data_8XYE
# 
_entry.id   8XYE 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8XYE         pdb_00008xye 10.2210/pdb8xye/pdb 
WWPDB D_1300044510 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-01-22 ? 
2 'Structure model' 1 1 2025-04-16 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.journal_volume'          
7  2 'Structure model' '_citation.page_first'              
8  2 'Structure model' '_citation.page_last'               
9  2 'Structure model' '_citation.pdbx_database_id_DOI'    
10 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
11 2 'Structure model' '_citation.title'                   
12 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8XYE 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              lanjun2022@hnu.edu.cn 
_pdbx_contact_author.name_first         Jun 
_pdbx_contact_author.name_last          Lan 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0009-0005-5047-7397 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lan, J.'    1 ? 
'Wang, C.H.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Virology 
_citation.journal_id_ASTM           VIRLAX 
_citation.journal_id_CSD            0922 
_citation.journal_id_ISSN           0042-6822 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            600 
_citation.language                  ? 
_citation.page_first                110241 
_citation.page_last                 110241 
_citation.title                     'Receptor binding mechanism and immune evasion capacity of SARS-CoV-2 BQ.1.1 lineage.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.virol.2024.110241 
_citation.pdbx_database_id_PubMed   39270455 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wang, C.'  1 ? 
primary 'Zhang, Y.' 2 ? 
primary 'Yang, C.'  3 ? 
primary 'Ren, W.'   4 ? 
primary 'Qiu, C.'   5 ? 
primary 'Fan, S.'   6 ? 
primary 'Ding, Q.'  7 ? 
primary 'Lan, J.'   8 ? 
# 
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 'Processed angiotensin-converting enzyme 2' 69250.781 2 ? ? ?   ? 
2 polymer     man 'Spike protein S1' 21939.711 2 ? ? RBD ? 
3 branched    syn 
'beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 586.542   3 ? 
? ?   ? 
4 branched    syn '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   1 ? ? ?   ? 
5 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   7 ? ? ?   ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;DPSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQ
LQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQL
RPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYI
SPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDP
GNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPK
HLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDET
YCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGA
KNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYA
;
;DPSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQ
LQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQL
RPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYI
SPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDP
GNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPK
HLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDET
YCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGA
KNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYA
;
B,A ? 
2 'polypeptide(L)' no no 
;TNLCPFDEVFNATRFASVYAWNRKRISNCVADYSVLYNFAPFFTFKCYGVSPTKLNDLCFTNVYADSFVIRGNEVSQIAP
GQTGNIADYNYKLPDDFTGCVIAWNSNKLDSKVGGNYNYRYRLFRKSNLKPFERDISTEIYQAGNKPCNGVAGVNCYFPL
QSYGFRPTYGVGHQPYRVVVLSFELLHAPATVCG
;
;TNLCPFDEVFNATRFASVYAWNRKRISNCVADYSVLYNFAPFFTFKCYGVSPTKLNDLCFTNVYADSFVIRGNEVSQIAP
GQTGNIADYNYKLPDDFTGCVIAWNSNKLDSKVGGNYNYRYRLFRKSNLKPFERDISTEIYQAGNKPCNGVAGVNCYFPL
QSYGFRPTYGVGHQPYRVVVLSFELLHAPATVCG
;
C,D ? 
