
ATOM   2086 C CB  . LEU   A 1 276 ? 15.109  42.864 12.934  1.00 47.59  ? 79   LEU   A CB  1 
ATOM   2087 C CG  . LEU   A 1 276 ? 16.486  43.400 12.497  1.00 51.23  ? 79   LEU   A CG  1 
ATOM   2088 C CD1 . LEU   A 1 276 ? 17.616  42.562 13.035  1.00 53.30  ? 79   LEU   A CD1 1 
ATOM   2089 C CD2 . LEU   A 1 276 ? 16.577  43.446 10.969  1.00 52.36  ? 79   LEU   A CD2 1 
ATOM   2090 N N   . ALA   A 1 277 ? 12.461  42.355 14.477  1.00 45.07  ? 80   ALA   A N   1 
ATOM   2091 C CA  . ALA   A 1 277 ? 11.089  42.759 14.775  1.00 43.78  ? 80   ALA   A CA  1 
ATOM   2092 C C   . ALA   A 1 277 ? 10.836  42.824 16.274  1.00 43.28  ? 80   ALA   A C   1 
ATOM   2093 O O   . ALA   A 1 277 ? 10.196  43.778 16.764  1.00 41.89  ? 80   ALA   A O   1 
ATOM   2094 C CB  . ALA   A 1 277 ? 10.101  41.790 14.104  1.00 41.11  ? 80   ALA   A CB  1 
ATOM   2095 N N   . LYS   A 1 278 ? 11.318  41.824 17.017  1.00 43.09  ? 81   LYS   A N   1 
ATOM   2096 C CA  . LYS   A 1 278 ? 11.232  41.892 18.468  1.00 40.40  ? 81   LYS   A CA  1 
ATOM   2097 C C   . LYS   A 1 278 ? 11.932  43.169 18.997  1.00 40.84  ? 81   LYS   A C   1 
ATOM   2098 O O   . LYS   A 1 278 ? 11.421  43.850 19.909  1.00 40.40  ? 81   LYS   A O   1 
ATOM   2099 C CB  . LYS   A 1 278 ? 11.862  40.633 19.056  1.00 39.37  ? 81   LYS   A CB  1 
ATOM   2100 C CG  . LYS   A 1 278 ? 11.940  40.625 20.591  1.00 43.07  ? 81   LYS   A CG  1 
ATOM   2101 C CD  . LYS   A 1 278 ? 12.474  39.238 21.078  1.00 48.04  ? 81   LYS   A CD  1 
ATOM   2102 C CE  . LYS   A 1 278 ? 12.428  39.124 22.607  1.00 49.65  ? 81   LYS   A CE  1 
ATOM   2103 N NZ  . LYS   A 1 278 ? 13.417  40.005 23.224  1.00 51.88  ? 81   LYS   A NZ  1 
ATOM   2104 N N   . GLU   A 1 279 ? 13.103  43.494 18.452  1.00 41.76  ? 82   GLU   A N   1 
ATOM   2105 C CA  . GLU   A 1 279 ? 13.831  44.650 18.925  1.00 45.47  ? 82   GLU   A CA  1 
ATOM   2106 C C   . GLU   A 1 279 ? 13.044  45.926 18.637  1.00 43.95  ? 82   GLU   A C   1 
ATOM   2107 O O   . GLU   A 1 279 ? 12.931  46.804 19.496  1.00 42.46  ? 82   GLU   A O   1 
ATOM   2108 C CB  . GLU   A 1 279 ? 15.227  44.667 18.280  1.00 49.55  ? 82   GLU   A CB  1 
ATOM   2109 C CG  . GLU   A 1 279 ? 16.028  45.948 18.533  1.00 53.18  ? 82   GLU   A CG  1 
ATOM   2110 C CD  . GLU   A 1 279 ? 16.448  46.103 19.988  1.00 57.43  ? 82   GLU   A CD  1 
ATOM   2111 O OE1 . GLU   A 1 279 ? 16.190  45.178 20.790  1.00 58.80  ? 82   GLU   A OE1 1 
ATOM   2112 O OE2 . GLU   A 1 279 ? 17.032  47.165 20.336  1.00 59.34  ? 82   GLU   A OE2 1 
ATOM   2113 N N   . PHE   A 1 280 ? 12.453  46.017 17.443  1.00 44.75  ? 83   PHE   A N   1 
ATOM   2114 C CA  . PHE   A 1 280 ? 11.672  47.199 17.086  1.00 43.55  ? 83   PHE   A CA  1 
ATOM   2115 C C   . PHE   A 1 280 ? 10.438  47.308 17.959  1.00 42.50  ? 83   PHE   A C   1 
ATOM   2116 O O   . PHE   A 1 280 ? 10.145  48.387 18.513  1.00 42.07  ? 83   PHE   A O   1 
ATOM   2117 C CB  . PHE   A 1 280 ? 11.287  47.131 15.598  1.00 42.68  ? 83   PHE   A CB  1 
ATOM   2118 C CG  . PHE   A 1 280 ? 10.287  48.162 15.167  1.00 40.89  ? 83   PHE   A CG  1 
ATOM   2119 C CD1 . PHE   A 1 280 ? 10.705  49.459 14.812  1.00 40.12  ? 83   PHE   A CD1 1 
ATOM   2120 C CD2 . PHE   A 1 280 ? 8.953   47.845 15.060  1.00 39.68  ? 83   PHE   A CD2 1 
ATOM   2121 C CE1 . PHE   A 1 280 ? 9.821   50.398 14.386  1.00 41.64  ? 83   PHE   A CE1 1 
ATOM   2122 C CE2 . PHE   A 1 280 ? 8.010   48.794 14.662  1.00 39.97  ? 83   PHE   A CE2 1 
ATOM   2123 C CZ  . PHE   A 1 280 ? 8.457   50.091 14.304  1.00 43.55  ? 83   PHE   A CZ  1 
ATOM   2124 N N   . LEU   A 1 281 ? 9.691   46.190 18.106  1.00 40.75  ? 84   LEU   A N   1 
ATOM   2125 C CA  . LEU   A 1 281 ? 8.431   46.289 18.834  1.00 40.86  ? 84   LEU   A CA  1 
ATOM   2126 C C   . LEU   A 1 281 ? 8.653   46.563 20.319  1.00 42.07  ? 84   LEU   A C   1 
ATOM   2127 O O   . LEU   A 1 281 ? 7.924   47.358 20.908  1.00 43.91  ? 84   LEU   A O   1 
ATOM   2128 C CB  . LEU   A 1 281 ? 7.610   45.026 18.650  1.00 40.17  ? 84   LEU   A CB  1 
ATOM   2129 C CG  . LEU   A 1 281 ? 7.158   44.822 17.221  1.00 42.05  ? 84   LEU   A CG  1 
ATOM   2130 C CD1 . LEU   A 1 281 ? 6.467   43.419 17.052  1.00 31.29  ? 84   LEU   A CD1 1 
ATOM   2131 C CD2 . LEU   A 1 281 ? 6.253   45.989 16.749  1.00 39.50  ? 84   LEU   A CD2 1 
ATOM   2132 N N   . GLU   A 1 282 ? 9.662   45.931 20.930  1.00 42.78  ? 85   GLU   A N   1 
ATOM   2133 C CA  . GLU   A 1 282 ? 9.866   46.050 22.373  1.00 44.75  ? 85   GLU   A CA  1 
ATOM   2134 C C   . GLU   A 1 282 ? 10.611  47.321 22.767  1.00 47.40  ? 85   GLU   A C   1 
ATOM   2135 O O   . GLU   A 1 282 ? 10.278  47.941 23.790  1.00 45.43  ? 85   GLU   A O   1 
ATOM   2136 C CB  . GLU   A 1 282 ? 10.637  44.828 22.902  1.00 46.34  ? 85   GLU   A CB  1 
ATOM   2137 C CG  . GLU   A 1 282 ? 9.801   43.592 23.138  1.00 44.82  ? 85   GLU   A CG  1 
ATOM   2138 C CD  . GLU   A 1 282 ? 10.605  42.467 23.829  1.00 50.45  ? 85   GLU   A CD  1 
ATOM   2139 O OE1 . GLU   A 1 282 ? 11.622  42.768 24.517  1.00 53.42  ? 85   GLU   A OE1 1 
ATOM   2140 O OE2 . GLU   A 1 282 ? 10.208  41.277 23.676  1.00 50.50  ? 85   GLU   A OE2 1 
ATOM   2141 N N   . ASN   A 1 283 ? 11.631  47.715 22.002  1.00 49.46  ? 86   ASN   A N   1 
ATOM   2142 C CA  . ASN   A 1 283 ? 12.548  48.781 22.426  1.00 50.99  ? 86   ASN   A CA  1 
ATOM   2143 C C   . ASN   A 1 283 ? 12.365  50.094 21.667  1.00 50.18  ? 86   ASN   A C   1 
ATOM   2144 O O   . ASN   A 1 283 ? 13.042  51.070 21.981  1.00 50.22  ? 86   ASN   A O   1 
ATOM   2145 C CB  . ASN   A 1 283 ? 13.995  48.329 22.292  1.00 52.92  ? 86   ASN   A CB  1 
ATOM   2146 C CG  . ASN   A 1 283 ? 14.349  47.234 23.268  1.00 56.90  ? 86   ASN   A CG  1 
ATOM   2147 O OD1 . ASN   A 1 283 ? 13.947  47.288 24.436  1.00 59.29  ? 86   ASN   A OD1 1 
ATOM   2148 N ND2 . ASN   A 1 283 ? 15.104  46.201 22.791  1.00 55.78  ? 86   ASN   A ND2 1 
ATOM   2149 N N   . TYR   A 1 284 ? 11.504  50.139 20.648  1.00 50.65  ? 87   TYR   A N   1 
ATOM   2150 C CA  . TYR   A 1 284 ? 11.217  51.380 19.939  1.00 48.40  ? 87   TYR   A CA  1 
ATOM   2151 C C   . TYR   A 1 284 ? 9.739   51.724 19.970  1.00 49.62  ? 87   TYR   A C   1 
ATOM   2152 O O   . TYR   A 1 284 ? 9.379   52.847 20.381  1.00 53.22  ? 87   TYR   A O   1 
ATOM   2153 C CB  . TYR   A 1 284 ? 11.706  51.267 18.483  1.00 46.16  ? 87   TYR   A CB  1 
ATOM   2154 C CG  . TYR   A 1 284 ? 13.216  51.251 18.364  1.00 46.98  ? 87   TYR   A CG  1 
ATOM   2155 C CD1 . TYR   A 1 284 ? 13.940  50.101 18.696  1.00 49.29  ? 87   TYR   A CD1 1 
ATOM   2156 C CD2 . TYR   A 1 284 ? 13.924  52.363 17.933  1.00 45.33  ? 87   TYR   A CD2 1 
ATOM   2157 C CE1 . TYR   A 1 284 ? 15.313  50.063 18.596  1.00 48.99  ? 87   TYR   A CE1 1 
ATOM   2158 C CE2 . TYR   A 1 284 ? 15.294  52.342 17.834  1.00 46.39  ? 87   TYR   A CE2 1 
ATOM   2159 C CZ  . TYR   A 1 284 ? 15.989  51.192 18.167  1.00 46.86  ? 87   TYR   A CZ  1 
ATOM   2160 O OH  . TYR   A 1 284 ? 17.341  51.144 18.068  1.00 45.66  ? 87   TYR   A OH  1 
ATOM   2161 N N   . LEU   A 1 285 ? 8.863   50.799 19.548  1.00 46.17  ? 88   LEU   A N   1 
ATOM   2162 C CA  . LEU   A 1 285 ? 7.439   51.111 19.450  1.00 43.59  ? 88   LEU   A CA  1 
ATOM   2163 C C   . LEU   A 1 285 ? 6.816   51.191 20.831  1.00 42.38  ? 88   LEU   A C   1 
ATOM   2164 O O   . LEU   A 1 285 ? 6.224   52.215 21.201  1.00 39.20  ? 88   LEU   A O   1 
ATOM   2165 C CB  . LEU   A 1 285 ? 6.701   50.054 18.592  1.00 39.67  ? 88   LEU   A CB  1 
ATOM   2166 C CG  . LEU   A 1 285 ? 5.187   50.274 18.546  1.00 37.64  ? 88   LEU   A CG  1 
ATOM   2167 C CD1 . LEU   A 1 285 ? 4.867   51.784 18.200  1.00 35.68  ? 88   LEU   A CD1 1 
ATOM   2168 C CD2 . LEU   A 1 285 ? 4.468   49.371 17.586  1.00 36.00  ? 88   LEU   A CD2 1 
ATOM   2169 N N   . LEU   A 1 286 ? 6.928   50.104 21.607  1.00 41.59  ? 89   LEU   A N   1 
ATOM   2170 C CA  . LEU   A 1 286 ? 6.234   49.991 22.895  1.00 40.38  ? 89   LEU   A CA  1 
ATOM   2171 C C   . LEU   A 1 286 ? 7.014   50.749 23.987  1.00 43.85  ? 89   LEU   A C   1 
ATOM   2172 O O   . LEU   A 1 286 ? 7.394   50.238 25.019  1.00 42.71  ? 89   LEU   A O   1 
ATOM   2173 C CB  . LEU   A 1 286 ? 6.064   48.534 23.254  1.00 38.92  ? 89   LEU   A CB  1 
ATOM   2174 C CG  . LEU   A 1 286 ? 4.827   47.937 22.612  1.00 38.04  ? 89   LEU   A CG  1 
ATOM   2175 C CD1 . LEU   A 1 286 ? 4.756   46.446 22.804  1.00 36.80  ? 89   LEU   A CD1 1 
ATOM   2176 C CD2 . LEU   A 1 286 ? 3.576   48.645 23.193  1.00 39.73  ? 89   LEU   A CD2 1 
ATOM   2177 N N   . THR   A 1 287 ? 7.226   52.052 23.697  1.00 46.02  ? 90   THR   A N   1 
ATOM   2178 C CA  . THR   A 1 287 ? 7.892   52.982 24.597  1.00 45.53  ? 90   THR   A CA  1 
ATOM   2179 C C   . THR   A 1 287 ? 7.079   54.286 24.614  1.00 45.65  ? 90   THR   A C   1 
ATOM   2180 O O   . THR   A 1 287 ? 6.227   54.515 23.744  1.00 44.09  ? 90   THR   A O   1 
ATOM   2181 C CB  . THR   A 1 287 ? 9.343   53.271 24.162  1.00 45.23  ? 90   THR   A CB  1 
ATOM   2182 O OG1 . THR   A 1 287 ? 9.327   54.217 23.111  1.00 42.41  ? 90   THR   A OG1 1 
ATOM   2183 C CG2 . THR   A 1 287 ? 10.001  52.000 23.615  1.00 47.97  ? 90   THR   A CG2 1 
ATOM   2184 N N   . ASP   A 1 288 ? 7.343   55.125 25.627  1.00 45.80  ? 91   ASP   A N   1 
ATOM   2185 C CA  . ASP   A 1 288 ? 6.640   56.392 25.745  1.00 46.67  ? 91   ASP   A CA  1 
ATOM   2186 C C   . ASP   A 1 288 ? 6.735   57.186 24.460  1.00 44.88  ? 91   ASP   A C   1 
ATOM   2187 O O   . ASP   A 1 288 ? 5.720   57.656 23.937  1.00 43.95  ? 91   ASP   A O   1 
ATOM   2188 C CB  . ASP   A 1 288 ? 7.215   57.214 26.920  1.00 51.29  ? 91   ASP   A CB  1 
ATOM   2189 C CG  . ASP   A 1 288 ? 6.671   56.768 28.277  1.00 53.93  ? 91   ASP   A CG  1 
ATOM   2190 O OD1 . ASP   A 1 288 ? 5.602   56.104 28.322  1.00 54.34  ? 91   ASP   A OD1 1 
ATOM   2191 O OD2 . ASP   A 1 288 ? 7.318   57.052 29.299  1.00 56.15  ? 91   ASP   A OD2 1 
ATOM   2192 N N   . GLU   A 1 289 ? 7.953   57.344 23.929  1.00 46.95  ? 92   GLU   A N   1 
ATOM   2193 C CA  . GLU   A 1 289 ? 8.125   58.138 22.708  1.00 50.66  ? 92   GLU   A CA  1 
ATOM   2194 C C   . GLU   A 1 289 ? 7.556   57.418 21.487  1.00 48.59  ? 92   GLU   A C   1 
ATOM   2195 O O   . GLU   A 1 289 ? 7.003   58.055 20.581  1.00 47.83  ? 92   GLU   A O   1 
ATOM   2196 C CB  . GLU   A 1 289 ? 9.593   58.474 22.487  1.00 56.32  ? 92   GLU   A CB  1 
ATOM   2197 C CG  . GLU   A 1 289 ? 10.481  57.261 22.300  1.00 62.05  ? 92   GLU   A CG  1 
ATOM   2198 C CD  . GLU   A 1 289 ? 11.147  56.788 23.614  1.00 66.69  ? 92   GLU   A CD  1 
ATOM   2199 O OE1 . GLU   A 1 289 ? 10.804  57.373 24.703  1.00 70.88  ? 92   GLU   A OE1 1 
ATOM   2200 O OE2 . GLU   A 1 289 ? 12.005  55.853 23.542  1.00 62.58  ? 92   GLU   A OE2 1 
ATOM   2201 N N   . GLY   A 1 290 ? 7.661   56.074 21.451  1.00 45.63  ? 93   GLY   A N   1 
ATOM   2202 C CA  . GLY   A 1 290 ? 7.189   55.349 20.282  1.00 42.25  ? 93   GLY   A CA  1 
ATOM   2203 C C   . GLY   A 1 290 ? 5.683   55.452 20.117  1.00 40.52  ? 93   GLY   A C   1 
ATOM   2204 O O   . GLY   A 1 290 ? 5.176   55.774 19.032  1.00 38.77  ? 93   GLY   A O   1 
ATOM   2205 N N   . LEU   A 1 291 ? 4.944   55.181 21.196  1.00 41.10  ? 94   LEU   A N   1 
ATOM   2206 C CA  . LEU   A 1 291 ? 3.482   55.228 21.110  1.00 42.53  ? 94   LEU   A CA  1 
ATOM   2207 C C   . LEU   A 1 291 ? 2.996   56.670 20.918  1.00 44.88  ? 94   LEU   A C   1 
ATOM   2208 O O   . LEU   A 1 291 ? 2.039   56.911 20.175  1.00 44.14  ? 94   LEU   A O   1 
ATOM   2209 C CB  . LEU   A 1 291 ? 2.840   54.614 22.366  1.00 41.98  ? 94   LEU   A CB  1 
ATOM   2210 C CG  . LEU   A 1 291 ? 3.152   53.168 22.679  1.00 43.67  ? 94   LEU   A CG  1 
ATOM   2211 C CD1 . LEU   A 1 291 ? 2.457   52.740 23.976  1.00 43.38  ? 94   LEU   A CD1 1 
ATOM   2212 C CD2 . LEU   A 1 291 ? 2.758   52.276 21.531  1.00 45.04  ? 94   LEU   A CD2 1 
ATOM   2213 N N   . GLU   A 1 292 ? 3.646   57.639 21.587  1.00 47.27  ? 95   GLU   A N   1 
ATOM   2214 C CA  . GLU   A 1 292 ? 3.296   59.037 21.361  1.00 48.05  ? 95   GLU   A CA  1 
ATOM   2215 C C   . GLU   A 1 292 ? 3.398   59.379 19.885  1.00 42.16  ? 95   GLU   A C   1 
ATOM   2216 O O   . GLU   A 1 292 ? 2.483   59.967 19.308  1.00 39.69  ? 95   GLU   A O   1 
ATOM   2217 C CB  . GLU   A 1 292 ? 4.182   59.944 22.206  1.00 54.50  ? 95   GLU   A CB  1 
ATOM   2218 C CG  . GLU   A 1 292 ? 3.849   61.410 22.081  1.00 60.71  ? 95   GLU   A CG  1 
ATOM   2219 C CD  . GLU   A 1 292 ? 4.633   62.265 23.071  1.00 68.06  ? 95   GLU   A CD  1 
ATOM   2220 O OE1 . GLU   A 1 292 ? 5.892   62.199 23.056  1.00 71.17  ? 95   GLU   A OE1 1 
ATOM   2221 O OE2 . GLU   A 1 292 ? 3.995   63.009 23.871  1.00 71.08  ? 95   GLU   A OE2 1 
ATOM   2222 N N   . ALA   A 1 293 ? 4.505   58.992 19.251  1.00 41.28  ? 96   ALA   A N   1 
ATOM   2223 C CA  . ALA   A 1 293 ? 4.686   59.248 17.823  1.00 40.03  ? 96   ALA   A CA  1 
ATOM   2224 C C   . ALA   A 1 293 ? 3.504   58.699 17.013  1.00 41.83  ? 96   ALA   A C   1 
ATOM   2225 O O   . ALA   A 1 293 ? 2.973   59.384 16.136  1.00 43.02  ? 96   ALA   A O   1 
ATOM   2226 C CB  . ALA   A 1 293 ? 6.006   58.636 17.348  1.00 37.04  ? 96   ALA   A CB  1 
ATOM   2227 N N   . VAL   A 1 294 ? 3.076   57.455 17.294  1.00 39.78  ? 97   VAL   A N   1 
ATOM   2228 C CA  . VAL   A 1 294 ? 1.895   56.949 16.600  1.00 37.91  ? 97   VAL   A CA  1 
ATOM   2229 C C   . VAL   A 1 294 ? 0.639   57.693 17.027  1.00 37.25  ? 97   VAL   A C   1 
ATOM   2230 O O   . VAL   A 1 294 ? -0.177  58.077 16.176  1.00 37.87  ? 97   VAL   A O   1 
ATOM   2231 C CB  . VAL   A 1 294 ? 1.719   55.436 16.818  1.00 33.37  ? 97   VAL   A CB  1 
ATOM   2232 C CG1 . VAL   A 1 294 ? 0.424   54.984 16.154  1.00 30.16  ? 97   VAL   A CG1 1 
ATOM   2233 C CG2 . VAL   A 1 294 ? 2.940   54.649 16.257  1.00 34.13  ? 97   VAL   A CG2 1 
ATOM   2234 N N   . ASN   A 1 295 ? 0.464   57.884 18.338  1.00 37.72  ? 98   ASN   A N   1 
ATOM   2235 C CA  . ASN   A 1 295 ? -0.735  58.527 18.883  1.00 40.48  ? 98   ASN   A CA  1 
ATOM   2236 C C   . ASN   A 1 295 ? -0.974  59.913 18.285  1.00 41.63  ? 98   ASN   A C   1 
ATOM   2237 O O   . ASN   A 1 295 ? -2.120  60.302 18.061  1.00 40.45  ? 98   ASN   A O   1 
ATOM   2238 C CB  . ASN   A 1 295 ? -0.619  58.615 20.398  1.00 41.84  ? 98   ASN   A CB  1 
ATOM   2239 C CG  . ASN   A 1 295 ? -1.986  58.863 21.082  1.00 43.92  ? 98   ASN   A CG  1 
ATOM   2240 O OD1 . ASN   A 1 295 ? -2.822  57.904 21.229  1.00 44.20  ? 98   ASN   A OD1 1 
ATOM   2241 N ND2 . ASN   A 1 295 ? -2.211  60.107 21.558  1.00 40.66  ? 98   ASN   A ND2 1 
ATOM   2242 N N   . LYS   A 1 296 ? 0.091   60.663 18.026  1.00 45.69  ? 99   LYS   A N   1 
ATOM   2243 C CA  . LYS   A 1 296 ? -0.052  62.015 17.454  1.00 49.53  ? 99   LYS   A CA  1 
ATOM   2244 C C   . LYS   A 1 296 ? -0.537  61.963 16.017  1.00 49.98  ? 99   LYS   A C   1 
ATOM   2245 O O   . LYS   A 1 296 ? -1.082  62.944 15.532  1.00 50.16  ? 99   LYS   A O   1 
ATOM   2246 C CB  . LYS   A 1 296 ? 1.274   62.778 17.514  1.00 52.40  ? 99   LYS   A CB  1 
ATOM   2247 C CG  . LYS   A 1 296 ? 1.747   63.101 18.913  1.00 57.21  ? 99   LYS   A CG  1 
ATOM   2248 C CD  . LYS   A 1 296 ? 2.453   64.470 18.949  1.00 64.70  ? 99   LYS   A CD  1 
ATOM   2249 C CE  . LYS   A 1 296 ? 3.660   64.492 18.000  1.00 69.64  ? 99   LYS   A CE  1 
ATOM   2250 N NZ  . LYS   A 1 296 ? 4.956   64.435 18.750  1.00 72.00  ? 99   LYS   A NZ  1 
ATOM   2251 N N   . ASP   A 1 297 ? -0.362  60.822 15.337  1.00 50.52  ? 100  ASP   A N   1 
ATOM   2252 C CA  . ASP   A 1 297 ? -0.901  60.662 13.975  1.00 47.87  ? 100  ASP   A CA  1 
ATOM   2253 C C   . ASP   A 1 297 ? -2.389  60.336 14.056  1.00 43.40  ? 100  ASP   A C   1 
ATOM   2254 O O   . ASP   A 1 297 ? -3.240  61.116 13.623  1.00 40.62  ? 100  ASP   A O   1 
ATOM   2255 C CB  . ASP   A 1 297 ? -0.122  59.566 13.239  1.00 49.88  ? 100  ASP   A CB  1 
ATOM   2256 C CG  . ASP   A 1 297 ? -0.523  59.445 11.787  1.00 49.75  ? 100  ASP   A CG  1 
ATOM   2257 O OD1 . ASP   A 1 297 ? -1.290  60.324 11.328  1.00 51.53  ? 100  ASP   A OD1 1 
ATOM   2258 O OD2 . ASP   A 1 297 ? -0.068  58.491 11.101  1.00 47.57  ? 100  ASP   A OD2 1 
ATOM   2259 N N   . LYS   A 1 298 ? -2.731  59.155 14.623  1.00 42.72  ? 101  LYS   A N   1 
ATOM   2260 C CA  . LYS   A 1 298 ? -4.116  58.850 14.900  1.00 43.60  ? 101  LYS   A CA  1 
ATOM   2261 C C   . LYS   A 1 298 ? -4.193  58.295 16.313  1.00 42.89  ? 101  LYS   A C   1 
ATOM   2262 O O   . LYS   A 1 298 ? -3.463  57.353 16.637  1.00 43.67  ? 101  LYS   A O   1 
ATOM   2263 C CB  . LYS   A 1 298 ? -4.677  57.842 13.897  1.00 48.70  ? 101  LYS   A CB  1 
ATOM   2264 C CG  . LYS   A 1 298 ? -4.682  58.348 12.444  1.00 50.60  ? 101  LYS   A CG  1 
ATOM   2265 C CD  . LYS   A 1 298 ? -5.504  59.626 12.315  1.00 54.15  ? 101  LYS   A CD  1 
ATOM   2266 C CE  . LYS   A 1 298 ? -5.387  60.224 10.905  1.00 59.18  ? 101  LYS   A CE  1 
ATOM   2267 N NZ  . LYS   A 1 298 ? -5.531  59.172 9.871   1.00 64.10  ? 101  LYS   A NZ  1 
ATOM   2268 N N   . PRO   A 1 299 ? -5.008  58.873 17.203  1.00 42.99  ? 102  PRO   A N   1 
ATOM   2269 C CA  . PRO   A 1 299 ? -5.021  58.396 18.598  1.00 40.26  ? 102  PRO   A CA  1 
ATOM   2270 C C   . PRO   A 1 299 ? -5.198  56.888 18.656  1.00 38.82  ? 102  PRO   A C   1 
ATOM   2271 O O   . PRO   A 1 299 ? -5.960  56.327 17.882  1.00 36.77  ? 102  PRO   A O   1 
ATOM   2272 C CB  . PRO   A 1 299 ? -6.208  59.120 19.208  1.00 38.69  ? 102  PRO   A CB  1 
ATOM   2273 C CG  . PRO   A 1 299 ? -6.304  60.368 18.406  1.00 42.84  ? 102  PRO   A CG  1 
ATOM   2274 C CD  . PRO   A 1 299 ? -5.949  59.972 16.994  1.00 42.81  ? 102  PRO   A CD  1 
ATOM   2275 N N   . LEU   A 1 300 ? -4.512  56.255 19.610  1.00 40.02  ? 103  LEU   A N   1 
ATOM   2276 C CA  . LEU   A 1 300 ? -4.511  54.798 19.746  1.00 41.86  ? 103  LEU   A CA  1 
ATOM   2277 C C   . LEU   A 1 300 ? -5.596  54.276 20.683  1.00 43.76  ? 103  LEU   A C   1 
ATOM   2278 O O   . LEU   A 1 300 ? -5.978  53.100 20.576  1.00 40.60  ? 103  LEU   A O   1 
ATOM   2279 C CB  . LEU   A 1 300 ? -3.150  54.309 20.283  1.00 38.97  ? 103  LEU   A CB  1 
ATOM   2280 C CG  . LEU   A 1 300 ? -1.960  54.287 19.312  1.00 36.79  ? 103  LEU   A CG  1 
ATOM   2281 C CD1 . LEU   A 1 300 ? -0.649  54.334 20.057  1.00 36.23  ? 103  LEU   A CD1 1 
ATOM   2282 C CD2 . LEU   A 1 300 ? -2.035  53.060 18.384  1.00 30.82  ? 103  LEU   A CD2 1 
ATOM   2283 N N   . GLY   A 1 301 ? -6.049  55.111 21.649  1.00 44.27  ? 104  GLY   A N   1 
ATOM   2284 C CA  . GLY   A 1 301 ? -6.915  54.617 22.709  1.00 43.05  ? 104  GLY   A CA  1 
ATOM   2285 C C   . GLY   A 1 301 ? -6.174  54.463 24.023  1.00 43.50  ? 104  GLY   A C   1 
ATOM   2286 O O   . GLY   A 1 301 ? -5.180  55.146 24.248  1.00 45.93  ? 104  GLY   A O   1 
ATOM   2287 N N   . ALA   A 1 302 ? -6.642  53.581 24.901  1.00 42.85  ? 105  ALA   A N   1 
ATOM   2288 C CA  . ALA   A 1 302 ? -5.966  53.333 26.164  1.00 42.37  ? 105  ALA   A CA  1 
ATOM   2289 C C   . ALA   A 1 302 ? -4.834  52.334 25.883  1.00 43.56  ? 105  ALA   A C   1 
ATOM   2290 O O   . ALA   A 1 302 ? -5.044  51.105 25.773  1.00 42.72  ? 105  ALA   A O   1 
ATOM   2291 C CB  . ALA   A 1 302 ? -6.937  52.807 27.208  1.00 42.69  ? 105  ALA   A CB  1 
ATOM   2292 N N   . VAL   A 1 303 ? -3.615  52.852 25.785  1.00 42.65  ? 106  VAL   A N   1 
ATOM   2293 C CA  . VAL   A 1 303 ? -2.496  52.007 25.384  1.00 40.73  ? 106  VAL   A CA  1 
ATOM   2294 C C   . VAL   A 1 303 ? -2.203  50.954 26.455  1.00 42.53  ? 106  VAL   A C   1 
ATOM   2295 O O   . VAL   A 1 303 ? -2.511  51.090 27.679  1.00 41.76  ? 106  VAL   A O   1 
ATOM   2296 C CB  . VAL   A 1 303 ? -1.269  52.888 25.096  1.00 39.17  ? 106  VAL   A CB  1 
ATOM   2297 C CG1 . VAL   A 1 303 ? -1.548  53.786 23.928  1.00 36.59  ? 106  VAL   A CG1 1 
ATOM   2298 C CG2 . VAL   A 1 303 ? -0.921  53.726 26.344  1.00 40.04  ? 106  VAL   A CG2 1 
ATOM   2299 N N   . ALA   A 1 304 ? -1.526  49.881 26.004  1.00 40.09  ? 107  ALA   A N   1 
ATOM   2300 C CA  . ALA   A 1 304 ? -1.168  48.786 26.889  1.00 39.56  ? 107  ALA   A CA  1 
ATOM   2301 C C   . ALA   A 1 304 ? 0.020   49.100 27.772  1.00 41.86  ? 107  ALA   A C   1 
ATOM   2302 O O   . ALA   A 1 304 ? 0.223   48.395 28.775  1.00 43.55  ? 107  ALA   A O   1 
ATOM   2303 C CB  . ALA   A 1 304 ? -0.893  47.528 26.080  1.00 36.13  ? 107  ALA   A CB  1 
ATOM   2304 N N   . LEU   A 1 305 ? 0.805   50.124 27.421  1.00 42.14  ? 108  LEU   A N   1 
ATOM   2305 C CA  . LEU   A 1 305 ? 1.998   50.463 28.203  1.00 45.40  ? 108  LEU   A CA  1 
ATOM   2306 C C   . LEU   A 1 305 ? 1.629   51.336 29.399  1.00 46.29  ? 108  LEU   A C   1 
ATOM   2307 O O   . LEU   A 1 305 ? 1.178   52.488 29.223  1.00 46.03  ? 108  LEU   A O   1 
ATOM   2308 C CB  . LEU   A 1 305 ? 3.039   51.164 27.299  1.00 45.57  ? 108  LEU   A CB  1 
ATOM   2309 C CG  . LEU   A 1 305 ? 4.381   51.530 27.945  1.00 44.82  ? 108  LEU   A CG  1 
ATOM   2310 C CD1 . LEU   A 1 305 ? 5.222   50.292 28.177  1.00 42.18  ? 108  LEU   A CD1 1 
ATOM   2311 C CD2 . LEU   A 1 305 ? 5.115   52.574 27.117  1.00 45.02  ? 108  LEU   A CD2 1 
ATOM   2312 N N   . LYS   A 1 306 ? 1.838   50.797 30.606  1.00 47.47  ? 109  LYS   A N   1 
ATOM   2313 C CA  . LYS   A 1 306 ? 1.374   51.451 31.825  1.00 49.57  ? 109  LYS   A CA  1 
ATOM   2314 C C   . LYS   A 1 306 ? 1.907   52.876 31.942  1.00 51.05  ? 109  LYS   A C   1 
ATOM   2315 O O   . LYS   A 1 306 ? 1.163   53.796 32.314  1.00 49.38  ? 109  LYS   A O   1 
ATOM   2316 C CB  . LYS   A 1 306 ? 1.788   50.634 33.061  1.00 50.52  ? 109  LYS   A CB  1 
ATOM   2317 C CG  . LYS   A 1 306 ? 1.338   49.201 33.050  1.00 50.03  ? 109  LYS   A CG  1 
ATOM   2318 C CD  . LYS   A 1 306 ? 2.034   48.419 34.155  1.00 54.56  ? 109  LYS   A CD  1 
ATOM   2319 C CE  . LYS   A 1 306 ? 1.410   47.060 34.338  1.00 58.12  ? 109  LYS   A CE  1 
ATOM   2320 N NZ  . LYS   A 1 306 ? 1.875   46.432 35.632  1.00 62.67  ? 109  LYS   A NZ  1 
ATOM   2321 N N   . SER   A 1 307 ? 3.199   53.080 31.647  1.00 52.05  ? 110  SER   A N   1 
ATOM   2322 C CA  . SER   A 1 307 ? 3.778   54.405 31.893  1.00 53.25  ? 110  SER   A CA  1 
ATOM   2323 C C   . SER   A 1 307 ? 3.045   55.474 31.090  1.00 53.28  ? 110  SER   A C   1 
ATOM   2324 O O   . SER   A 1 307 ? 2.798   56.565 31.587  1.00 54.23  ? 110  SER   A O   1 
ATOM   2325 C CB  . SER   A 1 307 ? 5.277   54.397 31.555  1.00 51.97  ? 110  SER   A CB  1 
ATOM   2326 O OG  . SER   A 1 307 ? 5.524   54.048 30.187  1.00 48.91  ? 110  SER   A OG  1 
ATOM   2327 N N   . TYR   A 1 308 ? 2.677   55.165 29.844  1.00 52.99  ? 111  TYR   A N   1 
ATOM   2328 C CA  . TYR   A 1 308 ? 2.035   56.118 28.957  1.00 53.53  ? 111  TYR   A CA  1 
ATOM   2329 C C   . TYR   A 1 308 ? 0.526   56.178 29.149  1.00 52.83  ? 111  TYR   A C   1 
ATOM   2330 O O   . TYR   A 1 308 ? -0.063  57.264 29.043  1.00 54.47  ? 111  TYR   A O   1 
ATOM   2331 C CB  . TYR   A 1 308 ? 2.365   55.766 27.497  1.00 55.25  ? 111  TYR   A CB  1 
ATOM   2332 C CG  . TYR   A 1 308 ? 1.964   56.817 26.476  1.00 56.05  ? 111  TYR   A CG  1 
ATOM   2333 C CD1 . TYR   A 1 308 ? 1.991   58.181 26.795  1.00 60.58  ? 111  TYR   A CD1 1 
ATOM   2334 C CD2 . TYR   A 1 308 ? 1.560   56.451 25.210  1.00 53.38  ? 111  TYR   A CD2 1 
ATOM   2335 C CE1 . TYR   A 1 308 ? 1.609   59.152 25.857  1.00 61.25  ? 111  TYR   A CE1 1 
ATOM   2336 C CE2 . TYR   A 1 308 ? 1.182   57.388 24.266  1.00 55.05  ? 111  TYR   A CE2 1 
ATOM   2337 C CZ  . TYR   A 1 308 ? 1.207   58.738 24.584  1.00 59.34  ? 111  TYR   A CZ  1 
ATOM   2338 O OH  . TYR   A 1 308 ? 0.839   59.661 23.636  1.00 59.57  ? 111  TYR   A OH  1 
ATOM   2339 N N   . GLU   A 1 309 ? -0.124  55.045 29.432  1.00 50.36  ? 112  GLU   A N   1 
ATOM   2340 C CA  . GLU   A 1 309 ? -1.568  55.067 29.673  1.00 48.23  ? 112  GLU   A CA  1 
ATOM   2341 C C   . GLU   A 1 309 ? -1.932  55.891 30.918  1.00 50.73  ? 112  GLU   A C   1 
ATOM   2342 O O   . GLU   A 1 309 ? -3.082  56.348 31.041  1.00 48.56  ? 112  GLU   A O   1 
ATOM   2343 C CB  . GLU   A 1 309 ? -2.103  53.645 29.818  1.00 45.98  ? 112  GLU   A CB  1 
ATOM   2344 C CG  . GLU   A 1 309 ? -3.539  53.548 30.244  1.00 49.17  ? 112  GLU   A CG  1 
ATOM   2345 C CD  . GLU   A 1 309 ? -4.515  54.148 29.234  1.00 52.77  ? 112  GLU   A CD  1 
ATOM   2346 O OE1 . GLU   A 1 309 ? -5.743  54.248 29.540  1.00 51.98  ? 112  GLU   A OE1 1 
ATOM   2347 O OE2 . GLU   A 1 309 ? -4.057  54.519 28.132  1.00 55.92  ? 112  GLU   A OE2 1 
ATOM   2348 N N   . GLU   A 1 310 ? -0.979  56.078 31.846  1.00 54.01  ? 113  GLU   A N   1 
ATOM   2349 C CA  . GLU   A 1 310 ? -1.267  56.848 33.039  1.00 57.13  ? 113  GLU   A CA  1 
ATOM   2350 C C   . GLU   A 1 310 ? -1.468  58.319 32.699  1.00 60.32  ? 113  GLU   A C   1 
ATOM   2351 O O   . GLU   A 1 310 ? -2.215  59.019 33.388  1.00 62.54  ? 113  GLU   A O   1 
ATOM   2352 C CB  . GLU   A 1 310 ? -0.146  56.661 34.049  1.00 59.22  ? 113  GLU   A CB  1 
ATOM   2353 C CG  . GLU   A 1 310 ? -0.192  55.304 34.742  1.00 61.71  ? 113  GLU   A CG  1 
ATOM   2354 C CD  . GLU   A 1 310 ? 1.077   54.988 35.516  1.00 66.23  ? 113  GLU   A CD  1 
ATOM   2355 O OE1 . GLU   A 1 310 ? 1.859   55.920 35.837  1.00 69.04  ? 113  GLU   A OE1 1 
ATOM   2356 O OE2 . GLU   A 1 310 ? 1.301   53.794 35.801  1.00 67.16  ? 113  GLU   A OE2 1 
ATOM   2357 N N   . GLU   A 1 311 ? -0.839  58.800 31.626  1.00 59.99  ? 114  GLU   A N   1 
ATOM   2358 C CA  . GLU   A 1 311 ? -1.032  60.180 31.202  1.00 59.57  ? 114  GLU   A CA  1 
ATOM   2359 C C   . GLU   A 1 311 ? -2.266  60.322 30.312  1.00 59.50  ? 114  GLU   A C   1 
ATOM   2360 O O   . GLU   A 1 311 ? -3.049  61.260 30.473  1.00 61.29  ? 114  GLU   A O   1 
ATOM   2361 C CB  . GLU   A 1 311 ? 0.219   60.681 30.479  1.00 59.01  ? 114  GLU   A CB  1 
ATOM   2362 C CG  . GLU   A 1 311 ? 1.493   60.586 31.303  1.00 63.14  ? 114  GLU   A CG  1 
ATOM   2363 C CD  . GLU   A 1 311 ? 1.429   61.394 32.629  1.00 67.93  ? 114  GLU   A CD  1 
ATOM   2364 O OE1 . GLU   A 1 311 ? 0.647   62.381 32.723  1.00 68.36  ? 114  GLU   A OE1 1 
ATOM   2365 O OE2 . GLU   A 1 311 ? 2.166   61.032 33.585  1.00 69.61  ? 114  GLU   A OE2 1 
ATOM   2366 N N   . LEU   A 1 312 ? -2.479  59.383 29.383  1.00 58.64  ? 115  LEU   A N   1 
ATOM   2367 C CA  . LEU   A 1 312 ? -3.633  59.496 28.490  1.00 56.74  ? 115  LEU   A CA  1 
ATOM   2368 C C   . LEU   A 1 312 ? -4.959  59.344 29.246  1.00 55.48  ? 115  LEU   A C   1 
ATOM   2369 O O   . LEU   A 1 312 ? -5.947  60.012 28.913  1.00 56.00  ? 115  LEU   A O   1 
ATOM   2370 C CB  . LEU   A 1 312 ? -3.521  58.457 27.371  1.00 54.89  ? 115  LEU   A CB  1 
ATOM   2371 C CG  . LEU   A 1 312 ? -2.252  58.567 26.518  1.00 51.96  ? 115  LEU   A CG  1 
ATOM   2372 C CD1 . LEU   A 1 312 ? -2.191  57.501 25.463  1.00 46.01  ? 115  LEU   A CD1 1 
ATOM   2373 C CD2 . LEU   A 1 312 ? -2.140  59.955 25.894  1.00 48.70  ? 115  LEU   A CD2 1 
ATOM   2374 N N   . ALA   A 1 313 ? -5.009  58.457 30.249  1.00 54.24  ? 116  ALA   A N   1 
ATOM   2375 C CA  . ALA   A 1 313 ? -6.251  58.225 30.989  1.00 53.14  ? 116  ALA   A CA  1 
ATOM   2376 C C   . ALA   A 1 313 ? -6.853  59.524 31.506  1.00 51.44  ? 116  ALA   A C   1 
ATOM   2377 O O   . ALA   A 1 313 ? -8.074  59.615 31.664  1.00 50.75  ? 116  ALA   A O   1 
ATOM   2378 C CB  . ALA   A 1 313 ? -6.010  57.257 32.164  1.00 55.18  ? 116  ALA   A CB  1 
ATOM   2379 N N   . LYS   A 1 314 ? -6.014  60.529 31.778  1.00 49.80  ? 117  LYS   A N   1 
ATOM   2380 C CA  . LYS   A 1 314 ? -6.517  61.810 32.250  1.00 53.73  ? 117  LYS   A CA  1 
ATOM   2381 C C   . LYS   A 1 314 ? -7.373  62.532 31.212  1.00 52.80  ? 117  LYS   A C   1 
ATOM   2382 O O   . LYS   A 1 314 ? -8.127  63.434 31.577  1.00 54.95  ? 117  LYS   A O   1 
ATOM   2383 C CB  . LYS   A 1 314 ? -5.343  62.694 32.682  1.00 56.97  ? 117  LYS   A CB  1 
ATOM   2384 C CG  . LYS   A 1 314 ? -4.392  62.002 33.651  1.00 58.16  ? 117  LYS   A CG  1 
ATOM   2385 C CD  . LYS   A 1 314 ? -3.038  62.687 33.707  1.00 59.47  ? 117  LYS   A CD  1 
ATOM   2386 C CE  . LYS   A 1 314 ? -2.333  62.440 35.035  1.00 61.12  ? 117  LYS   A CE  1 
ATOM   2387 N NZ  . LYS   A 1 314 ? -0.927  62.988 35.039  1.00 63.23  ? 117  LYS   A NZ  1 
ATOM   2388 N N   . ASP   A 1 315 ? -7.265  62.160 29.952  1.00 51.64  ? 118  ASP   A N   1 
ATOM   2389 C CA  . ASP   A 1 315 ? -8.057  62.755 28.885  1.00 52.82  ? 118  ASP   A CA  1 
ATOM   2390 C C   . ASP   A 1 315 ? -9.493  62.220 28.944  1.00 49.98  ? 118  ASP   A C   1 
ATOM   2391 O O   . ASP   A 1 315 ? -9.685  61.000 28.922  1.00 50.07  ? 118  ASP   A O   1 
ATOM   2392 C CB  . ASP   A 1 315 ? -7.435  62.431 27.527  1.00 53.72  ? 118  ASP   A CB  1 
ATOM   2393 C CG  . ASP   A 1 315 ? -8.202  63.027 26.371  1.00 53.86  ? 118  ASP   A CG  1 
ATOM   2394 O OD1 . ASP   A 1 315 ? -9.410  63.297 26.522  1.00 54.01  ? 118  ASP   A OD1 1 
ATOM   2395 O OD2 . ASP   A 1 315 ? -7.590  63.206 25.295  1.00 53.86  ? 118  ASP   A OD2 1 
ATOM   2396 N N   . PRO   A 1 316 ? -10.497 63.084 29.025  1.00 47.42  ? 119  PRO   A N   1 
ATOM   2397 C CA  . PRO   A 1 316 ? -11.879 62.575 29.129  1.00 45.82  ? 119  PRO   A CA  1 
ATOM   2398 C C   . PRO   A 1 316 ? -12.291 61.730 27.955  1.00 45.91  ? 119  PRO   A C   1 
ATOM   2399 O O   . PRO   A 1 316 ? -13.082 60.795 28.127  1.00 46.80  ? 119  PRO   A O   1 
ATOM   2400 C CB  . PRO   A 1 316 ? -12.728 63.865 29.240  1.00 46.01  ? 119  PRO   A CB  1 
ATOM   2401 C CG  . PRO   A 1 316 ? -11.764 65.030 28.995  1.00 46.17  ? 119  PRO   A CG  1 
ATOM   2402 C CD  . PRO   A 1 316 ? -10.398 64.535 29.343  1.00 46.54  ? 119  PRO   A CD  1 
ATOM   2403 N N   . ARG   A 1 317 ? -11.784 62.002 26.753  1.00 44.74  ? 120  ARG   A N   1 
ATOM   2404 C CA  . ARG   A 1 317 ? -12.072 61.111 25.633  1.00 42.06  ? 120  ARG   A CA  1 
ATOM   2405 C C   . ARG   A 1 317 ? -11.568 59.655 25.892  1.00 41.93  ? 120  ARG   A C   1 
ATOM   2406 O O   . ARG   A 1 317 ? -12.190 58.680 25.434  1.00 36.86  ? 120  ARG   A O   1 
ATOM   2407 C CB  . ARG   A 1 317 ? -11.475 61.684 24.346  1.00 39.49  ? 120  ARG   A CB  1 
ATOM   2408 C CG  . ARG   A 1 317 ? -11.789 63.166 24.125  1.00 40.02  ? 120  ARG   A CG  1 
ATOM   2409 C CD  . ARG   A 1 317 ? -11.017 63.771 22.932  1.00 38.40  ? 120  ARG   A CD  1 
ATOM   2410 N NE  . ARG   A 1 317 ? -9.575  63.753 23.149  1.00 40.98  ? 120  ARG   A NE  1 
ATOM   2411 C CZ  . ARG   A 1 317 ? -8.667  63.745 22.166  1.00 45.03  ? 120  ARG   A CZ  1 
ATOM   2412 N NH1 . ARG   A 1 317 ? -9.046  63.778 20.871  1.00 43.88  ? 120  ARG   A NH1 1 
ATOM   2413 N NH2 . ARG   A 1 317 ? -7.353  63.684 22.458  1.00 47.00  ? 120  ARG   A NH2 1 
ATOM   2414 N N   . ILE   A 1 318 ? -10.468 59.503 26.630  1.00 42.63  ? 121  ILE   A N   1 
ATOM   2415 C CA  . ILE   A 1 318 ? -9.992  58.175 26.950  1.00 46.99  ? 121  ILE   A CA  1 
ATOM   2416 C C   . ILE   A 1 318 ? -10.809 57.572 28.092  1.00 48.50  ? 121  ILE   A C   1 
ATOM   2417 O O   . ILE   A 1 318 ? -11.108 56.346 28.084  1.00 48.98  ? 121  ILE   A O   1 
ATOM   2418 C CB  . ILE   A 1 318 ? -8.487  58.204 27.285  1.00 49.03  ? 121  ILE   A CB  1 
ATOM   2419 C CG1 . ILE   A 1 318 ? -7.677  58.704 26.092  1.00 50.66  ? 121  ILE   A CG1 1 
ATOM   2420 C CG2 . ILE   A 1 318 ? -8.009  56.825 27.709  1.00 46.42  ? 121  ILE   A CG2 1 
ATOM   2421 C CD1 . ILE   A 1 318 ? -7.297  57.602 25.146  1.00 50.29  ? 121  ILE   A CD1 1 
ATOM   2422 N N   . ALA   A 1 319 ? -11.172 58.399 29.083  1.00 44.63  ? 122  ALA   A N   1 
ATOM   2423 C CA  . ALA   A 1 319 ? -12.036 57.915 30.142  1.00 44.71  ? 122  ALA   A CA  1 
ATOM   2424 C C   . ALA   A 1 319 ? -13.376 57.449 29.584  1.00 47.29  ? 122  ALA   A C   1 
ATOM   2425 O O   . ALA   A 1 319 ? -13.926 56.421 30.022  1.00 50.84  ? 122  ALA   A O   1 
ATOM   2426 C CB  . ALA   A 1 319 ? -12.239 58.994 31.205  1.00 45.17  ? 122  ALA   A CB  1 
ATOM   2427 N N   . ALA   A 1 320 ? -13.927 58.181 28.620  1.00 44.33  ? 123  ALA   A N   1 
ATOM   2428 C CA  . ALA   A 1 320 ? -15.144 57.729 27.972  1.00 43.31  ? 123  ALA   A CA  1 
ATOM   2429 C C   . ALA   A 1 320 ? -14.904 56.429 27.204  1.00 41.51  ? 123  ALA   A C   1 
ATOM   2430 O O   . ALA   A 1 320 ? -15.731 55.517 27.223  1.00 38.73  ? 123  ALA   A O   1 
ATOM   2431 C CB  . ALA   A 1 320 ? -15.654 58.813 27.027  1.00 43.96  ? 123  ALA   A CB  1 
ATOM   2432 N N   . THR   A 1 321 ? -13.773 56.327 26.509  1.00 43.24  ? 124  THR   A N   1 
ATOM   2433 C CA  . THR   A 1 321 ? -13.445 55.090 25.816  1.00 43.90  ? 124  THR   A CA  1 
ATOM   2434 C C   . THR   A 1 321 ? -13.433 53.907 26.787  1.00 46.29  ? 124  THR   A C   1 
ATOM   2435 O O   . THR   A 1 321 ? -14.022 52.838 26.516  1.00 45.97  ? 124  THR   A O   1 
ATOM   2436 C CB  . THR   A 1 321 ? -12.092 55.222 25.109  1.00 41.08  ? 124  THR   A CB  1 
ATOM   2437 O OG1 . THR   A 1 321 ? -12.151 56.268 24.121  1.00 41.58  ? 124  THR   A OG1 1 
ATOM   2438 C CG2 . THR   A 1 321 ? -11.763 53.920 24.437  1.00 37.65  ? 124  THR   A CG2 1 
ATOM   2439 N N   . MET   A 1 322 ? -12.744 54.066 27.923  1.00 46.57  ? 125  MET   A N   1 
ATOM   2440 C CA  . MET   A 1 322 ? -12.610 52.924 28.837  1.00 46.05  ? 125  MET   A CA  1 
ATOM   2441 C C   . MET   A 1 322 ? -13.897 52.644 29.590  1.00 43.89  ? 125  MET   A C   1 
ATOM   2442 O O   . MET   A 1 322 ? -14.104 51.507 30.011  1.00 43.35  ? 125  MET   A O   1 
ATOM   2443 C CB  . MET   A 1 322 ? -11.460 53.162 29.819  1.00 48.36  ? 125  MET   A CB  1 
ATOM   2444 C CG  . MET   A 1 322 ? -10.090 53.000 29.184  1.00 51.42  ? 125  MET   A CG  1 
ATOM   2445 S SD  . MET   A 1 322 ? -9.830  51.290 28.545  1.00 54.29  ? 125  MET   A SD  1 
ATOM   2446 C CE  . MET   A 1 322 ? -10.781 51.349 27.105  1.00 55.07  ? 125  MET   A CE  1 
ATOM   2447 N N   . GLU   A 1 323 ? -14.770 53.646 29.731  1.00 44.16  ? 126  GLU   A N   1 
ATOM   2448 C CA  . GLU   A 1 323 ? -16.077 53.393 30.305  1.00 47.03  ? 126  GLU   A CA  1 
ATOM   2449 C C   . GLU   A 1 323 ? -16.952 52.604 29.342  1.00 45.19  ? 126  GLU   A C   1 
ATOM   2450 O O   . GLU   A 1 323 ? -17.654 51.671 29.750  1.00 47.35  ? 126  GLU   A O   1 
ATOM   2451 C CB  . GLU   A 1 323 ? -16.732 54.707 30.687  1.00 52.77  ? 126  GLU   A CB  1 
ATOM   2452 C CG  . GLU   A 1 323 ? -18.246 54.695 30.644  1.00 57.90  ? 126  GLU   A CG  1 
ATOM   2453 C CD  . GLU   A 1 323 ? -18.841 56.090 30.897  1.00 62.59  ? 126  GLU   A CD  1 
ATOM   2454 O OE1 . GLU   A 1 323 ? -18.093 56.974 31.369  1.00 64.31  ? 126  GLU   A OE1 1 
ATOM   2455 O OE2 . GLU   A 1 323 ? -20.040 56.298 30.611  1.00 63.49  ? 126  GLU   A OE2 1 
ATOM   2456 N N   . ASN   A 1 324 ? -16.927 52.954 28.053  1.00 42.56  ? 127  ASN   A N   1 
ATOM   2457 C CA  . ASN   A 1 324 ? -17.646 52.155 27.059  1.00 42.35  ? 127  ASN   A CA  1 
ATOM   2458 C C   . ASN   A 1 324 ? -17.079 50.731 26.973  1.00 39.98  ? 127  ASN   A C   1 
ATOM   2459 O O   . ASN   A 1 324 ? -17.827 49.787 26.741  1.00 37.30  ? 127  ASN   A O   1 
ATOM   2460 C CB  . ASN   A 1 324 ? -17.587 52.823 25.689  1.00 42.00  ? 127  ASN   A CB  1 
ATOM   2461 C CG  . ASN   A 1 324 ? -18.631 53.945 25.537  1.00 41.98  ? 127  ASN   A CG  1 
ATOM   2462 O OD1 . ASN   A 1 324 ? -19.822 53.750 25.837  1.00 42.64  ? 127  ASN   A OD1 1 
ATOM   2463 N ND2 . ASN   A 1 324 ? -18.190 55.095 25.079  1.00 39.46  ? 127  ASN   A ND2 1 
ATOM   2464 N N   . ALA   A 1 325 ? -15.766 50.580 27.156  1.00 41.54  ? 128  ALA   A N   1 
ATOM   2465 C CA  . ALA   A 1 325 ? -15.150 49.255 27.156  1.00 42.03  ? 128  ALA   A CA  1 
ATOM   2466 C C   . ALA   A 1 325 ? -15.675 48.420 28.320  1.00 47.39  ? 128  ALA   A C   1 
ATOM   2467 O O   . ALA   A 1 325 ? -16.107 47.279 28.129  1.00 48.17  ? 128  ALA   A O   1 
ATOM   2468 C CB  . ALA   A 1 325 ? -13.635 49.374 27.229  1.00 38.00  ? 128  ALA   A CB  1 
ATOM   2469 N N   . GLN   A 1 326 ? -15.665 48.994 29.530  1.00 50.90  ? 129  GLN   A N   1 
ATOM   2470 C CA  . GLN   A 1 326 ? -16.099 48.241 30.712  1.00 55.76  ? 129  GLN   A CA  1 
ATOM   2471 C C   . GLN   A 1 326 ? -17.549 47.783 30.584  1.00 55.25  ? 129  GLN   A C   1 
ATOM   2472 O O   . GLN   A 1 326 ? -17.957 46.817 31.222  1.00 58.14  ? 129  GLN   A O   1 
ATOM   2473 C CB  . GLN   A 1 326 ? -15.917 49.089 31.976  1.00 61.35  ? 129  GLN   A CB  1 
ATOM   2474 C CG  . GLN   A 1 326 ? -15.936 48.316 33.269  1.00 68.97  ? 129  GLN   A CG  1 
ATOM   2475 C CD  . GLN   A 1 326 ? -14.610 47.589 33.534  1.00 75.91  ? 129  GLN   A CD  1 
ATOM   2476 O OE1 . GLN   A 1 326 ? -14.083 46.877 32.664  1.00 75.38  ? 129  GLN   A OE1 1 
ATOM   2477 N NE2 . GLN   A 1 326 ? -14.071 47.757 34.751  1.00 80.66  ? 129  GLN   A NE2 1 
ATOM   2478 N N   . LYS   A 1 327 ? -18.370 48.492 29.804  1.00 52.48  ? 130  LYS   A N   1 
ATOM   2479 C CA  . LYS   A 1 327 ? -19.729 48.028 29.534  1.00 48.41  ? 130  LYS   A CA  1 
ATOM   2480 C C   . LYS   A 1 327 ? -19.789 46.990 28.409  1.00 45.72  ? 130  LYS   A C   1 
ATOM   2481 O O   . LYS   A 1 327 ? -20.778 46.245 28.323  1.00 46.05  ? 130  LYS   A O   1 
ATOM   2482 C CB  . LYS   A 1 327 ? -20.641 49.216 29.180  1.00 44.02  ? 130  LYS   A CB  1 
ATOM   2483 C CG  . LYS   A 1 327 ? -21.011 50.070 30.343  1.00 45.84  ? 130  LYS   A CG  1 
ATOM   2484 C CD  . LYS   A 1 327 ? -21.733 51.334 29.846  1.00 49.01  ? 130  LYS   A CD  1 
ATOM   2485 C CE  . LYS   A 1 327 ? -22.116 52.258 31.003  1.00 53.37  ? 130  LYS   A CE  1 
ATOM   2486 N NZ  . LYS   A 1 327 ? -20.896 52.677 31.736  1.00 55.93  ? 130  LYS   A NZ  1 
ATOM   2487 N N   . GLY   A 1 328 ? -18.794 46.958 27.543  1.00 43.93  ? 131  GLY   A N   1 
ATOM   2488 C CA  . GLY   A 1 328 ? -18.736 46.032 26.450  1.00 45.73  ? 131  GLY   A CA  1 
ATOM   2489 C C   . GLY   A 1 328 ? -18.019 44.756 26.874  1.00 48.71  ? 131  GLY   A C   1 
ATOM   2490 O O   . GLY   A 1 328 ? -18.008 44.383 28.053  1.00 51.77  ? 131  GLY   A O   1 
ATOM   2491 N N   . GLU   A 1 329 ? -17.375 44.097 25.908  1.00 47.15  ? 132  GLU   A N   1 
ATOM   2492 C CA  . GLU   A 1 329 ? -16.717 42.832 26.187  1.00 50.54  ? 132  GLU   A CA  1 
ATOM   2493 C C   . GLU   A 1 329 ? -15.533 42.666 25.248  1.00 49.05  ? 132  GLU   A C   1 
ATOM   2494 O O   . GLU   A 1 329 ? -15.666 42.857 24.024  1.00 45.07  ? 132  GLU   A O   1 
ATOM   2495 C CB  . GLU   A 1 329 ? -17.690 41.641 26.032  1.00 52.53  ? 132  GLU   A CB  1 
ATOM   2496 C CG  . GLU   A 1 329 ? -18.917 41.752 26.901  1.00 57.48  ? 132  GLU   A CG  1 
ATOM   2497 C CD  . GLU   A 1 329 ? -19.567 40.410 27.141  1.00 66.58  ? 132  GLU   A CD  1 
ATOM   2498 O OE1 . GLU   A 1 329 ? -19.123 39.384 26.510  1.00 66.37  ? 132  GLU   A OE1 1 
ATOM   2499 O OE2 . GLU   A 1 329 ? -20.530 40.364 27.956  1.00 71.63  ? 132  GLU   A OE2 1 
ATOM   2500 N N   . ILE   A 1 330 ? -14.388 42.264 25.829  1.00 51.84  ? 133  ILE   A N   1 
ATOM   2501 C CA  . ILE   A 1 330 ? -13.226 41.896 25.021  1.00 48.99  ? 133  ILE   A CA  1 
ATOM   2502 C C   . ILE   A 1 330 ? -13.632 40.834 24.017  1.00 44.93  ? 133  ILE   A C   1 
ATOM   2503 O O   . ILE   A 1 330 ? -14.307 39.876 24.379  1.00 46.67  ? 133  ILE   A O   1 
ATOM   2504 C CB  . ILE   A 1 330 ? -12.079 41.427 25.932  1.00 51.37  ? 133  ILE   A CB  1 
ATOM   2505 C CG1 . ILE   A 1 330 ? -10.773 41.332 25.152  1.00 50.66  ? 133  ILE   A CG1 1 
ATOM   2506 C CG2 . ILE   A 1 330 ? -12.424 40.106 26.554  1.00 54.90  ? 133  ILE   A CG2 1 
ATOM   2507 C CD1 . ILE   A 1 330 ? -10.061 42.670 24.979  1.00 50.69  ? 133  ILE   A CD1 1 
ATOM   2508 N N   . MET   A 1 331 ? -13.265 41.023 22.746  1.00 39.33  ? 134  MET   A N   1 
ATOM   2509 C CA  . MET   A 1 331 ? -13.577 40.049 21.736  1.00 36.63  ? 134  MET   A CA  1 
ATOM   2510 C C   . MET   A 1 331 ? -12.831 38.744 22.040  1.00 40.99  ? 134  MET   A C   1 
ATOM   2511 O O   . MET   A 1 331 ? -11.705 38.753 22.533  1.00 42.04  ? 134  MET   A O   1 
ATOM   2512 C CB  . MET   A 1 331 ? -13.168 40.523 20.358  1.00 35.83  ? 134  MET   A CB  1 
ATOM   2513 C CG  . MET   A 1 331 ? -14.012 41.743 19.837  1.00 39.64  ? 134  MET   A CG  1 
ATOM   2514 S SD  . MET   A 1 331 ? -13.572 42.159 18.150  1.00 39.49  ? 134  MET   A SD  1 
ATOM   2515 C CE  . MET   A 1 331 ? -12.003 43.018 18.378  1.00 39.29  ? 134  MET   A CE  1 
ATOM   2516 N N   . PRO   A 1 332 ? -13.450 37.601 21.734  1.00 42.96  ? 135  PRO   A N   1 
ATOM   2517 C CA  . PRO   A 1 332 ? -12.666 36.361 21.667  1.00 45.28  ? 135  PRO   A CA  1 
ATOM   2518 C C   . PRO   A 1 332 ? -11.611 36.493 20.585  1.00 44.82  ? 135  PRO   A C   1 
ATOM   2519 O O   . PRO   A 1 332 ? -11.696 37.358 19.702  1.00 41.00  ? 135  PRO   A O   1 
ATOM   2520 C CB  . PRO   A 1 332 ? -13.701 35.269 21.312  1.00 46.08  ? 135  PRO   A CB  1 
ATOM   2521 C CG  . PRO   A 1 332 ? -15.051 35.901 21.598  1.00 46.15  ? 135  PRO   A CG  1 
ATOM   2522 C CD  . PRO   A 1 332 ? -14.882 37.402 21.456  1.00 42.20  ? 135  PRO   A CD  1 
ATOM   2523 N N   . ASN   A 1 333 ? -10.598 35.623 20.668  1.00 43.61  ? 136  ASN   A N   1 
ATOM   2524 C CA  . ASN   A 1 333 ? -9.603  35.470 19.614  1.00 42.55  ? 136  ASN   A CA  1 
ATOM   2525 C C   . ASN   A 1 333 ? -9.675  34.081 18.986  1.00 48.85  ? 136  ASN   A C   1 
ATOM   2526 O O   . ASN   A 1 333 ? -8.821  33.737 18.145  1.00 54.44  ? 136  ASN   A O   1 
ATOM   2527 C CB  . ASN   A 1 333 ? -8.205  35.736 20.168  1.00 41.55  ? 136  ASN   A CB  1 
ATOM   2528 C CG  . ASN   A 1 333 ? -7.709  34.595 21.079  1.00 44.54  ? 136  ASN   A CG  1 
ATOM   2529 O OD1 . ASN   A 1 333 ? -8.460  33.694 21.414  1.00 43.97  ? 136  ASN   A OD1 1 
ATOM   2530 N ND2 . ASN   A 1 333 ? -6.448  34.635 21.451  1.00 47.59  ? 136  ASN   A ND2 1 
ATOM   2531 N N   . ILE   A 1 334 ? -10.671 33.278 19.334  1.00 47.62  ? 137  ILE   A N   1 
ATOM   2532 C CA  . ILE   A 1 334 ? -10.779 31.932 18.782  1.00 51.26  ? 137  ILE   A CA  1 
ATOM   2533 C C   . ILE   A 1 334 ? -10.858 32.002 17.262  1.00 48.58  ? 137  ILE   A C   1 
ATOM   2534 O O   . ILE   A 1 334 ? -11.217 33.056 16.695  1.00 45.02  ? 137  ILE   A O   1 
ATOM   2535 C CB  . ILE   A 1 334 ? -11.983 31.175 19.375  1.00 54.33  ? 137  ILE   A CB  1 
ATOM   2536 C CG1 . ILE   A 1 334 ? -13.291 31.863 18.976  1.00 55.30  ? 137  ILE   A CG1 1 
ATOM   2537 C CG2 . ILE   A 1 334 ? -11.865 31.125 20.897  1.00 54.62  ? 137  ILE   A CG2 1 
ATOM   2538 C CD1 . ILE   A 1 334 ? -14.493 31.284 19.701  1.00 58.21  ? 137  ILE   A CD1 1 
ATOM   2539 N N   . PRO   A 1 335 ? -10.502 30.902 16.571  1.00 46.16  ? 138  PRO   A N   1 
ATOM   2540 C CA  . PRO   A 1 335 ? -10.413 30.944 15.101  1.00 43.94  ? 138  PRO   A CA  1 
ATOM   2541 C C   . PRO   A 1 335 ? -11.738 31.186 14.416  1.00 47.18  ? 138  PRO   A C   1 
ATOM   2542 O O   . PRO   A 1 335 ? -11.769 31.786 13.317  1.00 48.07  ? 138  PRO   A O   1 
ATOM   2543 C CB  . PRO   A 1 335 ? -9.843  29.554 14.759  1.00 44.38  ? 138  PRO   A CB  1 
ATOM   2544 C CG  . PRO   A 1 335 ? -9.022  29.192 15.971  1.00 43.65  ? 138  PRO   A CG  1 
ATOM   2545 C CD  . PRO   A 1 335 ? -9.832  29.717 17.145  1.00 45.51  ? 138  PRO   A CD  1 
ATOM   2546 N N   . GLN   A 1 336 ? -12.852 30.806 15.049  1.00 47.37  ? 139  GLN   A N   1 
ATOM   2547 C CA  . GLN   A 1 336 ? -14.166 31.040 14.469  1.00 48.38  ? 139  GLN   A CA  1 
ATOM   2548 C C   . GLN   A 1 336 ? -14.599 32.524 14.460  1.00 45.75  ? 139  GLN   A C   1 
ATOM   2549 O O   . GLN   A 1 336 ? -15.655 32.851 13.896  1.00 44.53  ? 139  GLN   A O   1 
ATOM   2550 C CB  . GLN   A 1 336 ? -15.193 30.217 15.231  1.00 55.69  ? 139  GLN   A CB  1 
ATOM   2551 C CG  . GLN   A 1 336 ? -14.775 28.731 15.456  1.00 62.89  ? 139  GLN   A CG  1 
ATOM   2552 C CD  . GLN   A 1 336 ? -13.865 28.545 16.702  1.00 66.26  ? 139  GLN   A CD  1 
ATOM   2553 O OE1 . GLN   A 1 336 ? -14.079 29.163 17.749  1.00 68.64  ? 139  GLN   A OE1 1 
ATOM   2554 N NE2 . GLN   A 1 336 ? -12.863 27.705 16.577  1.00 67.29  ? 139  GLN   A NE2 1 
ATOM   2555 N N   . MET   A 1 337 ? -13.824 33.434 15.061  1.00 43.18  ? 140  MET   A N   1 
ATOM   2556 C CA  . MET   A 1 337 ? -14.259 34.844 15.095  1.00 42.93  ? 140  MET   A CA  1 
ATOM   2557 C C   . MET   A 1 337 ? -14.463 35.388 13.680  1.00 42.91  ? 140  MET   A C   1 
ATOM   2558 O O   . MET   A 1 337 ? -15.476 36.061 13.378  1.00 41.77  ? 140  MET   A O   1 
ATOM   2559 C CB  . MET   A 1 337 ? -13.242 35.711 15.841  1.00 42.15  ? 140  MET   A CB  1 
ATOM   2560 C CG  . MET   A 1 337 ? -13.423 35.635 17.356  1.00 44.58  ? 140  MET   A CG  1 
ATOM   2561 S SD  . MET   A 1 337 ? -15.147 36.075 17.819  1.00 44.97  ? 140  MET   A SD  1 
ATOM   2562 C CE  . MET   A 1 337 ? -15.102 37.856 17.385  1.00 45.90  ? 140  MET   A CE  1 
ATOM   2563 N N   . SER   A 1 338 ? -13.539 35.074 12.773  1.00 44.45  ? 141  SER   A N   1 
ATOM   2564 C CA  . SER   A 1 338 ? -13.657 35.547 11.406  1.00 46.11  ? 141  SER   A CA  1 
ATOM   2565 C C   . SER   A 1 338 ? -14.982 35.083 10.772  1.00 46.17  ? 141  SER   A C   1 
ATOM   2566 O O   . SER   A 1 338 ? -15.693 35.892 10.159  1.00 49.96  ? 141  SER   A O   1 
ATOM   2567 C CB  . SER   A 1 338 ? -12.416 35.112 10.621  1.00 50.34  ? 141  SER   A CB  1 
ATOM   2568 O OG  . SER   A 1 338 ? -12.651 35.134 9.238   1.00 56.07  ? 141  SER   A OG  1 
ATOM   2569 N N   . ALA   A 1 339 ? -15.302 33.807 10.952  1.00 38.52  ? 142  ALA   A N   1 
ATOM   2570 C CA  . ALA   A 1 339 ? -16.556 33.291 10.391  1.00 37.44  ? 142  ALA   A CA  1 
ATOM   2571 C C   . ALA   A 1 339 ? -17.758 33.965 11.007  1.00 37.93  ? 142  ALA   A C   1 
ATOM   2572 O O   . ALA   A 1 339 ? -18.744 34.265 10.326  1.00 39.64  ? 142  ALA   A O   1 
ATOM   2573 C CB  . ALA   A 1 339 ? -16.650 31.728 10.599  1.00 39.73  ? 142  ALA   A CB  1 
ATOM   2574 N N   . PHE   A 1 340 ? -17.718 34.215 12.304  1.00 39.20  ? 143  PHE   A N   1 
ATOM   2575 C CA  . PHE   A 1 340 ? -18.792 34.970 12.945  1.00 40.79  ? 143  PHE   A CA  1 
ATOM   2576 C C   . PHE   A 1 340 ? -18.959 36.349 12.302  1.00 40.95  ? 143  PHE   A C   1 
ATOM   2577 O O   . PHE   A 1 340 ? -20.082 36.776 11.938  1.00 37.06  ? 143  PHE   A O   1 
ATOM   2578 C CB  . PHE   A 1 340 ? -18.488 35.099 14.462  1.00 41.22  ? 143  PHE   A CB  1 
ATOM   2579 C CG  . PHE   A 1 340 ? -19.147 36.235 15.107  1.00 38.86  ? 143  PHE   A CG  1 
ATOM   2580 C CD1 . PHE   A 1 340 ? -20.504 36.204 15.376  1.00 41.76  ? 143  PHE   A CD1 1 
ATOM   2581 C CD2 . PHE   A 1 340 ? -18.424 37.419 15.423  1.00 35.95  ? 143  PHE   A CD2 1 
ATOM   2582 C CE1 . PHE   A 1 340 ? -21.134 37.371 15.925  1.00 39.48  ? 143  PHE   A CE1 1 
ATOM   2583 C CE2 . PHE   A 1 340 ? -19.027 38.454 15.986  1.00 31.02  ? 143  PHE   A CE2 1 
ATOM   2584 C CZ  . PHE   A 1 340 ? -20.370 38.440 16.244  1.00 34.50  ? 143  PHE   A CZ  1 
ATOM   2585 N N   . TRP   A 1 341 ? -17.839 37.079 12.150  1.00 42.45  ? 144  TRP   A N   1 
ATOM   2586 C CA  . TRP   A 1 341 ? -17.893 38.441 11.626  1.00 39.02  ? 144  TRP   A CA  1 
ATOM   2587 C C   . TRP   A 1 341 ? -18.424 38.470 10.186  1.00 42.00  ? 144  TRP   A C   1 
ATOM   2588 O O   . TRP   A 1 341 ? -19.219 39.355 9.804   1.00 41.35  ? 144  TRP   A O   1 
ATOM   2589 C CB  . TRP   A 1 341 ? -16.501 39.081 11.667  1.00 35.16  ? 144  TRP   A CB  1 
ATOM   2590 C CG  . TRP   A 1 341 ? -16.073 39.693 12.980  1.00 36.93  ? 144  TRP   A CG  1 
ATOM   2591 C CD1 . TRP   A 1 341 ? -14.890 39.464 13.643  1.00 38.74  ? 144  TRP   A CD1 1 
ATOM   2592 C CD2 . TRP   A 1 341 ? -16.807 40.635 13.789  1.00 36.08  ? 144  TRP   A CD2 1 
ATOM   2593 N NE1 . TRP   A 1 341 ? -14.847 40.208 14.810  1.00 39.14  ? 144  TRP   A NE1 1 
ATOM   2594 C CE2 . TRP   A 1 341 ? -16.010 40.941 14.912  1.00 36.64  ? 144  TRP   A CE2 1 
ATOM   2595 C CE3 . TRP   A 1 341 ? -18.055 41.248 13.664  1.00 37.57  ? 144  TRP   A CE3 1 
ATOM   2596 C CZ2 . TRP   A 1 341 ? -16.423 41.841 15.910  1.00 32.78  ? 144  TRP   A CZ2 1 
ATOM   2597 C CZ3 . TRP   A 1 341 ? -18.467 42.165 14.658  1.00 36.49  ? 144  TRP   A CZ3 1 
ATOM   2598 C CH2 . TRP   A 1 341 ? -17.646 42.434 15.761  1.00 34.19  ? 144  TRP   A CH2 1 
ATOM   2599 N N   . TYR   A 1 342 ? -17.941 37.577 9.343   1.00 44.46  ? 145  TYR   A N   1 
ATOM   2600 C CA  . TYR   A 1 342 ? -18.444 37.513 7.973   1.00 45.14  ? 145  TYR   A CA  1 
ATOM   2601 C C   . TYR   A 1 342 ? -19.956 37.299 7.970   1.00 39.33  ? 145  TYR   A C   1 
ATOM   2602 O O   . TYR   A 1 342 ? -20.676 37.876 7.161   1.00 36.68  ? 145  TYR   A O   1 
ATOM   2603 C CB  . TYR   A 1 342 ? -17.722 36.373 7.220   1.00 54.17  ? 145  TYR   A CB  1 
ATOM   2604 C CG  . TYR   A 1 342 ? -18.180 36.176 5.793   1.00 62.54  ? 145  TYR   A CG  1 
ATOM   2605 C CD1 . TYR   A 1 342 ? -17.683 36.977 4.770   1.00 66.54  ? 145  TYR   A CD1 1 
ATOM   2606 C CD2 . TYR   A 1 342 ? -19.115 35.211 5.464   1.00 67.77  ? 145  TYR   A CD2 1 
ATOM   2607 C CE1 . TYR   A 1 342 ? -18.093 36.821 3.469   1.00 70.84  ? 145  TYR   A CE1 1 
ATOM   2608 C CE2 . TYR   A 1 342 ? -19.527 35.026 4.154   1.00 73.51  ? 145  TYR   A CE2 1 
ATOM   2609 C CZ  . TYR   A 1 342 ? -19.015 35.842 3.160   1.00 76.31  ? 145  TYR   A CZ  1 
ATOM   2610 O OH  . TYR   A 1 342 ? -19.423 35.673 1.849   1.00 81.62  ? 145  TYR   A OH  1 
ATOM   2611 N N   . ALA   A 1 343 ? -20.445 36.421 8.845   1.00 37.81  ? 146  ALA   A N   1 
ATOM   2612 C CA  . ALA   A 1 343 ? -21.872 36.126 8.848   1.00 37.90  ? 146  ALA   A CA  1 
ATOM   2613 C C   . ALA   A 1 343 ? -22.681 37.348 9.304   1.00 34.88  ? 146  ALA   A C   1 
ATOM   2614 O O   . ALA   A 1 343 ? -23.714 37.669 8.725   1.00 36.90  ? 146  ALA   A O   1 
ATOM   2615 C CB  . ALA   A 1 343 ? -22.172 34.888 9.717   1.00 34.85  ? 146  ALA   A CB  1 
ATOM   2616 N N   . VAL   A 1 344 ? -22.270 37.972 10.410  1.00 34.71  ? 147  VAL   A N   1 
ATOM   2617 C CA  . VAL   A 1 344 ? -23.077 39.072 10.941  1.00 35.83  ? 147  VAL   A CA  1 
ATOM   2618 C C   . VAL   A 1 344 ? -23.021 40.292 10.008  1.00 36.39  ? 147  VAL   A C   1 
ATOM   2619 O O   . VAL   A 1 344 ? -24.013 41.018 9.881   1.00 34.61  ? 147  VAL   A O   1 
ATOM   2620 C CB  . VAL   A 1 344 ? -22.615 39.468 12.361  1.00 35.89  ? 147  VAL   A CB  1 
ATOM   2621 C CG1 . VAL   A 1 344 ? -23.413 40.699 12.825  1.00 29.37  ? 147  VAL   A CG1 1 
ATOM   2622 C CG2 . VAL   A 1 344 ? -22.841 38.287 13.319  1.00 31.02  ? 147  VAL   A CG2 1 
ATOM   2623 N N   . ARG   A 1 345 ? -21.890 40.499 9.325   1.00 38.37  ? 148  ARG   A N   1 
ATOM   2624 C CA  . ARG   A 1 345 ? -21.791 41.567 8.334   1.00 40.70  ? 148  ARG   A CA  1 
ATOM   2625 C C   . ARG   A 1 345 ? -22.832 41.380 7.246   1.00 37.66  ? 148  ARG   A C   1 
ATOM   2626 O O   . ARG   A 1 345 ? -23.537 42.323 6.874   1.00 35.26  ? 148  ARG   A O   1 
ATOM   2627 C CB  . ARG   A 1 345 ? -20.385 41.584 7.719   1.00 46.13  ? 148  ARG   A CB  1 
ATOM   2628 C CG  . ARG   A 1 345 ? -20.234 42.555 6.520   1.00 49.58  ? 148  ARG   A CG  1 
ATOM   2629 C CD  . ARG   A 1 345 ? -18.857 42.460 5.837   1.00 56.70  ? 148  ARG   A CD  1 
ATOM   2630 N NE  . ARG   A 1 345 ? -17.755 42.752 6.772   1.00 64.69  ? 148  ARG   A NE  1 
ATOM   2631 C CZ  . ARG   A 1 345 ? -16.853 41.847 7.191   1.00 68.43  ? 148  ARG   A CZ  1 
ATOM   2632 N NH1 . ARG   A 1 345 ? -16.902 40.583 6.753   1.00 67.76  ? 148  ARG   A NH1 1 
ATOM   2633 N NH2 . ARG   A 1 345 ? -15.899 42.205 8.053   1.00 68.73  ? 148  ARG   A NH2 1 
ATOM   2634 N N   . THR   A 1 346 ? -22.916 40.153 6.709   1.00 35.34  ? 149  THR   A N   1 
ATOM   2635 C CA  . THR   A 1 346 ? -23.921 39.916 5.686   1.00 36.91  ? 149  THR   A CA  1 
ATOM   2636 C C   . THR   A 1 346 ? -25.323 40.141 6.230   1.00 40.57  ? 149  THR   A C   1 
ATOM   2637 O O   . THR   A 1 346 ? -26.209 40.693 5.536   1.00 41.27  ? 149  THR   A O   1 
ATOM   2638 C CB  . THR   A 1 346 ? -23.781 38.494 5.182   1.00 38.44  ? 149  THR   A CB  1 
ATOM   2639 O OG1 . THR   A 1 346 ? -22.586 38.453 4.391   1.00 36.68  ? 149  THR   A OG1 1 
ATOM   2640 C CG2 . THR   A 1 346 ? -24.982 38.067 4.362   1.00 34.60  ? 149  THR   A CG2 1 
ATOM   2641 N N   . ALA   A 1 347 ? -25.589 39.758 7.483   1.00 39.88  ? 150  ALA   A N   1 
ATOM   2642 C CA  . ALA   A 1 347 ? -26.937 39.845 8.026   1.00 38.23  ? 150  ALA   A CA  1 
ATOM   2643 C C   . ALA   A 1 347 ? -27.337 41.286 8.292   1.00 37.06  ? 150  ALA   A C   1 
ATOM   2644 O O   . ALA   A 1 347 ? -28.485 41.680 8.031   1.00 34.06  ? 150  ALA   A O   1 
ATOM   2645 C CB  . ALA   A 1 347 ? -27.033 39.013 9.306   1.00 36.94  ? 150  ALA   A CB  1 
ATOM   2646 N N   . VAL   A 1 348 ? -26.415 42.087 8.844   1.00 37.43  ? 151  VAL   A N   1 
ATOM   2647 C CA  . VAL   A 1 348 ? -26.756 43.487 9.084   1.00 39.40  ? 151  VAL   A CA  1 
ATOM   2648 C C   . VAL   A 1 348 ? -27.059 44.208 7.770   1.00 38.57  ? 151  VAL   A C   1 
ATOM   2649 O O   . VAL   A 1 348 ? -28.031 44.972 7.654   1.00 38.18  ? 151  VAL   A O   1 
ATOM   2650 C CB  . VAL   A 1 348 ? -25.626 44.182 9.888   1.00 36.50  ? 151  VAL   A CB  1 
ATOM   2651 C CG1 . VAL   A 1 348 ? -25.789 45.696 9.848   1.00 32.83  ? 151  VAL   A CG1 1 
ATOM   2652 C CG2 . VAL   A 1 348 ? -25.633 43.647 11.315  1.00 28.17  ? 151  VAL   A CG2 1 
ATOM   2653 N N   . ILE   A 1 349 ? -26.257 43.943 6.749   1.00 40.94  ? 152  ILE   A N   1 
ATOM   2654 C CA  . ILE   A 1 349 ? -26.420 44.642 5.475   1.00 40.28  ? 152  ILE   A CA  1 
ATOM   2655 C C   . ILE   A 1 349 ? -27.722 44.224 4.797   1.00 39.73  ? 152  ILE   A C   1 
ATOM   2656 O O   . ILE   A 1 349 ? -28.477 45.067 4.312   1.00 40.77  ? 152  ILE   A O   1 
ATOM   2657 C CB  . ILE   A 1 349 ? -25.203 44.373 4.576   1.00 40.30  ? 152  ILE   A CB  1 
ATOM   2658 C CG1 . ILE   A 1 349 ? -24.021 45.240 5.045   1.00 39.61  ? 152  ILE   A CG1 1 
ATOM   2659 C CG2 . ILE   A 1 349 ? -25.560 44.635 3.086   1.00 38.47  ? 152  ILE   A CG2 1 
ATOM   2660 C CD1 . ILE   A 1 349 ? -22.648 44.837 4.521   1.00 37.68  ? 152  ILE   A CD1 1 
ATOM   2661 N N   . ASN   A 1 350 ? -27.997 42.901 4.726   1.00 36.66  ? 153  ASN   A N   1 
ATOM   2662 C CA  . ASN   A 1 350 ? -29.241 42.445 4.122   1.00 37.89  ? 153  ASN   A CA  1 
ATOM   2663 C C   . ASN   A 1 350 ? -30.472 42.951 4.891   1.00 38.93  ? 153  ASN   A C   1 
ATOM   2664 O O   . ASN   A 1 350 ? -31.489 43.302 4.286   1.00 40.70  ? 153  ASN   A O   1 
ATOM   2665 C CB  . ASN   A 1 350 ? -29.271 40.911 4.068   1.00 43.64  ? 153  ASN   A CB  1 
ATOM   2666 C CG  . ASN   A 1 350 ? -28.316 40.353 3.035   1.00 44.83  ? 153  ASN   A CG  1 
ATOM   2667 O OD1 . ASN   A 1 350 ? -27.700 41.127 2.265   1.00 47.56  ? 153  ASN   A OD1 1 
ATOM   2668 N ND2 . ASN   A 1 350 ? -28.154 39.066 3.030   1.00 42.36  ? 153  ASN   A ND2 1 
ATOM   2669 N N   . ALA   A 1 351 ? -30.419 42.960 6.222   1.00 37.59  ? 154  ALA   A N   1 
ATOM   2670 C CA  . ALA   A 1 351 ? -31.556 43.449 6.997   1.00 38.84  ? 154  ALA   A CA  1 
ATOM   2671 C C   . ALA   A 1 351 ? -31.735 44.982 6.837   1.00 41.17  ? 154  ALA   A C   1 
ATOM   2672 O O   . ALA   A 1 351 ? -32.871 45.487 6.723   1.00 41.20  ? 154  ALA   A O   1 
ATOM   2673 C CB  . ALA   A 1 351 ? -31.378 43.065 8.488   1.00 34.11  ? 154  ALA   A CB  1 
ATOM   2674 N N   . ALA   A 1 352 ? -30.636 45.725 6.820   1.00 40.21  ? 155  ALA   A N   1 
ATOM   2675 C CA  . ALA   A 1 352 ? -30.739 47.173 6.642   1.00 38.46  ? 155  ALA   A CA  1 
ATOM   2676 C C   . ALA   A 1 352 ? -31.294 47.525 5.262   1.00 43.24  ? 155  ALA   A C   1 
ATOM   2677 O O   . ALA   A 1 352 ? -32.081 48.463 5.126   1.00 44.40  ? 155  ALA   A O   1 
ATOM   2678 C CB  . ALA   A 1 352 ? -29.377 47.823 6.842   1.00 33.62  ? 155  ALA   A CB  1 
ATOM   2679 N N   . SER   A 1 353 ? -30.912 46.778 4.218   1.00 44.26  ? 156  SER   A N   1 
ATOM   2680 C CA  . SER   A 1 353 ? -31.305 47.082 2.864   1.00 41.52  ? 156  SER   A CA  1 
ATOM   2681 C C   . SER   A 1 353 ? -32.643 46.470 2.501   1.00 46.45  ? 156  SER   A C   1 
ATOM   2682 O O   . SER   A 1 353 ? -33.199 46.819 1.466   1.00 50.99  ? 156  SER   A O   1 
ATOM   2683 C CB  . SER   A 1 353 ? -30.240 46.647 1.896   1.00 40.39  ? 156  SER   A CB  1 
ATOM   2684 O OG  . SER   A 1 353 ? -30.366 45.230 1.629   1.00 42.48  ? 156  SER   A OG  1 
ATOM   2685 N N   . GLY   A 1 354 ? -33.158 45.541 3.298   1.00 46.03  ? 157  GLY   A N   1 
ATOM   2686 C CA  . GLY   A 1 354 ? -34.429 44.899 2.961   1.00 45.48  ? 157  GLY   A CA  1 
ATOM   2687 C C   . GLY   A 1 354 ? -34.318 43.586 2.202   1.00 44.86  ? 157  GLY   A C   1 
ATOM   2688 O O   . GLY   A 1 354 ? -35.342 42.967 1.936   1.00 48.36  ? 157  GLY   A O   1 
ATOM   2689 N N   . ARG   A 1 355 ? -33.119 43.150 1.825   1.00 43.34  ? 158  ARG   A N   1 
ATOM   2690 C CA  . ARG   A 1 355 ? -32.982 41.880 1.082   1.00 45.60  ? 158  ARG   A CA  1 
ATOM   2691 C C   . ARG   A 1 355 ? -33.534 40.691 1.893   1.00 47.64  ? 158  ARG   A C   1 
ATOM   2692 O O   . ARG   A 1 355 ? -34.137 39.779 1.342   1.00 48.80  ? 158  ARG   A O   1 
ATOM   2693 C CB  . ARG   A 1 355 ? -31.533 41.630 0.686   1.00 41.56  ? 158  ARG   A CB  1 
ATOM   2694 N N   . GLN   A 1 356 ? -33.362 40.713 3.213   1.00 47.18  ? 159  GLN   A N   1 
ATOM   2695 C CA  . GLN   A 1 356 ? -33.986 39.766 4.113   1.00 47.76  ? 159  GLN   A CA  1 
ATOM   2696 C C   . GLN   A 1 356 ? -34.643 40.523 5.268   1.00 48.23  ? 159  GLN   A C   1 
ATOM   2697 O O   . GLN   A 1 356 ? -34.269 41.649 5.582   1.00 46.30  ? 159  GLN   A O   1 
ATOM   2698 C CB  . GLN   A 1 356 ? -32.969 38.763 4.677   1.00 45.31  ? 159  GLN   A CB  1 
ATOM   2699 C CG  . GLN   A 1 356 ? -32.096 38.094 3.632   1.00 43.63  ? 159  GLN   A CG  1 
ATOM   2700 C CD  . GLN   A 1 356 ? -31.090 37.141 4.257   1.00 43.66  ? 159  GLN   A CD  1 
ATOM   2701 O OE1 . GLN   A 1 356 ? -30.014 37.539 4.704   1.00 44.48  ? 159  GLN   A OE1 1 
ATOM   2702 N NE2 . GLN   A 1 356 ? -31.449 35.866 4.311   1.00 46.18  ? 159  GLN   A NE2 1 
ATOM   2703 N N   . THR   A 1 357 ? -35.612 39.863 5.925   1.00 48.79  ? 160  THR   A N   1 
ATOM   2704 C CA  . THR   A 1 357 ? -36.123 40.329 7.213   1.00 45.94  ? 160  THR   A CA  1 
ATOM   2705 C C   . THR   A 1 357 ? -35.055 40.156 8.301   1.00 43.12  ? 160  THR   A C   1 
ATOM   2706 O O   . THR   A 1 357 ? -34.062 39.396 8.135   1.00 45.22  ? 160  THR   A O   1 
ATOM   2707 C CB  . THR   A 1 357 ? -37.388 39.532 7.591   1.00 47.02  ? 160  THR   A CB  1 
ATOM   2708 O OG1 . THR   A 1 357 ? -37.021 38.165 7.876   1.00 47.97  ? 160  THR   A OG1 1 
ATOM   2709 C CG2 . THR   A 1 357 ? -38.385 39.535 6.472   1.00 46.52  ? 160  THR   A CG2 1 
ATOM   2710 N N   . VAL   A 1 358 ? -35.294 40.761 9.459   1.00 68.42  ? 161  VAL   A N   1 
ATOM   2711 C CA  . VAL   A 1 358 ? -34.410 40.521 10.591  1.00 62.55  ? 161  VAL   A CA  1 
ATOM   2712 C C   . VAL   A 1 358 ? -34.388 39.030 10.934  1.00 59.67  ? 161  VAL   A C   1 
ATOM   2713 O O   . VAL   A 1 358 ? -33.314 38.431 11.170  1.00 56.85  ? 161  VAL   A O   1 
ATOM   2714 C CB  . VAL   A 1 358 ? -34.835 41.392 11.785  1.00 65.04  ? 161  VAL   A CB  1 
ATOM   2715 C CG1 . VAL   A 1 358 ? -34.111 40.955 13.054  1.00 63.34  ? 161  VAL   A CG1 1 
ATOM   2716 C CG2 . VAL   A 1 358 ? -34.557 42.885 11.477  1.00 67.53  ? 161  VAL   A CG2 1 
ATOM   2717 N N   . ASP   A 1 359 ? -35.561 38.386 10.892  1.00 61.12  ? 162  ASP   A N   1 
ATOM   2718 C CA  . ASP   A 1 359 ? -35.602 36.935 11.182  1.00 58.64  ? 162  ASP   A CA  1 
ATOM   2719 C C   . ASP   A 1 359 ? -34.741 36.152 10.202  1.00 55.59  ? 162  ASP   A C   1 
ATOM   2720 O O   . ASP   A 1 359 ? -33.860 35.392 10.604  1.00 52.51  ? 162  ASP   A O   1 
ATOM   2721 C CB  . ASP   A 1 359 ? -37.044 36.440 11.158  1.00 61.25  ? 162  ASP   A CB  1 
ATOM   2722 C CG  . ASP   A 1 359 ? -37.844 36.887 12.380  1.00 68.32  ? 162  ASP   A CG  1 
ATOM   2723 O OD1 . ASP   A 1 359 ? -37.235 37.216 13.417  1.00 67.76  ? 162  ASP   A OD1 1 
ATOM   2724 O OD2 . ASP   A 1 359 ? -39.084 36.915 12.309  1.00 70.96  ? 162  ASP   A OD2 1 
ATOM   2725 N N   . GLU   A 1 360 ? -34.992 36.335 8.897   1.00 59.09  ? 163  GLU   A N   1 
ATOM   2726 C CA  . GLU   A 1 360 ? -34.163 35.680 7.875   1.00 56.48  ? 163  GLU   A CA  1 
ATOM   2727 C C   . GLU   A 1 360 ? -32.692 35.973 8.090   1.00 52.56  ? 163  GLU   A C   1 
ATOM   2728 O O   . GLU   A 1 360 ? -31.853 35.060 8.182   1.00 49.10  ? 163  GLU   A O   1 
ATOM   2729 C CB  . GLU   A 1 360 ? -34.543 36.183 6.479   1.00 61.78  ? 163  GLU   A CB  1 
ATOM   2730 C CG  . GLU   A 1 360 ? -35.904 35.817 5.945   1.00 67.88  ? 163  GLU   A CG  1 
ATOM   2731 C CD  . GLU   A 1 360 ? -36.314 36.680 4.745   1.00 73.17  ? 163  GLU   A CD  1 
ATOM   2732 O OE1 . GLU   A 1 360 ? -37.420 37.238 4.745   1.00 77.42  ? 163  GLU   A OE1 1 
ATOM   2733 O OE2 . GLU   A 1 360 ? -35.488 36.809 3.809   1.00 73.82  ? 163  GLU   A OE2 1 
ATOM   2734 N N   . ALA   A 1 361 ? -32.327 37.264 8.198   1.00 55.42  ? 164  ALA   A N   1 
ATOM   2735 C CA  . ALA   A 1 361 ? -30.935 37.674 8.201   1.00 54.85  ? 164  ALA   A CA  1 
ATOM   2736 C C   . ALA   A 1 361 ? -30.188 37.039 9.357   1.00 49.13  ? 164  ALA   A C   1 
ATOM   2737 O O   . ALA   A 1 361 ? -29.094 36.498 9.174   1.00 52.63  ? 164  ALA   A O   1 
ATOM   2738 C CB  . ALA   A 1 361 ? -30.858 39.214 8.255   1.00 58.45  ? 164  ALA   A CB  1 
ATOM   2739 N N   . LEU   A 1 362 ? -30.768 37.059 10.547  1.00 49.77  ? 165  LEU   A N   1 
ATOM   2740 C CA  . LEU   A 1 362 ? -30.073 36.514 11.713  1.00 53.84  ? 165  LEU   A CA  1 
ATOM   2741 C C   . LEU   A 1 362 ? -30.079 35.001 11.753  1.00 51.52  ? 165  LEU   A C   1 
ATOM   2742 O O   . LEU   A 1 362 ? -29.113 34.376 12.250  1.00 43.04  ? 165  LEU   A O   1 
ATOM   2743 C CB  . LEU   A 1 362 ? -30.692 37.077 12.997  1.00 56.03  ? 165  LEU   A CB  1 
ATOM   2744 C CG  . LEU   A 1 362 ? -30.429 38.566 13.204  1.00 51.94  ? 165  LEU   A CG  1 
ATOM   2745 C CD1 . LEU   A 1 362 ? -31.125 39.085 14.472  1.00 54.24  ? 165  LEU   A CD1 1 
ATOM   2746 C CD2 . LEU   A 1 362 ? -28.941 38.795 13.294  1.00 50.35  ? 165  LEU   A CD2 1 
ATOM   2747 N N   . LYS   A 1 363 ? -31.126 34.368 11.222  1.00 53.72  ? 166  LYS   A N   1 
ATOM   2748 C CA  . LYS   A 1 363 ? -31.104 32.894 11.161  1.00 49.42  ? 166  LYS   A CA  1 
ATOM   2749 C C   . LYS   A 1 363 ? -29.923 32.405 10.333  1.00 45.38  ? 166  LYS   A C   1 
ATOM   2750 O O   . LYS   A 1 363 ? -29.145 31.565 10.786  1.00 43.53  ? 166  LYS   A O   1 
ATOM   2751 C CB  . LYS   A 1 363 ? -32.422 32.359 10.594  1.00 53.09  ? 166  LYS   A CB  1 
ATOM   2752 N N   . ASP   A 1 364 ? -29.753 32.975 9.129   1.00 49.20  ? 167  ASP   A N   1 
ATOM   2753 C CA  . ASP   A 1 364 ? -28.614 32.632 8.267   1.00 47.22  ? 167  ASP   A CA  1 
ATOM   2754 C C   . ASP   A 1 364 ? -27.302 32.892 8.986   1.00 46.29  ? 167  ASP   A C   1 
ATOM   2755 O O   . ASP   A 1 364 ? -26.370 32.101 8.879   1.00 40.94  ? 167  ASP   A O   1 
ATOM   2756 C CB  . ASP   A 1 364 ? -28.661 33.455 6.973   1.00 45.93  ? 167  ASP   A CB  1 
ATOM   2757 C CG  . ASP   A 1 364 ? -29.661 32.934 5.993   1.00 47.22  ? 167  ASP   A CG  1 
ATOM   2758 O OD1 . ASP   A 1 364 ? -30.320 31.942 6.320   1.00 46.24  ? 167  ASP   A OD1 1 
ATOM   2759 O OD2 . ASP   A 1 364 ? -29.794 33.504 4.903   1.00 49.57  ? 167  ASP   A OD2 1 
ATOM   2760 N N   . ALA   A 1 365 ? -27.204 34.026 9.687   1.00 47.34  ? 168  ALA   A N   1 
ATOM   2761 C CA  . ALA   A 1 365 ? -25.971 34.343 10.381  1.00 48.21  ? 168  ALA   A CA  1 
ATOM   2762 C C   . ALA   A 1 365 ? -25.731 33.368 11.512  1.00 46.16  ? 168  ALA   A C   1 
ATOM   2763 O O   . ALA   A 1 365 ? -24.575 33.038 11.796  1.00 44.09  ? 168  ALA   A O   1 
ATOM   2764 C CB  . ALA   A 1 365 ? -25.998 35.795 10.906  1.00 41.98  ? 168  ALA   A CB  1 
ATOM   2765 N N   . GLN   A 1 366 ? -26.799 32.954 12.204  1.00 45.58  ? 169  GLN   A N   1 
ATOM   2766 C CA  . GLN   A 1 366 ? -26.657 31.903 13.204  1.00 46.78  ? 169  GLN   A CA  1 
ATOM   2767 C C   . GLN   A 1 366 ? -26.166 30.603 12.568  1.00 43.21  ? 169  GLN   A C   1 
ATOM   2768 O O   . GLN   A 1 366 ? -25.306 29.910 13.122  1.00 41.45  ? 169  GLN   A O   1 
ATOM   2769 C CB  . GLN   A 1 366 ? -27.978 31.660 13.927  1.00 50.46  ? 169  GLN   A CB  1 
ATOM   2770 C CG  . GLN   A 1 366 ? -27.920 30.579 14.978  1.00 48.54  ? 169  GLN   A CG  1 
ATOM   2771 C CD  . GLN   A 1 366 ? -27.385 31.100 16.305  1.00 50.27  ? 169  GLN   A CD  1 
ATOM   2772 O OE1 . GLN   A 1 366 ? -27.379 32.284 16.549  1.00 49.29  ? 169  GLN   A OE1 1 
ATOM   2773 N NE2 . GLN   A 1 366 ? -26.897 30.163 17.180  1.00 48.40  ? 169  GLN   A NE2 1 
ATOM   2774 N N   . THR   A 1 367 ? -26.714 30.244 11.422  1.00 43.10  ? 170  THR   A N   1 
ATOM   2775 C CA  . THR   A 1 367 ? -26.267 29.006 10.753  1.00 42.01  ? 170  THR   A CA  1 
ATOM   2776 C C   . THR   A 1 367 ? -24.830 29.130 10.272  1.00 39.50  ? 170  THR   A C   1 
ATOM   2777 O O   . THR   A 1 367 ? -24.044 28.171 10.383  1.00 33.31  ? 170  THR   A O   1 
ATOM   2778 C CB  . THR   A 1 367 ? -27.192 28.675 9.587   1.00 44.46  ? 170  THR   A CB  1 
ATOM   2779 O OG1 . THR   A 1 367 ? -28.531 28.469 10.108  1.00 44.88  ? 170  THR   A OG1 1 
ATOM   2780 C CG2 . THR   A 1 367 ? -26.730 27.388 8.861   1.00 45.13  ? 170  THR   A CG2 1 
ATOM   2781 N N   . GLY   A 1 368 ? -24.424 30.350 9.866   1.00 39.92  ? 171  GLY   A N   1 
ATOM   2782 C CA  . GLY   A 1 368 ? -23.056 30.543 9.449   1.00 38.96  ? 171  GLY   A CA  1 
ATOM   2783 C C   . GLY   A 1 368 ? -22.066 30.495 10.589  1.00 38.76  ? 171  GLY   A C   1 
ATOM   2784 O O   . GLY   A 1 368 ? -21.009 29.854 10.457  1.00 38.73  ? 171  GLY   A O   1 
ATOM   2785 N N   . SER   A 1 369 ? -22.373 31.154 11.710  1.00 38.54  ? 172  SER   A N   1 
ATOM   2786 C CA  . SER   A 1 369 ? -21.444 31.139 12.840  1.00 40.75  ? 172  SER   A CA  1 
ATOM   2787 C C   . SER   A 1 369 ? -21.291 29.732 13.454  1.00 44.87  ? 172  SER   A C   1 
ATOM   2788 O O   . SER   A 1 369 ? -20.251 29.440 14.088  1.00 44.77  ? 172  SER   A O   1 
ATOM   2789 C CB  . SER   A 1 369 ? -21.893 32.110 13.910  1.00 40.21  ? 172  SER   A CB  1 
ATOM   2790 O OG  . SER   A 1 369 ? -22.410 33.358 13.344  1.00 42.24  ? 172  SER   A OG  1 
ATOM   2791 N N   . GLU   A 1 370 ? -22.308 28.871 13.309  1.00 46.45  ? 173  GLU   A N   1 
ATOM   2792 C CA  . GLU   A 1 370 ? -22.284 27.525 13.892  1.00 44.83  ? 173  GLU   A CA  1 
ATOM   2793 C C   . GLU   A 1 370 ? -21.754 26.473 12.917  1.00 44.20  ? 173  GLU   A C   1 
ATOM   2794 O O   . GLU   A 1 370 ? -21.533 25.313 13.313  1.00 43.79  ? 173  GLU   A O   1 
ATOM   2795 C CB  . GLU   A 1 370 ? -23.689 27.127 14.338  1.00 44.89  ? 173  GLU   A CB  1 
ATOM   2796 C CG  . GLU   A 1 370 ? -24.011 27.484 15.790  1.00 51.65  ? 173  GLU   A CG  1 
ATOM   2797 C CD  . GLU   A 1 370 ? -25.494 27.319 16.128  1.00 58.48  ? 173  GLU   A CD  1 
ATOM   2798 O OE1 . GLU   A 1 370 ? -26.316 27.077 15.188  1.00 61.35  ? 173  GLU   A OE1 1 
ATOM   2799 O OE2 . GLU   A 1 370 ? -25.847 27.386 17.339  1.00 60.68  ? 173  GLU   A OE2 1 
ATOM   2800 N N   . LEU   A 1 371 ? -21.519 26.846 11.655  1.00 45.31  ? 174  LEU   A N   1 
ATOM   2801 C CA  . LEU   A 1 371 ? -21.278 25.852 10.615  1.00 42.92  ? 174  LEU   A CA  1 
ATOM   2802 C C   . LEU   A 1 371 ? -20.075 24.973 10.952  1.00 39.58  ? 174  LEU   A C   1 
ATOM   2803 O O   . LEU   A 1 371 ? -20.141 23.747 10.799  1.00 38.14  ? 174  LEU   A O   1 
ATOM   2804 C CB  . LEU   A 1 371 ? -21.070 26.543 9.280   1.00 43.31  ? 174  LEU   A CB  1 
ATOM   2805 C CG  . LEU   A 1 371 ? -21.108 25.610 8.069   1.00 40.31  ? 174  LEU   A CG  1 
ATOM   2806 C CD1 . LEU   A 1 371 ? -22.289 24.693 8.129   1.00 34.59  ? 174  LEU   A CD1 1 
ATOM   2807 C CD2 . LEU   A 1 371 ? -21.185 26.540 6.812   1.00 43.77  ? 174  LEU   A CD2 1 
ATOM   2808 N N   . TYR   A 1 372 ? -18.959 25.583 11.369  1.00 39.40  ? 175  TYR   A N   1 
ATOM   2809 C CA  . TYR   A 1 372 ? -17.759 24.796 11.570  1.00 43.14  ? 175  TYR   A CA  1 
ATOM   2810 C C   . TYR   A 1 372 ? -17.923 23.792 12.719  1.00 41.55  ? 175  TYR   A C   1 