# 
_pdbx_entity_nonpoly.entity_id   5 
_pdbx_entity_nonpoly.name        2-acetamido-2-deoxy-beta-D-glucopyranose 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASP n 
1 2   PRO n 
1 3   SER n 
1 4   THR n 
1 5   ILE n 
1 6   GLU n 
1 7   GLU n 
1 8   GLN n 
1 9   ALA n 
1 10  LYS n 
1 11  THR n 
1 12  PHE n 
1 13  LEU n 
1 14  ASP n 
1 15  LYS n 
1 16  PHE n 
1 17  ASN n 
1 18  HIS n 
1 19  GLU n 
1 20  ALA n 
1 21  GLU n 
1 22  ASP n 
1 23  LEU n 
1 24  PHE n 
1 25  TYR n 
1 26  GLN n 
1 27  SER n 
1 28  SER n 
1 29  LEU n 
1 30  ALA n 
1 31  SER n 
1 32  TRP n 
1 33  ASN n 
1 34  TYR n 
1 35  ASN n 
1 36  THR n 
1 37  ASN n 
1 38  ILE n 
1 39  THR n 
1 40  GLU n 
1 41  GLU n 
1 42  ASN n 
1 43  VAL n 
1 44  GLN n 
1 45  ASN n 
1 46  MET n 
1 47  ASN n 
1 48  ASN n 
1 49  ALA n 
1 50  GLY n 
1 51  ASP n 
1 52  LYS n 
1 53  TRP n 
1 54  SER n 
1 55  ALA n 
1 56  PHE n 
1 57  LEU n 
1 58  LYS n 
1 59  GLU n 
1 60  GLN n 
1 61  SER n 
1 62  THR n 
1 63  LEU n 
1 64  ALA n 
1 65  GLN n 
1 66  MET n 
1 67  TYR n 
1 68  PRO n 
1 69  LEU n 
1 70  GLN n 
1 71  GLU n 
1 72  ILE n 
1 73  GLN n 
1 74  ASN n 
1 75  LEU n 
1 76  THR n 
1 77  VAL n 
1 78  LYS n 
1 79  LEU n 
1 80  GLN n 
1 81  LEU n 
1 82  GLN n 
1 83  ALA n 
1 84  LEU n 
1 85  GLN n 
1 86  GLN n 
1 87  ASN n 
1 88  GLY n 
1 89  SER n 
1 90  SER n 
1 91  VAL n 
1 92  LEU n 
1 93  SER n 
1 94  GLU n 
1 95  ASP n 
1 96  LYS n 
1 97  SER n 
1 98  LYS n 
1 99  ARG n 
1 100 LEU n 
1 101 ASN n 
1 102 THR n 
1 103 ILE n 
1 104 LEU n 
1 105 ASN n 
1 106 THR n 
1 107 MET n 
1 108 SER n 
1 109 THR n 
1 110 ILE n 
1 111 TYR n 
1 112 SER n 
1 113 THR n 
1 114 GLY n 
1 115 LYS n 
1 116 VAL n 
1 117 CYS n 
1 118 ASN n 
1 119 PRO n 
1 120 ASP n 
1 121 ASN n 
1 122 PRO n 
1 123 GLN n 
1 124 GLU n 
1 125 CYS n 
1 126 LEU n 
1 127 LEU n 
1 128 LEU n 
1 129 GLU n 
1 130 PRO n 
1 131 GLY n 
1 132 LEU n 
1 133 ASN n 
1 134 GLU n 
1 135 ILE n 
1 136 MET n 
1 137 ALA n 
1 138 ASN n 
1 139 SER n 
1 140 LEU n 
1 141 ASP n 
1 142 TYR n 
1 143 ASN n 
1 144 GLU n 
1 145 ARG n 
1 146 LEU n 
1 147 TRP n 
1 148 ALA n 
1 149 TRP n 
1 150 GLU n 
1 151 SER n 
1 152 TRP n 
1 153 ARG n 