ATOM   2811 O O   . TYR   A 1 372 ? -17.689 22.598 12.542  1.00 41.67  ? 175  TYR   A O   1 
ATOM   2812 C CB  . TYR   A 1 372 ? -16.559 25.692 11.814  1.00 46.83  ? 175  TYR   A CB  1 
ATOM   2813 C CG  . TYR   A 1 372 ? -15.300 24.866 12.043  1.00 50.71  ? 175  TYR   A CG  1 
ATOM   2814 C CD1 . TYR   A 1 372 ? -14.987 24.378 13.313  1.00 50.45  ? 175  TYR   A CD1 1 
ATOM   2815 C CD2 . TYR   A 1 372 ? -14.463 24.522 10.976  1.00 53.09  ? 175  TYR   A CD2 1 
ATOM   2816 C CE1 . TYR   A 1 372 ? -13.851 23.600 13.533  1.00 50.13  ? 175  TYR   A CE1 1 
ATOM   2817 C CE2 . TYR   A 1 372 ? -13.326 23.724 11.189  1.00 53.49  ? 175  TYR   A CE2 1 
ATOM   2818 C CZ  . TYR   A 1 372 ? -13.034 23.281 12.472  1.00 51.76  ? 175  TYR   A CZ  1 
ATOM   2819 O OH  . TYR   A 1 372 ? -11.901 22.548 12.701  1.00 54.07  ? 175  TYR   A OH  1 
ATOM   2820 N N   . ARG   A 1 373 ? -18.336 24.257 13.883  1.00 40.11  ? 176  ARG   A N   1 
ATOM   2821 C CA  . ARG   A 1 373 ? -18.503 23.370 15.023  1.00 41.80  ? 176  ARG   A CA  1 
ATOM   2822 C C   . ARG   A 1 373 ? -19.469 22.219 14.698  1.00 39.97  ? 176  ARG   A C   1 
ATOM   2823 O O   . ARG   A 1 373 ? -19.198 21.064 15.007  1.00 38.27  ? 176  ARG   A O   1 
ATOM   2824 C CB  . ARG   A 1 373 ? -18.990 24.148 16.242  1.00 44.99  ? 176  ARG   A CB  1 
ATOM   2825 C CG  . ARG   A 1 373 ? -18.852 23.387 17.518  1.00 52.56  ? 176  ARG   A CG  1 
ATOM   2826 C CD  . ARG   A 1 373 ? -17.394 22.916 17.708  1.00 60.21  ? 176  ARG   A CD  1 
ATOM   2827 N NE  . ARG   A 1 373 ? -17.275 21.727 18.543  1.00 65.76  ? 176  ARG   A NE  1 
ATOM   2828 C CZ  . ARG   A 1 373 ? -17.358 20.487 18.070  1.00 70.29  ? 176  ARG   A CZ  1 
ATOM   2829 N NH1 . ARG   A 1 373 ? -17.228 19.433 18.890  1.00 73.12  ? 176  ARG   A NH1 1 
ATOM   2830 N NH2 . ARG   A 1 373 ? -17.564 20.294 16.770  1.00 70.22  ? 176  ARG   A NH2 1 
ATOM   2831 N N   . GLN   A 1 374 ? -20.592 22.528 14.064  1.00 41.06  ? 177  GLN   A N   1 
ATOM   2832 C CA  . GLN   A 1 374 ? -21.602 21.523 13.816  1.00 42.30  ? 177  GLN   A CA  1 
ATOM   2833 C C   . GLN   A 1 374 ? -21.097 20.498 12.810  1.00 38.07  ? 177  GLN   A C   1 
ATOM   2834 O O   . GLN   A 1 374 ? -21.237 19.301 13.038  1.00 37.83  ? 177  GLN   A O   1 
ATOM   2835 C CB  . GLN   A 1 374 ? -22.890 22.175 13.327  1.00 48.58  ? 177  GLN   A CB  1 
ATOM   2836 C CG  . GLN   A 1 374 ? -23.980 21.142 12.989  1.00 54.07  ? 177  GLN   A CG  1 
ATOM   2837 C CD  . GLN   A 1 374 ? -25.376 21.626 13.336  1.00 61.35  ? 177  GLN   A CD  1 
ATOM   2838 O OE1 . GLN   A 1 374 ? -26.233 20.821 13.716  1.00 64.33  ? 177  GLN   A OE1 1 
ATOM   2839 N NE2 . GLN   A 1 374 ? -25.615 22.953 13.213  1.00 62.63  ? 177  GLN   A NE2 1 
ATOM   2840 N N   . SER   A 1 375 ? -20.440 20.950 11.729  1.00 37.01  ? 178  SER   A N   1 
ATOM   2841 C CA  . SER   A 1 375 ? -19.846 20.051 10.769  1.00 36.18  ? 178  SER   A CA  1 
ATOM   2842 C C   . SER   A 1 375 ? -18.791 19.154 11.439  1.00 36.90  ? 178  SER   A C   1 
ATOM   2843 O O   . SER   A 1 375 ? -18.768 17.960 11.203  1.00 34.17  ? 178  SER   A O   1 
ATOM   2844 C CB  . SER   A 1 375 ? -19.266 20.825 9.594   1.00 33.57  ? 178  SER   A CB  1 
ATOM   2845 O OG  . SER   A 1 375 ? -20.224 21.745 9.099   1.00 35.70  ? 178  SER   A OG  1 
ATOM   2846 N N   . LEU   A 1 376 ? -17.891 19.774 12.223  1.00 38.24  ? 179  LEU   A N   1 
ATOM   2847 C CA  . LEU   A 1 376 ? -16.887 18.942 12.919  1.00 37.21  ? 179  LEU   A CA  1 
ATOM   2848 C C   . LEU   A 1 376 ? -17.539 17.879 13.805  1.00 39.21  ? 179  LEU   A C   1 
ATOM   2849 O O   . LEU   A 1 376 ? -17.096 16.717 13.825  1.00 42.24  ? 179  LEU   A O   1 
ATOM   2850 C CB  . LEU   A 1 376 ? -15.956 19.809 13.753  1.00 33.75  ? 179  LEU   A CB  1 
ATOM   2851 C CG  . LEU   A 1 376 ? -14.868 19.065 14.514  1.00 32.72  ? 179  LEU   A CG  1 
ATOM   2852 C CD1 . LEU   A 1 376 ? -13.945 18.255 13.555  1.00 33.01  ? 179  LEU   A CD1 1 
ATOM   2853 C CD2 . LEU   A 1 376 ? -14.016 20.032 15.399  1.00 33.70  ? 179  LEU   A CD2 1 
ATOM   2854 N N   . GLU   A 1 377 ? -18.580 18.250 14.539  1.00 37.03  ? 180  GLU   A N   1 
ATOM   2855 C CA  . GLU   A 1 377 ? -19.259 17.297 15.407  1.00 39.10  ? 180  GLU   A CA  1 
ATOM   2856 C C   . GLU   A 1 377 ? -19.718 16.079 14.611  1.00 36.24  ? 180  GLU   A C   1 
ATOM   2857 O O   . GLU   A 1 377 ? -19.446 14.941 14.995  1.00 36.46  ? 180  GLU   A O   1 
ATOM   2858 C CB  . GLU   A 1 377 ? -20.440 17.967 16.103  1.00 44.12  ? 180  GLU   A CB  1 
ATOM   2859 C CG  . GLU   A 1 377 ? -21.037 17.149 17.252  1.00 52.57  ? 180  GLU   A CG  1 
ATOM   2860 C CD  . GLU   A 1 377 ? -20.095 17.085 18.454  1.00 58.60  ? 180  GLU   A CD  1 
ATOM   2861 O OE1 . GLU   A 1 377 ? -19.772 15.953 18.915  1.00 59.81  ? 180  GLU   A OE1 1 
ATOM   2862 O OE2 . GLU   A 1 377 ? -19.671 18.162 18.934  1.00 60.02  ? 180  GLU   A OE2 1 
ATOM   2863 N N   . ILE   A 1 378 ? -20.395 16.312 13.483  1.00 34.49  ? 181  ILE   A N   1 
ATOM   2864 C CA  . ILE   A 1 378 ? -20.886 15.229 12.661  1.00 32.87  ? 181  ILE   A CA  1 
ATOM   2865 C C   . ILE   A 1 378 ? -19.716 14.425 12.081  1.00 33.60  ? 181  ILE   A C   1 
ATOM   2866 O O   . ILE   A 1 378 ? -19.677 13.190 12.178  1.00 31.33  ? 181  ILE   A O   1 
ATOM   2867 C CB  . ILE   A 1 378 ? -21.789 15.761 11.541  1.00 32.87  ? 181  ILE   A CB  1 
ATOM   2868 C CG1 . ILE   A 1 378 ? -22.982 16.555 12.124  1.00 30.48  ? 181  ILE   A CG1 1 
ATOM   2869 C CG2 . ILE   A 1 378 ? -22.303 14.602 10.695  1.00 33.07  ? 181  ILE   A CG2 1 
ATOM   2870 C CD1 . ILE   A 1 378 ? -23.540 17.605 11.121  1.00 26.76  ? 181  ILE   A CD1 1 
ATOM   2871 N N   . ILE   A 1 379 ? -18.756 15.121 11.459  1.00 32.13  ? 182  ILE   A N   1 
ATOM   2872 C CA  . ILE   A 1 379 ? -17.731 14.405 10.706  1.00 32.24  ? 182  ILE   A CA  1 
ATOM   2873 C C   . ILE   A 1 379 ? -16.837 13.626 11.655  1.00 32.57  ? 182  ILE   A C   1 
ATOM   2874 O O   . ILE   A 1 379 ? -16.417 12.489 11.348  1.00 33.80  ? 182  ILE   A O   1 
ATOM   2875 C CB  . ILE   A 1 379 ? -16.926 15.396 9.846   1.00 31.20  ? 182  ILE   A CB  1 
ATOM   2876 C CG1 . ILE   A 1 379 ? -17.823 15.916 8.712   1.00 32.88  ? 182  ILE   A CG1 1 
ATOM   2877 C CG2 . ILE   A 1 379 ? -15.659 14.780 9.293   1.00 27.41  ? 182  ILE   A CG2 1 
ATOM   2878 C CD1 . ILE   A 1 379 ? -17.272 17.177 8.017   1.00 34.46  ? 182  ILE   A CD1 1 
ATOM   2879 N N   . SER   A 1 380 ? -16.506 14.199 12.813  1.00 30.13  ? 183  SER   A N   1 
ATOM   2880 C CA  . SER   A 1 380 ? -15.673 13.500 13.753  1.00 32.26  ? 183  SER   A CA  1 
ATOM   2881 C C   . SER   A 1 380 ? -16.379 12.246 14.310  1.00 33.80  ? 183  SER   A C   1 
ATOM   2882 O O   . SER   A 1 380 ? -15.742 11.208 14.431  1.00 31.31  ? 183  SER   A O   1 
ATOM   2883 C CB  . SER   A 1 380 ? -15.176 14.432 14.838  1.00 34.48  ? 183  SER   A CB  1 
ATOM   2884 O OG  . SER   A 1 380 ? -14.924 13.733 16.050  1.00 35.94  ? 183  SER   A OG  1 
ATOM   2885 N N   . ARG   A 1 381 ? -17.640 12.409 14.697  1.00 34.21  ? 184  ARG   A N   1 
ATOM   2886 C CA  . ARG   A 1 381 ? -18.339 11.221 15.233  1.00 34.11  ? 184  ARG   A CA  1 
ATOM   2887 C C   . ARG   A 1 381 ? -18.420 10.121 14.189  1.00 32.19  ? 184  ARG   A C   1 
ATOM   2888 O O   . ARG   A 1 381 ? -18.169 8.951  14.511  1.00 35.75  ? 184  ARG   A O   1 
ATOM   2889 C CB  . ARG   A 1 381 ? -19.744 11.568 15.734  1.00 34.77  ? 184  ARG   A CB  1 
ATOM   2890 C CG  . ARG   A 1 381 ? -19.751 12.110 17.147  1.00 38.33  ? 184  ARG   A CG  1 
ATOM   2891 C CD  . ARG   A 1 381 ? -21.074 12.833 17.423  1.00 43.39  ? 184  ARG   A CD  1 
ATOM   2892 N NE  . ARG   A 1 381 ? -21.046 13.558 18.699  1.00 47.01  ? 184  ARG   A NE  1 
ATOM   2893 C CZ  . ARG   A 1 381 ? -21.559 13.078 19.834  1.00 48.62  ? 184  ARG   A CZ  1 
ATOM   2894 N NH1 . ARG   A 1 381 ? -22.124 11.866 19.852  1.00 51.72  ? 184  ARG   A NH1 1 
ATOM   2895 N NH2 . ARG   A 1 381 ? -21.477 13.782 20.949  1.00 46.66  ? 184  ARG   A NH2 1 
ATOM   2896 N N   . TYR   A 1 382 ? -18.682 10.471 12.923  1.00 28.05  ? 185  TYR   A N   1 
ATOM   2897 C CA  . TYR   A 1 382 ? -18.797 9.445  11.899  1.00 31.78  ? 185  TYR   A CA  1 
ATOM   2898 C C   . TYR   A 1 382 ? -17.452 8.742  11.675  1.00 33.51  ? 185  TYR   A C   1 
ATOM   2899 O O   . TYR   A 1 382 ? -17.390 7.517  11.632  1.00 32.40  ? 185  TYR   A O   1 
ATOM   2900 C CB  . TYR   A 1 382 ? -19.342 10.026 10.577  1.00 31.27  ? 185  TYR   A CB  1 
ATOM   2901 C CG  . TYR   A 1 382 ? -19.589 8.970  9.507   1.00 31.00  ? 185  TYR   A CG  1 
ATOM   2902 C CD1 . TYR   A 1 382 ? -20.454 7.880  9.757   1.00 33.37  ? 185  TYR   A CD1 1 
ATOM   2903 C CD2 . TYR   A 1 382 ? -18.943 9.026  8.284   1.00 29.45  ? 185  TYR   A CD2 1 
ATOM   2904 C CE1 . TYR   A 1 382 ? -20.690 6.895  8.790   1.00 31.90  ? 185  TYR   A CE1 1 
ATOM   2905 C CE2 . TYR   A 1 382 ? -19.146 8.099  7.310   1.00 30.17  ? 185  TYR   A CE2 1 
ATOM   2906 C CZ  . TYR   A 1 382 ? -20.029 7.008  7.559   1.00 32.71  ? 185  TYR   A CZ  1 
ATOM   2907 O OH  . TYR   A 1 382 ? -20.215 6.086  6.599   1.00 34.32  ? 185  TYR   A OH  1 
ATOM   2908 N N   . LEU   A 1 383 ? -16.363 9.520  11.553  1.00 33.19  ? 186  LEU   A N   1 
ATOM   2909 C CA  . LEU   A 1 383 ? -15.064 8.916  11.324  1.00 32.39  ? 186  LEU   A CA  1 
ATOM   2910 C C   . LEU   A 1 383 ? -14.689 7.952  12.458  1.00 33.05  ? 186  LEU   A C   1 
ATOM   2911 O O   . LEU   A 1 383 ? -14.119 6.900  12.198  1.00 29.66  ? 186  LEU   A O   1 
ATOM   2912 C CB  . LEU   A 1 383 ? -13.965 9.970  11.173  1.00 27.87  ? 186  LEU   A CB  1 
ATOM   2913 C CG  . LEU   A 1 383 ? -13.620 10.310 9.678   1.00 27.85  ? 186  LEU   A CG  1 
ATOM   2914 C CD1 . LEU   A 1 383 ? -14.859 10.679 8.855   1.00 24.53  ? 186  LEU   A CD1 1 
ATOM   2915 C CD2 . LEU   A 1 383 ? -12.582 11.467 9.604   1.00 26.68  ? 186  LEU   A CD2 1 
ATOM   2916 N N   . ARG   A 1 384 ? -14.933 8.356  13.719  1.00 31.24  ? 187  ARG   A N   1 
ATOM   2917 C CA  . ARG   A 1 384 ? -14.489 7.595  14.869  1.00 31.34  ? 187  ARG   A CA  1 
ATOM   2918 C C   . ARG   A 1 384 ? -15.346 6.345  15.091  1.00 31.64  ? 187  ARG   A C   1 
ATOM   2919 O O   . ARG   A 1 384 ? -14.810 5.303  15.491  1.00 33.29  ? 187  ARG   A O   1 
ATOM   2920 C CB  . ARG   A 1 384 ? -14.493 8.473  16.119  1.00 30.15  ? 187  ARG   A CB  1 
ATOM   2921 C CG  . ARG   A 1 384 ? -13.569 9.687  15.988  1.00 32.54  ? 187  ARG   A CG  1 
ATOM   2922 C CD  . ARG   A 1 384 ? -13.438 10.452 17.319  1.00 35.53  ? 187  ARG   A CD  1 
ATOM   2923 N NE  . ARG   A 1 384 ? -14.590 11.348 17.550  1.00 39.70  ? 187  ARG   A NE  1 
ATOM   2924 C CZ  . ARG   A 1 384 ? -15.562 11.086 18.428  1.00 42.08  ? 187  ARG   A CZ  1 
ATOM   2925 N NH1 . ARG   A 1 384 ? -15.537 9.961  19.144  1.00 44.03  ? 187  ARG   A NH1 1 
ATOM   2926 N NH2 . ARG   A 1 384 ? -16.557 11.936 18.600  1.00 42.07  ? 187  ARG   A NH2 1 
ATOM   2927 N N   . GLU   A 1 385 ? -16.655 6.440  14.888  1.00 29.25  ? 188  GLU   A N   1 
ATOM   2928 C CA  . GLU   A 1 385 ? -17.468 5.245  15.039  1.00 32.07  ? 188  GLU   A CA  1 
ATOM   2929 C C   . GLU   A 1 385 ? -17.194 4.250  13.906  1.00 32.76  ? 188  GLU   A C   1 
ATOM   2930 O O   . GLU   A 1 385 ? -17.215 3.012  14.124  1.00 34.04  ? 188  GLU   A O   1 
ATOM   2931 C CB  . GLU   A 1 385 ? -18.945 5.608  15.137  1.00 31.37  ? 188  GLU   A CB  1 
ATOM   2932 C CG  . GLU   A 1 385 ? -19.572 6.053  13.846  1.00 33.21  ? 188  GLU   A CG  1 
ATOM   2933 C CD  . GLU   A 1 385 ? -21.063 6.436  13.998  1.00 34.38  ? 188  GLU   A CD  1 
ATOM   2934 O OE1 . GLU   A 1 385 ? -21.473 6.881  15.096  1.00 34.71  ? 188  GLU   A OE1 1 
ATOM   2935 O OE2 . GLU   A 1 385 ? -21.813 6.278  13.012  1.00 35.94  ? 188  GLU   A OE2 1 
ATOM   2936 N N   . GLN   A 1 386 ? -16.864 4.769  12.722  1.00 31.11  ? 189  GLN   A N   1 
ATOM   2937 C CA  . GLN   A 1 386 ? -16.496 3.917  11.629  1.00 33.92  ? 189  GLN   A CA  1 
ATOM   2938 C C   . GLN   A 1 386 ? -15.173 3.200  11.933  1.00 37.71  ? 189  GLN   A C   1 
ATOM   2939 O O   . GLN   A 1 386 ? -15.031 1.981  11.685  1.00 36.50  ? 189  GLN   A O   1 
ATOM   2940 C CB  . GLN   A 1 386 ? -16.407 4.736  10.347  1.00 31.55  ? 189  GLN   A CB  1 
ATOM   2941 C CG  . GLN   A 1 386 ? -17.778 5.146  9.803   1.00 31.80  ? 189  GLN   A CG  1 
ATOM   2942 C CD  . GLN   A 1 386 ? -18.402 4.082  8.947   1.00 35.69  ? 189  GLN   A CD  1 
ATOM   2943 O OE1 . GLN   A 1 386 ? -17.753 3.552  8.004   1.00 35.86  ? 189  GLN   A OE1 1 
ATOM   2944 N NE2 . GLN   A 1 386 ? -19.661 3.700  9.269   1.00 37.16  ? 189  GLN   A NE2 1 
ATOM   2945 N N   . ALA   A 1 387 ? -14.184 3.948  12.442  1.00 37.39  ? 190  ALA   A N   1 
ATOM   2946 C CA  . ALA   A 1 387 ? -12.879 3.348  12.720  1.00 39.11  ? 190  ALA   A CA  1 
ATOM   2947 C C   . ALA   A 1 387 ? -12.938 2.351  13.877  1.00 40.78  ? 190  ALA   A C   1 
ATOM   2948 O O   . ALA   A 1 387 ? -12.281 1.292  13.835  1.00 40.91  ? 190  ALA   A O   1 
ATOM   2949 C CB  . ALA   A 1 387 ? -11.855 4.453  13.000  1.00 36.26  ? 190  ALA   A CB  1 
ATOM   2950 N N   . THR   A 1 388 ? -13.672 2.688  14.950  1.00 38.87  ? 191  THR   A N   1 
ATOM   2951 C CA  . THR   A 1 388 ? -13.582 1.859  16.148  1.00 39.42  ? 191  THR   A CA  1 
ATOM   2952 C C   . THR   A 1 388 ? -14.666 0.785  16.229  1.00 39.00  ? 191  THR   A C   1 
ATOM   2953 O O   . THR   A 1 388 ? -14.492 -0.159 16.996  1.00 40.47  ? 191  THR   A O   1 
ATOM   2954 C CB  . THR   A 1 388 ? -13.654 2.727  17.425  1.00 36.55  ? 191  THR   A CB  1 
ATOM   2955 O OG1 . THR   A 1 388 ? -14.902 3.457  17.464  1.00 37.47  ? 191  THR   A OG1 1 
ATOM   2956 C CG2 . THR   A 1 388 ? -12.474 3.656  17.511  1.00 31.62  ? 191  THR   A CG2 1 
ATOM   2957 N N   . GLY   A 1 389 ? -15.779 0.944  15.510  1.00 36.85  ? 192  GLY   A N   1 
ATOM   2958 C CA  . GLY   A 1 389 ? -16.928 0.077  15.608  1.00 37.63  ? 192  GLY   A CA  1 
ATOM   2959 C C   . GLY   A 1 389 ? -17.967 0.482  16.631  1.00 41.88  ? 192  GLY   A C   1 
ATOM   2960 O O   . GLY   A 1 389 ? -19.018 -0.167 16.712  1.00 42.95  ? 192  GLY   A O   1 
ATOM   2961 N N   . ALA   A 1 390 ? -17.725 1.539  17.424  1.00 41.14  ? 193  ALA   A N   1 
ATOM   2962 C CA  . ALA   A 1 390 ? -18.603 1.913  18.525  1.00 37.37  ? 193  ALA   A CA  1 
ATOM   2963 C C   . ALA   A 1 390 ? -18.840 3.425  18.463  1.00 37.39  ? 193  ALA   A C   1 
ATOM   2964 O O   . ALA   A 1 390 ? -17.961 4.182  18.049  1.00 34.26  ? 193  ALA   A O   1 
ATOM   2965 C CB  . ALA   A 1 390 ? -18.017 1.529  19.891  1.00 33.34  ? 193  ALA   A CB  1 
ATOM   2966 N N   . ALA   A 1 391 ? -20.036 3.842  18.882  1.00 36.97  ? 194  ALA   A N   1 
ATOM   2967 C CA  . ALA   A 1 391 ? -20.466 5.215  18.768  1.00 36.81  ? 194  ALA   A CA  1 
ATOM   2968 C C   . ALA   A 1 391 ? -20.014 6.004  19.982  1.00 39.82  ? 194  ALA   A C   1 
ATOM   2969 O O   . ALA   A 1 391 ? -19.628 5.441  21.017  1.00 41.74  ? 194  ALA   A O   1 
ATOM   2970 C CB  . ALA   A 1 391 ? -21.989 5.306  18.598  1.00 33.83  ? 194  ALA   A CB  1 
ATOM   2971 N N   . ASP   A 1 392 ? -20.087 7.318  19.852  1.00 37.61  ? 195  ASP   A N   1 
ATOM   2972 C CA  . ASP   A 1 392 ? -19.765 8.220  20.945  1.00 35.93  ? 195  ASP   A CA  1 
ATOM   2973 C C   . ASP   A 1 392 ? -20.972 8.359  21.862  1.00 37.02  ? 195  ASP   A C   1 
ATOM   2974 O O   . ASP   A 1 392 ? -22.072 8.695  21.416  1.00 39.40  ? 195  ASP   A O   1 
ATOM   2975 C CB  . ASP   A 1 392 ? -19.355 9.570  20.352  1.00 38.68  ? 195  ASP   A CB  1 
ATOM   2976 C CG  . ASP   A 1 392 ? -18.684 10.493 21.383  1.00 41.92  ? 195  ASP   A CG  1 
ATOM   2977 O OD1 . ASP   A 1 392 ? -19.008 10.403 22.630  1.00 40.72  ? 195  ASP   A OD1 1 
ATOM   2978 O OD2 . ASP   A 1 392 ? -17.845 11.335 20.910  1.00 43.36  ? 195  ASP   A OD2 1 
ATOM   2979 N N   . THR   A 1 393 ? -20.786 8.096  23.142  1.00 42.62  ? 196  THR   A N   1 
ATOM   2980 C CA  . THR   A 1 393 ? -21.916 8.134  24.062  1.00 49.22  ? 196  THR   A CA  1 
ATOM   2981 C C   . THR   A 1 393 ? -22.248 9.540  24.533  1.00 53.31  ? 196  THR   A C   1 
ATOM   2982 O O   . THR   A 1 393 ? -23.187 9.711  25.323  1.00 57.81  ? 196  THR   A O   1 
ATOM   2983 C CB  . THR   A 1 393 ? -21.639 7.241  25.272  1.00 52.53  ? 196  THR   A CB  1 
ATOM   2984 O OG1 . THR   A 1 393 ? -20.353 7.556  25.805  1.00 52.56  ? 196  THR   A OG1 1 
ATOM   2985 C CG2 . THR   A 1 393 ? -21.673 5.765  24.873  1.00 51.26  ? 196  THR   A CG2 1 
ATOM   2986 N N   . ALA   A 1 394 ? -21.519 10.544 24.064  1.00 50.96  ? 197  ALA   A N   1 
ATOM   2987 C CA  . ALA   A 1 394 ? -21.688 11.879 24.617  1.00 53.16  ? 197  ALA   A CA  1 
ATOM   2988 C C   . ALA   A 1 394 ? -22.908 12.558 24.000  1.00 56.41  ? 197  ALA   A C   1 
ATOM   2989 O O   . ALA   A 1 394 ? -23.128 12.453 22.796  1.00 59.41  ? 197  ALA   A O   1 
ATOM   2990 C CB  . ALA   A 1 394 ? -20.434 12.728 24.354  1.00 50.83  ? 197  ALA   A CB  1 
ATOM   2991 N N   . PRO   A 1 395 ? -23.711 13.241 24.797  1.00 56.98  ? 198  PRO   A N   1 
ATOM   2992 C CA  . PRO   A 1 395 ? -24.817 14.033 24.242  1.00 58.80  ? 198  PRO   A CA  1 
ATOM   2993 C C   . PRO   A 1 395 ? -24.368 14.885 23.070  1.00 59.30  ? 198  PRO   A C   1 
ATOM   2994 O O   . PRO   A 1 395 ? -23.229 15.347 23.010  1.00 59.70  ? 198  PRO   A O   1 
ATOM   2995 C CB  . PRO   A 1 395 ? -25.262 14.912 25.430  1.00 60.51  ? 198  PRO   A CB  1 
ATOM   2996 C CG  . PRO   A 1 395 ? -24.916 14.084 26.644  1.00 62.31  ? 198  PRO   A CG  1 
ATOM   2997 C CD  . PRO   A 1 395 ? -23.680 13.253 26.267  1.00 59.71  ? 198  PRO   A CD  1 
ATOM   2998 N N   . MET   A 1 396 ? -25.299 15.136 22.153  1.00 62.51  ? 199  MET   A N   1 
ATOM   2999 C CA  . MET   A 1 396 ? -24.984 15.994 21.007  1.00 64.29  ? 199  MET   A CA  1 
ATOM   3000 C C   . MET   A 1 396 ? -24.986 17.474 21.387  1.00 66.25  ? 199  MET   A C   1 
ATOM   3001 O O   . MET   A 1 396 ? -24.124 18.232 20.940  1.00 64.14  ? 199  MET   A O   1 
ATOM   3002 C CB  . MET   A 1 396 ? -25.973 15.732 19.869  1.00 65.20  ? 199  MET   A CB  1 
ATOM   3003 C CG  . MET   A 1 396 ? -25.813 14.374 19.201  1.00 65.71  ? 199  MET   A CG  1 
ATOM   3004 S SD  . MET   A 1 396 ? -24.610 14.408 17.822  1.00 65.55  ? 199  MET   A SD  1 
ATOM   3005 C CE  . MET   A 1 396 ? -24.844 12.743 17.178  1.00 62.78  ? 199  MET   A CE  1 
ATOM   3006 N N   . GLY   A 1 397 ? -25.946 17.898 22.197  1.00 71.95  ? 200  GLY   A N   1 
ATOM   3007 C CA  . GLY   A 1 397 ? -25.973 19.276 22.659  1.00 76.14  ? 200  GLY   A CA  1 
ATOM   3008 C C   . GLY   A 1 397 ? -26.730 20.226 21.768  1.00 77.35  ? 200  GLY   A C   1 
ATOM   3009 O O   . GLY   A 1 397 ? -27.764 19.855 21.209  1.00 77.44  ? 200  GLY   A O   1 
ATOM   3010 N N   . ALA   A 1 398 ? -26.212 21.453 21.632  1.00 78.94  ? 201  ALA   A N   1 
ATOM   3011 C CA  . ALA   A 1 398 ? -26.914 22.527 20.931  1.00 78.99  ? 201  ALA   A CA  1 
ATOM   3012 C C   . ALA   A 1 398 ? -27.180 22.153 19.480  1.00 76.12  ? 201  ALA   A C   1 
ATOM   3013 O O   . ALA   A 1 398 ? -26.276 21.691 18.763  1.00 73.48  ? 201  ALA   A O   1 
ATOM   3014 C CB  . ALA   A 1 398 ? -26.093 23.814 20.991  1.00 80.16  ? 201  ALA   A CB  1 
ATOM   3015 N N   . SER   A 1 399 ? -28.421 22.375 19.030  1.00 74.84  ? 202  SER   A N   1 
ATOM   3016 C CA  . SER   A 1 399 ? -28.866 21.903 17.713  1.00 70.77  ? 202  SER   A CA  1 
ATOM   3017 C C   . SER   A 1 399 ? -28.663 20.380 17.572  1.00 66.59  ? 202  SER   A C   1 
ATOM   3018 O O   . SER   A 1 399 ? -28.381 19.870 16.493  1.00 62.79  ? 202  SER   A O   1 
ATOM   3019 C CB  . SER   A 1 399 ? -28.148 22.660 16.589  1.00 68.45  ? 202  SER   A CB  1 
ATOM   3020 O OG  . SER   A 1 399 ? -28.181 24.075 16.819  1.00 69.04  ? 202  SER   A OG  1 
ATOM   3021 N N   . GLY   A 1 400 ? -28.834 19.680 18.697  1.00 66.09  ? 203  GLY   A N   1 
ATOM   3022 C CA  . GLY   A 1 400 ? -28.543 18.270 18.727  1.00 63.50  ? 203  GLY   A CA  1 
ATOM   3023 C C   . GLY   A 1 400 ? -29.500 17.445 17.886  1.00 63.51  ? 203  GLY   A C   1 
ATOM   3024 O O   . GLY   A 1 400 ? -29.182 16.332 17.470  1.00 62.41  ? 203  GLY   A O   1 
ATOM   3025 N N   . ALA   A 1 401 ? -30.718 17.965 17.646  1.00 62.85  ? 204  ALA   A N   1 
ATOM   3026 C CA  . ALA   A 1 401 ? -31.622 17.251 16.738  1.00 60.80  ? 204  ALA   A CA  1 
ATOM   3027 C C   . ALA   A 1 401 ? -31.032 17.195 15.338  1.00 55.94  ? 204  ALA   A C   1 
ATOM   3028 O O   . ALA   A 1 401 ? -31.055 16.140 14.686  1.00 55.51  ? 204  ALA   A O   1 
ATOM   3029 C CB  . ALA   A 1 401 ? -33.007 17.919 16.731  1.00 60.97  ? 204  ALA   A CB  1 
ATOM   3030 N N   . THR   A 1 402 ? -30.492 18.315 14.869  1.00 55.63  ? 205  THR   A N   1 
ATOM   3031 C CA  . THR   A 1 402 ? -29.892 18.358 13.541  1.00 55.59  ? 205  THR   A CA  1 
ATOM   3032 C C   . THR   A 1 402 ? -28.707 17.402 13.451  1.00 52.61  ? 205  THR   A C   1 
ATOM   3033 O O   . THR   A 1 402 ? -28.642 16.544 12.553  1.00 51.82  ? 205  THR   A O   1 
ATOM   3034 C CB  . THR   A 1 402 ? -29.448 19.781 13.209  1.00 55.18  ? 205  THR   A CB  1 
ATOM   3035 O OG1 . THR   A 1 402 ? -30.590 20.642 13.249  1.00 60.27  ? 205  THR   A OG1 1 
ATOM   3036 C CG2 . THR   A 1 402 ? -28.819 19.831 11.839  1.00 52.24  ? 205  THR   A CG2 1 
ATOM   3037 N N   . SER   A 1 403 ? -27.757 17.539 14.383  1.00 51.02  ? 206  SER   A N   1 
ATOM   3038 C CA  . SER   A 1 403 ? -26.566 16.694 14.366  1.00 49.07  ? 206  SER   A CA  1 
ATOM   3039 C C   . SER   A 1 403 ? -26.935 15.210 14.421  1.00 48.38  ? 206  SER   A C   1 
ATOM   3040 O O   . SER   A 1 403 ? -26.427 14.405 13.632  1.00 46.57  ? 206  SER   A O   1 
ATOM   3041 C CB  . SER   A 1 403 ? -25.656 17.071 15.523  1.00 50.94  ? 206  SER   A CB  1 
ATOM   3042 O OG  . SER   A 1 403 ? -25.061 18.347 15.270  1.00 53.38  ? 206  SER   A OG  1 
ATOM   3043 N N   . ARG   A 1 404 ? -27.839 14.836 15.333  1.00 49.47  ? 207  ARG   A N   1 
ATOM   3044 C CA  . ARG   A 1 404 ? -28.210 13.430 15.447  1.00 51.58  ? 207  ARG   A CA  1 
ATOM   3045 C C   . ARG   A 1 404 ? -28.772 12.898 14.131  1.00 51.58  ? 207  ARG   A C   1 
ATOM   3046 O O   . ARG   A 1 404 ? -28.428 11.779 13.695  1.00 49.29  ? 207  ARG   A O   1 
ATOM   3047 C CB  . ARG   A 1 404 ? -29.213 13.231 16.579  1.00 54.88  ? 207  ARG   A CB  1 
ATOM   3048 C CG  . ARG   A 1 404 ? -29.881 11.866 16.539  1.00 57.84  ? 207  ARG   A CG  1 
ATOM   3049 C CD  . ARG   A 1 404 ? -30.673 11.575 17.815  1.00 62.79  ? 207  ARG   A CD  1 
ATOM   3050 N NE  . ARG   A 1 404 ? -31.578 12.665 18.181  1.00 65.73  ? 207  ARG   A NE  1 
ATOM   3051 C CZ  . ARG   A 1 404 ? -32.786 12.854 17.641  1.00 68.22  ? 207  ARG   A CZ  1 
ATOM   3052 N NH1 . ARG   A 1 404 ? -33.550 13.868 18.052  1.00 68.71  ? 207  ARG   A NH1 1 
ATOM   3053 N NH2 . ARG   A 1 404 ? -33.234 12.042 16.687  1.00 69.48  ? 207  ARG   A NH2 1 
ATOM   3054 N N   . LYS   A 1 405 ? -29.632 13.665 13.456  1.00 52.99  ? 208  LYS   A N   1 
ATOM   3055 C CA  . LYS   A 1 405 ? -30.234 13.157 12.235  1.00 53.35  ? 208  LYS   A CA  1 
ATOM   3056 C C   . LYS   A 1 405 ? -29.281 13.301 11.048  1.00 47.74  ? 208  LYS   A C   1 
ATOM   3057 O O   . LYS   A 1 405 ? -29.341 12.514 10.128  1.00 48.62  ? 208  LYS   A O   1 
ATOM   3058 C CB  . LYS   A 1 405 ? -31.594 13.802 11.997  1.00 59.18  ? 208  LYS   A CB  1 
ATOM   3059 C CG  . LYS   A 1 405 ? -32.461 13.767 13.255  1.00 66.17  ? 208  LYS   A CG  1 
ATOM   3060 C CD  . LYS   A 1 405 ? -33.327 15.022 13.373  1.00 69.27  ? 208  LYS   A CD  1 
ATOM   3061 C CE  . LYS   A 1 405 ? -34.769 14.726 12.967  1.00 73.34  ? 208  LYS   A CE  1 
ATOM   3062 N NZ  . LYS   A 1 405 ? -35.497 13.866 13.969  1.00 75.81  ? 208  LYS   A NZ  1 
ATOM   3063 N N   . ALA   A 1 406 ? -28.449 14.299 11.059  1.00 43.84  ? 209  ALA   A N   1 
ATOM   3064 C CA  . ALA   A 1 406 ? -27.384 14.355 10.050  1.00 39.66  ? 209  ALA   A CA  1 
ATOM   3065 C C   . ALA   A 1 406 ? -26.525 13.105 10.134  1.00 39.10  ? 209  ALA   A C   1 
ATOM   3066 O O   . ALA   A 1 406 ? -26.201 12.493 9.106   1.00 36.89  ? 209  ALA   A O   1 
ATOM   3067 C CB  . ALA   A 1 406 ? -26.503 15.618 10.223  1.00 35.86  ? 209  ALA   A CB  1 
ATOM   3068 N N   . LEU   A 1 407 ? -26.097 12.743 11.356  1.00 39.17  ? 210  LEU   A N   1 
ATOM   3069 C CA  . LEU   A 1 407 ? -25.256 11.550 11.517  1.00 40.79  ? 210  LEU   A CA  1 
ATOM   3070 C C   . LEU   A 1 407 ? -26.007 10.281 11.097  1.00 41.43  ? 210  LEU   A C   1 
ATOM   3071 O O   . LEU   A 1 407 ? -25.441 9.394  10.421  1.00 41.26  ? 210  LEU   A O   1 
ATOM   3072 C CB  . LEU   A 1 407 ? -24.783 11.425 12.971  1.00 40.28  ? 210  LEU   A CB  1 
ATOM   3073 C CG  . LEU   A 1 407 ? -23.908 10.213 13.276  1.00 38.86  ? 210  LEU   A CG  1 
ATOM   3074 C CD1 . LEU   A 1 407 ? -22.621 10.241 12.451  1.00 32.74  ? 210  LEU   A CD1 1 
ATOM   3075 C CD2 . LEU   A 1 407 ? -23.568 10.137 14.774  1.00 39.36  ? 210  LEU   A CD2 1 
ATOM   3076 N N   . GLU   A 1 408 ? -27.285 10.181 11.462  1.00 42.06  ? 211  GLU   A N   1 
ATOM   3077 C CA  . GLU   A 1 408 ? -28.063 9.019  11.050  1.00 46.26  ? 211  GLU   A CA  1 
ATOM   3078 C C   . GLU   A 1 408 ? -28.189 8.980  9.524   1.00 45.64  ? 211  GLU   A C   1 
ATOM   3079 O O   . GLU   A 1 408 ? -27.986 7.952  8.888   1.00 44.71  ? 211  GLU   A O   1 
ATOM   3080 C CB  . GLU   A 1 408 ? -29.427 9.028  11.728  1.00 52.09  ? 211  GLU   A CB  1 
ATOM   3081 C CG  . GLU   A 1 408 ? -29.345 8.655  13.192  1.00 60.17  ? 211  GLU   A CG  1 
ATOM   3082 C CD  . GLU   A 1 408 ? -30.660 8.851  13.950  1.00 68.85  ? 211  GLU   A CD  1 
ATOM   3083 O OE1 . GLU   A 1 408 ? -30.837 8.183  15.003  1.00 71.24  ? 211  GLU   A OE1 1 
ATOM   3084 O OE2 . GLU   A 1 408 ? -31.509 9.684  13.507  1.00 72.53  ? 211  GLU   A OE2 1 
ATOM   3085 N N   . THR   A 1 409 ? -28.510 10.122 8.914   1.00 45.73  ? 212  THR   A N   1 
ATOM   3086 C CA  . THR   A 1 409 ? -28.508 10.198 7.450   1.00 43.61  ? 212  THR   A CA  1 
ATOM   3087 C C   . THR   A 1 409 ? -27.163 9.757  6.896   1.00 40.39  ? 212  THR   A C   1 
ATOM   3088 O O   . THR   A 1 409 ? -27.092 8.945  5.970   1.00 40.97  ? 212  THR   A O   1 
ATOM   3089 C CB  . THR   A 1 409 ? -28.831 11.631 6.995   1.00 43.46  ? 212  THR   A CB  1 
ATOM   3090 O OG1 . THR   A 1 409 ? -30.208 11.925 7.299   1.00 48.02  ? 212  THR   A OG1 1 
ATOM   3091 C CG2 . THR   A 1 409 ? -28.622 11.795 5.502   1.00 41.00  ? 212  THR   A CG2 1 
ATOM   3092 N N   . LEU   A 1 410 ? -26.069 10.297 7.458   1.00 39.51  ? 213  LEU   A N   1 
ATOM   3093 C CA  . LEU   A 1 410 ? -24.730 9.941  6.985   1.00 41.11  ? 213  LEU   A CA  1 
ATOM   3094 C C   . LEU   A 1 410 ? -24.463 8.430  7.114   1.00 43.37  ? 213  LEU   A C   1 
ATOM   3095 O O   . LEU   A 1 410 ? -23.841 7.830  6.241   1.00 44.27  ? 213  LEU   A O   1 
ATOM   3096 C CB  . LEU   A 1 410 ? -23.685 10.720 7.765   1.00 40.49  ? 213  LEU   A CB  1 
ATOM   3097 C CG  . LEU   A 1 410 ? -22.248 10.804 7.286   1.00 37.38  ? 213  LEU   A CG  1 
ATOM   3098 C CD1 . LEU   A 1 410 ? -22.205 11.139 5.815   1.00 38.67  ? 213  LEU   A CD1 1 
ATOM   3099 C CD2 . LEU   A 1 410 ? -21.546 11.895 8.110   1.00 32.55  ? 213  LEU   A CD2 1 
ATOM   3100 N N   . ARG   A 1 411 ? -24.884 7.810  8.216   1.00 42.01  ? 214  ARG   A N   1 
ATOM   3101 C CA  . ARG   A 1 411 ? -24.713 6.364  8.336   1.00 42.59  ? 214  ARG   A CA  1 
ATOM   3102 C C   . ARG   A 1 411 ? -25.365 5.665  7.159   1.00 44.70  ? 214  ARG   A C   1 
ATOM   3103 O O   . ARG   A 1 411 ? -24.761 4.808  6.546   1.00 47.92  ? 214  ARG   A O   1 
ATOM   3104 C CB  . ARG   A 1 411 ? -25.306 5.855  9.655   1.00 40.78  ? 214  ARG   A CB  1 
ATOM   3105 C CG  . ARG   A 1 411 ? -24.450 6.186  10.876  1.00 40.49  ? 214  ARG   A CG  1 
ATOM   3106 C CD  . ARG   A 1 411 ? -25.305 6.156  12.129  1.00 42.02  ? 214  ARG   A CD  1 
ATOM   3107 N NE  . ARG   A 1 411 ? -24.536 6.461  13.341  1.00 42.35  ? 214  ARG   A NE  1 
ATOM   3108 C CZ  . ARG   A 1 411 ? -25.064 6.574  14.555  1.00 41.83  ? 214  ARG   A CZ  1 
ATOM   3109 N NH1 . ARG   A 1 411 ? -26.378 6.451  14.701  1.00 45.10  ? 214  ARG   A NH1 1 
ATOM   3110 N NH2 . ARG   A 1 411 ? -24.289 6.801  15.609  1.00 36.60  ? 214  ARG   A NH2 1 
ATOM   3111 N N   . ARG   A 1 412 ? -26.567 6.047  6.799   1.00 47.01  ? 215  ARG   A N   1 
ATOM   3112 C CA  . ARG   A 1 412 ? -27.251 5.478  5.659   1.00 53.73  ? 215  ARG   A CA  1 
ATOM   3113 C C   . ARG   A 1 412 ? -26.447 5.659  4.359   1.00 54.45  ? 215  ARG   A C   1 
ATOM   3114 O O   . ARG   A 1 412 ? -25.964 4.663  3.777   1.00 55.96  ? 215  ARG   A O   1 
ATOM   3115 C CB  . ARG   A 1 412 ? -28.643 6.109  5.507   1.00 59.29  ? 215  ARG   A CB  1 
ATOM   3116 C CG  . ARG   A 1 412 ? -29.602 5.767  6.638   1.00 62.04  ? 215  ARG   A CG  1 
ATOM   3117 C CD  . ARG   A 1 412 ? -31.061 5.795  6.167   1.00 64.06  ? 215  ARG   A CD  1 
ATOM   3118 N NE  . ARG   A 1 412 ? -31.514 7.154  5.940   1.00 66.04  ? 215  ARG   A NE  1 
ATOM   3119 C CZ  . ARG   A 1 412 ? -31.489 7.773  4.755   1.00 66.02  ? 215  ARG   A CZ  1 
ATOM   3120 N NH1 . ARG   A 1 412 ? -31.047 7.142  3.673   1.00 65.96  ? 215  ARG   A NH1 1 
ATOM   3121 N NH2 . ARG   A 1 412 ? -31.923 9.017  4.661   1.00 64.57  ? 215  ARG   A NH2 1 
ATOM   3122 N N   . VAL   A 1 413 ? -26.282 6.910  3.911   1.00 50.31  ? 216  VAL   A N   1 
ATOM   3123 C CA  . VAL   A 1 413 ? -25.739 7.117  2.581   1.00 48.88  ? 216  VAL   A CA  1 
ATOM   3124 C C   . VAL   A 1 413 ? -24.226 6.941  2.514   1.00 49.18  ? 216  VAL   A C   1 
ATOM   3125 O O   . VAL   A 1 413 ? -23.696 6.668  1.423   1.00 49.26  ? 216  VAL   A O   1 
ATOM   3126 C CB  . VAL   A 1 413 ? -26.140 8.506  2.057   1.00 47.41  ? 216  VAL   A CB  1 
ATOM   3127 C CG1 . VAL   A 1 413 ? -27.603 8.733  2.320   1.00 47.51  ? 216  VAL   A CG1 1 
ATOM   3128 C CG2 . VAL   A 1 413 ? -25.308 9.581  2.739   1.00 45.84  ? 216  VAL   A CG2 1 
ATOM   3129 N N   . GLY   A 1 414 ? -23.512 7.066  3.629   1.00 49.94  ? 217  GLY   A N   1 
ATOM   3130 C CA  . GLY   A 1 414 ? -22.061 6.933  3.647   1.00 51.52  ? 217  GLY   A CA  1 
ATOM   3131 C C   . GLY   A 1 414 ? -21.598 5.467  3.545   1.00 54.22  ? 217  GLY   A C   1 
ATOM   3132 O O   . GLY   A 1 414 ? -20.597 5.167  2.895   1.00 53.78  ? 217  GLY   A O   1 
ATOM   3133 N N   . ASP   A 1 415 ? -22.336 4.566  4.183   1.00 56.02  ? 218  ASP   A N   1 
ATOM   3134 C CA  . ASP   A 1 415 ? -21.920 3.165  4.169   1.00 57.50  ? 218  ASP   A CA  1 
ATOM   3135 C C   . ASP   A 1 415 ? -22.117 2.558  2.794   1.00 57.95  ? 218  ASP   A C   1 
ATOM   3136 O O   . ASP   A 1 415 ? -21.363 1.660  2.383   1.00 59.25  ? 218  ASP   A O   1 
ATOM   3137 C CB  . ASP   A 1 415 ? -22.694 2.374  5.231   1.00 57.54  ? 218  ASP   A CB  1 
ATOM   3138 C CG  . ASP   A 1 415 ? -22.185 2.643  6.640   1.00 59.01  ? 218  ASP   A CG  1 
ATOM   3139 O OD1 . ASP   A 1 415 ? -22.049 3.835  7.017   1.00 55.96  ? 218  ASP   A OD1 1 
ATOM   3140 O OD2 . ASP   A 1 415 ? -21.900 1.662  7.361   1.00 64.47  ? 218  ASP   A OD2 1 
ATOM   3141 N N   . GLY   A 1 416 ? -23.129 3.026  2.070   1.00 55.92  ? 219  GLY   A N   1 
ATOM   3142 C CA  . GLY   A 1 416 ? -23.303 2.573  0.696   1.00 54.42  ? 219  GLY   A CA  1 
ATOM   3143 C C   . GLY   A 1 416 ? -22.207 3.078  -0.233  1.00 49.04  ? 219  GLY   A C   1 
ATOM   3144 O O   . GLY   A 1 416 ? -21.860 2.417  -1.223  1.00 48.91  ? 219  GLY   A O   1 
ATOM   3145 N N   . VAL   A 1 417 ? -21.649 4.257  0.067   1.00 44.98  ? 220  VAL   A N   1 
ATOM   3146 C CA  . VAL   A 1 417 ? -20.584 4.753  -0.793  1.00 43.41  ? 220  VAL   A CA  1 
ATOM   3147 C C   . VAL   A 1 417 ? -19.276 3.994  -0.564  1.00 40.85  ? 220  VAL   A C   1 
ATOM   3148 O O   . VAL   A 1 417 ? -18.556 3.684  -1.515  1.00 39.23  ? 220  VAL   A O   1 
ATOM   3149 C CB  . VAL   A 1 417 ? -20.407 6.252  -0.604  1.00 41.01  ? 220  VAL   A CB  1 
ATOM   3150 C CG1 . VAL   A 1 417 ? -18.988 6.643  -0.982  1.00 37.93  ? 220  VAL   A CG1 1 
ATOM   3151 C CG2 . VAL   A 1 417 ? -21.413 6.988  -1.461  1.00 43.86  ? 220  VAL   A CG2 1 
ATOM   3152 N N   . GLN   A 1 418 ? -18.953 3.681  0.697   1.00 40.43  ? 221  GLN   A N   1 
ATOM   3153 C CA  . GLN   A 1 418 ? -17.712 2.971  0.973   1.00 41.12  ? 221  GLN   A CA  1 
ATOM   3154 C C   . GLN   A 1 418 ? -17.737 1.599  0.372   1.00 45.20  ? 221  GLN   A C   1 
ATOM   3155 O O   . GLN   A 1 418 ? -16.676 1.089  -0.034  1.00 48.10  ? 221  GLN   A O   1 
ATOM   3156 C CB  . GLN   A 1 418 ? -17.474 2.899  2.488   1.00 38.31  ? 221  GLN   A CB  1 
ATOM   3157 C CG  . GLN   A 1 418 ? -17.171 4.298  3.116   1.00 39.27  ? 221  GLN   A CG  1 
ATOM   3158 C CD  . GLN   A 1 418 ? -16.774 4.159  4.585   1.00 37.55  ? 221  GLN   A CD  1 
ATOM   3159 O OE1 . GLN   A 1 418 ? -15.767 3.527  4.907   1.00 35.67  ? 221  GLN   A OE1 1 
ATOM   3160 N NE2 . GLN   A 1 418 ? -17.598 4.733  5.477   1.00 36.08  ? 221  GLN   A NE2 1 
ATOM   3161 N N   . ARG   A 1 419 ? -18.923 0.974  0.310   1.00 47.96  ? 222  ARG   A N   1 
ATOM   3162 C CA  . ARG   A 1 419 ? -19.027 -0.345 -0.323  1.00 51.13  ? 222  ARG   A CA  1 
ATOM   3163 C C   . ARG   A 1 419 ? -18.944 -0.218 -1.832  1.00 45.69  ? 222  ARG   A C   1 
ATOM   3164 O O   . ARG   A 1 419 ? -18.119 -0.860 -2.478  1.00 43.40  ? 222  ARG   A O   1 
ATOM   3165 C CB  . ARG   A 1 419 ? -20.342 -1.025 0.065   1.00 57.39  ? 222  ARG   A CB  1 
ATOM   3166 C CG  . ARG   A 1 419 ? -20.644 -1.113 1.561   1.00 59.81  ? 222  ARG   A CG  1 
ATOM   3167 C CD  . ARG   A 1 419 ? -21.919 -1.957 1.789   1.00 62.86  ? 222  ARG   A CD  1 
ATOM   3168 N NE  . ARG   A 1 419 ? -22.982 -1.606 0.832   1.00 66.27  ? 222  ARG   A NE  1 
ATOM   3169 C CZ  . ARG   A 1 419 ? -23.166 -2.198 -0.357  1.00 67.64  ? 222  ARG   A CZ  1 
ATOM   3170 N NH1 . ARG   A 1 419 ? -24.153 -1.796 -1.170  1.00 67.52  ? 222  ARG   A NH1 1 
ATOM   3171 N NH2 . ARG   A 1 419 ? -22.354 -3.171 -0.737  1.00 68.76  ? 222  ARG   A NH2 1 
ATOM   3172 N N   . ASN   A 1 420 ? -19.811 0.607  -2.412  1.00 45.19  ? 223  ASN   A N   1 
ATOM   3173 C CA  . ASN   A 1 420 ? -19.857 0.682  -3.872  1.00 48.55  ? 223  ASN   A CA  1 
ATOM   3174 C C   . ASN   A 1 420 ? -18.531 1.201  -4.451  1.00 45.65  ? 223  ASN   A C   1 
ATOM   3175 O O   . ASN   A 1 420 ? -18.099 0.766  -5.529  1.00 42.59  ? 223  ASN   A O   1 
ATOM   3176 C CB  . ASN   A 1 420 ? -21.010 1.577  -4.309  1.00 50.37  ? 223  ASN   A CB  1 
ATOM   3177 C CG  . ASN   A 1 420 ? -22.340 0.851  -4.275  1.00 52.35  ? 223  ASN   A CG  1 
ATOM   3178 O OD1 . ASN   A 1 420 ? -22.437 -0.271 -4.742  1.00 55.86  ? 223  ASN   A OD1 1 
ATOM   3179 N ND2 . ASN   A 1 420 ? -23.375 1.505  -3.748  1.00 50.23  ? 223  ASN   A ND2 1 
ATOM   3180 N N   . HIS   A 1 421 ? -17.859 2.128  -3.732  1.00 41.64  ? 224  HIS   A N   1 
ATOM   3181 C CA  . HIS   A 1 421 ? -16.657 2.752  -4.260  1.00 41.96  ? 224  HIS   A CA  1 
ATOM   3182 C C   . HIS   A 1 421 ? -15.415 2.229  -3.563  1.00 42.75  ? 224  HIS   A C   1 
ATOM   3183 O O   . HIS   A 1 421 ? -14.404 2.914  -3.500  1.00 42.08  ? 224  HIS   A O   1 
ATOM   3184 C CB  . HIS   A 1 421 ? -16.753 4.276  -4.132  1.00 41.91  ? 224  HIS   A CB  1 
ATOM   3185 C CG  . HIS   A 1 421 ? -17.613 4.908  -5.174  1.00 43.31  ? 224  HIS   A CG  1 
ATOM   3186 N ND1 . HIS   A 1 421 ? -17.169 5.144  -6.466  1.00 45.89  ? 224  HIS   A ND1 1 
ATOM   3187 C CD2 . HIS   A 1 421 ? -18.905 5.310  -5.130  1.00 42.72  ? 224  HIS   A CD2 1 
ATOM   3188 C CE1 . HIS   A 1 421 ? -18.154 5.684  -7.169  1.00 47.55  ? 224  HIS   A CE1 1 
ATOM   3189 N NE2 . HIS   A 1 421 ? -19.214 5.808  -6.376  1.00 45.79  ? 224  HIS   A NE2 1 
ATOM   3190 N N   . GLU   A 1 422 ? -15.478 1.017  -3.026  1.00 43.63  ? 225  GLU   A N   1 
ATOM   3191 C CA  . GLU   A 1 422 ? -14.305 0.429  -2.366  1.00 48.31  ? 225  GLU   A CA  1 
ATOM   3192 C C   . GLU   A 1 422 ? -13.093 0.328  -3.292  1.00 47.33  ? 225  GLU   A C   1 
ATOM   3193 O O   . GLU   A 1 422 ? -11.958 0.443  -2.824  1.00 47.43  ? 225  GLU   A O   1 
ATOM   3194 C CB  . GLU   A 1 422 ? -14.630 -0.959 -1.807  1.00 54.11  ? 225  GLU   A CB  1 
ATOM   3195 C CG  . GLU   A 1 422 ? -13.426 -1.674 -1.230  1.00 61.12  ? 225  GLU   A CG  1 
ATOM   3196 C CD  . GLU   A 1 422 ? -13.796 -2.991 -0.533  1.00 66.61  ? 225  GLU   A CD  1 
ATOM   3197 O OE1 . GLU   A 1 422 ? -14.468 -2.957 0.518   1.00 66.37  ? 225  GLU   A OE1 1 
ATOM   3198 O OE2 . GLU   A 1 422 ? -13.414 -4.070 -1.041  1.00 71.50  ? 225  GLU   A OE2 1 
ATOM   3199 N N   . THR   A 1 423 ? -13.303 0.134  -4.592  1.00 48.45  ? 226  THR   A N   1 
ATOM   3200 C CA  . THR   A 1 423 ? -12.176 0.032  -5.511  1.00 53.83  ? 226  THR   A CA  1 
ATOM   3201 C C   . THR   A 1 423 ? -11.453 1.371  -5.649  1.00 54.22  ? 226  THR   A C   1 
ATOM   3202 O O   . THR   A 1 423 ? -10.239 1.457  -5.459  1.00 53.52  ? 226  THR   A O   1 
ATOM   3203 C CB  . THR   A 1 423 ? -12.642 -0.470 -6.880  1.00 57.96  ? 226  THR   A CB  1 
ATOM   3204 O OG1 . THR   A 1 423 ? -13.094 -1.834 -6.772  1.00 61.94  ? 226  THR   A OG1 1 
ATOM   3205 C CG2 . THR   A 1 423 ? -11.492 -0.434 -7.900  1.00 58.03  ? 226  THR   A CG2 1 
ATOM   3206 N N   . ALA   A 1 424 ? -12.190 2.432  -5.970  1.00 57.39  ? 227  ALA   A N   1 
ATOM   3207 C CA  . ALA   A 1 424 ? -11.574 3.757  -6.087  1.00 56.70  ? 227  ALA   A CA  1 
ATOM   3208 C C   . ALA   A 1 424 ? -10.984 4.194  -4.754  1.00 54.67  ? 227  ALA   A C   1 
ATOM   3209 O O   . ALA   A 1 424 ? -9.943  4.858  -4.719  1.00 60.94  ? 227  ALA   A O   1 
ATOM   3210 C CB  . ALA   A 1 424 ? -12.581 4.788  -6.601  1.00 57.95  ? 227  ALA   A CB  1 
ATOM   3211 N N   . PHE   A 1 425 ? -11.650 3.859  -3.636  1.00 45.44  ? 228  PHE   A N   1 
ATOM   3212 C CA  . PHE   A 1 425 ? -11.155 4.280  -2.335  1.00 41.55  ? 228  PHE   A CA  1 
ATOM   3213 C C   . PHE   A 1 425 ? -9.835  3.614  -2.008  1.00 44.05  ? 228  PHE   A C   1 
ATOM   3214 O O   . PHE   A 1 425 ? -8.891  4.284  -1.567  1.00 42.63  ? 228  PHE   A O   1 
ATOM   3215 C CB  . PHE   A 1 425 ? -12.188 3.994  -1.248  1.00 38.36  ? 228  PHE   A CB  1 
ATOM   3216 C CG  . PHE   A 1 425 ? -13.272 5.053  -1.151  1.00 39.55  ? 228  PHE   A CG  1 
ATOM   3217 C CD1 . PHE   A 1 425 ? -13.283 6.156  -2.047  1.00 41.68  ? 228  PHE   A CD1 1 
ATOM   3218 C CD2 . PHE   A 1 425 ? -14.257 4.979  -0.194  1.00 39.38  ? 228  PHE   A CD2 1 
ATOM   3219 C CE1 . PHE   A 1 425 ? -14.273 7.128  -1.952  1.00 41.04  ? 228  PHE   A CE1 1 
ATOM   3220 C CE2 . PHE   A 1 425 ? -15.255 5.962  -0.089  1.00 38.44  ? 228  PHE   A CE2 1 
ATOM   3221 C CZ  . PHE   A 1 425 ? -15.263 7.024  -0.989  1.00 37.97  ? 228  PHE   A CZ  1 
ATOM   3222 N N   . GLN   A 1 426 ? -9.746  2.289  -2.235  1.00 44.85  ? 229  GLN   A N   1 
ATOM   3223 C CA  . GLN   A 1 426 ? -8.491  1.584  -2.014  1.00 49.28  ? 229  GLN   A CA  1 
ATOM   3224 C C   . GLN   A 1 426 ? -7.377  2.187  -2.857  1.00 52.55  ? 229  GLN   A C   1 
ATOM   3225 O O   . GLN   A 1 426 ? -6.254  2.370  -2.375  1.00 54.66  ? 229  GLN   A O   1 
ATOM   3226 C CB  . GLN   A 1 426 ? -8.664  0.088  -2.321  1.00 54.41  ? 229  GLN   A CB  1 
ATOM   3227 C CG  . GLN   A 1 426 ? -7.750  -0.831 -1.520  1.00 60.11  ? 229  GLN   A CG  1 
ATOM   3228 C CD  . GLN   A 1 426 ? -7.647  -0.388 -0.056  1.00 63.43  ? 229  GLN   A CD  1 
ATOM   3229 O OE1 . GLN   A 1 426 ? -8.665  -0.205 0.618   1.00 62.46  ? 229  GLN   A OE1 1 
ATOM   3230 N NE2 . GLN   A 1 426 ? -6.413  -0.193 0.437   1.00 65.30  ? 229  GLN   A NE2 1 
ATOM   3231 N N   . GLY   A 1 427 ? -7.666  2.502  -4.125  1.00 53.58  ? 230  GLY   A N   1 
ATOM   3232 C CA  . GLY   A 1 427 ? -6.641  3.065  -4.980  1.00 58.78  ? 230  GLY   A CA  1 
ATOM   3233 C C   . GLY   A 1 427 ? -6.181  4.444  -4.536  1.00 59.81  ? 230  GLY   A C   1 
ATOM   3234 O O   . GLY   A 1 427 ? -4.983  4.730  -4.517  1.00 60.73  ? 230  GLY   A O   1 
ATOM   3235 N N   . MET   A 1 428 ? -7.119  5.313  -4.154  1.00 59.90  ? 231  MET   A N   1 
ATOM   3236 C CA  . MET   A 1 428 ? -6.728  6.617  -3.642  1.00 59.38  ? 231  MET   A CA  1 
ATOM   3237 C C   . MET   A 1 428 ? -5.945  6.482  -2.350  1.00 57.94  ? 231  MET   A C   1 
ATOM   3238 O O   . MET   A 1 428 ? -5.028  7.276  -2.109  1.00 62.48  ? 231  MET   A O   1 
ATOM   3239 C CB  . MET   A 1 428 ? -7.972  7.489  -3.430  1.00 58.55  ? 231  MET   A CB  1 
ATOM   3240 C CG  . MET   A 1 428 ? -7.689  8.857  -2.881  1.00 59.04  ? 231  MET   A CG  1 
ATOM   3241 S SD  . MET   A 1 428 ? -6.797  9.897  -4.069  1.00 63.51  ? 231  MET   A SD  1 
ATOM   3242 C CE  . MET   A 1 428 ? -7.502  11.495 -3.700  1.00 61.60  ? 231  MET   A CE  1 
ATOM   3243 N N   . LEU   A 1 429 ? -6.264  5.494  -1.532  1.00 53.14  ? 232  LEU   A N   1 
ATOM   3244 C CA  . LEU   A 1 429 ? -5.611  5.347  -0.249  1.00 54.54  ? 232  LEU   A CA  1 
ATOM   3245 C C   . LEU   A 1 429 ? -4.180  4.839  -0.377  1.00 62.39  ? 232  LEU   A C   1 
ATOM   3246 O O   . LEU   A 1 429 ? -3.449  4.853  0.621   1.00 65.93  ? 232  LEU   A O   1 
ATOM   3247 C CB  . LEU   A 1 429 ? -6.416  4.408  0.659   1.00 52.17  ? 232  LEU   A CB  1 
ATOM   3248 C CG  . LEU   A 1 429 ? -5.730  3.977  1.956   1.00 53.59  ? 232  LEU   A CG  1 
ATOM   3249 C CD1 . LEU   A 1 429 ? -5.461  5.187  2.848   1.00 53.70  ? 232  LEU   A CD1 1 
ATOM   3250 C CD2 . LEU   A 1 429 ? -6.560  2.954  2.708   1.00 52.09  ? 232  LEU   A CD2 1 
ATOM   3251 N N   . ARG   A 1 430 ? -3.783  4.338  -1.553  1.00 63.59  ? 233  ARG   A N   1 
ATOM   3252 C CA  . ARG   A 1 430 ? -2.413  3.891  -1.788  1.00 63.21  ? 233  ARG   A CA  1 
ATOM   3253 C C   . ARG   A 1 430 ? -1.557  4.989  -2.413  1.00 67.28  ? 233  ARG   A C   1 
ATOM   3254 O O   . ARG   A 1 430 ? -0.421  5.211  -1.981  1.00 69.40  ? 233  ARG   A O   1 
ATOM   3255 C CB  . ARG   A 1 430 ? -2.421  2.655  -2.671  1.00 61.10  ? 233  ARG   A CB  1 
ATOM   3256 N N   . LYS   A 1 431 ? -2.086  5.687  -3.430  1.00 69.54  ? 234  LYS   A N   1 
ATOM   3257 C CA  . LYS   A 1 431 ? -1.365  6.820  -4.014  1.00 74.50  ? 234  LYS   A CA  1 
ATOM   3258 C C   . LYS   A 1 431 ? -0.908  7.769  -2.916  1.00 76.75  ? 234  LYS   A C   1 
ATOM   3259 O O   . LYS   A 1 431 ? 0.271   8.161  -2.855  1.00 80.04  ? 234  LYS   A O   1 
ATOM   3260 C CB  . LYS   A 1 431 ? -2.246  7.547  -5.028  1.00 73.17  ? 234  LYS   A CB  1 
ATOM   3261 N N   . LEU   A 1 432 ? -1.835  8.161  -2.046  1.00 74.42  ? 235  LEU   A N   1 
ATOM   3262 C CA  . LEU   A 1 432 ? -1.482  8.685  -0.734  1.00 77.43  ? 235  LEU   A CA  1 
ATOM   3263 C C   . LEU   A 1 432 ? -1.143  7.504  0.140   1.00 85.62  ? 235  LEU   A C   1 
ATOM   3264 O O   . LEU   A 1 432 ? -1.960  6.582  0.275   1.00 86.77  ? 235  LEU   A O   1 
ATOM   3265 C CB  . LEU   A 1 432 ? -2.653  9.455  -0.112  1.00 69.82  ? 235  LEU   A CB  1 
ATOM   3266 C CG  . LEU   A 1 432 ? -3.505  10.332 -1.029  1.00 67.33  ? 235  LEU   A CG  1 
ATOM   3267 C CD1 . LEU   A 1 432 ? -4.877  10.477 -0.458  1.00 64.96  ? 235  LEU   A CD1 1 
ATOM   3268 C CD2 . LEU   A 1 432 ? -2.854  11.696 -1.204  1.00 68.68  ? 235  LEU   A CD2 1 
ATOM   3269 N N   . ASP   A 1 433 ? 0.000   7.467  0.761   1.00 92.71  ? 236  ASP   A N   1 
ATOM   3270 C CA  . ASP   A 1 433 ? 0.251   6.482  1.782   1.00 97.83  ? 236  ASP   A CA  1 
ATOM   3271 C C   . ASP   A 1 433 ? 0.361   7.161  3.093   1.00 97.20  ? 236  ASP   A C   1 
ATOM   3272 O O   . ASP   A 1 433 ? 1.303   7.947  3.334   1.00 101.24 ? 236  ASP   A O   1 
ATOM   3273 C CB  . ASP   A 1 433 ? 1.416   5.565  1.504   1.00 105.66 ? 236  ASP   A CB  1 
ATOM   3274 C CG  . ASP   A 1 433 ? 2.719   6.271  1.503   1.00 113.97 ? 236  ASP   A CG  1 
ATOM   3275 O OD1 . ASP   A 1 433 ? 3.692   5.736  2.087   1.00 118.00 ? 236  ASP   A OD1 1 
ATOM   3276 O OD2 . ASP   A 1 433 ? 2.805   7.378  0.933   1.00 116.48 ? 236  ASP   A OD2 1 
ATOM   3277 N N   . ILE   A 1 434 ? -0.584  6.936  4.003   1.00 91.88  ? 237  ILE   A N   1 
ATOM   3278 C CA  . ILE   A 1 434 ? -0.775  7.591  5.265   1.00 86.70  ? 237  ILE   A CA  1 
ATOM   3279 C C   . ILE   A 1 434 ? -0.266  6.666  6.353   1.00 86.58  ? 237  ILE   A C   1 
ATOM   3280 O O   . ILE   A 1 434 ? -0.864  5.617  6.612   1.00 84.15  ? 237  ILE   A O   1 
ATOM   3281 C CB  . ILE   A 1 434 ? -2.250  7.964  5.461   1.00 78.85  ? 237  ILE   A CB  1 
ATOM   3282 C CG1 . ILE   A 1 434 ? -2.811  8.564  4.162   1.00 74.68  ? 237  ILE   A CG1 1 
ATOM   3283 C CG2 . ILE   A 1 434 ? -2.380  8.937  6.627   1.00 77.05  ? 237  ILE   A CG2 1 
ATOM   3284 C CD1 . ILE   A 1 434 ? -4.148  9.256  4.320   1.00 69.33  ? 237  ILE   A CD1 1 
ATOM   3285 N N   . LYS   A 1 435 ? 0.842   7.053  6.975   1.00 89.46  ? 238  LYS   A N   1 
ATOM   3286 C CA  . LYS   A 1 435 ? 1.388   6.336  8.109   1.00 90.04  ? 238  LYS   A CA  1 
ATOM   3287 C C   . LYS   A 1 435 ? 1.640   7.219  9.318   1.00 89.65  ? 238  LYS   A C   1 
ATOM   3288 O O   . LYS   A 1 435 ? 1.796   6.676  10.417  1.00 89.81  ? 238  LYS   A O   1 
ATOM   3289 C CB  . LYS   A 1 435 ? 2.699   5.632  7.718   1.00 93.46  ? 238  LYS   A CB  1 
ATOM   3290 N N   . ASN   A 1 436 ? 1.671   8.549  9.166   1.00 88.13  ? 239  ASN   A N   1 
ATOM   3291 C CA  . ASN   A 1 436 ? 2.049   9.456  10.233  1.00 85.69  ? 239  ASN   A CA  1 
ATOM   3292 C C   . ASN   A 1 436 ? 0.952   10.483 10.429  1.00 82.91  ? 239  ASN   A C   1 
ATOM   3293 O O   . ASN   A 1 436 ? 0.116   10.721 9.548   1.00 79.96  ? 239  ASN   A O   1 
ATOM   3294 C CB  . ASN   A 1 436 ? 3.358   10.179 9.934   1.00 87.38  ? 239  ASN   A CB  1 
ATOM   3295 C CG  . ASN   A 1 436 ? 4.508   9.234  9.718   1.00 94.09  ? 239  ASN   A CG  1 
ATOM   3296 O OD1 . ASN   A 1 436 ? 5.038   9.114  8.605   1.00 97.45  ? 239  ASN   A OD1 1 
ATOM   3297 N ND2 . ASN   A 1 436 ? 4.925   8.554  10.787  1.00 97.36  ? 239  ASN   A ND2 1 
ATOM   3298 N N   . GLU   A 1 437 ? 0.984   11.115 11.604  1.00 83.86  ? 240  GLU   A N   1 
ATOM   3299 C CA  . GLU   A 1 437 ? 0.178   12.309 11.813  1.00 81.89  ? 240  GLU   A CA  1 
ATOM   3300 C C   . GLU   A 1 437 ? 0.624   13.443 10.895  1.00 81.62  ? 240  GLU   A C   1 
ATOM   3301 O O   . GLU   A 1 437 ? -0.183  14.307 10.534  1.00 80.40  ? 240  GLU   A O   1 
ATOM   3302 C CB  . GLU   A 1 437 ? 0.257   12.742 13.279  1.00 85.89  ? 240  GLU   A CB  1 
ATOM   3303 C CG  . GLU   A 1 437 ? -0.154  14.196 13.536  1.00 88.11  ? 240  GLU   A CG  1 
ATOM   3304 C CD  . GLU   A 1 437 ? -0.922  14.370 14.838  1.00 88.29  ? 240  GLU   A CD  1 
ATOM   3305 O OE1 . GLU   A 1 437 ? -1.233  13.344 15.491  1.00 88.41  ? 240  GLU   A OE1 1 
ATOM   3306 O OE2 . GLU   A 1 437 ? -1.218  15.525 15.208  1.00 87.95  ? 240  GLU   A OE2 1 
ATOM   3307 N N   . ASP   A 1 438 ? 1.900   13.457 10.498  1.00 82.40  ? 241  ASP   A N   1 
ATOM   3308 C CA  . ASP   A 1 438 ? 2.376   14.494 9.588   1.00 80.98  ? 241  ASP   A CA  1 
ATOM   3309 C C   . ASP   A 1 438 ? 1.783   14.329 8.190   1.00 77.00  ? 241  ASP   A C   1 
ATOM   3310 O O   . ASP   A 1 438 ? 1.341   15.310 7.575   1.00 75.97  ? 241  ASP   A O   1 
ATOM   3311 C CB  . ASP   A 1 438 ? 3.900   14.478 9.528   1.00 85.95  ? 241  ASP   A CB  1 
ATOM   3312 C CG  . ASP   A 1 438 ? 4.540   15.142 10.740  1.00 88.83  ? 241  ASP   A CG  1 
ATOM   3313 O OD1 . ASP   A 1 438 ? 5.349   14.481 11.433  1.00 91.03  ? 241  ASP   A OD1 1 
ATOM   3314 O OD2 . ASP   A 1 438 ? 4.232   16.329 10.998  1.00 88.84  ? 241  ASP   A OD2 1 
ATOM   3315 N N   . ASP   A 1 439 ? 1.761   13.093 7.668   1.00 73.95  ? 242  ASP   A N   1 
ATOM   3316 C CA  . ASP   A 1 439 ? 1.137   12.863 6.366   1.00 71.43  ? 242  ASP   A CA  1 
ATOM   3317 C C   . ASP   A 1 439 ? -0.277  13.453 6.308   1.00 70.05  ? 242  ASP   A C   1 
ATOM   3318 O O   . ASP   A 1 439 ? -0.663  14.091 5.313   1.00 69.63  ? 242  ASP   A O   1 
ATOM   3319 C CB  . ASP   A 1 439 ? 1.108   11.374 6.061   1.00 67.48  ? 242  ASP   A CB  1 
ATOM   3320 C CG  . ASP   A 1 439 ? 2.505   10.763 6.017   1.00 68.88  ? 242  ASP   A CG  1 
ATOM   3321 O OD1 . ASP   A 1 439 ? 3.486   11.526 5.887   1.00 70.86  ? 242  ASP   A OD1 1 
ATOM   3322 O OD2 . ASP   A 1 439 ? 2.618   9.523  6.111   1.00 68.33  ? 242  ASP   A OD2 1 
ATOM   3323 N N   . VAL   A 1 440 ? -1.053  13.272 7.379   1.00 68.22  ? 243  VAL   A N   1 
ATOM   3324 C CA  . VAL   A 1 440 ? -2.423  13.781 7.414   1.00 64.47  ? 243  VAL   A CA  1 
ATOM   3325 C C   . VAL   A 1 440 ? -2.463  15.277 7.137   1.00 65.94  ? 243  VAL   A C   1 
ATOM   3326 O O   . VAL   A 1 440 ? -3.439  15.785 6.567   1.00 65.06  ? 243  VAL   A O   1 
ATOM   3327 C CB  . VAL   A 1 440 ? -3.070  13.430 8.769   1.00 62.33  ? 243  VAL   A CB  1 
ATOM   3328 C CG1 . VAL   A 1 440 ? -4.409  14.109 8.930   1.00 58.28  ? 243  VAL   A CG1 1 
ATOM   3329 C CG2 . VAL   A 1 440 ? -3.220  11.901 8.888   1.00 64.38  ? 243  VAL   A CG2 1 
ATOM   3330 N N   . LYS   A 1 441 ? -1.412  16.008 7.523   1.00 67.99  ? 244  LYS   A N   1 
ATOM   3331 C CA  . LYS   A 1 441 ? -1.367  17.435 7.215   1.00 69.44  ? 244  LYS   A CA  1 
ATOM   3332 C C   . LYS   A 1 441 ? -1.109  17.689 5.729   1.00 72.57  ? 244  LYS   A C   1 
ATOM   3333 O O   . LYS   A 1 441 ? -1.478  18.741 5.207   1.00 74.11  ? 244  LYS   A O   1 
ATOM   3334 C CB  . LYS   A 1 441 ? -0.295  18.124 8.053   1.00 72.76  ? 244  LYS   A CB  1 
ATOM   3335 N N   . SER   A 1 442 ? -0.449  16.755 5.028   1.00 75.40  ? 245  SER   A N   1 
ATOM   3336 C CA  . SER   A 1 442 ? -0.246  16.895 3.585   1.00 78.02  ? 245  SER   A CA  1 
ATOM   3337 C C   . SER   A 1 442 ? -1.511  16.656 2.778   1.00 75.94  ? 245  SER   A C   1 
ATOM   3338 O O   . SER   A 1 442 ? -1.530  16.974 1.583   1.00 77.63  ? 245  SER   A O   1 
ATOM   3339 C CB  . SER   A 1 442 ? 0.824   15.923 3.109   1.00 81.51  ? 245  SER   A CB  1 
ATOM   3340 O OG  . SER   A 1 442 ? 1.821   15.771 4.089   1.00 85.74  ? 245  SER   A OG  1 
ATOM   3341 N N   . LEU   A 1 443 ? -2.554  16.102 3.395   1.00 71.94  ? 246  LEU   A N   1 
ATOM   3342 C CA  . LEU   A 1 443 ? -3.756  15.749 2.656   1.00 70.32  ? 246  LEU   A CA  1 
ATOM   3343 C C   . LEU   A 1 443 ? -4.468  16.987 2.137   1.00 72.43  ? 246  LEU   A C   1 
ATOM   3344 O O   . LEU   A 1 443 ? -4.964  16.990 1.007   1.00 74.57  ? 246  LEU   A O   1 
ATOM   3345 C CB  . LEU   A 1 443 ? -4.712  14.929 3.542   1.00 64.16  ? 246  LEU   A CB  1 
ATOM   3346 C CG  . LEU   A 1 443 ? -4.205  13.581 4.010   1.00 62.14  ? 246  LEU   A CG  1 
ATOM   3347 C CD1 . LEU   A 1 443 ? -5.216  12.955 4.953   1.00 58.61  ? 246  LEU   A CD1 1 
ATOM   3348 C CD2 . LEU   A 1 443 ? -3.964  12.704 2.810   1.00 64.66  ? 246  LEU   A CD2 1 
ATOM   3349 N N   . SER   A 1 444 ? -4.551  18.043 2.942   1.00 72.91  ? 247  SER   A N   1 
ATOM   3350 C CA  . SER   A 1 444 ? -5.377  19.198 2.589   1.00 72.43  ? 247  SER   A CA  1 
ATOM   3351 C C   . SER   A 1 444 ? -5.078  19.688 1.159   1.00 71.50  ? 247  SER   A C   1 
ATOM   3352 O O   . SER   A 1 444 ? -5.984  20.148 0.460   1.00 69.61  ? 247  SER   A O   1 
ATOM   3353 C CB  . SER   A 1 444 ? -5.219  20.320 3.619   1.00 73.50  ? 247  SER   A CB  1 
ATOM   3354 O OG  . SER   A 1 444 ? -3.913  20.832 3.590   1.00 78.10  ? 247  SER   A OG  1 
ATOM   3355 N N   . ARG   A 1 445 ? -3.800  19.606 0.747   1.00 71.42  ? 248  ARG   A N   1 
ATOM   3356 C CA  . ARG   A 1 445 ? -3.470  20.050 -0.612  1.00 72.03  ? 248  ARG   A CA  1 
ATOM   3357 C C   . ARG   A 1 445 ? -4.271  19.260 -1.656  1.00 70.25  ? 248  ARG   A C   1 
ATOM   3358 O O   . ARG   A 1 445 ? -5.095  19.819 -2.394  1.00 69.31  ? 248  ARG   A O   1 
ATOM   3359 C CB  . ARG   A 1 445 ? -1.961  19.925 -0.866  1.00 72.72  ? 248  ARG   A CB  1 
ATOM   3360 N N   . VAL   A 1 446 ? -4.071  17.942 -1.700  1.00 69.02  ? 249  VAL   A N   1 
ATOM   3361 C CA  . VAL   A 1 446 ? -4.780  17.126 -2.687  1.00 65.99  ? 249  VAL   A CA  1 
ATOM   3362 C C   . VAL   A 1 446 ? -6.278  17.091 -2.396  1.00 58.20  ? 249  VAL   A C   1 
ATOM   3363 O O   . VAL   A 1 446 ? -7.109  17.082 -3.312  1.00 55.04  ? 249  VAL   A O   1 
ATOM   3364 C CB  . VAL   A 1 446 ? -4.177  15.716 -2.738  1.00 67.66  ? 249  VAL   A CB  1 
ATOM   3365 C CG1 . VAL   A 1 446 ? -4.083  15.145 -1.343  1.00 66.21  ? 249  VAL   A CG1 1 
ATOM   3366 C CG2 . VAL   A 1 446 ? -5.029  14.826 -3.628  1.00 67.05  ? 249  VAL   A CG2 1 
ATOM   3367 N N   . MET   A 1 447 ? -6.648  17.079 -1.127  1.00 56.48  ? 250  MET   A N   1 
ATOM   3368 C CA  . MET   A 1 447 ? -8.063  17.083 -0.785  1.00 56.25  ? 250  MET   A CA  1 
ATOM   3369 C C   . MET   A 1 447 ? -8.774  18.287 -1.411  1.00 60.69  ? 250  MET   A C   1 
ATOM   3370 O O   . MET   A 1 447 ? -9.877  18.153 -1.974  1.00 61.65  ? 250  MET   A O   1 
ATOM   3371 C CB  . MET   A 1 447 ? -8.239  17.080 0.733   1.00 51.87  ? 250  MET   A CB  1 
ATOM   3372 C CG  . MET   A 1 447 ? -9.657  16.891 1.184   1.00 50.54  ? 250  MET   A CG  1 
ATOM   3373 S SD  . MET   A 1 447 ? -9.833  17.135 2.989   1.00 49.57  ? 250  MET   A SD  1 
ATOM   3374 C CE  . MET   A 1 447 ? -8.361  16.270 3.561   1.00 49.94  ? 250  MET   A CE  1 
ATOM   3375 N N   . ILE   A 1 448 ? -8.166  19.475 -1.328  1.00 61.50  ? 251  ILE   A N   1 
ATOM   3376 C CA  . ILE   A 1 448 ? -8.786  20.668 -1.894  1.00 58.46  ? 251  ILE   A CA  1 
ATOM   3377 C C   . ILE   A 1 448 ? -8.753  20.615 -3.415  1.00 57.81  ? 251  ILE   A C   1 
ATOM   3378 O O   . ILE   A 1 448 ? -9.753  20.893 -4.084  1.00 57.66  ? 251  ILE   A O   1 
ATOM   3379 C CB  . ILE   A 1 448 ? -8.105  21.944 -1.362  1.00 60.87  ? 251  ILE   A CB  1 
ATOM   3380 C CG1 . ILE   A 1 448 ? -8.271  22.024 0.161   1.00 59.53  ? 251  ILE   A CG1 1 
ATOM   3381 C CG2 . ILE   A 1 448 ? -8.671  23.192 -2.044  1.00 58.33  ? 251  ILE   A CG2 1 
ATOM   3382 C CD1 . ILE   A 1 448 ? -7.650  23.267 0.773   1.00 62.16  ? 251  ILE   A CD1 1 
ATOM   3383 N N   . HIS   A 1 449 ? -7.625  20.257 -4.001  1.00 59.27  ? 252  HIS   A N   1 
ATOM   3384 C CA  . HIS   A 1 449 ? -7.548  20.137 -5.445  1.00 62.86  ? 252  HIS   A CA  1 
ATOM   3385 C C   . HIS   A 1 449 ? -8.752  19.331 -5.997  1.00 58.56  ? 252  HIS   A C   1 
ATOM   3386 O O   . HIS   A 1 449 ? -9.349  19.747 -6.992  1.00 58.31  ? 252  HIS   A O   1 
ATOM   3387 C CB  . HIS   A 1 449 ? -6.188  19.584 -5.889  1.00 70.63  ? 252  HIS   A CB  1 
ATOM   3388 C CG  . HIS   A 1 449 ? -6.015  19.534 -7.376  1.00 77.09  ? 252  HIS   A CG  1 
ATOM   3389 N ND1 . HIS   A 1 449 ? -4.842  19.114 -7.964  1.00 81.29  ? 252  HIS   A ND1 1 
ATOM   3390 C CD2 . HIS   A 1 449 ? -6.858  19.842 -8.396  1.00 78.87  ? 252  HIS   A CD2 1 
ATOM   3391 C CE1 . HIS   A 1 449 ? -4.968  19.178 -9.280  1.00 84.43  ? 252  HIS   A CE1 1 
ATOM   3392 N NE2 . HIS   A 1 449 ? -6.183  19.612 -9.568  1.00 82.75  ? 252  HIS   A NE2 1 
ATOM   3393 N N   . VAL   A 1 450 ? -9.016  18.178 -5.343  1.00 54.08  ? 253  VAL   A N   1 
ATOM   3394 C CA  . VAL   A 1 450 ? -10.090 17.332 -5.886  1.00 53.08  ? 253  VAL   A CA  1 
ATOM   3395 C C   . VAL   A 1 450 ? -11.481 17.907 -5.571  1.00 50.67  ? 253  VAL   A C   1 
ATOM   3396 O O   . VAL   A 1 450 ? -12.347 18.001 -6.445  1.00 51.66  ? 253  VAL   A O   1 
ATOM   3397 C CB  . VAL   A 1 450 ? -9.943  15.883 -5.391  1.00 50.81  ? 253  VAL   A CB  1 
ATOM   3398 C CG1 . VAL   A 1 450 ? -11.106 15.043 -5.891  1.00 49.59  ? 253  VAL   A CG1 1 
ATOM   3399 C CG2 . VAL   A 1 450 ? -8.609  15.309 -5.838  1.00 52.99  ? 253  VAL   A CG2 1 
ATOM   3400 N N   . PHE   A 1 451 ? -11.711 18.240 -4.314  1.00 49.82  ? 254  PHE   A N   1 
ATOM   3401 C CA  . PHE   A 1 451 ? -13.039 18.721 -3.929  1.00 51.54  ? 254  PHE   A CA  1 
ATOM   3402 C C   . PHE   A 1 451 ? -13.409 20.017 -4.662  1.00 56.56  ? 254  PHE   A C   1 
ATOM   3403 O O   . PHE   A 1 451 ? -14.589 20.246 -4.967  1.00 57.35  ? 254  PHE   A O   1 
ATOM   3404 C CB  . PHE   A 1 451 ? -13.104 18.947 -2.413  1.00 47.73  ? 254  PHE   A CB  1 
ATOM   3405 C CG  . PHE   A 1 451 ? -14.510 19.002 -1.870  1.00 47.19  ? 254  PHE   A CG  1 
ATOM   3406 C CD1 . PHE   A 1 451 ? -15.376 17.924 -2.032  1.00 46.42  ? 254  PHE   A CD1 1 
ATOM   3407 C CD2 . PHE   A 1 451 ? -14.968 20.129 -1.214  1.00 47.73  ? 254  PHE   A CD2 1 
ATOM   3408 C CE1 . PHE   A 1 451 ? -16.657 17.969 -1.555  1.00 47.22  ? 254  PHE   A CE1 1 
ATOM   3409 C CE2 . PHE   A 1 451 ? -16.247 20.200 -0.727  1.00 47.26  ? 254  PHE   A CE2 1 
ATOM   3410 C CZ  . PHE   A 1 451 ? -17.110 19.112 -0.898  1.00 48.58  ? 254  PHE   A CZ  1 
ATOM   3411 N N   . SER   A 1 452 ? -12.425 20.852 -4.964  1.00 59.23  ? 255  SER   A N   1 
ATOM   3412 C CA  . SER   A 1 452 ? -12.712 22.168 -5.543  1.00 64.56  ? 255  SER   A CA  1 
ATOM   3413 C C   . SER   A 1 452 ? -13.072 22.108 -7.020  1.00 71.35  ? 255  SER   A C   1 
ATOM   3414 O O   . SER   A 1 452 ? -13.916 22.900 -7.454  1.00 72.39  ? 255  SER   A O   1 
ATOM   3415 C CB  . SER   A 1 452 ? -11.494 23.098 -5.378  1.00 63.04  ? 255  SER   A CB  1 
ATOM   3416 O OG  . SER   A 1 452 ? -10.958 23.019 -4.068  1.00 60.50  ? 255  SER   A OG  1 
ATOM   3417 N N   . ASP   A 1 453 ? -12.490 21.170 -7.783  1.00 76.88  ? 256  ASP   A N   1 
ATOM   3418 C CA  . ASP   A 1 453 ? -12.529 21.235 -9.237  1.00 85.55  ? 256  ASP   A CA  1 
ATOM   3419 C C   . ASP   A 1 453 ? -13.725 20.463 -9.781  1.00 86.35  ? 256  ASP   A C   1 
ATOM   3420 O O   . ASP   A 1 453 ? -13.588 19.463 -10.492 1.00 90.01  ? 256  ASP   A O   1 
ATOM   3421 C CB  . ASP   A 1 453 ? -11.220 20.734 -9.825  1.00 93.49  ? 256  ASP   A CB  1 
ATOM   3422 C CG  . ASP   A 1 453 ? -11.139 20.949 -11.329 1.00 103.34 ? 256  ASP   A CG  1 
ATOM   3423 O OD1 . ASP   A 1 453 ? -12.181 21.236 -11.948 1.00 105.95 ? 256  ASP   A OD1 1 
ATOM   3424 O OD2 . ASP   A 1 453 ? -10.024 20.825 -11.892 1.00 108.44 ? 256  ASP   A OD2 1 
ATOM   3425 N N   . GLY   A 1 454 ? -14.915 20.983 -9.487  1.00 81.89  ? 257  GLY   A N   1 
ATOM   3426 C CA  . GLY   A 1 454 ? -16.117 20.382 -10.044 1.00 78.98  ? 257  GLY   A CA  1 
ATOM   3427 C C   . GLY   A 1 454 ? -17.359 21.136 -9.638  1.00 72.82  ? 257  GLY   A C   1 
ATOM   3428 O O   . GLY   A 1 454 ? -17.299 22.292 -9.232  1.00 69.47  ? 257  GLY   A O   1 
ATOM   3429 N N   . VAL   A 1 455 ? -18.497 20.451 -9.734  1.00 71.80  ? 258  VAL   A N   1 
ATOM   3430 C CA  . VAL   A 1 455 ? -19.768 21.022 -9.306  1.00 71.99  ? 258  VAL   A CA  1 
ATOM   3431 C C   . VAL   A 1 455 ? -19.943 20.837 -7.792  1.00 66.02  ? 258  VAL   A C   1 
ATOM   3432 O O   . VAL   A 1 455 ? -19.124 20.182 -7.131  1.00 66.73  ? 258  VAL   A O   1 
ATOM   3433 C CB  . VAL   A 1 455 ? -20.936 20.400 -10.098 1.00 75.89  ? 258  VAL   A CB  1 
ATOM   3434 C CG1 . VAL   A 1 455 ? -21.401 19.094 -9.466  1.00 72.73  ? 258  VAL   A CG1 1 
ATOM   3435 C CG2 . VAL   A 1 455 ? -22.084 21.423 -10.223 1.00 79.68  ? 258  VAL   A CG2 1 
ATOM   3436 N N   . THR   A 1 456 ? -21.004 21.410 -7.236  1.00 58.03  ? 259  THR   A N   1 
ATOM   3437 C CA  . THR   A 1 456 ? -21.274 21.356 -5.816  1.00 52.39  ? 259  THR   A CA  1 
ATOM   3438 C C   . THR   A 1 456 ? -22.599 20.641 -5.590  1.00 52.80  ? 259  THR   A C   1 
ATOM   3439 O O   . THR   A 1 456 ? -23.603 20.961 -6.250  1.00 57.92  ? 259  THR   A O   1 
ATOM   3440 C CB  . THR   A 1 456 ? -21.326 22.762 -5.209  1.00 52.18  ? 259  THR   A CB  1 
ATOM   3441 O OG1 . THR   A 1 456 ? -20.026 23.355 -5.260  1.00 54.30  ? 259  THR   A OG1 1 
ATOM   3442 C CG2 . THR   A 1 456 ? -21.783 22.716 -3.745  1.00 46.89  ? 259  THR   A CG2 1 
ATOM   3443 N N   . ASN   A 1 457 ? -22.613 19.689 -4.661  1.00 47.57  ? 260  ASN   A N   1 
ATOM   3444 C CA  . ASN   A 1 457 ? -23.851 19.005 -4.287  1.00 45.89  ? 260  ASN   A CA  1 
ATOM   3445 C C   . ASN   A 1 457 ? -23.563 18.094 -3.093  1.00 43.19  ? 260  ASN   A C   1 
ATOM   3446 O O   . ASN   A 1 457 ? -22.403 17.821 -2.741  1.00 40.91  ? 260  ASN   A O   1 
ATOM   3447 C CB  . ASN   A 1 457 ? -24.434 18.215 -5.461  1.00 48.37  ? 260  ASN   A CB  1 
ATOM   3448 C CG  . ASN   A 1 457 ? -23.506 17.094 -5.927  1.00 52.73  ? 260  ASN   A CG  1 
ATOM   3449 O OD1 . ASN   A 1 457 ? -23.212 16.122 -5.156  1.00 51.86  ? 260  ASN   A OD1 1 
ATOM   3450 N ND2 . ASN   A 1 457 ? -23.010 17.211 -7.167  1.00 54.46  ? 260  ASN   A ND2 1 
ATOM   3451 N N   . TRP   A 1 458 ? -24.643 17.640 -2.454  1.00 41.49  ? 261  TRP   A N   1 
ATOM   3452 C CA  . TRP   A 1 458 ? -24.507 16.856 -1.250  1.00 38.27  ? 261  TRP   A CA  1 
ATOM   3453 C C   . TRP   A 1 458 ? -23.820 15.534 -1.531  1.00 39.52  ? 261  TRP   A C   1 
ATOM   3454 O O   . TRP   A 1 458 ? -23.210 14.969 -0.613  1.00 39.07  ? 261  TRP   A O   1 
ATOM   3455 C CB  . TRP   A 1 458 ? -25.867 16.621 -0.608  1.00 37.73  ? 261  TRP   A CB  1 
ATOM   3456 C CG  . TRP   A 1 458 ? -26.435 17.801 0.115   1.00 40.60  ? 261  TRP   A CG  1 
ATOM   3457 C CD1 . TRP   A 1 458 ? -27.565 18.521 -0.229  1.00 42.84  ? 261  TRP   A CD1 1 
ATOM   3458 C CD2 . TRP   A 1 458 ? -25.879 18.466 1.293   1.00 40.50  ? 261  TRP   A CD2 1 
ATOM   3459 N NE1 . TRP   A 1 458 ? -27.745 19.571 0.676   1.00 44.77  ? 261  TRP   A NE1 1 
ATOM   3460 C CE2 . TRP   A 1 458 ? -26.729 19.554 1.608   1.00 40.87  ? 261  TRP   A CE2 1 
ATOM   3461 C CE3 . TRP   A 1 458 ? -24.760 18.242 2.084   1.00 37.06  ? 261  TRP   A CE3 1 
ATOM   3462 C CZ2 . TRP   A 1 458 ? -26.506 20.368 2.693   1.00 38.92  ? 261  TRP   A CZ2 1 
ATOM   3463 C CZ3 . TRP   A 1 458 ? -24.531 19.035 3.161   1.00 35.00  ? 261  TRP   A CZ3 1 
ATOM   3464 C CH2 . TRP   A 1 458 ? -25.401 20.117 3.467   1.00 38.11  ? 261  TRP   A CH2 1 
ATOM   3465 N N   . GLY   A 1 459 ? -23.853 15.063 -2.775  1.00 40.61  ? 262  GLY   A N   1 
ATOM   3466 C CA  . GLY   A 1 459 ? -23.278 13.750 -3.064  1.00 43.33  ? 262  GLY   A CA  1 
ATOM   3467 C C   . GLY   A 1 459 ? -21.759 13.749 -2.958  1.00 42.69  ? 262  GLY   A C   1 
ATOM   3468 O O   . GLY   A 1 459 ? -21.174 12.807 -2.414  1.00 38.27  ? 262  GLY   A O   1 
ATOM   3469 N N   . ARG   A 1 460 ? -21.105 14.826 -3.442  1.00 42.04  ? 263  ARG   A N   1 
ATOM   3470 C CA  . ARG   A 1 460 ? -19.661 14.903 -3.313  1.00 42.05  ? 263  ARG   A CA  1 
ATOM   3471 C C   . ARG   A 1 460 ? -19.263 15.116 -1.876  1.00 40.13  ? 263  ARG   A C   1 
ATOM   3472 O O   . ARG   A 1 460 ? -18.221 14.616 -1.432  1.00 41.17  ? 263  ARG   A O   1 
ATOM   3473 C CB  . ARG   A 1 460 ? -19.123 16.026 -4.200  1.00 46.08  ? 263  ARG   A CB  1 
ATOM   3474 C CG  . ARG   A 1 460 ? -19.375 15.770 -5.699  1.00 48.77  ? 263  ARG   A CG  1 
ATOM   3475 C CD  . ARG   A 1 460 ? -18.548 16.724 -6.548  1.00 51.24  ? 263  ARG   A CD  1 
ATOM   3476 N NE  . ARG   A 1 460 ? -17.111 16.579 -6.308  1.00 48.98  ? 263  ARG   A NE  1 
ATOM   3477 C CZ  . ARG   A 1 460 ? -16.191 17.305 -6.908  1.00 47.65  ? 263  ARG   A CZ  1 
ATOM   3478 N NH1 . ARG   A 1 460 ? -16.566 18.248 -7.765  1.00 52.86  ? 263  ARG   A NH1 1 
ATOM   3479 N NH2 . ARG   A 1 460 ? -14.911 17.110 -6.648  1.00 43.34  ? 263  ARG   A NH2 1 
ATOM   3480 N N   . ILE   A 1 461 ? -20.105 15.803 -1.101  1.00 40.06  ? 264  ILE   A N   1 
ATOM   3481 C CA  . ILE   A 1 461 ? -19.837 15.969 0.337   1.00 37.40  ? 264  ILE   A CA  1 
ATOM   3482 C C   . ILE   A 1 461 ? -19.845 14.610 1.031   1.00 38.13  ? 264  ILE   A C   1 
ATOM   3483 O O   . ILE   A 1 461 ? -19.005 14.316 1.901   1.00 36.75  ? 264  ILE   A O   1 
ATOM   3484 C CB  . ILE   A 1 461 ? -20.862 16.945 0.963   1.00 34.74  ? 264  ILE   A CB  1 
ATOM   3485 C CG1 . ILE   A 1 461 ? -20.600 18.369 0.432   1.00 35.30  ? 264  ILE   A CG1 1 
ATOM   3486 C CG2 . ILE   A 1 461 ? -20.830 16.905 2.493   1.00 30.84  ? 264  ILE   A CG2 1 
ATOM   3487 C CD1 . ILE   A 1 461 ? -21.740 19.358 0.672   1.00 34.97  ? 264  ILE   A CD1 1 
ATOM   3488 N N   . VAL   A 1 462 ? -20.795 13.757 0.666   1.00 38.48  ? 265  VAL   A N   1 
ATOM   3489 C CA  . VAL   A 1 462 ? -20.802 12.395 1.199   1.00 37.58  ? 265  VAL   A CA  1 
ATOM   3490 C C   . VAL   A 1 462 ? -19.542 11.641 0.782   1.00 36.52  ? 265  VAL   A C   1 
ATOM   3491 O O   . VAL   A 1 462 ? -18.910 10.945 1.588   1.00 36.15  ? 265  VAL   A O   1 
ATOM   3492 C CB  . VAL   A 1 462 ? -22.066 11.669 0.713   1.00 38.64  ? 265  VAL   A CB  1 
ATOM   3493 C CG1 . VAL   A 1 462 ? -22.019 10.171 1.161   1.00 37.13  ? 265  VAL   A CG1 1 
ATOM   3494 C CG2 . VAL   A 1 462 ? -23.317 12.373 1.256   1.00 34.83  ? 265  VAL   A CG2 1 
ATOM   3495 N N   . THR   A 1 463 ? -19.125 11.795 -0.474  1.00 37.09  ? 266  THR   A N   1 
ATOM   3496 C CA  . THR   A 1 463 ? -17.871 11.171 -0.891  1.00 38.67  ? 266  THR   A CA  1 
ATOM   3497 C C   . THR   A 1 463 ? -16.716 11.640 -0.029  1.00 39.18  ? 266  THR   A C   1 
ATOM   3498 O O   . THR   A 1 463 ? -15.920 10.812 0.476   1.00 39.54  ? 266  THR   A O   1 
ATOM   3499 C CB  . THR   A 1 463 ? -17.592 11.450 -2.360  1.00 40.77  ? 266  THR   A CB  1 
ATOM   3500 O OG1 . THR   A 1 463 ? -18.703 10.975 -3.141  1.00 43.79  ? 266  THR   A OG1 1 
ATOM   3501 C CG2 . THR   A 1 463 ? -16.338 10.707 -2.829  1.00 40.86  ? 266  THR   A CG2 1 
ATOM   3502 N N   . LEU   A 1 464 ? -16.642 12.966 0.182   1.00 36.37  ? 267  LEU   A N   1 
ATOM   3503 C CA  . LEU   A 1 464 ? -15.591 13.562 0.984   1.00 34.92  ? 267  LEU   A CA  1 
ATOM   3504 C C   . LEU   A 1 464 ? -15.525 12.922 2.362   1.00 32.89  ? 267  LEU   A C   1 
ATOM   3505 O O   . LEU   A 1 464 ? -14.463 12.517 2.819   1.00 35.77  ? 267  LEU   A O   1 
ATOM   3506 C CB  . LEU   A 1 464 ? -15.835 15.098 1.101   1.00 32.22  ? 267  LEU   A CB  1 
ATOM   3507 C CG  . LEU   A 1 464 ? -14.877 15.809 2.005   1.00 34.71  ? 267  LEU   A CG  1 
ATOM   3508 C CD1 . LEU   A 1 464 ? -13.511 15.883 1.330   1.00 36.57  ? 267  LEU   A CD1 1 
ATOM   3509 C CD2 . LEU   A 1 464 ? -15.395 17.278 2.322   1.00 37.91  ? 267  LEU   A CD2 1 
ATOM   3510 N N   . ILE   A 1 465 ? -16.647 12.882 3.063   1.00 31.44  ? 268  ILE   A N   1 
ATOM   3511 C CA  . ILE   A 1 465 ? -16.679 12.329 4.407   1.00 30.56  ? 268  ILE   A CA  1 
ATOM   3512 C C   . ILE   A 1 465 ? -16.520 10.799 4.400   1.00 32.13  ? 268  ILE   A C   1 
ATOM   3513 O O   . ILE   A 1 465 ? -15.929 10.234 5.316   1.00 33.97  ? 268  ILE   A O   1 
ATOM   3514 C CB  . ILE   A 1 465 ? -17.996 12.769 5.082   1.00 30.41  ? 268  ILE   A CB  1 
ATOM   3515 C CG1 . ILE   A 1 465 ? -17.971 14.315 5.265   1.00 31.11  ? 268  ILE   A CG1 1 
ATOM   3516 C CG2 . ILE   A 1 465 ? -18.173 12.049 6.442   1.00 28.61  ? 268  ILE   A CG2 1 
ATOM   3517 C CD1 . ILE   A 1 465 ? -19.369 14.931 5.343   1.00 30.99  ? 268  ILE   A CD1 1 
ATOM   3518 N N   . SER   A 1 466 ? -17.024 10.118 3.373   1.00 31.12  ? 269  SER   A N   1 
ATOM   3519 C CA  . SER   A 1 466 ? -16.952 8.639  3.323   1.00 29.55  ? 269  SER   A CA  1 
ATOM   3520 C C   . SER   A 1 466 ? -15.506 8.158  3.109   1.00 33.89  ? 269  SER   A C   1 
ATOM   3521 O O   . SER   A 1 466 ? -15.018 7.220  3.788   1.00 32.86  ? 269  SER   A O   1 
ATOM   3522 C CB  . SER   A 1 466 ? -17.796 8.113  2.173   1.00 28.36  ? 269  SER   A CB  1 
ATOM   3523 O OG  . SER   A 1 466 ? -19.149 8.198  2.528   1.00 34.41  ? 269  SER   A OG  1 
ATOM   3524 N N   . PHE   A 1 467 ? -14.766 8.777  2.172   1.00 35.52  ? 270  PHE   A N   1 
ATOM   3525 C CA  . PHE   A 1 467 ? -13.360 8.471  2.096   1.00 34.93  ? 270  PHE   A CA  1 
ATOM   3526 C C   . PHE   A 1 467 ? -12.687 8.813  3.408   1.00 30.75  ? 270  PHE   A C   1 
ATOM   3527 O O   . PHE   A 1 467 ? -11.791 8.076  3.860   1.00 31.04  ? 270  PHE   A O   1 
ATOM   3528 C CB  . PHE   A 1 467 ? -12.711 9.240  0.954   1.00 38.71  ? 270  PHE   A CB  1 
ATOM   3529 C CG  . PHE   A 1 467 ? -11.268 8.818  0.714   1.00 39.87  ? 270  PHE   A CG  1 
ATOM   3530 C CD1 . PHE   A 1 467 ? -10.970 7.477  0.480   1.00 40.78  ? 270  PHE   A CD1 1 
ATOM   3531 C CD2 . PHE   A 1 467 ? -10.234 9.747  0.779   1.00 35.57  ? 270  PHE   A CD2 1 
ATOM   3532 C CE1 . PHE   A 1 467 ? -9.650  7.067  0.256   1.00 42.96  ? 270  PHE   A CE1 1 
ATOM   3533 C CE2 . PHE   A 1 467 ? -8.956  9.378  0.582   1.00 38.10  ? 270  PHE   A CE2 1 
ATOM   3534 C CZ  . PHE   A 1 467 ? -8.629  8.018  0.302   1.00 41.20  ? 270  PHE   A CZ  1 
ATOM   3535 N N   . GLY   A 1 468 ? -13.116 9.922  4.048   1.00 26.72  ? 271  GLY   A N   1 
ATOM   3536 C CA  . GLY   A 1 468 ? -12.595 10.236 5.368   1.00 26.29  ? 271  GLY   A CA  1 
ATOM   3537 C C   . GLY   A 1 468 ? -12.741 9.079  6.326   1.00 30.58  ? 271  GLY   A C   1 
ATOM   3538 O O   . GLY   A 1 468 ? -11.789 8.733  7.043   1.00 33.66  ? 271  GLY   A O   1 
ATOM   3539 N N   . ALA   A 1 469 ? -13.923 8.449  6.341   1.00 26.65  ? 272  ALA   A N   1 
ATOM   3540 C CA  . ALA   A 1 469 ? -14.137 7.297  7.202   1.00 31.90  ? 272  ALA   A CA  1 
ATOM   3541 C C   . ALA   A 1 469 ? -13.299 6.089  6.726   1.00 32.80  ? 272  ALA   A C   1 
ATOM   3542 O O   . ALA   A 1 469 ? -12.769 5.351  7.540   1.00 31.78  ? 272  ALA   A O   1 
ATOM   3543 C CB  . ALA   A 1 469 ? -15.630 6.890  7.211   1.00 30.28  ? 272  ALA   A CB  1 
ATOM   3544 N N   . PHE   A 1 470 ? -13.187 5.910  5.425   1.00 35.20  ? 273  PHE   A N   1 
ATOM   3545 C CA  . PHE   A 1 470 ? -12.333 4.865  4.869   1.00 37.46  ? 273  PHE   A CA  1 
ATOM   3546 C C   . PHE   A 1 470 ? -10.903 5.049  5.341   1.00 40.28  ? 273  PHE   A C   1 
ATOM   3547 O O   . PHE   A 1 470 ? -10.243 4.085  5.737   1.00 43.72  ? 273  PHE   A O   1 
ATOM   3548 C CB  . PHE   A 1 470 ? -12.399 4.896  3.351   1.00 34.17  ? 273  PHE   A CB  1 
ATOM   3549 C CG  . PHE   A 1 470 ? -11.898 3.596  2.686   1.00 36.64  ? 273  PHE   A CG  1 
ATOM   3550 C CD1 . PHE   A 1 470 ? -12.783 2.546  2.454   1.00 36.01  ? 273  PHE   A CD1 1 
ATOM   3551 C CD2 . PHE   A 1 470 ? -10.590 3.477  2.291   1.00 36.09  ? 273  PHE   A CD2 1 
ATOM   3552 C CE1 . PHE   A 1 470 ? -12.342 1.366  1.824   1.00 38.33  ? 273  PHE   A CE1 1 
ATOM   3553 C CE2 . PHE   A 1 470 ? -10.144 2.316  1.664   1.00 40.22  ? 273  PHE   A CE2 1 
ATOM   3554 C CZ  . PHE   A 1 470 ? -11.027 1.249  1.422   1.00 39.09  ? 273  PHE   A CZ  1 
ATOM   3555 N N   . VAL   A 1 471 ? -10.411 6.280  5.325   1.00 38.17  ? 274  VAL   A N   1 
ATOM   3556 C CA  . VAL   A 1 471 ? -9.053  6.535  5.783   1.00 39.51  ? 274  VAL   A CA  1 
ATOM   3557 C C   . VAL   A 1 471 ? -8.939  6.378  7.297   1.00 38.28  ? 274  VAL   A C   1 
ATOM   3558 O O   . VAL   A 1 471 ? -7.883  5.944  7.806   1.00 39.73  ? 274  VAL   A O   1 
ATOM   3559 C CB  . VAL   A 1 471 ? -8.596  7.931  5.303   1.00 38.16  ? 274  VAL   A CB  1 
ATOM   3560 C CG1 . VAL   A 1 471 ? -7.331  8.376  6.049   1.00 37.53  ? 274  VAL   A CG1 1 
ATOM   3561 C CG2 . VAL   A 1 471 ? -8.369  7.862  3.809   1.00 39.88  ? 274  VAL   A CG2 1 
ATOM   3562 N N   . ALA   A 1 472 ? -10.007 6.711  8.038   1.00 34.47  ? 275  ALA   A N   1 
ATOM   3563 C CA  . ALA   A 1 472 ? -9.960  6.558  9.498   1.00 35.12  ? 275  ALA   A CA  1 
ATOM   3564 C C   . ALA   A 1 472 ? -9.822  5.081  9.874   1.00 34.54  ? 275  ALA   A C   1 
ATOM   3565 O O   . ALA   A 1 472 ? -9.036  4.741  10.786  1.00 36.14  ? 275  ALA   A O   1 
ATOM   3566 C CB  . ALA   A 1 472 ? -11.215 7.174  10.159  1.00 24.91  ? 275  ALA   A CB  1 
ATOM   3567 N N   . LYS   A 1 473 ? -10.574 4.204  9.195   1.00 34.86  ? 276  LYS   A N   1 
ATOM   3568 C CA  . LYS   A 1 473 ? -10.459 2.756  9.479   1.00 36.93  ? 276  LYS   A CA  1 
ATOM   3569 C C   . LYS   A 1 473 ? -9.021  2.293  9.314   1.00 38.91  ? 276  LYS   A C   1 
ATOM   3570 O O   . LYS   A 1 473 ? -8.503  1.525  10.161  1.00 42.50  ? 276  LYS   A O   1 
ATOM   3571 C CB  . LYS   A 1 473 ? -11.358 1.942  8.564   1.00 39.07  ? 276  LYS   A CB  1 
ATOM   3572 C CG  . LYS   A 1 473 ? -12.858 2.155  8.730   1.00 40.46  ? 276  LYS   A CG  1 
ATOM   3573 C CD  . LYS   A 1 473 ? -13.622 1.311  7.645   1.00 40.73  ? 276  LYS   A CD  1 
ATOM   3574 C CE  . LYS   A 1 473 ? -15.123 1.589  7.692   1.00 38.49  ? 276  LYS   A CE  1 
ATOM   3575 N NZ  . LYS   A 1 473 ? -15.903 0.818  6.664   1.00 40.32  ? 276  LYS   A NZ  1 
ATOM   3576 N N   . HIS   A 1 474 ? -8.362  2.752  8.252   1.00 38.31  ? 277  HIS   A N   1 
ATOM   3577 C CA  . HIS   A 1 474 ? -6.968  2.404  8.035   1.00 44.18  ? 277  HIS   A CA  1 
ATOM   3578 C C   . HIS   A 1 474 ? -6.078  2.961  9.138   1.00 49.40  ? 277  HIS   A C   1 
ATOM   3579 O O   . HIS   A 1 474 ? -5.190  2.261  9.640   1.00 52.81  ? 277  HIS   A O   1 
ATOM   3580 C CB  . HIS   A 1 474 ? -6.521  2.924  6.676   1.00 46.55  ? 277  HIS   A CB  1 
ATOM   3581 C CG  . HIS   A 1 474 ? -5.058  2.778  6.430   1.00 53.36  ? 277  HIS   A CG  1 
ATOM   3582 N ND1 . HIS   A 1 474 ? -4.466  1.550  6.167   1.00 56.57  ? 277  HIS   A ND1 1 
ATOM   3583 C CD2 . HIS   A 1 474 ? -4.061  3.694  6.395   1.00 55.72  ? 277  HIS   A CD2 1 
ATOM   3584 C CE1 . HIS   A 1 474 ? -3.168  1.727  5.977   1.00 59.41  ? 277  HIS   A CE1 1 
ATOM   3585 N NE2 . HIS   A 1 474 ? -2.897  3.015  6.114   1.00 58.53  ? 277  HIS   A NE2 1 
ATOM   3586 N N   . LEU   A 1 475 ? -6.298  4.211  9.557   1.00 48.95  ? 278  LEU   A N   1 
ATOM   3587 C CA  . LEU   A 1 475 ? -5.436  4.754  10.592  1.00 49.90  ? 278  LEU   A CA  1 
ATOM   3588 C C   . LEU   A 1 475 ? -5.571  3.954  11.891  1.00 50.17  ? 278  LEU   A C   1 
ATOM   3589 O O   . LEU   A 1 475 ? -4.595  3.812  12.631  1.00 52.26  ? 278  LEU   A O   1 
ATOM   3590 C CB  . LEU   A 1 475 ? -5.728  6.239  10.800  1.00 47.95  ? 278  LEU   A CB  1 
ATOM   3591 C CG  . LEU   A 1 475 ? -5.249  7.115  9.634   1.00 50.34  ? 278  LEU   A CG  1 
ATOM   3592 C CD1 . LEU   A 1 475 ? -5.858  8.538  9.726   1.00 47.18  ? 278  LEU   A CD1 1 
ATOM   3593 C CD2 . LEU   A 1 475 ? -3.739  7.183  9.603   1.00 55.27  ? 278  LEU   A CD2 1 
ATOM   3594 N N   . LYS   A 1 476 ? -6.720  3.403  12.132  1.00 48.03  ? 279  LYS   A N   1 
ATOM   3595 C CA  . LYS   A 1 476 ? -6.907  2.671  13.332  1.00 50.05  ? 279  LYS   A CA  1 
ATOM   3596 C C   . LYS   A 1 476 ? -6.200  1.341  13.288  1.00 51.02  ? 279  LYS   A C   1 
ATOM   3597 O O   . LYS   A 1 476 ? -5.746  0.864  14.272  1.00 50.66  ? 279  LYS   A O   1 
ATOM   3598 C CB  . LYS   A 1 476 ? -8.374  2.436  13.601  1.00 50.65  ? 279  LYS   A CB  1 
ATOM   3599 C CG  . LYS   A 1 476 ? -8.635  1.673  14.875  1.00 54.26  ? 279  LYS   A CG  1 
ATOM   3600 C CD  . LYS   A 1 476 ? -8.957  0.240  14.590  1.00 59.75  ? 279  LYS   A CD  1 
ATOM   3601 C CE  . LYS   A 1 476 ? -9.480  -0.491 15.814  1.00 62.10  ? 279  LYS   A CE  1 
ATOM   3602 N NZ  . LYS   A 1 476 ? -9.389  0.349  17.024  1.00 64.13  ? 279  LYS   A NZ  1 
ATOM   3603 N N   . THR   A 1 477 ? -6.145  0.743  12.131  1.00 53.00  ? 280  THR   A N   1 
ATOM   3604 C CA  . THR   A 1 477 ? -5.497  -0.563 12.017  1.00 58.40  ? 280  THR   A CA  1 
ATOM   3605 C C   . THR   A 1 477 ? -3.986  -0.461 12.167  1.00 59.19  ? 280  THR   A C   1 
ATOM   3606 O O   . THR   A 1 477 ? -3.352  -1.402 12.655  1.00 62.63  ? 280  THR   A O   1 
ATOM   3607 C CB  . THR   A 1 477 ? -5.853  -1.237 10.684  1.00 61.48  ? 280  THR   A CB  1 
ATOM   3608 O OG1 . THR   A 1 477 ? -5.220  -0.524 9.600   1.00 65.26  ? 280  THR   A OG1 1 
ATOM   3609 C CG2 . THR   A 1 477 ? -7.383  -1.267 10.474  1.00 56.41  ? 280  THR   A CG2 1 
ATOM   3610 N N   . ILE   A 1 478 ? -3.396  0.669  11.756  1.00 54.95  ? 281  ILE   A N   1 
ATOM   3611 C CA  . ILE   A 1 478 ? -1.942  0.817  11.888  1.00 53.75  ? 281  ILE   A CA  1 
ATOM   3612 C C   . ILE   A 1 478 ? -1.604  1.579  13.163  1.00 52.80  ? 281  ILE   A C   1 
ATOM   3613 O O   . ILE   A 1 478 ? -0.521  2.185  13.271  1.00 57.04  ? 281  ILE   A O   1 
ATOM   3614 C CB  . ILE   A 1 478 ? -1.363  1.563  10.662  1.00 51.01  ? 281  ILE   A CB  1 
ATOM   3615 C CG1 . ILE   A 1 478 ? -2.000  2.946  10.502  1.00 46.91  ? 281  ILE   A CG1 1 
ATOM   3616 C CG2 . ILE   A 1 478 ? -1.551  0.741  9.393   1.00 49.00  ? 281  ILE   A CG2 1 
ATOM   3617 C CD1 . ILE   A 1 478 ? -1.174  3.858  9.640   1.00 48.31  ? 281  ILE   A CD1 1 
ATOM   3618 N N   . ASN   A 1 479 ? -2.498  1.525  14.168  1.00 48.74  ? 282  ASN   A N   1 
ATOM   3619 C CA  . ASN   A 1 479 ? -2.204  2.109  15.488  1.00 49.65  ? 282  ASN   A CA  1 
ATOM   3620 C C   . ASN   A 1 479 ? -1.976  3.617  15.396  1.00 51.03  ? 282  ASN   A C   1 
ATOM   3621 O O   . ASN   A 1 479 ? -1.149  4.179  16.117  1.00 52.62  ? 282  ASN   A O   1 
ATOM   3622 C CB  . ASN   A 1 479 ? -1.001  1.434  16.143  1.00 52.32  ? 282  ASN   A CB  1 
ATOM   3623 C CG  . ASN   A 1 479 ? -0.916  1.694  17.629  1.00 54.55  ? 282  ASN   A CG  1 
ATOM   3624 O OD1 . ASN   A 1 479 ? -1.943  1.800  18.297  1.00 51.83  ? 282  ASN   A OD1 1 
ATOM   3625 N ND2 . ASN   A 1 479 ? 0.296   1.806  18.150  1.00 52.59  ? 282  ASN   A ND2 1 
ATOM   3626 N N   . GLN   A 1 480 ? -2.695  4.287  14.485  1.00 50.85  ? 283  GLN   A N   1 
ATOM   3627 C CA  . GLN   A 1 480 ? -2.595  5.732  14.317  1.00 52.43  ? 283  GLN   A CA  1 
ATOM   3628 C C   . GLN   A 1 480 ? -3.931  6.399  14.619  1.00 52.08  ? 283  GLN   A C   1 
ATOM   3629 O O   . GLN   A 1 480 ? -4.313  7.379  13.984  1.00 49.85  ? 283  GLN   A O   1 
ATOM   3630 C CB  . GLN   A 1 480 ? -2.111  6.085  12.913  1.00 52.52  ? 283  GLN   A CB  1 
ATOM   3631 C CG  . GLN   A 1 480 ? -0.606  5.801  12.702  1.00 55.20  ? 283  GLN   A CG  1 
ATOM   3632 C CD  . GLN   A 1 480 ? 0.283   6.666  13.563  1.00 56.29  ? 283  GLN   A CD  1 
ATOM   3633 O OE1 . GLN   A 1 480 ? 1.379   6.264  13.930  1.00 59.90  ? 283  GLN   A OE1 1 
ATOM   3634 N NE2 . GLN   A 1 480 ? -0.185  7.876  13.885  1.00 54.89  ? 283  GLN   A NE2 1 
ATOM   3635 N N   . GLU   A 1 481 ? -4.652  5.846  15.601  1.00 51.58  ? 284  GLU   A N   1 
ATOM   3636 C CA  . GLU   A 1 481 ? -5.958  6.357  15.975  1.00 46.87  ? 284  GLU   A CA  1 
ATOM   3637 C C   . GLU   A 1 481 ? -5.874  7.820  16.391  1.00 45.62  ? 284  GLU   A C   1 
ATOM   3638 O O   . GLU   A 1 481 ? -6.853  8.551  16.278  1.00 42.32  ? 284  GLU   A O   1 
ATOM   3639 C CB  . GLU   A 1 481 ? -6.545  5.514  17.104  1.00 46.45  ? 284  GLU   A CB  1 
ATOM   3640 C CG  . GLU   A 1 481 ? -8.020  5.771  17.336  1.00 48.37  ? 284  GLU   A CG  1 
ATOM   3641 C CD  . GLU   A 1 481 ? -8.669  4.786  18.296  1.00 51.66  ? 284  GLU   A CD  1 
ATOM   3642 O OE1 . GLU   A 1 481 ? -8.130  3.646  18.457  1.00 57.80  ? 284  GLU   A OE1 1 
ATOM   3643 O OE2 . GLU   A 1 481 ? -9.720  5.143  18.876  1.00 47.52  ? 284  GLU   A OE2 1 
ATOM   3644 N N   . SER   A 1 482 ? -4.709  8.262  16.882  1.00 50.91  ? 285  SER   A N   1 
ATOM   3645 C CA  . SER   A 1 482 ? -4.536  9.676  17.263  1.00 54.55  ? 285  SER   A CA  1 
ATOM   3646 C C   . SER   A 1 482 ? -4.715  10.638 16.086  1.00 52.97  ? 285  SER   A C   1 
ATOM   3647 O O   . SER   A 1 482 ? -4.981  11.833 16.310  1.00 53.44  ? 285  SER   A O   1 
ATOM   3648 C CB  . SER   A 1 482 ? -3.159  9.894  17.890  1.00 58.40  ? 285  SER   A CB  1 
ATOM   3649 O OG  . SER   A 1 482 ? -2.148  9.423  17.026  1.00 60.79  ? 285  SER   A OG  1 
ATOM   3650 N N   . CYS   A 1 483 ? -4.571  10.157 14.849  1.00 48.58  ? 286  CYS   A N   1 
ATOM   3651 C CA  . CYS   A 1 483 ? -4.664  10.991 13.664  1.00 47.19  ? 286  CYS   A CA  1 
ATOM   3652 C C   . CYS   A 1 483 ? -6.082  11.165 13.154  1.00 44.63  ? 286  CYS   A C   1 
ATOM   3653 O O   . CYS   A 1 483 ? -6.288  11.865 12.163  1.00 45.88  ? 286  CYS   A O   1 
ATOM   3654 C CB  . CYS   A 1 483 ? -3.793  10.426 12.545  1.00 48.99  ? 286  CYS   A CB  1 
ATOM   3655 S SG  . CYS   A 1 483 ? -2.106  10.005 13.091  1.00 54.91  ? 286  CYS   A SG  1 
ATOM   3656 N N   . ILE   A 1 484 ? -7.072  10.528 13.769  1.00 41.21  ? 287  ILE   A N   1 
ATOM   3657 C CA  . ILE   A 1 484 ? -8.427  10.577 13.216  1.00 33.98  ? 287  ILE   A CA  1 
ATOM   3658 C C   . ILE   A 1 484 ? -9.041  11.944 13.458  1.00 36.13  ? 287  ILE   A C   1 
ATOM   3659 O O   . ILE   A 1 484 ? -9.727  12.493 12.576  1.00 37.21  ? 287  ILE   A O   1 
ATOM   3660 C CB  . ILE   A 1 484 ? -9.277  9.449  13.827  1.00 29.87  ? 287  ILE   A CB  1 
ATOM   3661 C CG1 . ILE   A 1 484 ? -8.797  8.074  13.282  1.00 32.63  ? 287  ILE   A CG1 1 
ATOM   3662 C CG2 . ILE   A 1 484 ? -10.745 9.665  13.527  1.00 25.44  ? 287  ILE   A CG2 1 
ATOM   3663 C CD1 . ILE   A 1 484 ? -9.623  6.848  13.817  1.00 32.22  ? 287  ILE   A CD1 1 
ATOM   3664 N N   . GLU   A 1 485 ? -8.841  12.515 14.668  1.00 35.22  ? 288  GLU   A N   1 
ATOM   3665 C CA  . GLU   A 1 485 ? -9.443  13.833 14.929  1.00 39.01  ? 288  GLU   A CA  1 
ATOM   3666 C C   . GLU   A 1 485 ? -8.770  14.907 14.122  1.00 39.01  ? 288  GLU   A C   1 
ATOM   3667 O O   . GLU   A 1 485 ? -9.503  15.714 13.490  1.00 36.15  ? 288  GLU   A O   1 
ATOM   3668 C CB  . GLU   A 1 485 ? -9.411  14.108 16.434  1.00 41.09  ? 288  GLU   A CB  1 
ATOM   3669 C CG  . GLU   A 1 485 ? -10.157 15.423 16.828  1.00 43.02  ? 288  GLU   A CG  1 
ATOM   3670 C CD  . GLU   A 1 485 ? -11.696 15.299 16.709  1.00 43.49  ? 288  GLU   A CD  1 
ATOM   3671 O OE1 . GLU   A 1 485 ? -12.246 14.162 16.703  1.00 41.79  ? 288  GLU   A OE1 1 
ATOM   3672 O OE2 . GLU   A 1 485 ? -12.385 16.365 16.628  1.00 44.47  ? 288  GLU   A OE2 1 
ATOM   3673 N N   . PRO   A 1 486 ? -7.454  14.988 14.014  1.00 41.81  ? 289  PRO   A N   1 
ATOM   3674 C CA  . PRO   A 1 486 ? -6.836  15.945 13.084  1.00 41.90  ? 289  PRO   A CA  1 
ATOM   3675 C C   . PRO   A 1 486 ? -7.298  15.726 11.646  1.00 42.67  ? 289  PRO   A C   1 
ATOM   3676 O O   . PRO   A 1 486 ? -7.405  16.708 10.877  1.00 41.84  ? 289  PRO   A O   1 
ATOM   3677 C CB  . PRO   A 1 486 ? -5.324  15.674 13.240  1.00 41.55  ? 289  PRO   A CB  1 
ATOM   3678 C CG  . PRO   A 1 486 ? -5.181  14.939 14.563  1.00 42.11  ? 289  PRO   A CG  1 
ATOM   3679 C CD  . PRO   A 1 486 ? -6.457  14.130 14.712  1.00 40.26  ? 289  PRO   A CD  1 
ATOM   3680 N N   . LEU   A 1 487 ? -7.604  14.468 11.261  1.00 36.87  ? 290  LEU   A N   1 
ATOM   3681 C CA  . LEU   A 1 487 ? -8.191  14.230 9.947   1.00 33.42  ? 290  LEU   A CA  1 
ATOM   3682 C C   . LEU   A 1 487 ? -9.604  14.822 9.852   1.00 33.46  ? 290  LEU   A C   1 
ATOM   3683 O O   . LEU   A 1 487 ? -9.982  15.394 8.827   1.00 34.88  ? 290  LEU   A O   1 
ATOM   3684 C CB  . LEU   A 1 487 ? -8.217  12.724 9.661   1.00 32.80  ? 290  LEU   A CB  1 
ATOM   3685 C CG  . LEU   A 1 487 ? -8.786  12.267 8.307   1.00 33.80  ? 290  LEU   A CG  1 
ATOM   3686 C CD1 . LEU   A 1 487 ? -7.894  12.708 7.165   1.00 39.47  ? 290  LEU   A CD1 1 
ATOM   3687 C CD2 . LEU   A 1 487 ? -8.949  10.738 8.265   1.00 33.14  ? 290  LEU   A CD2 1 
ATOM   3688 N N   . ALA   A 1 488 ? -10.401 14.673 10.896  1.00 33.25  ? 291  ALA   A N   1 
ATOM   3689 C CA  . ALA   A 1 488 ? -11.750 15.201 10.877  1.00 31.11  ? 291  ALA   A CA  1 
ATOM   3690 C C   . ALA   A 1 488 ? -11.720 16.747 10.820  1.00 33.13  ? 291  ALA   A C   1 
ATOM   3691 O O   . ALA   A 1 488 ? -12.561 17.350 10.161  1.00 33.13  ? 291  ALA   A O   1 
ATOM   3692 C CB  . ALA   A 1 488 ? -12.544 14.714 12.103  1.00 25.98  ? 291  ALA   A CB  1 
ATOM   3693 N N   . GLU   A 1 489 ? -10.764 17.363 11.485  1.00 33.56  ? 292  GLU   A N   1 
ATOM   3694 C CA  . GLU   A 1 489 ? -10.640 18.816 11.446  1.00 39.35  ? 292  GLU   A CA  1 
ATOM   3695 C C   . GLU   A 1 489 ? -10.234 19.289 10.066  1.00 40.18  ? 292  GLU   A C   1 
ATOM   3696 O O   . GLU   A 1 489 ? -10.772 20.271 9.565   1.00 38.49  ? 292  GLU   A O   1 
ATOM   3697 C CB  . GLU   A 1 489 ? -9.615  19.308 12.492  1.00 41.20  ? 292  GLU   A CB  1 
ATOM   3698 C CG  . GLU   A 1 489 ? -9.938  18.809 13.882  1.00 47.75  ? 292  GLU   A CG  1 
ATOM   3699 C CD  . GLU   A 1 489 ? -8.881  19.120 14.924  1.00 55.47  ? 292  GLU   A CD  1 
ATOM   3700 O OE1 . GLU   A 1 489 ? -9.252  19.180 16.116  1.00 56.86  ? 292  GLU   A OE1 1 
ATOM   3701 O OE2 . GLU   A 1 489 ? -7.686  19.317 14.564  1.00 60.31  ? 292  GLU   A OE2 1 
ATOM   3702 N N   . SER   A 1 490 ? -9.313  18.606 9.405   1.00 41.57  ? 293  SER   A N   1 
ATOM   3703 C CA  . SER   A 1 490 ? -8.903  19.024 8.082   1.00 42.57  ? 293  SER   A CA  1 
ATOM   3704 C C   . SER   A 1 490 ? -10.048 18.839 7.063   1.00 40.96  ? 293  SER   A C   1 
ATOM   3705 O O   . SER   A 1 490 ? -10.251 19.700 6.212   1.00 46.07  ? 293  SER   A O   1 
ATOM   3706 C CB  . SER   A 1 490 ? -7.611  18.329 7.697   1.00 46.60  ? 293  SER   A CB  1 
ATOM   3707 O OG  . SER   A 1 490 ? -7.304  18.598 6.348   1.00 52.72  ? 293  SER   A OG  1 
ATOM   3708 N N   . ILE   A 1 491 ? -10.722 17.697 7.140   1.00 34.39  ? 294  ILE   A N   1 
ATOM   3709 C CA  . ILE   A 1 491 ? -11.885 17.561 6.259   1.00 34.51  ? 294  ILE   A CA  1 
ATOM   3710 C C   . ILE   A 1 491 ? -12.882 18.707 6.511   1.00 35.52  ? 294  ILE   A C   1 
ATOM   3711 O O   . ILE   A 1 491 ? -13.475 19.251 5.564   1.00 35.03  ? 294  ILE   A O   1 
ATOM   3712 C CB  . ILE   A 1 491 ? -12.580 16.186 6.450   1.00 32.41  ? 294  ILE   A CB  1 
ATOM   3713 C CG1 . ILE   A 1 491 ? -11.637 15.034 5.975   1.00 33.02  ? 294  ILE   A CG1 1 
ATOM   3714 C CG2 . ILE   A 1 491 ? -13.885 16.116 5.729   1.00 27.22  ? 294  ILE   A CG2 1 
ATOM   3715 C CD1 . ILE   A 1 491 ? -12.131 13.708 6.464   1.00 31.01  ? 294  ILE   A CD1 1 
ATOM   3716 N N   . THR   A 1 492 ? -13.144 19.020 7.787   1.00 30.86  ? 295  THR   A N   1 
ATOM   3717 C CA  . THR   A 1 492 ? -14.179 19.981 8.076   1.00 33.68  ? 295  THR   A CA  1 
ATOM   3718 C C   . THR   A 1 492 ? -13.747 21.381 7.597   1.00 37.00  ? 295  THR   A C   1 
ATOM   3719 O O   . THR   A 1 492 ? -14.546 22.110 6.998   1.00 37.74  ? 295  THR   A O   1 
ATOM   3720 C CB  . THR   A 1 492 ? -14.466 20.010 9.575   1.00 35.74  ? 295  THR   A CB  1 
ATOM   3721 O OG1 . THR   A 1 492 ? -15.114 18.811 9.949   1.00 37.70  ? 295  THR   A OG1 1 
ATOM   3722 C CG2 . THR   A 1 492 ? -15.402 21.187 9.908   1.00 33.38  ? 295  THR   A CG2 1 
ATOM   3723 N N   . ASP   A 1 493 ? -12.470 21.740 7.806   1.00 37.85  ? 296  ASP   A N   1 
ATOM   3724 C CA  . ASP   A 1 493 ? -11.983 23.026 7.325   1.00 44.64  ? 296  ASP   A CA  1 
ATOM   3725 C C   . ASP   A 1 493 ? -12.111 23.143 5.800   1.00 46.85  ? 296  ASP   A C   1 
ATOM   3726 O O   . ASP   A 1 493 ? -12.554 24.179 5.266   1.00 47.57  ? 296  ASP   A O   1 
ATOM   3727 C CB  . ASP   A 1 493 ? -10.529 23.230 7.766   1.00 49.44  ? 296  ASP   A CB  1 
ATOM   3728 C CG  . ASP   A 1 493 ? -9.984  24.581 7.310   1.00 58.88  ? 296  ASP   A CG  1 
ATOM   3729 O OD1 . ASP   A 1 493 ? -9.429  24.663 6.184   1.00 63.19  ? 296  ASP   A OD1 1 
ATOM   3730 O OD2 . ASP   A 1 493 ? -10.117 25.579 8.063   1.00 62.31  ? 296  ASP   A OD2 1 
ATOM   3731 N N   . VAL   A 1 494 ? -11.728 22.092 5.068   1.00 46.70  ? 297  VAL   A N   1 
ATOM   3732 C CA  . VAL   A 1 494 ? -11.847 22.121 3.610   1.00 46.30  ? 297  VAL   A CA  1 
ATOM   3733 C C   . VAL   A 1 494 ? -13.306 22.274 3.202   1.00 44.03  ? 297  VAL   A C   1 
ATOM   3734 O O   . VAL   A 1 494 ? -13.645 23.105 2.346   1.00 47.03  ? 297  VAL   A O   1 
ATOM   3735 C CB  . VAL   A 1 494 ? -11.216 20.865 2.995   1.00 47.18  ? 297  VAL   A CB  1 
ATOM   3736 C CG1 . VAL   A 1 494 ? -11.503 20.798 1.506   1.00 48.05  ? 297  VAL   A CG1 1 
ATOM   3737 C CG2 . VAL   A 1 494 ? -9.720  20.838 3.280   1.00 48.85  ? 297  VAL   A CG2 1 
ATOM   3738 N N   . LEU   A 1 495 ? -14.184 21.501 3.842   1.00 40.03  ? 298  LEU   A N   1 
ATOM   3739 C CA  . LEU   A 1 495 ? -15.612 21.556 3.508   1.00 38.08  ? 298  LEU   A CA  1 
ATOM   3740 C C   . LEU   A 1 495 ? -16.210 22.978 3.767   1.00 40.41  ? 298  LEU   A C   1 
ATOM   3741 O O   . LEU   A 1 495 ? -16.934 23.526 2.925   1.00 41.73  ? 298  LEU   A O   1 
ATOM   3742 C CB  . LEU   A 1 495 ? -16.376 20.540 4.306   1.00 31.33  ? 298  LEU   A CB  1 
ATOM   3743 C CG  . LEU   A 1 495 ? -17.902 20.686 4.206   1.00 31.89  ? 298  LEU   A CG  1 
ATOM   3744 C CD1 . LEU   A 1 495 ? -18.367 20.399 2.769   1.00 29.90  ? 298  LEU   A CD1 1 
ATOM   3745 C CD2 . LEU   A 1 495 ? -18.618 19.755 5.238   1.00 30.69  ? 298  LEU   A CD2 1 
ATOM   3746 N N   . VAL   A 1 496 ? -15.951 23.529 4.940   1.00 40.43  ? 299  VAL   A N   1 
ATOM   3747 C CA  . VAL   A 1 496 ? -16.665 24.709 5.378   1.00 45.55  ? 299  VAL   A CA  1 
ATOM   3748 C C   . VAL   A 1 496 ? -16.176 25.936 4.631   1.00 51.99  ? 299  VAL   A C   1 
ATOM   3749 O O   . VAL   A 1 496 ? -16.971 26.808 4.262   1.00 56.28  ? 299  VAL   A O   1 
ATOM   3750 C CB  . VAL   A 1 496 ? -16.501 24.887 6.891   1.00 45.54  ? 299  VAL   A CB  1 
ATOM   3751 C CG1 . VAL   A 1 496 ? -17.187 26.185 7.333   1.00 51.42  ? 299  VAL   A CG1 1 
ATOM   3752 C CG2 . VAL   A 1 496 ? -17.157 23.700 7.617   1.00 43.12  ? 299  VAL   A CG2 1 
ATOM   3753 N N   . ARG   A 1 497 ? -14.887 26.030 4.342   1.00 52.24  ? 300  ARG   A N   1 
ATOM   3754 C CA  . ARG   A 1 497 ? -14.378 27.209 3.681   1.00 57.33  ? 300  ARG   A CA  1 
ATOM   3755 C C   . ARG   A 1 497 ? -14.551 27.174 2.177   1.00 55.19  ? 300  ARG   A C   1 
ATOM   3756 O O   . ARG   A 1 497 ? -14.568 28.253 1.560   1.00 57.84  ? 300  ARG   A O   1 
ATOM   3757 C CB  . ARG   A 1 497 ? -12.916 27.442 4.023   1.00 64.30  ? 300  ARG   A CB  1 
ATOM   3758 C CG  . ARG   A 1 497 ? -12.558 27.331 5.502   1.00 68.32  ? 300  ARG   A CG  1 
ATOM   3759 C CD  . ARG   A 1 497 ? -11.141 27.855 5.779   1.00 71.69  ? 300  ARG   A CD  1 
ATOM   3760 N NE  . ARG   A 1 497 ? -10.097 26.990 5.222   1.00 74.04  ? 300  ARG   A NE  1 
ATOM   3761 C CZ  . ARG   A 1 497 ? -9.807  26.876 3.922   1.00 75.97  ? 300  ARG   A CZ  1 
ATOM   3762 N NH1 . ARG   A 1 497 ? -10.476 27.565 3.007   1.00 78.16  ? 300  ARG   A NH1 1 
ATOM   3763 N NH2 . ARG   A 1 497 ? -8.839  26.066 3.525   1.00 75.57  ? 300  ARG   A NH2 1 
ATOM   3764 N N   . THR   A 1 498 ? -14.652 26.003 1.576   1.00 48.04  ? 301  THR   A N   1 
ATOM   3765 C CA  . THR   A 1 498 ? -14.884 25.951 0.132   1.00 47.69  ? 301  THR   A CA  1 
ATOM   3766 C C   . THR   A 1 498 ? -16.369 25.987 -0.231  1.00 47.03  ? 301  THR   A C   1 
ATOM   3767 O O   . THR   A 1 498 ? -16.697 26.335 -1.361  1.00 50.53  ? 301  THR   A O   1 
ATOM   3768 C CB  . THR   A 1 498 ? -14.273 24.658 -0.506  1.00 48.09  ? 301  THR   A CB  1 
ATOM   3769 O OG1 . THR   A 1 498 ? -14.851 23.507 0.073   1.00 41.38  ? 301  THR   A OG1 1 
ATOM   3770 C CG2 . THR   A 1 498 ? -12.771 24.602 -0.313  1.00 52.18  ? 301  THR   A CG2 1 
ATOM   3771 N N   . LYS   A 1 499 ? -17.272 25.605 0.681   1.00 43.20  ? 302  LYS   A N   1 
ATOM   3772 C CA  . LYS   A 1 499 ? -18.693 25.582 0.366   1.00 43.20  ? 302  LYS   A CA  1 
ATOM   3773 C C   . LYS   A 1 499 ? -19.526 26.379 1.372   1.00 45.26  ? 302  LYS   A C   1 
ATOM   3774 O O   . LYS   A 1 499 ? -20.750 26.167 1.454   1.00 45.20  ? 302  LYS   A O   1 
ATOM   3775 C CB  . LYS   A 1 499 ? -19.214 24.120 0.285   1.00 41.27  ? 302  LYS   A CB  1 
ATOM   3776 C CG  . LYS   A 1 499 ? -18.392 23.215 -0.632  1.00 39.18  ? 302  LYS   A CG  1 
ATOM   3777 C CD  . LYS   A 1 499 ? -18.389 23.690 -2.073  1.00 44.12  ? 302  LYS   A CD  1 
ATOM   3778 C CE  . LYS   A 1 499 ? -17.745 22.643 -3.006  1.00 47.19  ? 302  LYS   A CE  1 
ATOM   3779 N NZ  . LYS   A 1 499 ? -17.574 23.064 -4.453  1.00 52.84  ? 302  LYS   A NZ  1 
ATOM   3780 N N   . ARG   A 1 500 ? -18.905 27.302 2.115   1.00 45.67  ? 303  ARG   A N   1 
ATOM   3781 C CA  . ARG   A 1 500 ? -19.611 28.080 3.144   1.00 44.57  ? 303  ARG   A CA  1 
ATOM   3782 C C   . ARG   A 1 500 ? -20.942 28.620 2.638   1.00 46.20  ? 303  ARG   A C   1 
ATOM   3783 O O   . ARG   A 1 500 ? -22.004 28.325 3.188   1.00 42.50  ? 303  ARG   A O   1 
ATOM   3784 C CB  . ARG   A 1 500 ? -18.717 29.221 3.644   1.00 41.39  ? 303  ARG   A CB  1 
ATOM   3785 C CG  . ARG   A 1 500 ? -19.444 30.158 4.591   1.00 44.41  ? 303  ARG   A CG  1 
ATOM   3786 C CD  . ARG   A 1 500 ? -18.487 30.999 5.454   1.00 47.67  ? 303  ARG   A CD  1 
ATOM   3787 N NE  . ARG   A 1 500 ? -17.805 30.202 6.507   1.00 47.41  ? 303  ARG   A NE  1 
ATOM   3788 C CZ  . ARG   A 1 500 ? -18.367 29.830 7.663   1.00 43.98  ? 303  ARG   A CZ  1 
ATOM   3789 N NH1 . ARG   A 1 500 ? -17.649 29.087 8.550   1.00 46.92  ? 303  ARG   A NH1 1 
ATOM   3790 N NH2 . ARG   A 1 500 ? -19.640 30.125 7.926   1.00 36.82  ? 303  ARG   A NH2 1 
ATOM   3791 N N   . ASP   A 1 501 ? -20.898 29.437 1.589   1.00 50.83  ? 304  ASP   A N   1 
ATOM   3792 C CA  . ASP   A 1 501 ? -22.118 30.123 1.133   1.00 53.10  ? 304  ASP   A CA  1 
ATOM   3793 C C   . ASP   A 1 501 ? -23.153 29.112 0.601   1.00 52.51  ? 304  ASP   A C   1 
ATOM   3794 O O   . ASP   A 1 501 ? -24.359 29.240 0.849   1.00 50.79  ? 304  ASP   A O   1 
ATOM   3795 C CB  . ASP   A 1 501 ? -21.769 31.166 0.056   1.00 55.37  ? 304  ASP   A CB  1 
ATOM   3796 C CG  . ASP   A 1 501 ? -20.876 32.289 0.584   1.00 57.28  ? 304  ASP   A CG  1 
ATOM   3797 O OD1 . ASP   A 1 501 ? -20.913 32.602 1.813   1.00 57.84  ? 304  ASP   A OD1 1 
ATOM   3798 O OD2 . ASP   A 1 501 ? -20.118 32.868 -0.218  1.00 59.77  ? 304  ASP   A OD2 1 
ATOM   3799 N N   . TRP   A 1 502 ? -22.703 28.093 -0.126  1.00 52.83  ? 305  TRP   A N   1 
ATOM   3800 C CA  . TRP   A 1 502 ? -23.633 27.035 -0.565  1.00 49.27  ? 305  TRP   A CA  1 
ATOM   3801 C C   . TRP   A 1 502 ? -24.314 26.355 0.618   1.00 47.82  ? 305  TRP   A C   1 
ATOM   3802 O O   . TRP   A 1 502 ? -25.548 26.203 0.649   1.00 47.40  ? 305  TRP   A O   1 
ATOM   3803 C CB  . TRP   A 1 502 ? -22.899 26.038 -1.426  1.00 46.62  ? 305  TRP   A CB  1 
ATOM   3804 C CG  . TRP   A 1 502 ? -23.793 25.040 -2.066  1.00 48.21  ? 305  TRP   A CG  1 
ATOM   3805 C CD1 . TRP   A 1 502 ? -24.447 25.157 -3.264  1.00 50.10  ? 305  TRP   A CD1 1 
ATOM   3806 C CD2 . TRP   A 1 502 ? -24.159 23.740 -1.520  1.00 46.14  ? 305  TRP   A CD2 1 
ATOM   3807 N NE1 . TRP   A 1 502 ? -25.177 24.020 -3.509  1.00 52.43  ? 305  TRP   A NE1 1 
ATOM   3808 C CE2 . TRP   A 1 502 ? -25.014 23.128 -2.463  1.00 50.40  ? 305  TRP   A CE2 1 
ATOM   3809 C CE3 . TRP   A 1 502 ? -23.828 23.050 -0.352  1.00 40.64  ? 305  TRP   A CE3 1 
ATOM   3810 C CZ2 . TRP   A 1 502 ? -25.569 21.828 -2.262  1.00 47.68  ? 305  TRP   A CZ2 1 
ATOM   3811 C CZ3 . TRP   A 1 502 ? -24.357 21.784 -0.149  1.00 39.98  ? 305  TRP   A CZ3 1 
ATOM   3812 C CH2 . TRP   A 1 502 ? -25.230 21.172 -1.107  1.00 42.38  ? 305  TRP   A CH2 1 
ATOM   3813 N N   . LEU   A 1 503 ? -23.528 25.955 1.622   1.00 47.38  ? 306  LEU   A N   1 
ATOM   3814 C CA  . LEU   A 1 503 ? -24.089 25.242 2.768   1.00 46.60  ? 306  LEU   A CA  1 
ATOM   3815 C C   . LEU   A 1 503 ? -25.106 26.121 3.523   1.00 44.65  ? 306  LEU   A C   1 
ATOM   3816 O O   . LEU   A 1 503 ? -26.208 25.678 3.870   1.00 43.02  ? 306  LEU   A O   1 
ATOM   3817 C CB  . LEU   A 1 503 ? -22.955 24.784 3.719   1.00 43.86  ? 306  LEU   A CB  1 
ATOM   3818 C CG  . LEU   A 1 503 ? -21.953 23.745 3.205   1.00 39.27  ? 306  LEU   A CG  1 
ATOM   3819 C CD1 . LEU   A 1 503 ? -20.654 23.875 3.993   1.00 36.57  ? 306  LEU   A CD1 1 
ATOM   3820 C CD2 . LEU   A 1 503 ? -22.540 22.315 3.298   1.00 33.26  ? 306  LEU   A CD2 1 
ATOM   3821 N N   . VAL   A 1 504 ? -24.739 27.359 3.817   1.00 45.57  ? 307  VAL   A N   1 
ATOM   3822 C CA  . VAL   A 1 504 ? -25.698 28.271 4.444   1.00 45.65  ? 307  VAL   A CA  1 
ATOM   3823 C C   . VAL   A 1 504 ? -26.963 28.421 3.603   1.00 44.47  ? 307  VAL   A C   1 
ATOM   3824 O O   . VAL   A 1 504 ? -28.072 28.389 4.131   1.00 45.73  ? 307  VAL   A O   1 
ATOM   3825 C CB  . VAL   A 1 504 ? -25.046 29.626 4.704   1.00 49.22  ? 307  VAL   A CB  1 
ATOM   3826 C CG1 . VAL   A 1 504 ? -26.122 30.673 4.954   1.00 50.33  ? 307  VAL   A CG1 1 
ATOM   3827 C CG2 . VAL   A 1 504 ? -24.104 29.528 5.938   1.00 50.05  ? 307  VAL   A CG2 1 
ATOM   3828 N N   . LYS   A 1 505 ? -26.819 28.538 2.280   1.00 43.68  ? 308  LYS   A N   1 
ATOM   3829 C CA  . LYS   A 1 505 ? -27.990 28.575 1.414   1.00 48.98  ? 308  LYS   A CA  1 
ATOM   3830 C C   . LYS   A 1 505 ? -28.832 27.297 1.481   1.00 51.19  ? 308  LYS   A C   1 
ATOM   3831 O O   . LYS   A 1 505 ? -30.041 27.340 1.206   1.00 54.12  ? 308  LYS   A O   1 
ATOM   3832 C CB  . LYS   A 1 505 ? -27.573 28.820 -0.015  1.00 55.98  ? 308  LYS   A CB  1 
ATOM   3833 C CG  . LYS   A 1 505 ? -28.771 28.987 -0.968  1.00 64.03  ? 308  LYS   A CG  1 
ATOM   3834 C CD  . LYS   A 1 505 ? -28.449 29.881 -2.188  1.00 68.47  ? 308  LYS   A CD  1 
ATOM   3835 C CE  . LYS   A 1 505 ? -29.716 30.550 -2.763  1.00 71.27  ? 308  LYS   A CE  1 
ATOM   3836 N NZ  . LYS   A 1 505 ? -29.575 30.948 -4.201  1.00 74.25  ? 308  LYS   A NZ  1 
ATOM   3837 N N   . GLN   A 1 506 ? -28.225 26.131 1.815   1.00 49.36  ? 309  GLN   A N   1 
ATOM   3838 C CA  . GLN   A 1 506 ? -29.000 24.884 1.946   1.00 49.02  ? 309  GLN   A CA  1 
ATOM   3839 C C   . GLN   A 1 506 ? -29.625 24.721 3.328   1.00 49.92  ? 309  GLN   A C   1 
ATOM   3840 O O   . GLN   A 1 506 ? -30.189 23.666 3.604   1.00 53.20  ? 309  GLN   A O   1 
ATOM   3841 C CB  . GLN   A 1 506 ? -28.115 23.652 1.664   1.00 46.75  ? 309  GLN   A CB  1 
ATOM   3842 C CG  . GLN   A 1 506 ? -27.354 23.709 0.337   1.00 49.94  ? 309  GLN   A CG  1 
ATOM   3843 C CD  . GLN   A 1 506 ? -28.281 24.001 -0.850  1.00 55.97  ? 309  GLN   A CD  1 
ATOM   3844 O OE1 . GLN   A 1 506 ? -29.366 23.396 -0.993  1.00 54.29  ? 309  GLN   A OE1 1 
ATOM   3845 N NE2 . GLN   A 1 506 ? -27.838 24.886 -1.732  1.00 60.88  ? 309  GLN   A NE2 1 
ATOM   3846 N N   . ARG   A 1 507 ? -29.575 25.744 4.183   1.00 50.57  ? 310  ARG   A N   1 
ATOM   3847 C CA  . ARG   A 1 507 ? -29.963 25.623 5.591   1.00 50.44  ? 310  ARG   A CA  1 
ATOM   3848 C C   . ARG   A 1 507 ? -29.065 24.596 6.282   1.00 48.91  ? 310  ARG   A C   1 
ATOM   3849 O O   . ARG   A 1 507 ? -29.506 23.785 7.118   1.00 49.65  ? 310  ARG   A O   1 
ATOM   3850 C CB  . ARG   A 1 507 ? -31.445 25.271 5.749   1.00 54.51  ? 310  ARG   A CB  1 
ATOM   3851 C CG  . ARG   A 1 507 ? -32.410 26.397 5.304   1.00 58.61  ? 310  ARG   A CG  1 
ATOM   3852 C CD  . ARG   A 1 507 ? -33.871 26.067 5.618   1.00 62.27  ? 310  ARG   A CD  1 
ATOM   3853 N NE  . ARG   A 1 507 ? -34.307 24.819 4.996   1.00 64.53  ? 310  ARG   A NE  1 
ATOM   3854 C CZ  . ARG   A 1 507 ? -34.592 23.702 5.683   1.00 67.03  ? 310  ARG   A CZ  1 
ATOM   3855 N NH1 . ARG   A 1 507 ? -34.500 23.687 7.017   1.00 68.44  ? 310  ARG   A NH1 1 
ATOM   3856 N NH2 . ARG   A 1 507 ? -34.966 22.592 5.056   1.00 67.30  ? 310  ARG   A NH2 1 
ATOM   3857 N N   . GLY   A 1 508 ? -27.793 24.607 5.906   1.00 45.25  ? 311  GLY   A N   1 
ATOM   3858 C CA  . GLY   A 1 508 ? -26.835 23.766 6.602   1.00 42.97  ? 311  GLY   A CA  1 
ATOM   3859 C C   . GLY   A 1 508 ? -27.236 22.310 6.609   1.00 40.54  ? 311  GLY   A C   1 
ATOM   3860 O O   . GLY   A 1 508 ? -27.836 21.818 5.662   1.00 40.69  ? 311  GLY   A O   1 
ATOM   3861 N N   . TRP   A 1 509 ? -26.926 21.624 7.702   1.00 39.05  ? 312  TRP   A N   1 
ATOM   3862 C CA  . TRP   A 1 509 ? -27.158 20.204 7.811   1.00 37.92  ? 312  TRP   A CA  1 
ATOM   3863 C C   . TRP   A 1 509 ? -28.642 19.836 7.890   1.00 42.52  ? 312  TRP   A C   1 
ATOM   3864 O O   . TRP   A 1 509 ? -28.988 18.650 7.759   1.00 42.54  ? 312  TRP   A O   1 
ATOM   3865 C CB  . TRP   A 1 509 ? -26.378 19.667 9.007   1.00 33.61  ? 312  TRP   A CB  1 
ATOM   3866 C CG  . TRP   A 1 509 ? -24.903 19.670 8.727   1.00 36.00  ? 312  TRP   A CG  1 
ATOM   3867 C CD1 . TRP   A 1 509 ? -23.995 20.609 9.101   1.00 36.57  ? 312  TRP   A CD1 1 
ATOM   3868 C CD2 . TRP   A 1 509 ? -24.166 18.686 7.930   1.00 37.02  ? 312  TRP   A CD2 1 
ATOM   3869 N NE1 . TRP   A 1 509 ? -22.730 20.277 8.614   1.00 38.40  ? 312  TRP   A NE1 1 
ATOM   3870 C CE2 . TRP   A 1 509 ? -22.814 19.100 7.901   1.00 37.71  ? 312  TRP   A CE2 1 
ATOM   3871 C CE3 . TRP   A 1 509 ? -24.529 17.490 7.280   1.00 37.46  ? 312  TRP   A CE3 1 
ATOM   3872 C CZ2 . TRP   A 1 509 ? -21.828 18.381 7.233   1.00 36.89  ? 312  TRP   A CZ2 1 
ATOM   3873 C CZ3 . TRP   A 1 509 ? -23.530 16.754 6.623   1.00 34.30  ? 312  TRP   A CZ3 1 
ATOM   3874 C CH2 . TRP   A 1 509 ? -22.208 17.191 6.603   1.00 34.43  ? 312  TRP   A CH2 1 
ATOM   3875 N N   . ASP   A 1 510 ? -29.538 20.807 8.095   1.00 44.78  ? 313  ASP   A N   1 
ATOM   3876 C CA  . ASP   A 1 510 ? -30.954 20.507 7.942   1.00 44.52  ? 313  ASP   A CA  1 
ATOM   3877 C C   . ASP   A 1 510 ? -31.280 20.171 6.487   1.00 44.01  ? 313  ASP   A C   1 
ATOM   3878 O O   . ASP   A 1 510 ? -32.072 19.249 6.226   1.00 44.70  ? 313  ASP   A O   1 
ATOM   3879 C CB  . ASP   A 1 510 ? -31.812 21.666 8.429   1.00 47.98  ? 313  ASP   A CB  1 
ATOM   3880 C CG  . ASP   A 1 510 ? -31.840 21.768 9.921   1.00 51.54  ? 313  ASP   A CG  1 
ATOM   3881 O OD1 . ASP   A 1 510 ? -31.837 20.714 10.598  1.00 52.52  ? 313  ASP   A OD1 1 
ATOM   3882 O OD2 . ASP   A 1 510 ? -31.858 22.902 10.443  1.00 54.51  ? 313  ASP   A OD2 1 
ATOM   3883 N N   . GLY   A 1 511 ? -30.658 20.881 5.533   1.00 39.38  ? 314  GLY   A N   1 
ATOM   3884 C CA  . GLY   A 1 511 ? -30.846 20.540 4.140   1.00 38.87  ? 314  GLY   A CA  1 
ATOM   3885 C C   . GLY   A 1 511 ? -30.325 19.150 3.817   1.00 38.57  ? 314  GLY   A C   1 
ATOM   3886 O O   . GLY   A 1 511 ? -30.989 18.364 3.128   1.00 39.64  ? 314  GLY   A O   1 
ATOM   3887 N N   . PHE   A 1 512 ? -29.127 18.835 4.291   1.00 36.69  ? 315  PHE   A N   1 
ATOM   3888 C CA  . PHE   A 1 512 ? -28.595 17.485 4.157   1.00 36.78  ? 315  PHE   A CA  1 
ATOM   3889 C C   . PHE   A 1 512 ? -29.638 16.444 4.536   1.00 40.80  ? 315  PHE   A C   1 
ATOM   3890 O O   . PHE   A 1 512 ? -29.999 15.578 3.727   1.00 42.74  ? 315  PHE   A O   1 
ATOM   3891 C CB  . PHE   A 1 512 ? -27.345 17.335 5.031   1.00 36.33  ? 315  PHE   A CB  1 
ATOM   3892 C CG  . PHE   A 1 512 ? -26.682 15.963 4.936   1.00 37.88  ? 315  PHE   A CG  1 
ATOM   3893 C CD1 . PHE   A 1 512 ? -26.073 15.549 3.761   1.00 38.59  ? 315  PHE   A CD1 1 
ATOM   3894 C CD2 . PHE   A 1 512 ? -26.675 15.119 6.050   1.00 37.25  ? 315  PHE   A CD2 1 
ATOM   3895 C CE1 . PHE   A 1 512 ? -25.413 14.292 3.700   1.00 40.08  ? 315  PHE   A CE1 1 
ATOM   3896 C CE2 . PHE   A 1 512 ? -26.037 13.869 5.993   1.00 39.74  ? 315  PHE   A CE2 1 
ATOM   3897 C CZ  . PHE   A 1 512 ? -25.397 13.457 4.805   1.00 38.93  ? 315  PHE   A CZ  1 
ATOM   3898 N N   . VAL   A 1 513 ? -30.144 16.525 5.768   1.00 42.98  ? 316  VAL   A N   1 
ATOM   3899 C CA  . VAL   A 1 513 ? -31.141 15.562 6.240   1.00 46.02  ? 316  VAL   A CA  1 
ATOM   3900 C C   . VAL   A 1 513 ? -32.362 15.549 5.327   1.00 50.84  ? 316  VAL   A C   1 
ATOM   3901 O O   . VAL   A 1 513 ? -32.925 14.481 5.024   1.00 53.07  ? 316  VAL   A O   1 
ATOM   3902 C CB  . VAL   A 1 513 ? -31.536 15.887 7.696   1.00 46.73  ? 316  VAL   A CB  1 
ATOM   3903 C CG1 . VAL   A 1 513 ? -32.738 15.054 8.140   1.00 46.08  ? 316  VAL   A CG1 1 
ATOM   3904 C CG2 . VAL   A 1 513 ? -30.346 15.671 8.628   1.00 44.73  ? 316  VAL   A CG2 1 
ATOM   3905 N N   . GLU   A 1 514 ? -32.810 16.728 4.880   1.00 53.45  ? 317  GLU   A N   1 
ATOM   3906 C CA  . GLU   A 1 514 ? -34.004 16.783 4.034   1.00 57.23  ? 317  GLU   A CA  1 
ATOM   3907 C C   . GLU   A 1 514 ? -33.713 16.247 2.630   1.00 56.55  ? 317  GLU   A C   1 
ATOM   3908 O O   . GLU   A 1 514 ? -34.554 15.567 2.023   1.00 55.98  ? 317  GLU   A O   1 
ATOM   3909 C CB  . GLU   A 1 514 ? -34.524 18.217 3.962   1.00 60.43  ? 317  GLU   A CB  1 
ATOM   3910 C CG  . GLU   A 1 514 ? -35.809 18.349 3.191   1.00 68.05  ? 317  GLU   A CG  1 
ATOM   3911 C CD  . GLU   A 1 514 ? -36.872 19.097 3.986   1.00 76.43  ? 317  GLU   A CD  1 
ATOM   3912 O OE1 . GLU   A 1 514 ? -36.499 19.946 4.855   1.00 77.16  ? 317  GLU   A OE1 1 
ATOM   3913 O OE2 . GLU   A 1 514 ? -38.081 18.846 3.745   1.00 81.82  ? 317  GLU   A OE2 1 
ATOM   3914 N N   . PHE   A 1 515 ? -32.514 16.539 2.104   1.00 54.13  ? 318  PHE   A N   1 
ATOM   3915 C CA  . PHE   A 1 515 ? -32.189 16.134 0.747   1.00 54.28  ? 318  PHE   A CA  1 
ATOM   3916 C C   . PHE   A 1 515 ? -32.182 14.601 0.608   1.00 56.62  ? 318  PHE   A C   1 
ATOM   3917 O O   . PHE   A 1 515 ? -32.655 14.058 -0.402  1.00 57.48  ? 318  PHE   A O   1 
ATOM   3918 C CB  . PHE   A 1 515 ? -30.839 16.744 0.347   1.00 50.93  ? 318  PHE   A CB  1 
ATOM   3919 C CG  . PHE   A 1 515 ? -30.378 16.333 -1.022  1.00 54.29  ? 318  PHE   A CG  1 
ATOM   3920 C CD1 . PHE   A 1 515 ? -30.776 17.036 -2.141  1.00 54.16  ? 318  PHE   A CD1 1 
ATOM   3921 C CD2 . PHE   A 1 515 ? -29.575 15.168 -1.192  1.00 54.08  ? 318  PHE   A CD2 1 
ATOM   3922 C CE1 . PHE   A 1 515 ? -30.377 16.632 -3.406  1.00 56.08  ? 318  PHE   A CE1 1 
ATOM   3923 C CE2 . PHE   A 1 515 ? -29.169 14.783 -2.466  1.00 53.51  ? 318  PHE   A CE2 1 
ATOM   3924 C CZ  . PHE   A 1 515 ? -29.574 15.507 -3.568  1.00 54.16  ? 318  PHE   A CZ  1 
ATOM   3925 N N   . PHE   A 1 516 ? -31.659 13.894 1.611   1.00 57.42  ? 319  PHE   A N   1 
ATOM   3926 C CA  . PHE   A 1 516 ? -31.575 12.433 1.575   1.00 61.10  ? 319  PHE   A CA  1 
ATOM   3927 C C   . PHE   A 1 516 ? -32.712 11.769 2.337   1.00 65.87  ? 319  PHE   A C   1 
ATOM   3928 O O   . PHE   A 1 516 ? -32.612 10.592 2.688   1.00 61.10  ? 319  PHE   A O   1 
ATOM   3929 C CB  . PHE   A 1 516 ? -30.238 11.956 2.129   1.00 56.06  ? 319  PHE   A CB  1 
ATOM   3930 C CG  . PHE   A 1 516 ? -29.085 12.189 1.201   1.00 51.74  ? 319  PHE   A CG  1 
ATOM   3931 C CD1 . PHE   A 1 516 ? -28.987 11.478 0.012   1.00 51.02  ? 319  PHE   A CD1 1 
ATOM   3932 C CD2 . PHE   A 1 516 ? -28.119 13.116 1.505   1.00 48.09  ? 319  PHE   A CD2 1 
ATOM   3933 C CE1 . PHE   A 1 516 ? -27.918 11.674 -0.838  1.00 50.12  ? 319  PHE   A CE1 1 
ATOM   3934 C CE2 . PHE   A 1 516 ? -27.042 13.357 0.645   1.00 48.61  ? 319  PHE   A CE2 1 
ATOM   3935 C CZ  . PHE   A 1 516 ? -26.946 12.623 -0.539  1.00 50.00  ? 319  PHE   A CZ  1 
ATOM   3936 N N   . HIS   A 1 517 ? -33.781 12.508 2.615   1.00 74.57  ? 320  HIS   A N   1 
ATOM   3937 C CA  . HIS   A 1 517 ? -34.918 11.922 3.307   1.00 82.22  ? 320  HIS   A CA  1 
ATOM   3938 C C   . HIS   A 1 517 ? -35.555 10.839 2.446   1.00 85.66  ? 320  HIS   A C   1 
ATOM   3939 O O   . HIS   A 1 517 ? -35.717 11.003 1.230   1.00 89.14  ? 320  HIS   A O   1 
ATOM   3940 C CB  . HIS   A 1 517 ? -35.954 12.997 3.647   1.00 88.55  ? 320  HIS   A CB  1 
ATOM   3941 C CG  . HIS   A 1 517 ? -37.012 12.529 4.595   1.00 94.13  ? 320  HIS   A CG  1 
ATOM   3942 N ND1 . HIS   A 1 517 ? -38.292 12.221 4.185   1.00 98.86  ? 320  HIS   A ND1 1 
ATOM   3943 C CD2 . HIS   A 1 517 ? -36.980 12.310 5.932   1.00 94.33  ? 320  HIS   A CD2 1 
ATOM   3944 C CE1 . HIS   A 1 517 ? -39.005 11.835 5.229   1.00 100.76 ? 320  HIS   A CE1 1 
ATOM   3945 N NE2 . HIS   A 1 517 ? -38.233 11.881 6.302   1.00 97.91  ? 320  HIS   A NE2 1 
ATOM   3946 N N   . VAL   A 1 518 ? -35.913 9.731  3.090   1.00 84.53  ? 321  VAL   A N   1 
ATOM   3947 C CA  . VAL   A 1 518 ? -36.632 8.652  2.421   1.00 85.27  ? 321  VAL   A CA  1 
ATOM   3948 C C   . VAL   A 1 518 ? -38.103 9.032  2.244   1.00 86.89  ? 321  VAL   A C   1 
ATOM   3949 O O   . VAL   A 1 518 ? -38.552 9.339  1.137   1.00 88.17  ? 321  VAL   A O   1 
ATOM   3950 C CB  . VAL   A 1 518 ? -36.500 7.340  3.215   1.00 83.92  ? 321  VAL   A CB  1 
ATOM   3951 C CG1 . VAL   A 1 518 ? -37.029 7.533  4.638   1.00 83.85  ? 321  VAL   A CG1 1 
ATOM   3952 C CG2 . VAL   A 1 518 ? -37.244 6.200  2.502   1.00 86.42  ? 321  VAL   A CG2 1 
HETATM 3953 C C1  . GLC   B 2 .   ? -11.234 49.527 13.290  1.00 39.58  ? 1    GLC   B C1  1 
HETATM 3954 C C2  . GLC   B 2 .   ? -10.861 48.592 14.461  1.00 40.98  ? 1    GLC   B C2  1 
HETATM 3955 C C3  . GLC   B 2 .   ? -11.065 47.083 14.121  1.00 39.49  ? 1    GLC   B C3  1 
HETATM 3956 C C4  . GLC   B 2 .   ? -12.446 46.860 13.550  1.00 36.36  ? 1    GLC   B C4  1 
HETATM 3957 C C5  . GLC   B 2 .   ? -12.693 47.832 12.355  1.00 35.40  ? 1    GLC   B C5  1 
HETATM 3958 C C6  . GLC   B 2 .   ? -14.132 47.664 11.889  1.00 32.49  ? 1    GLC   B C6  1 
HETATM 3959 O O1  . GLC   B 2 .   ? -10.278 49.416 12.259  1.00 42.31  ? 1    GLC   B O1  1 
HETATM 3960 O O2  . GLC   B 2 .   ? -9.501  48.775 14.822  1.00 40.26  ? 1    GLC   B O2  1 
HETATM 3961 O O3  . GLC   B 2 .   ? -10.933 46.353 15.293  1.00 38.10  ? 1    GLC   B O3  1 
HETATM 3962 O O4  . GLC   B 2 .   ? -12.539 45.512 13.133  1.00 36.87  ? 1    GLC   B O4  1 
HETATM 3963 O O5  . GLC   B 2 .   ? -12.505 49.208 12.743  1.00 36.68  ? 1    GLC   B O5  1 
HETATM 3964 O O6  . GLC   B 2 .   ? -14.275 48.141 10.578  1.00 34.33  ? 1    GLC   B O6  1 
HETATM 3965 C C1  . GLC   B 2 .   ? -13.323 44.660 13.945  1.00 35.64  ? 2    GLC   B C1  1 
HETATM 3966 C C2  . GLC   B 2 .   ? -12.592 43.359 14.071  1.00 36.16  ? 2    GLC   B C2  1 
HETATM 3967 C C3  . GLC   B 2 .   ? -12.487 42.717 12.678  1.00 38.48  ? 2    GLC   B C3  1 
HETATM 3968 C C4  . GLC   B 2 .   ? -13.909 42.498 12.152  1.00 36.74  ? 2    GLC   B C4  1 
HETATM 3969 C C5  . GLC   B 2 .   ? -14.596 43.882 12.080  1.00 36.00  ? 2    GLC   B C5  1 
HETATM 3970 C C6  . GLC   B 2 .   ? -16.046 43.583 11.632  1.00 34.82  ? 2    GLC   B C6  1 
HETATM 3971 O O2  . GLC   B 2 .   ? -11.280 43.597 14.587  1.00 32.94  ? 2    GLC   B O2  1 
HETATM 3972 O O3  . GLC   B 2 .   ? -11.838 41.458 12.755  1.00 39.70  ? 2    GLC   B O3  1 
HETATM 3973 O O4  . GLC   B 2 .   ? -13.905 41.925 10.864  1.00 34.56  ? 2    GLC   B O4  1 
HETATM 3974 O O5  . GLC   B 2 .   ? -14.596 44.498 13.374  1.00 34.25  ? 2    GLC   B O5  1 
HETATM 3975 O O6  . GLC   B 2 .   ? -16.680 44.821 11.457  1.00 35.94  ? 2    GLC   B O6  1 
HETATM 3976 C C1  . A1LXV C 3 .   ? -11.469 9.095  -3.984  1.00 45.84  ? 401  A1LXV A C1  1 
HETATM 3977 C C10 . A1LXV C 3 .   ? -11.257 8.883  -7.332  1.00 53.28  ? 401  A1LXV A C10 1 
HETATM 3978 C C11 . A1LXV C 3 .   ? -13.417 8.334  -6.865  1.00 51.37  ? 401  A1LXV A C11 1 
HETATM 3979 C C12 . A1LXV C 3 .   ? -9.845  9.423  -7.208  1.00 53.78  ? 401  A1LXV A C12 1 
HETATM 3980 C C13 . A1LXV C 3 .   ? -17.045 8.738  -6.666  1.00 67.39  ? 401  A1LXV A C13 1 
HETATM 3981 C C14 . A1LXV C 3 .   ? -17.456 8.327  -5.251  1.00 71.50  ? 401  A1LXV A C14 1 
HETATM 3982 C C15 . A1LXV C 3 .   ? -18.704 8.571  -4.824  1.00 75.07  ? 401  A1LXV A C15 1 
HETATM 3983 C C16 . A1LXV C 3 .   ? -19.715 9.247  -5.756  1.00 78.08  ? 401  A1LXV A C16 1 
HETATM 3984 C C17 . A1LXV C 3 .   ? -19.349 9.606  -6.984  1.00 73.62  ? 401  A1LXV A C17 1 
HETATM 3985 C C18 . A1LXV C 3 .   ? -17.923 9.335  -7.480  1.00 69.86  ? 401  A1LXV A C18 1 
HETATM 3986 C C19 . A1LXV C 3 .   ? -21.734 10.790 -5.657  1.00 87.77  ? 401  A1LXV A C19 1 
HETATM 3987 C C2  . A1LXV C 3 .   ? -11.333 9.660  -2.694  1.00 44.55  ? 401  A1LXV A C2  1 
HETATM 3988 C C20 . A1LXV C 3 .   ? -23.271 10.603 -5.663  1.00 90.49  ? 401  A1LXV A C20 1 
HETATM 3989 C C21 . A1LXV C 3 .   ? -22.767 9.348  -3.501  1.00 90.92  ? 401  A1LXV A C21 1 
HETATM 3990 C C22 . A1LXV C 3 .   ? -21.740 8.623  -4.372  1.00 88.77  ? 401  A1LXV A C22 1 
HETATM 3991 C C23 . A1LXV C 3 .   ? -13.985 7.139  -9.052  1.00 54.55  ? 401  A1LXV A C23 1 
HETATM 3992 C C24 . A1LXV C 3 .   ? -24.930 9.937  -1.134  1.00 100.77 ? 401  A1LXV A C24 1 
HETATM 3993 C C25 . A1LXV C 3 .   ? -26.313 8.246  -2.364  1.00 98.92  ? 401  A1LXV A C25 1 
HETATM 3994 C C26 . A1LXV C 3 .   ? -14.282 11.648 -6.698  1.00 63.31  ? 401  A1LXV A C26 1 
HETATM 3995 C C27 . A1LXV C 3 .   ? -13.657 12.723 -7.630  1.00 71.34  ? 401  A1LXV A C27 1 
HETATM 3996 C C28 . A1LXV C 3 .   ? -14.902 12.416 -9.398  1.00 73.61  ? 401  A1LXV A C28 1 
HETATM 3997 C C29 . A1LXV C 3 .   ? -14.995 11.823 -10.814 1.00 75.24  ? 401  A1LXV A C29 1 
HETATM 3998 C C3  . A1LXV C 3 .   ? -12.018 10.854 -2.378  1.00 45.94  ? 401  A1LXV A C3  1 
HETATM 3999 C C30 . A1LXV C 3 .   ? -12.758 12.438 -11.073 1.00 76.05  ? 401  A1LXV A C30 1 
HETATM 4000 C C31 . A1LXV C 3 .   ? -12.816 12.953 -9.620  1.00 74.06  ? 401  A1LXV A C31 1 
HETATM 4001 C C32 . A1LXV C 3 .   ? -15.175 13.915 -5.063  1.00 52.22  ? 401  A1LXV A C32 1 
HETATM 4002 C C33 . A1LXV C 3 .   ? -13.838 13.612 -2.296  1.00 45.81  ? 401  A1LXV A C33 1 
HETATM 4003 C C34 . A1LXV C 3 .   ? -12.761 14.737 -2.375  1.00 43.17  ? 401  A1LXV A C34 1 
HETATM 4004 C C35 . A1LXV C 3 .   ? -11.331 14.175 -2.088  1.00 41.00  ? 401  A1LXV A C35 1 
HETATM 4005 C C36 . A1LXV C 3 .   ? -9.940  13.445 -0.193  1.00 40.29  ? 401  A1LXV A C36 1 
HETATM 4006 C C37 . A1LXV C 3 .   ? -9.918  13.139 0.929   1.00 42.13  ? 401  A1LXV A C37 1 
HETATM 4007 C C38 . A1LXV C 3 .   ? -8.669  12.591 1.620   1.00 41.78  ? 401  A1LXV A C38 1 
HETATM 4008 C C39 . A1LXV C 3 .   ? -7.462  12.397 0.945   1.00 44.36  ? 401  A1LXV A C39 1 
HETATM 4009 C C4  . A1LXV C 3 .   ? -12.803 11.451 -3.336  1.00 47.71  ? 401  A1LXV A C4  1 
HETATM 4010 C C40 . A1LXV C 3 .   ? -7.529  12.836 -0.585  1.00 41.44  ? 401  A1LXV A C40 1 
HETATM 4011 C C41 . A1LXV C 3 .   ? -8.918  13.376 -1.027  1.00 39.32  ? 401  A1LXV A C41 1 
HETATM 4012 C C42 . A1LXV C 3 .   ? -10.953 13.168 1.867   1.00 44.15  ? 401  A1LXV A C42 1 
HETATM 4013 C C43 . A1LXV C 3 .   ? -10.919 12.850 2.959   1.00 43.27  ? 401  A1LXV A C43 1 
HETATM 4014 C C44 . A1LXV C 3 .   ? -10.127 12.491 3.513   1.00 42.90  ? 401  A1LXV A C44 1 
HETATM 4015 C C45 . A1LXV C 3 .   ? -8.997  12.273 3.145   1.00 41.77  ? 401  A1LXV A C45 1 
HETATM 4016 C C46 . A1LXV C 3 .   ? -14.759 8.229  -6.143  1.00 55.15  ? 401  A1LXV A C46 1 
HETATM 4017 C C5  . A1LXV C 3 .   ? -12.928 10.814 -4.709  1.00 49.52  ? 401  A1LXV A C5  1 
HETATM 4018 C C6  . A1LXV C 3 .   ? -12.245 9.647  -4.966  1.00 47.81  ? 401  A1LXV A C6  1 
HETATM 4019 C C7  . A1LXV C 3 .   ? -13.644 12.602 -3.486  1.00 48.20  ? 401  A1LXV A C7  1 
HETATM 4020 C C8  . A1LXV C 3 .   ? -14.232 12.799 -4.618  1.00 50.91  ? 401  A1LXV A C8  1 
HETATM 4021 C C9  . A1LXV C 3 .   ? -12.314 8.967  -6.360  1.00 50.52  ? 401  A1LXV A C9  1 
HETATM 4022 N N1  . A1LXV C 3 .   ? -13.819 11.788 -5.321  1.00 52.94  ? 401  A1LXV A N1  1 
HETATM 4023 N N2  . A1LXV C 3 .   ? -11.746 8.195  -8.410  1.00 54.45  ? 401  A1LXV A N2  1 
HETATM 4024 N N3  . A1LXV C 3 .   ? -13.097 7.855  -8.142  1.00 52.94  ? 401  A1LXV A N3  1 
HETATM 4025 N N4  . A1LXV C 3 .   ? -21.082 9.541  -5.262  1.00 85.39  ? 401  A1LXV A N4  1 
HETATM 4026 N N5  . A1LXV C 3 .   ? -23.694 10.100 -4.338  1.00 92.95  ? 401  A1LXV A N5  1 
HETATM 4027 N N6  . A1LXV C 3 .   ? -25.617 9.527  -2.345  1.00 99.36  ? 401  A1LXV A N6  1 
HETATM 4028 N N7  . A1LXV C 3 .   ? -13.696 12.289 -8.890  1.00 73.57  ? 401  A1LXV A N7  1 
HETATM 4029 O O1  . A1LXV C 3 .   ? -26.273 10.000 -4.849  1.00 99.26  ? 401  A1LXV A O1  1 
HETATM 4030 O O2  . A1LXV C 3 .   ? -25.603 11.811 -3.678  1.00 97.49  ? 401  A1LXV A O2  1 
HETATM 4031 O O3  . A1LXV C 3 .   ? -14.002 12.287 -11.682 1.00 76.47  ? 401  A1LXV A O3  1 
HETATM 4032 O O4  . A1LXV C 3 .   ? -16.312 13.587 -5.518  1.00 54.30  ? 401  A1LXV A O4  1 
HETATM 4033 O O5  . A1LXV C 3 .   ? -14.826 15.127 -4.992  1.00 49.41  ? 401  A1LXV A O5  1 
HETATM 4034 O O6  . A1LXV C 3 .   ? -11.182 13.943 -0.677  1.00 42.05  ? 401  A1LXV A O6  1 
HETATM 4035 O O7  . A1LXV C 3 .   ? -15.717 8.465  -7.127  1.00 60.51  ? 401  A1LXV A O7  1 
HETATM 4036 S S1  . A1LXV C 3 .   ? -25.312 10.379 -3.805  1.00 97.47  ? 401  A1LXV A S1  1 
HETATM 4037 H H1  . A1LXV C 3 .   ? -11.008 8.310  -4.173  1.00 55.01  ? 401  A1LXV A H1  1 
HETATM 4038 H H5  . A1LXV C 3 .   ? -9.340  9.153  -7.952  1.00 64.54  ? 401  A1LXV A H5  1 
HETATM 4039 H H6  . A1LXV C 3 .   ? -9.451  9.090  -6.424  1.00 64.54  ? 401  A1LXV A H6  1 
HETATM 4040 H H4  . A1LXV C 3 .   ? -9.871  10.361 -7.171  1.00 64.54  ? 401  A1LXV A H4  1 
HETATM 4041 H H7  . A1LXV C 3 .   ? -16.843 7.911  -4.689  1.00 85.80  ? 401  A1LXV A H7  1 
HETATM 4042 H H8  . A1LXV C 3 .   ? -18.955 8.330  -3.962  1.00 90.09  ? 401  A1LXV A H8  1 
HETATM 4043 H H9  . A1LXV C 3 .   ? -19.961 10.024 -7.546  1.00 88.34  ? 401  A1LXV A H9  1 
HETATM 4044 H H10 . A1LXV C 3 .   ? -17.671 9.583  -8.340  1.00 83.84  ? 401  A1LXV A H10 1 
HETATM 4045 H H12 . A1LXV C 3 .   ? -21.505 11.467 -5.046  1.00 105.32 ? 401  A1LXV A H12 1 
HETATM 4046 H H11 . A1LXV C 3 .   ? -21.446 11.033 -6.517  1.00 105.32 ? 401  A1LXV A H11 1 
HETATM 4047 H H2  . A1LXV C 3 .   ? -10.796 9.248  -2.058  1.00 53.47  ? 401  A1LXV A H2  1 
HETATM 4048 H H13 . A1LXV C 3 .   ? -23.510 9.982  -6.326  1.00 108.58 ? 401  A1LXV A H13 1 
HETATM 4049 H H14 . A1LXV C 3 .   ? -23.688 11.427 -5.835  1.00 108.58 ? 401  A1LXV A H14 1 
HETATM 4050 H H16 . A1LXV C 3 .   ? -22.320 9.940  -2.925  1.00 109.11 ? 401  A1LXV A H16 1 
HETATM 4051 H H15 . A1LXV C 3 .   ? -23.247 8.717  -2.998  1.00 109.11 ? 401  A1LXV A H15 1 
HETATM 4052 H H17 . A1LXV C 3 .   ? -21.099 8.218  -3.819  1.00 106.52 ? 401  A1LXV A H17 1 
HETATM 4053 H H18 . A1LXV C 3 .   ? -22.178 7.964  -4.879  1.00 106.52 ? 401  A1LXV A H18 1 
HETATM 4054 H H20 . A1LXV C 3 .   ? -13.475 6.702  -9.708  1.00 65.46  ? 401  A1LXV A H20 1 
HETATM 4055 H H19 . A1LXV C 3 .   ? -14.568 7.749  -9.464  1.00 65.46  ? 401  A1LXV A H19 1 
HETATM 4056 H H21 . A1LXV C 3 .   ? -14.484 6.506  -8.569  1.00 65.46  ? 401  A1LXV A H21 1 
HETATM 4057 H H22 . A1LXV C 3 .   ? -24.544 10.783 -1.265  1.00 120.92 ? 401  A1LXV A H22 1 
HETATM 4058 H H24 . A1LXV C 3 .   ? -24.258 9.314  -0.930  1.00 120.92 ? 401  A1LXV A H24 1 
HETATM 4059 H H23 . A1LXV C 3 .   ? -25.544 9.979  -0.425  1.00 120.92 ? 401  A1LXV A H23 1 
HETATM 4060 H H25 . A1LXV C 3 .   ? -27.205 8.378  -2.627  1.00 118.70 ? 401  A1LXV A H25 1 
HETATM 4061 H H26 . A1LXV C 3 .   ? -26.293 7.865  -1.506  1.00 118.70 ? 401  A1LXV A H26 1 
HETATM 4062 H H27 . A1LXV C 3 .   ? -25.890 7.669  -2.972  1.00 118.70 ? 401  A1LXV A H27 1 
HETATM 4063 H H29 . A1LXV C 3 .   ? -14.044 10.797 -7.014  1.00 75.97  ? 401  A1LXV A H29 1 
HETATM 4064 H H28 . A1LXV C 3 .   ? -15.217 11.738 -6.715  1.00 75.97  ? 401  A1LXV A H28 1 
HETATM 4065 H H31 . A1LXV C 3 .   ? -14.144 13.522 -7.558  1.00 85.61  ? 401  A1LXV A H31 1 
HETATM 4066 H H30 . A1LXV C 3 .   ? -12.765 12.876 -7.378  1.00 85.61  ? 401  A1LXV A H30 1 
HETATM 4067 H H33 . A1LXV C 3 .   ? -15.514 11.970 -8.841  1.00 88.34  ? 401  A1LXV A H33 1 
HETATM 4068 H H32 . A1LXV C 3 .   ? -15.122 13.328 -9.434  1.00 88.34  ? 401  A1LXV A H32 1 
HETATM 4069 H H35 . A1LXV C 3 .   ? -14.924 10.889 -10.752 1.00 90.28  ? 401  A1LXV A H35 1 
HETATM 4070 H H34 . A1LXV C 3 .   ? -15.833 12.045 -11.175 1.00 90.28  ? 401  A1LXV A H34 1 
HETATM 4071 H H3  . A1LXV C 3 .   ? -11.939 11.232 -1.533  1.00 55.13  ? 401  A1LXV A H3  1 
HETATM 4072 H H37 . A1LXV C 3 .   ? -12.254 13.046 -11.580 1.00 91.26  ? 401  A1LXV A H37 1 
HETATM 4073 H H36 . A1LXV C 3 .   ? -12.327 11.604 -11.073 1.00 91.26  ? 401  A1LXV A H36 1 
HETATM 4074 H H38 . A1LXV C 3 .   ? -13.054 13.861 -9.629  1.00 88.87  ? 401  A1LXV A H38 1 
HETATM 4075 H H39 . A1LXV C 3 .   ? -11.967 12.858 -9.231  1.00 88.87  ? 401  A1LXV A H39 1 
HETATM 4076 H H41 . A1LXV C 3 .   ? -13.750 13.154 -1.481  1.00 54.98  ? 401  A1LXV A H41 1 
HETATM 4077 H H40 . A1LXV C 3 .   ? -14.693 13.995 -2.350  1.00 54.98  ? 401  A1LXV A H40 1 
HETATM 4078 H H43 . A1LXV C 3 .   ? -12.963 15.399 -1.740  1.00 51.80  ? 401  A1LXV A H43 1 
HETATM 4079 H H42 . A1LXV C 3 .   ? -12.775 15.114 -3.235  1.00 51.80  ? 401  A1LXV A H42 1 
HETATM 4080 H H44 . A1LXV C 3 .   ? -10.688 14.797 -2.373  1.00 49.20  ? 401  A1LXV A H44 1 
HETATM 4081 H H45 . A1LXV C 3 .   ? -11.213 13.368 -2.553  1.00 49.20  ? 401  A1LXV A H45 1 
HETATM 4082 H H46 . A1LXV C 3 .   ? -6.700  12.048 1.347   1.00 53.23  ? 401  A1LXV A H46 1 
HETATM 4083 H H47 . A1LXV C 3 .   ? -6.803  12.775 -1.161  1.00 49.73  ? 401  A1LXV A H47 1 
HETATM 4084 H H48 . A1LXV C 3 .   ? -9.159  13.119 -1.887  1.00 47.18  ? 401  A1LXV A H48 1 
HETATM 4085 H H49 . A1LXV C 3 .   ? -11.581 13.831 1.698   1.00 52.98  ? 401  A1LXV A H49 1 
HETATM 4086 H H50 . A1LXV C 3 .   ? -11.532 13.313 3.481   1.00 51.93  ? 401  A1LXV A H50 1 
HETATM 4087 H H51 . A1LXV C 3 .   ? -10.393 11.942 4.214   1.00 51.48  ? 401  A1LXV A H51 1 
HETATM 4088 H H52 . A1LXV C 3 .   ? -8.352  11.937 3.723   1.00 50.12  ? 401  A1LXV A H52 1 
HETATM 4089 H H53 . A1LXV C 3 .   ? -14.869 7.372  -5.775  1.00 66.18  ? 401  A1LXV A H53 1 
HETATM 4090 H H54 . A1LXV C 3 .   ? -14.819 8.873  -5.463  1.00 66.18  ? 401  A1LXV A H54 1 
HETATM 4091 O O   . HOH   D 4 .   ? -27.085 56.770 7.592   1.00 46.78  ? 501  HOH   A O   1 
HETATM 4092 O O   . HOH   D 4 .   ? 17.245  47.206 5.444   1.00 68.12  ? 502  HOH   A O   1 
HETATM 4093 O O   . HOH   D 4 .   ? 7.625   14.566 12.350  1.00 62.80  ? 503  HOH   A O   1 
HETATM 4094 O O   . HOH   D 4 .   ? -32.374 12.134 5.603   1.00 49.35  ? 504  HOH   A O   1 
HETATM 4095 O O   . HOH   D 4 .   ? -18.356 12.177 -5.619  1.00 43.25  ? 505  HOH   A O   1 
HETATM 4096 O O   . HOH   D 4 .   ? -16.299 58.713 31.214  1.00 61.60  ? 506  HOH   A O   1 
HETATM 4097 O O   . HOH   D 4 .   ? 1.545   30.360 15.027  1.00 45.75  ? 507  HOH   A O   1 
HETATM 4098 O O   . HOH   D 4 .   ? -34.992 43.737 6.777   1.00 46.26  ? 508  HOH   A O   1 
HETATM 4099 O O   . HOH   D 4 .   ? -21.444 4.321  11.475  1.00 34.12  ? 509  HOH   A O   1 
HETATM 4100 O O   . HOH   D 4 .   ? 0.126   9.971  1.220   1.00 64.17  ? 510  HOH   A O   1 
HETATM 4101 O O   . HOH   D 4 .   ? -25.695 55.411 9.931   1.00 34.77  ? 511  HOH   A O   1 
HETATM 4102 O O   . HOH   D 4 .   ? -34.116 55.012 4.561   1.00 44.72  ? 512  HOH   A O   1 
HETATM 4103 O O   . HOH   D 4 .   ? -18.131 8.714  17.146  1.00 40.91  ? 513  HOH   A O   1 
HETATM 4104 O O   . HOH   D 4 .   ? -39.442 65.213 17.768  1.00 49.71  ? 514  HOH   A O   1 
HETATM 4105 O O   . HOH   D 4 .   ? -18.913 72.669 16.343  1.00 49.96  ? 515  HOH   A O   1 
HETATM 4106 O O   . HOH   D 4 .   ? 16.036  40.886 19.557  1.00 45.83  ? 516  HOH   A O   1 
HETATM 4107 O O   . HOH   D 4 .   ? -9.160  34.561 15.117  1.00 45.11  ? 517  HOH   A O   1 
HETATM 4108 O O   . HOH   D 4 .   ? -20.951 47.218 1.848   1.00 66.18  ? 518  HOH   A O   1 
HETATM 4109 O O   . HOH   D 4 .   ? 11.574  42.057 4.673   1.00 46.84  ? 519  HOH   A O   1 
HETATM 4110 O O   . HOH   D 4 .   ? 3.535   36.701 16.568  1.00 36.15  ? 520  HOH   A O   1 
HETATM 4111 O O   . HOH   D 4 .   ? -13.475 61.432 11.766  1.00 42.34  ? 521  HOH   A O   1 
HETATM 4112 O O   . HOH   D 4 .   ? -37.757 59.053 19.903  1.00 47.19  ? 522  HOH   A O   1 
HETATM 4113 O O   . HOH   D 4 .   ? -10.957 58.443 10.861  1.00 51.74  ? 523  HOH   A O   1 
HETATM 4114 O O   . HOH   D 4 .   ? 12.156  41.139 26.578  1.00 46.44  ? 524  HOH   A O   1 
HETATM 4115 O O   . HOH   D 4 .   ? -14.886 16.622 17.568  1.00 42.06  ? 525  HOH   A O   1 
HETATM 4116 O O   . HOH   D 4 .   ? -22.925 9.578  18.668  1.00 37.44  ? 526  HOH   A O   1 
HETATM 4117 O O   . HOH   D 4 .   ? -37.373 54.478 13.991  1.00 35.37  ? 527  HOH   A O   1 
HETATM 4118 O O   . HOH   D 4 .   ? -5.726  52.006 17.931  1.00 52.24  ? 528  HOH   A O   1 
HETATM 4119 O O   . HOH   D 4 .   ? -11.377 47.299 18.016  1.00 31.43  ? 529  HOH   A O   1 
HETATM 4120 O O   . HOH   D 4 .   ? -21.344 67.474 13.460  1.00 38.20  ? 530  HOH   A O   1 
HETATM 4121 O O   . HOH   D 4 .   ? -36.100 57.040 25.639  1.00 42.51  ? 531  HOH   A O   1 
HETATM 4122 O O   . HOH   D 4 .   ? -15.511 -0.697 -6.287  1.00 49.68  ? 532  HOH   A O   1 
HETATM 4123 O O   . HOH   D 4 .   ? -32.596 63.483 23.132  1.00 51.06  ? 533  HOH   A O   1 
HETATM 4124 O O   . HOH   D 4 .   ? -2.783  6.648  17.919  1.00 50.71  ? 534  HOH   A O   1 
HETATM 4125 O O   . HOH   D 4 .   ? -21.263 65.258 4.016   1.00 43.72  ? 535  HOH   A O   1 
HETATM 4126 O O   . HOH   D 4 .   ? 3.708   32.480 7.943   1.00 43.98  ? 536  HOH   A O   1 
HETATM 4127 O O   . HOH   D 4 .   ? 7.173   51.898 30.452  1.00 52.51  ? 537  HOH   A O   1 
HETATM 4128 O O   . HOH   D 4 .   ? -35.520 62.877 21.865  1.00 53.69  ? 538  HOH   A O   1 
HETATM 4129 O O   . HOH   D 4 .   ? -5.517  52.664 3.414   1.00 43.79  ? 539  HOH   A O   1 
HETATM 4130 O O   . HOH   D 4 .   ? -35.224 71.260 7.075   1.00 49.75  ? 540  HOH   A O   1 
HETATM 4131 O O   . HOH   D 4 .   ? -32.763 52.669 26.664  1.00 62.49  ? 541  HOH   A O   1 
HETATM 4132 O O   . HOH   D 4 .   ? -21.147 0.392  15.088  1.00 54.42  ? 542  HOH   A O   1 
HETATM 4133 O O   . HOH   D 4 .   ? -30.392 60.560 12.601  1.00 39.58  ? 543  HOH   A O   1 
HETATM 4134 O O   . HOH   D 4 .   ? -10.908 66.356 8.713   1.00 58.11  ? 544  HOH   A O   1 
HETATM 4135 O O   . HOH   D 4 .   ? -30.002 44.187 21.610  1.00 49.32  ? 545  HOH   A O   1 
HETATM 4136 O O   . HOH   D 4 .   ? -5.095  57.476 22.736  1.00 41.54  ? 546  HOH   A O   1 
HETATM 4137 O O   . HOH   D 4 .   ? 18.770  48.219 18.466  1.00 50.05  ? 547  HOH   A O   1 
HETATM 4138 O O   . HOH   D 4 .   ? -31.194 60.943 8.079   1.00 37.36  ? 548  HOH   A O   1 
HETATM 4139 O O   . HOH   D 4 .   ? -15.211 30.233 33.093  1.00 52.25  ? 549  HOH   A O   1 
HETATM 4140 O O   . HOH   D 4 .   ? -3.146  54.857 15.485  1.00 39.71  ? 550  HOH   A O   1 
HETATM 4141 O O   . HOH   D 4 .   ? 4.996   32.951 24.681  1.00 53.70  ? 551  HOH   A O   1 
HETATM 4142 O O   . HOH   D 4 .   ? -38.380 55.162 19.585  1.00 52.90  ? 552  HOH   A O   1 
HETATM 4143 O O   . HOH   D 4 .   ? -27.754 36.849 6.766   1.00 39.83  ? 553  HOH   A O   1 
HETATM 4144 O O   . HOH   D 4 .   ? -31.004 54.525 30.190  1.00 50.95  ? 554  HOH   A O   1 
HETATM 4145 O O   . HOH   D 4 .   ? -13.352 55.192 32.456  1.00 58.65  ? 555  HOH   A O   1 
HETATM 4146 O O   . HOH   D 4 .   ? -17.922 47.143 18.666  1.00 38.05  ? 556  HOH   A O   1 
HETATM 4147 O O   . HOH   D 4 .   ? -20.133 19.420 -3.050  1.00 58.42  ? 557  HOH   A O   1 
HETATM 4148 O O   . HOH   D 4 .   ? -12.836 40.881 7.038   1.00 45.64  ? 558  HOH   A O   1 
HETATM 4149 O O   . HOH   D 4 .   ? -24.295 49.956 17.712  1.00 48.57  ? 559  HOH   A O   1 
HETATM 4150 O O   . HOH   D 4 .   ? -23.149 71.025 4.487   1.00 45.11  ? 560  HOH   A O   1 
HETATM 4151 O O   . HOH   D 4 .   ? -16.224 73.397 12.276  1.00 57.24  ? 561  HOH   A O   1 
HETATM 4152 O O   . HOH   D 4 .   ? -25.198 35.873 7.149   1.00 34.41  ? 562  HOH   A O   1 
HETATM 4153 O O   . HOH   D 4 .   ? -26.447 56.241 28.084  1.00 46.37  ? 563  HOH   A O   1 
HETATM 4154 O O   . HOH   D 4 .   ? -26.159 48.510 5.694   1.00 41.43  ? 564  HOH   A O   1 
HETATM 4155 O O   . HOH   D 4 .   ? -24.222 33.105 7.345   1.00 42.59  ? 565  HOH   A O   1 
HETATM 4156 O O   . HOH   D 4 .   ? 3.545   57.947 33.934  1.00 60.65  ? 566  HOH   A O   1 
HETATM 4157 O O   . HOH   D 4 .   ? -16.914 51.925 5.171   1.00 41.80  ? 567  HOH   A O   1 
HETATM 4158 O O   . HOH   D 4 .   ? 2.069   57.984 3.733   1.00 62.20  ? 568  HOH   A O   1 
HETATM 4159 O O   . HOH   D 4 .   ? -17.512 59.128 12.168  1.00 29.26  ? 569  HOH   A O   1 
HETATM 4160 O O   . HOH   D 4 .   ? -31.811 53.403 3.299   1.00 54.32  ? 570  HOH   A O   1 
HETATM 4161 O O   . HOH   D 4 .   ? -21.766 62.497 3.939   1.00 42.09  ? 571  HOH   A O   1 
HETATM 4162 O O   . HOH   D 4 .   ? -38.773 67.101 10.950  1.00 47.04  ? 572  HOH   A O   1 
HETATM 4163 O O   . HOH   D 4 .   ? -36.036 14.752 16.986  1.00 46.62  ? 573  HOH   A O   1 
HETATM 4164 O O   . HOH   D 4 .   ? -18.586 28.640 11.326  1.00 43.89  ? 574  HOH   A O   1 
HETATM 4165 O O   . HOH   D 4 .   ? -23.549 4.250  -3.011  1.00 55.23  ? 575  HOH   A O   1 
HETATM 4166 O O   . HOH   D 4 .   ? -15.544 48.736 20.184  1.00 34.28  ? 576  HOH   A O   1 
HETATM 4167 O O   . HOH   D 4 .   ? 16.034  37.141 13.434  1.00 50.86  ? 577  HOH   A O   1 
HETATM 4168 O O   . HOH   D 4 .   ? -25.492 7.309  18.148  1.00 43.82  ? 578  HOH   A O   1 
HETATM 4169 O O   . HOH   D 4 .   ? -8.208  35.043 11.442  1.00 39.15  ? 579  HOH   A O   1 
HETATM 4170 O O   . HOH   D 4 .   ? -8.298  57.513 10.785  1.00 41.10  ? 580  HOH   A O   1 
HETATM 4171 O O   . HOH   D 4 .   ? -40.138 57.662 13.490  1.00 45.75  ? 581  HOH   A O   1 
HETATM 4172 O O   . HOH   D 4 .   ? -15.805 61.552 12.480  1.00 32.94  ? 582  HOH   A O   1 
HETATM 4173 O O   . HOH   D 4 .   ? -3.849  3.943  18.092  1.00 45.02  ? 583  HOH   A O   1 
HETATM 4174 O O   . HOH   D 4 .   ? -18.994 55.504 11.836  1.00 31.87  ? 584  HOH   A O   1 
HETATM 4175 O O   . HOH   D 4 .   ? -30.283 20.857 0.142   1.00 46.92  ? 585  HOH   A O   1 
HETATM 4176 O O   . HOH   D 4 .   ? -20.883 8.692  17.277  1.00 30.43  ? 586  HOH   A O   1 
HETATM 4177 O O   . HOH   D 4 .   ? -36.059 52.433 15.565  1.00 41.84  ? 587  HOH   A O   1 
HETATM 4178 O O   . HOH   D 4 .   ? -14.667 57.653 20.080  1.00 33.24  ? 588  HOH   A O   1 
HETATM 4179 O O   . HOH   D 4 .   ? -15.658 54.214 3.840   1.00 48.74  ? 589  HOH   A O   1 
HETATM 4180 O O   . HOH   D 4 .   ? -8.255  10.932 17.173  1.00 51.59  ? 590  HOH   A O   1 
HETATM 4181 O O   . HOH   D 4 .   ? -4.981  62.515 21.248  1.00 45.23  ? 591  HOH   A O   1 
HETATM 4182 O O   . HOH   D 4 .   ? -18.518 27.014 14.799  1.00 36.95  ? 592  HOH   A O   1 
HETATM 4183 O O   . HOH   D 4 .   ? -10.059 1.262  5.006   1.00 49.60  ? 593  HOH   A O   1 
HETATM 4184 O O   . HOH   D 4 .   ? -36.037 62.358 7.248   1.00 44.20  ? 594  HOH   A O   1 
HETATM 4185 O O   . HOH   D 4 .   ? -20.937 72.410 13.747  1.00 46.45  ? 595  HOH   A O   1 
HETATM 4186 O O   . HOH   D 4 .   ? -28.977 5.609  10.374  1.00 51.61  ? 596  HOH   A O   1 
HETATM 4187 O O   . HOH   D 4 .   ? -7.495  21.508 5.929   1.00 58.08  ? 597  HOH   A O   1 
HETATM 4188 O O   . HOH   D 4 .   ? -16.731 6.774  18.752  1.00 39.64  ? 598  HOH   A O   1 
HETATM 4189 O O   . HOH   D 4 .   ? 5.031   50.672 31.729  1.00 37.55  ? 599  HOH   A O   1 
HETATM 4190 O O   . HOH   D 4 .   ? -15.140 60.855 30.266  1.00 55.49  ? 600  HOH   A O   1 
HETATM 4191 O O   . HOH   D 4 .   ? 14.353  35.186 12.418  1.00 55.50  ? 601  HOH   A O   1 
HETATM 4192 O O   . HOH   D 4 .   ? 7.408   53.425 5.139   1.00 59.92  ? 602  HOH   A O   1 
HETATM 4193 O O   . HOH   D 4 .   ? -19.019 1.031  6.892   1.00 49.82  ? 603  HOH   A O   1 
HETATM 4194 O O   . HOH   D 4 .   ? -36.891 46.690 18.720  1.00 49.76  ? 604  HOH   A O   1 
HETATM 4195 O O   . HOH   D 4 .   ? -12.462 64.427 7.711   1.00 46.33  ? 605  HOH   A O   1 
HETATM 4196 O O   . HOH   D 4 .   ? -15.311 64.296 25.742  1.00 51.84  ? 606  HOH   A O   1 
HETATM 4197 O O   . HOH   D 4 .   ? 7.482   61.013 20.315  1.00 52.78  ? 607  HOH   A O   1 
HETATM 4198 O O   . HOH   D 4 .   ? 6.527   59.551 8.765   1.00 49.05  ? 608  HOH   A O   1 
HETATM 4199 O O   . HOH   D 4 .   ? -19.988 28.174 -1.428  1.00 51.49  ? 609  HOH   A O   1 
HETATM 4200 O O   . HOH   D 4 .   ? -30.641 53.463 0.833   1.00 56.98  ? 610  HOH   A O   1 
HETATM 4201 O O   . HOH   D 4 .   ? 7.676   30.414 17.267  1.00 58.07  ? 611  HOH   A O   1 
HETATM 4202 O O   . HOH   D 4 .   ? -24.373 70.882 28.253  1.00 46.10  ? 612  HOH   A O   1 
HETATM 4203 O O   . HOH   D 4 .   ? -17.424 56.991 10.268  1.00 33.04  ? 613  HOH   A O   1 
HETATM 4204 O O   . HOH   D 4 .   ? -30.352 22.847 21.318  1.00 57.21  ? 614  HOH   A O   1 
HETATM 4205 O O   . HOH   D 4 .   ? -24.474 25.337 11.415  1.00 47.00  ? 615  HOH   A O   1 
HETATM 4206 O O   . HOH   D 4 .   ? 14.054  38.895 25.989  1.00 66.57  ? 616  HOH   A O   1 
HETATM 4207 O O   . HOH   D 4 .   ? 4.320   43.814 0.414   1.00 46.23  ? 617  HOH   A O   1 
HETATM 4208 O O   . HOH   D 4 .   ? -15.255 50.374 6.750   1.00 47.81  ? 618  HOH   A O   1 
HETATM 4209 O O   . HOH   D 4 .   ? -26.857 72.057 28.716  1.00 32.61  ? 619  HOH   A O   1 
HETATM 4210 O O   . HOH   D 4 .   ? -27.091 64.682 7.453   1.00 47.92  ? 620  HOH   A O   1 
HETATM 4211 O O   . HOH   D 4 .   ? -8.936  6.001  -7.456  1.00 56.47  ? 621  HOH   A O   1 
HETATM 4212 O O   . HOH   D 4 .   ? -20.080 2.184  13.153  1.00 47.07  ? 622  HOH   A O   1 
HETATM 4213 O O   . HOH   D 4 .   ? -29.220 51.474 -2.944  1.00 55.46  ? 623  HOH   A O   1 
HETATM 4214 O O   . HOH   D 4 .   ? -20.330 38.056 23.102  1.00 52.91  ? 624  HOH   A O   1 
HETATM 4215 O O   . HOH   D 4 .   ? -17.740 19.709 -4.334  1.00 48.38  ? 625  HOH   A O   1 
HETATM 4216 O O   . HOH   D 4 .   ? -37.271 43.148 8.736   1.00 60.42  ? 626  HOH   A O   1 
HETATM 4217 O O   . HOH   D 4 .   ? 10.017  41.317 2.318   1.00 59.69  ? 627  HOH   A O   1 
HETATM 4218 O O   . HOH   D 4 .   ? -14.535 50.884 9.336   1.00 36.69  ? 628  HOH   A O   1 
HETATM 4219 O O   . HOH   D 4 .   ? -8.593  47.306 11.653  1.00 43.35  ? 629  HOH   A O   1 
HETATM 4220 O O   . HOH   D 4 .   ? -21.707 32.394 6.535   1.00 49.89  ? 630  HOH   A O   1 
HETATM 4221 O O   . HOH   D 4 .   ? -27.053 35.098 3.285   1.00 51.06  ? 631  HOH   A O   1 
HETATM 4222 O O   . HOH   D 4 .   ? -39.333 72.696 9.361   1.00 57.12  ? 632  HOH   A O   1 
HETATM 4223 O O   . HOH   D 4 .   ? -28.896 35.854 1.492   1.00 56.28  ? 633  HOH   A O   1 
HETATM 4224 O O   . HOH   D 4 .   ? -19.568 72.670 11.613  1.00 52.09  ? 634  HOH   A O   1 
HETATM 4225 O O   . HOH   D 4 .   ? -37.943 57.933 24.080  1.00 57.89  ? 635  HOH   A O   1 
HETATM 4226 O O   . HOH   D 4 .   ? -7.179  12.500 19.296  1.00 50.55  ? 636  HOH   A O   1 
HETATM 4227 O O   . HOH   D 4 .   ? -29.764 62.698 6.838   1.00 49.96  ? 637  HOH   A O   1 
HETATM 4228 O O   . HOH   D 4 .   ? -12.753 46.604 8.824   1.00 36.37  ? 638  HOH   A O   1 
HETATM 4229 O O   . HOH   D 4 .   ? -10.772 55.599 32.766  1.00 42.38  ? 639  HOH   A O   1 
HETATM 4230 O O   . HOH   D 4 .   ? -38.765 60.164 22.393  1.00 51.80  ? 640  HOH   A O   1 
HETATM 4231 O O   . HOH   D 4 .   ? -20.333 62.120 1.834   1.00 50.08  ? 641  HOH   A O   1 
HETATM 4232 O O   . HOH   D 4 .   ? -11.337 -4.347 -9.864  1.00 44.11  ? 642  HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . LYS A 2   ? 0.8011 0.9818 0.8433 0.1497  0.0398  -0.2430 -195 LYS A N   
2    C CA  . LYS A 2   ? 0.8168 1.0114 0.8304 0.1454  0.0496  -0.2347 -195 LYS A CA  
3    C C   . LYS A 2   ? 0.8267 1.0185 0.8286 0.1315  0.0593  -0.2086 -195 LYS A C   
4    O O   . LYS A 2   ? 0.8547 1.0691 0.8400 0.1284  0.0719  -0.1996 -195 LYS A O   
5    C CB  . LYS A 2   ? 0.8391 1.0139 0.8420 0.1452  0.0412  -0.2373 -195 LYS A CB  
6    C CG  . LYS A 2   ? 0.8957 1.0771 0.9109 0.1592  0.0316  -0.2658 -195 LYS A CG  
7    C CD  . LYS A 2   ? 0.9195 1.0888 0.9219 0.1591  0.0250  -0.2692 -195 LYS A CD  
8    C CE  . LYS A 2   ? 0.9537 1.1514 0.9518 0.1735  0.0229  -0.2964 -195 LYS A CE  
9    N NZ  . LYS A 2   ? 0.9614 1.1987 0.9332 0.1768  0.0377  -0.2935 -195 LYS A NZ  
10   N N   . ILE A 3   ? 0.7814 0.9464 0.7933 0.1237  0.0533  -0.1961 -194 ILE A N   
11   C CA  . ILE A 3   ? 0.7207 0.8805 0.7252 0.1111  0.0599  -0.1742 -194 ILE A CA  
12   C C   . ILE A 3   ? 0.7079 0.8914 0.7265 0.1107  0.0680  -0.1735 -194 ILE A C   
13   O O   . ILE A 3   ? 0.7016 0.8889 0.7408 0.1174  0.0631  -0.1847 -194 ILE A O   
14   C CB  . ILE A 3   ? 0.6668 0.7924 0.6756 0.1047  0.0498  -0.1632 -194 ILE A CB  
15   C CG1 . ILE A 3   ? 0.6612 0.7658 0.6558 0.1032  0.0442  -0.1609 -194 ILE A CG1 
16   C CG2 . ILE A 3   ? 0.6208 0.7434 0.6276 0.0933  0.0548  -0.1450 -194 ILE A CG2 
17   C CD1 . ILE A 3   ? 0.6532 0.7266 0.6528 0.0990  0.0345  -0.1514 -194 ILE A CD1 
18   N N   . GLU A 4   ? 0.7234 0.9231 0.7339 0.1029  0.0804  -0.1599 -193 GLU A N   
19   C CA  . GLU A 4   ? 0.7570 0.9825 0.7834 0.1019  0.0896  -0.1586 -193 GLU A CA  
20   C C   . GLU A 4   ? 0.7227 0.9331 0.7666 0.0947  0.0840  -0.1507 -193 GLU A C   
21   O O   . GLU A 4   ? 0.7031 0.8903 0.7407 0.0858  0.0798  -0.1379 -193 GLU A O   
22   C CB  . GLU A 4   ? 0.8424 1.0928 0.8580 0.0962  0.1058  -0.1453 -193 GLU A CB  
23   N N   . GLU A 5   ? 0.7383 0.9629 0.8048 0.0996  0.0831  -0.1598 -192 GLU A N   
24   C CA  . GLU A 5   ? 0.7720 0.9872 0.8570 0.0953  0.0765  -0.1557 -192 GLU A CA  
25   C C   . GLU A 5   ? 0.7804 1.0122 0.8751 0.0849  0.0870  -0.1436 -192 GLU A C   
26   O O   . GLU A 5   ? 0.7850 1.0430 0.8793 0.0833  0.1010  -0.1404 -192 GLU A O   
27   C CB  . GLU A 5   ? 0.8046 1.0283 0.9119 0.1064  0.0696  -0.1717 -192 GLU A CB  
28   C CG  . GLU A 5   ? 0.8245 1.0410 0.9509 0.1041  0.0613  -0.1685 -192 GLU A CG  
29   C CD  . GLU A 5   ? 0.8622 1.0909 1.0123 0.1157  0.0556  -0.1838 -192 GLU A CD  
30   O OE1 . GLU A 5   ? 0.8714 1.1125 1.0419 0.1146  0.0547  -0.1841 -192 GLU A OE1 
31   O OE2 . GLU A 5   ? 0.8826 1.1089 1.0330 0.1261  0.0514  -0.1964 -192 GLU A OE2 