1 154 SER n 
1 155 GLU n 
1 156 VAL n 
1 157 GLY n 
1 158 LYS n 
1 159 GLN n 
1 160 LEU n 
1 161 ARG n 
1 162 PRO n 
1 163 LEU n 
1 164 TYR n 
1 165 GLU n 
1 166 GLU n 
1 167 TYR n 
1 168 VAL n 
1 169 VAL n 
1 170 LEU n 
1 171 LYS n 
1 172 ASN n 
1 173 GLU n 
1 174 MET n 
1 175 ALA n 
1 176 ARG n 
1 177 ALA n 
1 178 ASN n 
1 179 HIS n 
1 180 TYR n 
1 181 GLU n 
1 182 ASP n 
1 183 TYR n 
1 184 GLY n 
1 185 ASP n 
1 186 TYR n 
1 187 TRP n 
1 188 ARG n 
1 189 GLY n 
1 190 ASP n 
1 191 TYR n 
1 192 GLU n 
1 193 VAL n 
1 194 ASN n 
1 195 GLY n 
1 196 VAL n 
1 197 ASP n 
1 198 GLY n 
1 199 TYR n 
1 200 ASP n 
1 201 TYR n 
1 202 SER n 
1 203 ARG n 
1 204 GLY n 
1 205 GLN n 
1 206 LEU n 
1 207 ILE n 
1 208 GLU n 
1 209 ASP n 
1 210 VAL n 
1 211 GLU n 
1 212 HIS n 
1 213 THR n 
1 214 PHE n 
1 215 GLU n 
1 216 GLU n 
1 217 ILE n 
1 218 LYS n 
1 219 PRO n 
1 220 LEU n 
1 221 TYR n 
1 222 GLU n 
1 223 HIS n 
1 224 LEU n 
1 225 HIS n 
1 226 ALA n 
1 227 TYR n 
1 228 VAL n 
1 229 ARG n 
1 230 ALA n 
1 231 LYS n 
1 232 LEU n 
1 233 MET n 
1 234 ASN n 
1 235 ALA n 
1 236 TYR n 
1 237 PRO n 
1 238 SER n 
1 239 TYR n 
1 240 ILE n 
1 241 SER n 
1 242 PRO n 
1 243 ILE n 
1 244 GLY n 
1 245 CYS n 
1 246 LEU n 
1 247 PRO n 
1 248 ALA n 
1 249 HIS n 
1 250 LEU n 
1 251 LEU n 
1 252 GLY n 
1 253 ASP n 
1 254 MET n 
1 255 TRP n 
1 256 GLY n 
1 257 ARG n 
1 258 PHE n 
1 259 TRP n 
1 260 THR n 
1 261 ASN n 
1 262 LEU n 
1 263 TYR n 
1 264 SER n 
1 265 LEU n 
1 266 THR n 
1 267 VAL n 
1 268 PRO n 
1 269 PHE n 
1 270 GLY n 
1 271 GLN n 
1 272 LYS n 
1 273 PRO n 
1 274 ASN n 
1 275 ILE n 
1 276 ASP n 
1 277 VAL n 
1 278 THR n 
1 279 ASP n 
1 280 ALA n 
1 281 MET n 
1 282 VAL n 
1 283 ASP n 
1 284 GLN n 
1 285 ALA n 
1 286 TRP n 
1 287 ASP n 
1 288 ALA n 
1 289 GLN n 
1 290 ARG n 
1 291 ILE n 
1 292 PHE n 
1 293 LYS n 
1 294 GLU n 
1 295 ALA n 
1 296 GLU n 
1 297 LYS n 
1 298 PHE n 
1 299 PHE n 
1 300 VAL n 
1 301 SER n 
1 302 VAL n 
1 303 GLY n 
1 304 LEU n 
1 305 PRO n 
1 306 ASN n 
1 307 MET n 
1 308 THR n 
1 309 GLN n 
1 310 GLY n 
1 311 PHE n 
1 312 TRP n 
1 313 GLU n 
1 314 ASN n 
1 315 SER n 
1 316 MET n 
1 317 LEU n 
1 318 THR n 
1 319 ASP n 