32   N N   . GLY A 6   ? 0.7832 1.0011 0.8884 0.0781  0.0801  -0.1368 -191 GLY A N   
33   C CA  . GLY A 6   ? 0.7727 1.0033 0.8931 0.0676  0.0877  -0.1269 -191 GLY A CA  
34   C C   . GLY A 6   ? 0.7514 0.9701 0.8585 0.0562  0.0927  -0.1108 -191 GLY A C   
35   O O   . GLY A 6   ? 0.7164 0.9491 0.8375 0.0473  0.1022  -0.1012 -191 GLY A O   
36   N N   . LYS A 7   ? 0.7385 0.9320 0.8217 0.0561  0.0866  -0.1072 -190 LYS A N   
37   C CA  . LYS A 7   ? 0.7109 0.8905 0.7816 0.0462  0.0896  -0.0927 -190 LYS A CA  
38   C C   . LYS A 7   ? 0.6588 0.8081 0.7094 0.0483  0.0779  -0.0929 -190 LYS A C   
39   O O   . LYS A 7   ? 0.6471 0.7874 0.6956 0.0568  0.0687  -0.1026 -190 LYS A O   
40   C CB  . LYS A 7   ? 0.7268 0.9230 0.7860 0.0441  0.1041  -0.0839 -190 LYS A CB  
41   C CG  . LYS A 7   ? 0.7564 0.9517 0.7915 0.0532  0.1039  -0.0906 -190 LYS A CG  
42   C CD  . LYS A 7   ? 0.8149 1.0334 0.8385 0.0529  0.1188  -0.0821 -190 LYS A CD  
43   C CE  . LYS A 7   ? 0.8716 1.0746 0.8787 0.0448  0.1210  -0.0655 -190 LYS A CE  
44   N NZ  . LYS A 7   ? 0.9197 1.1166 0.8990 0.0517  0.1185  -0.0693 -190 LYS A NZ  
45   N N   . LEU A 8   ? 0.5972 0.7311 0.6351 0.0406  0.0787  -0.0815 -189 LEU A N   
46   C CA  . LEU A 8   ? 0.5581 0.6652 0.5776 0.0416  0.0693  -0.0800 -189 LEU A CA  
47   C C   . LEU A 8   ? 0.6057 0.7068 0.6055 0.0375  0.0755  -0.0703 -189 LEU A C   
48   O O   . LEU A 8   ? 0.6545 0.7600 0.6574 0.0291  0.0829  -0.0592 -189 LEU A O   
49   C CB  . LEU A 8   ? 0.5123 0.6046 0.5388 0.0372  0.0602  -0.0773 -189 LEU A CB  
50   C CG  . LEU A 8   ? 0.5022 0.5944 0.5415 0.0438  0.0498  -0.0863 -189 LEU A CG  
51   C CD1 . LEU A 8   ? 0.4682 0.5491 0.5109 0.0404  0.0409  -0.0839 -189 LEU A CD1 
52   C CD2 . LEU A 8   ? 0.4804 0.5620 0.5093 0.0534  0.0433  -0.0918 -189 LEU A CD2 
53   N N   . VAL A 9   ? 0.5882 0.6796 0.5703 0.0435  0.0720  -0.0745 -188 VAL A N   
54   C CA  . VAL A 9   ? 0.5515 0.6343 0.5137 0.0409  0.0748  -0.0668 -188 VAL A CA  
55   C C   . VAL A 9   ? 0.5350 0.5904 0.4883 0.0400  0.0644  -0.0651 -188 VAL A C   
56   O O   . VAL A 9   ? 0.5176 0.5635 0.4728 0.0461  0.0560  -0.0728 -188 VAL A O   
57   C CB  . VAL A 9   ? 0.5461 0.6422 0.4963 0.0490  0.0785  -0.0744 -188 VAL A CB  
58   C CG1 . VAL A 9   ? 0.5059 0.5957 0.4350 0.0472  0.0808  -0.0666 -188 VAL A CG1 
59   C CG2 . VAL A 9   ? 0.5564 0.6840 0.5158 0.0514  0.0896  -0.0766 -188 VAL A CG2 
60   N N   . ILE A 10  ? 0.5173 0.5610 0.4625 0.0329  0.0653  -0.0543 -187 ILE A N   
61   C CA  . ILE A 10  ? 0.5409 0.5616 0.4780 0.0317  0.0570  -0.0517 -187 ILE A CA  
62   C C   . ILE A 10  ? 0.5525 0.5655 0.4722 0.0302  0.0591  -0.0457 -187 ILE A C   
63   O O   . ILE A 10  ? 0.5676 0.5885 0.4836 0.0259  0.0667  -0.0376 -187 ILE A O   
64   C CB  . ILE A 10  ? 0.5574 0.5715 0.5040 0.0253  0.0542  -0.0466 -187 ILE A CB  
65   C CG1 . ILE A 10  ? 0.5836 0.6083 0.5487 0.0273  0.0515  -0.0533 -187 ILE A CG1 
66   C CG2 . ILE A 10  ? 0.5339 0.5278 0.4708 0.0257  0.0462  -0.0445 -187 ILE A CG2 
67   C CD1 . ILE A 10  ? 0.5768 0.6002 0.5553 0.0208  0.0490  -0.0508 -187 ILE A CD1 
68   N N   . TRP A 11  ? 0.5406 0.5382 0.4513 0.0338  0.0522  -0.0485 -186 TRP A N   
69   C CA  . TRP A 11  ? 0.5227 0.5109 0.4186 0.0326  0.0521  -0.0438 -186 TRP A CA  
70   C C   . TRP A 11  ? 0.5132 0.4829 0.4071 0.0284  0.0471  -0.0374 -186 TRP A C   
71   O O   . TRP A 11  ? 0.5110 0.4723 0.4099 0.0306  0.0410  -0.0397 -186 TRP A O   
72   C CB  . TRP A 11  ? 0.5560 0.5424 0.4467 0.0397  0.0480  -0.0529 -186 TRP A CB  
73   C CG  . TRP A 11  ? 0.5869 0.5934 0.4747 0.0449  0.0529  -0.0604 -186 TRP A CG  
74   C CD1 . TRP A 11  ? 0.5926 0.6199 0.4821 0.0441  0.0617  -0.0581 -186 TRP A CD1 
75   C CD2 . TRP A 11  ? 0.6014 0.6120 0.4855 0.0527  0.0493  -0.0724 -186 TRP A CD2 
76   N NE1 . TRP A 11  ? 0.6035 0.6492 0.4873 0.0516  0.0645  -0.0674 -186 TRP A NE1 
77   C CE2 . TRP A 11  ? 0.6171 0.6528 0.4978 0.0573  0.0562  -0.0778 -186 TRP A CE2 
78   C CE3 . TRP A 11  ? 0.5933 0.5900 0.4792 0.0564  0.0408  -0.0797 -186 TRP A CE3 
79   C CZ2 . TRP A 11  ? 0.6166 0.6648 0.4936 0.0667  0.0538  -0.0927 -186 TRP A CZ2 
80   C CZ3 . TRP A 11  ? 0.5790 0.5857 0.4645 0.0645  0.0380  -0.0941 -186 TRP A CZ3 
81   C CH2 . TRP A 11  ? 0.5898 0.6225 0.4699 0.0701  0.0440  -0.1017 -186 TRP A CH2 
82   N N   . ILE A 12  ? 0.5335 0.4984 0.4201 0.0232  0.0498  -0.0289 -185 ILE A N   
83   C CA  . ILE A 12  ? 0.5137 0.4625 0.3972 0.0202  0.0454  -0.0241 -185 ILE A CA  
84   C C   . ILE A 12  ? 0.5363 0.4804 0.4083 0.0182  0.0474  -0.0178 -185 ILE A C   
85   O O   . ILE A 12  ? 0.5373 0.4923 0.4053 0.0177  0.0533  -0.0143 -185 ILE A O   
86   C CB  . ILE A 12  ? 0.5008 0.4494 0.3953 0.0154  0.0451  -0.0215 -185 ILE A CB  
87   C CG1 . ILE A 12  ? 0.5103 0.4450 0.4013 0.0151  0.0392  -0.0202 -185 ILE A CG1 
88   C CG2 . ILE A 12  ? 0.5069 0.4618 0.4065 0.0093  0.0518  -0.0141 -185 ILE A CG2 
89   C CD1 . ILE A 12  ? 0.5340 0.4703 0.4369 0.0123  0.0366  -0.0219 -185 ILE A CD1 
90   N N   . ASN A 13  ? 0.5689 0.4989 0.4355 0.0180  0.0428  -0.0159 -184 ASN A N   
91   C CA  . ASN A 13  ? 0.5756 0.5002 0.4320 0.0172  0.0431  -0.0112 -184 ASN A CA  
92   C C   . ASN A 13  ? 0.5713 0.4964 0.4288 0.0117  0.0473  -0.0018 -184 ASN A C   
93   O O   . ASN A 13  ? 0.5678 0.4910 0.4359 0.0077  0.0476  0.0001  -184 ASN A O   
94   C CB  . ASN A 13  ? 0.5843 0.4949 0.4381 0.0183  0.0375  -0.0116 -184 ASN A CB  
95   C CG  . ASN A 13  ? 0.6151 0.5224 0.4601 0.0198  0.0362  -0.0107 -184 ASN A CG  
96   O OD1 . ASN A 13  ? 0.6167 0.5319 0.4578 0.0234  0.0364  -0.0155 -184 ASN A OD1 
97   N ND2 . ASN A 13  ? 0.6083 0.5055 0.4510 0.0178  0.0343  -0.0060 -184 ASN A ND2 
98   N N   . GLY A 14  ? 0.5621 0.4895 0.4104 0.0120  0.0497  0.0038  -183 GLY A N   
99   C CA  . GLY A 14  ? 0.5818 0.5110 0.4326 0.0075  0.0544  0.0154  -183 GLY A CA  
100  C C   . GLY A 14  ? 0.6212 0.5356 0.4787 0.0033  0.0512  0.0195  -183 GLY A C   
101  O O   . GLY A 14  ? 0.6627 0.5770 0.5287 -0.0011 0.0546  0.0289  -183 GLY A O   
102  N N   . ASP A 15  ? 0.6081 0.5115 0.4638 0.0049  0.0451  0.0133  -182 ASP A N   
103  C CA  . ASP A 15  ? 0.5841 0.4762 0.4463 0.0023  0.0419  0.0148  -182 ASP A CA  
104  C C   . ASP A 15  ? 0.5469 0.4389 0.4217 0.0007  0.0398  0.0089  -182 ASP A C   
105  O O   . ASP A 15  ? 0.5945 0.4792 0.4755 -0.0002 0.0361  0.0068  -182 ASP A O   
106  C CB  . ASP A 15  ? 0.6012 0.4842 0.4547 0.0055  0.0372  0.0121  -182 ASP A CB  
107  C CG  . ASP A 15  ? 0.6583 0.5424 0.5078 0.0096  0.0346  0.0048  -182 ASP A CG  
108  O OD1 . ASP A 15  ? 0.6759 0.5670 0.5288 0.0105  0.0357  0.0010  -182 ASP A OD1 
109  O OD2 . ASP A 15  ? 0.6628 0.5409 0.5083 0.0119  0.0316  0.0037  -182 ASP A OD2 
110  N N   . LYS A 16  ? 0.5167 0.4180 0.3961 0.0012  0.0413  0.0049  -181 LYS A N   
111  C CA  . LYS A 16  ? 0.5432 0.4469 0.4348 0.0007  0.0383  -0.0019 -181 LYS A CA  
112  C C   . LYS A 16  ? 0.5513 0.4618 0.4608 -0.0048 0.0421  0.0010  -181 LYS A C   
113  O O   . LYS A 16  ? 0.5422 0.4571 0.4532 -0.0078 0.0484  0.0100  -181 LYS A O   
114  C CB  . LYS A 16  ? 0.5372 0.4466 0.4247 0.0056  0.0362  -0.0086 -181 LYS A CB  
115  C CG  . LYS A 16  ? 0.5292 0.4321 0.4039 0.0108  0.0328  -0.0098 -181 LYS A CG  
116  C CD  . LYS A 16  ? 0.5159 0.4102 0.3877 0.0110  0.0295  -0.0090 -181 LYS A CD  
117  C CE  . LYS A 16  ? 0.5164 0.4078 0.3805 0.0163  0.0265  -0.0097 -181 LYS A CE  
118  N NZ  . LYS A 16  ? 0.4982 0.3854 0.3558 0.0176  0.0277  -0.0066 -181 LYS A NZ  
119  N N   . GLY A 17  ? 0.5744 0.4876 0.4988 -0.0057 0.0382  -0.0064 -180 GLY A N   
120  C CA  . GLY A 17  ? 0.5430 0.4622 0.4906 -0.0116 0.0408  -0.0049 -180 GLY A CA  
121  C C   . GLY A 17  ? 0.5412 0.4749 0.4947 -0.0122 0.0462  -0.0042 -180 GLY A C   
122  O O   . GLY A 17  ? 0.5473 0.4885 0.5154 -0.0124 0.0434  -0.0121 -180 GLY A O   
123  N N   . TYR A 18  ? 0.5538 0.4935 0.4973 -0.0122 0.0539  0.0047  -179 TYR A N   
124  C CA  . TYR A 18  ? 0.5433 0.4994 0.4905 -0.0113 0.0597  0.0042  -179 TYR A CA  
125  C C   . TYR A 18  ? 0.5312 0.4976 0.5048 -0.0182 0.0655  0.0101  -179 TYR A C   
126  O O   . TYR A 18  ? 0.4898 0.4707 0.4746 -0.0181 0.0685  0.0063  -179 TYR A O   
127  C CB  . TYR A 18  ? 0.5714 0.5337 0.4990 -0.0075 0.0655  0.0097  -179 TYR A CB  
128  C CG  . TYR A 18  ? 0.6161 0.5757 0.5373 -0.0100 0.0704  0.0231  -179 TYR A CG  
129  C CD1 . TYR A 18  ? 0.6214 0.5928 0.5541 -0.0145 0.0797  0.0362  -179 TYR A CD1 
130  C CD2 . TYR A 18  ? 0.6419 0.5885 0.5464 -0.0074 0.0660  0.0239  -179 TYR A CD2 
131  C CE1 . TYR A 18  ? 0.6155 0.5853 0.5416 -0.0157 0.0841  0.0508  -179 TYR A CE1 
132  C CE2 . TYR A 18  ? 0.6389 0.5837 0.5378 -0.0089 0.0696  0.0366  -179 TYR A CE2 
133  C CZ  . TYR A 18  ? 0.6257 0.5821 0.5343 -0.0126 0.0784  0.0502  -179 TYR A CZ  
134  O OH  . TYR A 18  ? 0.6691 0.6246 0.5708 -0.0127 0.0817  0.0643  -179 TYR A OH  
135  N N   . ASN A 19  ? 0.5295 0.4894 0.5161 -0.0244 0.0677  0.0200  -178 ASN A N   
136  C CA  . ASN A 19  ? 0.5723 0.5402 0.5911 -0.0319 0.0723  0.0255  -178 ASN A CA  
137  C C   . ASN A 19  ? 0.5501 0.5175 0.5894 -0.0326 0.0633  0.0099  -178 ASN A C   
138  O O   . ASN A 19  ? 0.5414 0.5223 0.6014 -0.0350 0.0656  0.0069  -178 ASN A O   
139  C CB  . ASN A 19  ? 0.5901 0.5484 0.6230 -0.0381 0.0751  0.0398  -178 ASN A CB  
140  C CG  . ASN A 19  ? 0.5979 0.5619 0.6133 -0.0371 0.0848  0.0574  -178 ASN A CG  
141  O OD1 . ASN A 19  ? 0.6202 0.6024 0.6290 -0.0353 0.0936  0.0631  -178 ASN A OD1 
142  N ND2 . ASN A 19  ? 0.5841 0.5346 0.5914 -0.0371 0.0830  0.0657  -178 ASN A ND2 
143  N N   . GLY A 20  ? 0.5260 0.4801 0.5592 -0.0295 0.0528  -0.0008 -177 GLY A N   
144  C CA  . GLY A 20  ? 0.4762 0.4327 0.5223 -0.0273 0.0430  -0.0172 -177 GLY A CA  
145  C C   . GLY A 20  ? 0.5073 0.4766 0.5447 -0.0218 0.0427  -0.0243 -177 GLY A C   
146  O O   . GLY A 20  ? 0.5104 0.4907 0.5685 -0.0226 0.0399  -0.0324 -177 GLY A O   
147  N N   . LEU A 21  ? 0.5150 0.4830 0.5235 -0.0158 0.0448  -0.0219 -176 LEU A N   
148  C CA  . LEU A 21  ? 0.4960 0.4752 0.4988 -0.0101 0.0444  -0.0282 -176 LEU A CA  
149  C C   . LEU A 21  ? 0.4882 0.4846 0.5098 -0.0139 0.0527  -0.0249 -176 LEU A C   
150  O O   . LEU A 21  ? 0.4874 0.4953 0.5211 -0.0116 0.0501  -0.0334 -176 LEU A O   
151  C CB  . LEU A 21  ? 0.5201 0.4944 0.4947 -0.0039 0.0457  -0.0259 -176 LEU A CB  
152  C CG  . LEU A 21  ? 0.4772 0.4597 0.4479 0.0031  0.0429  -0.0336 -176 LEU A CG  
153  C CD1 . LEU A 21  ? 0.4420 0.4239 0.4189 0.0069  0.0326  -0.0431 -176 LEU A CD1 
154  C CD2 . LEU A 21  ? 0.4799 0.4555 0.4275 0.0090  0.0431  -0.0321 -176 LEU A CD2 
155  N N   . ALA A 22  ? 0.4906 0.4908 0.5154 -0.0192 0.0631  -0.0118 -175 ALA A N   
156  C CA  . ALA A 22  ? 0.5199 0.5396 0.5633 -0.0226 0.0726  -0.0069 -175 ALA A CA  
157  C C   . ALA A 22  ? 0.5716 0.5973 0.6513 -0.0288 0.0699  -0.0116 -175 ALA A C   
158  O O   . ALA A 22  ? 0.5889 0.6322 0.6860 -0.0293 0.0736  -0.0145 -175 ALA A O   
159  C CB  . ALA A 22  ? 0.5137 0.5382 0.5530 -0.0264 0.0847  0.0106  -175 ALA A CB  
160  N N   . GLU A 23  ? 0.5443 0.5567 0.6382 -0.0332 0.0630  -0.0136 -174 GLU A N   
161  C CA  . GLU A 23  ? 0.5375 0.5553 0.6693 -0.0386 0.0581  -0.0213 -174 GLU A CA  
162  C C   . GLU A 23  ? 0.5268 0.5537 0.6607 -0.0321 0.0487  -0.0389 -174 GLU A C   
163  O O   . GLU A 23  ? 0.5301 0.5720 0.6926 -0.0348 0.0490  -0.0441 -174 GLU A O   
164  C CB  . GLU A 23  ? 0.5637 0.5649 0.7076 -0.0422 0.0501  -0.0243 -174 GLU A CB  
165  C CG  . GLU A 23  ? 0.6415 0.6355 0.7985 -0.0504 0.0589  -0.0061 -174 GLU A CG  
166  C CD  . GLU A 23  ? 0.6562 0.6332 0.8309 -0.0535 0.0496  -0.0115 -174 GLU A CD  
167  O OE1 . GLU A 23  ? 0.6272 0.6027 0.8113 -0.0503 0.0368  -0.0310 -174 GLU A OE1 
168  O OE2 . GLU A 23  ? 0.6565 0.6232 0.8346 -0.0581 0.0548  0.0033  -174 GLU A OE2 
169  N N   . VAL A 24  ? 0.4884 0.5070 0.5935 -0.0231 0.0401  -0.0474 -173 VAL A N   
170  C CA  . VAL A 24  ? 0.4696 0.4976 0.5738 -0.0156 0.0316  -0.0611 -173 VAL A CA  
171  C C   . VAL A 24  ? 0.4922 0.5362 0.5987 -0.0141 0.0396  -0.0583 -173 VAL A C   
172  O O   . VAL A 24  ? 0.4943 0.5526 0.6195 -0.0122 0.0360  -0.0675 -173 VAL A O   
173  C CB  . VAL A 24  ? 0.4665 0.4833 0.5384 -0.0062 0.0234  -0.0657 -173 VAL A CB  
174  C CG1 . VAL A 24  ? 0.4837 0.5108 0.5548 0.0028  0.0139  -0.0778 -173 VAL A CG1 
175  C CG2 . VAL A 24  ? 0.4363 0.4394 0.5049 -0.0071 0.0168  -0.0683 -173 VAL A CG2 
176  N N   . GLY A 25  ? 0.5103 0.5541 0.5995 -0.0144 0.0505  -0.0467 -172 GLY A N   
177  C CA  . GLY A 25  ? 0.5328 0.5943 0.6244 -0.0121 0.0588  -0.0454 -172 GLY A CA  
178  C C   . GLY A 25  ? 0.5370 0.6169 0.6646 -0.0193 0.0654  -0.0436 -172 GLY A C   
179  O O   . GLY A 25  ? 0.5395 0.6364 0.6801 -0.0162 0.0659  -0.0506 -172 GLY A O   
180  N N   . LYS A 26  ? 0.5377 0.6151 0.6853 -0.0289 0.0703  -0.0340 -171 LYS A N   
181  C CA  . LYS A 26  ? 0.5677 0.6633 0.7536 -0.0366 0.0780  -0.0296 -171 LYS A CA  
182  C C   . LYS A 26  ? 0.5311 0.6329 0.7461 -0.0365 0.0664  -0.0463 -171 LYS A C   
183  O O   . LYS A 26  ? 0.5333 0.6553 0.7745 -0.0382 0.0705  -0.0490 -171 LYS A O   
184  C CB  . LYS A 26  ? 0.6325 0.7232 0.8363 -0.0471 0.0865  -0.0126 -171 LYS A CB  
185  C CG  . LYS A 26  ? 0.7076 0.8037 0.8889 -0.0468 0.1015  0.0064  -171 LYS A CG  
186  C CD  . LYS A 26  ? 0.7560 0.8765 0.9644 -0.0531 0.1176  0.0212  -171 LYS A CD  
187  C CE  . LYS A 26  ? 0.7685 0.9070 0.9476 -0.0460 0.1301  0.0290  -171 LYS A CE  
188  N NZ  . LYS A 26  ? 0.7617 0.9315 0.9663 -0.0486 0.1444  0.0368  -171 LYS A NZ  
189  N N   . LYS A 27  ? 0.5036 0.5907 0.7134 -0.0335 0.0518  -0.0583 -170 LYS A N   
190  C CA  . LYS A 27  ? 0.4995 0.5951 0.7330 -0.0310 0.0391  -0.0762 -170 LYS A CA  
191  C C   . LYS A 27  ? 0.4934 0.6022 0.7150 -0.0212 0.0363  -0.0846 -170 LYS A C   
192  O O   . LYS A 27  ? 0.4861 0.6120 0.7353 -0.0208 0.0328  -0.0942 -170 LYS A O   
193  C CB  . LYS A 27  ? 0.5359 0.6164 0.7619 -0.0274 0.0239  -0.0881 -170 LYS A CB  
194  C CG  . LYS A 27  ? 0.6010 0.6929 0.8515 -0.0236 0.0093  -0.1080 -170 LYS A CG  
195  C CD  . LYS A 27  ? 0.6765 0.7591 0.9449 -0.0264 -0.0019 -0.1185 -170 LYS A CD  
196  C CE  . LYS A 27  ? 0.7126 0.7980 0.9662 -0.0143 -0.0195 -0.1378 -170 LYS A CE  
197  N NZ  . LYS A 27  ? 0.7314 0.8095 0.9991 -0.0149 -0.0312 -0.1509 -170 LYS A NZ  
198  N N   . PHE A 28  ? 0.4768 0.5776 0.6601 -0.0130 0.0373  -0.0814 -169 PHE A N   
199  C CA  . PHE A 28  ? 0.4431 0.5555 0.6176 -0.0039 0.0364  -0.0872 -169 PHE A CA  
200  C C   . PHE A 28  ? 0.4649 0.5991 0.6617 -0.0077 0.0489  -0.0831 -169 PHE A C   
201  O O   . PHE A 28  ? 0.4822 0.6329 0.6960 -0.0036 0.0459  -0.0924 -169 PHE A O   
202  C CB  . PHE A 28  ? 0.4401 0.5393 0.5754 0.0036  0.0373  -0.0825 -169 PHE A CB  
203  C CG  . PHE A 28  ? 0.4655 0.5732 0.5932 0.0138  0.0345  -0.0890 -169 PHE A CG  
204  C CD1 . PHE A 28  ? 0.4506 0.5552 0.5721 0.0230  0.0208  -0.0982 -169 PHE A CD1 
205  C CD2 . PHE A 28  ? 0.5115 0.6307 0.6371 0.0155  0.0453  -0.0857 -169 PHE A CD2 
206  C CE1 . PHE A 28  ? 0.4606 0.5711 0.5768 0.0329  0.0181  -0.1024 -169 PHE A CE1 
207  C CE2 . PHE A 28  ? 0.4927 0.6182 0.6131 0.0258  0.0420  -0.0930 -169 PHE A CE2 
208  C CZ  . PHE A 28  ? 0.4615 0.5815 0.5788 0.0340  0.0283  -0.1007 -169 PHE A CZ  
209  N N   . GLU A 29  ? 0.5089 0.6454 0.7066 -0.0150 0.0634  -0.0686 -168 GLU A N   
210  C CA  . GLU A 29  ? 0.5112 0.6717 0.7291 -0.0184 0.0774  -0.0623 -168 GLU A CA  
211  C C   . GLU A 29  ? 0.5291 0.7051 0.7935 -0.0255 0.0762  -0.0672 -168 GLU A C   
212  O O   . GLU A 29  ? 0.5220 0.7200 0.8058 -0.0232 0.0793  -0.0729 -168 GLU A O   
213  C CB  . GLU A 29  ? 0.5111 0.6718 0.7199 -0.0245 0.0928  -0.0434 -168 GLU A CB  
214  C CG  . GLU A 29  ? 0.5337 0.7213 0.7519 -0.0249 0.1090  -0.0352 -168 GLU A CG  
215  C CD  . GLU A 29  ? 0.5847 0.7759 0.8011 -0.0321 0.1243  -0.0137 -168 GLU A CD  
216  O OE1 . GLU A 29  ? 0.6108 0.8270 0.8479 -0.0360 0.1390  -0.0029 -168 GLU A OE1 
217  O OE2 . GLU A 29  ? 0.6010 0.7715 0.7961 -0.0335 0.1220  -0.0063 -168 GLU A OE2 
218  N N   . LYS A 30  ? 0.5377 0.7032 0.8235 -0.0339 0.0708  -0.0665 -167 LYS A N   
219  C CA  . LYS A 30  ? 0.5640 0.7435 0.8996 -0.0415 0.0685  -0.0723 -167 LYS A CA  
220  C C   . LYS A 30  ? 0.5905 0.7820 0.9373 -0.0334 0.0554  -0.0925 -167 LYS A C   
221  O O   . LYS A 30  ? 0.5809 0.7925 0.9680 -0.0375 0.0565  -0.0976 -167 LYS A O   
222  C CB  . LYS A 30  ? 0.5780 0.7412 0.9336 -0.0499 0.0616  -0.0722 -167 LYS A CB  
223  C CG  . LYS A 30  ? 0.5969 0.7722 1.0078 -0.0574 0.0558  -0.0819 -167 LYS A CG  
224  C CD  . LYS A 30  ? 0.6132 0.7697 1.0406 -0.0625 0.0440  -0.0884 -167 LYS A CD  
225  C CE  . LYS A 30  ? 0.6306 0.7965 1.1211 -0.0754 0.0460  -0.0874 -167 LYS A CE  
226  N NZ  . LYS A 30  ? 0.6331 0.8129 1.1421 -0.0847 0.0680  -0.0631 -167 LYS A NZ  
227  N N   . ASP A 31  ? 0.6247 0.8053 0.9378 -0.0219 0.0432  -0.1027 -166 ASP A N   
228  C CA  . ASP A 31  ? 0.6402 0.8322 0.9608 -0.0126 0.0301  -0.1198 -166 ASP A CA  
229  C C   . ASP A 31  ? 0.6399 0.8484 0.9543 -0.0052 0.0367  -0.1202 -166 ASP A C   
230  O O   . ASP A 31  ? 0.6343 0.8625 0.9757 -0.0025 0.0326  -0.1306 -166 ASP A O   
231  C CB  . ASP A 31  ? 0.6342 0.8092 0.9234 -0.0025 0.0140  -0.1288 -166 ASP A CB  
232  C CG  . ASP A 31  ? 0.6065 0.7768 0.9142 -0.0051 0.0002  -0.1403 -166 ASP A CG  
233  O OD1 . ASP A 31  ? 0.6240 0.8057 0.9747 -0.0138 0.0004  -0.1449 -166 ASP A OD1 
234  O OD2 . ASP A 31  ? 0.5723 0.7291 0.8532 0.0021  -0.0109 -0.1452 -166 ASP A OD2 
235  N N   . THR A 32  ? 0.6415 0.8432 0.9227 -0.0013 0.0461  -0.1104 -165 THR A N   
236  C CA  . THR A 32  ? 0.6101 0.8230 0.8795 0.0088  0.0488  -0.1142 -165 THR A CA  
237  C C   . THR A 32  ? 0.6165 0.8481 0.8922 0.0057  0.0673  -0.1052 -165 THR A C   
238  O O   . THR A 32  ? 0.6185 0.8657 0.8952 0.0138  0.0698  -0.1114 -165 THR A O   
239  C CB  . THR A 32  ? 0.5778 0.7699 0.8048 0.0183  0.0430  -0.1135 -165 THR A CB  
240  O OG1 . THR A 32  ? 0.5463 0.7260 0.7509 0.0133  0.0534  -0.1004 -165 THR A OG1 
241  C CG2 . THR A 32  ? 0.5617 0.7379 0.7788 0.0229  0.0257  -0.1205 -165 THR A CG2 
242  N N   . GLY A 33  ? 0.6085 0.8399 0.8874 -0.0045 0.0803  -0.0904 -164 GLY A N   
243  C CA  . GLY A 33  ? 0.6042 0.8536 0.8795 -0.0054 0.0986  -0.0796 -164 GLY A CA  
244  C C   . GLY A 33  ? 0.6021 0.8414 0.8347 0.0025  0.1019  -0.0764 -164 GLY A C   
245  O O   . GLY A 33  ? 0.6247 0.8815 0.8505 0.0042  0.1162  -0.0697 -164 GLY A O   
246  N N   . ILE A 34  ? 0.5708 0.7842 0.7758 0.0077  0.0894  -0.0810 -163 ILE A N   
247  C CA  . ILE A 34  ? 0.5566 0.7589 0.7250 0.0147  0.0911  -0.0791 -163 ILE A CA  
248  C C   . ILE A 34  ? 0.5613 0.7487 0.7129 0.0072  0.0966  -0.0645 -163 ILE A C   
249  O O   . ILE A 34  ? 0.5308 0.7005 0.6855 0.0010  0.0897  -0.0614 -163 ILE A O   
250  C CB  . ILE A 34  ? 0.5199 0.7031 0.6703 0.0243  0.0754  -0.0902 -163 ILE A CB  
251  C CG1 . ILE A 34  ? 0.4765 0.6731 0.6466 0.0318  0.0680  -0.1035 -163 ILE A CG1 
252  C CG2 . ILE A 34  ? 0.5123 0.6853 0.6313 0.0314  0.0769  -0.0896 -163 ILE A CG2 
253  C CD1 . ILE A 34  ? 0.4524 0.6749 0.6334 0.0365  0.0782  -0.1079 -163 ILE A CD1 
254  N N   . LYS A 35  ? 0.6276 0.8232 0.7609 0.0090  0.1083  -0.0565 -162 LYS A N   
255  C CA  . LYS A 35  ? 0.6525 0.8360 0.7674 0.0038  0.1137  -0.0421 -162 LYS A CA  
256  C C   . LYS A 35  ? 0.6573 0.8135 0.7421 0.0088  0.1024  -0.0466 -162 LYS A C   
257  O O   . LYS A 35  ? 0.6860 0.8389 0.7567 0.0184  0.0960  -0.0579 -162 LYS A O   
258  C CB  . LYS A 35  ? 0.7114 0.9175 0.8161 0.0059  0.1298  -0.0325 -162 LYS A CB  
259  C CG  . LYS A 35  ? 0.7841 0.9938 0.8948 -0.0040 0.1414  -0.0115 -162 LYS A CG  
260  C CD  . LYS A 35  ? 0.8371 1.0672 0.9878 -0.0127 0.1507  -0.0036 -162 LYS A CD  
261  C CE  . LYS A 35  ? 0.8760 1.1184 1.0328 -0.0201 0.1667  0.0206  -162 LYS A CE  
262  N NZ  . LYS A 35  ? 0.8757 1.1180 1.0758 -0.0336 0.1696  0.0316  -162 LYS A NZ  
263  N N   . VAL A 36  ? 0.6167 0.7538 0.6941 0.0023  0.1002  -0.0373 -161 VAL A N   
264  C CA  . VAL A 36  ? 0.6082 0.7202 0.6596 0.0058  0.0906  -0.0396 -161 VAL A CA  
265  C C   . VAL A 36  ? 0.6104 0.7175 0.6432 0.0029  0.0980  -0.0264 -161 VAL A C   
266  O O   . VAL A 36  ? 0.6427 0.7453 0.6850 -0.0056 0.1017  -0.0145 -161 VAL A O   
267  C CB  . VAL A 36  ? 0.5724 0.6654 0.6315 0.0024  0.0783  -0.0433 -161 VAL A CB  
268  C CG1 . VAL A 36  ? 0.5246 0.5946 0.5566 0.0067  0.0699  -0.0446 -161 VAL A CG1 
269  C CG2 . VAL A 36  ? 0.5701 0.6713 0.6480 0.0061  0.0704  -0.0560 -161 VAL A CG2 
270  N N   . THR A 37  ? 0.6051 0.7127 0.6133 0.0106  0.0990  -0.0292 -160 THR A N   
271  C CA  . THR A 37  ? 0.5744 0.6788 0.5616 0.0101  0.1043  -0.0186 -160 THR A CA  
272  C C   . THR A 37  ? 0.5731 0.6509 0.5418 0.0119  0.0934  -0.0219 -160 THR A C   
273  O O   . THR A 37  ? 0.5904 0.6602 0.5521 0.0186  0.0849  -0.0338 -160 THR A O   
274  C CB  . THR A 37  ? 0.5313 0.6580 0.5043 0.0184  0.1124  -0.0212 -160 THR A CB  
275  O OG1 . THR A 37  ? 0.5288 0.6831 0.5199 0.0172  0.1237  -0.0177 -160 THR A OG1 
276  C CG2 . THR A 37  ? 0.4876 0.6137 0.4382 0.0189  0.1173  -0.0100 -160 THR A CG2 
277  N N   . VAL A 38  ? 0.5708 0.6350 0.5342 0.0059  0.0936  -0.0106 -159 VAL A N   
278  C CA  . VAL A 38  ? 0.5582 0.5991 0.5051 0.0071  0.0847  -0.0120 -159 VAL A CA  
279  C C   . VAL A 38  ? 0.5809 0.6237 0.5071 0.0094  0.0894  -0.0047 -159 VAL A C   
280  O O   . VAL A 38  ? 0.5777 0.6306 0.5056 0.0055  0.0984  0.0086  -159 VAL A O   
281  C CB  . VAL A 38  ? 0.5670 0.5913 0.5253 -0.0003 0.0797  -0.0075 -159 VAL A CB  
282  C CG1 . VAL A 38  ? 0.5318 0.5347 0.4725 0.0014  0.0717  -0.0083 -159 VAL A CG1 
283  C CG2 . VAL A 38  ? 0.5620 0.5875 0.5404 -0.0013 0.0738  -0.0166 -159 VAL A CG2 
284  N N   . GLU A 39  ? 0.6007 0.6352 0.5090 0.0161  0.0831  -0.0129 -158 GLU A N   
285  C CA  . GLU A 39  ? 0.6278 0.6638 0.5162 0.0196  0.0850  -0.0090 -158 GLU A CA  
286  C C   . GLU A 39  ? 0.5824 0.5948 0.4607 0.0197  0.0755  -0.0111 -158 GLU A C   
287  O O   . GLU A 39  ? 0.5675 0.5662 0.4507 0.0204  0.0677  -0.0186 -158 GLU A O   
288  C CB  . GLU A 39  ? 0.6659 0.7210 0.5449 0.0291  0.0871  -0.0196 -158 GLU A CB  
289  C CG  . GLU A 39  ? 0.7104 0.7918 0.5993 0.0301  0.0971  -0.0186 -158 GLU A CG  
290  C CD  . GLU A 39  ? 0.7440 0.8458 0.6250 0.0410  0.0982  -0.0327 -158 GLU A CD  
291  O OE1 . GLU A 39  ? 0.7704 0.8623 0.6447 0.0474  0.0890  -0.0466 -158 GLU A OE1 
292  O OE2 . GLU A 39  ? 0.7603 0.8889 0.6438 0.0436  0.1083  -0.0306 -158 GLU A OE2 
293  N N   . HIS A 40  ? 0.5716 0.5809 0.4362 0.0197  0.0765  -0.0035 -157 HIS A N   
294  C CA  . HIS A 40  ? 0.5675 0.5568 0.4231 0.0199  0.0685  -0.0047 -157 HIS A CA  
295  C C   . HIS A 40  ? 0.5653 0.5612 0.4036 0.0265  0.0676  -0.0075 -157 HIS A C   
296  O O   . HIS A 40  ? 0.5485 0.5407 0.3774 0.0254  0.0679  0.0013  -157 HIS A O   
297  C CB  . HIS A 40  ? 0.5487 0.5244 0.4088 0.0125  0.0685  0.0073  -157 HIS A CB  
298  C CG  . HIS A 40  ? 0.5712 0.5578 0.4331 0.0089  0.0773  0.0222  -157 HIS A CG  
299  N ND1 . HIS A 40  ? 0.5865 0.5726 0.4360 0.0098  0.0787  0.0321  -157 HIS A ND1 
300  C CD2 . HIS A 40  ? 0.5742 0.5730 0.4509 0.0044  0.0853  0.0303  -157 HIS A CD2 
301  C CE1 . HIS A 40  ? 0.5934 0.5907 0.4489 0.0064  0.0874  0.0472  -157 HIS A CE1 
302  N NE2 . HIS A 40  ? 0.5934 0.5988 0.4666 0.0026  0.0920  0.0465  -157 HIS A NE2 
303  N N   . PRO A 41  ? 0.6061 0.6114 0.4416 0.0340  0.0652  -0.0213 -156 PRO A N   
304  C CA  . PRO A 41  ? 0.6383 0.6541 0.4588 0.0415  0.0635  -0.0272 -156 PRO A CA  
305  C C   . PRO A 41  ? 0.6171 0.6143 0.4332 0.0417  0.0546  -0.0298 -156 PRO A C   
306  O O   . PRO A 41  ? 0.5731 0.5509 0.3980 0.0379  0.0495  -0.0305 -156 PRO A O   
307  C CB  . PRO A 41  ? 0.6340 0.6633 0.4590 0.0495  0.0617  -0.0445 -156 PRO A CB  
308  C CG  . PRO A 41  ? 0.6113 0.6263 0.4530 0.0461  0.0581  -0.0481 -156 PRO A CG  
309  C CD  . PRO A 41  ? 0.5790 0.5862 0.4267 0.0368  0.0626  -0.0333 -156 PRO A CD  
310  N N   . ASP A 42  ? 0.7005 0.7066 0.5026 0.0469  0.0532  -0.0311 -155 ASP A N   
311  C CA  . ASP A 42  ? 0.7649 0.7571 0.5642 0.0481  0.0445  -0.0355 -155 ASP A CA  
312  C C   . ASP A 42  ? 0.7469 0.7306 0.5587 0.0516  0.0363  -0.0521 -155 ASP A C   
313  O O   . ASP A 42  ? 0.7126 0.7088 0.5285 0.0577  0.0355  -0.0651 -155 ASP A O   
314  C CB  . ASP A 42  ? 0.8507 0.8590 0.6330 0.0550  0.0437  -0.0362 -155 ASP A CB  
315  C CG  . ASP A 42  ? 0.9000 0.9079 0.6725 0.0508  0.0488  -0.0164 -155 ASP A CG  
316  O OD1 . ASP A 42  ? 0.9005 0.8886 0.6807 0.0429  0.0485  -0.0065 -155 ASP A OD1 
317  O OD2 . ASP A 42  ? 0.9199 0.9485 0.6773 0.0563  0.0529  -0.0108 -155 ASP A OD2 
318  N N   . LYS A 43  ? 0.7536 0.7166 0.5733 0.0478  0.0304  -0.0509 -154 LYS A N   
319  C CA  . LYS A 43  ? 0.7519 0.7049 0.5865 0.0504  0.0226  -0.0631 -154 LYS A CA  
320  C C   . LYS A 43  ? 0.6969 0.6514 0.5445 0.0520  0.0233  -0.0695 -154 LYS A C   
321  O O   . LYS A 43  ? 0.6923 0.6491 0.5518 0.0578  0.0178  -0.0840 -154 LYS A O   
322  C CB  . LYS A 43  ? 0.8466 0.8091 0.6794 0.0581  0.0159  -0.0777 -154 LYS A CB  
323  C CG  . LYS A 43  ? 0.8988 0.8557 0.7251 0.0571  0.0118  -0.0737 -154 LYS A CG  
324  C CD  . LYS A 43  ? 0.9401 0.8971 0.7783 0.0629  0.0014  -0.0912 -154 LYS A CD  
325  C CE  . LYS A 43  ? 0.9637 0.9440 0.7879 0.0724  -0.0016 -0.1033 -154 LYS A CE  
326  N NZ  . LYS A 43  ? 0.9741 0.9587 0.7797 0.0719  -0.0005 -0.0923 -154 LYS A NZ  
327  N N   . LEU A 44  ? 0.6242 0.5774 0.4723 0.0471  0.0291  -0.0597 -153 LEU A N   
328  C CA  . LEU A 44  ? 0.6051 0.5627 0.4647 0.0491  0.0301  -0.0652 -153 LEU A CA  
329  C C   . LEU A 44  ? 0.6251 0.5677 0.5022 0.0506  0.0230  -0.0701 -153 LEU A C   
330  O O   . LEU A 44  ? 0.6003 0.5468 0.4894 0.0547  0.0214  -0.0780 -153 LEU A O   
331  C CB  . LEU A 44  ? 0.5353 0.4946 0.3941 0.0433  0.0366  -0.0541 -153 LEU A CB  
332  C CG  . LEU A 44  ? 0.4945 0.4364 0.3584 0.0380  0.0345  -0.0453 -153 LEU A CG  
333  C CD1 . LEU A 44  ? 0.4456 0.3838 0.3234 0.0404  0.0311  -0.0494 -153 LEU A CD1 
334  C CD2 . LEU A 44  ? 0.5289 0.4731 0.3886 0.0316  0.0403  -0.0343 -153 LEU A CD2 
335  N N   . GLU A 45  ? 0.6309 0.5573 0.5110 0.0475  0.0192  -0.0641 -152 GLU A N   
336  C CA  . GLU A 45  ? 0.6103 0.5234 0.5084 0.0487  0.0137  -0.0649 -152 GLU A CA  
337  C C   . GLU A 45  ? 0.6267 0.5405 0.5396 0.0546  0.0069  -0.0797 -152 GLU A C   
338  O O   . GLU A 45  ? 0.5903 0.4959 0.5235 0.0570  0.0024  -0.0825 -152 GLU A O   
339  C CB  . GLU A 45  ? 0.5862 0.4848 0.4835 0.0437  0.0132  -0.0525 -152 GLU A CB  
340  C CG  . GLU A 45  ? 0.6464 0.5403 0.5443 0.0433  0.0096  -0.0550 -152 GLU A CG  
341  C CD  . GLU A 45  ? 0.6713 0.5719 0.5498 0.0412  0.0127  -0.0524 -152 GLU A CD  
342  O OE1 . GLU A 45  ? 0.6196 0.5319 0.4862 0.0414  0.0174  -0.0524 -152 GLU A OE1 
343  O OE2 . GLU A 45  ? 0.7367 0.6313 0.6136 0.0394  0.0106  -0.0495 -152 GLU A OE2 
344  N N   . GLU A 46  ? 0.6415 0.5656 0.5459 0.0576  0.0056  -0.0894 -151 GLU A N   
345  C CA  . GLU A 46  ? 0.6584 0.5875 0.5772 0.0647  -0.0018 -0.1080 -151 GLU A CA  
346  C C   . GLU A 46  ? 0.6522 0.6005 0.5688 0.0718  -0.0002 -0.1215 -151 GLU A C   
347  O O   . GLU A 46  ? 0.6980 0.6485 0.6335 0.0784  -0.0066 -0.1379 -151 GLU A O   
348  C CB  . GLU A 46  ? 0.7041 0.6371 0.6158 0.0662  -0.0059 -0.1144 -151 GLU A CB  
349  C CG  . GLU A 46  ? 0.7781 0.6952 0.6898 0.0594  -0.0063 -0.1008 -151 GLU A CG  
350  C CD  . GLU A 46  ? 0.8631 0.7843 0.7713 0.0615  -0.0118 -0.1086 -151 GLU A CD  
351  O OE1 . GLU A 46  ? 0.8814 0.8208 0.7780 0.0681  -0.0135 -0.1210 -151 GLU A OE1 
352  O OE2 . GLU A 46  ? 0.9129 0.8211 0.8300 0.0572  -0.0144 -0.1020 -151 GLU A OE2 
353  N N   . LYS A 47  ? 0.5894 0.5521 0.4864 0.0706  0.0083  -0.1151 -150 LYS A N   
354  C CA  . LYS A 47  ? 0.6254 0.6093 0.5210 0.0776  0.0111  -0.1273 -150 LYS A CA  
355  C C   . LYS A 47  ? 0.6088 0.5884 0.5220 0.0784  0.0110  -0.1285 -150 LYS A C   
356  O O   . LYS A 47  ? 0.6066 0.5966 0.5323 0.0862  0.0080  -0.1448 -150 LYS A O   
357  C CB  . LYS A 47  ? 0.6964 0.6991 0.5682 0.0761  0.0212  -0.1181 -150 LYS A CB  
358  C CG  . LYS A 47  ? 0.7206 0.7358 0.5744 0.0798  0.0205  -0.1212 -150 LYS A CG  
359  C CD  . LYS A 47  ? 0.7452 0.7791 0.5778 0.0784  0.0312  -0.1086 -150 LYS A CD  
360  C CE  . LYS A 47  ? 0.7475 0.7865 0.5616 0.0796  0.0303  -0.1035 -150 LYS A CE  
361  N NZ  . LYS A 47  ? 0.7606 0.8138 0.5570 0.0766  0.0415  -0.0852 -150 LYS A NZ  
362  N N   . PHE A 48  ? 0.5956 0.5606 0.5113 0.0713  0.0134  -0.1125 -149 PHE A N   
363  C CA  . PHE A 48  ? 0.5750 0.5377 0.5061 0.0728  0.0128  -0.1126 -149 PHE A CA  
364  C C   . PHE A 48  ? 0.5447 0.5006 0.5018 0.0800  0.0037  -0.1268 -149 PHE A C   
365  O O   . PHE A 48  ? 0.5329 0.4998 0.5007 0.0864  0.0029  -0.1387 -149 PHE A O   
366  C CB  . PHE A 48  ? 0.5650 0.5126 0.4964 0.0660  0.0140  -0.0952 -149 PHE A CB  
367  C CG  . PHE A 48  ? 0.5635 0.5093 0.5105 0.0687  0.0121  -0.0947 -149 PHE A CG  
368  C CD1 . PHE A 48  ? 0.5274 0.4890 0.4736 0.0700  0.0168  -0.0974 -149 PHE A CD1 
369  C CD2 . PHE A 48  ? 0.5663 0.4958 0.5310 0.0704  0.0056  -0.0908 -149 PHE A CD2 
370  C CE1 . PHE A 48  ? 0.5256 0.4864 0.4868 0.0732  0.0141  -0.0974 -149 PHE A CE1 
371  C CE2 . PHE A 48  ? 0.5616 0.4902 0.5403 0.0739  0.0033  -0.0890 -149 PHE A CE2 
372  C CZ  . PHE A 48  ? 0.5337 0.4778 0.5105 0.0757  0.0069  -0.0933 -149 PHE A CZ  
373  N N   . PRO A 49  ? 0.5742 0.5121 0.5443 0.0787  -0.0029 -0.1249 -148 PRO A N   
374  C CA  . PRO A 49  ? 0.5987 0.5285 0.5996 0.0850  -0.0118 -0.1370 -148 PRO A CA  
375  C C   . PRO A 49  ? 0.6577 0.6038 0.6651 0.0940  -0.0159 -0.1616 -148 PRO A C   
376  O O   . PRO A 49  ? 0.7291 0.6762 0.7597 0.1009  -0.0210 -0.1743 -148 PRO A O   
377  C CB  . PRO A 49  ? 0.5834 0.4934 0.5967 0.0808  -0.0168 -0.1291 -148 PRO A CB  
378  C CG  . PRO A 49  ? 0.6124 0.5240 0.5986 0.0741  -0.0114 -0.1188 -148 PRO A CG  
379  C CD  . PRO A 49  ? 0.6034 0.5271 0.5659 0.0716  -0.0027 -0.1110 -148 PRO A CD  
380  N N   . GLN A 50  ? 0.6599 0.6211 0.6475 0.0954  -0.0140 -0.1698 -147 GLN A N   
381  C CA  . GLN A 50  ? 0.7090 0.6905 0.7004 0.1060  -0.0181 -0.1952 -147 GLN A CA  
382  C C   . GLN A 50  ? 0.6719 0.6746 0.6581 0.1115  -0.0119 -0.2016 -147 GLN A C   
383  O O   . GLN A 50  ? 0.6525 0.6636 0.6575 0.1207  -0.0170 -0.2212 -147 GLN A O   
384  C CB  . GLN A 50  ? 0.7811 0.7761 0.7500 0.1074  -0.0176 -0.2005 -147 GLN A CB  
385  C CG  . GLN A 50  ? 0.8557 0.8310 0.8272 0.1006  -0.0221 -0.1910 -147 GLN A CG  
386  C CD  . GLN A 50  ? 0.9293 0.9192 0.8759 0.1021  -0.0213 -0.1940 -147 GLN A CD  
387  O OE1 . GLN A 50  ? 0.9643 0.9728 0.8831 0.1025  -0.0125 -0.1874 -147 GLN A OE1 
388  N NE2 . GLN A 50  ? 0.9289 0.9114 0.8871 0.1030  -0.0307 -0.2029 -147 GLN A NE2 
389  N N   . VAL A 51  ? 0.6690 0.6805 0.6322 0.1059  -0.0009 -0.1853 -146 VAL A N   
390  C CA  . VAL A 51  ? 0.6445 0.6793 0.6037 0.1107  0.0061  -0.1909 -146 VAL A CA  
391  C C   . VAL A 51  ? 0.6171 0.6423 0.5997 0.1115  0.0037  -0.1901 -146 VAL A C   
392  O O   . VAL A 51  ? 0.6065 0.6480 0.5999 0.1196  0.0038  -0.2046 -146 VAL A O   
393  C CB  . VAL A 51  ? 0.6135 0.6609 0.5460 0.1038  0.0186  -0.1729 -146 VAL A CB  
394  C CG1 . VAL A 51  ? 0.5946 0.6624 0.5044 0.1075  0.0221  -0.1774 -146 VAL A CG1 
395  C CG2 . VAL A 51  ? 0.6091 0.6325 0.5375 0.0921  0.0197  -0.1504 -146 VAL A CG2 
396  N N   . ALA A 52  ? 0.6149 0.6159 0.6049 0.1040  0.0016  -0.1729 -145 ALA A N   
397  C CA  . ALA A 52  ? 0.6028 0.5955 0.6120 0.1049  -0.0007 -0.1686 -145 ALA A CA  
398  C C   . ALA A 52  ? 0.6409 0.6253 0.6815 0.1135  -0.0112 -0.1845 -145 ALA A C   
399  O O   . ALA A 52  ? 0.6543 0.6403 0.7133 0.1185  -0.0135 -0.1884 -145 ALA A O   
400  C CB  . ALA A 52  ? 0.5633 0.5354 0.5690 0.0960  -0.0001 -0.1455 -145 ALA A CB  
401  N N   . ALA A 53  ? 0.6452 0.6212 0.6950 0.1155  -0.0183 -0.1944 -144 ALA A N   
402  C CA  . ALA A 53  ? 0.6436 0.6123 0.7281 0.1239  -0.0293 -0.2124 -144 ALA A CA  
403  C C   . ALA A 53  ? 0.6563 0.6493 0.7477 0.1352  -0.0299 -0.2367 -144 ALA A C   
404  O O   . ALA A 53  ? 0.7025 0.6908 0.8255 0.1428  -0.0377 -0.2494 -144 ALA A O   
405  C CB  . ALA A 53  ? 0.6339 0.5926 0.7279 0.1239  -0.0370 -0.2212 -144 ALA A CB  
406  N N   . THR A 54  ? 0.6233 0.6432 0.6873 0.1371  -0.0215 -0.2431 -143 THR A N   
407  C CA  . THR A 54  ? 0.6484 0.6962 0.7167 0.1487  -0.0203 -0.2658 -143 THR A CA  
408  C C   . THR A 54  ? 0.6355 0.6961 0.6984 0.1474  -0.0111 -0.2562 -143 THR A C   
409  O O   . THR A 54  ? 0.5720 0.6609 0.6314 0.1553  -0.0061 -0.2705 -143 THR A O   
410  C CB  . THR A 54  ? 0.6737 0.7487 0.7174 0.1539  -0.0166 -0.2801 -143 THR A CB  
411  O OG1 . THR A 54  ? 0.6727 0.7530 0.6826 0.1444  -0.0054 -0.2581 -143 THR A OG1 
412  C CG2 . THR A 54  ? 0.6827 0.7475 0.7378 0.1573  -0.0283 -0.2951 -143 THR A CG2 
413  N N   . GLY A 55  ? 0.6923 0.7346 0.7540 0.1379  -0.0087 -0.2324 -142 GLY A N   
414  C CA  . GLY A 55  ? 0.7198 0.7737 0.7791 0.1364  -0.0013 -0.2238 -142 GLY A CA  
415  C C   . GLY A 55  ? 0.7284 0.8012 0.7582 0.1295  0.0119  -0.2119 -142 GLY A C   
416  O O   . GLY A 55  ? 0.7150 0.8045 0.7451 0.1295  0.0188  -0.2093 -142 GLY A O   
417  N N   . ASP A 56  ? 0.7374 0.8084 0.7445 0.1239  0.0152  -0.2043 -141 ASP A N   
418  C CA  . ASP A 56  ? 0.7609 0.8496 0.7423 0.1179  0.0274  -0.1925 -141 ASP A CA  
419  C C   . ASP A 56  ? 0.7120 0.7794 0.6813 0.1053  0.0292  -0.1690 -141 ASP A C   
420  O O   . ASP A 56  ? 0.7084 0.7507 0.6878 0.1019  0.0221  -0.1616 -141 ASP A O   
421  C CB  . ASP A 56  ? 0.8190 0.9285 0.7835 0.1242  0.0299  -0.2048 -141 ASP A CB  
422  C CG  . ASP A 56  ? 0.8810 1.0192 0.8239 0.1222  0.0443  -0.1957 -141 ASP A CG  
423  O OD1 . ASP A 56  ? 0.8846 1.0260 0.8296 0.1154  0.0520  -0.1816 -141 ASP A OD1 
424  O OD2 . ASP A 56  ? 0.9247 1.0831 0.8497 0.1276  0.0477  -0.2021 -141 ASP A OD2 
425  N N   . GLY A 57  ? 0.6903 0.7691 0.6388 0.0990  0.0391  -0.1566 -140 GLY A N   
426  C CA  . GLY A 57  ? 0.6448 0.7054 0.5818 0.0881  0.0406  -0.1370 -140 GLY A CA  
427  C C   . GLY A 57  ? 0.6095 0.6715 0.5493 0.0807  0.0465  -0.1231 -140 GLY A C   
428  O O   . GLY A 57  ? 0.6366 0.7183 0.5840 0.0828  0.0522  -0.1266 -140 GLY A O   
429  N N   . PRO A 58  ? 0.5573 0.5999 0.4927 0.0721  0.0449  -0.1084 -139 PRO A N   
430  C CA  . PRO A 58  ? 0.5170 0.5604 0.4574 0.0653  0.0486  -0.0975 -139 PRO A CA  
431  C C   . PRO A 58  ? 0.5727 0.6074 0.5302 0.0680  0.0413  -0.1001 -139 PRO A C   
432  O O   . PRO A 58  ? 0.5900 0.6119 0.5553 0.0735  0.0330  -0.1056 -139 PRO A O   
433  C CB  . PRO A 58  ? 0.5150 0.5421 0.4429 0.0570  0.0486  -0.0836 -139 PRO A CB  
434  C CG  . PRO A 58  ? 0.5105 0.5192 0.4348 0.0600  0.0406  -0.0866 -139 PRO A CG  
435  C CD  . PRO A 58  ? 0.5040 0.5249 0.4307 0.0689  0.0395  -0.1024 -139 PRO A CD  
436  N N   . ASP A 59  ? 0.5696 0.6128 0.5355 0.0645  0.0442  -0.0958 -138 ASP A N   
437  C CA  . ASP A 59  ? 0.5510 0.5879 0.5314 0.0673  0.0368  -0.0968 -138 ASP A CA  
438  C C   . ASP A 59  ? 0.5079 0.5230 0.4819 0.0642  0.0301  -0.0867 -138 ASP A C   
439  O O   . ASP A 59  ? 0.4978 0.5027 0.4798 0.0694  0.0221  -0.0867 -138 ASP A O   
440  C CB  . ASP A 59  ? 0.5678 0.6217 0.5601 0.0645  0.0410  -0.0963 -138 ASP A CB  
441  C CG  . ASP A 59  ? 0.5454 0.6241 0.5457 0.0680  0.0487  -0.1053 -138 ASP A CG  
442  O OD1 . ASP A 59  ? 0.5832 0.6750 0.5759 0.0633  0.0588  -0.1009 -138 ASP A OD1 
443  O OD2 . ASP A 59  ? 0.4905 0.5770 0.5054 0.0757  0.0452  -0.1155 -138 ASP A OD2 
444  N N   . ILE A 60  ? 0.4626 0.4714 0.4233 0.0564  0.0334  -0.0774 -137 ILE A N   
445  C CA  . ILE A 60  ? 0.4958 0.4872 0.4492 0.0536  0.0283  -0.0684 -137 ILE A CA  
446  C C   . ILE A 60  ? 0.5463 0.5275 0.4844 0.0497  0.0308  -0.0636 -137 ILE A C   
447  O O   . ILE A 60  ? 0.5675 0.5563 0.4988 0.0453  0.0376  -0.0620 -137 ILE A O   
448  C CB  . ILE A 60  ? 0.5015 0.4969 0.4575 0.0483  0.0285  -0.0637 -137 ILE A CB  
449  C CG1 . ILE A 60  ? 0.4965 0.5038 0.4688 0.0526  0.0250  -0.0694 -137 ILE A CG1 
450  C CG2 . ILE A 60  ? 0.4727 0.4531 0.4189 0.0465  0.0236  -0.0560 -137 ILE A CG2 
451  C CD1 . ILE A 60  ? 0.4943 0.5105 0.4746 0.0469  0.0257  -0.0685 -137 ILE A CD1 
452  N N   . ILE A 61  ? 0.5505 0.5157 0.4845 0.0515  0.0255  -0.0599 -136 ILE A N   
453  C CA  . ILE A 61  ? 0.5777 0.5329 0.4989 0.0477  0.0269  -0.0550 -136 ILE A CA  
454  C C   . ILE A 61  ? 0.5577 0.5012 0.4728 0.0445  0.0242  -0.0454 -136 ILE A C   
455  O O   . ILE A 61  ? 0.5460 0.4846 0.4660 0.0482  0.0192  -0.0423 -136 ILE A O   
456  C CB  . ILE A 61  ? 0.6042 0.5521 0.5281 0.0525  0.0234  -0.0605 -136 ILE A CB  
457  C CG1 . ILE A 61  ? 0.6259 0.5618 0.5388 0.0487  0.0231  -0.0543 -136 ILE A CG1 
458  C CG2 . ILE A 61  ? 0.5664 0.5068 0.5050 0.0583  0.0167  -0.0609 -136 ILE A CG2 
459  C CD1 . ILE A 61  ? 0.6638 0.5974 0.5783 0.0518  0.0209  -0.0619 -136 ILE A CD1 
460  N N   . PHE A 62  ? 0.5243 0.4650 0.4290 0.0385  0.0276  -0.0404 -135 PHE A N   
461  C CA  . PHE A 62  ? 0.5152 0.4461 0.4134 0.0361  0.0253  -0.0331 -135 PHE A CA  
462  C C   . PHE A 62  ? 0.5110 0.4305 0.4016 0.0355  0.0248  -0.0294 -135 PHE A C   
463  O O   . PHE A 62  ? 0.5420 0.4625 0.4280 0.0339  0.0276  -0.0314 -135 PHE A O   
464  C CB  . PHE A 62  ? 0.5286 0.4631 0.4247 0.0300  0.0284  -0.0308 -135 PHE A CB  
465  C CG  . PHE A 62  ? 0.5239 0.4682 0.4305 0.0299  0.0268  -0.0341 -135 PHE A CG  
466  C CD1 . PHE A 62  ? 0.5076 0.4649 0.4249 0.0304  0.0297  -0.0393 -135 PHE A CD1 
467  C CD2 . PHE A 62  ? 0.4735 0.4161 0.3802 0.0300  0.0225  -0.0334 -135 PHE A CD2 
468  C CE1 . PHE A 62  ? 0.4538 0.4209 0.3835 0.0301  0.0277  -0.0431 -135 PHE A CE1 
469  C CE2 . PHE A 62  ? 0.4437 0.3965 0.3617 0.0305  0.0196  -0.0386 -135 PHE A CE2 
470  C CZ  . PHE A 62  ? 0.4354 0.3998 0.3657 0.0302  0.0220  -0.0431 -135 PHE A CZ  
471  N N   . TRP A 63  ? 0.4949 0.4056 0.3842 0.0373  0.0215  -0.0236 -134 TRP A N   
472  C CA  . TRP A 63  ? 0.4483 0.3489 0.3332 0.0363  0.0211  -0.0192 -134 TRP A CA  
473  C C   . TRP A 63  ? 0.4671 0.3635 0.3511 0.0386  0.0189  -0.0113 -134 TRP A C   
474  O O   . TRP A 63  ? 0.5226 0.4241 0.4092 0.0422  0.0168  -0.0099 -134 TRP A O   
475  C CB  . TRP A 63  ? 0.5113 0.4081 0.4041 0.0391  0.0193  -0.0235 -134 TRP A CB  
476  C CG  . TRP A 63  ? 0.5202 0.4094 0.4094 0.0369  0.0193  -0.0215 -134 TRP A CG  
477  C CD1 . TRP A 63  ? 0.5182 0.3984 0.4134 0.0376  0.0172  -0.0158 -134 TRP A CD1 
478  C CD2 . TRP A 63  ? 0.5235 0.4149 0.4033 0.0338  0.0214  -0.0244 -134 TRP A CD2 
479  N NE1 . TRP A 63  ? 0.5336 0.4099 0.4251 0.0350  0.0173  -0.0168 -134 TRP A NE1 
480  C CE2 . TRP A 63  ? 0.5662 0.4494 0.4470 0.0332  0.0195  -0.0220 -134 TRP A CE2 
481  C CE3 . TRP A 63  ? 0.4979 0.3986 0.3696 0.0320  0.0251  -0.0274 -134 TRP A CE3 
482  C CZ2 . TRP A 63  ? 0.5982 0.4820 0.4708 0.0313  0.0200  -0.0237 -134 TRP A CZ2 
483  C CZ3 . TRP A 63  ? 0.5256 0.4272 0.3885 0.0303  0.0263  -0.0272 -134 TRP A CZ3 
484  C CH2 . TRP A 63  ? 0.5581 0.4511 0.4206 0.0302  0.0233  -0.0259 -134 TRP A CH2 
485  N N   . ALA A 64  ? 0.4332 0.3225 0.3130 0.0371  0.0195  -0.0059 -133 ALA A N   
486  C CA  . ALA A 64  ? 0.4636 0.3514 0.3431 0.0403  0.0185  0.0031  -133 ALA A CA  
487  C C   . ALA A 64  ? 0.5090 0.3944 0.4017 0.0451  0.0163  0.0074  -133 ALA A C   
488  O O   . ALA A 64  ? 0.5192 0.4005 0.4226 0.0451  0.0151  0.0025  -133 ALA A O   
489  C CB  . ALA A 64  ? 0.4345 0.3163 0.3098 0.0379  0.0203  0.0079  -133 ALA A CB  
490  N N   . HIS A 65  ? 0.5187 0.4075 0.4115 0.0499  0.0155  0.0168  -132 HIS A N   
491  C CA  . HIS A 65  ? 0.5200 0.4074 0.4269 0.0552  0.0131  0.0231  -132 HIS A CA  
492  C C   . HIS A 65  ? 0.5452 0.4218 0.4687 0.0541  0.0132  0.0275  -132 HIS A C   
493  O O   . HIS A 65  ? 0.5817 0.4543 0.5230 0.0576  0.0103  0.0294  -132 HIS A O   
494  C CB  . HIS A 65  ? 0.5005 0.3960 0.4021 0.0614  0.0127  0.0353  -132 HIS A CB  
495  C CG  . HIS A 65  ? 0.5577 0.4526 0.4553 0.0617  0.0163  0.0476  -132 HIS A CG  
496  N ND1 . HIS A 65  ? 0.5557 0.4538 0.4390 0.0588  0.0189  0.0449  -132 HIS A ND1 
497  C CD2 . HIS A 65  ? 0.5730 0.4653 0.4815 0.0646  0.0182  0.0633  -132 HIS A CD2 
498  C CE1 . HIS A 65  ? 0.5580 0.4570 0.4420 0.0603  0.0224  0.0575  -132 HIS A CE1 
499  N NE2 . HIS A 65  ? 0.5797 0.4755 0.4790 0.0635  0.0225  0.0698  -132 HIS A NE2 
500  N N   . ASP A 66  ? 0.5261 0.3975 0.4476 0.0497  0.0155  0.0287  -131 ASP A N   
501  C CA  . ASP A 66  ? 0.5669 0.4288 0.5090 0.0489  0.0149  0.0338  -131 ASP A CA  
502  C C   . ASP A 66  ? 0.5643 0.4205 0.5235 0.0491  0.0105  0.0213  -131 ASP A C   
503  O O   . ASP A 66  ? 0.5845 0.4333 0.5678 0.0506  0.0080  0.0246  -131 ASP A O   
504  C CB  . ASP A 66  ? 0.5395 0.3982 0.4778 0.0442  0.0175  0.0351  -131 ASP A CB  
505  C CG  . ASP A 66  ? 0.5455 0.4050 0.4701 0.0401  0.0171  0.0213  -131 ASP A CG  
506  O OD1 . ASP A 66  ? 0.5105 0.3764 0.4178 0.0398  0.0183  0.0175  -131 ASP A OD1 
507  O OD2 . ASP A 66  ? 0.5477 0.4021 0.4804 0.0376  0.0153  0.0144  -131 ASP A OD2 
508  N N   . ARG A 67  ? 0.5610 0.4218 0.5102 0.0481  0.0096  0.0068  -130 ARG A N   
509  C CA  . ARG A 67  ? 0.5911 0.4502 0.5551 0.0498  0.0055  -0.0071 -130 ARG A CA  
510  C C   . ARG A 67  ? 0.5846 0.4451 0.5622 0.0554  0.0025  -0.0083 -130 ARG A C   
511  O O   . ARG A 67  ? 0.6096 0.4682 0.6045 0.0581  -0.0016 -0.0197 -130 ARG A O   
512  C CB  . ARG A 67  ? 0.6369 0.5039 0.5847 0.0478  0.0067  -0.0208 -130 ARG A CB  
513  C CG  . ARG A 67  ? 0.6916 0.5573 0.6281 0.0433  0.0084  -0.0216 -130 ARG A CG  
514  C CD  . ARG A 67  ? 0.7517 0.6150 0.7010 0.0443  0.0040  -0.0329 -130 ARG A CD  
515  N NE  . ARG A 67  ? 0.7849 0.6463 0.7261 0.0406  0.0046  -0.0319 -130 ARG A NE  
516  C CZ  . ARG A 67  ? 0.8175 0.6790 0.7665 0.0415  0.0002  -0.0428 -130 ARG A CZ  
517  N NH1 . ARG A 67  ? 0.8056 0.6694 0.7707 0.0461  -0.0052 -0.0569 -130 ARG A NH1 
518  N NH2 . ARG A 67  ? 0.8109 0.6716 0.7525 0.0386  0.0003  -0.0412 -130 ARG A NH2 
519  N N   . PHE A 68  ? 0.5535 0.4185 0.5247 0.0580  0.0037  0.0017  -129 PHE A N   
520  C CA  . PHE A 68  ? 0.5523 0.4215 0.5330 0.0635  0.0006  -0.0020 -129 PHE A CA  
521  C C   . PHE A 68  ? 0.5453 0.4054 0.5543 0.0683  -0.0036 0.0055  -129 PHE A C   
522  O O   . PHE A 68  ? 0.5579 0.4187 0.5822 0.0732  -0.0076 -0.0021 -129 PHE A O   
523  C CB  . PHE A 68  ? 0.5663 0.4456 0.5307 0.0653  0.0021  0.0040  -129 PHE A CB  
524  C CG  . PHE A 68  ? 0.6028 0.4921 0.5499 0.0617  0.0047  -0.0074 -129 PHE A CG  
525  C CD1 . PHE A 68  ? 0.6740 0.5626 0.6081 0.0558  0.0081  -0.0108 -129 PHE A CD1 
526  C CD2 . PHE A 68  ? 0.6259 0.5253 0.5727 0.0644  0.0037  -0.0135 -129 PHE A CD2 
527  C CE1 . PHE A 68  ? 0.7145 0.6117 0.6363 0.0523  0.0110  -0.0183 -129 PHE A CE1 
528  C CE2 . PHE A 68  ? 0.6753 0.5841 0.6113 0.0606  0.0066  -0.0220 -129 PHE A CE2 
529  C CZ  . PHE A 68  ? 0.7067 0.6142 0.6304 0.0544  0.0106  -0.0237 -129 PHE A CZ  
530  N N   . GLY A 69  ? 0.5732 0.4250 0.5917 0.0672  -0.0025 0.0204  -128 GLY A N   
531  C CA  . GLY A 69  ? 0.5753 0.4170 0.6260 0.0708  -0.0062 0.0292  -128 GLY A CA  
532  C C   . GLY A 69  ? 0.5506 0.3855 0.6260 0.0714  -0.0119 0.0106  -128 GLY A C   
533  O O   . GLY A 69  ? 0.5583 0.3903 0.6556 0.0769  -0.0169 0.0067  -128 GLY A O   
534  N N   . GLY A 70  ? 0.5016 0.3354 0.5731 0.0667  -0.0119 -0.0026 -127 GLY A N   
535  C CA  . GLY A 70  ? 0.4603 0.2921 0.5508 0.0685  -0.0179 -0.0244 -127 GLY A CA  
536  C C   . GLY A 70  ? 0.5494 0.3910 0.6359 0.0739  -0.0201 -0.0402 -127 GLY A C   
537  O O   . GLY A 70  ? 0.5290 0.3675 0.6421 0.0793  -0.0263 -0.0516 -127 GLY A O   
538  N N   . TYR A 71  ? 0.5493 0.4034 0.6050 0.0727  -0.0150 -0.0413 -126 TYR A N   
539  C CA  . TYR A 71  ? 0.5375 0.4035 0.5901 0.0775  -0.0158 -0.0553 -126 TYR A CA  
540  C C   . TYR A 71  ? 0.5544 0.4172 0.6280 0.0839  -0.0198 -0.0494 -126 TYR A C   
541  O O   . TYR A 71  ? 0.5801 0.4459 0.6717 0.0897  -0.0242 -0.0637 -126 TYR A O   
542  C CB  . TYR A 71  ? 0.5707 0.4497 0.5914 0.0740  -0.0093 -0.0534 -126 TYR A CB  
543  C CG  . TYR A 71  ? 0.5706 0.4537 0.5693 0.0681  -0.0049 -0.0571 -126 TYR A CG  
544  C CD1 . TYR A 71  ? 0.5821 0.4638 0.5858 0.0679  -0.0073 -0.0689 -126 TYR A CD1 
545  C CD2 . TYR A 71  ? 0.5662 0.4553 0.5406 0.0633  0.0008  -0.0492 -126 TYR A CD2 
546  C CE1 . TYR A 71  ? 0.5793 0.4659 0.5623 0.0634  -0.0037 -0.0709 -126 TYR A CE1 
547  C CE2 . TYR A 71  ? 0.5698 0.4617 0.5266 0.0583  0.0044  -0.0509 -126 TYR A CE2 
548  C CZ  . TYR A 71  ? 0.6090 0.4997 0.5691 0.0585  0.0024  -0.0606 -126 TYR A CZ  
549  O OH  . TYR A 71  ? 0.6645 0.5591 0.6054 0.0541  0.0059  -0.0606 -126 TYR A OH  
550  N N   . ALA A 72  ? 0.5704 0.4287 0.6418 0.0838  -0.0184 -0.0283 -125 ALA A N   
551  C CA  . ALA A 72  ? 0.5530 0.4092 0.6430 0.0907  -0.0224 -0.0198 -125 ALA A CA  
552  C C   . ALA A 72  ? 0.5911 0.4333 0.7204 0.0945  -0.0289 -0.0214 -125 ALA A C   
553  O O   . ALA A 72  ? 0.5866 0.4284 0.7377 0.1014  -0.0343 -0.0282 -125 ALA A O   
554  C CB  . ALA A 72  ? 0.5139 0.3706 0.5913 0.0910  -0.0196 0.0044  -125 ALA A CB  
555  N N   . GLN A 73  ? 0.5950 0.4257 0.7370 0.0900  -0.0290 -0.0164 -124 GLN A N   
556  C CA  . GLN A 73  ? 0.5957 0.4121 0.7808 0.0928  -0.0358 -0.0189 -124 GLN A CA  
557  C C   . GLN A 73  ? 0.5583 0.3782 0.7591 0.0972  -0.0422 -0.0484 -124 GLN A C   
558  O O   . GLN A 73  ? 0.5486 0.3599 0.7868 0.1029  -0.0496 -0.0542 -124 GLN A O   
559  C CB  . GLN A 73  ? 0.6249 0.4310 0.8202 0.0861  -0.0344 -0.0109 -124 GLN A CB  
560  C CG  . GLN A 73  ? 0.6597 0.4497 0.9048 0.0874  -0.0412 -0.0100 -124 GLN A CG  
561  C CD  . GLN A 73  ? 0.7258 0.5075 0.9957 0.0922  -0.0422 0.0143  -124 GLN A CD  
562  O OE1 . GLN A 73  ? 0.7598 0.5426 1.0173 0.0908  -0.0359 0.0416  -124 GLN A OE1 
563  N NE2 . GLN A 73  ? 0.7420 0.5168 1.0476 0.0988  -0.0504 0.0044  -124 GLN A NE2 
564  N N   . SER A 74  ? 0.5423 0.3755 0.7163 0.0954  -0.0396 -0.0670 -123 SER A N   
565  C CA  . SER A 74  ? 0.5349 0.3771 0.7172 0.1006  -0.0443 -0.0959 -123 SER A CA  
566  C C   . SER A 74  ? 0.5532 0.4085 0.7303 0.1071  -0.0440 -0.1039 -123 SER A C   
567  O O   . SER A 74  ? 0.5513 0.4188 0.7307 0.1122  -0.0462 -0.1278 -123 SER A O   
568  C CB  . SER A 74  ? 0.5586 0.4130 0.7115 0.0965  -0.0403 -0.1095 -123 SER A CB  
569  O OG  . SER A 74  ? 0.5621 0.4062 0.7227 0.0914  -0.0420 -0.1067 -123 SER A OG  
570  N N   . GLY A 75  ? 0.5926 0.4477 0.7628 0.1078  -0.0414 -0.0851 -122 GLY A N   
571  C CA  . GLY A 75  ? 0.6165 0.4851 0.7828 0.1138  -0.0413 -0.0922 -122 GLY A CA  
572  C C   . GLY A 75  ? 0.6063 0.4954 0.7387 0.1110  -0.0341 -0.1023 -122 GLY A C   
573  O O   . GLY A 75  ? 0.6230 0.5266 0.7575 0.1165  -0.0341 -0.1159 -122 GLY A O   
574  N N   . LEU A 76  ? 0.5578 0.4490 0.6618 0.1030  -0.0277 -0.0956 -121 LEU A N   
575  C CA  . LEU A 76  ? 0.5647 0.4741 0.6406 0.0998  -0.0206 -0.1042 -121 LEU A CA  
576  C C   . LEU A 76  ? 0.5700 0.4874 0.6261 0.0966  -0.0155 -0.0913 -121 LEU A C   
577  O O   . LEU A 76  ? 0.5719 0.5051 0.6107 0.0942  -0.0096 -0.0974 -121 LEU A O   
578  C CB  . LEU A 76  ? 0.5682 0.4764 0.6256 0.0933  -0.0171 -0.1053 -121 LEU A CB  
579  C CG  . LEU A 76  ? 0.5889 0.4922 0.6635 0.0961  -0.0228 -0.1207 -121 LEU A CG  
580  C CD1 . LEU A 76  ? 0.6230 0.5272 0.6764 0.0899  -0.0193 -0.1201 -121 LEU A CD1 
581  C CD2 . LEU A 76  ? 0.5983 0.5169 0.6836 0.1046  -0.0254 -0.1448 -121 LEU A CD2 
582  N N   . LEU A 77  ? 0.5789 0.4874 0.6383 0.0969  -0.0176 -0.0737 -120 LEU A N   
583  C CA  . LEU A 77  ? 0.5590 0.4752 0.6001 0.0945  -0.0144 -0.0628 -120 LEU A CA  
584  C C   . LEU A 77  ? 0.5634 0.4829 0.6193 0.1020  -0.0194 -0.0587 -120 LEU A C   
585  O O   . LEU A 77  ? 0.5867 0.4954 0.6640 0.1076  -0.0251 -0.0528 -120 LEU A O   
586  C CB  . LEU A 77  ? 0.5604 0.4670 0.5866 0.0891  -0.0125 -0.0451 -120 LEU A CB  
587  C CG  . LEU A 77  ? 0.5361 0.4401 0.5463 0.0817  -0.0077 -0.0476 -120 LEU A CG  
588  C CD1 . LEU A 77  ? 0.5445 0.4394 0.5442 0.0779  -0.0064 -0.0306 -120 LEU A CD1 
589  C CD2 . LEU A 77  ? 0.5263 0.4454 0.5181 0.0776  -0.0021 -0.0559 -120 LEU A CD2 
590  N N   . ALA A 78  ? 0.5821 0.5167 0.6287 0.1022  -0.0176 -0.0613 -119 ALA A N   
591  C CA  . ALA A 78  ? 0.5969 0.5369 0.6552 0.1097  -0.0229 -0.0572 -119 ALA A CA  
592  C C   . ALA A 78  ? 0.6318 0.5673 0.6799 0.1104  -0.0252 -0.0373 -119 ALA A C   
593  O O   . ALA A 78  ? 0.6173 0.5531 0.6442 0.1043  -0.0213 -0.0309 -119 ALA A O   
594  C CB  . ALA A 78  ? 0.5646 0.5247 0.6197 0.1096  -0.0204 -0.0688 -119 ALA A CB  
595  N N   . GLU A 79  ? 0.6324 0.5650 0.6954 0.1190  -0.0316 -0.0275 -118 GLU A N   
596  C CA  . GLU A 79  ? 0.6656 0.5992 0.7167 0.1219  -0.0337 -0.0085 -118 GLU A CA  
597  C C   . GLU A 79  ? 0.6519 0.6038 0.6860 0.1213  -0.0338 -0.0135 -118 GLU A C   
598  O O   . GLU A 79  ? 0.6652 0.6292 0.7081 0.1240  -0.0359 -0.0258 -118 GLU A O   
599  C CB  . GLU A 79  ? 0.6821 0.6106 0.7539 0.1323  -0.0407 0.0051  -118 GLU A CB  
600  C CG  . GLU A 79  ? 0.7211 0.6525 0.7800 0.1371  -0.0424 0.0277  -118 GLU A CG  
601  C CD  . GLU A 79  ? 0.7871 0.7152 0.8678 0.1485  -0.0493 0.0430  -118 GLU A CD  
602  O OE1 . GLU A 79  ? 0.8333 0.7503 0.9429 0.1510  -0.0523 0.0378  -118 GLU A OE1 
603  O OE2 . GLU A 79  ? 0.7850 0.7225 0.8547 0.1558  -0.0522 0.0598  -118 GLU A OE2 
604  N N   . ILE A 80  ? 0.6233 0.5783 0.6360 0.1184  -0.0320 -0.0050 -117 ILE A N   
605  C CA  . ILE A 80  ? 0.6255 0.5975 0.6252 0.1180  -0.0334 -0.0111 -117 ILE A CA  
606  C C   . ILE A 80  ? 0.6578 0.6388 0.6546 0.1287  -0.0407 0.0013  -117 ILE A C   
607  O O   . ILE A 80  ? 0.6618 0.6362 0.6546 0.1334  -0.0414 0.0193  -117 ILE A O   
608  C CB  . ILE A 80  ? 0.6181 0.5897 0.5973 0.1088  -0.0278 -0.0129 -117 ILE A CB  
609  C CG1 . ILE A 80  ? 0.6399 0.6060 0.6051 0.1108  -0.0275 0.0036  -117 ILE A CG1 
610  C CG2 . ILE A 80  ? 0.5967 0.5593 0.5778 0.0994  -0.0206 -0.0222 -117 ILE A CG2 
611  C CD1 . ILE A 80  ? 0.7002 0.6705 0.6458 0.1047  -0.0244 0.0008  -117 ILE A CD1 
612  N N   . THR A 81  ? 0.6737 0.6716 0.6733 0.1331  -0.0461 -0.0076 -116 THR A N   
613  C CA  . THR A 81  ? 0.7137 0.7234 0.7133 0.1456  -0.0548 0.0019  -116 THR A CA  
614  C C   . THR A 81  ? 0.7113 0.7412 0.6991 0.1466  -0.0592 -0.0081 -116 THR A C   
615  O O   . THR A 81  ? 0.7464 0.7908 0.7454 0.1511  -0.0653 -0.0185 -116 THR A O   
616  C CB  . THR A 81  ? 0.7335 0.7440 0.7577 0.1532  -0.0601 -0.0006 -116 THR A CB  
617  O OG1 . THR A 81  ? 0.7148 0.7318 0.7507 0.1472  -0.0578 -0.0214 -116 THR A OG1 
618  C CG2 . THR A 81  ? 0.7484 0.7390 0.7878 0.1545  -0.0581 0.0107  -116 THR A CG2 
619  N N   . PRO A 82  ? 0.6617 0.6937 0.6292 0.1427  -0.0568 -0.0066 -115 PRO A N   
620  C CA  . PRO A 82  ? 0.6425 0.6945 0.6011 0.1454  -0.0630 -0.0168 -115 PRO A CA  
621  C C   . PRO A 82  ? 0.6175 0.6852 0.5690 0.1609  -0.0726 -0.0065 -115 PRO A C   
622  O O   . PRO A 82  ? 0.6307 0.6932 0.5756 0.1681  -0.0722 0.0135  -115 PRO A O   
623  C CB  . PRO A 82  ? 0.6544 0.7018 0.5947 0.1378  -0.0575 -0.0173 -115 PRO A CB  
624  C CG  . PRO A 82  ? 0.6642 0.6941 0.5981 0.1371  -0.0510 0.0008  -115 PRO A CG  
625  C CD  . PRO A 82  ? 0.6494 0.6667 0.6037 0.1360  -0.0491 0.0027  -115 PRO A CD  
626  N N   . ASP A 83  ? 0.5841 0.6725 0.5385 0.1664  -0.0816 -0.0196 -114 ASP A N   
627  C CA  . ASP A 83  ? 0.5853 0.6932 0.5291 0.1823  -0.0919 -0.0117 -114 ASP A CA  
628  C C   . ASP A 83  ? 0.5862 0.7023 0.5030 0.1859  -0.0916 -0.0058 -114 ASP A C   
629  O O   . ASP A 83  ? 0.5569 0.6634 0.4656 0.1755  -0.0844 -0.0103 -114 ASP A O   
630  C CB  . ASP A 83  ? 0.5780 0.7074 0.5347 0.1875  -0.1027 -0.0300 -114 ASP A CB  
631  C CG  . ASP A 83  ? 0.5972 0.7368 0.5537 0.1794  -0.1042 -0.0520 -114 ASP A CG  
632  O OD1 . ASP A 83  ? 0.6104 0.7408 0.5549 0.1709  -0.0974 -0.0529 -114 ASP A OD1 
633  O OD2 . ASP A 83  ? 0.6195 0.7764 0.5902 0.1820  -0.1128 -0.0686 -114 ASP A OD2 
634  N N   . LYS A 84  ? 0.6088 0.7439 0.5112 0.2018  -0.0994 0.0053  -113 LYS A N   
635  C CA  . LYS A 84  ? 0.6148 0.7621 0.4901 0.2079  -0.0990 0.0117  -113 LYS A CA  
636  C C   . LYS A 84  ? 0.6327 0.7917 0.5032 0.2028  -0.1027 -0.0140 -113 LYS A C   
637  O O   . LYS A 84  ? 0.6116 0.7692 0.4662 0.1993  -0.0977 -0.0146 -113 LYS A O   
638  C CB  . LYS A 84  ? 0.5987 0.7698 0.4591 0.2280  -0.1076 0.0275  -113 LYS A CB  
639  C CG  . LYS A 84  ? 0.6219 0.8137 0.4523 0.2374  -0.1085 0.0312  -113 LYS A CG  
640  C CD  . LYS A 84  ? 0.6781 0.8979 0.4924 0.2589  -0.1173 0.0469  -113 LYS A CD  
641  C CE  . LYS A 84  ? 0.7127 0.9627 0.4967 0.2711  -0.1215 0.0418  -113 LYS A CE  
642  N NZ  . LYS A 84  ? 0.7354 0.9777 0.5022 0.2675  -0.1085 0.0588  -113 LYS A NZ  
643  N N   . ALA A 85  ? 0.6487 0.8198 0.5353 0.2025  -0.1118 -0.0357 -112 ALA A N   
644  C CA  . ALA A 85  ? 0.6275 0.8082 0.5168 0.1968  -0.1159 -0.0608 -112 ALA A CA  
645  C C   . ALA A 85  ? 0.6203 0.7776 0.5133 0.1791  -0.1039 -0.0642 -112 ALA A C   
646  O O   . ALA A 85  ? 0.6213 0.7818 0.5047 0.1766  -0.1036 -0.0735 -112 ALA A O   
647  C CB  . ALA A 85  ? 0.6015 0.7946 0.5162 0.1959  -0.1256 -0.0822 -112 ALA A CB  
648  N N   . PHE A 86  ? 0.6162 0.7508 0.5233 0.1678  -0.0945 -0.0573 -111 PHE A N   
649  C CA  . PHE A 86  ? 0.6214 0.7354 0.5302 0.1524  -0.0835 -0.0592 -111 PHE A CA  
650  C C   . PHE A 86  ? 0.6388 0.7418 0.5259 0.1532  -0.0757 -0.0412 -111 PHE A C   
651  O O   . PHE A 86  ? 0.6456 0.7427 0.5251 0.1462  -0.0712 -0.0459 -111 PHE A O   
652  C CB  . PHE A 86  ? 0.5839 0.6806 0.5134 0.1409  -0.0759 -0.0594 -111 PHE A CB  
653  C CG  . PHE A 86  ? 0.5889 0.6668 0.5188 0.1264  -0.0652 -0.0605 -111 PHE A CG  
654  C CD1 . PHE A 86  ? 0.5763 0.6558 0.5180 0.1164  -0.0645 -0.0768 -111 PHE A CD1 
655  C CD2 . PHE A 86  ? 0.6254 0.6847 0.5458 0.1229  -0.0563 -0.0451 -111 PHE A CD2 
656  C CE1 . PHE A 86  ? 0.5973 0.6604 0.5388 0.1040  -0.0549 -0.0759 -111 PHE A CE1 
657  C CE2 . PHE A 86  ? 0.6434 0.6869 0.5631 0.1106  -0.0473 -0.0462 -111 PHE A CE2 
658  C CZ  . PHE A 86  ? 0.6215 0.6671 0.5505 0.1013  -0.0465 -0.0611 -111 PHE A CZ  
659  N N   . GLN A 87  ? 0.5975 0.6976 0.4771 0.1614  -0.0740 -0.0200 -110 GLN A N   
660  C CA  . GLN A 87  ? 0.5941 0.6844 0.4574 0.1614  -0.0658 -0.0018 -110 GLN A CA  
661  C C   . GLN A 87  ? 0.6064 0.7148 0.4473 0.1690  -0.0686 -0.0043 -110 GLN A C   
662  O O   . GLN A 87  ? 0.6396 0.7399 0.4698 0.1643  -0.0611 0.0012  -110 GLN A O   
663  C CB  . GLN A 87  ? 0.6255 0.7112 0.4896 0.1695  -0.0642 0.0224  -110 GLN A CB  
664  C CG  . GLN A 87  ? 0.6504 0.7137 0.5368 0.1610  -0.0594 0.0257  -110 GLN A CG  
665  C CD  . GLN A 87  ? 0.6630 0.7197 0.5547 0.1689  -0.0582 0.0502  -110 GLN A CD  
666  O OE1 . GLN A 87  ? 0.6781 0.7318 0.5594 0.1713  -0.0529 0.0689  -110 GLN A OE1 
667  N NE2 . GLN A 87  ? 0.6408 0.6960 0.5511 0.1731  -0.0631 0.0506  -110 GLN A NE2 
668  N N   . ASP A 88  ? 0.6162 0.7505 0.4503 0.1814  -0.0797 -0.0138 -109 ASP A N   
669  C CA  . ASP A 88  ? 0.6637 0.8195 0.4764 0.1908  -0.0837 -0.0196 -109 ASP A CA  
670  C C   . ASP A 88  ? 0.6951 0.8455 0.5116 0.1800  -0.0826 -0.0412 -109 ASP A C   
671  O O   . ASP A 88  ? 0.7074 0.8700 0.5069 0.1854  -0.0829 -0.0450 -109 ASP A O   
672  C CB  . ASP A 88  ? 0.6911 0.8779 0.4978 0.2073  -0.0978 -0.0289 -109 ASP A CB  
673  C CG  . ASP A 88  ? 0.7654 0.9650 0.5583 0.2230  -0.0990 -0.0033 -109 ASP A CG  
674  O OD1 . ASP A 88  ? 0.7969 0.9842 0.5825 0.2221  -0.0885 0.0220  -109 ASP A OD1 
675  O OD2 . ASP A 88  ? 0.7847 1.0068 0.5767 0.2363  -0.1107 -0.0076 -109 ASP A OD2 
676  N N   . LYS A 89  ? 0.6858 0.8197 0.5252 0.1655  -0.0810 -0.0547 -108 LYS A N   
677  C CA  . LYS A 89  ? 0.6890 0.8170 0.5364 0.1550  -0.0803 -0.0733 -108 LYS A CA  
678  C C   . LYS A 89  ? 0.6991 0.8052 0.5402 0.1446  -0.0680 -0.0628 -108 LYS A C   
679  O O   . LYS A 89  ? 0.6901 0.7919 0.5345 0.1378  -0.0671 -0.0756 -108 LYS A O   
680  C CB  . LYS A 89  ? 0.6809 0.8021 0.5569 0.1438  -0.0826 -0.0893 -108 LYS A CB  
681  C CG  . LYS A 89  ? 0.7296 0.8721 0.6169 0.1527  -0.0951 -0.1017 -108 LYS A CG  
682  C CD  . LYS A 89  ? 0.7694 0.9040 0.6874 0.1405  -0.0944 -0.1127 -108 LYS A CD  
683  C CE  . LYS A 89  ? 0.8256 0.9609 0.7624 0.1313  -0.0972 -0.1339 -108 LYS A CE  
684  N NZ  . LYS A 89  ? 0.8432 0.9887 0.8112 0.1277  -0.1041 -0.1503 -108 LYS A NZ  
685  N N   . LEU A 90  ? 0.6734 0.7651 0.5088 0.1430  -0.0592 -0.0408 -107 LEU A N   
686  C CA  . LEU A 90  ? 0.6338 0.7068 0.4639 0.1342  -0.0485 -0.0311 -107 LEU A CA  
687  C C   . LEU A 90  ? 0.6270 0.7095 0.4356 0.1446  -0.0452 -0.0138 -107 LEU A C   
688  O O   . LEU A 90  ? 0.5707 0.6685 0.3706 0.1573  -0.0488 -0.0021 -107 LEU A O   
689  C CB  . LEU A 90  ? 0.5842 0.6335 0.4273 0.1234  -0.0406 -0.0211 -107 LEU A CB  
690  C CG  . LEU A 90  ? 0.5844 0.6260 0.4487 0.1141  -0.0416 -0.0335 -107 LEU A CG  
691  C CD1 . LEU A 90  ? 0.5916 0.6104 0.4633 0.1032  -0.0320 -0.0253 -107 LEU A CD1 
692  C CD2 . LEU A 90  ? 0.5696 0.6165 0.4426 0.1085  -0.0454 -0.0535 -107 LEU A CD2 
693  N N   . TYR A 91  ? 0.6233 0.6978 0.4245 0.1396  -0.0382 -0.0114 -106 TYR A N   
694  C CA  . TYR A 91  ? 0.6208 0.7054 0.4034 0.1484  -0.0332 0.0056  -106 TYR A CA  
695  C C   . TYR A 91  ? 0.6007 0.6754 0.3866 0.1493  -0.0269 0.0316  -106 TYR A C   
696  O O   . TYR A 91  ? 0.5924 0.6435 0.3937 0.1380  -0.0220 0.0357  -106 TYR A O   
697  C CB  . TYR A 91  ? 0.5898 0.6655 0.3683 0.1413  -0.0265 0.0025  -106 TYR A CB  
698  C CG  . TYR A 91  ? 0.5987 0.6880 0.3731 0.1440  -0.0330 -0.0207 -106 TYR A CG  
699  C CD1 . TYR A 91  ? 0.6426 0.7611 0.3988 0.1595  -0.0382 -0.0253 -106 TYR A CD1 
700  C CD2 . TYR A 91  ? 0.5437 0.6179 0.3334 0.1320  -0.0343 -0.0382 -106 TYR A CD2 
701  C CE1 . TYR A 91  ? 0.6770 0.8084 0.4326 0.1627  -0.0456 -0.0502 -106 TYR A CE1 
702  C CE2 . TYR A 91  ? 0.5948 0.6802 0.3862 0.1344  -0.0413 -0.0605 -106 TYR A CE2 
703  C CZ  . TYR A 91  ? 0.6581 0.7712 0.4335 0.1495  -0.0473 -0.0679 -106 TYR A CZ  
704  O OH  . TYR A 91  ? 0.7256 0.8495 0.5061 0.1522  -0.0555 -0.0931 -106 TYR A OH  
705  N N   . PRO A 92  ? 0.6057 0.6985 0.3789 0.1629  -0.0270 0.0496  -105 PRO A N   
706  C CA  . PRO A 92  ? 0.6504 0.7324 0.4321 0.1635  -0.0212 0.0760  -105 PRO A CA  
707  C C   . PRO A 92  ? 0.6797 0.7367 0.4729 0.1509  -0.0110 0.0854  -105 PRO A C   
708  O O   . PRO A 92  ? 0.6834 0.7211 0.4955 0.1446  -0.0090 0.0936  -105 PRO A O   
709  C CB  . PRO A 92  ? 0.6906 0.7992 0.4531 0.1799  -0.0203 0.0953  -105 PRO A CB  
710  C CG  . PRO A 92  ? 0.6787 0.8144 0.4251 0.1908  -0.0308 0.0749  -105 PRO A CG  
711  C CD  . PRO A 92  ? 0.6128 0.7378 0.3652 0.1790  -0.0329 0.0468  -105 PRO A CD  
712  N N   . PHE A 93  ? 0.6717 0.7293 0.4558 0.1472  -0.0055 0.0822  -104 PHE A N   
713  C CA  . PHE A 93  ? 0.6536 0.6907 0.4486 0.1368  0.0037  0.0927  -104 PHE A CA  
714  C C   . PHE A 93  ? 0.6728 0.6847 0.4852 0.1228  0.0030  0.0790  -104 PHE A C   
715  O O   . PHE A 93  ? 0.6938 0.6871 0.5211 0.1153  0.0081  0.0882  -104 PHE A O   
716  C CB  . PHE A 93  ? 0.6338 0.6794 0.4155 0.1370  0.0095  0.0920  -104 PHE A CB  
717  C CG  . PHE A 93  ? 0.6168 0.6579 0.3956 0.1300  0.0065  0.0670  -104 PHE A CG  
718  C CD1 . PHE A 93  ? 0.6453 0.7055 0.4115 0.1372  -0.0006 0.0491  -104 PHE A CD1 
719  C CD2 . PHE A 93  ? 0.6186 0.6370 0.4091 0.1167  0.0105  0.0616  -104 PHE A CD2 
720  C CE1 . PHE A 93  ? 0.6177 0.6725 0.3860 0.1304  -0.0037 0.0265  -104 PHE A CE1 
721  C CE2 . PHE A 93  ? 0.6120 0.6261 0.4015 0.1105  0.0081  0.0412  -104 PHE A CE2 
722  C CZ  . PHE A 93  ? 0.6142 0.6457 0.3941 0.1171  0.0011  0.0243  -104 PHE A CZ  
723  N N   . THR A 94  ? 0.6355 0.6478 0.4480 0.1195  -0.0033 0.0572  -103 THR A N   
724  C CA  . THR A 94  ? 0.6052 0.5971 0.4331 0.1074  -0.0029 0.0464  -103 THR A CA  
725  C C   . THR A 94  ? 0.5877 0.5719 0.4312 0.1080  -0.0050 0.0523  -103 THR A C   
726  O O   . THR A 94  ? 0.5685 0.5349 0.4264 0.0998  -0.0022 0.0514  -103 THR A O   
727  C CB  . THR A 94  ? 0.5606 0.5555 0.3875 0.1028  -0.0075 0.0239  -103 THR A CB  
728  O OG1 . THR A 94  ? 0.5695 0.5782 0.3978 0.1094  -0.0153 0.0157  -103 THR A OG1 
729  C CG2 . THR A 94  ? 0.5604 0.5648 0.3740 0.1047  -0.0071 0.0173  -103 THR A CG2 
730  N N   . TRP A 95  ? 0.5715 0.5699 0.4130 0.1185  -0.0105 0.0571  -102 TRP A N   
731  C CA  . TRP A 95  ? 0.5833 0.5746 0.4414 0.1205  -0.0126 0.0646  -102 TRP A CA  
732  C C   . TRP A 95  ? 0.6252 0.6030 0.4949 0.1195  -0.0067 0.0851  -102 TRP A C   
733  O O   . TRP A 95  ? 0.6446 0.6066 0.5341 0.1151  -0.0065 0.0856  -102 TRP A O   
734  C CB  . TRP A 95  ? 0.5576 0.5686 0.4107 0.1337  -0.0201 0.0685  -102 TRP A CB  
735  C CG  . TRP A 95  ? 0.5350 0.5558 0.3893 0.1342  -0.0278 0.0476  -102 TRP A CG  
736  C CD1 . TRP A 95  ? 0.5684 0.6111 0.4097 0.1422  -0.0347 0.0380  -102 TRP A CD1 
737  C CD2 . TRP A 95  ? 0.5406 0.5517 0.4119 0.1266  -0.0295 0.0334  -102 TRP A CD2 
738  N NE1 . TRP A 95  ? 0.5952 0.6411 0.4473 0.1392  -0.0408 0.0188  -102 TRP A NE1 
739  C CE2 . TRP A 95  ? 0.5752 0.6026 0.4452 0.1297  -0.0370 0.0167  -102 TRP A CE2 
740  C CE3 . TRP A 95  ? 0.5608 0.5532 0.4490 0.1182  -0.0254 0.0320  -102 TRP A CE3 
741  C CZ2 . TRP A 95  ? 0.5805 0.6058 0.4666 0.1238  -0.0393 0.0013  -102 TRP A CZ2 
742  C CZ3 . TRP A 95  ? 0.5814 0.5731 0.4825 0.1134  -0.0276 0.0158  -102 TRP A CZ3 
743  C CH2 . TRP A 95  ? 0.5820 0.5899 0.4824 0.1158  -0.0338 0.0018  -102 TRP A CH2 
744  N N   . ASP A 96  ? 0.6162 0.6015 0.4758 0.1242  -0.0020 0.1020  -101 ASP A N   
745  C CA  . ASP A 96  ? 0.5919 0.5649 0.4667 0.1222  0.0043  0.1224  -101 ASP A CA  
746  C C   . ASP A 96  ? 0.5903 0.5413 0.4798 0.1093  0.0075  0.1126  -101 ASP A C   
747  O O   . ASP A 96  ? 0.5622 0.4981 0.4745 0.1064  0.0086  0.1207  -101 ASP A O   
748  C CB  . ASP A 96  ? 0.6111 0.5978 0.4716 0.1274  0.0107  0.1398  -101 ASP A CB  
749  C CG  . ASP A 96  ? 0.6581 0.6695 0.5036 0.1424  0.0081  0.1535  -101 ASP A CG  
750  O OD1 . ASP A 96  ? 0.6638 0.6772 0.5170 0.1488  0.0023  0.1582  -101 ASP A OD1 
751  O OD2 . ASP A 96  ? 0.6915 0.7224 0.5163 0.1487  0.0115  0.1583  -101 ASP A OD2 
752  N N   . ALA A 97  ? 0.5406 0.4901 0.4186 0.1019  0.0082  0.0942  -100 ALA A N   
753  C CA  . ALA A 97  ? 0.5206 0.4523 0.4093 0.0911  0.0113  0.0863  -100 ALA A CA  
754  C C   . ALA A 97  ? 0.5343 0.4536 0.4407 0.0873  0.0077  0.0760  -100 ALA A C   
755  O O   . ALA A 97  ? 0.5535 0.4587 0.4731 0.0805  0.0094  0.0721  -100 ALA A O   
756  C CB  . ALA A 97  ? 0.5145 0.4483 0.3877 0.0852  0.0125  0.0711  -100 ALA A CB  
757  N N   . VAL A 98  ? 0.5216 0.4477 0.4292 0.0921  0.0025  0.0700  -99  VAL A N   
758  C CA  . VAL A 98  ? 0.5309 0.4490 0.4544 0.0896  -0.0006 0.0583  -99  VAL A CA  
759  C C   . VAL A 98  ? 0.5889 0.5059 0.5301 0.0975  -0.0045 0.0691  -99  VAL A C   
760  O O   . VAL A 98  ? 0.6026 0.5192 0.5551 0.0990  -0.0087 0.0590  -99  VAL A O   
761  C CB  . VAL A 98  ? 0.5498 0.4766 0.4643 0.0875  -0.0031 0.0401  -99  VAL A CB  
762  C CG1 . VAL A 98  ? 0.5364 0.4616 0.4380 0.0792  0.0007  0.0307  -99  VAL A CG1 
763  C CG2 . VAL A 98  ? 0.5387 0.4828 0.4430 0.0961  -0.0078 0.0424  -99  VAL A CG2 
764  N N   . ARG A 99  ? 0.6127 0.5308 0.5573 0.1030  -0.0030 0.0905  -98  ARG A N   
765  C CA  . ARG A 99  ? 0.6700 0.5849 0.6353 0.1104  -0.0062 0.1050  -98  ARG A CA  
766  C C   . ARG A 99  ? 0.6906 0.5866 0.6833 0.1056  -0.0040 0.1116  -98  ARG A C   
767  O O   . ARG A 99  ? 0.7291 0.6211 0.7212 0.1014  0.0015  0.1213  -98  ARG A O   
768  C CB  . ARG A 99  ? 0.6804 0.6104 0.6341 0.1206  -0.0058 0.1269  -98  ARG A CB  
769  C CG  . ARG A 99  ? 0.7316 0.6594 0.7069 0.1294  -0.0097 0.1438  -98  ARG A CG  
770  C CD  . ARG A 99  ? 0.7810 0.7284 0.7406 0.1412  -0.0094 0.1666  -98  ARG A CD  
771  N NE  . ARG A 99  ? 0.7894 0.7578 0.7221 0.1472  -0.0142 0.1539  -98  ARG A NE  
772  C CZ  . ARG A 99  ? 0.7718 0.7567 0.6768 0.1488  -0.0118 0.1514  -98  ARG A CZ  
773  N NH1 . ARG A 99  ? 0.7620 0.7457 0.6605 0.1450  -0.0037 0.1618  -98  ARG A NH1 
774  N NH2 . ARG A 99  ? 0.7623 0.7659 0.6485 0.1546  -0.0179 0.1375  -98  ARG A NH2 
775  N N   . TYR A 100 ? 0.6519 0.5372 0.6702 0.1063  -0.0087 0.1044  -97  TYR A N   
776  C CA  . TYR A 100 ? 0.6508 0.5184 0.6999 0.1023  -0.0087 0.1063  -97  TYR A CA  
777  C C   . TYR A 100 ? 0.6982 0.5595 0.7775 0.1100  -0.0138 0.1180  -97  TYR A C   
778  O O   . TYR A 100 ? 0.6954 0.5596 0.7797 0.1150  -0.0195 0.1071  -97  TYR A O   
779  C CB  . TYR A 100 ? 0.6216 0.4815 0.6754 0.0952  -0.0102 0.0800  -97  TYR A CB  
780  C CG  . TYR A 100 ? 0.6089 0.4523 0.6947 0.0916  -0.0115 0.0784  -97  TYR A CG  
781  C CD1 . TYR A 100 ? 0.5895 0.4267 0.6796 0.0860  -0.0070 0.0883  -97  TYR A CD1 
782  C CD2 . TYR A 100 ? 0.6575 0.4923 0.7731 0.0945  -0.0180 0.0658  -97  TYR A CD2 
783  C CE1 . TYR A 100 ? 0.6191 0.4415 0.7433 0.0827  -0.0093 0.0858  -97  TYR A CE1 
784  C CE2 . TYR A 100 ? 0.6362 0.4559 0.7863 0.0919  -0.0209 0.0621  -97  TYR A CE2 
785  C CZ  . TYR A 100 ? 0.6448 0.4583 0.7990 0.0857  -0.0167 0.0721  -97  TYR A CZ  
786  O OH  . TYR A 100 ? 0.6842 0.4837 0.8755 0.0830  -0.0205 0.0667  -97  TYR A OH  
787  N N   . ASN A 101 ? 0.7528 0.6058 0.8543 0.1111  -0.0116 0.1410  -96  ASN A N   
788  C CA  . ASN A 101 ? 0.8024 0.6479 0.9372 0.1184  -0.0161 0.1566  -96  ASN A CA  
789  C C   . ASN A 101 ? 0.7716 0.6319 0.8910 0.1290  -0.0200 0.1630  -96  ASN A C   
790  O O   . ASN A 101 ? 0.7818 0.6385 0.9209 0.1349  -0.0269 0.1579  -96  ASN A O   
791  C CB  . ASN A 101 ? 0.8622 0.6906 1.0333 0.1162  -0.0227 0.1371  -96  ASN A CB  
792  C CG  . ASN A 101 ? 0.9155 0.7282 1.1141 0.1083  -0.0208 0.1373  -96  ASN A CG  
793  O OD1 . ASN A 101 ? 0.9296 0.7409 1.1329 0.1060  -0.0149 0.1603  -96  ASN A OD1 
794  N ND2 . ASN A 101 ? 0.9416 0.7444 1.1589 0.1047  -0.0260 0.1109  -96  ASN A ND2 
795  N N   . GLY A 102 ? 0.7236 0.6022 0.8084 0.1321  -0.0161 0.1728  -95  GLY A N   
796  C CA  . GLY A 102 ? 0.7292 0.6253 0.7972 0.1432  -0.0201 0.1802  -95  GLY A CA  
797  C C   . GLY A 102 ? 0.7356 0.6409 0.7878 0.1440  -0.0258 0.1535  -95  GLY A C   
798  O O   . GLY A 102 ? 0.7769 0.6980 0.8171 0.1535  -0.0305 0.1571  -95  GLY A O   
799  N N   . LYS A 103 ? 0.7051 0.6031 0.7577 0.1350  -0.0256 0.1273  -94  LYS A N   
800  C CA  . LYS A 103 ? 0.6792 0.5872 0.7198 0.1351  -0.0296 0.1036  -94  LYS A CA  
801  C C   . LYS A 103 ? 0.6648 0.5784 0.6791 0.1261  -0.0248 0.0875  -94  LYS A C   
802  O O   . LYS A 103 ? 0.6435 0.5473 0.6566 0.1177  -0.0196 0.0858  -94  LYS A O   
803  C CB  . LYS A 103 ? 0.6779 0.5756 0.7460 0.1347  -0.0341 0.0868  -94  LYS A CB  
804  C CG  . LYS A 103 ? 0.7052 0.5923 0.8074 0.1428  -0.0390 0.1030  -94  LYS A CG  
805  C CD  . LYS A 103 ? 0.7171 0.5985 0.8461 0.1455  -0.0453 0.0840  -94  LYS A CD  
806  C CE  . LYS A 103 ? 0.7617 0.6403 0.9175 0.1572  -0.0522 0.1006  -94  LYS A CE  
807  N NZ  . LYS A 103 ? 0.7864 0.6776 0.9429 0.1642  -0.0586 0.0855  -94  LYS A NZ  
808  N N   . LEU A 104 ? 0.6534 0.5831 0.6486 0.1279  -0.0272 0.0762  -93  LEU A N   
809  C CA  . LEU A 104 ? 0.6182 0.5527 0.5935 0.1195  -0.0236 0.0599  -93  LEU A CA  
810  C C   . LEU A 104 ? 0.5855 0.5121 0.5728 0.1123  -0.0226 0.0397  -93  LEU A C   
811  O O   . LEU A 104 ? 0.5639 0.4934 0.5655 0.1157  -0.0266 0.0298  -93  LEU A O   
812  C CB  . LEU A 104 ? 0.6145 0.5689 0.5719 0.1240  -0.0274 0.0536  -93  LEU A CB  
813  C CG  . LEU A 104 ? 0.6060 0.5742 0.5475 0.1335  -0.0294 0.0706  -93  LEU A CG  
814  C CD1 . LEU A 104 ? 0.6105 0.5992 0.5384 0.1383  -0.0354 0.0585  -93  LEU A CD1 
815  C CD2 . LEU A 104 ? 0.5988 0.5646 0.5250 0.1295  -0.0228 0.0801  -93  LEU A CD2 