1 320 PRO n 
1 321 GLY n 
1 322 ASN n 
1 323 VAL n 
1 324 GLN n 
1 325 LYS n 
1 326 ALA n 
1 327 VAL n 
1 328 CYS n 
1 329 HIS n 
1 330 PRO n 
1 331 THR n 
1 332 ALA n 
1 333 TRP n 
1 334 ASP n 
1 335 LEU n 
1 336 GLY n 
1 337 LYS n 
1 338 GLY n 
1 339 ASP n 
1 340 PHE n 
1 341 ARG n 
1 342 ILE n 
1 343 LEU n 
1 344 MET n 
1 345 CYS n 
1 346 THR n 
1 347 LYS n 
1 348 VAL n 
1 349 THR n 
1 350 MET n 
1 351 ASP n 
1 352 ASP n 
1 353 PHE n 
1 354 LEU n 
1 355 THR n 
1 356 ALA n 
1 357 HIS n 
1 358 HIS n 
1 359 GLU n 
1 360 MET n 
1 361 GLY n 
1 362 HIS n 
1 363 ILE n 
1 364 GLN n 
1 365 TYR n 
1 366 ASP n 
1 367 MET n 
1 368 ALA n 
1 369 TYR n 
1 370 ALA n 
1 371 ALA n 
1 372 GLN n 
1 373 PRO n 
1 374 PHE n 
1 375 LEU n 
1 376 LEU n 
1 377 ARG n 
1 378 ASN n 
1 379 GLY n 
1 380 ALA n 
1 381 ASN n 
1 382 GLU n 
1 383 GLY n 
1 384 PHE n 
1 385 HIS n 
1 386 GLU n 
1 387 ALA n 
1 388 VAL n 
1 389 GLY n 
1 390 GLU n 
1 391 ILE n 
1 392 MET n 
1 393 SER n 
1 394 LEU n 
1 395 SER n 
1 396 ALA n 
1 397 ALA n 
1 398 THR n 
1 399 PRO n 
1 400 LYS n 
1 401 HIS n 
1 402 LEU n 
1 403 LYS n 
1 404 SER n 
1 405 ILE n 
1 406 GLY n 
1 407 LEU n 
1 408 LEU n 
1 409 SER n 
1 410 PRO n 
1 411 ASP n 
1 412 PHE n 
1 413 GLN n 
1 414 GLU n 
1 415 ASP n 
1 416 ASN n 
1 417 GLU n 
1 418 THR n 
1 419 GLU n 
1 420 ILE n 
1 421 ASN n 
1 422 PHE n 
1 423 LEU n 
1 424 LEU n 
1 425 LYS n 
1 426 GLN n 
1 427 ALA n 
1 428 LEU n 
1 429 THR n 
1 430 ILE n 
1 431 VAL n 
1 432 GLY n 
1 433 THR n 
1 434 LEU n 
1 435 PRO n 
1 436 PHE n 
1 437 THR n 
1 438 TYR n 
1 439 MET n 
1 440 LEU n 
1 441 GLU n 
1 442 LYS n 
1 443 TRP n 
1 444 ARG n 
1 445 TRP n 
1 446 MET n 
1 447 VAL n 
1 448 PHE n 
1 449 LYS n 
1 450 GLY n 
1 451 GLU n 
1 452 ILE n 
1 453 PRO n 
1 454 LYS n 
1 455 ASP n 
1 456 GLN n 
1 457 TRP n 
1 458 MET n 
1 459 LYS n 
1 460 LYS n 
1 461 TRP n 
1 462 TRP n 
1 463 GLU n 
1 464 MET n 
1 465 LYS n 
1 466 ARG n 
1 467 GLU n 
1 468 ILE n 
1 469 VAL n 
1 470 GLY n 
1 471 VAL n 
1 472 VAL n 
1 473 GLU n 
1 474 PRO n 
1 475 VAL n 
1 476 PRO n 
1 477 HIS n 
1 478 ASP n 
1 479 GLU n 
1 480 THR n 
1 481 TYR n 
1 482 CYS n 
1 483 ASP n 
1 484 PRO n 