816  N N   . ILE A 105 ? 0.5491 0.4676 0.5302 0.1032  -0.0171 0.0338  -92  ILE A N   
817  C CA  . ILE A 105 ? 0.5566 0.4695 0.5465 0.0973  -0.0155 0.0163  -92  ILE A CA  
818  C C   . ILE A 105 ? 0.5798 0.4999 0.5515 0.0897  -0.0114 0.0036  -92  ILE A C   
819  O O   . ILE A 105 ? 0.5725 0.4910 0.5474 0.0849  -0.0089 -0.0094 -92  ILE A O   
820  C CB  . ILE A 105 ? 0.5874 0.4841 0.5921 0.0941  -0.0140 0.0190  -92  ILE A CB  
821  C CG1 . ILE A 105 ? 0.6280 0.5203 0.6188 0.0893  -0.0094 0.0308  -92  ILE A CG1 
822  C CG2 . ILE A 105 ? 0.6324 0.5205 0.6648 0.1014  -0.0189 0.0289  -92  ILE A CG2 
823  C CD1 . ILE A 105 ? 0.6794 0.5617 0.6725 0.0817  -0.0063 0.0225  -92  ILE A CD1 
824  N N   . ALA A 106 ? 0.5933 0.5223 0.5467 0.0890  -0.0107 0.0071  -91  ALA A N   
825  C CA  . ALA A 106 ? 0.5531 0.4877 0.4936 0.0817  -0.0072 -0.0036 -91  ALA A CA  
826  C C   . ALA A 106 ? 0.5483 0.4956 0.4762 0.0841  -0.0098 -0.0026 -91  ALA A C   
827  O O   . ALA A 106 ? 0.5469 0.4983 0.4694 0.0910  -0.0129 0.0084  -91  ALA A O   
828  C CB  . ALA A 106 ? 0.5319 0.4560 0.4643 0.0744  -0.0021 -0.0021 -91  ALA A CB  
829  N N   . TYR A 107 ? 0.5137 0.4683 0.4380 0.0787  -0.0086 -0.0142 -90  TYR A N   
830  C CA  . TYR A 107 ? 0.5573 0.5229 0.4717 0.0798  -0.0115 -0.0166 -90  TYR A CA  
831  C C   . TYR A 107 ? 0.5590 0.5181 0.4601 0.0745  -0.0076 -0.0138 -90  TYR A C   
832  O O   . TYR A 107 ? 0.5636 0.5153 0.4651 0.0662  -0.0026 -0.0182 -90  TYR A O   
833  C CB  . TYR A 107 ? 0.5690 0.5455 0.4920 0.0761  -0.0126 -0.0304 -90  TYR A CB  
834  C CG  . TYR A 107 ? 0.5596 0.5468 0.4959 0.0826  -0.0177 -0.0346 -90  TYR A CG  
835  C CD1 . TYR A 107 ? 0.5647 0.5653 0.4997 0.0908  -0.0255 -0.0352 -90  TYR A CD1 
836  C CD2 . TYR A 107 ? 0.5533 0.5391 0.5032 0.0815  -0.0151 -0.0390 -90  TYR A CD2 
837  C CE1 . TYR A 107 ? 0.5747 0.5860 0.5229 0.0973  -0.0310 -0.0393 -90  TYR A CE1 
838  C CE2 . TYR A 107 ? 0.5500 0.5464 0.5141 0.0879  -0.0199 -0.0437 -90  TYR A CE2 
839  C CZ  . TYR A 107 ? 0.5741 0.5825 0.5376 0.0954  -0.0279 -0.0433 -90  TYR A CZ  
840  O OH  . TYR A 107 ? 0.5921 0.6116 0.5703 0.1022  -0.0333 -0.0479 -90  TYR A OH  
841  N N   . PRO A 108 ? 0.5423 0.5056 0.4313 0.0797  -0.0096 -0.0066 -89  PRO A N   
842  C CA  . PRO A 108 ? 0.5141 0.4729 0.3919 0.0752  -0.0062 -0.0059 -89  PRO A CA  
843  C C   . PRO A 108 ? 0.5405 0.5058 0.4187 0.0706  -0.0079 -0.0195 -89  PRO A C   
844  O O   . PRO A 108 ? 0.5812 0.5588 0.4648 0.0737  -0.0133 -0.0280 -89  PRO A O   
845  C CB  . PRO A 108 ? 0.4829 0.4490 0.3490 0.0842  -0.0079 0.0056  -89  PRO A CB  
846  C CG  . PRO A 108 ? 0.5234 0.5034 0.3918 0.0932  -0.0144 0.0052  -89  PRO A CG  
847  C CD  . PRO A 108 ? 0.5247 0.4993 0.4093 0.0907  -0.0150 0.0011  -89  PRO A CD  
848  N N   . ILE A 109 ? 0.4944 0.4511 0.3698 0.0630  -0.0036 -0.0215 -88  ILE A N   
849  C CA  . ILE A 109 ? 0.5182 0.4778 0.3993 0.0572  -0.0044 -0.0329 -88  ILE A CA  
850  C C   . ILE A 109 ? 0.5441 0.5043 0.4158 0.0583  -0.0056 -0.0346 -88  ILE A C   
851  O O   . ILE A 109 ? 0.5566 0.5285 0.4291 0.0624  -0.0116 -0.0439 -88  ILE A O   
852  C CB  . ILE A 109 ? 0.5420 0.4919 0.4311 0.0474  0.0016  -0.0339 -88  ILE A CB  
853  C CG1 . ILE A 109 ? 0.5775 0.5277 0.4742 0.0478  0.0035  -0.0327 -88  ILE A CG1 
854  C CG2 . ILE A 109 ? 0.5598 0.5129 0.4594 0.0413  0.0011  -0.0428 -88  ILE A CG2 
855  C CD1 . ILE A 109 ? 0.5775 0.5409 0.4859 0.0511  -0.0009 -0.0399 -88  ILE A CD1 
856  N N   . ALA A 110 ? 0.5519 0.5014 0.4157 0.0556  -0.0006 -0.0268 -87  ALA A N   
857  C CA  . ALA A 110 ? 0.5567 0.5058 0.4137 0.0557  -0.0007 -0.0290 -87  ALA A CA  
858  C C   . ALA A 110 ? 0.5334 0.4764 0.3797 0.0577  0.0039  -0.0170 -87  ALA A C   
859  O O   . ALA A 110 ? 0.5435 0.4771 0.3918 0.0549  0.0078  -0.0087 -87  ALA A O   
860  C CB  . ALA A 110 ? 0.5523 0.4929 0.4188 0.0465  0.0011  -0.0356 -87  ALA A CB  
861  N N   . VAL A 111 ? 0.5314 0.4811 0.3686 0.0625  0.0032  -0.0173 -86  VAL A N   
862  C CA  . VAL A 111 ? 0.5329 0.4795 0.3621 0.0643  0.0081  -0.0059 -86  VAL A CA  
863  C C   . VAL A 111 ? 0.5451 0.4811 0.3762 0.0575  0.0107  -0.0096 -86  VAL A C   
864  O O   . VAL A 111 ? 0.5645 0.5039 0.3968 0.0574  0.0076  -0.0205 -86  VAL A O   
865  C CB  . VAL A 111 ? 0.5424 0.5068 0.3595 0.0754  0.0067  -0.0027 -86  VAL A CB  
866  C CG1 . VAL A 111 ? 0.5379 0.5011 0.3491 0.0768  0.0132  0.0101  -86  VAL A CG1 
867  C CG2 . VAL A 111 ? 0.5584 0.5336 0.3736 0.0829  0.0038  0.0031  -86  VAL A CG2 
868  N N   . GLU A 112 ? 0.5374 0.4611 0.3706 0.0525  0.0154  -0.0011 -85  GLU A N   
869  C CA  . GLU A 112 ? 0.5821 0.4955 0.4173 0.0465  0.0177  -0.0026 -85  GLU A CA  
870  C C   . GLU A 112 ? 0.6085 0.5217 0.4396 0.0487  0.0215  0.0061  -85  GLU A C   
871  O O   . GLU A 112 ? 0.6412 0.5535 0.4739 0.0501  0.0243  0.0168  -85  GLU A O   
872  C CB  . GLU A 112 ? 0.6192 0.5203 0.4611 0.0389  0.0194  -0.0016 -85  GLU A CB  
873  C CG  . GLU A 112 ? 0.6388 0.5414 0.4864 0.0370  0.0176  -0.0064 -85  GLU A CG  
874  C CD  . GLU A 112 ? 0.6029 0.4971 0.4548 0.0312  0.0202  -0.0052 -85  GLU A CD  
875  O OE1 . GLU A 112 ? 0.5808 0.4685 0.4316 0.0305  0.0221  -0.0001 -85  GLU A OE1 
876  O OE2 . GLU A 112 ? 0.5919 0.4876 0.4491 0.0279  0.0203  -0.0097 -85  GLU A OE2 
877  N N   . ALA A 113 ? 0.5596 0.4735 0.3886 0.0488  0.0217  0.0017  -84  ALA A N   
878  C CA  . ALA A 113 ? 0.5356 0.4496 0.3632 0.0499  0.0258  0.0089  -84  ALA A CA  
879  C C   . ALA A 113 ? 0.5613 0.4669 0.3924 0.0455  0.0251  0.0025  -84  ALA A C   
880  O O   . ALA A 113 ? 0.5386 0.4430 0.3721 0.0442  0.0214  -0.0078 -84  ALA A O   
881  C CB  . ALA A 113 ? 0.5073 0.4388 0.3264 0.0592  0.0274  0.0115  -84  ALA A CB  
882  N N   . LEU A 114 ? 0.5416 0.4408 0.3760 0.0428  0.0282  0.0088  -83  LEU A N   
883  C CA  . LEU A 114 ? 0.5535 0.4458 0.3913 0.0398  0.0272  0.0041  -83  LEU A CA  
884  C C   . LEU A 114 ? 0.5416 0.4443 0.3769 0.0458  0.0270  -0.0018 -83  LEU A C   
885  O O   . LEU A 114 ? 0.5325 0.4488 0.3624 0.0523  0.0300  0.0018  -83  LEU A O   
886  C CB  . LEU A 114 ? 0.5322 0.4169 0.3750 0.0363  0.0296  0.0112  -83  LEU A CB  
887  C CG  . LEU A 114 ? 0.5214 0.3966 0.3677 0.0311  0.0286  0.0134  -83  LEU A CG  
888  C CD1 . LEU A 114 ? 0.5010 0.3717 0.3546 0.0292  0.0297  0.0187  -83  LEU A CD1 
889  C CD2 . LEU A 114 ? 0.5115 0.3798 0.3572 0.0272  0.0258  0.0077  -83  LEU A CD2 
890  N N   . SER A 115 ? 0.5232 0.4202 0.3636 0.0441  0.0236  -0.0107 -82  SER A N   
891  C CA  . SER A 115 ? 0.4885 0.3938 0.3298 0.0499  0.0226  -0.0185 -82  SER A CA  
892  C C   . SER A 115 ? 0.5030 0.3973 0.3525 0.0464  0.0219  -0.0189 -82  SER A C   
893  O O   . SER A 115 ? 0.5235 0.4046 0.3768 0.0399  0.0212  -0.0142 -82  SER A O   
894  C CB  . SER A 115 ? 0.4989 0.4108 0.3422 0.0539  0.0171  -0.0327 -82  SER A CB  
895  O OG  . SER A 115 ? 0.5446 0.4651 0.3817 0.0563  0.0162  -0.0332 -82  SER A OG  
896  N N   . LEU A 116 ? 0.5127 0.4144 0.3646 0.0519  0.0217  -0.0252 -81  LEU A N   
897  C CA  . LEU A 116 ? 0.5532 0.4447 0.4151 0.0497  0.0193  -0.0279 -81  LEU A CA  
898  C C   . LEU A 116 ? 0.5392 0.4237 0.4116 0.0489  0.0129  -0.0390 -81  LEU A C   
899  O O   . LEU A 116 ? 0.6068 0.5013 0.4808 0.0546  0.0099  -0.0510 -81  LEU A O   
900  C CB  . LEU A 116 ? 0.5333 0.4364 0.3963 0.0563  0.0218  -0.0304 -81  LEU A CB  
901  C CG  . LEU A 116 ? 0.4590 0.3533 0.3338 0.0558  0.0189  -0.0339 -81  LEU A CG  
902  C CD1 . LEU A 116 ? 0.4240 0.3061 0.3005 0.0490  0.0201  -0.0218 -81  LEU A CD1 
903  C CD2 . LEU A 116 ? 0.4421 0.3526 0.3185 0.0644  0.0214  -0.0402 -81  LEU A CD2 
904  N N   . ILE A 117 ? 0.5050 0.3738 0.3855 0.0422  0.0107  -0.0346 -80  ILE A N   
905  C CA  . ILE A 117 ? 0.5042 0.3641 0.4001 0.0400  0.0053  -0.0417 -80  ILE A CA  
906  C C   . ILE A 117 ? 0.4814 0.3330 0.3888 0.0408  0.0029  -0.0419 -80  ILE A C   
907  O O   . ILE A 117 ? 0.4706 0.3166 0.3742 0.0384  0.0050  -0.0314 -80  ILE A O   
908  C CB  . ILE A 117 ? 0.5179 0.3676 0.4163 0.0320  0.0057  -0.0333 -80  ILE A CB  
909  C CG1 . ILE A 117 ? 0.5011 0.3589 0.3895 0.0316  0.0077  -0.0334 -80  ILE A CG1 
910  C CG2 . ILE A 117 ? 0.5572 0.3977 0.4766 0.0291  0.0008  -0.0383 -80  ILE A CG2 
911  C CD1 . ILE A 117 ? 0.4717 0.3224 0.3600 0.0243  0.0097  -0.0239 -80  ILE A CD1 
912  N N   . TYR A 118 ? 0.4940 0.3464 0.4161 0.0452  -0.0022 -0.0550 -79  TYR A N   
913  C CA  . TYR A 118 ? 0.5200 0.3662 0.4546 0.0478  -0.0050 -0.0570 -79  TYR A CA  
914  C C   . TYR A 118 ? 0.5287 0.3635 0.4887 0.0466  -0.0120 -0.0646 -79  TYR A C   
915  O O   . TYR A 118 ? 0.5514 0.3884 0.5206 0.0468  -0.0155 -0.0751 -79  TYR A O   
916  C CB  . TYR A 118 ? 0.5146 0.3767 0.4447 0.0570  -0.0039 -0.0671 -79  TYR A CB  
917  C CG  . TYR A 118 ? 0.5403 0.4158 0.4762 0.0651  -0.0080 -0.0870 -79  TYR A CG  
918  C CD1 . TYR A 118 ? 0.5196 0.4096 0.4422 0.0679  -0.0064 -0.0916 -79  TYR A CD1 
919  C CD2 . TYR A 118 ? 0.5666 0.4414 0.5217 0.0709  -0.0142 -0.1020 -79  TYR A CD2 
920  C CE1 . TYR A 118 ? 0.5566 0.4615 0.4827 0.0765  -0.0110 -0.1106 -79  TYR A CE1 
921  C CE2 . TYR A 118 ? 0.6049 0.4940 0.5659 0.0795  -0.0191 -0.1231 -79  TYR A CE2 
922  C CZ  . TYR A 118 ? 0.6220 0.5272 0.5672 0.0825  -0.0176 -0.1276 -79  TYR A CZ  
923  O OH  . TYR A 118 ? 0.6843 0.6063 0.6344 0.0923  -0.0235 -0.1500 -79  TYR A OH  
924  N N   . ASN A 119 ? 0.5276 0.3502 0.5008 0.0456  -0.0145 -0.0589 -78  ASN A N   
925  C CA  . ASN A 119 ? 0.5436 0.3525 0.5458 0.0440  -0.0211 -0.0625 -78  ASN A CA  
926  C C   . ASN A 119 ? 0.5538 0.3683 0.5724 0.0531  -0.0272 -0.0833 -78  ASN A C   
927  O O   . ASN A 119 ? 0.5480 0.3656 0.5657 0.0587  -0.0273 -0.0854 -78  ASN A O   
928  C CB  . ASN A 119 ? 0.5277 0.3216 0.5358 0.0396  -0.0208 -0.0441 -78  ASN A CB  
929  C CG  . ASN A 119 ? 0.5686 0.3472 0.6095 0.0377  -0.0269 -0.0436 -78  ASN A CG  
930  O OD1 . ASN A 119 ? 0.5853 0.3631 0.6489 0.0427  -0.0335 -0.0611 -78  ASN A OD1 
931  N ND2 . ASN A 119 ? 0.4922 0.2592 0.5375 0.0314  -0.0252 -0.0236 -78  ASN A ND2 
932  N N   . LYS A 120 ? 0.5603 0.3784 0.5946 0.0553  -0.0326 -0.1004 -77  LYS A N   
933  C CA  . LYS A 120 ? 0.5929 0.4202 0.6418 0.0655  -0.0391 -0.1242 -77  LYS A CA  
934  C C   . LYS A 120 ? 0.6253 0.4375 0.7048 0.0671  -0.0456 -0.1267 -77  LYS A C   
935  O O   . LYS A 120 ? 0.6599 0.4803 0.7508 0.0769  -0.0507 -0.1463 -77  LYS A O   
936  C CB  . LYS A 120 ? 0.6290 0.4643 0.6902 0.0678  -0.0452 -0.1440 -77  LYS A CB  
937  C CG  . LYS A 120 ? 0.6417 0.4949 0.6758 0.0690  -0.0407 -0.1455 -77  LYS A CG  
938  C CD  . LYS A 120 ? 0.7026 0.5646 0.7531 0.0729  -0.0492 -0.1684 -77  LYS A CD  
939  C CE  . LYS A 120 ? 0.7166 0.6004 0.7392 0.0771  -0.0460 -0.1722 -77  LYS A CE  
940  N NZ  . LYS A 120 ? 0.7478 0.6436 0.7871 0.0831  -0.0562 -0.1981 -77  LYS A NZ  
941  N N   . ASP A 121 ? 0.5815 0.3731 0.6747 0.0587  -0.0457 -0.1075 -76  ASP A N   
942  C CA  . ASP A 121 ? 0.6146 0.3914 0.7376 0.0608  -0.0519 -0.1073 -76  ASP A CA  
943  C C   . ASP A 121 ? 0.6500 0.4282 0.7588 0.0647  -0.0489 -0.0978 -76  ASP A C   
944  O O   . ASP A 121 ? 0.6959 0.4682 0.8269 0.0706  -0.0548 -0.1047 -76  ASP A O   
945  C CB  . ASP A 121 ? 0.5907 0.3463 0.7381 0.0512  -0.0535 -0.0892 -76  ASP A CB  
946  C CG  . ASP A 121 ? 0.6230 0.3749 0.7994 0.0482  -0.0592 -0.1023 -76  ASP A CG  
947  O OD1 . ASP A 121 ? 0.6391 0.4026 0.8236 0.0554  -0.0650 -0.1293 -76  ASP A OD1 
948  O OD2 . ASP A 121 ? 0.6385 0.3780 0.8300 0.0389  -0.0577 -0.0860 -76  ASP A OD2 
949  N N   . LEU A 122 ? 0.6031 0.3889 0.6792 0.0620  -0.0407 -0.0835 -75  LEU A N   
950  C CA  . LEU A 122 ? 0.5898 0.3799 0.6528 0.0657  -0.0380 -0.0763 -75  LEU A CA  
951  C C   . LEU A 122 ? 0.6179 0.4299 0.6646 0.0737  -0.0344 -0.0908 -75  LEU A C   
952  O O   . LEU A 122 ? 0.6423 0.4594 0.6942 0.0804  -0.0354 -0.0958 -75  LEU A O   
953  C CB  . LEU A 122 ? 0.5243 0.3110 0.5646 0.0585  -0.0319 -0.0528 -75  LEU A CB  
954  C CG  . LEU A 122 ? 0.5664 0.3368 0.6145 0.0506  -0.0326 -0.0338 -75  LEU A CG  
955  C CD1 . LEU A 122 ? 0.5958 0.3693 0.6160 0.0459  -0.0264 -0.0154 -75  LEU A CD1 
956  C CD2 . LEU A 122 ? 0.5748 0.3302 0.6503 0.0527  -0.0392 -0.0281 -75  LEU A CD2 
957  N N   . LEU A 123 ? 0.5935 0.4197 0.6209 0.0734  -0.0297 -0.0960 -74  LEU A N   
958  C CA  . LEU A 123 ? 0.5593 0.4090 0.5694 0.0810  -0.0247 -0.1063 -74  LEU A CA  
959  C C   . LEU A 123 ? 0.5455 0.4080 0.5574 0.0863  -0.0275 -0.1260 -74  LEU A C   
960  O O   . LEU A 123 ? 0.5536 0.4232 0.5487 0.0834  -0.0239 -0.1231 -74  LEU A O   
961  C CB  . LEU A 123 ? 0.5925 0.4494 0.5752 0.0763  -0.0157 -0.0902 -74  LEU A CB  
962  C CG  . LEU A 123 ? 0.5931 0.4449 0.5694 0.0726  -0.0123 -0.0734 -74  LEU A CG  
963  C CD1 . LEU A 123 ? 0.5872 0.4442 0.5410 0.0670  -0.0052 -0.0606 -74  LEU A CD1 
964  C CD2 . LEU A 123 ? 0.5818 0.4464 0.5629 0.0807  -0.0111 -0.0804 -74  LEU A CD2 
965  N N   . PRO A 124 ? 0.5458 0.4131 0.5781 0.0950  -0.0345 -0.1473 -73  PRO A N   
966  C CA  . PRO A 124 ? 0.5923 0.4773 0.6238 0.1025  -0.0378 -0.1692 -73  PRO A CA  
967  C C   . PRO A 124 ? 0.6199 0.5330 0.6208 0.1092  -0.0295 -0.1702 -73  PRO A C   
968  O O   . PRO A 124 ? 0.6089 0.5381 0.6012 0.1142  -0.0309 -0.1826 -73  PRO A O   
969  C CB  . PRO A 124 ? 0.5561 0.4431 0.6159 0.1124  -0.0469 -0.1931 -73  PRO A CB  
970  C CG  . PRO A 124 ? 0.5466 0.4255 0.6119 0.1125  -0.0447 -0.1824 -73  PRO A CG  
971  C CD  . PRO A 124 ? 0.5297 0.3882 0.5874 0.0996  -0.0405 -0.1544 -73  PRO A CD  
972  N N   . ASN A 125 ? 0.6579 0.5784 0.6441 0.1098  -0.0211 -0.1570 -72  ASN A N   
973  C CA  . ASN A 125 ? 0.6836 0.6305 0.6436 0.1154  -0.0116 -0.1532 -72  ASN A CA  
974  C C   . ASN A 125 ? 0.6636 0.6028 0.6085 0.1058  -0.0031 -0.1274 -72  ASN A C   
975  O O   . ASN A 125 ? 0.6273 0.5625 0.5763 0.1042  0.0000  -0.1182 -72  ASN A O   
976  C CB  . ASN A 125 ? 0.7112 0.6812 0.6738 0.1284  -0.0096 -0.1670 -72  ASN A CB  
977  C CG  . ASN A 125 ? 0.7198 0.7070 0.6901 0.1408  -0.0169 -0.1953 -72  ASN A CG  
978  O OD1 . ASN A 125 ? 0.7242 0.7241 0.6819 0.1438  -0.0179 -0.2019 -72  ASN A OD1 
979  N ND2 . ASN A 125 ? 0.7321 0.7200 0.7246 0.1485  -0.0232 -0.2135 -72  ASN A ND2 
980  N N   . PRO A 126 ? 0.7253 0.6628 0.6549 0.0997  0.0000  -0.1166 -71  PRO A N   
981  C CA  . PRO A 126 ? 0.7147 0.6446 0.6328 0.0909  0.0069  -0.0943 -71  PRO A CA  
982  C C   . PRO A 126 ? 0.6623 0.6127 0.5695 0.0956  0.0164  -0.0867 -71  PRO A C   
983  O O   . PRO A 126 ? 0.6346 0.6096 0.5337 0.1055  0.0200  -0.0947 -71  PRO A O   
984  C CB  . PRO A 126 ? 0.7578 0.6847 0.6642 0.0858  0.0072  -0.0890 -71  PRO A CB  
985  C CG  . PRO A 126 ? 0.7755 0.7205 0.6795 0.0953  0.0039  -0.1072 -71  PRO A CG  
986  C CD  . PRO A 126 ? 0.7689 0.7127 0.6928 0.1015  -0.0034 -0.1260 -71  PRO A CD  
987  N N   . PRO A 127 ? 0.6375 0.5801 0.5451 0.0891  0.0207  -0.0707 -70  PRO A N   
988  C CA  . PRO A 127 ? 0.6294 0.5910 0.5324 0.0925  0.0301  -0.0620 -70  PRO A CA  
989  C C   . PRO A 127 ? 0.5831 0.5608 0.4694 0.0939  0.0374  -0.0534 -70  PRO A C   
990  O O   . PRO A 127 ? 0.5691 0.5368 0.4476 0.0882  0.0361  -0.0474 -70  PRO A O   
991  C CB  . PRO A 127 ? 0.6390 0.5848 0.5494 0.0835  0.0306  -0.0481 -70  PRO A CB  
992  C CG  . PRO A 127 ? 0.6198 0.5420 0.5282 0.0749  0.0243  -0.0444 -70  PRO A CG  
993  C CD  . PRO A 127 ? 0.6271 0.5452 0.5394 0.0785  0.0174  -0.0595 -70  PRO A CD  
994  N N   . LYS A 128 ? 0.5533 0.5570 0.4349 0.1022  0.0454  -0.0520 -69  LYS A N   
995  C CA  . LYS A 128 ? 0.6089 0.6295 0.4761 0.1045  0.0532  -0.0404 -69  LYS A CA  
996  C C   . LYS A 128 ? 0.5634 0.5803 0.4353 0.0967  0.0609  -0.0187 -69  LYS A C   
997  O O   . LYS A 128 ? 0.5402 0.5617 0.4039 0.0952  0.0656  -0.0060 -69  LYS A O   
998  C CB  . LYS A 128 ? 0.6419 0.6967 0.5001 0.1187  0.0589  -0.0478 -69  LYS A CB  
999  C CG  . LYS A 128 ? 0.7226 0.7849 0.5703 0.1268  0.0514  -0.0666 -69  LYS A CG  
1000 C CD  . LYS A 128 ? 0.7778 0.8738 0.6197 0.1426  0.0542  -0.0809 -69  LYS A CD  
1001 C CE  . LYS A 128 ? 0.8158 0.9143 0.6572 0.1503  0.0427  -0.1074 -69  LYS A CE  
1002 N NZ  . LYS A 128 ? 0.8428 0.9480 0.6988 0.1586  0.0380  -0.1295 -69  LYS A NZ  
1003 N N   . THR A 129 ? 0.5736 0.5824 0.4609 0.0921  0.0612  -0.0154 -68  THR A N   
1004 C CA  . THR A 129 ? 0.5386 0.5451 0.4363 0.0852  0.0673  0.0020  -68  THR A CA  
1005 C C   . THR A 129 ? 0.5324 0.5116 0.4399 0.0752  0.0593  0.0023  -68  THR A C   
1006 O O   . THR A 129 ? 0.5263 0.4934 0.4379 0.0751  0.0515  -0.0090 -68  THR A O   
1007 C CB  . THR A 129 ? 0.5312 0.5589 0.4410 0.0901  0.0757  0.0058  -68  THR A CB  
1008 O OG1 . THR A 129 ? 0.5377 0.5555 0.4609 0.0892  0.0695  -0.0045 -68  THR A OG1 
1009 C CG2 . THR A 129 ? 0.5206 0.5788 0.4190 0.1027  0.0825  0.0011  -68  THR A CG2 
1010 N N   . TRP A 130 ? 0.4881 0.4586 0.4006 0.0674  0.0610  0.0154  -67  TRP A N   
1011 C CA  . TRP A 130 ? 0.4507 0.4010 0.3734 0.0594  0.0542  0.0158  -67  TRP A CA  
1012 C C   . TRP A 130 ? 0.4515 0.4057 0.3910 0.0603  0.0538  0.0136  -67  TRP A C   
1013 O O   . TRP A 130 ? 0.4453 0.3851 0.3901 0.0574  0.0458  0.0085  -67  TRP A O   
1014 C CB  . TRP A 130 ? 0.4402 0.3844 0.3686 0.0525  0.0562  0.0281  -67  TRP A CB  
1015 C CG  . TRP A 130 ? 0.4412 0.3743 0.3564 0.0495  0.0531  0.0288  -67  TRP A CG  
1016 C CD1 . TRP A 130 ? 0.4178 0.3586 0.3227 0.0519  0.0576  0.0345  -67  TRP A CD1 
1017 C CD2 . TRP A 130 ? 0.4548 0.3684 0.3659 0.0442  0.0447  0.0240  -67  TRP A CD2 
1018 N NE1 . TRP A 130 ? 0.4149 0.3412 0.3113 0.0479  0.0523  0.0326  -67  TRP A NE1 
1019 C CE2 . TRP A 130 ? 0.4478 0.3582 0.3478 0.0431  0.0450  0.0264  -67  TRP A CE2 
1020 C CE3 . TRP A 130 ? 0.4482 0.3491 0.3636 0.0411  0.0372  0.0186  -67  TRP A CE3 
1021 C CZ2 . TRP A 130 ? 0.4686 0.3642 0.3625 0.0387  0.0390  0.0231  -67  TRP A CZ2 
1022 C CZ3 . TRP A 130 ? 0.4532 0.3402 0.3608 0.0372  0.0314  0.0166  -67  TRP A CZ3 
1023 C CH2 . TRP A 130 ? 0.4700 0.3547 0.3673 0.0359  0.0327  0.0185  -67  TRP A CH2 
1024 N N   . GLU A 131 ? 0.4894 0.4646 0.4383 0.0644  0.0629  0.0190  -66  GLU A N   
1025 C CA  . GLU A 131 ? 0.5497 0.5319 0.5182 0.0652  0.0637  0.0179  -66  GLU A CA  
1026 C C   . GLU A 131 ? 0.6027 0.5800 0.5713 0.0700  0.0562  0.0032  -66  GLU A C   
1027 O O   . GLU A 131 ? 0.6152 0.5891 0.5993 0.0690  0.0520  0.0008  -66  GLU A O   
1028 C CB  . GLU A 131 ? 0.5565 0.5665 0.5331 0.0704  0.0766  0.0262  -66  GLU A CB  
1029 C CG  . GLU A 131 ? 0.5611 0.5757 0.5510 0.0643  0.0841  0.0441  -66  GLU A CG  
1030 C CD  . GLU A 131 ? 0.5534 0.5710 0.5272 0.0651  0.0890  0.0534  -66  GLU A CD  
1031 O OE1 . GLU A 131 ? 0.5658 0.5796 0.5175 0.0690  0.0850  0.0447  -66  GLU A OE1 
1032 O OE2 . GLU A 131 ? 0.5816 0.6057 0.5676 0.0616  0.0965  0.0697  -66  GLU A OE2 
1033 N N   . GLU A 132 ? 0.6076 0.5850 0.5619 0.0757  0.0538  -0.0070 -65  GLU A N   
1034 C CA  . GLU A 132 ? 0.5581 0.5303 0.5166 0.0808  0.0465  -0.0211 -65  GLU A CA  
1035 C C   . GLU A 132 ? 0.5872 0.5330 0.5435 0.0755  0.0353  -0.0239 -65  GLU A C   
1036 O O   . GLU A 132 ? 0.5911 0.5293 0.5530 0.0791  0.0283  -0.0337 -65  GLU A O   
1037 C CB  . GLU A 132 ? 0.5141 0.5011 0.4633 0.0905  0.0485  -0.0331 -65  GLU A CB  
1038 C CG  . GLU A 132 ? 0.5074 0.4844 0.4409 0.0893  0.0444  -0.0370 -65  GLU A CG  
1039 C CD  . GLU A 132 ? 0.5706 0.5695 0.4938 0.0995  0.0482  -0.0468 -65  GLU A CD  
1040 O OE1 . GLU A 132 ? 0.5630 0.5783 0.4751 0.1011  0.0566  -0.0378 -65  GLU A OE1 
1041 O OE2 . GLU A 132 ? 0.6042 0.6045 0.5313 0.1067  0.0422  -0.0645 -65  GLU A OE2 
1042 N N   . ILE A 133 ? 0.5872 0.5197 0.5370 0.0676  0.0335  -0.0152 -64  ILE A N   
1043 C CA  . ILE A 133 ? 0.5880 0.4989 0.5334 0.0634  0.0243  -0.0166 -64  ILE A CA  
1044 C C   . ILE A 133 ? 0.5641 0.4667 0.5216 0.0625  0.0175  -0.0159 -64  ILE A C   
1045 O O   . ILE A 133 ? 0.5502 0.4398 0.5086 0.0634  0.0100  -0.0192 -64  ILE A O   
1046 C CB  . ILE A 133 ? 0.6110 0.5133 0.5447 0.0566  0.0248  -0.0089 -64  ILE A CB  
1047 C CG1 . ILE A 133 ? 0.5927 0.5015 0.5141 0.0587  0.0292  -0.0111 -64  ILE A CG1 
1048 C CG2 . ILE A 133 ? 0.5944 0.4776 0.5244 0.0524  0.0164  -0.0079 -64  ILE A CG2 
1049 C CD1 . ILE A 133 ? 0.5859 0.4835 0.4960 0.0527  0.0278  -0.0061 -64  ILE A CD1 
1050 N N   . PRO A 134 ? 0.5382 0.4482 0.5070 0.0610  0.0193  -0.0113 -63  PRO A N   
1051 C CA  . PRO A 134 ? 0.5470 0.4516 0.5278 0.0617  0.0116  -0.0123 -63  PRO A CA  
1052 C C   . PRO A 134 ? 0.5734 0.4785 0.5628 0.0688  0.0078  -0.0205 -63  PRO A C   
1053 O O   . PRO A 134 ? 0.6100 0.5025 0.6016 0.0697  -0.0009 -0.0209 -63  PRO A O   
1054 C CB  . PRO A 134 ? 0.5387 0.4562 0.5346 0.0597  0.0157  -0.0081 -63  PRO A CB  
1055 C CG  . PRO A 134 ? 0.5441 0.4638 0.5327 0.0548  0.0224  -0.0014 -63  PRO A CG  
1056 C CD  . PRO A 134 ? 0.5537 0.4743 0.5260 0.0575  0.0268  -0.0037 -63  PRO A CD  
1057 N N   . ALA A 135 ? 0.5474 0.4680 0.5424 0.0746  0.0141  -0.0268 -62  ALA A N   
1058 C CA  . ALA A 135 ? 0.5134 0.4356 0.5194 0.0823  0.0101  -0.0369 -62  ALA A CA  
1059 C C   . ALA A 135 ? 0.5553 0.4616 0.5551 0.0835  0.0038  -0.0422 -62  ALA A C   
1060 O O   . ALA A 135 ? 0.5873 0.4828 0.5978 0.0867  -0.0044 -0.0458 -62  ALA A O   
1061 C CB  . ALA A 135 ? 0.5062 0.4522 0.5184 0.0894  0.0188  -0.0439 -62  ALA A CB  
1062 N N   . LEU A 136 ? 0.5047 0.4092 0.4900 0.0810  0.0070  -0.0424 -61  LEU A N   
1063 C CA  . LEU A 136 ? 0.5039 0.3926 0.4867 0.0805  0.0009  -0.0464 -61  LEU A CA  
1064 C C   . LEU A 136 ? 0.5711 0.4397 0.5537 0.0750  -0.0065 -0.0364 -61  LEU A C   
1065 O O   . LEU A 136 ? 0.6296 0.4847 0.6212 0.0766  -0.0134 -0.0380 -61  LEU A O   
1066 C CB  . LEU A 136 ? 0.5160 0.4081 0.4841 0.0786  0.0055  -0.0479 -61  LEU A CB  
1067 C CG  . LEU A 136 ? 0.6212 0.4990 0.5910 0.0780  -0.0007 -0.0537 -61  LEU A CG  
1068 C CD1 . LEU A 136 ? 0.6227 0.5074 0.6063 0.0872  -0.0038 -0.0711 -61  LEU A CD1 
1069 C CD2 . LEU A 136 ? 0.6580 0.5366 0.6118 0.0735  0.0030  -0.0510 -61  LEU A CD2 
1070 N N   . ASP A 137 ? 0.5600 0.4276 0.5339 0.0693  -0.0051 -0.0259 -60  ASP A N   
1071 C CA  . ASP A 137 ? 0.5663 0.4195 0.5375 0.0657  -0.0119 -0.0167 -60  ASP A CA  
1072 C C   . ASP A 137 ? 0.5519 0.4017 0.5376 0.0707  -0.0191 -0.0166 -60  ASP A C   
1073 O O   . ASP A 137 ? 0.5717 0.4085 0.5595 0.0709  -0.0254 -0.0110 -60  ASP A O   
1074 C CB  . ASP A 137 ? 0.5549 0.4107 0.5155 0.0603  -0.0102 -0.0089 -60  ASP A CB  
1075 C CG  . ASP A 137 ? 0.5633 0.4078 0.5167 0.0578  -0.0166 -0.0002 -60  ASP A CG  
1076 O OD1 . ASP A 137 ? 0.5620 0.3968 0.5078 0.0554  -0.0169 0.0035  -60  ASP A OD1 
1077 O OD2 . ASP A 137 ? 0.5528 0.3997 0.5086 0.0589  -0.0215 0.0030  -60  ASP A OD2 
1078 N N   . LYS A 138 ? 0.5815 0.4438 0.5785 0.0748  -0.0180 -0.0214 -59  LYS A N   
1079 C CA  . LYS A 138 ? 0.6109 0.4716 0.6243 0.0808  -0.0253 -0.0231 -59  LYS A CA  
1080 C C   . LYS A 138 ? 0.5795 0.4303 0.6039 0.0857  -0.0294 -0.0291 -59  LYS A C   
1081 O O   . LYS A 138 ? 0.6010 0.4397 0.6342 0.0881  -0.0375 -0.0241 -59  LYS A O   
1082 C CB  . LYS A 138 ? 0.6543 0.5331 0.6808 0.0848  -0.0216 -0.0296 -59  LYS A CB  
1083 C CG  . LYS A 138 ? 0.7155 0.6012 0.7434 0.0816  -0.0226 -0.0240 -59  LYS A CG  
1084 C CD  . LYS A 138 ? 0.7449 0.6509 0.7875 0.0837  -0.0158 -0.0292 -59  LYS A CD  
1085 C CE  . LYS A 138 ? 0.7256 0.6396 0.7664 0.0768  -0.0110 -0.0235 -59  LYS A CE  
1086 N NZ  . LYS A 138 ? 0.7169 0.6500 0.7658 0.0771  0.0009  -0.0250 -59  LYS A NZ  
1087 N N   . GLU A 139 ? 0.5203 0.3767 0.5455 0.0876  -0.0244 -0.0397 -58  GLU A N   
1088 C CA  . GLU A 139 ? 0.5535 0.4011 0.5928 0.0924  -0.0292 -0.0487 -58  GLU A CA  
1089 C C   . GLU A 139 ? 0.5204 0.3475 0.5577 0.0873  -0.0342 -0.0391 -58  GLU A C   
1090 O O   . GLU A 139 ? 0.5394 0.3532 0.5930 0.0900  -0.0414 -0.0371 -58  GLU A O   
1091 C CB  . GLU A 139 ? 0.5780 0.4397 0.6160 0.0962  -0.0232 -0.0641 -58  GLU A CB  
1092 C CG  . GLU A 139 ? 0.5970 0.4559 0.6532 0.1034  -0.0282 -0.0787 -58  GLU A CG  
1093 C CD  . GLU A 139 ? 0.6019 0.4645 0.6793 0.1116  -0.0329 -0.0851 -58  GLU A CD  
1094 O OE1 . GLU A 139 ? 0.6175 0.4649 0.7152 0.1151  -0.0418 -0.0883 -58  GLU A OE1 
1095 O OE2 . GLU A 139 ? 0.5871 0.4678 0.6626 0.1144  -0.0276 -0.0862 -58  GLU A OE2 
1096 N N   . LEU A 140 ? 0.5311 0.3560 0.5498 0.0799  -0.0298 -0.0317 -57  LEU A N   
1097 C CA  . LEU A 140 ? 0.5246 0.3328 0.5421 0.0749  -0.0329 -0.0218 -57  LEU A CA  
1098 C C   . LEU A 140 ? 0.5561 0.3556 0.5720 0.0738  -0.0380 -0.0053 -57  LEU A C   
1099 O O   . LEU A 140 ? 0.5886 0.3742 0.6136 0.0731  -0.0425 0.0039  -57  LEU A O   
1100 C CB  . LEU A 140 ? 0.4848 0.2957 0.4833 0.0681  -0.0266 -0.0197 -57  LEU A CB  
1101 C CG  . LEU A 140 ? 0.4972 0.3143 0.4980 0.0697  -0.0235 -0.0345 -57  LEU A CG  
1102 C CD1 . LEU A 140 ? 0.4910 0.3156 0.4708 0.0642  -0.0166 -0.0318 -57  LEU A CD1 
1103 C CD2 . LEU A 140 ? 0.4823 0.2861 0.5015 0.0698  -0.0290 -0.0391 -57  LEU A CD2 
1104 N N   . LYS A 141 ? 0.5500 0.3585 0.5548 0.0737  -0.0374 -0.0006 -56  LYS A N   
1105 C CA  . LYS A 141 ? 0.5798 0.3835 0.5814 0.0746  -0.0434 0.0133  -56  LYS A CA  
1106 C C   . LYS A 141 ? 0.6124 0.4070 0.6355 0.0811  -0.0512 0.0159  -56  LYS A C   
1107 O O   . LYS A 141 ? 0.6041 0.3884 0.6293 0.0816  -0.0560 0.0303  -56  LYS A O   
1108 C CB  . LYS A 141 ? 0.5587 0.3758 0.5514 0.0751  -0.0434 0.0128  -56  LYS A CB  
1109 C CG  . LYS A 141 ? 0.5428 0.3662 0.5155 0.0687  -0.0378 0.0146  -56  LYS A CG  
1110 C CD  . LYS A 141 ? 0.5588 0.3791 0.5169 0.0673  -0.0415 0.0274  -56  LYS A CD  
1111 C CE  . LYS A 141 ? 0.5760 0.3990 0.5164 0.0609  -0.0356 0.0282  -56  LYS A CE  
1112 N NZ  . LYS A 141 ? 0.5523 0.3872 0.4901 0.0592  -0.0332 0.0204  -56  LYS A NZ  
1113 N N   . ALA A 142 ? 0.6643 0.4636 0.7045 0.0867  -0.0525 0.0026  -55  ALA A N   
1114 C CA  . ALA A 142 ? 0.6687 0.4592 0.7326 0.0938  -0.0605 0.0030  -55  ALA A CA  
1115 C C   . ALA A 142 ? 0.6683 0.4411 0.7463 0.0924  -0.0632 0.0079  -55  ALA A C   
1116 O O   . ALA A 142 ? 0.6757 0.4372 0.7725 0.0969  -0.0705 0.0158  -55  ALA A O   
1117 C CB  . ALA A 142 ? 0.6569 0.4581 0.7371 0.1005  -0.0602 -0.0153 -55  ALA A CB  
1118 N N   . LYS A 143 ? 0.6614 0.4316 0.7329 0.0864  -0.0577 0.0046  -54  LYS A N   
1119 C CA  . LYS A 143 ? 0.7091 0.4630 0.7959 0.0834  -0.0598 0.0100  -54  LYS A CA  
1120 C C   . LYS A 143 ? 0.6828 0.4310 0.7535 0.0764  -0.0571 0.0307  -54  LYS A C   
1121 O O   . LYS A 143 ? 0.6937 0.4305 0.7762 0.0721  -0.0567 0.0366  -54  LYS A O   
1122 C CB  . LYS A 143 ? 0.7294 0.4855 0.8227 0.0819  -0.0564 -0.0089 -54  LYS A CB  
1123 C CG  . LYS A 143 ? 0.7112 0.4782 0.8164 0.0897  -0.0574 -0.0319 -54  LYS A CG  
1124 C CD  . LYS A 143 ? 0.6887 0.4644 0.7886 0.0883  -0.0527 -0.0487 -54  LYS A CD  
1125 C CE  . LYS A 143 ? 0.7083 0.4996 0.8170 0.0975  -0.0527 -0.0717 -54  LYS A CE  
1126 N NZ  . LYS A 143 ? 0.7557 0.5369 0.8989 0.1044  -0.0616 -0.0840 -54  LYS A NZ  
1127 N N   . GLY A 144 ? 0.6194 0.3770 0.6654 0.0753  -0.0552 0.0408  -53  GLY A N   
1128 C CA  . GLY A 144 ? 0.6028 0.3586 0.6322 0.0702  -0.0525 0.0594  -53  GLY A CA  
1129 C C   . GLY A 144 ? 0.5832 0.3437 0.5956 0.0627  -0.0446 0.0554  -53  GLY A C   
1130 O O   . GLY A 144 ? 0.5317 0.2904 0.5341 0.0581  -0.0414 0.0692  -53  GLY A O   
1131 N N   . LYS A 145 ? 0.5814 0.3501 0.5894 0.0620  -0.0410 0.0374  -52  LYS A N   
1132 C CA  . LYS A 145 ? 0.5621 0.3364 0.5544 0.0560  -0.0341 0.0325  -52  LYS A CA  
1133 C C   . LYS A 145 ? 0.5350 0.3236 0.5087 0.0563  -0.0308 0.0262  -52  LYS A C   
1134 O O   . LYS A 145 ? 0.5500 0.3445 0.5253 0.0609  -0.0338 0.0239  -52  LYS A O   
1135 C CB  . LYS A 145 ? 0.5358 0.3073 0.5427 0.0552  -0.0328 0.0176  -52  LYS A CB  
1136 C CG  . LYS A 145 ? 0.5355 0.2916 0.5694 0.0551  -0.0375 0.0213  -52  LYS A CG  
1137 C CD  . LYS A 145 ? 0.5393 0.2893 0.5702 0.0476  -0.0340 0.0350  -52  LYS A CD  
1138 C CE  . LYS A 145 ? 0.5755 0.3088 0.6399 0.0468  -0.0388 0.0426  -52  LYS A CE  
1139 N NZ  . LYS A 145 ? 0.5745 0.3042 0.6374 0.0392  -0.0341 0.0583  -52  LYS A NZ  
1140 N N   . SER A 146 ? 0.5117 0.3060 0.4712 0.0515  -0.0248 0.0227  -51  SER A N   
1141 C CA  . SER A 146 ? 0.4958 0.3027 0.4430 0.0513  -0.0211 0.0162  -51  SER A CA  
1142 C C   . SER A 146 ? 0.5247 0.3368 0.4702 0.0498  -0.0155 0.0052  -51  SER A C   
1143 O O   . SER A 146 ? 0.5437 0.3501 0.4936 0.0479  -0.0150 0.0028  -51  SER A O   
1144 C CB  . SER A 146 ? 0.4639 0.2746 0.3930 0.0480  -0.0201 0.0253  -51  SER A CB  
1145 O OG  . SER A 146 ? 0.4995 0.3085 0.4189 0.0428  -0.0156 0.0277  -51  SER A OG  
1146 N N   . ALA A 147 ? 0.5222 0.3463 0.4626 0.0509  -0.0117 -0.0007 -50  ALA A N   
1147 C CA  . ALA A 147 ? 0.5060 0.3387 0.4436 0.0514  -0.0062 -0.0099 -50  ALA A CA  
1148 C C   . ALA A 147 ? 0.5142 0.3464 0.4381 0.0459  -0.0025 -0.0061 -50  ALA A C   
1149 O O   . ALA A 147 ? 0.4908 0.3223 0.4148 0.0454  -0.0014 -0.0114 -50  ALA A O   
1150 C CB  . ALA A 147 ? 0.4627 0.3100 0.4009 0.0544  -0.0021 -0.0137 -50  ALA A CB  
1151 N N   . LEU A 148 ? 0.4949 0.3283 0.4083 0.0423  -0.0012 0.0014  -49  LEU A N   
1152 C CA  . LEU A 148 ? 0.5378 0.3737 0.4395 0.0383  0.0031  0.0029  -49  LEU A CA  
1153 C C   . LEU A 148 ? 0.5671 0.4001 0.4599 0.0347  0.0018  0.0107  -49  LEU A C   
1154 O O   . LEU A 148 ? 0.5456 0.3810 0.4391 0.0357  -0.0008 0.0129  -49  LEU A O   
1155 C CB  . LEU A 148 ? 0.5353 0.3833 0.4353 0.0396  0.0084  -0.0003 -49  LEU A CB  
1156 C CG  . LEU A 148 ? 0.4865 0.3374 0.3769 0.0360  0.0123  0.0032  -49  LEU A CG  
1157 C CD1 . LEU A 148 ? 0.4545 0.3046 0.3387 0.0352  0.0139  0.0002  -49  LEU A CD1 
1158 C CD2 . LEU A 148 ? 0.4277 0.2896 0.3212 0.0371  0.0171  0.0044  -49  LEU A CD2 
1159 N N   . MET A 149 ? 0.5809 0.4105 0.4662 0.0312  0.0032  0.0136  -48  MET A N   
1160 C CA  . MET A 149 ? 0.5804 0.4106 0.4557 0.0289  0.0029  0.0192  -48  MET A CA  
1161 C C   . MET A 149 ? 0.5909 0.4234 0.4594 0.0258  0.0071  0.0177  -48  MET A C   
1162 O O   . MET A 149 ? 0.5781 0.4082 0.4485 0.0244  0.0087  0.0164  -48  MET A O   
1163 C CB  . MET A 149 ? 0.5905 0.4155 0.4643 0.0288  0.0000  0.0275  -48  MET A CB  
1164 C CG  . MET A 149 ? 0.5702 0.3929 0.4501 0.0326  -0.0052 0.0308  -48  MET A CG  
1165 S SD  . MET A 149 ? 0.6550 0.4735 0.5318 0.0332  -0.0076 0.0452  -48  MET A SD  
1166 C CE  . MET A 149 ? 0.6768 0.5070 0.5350 0.0344  -0.0083 0.0467  -48  MET A CE  
1167 N N   . PHE A 150 ? 0.5593 0.3967 0.4227 0.0250  0.0080  0.0170  -47  PHE A N   
1168 C CA  . PHE A 150 ? 0.5289 0.3685 0.3868 0.0227  0.0113  0.0161  -47  PHE A CA  
1169 C C   . PHE A 150 ? 0.5160 0.3592 0.3693 0.0226  0.0098  0.0157  -47  PHE A C   
1170 O O   . PHE A 150 ? 0.4863 0.3316 0.3427 0.0243  0.0063  0.0145  -47  PHE A O   
1171 C CB  . PHE A 150 ? 0.4845 0.3277 0.3455 0.0234  0.0148  0.0126  -47  PHE A CB  
1172 C CG  . PHE A 150 ? 0.5149 0.3628 0.3820 0.0247  0.0156  0.0124  -47  PHE A CG  
1173 C CD1 . PHE A 150 ? 0.5215 0.3717 0.3962 0.0270  0.0152  0.0117  -47  PHE A CD1 
1174 C CD2 . PHE A 150 ? 0.5196 0.3703 0.3881 0.0236  0.0171  0.0130  -47  PHE A CD2 
1175 C CE1 . PHE A 150 ? 0.5472 0.4032 0.4312 0.0277  0.0171  0.0128  -47  PHE A CE1 
1176 C CE2 . PHE A 150 ? 0.5141 0.3688 0.3935 0.0241  0.0184  0.0144  -47  PHE A CE2 
1177 C CZ  . PHE A 150 ? 0.5195 0.3775 0.4070 0.0258  0.0188  0.0149  -47  PHE A CZ  
1178 N N   . ASN A 151 ? 0.5136 0.3586 0.3614 0.0210  0.0120  0.0153  -46  ASN A N   
1179 C CA  . ASN A 151 ? 0.5446 0.3942 0.3884 0.0216  0.0105  0.0127  -46  ASN A CA  
1180 C C   . ASN A 151 ? 0.5660 0.4172 0.4192 0.0226  0.0082  0.0081  -46  ASN A C   
1181 O O   . ASN A 151 ? 0.5584 0.4089 0.4186 0.0217  0.0109  0.0080  -46  ASN A O   
1182 C CB  . ASN A 151 ? 0.5000 0.3517 0.3400 0.0200  0.0139  0.0117  -46  ASN A CB  
1183 C CG  . ASN A 151 ? 0.5432 0.4012 0.3788 0.0217  0.0123  0.0077  -46  ASN A CG  
1184 O OD1 . ASN A 151 ? 0.5978 0.4599 0.4317 0.0245  0.0079  0.0048  -46  ASN A OD1 
1185 N ND2 . ASN A 151 ? 0.5337 0.3945 0.3676 0.0209  0.0151  0.0060  -46  ASN A ND2 
1186 N N   . LEU A 152 ? 0.5867 0.4413 0.4415 0.0249  0.0030  0.0048  -45  LEU A N   
1187 C CA  . LEU A 152 ? 0.5756 0.4318 0.4448 0.0254  -0.0001 -0.0006 -45  LEU A CA  
1188 C C   . LEU A 152 ? 0.5743 0.4349 0.4455 0.0268  -0.0036 -0.0086 -45  LEU A C   
1189 O O   . LEU A 152 ? 0.5802 0.4421 0.4673 0.0273  -0.0076 -0.0147 -45  LEU A O   
1190 C CB  . LEU A 152 ? 0.5381 0.3959 0.4136 0.0273  -0.0050 -0.0016 -45  LEU A CB  
1191 C CG  . LEU A 152 ? 0.5345 0.3887 0.4108 0.0271  -0.0024 0.0044  -45  LEU A CG  
1192 C CD1 . LEU A 152 ? 0.5027 0.3597 0.3882 0.0295  -0.0079 0.0022  -45  LEU A CD1 
1193 C CD2 . LEU A 152 ? 0.5229 0.3755 0.4064 0.0250  0.0039  0.0072  -45  LEU A CD2 
1194 N N   . GLN A 153 ? 0.5886 0.4525 0.4468 0.0277  -0.0023 -0.0094 -44  GLN A N   
1195 C CA  . GLN A 153 ? 0.6062 0.4765 0.4661 0.0304  -0.0058 -0.0192 -44  GLN A CA  
1196 C C   . GLN A 153 ? 0.5993 0.4660 0.4676 0.0285  -0.0025 -0.0204 -44  GLN A C   
1197 O O   . GLN A 153 ? 0.6069 0.4772 0.4833 0.0308  -0.0061 -0.0299 -44  GLN A O   
1198 C CB  . GLN A 153 ? 0.5967 0.4764 0.4381 0.0339  -0.0060 -0.0199 -44  GLN A CB  
1199 C CG  . GLN A 153 ? 0.6110 0.4951 0.4414 0.0366  -0.0085 -0.0149 -44  GLN A CG  
1200 C CD  . GLN A 153 ? 0.6113 0.4976 0.4512 0.0395  -0.0165 -0.0219 -44  GLN A CD  
1201 O OE1 . GLN A 153 ? 0.6060 0.4999 0.4520 0.0434  -0.0229 -0.0344 -44  GLN A OE1 
1202 N NE2 . GLN A 153 ? 0.6291 0.5101 0.4715 0.0385  -0.0170 -0.0150 -44  GLN A NE2 
1203 N N   . GLU A 154 ? 0.5696 0.4306 0.4367 0.0252  0.0035  -0.0119 -43  GLU A N   
1204 C CA  . GLU A 154 ? 0.5368 0.3954 0.4105 0.0242  0.0066  -0.0112 -43  GLU A CA  
1205 C C   . GLU A 154 ? 0.5316 0.3854 0.4188 0.0224  0.0090  -0.0047 -43  GLU A C   
1206 O O   . GLU A 154 ? 0.5464 0.3990 0.4286 0.0214  0.0122  0.0018  -43  GLU A O   
1207 C CB  . GLU A 154 ? 0.5012 0.3611 0.3619 0.0232  0.0114  -0.0072 -43  GLU A CB  
1208 C CG  . GLU A 154 ? 0.5314 0.3986 0.3836 0.0253  0.0108  -0.0128 -43  GLU A CG  
1209 C CD  . GLU A 154 ? 0.6114 0.4810 0.4751 0.0280  0.0076  -0.0222 -43  GLU A CD  
1210 O OE1 . GLU A 154 ? 0.6807 0.5588 0.5398 0.0315  0.0049  -0.0307 -43  GLU A OE1 
1211 O OE2 . GLU A 154 ? 0.5566 0.4204 0.4345 0.0271  0.0077  -0.0207 -43  GLU A OE2 
1212 N N   . PRO A 155 ? 0.4950 0.3468 0.4005 0.0225  0.0078  -0.0056 -42  PRO A N   
1213 C CA  . PRO A 155 ? 0.4736 0.3233 0.3931 0.0211  0.0112  0.0035  -42  PRO A CA  
1214 C C   . PRO A 155 ? 0.4852 0.3361 0.3947 0.0213  0.0175  0.0128  -42  PRO A C   
1215 O O   . PRO A 155 ? 0.4584 0.3114 0.3724 0.0213  0.0215  0.0211  -42  PRO A O   
1216 C CB  . PRO A 155 ? 0.4524 0.2994 0.3968 0.0211  0.0084  0.0014  -42  PRO A CB  
1217 C CG  . PRO A 155 ? 0.4116 0.2593 0.3516 0.0233  0.0042  -0.0095 -42  PRO A CG  
1218 C CD  . PRO A 155 ? 0.4810 0.3336 0.3978 0.0244  0.0029  -0.0154 -42  PRO A CD  
1219 N N   . TYR A 156 ? 0.5164 0.3682 0.4131 0.0221  0.0184  0.0112  -41  TYR A N   
1220 C CA  . TYR A 156 ? 0.5282 0.3830 0.4151 0.0231  0.0229  0.0175  -41  TYR A CA  
1221 C C   . TYR A 156 ? 0.5160 0.3732 0.3961 0.0233  0.0252  0.0204  -41  TYR A C   
1222 O O   . TYR A 156 ? 0.4861 0.3484 0.3639 0.0254  0.0288  0.0261  -41  TYR A O   
1223 C CB  . TYR A 156 ? 0.5160 0.3721 0.3905 0.0232  0.0224  0.0126  -41  TYR A CB  
1224 C CG  . TYR A 156 ? 0.5374 0.3975 0.4036 0.0246  0.0250  0.0155  -41  TYR A CG  
1225 C CD1 . TYR A 156 ? 0.5354 0.3988 0.4054 0.0274  0.0263  0.0203  -41  TYR A CD1 
1226 C CD2 . TYR A 156 ? 0.5197 0.3811 0.3757 0.0237  0.0253  0.0130  -41  TYR A CD2 
1227 C CE1 . TYR A 156 ? 0.5217 0.3916 0.3831 0.0300  0.0274  0.0213  -41  TYR A CE1 
1228 C CE2 . TYR A 156 ? 0.5161 0.3824 0.3671 0.0255  0.0262  0.0127  -41  TYR A CE2 
1229 C CZ  . TYR A 156 ? 0.5514 0.4227 0.4038 0.0289  0.0270  0.0160  -41  TYR A CZ  
1230 O OH  . TYR A 156 ? 0.5623 0.4409 0.4092 0.0318  0.0266  0.0141  -41  TYR A OH  
1231 N N   . PHE A 157 ? 0.5128 0.3677 0.3893 0.0219  0.0227  0.0162  -40  PHE A N   
1232 C CA  . PHE A 157 ? 0.4965 0.3529 0.3673 0.0225  0.0240  0.0172  -40  PHE A CA  
1233 C C   . PHE A 157 ? 0.5036 0.3624 0.3853 0.0232  0.0253  0.0208  -40  PHE A C   
1234 O O   . PHE A 157 ? 0.5218 0.3849 0.4012 0.0251  0.0279  0.0226  -40  PHE A O   
1235 C CB  . PHE A 157 ? 0.4602 0.3131 0.3237 0.0212  0.0207  0.0130  -40  PHE A CB  
1236 C CG  . PHE A 157 ? 0.4799 0.3322 0.3344 0.0202  0.0209  0.0111  -40  PHE A CG  
1237 C CD1 . PHE A 157 ? 0.5125 0.3655 0.3656 0.0197  0.0196  0.0085  -40  PHE A CD1 
1238 C CD2 . PHE A 157 ? 0.5139 0.3663 0.3639 0.0201  0.0221  0.0109  -40  PHE A CD2 
1239 C CE1 . PHE A 157 ? 0.5570 0.4118 0.4036 0.0187  0.0207  0.0075  -40  PHE A CE1 
1240 C CE2 . PHE A 157 ? 0.5451 0.3978 0.3911 0.0184  0.0224  0.0097  -40  PHE A CE2 
1241 C CZ  . PHE A 157 ? 0.5329 0.3872 0.3768 0.0176  0.0224  0.0089  -40  PHE A CZ  
1242 N N   . THR A 158 ? 0.5088 0.3661 0.4047 0.0219  0.0235  0.0211  -39  THR A N   
1243 C CA  . THR A 158 ? 0.5195 0.3800 0.4303 0.0218  0.0249  0.0249  -39  THR A CA  
1244 C C   . THR A 158 ? 0.5269 0.3923 0.4499 0.0225  0.0306  0.0349  -39  THR A C   
1245 O O   . THR A 158 ? 0.5120 0.3838 0.4452 0.0231  0.0347  0.0411  -39  THR A O   
1246 C CB  . THR A 158 ? 0.5547 0.4120 0.4785 0.0202  0.0188  0.0189  -39  THR A CB  
1247 O OG1 . THR A 158 ? 0.5944 0.4502 0.5062 0.0209  0.0144  0.0128  -39  THR A OG1 
1248 C CG2 . THR A 158 ? 0.6021 0.4630 0.5480 0.0193  0.0202  0.0229  -39  THR A CG2 
1249 N N   . TRP A 159 ? 0.5158 0.3798 0.4382 0.0229  0.0314  0.0377  -38  TRP A N   
1250 C CA  . TRP A 159 ? 0.4911 0.3598 0.4250 0.0242  0.0368  0.0498  -38  TRP A CA  
1251 C C   . TRP A 159 ? 0.5219 0.4028 0.4480 0.0280  0.0439  0.0587  -38  TRP A C   
1252 O O   . TRP A 159 ? 0.5085 0.3964 0.4492 0.0288  0.0495  0.0709  -38  TRP A O   
1253 C CB  . TRP A 159 ? 0.4950 0.3609 0.4244 0.0253  0.0357  0.0503  -38  TRP A CB  
1254 C CG  . TRP A 159 ? 0.5357 0.4050 0.4810 0.0268  0.0402  0.0644  -38  TRP A CG  
1255 C CD1 . TRP A 159 ? 0.5563 0.4347 0.4929 0.0313  0.0452  0.0752  -38  TRP A CD1 
1256 C CD2 . TRP A 159 ? 0.5292 0.3939 0.5042 0.0242  0.0398  0.0703  -38  TRP A CD2 
1257 N NE1 . TRP A 159 ? 0.5681 0.4478 0.5258 0.0319  0.0488  0.0900  -38  TRP A NE1 
1258 C CE2 . TRP A 159 ? 0.5229 0.3933 0.5067 0.0270  0.0457  0.0874  -38  TRP A CE2 
1259 C CE3 . TRP A 159 ? 0.5243 0.3817 0.5210 0.0203  0.0345  0.0625  -38  TRP A CE3 
1260 C CZ2 . TRP A 159 ? 0.5093 0.3765 0.5247 0.0251  0.0472  0.0986  -38  TRP A CZ2 
1261 C CZ3 . TRP A 159 ? 0.5655 0.4197 0.5950 0.0183  0.0348  0.0705  -38  TRP A CZ3 
1262 C CH2 . TRP A 159 ? 0.5424 0.4007 0.5827 0.0203  0.0417  0.0897  -38  TRP A CH2 
1263 N N   . PRO A 160 ? 0.5492 0.4344 0.4545 0.0310  0.0440  0.0534  -37  PRO A N   
1264 C CA  . PRO A 160 ? 0.5533 0.4535 0.4513 0.0365  0.0503  0.0595  -37  PRO A CA  
1265 C C   . PRO A 160 ? 0.5588 0.4657 0.4704 0.0363  0.0547  0.0649  -37  PRO A C   
1266 O O   . PRO A 160 ? 0.5530 0.4734 0.4702 0.0397  0.0621  0.0771  -37  PRO A O   
1267 C CB  . PRO A 160 ? 0.5188 0.4191 0.3981 0.0386  0.0468  0.0474  -37  PRO A CB  
1268 C CG  . PRO A 160 ? 0.4882 0.3761 0.3633 0.0348  0.0409  0.0402  -37  PRO A CG  
1269 C CD  . PRO A 160 ? 0.4765 0.3550 0.3666 0.0301  0.0387  0.0416  -37  PRO A CD  
1270 N N   . LEU A 161 ? 0.5629 0.4624 0.4803 0.0329  0.0504  0.0566  -36  LEU A N   
1271 C CA  . LEU A 161 ? 0.5396 0.4458 0.4729 0.0325  0.0537  0.0605  -36  LEU A CA  
1272 C C   . LEU A 161 ? 0.5710 0.4776 0.5300 0.0292  0.0570  0.0721  -36  LEU A C   
1273 O O   . LEU A 161 ? 0.5579 0.4761 0.5315 0.0301  0.0641  0.0825  -36  LEU A O   
1274 C CB  . LEU A 161 ? 0.4634 0.3611 0.3979 0.0301  0.0469  0.0490  -36  LEU A CB  
1275 C CG  . LEU A 161 ? 0.4557 0.3588 0.4093 0.0292  0.0483  0.0505  -36  LEU A CG  
1276 C CD1 . LEU A 161 ? 0.4567 0.3764 0.4083 0.0344  0.0563  0.0555  -36  LEU A CD1 
1277 C CD2 . LEU A 161 ? 0.4551 0.3491 0.4074 0.0277  0.0396  0.0388  -36  LEU A CD2 
1278 N N   . ILE A 162 ? 0.5640 0.4586 0.5315 0.0254  0.0520  0.0706  -35  ILE A N   
1279 C CA  . ILE A 162 ? 0.5345 0.4267 0.5323 0.0218  0.0530  0.0791  -35  ILE A CA  
1280 C C   . ILE A 162 ? 0.5304 0.4323 0.5347 0.0243  0.0621  0.0978  -35  ILE A C   
1281 O O   . ILE A 162 ? 0.4807 0.3885 0.5110 0.0226  0.0678  0.1110  -35  ILE A O   
1282 C CB  . ILE A 162 ? 0.5299 0.4074 0.5350 0.0184  0.0439  0.0688  -35  ILE A CB  
1283 C CG1 . ILE A 162 ? 0.4925 0.3642 0.4975 0.0164  0.0354  0.0532  -35  ILE A CG1 
1284 C CG2 . ILE A 162 ? 0.5181 0.3924 0.5558 0.0155  0.0445  0.0775  -35  ILE A CG2 
1285 C CD1 . ILE A 162 ? 0.5115 0.3730 0.5247 0.0146  0.0266  0.0423  -35  ILE A CD1 
1286 N N   . ALA A 163 ? 0.5505 0.4555 0.5322 0.0288  0.0635  0.1002  -34  ALA A N   
1287 C CA  . ALA A 163 ? 0.5571 0.4736 0.5418 0.0329  0.0718  0.1192  -34  ALA A CA  
1288 C C   . ALA A 163 ? 0.5836 0.5215 0.5591 0.0386  0.0814  0.1287  -34  ALA A C   
1289 O O   . ALA A 163 ? 0.5709 0.5224 0.5532 0.0423  0.0901  0.1483  -34  ALA A O   
1290 C CB  . ALA A 163 ? 0.5373 0.4518 0.5013 0.0368  0.0690  0.1174  -34  ALA A CB  
1291 N N   . ALA A 164 ? 0.5583 0.5006 0.5195 0.0401  0.0801  0.1159  -33  ALA A N   
1292 C CA  . ALA A 164 ? 0.5407 0.5053 0.4889 0.0476  0.0882  0.1208  -33  ALA A CA  
1293 C C   . ALA A 164 ? 0.5196 0.5000 0.4902 0.0482  0.0994  0.1414  -33  ALA A C   
1294 O O   . ALA A 164 ? 0.4921 0.4940 0.4535 0.0557  0.1085  0.1551  -33  ALA A O   
1295 C CB  . ALA A 164 ? 0.5039 0.4685 0.4421 0.0484  0.0842  0.1032  -33  ALA A CB  
1296 N N   . ASP A 165 ? 0.5177 0.4897 0.5187 0.0407  0.0989  0.1436  -32  ASP A N   
1297 C CA  . ASP A 165 ? 0.5289 0.5157 0.5573 0.0399  0.1097  0.1629  -32  ASP A CA  
1298 C C   . ASP A 165 ? 0.5723 0.5525 0.6310 0.0351  0.1125  0.1818  -32  ASP A C   
1299 O O   . ASP A 165 ? 0.5737 0.5615 0.6653 0.0317  0.1201  0.1976  -32  ASP A O   
1300 C CB  . ASP A 165 ? 0.5138 0.4984 0.5625 0.0349  0.1077  0.1537  -32  ASP A CB  
1301 C CG  . ASP A 165 ? 0.5398 0.5462 0.6118 0.0358  0.1206  0.1717  -32  ASP A CG  
1302 O OD1 . ASP A 165 ? 0.5553 0.5846 0.6127 0.0438  0.1315  0.1853  -32  ASP A OD1 
1303 O OD2 . ASP A 165 ? 0.5450 0.5476 0.6510 0.0291  0.1201  0.1729  -32  ASP A OD2 
1304 N N   . GLY A 166 ? 0.5702 0.5372 0.6217 0.0350  0.1067  0.1813  -31  GLY A N   
1305 C CA  . GLY A 166 ? 0.5377 0.5002 0.6189 0.0322  0.1101  0.2014  -31  GLY A CA  
1306 C C   . GLY A 166 ? 0.5930 0.5299 0.6881 0.0263  0.0981  0.1897  -31  GLY A C   
1307 O O   . GLY A 166 ? 0.6306 0.5608 0.7504 0.0246  0.0988  0.2038  -31  GLY A O   
1308 N N   . GLY A 167 ? 0.5803 0.5036 0.6614 0.0238  0.0871  0.1644  -30  GLY A N   
1309 C CA  . GLY A 167 ? 0.5346 0.4374 0.6252 0.0199  0.0760  0.1514  -30  GLY A CA  
1310 C C   . GLY A 167 ? 0.5739 0.4746 0.6448 0.0247  0.0751  0.1554  -30  GLY A C   
1311 O O   . GLY A 167 ? 0.6119 0.5239 0.6502 0.0309  0.0784  0.1566  -30  GLY A O   
1312 N N   . TYR A 168 ? 0.5541 0.4410 0.6470 0.0222  0.0696  0.1557  -29  TYR A N   
1313 C CA  . TYR A 168 ? 0.5411 0.4251 0.6177 0.0268  0.0674  0.1575  -29  TYR A CA  
1314 C C   . TYR A 168 ? 0.5496 0.4151 0.6491 0.0233  0.0575  0.1460  -29  TYR A C   
1315 O O   . TYR A 168 ? 0.5615 0.4179 0.6939 0.0179  0.0531  0.1402  -29  TYR A O   
1316 C CB  . TYR A 168 ? 0.5776 0.4750 0.6571 0.0322  0.0773  0.1850  -29  TYR A CB  
1317 C CG  . TYR A 168 ? 0.6111 0.5060 0.7376 0.0285  0.0822  0.2066  -29  TYR A CG  
1318 C CD1 . TYR A 168 ? 0.6421 0.5493 0.7862 0.0264  0.0918  0.2216  -29  TYR A CD1 
1319 C CD2 . TYR A 168 ? 0.6115 0.4921 0.7665 0.0270  0.0773  0.2111  -29  TYR A CD2 
1320 C CE1 . TYR A 168 ? 0.6331 0.5386 0.8234 0.0223  0.0969  0.2422  -29  TYR A CE1 
1321 C CE2 . TYR A 168 ? 0.6334 0.5104 0.8374 0.0231  0.0815  0.2318  -29  TYR A CE2 
1322 C CZ  . TYR A 168 ? 0.6409 0.5305 0.8621 0.0204  0.0915  0.2476  -29  TYR A CZ  
1323 O OH  . TYR A 168 ? 0.6284 0.5151 0.9005 0.0160  0.0963  0.2688  -29  TYR A OH  
1324 N N   . ALA A 169 ? 0.5024 0.3640 0.5854 0.0271  0.0534  0.1413  -28  ALA A N   
1325 C CA  . ALA A 169 ? 0.5218 0.3683 0.6233 0.0255  0.0441  0.1287  -28  ALA A CA  
1326 C C   . ALA A 169 ? 0.5663 0.4077 0.7044 0.0261  0.0457  0.1476  -28  ALA A C   
1327 O O   . ALA A 169 ? 0.6055 0.4393 0.7837 0.0214  0.0441  0.1500  -28  ALA A O   
1328 C CB  . ALA A 169 ? 0.5311 0.3768 0.6009 0.0292  0.0393  0.1145  -28  ALA A CB  
1329 N N   . PHE A 170 ? 0.5509 0.3972 0.6775 0.0320  0.0489  0.1619  -27  PHE A N   
1330 C CA  . PHE A 170 ? 0.6088 0.4518 0.7676 0.0339  0.0513  0.1839  -27  PHE A CA  
1331 C C   . PHE A 170 ? 0.6711 0.5323 0.8160 0.0394  0.0630  0.2125  -27  PHE A C   
1332 O O   . PHE A 170 ? 0.6543 0.5285 0.7589 0.0453  0.0652  0.2112  -27  PHE A O   
1333 C CB  . PHE A 170 ? 0.6107 0.4441 0.7706 0.0377  0.0433  0.1753  -27  PHE A CB  
1334 C CG  . PHE A 170 ? 0.5950 0.4157 0.7600 0.0343  0.0324  0.1448  -27  PHE A CG  
1335 C CD1 . PHE A 170 ? 0.5713 0.3784 0.7800 0.0303  0.0257  0.1365  -27  PHE A CD1 
1336 C CD2 . PHE A 170 ? 0.6121 0.4365 0.7385 0.0357  0.0288  0.1240  -27  PHE A CD2 
1337 C CE1 . PHE A 170 ? 0.5866 0.3860 0.7980 0.0290  0.0155  0.1078  -27  PHE A CE1 
1338 C CE2 . PHE A 170 ? 0.5904 0.4070 0.7189 0.0337  0.0199  0.0976  -27  PHE A CE2 
1339 C CZ  . PHE A 170 ? 0.5896 0.3949 0.7578 0.0310  0.0132  0.0886  -27  PHE A CZ  
1340 N N   . LYS A 171 ? 0.7178 0.5811 0.8981 0.0379  0.0703  0.2384  -26  LYS A N   
1341 C CA  . LYS A 171 ? 0.7673 0.6521 0.9361 0.0434  0.0831  0.2675  -26  LYS A CA  
1342 C C   . LYS A 171 ? 0.8100 0.7052 0.9517 0.0537  0.0841  0.2796  -26  LYS A C   
1343 O O   . LYS A 171 ? 0.7753 0.6584 0.9218 0.0557  0.0759  0.2730  -26  LYS A O   
1344 C CB  . LYS A 171 ? 0.7927 0.6769 1.0109 0.0395  0.0909  0.2955  -26  LYS A CB  
1345 N N   . TYR A 172 ? 0.8987 0.8187 1.0130 0.0611  0.0941  0.2974  -25  TYR A N   
1346 C CA  . TYR A 172 ? 0.9669 0.9034 1.0496 0.0729  0.0953  0.3085  -25  TYR A CA  
1347 C C   . TYR A 172 ? 0.9866 0.9131 1.0459 0.0748  0.0832  0.2820  -25  TYR A C   
1348 O O   . TYR A 172 ? 1.0022 0.9410 1.0358 0.0843  0.0817  0.2859  -25  TYR A O   
1349 C CB  . TYR A 172 ? 0.9977 0.9382 1.1079 0.0772  0.0999  0.3407  -25  TYR A CB  
1350 N N   . LYS A 176 ? 1.0455 0.9814 1.1451 0.1006  0.0788  0.3532  -21  LYS A N   
1351 C CA  . LYS A 176 ? 1.0496 0.9584 1.1581 0.0953  0.0684  0.3277  -21  LYS A CA  
1352 C C   . LYS A 176 ? 1.0458 0.9394 1.1752 0.0826  0.0689  0.3112  -21  LYS A C   
1353 O O   . LYS A 176 ? 1.0501 0.9490 1.1957 0.0788  0.0781  0.3284  -21  LYS A O   
1354 C CB  . LYS A 176 ? 1.0690 0.9598 1.2115 0.0968  0.0604  0.3318  -21  LYS A CB  
1355 N N   . TYR A 177 ? 1.0266 0.9036 1.1551 0.0766  0.0591  0.2783  -20  TYR A N   
1356 C CA  . TYR A 177 ? 0.9800 0.8429 1.1281 0.0657  0.0571  0.2599  -20  TYR A CA  
1357 C C   . TYR A 177 ? 0.9764 0.8210 1.1814 0.0605  0.0551  0.2699  -20  TYR A C   
1358 O O   . TYR A 177 ? 1.0405 0.8718 1.2688 0.0626  0.0476  0.2672  -20  TYR A O   
1359 C CB  . TYR A 177 ? 0.9549 0.8085 1.0845 0.0627  0.0474  0.2241  -20  TYR A CB  
1360 C CG  . TYR A 177 ? 0.9512 0.8196 1.0314 0.0660  0.0482  0.2110  -20  TYR A CG  
1361 C CD1 . TYR A 177 ? 0.9525 0.8305 1.0127 0.0629  0.0536  0.2068  -20  TYR A CD1 
1362 C CD2 . TYR A 177 ? 0.9356 0.8085 0.9923 0.0721  0.0428  0.2014  -20  TYR A CD2 
1363 C CE1 . TYR A 177 ? 0.9129 0.8034 0.9324 0.0660  0.0534  0.1935  -20  TYR A CE1 
1364 C CE2 . TYR A 177 ? 0.9231 0.8091 0.9399 0.0746  0.0428  0.1884  -20  TYR A CE2 
1365 C CZ  . TYR A 177 ? 0.9087 0.8028 0.9077 0.0715  0.0480  0.1845  -20  TYR A CZ  
1366 O OH  . TYR A 177 ? 0.9090 0.8149 0.8730 0.0741  0.0471  0.1708  -20  TYR A OH  
1367 N N   . ASP A 178 ? 0.8974 0.7416 1.1281 0.0541  0.0615  0.2808  -19  ASP A N   
1368 C CA  . ASP A 178 ? 0.8414 0.6693 1.1300 0.0472  0.0582  0.2837  -19  ASP A CA  
1369 C C   . ASP A 178 ? 0.8149 0.6265 1.1137 0.0400  0.0484  0.2494  -19  ASP A C   
1370 O O   . ASP A 178 ? 0.8157 0.6309 1.1120 0.0341  0.0510  0.2411  -19  ASP A O   
1371 C CB  . ASP A 178 ? 0.8144 0.6588 1.1234 0.0428  0.0687  0.3051  -19  ASP A CB  
1372 C CG  . ASP A 178 ? 0.7843 0.6180 1.1525 0.0346  0.0641  0.3018  -19  ASP A CG  
1373 O OD1 . ASP A 178 ? 0.7862 0.6325 1.1787 0.0305  0.0722  0.3183  -19  ASP A OD1 
1374 O OD2 . ASP A 178 ? 0.7685 0.5831 1.1608 0.0327  0.0522  0.2816  -19  ASP A OD2 
1375 N N   . ILE A 179 ? 0.7845 0.5819 1.0929 0.0413  0.0367  0.2274  -18  ILE A N   
1376 C CA  . ILE A 179 ? 0.7303 0.5168 1.0453 0.0363  0.0263  0.1920  -18  ILE A CA  
1377 C C   . ILE A 179 ? 0.6899 0.4667 1.0548 0.0285  0.0243  0.1902  -18  ILE A C   
1378 O O   . ILE A 179 ? 0.6639 0.4353 1.0333 0.0246  0.0162  0.1617  -18  ILE A O   
1379 C CB  . ILE A 179 ? 0.7088 0.4840 1.0315 0.0405  0.0149  0.1716  -18  ILE A CB  
1380 C CG1 . ILE A 179 ? 0.7519 0.5125 1.1334 0.0412  0.0111  0.1859  -18  ILE A CG1 
1381 C CG2 . ILE A 179 ? 0.6788 0.4644 0.9560 0.0480  0.0164  0.1729  -18  ILE A CG2 
1382 C CD1 . ILE A 179 ? 0.7544 0.5041 1.1492 0.0463  -0.0006 0.1652  -18  ILE A CD1 
1383 N N   . LYS A 180 ? 0.6857 0.4666 1.0842 0.0259  0.0313  0.2173  -17  LYS A N   
1384 C CA  . LYS A 180 ? 0.7203 0.5009 1.1642 0.0176  0.0293  0.2127  -17  LYS A CA  
1385 C C   . LYS A 180 ? 0.7684 0.5602 1.2019 0.0131  0.0390  0.2223  -17  LYS A C   
1386 O O   . LYS A 180 ? 0.8144 0.6057 1.2825 0.0062  0.0365  0.2143  -17  LYS A O   
1387 C CB  . LYS A 180 ? 0.7135 0.4993 1.2017 0.0164  0.0309  0.2320  -17  LYS A CB  
1388 N N   . ASP A 181 ? 0.7666 0.5699 1.1545 0.0174  0.0495  0.2379  -16  ASP A N   
1389 C CA  . ASP A 181 ? 0.7341 0.5499 1.1083 0.0143  0.0593  0.2464  -16  ASP A CA  
1390 C C   . ASP A 181 ? 0.6940 0.5133 1.0193 0.0150  0.0542  0.2167  -16  ASP A C   
1391 O O   . ASP A 181 ? 0.6888 0.5174 0.9654 0.0210  0.0564  0.2146  -16  ASP A O   
1392 C CB  . ASP A 181 ? 0.7312 0.5706 1.0831 0.0193  0.0737  0.2780  -16  ASP A CB  
1393 C CG  . ASP A 181 ? 0.7262 0.5819 1.0695 0.0166  0.0846  0.2873  -16  ASP A CG  
1394 O OD1 . ASP A 181 ? 0.6887 0.5378 1.0357 0.0110  0.0804  0.2674  -16  ASP A OD1 
1395 O OD2 . ASP A 181 ? 0.7514 0.6299 1.0831 0.0209  0.0965  0.3119  -16  ASP A OD2 
1396 N N   . VAL A 182 ? 0.6894 0.5028 1.0287 0.0092  0.0472  0.1937  -15  VAL A N   
1397 C CA  . VAL A 182 ? 0.6500 0.4669 0.9477 0.0095  0.0420  0.1661  -15  VAL A CA  
1398 C C   . VAL A 182 ? 0.6381 0.4672 0.9293 0.0061  0.0492  0.1705  -15  VAL A C   
1399 O O   . VAL A 182 ? 0.6375 0.4657 0.9705 0.0005  0.0506  0.1771  -15  VAL A O   
1400 C CB  . VAL A 182 ? 0.6204 0.4236 0.9345 0.0075  0.0271  0.1341  -15  VAL A CB  
1401 C CG1 . VAL A 182 ? 0.5498 0.3583 0.8265 0.0073  0.0227  0.1097  -15  VAL A CG1 
1402 C CG2 . VAL A 182 ? 0.6391 0.4328 0.9525 0.0123  0.0203  0.1268  -15  VAL A CG2 
1403 N N   . GLY A 183 ? 0.6436 0.4841 0.8861 0.0094  0.0530  0.1657  -14  GLY A N   
1404 C CA  . GLY A 183 ? 0.6234 0.4773 0.8573 0.0076  0.0604  0.1704  -14  GLY A CA  
1405 C C   . GLY A 183 ? 0.5941 0.4467 0.8037 0.0064  0.0528  0.1433  -14  GLY A C   
1406 O O   . GLY A 183 ? 0.5512 0.4149 0.7265 0.0088  0.0574  0.1418  -14  GLY A O   
1407 N N   . VAL A 184 ? 0.5819 0.4220 0.8100 0.0034  0.0407  0.1215  -13  VAL A N   
1408 C CA  . VAL A 184 ? 0.6008 0.4407 0.8053 0.0034  0.0329  0.0968  -13  VAL A CA  
1409 C C   . VAL A 184 ? 0.5834 0.4271 0.8116 -0.0010 0.0314  0.0920  -13  VAL A C   
1410 O O   . VAL A 184 ? 0.5438 0.3919 0.7482 -0.0002 0.0285  0.0788  -13  VAL A O   
1411 C CB  . VAL A 184 ? 0.6081 0.4368 0.8124 0.0046  0.0202  0.0736  -13  VAL A CB  
1412 C CG1 . VAL A 184 ? 0.6002 0.4306 0.7877 0.0047  0.0119  0.0502  -13  VAL A CG1 
1413 C CG2 . VAL A 184 ? 0.6082 0.4358 0.7803 0.0094  0.0218  0.0753  -13  VAL A CG2 
1414 N N   . ASP A 185 ? 0.5927 0.4351 0.8699 -0.0055 0.0332  0.1029  -12  ASP A N   
1415 C CA  . ASP A 185 ? 0.6101 0.4568 0.9140 -0.0098 0.0307  0.0964  -12  ASP A CA  
1416 C C   . ASP A 185 ? 0.5941 0.4529 0.9198 -0.0126 0.0445  0.1225  -12  ASP A C   
1417 O O   . ASP A 185 ? 0.6150 0.4769 0.9790 -0.0175 0.0434  0.1216  -12  ASP A O   
1418 C CB  . ASP A 185 ? 0.6072 0.4429 0.9555 -0.0131 0.0170  0.0777  -12  ASP A CB  
1419 C CG  . ASP A 185 ? 0.6094 0.4402 1.0156 -0.0179 0.0202  0.0946  -12  ASP A CG  
1420 O OD1 . ASP A 185 ? 0.6054 0.4342 1.0124 -0.0167 0.0286  0.1164  -12  ASP A OD1 
1421 O OD2 . ASP A 185 ? 0.6246 0.4540 1.0764 -0.0226 0.0136  0.0859  -12  ASP A OD2 
1422 N N   . ASN A 186 ? 0.5603 0.4287 0.8618 -0.0090 0.0573  0.1448  -11  ASN A N   
1423 C CA  . ASN A 186 ? 0.5592 0.4438 0.8761 -0.0101 0.0719  0.1704  -11  ASN A CA  
1424 C C   . ASN A 186 ? 0.5531 0.4518 0.8414 -0.0080 0.0755  0.1634  -11  ASN A C   
1425 O O   . ASN A 186 ? 0.4927 0.3875 0.7490 -0.0057 0.0670  0.1412  -11  ASN A O   
1426 C CB  . ASN A 186 ? 0.5610 0.4532 0.8643 -0.0054 0.0837  0.1971  -11  ASN A CB  
1427 C CG  . ASN A 186 ? 0.5568 0.4561 0.7991 0.0025  0.0856  0.1920  -11  ASN A CG  
1428 O OD1 . ASN A 186 ? 0.4718 0.3776 0.6837 0.0045  0.0844  0.1777  -11  ASN A OD1 
1429 N ND2 . ASN A 186 ? 0.5922 0.4912 0.8200 0.0072  0.0887  0.2049  -11  ASN A ND2 
1430 N N   . ALA A 187 ? 0.5862 0.5027 0.8883 -0.0083 0.0887  0.1837  -10  ALA A N   
1431 C CA  . ALA A 187 ? 0.5713 0.5022 0.8576 -0.0066 0.0923  0.1775  -10  ALA A CA  
1432 C C   . ALA A 187 ? 0.5564 0.4916 0.7847 0.0009  0.0918  0.1669  -10  ALA A C   
1433 O O   . ALA A 187 ? 0.5234 0.4609 0.7350 0.0021  0.0873  0.1503  -10  ALA A O   
1434 C CB  . ALA A 187 ? 0.4586 0.4113 0.7687 -0.0070 0.1088  0.2040  -10  ALA A CB  
1435 N N   . GLY A 188 ? 0.5581 0.4949 0.7584 0.0061  0.0962  0.1765  -9   GLY A N   
1436 C CA  . GLY A 188 ? 0.5642 0.5054 0.7146 0.0130  0.0954  0.1662  -9   GLY A CA  
1437 C C   . GLY A 188 ? 0.5900 0.5130 0.7219 0.0117  0.0808  0.1400  -9   GLY A C   
1438 O O   . GLY A 188 ? 0.5879 0.5124 0.6970 0.0137  0.0771  0.1252  -9   GLY A O   
1439 N N   . ALA A 189 ? 0.5735 0.4799 0.7161 0.0088  0.0726  0.1345  -8   ALA A N   
1440 C CA  . ALA A 189 ? 0.5478 0.4397 0.6766 0.0078  0.0594  0.1106  -8   ALA A CA  
1441 C C   . ALA A 189 ? 0.5317 0.4236 0.6702 0.0052  0.0533  0.0962  -8   ALA A C   
1442 O O   . ALA A 189 ? 0.4949 0.3844 0.6070 0.0073  0.0472  0.0809  -8   ALA A O   
1443 C CB  . ALA A 189 ? 0.5556 0.4329 0.7072 0.0049  0.0520  0.1071  -8   ALA A CB  
1444 N N   . LYS A 190 ? 0.5212 0.4162 0.7008 0.0007  0.0544  0.1014  -7   LYS A N   
1445 C CA  . LYS A 190 ? 0.5169 0.4134 0.7085 -0.0011 0.0474  0.0870  -7   LYS A CA  
1446 C C   . LYS A 190 ? 0.5274 0.4354 0.6909 0.0030  0.0522  0.0860  -7   LYS A C   
1447 O O   . LYS A 190 ? 0.5292 0.4346 0.6795 0.0043  0.0440  0.0700  -7   LYS A O   
1448 C CB  . LYS A 190 ? 0.4926 0.3932 0.7371 -0.0068 0.0491  0.0944  -7   LYS A CB  
1449 N N   . ALA A 191 ? 0.5376 0.4598 0.6942 0.0058  0.0654  0.1033  -6   ALA A N   
1450 C CA  . ALA A 191 ? 0.5137 0.4488 0.6489 0.0105  0.0702  0.1014  -6   ALA A CA  
1451 C C   . ALA A 191 ? 0.5165 0.4439 0.6106 0.0148  0.0635  0.0868  -6   ALA A C   
1452 O O   . ALA A 191 ? 0.5188 0.4467 0.6024 0.0167  0.0587  0.0749  -6   ALA A O   
1453 C CB  . ALA A 191 ? 0.4763 0.4310 0.6093 0.0144  0.0857  0.1220  -6   ALA A CB  
1454 N N   . GLY A 192 ? 0.5185 0.4385 0.5919 0.0162  0.0627  0.0879  -5   GLY A N   
1455 C CA  . GLY A 192 ? 0.5217 0.4341 0.5601 0.0193  0.0565  0.0749  -5   GLY A CA  
1456 C C   . GLY A 192 ? 0.5150 0.4142 0.5531 0.0168  0.0441  0.0584  -5   GLY A C   
1457 O O   . GLY A 192 ? 0.4916 0.3893 0.5126 0.0190  0.0396  0.0486  -5   GLY A O   
1458 N N   . LEU A 193 ? 0.4861 0.3769 0.5444 0.0129  0.0382  0.0553  -4   LEU A N   
1459 C CA  . LEU A 193 ? 0.5092 0.3910 0.5637 0.0123  0.0262  0.0387  -4   LEU A CA  
1460 C C   . LEU A 193 ? 0.5215 0.4081 0.5876 0.0125  0.0218  0.0319  -4   LEU A C   
1461 O O   . LEU A 193 ? 0.5429 0.4259 0.5947 0.0145  0.0132  0.0201  -4   LEU A O   
1462 C CB  . LEU A 193 ? 0.5189 0.3928 0.5949 0.0094  0.0198  0.0339  -4   LEU A CB  
1463 C CG  . LEU A 193 ? 0.5196 0.3875 0.5886 0.0106  0.0072  0.0155  -4   LEU A CG  
1464 C CD1 . LEU A 193 ? 0.5818 0.4476 0.6116 0.0140  0.0063  0.0114  -4   LEU A CD1 
1465 C CD2 . LEU A 193 ? 0.4608 0.3223 0.5470 0.0093  0.0016  0.0093  -4   LEU A CD2 
1466 N N   . THR A 194 ? 0.5317 0.4275 0.6251 0.0106  0.0274  0.0400  -3   THR A N   
1467 C CA  . THR A 194 ? 0.5202 0.4225 0.6260 0.0112  0.0238  0.0340  -3   THR A CA  
1468 C C   . THR A 194 ? 0.5241 0.4298 0.6013 0.0161  0.0254  0.0317  -3   THR A C   
1469 O O   . THR A 194 ? 0.5385 0.4433 0.6118 0.0182  0.0173  0.0216  -3   THR A O   
1470 C CB  . THR A 194 ? 0.4735 0.3874 0.6155 0.0082  0.0319  0.0452  -3   THR A CB  
1471 O OG1 . THR A 194 ? 0.4285 0.3377 0.6034 0.0032  0.0292  0.0467  -3   THR A OG1 
1472 C CG2 . THR A 194 ? 0.4530 0.3752 0.6090 0.0093  0.0280  0.0380  -3   THR A CG2 
1473 N N   . PHE A 195 ? 0.5245 0.4353 0.5837 0.0187  0.0352  0.0407  -2   PHE A N   
1474 C CA  . PHE A 195 ? 0.5436 0.4568 0.5788 0.0238  0.0356  0.0364  -2   PHE A CA  
1475 C C   . PHE A 195 ? 0.5531 0.4532 0.5652 0.0248  0.0258  0.0260  -2   PHE A C   
1476 O O   . PHE A 195 ? 0.5497 0.4484 0.5537 0.0277  0.0208  0.0195  -2   PHE A O   
1477 C CB  . PHE A 195 ? 0.5505 0.4725 0.5703 0.0273  0.0462  0.0450  -2   PHE A CB  
1478 C CG  . PHE A 195 ? 0.5362 0.4633 0.5394 0.0330  0.0469  0.0392  -2   PHE A CG  
1479 C CD1 . PHE A 195 ? 0.5507 0.4919 0.5663 0.0362  0.0516  0.0401  -2   PHE A CD1 
1480 C CD2 . PHE A 195 ? 0.5350 0.4530 0.5131 0.0353  0.0425  0.0322  -2   PHE A CD2 
1481 C CE1 . PHE A 195 ? 0.5732 0.5191 0.5760 0.0425  0.0513  0.0324  -2   PHE A CE1 
1482 C CE2 . PHE A 195 ? 0.5559 0.4770 0.5234 0.0406  0.0418  0.0254  -2   PHE A CE2 
1483 C CZ  . PHE A 195 ? 0.5790 0.5137 0.5586 0.0445  0.0458  0.0248  -2   PHE A CZ  
1484 N N   . LEU A 196 ? 0.5472 0.4383 0.5501 0.0227  0.0233  0.0253  -1   LEU A N   
1485 C CA  . LEU A 196 ? 0.5698 0.4513 0.5521 0.0236  0.0154  0.0172  -1   LEU A CA  
1486 C C   . LEU A 196 ? 0.5843 0.4644 0.5749 0.0241  0.0052  0.0085  -1   LEU A C   
1487 O O   . LEU A 196 ? 0.6095 0.4871 0.5860 0.0270  -0.0001 0.0043  -1   LEU A O   
1488 C CB  . LEU A 196 ? 0.5841 0.4589 0.5575 0.0217  0.0153  0.0176  -1   LEU A CB  
1489 C CG  . LEU A 196 ? 0.5666 0.4342 0.5184 0.0229  0.0088  0.0108  -1   LEU A CG  
1490 C CD1 . LEU A 196 ? 0.5791 0.4443 0.5101 0.0240  0.0135  0.0142  -1   LEU A CD1 
1491 C CD2 . LEU A 196 ? 0.5537 0.4177 0.5080 0.0217  0.0032  0.0050  -1   LEU A CD2 
1492 N N   . VAL A 197 ? 0.5448 0.4275 0.5602 0.0217  0.0019  0.0057  0    VAL A N   
1493 C CA  . VAL A 197 ? 0.5127 0.3967 0.5372 0.0231  -0.0093 -0.0048 0    VAL A CA  
1494 C C   . VAL A 197 ? 0.5164 0.4060 0.5438 0.0262  -0.0109 -0.0054 0    VAL A C   
1495 O O   . VAL A 197 ? 0.5031 0.3924 0.5202 0.0301  -0.0196 -0.0116 0    VAL A O   
1496 C CB  . VAL A 197 ? 0.5062 0.3928 0.5637 0.0198  -0.0130 -0.0092 0    VAL A CB  
1497 C CG1 . VAL A 197 ? 0.5339 0.4259 0.6061 0.0221  -0.0247 -0.0210 0    VAL A CG1 
1498 C CG2 . VAL A 197 ? 0.4503 0.3304 0.5042 0.0185  -0.0155 -0.0132 0    VAL A CG2 
1499 N N   . ASP A 198 ? 0.5228 0.4193 0.5639 0.0253  -0.0022 0.0018  1    ASP A N   
1500 C CA  . ASP A 198 ? 0.5364 0.4395 0.5823 0.0288  -0.0030 0.0006  1    ASP A CA  
1501 C C   . ASP A 198 ? 0.5708 0.4679 0.5889 0.0332  -0.0048 -0.0002 1    ASP A C   
1502 O O   . ASP A 198 ? 0.6101 0.5077 0.6274 0.0371  -0.0118 -0.0044 1    ASP A O   
1503 C CB  . ASP A 198 ? 0.5046 0.4189 0.5682 0.0280  0.0081  0.0086  1    ASP A CB  
1504 C CG  . ASP A 198 ? 0.5251 0.4473 0.6251 0.0239  0.0086  0.0098  1    ASP A CG  
1505 O OD1 . ASP A 198 ? 0.5401 0.4611 0.6553 0.0232  -0.0021 0.0007  1    ASP A OD1 
1506 O OD2 . ASP A 198 ? 0.5315 0.4626 0.6471 0.0218  0.0198  0.0202  1    ASP A OD2 
1507 N N   . LEU A 199 ? 0.5595 0.4509 0.5573 0.0328  0.0009  0.0041  2    LEU A N   
1508 C CA  . LEU A 199 ? 0.5495 0.4339 0.5256 0.0361  -0.0012 0.0033  2    LEU A CA  
1509 C C   . LEU A 199 ? 0.5905 0.4691 0.5573 0.0377  -0.0117 -0.0005 2    LEU A C   
1510 O O   . LEU A 199 ? 0.6558 0.5319 0.6166 0.0416  -0.0162 -0.0007 2    LEU A O   
1511 C CB  . LEU A 199 ? 0.5119 0.3915 0.4706 0.0348  0.0050  0.0069  2    LEU A CB  
1512 C CG  . LEU A 199 ? 0.5220 0.4089 0.4810 0.0362  0.0147  0.0103  2    LEU A CG  
1513 C CD1 . LEU A 199 ? 0.4995 0.3820 0.4416 0.0350  0.0184  0.0125  2    LEU A CD1 
1514 C CD2 . LEU A 199 ? 0.5152 0.4052 0.4747 0.0412  0.0145  0.0068  2    LEU A CD2 
1515 N N   . ILE A 200 ? 0.4963 0.3741 0.4625 0.0357  -0.0157 -0.0034 3    ILE A N   
1516 C CA  . ILE A 200 ? 0.5205 0.3972 0.4760 0.0386  -0.0254 -0.0074 3    ILE A CA  
1517 C C   . ILE A 200 ? 0.5566 0.4401 0.5260 0.0424  -0.0340 -0.0124 3    ILE A C   
1518 O O   . ILE A 200 ? 0.5623 0.4460 0.5209 0.0474  -0.0411 -0.0122 3    ILE A O   
1519 C CB  . ILE A 200 ? 0.5656 0.4424 0.5190 0.0365  -0.0276 -0.0120 3    ILE A CB  
1520 C CG1 . ILE A 200 ? 0.5477 0.4178 0.4845 0.0338  -0.0201 -0.0069 3    ILE A CG1 
1521 C CG2 . ILE A 200 ? 0.5890 0.4704 0.5337 0.0412  -0.0384 -0.0186 3    ILE A CG2 
1522 C CD1 . ILE A 200 ? 0.4742 0.3445 0.4150 0.0312  -0.0200 -0.0109 3    ILE A CD1 
1523 N N   . LYS A 201 ? 0.5698 0.4602 0.5652 0.0404  -0.0337 -0.0162 4    LYS A N   
1524 C CA  . LYS A 201 ? 0.5556 0.4542 0.5685 0.0439  -0.0426 -0.0225 4    LYS A CA  
1525 C C   . LYS A 201 ? 0.5653 0.4640 0.5747 0.0485  -0.0431 -0.0189 4    LYS A C   
1526 O O   . LYS A 201 ? 0.5538 0.4567 0.5648 0.0537  -0.0529 -0.0225 4    LYS A O   
1527 C CB  . LYS A 201 ? 0.5451 0.4512 0.5913 0.0397  -0.0400 -0.0254 4    LYS A CB  
1528 C CG  . LYS A 201 ? 0.6212 0.5275 0.6800 0.0360  -0.0430 -0.0316 4    LYS A CG  
1529 C CD  . LYS A 201 ? 0.6654 0.5796 0.7648 0.0319  -0.0421 -0.0339 4    LYS A CD  
1530 C CE  . LYS A 201 ? 0.6899 0.6033 0.8083 0.0284  -0.0465 -0.0412 4    LYS A CE  
1531 N NZ  . LYS A 201 ? 0.6901 0.6102 0.8525 0.0233  -0.0439 -0.0405 4    LYS A NZ  
1532 N N   . ASN A 202 ? 0.5765 0.4721 0.5836 0.0473  -0.0333 -0.0128 5    ASN A N   
1533 C CA  . ASN A 202 ? 0.6054 0.5011 0.6133 0.0520  -0.0337 -0.0111 5    ASN A CA  
1534 C C   . ASN A 202 ? 0.6055 0.4906 0.5906 0.0552  -0.0364 -0.0066 5    ASN A C   
1535 O O   . ASN A 202 ? 0.6136 0.4959 0.5996 0.0586  -0.0356 -0.0048 5    ASN A O   
1536 C CB  . ASN A 202 ? 0.6132 0.5138 0.6315 0.0507  -0.0224 -0.0090 5    ASN A CB  
1537 C CG  . ASN A 202 ? 0.6015 0.5148 0.6474 0.0481  -0.0188 -0.0106 5    ASN A CG  
1538 O OD1 . ASN A 202 ? 0.6316 0.5512 0.6948 0.0498  -0.0265 -0.0155 5    ASN A OD1 
1539 N ND2 . ASN A 202 ? 0.5222 0.4406 0.5737 0.0444  -0.0073 -0.0057 5    ASN A ND2 
1540 N N   . LYS A 203 ? 0.6289 0.5091 0.5961 0.0543  -0.0395 -0.0046 6    LYS A N   
1541 C CA  . LYS A 203 ? 0.6776 0.5494 0.6255 0.0568  -0.0418 0.0020  6    LYS A CA  
1542 C C   . LYS A 203 ? 0.6325 0.4954 0.5737 0.0541  -0.0333 0.0062  6    LYS A C   
1543 O O   . LYS A 203 ? 0.6321 0.4871 0.5645 0.0559  -0.0345 0.0122  6    LYS A O   
1544 C CB  . LYS A 203 ? 0.7568 0.6293 0.7077 0.0636  -0.0504 0.0045  6    LYS A CB  
1545 C CG  . LYS A 203 ? 0.8105 0.6941 0.7684 0.0676  -0.0606 -0.0013 6    LYS A CG  
1546 C CD  . LYS A 203 ? 0.8217 0.7090 0.7620 0.0685  -0.0654 -0.0016 6    LYS A CD  
1547 C CE  . LYS A 203 ? 0.8274 0.7282 0.7766 0.0731  -0.0768 -0.0114 6    LYS A CE  
1548 N NZ  . LYS A 203 ? 0.8255 0.7313 0.7735 0.0818  -0.0868 -0.0081 6    LYS A NZ  
1549 N N   . HIS A 204 ? 0.5690 0.4340 0.5156 0.0503  -0.0251 0.0036  7    HIS A N   
1550 C CA  . HIS A 204 ? 0.5830 0.4421 0.5220 0.0485  -0.0180 0.0055  7    HIS A CA  
1551 C C   . HIS A 204 ? 0.6056 0.4591 0.5278 0.0447  -0.0161 0.0089  7    HIS A C   
1552 O O   . HIS A 204 ? 0.6172 0.4642 0.5323 0.0436  -0.0129 0.0111  7    HIS A O   
1553 C CB  . HIS A 204 ? 0.5454 0.4122 0.4941 0.0474  -0.0098 0.0022  7    HIS A CB  
1554 C CG  . HIS A 204 ? 0.5368 0.4123 0.5032 0.0513  -0.0100 -0.0013 7    HIS A CG  
1555 N ND1 . HIS A 204 ? 0.5341 0.4066 0.5056 0.0566  -0.0144 -0.0032 7    HIS A ND1 
1556 C CD2 . HIS A 204 ? 0.4841 0.3715 0.4666 0.0509  -0.0061 -0.0028 7    HIS A CD2 
1557 C CE1 . HIS A 204 ? 0.5082 0.3915 0.4968 0.0597  -0.0133 -0.0071 7    HIS A CE1 
1558 N NE2 . HIS A 204 ? 0.5322 0.4253 0.5278 0.0560  -0.0077 -0.0064 7    HIS A NE2 
1559 N N   . MET A 205 ? 0.5925 0.4491 0.5102 0.0430  -0.0186 0.0082  8    MET A N   
1560 C CA  . MET A 205 ? 0.5830 0.4365 0.4858 0.0402  -0.0169 0.0104  8    MET A CA  
1561 C C   . MET A 205 ? 0.5736 0.4320 0.4709 0.0422  -0.0240 0.0087  8    MET A C   
1562 O O   . MET A 205 ? 0.5870 0.4517 0.4945 0.0448  -0.0299 0.0040  8    MET A O   
1563 C CB  . MET A 205 ? 0.5653 0.4201 0.4696 0.0360  -0.0099 0.0084  8    MET A CB  
1564 C CG  . MET A 205 ? 0.6101 0.4628 0.5145 0.0351  -0.0029 0.0096  8    MET A CG  
1565 S SD  . MET A 205 ? 0.6192 0.4725 0.5170 0.0313  0.0041  0.0102  8    MET A SD  
1566 C CE  . MET A 205 ? 0.6771 0.5374 0.5903 0.0298  0.0049  0.0092  8    MET A CE  
1567 N N   . ASN A 206 ? 0.5789 0.4365 0.4607 0.0417  -0.0237 0.0115  9    ASN A N   
1568 C CA  . ASN A 206 ? 0.5980 0.4634 0.4709 0.0452  -0.0301 0.0089  9    ASN A CA  
1569 C C   . ASN A 206 ? 0.6288 0.4972 0.4997 0.0424  -0.0278 0.0026  9    ASN A C   
1570 O O   . ASN A 206 ? 0.6197 0.4836 0.4838 0.0390  -0.0213 0.0058  9    ASN A O   
1571 C CB  . ASN A 206 ? 0.6355 0.5009 0.4918 0.0483  -0.0310 0.0187  9    ASN A CB  
1572 C CG  . ASN A 206 ? 0.7019 0.5799 0.5471 0.0545  -0.0386 0.0165  9    ASN A CG  
1573 O OD1 . ASN A 206 ? 0.6975 0.5830 0.5365 0.0550  -0.0393 0.0095  9    ASN A OD1 
1574 N ND2 . ASN A 206 ? 0.7726 0.6543 0.6153 0.0605  -0.0448 0.0222  9    ASN A ND2 
1575 N N   . ALA A 207 ? 0.6539 0.5300 0.5334 0.0443  -0.0340 -0.0075 10   ALA A N   
1576 C CA  . ALA A 207 ? 0.6401 0.5182 0.5228 0.0421  -0.0330 -0.0150 10   ALA A CA  
1577 C C   . ALA A 207 ? 0.6562 0.5373 0.5185 0.0436  -0.0311 -0.0132 10   ALA A C   
1578 O O   . ALA A 207 ? 0.6315 0.5119 0.4951 0.0412  -0.0279 -0.0172 10   ALA A O   
1579 C CB  . ALA A 207 ? 0.6170 0.5037 0.5154 0.0450  -0.0423 -0.0281 10   ALA A CB  
1580 N N   . ASP A 208 ? 0.6279 0.5133 0.4730 0.0478  -0.0326 -0.0063 11   ASP A N   
1581 C CA  . ASP A 208 ? 0.6341 0.5261 0.4608 0.0499  -0.0301 -0.0034 11   ASP A CA  
1582 C C   . ASP A 208 ? 0.6440 0.5269 0.4651 0.0447  -0.0206 0.0077  11   ASP A C   
1583 O O   . ASP A 208 ? 0.6999 0.5882 0.5084 0.0452  -0.0168 0.0114  11   ASP A O   
1584 C CB  . ASP A 208 ? 0.6936 0.5979 0.5048 0.0577  -0.0357 0.0008  11   ASP A CB  
1585 C CG  . ASP A 208 ? 0.8052 0.7229 0.6192 0.0645  -0.0465 -0.0135 11   ASP A CG  
1586 O OD1 . ASP A 208 ? 0.8302 0.7519 0.6527 0.0643  -0.0491 -0.0280 11   ASP A OD1 
1587 O OD2 . ASP A 208 ? 0.8756 0.8010 0.6846 0.0708  -0.0535 -0.0111 11   ASP A OD2 
1588 N N   . THR A 209 ? 0.6126 0.4838 0.4435 0.0402  -0.0168 0.0125  12   THR A N   
1589 C CA  . THR A 209 ? 0.6098 0.4736 0.4378 0.0359  -0.0094 0.0208  12   THR A CA  
1590 C C   . THR A 209 ? 0.5879 0.4525 0.4144 0.0328  -0.0046 0.0163  12   THR A C   
1591 O O   . THR A 209 ? 0.6001 0.4641 0.4353 0.0316  -0.0051 0.0084  12   THR A O   
1592 C CB  . THR A 209 ? 0.5986 0.4521 0.4386 0.0332  -0.0075 0.0229  12   THR A CB  
1593 O OG1 . THR A 209 ? 0.5683 0.4208 0.4115 0.0367  -0.0123 0.0268  12   THR A OG1 
1594 C CG2 . THR A 209 ? 0.5927 0.4393 0.4323 0.0294  -0.0014 0.0287  12   THR A CG2 
1595 N N   . ASP A 210 ? 0.5578 0.4246 0.3750 0.0317  -0.0001 0.0222  13   ASP A N   
1596 C CA  . ASP A 210 ? 0.5889 0.4571 0.4053 0.0290  0.0045  0.0186  13   ASP A CA  
1597 C C   . ASP A 210 ? 0.6123 0.4734 0.4318 0.0244  0.0103  0.0253  13   ASP A C   
1598 O O   . ASP A 210 ? 0.6231 0.4766 0.4483 0.0230  0.0104  0.0309  13   ASP A O   
1599 C CB  . ASP A 210 ? 0.6217 0.5030 0.4262 0.0327  0.0044  0.0165  13   ASP A CB  
1600 C CG  . ASP A 210 ? 0.6829 0.5707 0.4763 0.0346  0.0068  0.0288  13   ASP A CG  
1601 O OD1 . ASP A 210 ? 0.7068 0.5863 0.5047 0.0326  0.0076  0.0389  13   ASP A OD1 
1602 O OD2 . ASP A 210 ? 0.6920 0.5940 0.4738 0.0385  0.0081  0.0290  13   ASP A OD2 
1603 N N   . TYR A 211 ? 0.5704 0.4345 0.3882 0.0224  0.0144  0.0235  14   TYR A N   
1604 C CA  . TYR A 211 ? 0.5725 0.4315 0.3957 0.0182  0.0188  0.0276  14   TYR A CA  
1605 C C   . TYR A 211 ? 0.5964 0.4540 0.4205 0.0170  0.0205  0.0388  14   TYR A C   
1606 O O   . TYR A 211 ? 0.6243 0.4732 0.4585 0.0147  0.0205  0.0415  14   TYR A O   
1607 C CB  . TYR A 211 ? 0.5577 0.4224 0.3795 0.0169  0.0225  0.0243  14   TYR A CB  
1608 C CG  . TYR A 211 ? 0.5201 0.3803 0.3503 0.0130  0.0255  0.0252  14   TYR A CG  
1609 C CD1 . TYR A 211 ? 0.5369 0.3972 0.3718 0.0099  0.0287  0.0328  14   TYR A CD1 
1610 C CD2 . TYR A 211 ? 0.4946 0.3516 0.3296 0.0127  0.0249  0.0187  14   TYR A CD2 
1611 C CE1 . TYR A 211 ? 0.5458 0.4025 0.3921 0.0065  0.0300  0.0310  14   TYR A CE1 
1612 C CE2 . TYR A 211 ? 0.4821 0.3375 0.3239 0.0105  0.0262  0.0174  14   TYR A CE2 
1613 C CZ  . TYR A 211 ? 0.5196 0.3747 0.3676 0.0074  0.0282  0.0220  14   TYR A CZ  
1614 O OH  . TYR A 211 ? 0.5219 0.3763 0.3800 0.0055  0.0281  0.0179  14   TYR A OH  
1615 N N   . SER A 212 ? 0.6346 0.5014 0.4499 0.0191  0.0221  0.0458  15   SER A N   
1616 C CA  . SER A 212 ? 0.6947 0.5609 0.5134 0.0175  0.0251  0.0599  15   SER A CA  
1617 C C   . SER A 212 ? 0.6884 0.5461 0.5123 0.0191  0.0206  0.0656  15   SER A C   
1618 O O   . SER A 212 ? 0.7174 0.5662 0.5545 0.0161  0.0215  0.0725  15   SER A O   
1619 C CB  . SER A 212 ? 0.7775 0.6594 0.5847 0.0201  0.0295  0.0683  15   SER A CB  
1620 O OG  . SER A 212 ? 0.8529 0.7410 0.6612 0.0174  0.0347  0.0639  15   SER A OG  
1621 N N   . ILE A 213 ? 0.6772 0.5384 0.4927 0.0242  0.0153  0.0617  16   ILE A N   
1622 C CA  . ILE A 213 ? 0.6492 0.5029 0.4708 0.0263  0.0106  0.0665  16   ILE A CA  
1623 C C   . ILE A 213 ? 0.6287 0.4689 0.4663 0.0230  0.0096  0.0605  16   ILE A C   
1624 O O   . ILE A 213 ? 0.6185 0.4500 0.4680 0.0226  0.0082  0.0666  16   ILE A O   
1625 C CB  . ILE A 213 ? 0.6757 0.5362 0.4885 0.0323  0.0041  0.0607  16   ILE A CB  
1626 C CG1 . ILE A 213 ? 0.6708 0.5467 0.4675 0.0379  0.0036  0.0679  16   ILE A CG1 
1627 C CG2 . ILE A 213 ? 0.6534 0.5053 0.4760 0.0342  -0.0012 0.0623  16   ILE A CG2 
1628 C CD1 . ILE A 213 ? 0.6436 0.5302 0.4315 0.0441  -0.0034 0.0565  16   ILE A CD1 
1629 N N   . ALA A 214 ? 0.5668 0.4061 0.4057 0.0214  0.0101  0.0484  17   ALA A N   
1630 C CA  . ALA A 214 ? 0.5469 0.3779 0.3981 0.0201  0.0094  0.0421  17   ALA A CA  
1631 C C   . ALA A 214 ? 0.5594 0.3847 0.4216 0.0163  0.0121  0.0444  17   ALA A C   
1632 O O   . ALA A 214 ? 0.5018 0.3196 0.3775 0.0164  0.0100  0.0431  17   ALA A O   
1633 C CB  . ALA A 214 ? 0.5143 0.3483 0.3638 0.0201  0.0101  0.0316  17   ALA A CB  
1634 N N   . GLU A 215 ? 0.5883 0.4182 0.4474 0.0132  0.0163  0.0464  18   GLU A N   
1635 C CA  . GLU A 215 ? 0.6081 0.4338 0.4812 0.0091  0.0184  0.0477  18   GLU A CA  
1636 C C   . GLU A 215 ? 0.6164 0.4351 0.5030 0.0080  0.0176  0.0592  18   GLU A C   
1637 O O   . GLU A 215 ? 0.6186 0.4288 0.5241 0.0065  0.0154  0.0563  18   GLU A O   
1638 C CB  . GLU A 215 ? 0.5890 0.4225 0.4575 0.0062  0.0233  0.0489  18   GLU A CB  
1639 C CG  . GLU A 215 ? 0.6082 0.4388 0.4950 0.0013  0.0255  0.0514  18   GLU A CG  
1640 C CD  . GLU A 215 ? 0.5948 0.4348 0.4787 -0.0014 0.0305  0.0522  18   GLU A CD  
1641 O OE1 . GLU A 215 ? 0.6092 0.4581 0.4813 -0.0004 0.0344  0.0604  18   GLU A OE1 
1642 O OE2 . GLU A 215 ? 0.5864 0.4268 0.4798 -0.0037 0.0305  0.0441  18   GLU A OE2 
1643 N N   . ALA A 216 ? 0.5981 0.4212 0.4765 0.0096  0.0189  0.0725  19   ALA A N   
1644 C CA  . ALA A 216 ? 0.5702 0.3873 0.4621 0.0090  0.0187  0.0875  19   ALA A CA  
1645 C C   . ALA A 216 ? 0.5808 0.3876 0.4829 0.0123  0.0123  0.0848  19   ALA A C   
1646 O O   . ALA A 216 ? 0.5578 0.3546 0.4806 0.0111  0.0105  0.0917  19   ALA A O   
1647 C CB  . ALA A 216 ? 0.5610 0.3891 0.4380 0.0117  0.0219  0.1035  19   ALA A CB  
1648 N N   . ALA A 217 ? 0.5939 0.4028 0.4845 0.0165  0.0086  0.0751  20   ALA A N   
1649 C CA  . ALA A 217 ? 0.5838 0.3848 0.4850 0.0201  0.0029  0.0719  20   ALA A CA  
1650 C C   . ALA A 217 ? 0.5588 0.3518 0.4790 0.0185  0.0014  0.0599  20   ALA A C   
1651 O O   . ALA A 217 ? 0.5769 0.3605 0.5170 0.0194  -0.0022 0.0613  20   ALA A O   
1652 C CB  . ALA A 217 ? 0.5691 0.3763 0.4566 0.0246  -0.0002 0.0642  20   ALA A CB  
1653 N N   . PHE A 218 ? 0.5153 0.3131 0.4306 0.0168  0.0036  0.0475  21   PHE A N   
1654 C CA  . PHE A 218 ? 0.5576 0.3517 0.4886 0.0169  0.0016  0.0342  21   PHE A CA  
1655 C C   . PHE A 218 ? 0.5964 0.3829 0.5499 0.0127  0.0012  0.0381  21   PHE A C   
1656 O O   . PHE A 218 ? 0.5908 0.3698 0.5659 0.0139  -0.0033 0.0309  21   PHE A O   
1657 C CB  . PHE A 218 ? 0.4960 0.2990 0.4153 0.0169  0.0041  0.0223  21   PHE A CB  
1658 C CG  . PHE A 218 ? 0.5228 0.3266 0.4539 0.0193  0.0014  0.0074  21   PHE A CG  
1659 C CD1 . PHE A 218 ? 0.5308 0.3380 0.4617 0.0251  -0.0008 -0.0021 21   PHE A CD1 
1660 C CD2 . PHE A 218 ? 0.5504 0.3534 0.4943 0.0166  0.0008  0.0017  21   PHE A CD2 
1661 C CE1 . PHE A 218 ? 0.5289 0.3405 0.4691 0.0290  -0.0033 -0.0173 21   PHE A CE1 
1662 C CE2 . PHE A 218 ? 0.5612 0.3673 0.5166 0.0204  -0.0032 -0.0150 21   PHE A CE2 
1663 C CZ  . PHE A 218 ? 0.5513 0.3623 0.5032 0.0270  -0.0051 -0.0245 21   PHE A CZ  
1664 N N   . ASN A 219 ? 0.6131 0.4024 0.5642 0.0077  0.0059  0.0479  22   ASN A N   
1665 C CA  . ASN A 219 ? 0.6170 0.4008 0.5920 0.0026  0.0066  0.0520  22   ASN A CA  
1666 C C   . ASN A 219 ? 0.6309 0.4039 0.6273 0.0020  0.0047  0.0667  22   ASN A C   
1667 O O   . ASN A 219 ? 0.5987 0.3645 0.6236 -0.0022 0.0039  0.0692  22   ASN A O   
1668 C CB  . ASN A 219 ? 0.5847 0.3772 0.5510 -0.0021 0.0133  0.0601  22   ASN A CB  
1669 C CG  . ASN A 219 ? 0.5828 0.3844 0.5350 -0.0018 0.0144  0.0453  22   ASN A CG  
1670 O OD1 . ASN A 219 ? 0.6008 0.4037 0.5464 0.0023  0.0110  0.0312  22   ASN A OD1 
1671 N ND2 . ASN A 219 ? 0.5186 0.3277 0.4675 -0.0056 0.0195  0.0494  22   ASN A ND2 
1672 N N   . LYS A 220 ? 0.6518 0.4238 0.6374 0.0062  0.0035  0.0768  23   LYS A N   
1673 C CA  . LYS A 220 ? 0.6535 0.4151 0.6589 0.0073  0.0005  0.0908  23   LYS A CA  
1674 C C   . LYS A 220 ? 0.6395 0.3926 0.6580 0.0126  -0.0072 0.0779  23   LYS A C   
1675 O O   . LYS A 220 ? 0.6158 0.3584 0.6554 0.0142  -0.0111 0.0870  23   LYS A O   
1676 C CB  . LYS A 220 ? 0.6607 0.4285 0.6463 0.0102  0.0031  0.1112  23   LYS A CB  
1677 C CG  . LYS A 220 ? 0.7200 0.4965 0.6995 0.0059  0.0111  0.1290  23   LYS A CG  
1678 C CD  . LYS A 220 ? 0.7800 0.5701 0.7289 0.0111  0.0134  0.1414  23   LYS A CD  
1679 C CE  . LYS A 220 ? 0.8092 0.5949 0.7558 0.0181  0.0066  0.1457  23   LYS A CE  
1680 N NZ  . LYS A 220 ? 0.8350 0.6334 0.7614 0.0233  0.0084  0.1654  23   LYS A NZ  
1681 N N   . GLY A 221 ? 0.6029 0.3614 0.6100 0.0159  -0.0092 0.0579  24   GLY A N   
1682 C CA  . GLY A 221 ? 0.6062 0.3600 0.6261 0.0216  -0.0156 0.0442  24   GLY A CA  
1683 C C   . GLY A 221 ? 0.6250 0.3806 0.6323 0.0273  -0.0178 0.0489  24   GLY A C   
1684 O O   . GLY A 221 ? 0.6139 0.3648 0.6361 0.0324  -0.0233 0.0407  24   GLY A O   
1685 N N   . GLU A 222 ? 0.6210 0.3849 0.6026 0.0272  -0.0143 0.0596  25   GLU A N   
1686 C CA  . GLU A 222 ? 0.6350 0.4025 0.6059 0.0329  -0.0175 0.0622  25   GLU A CA  
1687 C C   . GLU A 222 ? 0.5936 0.3700 0.5534 0.0358  -0.0174 0.0452  25   GLU A C   
1688 O O   . GLU A 222 ? 0.6071 0.3848 0.5696 0.0411  -0.0212 0.0412  25   GLU A O   
1689 C CB  . GLU A 222 ? 0.6909 0.4656 0.6406 0.0328  -0.0151 0.0785  25   GLU A CB  
1690 C CG  . GLU A 222 ? 0.7113 0.4808 0.6699 0.0311  -0.0139 0.0997  25   GLU A CG  
1691 C CD  . GLU A 222 ? 0.7491 0.5301 0.6841 0.0334  -0.0120 0.1148  25   GLU A CD  
1692 O OE1 . GLU A 222 ? 0.7691 0.5620 0.6817 0.0326  -0.0086 0.1092  25   GLU A OE1 
1693 O OE2 . GLU A 222 ? 0.7603 0.5397 0.6994 0.0369  -0.0142 0.1324  25   GLU A OE2 
1694 N N   . THR A 223 ? 0.5661 0.3495 0.5148 0.0329  -0.0129 0.0363  26   THR A N   
1695 C CA  . THR A 223 ? 0.5384 0.3313 0.4781 0.0355  -0.0115 0.0230  26   THR A CA  
1696 C C   . THR A 223 ? 0.5284 0.3228 0.4772 0.0359  -0.0108 0.0087  26   THR A C   
1697 O O   . THR A 223 ? 0.5402 0.3312 0.4943 0.0320  -0.0098 0.0084  26   THR A O   
1698 C CB  . THR A 223 ? 0.5418 0.3437 0.4600 0.0330  -0.0072 0.0259  26   THR A CB  
1699 O OG1 . THR A 223 ? 0.5526 0.3632 0.4658 0.0358  -0.0063 0.0178  26   THR A OG1 
1700 C CG2 . THR A 223 ? 0.5105 0.3142 0.4230 0.0283  -0.0028 0.0244  26   THR A CG2 
1701 N N   . ALA A 224 ? 0.5174 0.3194 0.4679 0.0410  -0.0111 -0.0034 27   ALA A N   
1702 C CA  . ALA A 224 ? 0.5131 0.3206 0.4711 0.0440  -0.0112 -0.0191 27   ALA A CA  
1703 C C   . ALA A 224 ? 0.5265 0.3446 0.4689 0.0424  -0.0062 -0.0233 27   ALA A C   
1704 O O   . ALA A 224 ? 0.5210 0.3434 0.4689 0.0443  -0.0072 -0.0352 27   ALA A O   
1705 C CB  . ALA A 224 ? 0.5036 0.3188 0.4679 0.0515  -0.0126 -0.0297 27   ALA A CB  
1706 N N   . MET A 225 ? 0.4815 0.3045 0.4065 0.0397  -0.0017 -0.0151 28   MET A N   
1707 C CA  . MET A 225 ? 0.4918 0.3248 0.4037 0.0390  0.0029  -0.0178 28   MET A CA  
1708 C C   . MET A 225 ? 0.5044 0.3351 0.4042 0.0334  0.0056  -0.0071 28   MET A C   
1709 O O   . MET A 225 ? 0.5100 0.3365 0.4068 0.0317  0.0048  0.0015  28   MET A O   
1710 C CB  . MET A 225 ? 0.5057 0.3526 0.4120 0.0440  0.0065  -0.0219 28   MET A CB  
1711 C CG  . MET A 225 ? 0.5439 0.3991 0.4590 0.0514  0.0050  -0.0350 28   MET A CG  
1712 S SD  . MET A 225 ? 0.5538 0.4285 0.4624 0.0574  0.0114  -0.0360 28   MET A SD  
1713 C CE  . MET A 225 ? 0.5158 0.3840 0.4332 0.0561  0.0099  -0.0286 28   MET A CE  
1714 N N   . THR A 226 ? 0.5166 0.3516 0.4093 0.0316  0.0081  -0.0087 29   THR A N   
1715 C CA  . THR A 226 ? 0.5268 0.3624 0.4081 0.0277  0.0110  -0.0011 29   THR A CA  
1716 C C   . THR A 226 ? 0.5485 0.3940 0.4222 0.0292  0.0145  -0.0046 29   THR A C   
1717 O O   . THR A 226 ? 0.5434 0.3965 0.4185 0.0335  0.0147  -0.0122 29   THR A O   
1718 C CB  . THR A 226 ? 0.5402 0.3687 0.4227 0.0228  0.0104  0.0048  29   THR A CB  
1719 O OG1 . THR A 226 ? 0.5852 0.4161 0.4563 0.0205  0.0128  0.0109  29   THR A OG1 
1720 C CG2 . THR A 226 ? 0.5239 0.3530 0.4127 0.0215  0.0102  -0.0011 29   THR A CG2 
1721 N N   . ILE A 227 ? 0.5326 0.3794 0.3985 0.0267  0.0169  0.0009  30   ILE A N   
1722 C CA  . ILE A 227 ? 0.5139 0.3688 0.3740 0.0280  0.0200  0.0005  30   ILE A CA  
1723 C C   . ILE A 227 ? 0.5065 0.3588 0.3627 0.0243  0.0202  0.0024  30   ILE A C   
1724 O O   . ILE A 227 ? 0.5105 0.3588 0.3646 0.0214  0.0201  0.0068  30   ILE A O   
1725 C CB  . ILE A 227 ? 0.4870 0.3463 0.3465 0.0291  0.0227  0.0054  30   ILE A CB  
1726 C CG1 . ILE A 227 ? 0.4332 0.2985 0.2975 0.0332  0.0238  0.0037  30   ILE A CG1 
1727 C CG2 . ILE A 227 ? 0.4575 0.3232 0.3130 0.0299  0.0258  0.0082  30   ILE A CG2 
1728 C CD1 . ILE A 227 ? 0.4547 0.3243 0.3237 0.0331  0.0269  0.0102  30   ILE A CD1 
1729 N N   . ASN A 228 ? 0.5432 0.3995 0.3990 0.0250  0.0201  -0.0020 31   ASN A N   
1730 C CA  . ASN A 228 ? 0.5532 0.4085 0.4077 0.0216  0.0204  -0.0009 31   ASN A CA  
1731 C C   . ASN A 228 ? 0.5233 0.3867 0.3769 0.0243  0.0200  -0.0063 31   ASN A C   
1732 O O   . ASN A 228 ? 0.5085 0.3793 0.3607 0.0294  0.0195  -0.0106 31   ASN A O   
1733 C CB  . ASN A 228 ? 0.5860 0.4343 0.4468 0.0174  0.0192  0.0007  31   ASN A CB  
1734 C CG  . ASN A 228 ? 0.6238 0.4716 0.4804 0.0140  0.0212  0.0063  31   ASN A CG  
1735 O OD1 . ASN A 228 ? 0.6659 0.5184 0.5183 0.0142  0.0227  0.0055  31   ASN A OD1 
1736 N ND2 . ASN A 228 ? 0.6413 0.4849 0.4987 0.0118  0.0214  0.0122  31   ASN A ND2 
1737 N N   . GLY A 229 ? 0.5503 0.4145 0.4040 0.0218  0.0204  -0.0060 32   GLY A N   
1738 C CA  . GLY A 229 ? 0.5578 0.4305 0.4110 0.0246  0.0192  -0.0109 32   GLY A CA  
1739 C C   . GLY A 229 ? 0.5897 0.4626 0.4535 0.0225  0.0162  -0.0182 32   GLY A C   
1740 O O   . GLY A 229 ? 0.5507 0.4162 0.4237 0.0186  0.0155  -0.0179 32   GLY A O   
1741 N N   . PRO A 230 ? 0.6005 0.4824 0.4655 0.0254  0.0138  -0.0246 33   PRO A N   
1742 C CA  . PRO A 230 ? 0.6153 0.4989 0.4948 0.0237  0.0097  -0.0339 33   PRO A CA  
1743 C C   . PRO A 230 ? 0.6174 0.4942 0.5085 0.0157  0.0120  -0.0290 33   PRO A C   
1744 O O   . PRO A 230 ? 0.5878 0.4613 0.4964 0.0123  0.0095  -0.0333 33   PRO A O   
1745 C CB  . PRO A 230 ? 0.6238 0.5206 0.5002 0.0291  0.0067  -0.0405 33   PRO A CB  
1746 C CG  . PRO A 230 ? 0.6029 0.5054 0.4627 0.0356  0.0088  -0.0351 33   PRO A CG  
1747 C CD  . PRO A 230 ? 0.5920 0.4840 0.4472 0.0313  0.0140  -0.0238 33   PRO A CD  
1748 N N   . TRP A 231 ? 0.5579 0.4335 0.4415 0.0132  0.0166  -0.0202 34   TRP A N   
1749 C CA  . TRP A 231 ? 0.5638 0.4370 0.4559 0.0069  0.0200  -0.0145 34   TRP A CA  
1750 C C   . TRP A 231 ? 0.5684 0.4326 0.4679 0.0029  0.0212  -0.0082 34   TRP A C   
1751 O O   . TRP A 231 ? 0.5774 0.4408 0.4886 -0.0022 0.0239  -0.0026 34   TRP A O   
1752 C CB  . TRP A 231 ? 0.5393 0.4150 0.4202 0.0068  0.0243  -0.0081 34   TRP A CB  
1753 C CG  . TRP A 231 ? 0.5320 0.4027 0.4000 0.0092  0.0251  -0.0037 34   TRP A CG  
1754 C CD1 . TRP A 231 ? 0.5298 0.3950 0.3945 0.0074  0.0268  0.0027  34   TRP A CD1 
1755 C CD2 . TRP A 231 ? 0.5181 0.3901 0.3772 0.0140  0.0239  -0.0049 34   TRP A CD2 
1756 N NE1 . TRP A 231 ? 0.5377 0.4006 0.3929 0.0106  0.0261  0.0036  34   TRP A NE1 
1757 C CE2 . TRP A 231 ? 0.5117 0.3782 0.3647 0.0142  0.0248  -0.0002 34   TRP A CE2 
1758 C CE3 . TRP A 231 ? 0.5367 0.4149 0.3936 0.0186  0.0220  -0.0084 34   TRP A CE3 
1759 C CZ2 . TRP A 231 ? 0.5237 0.3901 0.3719 0.0177  0.0245  0.0010  34   TRP A CZ2 
1760 C CZ3 . TRP A 231 ? 0.5579 0.4361 0.4080 0.0225  0.0224  -0.0050 34   TRP A CZ3 
1761 C CH2 . TRP A 231 ? 0.5328 0.4046 0.3801 0.0214  0.0239  -0.0004 34   TRP A CH2 
1762 N N   . ALA A 232 ? 0.5830 0.4415 0.4766 0.0055  0.0197  -0.0076 35   ALA A N   
1763 C CA  . ALA A 232 ? 0.5680 0.4177 0.4679 0.0029  0.0201  -0.0010 35   ALA A CA  
1764 C C   . ALA A 232 ? 0.5871 0.4322 0.5078 0.0017  0.0157  -0.0072 35   ALA A C   
1765 O O   . ALA A 232 ? 0.6276 0.4645 0.5585 -0.0007 0.0157  -0.0006 35   ALA A O   
1766 C CB  . ALA A 232 ? 0.5370 0.3831 0.4240 0.0065  0.0196  0.0014  35   ALA A CB  
1767 N N   . TRP A 233 ? 0.6066 0.4573 0.5352 0.0042  0.0114  -0.0200 36   TRP A N   
1768 C CA  . TRP A 233 ? 0.6254 0.4724 0.5758 0.0044  0.0056  -0.0298 36   TRP A CA  
1769 C C   . TRP A 233 ? 0.6594 0.5006 0.6353 -0.0031 0.0065  -0.0237 36   TRP A C   
1770 O O   . TRP A 233 ? 0.6747 0.5072 0.6718 -0.0046 0.0031  -0.0250 36   TRP A O   
1771 C CB  . TRP A 233 ? 0.6067 0.4647 0.5590 0.0101  -0.0003 -0.0469 36   TRP A CB  
1772 C CG  . TRP A 233 ? 0.5966 0.4626 0.5260 0.0182  -0.0005 -0.0509 36   TRP A CG  
1773 C CD1 . TRP A 233 ? 0.5895 0.4521 0.5038 0.0203  0.0028  -0.0437 36   TRP A CD1 
1774 C CD2 . TRP A 233 ? 0.5833 0.4637 0.5039 0.0254  -0.0038 -0.0619 36   TRP A CD2 
1775 N NE1 . TRP A 233 ? 0.5956 0.4692 0.4946 0.0278  0.0025  -0.0484 36   TRP A NE1 
1776 C CE2 . TRP A 233 ? 0.5993 0.4844 0.4998 0.0314  -0.0012 -0.0584 36   TRP A CE2 
1777 C CE3 . TRP A 233 ? 0.5714 0.4625 0.4998 0.0279  -0.0089 -0.0736 36   TRP A CE3 
1778 C CZ2 . TRP A 233 ? 0.6174 0.5178 0.5041 0.0399  -0.0024 -0.0638 36   TRP A CZ2 
1779 C CZ3 . TRP A 233 ? 0.5962 0.5029 0.5091 0.0371  -0.0113 -0.0807 36   TRP A CZ3 
1780 C CH2 . TRP A 233 ? 0.6300 0.5415 0.5217 0.0432  -0.0076 -0.0747 36   TRP A CH2 
1781 N N   . SER A 234 ? 0.6667 0.5127 0.6442 -0.0077 0.0112  -0.0167 37   SER A N   
1782 C CA  . SER A 234 ? 0.6918 0.5346 0.6968 -0.0151 0.0132  -0.0097 37   SER A CA  
1783 C C   . SER A 234 ? 0.6541 0.4864 0.6643 -0.0182 0.0167  0.0068  37   SER A C   
1784 O O   . SER A 234 ? 0.6570 0.4815 0.6963 -0.0221 0.0146  0.0093  37   SER A O   
1785 C CB  . SER A 234 ? 0.7575 0.6107 0.7621 -0.0188 0.0188  -0.0046 37   SER A CB  
1786 O OG  . SER A 234 ? 0.8041 0.6658 0.8173 -0.0170 0.0135  -0.0205 37   SER A OG  
1787 N N   . ASN A 235 ? 0.5905 0.4235 0.5742 -0.0160 0.0213  0.0173  38   ASN A N   
1788 C CA  . ASN A 235 ? 0.6143 0.4396 0.6012 -0.0178 0.0241  0.0338  38   ASN A CA  
1789 C C   . ASN A 235 ? 0.6342 0.4476 0.6331 -0.0151 0.0175  0.0287  38   ASN A C   
1790 O O   . ASN A 235 ? 0.6586 0.4632 0.6763 -0.0178 0.0176  0.0401  38   ASN A O   
1791 C CB  . ASN A 235 ? 0.6045 0.4346 0.5625 -0.0151 0.0290  0.0443  38   ASN A CB  
1792 C CG  . ASN A 235 ? 0.6313 0.4735 0.5816 -0.0175 0.0362  0.0519  38   ASN A CG  
1793 O OD1 . ASN A 235 ? 0.6119 0.4580 0.5813 -0.0223 0.0389  0.0538  38   ASN A OD1 
1794 N ND2 . ASN A 235 ? 0.6543 0.5038 0.5784 -0.0137 0.0390  0.0546  38   ASN A ND2 
1795 N N   . ILE A 236 ? 0.6036 0.4176 0.5935 -0.0095 0.0120  0.0126  39   ILE A N   
1796 C CA  . ILE A 236 ? 0.6086 0.4138 0.6122 -0.0061 0.0056  0.0050  39   ILE A CA  
1797 C C   . ILE A 236 ? 0.5759 0.3756 0.6161 -0.0092 0.0004  -0.0032 39   ILE A C   
1798 O O   . ILE A 236 ? 0.5779 0.3666 0.6408 -0.0099 -0.0029 -0.0001 39   ILE A O   
1799 C CB  . ILE A 236 ? 0.6310 0.4421 0.6163 0.0015  0.0020  -0.0104 39   ILE A CB  
1800 C CG1 . ILE A 236 ? 0.5841 0.4021 0.5379 0.0034  0.0072  -0.0039 39   ILE A CG1 
1801 C CG2 . ILE A 236 ? 0.6301 0.4336 0.6257 0.0058  -0.0031 -0.0155 39   ILE A CG2 
1802 C CD1 . ILE A 236 ? 0.5823 0.4060 0.5210 0.0102  0.0052  -0.0141 39   ILE A CD1 
1803 N N   . ASP A 237 ? 0.5902 0.3977 0.6393 -0.0109 -0.0010 -0.0139 40   ASP A N   
1804 C CA  . ASP A 237 ? 0.6305 0.4340 0.7190 -0.0143 -0.0068 -0.0234 40   ASP A CA  
1805 C C   . ASP A 237 ? 0.6494 0.4417 0.7657 -0.0220 -0.0031 -0.0037 40   ASP A C   
1806 O O   . ASP A 237 ? 0.6310 0.4121 0.7804 -0.0231 -0.0089 -0.0068 40   ASP A O   
1807 C CB  . ASP A 237 ? 0.6472 0.4627 0.7402 -0.0158 -0.0078 -0.0344 40   ASP A CB  
1808 C CG  . ASP A 237 ? 0.6939 0.5210 0.7688 -0.0068 -0.0142 -0.0566 40   ASP A CG  
1809 O OD1 . ASP A 237 ? 0.7091 0.5350 0.7786 0.0002  -0.0192 -0.0674 40   ASP A OD1 
1810 O OD2 . ASP A 237 ? 0.6925 0.5316 0.7591 -0.0061 -0.0140 -0.0626 40   ASP A OD2 
1811 N N   . THR A 238 ? 0.6552 0.4512 0.7580 -0.0266 0.0065  0.0174  41   THR A N   
1812 C CA  . THR A 238 ? 0.6715 0.4609 0.7974 -0.0333 0.0120  0.0400  41   THR A CA  
1813 C C   . THR A 238 ? 0.6738 0.4503 0.8035 -0.0308 0.0101  0.0511  41   THR A C   
1814 O O   . THR A 238 ? 0.6652 0.4315 0.8288 -0.0352 0.0099  0.0634  41   THR A O   
1815 C CB  . THR A 238 ? 0.6508 0.4518 0.7548 -0.0362 0.0231  0.0586  41   THR A CB  
1816 O OG1 . THR A 238 ? 0.6211 0.4342 0.7204 -0.0372 0.0239  0.0463  41   THR A OG1 
1817 C CG2 . THR A 238 ? 0.6561 0.4546 0.7880 -0.0435 0.0302  0.0835  41   THR A CG2 
1818 N N   . SER A 239 ? 0.6570 0.4342 0.7541 -0.0240 0.0092  0.0488  42   SER A N   
1819 C CA  . SER A 239 ? 0.6567 0.4225 0.7579 -0.0207 0.0063  0.0574  42   SER A CA  
1820 C C   . SER A 239 ? 0.6403 0.3950 0.7720 -0.0182 -0.0037 0.0402  42   SER A C   
1821 O O   . SER A 239 ? 0.6529 0.3974 0.7921 -0.0150 -0.0071 0.0456  42   SER A O   
1822 C CB  . SER A 239 ? 0.6754 0.4464 0.7368 -0.0140 0.0071  0.0567  42   SER A CB  
1823 O OG  . SER A 239 ? 0.6689 0.4435 0.7204 -0.0090 0.0017  0.0332  42   SER A OG  
1824 N N   . ALA A 240 ? 0.5890 0.3470 0.7366 -0.0182 -0.0093 0.0178  43   ALA A N   
1825 C CA  . ALA A 240 ? 0.6102 0.3602 0.7896 -0.0148 -0.0200 -0.0026 43   ALA A CA  
1826 C C   . ALA A 240 ? 0.6620 0.4120 0.8222 -0.0053 -0.0246 -0.0148 43   ALA A C   
1827 O O   . ALA A 240 ? 0.6790 0.4221 0.8636 -0.0010 -0.0330 -0.0294 43   ALA A O   
1828 C CB  . ALA A 240 ? 0.5580 0.2919 0.7855 -0.0203 -0.0225 0.0092  43   ALA A CB  
1829 N N   . VAL A 241 ? 0.6664 0.4251 0.7850 -0.0017 -0.0195 -0.0100 44   VAL A N   
1830 C CA  . VAL A 241 ? 0.6619 0.4236 0.7635 0.0071  -0.0230 -0.0221 44   VAL A CA  
1831 C C   . VAL A 241 ? 0.6473 0.4196 0.7505 0.0132  -0.0291 -0.0501 44   VAL A C   
1832 O O   . VAL A 241 ? 0.6230 0.4053 0.7220 0.0118  -0.0287 -0.0587 44   VAL A O   
1833 C CB  . VAL A 241 ? 0.6912 0.4607 0.7516 0.0086  -0.0159 -0.0105 44   VAL A CB  
1834 C CG1 . VAL A 241 ? 0.6851 0.4627 0.7272 0.0173  -0.0183 -0.0256 44   VAL A CG1 
1835 C CG2 . VAL A 241 ? 0.6936 0.4543 0.7521 0.0063  -0.0126 0.0132  44   VAL A CG2 
1836 N N   . ASN A 242 ? 0.6621 0.4345 0.7710 0.0211  -0.0350 -0.0647 45   ASN A N   
1837 C CA  . ASN A 242 ? 0.6394 0.4250 0.7496 0.0295  -0.0413 -0.0924 45   ASN A CA  
1838 C C   . ASN A 242 ? 0.5835 0.3856 0.6531 0.0356  -0.0360 -0.0942 45   ASN A C   
1839 O O   . ASN A 242 ? 0.5802 0.3857 0.6399 0.0421  -0.0358 -0.0971 45   ASN A O   
1840 C CB  . ASN A 242 ? 0.5984 0.3775 0.7388 0.0357  -0.0503 -0.1083 45   ASN A CB  
1841 C CG  . ASN A 242 ? 0.6310 0.4260 0.7765 0.0454  -0.0580 -0.1392 45   ASN A CG  
1842 O OD1 . ASN A 242 ? 0.6318 0.4401 0.7674 0.0461  -0.0583 -0.1489 45   ASN A OD1 
1843 N ND2 . ASN A 242 ? 0.6770 0.4720 0.8390 0.0540  -0.0648 -0.1560 45   ASN A ND2 
1844 N N   . TYR A 243 ? 0.5625 0.3753 0.6115 0.0338  -0.0318 -0.0925 46   TYR A N   
1845 C CA  . TYR A 243 ? 0.5638 0.3890 0.5766 0.0373  -0.0251 -0.0871 46   TYR A CA  
1846 C C   . TYR A 243 ? 0.5764 0.4216 0.5774 0.0454  -0.0273 -0.1053 46   TYR A C   
1847 O O   . TYR A 243 ? 0.5930 0.4431 0.6086 0.0463  -0.0331 -0.1197 46   TYR A O   
1848 C CB  . TYR A 243 ? 0.5092 0.3313 0.5042 0.0295  -0.0175 -0.0669 46   TYR A CB  
1849 C CG  . TYR A 243 ? 0.5387 0.3657 0.5354 0.0255  -0.0172 -0.0689 46   TYR A CG  
1850 C CD1 . TYR A 243 ? 0.5384 0.3569 0.5628 0.0191  -0.0200 -0.0683 46   TYR A CD1 
1851 C CD2 . TYR A 243 ? 0.5715 0.4121 0.5438 0.0279  -0.0137 -0.0697 46   TYR A CD2 
1852 C CE1 . TYR A 243 ? 0.5495 0.3737 0.5781 0.0153  -0.0197 -0.0706 46   TYR A CE1 
1853 C CE2 . TYR A 243 ? 0.5875 0.4334 0.5617 0.0246  -0.0136 -0.0715 46   TYR A CE2 
1854 C CZ  . TYR A 243 ? 0.5731 0.4112 0.5754 0.0183  -0.0167 -0.0726 46   TYR A CZ  
1855 O OH  . TYR A 243 ? 0.5543 0.3987 0.5615 0.0151  -0.0169 -0.0750 46   TYR A OH  
1856 N N   . GLY A 244 ? 0.5405 0.3983 0.5169 0.0519  -0.0229 -0.1046 47   GLY A N   
1857 C CA  . GLY A 244 ? 0.5532 0.4325 0.5111 0.0598  -0.0222 -0.1147 47   GLY A CA  
1858 C C   . GLY A 244 ? 0.5659 0.4495 0.4972 0.0570  -0.0137 -0.0974 47   GLY A C   
1859 O O   . GLY A 244 ? 0.5290 0.4011 0.4549 0.0508  -0.0086 -0.0806 47   GLY A O   
1860 N N   . VAL A 245 ? 0.6187 0.5190 0.5350 0.0619  -0.0128 -0.1016 48   VAL A N   
1861 C CA  . VAL A 245 ? 0.5856 0.4909 0.4794 0.0603  -0.0054 -0.0859 48   VAL A CA  
1862 C C   . VAL A 245 ? 0.5622 0.4902 0.4395 0.0714  -0.0028 -0.0903 48   VAL A C   
1863 O O   . VAL A 245 ? 0.5433 0.4877 0.4201 0.0800  -0.0077 -0.1059 48   VAL A O   
1864 C CB  . VAL A 245 ? 0.5298 0.4345 0.4230 0.0558  -0.0064 -0.0838 48   VAL A CB  
1865 C CG1 . VAL A 245 ? 0.5008 0.4125 0.3728 0.0562  0.0003  -0.0697 48   VAL A CG1 
1866 C CG2 . VAL A 245 ? 0.5048 0.3905 0.4145 0.0454  -0.0073 -0.0779 48   VAL A CG2 
1867 N N   . THR A 246 ? 0.5168 0.4474 0.3820 0.0718  0.0047  -0.0767 49   THR A N   
1868 C CA  . THR A 246 ? 0.5248 0.4779 0.3780 0.0827  0.0083  -0.0794 49   THR A CA  
1869 C C   . THR A 246 ? 0.5507 0.5081 0.3905 0.0812  0.0176  -0.0594 49   THR A C   
1870 O O   . THR A 246 ? 0.5605 0.5034 0.4004 0.0725  0.0199  -0.0462 49   THR A O   
1871 C CB  . THR A 246 ? 0.4939 0.4491 0.3572 0.0874  0.0067  -0.0898 49   THR A CB  
1872 O OG1 . THR A 246 ? 0.5465 0.5287 0.3984 0.0998  0.0099  -0.0959 49   THR A OG1 
1873 C CG2 . THR A 246 ? 0.4963 0.4366 0.3643 0.0804  0.0112  -0.0762 49   THR A CG2 
1874 N N   . VAL A 247 ? 0.5584 0.5373 0.3885 0.0905  0.0228  -0.0577 50   VAL A N   
1875 C CA  . VAL A 247 ? 0.5817 0.5674 0.4030 0.0900  0.0319  -0.0380 50   VAL A CA  
1876 C C   . VAL A 247 ? 0.5984 0.5675 0.4302 0.0815  0.0353  -0.0278 50   VAL A C   
1877 O O   . VAL A 247 ? 0.6053 0.5698 0.4462 0.0816  0.0334  -0.0353 50   VAL A O   
1878 C CB  . VAL A 247 ? 0.5766 0.5926 0.3867 0.1027  0.0375  -0.0378 50   VAL A CB  
1879 C CG1 . VAL A 247 ? 0.5879 0.6113 0.4048 0.1084  0.0363  -0.0520 50   VAL A CG1 
1880 C CG2 . VAL A 247 ? 0.5300 0.5535 0.3361 0.1020  0.0481  -0.0149 50   VAL A CG2 
1881 N N   . LEU A 248 ? 0.5877 0.5482 0.4194 0.0749  0.0395  -0.0116 51   LEU A N   
1882 C CA  . LEU A 248 ? 0.5793 0.5264 0.4216 0.0677  0.0417  -0.0032 51   LEU A CA  
1883 C C   . LEU A 248 ? 0.6154 0.5774 0.4616 0.0727  0.0479  0.0004  51   LEU A C   
1884 O O   . LEU A 248 ? 0.6194 0.6035 0.4581 0.0814  0.0528  0.0015  51   LEU A O   
1885 C CB  . LEU A 248 ? 0.5495 0.4874 0.3936 0.0611  0.0440  0.0105  51   LEU A CB  
1886 C CG  . LEU A 248 ? 0.5392 0.4608 0.3824 0.0547  0.0386  0.0081  51   LEU A CG  
1887 C CD1 . LEU A 248 ? 0.5583 0.4803 0.4002 0.0530  0.0417  0.0201  51   LEU A CD1 
1888 C CD2 . LEU A 248 ? 0.4615 0.3652 0.3126 0.0474  0.0349  0.0063  51   LEU A CD2 
1889 N N   . PRO A 249 ? 0.6521 0.6044 0.5101 0.0681  0.0478  0.0020  52   PRO A N   
1890 C CA  . PRO A 249 ? 0.6582 0.6257 0.5228 0.0729  0.0538  0.0047  52   PRO A CA  
1891 C C   . PRO A 249 ? 0.6727 0.6521 0.5397 0.0727  0.0630  0.0223  52   PRO A C   
1892 O O   . PRO A 249 ? 0.6865 0.6554 0.5563 0.0665  0.0632  0.0325  52   PRO A O   
1893 C CB  . PRO A 249 ? 0.6489 0.6002 0.5270 0.0670  0.0497  0.0023  52   PRO A CB  
1894 C CG  . PRO A 249 ? 0.6627 0.5927 0.5387 0.0612  0.0412  -0.0036 52   PRO A CG  
1895 C CD  . PRO A 249 ? 0.6709 0.6005 0.5367 0.0596  0.0420  0.0009  52   PRO A CD  
1896 N N   . THR A 250 ? 0.6088 0.6113 0.4763 0.0802  0.0708  0.0261  53   THR A N   
1897 C CA  . THR A 250 ? 0.5815 0.5959 0.4564 0.0796  0.0806  0.0454  53   THR A CA  
1898 C C   . THR A 250 ? 0.5719 0.5755 0.4691 0.0716  0.0816  0.0516  53   THR A C   
1899 O O   . THR A 250 ? 0.5336 0.5279 0.4379 0.0696  0.0763  0.0408  53   THR A O   
1900 C CB  . THR A 250 ? 0.5863 0.6331 0.4541 0.0910  0.0902  0.0498  53   THR A CB  
1901 O OG1 . THR A 250 ? 0.6023 0.6580 0.4777 0.0947  0.0913  0.0401  53   THR A OG1 
1902 C CG2 . THR A 250 ? 0.5904 0.6501 0.4360 0.1004  0.0874  0.0405  53   THR A CG2 
1903 N N   . PHE A 251 ? 0.5494 0.5553 0.4599 0.0675  0.0881  0.0695  54   PHE A N   
1904 C CA  . PHE A 251 ? 0.5323 0.5323 0.4682 0.0606  0.0895  0.0758  54   PHE A CA  
1905 C C   . PHE A 251 ? 0.5270 0.5499 0.4762 0.0635  0.1025  0.0944  54   PHE A C   
1906 O O   . PHE A 251 ? 0.5043 0.5354 0.4503 0.0653  0.1086  0.1093  54   PHE A O   
1907 C CB  . PHE A 251 ? 0.5098 0.4862 0.4565 0.0510  0.0827  0.0778  54   PHE A CB  
1908 C CG  . PHE A 251 ? 0.5300 0.5015 0.5050 0.0445  0.0827  0.0822  54   PHE A CG  
1909 C CD1 . PHE A 251 ? 0.5493 0.5192 0.5323 0.0440  0.0787  0.0720  54   PHE A CD1 
1910 C CD2 . PHE A 251 ? 0.5278 0.4957 0.5246 0.0390  0.0854  0.0958  54   PHE A CD2 
1911 C CE1 . PHE A 251 ? 0.5620 0.5288 0.5732 0.0383  0.0773  0.0745  54   PHE A CE1 
1912 C CE2 . PHE A 251 ? 0.5258 0.4894 0.5529 0.0329  0.0840  0.0975  54   PHE A CE2 
1913 C CZ  . PHE A 251 ? 0.5454 0.5095 0.5790 0.0327  0.0799  0.0865  54   PHE A CZ  
1914 N N   . LYS A 252 ? 0.5550 0.5894 0.5202 0.0643  0.1071  0.0945  55   LYS A N   
1915 C CA  . LYS A 252 ? 0.5879 0.6465 0.5694 0.0667  0.1208  0.1134  55   LYS A CA  
1916 C C   . LYS A 252 ? 0.5961 0.6805 0.5557 0.0774  0.1301  0.1225  55   LYS A C   
1917 O O   . LYS A 252 ? 0.6119 0.7106 0.5793 0.0784  0.1405  0.1448  55   LYS A O   
1918 C CB  . LYS A 252 ? 0.5895 0.6378 0.6003 0.0570  0.1229  0.1302  55   LYS A CB  
1919 C CG  . LYS A 252 ? 0.5936 0.6215 0.6282 0.0478  0.1137  0.1205  55   LYS A CG  
1920 C CD  . LYS A 252 ? 0.5914 0.6098 0.6581 0.0389  0.1147  0.1348  55   LYS A CD  
1921 C CE  . LYS A 252 ? 0.5999 0.6412 0.6940 0.0392  0.1293  0.1567  55   LYS A CE  
1922 N NZ  . LYS A 252 ? 0.6028 0.6322 0.7362 0.0295  0.1285  0.1685  55   LYS A NZ  
1923 N N   . GLY A 253 ? 0.5517 0.6420 0.4846 0.0860  0.1254  0.1052  56   GLY A N   
1924 C CA  . GLY A 253 ? 0.5403 0.6581 0.4500 0.0983  0.1320  0.1085  56   GLY A CA  
1925 C C   . GLY A 253 ? 0.5892 0.7011 0.4816 0.0994  0.1288  0.1139  56   GLY A C   
1926 O O   . GLY A 253 ? 0.6414 0.7764 0.5113 0.1109  0.1319  0.1136  56   GLY A O   
1927 N N   . GLN A 254 ? 0.6092 0.6932 0.5112 0.0889  0.1224  0.1180  57   GLN A N   
1928 C CA  . GLN A 254 ? 0.6404 0.7191 0.5292 0.0897  0.1197  0.1244  57   GLN A CA  
1929 C C   . GLN A 254 ? 0.6002 0.6537 0.4777 0.0856  0.1059  0.1045  57   GLN A C   
1930 O O   . GLN A 254 ? 0.5730 0.6075 0.4578 0.0791  0.0985  0.0902  57   GLN A O   
1931 C CB  . GLN A 254 ? 0.6924 0.7621 0.6039 0.0821  0.1244  0.1475  57   GLN A CB  
1932 C CG  . GLN A 254 ? 0.7414 0.8341 0.6727 0.0839  0.1390  0.1703  57   GLN A CG  
1933 C CD  . GLN A 254 ? 0.7753 0.8515 0.7422 0.0726  0.1408  0.1866  57   GLN A CD  
1934 O OE1 . GLN A 254 ? 0.7755 0.8351 0.7638 0.0638  0.1359  0.1778  57   GLN A OE1 
1935 N NE2 . GLN A 254 ? 0.8173 0.8982 0.7924 0.0732  0.1471  0.2101  57   GLN A NE2 
1936 N N   . PRO A 255 ? 0.6126 0.6668 0.4726 0.0896  0.1023  0.1036  58   PRO A N   
1937 C CA  . PRO A 255 ? 0.6206 0.6543 0.4706 0.0862  0.0902  0.0848  58   PRO A CA  
1938 C C   . PRO A 255 ? 0.6392 0.6440 0.5048 0.0741  0.0847  0.0863  58   PRO A C   
1939 O O   . PRO A 255 ? 0.6252 0.6251 0.5066 0.0694  0.0886  0.1026  58   PRO A O   
1940 C CB  . PRO A 255 ? 0.6157 0.6619 0.4464 0.0942  0.0892  0.0869  58   PRO A CB  
1941 C CG  . PRO A 255 ? 0.6149 0.6774 0.4513 0.0975  0.1001  0.1136  58   PRO A CG  
1942 C CD  . PRO A 255 ? 0.6168 0.6929 0.4663 0.0980  0.1095  0.1212  58   PRO A CD  
1943 N N   . SER A 256 ? 0.6214 0.6077 0.4841 0.0694  0.0754  0.0693  59   SER A N   
1944 C CA  . SER A 256 ? 0.6107 0.5733 0.4816 0.0603  0.0693  0.0683  59   SER A CA  
1945 C C   . SER A 256 ? 0.6071 0.5693 0.4695 0.0620  0.0679  0.0732  59   SER A C   
1946 O O   . SER A 256 ? 0.6028 0.5770 0.4483 0.0692  0.0669  0.0684  59   SER A O   
1947 C CB  . SER A 256 ? 0.6146 0.5611 0.4825 0.0561  0.0607  0.0512  59   SER A CB  
1948 O OG  . SER A 256 ? 0.6121 0.5507 0.4941 0.0514  0.0599  0.0497  59   SER A OG  
1949 N N   . LYS A 257 ? 0.6034 0.5530 0.4787 0.0562  0.0672  0.0819  60   LYS A N   
1950 C CA  . LYS A 257 ? 0.6477 0.5976 0.5191 0.0582  0.0667  0.0894  60   LYS A CA  
1951 C C   . LYS A 257 ? 0.6374 0.5670 0.5121 0.0516  0.0588  0.0799  60   LYS A C   
1952 O O   . LYS A 257 ? 0.6760 0.5935 0.5680 0.0461  0.0578  0.0843  60   LYS A O   
1953 C CB  . LYS A 257 ? 0.6915 0.6486 0.5788 0.0592  0.0742  0.1110  60   LYS A CB  
1954 C CG  . LYS A 257 ? 0.7455 0.7287 0.6233 0.0686  0.0829  0.1231  60   LYS A CG  
1955 C CD  . LYS A 257 ? 0.7996 0.7899 0.7006 0.0672  0.0926  0.1457  60   LYS A CD  
1956 C CE  . LYS A 257 ? 0.8384 0.8132 0.7616 0.0616  0.0911  0.1577  60   LYS A CE  
1957 N NZ  . LYS A 257 ? 0.8863 0.8667 0.7982 0.0680  0.0904  0.1665  60   LYS A NZ  
1958 N N   . PRO A 258 ? 0.5911 0.5173 0.4512 0.0522  0.0531  0.0659  61   PRO A N   
1959 C CA  . PRO A 258 ? 0.5770 0.4871 0.4395 0.0466  0.0469  0.0581  61   PRO A CA  
1960 C C   . PRO A 258 ? 0.6278 0.5376 0.4936 0.0481  0.0466  0.0658  61   PRO A C   
1961 O O   . PRO A 258 ? 0.6580 0.5809 0.5164 0.0548  0.0490  0.0732  61   PRO A O   
1962 C CB  . PRO A 258 ? 0.5639 0.4742 0.4124 0.0475  0.0424  0.0437  61   PRO A CB  
1963 C CG  . PRO A 258 ? 0.5381 0.4674 0.3752 0.0561  0.0450  0.0443  61   PRO A CG  
1964 C CD  . PRO A 258 ? 0.5377 0.4759 0.3811 0.0583  0.0519  0.0559  61   PRO A CD  
1965 N N   . PHE A 259 ? 0.6143 0.5105 0.4919 0.0430  0.0434  0.0640  62   PHE A N   
1966 C CA  . PHE A 259 ? 0.6090 0.5028 0.4905 0.0444  0.0414  0.0672  62   PHE A CA  
1967 C C   . PHE A 259 ? 0.6149 0.5122 0.4805 0.0465  0.0376  0.0569  62   PHE A C   
1968 O O   . PHE A 259 ? 0.5992 0.4898 0.4605 0.0425  0.0343  0.0447  62   PHE A O   
1969 C CB  . PHE A 259 ? 0.6259 0.5057 0.5246 0.0390  0.0379  0.0634  62   PHE A CB  
1970 C CG  . PHE A 259 ? 0.6942 0.5712 0.6164 0.0386  0.0403  0.0764  62   PHE A CG  
1971 C CD1 . PHE A 259 ? 0.7295 0.5965 0.6710 0.0337  0.0378  0.0722  62   PHE A CD1 
1972 C CD2 . PHE A 259 ? 0.7281 0.6133 0.6546 0.0435  0.0446  0.0928  62   PHE A CD2 
1973 C CE1 . PHE A 259 ? 0.7685 0.6321 0.7372 0.0326  0.0392  0.0829  62   PHE A CE1 
1974 C CE2 . PHE A 259 ? 0.7953 0.6772 0.7483 0.0426  0.0472  0.1071  62   PHE A CE2 
1975 C CZ  . PHE A 259 ? 0.8126 0.6826 0.7888 0.0365  0.0444  0.1014  62   PHE A CZ  
1976 N N   . VAL A 260 ? 0.5971 0.5058 0.4550 0.0531  0.0380  0.0621  63   VAL A N   
1977 C CA  . VAL A 260 ? 0.5951 0.5086 0.4414 0.0554  0.0337  0.0514  63   VAL A CA  
1978 C C   . VAL A 260 ? 0.6043 0.5101 0.4583 0.0535  0.0302  0.0489  63   VAL A C   
1979 O O   . VAL A 260 ? 0.6147 0.5180 0.4801 0.0552  0.0308  0.0591  63   VAL A O   
1980 C CB  . VAL A 260 ? 0.6145 0.5467 0.4484 0.0647  0.0342  0.0556  63   VAL A CB  
1981 C CG1 . VAL A 260 ? 0.5923 0.5299 0.4178 0.0669  0.0284  0.0423  63   VAL A CG1 
1982 C CG2 . VAL A 260 ? 0.5929 0.5355 0.4197 0.0679  0.0384  0.0578  63   VAL A CG2 
1983 N N   . GLY A 261 ? 0.5896 0.4919 0.4403 0.0501  0.0267  0.0360  64   GLY A N   
1984 C CA  . GLY A 261 ? 0.5779 0.4757 0.4353 0.0487  0.0239  0.0316  64   GLY A CA  
1985 C C   . GLY A 261 ? 0.5908 0.4982 0.4415 0.0518  0.0205  0.0244  64   GLY A C   
1986 O O   . GLY A 261 ? 0.6079 0.5213 0.4506 0.0522  0.0194  0.0175  64   GLY A O   
1987 N N   . VAL A 262 ? 0.5566 0.4659 0.4133 0.0547  0.0182  0.0252  65   VAL A N   
1988 C CA  . VAL A 262 ? 0.5393 0.4577 0.3936 0.0573  0.0142  0.0171  65   VAL A CA  
1989 C C   . VAL A 262 ? 0.5409 0.4535 0.4035 0.0518  0.0138  0.0084  65   VAL A C   
1990 O O   . VAL A 262 ? 0.4927 0.4006 0.3647 0.0521  0.0137  0.0102  65   VAL A O   
1991 C CB  . VAL A 262 ? 0.5555 0.4836 0.4103 0.0660  0.0116  0.0248  65   VAL A CB  
1992 C CG1 . VAL A 262 ? 0.5513 0.4898 0.4055 0.0687  0.0065  0.0145  65   VAL A CG1 
1993 C CG2 . VAL A 262 ? 0.5476 0.4853 0.3925 0.0728  0.0133  0.0360  65   VAL A CG2 
1994 N N   . LEU A 263 ? 0.5333 0.4466 0.3942 0.0468  0.0139  -0.0009 66   LEU A N   
1995 C CA  . LEU A 263 ? 0.5100 0.4229 0.3785 0.0426  0.0144  -0.0079 66   LEU A CA  
1996 C C   . LEU A 263 ? 0.5072 0.4283 0.3825 0.0476  0.0111  -0.0099 66   LEU A C   
1997 O O   . LEU A 263 ? 0.5575 0.4883 0.4311 0.0523  0.0072  -0.0115 66   LEU A O   
1998 C CB  . LEU A 263 ? 0.4710 0.3860 0.3398 0.0373  0.0149  -0.0149 66   LEU A CB  
1999 C CG  . LEU A 263 ? 0.4890 0.4063 0.3662 0.0324  0.0172  -0.0200 66   LEU A CG  
2000 C CD1 . LEU A 263 ? 0.4909 0.4016 0.3663 0.0295  0.0212  -0.0174 66   LEU A CD1 
2001 C CD2 . LEU A 263 ? 0.4940 0.4135 0.3761 0.0273  0.0173  -0.0245 66   LEU A CD2 
2002 N N   . SER A 264 ? 0.5231 0.4419 0.4066 0.0474  0.0120  -0.0113 67   SER A N   
2003 C CA  . SER A 264 ? 0.5509 0.4767 0.4427 0.0529  0.0086  -0.0127 67   SER A CA  
2004 C C   . SER A 264 ? 0.5517 0.4799 0.4532 0.0507  0.0103  -0.0204 67   SER A C   
2005 O O   . SER A 264 ? 0.5621 0.4854 0.4629 0.0464  0.0141  -0.0228 67   SER A O   
2006 C CB  . SER A 264 ? 0.5724 0.4940 0.4677 0.0594  0.0065  -0.0028 67   SER A CB  
2007 O OG  . SER A 264 ? 0.5735 0.4927 0.4598 0.0608  0.0074  0.0067  67   SER A OG  
2008 N N   . ALA A 265 ? 0.4855 0.4235 0.3956 0.0543  0.0075  -0.0252 68   ALA A N   
2009 C CA  . ALA A 265 ? 0.4700 0.4147 0.3900 0.0528  0.0098  -0.0335 68   ALA A CA  
2010 C C   . ALA A 265 ? 0.5188 0.4644 0.4503 0.0599  0.0063  -0.0345 68   ALA A C   
2011 O O   . ALA A 265 ? 0.5371 0.4875 0.4730 0.0660  0.0012  -0.0321 68   ALA A O   
2012 C CB  . ALA A 265 ? 0.4401 0.3973 0.3653 0.0501  0.0097  -0.0396 68   ALA A CB  
2013 N N   . GLY A 266 ? 0.5111 0.4527 0.4481 0.0601  0.0084  -0.0384 69   GLY A N   
2014 C CA  . GLY A 266 ? 0.4979 0.4383 0.4495 0.0670  0.0047  -0.0410 69   GLY A CA  
2015 C C   . GLY A 266 ? 0.5130 0.4662 0.4743 0.0682  0.0067  -0.0531 69   GLY A C   
2016 O O   . GLY A 266 ? 0.5633 0.5242 0.5193 0.0631  0.0126  -0.0584 69   GLY A O   
2017 N N   . ILE A 267 ? 0.5123 0.4696 0.4885 0.0753  0.0022  -0.0563 70   ILE A N   
2018 C CA  . ILE A 267 ? 0.5243 0.4958 0.5124 0.0779  0.0038  -0.0685 70   ILE A CA  
2019 C C   . ILE A 267 ? 0.5391 0.5064 0.5389 0.0830  0.0024  -0.0768 70   ILE A C   
2020 O O   . ILE A 267 ? 0.5815 0.5370 0.5924 0.0882  -0.0037 -0.0728 70   ILE A O   
2021 C CB  . ILE A 267 ? 0.5198 0.5009 0.5192 0.0833  -0.0011 -0.0689 70   ILE A CB  
2022 C CG1 . ILE A 267 ? 0.5214 0.5102 0.5121 0.0782  -0.0002 -0.0654 70   ILE A CG1 
2023 C CG2 . ILE A 267 ? 0.4874 0.4831 0.5031 0.0876  0.0001  -0.0821 70   ILE A CG2 
2024 C CD1 . ILE A 267 ? 0.5374 0.5343 0.5361 0.0844  -0.0074 -0.0644 70   ILE A CD1 
2025 N N   . ASN A 268 ? 0.5344 0.5124 0.5330 0.0819  0.0077  -0.0880 71   ASN A N   
2026 C CA  . ASN A 268 ? 0.5536 0.5309 0.5623 0.0874  0.0060  -0.1000 71   ASN A CA  
2027 C C   . ASN A 268 ? 0.5515 0.5302 0.5841 0.0968  -0.0006 -0.1071 71   ASN A C   
2028 O O   . ASN A 268 ? 0.5700 0.5625 0.6099 0.0996  0.0001  -0.1110 71   ASN A O   
2029 C CB  . ASN A 268 ? 0.5599 0.5557 0.5603 0.0862  0.0137  -0.1109 71   ASN A CB  
2030 C CG  . ASN A 268 ? 0.5947 0.5913 0.6002 0.0918  0.0117  -0.1249 71   ASN A CG  
2031 O OD1 . ASN A 268 ? 0.6319 0.6229 0.6571 0.0992  0.0046  -0.1336 71   ASN A OD1 
2032 N ND2 . ASN A 268 ? 0.5944 0.5992 0.5838 0.0891  0.0172  -0.1278 71   ASN A ND2 
2033 N N   . ALA A 269 ? 0.5351 0.4993 0.5826 0.1016  -0.0072 -0.1086 72   ALA A N   
2034 C CA  . ALA A 269 ? 0.5419 0.5048 0.6155 0.1109  -0.0143 -0.1142 72   ALA A CA  
2035 C C   . ALA A 269 ? 0.5554 0.5383 0.6392 0.1170  -0.0125 -0.1342 72   ALA A C   
2036 O O   . ALA A 269 ? 0.5359 0.5240 0.6390 0.1243  -0.0168 -0.1391 72   ALA A O   
2037 C CB  . ALA A 269 ? 0.5024 0.4453 0.5953 0.1145  -0.0216 -0.1127 72   ALA A CB  
2038 N N   . ALA A 270 ? 0.5873 0.5840 0.6579 0.1147  -0.0057 -0.1452 73   ALA A N   
2039 C CA  . ALA A 270 ? 0.6093 0.6291 0.6875 0.1213  -0.0026 -0.1642 73   ALA A CA  
2040 C C   . ALA A 270 ? 0.5784 0.6204 0.6442 0.1170  0.0071  -0.1615 73   ALA A C   
2041 O O   . ALA A 270 ? 0.5607 0.6260 0.6293 0.1215  0.0125  -0.1752 73   ALA A O   
2042 C CB  . ALA A 270 ? 0.6001 0.6262 0.6738 0.1243  -0.0015 -0.1799 73   ALA A CB  
2043 N N   . SER A 271 ? 0.5581 0.5952 0.6126 0.1089  0.0095  -0.1452 74   SER A N   
2044 C CA  . SER A 271 ? 0.5606 0.6176 0.6079 0.1037  0.0184  -0.1426 74   SER A CA  
2045 C C   . SER A 271 ? 0.5753 0.6456 0.6423 0.1090  0.0163  -0.1478 74   SER A C   
2046 O O   . SER A 271 ? 0.6074 0.6659 0.6857 0.1125  0.0076  -0.1429 74   SER A O   
2047 C CB  . SER A 271 ? 0.5674 0.6151 0.5986 0.0933  0.0207  -0.1259 74   SER A CB  
2048 O OG  . SER A 271 ? 0.5540 0.6168 0.5897 0.0894  0.0250  -0.1229 74   SER A OG  
2049 N N   . PRO A 272 ? 0.5808 0.6771 0.6537 0.1104  0.0240  -0.1568 75   PRO A N   
2050 C CA  . PRO A 272 ? 0.5875 0.6986 0.6805 0.1147  0.0225  -0.1615 75   PRO A CA  
2051 C C   . PRO A 272 ? 0.5755 0.6888 0.6680 0.1068  0.0234  -0.1498 75   PRO A C   
2052 O O   . PRO A 272 ? 0.5570 0.6827 0.6674 0.1102  0.0209  -0.1536 75   PRO A O   
2053 C CB  . PRO A 272 ? 0.5922 0.7332 0.6901 0.1184  0.0326  -0.1750 75   PRO A CB  
2054 C CG  . PRO A 272 ? 0.5933 0.7379 0.6678 0.1105  0.0426  -0.1683 75   PRO A CG  
2055 C CD  . PRO A 272 ? 0.5922 0.7077 0.6529 0.1086  0.0352  -0.1621 75   PRO A CD  
2056 N N   . ASN A 273 ? 0.5723 0.6745 0.6469 0.0970  0.0260  -0.1370 76   ASN A N   
2057 C CA  . ASN A 273 ? 0.5601 0.6654 0.6357 0.0893  0.0266  -0.1283 76   ASN A CA  
2058 C C   . ASN A 273 ? 0.5489 0.6322 0.6160 0.0882  0.0169  -0.1181 76   ASN A C   
2059 O O   . ASN A 273 ? 0.5460 0.6247 0.6034 0.0802  0.0183  -0.1099 76   ASN A O   
2060 C CB  . ASN A 273 ? 0.5624 0.6766 0.6278 0.0789  0.0383  -0.1222 76   ASN A CB  
2061 C CG  . ASN A 273 ? 0.5524 0.6891 0.6197 0.0808  0.0495  -0.1295 76   ASN A CG  
2062 O OD1 . ASN A 273 ? 0.5886 0.7480 0.6737 0.0837  0.0538  -0.1366 76   ASN A OD1 
2063 N ND2 . ASN A 273 ? 0.5022 0.6351 0.5512 0.0800  0.0545  -0.1279 76   ASN A ND2 
2064 N N   . LYS A 274 ? 0.5368 0.6079 0.6090 0.0969  0.0071  -0.1182 77   LYS A N   
2065 C CA  . LYS A 274 ? 0.5234 0.5758 0.5855 0.0970  -0.0009 -0.1066 77   LYS A CA  
2066 C C   . LYS A 274 ? 0.5366 0.5969 0.6022 0.0961  -0.0058 -0.1034 77   LYS A C   
2067 O O   . LYS A 274 ? 0.5256 0.5769 0.5776 0.0925  -0.0085 -0.0947 77   LYS A O   
2068 C CB  . LYS A 274 ? 0.4967 0.5355 0.5666 0.1068  -0.0093 -0.1050 77   LYS A CB  
2069 C CG  . LYS A 274 ? 0.4826 0.5111 0.5520 0.1083  -0.0070 -0.1095 77   LYS A CG  
2070 C CD  . LYS A 274 ? 0.4939 0.5059 0.5762 0.1171  -0.0165 -0.1052 77   LYS A CD  
2071 C CE  . LYS A 274 ? 0.5179 0.5188 0.6038 0.1182  -0.0158 -0.1112 77   LYS A CE  
2072 N NZ  . LYS A 274 ? 0.5340 0.5511 0.6307 0.1221  -0.0120 -0.1306 77   LYS A NZ  
2073 N N   . GLU A 275 ? 0.5480 0.6266 0.6328 0.1000  -0.0076 -0.1117 78   GLU A N   
2074 C CA  . GLU A 275 ? 0.5479 0.6367 0.6386 0.0992  -0.0131 -0.1114 78   GLU A CA  
2075 C C   . GLU A 275 ? 0.5515 0.6457 0.6378 0.0873  -0.0061 -0.1107 78   GLU A C   
2076 O O   . GLU A 275 ? 0.5819 0.6744 0.6634 0.0848  -0.0113 -0.1076 78   GLU A O   
2077 C CB  . GLU A 275 ? 0.5882 0.6966 0.7033 0.1058  -0.0166 -0.1214 78   GLU A CB  
2078 C CG  . GLU A 275 ? 0.6818 0.7853 0.8046 0.1188  -0.0273 -0.1204 78   GLU A CG  
2079 C CD  . GLU A 275 ? 0.7590 0.8549 0.8712 0.1236  -0.0382 -0.1102 78   GLU A CD  
2080 O OE1 . GLU A 275 ? 0.7637 0.8716 0.8776 0.1220  -0.0425 -0.1125 78   GLU A OE1 
2081 O OE2 . GLU A 275 ? 0.8077 0.8872 0.9115 0.1297  -0.0427 -0.1000 78   GLU A OE2 
2082 N N   . LEU A 276 ? 0.5220 0.6240 0.6111 0.0805  0.0055  -0.1135 79   LEU A N   
2083 C CA  . LEU A 276 ? 0.5340 0.6392 0.6209 0.0689  0.0130  -0.1099 79   LEU A CA  
2084 C C   . LEU A 276 ? 0.5272 0.6116 0.5914 0.0647  0.0114  -0.1006 79   LEU A C   
2085 O O   . LEU A 276 ? 0.5178 0.6002 0.5813 0.0592  0.0091  -0.0983 79   LEU A O   
2086 C CB  . LEU A 276 ? 0.5331 0.6509 0.6240 0.0641  0.0267  -0.1112 79   LEU A CB  
2087 C CG  . LEU A 276 ? 0.5621 0.7056 0.6786 0.0607  0.0332  -0.1165 79   LEU A CG  
2088 C CD1 . LEU A 276 ? 0.5778 0.7337 0.7137 0.0698  0.0255  -0.1265 79   LEU A CD1 
2089 C CD2 . LEU A 276 ? 0.5719 0.7297 0.6876 0.0583  0.0477  -0.1159 79   LEU A CD2 
2090 N N   . ALA A 277 ? 0.5318 0.6013 0.5796 0.0677  0.0123  -0.0965 80   ALA A N   
2091 C CA  . ALA A 277 ? 0.5283 0.5793 0.5558 0.0639  0.0117  -0.0877 80   ALA A CA  
2092 C C   . ALA A 277 ? 0.5262 0.5700 0.5483 0.0676  0.0014  -0.0839 80   ALA A C   
2093 O O   . ALA A 277 ? 0.5138 0.5514 0.5263 0.0625  0.0007  -0.0799 80   ALA A O   
2094 C CB  . ALA A 277 ? 0.5028 0.5409 0.5185 0.0672  0.0135  -0.0855 80   ALA A CB  
2095 N N   . LYS A 278 ? 0.5211 0.5669 0.5492 0.0773  -0.0068 -0.0851 81   LYS A N   
2096 C CA  . LYS A 278 ? 0.4894 0.5340 0.5118 0.0827  -0.0166 -0.0812 81   LYS A CA  
2097 C C   . LYS A 278 ? 0.4877 0.5457 0.5184 0.0783  -0.0193 -0.0880 81   LYS A C   
2098 O O   . LYS A 278 ? 0.4864 0.5418 0.5068 0.0781  -0.0240 -0.0860 81   LYS A O   
2099 C CB  . LYS A 278 ? 0.4721 0.5203 0.5034 0.0945  -0.0246 -0.0809 81   LYS A CB  
2100 C CG  . LYS A 278 ? 0.5196 0.5719 0.5449 0.1026  -0.0353 -0.0762 81   LYS A CG  
2101 C CD  . LYS A 278 ? 0.5789 0.6329 0.6134 0.1151  -0.0428 -0.0723 81   LYS A CD  
2102 C CE  . LYS A 278 ? 0.6008 0.6601 0.6256 0.1249  -0.0531 -0.0643 81   LYS A CE  
2103 N NZ  . LYS A 278 ? 0.6203 0.6994 0.6515 0.1261  -0.0596 -0.0753 81   LYS A NZ  
2104 N N   . GLU A 279 ? 0.4872 0.5609 0.5387 0.0753  -0.0165 -0.0968 82   GLU A N   
2105 C CA  . GLU A 279 ? 0.5250 0.6116 0.5909 0.0708  -0.0197 -0.1043 82   GLU A CA  
2106 C C   . GLU A 279 ? 0.5105 0.5889 0.5703 0.0600  -0.0140 -0.1014 82   GLU A C   
2107 O O   . GLU A 279 ? 0.4910 0.5707 0.5517 0.0588  -0.0204 -0.1050 82   GLU A O   
2108 C CB  . GLU A 279 ? 0.5613 0.6670 0.6543 0.0691  -0.0162 -0.1129 82   GLU A CB  
2109 C CG  . GLU A 279 ? 0.5951 0.7149 0.7107 0.0620  -0.0177 -0.1208 82   GLU A CG  
2110 C CD  . GLU A 279 ? 0.6448 0.7724 0.7647 0.0694  -0.0327 -0.1285 82   GLU A CD  
2111 O OE1 . GLU A 279 ? 0.6687 0.7926 0.7729 0.0807  -0.0410 -0.1256 82   GLU A OE1 
2112 O OE2 . GLU A 279 ? 0.6586 0.7972 0.7988 0.0643  -0.0364 -0.1374 82   GLU A OE2 
2113 N N   . PHE A 280 ? 0.5254 0.5959 0.5789 0.0533  -0.0028 -0.0954 83   PHE A N   
2114 C CA  . PHE A 280 ? 0.5147 0.5767 0.5631 0.0435  0.0028  -0.0909 83   PHE A CA  
2115 C C   . PHE A 280 ? 0.5138 0.5606 0.5406 0.0461  -0.0029 -0.0864 83   PHE A C   
2116 O O   . PHE A 280 ? 0.5084 0.5532 0.5368 0.0422  -0.0061 -0.0886 83   PHE A O   
2117 C CB  . PHE A 280 ? 0.5064 0.5654 0.5498 0.0379  0.0155  -0.0844 83   PHE A CB  
2118 C CG  . PHE A 280 ? 0.4905 0.5383 0.5248 0.0295  0.0212  -0.0770 83   PHE A CG  
2119 C CD1 . PHE A 280 ? 0.4726 0.5267 0.5251 0.0200  0.0262  -0.0759 83   PHE A CD1 
2120 C CD2 . PHE A 280 ? 0.4885 0.5197 0.4993 0.0308  0.0217  -0.0705 83   PHE A CD2 
2121 C CE1 . PHE A 280 ? 0.4973 0.5410 0.5439 0.0128  0.0311  -0.0681 83   PHE A CE1 
2122 C CE2 . PHE A 280 ? 0.4982 0.5193 0.5011 0.0237  0.0263  -0.0637 83   PHE A CE2 
2123 C CZ  . PHE A 280 ? 0.5356 0.5628 0.5562 0.0148  0.0310  -0.0622 83   PHE A CZ  
2124 N N   . LEU A 281 ? 0.5011 0.5375 0.5096 0.0530  -0.0044 -0.0803 84   LEU A N   
2125 C CA  . LEU A 281 ? 0.5137 0.5369 0.5020 0.0549  -0.0077 -0.0741 84   LEU A CA  
2126 C C   . LEU A 281 ? 0.5269 0.5575 0.5139 0.0616  -0.0185 -0.0784 84   LEU A C   
2127 O O   . LEU A 281 ? 0.5545 0.5812 0.5326 0.0603  -0.0208 -0.0785 84   LEU A O   
2128 C CB  . LEU A 281 ? 0.5135 0.5249 0.4878 0.0602  -0.0065 -0.0657 84   LEU A CB  
2129 C CG  . LEU A 281 ? 0.5404 0.5448 0.5126 0.0547  0.0029  -0.0633 84   LEU A CG  
2130 C CD1 . LEU A 281 ? 0.4101 0.4037 0.3751 0.0609  0.0022  -0.0580 84   LEU A CD1 
2131 C CD2 . LEU A 281 ? 0.5134 0.5100 0.4773 0.0458  0.0085  -0.0598 84   LEU A CD2 
2132 N N   . GLU A 282 ? 0.5286 0.5719 0.5247 0.0697  -0.0257 -0.0830 85   GLU A N   
2133 C CA  . GLU A 282 ? 0.5517 0.6051 0.5436 0.0786  -0.0370 -0.0869 85   GLU A CA  
2134 C C   . GLU A 282 ? 0.5752 0.6418 0.5841 0.0750  -0.0423 -0.1009 85   GLU A C   
2135 O O   . GLU A 282 ? 0.5511 0.6223 0.5527 0.0791  -0.0498 -0.1059 85   GLU A O   
2136 C CB  . GLU A 282 ? 0.5677 0.6301 0.5628 0.0901  -0.0436 -0.0853 85   GLU A CB  
2137 C CG  . GLU A 282 ? 0.5578 0.6088 0.5364 0.0974  -0.0430 -0.0708 85   GLU A CG  
2138 C CD  . GLU A 282 ? 0.6240 0.6847 0.6080 0.1099  -0.0511 -0.0680 85   GLU A CD  
2139 O OE1 . GLU A 282 ? 0.6527 0.7311 0.6460 0.1154  -0.0598 -0.0773 85   GLU A OE1 
2140 O OE2 . GLU A 282 ? 0.6291 0.6795 0.6103 0.1146  -0.0494 -0.0565 85   GLU A OE2 
2141 N N   . ASN A 283 ? 0.5904 0.6648 0.6240 0.0680  -0.0389 -0.1080 86   ASN A N   
2142 C CA  . ASN A 283 ? 0.5969 0.6860 0.6545 0.0652  -0.0454 -0.1223 86   ASN A CA  
2143 C C   . ASN A 283 ? 0.5833 0.6668 0.6564 0.0516  -0.0382 -0.1241 86   ASN A C   
2144 O O   . ASN A 283 ? 0.5722 0.6659 0.6699 0.0479  -0.0435 -0.1358 86   ASN A O   
2145 C CB  . ASN A 283 ? 0.6079 0.7139 0.6890 0.0678  -0.0482 -0.1295 86   ASN A CB  
2146 C CG  . ASN A 283 ? 0.6587 0.7734 0.7298 0.0825  -0.0586 -0.1296 86   ASN A CG  
2147 O OD1 . ASN A 283 ? 0.6929 0.8110 0.7488 0.0912  -0.0682 -0.1312 86   ASN A OD1 
2148 N ND2 . ASN A 283 ? 0.6400 0.7597 0.7197 0.0863  -0.0565 -0.1275 86   ASN A ND2 
2149 N N   . TYR A 284 ? 0.5980 0.6662 0.6602 0.0443  -0.0267 -0.1126 87   TYR A N   
2150 C CA  . TYR A 284 ? 0.5673 0.6292 0.6425 0.0323  -0.0197 -0.1111 87   TYR A CA  
2151 C C   . TYR A 284 ? 0.5962 0.6406 0.6487 0.0308  -0.0175 -0.1039 87   TYR A C   
2152 O O   . TYR A 284 ? 0.6403 0.6814 0.7004 0.0272  -0.0212 -0.1092 87   TYR A O   
2153 C CB  . TYR A 284 ? 0.5340 0.5983 0.6215 0.0243  -0.0066 -0.1036 87   TYR A CB  
2154 C CG  . TYR A 284 ? 0.5280 0.6117 0.6454 0.0234  -0.0072 -0.1114 87   TYR A CG  
2155 C CD1 . TYR A 284 ? 0.5543 0.6484 0.6700 0.0328  -0.0120 -0.1158 87   TYR A CD1 
2156 C CD2 . TYR A 284 ? 0.4935 0.5855 0.6434 0.0132  -0.0031 -0.1137 87   TYR A CD2 
2157 C CE1 . TYR A 284 ? 0.5348 0.6479 0.6788 0.0325  -0.0128 -0.1236 87   TYR A CE1 
2158 C CE2 . TYR A 284 ? 0.4905 0.6016 0.6704 0.0121  -0.0033 -0.1207 87   TYR A CE2 
2159 C CZ  . TYR A 284 ? 0.4941 0.6163 0.6703 0.0219  -0.0083 -0.1263 87   TYR A CZ  
2160 O OH  . TYR A 284 ? 0.4619 0.6042 0.6686 0.0214  -0.0087 -0.1338 87   TYR A OH  
2161 N N   . LEU A 285 ? 0.5646 0.5978 0.5919 0.0337  -0.0121 -0.0929 88   LEU A N   
2162 C CA  . LEU A 285 ? 0.5437 0.5609 0.5515 0.0316  -0.0090 -0.0854 88   LEU A CA  
2163 C C   . LEU A 285 ? 0.5331 0.5502 0.5269 0.0397  -0.0188 -0.0900 88   LEU A C   
2164 O O   . LEU A 285 ? 0.4940 0.5069 0.4887 0.0372  -0.0212 -0.0940 88   LEU A O   
2165 C CB  . LEU A 285 ? 0.5039 0.5108 0.4924 0.0326  -0.0013 -0.0739 88   LEU A CB  
2166 C CG  . LEU A 285 ? 0.4900 0.4814 0.4588 0.0313  0.0011  -0.0664 88   LEU A CG  
2167 C CD1 . LEU A 285 ? 0.4632 0.4498 0.4427 0.0222  0.0038  -0.0671 88   LEU A CD1 
2168 C CD2 . LEU A 285 ? 0.4770 0.4591 0.4318 0.0312  0.0081  -0.0572 88   LEU A CD2 
2169 N N   . LEU A 286 ? 0.5256 0.5483 0.5065 0.0503  -0.0242 -0.0889 89   LEU A N   
2170 C CA  . LEU A 286 ? 0.5156 0.5406 0.4782 0.0598  -0.0317 -0.0896 89   LEU A CA  
2171 C C   . LEU A 286 ? 0.5497 0.5918 0.5246 0.0648  -0.0432 -0.1054 89   LEU A C   
2172 O O   . LEU A 286 ? 0.5331 0.5886 0.5012 0.0760  -0.0518 -0.1089 89   LEU A O   
2173 C CB  . LEU A 286 ? 0.5024 0.5276 0.4489 0.0692  -0.0324 -0.0794 89   LEU A CB  
2174 C CG  . LEU A 286 ? 0.5020 0.5101 0.4330 0.0665  -0.0240 -0.0657 89   LEU A CG  
2175 C CD1 . LEU A 286 ? 0.4896 0.4960 0.4126 0.0744  -0.0242 -0.0552 89   LEU A CD1 
2176 C CD2 . LEU A 286 ? 0.5301 0.5332 0.4463 0.0668  -0.0242 -0.0640 89   LEU A CD2 
2177 N N   . THR A 287 ? 0.5705 0.6120 0.5659 0.0562  -0.0436 -0.1152 90   THR A N   
2178 C CA  . THR A 287 ? 0.5535 0.6096 0.5669 0.0591  -0.0550 -0.1335 90   THR A CA  
2179 C C   . THR A 287 ? 0.5559 0.6032 0.5753 0.0534  -0.0551 -0.1393 90   THR A C   
2180 O O   . THR A 287 ? 0.5435 0.5741 0.5576 0.0454  -0.0455 -0.1282 90   THR A O   
2181 C CB  . THR A 287 ? 0.5352 0.6016 0.5819 0.0534  -0.0565 -0.1421 90   THR A CB  
2182 O OG1 . THR A 287 ? 0.4956 0.5518 0.5639 0.0397  -0.0483 -0.1397 90   THR A OG1 
2183 C CG2 . THR A 287 ? 0.5700 0.6393 0.6132 0.0554  -0.0515 -0.1327 90   THR A CG2 
2184 N N   . ASP A 288 ? 0.5498 0.6096 0.5809 0.0585  -0.0671 -0.1578 91   ASP A N   
2185 C CA  . ASP A 288 ? 0.5599 0.6126 0.6010 0.0544  -0.0693 -0.1665 91   ASP A CA  
2186 C C   . ASP A 288 ? 0.5335 0.5709 0.6008 0.0387  -0.0601 -0.1601 91   ASP A C   
2187 O O   . ASP A 288 ? 0.5289 0.5504 0.5904 0.0332  -0.0536 -0.1519 91   ASP A O   
2188 C CB  . ASP A 288 ? 0.6061 0.6773 0.6654 0.0618  -0.0851 -0.1917 91   ASP A CB  
2189 C CG  . ASP A 288 ? 0.6448 0.7313 0.6729 0.0787  -0.0938 -0.1981 91   ASP A CG  
2190 O OD1 . ASP A 288 ? 0.6631 0.7426 0.6590 0.0828  -0.0868 -0.1829 91   ASP A OD1 
2191 O OD2 . ASP A 288 ? 0.6632 0.7707 0.6995 0.0885  -0.1076 -0.2179 91   ASP A OD2 
2192 N N   . GLU A 289 ? 0.5478 0.5912 0.6450 0.0318  -0.0592 -0.1626 92   GLU A N   
2193 C CA  . GLU A 289 ? 0.5895 0.6214 0.7139 0.0171  -0.0496 -0.1542 92   GLU A CA  
2194 C C   . GLU A 289 ? 0.5746 0.5937 0.6777 0.0121  -0.0346 -0.1318 92   GLU A C   
2195 O O   . GLU A 289 ? 0.5674 0.5732 0.6766 0.0031  -0.0261 -0.1211 92   GLU A O   
2196 C CB  . GLU A 289 ? 0.6437 0.6885 0.8076 0.0113  -0.0516 -0.1619 92   GLU A CB  
2197 C CG  . GLU A 289 ? 0.7151 0.7718 0.8709 0.0152  -0.0489 -0.1574 92   GLU A CG  
2198 C CD  . GLU A 289 ? 0.7684 0.8442 0.9214 0.0281  -0.0638 -0.1746 92   GLU A CD  
2199 O OE1 . GLU A 289 ? 0.8201 0.9008 0.9722 0.0351  -0.0761 -0.1904 92   GLU A OE1 
2200 O OE2 . GLU A 289 ? 0.7129 0.8000 0.8648 0.0320  -0.0634 -0.1728 92   GLU A OE2 
2201 N N   . GLY A 290 ? 0.5440 0.5673 0.6224 0.0186  -0.0319 -0.1247 93   GLY A N   
2202 C CA  . GLY A 290 ? 0.5104 0.5235 0.5714 0.0147  -0.0191 -0.1068 93   GLY A CA  
2203 C C   . GLY A 290 ? 0.5019 0.4988 0.5389 0.0147  -0.0153 -0.0979 93   GLY A C   
2204 O O   . GLY A 290 ? 0.4833 0.4694 0.5202 0.0070  -0.0059 -0.0864 93   GLY A O   
2205 N N   . LEU A 291 ? 0.5161 0.5131 0.5325 0.0239  -0.0225 -0.1028 94   LEU A N   
2206 C CA  . LEU A 291 ? 0.5461 0.5293 0.5406 0.0245  -0.0190 -0.0947 94   LEU A CA  
2207 C C   . LEU A 291 ? 0.5731 0.5477 0.5845 0.0176  -0.0193 -0.0983 94   LEU A C   
2208 O O   . LEU A 291 ? 0.5708 0.5319 0.5742 0.0130  -0.0125 -0.0878 94   LEU A O   
2209 C CB  . LEU A 291 ? 0.5453 0.5340 0.5157 0.0366  -0.0256 -0.0980 94   LEU A CB  
2210 C CG  . LEU A 291 ? 0.5699 0.5655 0.5239 0.0446  -0.0259 -0.0920 94   LEU A CG  
2211 C CD1 . LEU A 291 ? 0.5712 0.5740 0.5032 0.0565  -0.0317 -0.0928 94   LEU A CD1 
2212 C CD2 . LEU A 291 ? 0.5943 0.5783 0.5387 0.0402  -0.0158 -0.0771 94   LEU A CD2 
2213 N N   . GLU A 292 ? 0.5923 0.5746 0.6291 0.0174  -0.0281 -0.1140 95   GLU A N   
2214 C CA  . GLU A 292 ? 0.5976 0.5707 0.6576 0.0103  -0.0290 -0.1178 95   GLU A CA  
2215 C C   . GLU A 292 ? 0.5218 0.4845 0.5955 -0.0016 -0.0173 -0.1015 95   GLU A C   
2216 O O   . GLU A 292 ? 0.4956 0.4447 0.5678 -0.0060 -0.0127 -0.0927 95   GLU A O   
2217 C CB  . GLU A 292 ? 0.6648 0.6491 0.7570 0.0113  -0.0408 -0.1385 95   GLU A CB  
2218 C CG  . GLU A 292 ? 0.7369 0.7111 0.8588 0.0046  -0.0435 -0.1445 95   GLU A CG  
2219 C CD  . GLU A 292 ? 0.8149 0.8012 0.9698 0.0074  -0.0577 -0.1693 95   GLU A CD  
2220 O OE1 . GLU A 292 ? 0.8427 0.8404 1.0213 0.0046  -0.0602 -0.1749 95   GLU A OE1 
2221 O OE2 . GLU A 292 ? 0.8521 0.8378 1.0109 0.0129  -0.0669 -0.1846 95   GLU A OE2 
2222 N N   . ALA A 293 ? 0.5037 0.4745 0.5901 -0.0060 -0.0122 -0.0967 96   ALA A N   
2223 C CA  . ALA A 293 ? 0.4859 0.4516 0.5834 -0.0161 0.0000  -0.0800 96   ALA A CA  
2224 C C   . ALA A 293 ? 0.5231 0.4773 0.5889 -0.0153 0.0085  -0.0645 96   ALA A C   
2225 O O   . ALA A 293 ? 0.5396 0.4843 0.6106 -0.0217 0.0150  -0.0526 96   ALA A O   
2226 C CB  . ALA A 293 ? 0.4393 0.4195 0.5484 -0.0181 0.0047  -0.0780 96   ALA A CB  
2227 N N   . VAL A 294 ? 0.5071 0.4625 0.5418 -0.0074 0.0079  -0.0641 97   VAL A N   
2228 C CA  . VAL A 294 ? 0.4959 0.4407 0.5040 -0.0065 0.0142  -0.0519 97   VAL A CA  
2229 C C   . VAL A 294 ? 0.4935 0.4262 0.4956 -0.0056 0.0105  -0.0530 97   VAL A C   
2230 O O   . VAL A 294 ? 0.5063 0.4288 0.5037 -0.0095 0.0162  -0.0421 97   VAL A O   
2231 C CB  . VAL A 294 ? 0.4459 0.3939 0.4280 0.0014  0.0140  -0.0512 97   VAL A CB  
2232 C CG1 . VAL A 294 ? 0.4166 0.3535 0.3757 0.0021  0.0191  -0.0408 97   VAL A CG1 
2233 C CG2 . VAL A 294 ? 0.4494 0.4094 0.4382 0.0011  0.0181  -0.0503 97   VAL A CG2 
2234 N N   . ASN A 295 ? 0.4987 0.4342 0.5002 0.0006  0.0010  -0.0664 98   ASN A N   
2235 C CA  . ASN A 295 ? 0.5387 0.4655 0.5337 0.0033  -0.0030 -0.0700 98   ASN A CA  
2236 C C   . ASN A 295 ? 0.5488 0.4654 0.5677 -0.0046 -0.0016 -0.0671 98   ASN A C   
2237 O O   . ASN A 295 ? 0.5401 0.4458 0.5510 -0.0047 -0.0003 -0.0619 98   ASN A O   
2238 C CB  . ASN A 295 ? 0.5527 0.4898 0.5472 0.0121  -0.0138 -0.0872 98   ASN A CB  
2239 C CG  . ASN A 295 ? 0.5860 0.5186 0.5644 0.0183  -0.0168 -0.0904 98   ASN A CG  
2240 O OD1 . ASN A 295 ? 0.5988 0.5307 0.5500 0.0235  -0.0135 -0.0826 98   ASN A OD1 
2241 N ND2 . ASN A 295 ? 0.5389 0.4697 0.5361 0.0182  -0.0233 -0.1026 98   ASN A ND2 
2242 N N   . LYS A 296 ? 0.5885 0.5085 0.6390 -0.0112 -0.0020 -0.0696 99   LYS A N   
2243 C CA  . LYS A 296 ? 0.6310 0.5408 0.7101 -0.0193 -0.0006 -0.0647 99   LYS A CA  
2244 C C   . LYS A 296 ? 0.6425 0.5441 0.7125 -0.0249 0.0109  -0.0428 99   LYS A C   
2245 O O   . LYS A 296 ? 0.6437 0.5345 0.7278 -0.0294 0.0125  -0.0351 99   LYS A O   
2246 C CB  . LYS A 296 ? 0.6514 0.5681 0.7713 -0.0256 -0.0032 -0.0713 99   LYS A CB  
2247 C CG  . LYS A 296 ? 0.7044 0.6298 0.8396 -0.0199 -0.0168 -0.0957 99   LYS A CG  
2248 C CD  . LYS A 296 ? 0.7830 0.7066 0.9689 -0.0276 -0.0217 -0.1035 99   LYS A CD  
2249 C CE  . LYS A 296 ? 0.8350 0.7646 1.0463 -0.0374 -0.0130 -0.0909 99   LYS A CE  
2250 N NZ  . LYS A 296 ? 0.8514 0.7971 1.0871 -0.0364 -0.0211 -0.1087 99   LYS A NZ  
2251 N N   . ASP A 297 ? 0.6549 0.5626 0.7019 -0.0237 0.0183  -0.0334 100  ASP A N   
2252 C CA  . ASP A 297 ? 0.6274 0.5305 0.6609 -0.0268 0.0283  -0.0146 100  ASP A CA  
2253 C C   . ASP A 297 ? 0.5832 0.4763 0.5894 -0.0215 0.0267  -0.0129 100  ASP A C   
2254 O O   . ASP A 297 ? 0.5504 0.4332 0.5597 -0.0236 0.0277  -0.0052 100  ASP A O   
2255 C CB  . ASP A 297 ? 0.6527 0.5682 0.6743 -0.0264 0.0357  -0.0087 100  ASP A CB  
2256 C CG  . ASP A 297 ? 0.6551 0.5709 0.6644 -0.0285 0.0458  0.0089  100  ASP A CG  
2257 O OD1 . ASP A 297 ? 0.6794 0.5855 0.6927 -0.0313 0.0473  0.0186  100  ASP A OD1 
2258 O OD2 . ASP A 297 ? 0.6283 0.5549 0.6244 -0.0265 0.0517  0.0124  100  ASP A OD2 
2259 N N   . LYS A 298 ? 0.5819 0.4783 0.5631 -0.0145 0.0242  -0.0193 101  LYS A N   
2260 C CA  . LYS A 298 ? 0.6029 0.4912 0.5627 -0.0095 0.0221  -0.0191 101  LYS A CA  
2261 C C   . LYS A 298 ? 0.5951 0.4883 0.5460 -0.0022 0.0150  -0.0324 101  LYS A C   
2262 O O   . LYS A 298 ? 0.6039 0.5063 0.5489 0.0009  0.0145  -0.0358 101  LYS A O   
2263 C CB  . LYS A 298 ? 0.6752 0.5631 0.6122 -0.0082 0.0283  -0.0086 101  LYS A CB  
2264 C CG  . LYS A 298 ? 0.6983 0.5850 0.6393 -0.0134 0.0355  0.0056  101  LYS A CG  
2265 C CD  . LYS A 298 ? 0.7435 0.6190 0.6951 -0.0161 0.0341  0.0108  101  LYS A CD  
2266 C CE  . LYS A 298 ? 0.8049 0.6811 0.7626 -0.0209 0.0416  0.0277  101  LYS A CE  
2267 N NZ  . LYS A 298 ? 0.8723 0.7566 0.8067 -0.0180 0.0472  0.0345  101  LYS A NZ  
2268 N N   . PRO A 299 ? 0.5976 0.4871 0.5485 0.0015  0.0093  -0.0402 102  PRO A N   
2269 C CA  . PRO A 299 ? 0.5632 0.4617 0.5049 0.0099  0.0029  -0.0522 102  PRO A CA  
2270 C C   . PRO A 299 ? 0.5513 0.4540 0.4697 0.0145  0.0059  -0.0462 102  PRO A C   
2271 O O   . PRO A 299 ? 0.5318 0.4277 0.4376 0.0133  0.0111  -0.0359 102  PRO A O   
2272 C CB  . PRO A 299 ? 0.5456 0.4392 0.4853 0.0135  -0.0008 -0.0575 102  PRO A CB  
2273 C CG  . PRO A 299 ? 0.5947 0.4773 0.5558 0.0062  0.0001  -0.0541 102  PRO A CG  
2274 C CD  . PRO A 299 ? 0.5963 0.4749 0.5554 -0.0005 0.0083  -0.0383 102  PRO A CD  
2275 N N   . LEU A 300 ? 0.5638 0.4781 0.4785 0.0205  0.0018  -0.0532 103  LEU A N   
2276 C CA  . LEU A 300 ? 0.5914 0.5099 0.4891 0.0253  0.0039  -0.0470 103  LEU A CA  
2277 C C   . LEU A 300 ? 0.6204 0.5413 0.5008 0.0330  0.0028  -0.0452 103  LEU A C   
2278 O O   . LEU A 300 ? 0.5847 0.5045 0.4533 0.0354  0.0061  -0.0362 103  LEU A O   
2279 C CB  . LEU A 300 ? 0.5488 0.4797 0.4523 0.0285  0.0001  -0.0532 103  LEU A CB  
2280 C CG  . LEU A 300 ? 0.5158 0.4480 0.4342 0.0221  0.0032  -0.0520 103  LEU A CG  
2281 C CD1 . LEU A 300 ? 0.4999 0.4455 0.4311 0.0251  -0.0030 -0.0626 103  LEU A CD1 
2282 C CD2 . LEU A 300 ? 0.4448 0.3735 0.3526 0.0215  0.0095  -0.0417 103  LEU A CD2 
2283 N N   . GLY A 301 ? 0.6251 0.5511 0.5060 0.0375  -0.0019 -0.0542 104  GLY A N   
2284 C CA  . GLY A 301 ? 0.6123 0.5464 0.4769 0.0464  -0.0025 -0.0528 104  GLY A CA  
2285 C C   . GLY A 301 ? 0.6132 0.5656 0.4741 0.0559  -0.0089 -0.0619 104  GLY A C   
2286 O O   . GLY A 301 ? 0.6375 0.5958 0.5120 0.0556  -0.0150 -0.0744 104  GLY A O   
2287 N N   . ALA A 302 ? 0.6070 0.5699 0.4512 0.0647  -0.0079 -0.0552 105  ALA A N   
2288 C CA  . ALA A 302 ? 0.5964 0.5796 0.4338 0.0755  -0.0140 -0.0616 105  ALA A CA  
2289 C C   . ALA A 302 ? 0.6104 0.5942 0.4506 0.0748  -0.0144 -0.0556 105  ALA A C   
2290 O O   . ALA A 302 ? 0.6033 0.5846 0.4354 0.0763  -0.0097 -0.0407 105  ALA A O   
2291 C CB  . ALA A 302 ? 0.6024 0.5988 0.4207 0.0860  -0.0115 -0.0539 105  ALA A CB  
2292 N N   . VAL A 303 ? 0.5927 0.5803 0.4474 0.0727  -0.0203 -0.0678 106  VAL A N   
2293 C CA  . VAL A 303 ? 0.5663 0.5542 0.4270 0.0712  -0.0205 -0.0637 106  VAL A CA  
2294 C C   . VAL A 303 ? 0.5884 0.5920 0.4356 0.0832  -0.0236 -0.0579 106  VAL A C   
2295 O O   . VAL A 303 ? 0.5773 0.5976 0.4118 0.0940  -0.0278 -0.0612 106  VAL A O   
2296 C CB  . VAL A 303 ? 0.5384 0.5291 0.4207 0.0662  -0.0259 -0.0784 106  VAL A CB  
2297 C CG1 . VAL A 303 ? 0.5063 0.4809 0.4028 0.0542  -0.0212 -0.0788 106  VAL A CG1 
2298 C CG2 . VAL A 303 ? 0.5425 0.5511 0.4278 0.0747  -0.0363 -0.0962 106  VAL A CG2 
2299 N N   . ALA A 304 ? 0.5575 0.5577 0.4081 0.0823  -0.0219 -0.0492 107  ALA A N   
2300 C CA  . ALA A 304 ? 0.5497 0.5627 0.3908 0.0933  -0.0247 -0.0407 107  ALA A CA  
2301 C C   . ALA A 304 ? 0.5710 0.6039 0.4156 0.1014  -0.0349 -0.0539 107  ALA A C   
2302 O O   . ALA A 304 ? 0.5910 0.6395 0.4242 0.1134  -0.0387 -0.0478 107  ALA A O   
2303 C CB  . ALA A 304 ? 0.5082 0.5096 0.3552 0.0900  -0.0201 -0.0280 107  ALA A CB  
2304 N N   . LEU A 305 ? 0.5686 0.6023 0.4304 0.0955  -0.0394 -0.0710 108  LEU A N   
2305 C CA  . LEU A 305 ? 0.6007 0.6539 0.4706 0.1026  -0.0503 -0.0861 108  LEU A CA  
2306 C C   . LEU A 305 ? 0.6091 0.6798 0.4700 0.1121  -0.0580 -0.0997 108  LEU A C   
2307 O O   . LEU A 305 ? 0.6047 0.6702 0.4738 0.1066  -0.0585 -0.1112 108  LEU A O   
2308 C CB  . LEU A 305 ? 0.5956 0.6431 0.4928 0.0917  -0.0517 -0.0983 108  LEU A CB  
2309 C CG  . LEU A 305 ? 0.5745 0.6413 0.4873 0.0970  -0.0632 -0.1155 108  LEU A CG  
2310 C CD1 . LEU A 305 ? 0.5391 0.6149 0.4486 0.1045  -0.0656 -0.1079 108  LEU A CD1 
2311 C CD2 . LEU A 305 ? 0.5687 0.6298 0.5120 0.0848  -0.0634 -0.1281 108  LEU A CD2 
2312 N N   . LYS A 306 ? 0.6220 0.7147 0.4671 0.1271  -0.0644 -0.0985 109  LYS A N   
2313 C CA  . LYS A 306 ? 0.6462 0.7599 0.4772 0.1392  -0.0710 -0.1100 109  LYS A CA  
2314 C C   . LYS A 306 ? 0.6560 0.7760 0.5076 0.1368  -0.0809 -0.1379 109  LYS A C   
2315 O O   . LYS A 306 ? 0.6345 0.7581 0.4837 0.1388  -0.0827 -0.1494 109  LYS A O   
2316 C CB  . LYS A 306 ? 0.6556 0.7960 0.4679 0.1569  -0.0775 -0.1048 109  LYS A CB  
2317 C CG  . LYS A 306 ? 0.6563 0.7917 0.4529 0.1602  -0.0688 -0.0761 109  LYS A CG  
2318 C CD  . LYS A 306 ? 0.7095 0.8706 0.4930 0.1770  -0.0764 -0.0703 109  LYS A CD  
2319 C CE  . LYS A 306 ? 0.7605 0.9187 0.5291 0.1820  -0.0675 -0.0397 109  LYS A CE  
2320 N NZ  . LYS A 306 ? 0.8139 1.0022 0.5650 0.2015  -0.0747 -0.0319 109  LYS A NZ  
2321 N N   . SER A 307 ? 0.6603 0.7822 0.5352 0.1327  -0.0877 -0.1497 110  SER A N   
2322 C CA  . SER A 307 ? 0.6645 0.7948 0.5637 0.1315  -0.0987 -0.1772 110  SER A CA  
2323 C C   . SER A 307 ? 0.6667 0.7761 0.5816 0.1184  -0.0931 -0.1814 110  SER A C   
2324 O O   . SER A 307 ? 0.6733 0.7895 0.5977 0.1213  -0.1006 -0.2010 110  SER A O   
2325 C CB  . SER A 307 ? 0.6381 0.7722 0.5645 0.1271  -0.1051 -0.1864 110  SER A CB  
2326 O OG  . SER A 307 ? 0.6023 0.7135 0.5427 0.1119  -0.0941 -0.1720 110  SER A OG  
2327 N N   . TYR A 308 ? 0.6703 0.7547 0.5884 0.1049  -0.0806 -0.1635 111  TYR A N   
2328 C CA  . TYR A 308 ? 0.6788 0.7428 0.6122 0.0923  -0.0748 -0.1642 111  TYR A CA  
2329 C C   . TYR A 308 ? 0.6793 0.7374 0.5907 0.0953  -0.0690 -0.1564 111  TYR A C   
2330 O O   . TYR A 308 ? 0.6986 0.7498 0.6214 0.0916  -0.0702 -0.1663 111  TYR A O   
2331 C CB  . TYR A 308 ? 0.7033 0.7468 0.6492 0.0778  -0.0644 -0.1488 111  TYR A CB  
2332 C CG  . TYR A 308 ? 0.7130 0.7373 0.6793 0.0643  -0.0590 -0.1487 111  TYR A CG  
2333 C CD1 . TYR A 308 ? 0.7621 0.7880 0.7517 0.0628  -0.0667 -0.1672 111  TYR A CD1 
2334 C CD2 . TYR A 308 ? 0.6864 0.6920 0.6498 0.0541  -0.0470 -0.1304 111  TYR A CD2 
2335 C CE1 . TYR A 308 ? 0.7698 0.7773 0.7802 0.0508  -0.0617 -0.1645 111  TYR A CE1 
2336 C CE2 . TYR A 308 ? 0.7073 0.6969 0.6876 0.0430  -0.0420 -0.1277 111  TYR A CE2 
2337 C CZ  . TYR A 308 ? 0.7536 0.7434 0.7577 0.0411  -0.0489 -0.1434 111  TYR A CZ  
2338 O OH  . TYR A 308 ? 0.7558 0.7291 0.7786 0.0302  -0.0438 -0.1382 111  TYR A OH  
2339 N N   . GLU A 309 ? 0.6566 0.7173 0.5396 0.1019  -0.0628 -0.1387 112  GLU A N   
2340 C CA  . GLU A 309 ? 0.6370 0.6948 0.5008 0.1052  -0.0568 -0.1309 112  GLU A CA  
2341 C C   . GLU A 309 ? 0.6636 0.7427 0.5213 0.1178  -0.0657 -0.1501 112  GLU A C   
2342 O O   . GLU A 309 ? 0.6394 0.7159 0.4897 0.1190  -0.0621 -0.1503 112  GLU A O   
2343 C CB  . GLU A 309 ? 0.6162 0.6751 0.4555 0.1102  -0.0488 -0.1076 112  GLU A CB  
2344 C CG  . GLU A 309 ? 0.6624 0.7234 0.4823 0.1152  -0.0427 -0.0986 112  GLU A CG  
2345 C CD  . GLU A 309 ? 0.7128 0.7512 0.5410 0.1034  -0.0356 -0.0956 112  GLU A CD  
2346 O OE1 . GLU A 309 ? 0.7063 0.7464 0.5224 0.1068  -0.0309 -0.0908 112  GLU A OE1 
2347 O OE2 . GLU A 309 ? 0.7524 0.7729 0.5994 0.0912  -0.0344 -0.0972 112  GLU A OE2 
2348 N N   . GLU A 310 ? 0.6964 0.7984 0.5574 0.1280  -0.0776 -0.1674 113  GLU A N   
2349 C CA  . GLU A 310 ? 0.7299 0.8556 0.5850 0.1417  -0.0873 -0.1886 113  GLU A CA  
2350 C C   . GLU A 310 ? 0.7646 0.8796 0.6475 0.1344  -0.0922 -0.2095 113  GLU A C   
2351 O O   . GLU A 310 ? 0.7907 0.9170 0.6687 0.1429  -0.0961 -0.2237 113  GLU A O   
2352 C CB  . GLU A 310 ? 0.7477 0.9015 0.6007 0.1549  -0.1001 -0.2030 113  GLU A CB  
2353 C CG  . GLU A 310 ? 0.7842 0.9553 0.6052 0.1674  -0.0965 -0.1829 113  GLU A CG  
2354 C CD  . GLU A 310 ? 0.8332 1.0289 0.6544 0.1788  -0.1089 -0.1935 113  GLU A CD  
2355 O OE1 . GLU A 310 ? 0.8580 1.0650 0.7004 0.1811  -0.1223 -0.2215 113  GLU A OE1 
2356 O OE2 . GLU A 310 ? 0.8484 1.0522 0.6510 0.1856  -0.1058 -0.1737 113  GLU A OE2 
2357 N N   . GLU A 311 ? 0.7575 0.8510 0.6708 0.1190  -0.0914 -0.2106 114  GLU A N   
2358 C CA  . GLU A 311 ? 0.7464 0.8267 0.6903 0.1108  -0.0951 -0.2264 114  GLU A CA  
2359 C C   . GLU A 311 ? 0.7550 0.8115 0.6943 0.1015  -0.0831 -0.2097 114  GLU A C   
2360 O O   . GLU A 311 ? 0.7760 0.8295 0.7234 0.1028  -0.0855 -0.2210 114  GLU A O   
2361 C CB  . GLU A 311 ? 0.7300 0.8004 0.7116 0.0988  -0.0992 -0.2332 114  GLU A CB  
2362 C CG  . GLU A 311 ? 0.7714 0.8655 0.7624 0.1073  -0.1121 -0.2513 114  GLU A CG  
2363 C CD  . GLU A 311 ? 0.8225 0.9416 0.8168 0.1224  -0.1276 -0.2822 114  GLU A CD  
2364 O OE1 . GLU A 311 ? 0.8261 0.9398 0.8313 0.1225  -0.1300 -0.2948 114  GLU A OE1 
2365 O OE2 . GLU A 311 ? 0.8377 0.9833 0.8238 0.1354  -0.1380 -0.2948 114  GLU A OE2 
2366 N N   . LEU A 312 ? 0.7536 0.7941 0.6803 0.0930  -0.0709 -0.1839 115  LEU A N   
2367 C CA  . LEU A 312 ? 0.7380 0.7571 0.6609 0.0846  -0.0605 -0.1687 115  LEU A CA  
2368 C C   . LEU A 312 ? 0.7273 0.7558 0.6250 0.0950  -0.0579 -0.1670 115  LEU A C   
2369 O O   . LEU A 312 ? 0.7360 0.7532 0.6384 0.0917  -0.0549 -0.1673 115  LEU A O   
2370 C CB  . LEU A 312 ? 0.7224 0.7258 0.6374 0.0749  -0.0494 -0.1443 115  LEU A CB  
2371 C CG  . LEU A 312 ? 0.6797 0.6754 0.6189 0.0646  -0.0498 -0.1440 115  LEU A CG  
2372 C CD1 . LEU A 312 ? 0.6117 0.5954 0.5411 0.0573  -0.0393 -0.1224 115  LEU A CD1 
2373 C CD2 . LEU A 312 ? 0.6319 0.6148 0.6036 0.0548  -0.0521 -0.1530 115  LEU A CD2 
2374 N N   . ALA A 313 ? 0.7131 0.7632 0.5846 0.1078  -0.0583 -0.1636 116  ALA A N   
2375 C CA  . ALA A 313 ? 0.7031 0.7656 0.5506 0.1182  -0.0540 -0.1591 116  ALA A CA  
2376 C C   . ALA A 313 ? 0.6758 0.7451 0.5335 0.1236  -0.0606 -0.1816 116  ALA A C   
2377 O O   . ALA A 313 ? 0.6705 0.7409 0.5167 0.1270  -0.0550 -0.1772 116  ALA A O   
2378 C CB  . ALA A 313 ? 0.7283 0.8186 0.5496 0.1333  -0.0554 -0.1545 116  ALA A CB  
2379 N N   . LYS A 314 ? 0.6453 0.7196 0.5272 0.1247  -0.0729 -0.2065 117  LYS A N   
2380 C CA  . LYS A 314 ? 0.6882 0.7680 0.5854 0.1301  -0.0809 -0.2309 117  LYS A CA  
2381 C C   . LYS A 314 ? 0.6797 0.7317 0.5947 0.1179  -0.0751 -0.2249 117  LYS A C   
2382 O O   . LYS A 314 ? 0.7032 0.7584 0.6263 0.1232  -0.0791 -0.2404 117  LYS A O   
2383 C CB  . LYS A 314 ? 0.7165 0.8058 0.6423 0.1326  -0.0963 -0.2594 117  LYS A CB  
2384 C CG  . LYS A 314 ? 0.7275 0.8449 0.6374 0.1448  -0.1034 -0.2661 117  LYS A CG  