1 485 ALA n 
1 486 SER n 
1 487 LEU n 
1 488 PHE n 
1 489 HIS n 
1 490 VAL n 
1 491 SER n 
1 492 ASN n 
1 493 ASP n 
1 494 TYR n 
1 495 SER n 
1 496 PHE n 
1 497 ILE n 
1 498 ARG n 
1 499 TYR n 
1 500 TYR n 
1 501 THR n 
1 502 ARG n 
1 503 THR n 
1 504 LEU n 
1 505 TYR n 
1 506 GLN n 
1 507 PHE n 
1 508 GLN n 
1 509 PHE n 
1 510 GLN n 
1 511 GLU n 
1 512 ALA n 
1 513 LEU n 
1 514 CYS n 
1 515 GLN n 
1 516 ALA n 
1 517 ALA n 
1 518 LYS n 
1 519 HIS n 
1 520 GLU n 
1 521 GLY n 
1 522 PRO n 
1 523 LEU n 
1 524 HIS n 
1 525 LYS n 
1 526 CYS n 
1 527 ASP n 
1 528 ILE n 
1 529 SER n 
1 530 ASN n 
1 531 SER n 
1 532 THR n 
1 533 GLU n 
1 534 ALA n 
1 535 GLY n 
1 536 GLN n 
1 537 LYS n 
1 538 LEU n 
1 539 PHE n 
1 540 ASN n 
1 541 MET n 
1 542 LEU n 
1 543 ARG n 
1 544 LEU n 
1 545 GLY n 
1 546 LYS n 
1 547 SER n 
1 548 GLU n 
1 549 PRO n 
1 550 TRP n 
1 551 THR n 
1 552 LEU n 
1 553 ALA n 
1 554 LEU n 
1 555 GLU n 
1 556 ASN n 
1 557 VAL n 
1 558 VAL n 
1 559 GLY n 
1 560 ALA n 
1 561 LYS n 
1 562 ASN n 
1 563 MET n 
1 564 ASN n 
1 565 VAL n 
1 566 ARG n 
1 567 PRO n 
1 568 LEU n 
1 569 LEU n 
1 570 ASN n 
1 571 TYR n 
1 572 PHE n 
1 573 GLU n 
1 574 PRO n 
1 575 LEU n 
1 576 PHE n 
1 577 THR n 
1 578 TRP n 
1 579 LEU n 
1 580 LYS n 
1 581 ASP n 
1 582 GLN n 
1 583 ASN n 
1 584 LYS n 
1 585 ASN n 
1 586 SER n 
1 587 PHE n 
1 588 VAL n 
1 589 GLY n 
1 590 TRP n 
1 591 SER n 
1 592 THR n 
1 593 ASP n 
1 594 TRP n 
1 595 SER n 
1 596 PRO n 
1 597 TYR n 
1 598 ALA n 
2 1   THR n 
2 2   ASN n 
2 3   LEU n 
2 4   CYS n 
2 5   PRO n 
2 6   PHE n 
2 7   ASP n 
2 8   GLU n 
2 9   VAL n 
2 10  PHE n 
2 11  ASN n 
2 12  ALA n 
2 13  THR n 
2 14  ARG n 
2 15  PHE n 
2 16  ALA n 
2 17  SER n 
2 18  VAL n 
2 19  TYR n 
2 20  ALA n 
2 21  TRP n 
2 22  ASN n 
2 23  ARG n 
2 24  LYS n 
2 25  ARG n 
2 26  ILE n 
2 27  SER n 
2 28  ASN n 
2 29  CYS n 
2 30  VAL n 
2 31  ALA n 
2 32  ASP n 
2 33  TYR n 
2 34  SER n 
2 35  VAL n 
2 36  LEU n 
2 37  TYR n 
2 38  ASN n 
2 39  PHE n 
2 40  ALA n 
2 41  PRO n 
2 42  PHE n 
2 43  PHE n 
2 44  THR n 
2 45  PHE n 
2 46  LYS n 
2 47  CYS n 
2 48  TYR n 
2 49  GLY n 
2 50  VAL n 
2 51  SER n 
2 52  PRO n 