2385 C CD  . LYS A 314 ? 0.7319 0.8522 0.6757 0.1422  -0.1171 -0.2888 117  LYS A CD  
2386 C CE  . LYS A 314 ? 0.7451 0.9017 0.6755 0.1603  -0.1296 -0.3079 117  LYS A CE  
2387 N NZ  . LYS A 314 ? 0.7589 0.9188 0.7248 0.1568  -0.1431 -0.3291 117  LYS A NZ  
2388 N N   . ASP A 315 ? 0.6715 0.6982 0.5926 0.1030  -0.0665 -0.2036 118  ASP A N   
2389 C CA  . ASP A 315 ? 0.6901 0.6914 0.6256 0.0919  -0.0608 -0.1946 118  ASP A CA  
2390 C C   . ASP A 315 ? 0.6623 0.6644 0.5721 0.0960  -0.0514 -0.1805 118  ASP A C   
2391 O O   . ASP A 315 ? 0.6705 0.6764 0.5555 0.0969  -0.0432 -0.1616 118  ASP A O   
2392 C CB  . ASP A 315 ? 0.7053 0.6841 0.6519 0.0764  -0.0543 -0.1758 118  ASP A CB  
2393 C CG  . ASP A 315 ? 0.7107 0.6651 0.6707 0.0657  -0.0485 -0.1646 118  ASP A CG  
2394 O OD1 . ASP A 315 ? 0.7156 0.6685 0.6681 0.0697  -0.0465 -0.1647 118  ASP A OD1 
2395 O OD2 . ASP A 315 ? 0.7103 0.6484 0.6879 0.0538  -0.0457 -0.1549 118  ASP A OD2 
2396 N N   . PRO A 316 ? 0.6284 0.6273 0.5461 0.0984  -0.0525 -0.1892 119  PRO A N   
2397 C CA  . PRO A 316 ? 0.6145 0.6167 0.5097 0.1027  -0.0434 -0.1764 119  PRO A CA  
2398 C C   . PRO A 316 ? 0.6252 0.6073 0.5121 0.0913  -0.0323 -0.1492 119  PRO A C   
2399 O O   . PRO A 316 ? 0.6416 0.6302 0.5065 0.0946  -0.0241 -0.1345 119  PRO A O   
2400 C CB  . PRO A 316 ? 0.6120 0.6106 0.5257 0.1057  -0.0483 -0.1931 119  PRO A CB  
2401 C CG  . PRO A 316 ? 0.6056 0.5935 0.5550 0.1004  -0.0594 -0.2115 119  PRO A CG  
2402 C CD  . PRO A 316 ? 0.6074 0.6061 0.5550 0.1011  -0.0638 -0.2153 119  PRO A CD  
2403 N N   . ARG A 317 ? 0.6119 0.5711 0.5168 0.0782  -0.0317 -0.1417 120  ARG A N   
2404 C CA  . ARG A 317 ? 0.5864 0.5300 0.4817 0.0688  -0.0220 -0.1178 120  ARG A CA  
2405 C C   . ARG A 317 ? 0.5884 0.5421 0.4625 0.0711  -0.0174 -0.1055 120  ARG A C   
2406 O O   . ARG A 317 ? 0.5306 0.4792 0.3908 0.0685  -0.0094 -0.0879 120  ARG A O   
2407 C CB  . ARG A 317 ? 0.5537 0.4759 0.4710 0.0561  -0.0222 -0.1126 120  ARG A CB  
2408 C CG  . ARG A 317 ? 0.5550 0.4666 0.4988 0.0539  -0.0278 -0.1238 120  ARG A CG  
2409 C CD  . ARG A 317 ? 0.5324 0.4257 0.5007 0.0417  -0.0277 -0.1167 120  ARG A CD  
2410 N NE  . ARG A 317 ? 0.5591 0.4586 0.5395 0.0396  -0.0319 -0.1240 120  ARG A NE  
2411 C CZ  . ARG A 317 ? 0.6092 0.4992 0.6027 0.0295  -0.0287 -0.1134 120  ARG A CZ  
2412 N NH1 . ARG A 317 ? 0.5994 0.4739 0.5940 0.0211  -0.0215 -0.0948 120  ARG A NH1 
2413 N NH2 . ARG A 317 ? 0.6273 0.5257 0.6329 0.0283  -0.0326 -0.1212 120  ARG A NH2 
2414 N N   . ILE A 318 ? 0.5928 0.5607 0.4664 0.0762  -0.0232 -0.1151 121  ILE A N   
2415 C CA  . ILE A 318 ? 0.6508 0.6286 0.5061 0.0796  -0.0197 -0.1035 121  ILE A CA  
2416 C C   . ILE A 318 ? 0.6704 0.6689 0.5034 0.0920  -0.0169 -0.1002 121  ILE A C   
2417 O O   . ILE A 318 ? 0.6810 0.6813 0.4989 0.0928  -0.0096 -0.0818 121  ILE A O   
2418 C CB  . ILE A 318 ? 0.6710 0.6573 0.5348 0.0808  -0.0272 -0.1140 121  ILE A CB  
2419 C CG1 . ILE A 318 ? 0.6901 0.6576 0.5772 0.0679  -0.0278 -0.1136 121  ILE A CG1 
2420 C CG2 . ILE A 318 ? 0.6402 0.6380 0.4856 0.0860  -0.0245 -0.1020 121  ILE A CG2 
2421 C CD1 . ILE A 318 ? 0.6907 0.6482 0.5717 0.0606  -0.0205 -0.0952 121  ILE A CD1 
2422 N N   . ALA A 319 ? 0.6160 0.6313 0.4483 0.1022  -0.0223 -0.1176 122  ALA A N   
2423 C CA  . ALA A 319 ? 0.6168 0.6546 0.4275 0.1147  -0.0181 -0.1135 122  ALA A CA  
2424 C C   . ALA A 319 ? 0.6548 0.6819 0.4602 0.1100  -0.0075 -0.0954 122  ALA A C   
2425 O O   . ALA A 319 ? 0.7014 0.7398 0.4904 0.1148  0.0002  -0.0789 122  ALA A O   
2426 C CB  . ALA A 319 ? 0.6151 0.6739 0.4274 0.1270  -0.0261 -0.1383 122  ALA A CB  
2427 N N   . ALA A 320 ? 0.6191 0.6252 0.4399 0.1007  -0.0070 -0.0973 123  ALA A N   
2428 C CA  . ALA A 320 ? 0.6107 0.6059 0.4289 0.0955  0.0019  -0.0809 123  ALA A CA  
2429 C C   . ALA A 320 ? 0.5934 0.5767 0.4070 0.0877  0.0081  -0.0600 123  ALA A C   
2430 O O   . ALA A 320 ? 0.5602 0.5457 0.3658 0.0882  0.0158  -0.0442 123  ALA A O   
2431 C CB  . ALA A 320 ? 0.6196 0.5946 0.4560 0.0877  -0.0003 -0.0873 123  ALA A CB  
2432 N N   . THR A 321 ? 0.6169 0.5879 0.4380 0.0804  0.0048  -0.0602 124  THR A N   
2433 C CA  . THR A 321 ? 0.6295 0.5910 0.4474 0.0744  0.0095  -0.0434 124  THR A CA  
2434 C C   . THR A 321 ? 0.6589 0.6377 0.4621 0.0828  0.0132  -0.0323 124  THR A C   
2435 O O   . THR A 321 ? 0.6572 0.6319 0.4577 0.0807  0.0199  -0.0154 124  THR A O   
2436 C CB  . THR A 321 ? 0.5939 0.5453 0.4218 0.0676  0.0052  -0.0478 124  THR A CB  
2437 O OG1 . THR A 321 ? 0.6006 0.5358 0.4433 0.0592  0.0033  -0.0536 124  THR A OG1 
2438 C CG2 . THR A 321 ? 0.5540 0.4977 0.3789 0.0629  0.0096  -0.0328 124  THR A CG2 
2439 N N   . MET A 322 ? 0.6584 0.6573 0.4538 0.0929  0.0083  -0.0413 125  MET A N   
2440 C CA  . MET A 322 ? 0.6506 0.6672 0.4319 0.1017  0.0116  -0.0282 125  MET A CA  
2441 C C   . MET A 322 ? 0.6216 0.6534 0.3925 0.1092  0.0190  -0.0182 125  MET A C   
2442 O O   . MET A 322 ? 0.6145 0.6546 0.3781 0.1130  0.0251  0.0005  125  MET A O   
2443 C CB  . MET A 322 ? 0.6755 0.7118 0.4503 0.1116  0.0034  -0.0406 125  MET A CB  
2444 C CG  . MET A 322 ? 0.7145 0.7394 0.4997 0.1051  -0.0020 -0.0445 125  MET A CG  
2445 S SD  . MET A 322 ? 0.7549 0.7677 0.5400 0.0999  0.0045  -0.0201 125  MET A SD  
2446 C CE  . MET A 322 ? 0.7698 0.7564 0.5661 0.0864  0.0108  -0.0138 125  MET A CE  
2447 N N   . GLU A 323 ? 0.6234 0.6587 0.3959 0.1110  0.0190  -0.0293 126  GLU A N   
2448 C CA  . GLU A 323 ? 0.6575 0.7068 0.4227 0.1169  0.0273  -0.0192 126  GLU A CA  
2449 C C   . GLU A 323 ? 0.6374 0.6677 0.4121 0.1065  0.0353  -0.0008 126  GLU A C   
2450 O O   . GLU A 323 ? 0.6625 0.7025 0.4339 0.1094  0.0437  0.0176  126  GLU A O   
2451 C CB  . GLU A 323 ? 0.7267 0.7852 0.4933 0.1222  0.0243  -0.0384 126  GLU A CB  
2452 C CG  . GLU A 323 ? 0.7902 0.8512 0.5585 0.1222  0.0328  -0.0301 126  GLU A CG  
2453 C CD  . GLU A 323 ? 0.8458 0.9131 0.6191 0.1272  0.0285  -0.0518 126  GLU A CD  
2454 O OE1 . GLU A 323 ? 0.8649 0.9400 0.6384 0.1331  0.0191  -0.0730 126  GLU A OE1 
2455 O OE2 . GLU A 323 ? 0.8562 0.9203 0.6357 0.1252  0.0337  -0.0485 126  GLU A OE2 
2456 N N   . ASN A 324 ? 0.6082 0.6127 0.3963 0.0946  0.0326  -0.0051 127  ASN A N   
2457 C CA  . ASN A 324 ? 0.6081 0.5953 0.4058 0.0853  0.0382  0.0099  127  ASN A CA  
2458 C C   . ASN A 324 ? 0.5789 0.5632 0.3771 0.0836  0.0410  0.0262  127  ASN A C   
2459 O O   . ASN A 324 ? 0.5438 0.5244 0.3491 0.0806  0.0472  0.0418  127  ASN A O   
2460 C CB  . ASN A 324 ? 0.6077 0.5710 0.4170 0.0746  0.0340  0.0016  127  ASN A CB  
2461 C CG  . ASN A 324 ? 0.6064 0.5681 0.4207 0.0746  0.0335  -0.0076 127  ASN A CG  
2462 O OD1 . ASN A 324 ? 0.6119 0.5813 0.4268 0.0773  0.0392  -0.0010 127  ASN A OD1 
2463 N ND2 . ASN A 324 ? 0.5756 0.5277 0.3961 0.0718  0.0270  -0.0219 127  ASN A ND2 
2464 N N   . ALA A 325 ? 0.5995 0.5854 0.3934 0.0855  0.0358  0.0221  128  ALA A N   
2465 C CA  . ALA A 325 ? 0.6058 0.5899 0.4013 0.0853  0.0374  0.0366  128  ALA A CA  
2466 C C   . ALA A 325 ? 0.6693 0.6736 0.4578 0.0946  0.0442  0.0540  128  ALA A C   
2467 O O   . ALA A 325 ? 0.6777 0.6766 0.4758 0.0918  0.0497  0.0721  128  ALA A O   
2468 C CB  . ALA A 325 ? 0.5554 0.5405 0.3478 0.0869  0.0301  0.0272  128  ALA A CB  
2469 N N   . GLN A 326 ? 0.7105 0.7394 0.4841 0.1061  0.0437  0.0487  129  GLN A N   
2470 C CA  . GLN A 326 ? 0.7672 0.8201 0.5314 0.1167  0.0508  0.0670  129  GLN A CA  
2471 C C   . GLN A 326 ? 0.7578 0.8099 0.5317 0.1133  0.0611  0.0830  129  GLN A C   
2472 O O   . GLN A 326 ? 0.7899 0.8546 0.5647 0.1180  0.0690  0.1051  129  GLN A O   
2473 C CB  . GLN A 326 ? 0.8345 0.9172 0.5792 0.1309  0.0480  0.0548  129  GLN A CB  
2474 C CG  . GLN A 326 ? 0.9261 1.0382 0.6563 0.1445  0.0535  0.0731  129  GLN A CG  
2475 C CD  . GLN A 326 ? 1.0147 1.1290 0.7407 0.1485  0.0480  0.0789  129  GLN A CD  
2476 O OE1 . GLN A 326 ? 1.0111 1.1016 0.7513 0.1389  0.0463  0.0854  129  GLN A OE1 
2477 N NE2 . GLN A 326 ? 1.0712 1.2160 0.7775 0.1640  0.0446  0.0759  129  GLN A NE2 
2478 N N   . LYS A 327 ? 0.7241 0.7629 0.5068 0.1057  0.0612  0.0729  130  LYS A N   
2479 C CA  . LYS A 327 ? 0.6691 0.7051 0.4652 0.1012  0.0699  0.0867  130  LYS A CA  
2480 C C   . LYS A 327 ? 0.6364 0.6475 0.4532 0.0896  0.0703  0.0974  130  LYS A C   
2481 O O   . LYS A 327 ? 0.6358 0.6462 0.4678 0.0865  0.0776  0.1132  130  LYS A O   
2482 C CB  . LYS A 327 ? 0.6136 0.6473 0.4116 0.0990  0.0691  0.0711  130  LYS A CB  
2483 C CG  . LYS A 327 ? 0.6324 0.6939 0.4154 0.1113  0.0710  0.0628  130  LYS A CG  
2484 C CD  . LYS A 327 ? 0.6732 0.7277 0.4614 0.1085  0.0677  0.0441  130  LYS A CD  
2485 C CE  . LYS A 327 ? 0.7232 0.8063 0.4983 0.1219  0.0687  0.0318  130  LYS A CE  
2486 N NZ  . LYS A 327 ? 0.7565 0.8523 0.5161 0.1307  0.0610  0.0184  130  LYS A NZ  
2487 N N   . GLY A 328 ? 0.6192 0.6113 0.4387 0.0835  0.0627  0.0881  131  GLY A N   
2488 C CA  . GLY A 328 ? 0.6431 0.6135 0.4809 0.0741  0.0616  0.0939  131  GLY A CA  
2489 C C   . GLY A 328 ? 0.6785 0.6510 0.5213 0.0772  0.0628  0.1099  131  GLY A C   
2490 O O   . GLY A 328 ? 0.7132 0.7055 0.5485 0.0861  0.0676  0.1238  131  GLY A O   
2491 N N   . GLU A 329 ? 0.6609 0.6144 0.5161 0.0706  0.0581  0.1077  132  GLU A N   
2492 C CA  . GLU A 329 ? 0.7010 0.6536 0.5658 0.0731  0.0584  0.1223  132  GLU A CA  
2493 C C   . GLU A 329 ? 0.6862 0.6231 0.5542 0.0689  0.0505  0.1098  132  GLU A C   
2494 O O   . GLU A 329 ? 0.6385 0.5594 0.5145 0.0609  0.0472  0.0978  132  GLU A O   
2495 C CB  . GLU A 329 ? 0.7195 0.6659 0.6106 0.0692  0.0642  0.1409  132  GLU A CB  
2496 C CG  . GLU A 329 ? 0.7765 0.7397 0.6677 0.0727  0.0735  0.1551  132  GLU A CG  
2497 C CD  . GLU A 329 ? 0.8829 0.8453 0.8015 0.0713  0.0802  0.1795  132  GLU A CD  
2498 O OE1 . GLU A 329 ? 0.8786 0.8240 0.8191 0.0669  0.0763  0.1830  132  GLU A OE1 
2499 O OE2 . GLU A 329 ? 0.9404 0.9199 0.8614 0.0748  0.0896  0.1954  132  GLU A OE2 
2500 N N   . ILE A 330 ? 0.7213 0.6649 0.5833 0.0751  0.0476  0.1133  133  ILE A N   
2501 C CA  . ILE A 330 ? 0.6874 0.6183 0.5558 0.0721  0.0410  0.1039  133  ILE A CA  
2502 C C   . ILE A 330 ? 0.6335 0.5465 0.5273 0.0653  0.0410  0.1079  133  ILE A C   
2503 O O   . ILE A 330 ? 0.6500 0.5627 0.5605 0.0661  0.0453  0.1252  133  ILE A O   
2504 C CB  . ILE A 330 ? 0.7158 0.6583 0.5776 0.0810  0.0384  0.1107  133  ILE A CB  
2505 C CG1 . ILE A 330 ? 0.7086 0.6418 0.5743 0.0786  0.0313  0.0971  133  ILE A CG1 
2506 C CG2 . ILE A 330 ? 0.7548 0.6998 0.6314 0.0852  0.0428  0.1348  133  ILE A CG2 
2507 C CD1 . ILE A 330 ? 0.7129 0.6507 0.5626 0.0777  0.0269  0.0772  133  ILE A CD1 
2508 N N   . MET A 331 ? 0.5654 0.4650 0.4638 0.0589  0.0363  0.0917  134  MET A N   
2509 C CA  . MET A 331 ? 0.5284 0.4130 0.4505 0.0538  0.0347  0.0910  134  MET A CA  
2510 C C   . MET A 331 ? 0.5789 0.4610 0.5177 0.0579  0.0327  0.1011  134  MET A C   
2511 O O   . MET A 331 ? 0.5931 0.4818 0.5222 0.0632  0.0303  0.1008  134  MET A O   
2512 C CB  . MET A 331 ? 0.5220 0.3975 0.4419 0.0484  0.0299  0.0714  134  MET A CB  
2513 C CG  . MET A 331 ? 0.5744 0.4495 0.4824 0.0438  0.0311  0.0624  134  MET A CG  
2514 S SD  . MET A 331 ? 0.5758 0.4422 0.4823 0.0386  0.0264  0.0435  134  MET A SD  
2515 C CE  . MET A 331 ? 0.5768 0.4506 0.4655 0.0408  0.0248  0.0357  134  MET A CE  
2516 N N   . PRO A 332 ? 0.5977 0.4699 0.5646 0.0556  0.0331  0.1095  135  PRO A N   
2517 C CA  . PRO A 332 ? 0.6223 0.4877 0.6105 0.0585  0.0292  0.1141  135  PRO A CA  
2518 C C   . PRO A 332 ? 0.6194 0.4789 0.6045 0.0572  0.0226  0.0927  135  PRO A C   
2519 O O   . PRO A 332 ? 0.5757 0.4340 0.5481 0.0528  0.0214  0.0762  135  PRO A O   
2520 C CB  . PRO A 332 ? 0.6245 0.4783 0.6481 0.0545  0.0299  0.1225  135  PRO A CB  
2521 C CG  . PRO A 332 ? 0.6253 0.4846 0.6436 0.0510  0.0363  0.1290  135  PRO A CG  
2522 C CD  . PRO A 332 ? 0.5842 0.4513 0.5678 0.0504  0.0365  0.1145  135  PRO A CD  
2523 N N   . ASN A 333 ? 0.6008 0.4580 0.5982 0.0618  0.0186  0.0942  136  ASN A N   
2524 C CA  . ASN A 333 ? 0.5877 0.4403 0.5888 0.0614  0.0127  0.0749  136  ASN A CA  
2525 C C   . ASN A 333 ? 0.6599 0.4998 0.6964 0.0617  0.0082  0.0730  136  ASN A C   
2526 O O   . ASN A 333 ? 0.7292 0.5665 0.7729 0.0631  0.0029  0.0570  136  ASN A O   
2527 C CB  . ASN A 333 ? 0.5767 0.4392 0.5628 0.0673  0.0108  0.0736  136  ASN A CB  
2528 C CG  . ASN A 333 ? 0.6089 0.4716 0.6120 0.0746  0.0091  0.0906  136  ASN A CG  
2529 O OD1 . ASN A 333 ? 0.5966 0.4525 0.6217 0.0750  0.0107  0.1062  136  ASN A OD1 
2530 N ND2 . ASN A 333 ? 0.6476 0.5182 0.6426 0.0804  0.0058  0.0881  136  ASN A ND2 
2531 N N   . ILE A 334 ? 0.6384 0.4712 0.6998 0.0604  0.0098  0.0877  137  ILE A N   
2532 C CA  . ILE A 334 ? 0.6755 0.4953 0.7768 0.0605  0.0045  0.0854  137  ILE A CA  
2533 C C   . ILE A 334 ? 0.6415 0.4563 0.7480 0.0571  -0.0011 0.0583  137  ILE A C   
2534 O O   . ILE A 334 ? 0.6028 0.4227 0.6851 0.0533  0.0006  0.0471  137  ILE A O   
2535 C CB  . ILE A 334 ? 0.7067 0.5202 0.8372 0.0582  0.0081  0.1064  137  ILE A CB  
2536 C CG1 . ILE A 334 ? 0.7208 0.5349 0.8455 0.0513  0.0114  0.1020  137  ILE A CG1 
2537 C CG2 . ILE A 334 ? 0.7103 0.5330 0.8320 0.0633  0.0146  0.1349  137  ILE A CG2 
2538 C CD1 . ILE A 334 ? 0.7497 0.5614 0.9005 0.0488  0.0169  0.1251  137  ILE A CD1 
2539 N N   . PRO A 335 ? 0.6033 0.4093 0.7412 0.0594  -0.0083 0.0471  138  PRO A N   
2540 C CA  . PRO A 335 ? 0.5747 0.3803 0.7146 0.0586  -0.0144 0.0189  138  PRO A CA  
2541 C C   . PRO A 335 ? 0.6148 0.4177 0.7603 0.0530  -0.0150 0.0114  138  PRO A C   
2542 O O   . PRO A 335 ? 0.6295 0.4382 0.7587 0.0522  -0.0174 -0.0089 138  PRO A O   
2543 C CB  . PRO A 335 ? 0.5703 0.3672 0.7489 0.0637  -0.0223 0.0109  138  PRO A CB  
2544 C CG  . PRO A 335 ? 0.5604 0.3575 0.7405 0.0684  -0.0199 0.0318  138  PRO A CG  
2545 C CD  . PRO A 335 ? 0.5878 0.3875 0.7540 0.0651  -0.0115 0.0581  138  PRO A CD  
2546 N N   . GLN A 336 ? 0.6124 0.4087 0.7790 0.0494  -0.0124 0.0284  139  GLN A N   
2547 C CA  . GLN A 336 ? 0.6231 0.4177 0.7973 0.0440  -0.0133 0.0220  139  GLN A CA  
2548 C C   . GLN A 336 ? 0.6001 0.4046 0.7335 0.0407  -0.0073 0.0222  139  GLN A C   
2549 O O   . GLN A 336 ? 0.5839 0.3885 0.7197 0.0368  -0.0085 0.0153  139  GLN A O   
2550 C CB  . GLN A 336 ? 0.7062 0.4924 0.9174 0.0408  -0.0110 0.0423  139  GLN A CB  
2551 C CG  . GLN A 336 ? 0.7861 0.5608 1.0427 0.0440  -0.0161 0.0480  139  GLN A CG  
2552 C CD  . GLN A 336 ? 0.8310 0.6078 1.0789 0.0487  -0.0106 0.0719  139  GLN A CD  
2553 O OE1 . GLN A 336 ? 0.8660 0.6509 1.0910 0.0482  -0.0017 0.0935  139  GLN A OE1 
2554 N NE2 . GLN A 336 ? 0.8398 0.6110 1.1061 0.0541  -0.0166 0.0667  139  GLN A NE2 
2555 N N   . MET A 337 ? 0.5765 0.3893 0.6750 0.0424  -0.0019 0.0291  140  MET A N   
2556 C CA  . MET A 337 ? 0.5820 0.4027 0.6465 0.0393  0.0032  0.0293  140  MET A CA  
2557 C C   . MET A 337 ? 0.5843 0.4074 0.6385 0.0378  -0.0013 0.0073  140  MET A C   
2558 O O   . MET A 337 ? 0.5719 0.3966 0.6185 0.0344  -0.0003 0.0057  140  MET A O   
2559 C CB  . MET A 337 ? 0.5797 0.4091 0.6127 0.0419  0.0077  0.0356  140  MET A CB  
2560 C CG  . MET A 337 ? 0.6097 0.4424 0.6417 0.0437  0.0138  0.0591  140  MET A CG  
2561 S SD  . MET A 337 ? 0.6134 0.4477 0.6478 0.0391  0.0197  0.0714  140  MET A SD  
2562 C CE  . MET A 337 ? 0.6357 0.4778 0.6305 0.0371  0.0211  0.0581  140  MET A CE  
2563 N N   . SER A 338 ? 0.6031 0.4281 0.6576 0.0413  -0.0065 -0.0097 141  SER A N   
2564 C CA  . SER A 338 ? 0.6261 0.4570 0.6690 0.0416  -0.0104 -0.0296 141  SER A CA  
2565 C C   . SER A 338 ? 0.6207 0.4474 0.6863 0.0397  -0.0159 -0.0374 141  SER A C   
2566 O O   . SER A 338 ? 0.6722 0.5038 0.7224 0.0379  -0.0161 -0.0431 141  SER A O   
2567 C CB  . SER A 338 ? 0.6778 0.5140 0.7207 0.0469  -0.0144 -0.0458 141  SER A CB  
2568 O OG  . SER A 338 ? 0.7488 0.5918 0.7900 0.0491  -0.0198 -0.0663 141  SER A OG  
2569 N N   . ALA A 339 ? 0.5140 0.3317 0.6180 0.0402  -0.0205 -0.0370 142  ALA A N   
2570 C CA  . ALA A 339 ? 0.4923 0.3060 0.6243 0.0381  -0.0267 -0.0455 142  ALA A CA  
2571 C C   . ALA A 339 ? 0.5003 0.3136 0.6273 0.0325  -0.0210 -0.0301 142  ALA A C   
2572 O O   . ALA A 339 ? 0.5203 0.3363 0.6496 0.0308  -0.0247 -0.0395 142  ALA A O   
2573 C CB  . ALA A 339 ? 0.5083 0.3107 0.6905 0.0390  -0.0327 -0.0458 142  ALA A CB  
2574 N N   . PHE A 340 ? 0.5193 0.3309 0.6394 0.0304  -0.0122 -0.0069 143  PHE A N   
2575 C CA  . PHE A 340 ? 0.5413 0.3556 0.6530 0.0261  -0.0057 0.0072  143  PHE A CA  
2576 C C   . PHE A 340 ? 0.5527 0.3748 0.6285 0.0258  -0.0052 -0.0022 143  PHE A C   
2577 O O   . PHE A 340 ? 0.5021 0.3262 0.5800 0.0232  -0.0064 -0.0053 143  PHE A O   
2578 C CB  . PHE A 340 ? 0.5491 0.3647 0.6523 0.0263  0.0038  0.0321  143  PHE A CB  
2579 C CG  . PHE A 340 ? 0.5247 0.3476 0.6041 0.0243  0.0112  0.0427  143  PHE A CG  
2580 C CD1 . PHE A 340 ? 0.5554 0.3791 0.6522 0.0207  0.0139  0.0509  143  PHE A CD1 
2581 C CD2 . PHE A 340 ? 0.4983 0.3284 0.5391 0.0263  0.0151  0.0431  143  PHE A CD2 
2582 C CE1 . PHE A 340 ? 0.5316 0.3637 0.6047 0.0198  0.0205  0.0583  143  PHE A CE1 
2583 C CE2 . PHE A 340 ? 0.4400 0.2766 0.4619 0.0252  0.0207  0.0502  143  PHE A CE2 
2584 C CZ  . PHE A 340 ? 0.4787 0.3167 0.5155 0.0224  0.0235  0.0576  143  PHE A CZ  
2585 N N   . TRP A 341 ? 0.5803 0.4075 0.6250 0.0283  -0.0034 -0.0062 144  TRP A N   
2586 C CA  . TRP A 341 ? 0.5454 0.3795 0.5577 0.0278  -0.0019 -0.0116 144  TRP A CA  
2587 C C   . TRP A 341 ? 0.5812 0.4187 0.5957 0.0290  -0.0095 -0.0301 144  TRP A C   
2588 O O   . TRP A 341 ? 0.5761 0.4173 0.5778 0.0276  -0.0096 -0.0314 144  TRP A O   
2589 C CB  . TRP A 341 ? 0.5037 0.3428 0.4895 0.0300  0.0010  -0.0126 144  TRP A CB  
2590 C CG  . TRP A 341 ? 0.5306 0.3711 0.5016 0.0295  0.0082  0.0030  144  TRP A CG  
2591 C CD1 . TRP A 341 ? 0.5545 0.3962 0.5211 0.0320  0.0101  0.0078  144  TRP A CD1 
2592 C CD2 . TRP A 341 ? 0.5232 0.3658 0.4819 0.0274  0.0134  0.0139  144  TRP A CD2 
2593 N NE1 . TRP A 341 ? 0.5632 0.4087 0.5150 0.0319  0.0157  0.0204  144  TRP A NE1 
2594 C CE2 . TRP A 341 ? 0.5331 0.3794 0.4798 0.0292  0.0180  0.0237  144  TRP A CE2 
2595 C CE3 . TRP A 341 ? 0.5422 0.3853 0.4999 0.0249  0.0141  0.0150  144  TRP A CE3 
2596 C CZ2 . TRP A 341 ? 0.4871 0.3383 0.4202 0.0292  0.0230  0.0332  144  TRP A CZ2 
2597 C CZ3 . TRP A 341 ? 0.5315 0.3786 0.4762 0.0245  0.0198  0.0254  144  TRP A CZ3 
2598 C CH2 . TRP A 341 ? 0.5050 0.3564 0.4376 0.0268  0.0241  0.0336  144  TRP A CH2 
2599 N N   . TYR A 342 ? 0.6075 0.4457 0.6360 0.0325  -0.0164 -0.0455 145  TYR A N   
2600 C CA  . TYR A 342 ? 0.6132 0.4579 0.6440 0.0354  -0.0247 -0.0649 145  TYR A CA  
2601 C C   . TYR A 342 ? 0.5332 0.3745 0.5865 0.0325  -0.0285 -0.0648 145  TYR A C   
2602 O O   . TYR A 342 ? 0.5006 0.3487 0.5445 0.0335  -0.0326 -0.0734 145  TYR A O   
2603 C CB  . TYR A 342 ? 0.7209 0.5674 0.7699 0.0408  -0.0322 -0.0831 145  TYR A CB  
2604 C CG  . TYR A 342 ? 0.8224 0.6788 0.8749 0.0459  -0.0422 -0.1063 145  TYR A CG  
2605 C CD1 . TYR A 342 ? 0.8790 0.7502 0.8990 0.0507  -0.0422 -0.1158 145  TYR A CD1 
2606 C CD2 . TYR A 342 ? 0.8779 0.7307 0.9666 0.0464  -0.0516 -0.1184 145  TYR A CD2 
2607 C CE1 . TYR A 342 ? 0.9293 0.8132 0.9490 0.0570  -0.0513 -0.1367 145  TYR A CE1 
2608 C CE2 . TYR A 342 ? 0.9457 0.8101 1.0372 0.0524  -0.0621 -0.1422 145  TYR A CE2 
2609 C CZ  . TYR A 342 ? 0.9879 0.8689 1.0426 0.0583  -0.0619 -0.1512 145  TYR A CZ  
2610 O OH  . TYR A 342 ? 1.0502 0.9464 1.1045 0.0660  -0.0725 -0.1746 145  TYR A OH  
2611 N N   . ALA A 343 ? 0.5062 0.3382 0.5921 0.0291  -0.0275 -0.0547 146  ALA A N   
2612 C CA  . ALA A 343 ? 0.4990 0.3287 0.6124 0.0258  -0.0308 -0.0545 146  ALA A CA  
2613 C C   . ALA A 343 ? 0.4667 0.3000 0.5586 0.0225  -0.0242 -0.0420 146  ALA A C   
2614 O O   . ALA A 343 ? 0.4895 0.3269 0.5857 0.0221  -0.0288 -0.0493 146  ALA A O   
2615 C CB  . ALA A 343 ? 0.4493 0.2689 0.6060 0.0225  -0.0298 -0.0434 146  ALA A CB  
2616 N N   . VAL A 344 ? 0.4714 0.3037 0.5439 0.0208  -0.0141 -0.0235 147  VAL A N   
2617 C CA  . VAL A 344 ? 0.4896 0.3255 0.5462 0.0184  -0.0081 -0.0127 147  VAL A CA  
2618 C C   . VAL A 344 ? 0.5052 0.3474 0.5301 0.0206  -0.0107 -0.0227 147  VAL A C   
2619 O O   . VAL A 344 ? 0.4829 0.3283 0.5040 0.0196  -0.0110 -0.0219 147  VAL A O   
2620 C CB  . VAL A 344 ? 0.4949 0.3308 0.5378 0.0175  0.0026  0.0070  147  VAL A CB  
2621 C CG1 . VAL A 344 ? 0.4165 0.2578 0.4418 0.0163  0.0078  0.0143  147  VAL A CG1 
2622 C CG2 . VAL A 344 ? 0.4239 0.2557 0.4991 0.0158  0.0061  0.0211  147  VAL A CG2 
2623 N N   . ARG A 345 ? 0.5362 0.3811 0.5407 0.0239  -0.0127 -0.0314 148  ARG A N   
2624 C CA  . ARG A 345 ? 0.5724 0.4244 0.5496 0.0265  -0.0150 -0.0391 148  ARG A CA  
2625 C C   . ARG A 345 ? 0.5285 0.3856 0.5167 0.0286  -0.0242 -0.0527 148  ARG A C   
2626 O O   . ARG A 345 ? 0.5011 0.3623 0.4762 0.0291  -0.0252 -0.0520 148  ARG A O   
2627 C CB  . ARG A 345 ? 0.6457 0.5021 0.6050 0.0300  -0.0152 -0.0462 148  ARG A CB  
2628 C CG  . ARG A 345 ? 0.6946 0.5610 0.6280 0.0334  -0.0174 -0.0532 148  ARG A CG  
2629 C CD  . ARG A 345 ? 0.7871 0.6612 0.7060 0.0373  -0.0168 -0.0603 148  ARG A CD  
2630 N NE  . ARG A 345 ? 0.8926 0.7624 0.8030 0.0346  -0.0089 -0.0494 148  ARG A NE  
2631 C CZ  . ARG A 345 ? 0.9371 0.8045 0.8585 0.0354  -0.0082 -0.0513 148  ARG A CZ  
2632 N NH1 . ARG A 345 ? 0.9214 0.7888 0.8643 0.0385  -0.0146 -0.0637 148  ARG A NH1 
2633 N NH2 . ARG A 345 ? 0.9444 0.8096 0.8573 0.0334  -0.0018 -0.0416 148  ARG A NH2 
2634 N N   . THR A 346 ? 0.4906 0.3477 0.5045 0.0306  -0.0319 -0.0663 149  THR A N   
2635 C CA  . THR A 346 ? 0.5038 0.3675 0.5310 0.0335  -0.0423 -0.0819 149  THR A CA  
2636 C C   . THR A 346 ? 0.5454 0.4062 0.5899 0.0292  -0.0416 -0.0739 149  THR A C   
2637 O O   . THR A 346 ? 0.5534 0.4213 0.5933 0.0313  -0.0473 -0.0804 149  THR A O   
2638 C CB  . THR A 346 ? 0.5129 0.3763 0.5712 0.0362  -0.0513 -0.0990 149  THR A CB  
2639 O OG1 . THR A 346 ? 0.4949 0.3660 0.5328 0.0422  -0.0531 -0.1103 149  THR A OG1 
2640 C CG2 . THR A 346 ? 0.4544 0.3235 0.5368 0.0384  -0.0631 -0.1157 149  THR A CG2 
2641 N N   . ALA A 347 ? 0.5330 0.3853 0.5971 0.0237  -0.0344 -0.0586 150  ALA A N   
2642 C CA  . ALA A 347 ? 0.5053 0.3572 0.5903 0.0197  -0.0328 -0.0508 150  ALA A CA  
2643 C C   . ALA A 347 ? 0.4986 0.3543 0.5553 0.0195  -0.0273 -0.0415 150  ALA A C   
2644 O O   . ALA A 347 ? 0.4566 0.3167 0.5209 0.0194  -0.0307 -0.0439 150  ALA A O   
2645 C CB  . ALA A 347 ? 0.4819 0.3266 0.5950 0.0147  -0.0252 -0.0348 150  ALA A CB  
2646 N N   . VAL A 348 ? 0.5138 0.3678 0.5406 0.0197  -0.0193 -0.0312 151  VAL A N   
2647 C CA  . VAL A 348 ? 0.5456 0.4024 0.5488 0.0200  -0.0151 -0.0239 151  VAL A CA  
2648 C C   . VAL A 348 ? 0.5383 0.4011 0.5259 0.0241  -0.0231 -0.0352 151  VAL A C   
2649 O O   . VAL A 348 ? 0.5329 0.3988 0.5189 0.0247  -0.0246 -0.0339 151  VAL A O   
2650 C CB  . VAL A 348 ? 0.5183 0.3725 0.4960 0.0197  -0.0064 -0.0133 151  VAL A CB  
2651 C CG1 . VAL A 348 ? 0.4791 0.3354 0.4328 0.0209  -0.0044 -0.0099 151  VAL A CG1 
2652 C CG2 . VAL A 348 ? 0.4090 0.2609 0.4005 0.0170  0.0017  0.0002  151  VAL A CG2 
2653 N N   . ILE A 349 ? 0.5709 0.4371 0.5476 0.0279  -0.0286 -0.0463 152  ILE A N   
2654 C CA  . ILE A 349 ? 0.5658 0.4408 0.5237 0.0332  -0.0355 -0.0549 152  ILE A CA  
2655 C C   . ILE A 349 ? 0.5498 0.4309 0.5288 0.0355  -0.0457 -0.0666 152  ILE A C   
2656 O O   . ILE A 349 ? 0.5643 0.4508 0.5340 0.0382  -0.0494 -0.0666 152  ILE A O   
2657 C CB  . ILE A 349 ? 0.5696 0.4505 0.5110 0.0377  -0.0377 -0.0637 152  ILE A CB  
2658 C CG1 . ILE A 349 ? 0.5704 0.4480 0.4865 0.0360  -0.0282 -0.0512 152  ILE A CG1 
2659 C CG2 . ILE A 349 ? 0.5459 0.4406 0.4752 0.0452  -0.0474 -0.0762 152  ILE A CG2 
2660 C CD1 . ILE A 349 ? 0.5482 0.4306 0.4528 0.0388  -0.0273 -0.0570 152  ILE A CD1 
2661 N N   . ASN A 350 ? 0.5008 0.3812 0.5109 0.0347  -0.0514 -0.0775 153  ASN A N   
2662 C CA  . ASN A 350 ? 0.5058 0.3924 0.5415 0.0365  -0.0621 -0.0904 153  ASN A CA  
2663 C C   . ASN A 350 ? 0.5150 0.3993 0.5647 0.0321  -0.0584 -0.0794 153  ASN A C   
2664 O O   . ASN A 350 ? 0.5333 0.4252 0.5880 0.0350  -0.0661 -0.0864 153  ASN A O   
2665 C CB  . ASN A 350 ? 0.5667 0.4509 0.6403 0.0353  -0.0683 -0.1032 153  ASN A CB  
2666 C CG  . ASN A 350 ? 0.5827 0.4736 0.6469 0.0420  -0.0757 -0.1208 153  ASN A CG  
2667 O OD1 . ASN A 350 ? 0.6263 0.5262 0.6544 0.0479  -0.0760 -0.1230 153  ASN A OD1 
2668 N ND2 . ASN A 350 ? 0.5418 0.4292 0.6383 0.0414  -0.0808 -0.1321 153  ASN A ND2 
2669 N N   . ALA A 351 ? 0.4985 0.3745 0.5555 0.0260  -0.0470 -0.0628 154  ALA A N   
2670 C CA  . ALA A 351 ? 0.5098 0.3864 0.5794 0.0227  -0.0423 -0.0525 154  ALA A CA  
2671 C C   . ALA A 351 ? 0.5487 0.4284 0.5872 0.0259  -0.0406 -0.0473 154  ALA A C   
2672 O O   . ALA A 351 ? 0.5446 0.4293 0.5914 0.0269  -0.0438 -0.0481 154  ALA A O   
2673 C CB  . ALA A 351 ? 0.4478 0.3182 0.5301 0.0170  -0.0297 -0.0355 154  ALA A CB  
2674 N N   . ALA A 352 ? 0.5484 0.4250 0.5543 0.0276  -0.0361 -0.0419 155  ALA A N   
2675 C CA  . ALA A 352 ? 0.5342 0.4122 0.5149 0.0304  -0.0350 -0.0364 155  ALA A CA  
2676 C C   . ALA A 352 ? 0.5941 0.4806 0.5681 0.0366  -0.0465 -0.0468 155  ALA A C   
2677 O O   . ALA A 352 ? 0.6093 0.4986 0.5792 0.0389  -0.0485 -0.0437 155  ALA A O   
2678 C CB  . ALA A 352 ? 0.4841 0.3572 0.4363 0.0304  -0.0284 -0.0290 155  ALA A CB  
2679 N N   . SER A 353 ? 0.6052 0.4978 0.5786 0.0403  -0.0547 -0.0599 156  SER A N   
2680 C CA  . SER A 353 ? 0.5702 0.4745 0.5330 0.0480  -0.0658 -0.0702 156  SER A CA  
2681 C C   . SER A 353 ? 0.6204 0.5319 0.6127 0.0496  -0.0764 -0.0829 156  SER A C   
2682 O O   . SER A 353 ? 0.6764 0.5994 0.6616 0.0567  -0.0867 -0.0912 156  SER A O   
2683 C CB  . SER A 353 ? 0.5592 0.4706 0.5049 0.0530  -0.0695 -0.0795 156  SER A CB  
2684 O OG  . SER A 353 ? 0.5759 0.4905 0.5478 0.0534  -0.0769 -0.0965 156  SER A OG  
2685 N N   . GLY A 354 ? 0.6053 0.5118 0.6320 0.0434  -0.0745 -0.0845 157  GLY A N   
2686 C CA  . GLY A 354 ? 0.5845 0.4981 0.6454 0.0440  -0.0848 -0.0972 157  GLY A CA  
2687 C C   . GLY A 354 ? 0.5674 0.4864 0.6506 0.0464  -0.0959 -0.1176 157  GLY A C   
2688 O O   . GLY A 354 ? 0.5986 0.5234 0.7156 0.0464  -0.1053 -0.1300 157  GLY A O   
2689 N N   . ARG A 355 ? 0.5535 0.4718 0.6212 0.0487  -0.0956 -0.1229 158  ARG A N   
2690 C CA  . ARG A 355 ? 0.5726 0.4968 0.6633 0.0521  -0.1071 -0.1452 158  ARG A CA  
2691 C C   . ARG A 355 ? 0.5844 0.4994 0.7264 0.0440  -0.1066 -0.1466 158  ARG A C   
2692 O O   . ARG A 355 ? 0.5856 0.5064 0.7622 0.0458  -0.1191 -0.1660 158  ARG A O   
2693 C CB  . ARG A 355 ? 0.5294 0.4541 0.5956 0.0558  -0.1049 -0.1490 158  ARG A CB  
2694 N N   . GLN A 356 ? 0.5805 0.4826 0.7294 0.0355  -0.0924 -0.1257 159  GLN A N   
2695 C CA  . GLN A 356 ? 0.5746 0.4693 0.7708 0.0275  -0.0890 -0.1202 159  GLN A CA  
2696 C C   . GLN A 356 ? 0.5818 0.4735 0.7773 0.0218  -0.0763 -0.0979 159  GLN A C   
2697 O O   . GLN A 356 ? 0.5702 0.4610 0.7281 0.0230  -0.0683 -0.0856 159  GLN A O   
2698 C CB  . GLN A 356 ? 0.5429 0.4266 0.7521 0.0239  -0.0835 -0.1159 159  GLN A CB  
2699 C CG  . GLN A 356 ? 0.5220 0.4089 0.7268 0.0304  -0.0942 -0.1374 159  GLN A CG  
2700 C CD  . GLN A 356 ? 0.5215 0.3968 0.7406 0.0271  -0.0885 -0.1318 159  GLN A CD  
2701 O OE1 . GLN A 356 ? 0.5439 0.4143 0.7317 0.0271  -0.0788 -0.1194 159  GLN A OE1 
2702 N NE2 . GLN A 356 ? 0.5382 0.4087 0.8079 0.0242  -0.0949 -0.1408 159  GLN A NE2 
2703 N N   . THR A 357 ? 0.5742 0.4650 0.8145 0.0155  -0.0741 -0.0928 160  THR A N   
2704 C CA  . THR A 357 ? 0.5372 0.4266 0.7815 0.0099  -0.0596 -0.0701 160  THR A CA  
2705 C C   . THR A 357 ? 0.5092 0.3894 0.7398 0.0067  -0.0457 -0.0515 160  THR A C   
2706 O O   . THR A 357 ? 0.5380 0.4112 0.7691 0.0070  -0.0475 -0.0556 160  THR A O   
2707 C CB  . THR A 357 ? 0.5311 0.4243 0.8312 0.0041  -0.0603 -0.0688 160  THR A CB  
2708 O OG1 . THR A 357 ? 0.5333 0.4187 0.8706 -0.0006 -0.0599 -0.0677 160  THR A OG1 
2709 C CG2 . THR A 357 ? 0.5153 0.4183 0.8340 0.0077  -0.0763 -0.0903 160  THR A CG2 
2710 N N   . VAL A 358 ? 1.0627 0.5482 0.9889 0.3569  -0.1627 -0.0329 161  VAL A N   
2711 C CA  . VAL A 358 ? 0.9993 0.4745 0.9029 0.3398  -0.1357 -0.0374 161  VAL A CA  
2712 C C   . VAL A 358 ? 0.9229 0.4622 0.8820 0.3308  -0.1222 -0.0394 161  VAL A C   
2713 O O   . VAL A 358 ? 0.8992 0.4302 0.8304 0.3052  -0.1151 -0.0377 161  VAL A O   
2714 C CB  . VAL A 358 ? 1.0387 0.4948 0.9377 0.3595  -0.1133 -0.0474 161  VAL A CB  
2715 C CG1 . VAL A 358 ? 1.0229 0.4780 0.9059 0.3448  -0.0851 -0.0542 161  VAL A CG1 
2716 C CG2 . VAL A 358 ? 1.1184 0.4999 0.9475 0.3616  -0.1275 -0.0451 161  VAL A CG2 
2717 N N   . ASP A 359 ? 0.8923 0.4973 0.9328 0.3500  -0.1199 -0.0425 162  ASP A N   
2718 C CA  . ASP A 359 ? 0.8207 0.4893 0.9181 0.3402  -0.1070 -0.0444 162  ASP A CA  
2719 C C   . ASP A 359 ? 0.7896 0.4567 0.8657 0.3137  -0.1290 -0.0365 162  ASP A C   
2720 O O   . ASP A 359 ? 0.7537 0.4243 0.8173 0.2937  -0.1175 -0.0367 162  ASP A O   
2721 C CB  . ASP A 359 ? 0.7987 0.5389 0.9897 0.3612  -0.1028 -0.0475 162  ASP A CB  
2722 C CG  . ASP A 359 ? 0.8731 0.6262 1.0964 0.3852  -0.0680 -0.0553 162  ASP A CG  
2723 O OD1 . ASP A 359 ? 0.8925 0.6099 1.0722 0.3820  -0.0434 -0.0607 162  ASP A OD1 
2724 O OD2 . ASP A 359 ? 0.8700 0.6670 1.1593 0.4070  -0.0649 -0.0563 162  ASP A OD2 
2725 N N   . GLU A 360 ? 0.8395 0.4982 0.9076 0.3142  -0.1607 -0.0298 163  GLU A N   
2726 C CA  . GLU A 360 ? 0.8203 0.4681 0.8575 0.2897  -0.1804 -0.0217 163  GLU A CA  
2727 C C   . GLU A 360 ? 0.8152 0.4054 0.7765 0.2651  -0.1710 -0.0168 163  GLU A C   
2728 O O   . GLU A 360 ? 0.7658 0.3749 0.7250 0.2386  -0.1607 -0.0142 163  GLU A O   
2729 C CB  . GLU A 360 ? 0.9045 0.5270 0.9160 0.2954  -0.2140 -0.0156 163  GLU A CB  
2730 C CG  . GLU A 360 ? 0.9413 0.6163 1.0214 0.3143  -0.2330 -0.0196 163  GLU A CG  
2731 C CD  . GLU A 360 ? 1.0358 0.6687 1.0756 0.3258  -0.2659 -0.0157 163  GLU A CD  
2732 O OE1 . GLU A 360 ? 1.0727 0.7201 1.1489 0.3511  -0.2749 -0.0203 163  GLU A OE1 
2733 O OE2 . GLU A 360 ? 1.0848 0.6669 1.0532 0.3093  -0.2809 -0.0079 163  GLU A OE2 
2734 N N   . ALA A 361 ? 0.8922 0.4206 0.7931 0.2658  -0.1698 -0.0150 164  ALA A N   
2735 C CA  . ALA A 361 ? 0.9277 0.3995 0.7569 0.2375  -0.1640 -0.0092 164  ALA A CA  
2736 C C   . ALA A 361 ? 0.8464 0.3369 0.6835 0.2200  -0.1388 -0.0145 164  ALA A C   
2737 O O   . ALA A 361 ? 0.8950 0.3910 0.7138 0.1868  -0.1325 -0.0091 164  ALA A O   
2738 C CB  . ALA A 361 ? 1.0122 0.4219 0.7866 0.2425  -0.1659 -0.0086 164  ALA A CB  
2739 N N   . LEU A 362 ? 0.8370 0.3494 0.7048 0.2377  -0.1199 -0.0249 165  LEU A N   
2740 C CA  . LEU A 362 ? 0.8816 0.4145 0.7496 0.2178  -0.0940 -0.0299 165  LEU A CA  
2741 C C   . LEU A 362 ? 0.8098 0.4161 0.7317 0.2032  -0.0839 -0.0286 165  LEU A C   
2742 O O   . LEU A 362 ? 0.7020 0.3206 0.6126 0.1767  -0.0714 -0.0280 165  LEU A O   
2743 C CB  . LEU A 362 ? 0.9129 0.4335 0.7824 0.2432  -0.0746 -0.0415 165  LEU A CB  
2744 C CG  . LEU A 362 ? 0.9069 0.3528 0.7138 0.2489  -0.0800 -0.0439 165  LEU A CG  
2745 C CD1 . LEU A 362 ? 0.9354 0.3787 0.7467 0.2721  -0.0577 -0.0554 165  LEU A CD1 
2746 C CD2 . LEU A 362 ? 0.9216 0.3224 0.6692 0.2136  -0.0831 -0.0408 165  LEU A CD2 
2747 N N   . LYS A 363 ? 0.8016 0.4563 0.7832 0.2195  -0.0914 -0.0284 166  LYS A N   
2748 C CA  . LYS A 363 ? 0.7097 0.4285 0.7394 0.2029  -0.0839 -0.0267 166  LYS A CA  
2749 C C   . LYS A 363 ? 0.6724 0.3829 0.6690 0.1711  -0.0941 -0.0182 166  LYS A C   
2750 O O   . LYS A 363 ? 0.6408 0.3742 0.6387 0.1486  -0.0797 -0.0176 166  LYS A O   
2751 C CB  . LYS A 363 ? 0.7160 0.4842 0.8170 0.2233  -0.0957 -0.0284 166  LYS A CB  
2752 N N   . ASP A 364 ? 0.7450 0.4173 0.7070 0.1706  -0.1179 -0.0114 167  ASP A N   
2753 C CA  . ASP A 364 ? 0.7374 0.3947 0.6621 0.1419  -0.1235 -0.0029 167  ASP A CA  
2754 C C   . ASP A 364 ? 0.7453 0.3804 0.6330 0.1168  -0.1062 -0.0027 167  ASP A C   
2755 O O   . ASP A 364 ? 0.6707 0.3264 0.5584 0.0919  -0.0985 0.0003  167  ASP A O   
2756 C CB  . ASP A 364 ? 0.7546 0.3576 0.6329 0.1480  -0.1479 0.0048  167  ASP A CB  
2757 C CG  . ASP A 364 ? 0.7533 0.3788 0.6619 0.1651  -0.1719 0.0056  167  ASP A CG  
2758 O OD1 . ASP A 364 ? 0.6995 0.3860 0.6715 0.1702  -0.1685 -0.0001 167  ASP A OD1 
2759 O OD2 . ASP A 364 ? 0.8121 0.3916 0.6797 0.1731  -0.1951 0.0119  167  ASP A OD2 
2760 N N   . ALA A 365 ? 0.7841 0.3746 0.6399 0.1237  -0.1023 -0.0065 168  ALA A N   
2761 C CA  . ALA A 365 ? 0.8143 0.3809 0.6367 0.0994  -0.0911 -0.0078 168  ALA A CA  
2762 C C   . ALA A 365 ? 0.7625 0.3758 0.6156 0.0921  -0.0738 -0.0142 168  ALA A C   
2763 O O   . ALA A 365 ? 0.7385 0.3559 0.5808 0.0666  -0.0686 -0.0137 168  ALA A O   
2764 C CB  . ALA A 365 ? 0.7718 0.2735 0.5497 0.1096  -0.0935 -0.0120 168  ALA A CB  
2765 N N   . GLN A 366 ? 0.7320 0.3774 0.6223 0.1149  -0.0643 -0.0204 169  GLN A N   
2766 C CA  . GLN A 366 ? 0.7249 0.4119 0.6406 0.1087  -0.0465 -0.0246 169  GLN A CA  
2767 C C   . GLN A 366 ? 0.6558 0.3877 0.5985 0.0889  -0.0479 -0.0187 169  GLN A C   
2768 O O   . GLN A 366 ? 0.6289 0.3764 0.5695 0.0713  -0.0399 -0.0193 169  GLN A O   
2769 C CB  . GLN A 366 ? 0.7499 0.4635 0.7039 0.1359  -0.0316 -0.0306 169  GLN A CB  
2770 C CG  . GLN A 366 ? 0.7074 0.4560 0.6807 0.1305  -0.0101 -0.0334 169  GLN A CG  
2771 C CD  . GLN A 366 ? 0.7581 0.4679 0.6839 0.1305  0.0020  -0.0404 169  GLN A CD  
2772 O OE1 . GLN A 366 ? 0.7744 0.4358 0.6628 0.1403  -0.0021 -0.0451 169  GLN A OE1 
2773 N NE2 . GLN A 366 ? 0.7298 0.4567 0.6523 0.1193  0.0152  -0.0414 169  GLN A NE2 
2774 N N   . THR A 367 ? 0.6403 0.3906 0.6065 0.0934  -0.0599 -0.0137 170  THR A N   
2775 C CA  . THR A 367 ? 0.6077 0.3944 0.5940 0.0761  -0.0618 -0.0090 170  THR A CA  
2776 C C   . THR A 367 ? 0.5952 0.3605 0.5451 0.0504  -0.0641 -0.0041 170  THR A C   
2777 O O   . THR A 367 ? 0.5042 0.2967 0.4646 0.0335  -0.0571 -0.0033 170  THR A O   
2778 C CB  . THR A 367 ? 0.6249 0.4274 0.6369 0.0874  -0.0781 -0.0061 170  THR A CB  
2779 O OG1 . THR A 367 ? 0.6035 0.4366 0.6651 0.1097  -0.0740 -0.0116 170  THR A OG1 
2780 C CG2 . THR A 367 ? 0.6187 0.4516 0.6444 0.0703  -0.0805 -0.0025 170  THR A CG2 
2781 N N   . GLY A 368 ? 0.6313 0.3464 0.5392 0.0470  -0.0717 -0.0013 171  GLY A N   
2782 C CA  . GLY A 368 ? 0.6350 0.3309 0.5146 0.0207  -0.0699 0.0034  171  GLY A CA  
2783 C C   . GLY A 368 ? 0.6309 0.3320 0.5096 0.0049  -0.0605 -0.0019 171  GLY A C   
2784 O O   . GLY A 368 ? 0.6206 0.3430 0.5081 -0.0158 -0.0558 -0.0002 171  GLY A O   
2785 N N   . SER A 369 ? 0.6387 0.3194 0.5060 0.0157  -0.0590 -0.0091 172  SER A N   
2786 C CA  . SER A 369 ? 0.6700 0.3488 0.5294 0.0020  -0.0552 -0.0155 172  SER A CA  
2787 C C   . SER A 369 ? 0.6950 0.4241 0.5859 0.0004  -0.0473 -0.0177 172  SER A C   
2788 O O   . SER A 369 ? 0.6921 0.4276 0.5812 -0.0151 -0.0484 -0.0210 172  SER A O   
2789 C CB  . SER A 369 ? 0.6860 0.3247 0.5171 0.0168  -0.0554 -0.0237 172  SER A CB  
2790 O OG  . SER A 369 ? 0.7369 0.3274 0.5404 0.0273  -0.0625 -0.0218 172  SER A OG  
2791 N N   . GLU A 370 ? 0.6942 0.4565 0.6142 0.0162  -0.0411 -0.0163 173  GLU A N   
2792 C CA  . GLU A 370 ? 0.6513 0.4546 0.5975 0.0156  -0.0322 -0.0174 173  GLU A CA  
2793 C C   . GLU A 370 ? 0.6244 0.4613 0.5938 0.0020  -0.0341 -0.0117 173  GLU A C   
2794 O O   . GLU A 370 ? 0.6030 0.4701 0.5909 -0.0010 -0.0283 -0.0121 173  GLU A O   
2795 C CB  . GLU A 370 ? 0.6386 0.4591 0.6077 0.0377  -0.0212 -0.0192 173  GLU A CB  
2796 C CG  . GLU A 370 ? 0.7380 0.5380 0.6866 0.0504  -0.0093 -0.0262 173  GLU A CG  
2797 C CD  . GLU A 370 ? 0.8104 0.6255 0.7861 0.0736  0.0064  -0.0277 173  GLU A CD  
2798 O OE1 . GLU A 370 ? 0.8253 0.6663 0.8395 0.0802  0.0025  -0.0243 173  GLU A OE1 
2799 O OE2 . GLU A 370 ? 0.8480 0.6498 0.8080 0.0853  0.0230  -0.0328 173  GLU A OE2 
2800 N N   . LEU A 371 ? 0.6441 0.4707 0.6068 -0.0056 -0.0411 -0.0063 174  LEU A N   
2801 C CA  . LEU A 371 ? 0.5994 0.4524 0.5789 -0.0132 -0.0412 -0.0015 174  LEU A CA  
2802 C C   . LEU A 371 ? 0.5450 0.4228 0.5359 -0.0287 -0.0358 -0.0025 174  LEU A C   
2803 O O   . LEU A 371 ? 0.5095 0.4177 0.5219 -0.0278 -0.0323 -0.0020 174  LEU A O   
2804 C CB  . LEU A 371 ? 0.6214 0.4469 0.5772 -0.0193 -0.0475 0.0046  174  LEU A CB  
2805 C CG  . LEU A 371 ? 0.5757 0.4178 0.5382 -0.0216 -0.0489 0.0089  174  LEU A CG  
2806 C CD1 . LEU A 371 ? 0.4838 0.3540 0.4764 -0.0062 -0.0534 0.0064  174  LEU A CD1 
2807 C CD2 . LEU A 371 ? 0.6465 0.4456 0.5710 -0.0221 -0.0563 0.0155  174  LEU A CD2 
2808 N N   . TYR A 372 ? 0.5514 0.4156 0.5302 -0.0431 -0.0367 -0.0044 175  TYR A N   
2809 C CA  . TYR A 372 ? 0.5840 0.4747 0.5804 -0.0566 -0.0344 -0.0057 175  TYR A CA  
2810 C C   . TYR A 372 ? 0.5523 0.4649 0.5615 -0.0475 -0.0337 -0.0101 175  TYR A C   
2811 O O   . TYR A 372 ? 0.5378 0.4789 0.5665 -0.0476 -0.0303 -0.0090 175  TYR A O   
2812 C CB  . TYR A 372 ? 0.6383 0.5132 0.6279 -0.0749 -0.0384 -0.0079 175  TYR A CB  
2813 C CG  . TYR A 372 ? 0.6668 0.5753 0.6848 -0.0869 -0.0382 -0.0104 175  TYR A CG  
2814 C CD1 . TYR A 372 ? 0.6576 0.5772 0.6821 -0.0826 -0.0466 -0.0170 175  TYR A CD1 
2815 C CD2 . TYR A 372 ? 0.6845 0.6118 0.7208 -0.0999 -0.0291 -0.0063 175  TYR A CD2 
2816 C CE1 . TYR A 372 ? 0.6337 0.5844 0.6867 -0.0903 -0.0503 -0.0197 175  TYR A CE1 
2817 C CE2 . TYR A 372 ? 0.6667 0.6293 0.7363 -0.1077 -0.0285 -0.0094 175  TYR A CE2 
2818 C CZ  . TYR A 372 ? 0.6372 0.6122 0.7170 -0.1023 -0.0412 -0.0163 175  TYR A CZ  
2819 O OH  . TYR A 372 ? 0.6438 0.6523 0.7581 -0.1076 -0.0448 -0.0199 175  TYR A OH  
2820 N N   . ARG A 373 ? 0.5459 0.4396 0.5385 -0.0387 -0.0358 -0.0148 176  ARG A N   
2821 C CA  . ARG A 373 ? 0.5635 0.4677 0.5569 -0.0297 -0.0329 -0.0178 176  ARG A CA  
2822 C C   . ARG A 373 ? 0.5252 0.4540 0.5395 -0.0196 -0.0227 -0.0138 176  ARG A C   
2823 O O   . ARG A 373 ? 0.4938 0.4416 0.5186 -0.0195 -0.0202 -0.0131 176  ARG A O   
2824 C CB  . ARG A 373 ? 0.6253 0.4963 0.5878 -0.0190 -0.0328 -0.0232 176  ARG A CB  
2825 C CG  . ARG A 373 ? 0.7264 0.5957 0.6750 -0.0124 -0.0312 -0.0264 176  ARG A CG  
2826 C CD  . ARG A 373 ? 0.8170 0.6987 0.7720 -0.0256 -0.0460 -0.0286 176  ARG A CD  
2827 N NE  . ARG A 373 ? 0.8866 0.7759 0.8362 -0.0182 -0.0451 -0.0285 176  ARG A NE  
2828 C CZ  . ARG A 373 ? 0.9257 0.8445 0.9002 -0.0170 -0.0381 -0.0232 176  ARG A CZ  
2829 N NH1 . ARG A 373 ? 0.9660 0.8835 0.9289 -0.0098 -0.0378 -0.0225 176  ARG A NH1 
2830 N NH2 . ARG A 373 ? 0.9065 0.8500 0.9115 -0.0225 -0.0323 -0.0189 176  ARG A NH2 
2831 N N   . GLN A 374 ? 0.5370 0.4641 0.5588 -0.0111 -0.0190 -0.0114 177  GLN A N   
2832 C CA  . GLN A 374 ? 0.5366 0.4867 0.5837 -0.0029 -0.0116 -0.0090 177  GLN A CA  
2833 C C   . GLN A 374 ? 0.4700 0.4426 0.5337 -0.0120 -0.0150 -0.0059 177  GLN A C   
2834 O O   . GLN A 374 ? 0.4563 0.4467 0.5345 -0.0111 -0.0099 -0.0052 177  GLN A O   
2835 C CB  . GLN A 374 ? 0.6143 0.5595 0.6720 0.0090  -0.0117 -0.0086 177  GLN A CB  
2836 C CG  . GLN A 374 ? 0.6623 0.6354 0.7566 0.0150  -0.0071 -0.0070 177  GLN A CG  
2837 C CD  . GLN A 374 ? 0.7472 0.7220 0.8618 0.0312  -0.0003 -0.0089 177  GLN A CD  
2838 O OE1 . GLN A 374 ? 0.7671 0.7640 0.9133 0.0357  0.0113  -0.0088 177  GLN A OE1 
2839 N NE2 . GLN A 374 ? 0.7766 0.7275 0.8755 0.0401  -0.0063 -0.0107 177  GLN A NE2 
2840 N N   . SER A 375 ? 0.4607 0.4279 0.5175 -0.0211 -0.0218 -0.0042 178  SER A N   
2841 C CA  . SER A 375 ? 0.4420 0.4251 0.5074 -0.0286 -0.0221 -0.0022 178  SER A CA  
2842 C C   . SER A 375 ? 0.4432 0.4428 0.5159 -0.0337 -0.0190 -0.0040 178  SER A C   
2843 O O   . SER A 375 ? 0.3993 0.4149 0.4842 -0.0324 -0.0165 -0.0035 178  SER A O   
2844 C CB  . SER A 375 ? 0.4197 0.3871 0.4688 -0.0375 -0.0248 0.0006  178  SER A CB  
2845 O OG  . SER A 375 ? 0.4584 0.4034 0.4945 -0.0302 -0.0312 0.0024  178  SER A OG  
2846 N N   . LEU A 376 ? 0.4652 0.4580 0.5298 -0.0392 -0.0218 -0.0066 179  LEU A N   
2847 C CA  . LEU A 376 ? 0.4442 0.4522 0.5175 -0.0413 -0.0239 -0.0090 179  LEU A CA  
2848 C C   . LEU A 376 ? 0.4688 0.4798 0.5411 -0.0302 -0.0205 -0.0088 179  LEU A C   
2849 O O   . LEU A 376 ? 0.4993 0.5244 0.5813 -0.0287 -0.0201 -0.0084 179  LEU A O   
2850 C CB  . LEU A 376 ? 0.4064 0.4041 0.4718 -0.0480 -0.0329 -0.0133 179  LEU A CB  
2851 C CG  . LEU A 376 ? 0.3849 0.3975 0.4608 -0.0485 -0.0413 -0.0170 179  LEU A CG  
2852 C CD1 . LEU A 376 ? 0.3686 0.4113 0.4745 -0.0539 -0.0375 -0.0161 179  LEU A CD1 
2853 C CD2 . LEU A 376 ? 0.4045 0.4034 0.4726 -0.0558 -0.0562 -0.0230 179  LEU A CD2 
2854 N N   . GLU A 377 ? 0.4506 0.4459 0.5103 -0.0221 -0.0159 -0.0087 180  GLU A N   
2855 C CA  . GLU A 377 ? 0.4784 0.4722 0.5349 -0.0133 -0.0073 -0.0072 180  GLU A CA  
2856 C C   . GLU A 377 ? 0.4285 0.4409 0.5076 -0.0138 -0.0024 -0.0039 180  GLU A C   
2857 O O   . GLU A 377 ? 0.4305 0.4459 0.5091 -0.0122 -0.0003 -0.0026 180  GLU A O   
2858 C CB  . GLU A 377 ? 0.5513 0.5282 0.5970 -0.0043 0.0028  -0.0074 180  GLU A CB  
2859 C CG  . GLU A 377 ? 0.6654 0.6328 0.6993 0.0037  0.0169  -0.0054 180  GLU A CG  
2860 C CD  . GLU A 377 ? 0.7621 0.7061 0.7583 0.0061  0.0104  -0.0076 180  GLU A CD  
2861 O OE1 . GLU A 377 ? 0.7808 0.7229 0.7689 0.0077  0.0114  -0.0049 180  GLU A OE1 
2862 O OE2 . GLU A 377 ? 0.7948 0.7185 0.7671 0.0068  0.0018  -0.0125 180  GLU A OE2 
2863 N N   . ILE A 378 ? 0.3983 0.4186 0.4935 -0.0155 -0.0031 -0.0030 181  ILE A N   
2864 C CA  . ILE A 378 ? 0.3673 0.4004 0.4812 -0.0167 -0.0023 -0.0016 181  ILE A CA  
2865 C C   . ILE A 378 ? 0.3748 0.4152 0.4868 -0.0214 -0.0065 -0.0023 181  ILE A C   
2866 O O   . ILE A 378 ? 0.3431 0.3872 0.4599 -0.0202 -0.0041 -0.0017 181  ILE A O   
2867 C CB  . ILE A 378 ? 0.3626 0.3976 0.4886 -0.0163 -0.0082 -0.0017 181  ILE A CB  
2868 C CG1 . ILE A 378 ? 0.3302 0.3620 0.4660 -0.0084 -0.0035 -0.0019 181  ILE A CG1 
2869 C CG2 . ILE A 378 ? 0.3564 0.4008 0.4994 -0.0183 -0.0117 -0.0018 181  ILE A CG2 
2870 C CD1 . ILE A 378 ? 0.2844 0.3101 0.4223 -0.0050 -0.0148 -0.0025 181  ILE A CD1 
2871 N N   . ILE A 379 ? 0.3579 0.3989 0.4639 -0.0266 -0.0109 -0.0035 182  ILE A N   
2872 C CA  . ILE A 379 ? 0.3550 0.4056 0.4644 -0.0297 -0.0107 -0.0047 182  ILE A CA  
2873 C C   . ILE A 379 ? 0.3555 0.4135 0.4685 -0.0262 -0.0114 -0.0060 182  ILE A C   
2874 O O   . ILE A 379 ? 0.3672 0.4316 0.4855 -0.0230 -0.0101 -0.0068 182  ILE A O   
2875 C CB  . ILE A 379 ? 0.3439 0.3932 0.4484 -0.0375 -0.0102 -0.0048 182  ILE A CB  
2876 C CG1 . ILE A 379 ? 0.3740 0.4088 0.4664 -0.0381 -0.0119 -0.0028 182  ILE A CG1 
2877 C CG2 . ILE A 379 ? 0.2884 0.3515 0.4015 -0.0402 -0.0050 -0.0066 182  ILE A CG2 
2878 C CD1 . ILE A 379 ? 0.4036 0.4249 0.4809 -0.0462 -0.0100 -0.0008 182  ILE A CD1 
2879 N N   . SER A 380 ? 0.3286 0.3815 0.4347 -0.0252 -0.0157 -0.0069 183  SER A N   
2880 C CA  . SER A 380 ? 0.3553 0.4104 0.4600 -0.0198 -0.0215 -0.0084 183  SER A CA  
2881 C C   . SER A 380 ? 0.3816 0.4258 0.4767 -0.0117 -0.0169 -0.0053 183  SER A C   
2882 O O   . SER A 380 ? 0.3487 0.3954 0.4455 -0.0062 -0.0201 -0.0056 183  SER A O   
2883 C CB  . SER A 380 ? 0.3905 0.4361 0.4834 -0.0206 -0.0311 -0.0111 183  SER A CB  
2884 O OG  . SER A 380 ? 0.4186 0.4520 0.4948 -0.0114 -0.0381 -0.0113 183  SER A OG  
2885 N N   . ARG A 381 ? 0.3941 0.4254 0.4805 -0.0110 -0.0087 -0.0023 184  ARG A N   
2886 C CA  . ARG A 381 ? 0.3991 0.4184 0.4786 -0.0065 -0.0006 0.0017  184  ARG A CA  
2887 C C   . ARG A 381 ? 0.3667 0.3943 0.4619 -0.0085 0.0002  0.0018  184  ARG A C   
2888 O O   . ARG A 381 ? 0.4177 0.4355 0.5052 -0.0042 0.0007  0.0034  184  ARG A O   
2889 C CB  . ARG A 381 ? 0.4113 0.4208 0.4892 -0.0066 0.0127  0.0048  184  ARG A CB  
2890 C CG  . ARG A 381 ? 0.4741 0.4610 0.5214 -0.0005 0.0169  0.0056  184  ARG A CG  
2891 C CD  . ARG A 381 ? 0.5377 0.5208 0.5901 0.0005  0.0323  0.0067  184  ARG A CD  
2892 N NE  . ARG A 381 ? 0.6047 0.5610 0.6205 0.0078  0.0372  0.0059  184  ARG A NE  
2893 C CZ  . ARG A 381 ? 0.6428 0.5735 0.6311 0.0136  0.0541  0.0100  184  ARG A CZ  
2894 N NH1 . ARG A 381 ? 0.6788 0.6094 0.6771 0.0109  0.0680  0.0160  184  ARG A NH1 
2895 N NH2 . ARG A 381 ? 0.6423 0.5423 0.5883 0.0215  0.0576  0.0082  184  ARG A NH2 
2896 N N   . TYR A 382 ? 0.3051 0.3449 0.4157 -0.0140 -0.0013 -0.0004 185  TYR A N   
2897 C CA  . TYR A 382 ? 0.3496 0.3904 0.4674 -0.0153 -0.0022 -0.0017 185  TYR A CA  
2898 C C   . TYR A 382 ? 0.3719 0.4158 0.4855 -0.0099 -0.0054 -0.0044 185  TYR A C   
2899 O O   . TYR A 382 ? 0.3623 0.3967 0.4721 -0.0059 -0.0048 -0.0045 185  TYR A O   
2900 C CB  . TYR A 382 ? 0.3391 0.3847 0.4644 -0.0205 -0.0060 -0.0040 185  TYR A CB  
2901 C CG  . TYR A 382 ? 0.3378 0.3770 0.4632 -0.0216 -0.0096 -0.0067 185  TYR A CG  
2902 C CD1 . TYR A 382 ? 0.3680 0.3986 0.5014 -0.0237 -0.0089 -0.0059 185  TYR A CD1 
2903 C CD2 . TYR A 382 ? 0.3226 0.3596 0.4368 -0.0213 -0.0123 -0.0103 185  TYR A CD2 
2904 C CE1 . TYR A 382 ? 0.3540 0.3734 0.4848 -0.0257 -0.0150 -0.0097 185  TYR A CE1 
2905 C CE2 . TYR A 382 ? 0.3390 0.3630 0.4445 -0.0210 -0.0164 -0.0140 185  TYR A CE2 
2906 C CZ  . TYR A 382 ? 0.3714 0.3860 0.4853 -0.0232 -0.0199 -0.0144 185  TYR A CZ  
2907 O OH  . TYR A 382 ? 0.4015 0.3985 0.5040 -0.0236 -0.0267 -0.0194 185  TYR A OH  
2908 N N   . LEU A 383 ? 0.3620 0.4194 0.4795 -0.0098 -0.0082 -0.0069 186  LEU A N   
2909 C CA  . LEU A 383 ? 0.3463 0.4138 0.4707 -0.0035 -0.0097 -0.0102 186  LEU A CA  
2910 C C   . LEU A 383 ? 0.3601 0.4181 0.4774 0.0068  -0.0153 -0.0091 186  LEU A C   
2911 O O   . LEU A 383 ? 0.3170 0.3736 0.4361 0.0153  -0.0159 -0.0111 186  LEU A O   
2912 C CB  . LEU A 383 ? 0.2775 0.3648 0.4166 -0.0075 -0.0109 -0.0129 186  LEU A CB  
2913 C CG  . LEU A 383 ? 0.2730 0.3681 0.4170 -0.0131 -0.0011 -0.0149 186  LEU A CG  
2914 C CD1 . LEU A 383 ? 0.2426 0.3207 0.3689 -0.0190 0.0010  -0.0126 186  LEU A CD1 
2915 C CD2 . LEU A 383 ? 0.2461 0.3596 0.4079 -0.0211 0.0012  -0.0162 186  LEU A CD2 
2916 N N   . ARG A 384 ? 0.3451 0.3924 0.4495 0.0078  -0.0197 -0.0061 187  ARG A N   
2917 C CA  . ARG A 384 ? 0.3572 0.3884 0.4450 0.0188  -0.0275 -0.0045 187  ARG A CA  
2918 C C   . ARG A 384 ? 0.3763 0.3805 0.4455 0.0217  -0.0200 0.0006  187  ARG A C   
2919 O O   . ARG A 384 ? 0.4062 0.3953 0.4632 0.0326  -0.0256 0.0015  187  ARG A O   
2920 C CB  . ARG A 384 ? 0.3523 0.3720 0.4214 0.0193  -0.0345 -0.0034 187  ARG A CB  
2921 C CG  . ARG A 384 ? 0.3684 0.4110 0.4568 0.0144  -0.0447 -0.0090 187  ARG A CG  
2922 C CD  . ARG A 384 ? 0.4210 0.4448 0.4842 0.0166  -0.0567 -0.0099 187  ARG A CD  
2923 N NE  . ARG A 384 ? 0.4850 0.4933 0.5302 0.0099  -0.0452 -0.0074 187  ARG A NE  
2924 C CZ  . ARG A 384 ? 0.5361 0.5143 0.5483 0.0146  -0.0355 -0.0025 187  ARG A CZ  
2925 N NH1 . ARG A 384 ? 0.5767 0.5320 0.5641 0.0240  -0.0359 0.0016  187  ARG A NH1 
2926 N NH2 . ARG A 384 ? 0.5422 0.5110 0.5451 0.0106  -0.0236 -0.0013 187  ARG A NH2 
2927 N N   . GLU A 385 ? 0.3486 0.3455 0.4172 0.0122  -0.0083 0.0040  188  GLU A N   
2928 C CA  . GLU A 385 ? 0.3959 0.3688 0.4540 0.0111  -0.0001 0.0086  188  GLU A CA  
2929 C C   . GLU A 385 ? 0.4011 0.3749 0.4687 0.0124  -0.0027 0.0047  188  GLU A C   
2930 O O   . GLU A 385 ? 0.4306 0.3792 0.4835 0.0169  -0.0018 0.0071  188  GLU A O   
2931 C CB  . GLU A 385 ? 0.3851 0.3556 0.4511 -0.0002 0.0131  0.0123  188  GLU A CB  
2932 C CG  . GLU A 385 ? 0.3919 0.3837 0.4861 -0.0092 0.0121  0.0081  188  GLU A CG  
2933 C CD  . GLU A 385 ? 0.3997 0.3946 0.5119 -0.0182 0.0227  0.0109  188  GLU A CD  
2934 O OE1 . GLU A 385 ? 0.4094 0.3967 0.5125 -0.0168 0.0337  0.0152  188  GLU A OE1 
2935 O OE2 . GLU A 385 ? 0.4086 0.4127 0.5442 -0.0256 0.0194  0.0081  188  GLU A OE2 
2936 N N   . GLN A 386 ? 0.3667 0.3633 0.4522 0.0097  -0.0054 -0.0012 189  GLN A N   
2937 C CA  . GLN A 386 ? 0.4028 0.3963 0.4897 0.0131  -0.0066 -0.0063 189  GLN A CA  
2938 C C   . GLN A 386 ? 0.4530 0.4446 0.5353 0.0290  -0.0115 -0.0085 189  GLN A C   
2939 O O   . GLN A 386 ? 0.4482 0.4191 0.5196 0.0365  -0.0120 -0.0100 189  GLN A O   
2940 C CB  . GLN A 386 ? 0.3629 0.3751 0.4609 0.0077  -0.0059 -0.0113 189  GLN A CB  
2941 C CG  . GLN A 386 ? 0.3658 0.3745 0.4679 -0.0045 -0.0061 -0.0105 189  GLN A CG  
2942 C CD  . GLN A 386 ? 0.4237 0.4126 0.5196 -0.0074 -0.0093 -0.0139 189  GLN A CD  
2943 O OE1 . GLN A 386 ? 0.4328 0.4135 0.5162 -0.0014 -0.0102 -0.0197 189  GLN A OE1 
2944 N NE2 . GLN A 386 ? 0.4426 0.4215 0.5476 -0.0167 -0.0102 -0.0111 189  GLN A NE2 
2945 N N   . ALA A 387 ? 0.4384 0.4511 0.5312 0.0347  -0.0171 -0.0097 190  ALA A N   
2946 C CA  . ALA A 387 ? 0.4564 0.4745 0.5552 0.0513  -0.0250 -0.0131 190  ALA A CA  
2947 C C   . ALA A 387 ? 0.4975 0.4823 0.5696 0.0624  -0.0328 -0.0080 190  ALA A C   
2948 O O   . ALA A 387 ? 0.5047 0.4775 0.5723 0.0777  -0.0377 -0.0102 190  ALA A O   
2949 C CB  . ALA A 387 ? 0.4009 0.4522 0.5248 0.0520  -0.0320 -0.0164 190  ALA A CB  
2950 N N   . THR A 388 ? 0.4871 0.4528 0.5372 0.0565  -0.0330 -0.0011 191  THR A N   
2951 C CA  . THR A 388 ? 0.5179 0.4462 0.5337 0.0682  -0.0402 0.0047  191  THR A CA  
2952 C C   . THR A 388 ? 0.5345 0.4227 0.5244 0.0625  -0.0279 0.0116  191  THR A C   
2953 O O   . THR A 388 ? 0.5767 0.4267 0.5343 0.0735  -0.0323 0.0167  191  THR A O   
2954 C CB  . THR A 388 ? 0.4916 0.4108 0.4862 0.0676  -0.0463 0.0086  191  THR A CB  
2955 O OG1 . THR A 388 ? 0.5046 0.4227 0.4963 0.0510  -0.0300 0.0125  191  THR A OG1 
2956 C CG2 . THR A 388 ? 0.4099 0.3626 0.4289 0.0731  -0.0634 0.0014  191  THR A CG2 
2957 N N   . GLY A 389 ? 0.5010 0.3950 0.5044 0.0453  -0.0141 0.0120  192  GLY A N   
2958 C CA  . GLY A 389 ? 0.5262 0.3878 0.5157 0.0349  -0.0019 0.0181  192  GLY A CA  
2959 C C   . GLY A 389 ? 0.5896 0.4361 0.5656 0.0244  0.0121  0.0268  192  GLY A C   
2960 O O   . GLY A 389 ? 0.6113 0.4358 0.5849 0.0123  0.0260  0.0323  192  GLY A O   
2961 N N   . ALA A 390 ? 0.5798 0.4361 0.5474 0.0282  0.0103  0.0279  193  ALA A N   
2962 C CA  . ALA A 390 ? 0.5465 0.3817 0.4917 0.0225  0.0262  0.0359  193  ALA A CA  
2963 C C   . ALA A 390 ? 0.5289 0.3971 0.4946 0.0177  0.0275  0.0317  193  ALA A C   
2964 O O   . ALA A 390 ? 0.4755 0.3708 0.4554 0.0226  0.0120  0.0246  193  ALA A O   
2965 C CB  . ALA A 390 ? 0.5286 0.3196 0.4186 0.0370  0.0215  0.0423  193  ALA A CB  
2966 N N   . ALA A 391 ? 0.5240 0.3882 0.4925 0.0080  0.0478  0.0362  194  ALA A N   
2967 C CA  . ALA A 391 ? 0.5062 0.3975 0.4950 0.0040  0.0513  0.0324  194  ALA A CA  
2968 C C   . ALA A 391 ? 0.5646 0.4357 0.5128 0.0140  0.0493  0.0333  194  ALA A C   
2969 O O   . ALA A 391 ? 0.6177 0.4495 0.5187 0.0230  0.0489  0.0384  194  ALA A O   
2970 C CB  . ALA A 391 ? 0.4553 0.3560 0.4743 -0.0088 0.0734  0.0354  194  ALA A CB  
2971 N N   . ASP A 392 ? 0.5251 0.4174 0.4866 0.0130  0.0467  0.0281  195  ASP A N   
2972 C CA  . ASP A 392 ? 0.5240 0.3949 0.4464 0.0212  0.0438  0.0270  195  ASP A CA  
2973 C C   . ASP A 392 ? 0.5539 0.3989 0.4539 0.0208  0.0730  0.0331  195  ASP A C   
2974 O O   . ASP A 392 ? 0.5647 0.4311 0.5013 0.0131  0.0910  0.0333  195  ASP A O   
2975 C CB  . ASP A 392 ? 0.5410 0.4417 0.4871 0.0190  0.0299  0.0186  195  ASP A CB  
2976 C CG  . ASP A 392 ? 0.6032 0.4807 0.5088 0.0270  0.0174  0.0147  195  ASP A CG  
2977 O OD1 . ASP A 392 ? 0.6190 0.4545 0.4738 0.0347  0.0276  0.0186  195  ASP A OD1 
2978 O OD2 . ASP A 392 ? 0.6085 0.5073 0.5318 0.0246  -0.0021 0.0075  195  ASP A OD2 
2979 N N   . THR A 393 ? 0.6608 0.4584 0.5004 0.0300  0.0783  0.0378  196  THR A N   
2980 C CA  . THR A 393 ? 0.7634 0.5309 0.5759 0.0301  0.1124  0.0446  196  THR A CA  
2981 C C   . THR A 393 ? 0.8204 0.5852 0.6199 0.0354  0.1194  0.0391  196  THR A C   
2982 O O   . THR A 393 ? 0.8932 0.6335 0.6698 0.0379  0.1511  0.0435  196  THR A O   
2983 C CB  . THR A 393 ? 0.8500 0.5561 0.5899 0.0389  0.1188  0.0533  196  THR A CB  
2984 O OG1 . THR A 393 ? 0.8733 0.5567 0.5673 0.0521  0.0857  0.0481  196  THR A OG1 
2985 C CG2 . THR A 393 ? 0.8317 0.5325 0.5836 0.0324  0.1219  0.0607  196  THR A CG2 
2986 N N   . ALA A 394 ? 0.7785 0.5658 0.5921 0.0370  0.0931  0.0297  197  ALA A N   
2987 C CA  . ALA A 394 ? 0.8189 0.5924 0.6086 0.0435  0.0958  0.0237  197  ALA A CA  
2988 C C   . ALA A 394 ? 0.8322 0.6382 0.6729 0.0388  0.1179  0.0224  197  ALA A C   
2989 O O   . ALA A 394 ? 0.8355 0.6854 0.7364 0.0297  0.1119  0.0213  197  ALA A O   
2990 C CB  . ALA A 394 ? 0.7871 0.5697 0.5746 0.0446  0.0588  0.0141  197  ALA A CB  
2991 N N   . PRO A 395 ? 0.8555 0.6382 0.6714 0.0466  0.1428  0.0220  198  PRO A N   
2992 C CA  . PRO A 395 ? 0.8507 0.6654 0.7180 0.0461  0.1602  0.0191  198  PRO A CA  
2993 C C   . PRO A 395 ? 0.8317 0.6821 0.7393 0.0417  0.1312  0.0117  198  PRO A C   
2994 O O   . PRO A 395 ? 0.8477 0.6891 0.7316 0.0414  0.1030  0.0066  198  PRO A O   
2995 C CB  . PRO A 395 ? 0.9041 0.6766 0.7184 0.0603  0.1823  0.0164  198  PRO A CB  
2996 C CG  . PRO A 395 ? 0.9694 0.6877 0.7106 0.0652  0.1931  0.0228  198  PRO A CG  
2997 C CD  . PRO A 395 ? 0.9369 0.6589 0.6728 0.0584  0.1577  0.0243  198  PRO A CD  
2998 N N   . MET A 396 ? 0.8391 0.7282 0.8079 0.0383  0.1386  0.0110  199  MET A N   
2999 C CA  . MET A 396 ? 0.8425 0.7580 0.8424 0.0351  0.1136  0.0052  199  MET A CA  
3000 C C   . MET A 396 ? 0.8828 0.7774 0.8568 0.0452  0.1112  -0.0015 199  MET A C   
3001 O O   . MET A 396 ? 0.8604 0.7521 0.8245 0.0421  0.0865  -0.0062 199  MET A O   
3002 C CB  . MET A 396 ? 0.8172 0.7750 0.8851 0.0297  0.1167  0.0064  199  MET A CB  
3003 C CG  . MET A 396 ? 0.8087 0.7857 0.9023 0.0176  0.1104  0.0108  199  MET A CG  
3004 S SD  . MET A 396 ? 0.7990 0.7921 0.8994 0.0094  0.0751  0.0075  199  MET A SD  
3005 C CE  . MET A 396 ? 0.7485 0.7580 0.8788 -0.0012 0.0758  0.0117  199  MET A CE  
3006 N N   . GLY A 397 ? 0.9640 0.8423 0.9274 0.0571  0.1384  -0.0022 200  GLY A N   
3007 C CA  . GLY A 397 ? 1.0373 0.8874 0.9683 0.0691  0.1378  -0.0095 200  GLY A CA  
3008 C C   . GLY A 397 ? 1.0291 0.9038 1.0062 0.0744  0.1351  -0.0132 200  GLY A C   
3009 O O   . GLY A 397 ? 0.9987 0.9096 1.0342 0.0751  0.1477  -0.0105 200  GLY A O   
3010 N N   . ALA A 398 ? 1.0651 0.9179 1.0163 0.0779  0.1163  -0.0196 201  ALA A N   
3011 C CA  . ALA A 398 ? 1.0529 0.9151 1.0334 0.0871  0.1129  -0.0234 201  ALA A CA  
3012 C C   . ALA A 398 ? 0.9813 0.8884 1.0224 0.0782  0.0977  -0.0196 201  ALA A C   
3013 O O   . ALA A 398 ? 0.9438 0.8616 0.9865 0.0629  0.0769  -0.0169 201  ALA A O   
3014 C CB  . ALA A 398 ? 1.0958 0.9194 1.0306 0.0879  0.0919  -0.0299 201  ALA A CB  
3015 N N   . SER A 399 ? 0.9401 0.8723 1.0312 0.0892  0.1070  -0.0201 202  SER A N   
3016 C CA  . SER A 399 ? 0.8558 0.8286 1.0045 0.0827  0.0917  -0.0172 202  SER A CA  
3017 C C   . SER A 399 ? 0.7882 0.7853 0.9566 0.0668  0.0947  -0.0118 202  SER A C   
3018 O O   . SER A 399 ? 0.7270 0.7430 0.9156 0.0558  0.0747  -0.0098 202  SER A O   
3019 C CB  . SER A 399 ? 0.8347 0.7971 0.9689 0.0773  0.0604  -0.0179 202  SER A CB  
3020 O OG  . SER A 399 ? 0.8631 0.7923 0.9679 0.0902  0.0572  -0.0226 202  SER A OG  
3021 N N   . GLY A 400 ? 0.7883 0.7783 0.9445 0.0671  0.1212  -0.0094 203  GLY A N   
3022 C CA  . GLY A 400 ? 0.7496 0.7510 0.9122 0.0530  0.1249  -0.0038 203  GLY A CA  
3023 C C   . GLY A 400 ? 0.7127 0.7559 0.9445 0.0463  0.1253  -0.0018 203  GLY A C   
3024 O O   . GLY A 400 ? 0.6923 0.7457 0.9334 0.0328  0.1181  0.0017  203  GLY A O   
3025 N N   . ALA A 401 ? 0.6791 0.7463 0.9627 0.0566  0.1326  -0.0048 204  ALA A N   
3026 C CA  . ALA A 401 ? 0.6153 0.7241 0.9708 0.0495  0.1250  -0.0047 204  ALA A CA  
3027 C C   . ALA A 401 ? 0.5527 0.6662 0.9067 0.0416  0.0865  -0.0060 204  ALA A C   
3028 O O   . ALA A 401 ? 0.5342 0.6634 0.9116 0.0283  0.0759  -0.0045 204  ALA A O   
3029 C CB  . ALA A 401 ? 0.5873 0.7242 1.0049 0.0646  0.1360  -0.0090 204  ALA A CB  
3030 N N   . THR A 402 ? 0.5658 0.6605 0.8876 0.0494  0.0669  -0.0086 205  THR A N   
3031 C CA  . THR A 402 ? 0.5699 0.6616 0.8806 0.0427  0.0347  -0.0090 205  THR A CA  
3032 C C   . THR A 402 ? 0.5470 0.6283 0.8236 0.0271  0.0313  -0.0057 205  THR A C   
3033 O O   . THR A 402 ? 0.5285 0.6209 0.8195 0.0175  0.0171  -0.0054 205  THR A O   
3034 C CB  . THR A 402 ? 0.5856 0.6510 0.8600 0.0523  0.0203  -0.0109 205  THR A CB  
3035 O OG1 . THR A 402 ? 0.6362 0.7101 0.9438 0.0701  0.0217  -0.0144 205  THR A OG1 
3036 C CG2 . THR A 402 ? 0.5573 0.6140 0.8135 0.0449  -0.0078 -0.0100 205  THR A CG2 
3037 N N   . SER A 403 ? 0.5499 0.6080 0.7806 0.0259  0.0426  -0.0042 206  SER A N   
3038 C CA  . SER A 403 ? 0.5378 0.5874 0.7393 0.0143  0.0381  -0.0018 206  SER A CA  
3039 C C   . SER A 403 ? 0.5158 0.5802 0.7422 0.0060  0.0465  0.0010  206  SER A C   
3040 O O   . SER A 403 ? 0.4918 0.5599 0.7179 -0.0027 0.0336  0.0013  206  SER A O   
3041 C CB  . SER A 403 ? 0.5857 0.6092 0.7404 0.0165  0.0467  -0.0016 206  SER A CB  
3042 O OG  . SER A 403 ? 0.6306 0.6374 0.7603 0.0191  0.0339  -0.0045 206  SER A OG  
3043 N N   . ARG A 404 ? 0.5209 0.5908 0.7679 0.0084  0.0701  0.0030  207  ARG A N   
3044 C CA  . ARG A 404 ? 0.5372 0.6160 0.8066 -0.0019 0.0803  0.0065  207  ARG A CA  
3045 C C   . ARG A 404 ? 0.5142 0.6169 0.8287 -0.0097 0.0607  0.0038  207  ARG A C   
3046 O O   . ARG A 404 ? 0.4867 0.5869 0.7994 -0.0201 0.0534  0.0048  207  ARG A O   
3047 C CB  . ARG A 404 ? 0.5719 0.6528 0.8605 0.0007  0.1132  0.0097  207  ARG A CB  
3048 C CG  . ARG A 404 ? 0.5926 0.6862 0.9190 -0.0127 0.1248  0.0134  207  ARG A CG  
3049 C CD  . ARG A 404 ? 0.6549 0.7423 0.9886 -0.0122 0.1648  0.0188  207  ARG A CD  
3050 N NE  . ARG A 404 ? 0.6775 0.7802 1.0395 0.0007  0.1813  0.0156  207  ARG A NE  
3051 C CZ  . ARG A 404 ? 0.6702 0.8130 1.1087 0.0009  0.1822  0.0118  207  ARG A CZ  
3052 N NH1 . ARG A 404 ? 0.6645 0.8194 1.1267 0.0163  0.1989  0.0085  207  ARG A NH1 
3053 N NH2 . ARG A 404 ? 0.6594 0.8292 1.1512 -0.0130 0.1645  0.0103  207  ARG A NH2 
3054 N N   . LYS A 405 ? 0.5131 0.6351 0.8652 -0.0035 0.0490  -0.0005 208  LYS A N   
3055 C CA  . LYS A 405 ? 0.4980 0.6387 0.8903 -0.0100 0.0261  -0.0041 208  LYS A CA  
3056 C C   . LYS A 405 ? 0.4453 0.5695 0.7991 -0.0112 -0.0019 -0.0063 208  LYS A C   
3057 O O   . LYS A 405 ? 0.4533 0.5787 0.8155 -0.0190 -0.0192 -0.0087 208  LYS A O   
3058 C CB  . LYS A 405 ? 0.5423 0.7110 0.9950 -0.0016 0.0218  -0.0081 208  LYS A CB  
3059 C CG  . LYS A 405 ? 0.6135 0.7981 1.1026 0.0011  0.0574  -0.0058 208  LYS A CG  
3060 C CD  . LYS A 405 ? 0.6363 0.8372 1.1584 0.0192  0.0598  -0.0097 208  LYS A CD  
3061 C CE  . LYS A 405 ? 0.6450 0.8876 1.2541 0.0180  0.0550  -0.0139 208  LYS A CE  
3062 N NZ  . LYS A 405 ? 0.6663 0.9168 1.2972 0.0076  0.0899  -0.0101 208  LYS A NZ  
3063 N N   . ALA A 406 ? 0.4158 0.5222 0.7276 -0.0041 -0.0049 -0.0056 209  ALA A N   
3064 C CA  . ALA A 406 ? 0.3821 0.4708 0.6539 -0.0074 -0.0230 -0.0063 209  ALA A CA  
3065 C C   . ALA A 406 ? 0.3832 0.4655 0.6368 -0.0170 -0.0178 -0.0048 209  ALA A C   
3066 O O   . ALA A 406 ? 0.3607 0.4366 0.6042 -0.0217 -0.0321 -0.0070 209  ALA A O   
3067 C CB  . ALA A 406 ? 0.3537 0.4236 0.5853 -0.0018 -0.0222 -0.0050 209  ALA A CB  
3068 N N   . LEU A 407 ? 0.3892 0.4677 0.6314 -0.0178 0.0020  -0.0014 210  LEU A N   
3069 C CA  . LEU A 407 ? 0.4191 0.4885 0.6424 -0.0239 0.0057  0.0002  210  LEU A CA  
3070 C C   . LEU A 407 ? 0.4160 0.4908 0.6674 -0.0321 0.0030  -0.0008 210  LEU A C   
3071 O O   . LEU A 407 ? 0.4218 0.4869 0.6590 -0.0363 -0.0060 -0.0026 210  LEU A O   
3072 C CB  . LEU A 407 ? 0.4233 0.4818 0.6254 -0.0211 0.0242  0.0043  210  LEU A CB  
3073 C CG  . LEU A 407 ? 0.4168 0.4623 0.5974 -0.0239 0.0264  0.0064  210  LEU A CG  
3074 C CD1 . LEU A 407 ? 0.3467 0.3903 0.5071 -0.0231 0.0121  0.0033  210  LEU A CD1 
3075 C CD2 . LEU A 407 ? 0.4379 0.4661 0.5914 -0.0191 0.0416  0.0108  210  LEU A CD2 
3076 N N   . GLU A 408 ? 0.4049 0.4947 0.6984 -0.0347 0.0112  -0.0002 211  GLU A N   
3077 C CA  . GLU A 408 ? 0.4448 0.5406 0.7721 -0.0456 0.0070  -0.0018 211  GLU A CA  
3078 C C   . GLU A 408 ? 0.4353 0.5314 0.7672 -0.0473 -0.0230 -0.0087 211  GLU A C   
3079 O O   . GLU A 408 ? 0.4306 0.5140 0.7542 -0.0544 -0.0336 -0.0115 211  GLU A O   
3080 C CB  . GLU A 408 ? 0.4934 0.6108 0.8751 -0.0492 0.0236  -0.0002 211  GLU A CB  
3081 C CG  . GLU A 408 ? 0.6040 0.7101 0.9719 -0.0503 0.0564  0.0073  211  GLU A CG  
3082 C CD  . GLU A 408 ? 0.6897 0.8170 1.1092 -0.0519 0.0811  0.0094  211  GLU A CD  
3083 O OE1 . GLU A 408 ? 0.7261 0.8407 1.1400 -0.0577 0.1103  0.0162  211  GLU A OE1 
3084 O OE2 . GLU A 408 ? 0.7121 0.8671 1.1767 -0.0463 0.0727  0.0046  211  GLU A OE2 
3085 N N   . THR A 409 ? 0.4319 0.5358 0.7697 -0.0392 -0.0378 -0.0116 212  THR A N   
3086 C CA  . THR A 409 ? 0.4127 0.5063 0.7379 -0.0382 -0.0674 -0.0174 212  THR A CA  
3087 C C   . THR A 409 ? 0.3992 0.4666 0.6688 -0.0388 -0.0694 -0.0176 212  THR A C   
3088 O O   . THR A 409 ? 0.4160 0.4681 0.6727 -0.0431 -0.0846 -0.0223 212  THR A O   
3089 C CB  . THR A 409 ? 0.4104 0.5066 0.7345 -0.0267 -0.0807 -0.0184 212  THR A CB  
3090 O OG1 . THR A 409 ? 0.4384 0.5622 0.8238 -0.0240 -0.0832 -0.0203 212  THR A OG1 
3091 C CG2 . THR A 409 ? 0.3978 0.4711 0.6889 -0.0240 -0.1095 -0.0228 212  THR A CG2 
3092 N N   . LEU A 410 ? 0.4007 0.4623 0.6381 -0.0341 -0.0540 -0.0133 213  LEU A N   
3093 C CA  . LEU A 410 ? 0.4414 0.4849 0.6357 -0.0336 -0.0526 -0.0137 213  LEU A CA  
3094 C C   . LEU A 410 ? 0.4735 0.5088 0.6657 -0.0388 -0.0483 -0.0149 213  LEU A C   
3095 O O   . LEU A 410 ? 0.4996 0.5175 0.6650 -0.0383 -0.0550 -0.0188 213  LEU A O   
3096 C CB  . LEU A 410 ? 0.4395 0.4847 0.6142 -0.0296 -0.0378 -0.0095 213  LEU A CB  
3097 C CG  . LEU A 410 ? 0.4149 0.4499 0.5555 -0.0282 -0.0348 -0.0098 213  LEU A CG  
3098 C CD1 . LEU A 410 ? 0.4443 0.4633 0.5618 -0.0276 -0.0473 -0.0127 213  LEU A CD1 
3099 C CD2 . LEU A 410 ? 0.3540 0.3946 0.4882 -0.0263 -0.0256 -0.0066 213  LEU A CD2 
3100 N N   . ARG A 411 ? 0.4462 0.4887 0.6611 -0.0429 -0.0349 -0.0115 214  ARG A N   
3101 C CA  . ARG A 411 ? 0.4600 0.4880 0.6702 -0.0481 -0.0316 -0.0119 214  ARG A CA  
3102 C C   . ARG A 411 ? 0.4877 0.5052 0.7056 -0.0546 -0.0515 -0.0190 214  ARG A C   
3103 O O   . ARG A 411 ? 0.5448 0.5404 0.7354 -0.0540 -0.0570 -0.0229 214  ARG A O   
3104 C CB  . ARG A 411 ? 0.4285 0.4603 0.6609 -0.0534 -0.0132 -0.0059 214  ARG A CB  
3105 C CG  . ARG A 411 ? 0.4341 0.4622 0.6421 -0.0458 0.0039  0.0003  214  ARG A CG  
3106 C CD  . ARG A 411 ? 0.4464 0.4772 0.6729 -0.0494 0.0241  0.0066  214  ARG A CD  
3107 N NE  . ARG A 411 ? 0.4654 0.4844 0.6593 -0.0410 0.0375  0.0118  214  ARG A NE  
3108 C CZ  . ARG A 411 ? 0.4614 0.4740 0.6541 -0.0408 0.0582  0.0178  214  ARG A CZ  
3109 N NH1 . ARG A 411 ? 0.4861 0.5099 0.7178 -0.0492 0.0713  0.0194  214  ARG A NH1 
3110 N NH2 . ARG A 411 ? 0.4145 0.4085 0.5676 -0.0320 0.0655  0.0215  214  ARG A NH2 
3111 N N   . ARG A 412 ? 0.5004 0.5317 0.7541 -0.0594 -0.0645 -0.0217 215  ARG A N   
3112 C CA  . ARG A 412 ? 0.5865 0.6067 0.8484 -0.0656 -0.0900 -0.0298 215  ARG A CA  
3113 C C   . ARG A 412 ? 0.6222 0.6158 0.8309 -0.0575 -0.1060 -0.0354 215  ARG A C   
3114 O O   . ARG A 412 ? 0.6606 0.6269 0.8389 -0.0586 -0.1109 -0.0403 215  ARG A O   
3115 C CB  . ARG A 412 ? 0.6307 0.6760 0.9459 -0.0688 -0.1048 -0.0323 215  ARG A CB  
3116 C CG  . ARG A 412 ? 0.6371 0.7084 1.0118 -0.0788 -0.0867 -0.0281 215  ARG A CG  
3117 C CD  . ARG A 412 ? 0.6333 0.7279 1.0728 -0.0863 -0.1082 -0.0344 215  ARG A CD  
3118 N NE  . ARG A 412 ? 0.6458 0.7609 1.1025 -0.0738 -0.1188 -0.0353 215  ARG A NE  
3119 C CZ  . ARG A 412 ? 0.6582 0.7602 1.0903 -0.0646 -0.1501 -0.0411 215  ARG A CZ  
3120 N NH1 . ARG A 412 ? 0.6833 0.7517 1.0711 -0.0669 -0.1727 -0.0472 215  ARG A NH1 
3121 N NH2 . ARG A 412 ? 0.6298 0.7470 1.0767 -0.0521 -0.1583 -0.0408 215  ARG A NH2 
3122 N N   . VAL A 413 ? 0.5741 0.5708 0.7668 -0.0490 -0.1117 -0.0344 216  VAL A N   
3123 C CA  . VAL A 413 ? 0.5833 0.5498 0.7242 -0.0428 -0.1264 -0.0391 216  VAL A CA  
3124 C C   . VAL A 413 ? 0.6070 0.5588 0.7027 -0.0371 -0.1062 -0.0372 216  VAL A C   
3125 O O   . VAL A 413 ? 0.6335 0.5548 0.6832 -0.0329 -0.1122 -0.0421 216  VAL A O   
3126 C CB  . VAL A 413 ? 0.5662 0.5339 0.7015 -0.0360 -0.1401 -0.0379 216  VAL A CB  
3127 C CG1 . VAL A 413 ? 0.5399 0.5319 0.7333 -0.0388 -0.1572 -0.0397 216  VAL A CG1 
3128 C CG2 . VAL A 413 ? 0.5455 0.5251 0.6710 -0.0309 -0.1174 -0.0300 216  VAL A CG2 
3129 N N   . GLY A 414 ? 0.6065 0.5776 0.7135 -0.0360 -0.0830 -0.0309 217  GLY A N   
3130 C CA  . GLY A 414 ? 0.6383 0.6036 0.7155 -0.0301 -0.0655 -0.0297 217  GLY A CA  
3131 C C   . GLY A 414 ? 0.6826 0.6305 0.7468 -0.0288 -0.0621 -0.0341 217  GLY A C   
3132 O O   . GLY A 414 ? 0.6931 0.6253 0.7248 -0.0217 -0.0548 -0.0374 217  GLY A O   
3133 N N   . ASP A 415 ? 0.6967 0.6454 0.7864 -0.0352 -0.0653 -0.0341 218  ASP A N   
3134 C CA  . ASP A 415 ? 0.7277 0.6542 0.8027 -0.0337 -0.0625 -0.0377 218  ASP A CA  
3135 C C   . ASP A 415 ? 0.7554 0.6479 0.7986 -0.0333 -0.0792 -0.0475 218  ASP A C   
3136 O O   . ASP A 415 ? 0.7907 0.6577 0.8028 -0.0260 -0.0745 -0.0525 218  ASP A O   
3137 C CB  . ASP A 415 ? 0.7165 0.6464 0.8233 -0.0430 -0.0596 -0.0338 218  ASP A CB  
3138 C CG  . ASP A 415 ? 0.7253 0.6735 0.8434 -0.0392 -0.0405 -0.0249 218  ASP A CG  
3139 O OD1 . ASP A 415 ? 0.6761 0.6473 0.8028 -0.0367 -0.0353 -0.0209 218  ASP A OD1 
3140 O OD2 . ASP A 415 ? 0.8010 0.7350 0.9138 -0.0380 -0.0324 -0.0221 218  ASP A OD2 
3141 N N   . GLY A 416 ? 0.7294 0.6179 0.7774 -0.0393 -0.1003 -0.0511 219  GLY A N   
3142 C CA  . GLY A 416 ? 0.7370 0.5864 0.7444 -0.0376 -0.1203 -0.0613 219  GLY A CA  
3143 C C   . GLY A 416 ? 0.6940 0.5234 0.6461 -0.0249 -0.1104 -0.0630 219  GLY A C   
3144 O O   . GLY A 416 ? 0.7217 0.5111 0.6255 -0.0189 -0.1150 -0.0713 219  GLY A O   
3145 N N   . VAL A 417 ? 0.6327 0.4868 0.5896 -0.0212 -0.0950 -0.0553 220  VAL A N   
3146 C CA  . VAL A 417 ? 0.6348 0.4711 0.5436 -0.0118 -0.0806 -0.0557 220  VAL A CA  
3147 C C   . VAL A 417 ? 0.6049 0.4421 0.5049 -0.0031 -0.0555 -0.0570 220  VAL A C   
3148 O O   . VAL A 417 ? 0.6093 0.4173 0.4638 0.0059  -0.0456 -0.0625 220  VAL A O   
3149 C CB  . VAL A 417 ? 0.5945 0.4524 0.5114 -0.0128 -0.0729 -0.0474 220  VAL A CB  
3150 C CG1 . VAL A 417 ? 0.5660 0.4207 0.4542 -0.0063 -0.0456 -0.0452 220  VAL A CG1 
3151 C CG2 . VAL A 417 ? 0.6447 0.4809 0.5409 -0.0144 -0.0982 -0.0486 220  VAL A CG2 
3152 N N   . GLN A 418 ? 0.5756 0.4437 0.5169 -0.0037 -0.0448 -0.0524 221  GLN A N   
3153 C CA  . GLN A 418 ? 0.5841 0.4556 0.5228 0.0072  -0.0249 -0.0539 221  GLN A CA  
3154 C C   . GLN A 418 ? 0.6587 0.4914 0.5673 0.0135  -0.0301 -0.0631 221  GLN A C   
3155 O O   . GLN A 418 ? 0.7065 0.5279 0.5933 0.0270  -0.0135 -0.0677 221  GLN A O   
3156 C CB  . GLN A 418 ? 0.5225 0.4277 0.5052 0.0063  -0.0187 -0.0471 221  GLN A CB  
3157 C CG  . GLN A 418 ? 0.5146 0.4554 0.5220 0.0022  -0.0112 -0.0394 221  GLN A CG  
3158 C CD  . GLN A 418 ? 0.4739 0.4397 0.5132 0.0041  -0.0064 -0.0341 221  GLN A CD  
3159 O OE1 . GLN A 418 ? 0.4475 0.4178 0.4901 0.0147  0.0020  -0.0357 221  GLN A OE1 
3160 N NE2 . GLN A 418 ? 0.4438 0.4228 0.5042 -0.0044 -0.0124 -0.0283 221  GLN A NE2 
3161 N N   . ARG A 419 ? 0.7003 0.5121 0.6100 0.0041  -0.0525 -0.0665 222  ARG A N   
3162 C CA  . ARG A 419 ? 0.7666 0.5332 0.6429 0.0082  -0.0611 -0.0766 222  ARG A CA  
3163 C C   . ARG A 419 ? 0.7309 0.4569 0.5482 0.0144  -0.0667 -0.0856 222  ARG A C   
3164 O O   . ARG A 419 ? 0.7256 0.4216 0.5018 0.0282  -0.0539 -0.0928 222  ARG A O   
3165 C CB  . ARG A 419 ? 0.8412 0.5978 0.7415 -0.0072 -0.0841 -0.0779 222  ARG A CB  
3166 C CG  . ARG A 419 ? 0.8435 0.6331 0.7959 -0.0155 -0.0773 -0.0679 222  ARG A CG  
3167 C CD  . ARG A 419 ? 0.8803 0.6534 0.8545 -0.0324 -0.0957 -0.0700 222  ARG A CD  
3168 N NE  . ARG A 419 ? 0.9269 0.6902 0.9006 -0.0427 -0.1221 -0.0769 222  ARG A NE  