2 53  THR n 
2 54  LYS n 
2 55  LEU n 
2 56  ASN n 
2 57  ASP n 
2 58  LEU n 
2 59  CYS n 
2 60  PHE n 
2 61  THR n 
2 62  ASN n 
2 63  VAL n 
2 64  TYR n 
2 65  ALA n 
2 66  ASP n 
2 67  SER n 
2 68  PHE n 
2 69  VAL n 
2 70  ILE n 
2 71  ARG n 
2 72  GLY n 
2 73  ASN n 
2 74  GLU n 
2 75  VAL n 
2 76  SER n 
2 77  GLN n 
2 78  ILE n 
2 79  ALA n 
2 80  PRO n 
2 81  GLY n 
2 82  GLN n 
2 83  THR n 
2 84  GLY n 
2 85  ASN n 
2 86  ILE n 
2 87  ALA n 
2 88  ASP n 
2 89  TYR n 
2 90  ASN n 
2 91  TYR n 
2 92  LYS n 
2 93  LEU n 
2 94  PRO n 
2 95  ASP n 
2 96  ASP n 
2 97  PHE n 
2 98  THR n 
2 99  GLY n 
2 100 CYS n 
2 101 VAL n 
2 102 ILE n 
2 103 ALA n 
2 104 TRP n 
2 105 ASN n 
2 106 SER n 
2 107 ASN n 
2 108 LYS n 
2 109 LEU n 
2 110 ASP n 
2 111 SER n 
2 112 LYS n 
2 113 VAL n 
2 114 GLY n 
2 115 GLY n 
2 116 ASN n 
2 117 TYR n 
2 118 ASN n 
2 119 TYR n 
2 120 ARG n 
2 121 TYR n 
2 122 ARG n 
2 123 LEU n 
2 124 PHE n 
2 125 ARG n 
2 126 LYS n 
2 127 SER n 
2 128 ASN n 
2 129 LEU n 
2 130 LYS n 
2 131 PRO n 
2 132 PHE n 
2 133 GLU n 
2 134 ARG n 
2 135 ASP n 
2 136 ILE n 
2 137 SER n 
2 138 THR n 
2 139 GLU n 
2 140 ILE n 
2 141 TYR n 
2 142 GLN n 
2 143 ALA n 
2 144 GLY n 
2 145 ASN n 
2 146 LYS n 
2 147 PRO n 
2 148 CYS n 
2 149 ASN n 
2 150 GLY n 
2 151 VAL n 
2 152 ALA n 
2 153 GLY n 
2 154 VAL n 
2 155 ASN n 
2 156 CYS n 
2 157 TYR n 
2 158 PHE n 
2 159 PRO n 
2 160 LEU n 
2 161 GLN n 
2 162 SER n 
2 163 TYR n 
2 164 GLY n 
2 165 PHE n 
2 166 ARG n 
2 167 PRO n 
2 168 THR n 
2 169 TYR n 
2 170 GLY n 
2 171 VAL n 
2 172 GLY n 
2 173 HIS n 
2 174 GLN n 
2 175 PRO n 
2 176 TYR n 
2 177 ARG n 
2 178 VAL n 
2 179 VAL n 
2 180 VAL n 
2 181 LEU n 
2 182 SER n 
2 183 PHE n 
2 184 GLU n 
2 185 LEU n 
2 186 LEU n 
2 187 HIS n 
2 188 ALA n 
2 189 PRO n 
2 190 ALA n 
2 191 THR n 
2 192 VAL n 
2 193 CYS n 
2 194 GLY 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' 1 598 human                   ? 'ACE2, UNQ868/PRO1885' ? ?            ? ? ? ? 'Homo sapiens' 9606 
? ? ? ? ? ? ? ? 'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 194 '2019-nCoV, SARS-CoV-2' ? 'S, 2'                 ? Omicron/BA.4 ? ? ? ? 