3169 C CZ  . ARG A 419 ? 0.9732 0.6915 0.9052 -0.0417 -0.1419 -0.0891 222  ARG A CZ  
3170 N NH1 . ARG A 419 ? 0.9742 0.6844 0.9068 -0.0500 -0.1708 -0.0954 222  ARG A NH1 
3171 N NH2 . ARG A 419 ? 1.0154 0.6944 0.9026 -0.0304 -0.1345 -0.0957 222  ARG A NH2 
3172 N N   . ASN A 420 ? 0.7289 0.4499 0.5380 0.0059  -0.0861 -0.0854 223  ASN A N   
3173 C CA  . ASN A 420 ? 0.8107 0.4817 0.5522 0.0120  -0.0962 -0.0940 223  ASN A CA  
3174 C C   . ASN A 420 ? 0.7891 0.4544 0.4911 0.0261  -0.0637 -0.0924 223  ASN A C   
3175 O O   . ASN A 420 ? 0.7879 0.4048 0.4257 0.0371  -0.0575 -0.1009 223  ASN A O   
3176 C CB  . ASN A 420 ? 0.8346 0.5026 0.5766 0.0024  -0.1256 -0.0930 223  ASN A CB  
3177 C CG  . ASN A 420 ? 0.8559 0.5121 0.6211 -0.0100 -0.1618 -0.1000 223  ASN A CG  
3178 O OD1 . ASN A 420 ? 0.9237 0.5392 0.6597 -0.0092 -0.1733 -0.1105 223  ASN A OD1 
3179 N ND2 . ASN A 420 ? 0.7993 0.4904 0.6189 -0.0215 -0.1797 -0.0949 223  ASN A ND2 
3180 N N   . HIS A 421 ? 0.7095 0.4229 0.4499 0.0253  -0.0410 -0.0817 224  HIS A N   
3181 C CA  . HIS A 421 ? 0.7219 0.4361 0.4362 0.0344  -0.0091 -0.0792 224  HIS A CA  
3182 C C   . HIS A 421 ? 0.7100 0.4561 0.4582 0.0442  0.0196  -0.0786 224  HIS A C   
3183 O O   . HIS A 421 ? 0.6879 0.4608 0.4500 0.0472  0.0468  -0.0737 224  HIS A O   
3184 C CB  . HIS A 421 ? 0.7083 0.4472 0.4369 0.0255  -0.0061 -0.0686 224  HIS A CB  
3185 C CG  . HIS A 421 ? 0.7577 0.4541 0.4338 0.0226  -0.0278 -0.0695 224  HIS A CG  
3186 N ND1 . HIS A 421 ? 0.8320 0.4787 0.4330 0.0303  -0.0154 -0.0720 224  HIS A ND1 
3187 C CD2 . HIS A 421 ? 0.7479 0.4412 0.4340 0.0144  -0.0622 -0.0686 224  HIS A CD2 
3188 C CE1 . HIS A 421 ? 0.8782 0.4888 0.4396 0.0274  -0.0448 -0.0723 224  HIS A CE1 
3189 N NE2 . HIS A 421 ? 0.8270 0.4687 0.4441 0.0181  -0.0744 -0.0706 224  HIS A NE2 
3190 N N   . GLU A 422 ? 0.7171 0.4598 0.4810 0.0491  0.0126  -0.0837 225  GLU A N   
3191 C CA  . GLU A 422 ? 0.7574 0.5263 0.5518 0.0622  0.0353  -0.0841 225  GLU A CA  
3192 C C   . GLU A 422 ? 0.7602 0.5157 0.5226 0.0788  0.0670  -0.0898 225  GLU A C   
3193 O O   . GLU A 422 ? 0.7355 0.5301 0.5365 0.0875  0.0908  -0.0876 225  GLU A O   
3194 C CB  . GLU A 422 ? 0.8346 0.5859 0.6356 0.0666  0.0211  -0.0891 225  GLU A CB  
3195 C CG  . GLU A 422 ? 0.9095 0.6787 0.7340 0.0847  0.0405  -0.0906 225  GLU A CG  
3196 C CD  . GLU A 422 ? 0.9848 0.7323 0.8140 0.0882  0.0251  -0.0932 225  GLU A CD  
3197 O OE1 . GLU A 422 ? 0.9652 0.7296 0.8270 0.0756  0.0102  -0.0854 225  GLU A OE1 
3198 O OE2 . GLU A 422 ? 1.0705 0.7793 0.8668 0.1039  0.0298  -0.1028 225  GLU A OE2 
3199 N N   . THR A 423 ? 0.8157 0.5163 0.5088 0.0836  0.0682  -0.0975 226  THR A N   
3200 C CA  . THR A 423 ? 0.9018 0.5848 0.5587 0.1002  0.1040  -0.1029 226  THR A CA  
3201 C C   . THR A 423 ? 0.8893 0.6068 0.5640 0.0941  0.1318  -0.0936 226  THR A C   
3202 O O   . THR A 423 ? 0.8563 0.6101 0.5670 0.1030  0.1643  -0.0928 226  THR A O   
3203 C CB  . THR A 423 ? 1.0103 0.6159 0.5761 0.1070  0.0974  -0.1136 226  THR A CB  
3204 O OG1 . THR A 423 ? 1.0769 0.6484 0.6281 0.1138  0.0761  -0.1240 226  THR A OG1 
3205 C CG2 . THR A 423 ? 1.0340 0.6168 0.5539 0.1242  0.1410  -0.1183 226  THR A CG2 
3206 N N   . ALA A 424 ? 0.9403 0.6470 0.5933 0.0787  0.1185  -0.0867 227  ALA A N   
3207 C CA  . ALA A 424 ? 0.9185 0.6511 0.5846 0.0702  0.1435  -0.0769 227  ALA A CA  
3208 C C   . ALA A 424 ? 0.8387 0.6442 0.5942 0.0636  0.1488  -0.0698 227  ALA A C   
3209 O O   . ALA A 424 ? 0.8972 0.7356 0.6827 0.0618  0.1793  -0.0654 227  ALA A O   
3210 C CB  . ALA A 424 ? 0.9586 0.6606 0.5827 0.0566  0.1224  -0.0705 227  ALA A CB  
3211 N N   . PHE A 425 ? 0.6996 0.5291 0.4977 0.0588  0.1192  -0.0685 228  PHE A N   
3212 C CA  . PHE A 425 ? 0.6056 0.4955 0.4777 0.0535  0.1200  -0.0623 228  PHE A CA  
3213 C C   . PHE A 425 ? 0.6137 0.5349 0.5251 0.0688  0.1430  -0.0669 228  PHE A C   
3214 O O   . PHE A 425 ? 0.5639 0.5310 0.5250 0.0657  0.1600  -0.0631 228  PHE A O   
3215 C CB  . PHE A 425 ? 0.5535 0.4528 0.4514 0.0467  0.0868  -0.0598 228  PHE A CB  
3216 C CG  . PHE A 425 ? 0.5714 0.4674 0.4640 0.0303  0.0673  -0.0528 228  PHE A CG  
3217 C CD1 . PHE A 425 ? 0.6152 0.4941 0.4744 0.0235  0.0764  -0.0489 228  PHE A CD1 
3218 C CD2 . PHE A 425 ? 0.5569 0.4639 0.4756 0.0230  0.0424  -0.0498 228  PHE A CD2 
3219 C CE1 . PHE A 425 ? 0.6102 0.4842 0.4650 0.0117  0.0567  -0.0428 228  PHE A CE1 
3220 C CE2 . PHE A 425 ? 0.5448 0.4517 0.4642 0.0108  0.0259  -0.0442 228  PHE A CE2 
3221 C CZ  . PHE A 425 ? 0.5552 0.4452 0.4425 0.0063  0.0313  -0.0412 228  PHE A CZ  
3222 N N   . GLN A 426 ? 0.6389 0.5348 0.5304 0.0860  0.1424  -0.0760 229  GLN A N   
3223 C CA  . GLN A 426 ? 0.6743 0.5966 0.6016 0.1052  0.1639  -0.0817 229  GLN A CA  
3224 C C   . GLN A 426 ? 0.7096 0.6466 0.6404 0.1088  0.2046  -0.0825 229  GLN A C   
3225 O O   . GLN A 426 ? 0.6977 0.6871 0.6921 0.1141  0.2226  -0.0823 229  GLN A O   
3226 C CB  . GLN A 426 ? 0.7659 0.6448 0.6566 0.1241  0.1577  -0.0920 229  GLN A CB  
3227 C CG  . GLN A 426 ? 0.8127 0.7199 0.7512 0.1446  0.1611  -0.0963 229  GLN A CG  
3228 C CD  . GLN A 426 ? 0.8156 0.7747 0.8196 0.1365  0.1425  -0.0879 229  GLN A CD  
3229 O OE1 . GLN A 426 ? 0.8071 0.7589 0.8072 0.1214  0.1159  -0.0816 229  GLN A OE1 
3230 N NE2 . GLN A 426 ? 0.8015 0.8128 0.8667 0.1467  0.1565  -0.0884 229  GLN A NE2 
3231 N N   . GLY A 427 ? 0.7611 0.6507 0.6239 0.1057  0.2198  -0.0834 230  GLY A N   
3232 C CA  . GLY A 427 ? 0.8264 0.7225 0.6847 0.1080  0.2643  -0.0830 230  GLY A CA  
3233 C C   . GLY A 427 ? 0.8052 0.7507 0.7168 0.0879  0.2751  -0.0724 230  GLY A C   
3234 O O   . GLY A 427 ? 0.7849 0.7737 0.7487 0.0900  0.3080  -0.0724 230  GLY A O   
3235 N N   . MET A 428 ? 0.8106 0.7511 0.7142 0.0684  0.2475  -0.0639 231  MET A N   
3236 C CA  . MET A 428 ? 0.7739 0.7563 0.7261 0.0490  0.2538  -0.0545 231  MET A CA  
3237 C C   . MET A 428 ? 0.7026 0.7527 0.7464 0.0511  0.2470  -0.0558 231  MET A C   
3238 O O   . MET A 428 ? 0.7273 0.8210 0.8256 0.0409  0.2660  -0.0524 231  MET A O   
3239 C CB  . MET A 428 ? 0.7807 0.7402 0.7038 0.0317  0.2225  -0.0465 231  MET A CB  
3240 C CG  . MET A 428 ? 0.7619 0.7549 0.7263 0.0117  0.2252  -0.0373 231  MET A CG  
3241 S SD  . MET A 428 ? 0.8320 0.8096 0.7714 0.0002  0.2735  -0.0310 231  MET A SD  
3242 C CE  . MET A 428 ? 0.8128 0.7819 0.7457 -0.0240 0.2539  -0.0190 231  MET A CE  
3243 N N   . LEU A 429 ? 0.6340 0.6906 0.6943 0.0636  0.2199  -0.0606 232  LEU A N   
3244 C CA  . LEU A 429 ? 0.6079 0.7197 0.7445 0.0675  0.2069  -0.0615 232  LEU A CA  
3245 C C   . LEU A 429 ? 0.6768 0.8277 0.8661 0.0843  0.2347  -0.0687 232  LEU A C   
3246 O O   . LEU A 429 ? 0.6810 0.8830 0.9411 0.0876  0.2245  -0.0699 232  LEU A O   
3247 C CB  . LEU A 429 ? 0.5850 0.6829 0.7141 0.0764  0.1710  -0.0632 232  LEU A CB  
3248 C CG  . LEU A 429 ? 0.5674 0.7089 0.7600 0.0869  0.1552  -0.0651 232  LEU A CG  
3249 C CD1 . LEU A 429 ? 0.5390 0.7216 0.7797 0.0692  0.1449  -0.0590 232  LEU A CD1 
3250 C CD2 . LEU A 429 ? 0.5648 0.6790 0.7353 0.0960  0.1257  -0.0656 232  LEU A CD2 
3251 N N   . ARG A 430 ? 0.7114 0.8376 0.8670 0.0972  0.2679  -0.0743 233  ARG A N   
3252 C CA  . ARG A 430 ? 0.6761 0.8409 0.8847 0.1149  0.3008  -0.0818 233  ARG A CA  
3253 C C   . ARG A 430 ? 0.7082 0.9015 0.9469 0.0993  0.3419  -0.0776 233  ARG A C   
3254 O O   . ARG A 430 ? 0.6900 0.9423 1.0046 0.0978  0.3437  -0.0776 233  ARG A O   
3255 C CB  . ARG A 430 ? 0.6826 0.8019 0.8370 0.1406  0.3173  -0.0914 233  ARG A CB  
3256 N N   . LYS A 431 ? 0.7762 0.9216 0.9443 0.0843  0.3606  -0.0714 234  LYS A N   
3257 C CA  . LYS A 431 ? 0.8294 0.9901 1.0110 0.0638  0.3876  -0.0631 234  LYS A CA  
3258 C C   . LYS A 431 ? 0.8096 1.0312 1.0752 0.0439  0.3703  -0.0577 234  LYS A C   
3259 O O   . LYS A 431 ? 0.8152 1.0838 1.1423 0.0375  0.3820  -0.0564 234  LYS A O   
3260 C CB  . LYS A 431 ? 0.8668 0.9591 0.9541 0.0496  0.4000  -0.0555 234  LYS A CB  
3261 N N   . LEU A 432 ? 0.7811 0.9997 1.0469 0.0334  0.3400  -0.0550 235  LEU A N   
3262 C CA  . LEU A 432 ? 0.7743 1.0483 1.1193 0.0223  0.3125  -0.0540 235  LEU A CA  
3263 C C   . LEU A 432 ? 0.8527 1.1576 1.2428 0.0470  0.2891  -0.0631 235  LEU A C   
3264 O O   . LEU A 432 ? 0.8958 1.1640 1.2370 0.0625  0.2666  -0.0655 235  LEU A O   
3265 C CB  . LEU A 432 ? 0.6990 0.9461 1.0077 0.0049  0.2752  -0.0462 235  LEU A CB  
3266 C CG  . LEU A 432 ? 0.7120 0.9029 0.9432 -0.0116 0.2851  -0.0372 235  LEU A CG  
3267 C CD1 . LEU A 432 ? 0.7068 0.8659 0.8955 -0.0149 0.2438  -0.0335 235  LEU A CD1 
3268 C CD2 . LEU A 432 ? 0.7132 0.9219 0.9743 -0.0372 0.3083  -0.0301 235  LEU A CD2 
3269 N N   . ASP A 433 ? 0.9005 1.2593 1.3629 0.0506  0.2798  -0.0653 236  ASP A N   
3270 C CA  . ASP A 433 ? 0.9441 1.3278 1.4453 0.0729  0.2496  -0.0723 236  ASP A CA  
3271 C C   . ASP A 433 ? 0.9099 1.3255 1.4577 0.0598  0.2128  -0.0696 236  ASP A C   
3272 O O   . ASP A 433 ? 0.9319 1.3855 1.5293 0.0455  0.2118  -0.0671 236  ASP A O   
3273 C CB  . ASP A 433 ? 1.0227 1.4338 1.5581 0.0967  0.2623  -0.0789 236  ASP A CB  
3274 C CG  . ASP A 433 ? 1.0892 1.5521 1.6891 0.0850  0.2725  -0.0767 236  ASP A CG  
3275 O OD1 . ASP A 433 ? 1.1068 1.6120 1.7646 0.1012  0.2588  -0.0815 236  ASP A OD1 
3276 O OD2 . ASP A 433 ? 1.1237 1.5843 1.7177 0.0596  0.2935  -0.0701 236  ASP A OD2 
3277 N N   . ILE A 434 ? 0.8537 1.2523 1.3853 0.0629  0.1809  -0.0704 237  ILE A N   
3278 C CA  . ILE A 434 ? 0.7761 1.1885 1.3298 0.0507  0.1438  -0.0680 237  ILE A CA  
3279 C C   . ILE A 434 ? 0.7585 1.1890 1.3423 0.0739  0.1109  -0.0729 237  ILE A C   
3280 O O   . ILE A 434 ? 0.7494 1.1502 1.2979 0.0937  0.0976  -0.0749 237  ILE A O   
3281 C CB  . ILE A 434 ? 0.7202 1.0787 1.1968 0.0382  0.1261  -0.0598 237  ILE A CB  
3282 C CG1 . ILE A 434 ? 0.6958 1.0208 1.1210 0.0231  0.1567  -0.0541 237  ILE A CG1 
3283 C CG2 . ILE A 434 ? 0.6873 1.0573 1.1827 0.0218  0.0958  -0.0569 237  ILE A CG2 
3284 C CD1 . ILE A 434 ? 0.6620 0.9444 1.0279 0.0077  0.1397  -0.0463 237  ILE A CD1 
3285 N N   . LYS A 435 ? 0.7644 1.2340 1.4006 0.0704  0.0958  -0.0731 238  LYS A N   
3286 C CA  . LYS A 435 ? 0.7585 1.2422 1.4204 0.0906  0.0604  -0.0767 238  LYS A CA  
3287 C C   . LYS A 435 ? 0.7420 1.2390 1.4252 0.0757  0.0249  -0.0754 238  LYS A C   
3288 O O   . LYS A 435 ? 0.7447 1.2380 1.4297 0.0915  -0.0103 -0.0776 238  LYS A O   
3289 C CB  . LYS A 435 ? 0.7746 1.2936 1.4830 0.1096  0.0738  -0.0810 238  LYS A CB  
3290 N N   . ASN A 436 ? 0.7170 1.2222 1.4093 0.0467  0.0322  -0.0719 239  ASN A N   
3291 C CA  . ASN A 436 ? 0.6753 1.1917 1.3887 0.0318  0.0006  -0.0723 239  ASN A CA  
3292 C C   . ASN A 436 ? 0.6649 1.1493 1.3361 0.0095  -0.0042 -0.0678 239  ASN A C   
3293 O O   . ASN A 436 ? 0.6457 1.1086 1.2839 0.0003  0.0223  -0.0636 239  ASN A O   
3294 C CB  . ASN A 436 ? 0.6618 1.2220 1.4362 0.0170  0.0119  -0.0735 239  ASN A CB  
3295 C CG  . ASN A 436 ? 0.7178 1.3155 1.5417 0.0390  0.0182  -0.0783 239  ASN A CG  
3296 O OD1 . ASN A 436 ? 0.7462 1.3643 1.5922 0.0390  0.0559  -0.0778 239  ASN A OD1 
3297 N ND2 . ASN A 436 ? 0.7519 1.3563 1.5911 0.0590  -0.0185 -0.0829 239  ASN A ND2 
3298 N N   . GLU A 437 ? 0.6791 1.1577 1.3495 0.0016  -0.0391 -0.0692 240  GLU A N   
3299 C CA  . GLU A 437 ? 0.6733 1.1258 1.3122 -0.0218 -0.0434 -0.0658 240  GLU A CA  
3300 C C   . GLU A 437 ? 0.6580 1.1246 1.3186 -0.0484 -0.0148 -0.0622 240  GLU A C   
3301 O O   . GLU A 437 ? 0.6624 1.1024 1.2899 -0.0666 -0.0034 -0.0573 240  GLU A O   
3302 C CB  . GLU A 437 ? 0.7306 1.1712 1.3618 -0.0230 -0.0867 -0.0695 240  GLU A CB  
3303 C CG  . GLU A 437 ? 0.7716 1.1922 1.3842 -0.0496 -0.0922 -0.0679 240  GLU A CG  
3304 C CD  . GLU A 437 ? 0.8023 1.1843 1.3680 -0.0447 -0.1280 -0.0701 240  GLU A CD  
3305 O OE1 . GLU A 437 ? 0.8163 1.1841 1.3590 -0.0214 -0.1465 -0.0713 240  GLU A OE1 
3306 O OE2 . GLU A 437 ? 0.8111 1.1725 1.3583 -0.0634 -0.1370 -0.0703 240  GLU A OE2 
3307 N N   . ASP A 438 ? 0.6364 1.1427 1.3516 -0.0508 -0.0024 -0.0642 241  ASP A N   
3308 C CA  . ASP A 438 ? 0.6082 1.1258 1.3430 -0.0761 0.0275  -0.0598 241  ASP A CA  
3309 C C   . ASP A 438 ? 0.5750 1.0738 1.2768 -0.0773 0.0706  -0.0536 241  ASP A C   
3310 O O   . ASP A 438 ? 0.5788 1.0540 1.2539 -0.0988 0.0895  -0.0472 241  ASP A O   
3311 C CB  . ASP A 438 ? 0.6306 1.1983 1.4367 -0.0773 0.0311  -0.0639 241  ASP A CB  
3312 C CG  . ASP A 438 ? 0.6516 1.2336 1.4897 -0.0874 -0.0080 -0.0695 241  ASP A CG  
3313 O OD1 . ASP A 438 ? 0.6567 1.2673 1.5347 -0.0707 -0.0321 -0.0763 241  ASP A OD1 
3314 O OD2 . ASP A 438 ? 0.6644 1.2259 1.4853 -0.1113 -0.0156 -0.0674 241  ASP A OD2 
3315 N N   . ASP A 439 ? 0.5361 1.0397 1.2340 -0.0536 0.0857  -0.0557 242  ASP A N   
3316 C CA  . ASP A 439 ? 0.5263 1.0045 1.1831 -0.0527 0.1243  -0.0512 242  ASP A CA  
3317 C C   . ASP A 439 ? 0.5442 0.9763 1.1412 -0.0648 0.1220  -0.0462 242  ASP A C   
3318 O O   . ASP A 439 ? 0.5583 0.9650 1.1222 -0.0796 0.1508  -0.0398 242  ASP A O   
3319 C CB  . ASP A 439 ? 0.4774 0.9578 1.1286 -0.0228 0.1320  -0.0561 242  ASP A CB  
3320 C CG  . ASP A 439 ? 0.4605 0.9859 1.1707 -0.0085 0.1373  -0.0611 242  ASP A CG  
3321 O OD1 . ASP A 439 ? 0.4607 1.0163 1.2154 -0.0246 0.1461  -0.0601 242  ASP A OD1 
3322 O OD2 . ASP A 439 ? 0.4511 0.9810 1.1641 0.0188  0.1328  -0.0662 242  ASP A OD2 
3323 N N   . VAL A 440 ? 0.5311 0.9496 1.1115 -0.0583 0.0877  -0.0486 243  VAL A N   
3324 C CA  . VAL A 440 ? 0.5162 0.8923 1.0410 -0.0675 0.0829  -0.0441 243  VAL A CA  
3325 C C   . VAL A 440 ? 0.5412 0.9042 1.0600 -0.0962 0.0922  -0.0386 243  VAL A C   
3326 O O   . VAL A 440 ? 0.5651 0.8839 1.0229 -0.1034 0.1017  -0.0312 243  VAL A O   
3327 C CB  . VAL A 440 ? 0.5023 0.8621 1.0038 -0.0553 0.0422  -0.0459 243  VAL A CB  
3328 C CG1 . VAL A 440 ? 0.4894 0.8005 0.9244 -0.0639 0.0342  -0.0390 243  VAL A CG1 
3329 C CG2 . VAL A 440 ? 0.5329 0.8904 1.0227 -0.0273 0.0367  -0.0487 243  VAL A CG2 
3330 N N   . LYS A 441 ? 0.5459 0.9326 1.1048 -0.1092 0.0842  -0.0392 244  LYS A N   
3331 C CA  . LYS A 441 ? 0.5735 0.9424 1.1227 -0.1365 0.0937  -0.0332 244  LYS A CA  
3332 C C   . LYS A 441 ? 0.6208 0.9801 1.1566 -0.1458 0.1379  -0.0259 244  LYS A C   
3333 O O   . LYS A 441 ? 0.6622 0.9882 1.1653 -0.1652 0.1514  -0.0185 244  LYS A O   
3334 C CB  . LYS A 441 ? 0.5903 0.9866 1.1876 -0.1490 0.0720  -0.0369 244  LYS A CB  
3335 N N   . SER A 442 ? 0.6421 1.0251 1.1978 -0.1313 0.1613  -0.0278 245  SER A N   
3336 C CA  . SER A 442 ? 0.6889 1.0552 1.2203 -0.1368 0.2052  -0.0213 245  SER A CA  
3337 C C   . SER A 442 ? 0.7043 1.0197 1.1616 -0.1315 0.2213  -0.0171 245  SER A C   
3338 O O   . SER A 442 ? 0.7492 1.0341 1.1661 -0.1380 0.2548  -0.0102 245  SER A O   
3339 C CB  . SER A 442 ? 0.7072 1.1111 1.2787 -0.1204 0.2254  -0.0260 245  SER A CB  
3340 O OG  . SER A 442 ? 0.7211 1.1746 1.3619 -0.1173 0.2007  -0.0325 245  SER A OG  
3341 N N   . LEU A 443 ? 0.6648 0.9680 1.1008 -0.1197 0.1979  -0.0210 246  LEU A N   
3342 C CA  . LEU A 443 ? 0.6902 0.9392 1.0424 -0.1086 0.2010  -0.0161 246  LEU A CA  
3343 C C   . LEU A 443 ? 0.7524 0.9518 1.0479 -0.1268 0.2056  -0.0063 246  LEU A C   
3344 O O   . LEU A 443 ? 0.8152 0.9706 1.0477 -0.1243 0.2248  -0.0007 246  LEU A O   
3345 C CB  . LEU A 443 ? 0.6222 0.8624 0.9531 -0.0893 0.1638  -0.0198 246  LEU A CB  
3346 C CG  . LEU A 443 ? 0.5729 0.8468 0.9414 -0.0673 0.1562  -0.0283 246  LEU A CG  
3347 C CD1 . LEU A 443 ? 0.5429 0.7997 0.8843 -0.0534 0.1213  -0.0295 246  LEU A CD1 
3348 C CD2 . LEU A 443 ? 0.6146 0.8792 0.9628 -0.0539 0.1874  -0.0300 246  LEU A CD2 
3349 N N   . SER A 444 ? 0.7532 0.9529 1.0640 -0.1434 0.1859  -0.0045 247  SER A N   
3350 C CA  . SER A 444 ? 0.7843 0.9313 1.0366 -0.1565 0.1836  0.0044  247  SER A CA  
3351 C C   . SER A 444 ? 0.7959 0.9100 1.0107 -0.1682 0.2239  0.0130  247  SER A C   
3352 O O   . SER A 444 ? 0.8153 0.8727 0.9569 -0.1674 0.2241  0.0206  247  SER A O   
3353 C CB  . SER A 444 ? 0.7860 0.9393 1.0672 -0.1747 0.1624  0.0038  247  SER A CB  
3354 O OG  . SER A 444 ? 0.8125 0.9996 1.1555 -0.1960 0.1817  0.0027  247  SER A OG  
3355 N N   . ARG A 445 ? 0.7667 0.9151 1.0316 -0.1780 0.2571  0.0119  248  ARG A N   
3356 C CA  . ARG A 445 ? 0.8022 0.9135 1.0210 -0.1845 0.2929  0.0212  248  ARG A CA  
3357 C C   . ARG A 445 ? 0.8204 0.8860 0.9626 -0.1676 0.3098  0.0229  248  ARG A C   
3358 O O   . ARG A 445 ? 0.8571 0.8583 0.9179 -0.1694 0.3107  0.0315  248  ARG A O   
3359 C CB  . ARG A 445 ? 0.7753 0.9327 1.0550 -0.1873 0.3150  0.0192  248  ARG A CB  
3360 N N   . VAL A 446 ? 0.7897 0.8828 0.9500 -0.1463 0.3131  0.0143  249  VAL A N   
3361 C CA  . VAL A 446 ? 0.7929 0.8390 0.8753 -0.1260 0.3188  0.0142  249  VAL A CA  
3362 C C   . VAL A 446 ? 0.7253 0.7331 0.7528 -0.1154 0.2752  0.0149  249  VAL A C   
3363 O O   . VAL A 446 ? 0.7318 0.6810 0.6786 -0.1081 0.2735  0.0189  249  VAL A O   
3364 C CB  . VAL A 446 ? 0.7903 0.8731 0.9072 -0.1051 0.3309  0.0037  249  VAL A CB  
3365 C CG1 . VAL A 446 ? 0.7293 0.8682 0.9183 -0.0968 0.2961  -0.0049 249  VAL A CG1 
3366 C CG2 . VAL A 446 ? 0.8282 0.8577 0.8615 -0.0839 0.3281  0.0016  249  VAL A CG2 
3367 N N   . MET A 447 ? 0.6787 0.7180 0.7492 -0.1142 0.2395  0.0108  250  MET A N   
3368 C CA  . MET A 447 ? 0.6995 0.7089 0.7289 -0.1051 0.2021  0.0114  250  MET A CA  
3369 C C   . MET A 447 ? 0.7955 0.7482 0.7624 -0.1153 0.2000  0.0212  250  MET A C   
3370 O O   . MET A 447 ? 0.8427 0.7510 0.7485 -0.1041 0.1835  0.0229  250  MET A O   
3371 C CB  . MET A 447 ? 0.6129 0.6616 0.6965 -0.1048 0.1707  0.0067  250  MET A CB  
3372 C CG  . MET A 447 ? 0.6132 0.6404 0.6666 -0.0936 0.1371  0.0061  250  MET A CG  
3373 S SD  . MET A 447 ? 0.5723 0.6345 0.6768 -0.0951 0.1067  0.0023  250  MET A SD  
3374 C CE  . MET A 447 ? 0.5346 0.6541 0.7086 -0.0926 0.1169  -0.0053 250  MET A CE  
3375 N N   . ILE A 448 ? 0.8012 0.7525 0.7829 -0.1363 0.2143  0.0276  251  ILE A N   
3376 C CA  . ILE A 448 ? 0.8031 0.6952 0.7228 -0.1455 0.2123  0.0377  251  ILE A CA  
3377 C C   . ILE A 448 ? 0.8382 0.6754 0.6830 -0.1428 0.2404  0.0444  251  ILE A C   
3378 O O   . ILE A 448 ? 0.8804 0.6594 0.6512 -0.1342 0.2251  0.0492  251  ILE A O   
3379 C CB  . ILE A 448 ? 0.8193 0.7197 0.7738 -0.1705 0.2202  0.0426  251  ILE A CB  
3380 C CG1 . ILE A 448 ? 0.7688 0.7114 0.7817 -0.1704 0.1873  0.0352  251  ILE A CG1 
3381 C CG2 . ILE A 448 ? 0.8343 0.6647 0.7175 -0.1796 0.2214  0.0542  251  ILE A CG2 
3382 C CD1 . ILE A 448 ? 0.7898 0.7369 0.8352 -0.1949 0.1886  0.0377  251  ILE A CD1 
3383 N N   . HIS A 449 ? 0.8466 0.6988 0.7066 -0.1486 0.2813  0.0443  252  HIS A N   
3384 C CA  . HIS A 449 ? 0.9376 0.7325 0.7185 -0.1444 0.3121  0.0501  252  HIS A CA  
3385 C C   . HIS A 449 ? 0.9206 0.6730 0.6313 -0.1196 0.2835  0.0460  252  HIS A C   
3386 O O   . HIS A 449 ? 0.9710 0.6520 0.5925 -0.1159 0.2826  0.0530  252  HIS A O   
3387 C CB  . HIS A 449 ? 1.0121 0.8406 0.8310 -0.1474 0.3590  0.0472  252  HIS A CB  
3388 C CG  . HIS A 449 ? 1.1393 0.9100 0.8799 -0.1391 0.3844  0.0512  252  HIS A CG  
3389 N ND1 . HIS A 449 ? 1.1755 0.9695 0.9436 -0.1363 0.4194  0.0479  252  HIS A ND1 
3390 C CD2 . HIS A 449 ? 1.2244 0.9130 0.8595 -0.1316 0.3776  0.0575  252  HIS A CD2 
3391 C CE1 . HIS A 449 ? 1.2668 0.9935 0.9476 -0.1289 0.4364  0.0522  252  HIS A CE1 
3392 N NE2 . HIS A 449 ? 1.2947 0.9561 0.8933 -0.1254 0.4096  0.0576  252  HIS A NE2 
3393 N N   . VAL A 450 ? 0.8352 0.6309 0.5886 -0.1040 0.2611  0.0344  253  VAL A N   
3394 C CA  . VAL A 450 ? 0.8548 0.6129 0.5493 -0.0832 0.2350  0.0292  253  VAL A CA  
3395 C C   . VAL A 450 ? 0.8411 0.5733 0.5110 -0.0798 0.1899  0.0318  253  VAL A C   
3396 O O   . VAL A 450 ? 0.8985 0.5711 0.4932 -0.0706 0.1735  0.0340  253  VAL A O   
3397 C CB  . VAL A 450 ? 0.7955 0.5989 0.5361 -0.0685 0.2280  0.0169  253  VAL A CB  
3398 C CG1 . VAL A 450 ? 0.8118 0.5757 0.4968 -0.0506 0.1976  0.0109  253  VAL A CG1 
3399 C CG2 . VAL A 450 ? 0.8097 0.6338 0.5700 -0.0674 0.2734  0.0137  253  VAL A CG2 
3400 N N   . PHE A 451 ? 0.7942 0.5709 0.5280 -0.0852 0.1685  0.0304  254  PHE A N   
3401 C CA  . PHE A 451 ? 0.8261 0.5854 0.5467 -0.0795 0.1286  0.0314  254  PHE A CA  
3402 C C   . PHE A 451 ? 0.9318 0.6293 0.5878 -0.0851 0.1274  0.0422  254  PHE A C   
3403 O O   . PHE A 451 ? 0.9676 0.6284 0.5829 -0.0738 0.0960  0.0431  254  PHE A O   
3404 C CB  . PHE A 451 ? 0.7350 0.5483 0.5303 -0.0846 0.1124  0.0284  254  PHE A CB  
3405 C CG  . PHE A 451 ? 0.7287 0.5385 0.5257 -0.0738 0.0741  0.0261  254  PHE A CG  
3406 C CD1 . PHE A 451 ? 0.7209 0.5311 0.5120 -0.0592 0.0534  0.0193  254  PHE A CD1 
3407 C CD2 . PHE A 451 ? 0.7338 0.5393 0.5403 -0.0785 0.0601  0.0301  254  PHE A CD2 
3408 C CE1 . PHE A 451 ? 0.7267 0.5388 0.5288 -0.0507 0.0216  0.0171  254  PHE A CE1 
3409 C CE2 . PHE A 451 ? 0.7257 0.5310 0.5389 -0.0672 0.0292  0.0276  254  PHE A CE2 
3410 C CZ  . PHE A 451 ? 0.7399 0.5514 0.5546 -0.0537 0.0105  0.0212  254  PHE A CZ  
3411 N N   . SER A 452 ? 0.9731 0.6572 0.6202 -0.1021 0.1606  0.0505  255  SER A N   
3412 C CA  . SER A 452 ? 1.0819 0.7035 0.6678 -0.1093 0.1607  0.0622  255  SER A CA  
3413 C C   . SER A 452 ? 1.2272 0.7722 0.7118 -0.0991 0.1650  0.0676  255  SER A C   
3414 O O   . SER A 452 ? 1.2792 0.7669 0.7044 -0.0932 0.1422  0.0741  255  SER A O   
3415 C CB  . SER A 452 ? 1.0517 0.6809 0.6625 -0.1346 0.1975  0.0700  255  SER A CB  
3416 O OG  . SER A 452 ? 0.9649 0.6654 0.6686 -0.1442 0.1947  0.0634  255  SER A OG  
3417 N N   . ASP A 453 ? 1.3071 0.8465 0.7676 -0.0944 0.1911  0.0641  256  ASP A N   
3418 C CA  . ASP A 453 ? 1.4795 0.9374 0.8335 -0.0882 0.2063  0.0704  256  ASP A CA  
3419 C C   . ASP A 453 ? 1.5189 0.9419 0.8200 -0.0646 0.1646  0.0626  256  ASP A C   
3420 O O   . ASP A 453 ? 1.5838 0.9889 0.8473 -0.0537 0.1735  0.0560  256  ASP A O   
3421 C CB  . ASP A 453 ? 1.5797 1.0430 0.9295 -0.0955 0.2616  0.0709  256  ASP A CB  
3422 C CG  . ASP A 453 ? 1.7572 1.1483 1.0207 -0.0867 0.2730  0.0727  256  ASP A CG  
3423 O OD1 . ASP A 453 ? 1.8361 1.1641 1.0256 -0.0737 0.2385  0.0742  256  ASP A OD1 
3424 O OD2 . ASP A 453 ? 1.8162 1.2145 1.0894 -0.0920 0.3154  0.0722  256  ASP A OD2 
3425 N N   . GLY A 454 ? 1.4687 0.8780 0.7649 -0.0565 0.1185  0.0632  257  GLY A N   
3426 C CA  . GLY A 454 ? 1.4587 0.8333 0.7087 -0.0357 0.0744  0.0559  257  GLY A CA  
3427 C C   . GLY A 454 ? 1.3799 0.7475 0.6394 -0.0277 0.0271  0.0573  257  GLY A C   
3428 O O   . GLY A 454 ? 1.3359 0.6986 0.6049 -0.0361 0.0305  0.0664  257  GLY A O   
3429 N N   . VAL A 455 ? 1.3662 0.7345 0.6275 -0.0111 -0.0174 0.0474  258  VAL A N   
3430 C CA  . VAL A 455 ? 1.3591 0.7317 0.6445 -0.0006 -0.0640 0.0464  258  VAL A CA  
3431 C C   . VAL A 455 ? 1.2166 0.6767 0.6151 -0.0063 -0.0673 0.0407  258  VAL A C   
3432 O O   . VAL A 455 ? 1.1901 0.7031 0.6422 -0.0171 -0.0393 0.0370  258  VAL A O   
3433 C CB  . VAL A 455 ? 1.4343 0.7707 0.6784 0.0186  -0.1119 0.0378  258  VAL A CB  
3434 C CG1 . VAL A 455 ? 1.3478 0.7480 0.6677 0.0208  -0.1289 0.0235  258  VAL A CG1 
3435 C CG2 . VAL A 455 ? 1.4993 0.8028 0.7255 0.0324  -0.1555 0.0417  258  VAL A CG2 
3436 N N   . THR A 456 ? 1.0997 0.5729 0.5324 0.0024  -0.1010 0.0397  259  THR A N   
3437 C CA  . THR A 456 ? 0.9725 0.5177 0.5003 -0.0011 -0.1035 0.0351  259  THR A CA  
3438 C C   . THR A 456 ? 0.9542 0.5269 0.5250 0.0127  -0.1435 0.0247  259  THR A C   
3439 O O   . THR A 456 ? 1.0414 0.5778 0.5813 0.0274  -0.1799 0.0238  259  THR A O   
3440 C CB  . THR A 456 ? 0.9684 0.5078 0.5063 -0.0036 -0.1016 0.0430  259  THR A CB  
3441 O OG1 . THR A 456 ? 1.0083 0.5322 0.5227 -0.0213 -0.0622 0.0517  259  THR A OG1 
3442 C CG2 . THR A 456 ? 0.8493 0.4555 0.4770 -0.0032 -0.1077 0.0370  259  THR A CG2 
3443 N N   . ASN A 457 ? 0.8430 0.4783 0.4860 0.0079  -0.1376 0.0170  260  ASN A N   
3444 C CA  . ASN A 457 ? 0.7926 0.4614 0.4897 0.0169  -0.1698 0.0077  260  ASN A CA  
3445 C C   . ASN A 457 ? 0.7126 0.4457 0.4828 0.0077  -0.1509 0.0027  260  ASN A C   
3446 O O   . ASN A 457 ? 0.6780 0.4258 0.4504 -0.0031 -0.1186 0.0048  260  ASN A O   
3447 C CB  . ASN A 457 ? 0.8504 0.4828 0.5046 0.0254  -0.1994 0.0009  260  ASN A CB  
3448 C CG  . ASN A 457 ? 0.9185 0.5422 0.5427 0.0178  -0.1770 -0.0028 260  ASN A CG  
3449 O OD1 . ASN A 457 ? 0.8734 0.5451 0.5517 0.0104  -0.1620 -0.0080 260  ASN A OD1 
3450 N ND2 . ASN A 457 ? 0.9918 0.5510 0.5263 0.0208  -0.1724 0.0001  260  ASN A ND2 
3451 N N   . TRP A 458 ? 0.6580 0.4288 0.4897 0.0124  -0.1714 -0.0037 261  TRP A N   
3452 C CA  . TRP A 458 ? 0.5778 0.4026 0.4737 0.0048  -0.1544 -0.0069 261  TRP A CA  
3453 C C   . TRP A 458 ? 0.5967 0.4232 0.4818 -0.0019 -0.1423 -0.0114 261  TRP A C   
3454 O O   . TRP A 458 ? 0.5684 0.4286 0.4874 -0.0090 -0.1201 -0.0117 261  TRP A O   
3455 C CB  . TRP A 458 ? 0.5374 0.3974 0.4988 0.0104  -0.1755 -0.0122 261  TRP A CB  
3456 C CG  . TRP A 458 ? 0.5598 0.4329 0.5500 0.0179  -0.1773 -0.0088 261  TRP A CG  
3457 C CD1 . TRP A 458 ? 0.5876 0.4518 0.5881 0.0317  -0.2060 -0.0101 261  TRP A CD1 
3458 C CD2 . TRP A 458 ? 0.5459 0.4386 0.5544 0.0141  -0.1507 -0.0042 261  TRP A CD2 
3459 N NE1 . TRP A 458 ? 0.5999 0.4772 0.6241 0.0375  -0.1955 -0.0066 261  TRP A NE1 
3460 C CE2 . TRP A 458 ? 0.5448 0.4370 0.5709 0.0261  -0.1623 -0.0032 261  TRP A CE2 
3461 C CE3 . TRP A 458 ? 0.4966 0.4046 0.5071 0.0031  -0.1214 -0.0018 261  TRP A CE3 
3462 C CZ2 . TRP A 458 ? 0.5115 0.4148 0.5525 0.0266  -0.1439 -0.0004 261  TRP A CZ2 
3463 C CZ3 . TRP A 458 ? 0.4610 0.3813 0.4876 0.0025  -0.1066 0.0009  261  TRP A CZ3 
3464 C CH2 . TRP A 458 ? 0.4981 0.4135 0.5366 0.0140  -0.1169 0.0015  261  TRP A CH2 
3465 N N   . GLY A 459 ? 0.6416 0.4272 0.4741 0.0016  -0.1565 -0.0150 262  GLY A N   
3466 C CA  . GLY A 459 ? 0.6809 0.4639 0.5013 -0.0024 -0.1462 -0.0209 262  GLY A CA  
3467 C C   . GLY A 459 ? 0.6793 0.4634 0.4792 -0.0081 -0.1073 -0.0164 262  GLY A C   
3468 O O   . GLY A 459 ? 0.6059 0.4160 0.4323 -0.0118 -0.0906 -0.0196 262  GLY A O   
3469 N N   . ARG A 460 ? 0.6948 0.4513 0.4512 -0.0091 -0.0926 -0.0087 263  ARG A N   
3470 C CA  . ARG A 460 ? 0.6946 0.4590 0.4442 -0.0165 -0.0547 -0.0046 263  ARG A CA  
3471 C C   . ARG A 460 ? 0.6305 0.4482 0.4460 -0.0235 -0.0409 -0.0025 263  ARG A C   
3472 O O   . ARG A 460 ? 0.6279 0.4712 0.4651 -0.0280 -0.0172 -0.0035 263  ARG A O   
3473 C CB  . ARG A 460 ? 0.7813 0.5001 0.4695 -0.0186 -0.0411 0.0038  263  ARG A CB  
3474 C CG  . ARG A 460 ? 0.8643 0.5187 0.4701 -0.0102 -0.0519 0.0019  263  ARG A CG  
3475 C CD  . ARG A 460 ? 0.9335 0.5402 0.4731 -0.0144 -0.0258 0.0117  263  ARG A CD  
3476 N NE  . ARG A 460 ? 0.8903 0.5222 0.4486 -0.0248 0.0191  0.0141  263  ARG A NE  
3477 C CZ  . ARG A 460 ? 0.8973 0.4992 0.4139 -0.0326 0.0517  0.0226  263  ARG A CZ  
3478 N NH1 . ARG A 460 ? 1.0084 0.5471 0.4530 -0.0308 0.0443  0.0307  263  ARG A NH1 
3479 N NH2 . ARG A 460 ? 0.8215 0.4555 0.3697 -0.0422 0.0913  0.0234  263  ARG A NH2 
3480 N N   . ILE A 461 ? 0.6131 0.4474 0.4616 -0.0226 -0.0569 -0.0006 264  ILE A N   
3481 C CA  . ILE A 461 ? 0.5463 0.4247 0.4501 -0.0277 -0.0464 0.0004  264  ILE A CA  
3482 C C   . ILE A 461 ? 0.5321 0.4426 0.4741 -0.0269 -0.0448 -0.0055 264  ILE A C   
3483 O O   . ILE A 461 ? 0.4963 0.4345 0.4655 -0.0309 -0.0283 -0.0055 264  ILE A O   
3484 C CB  . ILE A 461 ? 0.5041 0.3872 0.4288 -0.0238 -0.0629 0.0025  264  ILE A CB  
3485 C CG1 . ILE A 461 ? 0.5362 0.3842 0.4210 -0.0255 -0.0604 0.0095  264  ILE A CG1 
3486 C CG2 . ILE A 461 ? 0.4242 0.3474 0.4003 -0.0263 -0.0550 0.0017  264  ILE A CG2 
3487 C CD1 . ILE A 461 ? 0.5330 0.3714 0.4243 -0.0166 -0.0813 0.0111  264  ILE A CD1 
3488 N N   . VAL A 462 ? 0.5378 0.4423 0.4820 -0.0221 -0.0639 -0.0108 265  VAL A N   
3489 C CA  . VAL A 462 ? 0.5100 0.4352 0.4825 -0.0225 -0.0618 -0.0159 265  VAL A CA  
3490 C C   . VAL A 462 ? 0.5061 0.4250 0.4566 -0.0224 -0.0423 -0.0180 265  VAL A C   
3491 O O   . VAL A 462 ? 0.4846 0.4275 0.4615 -0.0228 -0.0297 -0.0190 265  VAL A O   
3492 C CB  . VAL A 462 ? 0.5255 0.4400 0.5028 -0.0200 -0.0878 -0.0217 265  VAL A CB  
3493 C CG1 . VAL A 462 ? 0.4950 0.4216 0.4943 -0.0223 -0.0843 -0.0267 265  VAL A CG1 
3494 C CG2 . VAL A 462 ? 0.4592 0.3903 0.4739 -0.0187 -0.1043 -0.0203 265  VAL A CG2 
3495 N N   . THR A 463 ? 0.5418 0.4260 0.4413 -0.0202 -0.0381 -0.0185 266  THR A N   
3496 C CA  . THR A 463 ? 0.5695 0.4493 0.4505 -0.0184 -0.0141 -0.0207 266  THR A CA  
3497 C C   . THR A 463 ? 0.5531 0.4677 0.4680 -0.0233 0.0093  -0.0165 266  THR A C   
3498 O O   . THR A 463 ? 0.5416 0.4793 0.4815 -0.0204 0.0219  -0.0196 266  THR A O   
3499 C CB  . THR A 463 ? 0.6341 0.4665 0.4487 -0.0154 -0.0079 -0.0207 266  THR A CB  
3500 O OG1 . THR A 463 ? 0.6951 0.4921 0.4765 -0.0101 -0.0365 -0.0262 266  THR A OG1 
3501 C CG2 . THR A 463 ? 0.6422 0.4705 0.4398 -0.0114 0.0210  -0.0242 266  THR A CG2 
3502 N N   . LEU A 464 ? 0.5158 0.4328 0.4331 -0.0301 0.0122  -0.0099 267  LEU A N   
3503 C CA  . LEU A 464 ? 0.4765 0.4236 0.4266 -0.0373 0.0298  -0.0066 267  LEU A CA  
3504 C C   . LEU A 464 ? 0.4221 0.4066 0.4209 -0.0352 0.0246  -0.0094 267  LEU A C   
3505 O O   . LEU A 464 ? 0.4420 0.4511 0.4662 -0.0348 0.0375  -0.0112 267  LEU A O   
3506 C CB  . LEU A 464 ? 0.4484 0.3848 0.3910 -0.0453 0.0265  0.0001  267  LEU A CB  
3507 C CG  . LEU A 464 ? 0.4592 0.4232 0.4364 -0.0549 0.0388  0.0024  267  LEU A CG  
3508 C CD1 . LEU A 464 ? 0.4833 0.4495 0.4568 -0.0618 0.0665  0.0036  267  LEU A CD1 
3509 C CD2 . LEU A 464 ? 0.5075 0.4559 0.4769 -0.0612 0.0296  0.0079  267  LEU A CD2 
3510 N N   . ILE A 465 ? 0.3980 0.3860 0.4104 -0.0334 0.0062  -0.0093 268  ILE A N   
3511 C CA  . ILE A 465 ? 0.3662 0.3806 0.4145 -0.0314 0.0030  -0.0105 268  ILE A CA  
3512 C C   . ILE A 465 ? 0.3839 0.4006 0.4363 -0.0245 0.0039  -0.0151 268  ILE A C   
3513 O O   . ILE A 465 ? 0.3937 0.4288 0.4681 -0.0213 0.0075  -0.0160 268  ILE A O   
3514 C CB  . ILE A 465 ? 0.3607 0.3748 0.4200 -0.0314 -0.0115 -0.0086 268  ILE A CB  
3515 C CG1 . ILE A 465 ? 0.3724 0.3823 0.4273 -0.0362 -0.0113 -0.0045 268  ILE A CG1 
3516 C CG2 . ILE A 465 ? 0.3228 0.3550 0.4091 -0.0288 -0.0120 -0.0091 268  ILE A CG2 
3517 C CD1 . ILE A 465 ? 0.3736 0.3741 0.4296 -0.0329 -0.0253 -0.0033 268  ILE A CD1 
3518 N N   . SER A 466 ? 0.3873 0.3804 0.4146 -0.0214 -0.0014 -0.0186 269  SER A N   
3519 C CA  . SER A 466 ? 0.3696 0.3571 0.3961 -0.0150 -0.0020 -0.0238 269  SER A CA  
3520 C C   . SER A 466 ? 0.4223 0.4176 0.4479 -0.0084 0.0165  -0.0266 269  SER A C   
3521 O O   . SER A 466 ? 0.3994 0.4061 0.4429 -0.0016 0.0189  -0.0287 269  SER A O   
3522 C CB  . SER A 466 ? 0.3760 0.3307 0.3708 -0.0139 -0.0146 -0.0284 269  SER A CB  
3523 O OG  . SER A 466 ? 0.4468 0.4023 0.4583 -0.0186 -0.0333 -0.0275 269  SER A OG  
3524 N N   . PHE A 467 ? 0.4517 0.4402 0.4575 -0.0094 0.0314  -0.0264 270  PHE A N   
3525 C CA  . PHE A 467 ? 0.4340 0.4399 0.4534 -0.0037 0.0523  -0.0288 270  PHE A CA  
3526 C C   . PHE A 467 ? 0.3523 0.3970 0.4191 -0.0057 0.0522  -0.0265 270  PHE A C   
3527 O O   . PHE A 467 ? 0.3409 0.4056 0.4328 0.0033  0.0577  -0.0300 270  PHE A O   
3528 C CB  . PHE A 467 ? 0.4945 0.4880 0.4884 -0.0075 0.0731  -0.0274 270  PHE A CB  
3529 C CG  . PHE A 467 ? 0.4962 0.5096 0.5089 -0.0006 0.0996  -0.0311 270  PHE A CG  
3530 C CD1 . PHE A 467 ? 0.5120 0.5184 0.5189 0.0145  0.1040  -0.0385 270  PHE A CD1 
3531 C CD2 . PHE A 467 ? 0.4233 0.4635 0.4647 -0.0091 0.1192  -0.0278 270  PHE A CD2 
3532 C CE1 . PHE A 467 ? 0.5250 0.5525 0.5546 0.0241  0.1293  -0.0428 270  PHE A CE1 
3533 C CE2 . PHE A 467 ? 0.4377 0.5025 0.5074 -0.0028 0.1437  -0.0317 270  PHE A CE2 
3534 C CZ  . PHE A 467 ? 0.4800 0.5403 0.5452 0.0156  0.1501  -0.0395 270  PHE A CZ  
3535 N N   . GLY A 468 ? 0.2951 0.3478 0.3723 -0.0159 0.0435  -0.0213 271  GLY A N   
3536 C CA  . GLY A 468 ? 0.2679 0.3494 0.3817 -0.0175 0.0383  -0.0201 271  GLY A CA  
3537 C C   . GLY A 468 ? 0.3170 0.4027 0.4421 -0.0072 0.0277  -0.0221 271  GLY A C   
3538 O O   . GLY A 468 ? 0.3403 0.4472 0.4913 -0.0008 0.0272  -0.0242 271  GLY A O   
3539 N N   . ALA A 469 ? 0.2807 0.3447 0.3873 -0.0056 0.0183  -0.0215 272  ALA A N   
3540 C CA  . ALA A 469 ? 0.3472 0.4068 0.4581 0.0024  0.0110  -0.0220 272  ALA A CA  
3541 C C   . ALA A 469 ? 0.3603 0.4166 0.4693 0.0150  0.0175  -0.0273 272  ALA A C   
3542 O O   . ALA A 469 ? 0.3420 0.4033 0.4624 0.0248  0.0137  -0.0280 272  ALA A O   
3543 C CB  . ALA A 469 ? 0.3385 0.3763 0.4359 -0.0020 0.0024  -0.0202 272  ALA A CB  
3544 N N   . PHE A 470 ? 0.4014 0.4446 0.4914 0.0163  0.0268  -0.0313 273  PHE A N   
3545 C CA  . PHE A 470 ? 0.4333 0.4713 0.5189 0.0302  0.0369  -0.0376 273  PHE A CA  
3546 C C   . PHE A 470 ? 0.4448 0.5183 0.5675 0.0379  0.0458  -0.0390 273  PHE A C   
3547 O O   . PHE A 470 ? 0.4824 0.5606 0.6180 0.0529  0.0447  -0.0426 273  PHE A O   
3548 C CB  . PHE A 470 ? 0.4107 0.4253 0.4624 0.0298  0.0485  -0.0416 273  PHE A CB  
3549 C CG  . PHE A 470 ? 0.4552 0.4490 0.4879 0.0458  0.0572  -0.0496 273  PHE A CG  
3550 C CD1 . PHE A 470 ? 0.4695 0.4259 0.4728 0.0483  0.0443  -0.0532 273  PHE A CD1 
3551 C CD2 . PHE A 470 ? 0.4379 0.4489 0.4845 0.0573  0.0786  -0.0538 273  PHE A CD2 
3552 C CE1 . PHE A 470 ? 0.5155 0.4456 0.4952 0.0636  0.0515  -0.0615 273  PHE A CE1 
3553 C CE2 . PHE A 470 ? 0.5040 0.4932 0.5309 0.0745  0.0886  -0.0619 273  PHE A CE2 
3554 C CZ  . PHE A 470 ? 0.5171 0.4622 0.5060 0.0782  0.0742  -0.0660 273  PHE A CZ  
3555 N N   . VAL A 471 ? 0.4032 0.5013 0.5459 0.0277  0.0527  -0.0365 274  VAL A N   
3556 C CA  . VAL A 471 ? 0.3921 0.5289 0.5802 0.0321  0.0586  -0.0388 274  VAL A CA  
3557 C C   . VAL A 471 ? 0.3647 0.5148 0.5751 0.0366  0.0371  -0.0374 274  VAL A C   
3558 O O   . VAL A 471 ? 0.3635 0.5382 0.6080 0.0490  0.0335  -0.0413 274  VAL A O   
3559 C CB  . VAL A 471 ? 0.3643 0.5191 0.5668 0.0163  0.0725  -0.0363 274  VAL A CB  
3560 C CG1 . VAL A 471 ? 0.3222 0.5216 0.5823 0.0155  0.0715  -0.0385 274  VAL A CG1 
3561 C CG2 . VAL A 471 ? 0.3993 0.5386 0.5773 0.0170  0.0983  -0.0383 274  VAL A CG2 
3562 N N   . ALA A 472 ? 0.3289 0.4614 0.5194 0.0285  0.0225  -0.0321 275  ALA A N   
3563 C CA  . ALA A 472 ? 0.3337 0.4686 0.5320 0.0335  0.0037  -0.0302 275  ALA A CA  
3564 C C   . ALA A 472 ? 0.3345 0.4537 0.5241 0.0516  -0.0026 -0.0318 275  ALA A C   
3565 O O   . ALA A 472 ? 0.3457 0.4754 0.5522 0.0637  -0.0156 -0.0333 275  ALA A O   
3566 C CB  . ALA A 472 ? 0.2191 0.3341 0.3933 0.0224  -0.0044 -0.0241 275  ALA A CB  
3567 N N   . LYS A 473 ? 0.3575 0.4480 0.5190 0.0539  0.0036  -0.0319 276  LYS A N   
3568 C CA  . LYS A 473 ? 0.3955 0.4635 0.5442 0.0705  -0.0015 -0.0334 276  LYS A CA  
3569 C C   . LYS A 473 ? 0.4030 0.4944 0.5810 0.0891  0.0011  -0.0401 276  LYS A C   
3570 O O   . LYS A 473 ? 0.4486 0.5351 0.6310 0.1057  -0.0120 -0.0405 276  LYS A O   
3571 C CB  . LYS A 473 ? 0.4444 0.4783 0.5618 0.0683  0.0050  -0.0348 276  LYS A CB  
3572 C CG  . LYS A 473 ? 0.4762 0.4881 0.5730 0.0517  0.0006  -0.0291 276  LYS A CG  
3573 C CD  . LYS A 473 ? 0.4989 0.4786 0.5701 0.0491  0.0033  -0.0331 276  LYS A CD  
3574 C CE  . LYS A 473 ? 0.4775 0.4436 0.5412 0.0317  -0.0024 -0.0289 276  LYS A CE  
3575 N NZ  . LYS A 473 ? 0.5181 0.4533 0.5608 0.0272  -0.0058 -0.0340 276  LYS A NZ  
3576 N N   . HIS A 474 ? 0.3806 0.4962 0.5790 0.0875  0.0186  -0.0452 277  HIS A N   
3577 C CA  . HIS A 474 ? 0.4318 0.5777 0.6692 0.1048  0.0258  -0.0522 277  HIS A CA  
3578 C C   . HIS A 474 ? 0.4702 0.6535 0.7531 0.1075  0.0091  -0.0524 277  HIS A C   
3579 O O   . HIS A 474 ? 0.5002 0.6969 0.8094 0.1280  -0.0015 -0.0567 277  HIS A O   
3580 C CB  . HIS A 474 ? 0.4529 0.6152 0.7004 0.0992  0.0535  -0.0563 277  HIS A CB  
3581 C CG  . HIS A 474 ? 0.5081 0.7113 0.8080 0.1140  0.0669  -0.0635 277  HIS A CG  
3582 N ND1 . HIS A 474 ? 0.5493 0.7468 0.8533 0.1396  0.0727  -0.0705 277  HIS A ND1 
3583 C CD2 . HIS A 474 ? 0.5033 0.7551 0.8586 0.1071  0.0768  -0.0652 277  HIS A CD2 
3584 C CE1 . HIS A 474 ? 0.5495 0.7946 0.9133 0.1492  0.0866  -0.0765 277  HIS A CE1 
3585 N NE2 . HIS A 474 ? 0.5153 0.7953 0.9133 0.1284  0.0894  -0.0733 277  HIS A NE2 
3586 N N   . LEU A 475 ? 0.4569 0.6544 0.7485 0.0882  0.0034  -0.0484 278  LEU A N   
3587 C CA  . LEU A 475 ? 0.4449 0.6740 0.7772 0.0898  -0.0162 -0.0502 278  LEU A CA  
3588 C C   . LEU A 475 ? 0.4637 0.6679 0.7747 0.1057  -0.0437 -0.0481 278  LEU A C   
3589 O O   . LEU A 475 ? 0.4719 0.6976 0.8161 0.1193  -0.0635 -0.0523 278  LEU A O   
3590 C CB  . LEU A 475 ? 0.4154 0.6545 0.7519 0.0657  -0.0179 -0.0468 278  LEU A CB  
3591 C CG  . LEU A 475 ? 0.4270 0.6936 0.7920 0.0509  0.0078  -0.0486 278  LEU A CG  
3592 C CD1 . LEU A 475 ? 0.3941 0.6536 0.7450 0.0266  0.0072  -0.0436 278  LEU A CD1 
3593 C CD2 . LEU A 475 ? 0.4494 0.7666 0.8840 0.0570  0.0104  -0.0559 278  LEU A CD2 
3594 N N   . LYS A 476 ? 0.4701 0.6281 0.7265 0.1036  -0.0453 -0.0416 279  LYS A N   
3595 C CA  . LYS A 476 ? 0.5171 0.6418 0.7429 0.1173  -0.0668 -0.0377 279  LYS A CA  
3596 C C   . LYS A 476 ? 0.5287 0.6477 0.7620 0.1439  -0.0721 -0.0420 279  LYS A C   
3597 O O   . LYS A 476 ? 0.5277 0.6379 0.7593 0.1614  -0.0959 -0.0420 279  LYS A O   
3598 C CB  . LYS A 476 ? 0.5584 0.6365 0.7296 0.1063  -0.0608 -0.0292 279  LYS A CB  
3599 C CG  . LYS A 476 ? 0.6327 0.6671 0.7620 0.1173  -0.0774 -0.0227 279  LYS A CG  
3600 C CD  . LYS A 476 ? 0.7193 0.7223 0.8288 0.1345  -0.0762 -0.0225 279  LYS A CD  
3601 C CE  . LYS A 476 ? 0.7859 0.7325 0.8410 0.1402  -0.0860 -0.0131 279  LYS A CE  
3602 N NZ  . LYS A 476 ? 0.8151 0.7616 0.8599 0.1406  -0.1041 -0.0103 279  LYS A NZ  
3603 N N   . THR A 477 ? 0.5518 0.6720 0.7901 0.1489  -0.0515 -0.0462 280  THR A N   
3604 C CA  . THR A 477 ? 0.6234 0.7317 0.8638 0.1761  -0.0547 -0.0510 280  THR A CA  
3605 C C   . THR A 477 ? 0.5957 0.7538 0.8996 0.1947  -0.0641 -0.0593 280  THR A C   
3606 O O   . THR A 477 ? 0.6406 0.7897 0.9495 0.2214  -0.0805 -0.0621 280  THR A O   
3607 C CB  . THR A 477 ? 0.6747 0.7645 0.8968 0.1773  -0.0297 -0.0547 280  THR A CB  
3608 O OG1 . THR A 477 ? 0.6950 0.8279 0.9567 0.1716  -0.0075 -0.0612 280  THR A OG1 
3609 C CG2 . THR A 477 ? 0.6425 0.6889 0.8120 0.1563  -0.0237 -0.0477 280  THR A CG2 
3610 N N   . ILE A 478 ? 0.5074 0.7177 0.8628 0.1810  -0.0545 -0.0633 281  ILE A N   
3611 C CA  . ILE A 478 ? 0.4491 0.7148 0.8786 0.1958  -0.0628 -0.0720 281  ILE A CA  
3612 C C   . ILE A 478 ? 0.4251 0.7068 0.8741 0.1907  -0.0966 -0.0710 281  ILE A C   
3613 O O   . ILE A 478 ? 0.4416 0.7730 0.9524 0.1880  -0.1029 -0.0761 281  ILE A O   
3614 C CB  . ILE A 478 ? 0.3812 0.6953 0.8616 0.1831  -0.0296 -0.0774 281  ILE A CB  
3615 C CG1 . ILE A 478 ? 0.3316 0.6495 0.8011 0.1494  -0.0210 -0.0717 281  ILE A CG1 
3616 C CG2 . ILE A 478 ? 0.3705 0.6643 0.8269 0.1929  0.0026  -0.0803 281  ILE A CG2 
3617 C CD1 . ILE A 478 ? 0.3125 0.6817 0.8413 0.1358  0.0047  -0.0761 281  ILE A CD1 
3618 N N   . ASN A 479 ? 0.4106 0.6434 0.7979 0.1867  -0.1168 -0.0629 282  ASN A N   
3619 C CA  . ASN A 479 ? 0.4212 0.6549 0.8104 0.1862  -0.1524 -0.0626 282  ASN A CA  
3620 C C   . ASN A 479 ? 0.4120 0.6860 0.8407 0.1600  -0.1502 -0.0652 282  ASN A C   
3621 O O   . ASN A 479 ? 0.4133 0.7111 0.8749 0.1587  -0.1753 -0.0695 282  ASN A O   
3622 C CB  . ASN A 479 ? 0.4411 0.6874 0.8593 0.2117  -0.1797 -0.0676 282  ASN A CB  
3623 C CG  . ASN A 479 ? 0.4900 0.7082 0.8746 0.2136  -0.2179 -0.0648 282  ASN A CG  
3624 O OD1 . ASN A 479 ? 0.4920 0.6623 0.8148 0.2107  -0.2276 -0.0583 282  ASN A OD1 
3625 N ND2 . ASN A 479 ? 0.4437 0.6886 0.8660 0.2188  -0.2389 -0.0699 282  ASN A ND2 
3626 N N   . GLN A 480 ? 0.4132 0.6881 0.8308 0.1363  -0.1191 -0.0616 283  GLN A N   
3627 C CA  . GLN A 480 ? 0.4144 0.7177 0.8600 0.1100  -0.1139 -0.0627 283  GLN A CA  
3628 C C   . GLN A 480 ? 0.4451 0.7060 0.8278 0.0912  -0.1103 -0.0543 283  GLN A C   
3629 O O   . GLN A 480 ? 0.4136 0.6821 0.7985 0.0694  -0.0918 -0.0524 283  GLN A O   
3630 C CB  . GLN A 480 ? 0.3861 0.7299 0.8795 0.0995  -0.0792 -0.0661 283  GLN A CB  
3631 C CG  . GLN A 480 ? 0.3789 0.7736 0.9450 0.1119  -0.0792 -0.0738 283  GLN A CG  
3632 C CD  . GLN A 480 ? 0.3744 0.7920 0.9723 0.1004  -0.1040 -0.0753 283  GLN A CD  
3633 O OE1 . GLN A 480 ? 0.4009 0.8412 1.0340 0.1133  -0.1180 -0.0789 283  GLN A OE1 
3634 N NE2 . GLN A 480 ? 0.3632 0.7734 0.9488 0.0764  -0.1103 -0.0734 283  GLN A NE2 
3635 N N   . GLU A 481 ? 0.4736 0.6872 0.7988 0.1009  -0.1268 -0.0489 284  GLU A N   
3636 C CA  . GLU A 481 ? 0.4463 0.6200 0.7146 0.0864  -0.1212 -0.0412 284  GLU A CA  
3637 C C   . GLU A 481 ? 0.4233 0.6084 0.7014 0.0679  -0.1305 -0.0432 284  GLU A C   
3638 O O   . GLU A 481 ? 0.3977 0.5640 0.6462 0.0523  -0.1176 -0.0385 284  GLU A O   
3639 C CB  . GLU A 481 ? 0.4778 0.5999 0.6872 0.1009  -0.1365 -0.0353 284  GLU A CB  
3640 C CG  . GLU A 481 ? 0.5336 0.6156 0.6885 0.0880  -0.1216 -0.0267 284  GLU A CG  
3641 C CD  . GLU A 481 ? 0.6129 0.6409 0.7089 0.1006  -0.1271 -0.0192 284  GLU A CD  
3642 O OE1 . GLU A 481 ? 0.6960 0.7122 0.7881 0.1200  -0.1374 -0.0194 284  GLU A OE1 
3643 O OE2 . GLU A 481 ? 0.5856 0.5811 0.6389 0.0916  -0.1191 -0.0128 284  GLU A OE2 
3644 N N   . SER A 482 ? 0.4660 0.6808 0.7874 0.0699  -0.1545 -0.0509 285  SER A N   
3645 C CA  . SER A 482 ? 0.5055 0.7289 0.8384 0.0506  -0.1656 -0.0543 285  SER A CA  
3646 C C   . SER A 482 ? 0.4693 0.7157 0.8277 0.0272  -0.1365 -0.0532 285  SER A C   
3647 O O   . SER A 482 ? 0.4815 0.7190 0.8300 0.0095  -0.1394 -0.0533 285  SER A O   
3648 C CB  . SER A 482 ? 0.5255 0.7818 0.9117 0.0557  -0.1990 -0.0643 285  SER A CB  
3649 O OG  . SER A 482 ? 0.5142 0.8231 0.9723 0.0614  -0.1888 -0.0695 285  SER A OG  
3650 N N   . CYS A 483 ? 0.3975 0.6667 0.7817 0.0279  -0.1090 -0.0523 286  CYS A N   
3651 C CA  . CYS A 483 ? 0.3689 0.6540 0.7702 0.0079  -0.0805 -0.0506 286  CYS A CA  
3652 C C   . CYS A 483 ? 0.3679 0.6151 0.7127 0.0007  -0.0618 -0.0426 286  CYS A C   
3653 O O   . CYS A 483 ? 0.3820 0.6324 0.7287 -0.0142 -0.0403 -0.0401 286  CYS A O   
3654 C CB  . CYS A 483 ? 0.3626 0.6857 0.8131 0.0131  -0.0579 -0.0539 286  CYS A CB  
3655 S SG  . CYS A 483 ? 0.3927 0.7692 0.9244 0.0270  -0.0798 -0.0646 286  CYS A SG  
3656 N N   . ILE A 484 ? 0.3531 0.5639 0.6488 0.0112  -0.0687 -0.0382 287  ILE A N   
3657 C CA  . ILE A 484 ? 0.2852 0.4669 0.5392 0.0054  -0.0515 -0.0316 287  ILE A CA  
3658 C C   . ILE A 484 ? 0.3228 0.4906 0.5596 -0.0105 -0.0527 -0.0294 287  ILE A C   
3659 O O   . ILE A 484 ? 0.3430 0.5029 0.5679 -0.0207 -0.0366 -0.0259 287  ILE A O   
3660 C CB  . ILE A 484 ? 0.2568 0.4065 0.4719 0.0194  -0.0561 -0.0276 287  ILE A CB  
3661 C CG1 . ILE A 484 ? 0.2854 0.4420 0.5123 0.0347  -0.0508 -0.0296 287  ILE A CG1 
3662 C CG2 . ILE A 484 ? 0.2209 0.3440 0.4015 0.0115  -0.0435 -0.0217 287  ILE A CG2 
3663 C CD1 . ILE A 484 ? 0.3059 0.4252 0.4929 0.0469  -0.0538 -0.0249 287  ILE A CD1 
3664 N N   . GLU A 485 ? 0.3167 0.4755 0.5460 -0.0112 -0.0735 -0.0318 288  GLU A N   
3665 C CA  . GLU A 485 ? 0.3779 0.5179 0.5864 -0.0245 -0.0743 -0.0306 288  GLU A CA  
3666 C C   . GLU A 485 ? 0.3600 0.5212 0.6010 -0.0423 -0.0670 -0.0327 288  GLU A C   
3667 O O   . GLU A 485 ? 0.3349 0.4808 0.5579 -0.0526 -0.0536 -0.0287 288  GLU A O   
3668 C CB  . GLU A 485 ? 0.4207 0.5372 0.6032 -0.0190 -0.0980 -0.0335 288  GLU A CB  
3669 C CG  . GLU A 485 ? 0.4648 0.5531 0.6164 -0.0291 -0.0980 -0.0331 288  GLU A CG  
3670 C CD  . GLU A 485 ? 0.4920 0.5540 0.6066 -0.0246 -0.0797 -0.0263 288  GLU A CD  
3671 O OE1 . GLU A 485 ? 0.4754 0.5328 0.5795 -0.0140 -0.0715 -0.0220 288  GLU A OE1 
3672 O OE2 . GLU A 485 ? 0.5153 0.5606 0.6138 -0.0318 -0.0737 -0.0254 288  GLU A OE2 
3673 N N   . PRO A 486 ? 0.3681 0.5629 0.6575 -0.0472 -0.0730 -0.0382 289  PRO A N   
3674 C CA  . PRO A 486 ? 0.3517 0.5662 0.6741 -0.0669 -0.0583 -0.0386 289  PRO A CA  
3675 C C   . PRO A 486 ? 0.3657 0.5778 0.6777 -0.0690 -0.0281 -0.0325 289  PRO A C   
3676 O O   . PRO A 486 ? 0.3600 0.5632 0.6664 -0.0850 -0.0133 -0.0291 289  PRO A O   
3677 C CB  . PRO A 486 ? 0.3107 0.5701 0.6979 -0.0675 -0.0678 -0.0461 289  PRO A CB  
3678 C CG  . PRO A 486 ? 0.3224 0.5762 0.7013 -0.0492 -0.0990 -0.0508 289  PRO A CG  
3679 C CD  . PRO A 486 ? 0.3309 0.5483 0.6506 -0.0338 -0.0928 -0.0442 289  PRO A CD  
3680 N N   . LEU A 487 ? 0.2952 0.5082 0.5976 -0.0528 -0.0200 -0.0312 290  LEU A N   
3681 C CA  . LEU A 487 ? 0.2629 0.4637 0.5433 -0.0533 0.0038  -0.0265 290  LEU A CA  
3682 C C   . LEU A 487 ? 0.2916 0.4553 0.5245 -0.0570 0.0031  -0.0209 290  LEU A C   
3683 O O   . LEU A 487 ? 0.3207 0.4695 0.5353 -0.0652 0.0173  -0.0169 290  LEU A O   
3684 C CB  . LEU A 487 ? 0.2545 0.4592 0.5327 -0.0350 0.0084  -0.0279 290  LEU A CB  
3685 C CG  . LEU A 487 ? 0.2821 0.4696 0.5327 -0.0328 0.0291  -0.0251 290  LEU A CG  
3686 C CD1 . LEU A 487 ? 0.3426 0.5451 0.6119 -0.0418 0.0536  -0.0256 290  LEU A CD1 
3687 C CD2 . LEU A 487 ? 0.2781 0.4607 0.5203 -0.0143 0.0279  -0.0275 290  LEU A CD2 
3688 N N   . ALA A 488 ? 0.3017 0.4484 0.5134 -0.0496 -0.0126 -0.0205 291  ALA A N   
3689 C CA  . ALA A 488 ? 0.2960 0.4135 0.4725 -0.0508 -0.0125 -0.0162 291  ALA A CA  
3690 C C   . ALA A 488 ? 0.3274 0.4331 0.4984 -0.0651 -0.0131 -0.0152 291  ALA A C   
3691 O O   . ALA A 488 ? 0.3420 0.4268 0.4899 -0.0682 -0.0071 -0.0112 291  ALA A O   
3692 C CB  . ALA A 488 ? 0.2421 0.3449 0.4001 -0.0399 -0.0241 -0.0160 291  ALA A CB  
3693 N N   . GLU A 489 ? 0.3223 0.4387 0.5139 -0.0733 -0.0225 -0.0192 292  GLU A N   
3694 C CA  . GLU A 489 ? 0.4024 0.5038 0.5889 -0.0888 -0.0236 -0.0188 292  GLU A CA  
3695 C C   . GLU A 489 ? 0.4100 0.5134 0.6031 -0.1019 -0.0037 -0.0146 292  GLU A C   
3696 O O   . GLU A 489 ? 0.4068 0.4820 0.5736 -0.1095 0.0013  -0.0102 292  GLU A O   
3697 C CB  . GLU A 489 ? 0.4141 0.5264 0.6250 -0.0967 -0.0417 -0.0256 292  GLU A CB  
3698 C CG  . GLU A 489 ? 0.5063 0.6084 0.6995 -0.0822 -0.0617 -0.0295 292  GLU A CG  
3699 C CD  . GLU A 489 ? 0.5945 0.7050 0.8082 -0.0869 -0.0857 -0.0377 292  GLU A CD  
3700 O OE1 . GLU A 489 ? 0.6314 0.7162 0.8129 -0.0780 -0.1032 -0.0409 292  GLU A OE1 
3701 O OE2 . GLU A 489 ? 0.6296 0.7710 0.8912 -0.0996 -0.0873 -0.0413 292  GLU A OE2 
3702 N N   . SER A 490 ? 0.4079 0.5400 0.6317 -0.1033 0.0094  -0.0156 293  SER A N   
3703 C CA  . SER A 490 ? 0.4215 0.5507 0.6451 -0.1153 0.0334  -0.0110 293  SER A CA  
3704 C C   . SER A 490 ? 0.4284 0.5251 0.6029 -0.1073 0.0428  -0.0050 293  SER A C   
3705 O O   . SER A 490 ? 0.5114 0.5804 0.6587 -0.1169 0.0539  0.0008  293  SER A O   
3706 C CB  . SER A 490 ? 0.4433 0.6127 0.7147 -0.1167 0.0481  -0.0146 293  SER A CB  
3707 O OG  . SER A 490 ? 0.5266 0.6877 0.7888 -0.1261 0.0772  -0.0094 293  SER A OG  
3708 N N   . ILE A 491 ? 0.3479 0.4466 0.5122 -0.0903 0.0370  -0.0065 294  ILE A N   
3709 C CA  . ILE A 491 ? 0.3738 0.4419 0.4957 -0.0833 0.0392  -0.0023 294  ILE A CA  
3710 C C   . ILE A 491 ? 0.4053 0.4435 0.5006 -0.0861 0.0277  0.0013  294  ILE A C   
3711 O O   . ILE A 491 ? 0.4206 0.4285 0.4819 -0.0873 0.0311  0.0061  294  ILE A O   
3712 C CB  . ILE A 491 ? 0.3465 0.4197 0.4654 -0.0670 0.0314  -0.0051 294  ILE A CB  
3713 C CG1 . ILE A 491 ? 0.3411 0.4354 0.4782 -0.0614 0.0443  -0.0087 294  ILE A CG1 
3714 C CG2 . ILE A 491 ? 0.3021 0.3465 0.3857 -0.0611 0.0264  -0.0023 294  ILE A CG2 
3715 C CD1 . ILE A 491 ? 0.3136 0.4122 0.4523 -0.0470 0.0343  -0.0119 294  ILE A CD1 
3716 N N   . THR A 492 ? 0.3416 0.3839 0.4472 -0.0842 0.0131  -0.0015 295  THR A N   
3717 C CA  . THR A 492 ? 0.3948 0.4090 0.4760 -0.0823 0.0036  0.0006  295  THR A CA  
3718 C C   . THR A 492 ? 0.4496 0.4398 0.5163 -0.0971 0.0087  0.0043  295  THR A C   
3719 O O   . THR A 492 ? 0.4804 0.4382 0.5155 -0.0950 0.0071  0.0087  295  THR A O   
3720 C CB  . THR A 492 ? 0.4166 0.4354 0.5058 -0.0762 -0.0092 -0.0037 295  THR A CB  
3721 O OG1 . THR A 492 ? 0.4360 0.4666 0.5300 -0.0630 -0.0116 -0.0048 295  THR A OG1 
3722 C CG2 . THR A 492 ? 0.4051 0.3932 0.4702 -0.0738 -0.0159 -0.0025 295  THR A CG2 
3723 N N   . ASP A 493 ? 0.4473 0.4522 0.5385 -0.1124 0.0145  0.0025  296  ASP A N   
3724 C CA  . ASP A 493 ? 0.5452 0.5258 0.6251 -0.1302 0.0222  0.0066  296  ASP A CA  
3725 C C   . ASP A 493 ? 0.5919 0.5480 0.6402 -0.1330 0.0400  0.0145  296  ASP A C   
3726 O O   . ASP A 493 ? 0.6276 0.5415 0.6383 -0.1375 0.0409  0.0205  296  ASP A O   
3727 C CB  . ASP A 493 ? 0.5820 0.5905 0.7059 -0.1481 0.0260  0.0025  296  ASP A CB  
3728 C CG  . ASP A 493 ? 0.7131 0.6949 0.8292 -0.1708 0.0357  0.0069  296  ASP A CG  
3729 O OD1 . ASP A 493 ? 0.7693 0.7479 0.8838 -0.1822 0.0596  0.0130  296  ASP A OD1 
3730 O OD2 . ASP A 493 ? 0.7672 0.7261 0.8744 -0.1777 0.0210  0.0046  296  ASP A OD2 
3731 N N   . VAL A 494 ? 0.5807 0.5566 0.6372 -0.1289 0.0541  0.0146  297  VAL A N   
3732 C CA  . VAL A 494 ? 0.5991 0.5449 0.6151 -0.1295 0.0712  0.0214  297  VAL A CA  
3733 C C   . VAL A 494 ? 0.5985 0.5067 0.5676 -0.1146 0.0548  0.0244  297  VAL A C   
3734 O O   . VAL A 494 ? 0.6669 0.5300 0.5902 -0.1173 0.0577  0.0315  297  VAL A O   
3735 C CB  . VAL A 494 ? 0.5967 0.5685 0.6273 -0.1244 0.0884  0.0188  297  VAL A CB  
3736 C CG1 . VAL A 494 ? 0.6397 0.5712 0.6148 -0.1212 0.1035  0.0248  297  VAL A CG1 
3737 C CG2 . VAL A 494 ? 0.5871 0.5981 0.6709 -0.1388 0.1061  0.0160  297  VAL A CG2 
3738 N N   . LEU A 495 ? 0.5378 0.4634 0.5196 -0.0988 0.0368  0.0192  298  LEU A N   
3739 C CA  . LEU A 495 ? 0.5318 0.4312 0.4837 -0.0841 0.0194  0.0205  298  LEU A CA  
3740 C C   . LEU A 495 ? 0.5793 0.4455 0.5104 -0.0847 0.0086  0.0241  298  LEU A C   
3741 O O   . LEU A 495 ? 0.6226 0.4496 0.5135 -0.0785 0.0012  0.0289  298  LEU A O   
3742 C CB  . LEU A 495 ? 0.4275 0.3556 0.4071 -0.0708 0.0059  0.0144  298  LEU A CB  
3743 C CG  . LEU A 495 ? 0.4446 0.3557 0.4113 -0.0568 -0.0132 0.0145  298  LEU A CG  
3744 C CD1 . LEU A 495 ? 0.4412 0.3242 0.3708 -0.0513 -0.0182 0.0168  298  LEU A CD1 
3745 C CD2 . LEU A 495 ? 0.4069 0.3497 0.4096 -0.0473 -0.0213 0.0090  298  LEU A CD2 
3746 N N   . VAL A 496 ? 0.5677 0.4458 0.5225 -0.0899 0.0053  0.0210  299  VAL A N   
3747 C CA  . VAL A 496 ? 0.6484 0.4965 0.5858 -0.0857 -0.0067 0.0221  299  VAL A CA  
3748 C C   . VAL A 496 ? 0.7567 0.5606 0.6582 -0.0993 0.0010  0.0293  299  VAL A C   
3749 O O   . VAL A 496 ? 0.8367 0.5989 0.7029 -0.0913 -0.0089 0.0334  299  VAL A O   
3750 C CB  . VAL A 496 ? 0.6326 0.4999 0.5978 -0.0865 -0.0124 0.0154  299  VAL A CB  
3751 C CG1 . VAL A 496 ? 0.7271 0.5573 0.6693 -0.0811 -0.0225 0.0155  299  VAL A CG1 
3752 C CG2 . VAL A 496 ? 0.5818 0.4832 0.5732 -0.0717 -0.0181 0.0101  299  VAL A CG2 
3753 N N   . ARG A 497 ? 0.7552 0.5650 0.6648 -0.1195 0.0195  0.0317  300  ARG A N   
3754 C CA  . ARG A 497 ? 0.8455 0.6108 0.7221 -0.1359 0.0307  0.0396  300  ARG A CA  
3755 C C   . ARG A 497 ? 0.8476 0.5753 0.6741 -0.1337 0.0415  0.0486  300  ARG A C   
3756 O O   . ARG A 497 ? 0.9146 0.5880 0.6952 -0.1409 0.0456  0.0570  300  ARG A O   
3757 C CB  . ARG A 497 ? 0.9145 0.7017 0.8268 -0.1615 0.0476  0.0384  300  ARG A CB  
3758 C CG  . ARG A 497 ? 0.9367 0.7617 0.8972 -0.1641 0.0343  0.0282  300  ARG A CG  
3759 C CD  . ARG A 497 ? 0.9632 0.8017 0.9588 -0.1919 0.0453  0.0268  300  ARG A CD  
3760 N NE  . ARG A 497 ? 0.9670 0.8467 0.9997 -0.2011 0.0670  0.0271  300  ARG A NE  
3761 C CZ  . ARG A 497 ? 1.0033 0.8686 1.0145 -0.2068 0.0931  0.0355  300  ARG A CZ  
3762 N NH1 . ARG A 497 ? 1.0713 0.8786 1.0197 -0.2048 0.0981  0.0451  300  ARG A NH1 
3763 N NH2 . ARG A 497 ? 0.9722 0.8777 1.0214 -0.2129 0.1147  0.0342  300  ARG A NH2 
3764 N N   . THR A 498 ? 0.7502 0.4977 0.5774 -0.1242 0.0458  0.0471  301  THR A N   
3765 C CA  . THR A 498 ? 0.7803 0.4834 0.5484 -0.1197 0.0531  0.0547  301  THR A CA  
3766 C C   . THR A 498 ? 0.7939 0.4667 0.5263 -0.0963 0.0241  0.0548  301  THR A C   
3767 O O   . THR A 498 ? 0.8766 0.4959 0.5473 -0.0913 0.0222  0.0620  301  THR A O   
3768 C CB  . THR A 498 ? 0.7738 0.5033 0.5499 -0.1193 0.0717  0.0522  301  THR A CB  
3769 O OG1 . THR A 498 ? 0.6629 0.4347 0.4747 -0.1040 0.0547  0.0430  301  THR A OG1 
3770 C CG2 . THR A 498 ? 0.8017 0.5633 0.6177 -0.1405 0.1023  0.0520  301  THR A CG2 
3771 N N   . LYS A 499 ? 0.7220 0.4273 0.4920 -0.0815 0.0017  0.0469  302  LYS A N   
3772 C CA  . LYS A 499 ? 0.7345 0.4210 0.4859 -0.0596 -0.0261 0.0458  302  LYS A CA  
3773 C C   . LYS A 499 ? 0.7527 0.4413 0.5255 -0.0494 -0.0435 0.0428  302  LYS A C   
3774 O O   . LYS A 499 ? 0.7460 0.4410 0.5303 -0.0299 -0.0658 0.0389  302  LYS A O   
3775 C CB  . LYS A 499 ? 0.6888 0.4125 0.4666 -0.0484 -0.0356 0.0384  302  LYS A CB  
3776 C CG  . LYS A 499 ? 0.6699 0.3920 0.4268 -0.0556 -0.0174 0.0392  302  LYS A CG  
3777 C CD  . LYS A 499 ? 0.7791 0.4370 0.4601 -0.0542 -0.0159 0.0471  302  LYS A CD  
3778 C CE  . LYS A 499 ? 0.8279 0.4814 0.4835 -0.0566 0.0016  0.0459  302  LYS A CE  
3779 N NZ  . LYS A 499 ? 0.9519 0.5348 0.5210 -0.0563 0.0098  0.0542  302  LYS A NZ  
3780 N N   . ARG A 500 ? 0.7581 0.4401 0.5371 -0.0618 -0.0338 0.0439  303  ARG A N   
3781 C CA  . ARG A 500 ? 0.7399 0.4193 0.5341 -0.0514 -0.0472 0.0399  303  ARG A CA  
3782 C C   . ARG A 500 ? 0.7807 0.4258 0.5489 -0.0282 -0.0704 0.0417  303  ARG A C   
3783 O O   . ARG A 500 ? 0.7146 0.3850 0.5153 -0.0095 -0.0850 0.0353  303  ARG A O   
3784 C CB  . ARG A 500 ? 0.7119 0.3659 0.4949 -0.0695 -0.0363 0.0423  303  ARG A CB  
3785 C CG  . ARG A 500 ? 0.7556 0.3923 0.5398 -0.0570 -0.0497 0.0380  303  ARG A CG  
3786 C CD  . ARG A 500 ? 0.7999 0.4246 0.5866 -0.0766 -0.0412 0.0358  303  ARG A CD  
3787 N NE  . ARG A 500 ? 0.7632 0.4410 0.5971 -0.0860 -0.0348 0.0276  303  ARG A NE  
3788 C CZ  . ARG A 500 ? 0.7021 0.4069 0.5619 -0.0720 -0.0421 0.0190  303  ARG A CZ  
3789 N NH1 . ARG A 500 ? 0.7145 0.4600 0.6083 -0.0807 -0.0377 0.0127  303  ARG A NH1 
3790 N NH2 . ARG A 500 ? 0.6179 0.3101 0.4710 -0.0481 -0.0528 0.0166  303  ARG A NH2 
3791 N N   . ASP A 501 ? 0.8786 0.4642 0.5885 -0.0288 -0.0738 0.0506  304  ASP A N   
3792 C CA  . ASP A 501 ? 0.9300 0.4759 0.6118 -0.0046 -0.1000 0.0524  304  ASP A CA  
3793 C C   . ASP A 501 ? 0.9082 0.4790 0.6079 0.0145  -0.1214 0.0479  304  ASP A C   
3794 O O   . ASP A 501 ? 0.8752 0.4553 0.5994 0.0372  -0.1441 0.0429  304  ASP A O   
3795 C CB  . ASP A 501 ? 1.0104 0.4781 0.6153 -0.0098 -0.0991 0.0644  304  ASP A CB  
3796 C CG  . ASP A 501 ? 1.0500 0.4872 0.6393 -0.0296 -0.0812 0.0687  304  ASP A CG  
3797 O OD1 . ASP A 501 ? 1.0358 0.4977 0.6642 -0.0296 -0.0806 0.0612  304  ASP A OD1 
3798 O OD2 . ASP A 501 ? 1.1167 0.5019 0.6524 -0.0462 -0.0667 0.0793  304  ASP A OD2 
3799 N N   . TRP A 502 ? 0.9114 0.4937 0.6022 0.0057  -0.1145 0.0486  305  TRP A N   
3800 C CA  . TRP A 502 ? 0.8511 0.4583 0.5626 0.0207  -0.1362 0.0425  305  TRP A CA  
3801 C C   . TRP A 502 ? 0.7848 0.4577 0.5746 0.0278  -0.1395 0.0326  305  TRP A C   
3802 O O   . TRP A 502 ? 0.7643 0.4522 0.5844 0.0467  -0.1636 0.0274  305  TRP A O   
3803 C CB  . TRP A 502 ? 0.8266 0.4323 0.5126 0.0087  -0.1242 0.0438  305  TRP A CB  
3804 C CG  . TRP A 502 ? 0.8414 0.4569 0.5335 0.0223  -0.1497 0.0377  305  TRP A CG  
3805 C CD1 . TRP A 502 ? 0.8991 0.4658 0.5385 0.0363  -0.1774 0.0396  305  TRP A CD1 
3806 C CD2 . TRP A 502 ? 0.7745 0.4498 0.5290 0.0226  -0.1524 0.0282  305  TRP A CD2 
3807 N NE1 . TRP A 502 ? 0.9099 0.5042 0.5780 0.0441  -0.1989 0.0307  305  TRP A NE1 
3808 C CE2 . TRP A 502 ? 0.8383 0.4989 0.5775 0.0349  -0.1824 0.0240  305  TRP A CE2 
3809 C CE3 . TRP A 502 ? 0.6653 0.3983 0.4807 0.0135  -0.1336 0.0231  305  TRP A CE3 
3810 C CZ2 . TRP A 502 ? 0.7723 0.4773 0.5619 0.0361  -0.1930 0.0146  305  TRP A CZ2 
3811 C CZ3 . TRP A 502 ? 0.6289 0.4020 0.4880 0.0158  -0.1416 0.0153  305  TRP A CZ3 
3812 C CH2 . TRP A 502 ? 0.6672 0.4273 0.5159 0.0259  -0.1705 0.0110  305  TRP A CH2 
3813 N N   . LEU A 503 ? 0.7548 0.4664 0.5792 0.0129  -0.1154 0.0299  306  LEU A N   
3814 C CA  . LEU A 503 ? 0.7047 0.4719 0.5938 0.0182  -0.1140 0.0218  306  LEU A CA  
3815 C C   . LEU A 503 ? 0.6726 0.4395 0.5844 0.0359  -0.1241 0.0188  306  LEU A C   
3816 O O   . LEU A 503 ? 0.6259 0.4247 0.5838 0.0503  -0.1348 0.0131  306  LEU A O   
3817 C CB  . LEU A 503 ? 0.6531 0.4507 0.5628 0.0003  -0.0884 0.0202  306  LEU A CB  
3818 C CG  . LEU A 503 ? 0.5926 0.4034 0.4962 -0.0144 -0.0751 0.0211  306  LEU A CG  
3819 C CD1 . LEU A 503 ? 0.5507 0.3753 0.4635 -0.0314 -0.0536 0.0213  306  LEU A CD1 
3820 C CD2 . LEU A 503 ? 0.4913 0.3406 0.4319 -0.0090 -0.0810 0.0151  306  LEU A CD2 
3821 N N   . VAL A 504 ? 0.7058 0.4373 0.5885 0.0348  -0.1190 0.0222  307  VAL A N   
3822 C CA  . VAL A 504 ? 0.7051 0.4279 0.6015 0.0549  -0.1282 0.0189  307  VAL A CA  
3823 C C   . VAL A 504 ? 0.6926 0.4044 0.5927 0.0782  -0.1569 0.0184  307  VAL A C   
3824 O O   . VAL A 504 ? 0.6831 0.4232 0.6313 0.0972  -0.1650 0.0121  307  VAL A O   
3825 C CB  . VAL A 504 ? 0.7812 0.4548 0.6342 0.0491  -0.1212 0.0229  307  VAL A CB  
3826 C CG1 . VAL A 504 ? 0.8037 0.4524 0.6561 0.0748  -0.1358 0.0205  307  VAL A CG1 
3827 C CG2 . VAL A 504 ? 0.7796 0.4741 0.6478 0.0317  -0.0987 0.0191  307  VAL A CG2 
3828 N N   . LYS A 505 ? 0.7127 0.3837 0.5633 0.0775  -0.1725 0.0247  308  LYS A N   
3829 C CA  . LYS A 505 ? 0.7835 0.4425 0.6351 0.1001  -0.2061 0.0234  308  LYS A CA  
3830 C C   . LYS A 505 ? 0.7699 0.4880 0.6871 0.1053  -0.2173 0.0150  308  LYS A C   
3831 O O   . LYS A 505 ? 0.7927 0.5211 0.7424 0.1266  -0.2452 0.0103  308  LYS A O   
3832 C CB  . LYS A 505 ? 0.9182 0.5158 0.6928 0.0969  -0.2197 0.0318  308  LYS A CB  
3833 C CG  . LYS A 505 ? 1.0316 0.6051 0.7960 0.1229  -0.2617 0.0305  308  LYS A CG  
3834 C CD  . LYS A 505 ? 1.1494 0.6354 0.8165 0.1268  -0.2757 0.0413  308  LYS A CD  
3835 C CE  . LYS A 505 ? 1.1912 0.6595 0.8574 0.1538  -0.3118 0.0360  308  LYS A CE  
3836 N NZ  . LYS A 505 ? 1.2793 0.6821 0.8597 0.1530  -0.3244 0.0395  308  LYS A NZ  
3837 N N   . GLN A 506 ? 0.7264 0.4830 0.6662 0.0862  -0.1978 0.0129  309  GLN A N   
3838 C CA  . GLN A 506 ? 0.6836 0.4930 0.6857 0.0881  -0.2061 0.0052  309  GLN A CA  
3839 C C   . GLN A 506 ? 0.6540 0.5152 0.7278 0.0933  -0.1901 -0.0006 309  GLN A C   
3840 O O   . GLN A 506 ? 0.6621 0.5683 0.7909 0.0909  -0.1900 -0.0060 309  GLN A O   
3841 C CB  . GLN A 506 ? 0.6547 0.4764 0.6453 0.0672  -0.1926 0.0055  309  GLN A CB  
3842 C CG  . GLN A 506 ? 0.7377 0.5071 0.6525 0.0605  -0.1994 0.0113  309  GLN A CG  
3843 C CD  . GLN A 506 ? 0.8355 0.5686 0.7227 0.0782  -0.2386 0.0107  309  GLN A CD  
3844 O OE1 . GLN A 506 ? 0.7894 0.5501 0.7232 0.0886  -0.2645 0.0031  309  GLN A OE1 
3845 N NE2 . GLN A 506 ? 0.9446 0.6136 0.7549 0.0806  -0.2441 0.0187  309  GLN A NE2 
3846 N N   . ARG A 507 ? 0.6664 0.5175 0.7374 0.1005  -0.1762 0.0002  310  ARG A N   
3847 C CA  . ARG A 507 ? 0.6343 0.5249 0.7573 0.1042  -0.1536 -0.0048 310  ARG A CA  
3848 C C   . ARG A 507 ? 0.6050 0.5206 0.7328 0.0824  -0.1280 -0.0044 310  ARG A C   
3849 O O   . ARG A 507 ? 0.5843 0.5411 0.7611 0.0812  -0.1135 -0.0083 310  ARG A O   
3850 C CB  . ARG A 507 ? 0.6469 0.5801 0.8440 0.1219  -0.1648 -0.0115 310  ARG A CB  
3851 C CG  . ARG A 507 ? 0.7036 0.6168 0.9064 0.1491  -0.1899 -0.0133 310  ARG A CG  
3852 C CD  . ARG A 507 ? 0.7027 0.6684 0.9949 0.1669  -0.1970 -0.0211 310  ARG A CD  
3853 N NE  . ARG A 507 ? 0.7054 0.7064 1.0399 0.1571  -0.2140 -0.0242 310  ARG A NE  
3854 C CZ  . ARG A 507 ? 0.7004 0.7523 1.0942 0.1446  -0.1937 -0.0276 310  ARG A CZ  
3855 N NH1 . ARG A 507 ? 0.7050 0.7769 1.1186 0.1422  -0.1551 -0.0277 310  ARG A NH1 
3856 N NH2 . ARG A 507 ? 0.6839 0.7611 1.1120 0.1342  -0.2118 -0.0307 310  ARG A NH2 
3857 N N   . GLY A 508 ? 0.5843 0.4737 0.6613 0.0654  -0.1219 0.0005  311  GLY A N   
3858 C CA  . GLY A 508 ? 0.5477 0.4576 0.6273 0.0475  -0.0998 0.0006  311  GLY A CA  
3859 C C   . GLY A 508 ? 0.4901 0.4394 0.6109 0.0430  -0.0990 -0.0024 311  GLY A C   
3860 O O   . GLY A 508 ? 0.4872 0.4403 0.6187 0.0463  -0.1183 -0.0037 311  GLY A O   
3861 N N   . TRP A 509 ? 0.4564 0.4304 0.5971 0.0358  -0.0782 -0.0038 312  TRP A N   
3862 C CA  . TRP A 509 ? 0.4207 0.4257 0.5944 0.0289  -0.0740 -0.0056 312  TRP A CA  
3863 C C   . TRP A 509 ? 0.4502 0.4840 0.6813 0.0390  -0.0806 -0.0095 312  TRP A C   
3864 O O   . TRP A 509 ? 0.4328 0.4893 0.6943 0.0318  -0.0817 -0.0112 312  TRP A O   
3865 C CB  . TRP A 509 ? 0.3637 0.3787 0.5346 0.0200  -0.0508 -0.0049 312  TRP A CB  
3866 C CG  . TRP A 509 ? 0.4131 0.4111 0.5435 0.0079  -0.0483 -0.0024 312  TRP A CG  
3867 C CD1 . TRP A 509 ? 0.4372 0.4150 0.5373 0.0042  -0.0430 -0.0011 312  TRP A CD1 
3868 C CD2 . TRP A 509 ? 0.4288 0.4293 0.5486 -0.0023 -0.0510 -0.0017 312  TRP A CD2 
3869 N NE1 . TRP A 509 ? 0.4690 0.4422 0.5480 -0.0086 -0.0410 0.0007  312  TRP A NE1 
3870 C CE2 . TRP A 509 ? 0.4524 0.4390 0.5415 -0.0112 -0.0444 0.0004  312  TRP A CE2 
3871 C CE3 . TRP A 509 ? 0.4255 0.4377 0.5603 -0.0047 -0.0579 -0.0033 312  TRP A CE3 
3872 C CZ2 . TRP A 509 ? 0.4463 0.4334 0.5221 -0.0201 -0.0414 0.0010  312  TRP A CZ2 
3873 C CZ3 . TRP A 509 ? 0.3947 0.4010 0.5075 -0.0130 -0.0563 -0.0030 312  TRP A CZ3 
3874 C CH2 . TRP A 509 ? 0.4090 0.4048 0.4943 -0.0195 -0.0467 -0.0008 312  TRP A CH2 
3875 N N   . ASP A 510 ? 0.4722 0.5063 0.7230 0.0552  -0.0848 -0.0114 313  ASP A N   
3876 C CA  . ASP A 510 ? 0.4373 0.5027 0.7515 0.0652  -0.0953 -0.0158 313  ASP A CA  
3877 C C   . ASP A 510 ? 0.4328 0.4923 0.7470 0.0650  -0.1297 -0.0176 313  ASP A C   
3878 O O   . ASP A 510 ? 0.4152 0.5037 0.7795 0.0616  -0.1401 -0.0216 313  ASP A O   
3879 C CB  . ASP A 510 ? 0.4730 0.5400 0.8101 0.0862  -0.0929 -0.0182 313  ASP A CB  
3880 C CG  . ASP A 510 ? 0.5110 0.5883 0.8588 0.0885  -0.0579 -0.0186 313  ASP A CG  
3881 O OD1 . ASP A 510 ? 0.5083 0.6087 0.8785 0.0770  -0.0376 -0.0180 313  ASP A OD1 
3882 O OD2 . ASP A 510 ? 0.5623 0.6187 0.8900 0.1023  -0.0504 -0.0195 313  ASP A OD2 
3883 N N   . GLY A 511 ? 0.4078 0.4258 0.6627 0.0672  -0.1473 -0.0145 314  GLY A N   
3884 C CA  . GLY A 511 ? 0.4128 0.4137 0.6502 0.0672  -0.1792 -0.0159 314  GLY A CA  
3885 C C   . GLY A 511 ? 0.4084 0.4168 0.6403 0.0495  -0.1763 -0.0170 314  GLY A C   
3886 O O   . GLY A 511 ? 0.4107 0.4286 0.6667 0.0483  -0.1991 -0.0221 314  GLY A O   
3887 N N   . PHE A 512 ? 0.3972 0.3994 0.5975 0.0365  -0.1505 -0.0131 315  PHE A N   
3888 C CA  . PHE A 512 ? 0.3966 0.4067 0.5942 0.0221  -0.1439 -0.0144 315  PHE A CA  
3889 C C   . PHE A 512 ? 0.4134 0.4604 0.6763 0.0190  -0.1470 -0.0195 315  PHE A C   
3890 O O   . PHE A 512 ? 0.4360 0.4817 0.7061 0.0144  -0.1672 -0.0241 315  PHE A O   
3891 C CB  . PHE A 512 ? 0.3979 0.4087 0.5739 0.0121  -0.1137 -0.0103 315  PHE A CB  
3892 C CG  . PHE A 512 ? 0.4177 0.4336 0.5879 0.0001  -0.1058 -0.0115 315  PHE A CG  
3893 C CD1 . PHE A 512 ? 0.4489 0.4395 0.5776 -0.0036 -0.1158 -0.0124 315  PHE A CD1 
3894 C CD2 . PHE A 512 ? 0.3912 0.4319 0.5923 -0.0057 -0.0870 -0.0115 315  PHE A CD2 
3895 C CE1 . PHE A 512 ? 0.4695 0.4623 0.5913 -0.0120 -0.1070 -0.0142 315  PHE A CE1 
3896 C CE2 . PHE A 512 ? 0.4256 0.4661 0.6183 -0.0146 -0.0805 -0.0123 315  PHE A CE2 
3897 C CZ  . PHE A 512 ? 0.4355 0.4534 0.5904 -0.0171 -0.0909 -0.0142 315  PHE A CZ  
3898 N N   . VAL A 513 ? 0.4156 0.4926 0.7249 0.0209  -0.1262 -0.0190 316  VAL A N   
3899 C CA  . VAL A 513 ? 0.4199 0.5329 0.7958 0.0155  -0.1222 -0.0226 316  VAL A CA  
3900 C C   . VAL A 513 ? 0.4618 0.5877 0.8820 0.0217  -0.1561 -0.0291 316  VAL A C   
3901 O O   . VAL A 513 ? 0.4721 0.6141 0.9300 0.0116  -0.1677 -0.0337 316  VAL A O   
3902 C CB  . VAL A 513 ? 0.4091 0.5460 0.8204 0.0197  -0.0906 -0.0203 316  VAL A CB  
3903 C CG1 . VAL A 513 ? 0.3623 0.5380 0.8507 0.0145  -0.0834 -0.0233 316  VAL A CG1 
3904 C CG2 . VAL A 513 ? 0.4032 0.5255 0.7708 0.0124  -0.0624 -0.0150 316  VAL A CG2 
3905 N N   . GLU A 514 ? 0.4989 0.6158 0.9161 0.0387  -0.1753 -0.0301 317  GLU A N   
3906 C CA  . GLU A 514 ? 0.5275 0.6571 0.9899 0.0477  -0.2129 -0.0370 317  GLU A CA  
3907 C C   . GLU A 514 ? 0.5458 0.6412 0.9615 0.0426  -0.2478 -0.0403 317  GLU A C   
3908 O O   . GLU A 514 ? 0.5300 0.6293 0.9679 0.0380  -0.2661 -0.0467 317  GLU A O   
3909 C CB  . GLU A 514 ? 0.5690 0.6923 1.0346 0.0705  -0.2248 -0.0369 317  GLU A CB  
3910 C CG  . GLU A 514 ? 0.6549 0.7826 1.1479 0.0784  -0.2523 -0.0436 317  GLU A CG  
3911 C CD  . GLU A 514 ? 0.7309 0.8910 1.2822 0.0924  -0.2377 -0.0454 317  GLU A CD  
3912 O OE1 . GLU A 514 ? 0.7423 0.9020 1.2873 0.1031  -0.2145 -0.0413 317  GLU A OE1 
3913 O OE2 . GLU A 514 ? 0.7739 0.9582 1.3767 0.0934  -0.2493 -0.0515 317  GLU A OE2 
3914 N N   . PHE A 515 ? 0.5593 0.6086 0.8888 0.0411  -0.2440 -0.0352 318  PHE A N   
3915 C CA  . PHE A 515 ? 0.5941 0.6022 0.8663 0.0389  -0.2729 -0.0379 318  PHE A CA  
3916 C C   . PHE A 515 ? 0.6146 0.6328 0.9036 0.0222  -0.2745 -0.0435 318  PHE A C   
3917 O O   . PHE A 515 ? 0.6344 0.6347 0.9149 0.0217  -0.3079 -0.0507 318  PHE A O   
3918 C CB  . PHE A 515 ? 0.5975 0.5581 0.7795 0.0388  -0.2579 -0.0303 318  PHE A CB  
3919 C CG  . PHE A 515 ? 0.6798 0.5915 0.7913 0.0371  -0.2791 -0.0323 318  PHE A CG  
3920 C CD1 . PHE A 515 ? 0.7071 0.5764 0.7743 0.0508  -0.3139 -0.0329 318  PHE A CD1 
3921 C CD2 . PHE A 515 ? 0.6882 0.5922 0.7744 0.0233  -0.2646 -0.0340 318  PHE A CD2 
3922 C CE1 . PHE A 515 ? 0.7737 0.5906 0.7665 0.0503  -0.3322 -0.0349 318  PHE A CE1 
3923 C CE2 . PHE A 515 ? 0.7209 0.5753 0.7370 0.0237  -0.2815 -0.0368 318  PHE A CE2 
3924 C CZ  . PHE A 515 ? 0.7603 0.5700 0.7275 0.0367  -0.3145 -0.0372 318  PHE A CZ  
3925 N N   . PHE A 516 ? 0.6115 0.6518 0.9182 0.0093  -0.2390 -0.0405 319  PHE A N   
3926 C CA  . PHE A 516 ? 0.6530 0.6974 0.9710 -0.0063 -0.2370 -0.0448 319  PHE A CA  
3927 C C   . PHE A 516 ? 0.6690 0.7587 1.0751 -0.0146 -0.2327 -0.0482 319  PHE A C   
3928 O O   . PHE A 516 ? 0.6025 0.6975 1.0215 -0.0291 -0.2190 -0.0490 319  PHE A O   
3929 C CB  . PHE A 516 ? 0.6070 0.6402 0.8829 -0.0145 -0.2020 -0.0391 319  PHE A CB  
3930 C CG  . PHE A 516 ? 0.5947 0.5833 0.7879 -0.0111 -0.2037 -0.0374 319  PHE A CG  
3931 C CD1 . PHE A 516 ? 0.6106 0.5648 0.7630 -0.0128 -0.2264 -0.0437 319  PHE A CD1 
3932 C CD2 . PHE A 516 ? 0.5639 0.5428 0.7203 -0.0067 -0.1818 -0.0300 319  PHE A CD2 
3933 C CE1 . PHE A 516 ? 0.6394 0.5509 0.7139 -0.0092 -0.2218 -0.0418 319  PHE A CE1 
3934 C CE2 . PHE A 516 ? 0.6072 0.5470 0.6927 -0.0053 -0.1784 -0.0277 319  PHE A CE2 
3935 C CZ  . PHE A 516 ? 0.6500 0.5561 0.6937 -0.0060 -0.1964 -0.0333 319  PHE A CZ  
3936 N N   . HIS A 517 ? 0.7556 0.8695 1.2081 -0.0045 -0.2341 -0.0484 320  HIS A N   
3937 C CA  . HIS A 517 ? 0.8173 0.9670 1.3394 -0.0117 -0.2191 -0.0499 320  HIS A CA  
3938 C C   . HIS A 517 ? 0.8612 1.0013 1.3923 -0.0215 -0.2434 -0.0570 320  HIS A C   
3939 O O   . HIS A 517 ? 0.9248 1.0371 1.4251 -0.0146 -0.2792 -0.0625 320  HIS A O   
3940 C CB  . HIS A 517 ? 0.8737 1.0492 1.4418 0.0029  -0.2184 -0.0504 320  HIS A CB  
3941 C CG  . HIS A 517 ? 0.9074 1.1224 1.5467 -0.0042 -0.1937 -0.0505 320  HIS A CG  
3942 N ND1 . HIS A 517 ? 0.9442 1.1773 1.6349 -0.0057 -0.2110 -0.0568 320  HIS A ND1 
3943 C CD2 . HIS A 517 ? 0.8940 1.1312 1.5588 -0.0104 -0.1523 -0.0449 320  HIS A CD2 
3944 C CE1 . HIS A 517 ? 0.9378 1.2050 1.6857 -0.0133 -0.1801 -0.0548 320  HIS A CE1 
3945 N NE2 . HIS A 517 ? 0.9078 1.1752 1.6370 -0.0158 -0.1434 -0.0473 320  HIS A NE2 
3946 N N   . VAL A 518 ? 0.8279 0.9866 1.3971 -0.0372 -0.2239 -0.0566 321  VAL A N   
3947 C CA  . VAL A 518 ? 0.8328 0.9863 1.4208 -0.0482 -0.2448 -0.0633 321  VAL A CA  
3948 C C   . VAL A 518 ? 0.8229 1.0042 1.4744 -0.0427 -0.2605 -0.0682 321  VAL A C   
3949 O O   . VAL A 518 ? 0.8480 1.0128 1.4891 -0.0339 -0.2983 -0.0749 321  VAL A O   
3950 C CB  . VAL A 518 ? 0.8074 0.9680 1.4130 -0.0677 -0.2176 -0.0604 321  VAL A CB  
3951 C CG1 . VAL A 518 ? 0.7758 0.9745 1.4355 -0.0706 -0.1781 -0.0537 321  VAL A CG1 
3952 C CG2 . VAL A 518 ? 0.8352 0.9880 1.4602 -0.0803 -0.2410 -0.0678 321  VAL A CG2 
# 