'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? ? ? ? 'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
? ? ? ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
3 oligosaccharide 
4 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 3 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH                                          'Glycam Condensed Sequence' GMML       1.0   
2 3 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1' WURCS                       PDB2Glycan 1.1.0 
3 3 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}'           LINUCS                      PDB-CARE   ?     
4 4 DGlcpNAcb1-4DGlcpNAcb1-ROH                                                   'Glycam Condensed Sequence' GMML       1.0   
5 4 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1'                        WURCS                       PDB2Glycan 1.1.0 
6 4 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}'                              LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 3 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 3 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
3 4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'          y ALANINE                                  ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'          y ARGININE                                 ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'          y ASPARAGINE                               ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'          y 'ASPARTIC ACID'                          ? 'C4 H7 N O4'     133.103 
BMA 'D-saccharide, beta linking' . beta-D-mannopyranose                     'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6'      
180.156 
CYS 'L-peptide linking'          y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking'          y GLUTAMINE                                ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE                                  ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'          y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking'          y ISOLEUCINE                               ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'          y LEUCINE                                  ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'          y LYSINE                                   ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'          y METHIONINE                               ? 'C5 H11 N O2 S'  149.211 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE 'L-peptide linking'          y PHENYLALANINE                            ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'          y PROLINE                                  ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking'          y SERINE                                   ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking'          y THREONINE                                ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'          y TRYPTOPHAN                               ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'          y TYROSINE                                 ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'          y VALINE                                   ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ASP 1   17  17  ASP ASP B . n 
A 1 2   PRO 2   18  18  PRO PRO B . n 
A 1 3   SER 3   19  19  SER SER B . n 
A 1 4   THR 4   20  20  THR THR B . n 
A 1 5   ILE 5   21  21  ILE ILE B . n 
A 1 6   GLU 6   22  22  GLU GLU B . n 
A 1 7   GLU 7   23  23  GLU GLU B . n 
A 1 8   GLN 8   24  24  GLN GLN B . n 
A 1 9   ALA 9   25  25  ALA ALA B . n 
A 1 10  LYS 10  26  26  LYS LYS B . n 
A 1 11  THR 11  27  27  THR THR B . n 
A 1 12  PHE 12  28  28  PHE PHE B . n 
A 1 13  LEU 13  29  29  LEU LEU B . n 
A 1 14  ASP 14  30  30  ASP ASP B . n 
A 1 15  LYS 15  31  31  LYS LYS B . n 
A 1 16  PHE 16  32  32  PHE PHE B . n 
A 1 17  ASN 17  33  33  ASN ASN B . n 
A 1 18  HIS 18  34  34  HIS HIS B . n 
A 1 19  GLU 19  35  35  GLU GLU B . n 
A 1 20  ALA 20  36  36  ALA ALA B . n 
A 1 21  GLU 21  37  37  GLU GLU B . n 
A 1 22  ASP 22  38  38  ASP ASP B . n 
A 1 23  LEU 23  39  39  LEU LEU B . n 
A 1 24  PHE 24  40  40  PHE PHE B . n 
A 1 25  TYR 25  41  41  TYR TYR B . n 
A 1 26  GLN 26  42  42  GLN GLN B . n 
A 1 27  SER 27  43  43  SER SER B . n 
A 1 28  SER 28  44  44  SER SER B . n 
A 1 29  LEU 29  45  45  LEU LEU B . n 
A 1 30  ALA 30  46  46  ALA ALA B . n 
A 1 31  SER 31  47  47  SER SER B . n 
A 1 32  TRP 32  48  48  TRP TRP B . n 
A 1 33  ASN 33  49  49  ASN ASN B . n 
A 1 34  TYR 34  50  50  TYR TYR B . n 
A 1 35  ASN 35  51  51  ASN ASN B . n 
A 1 36  THR 36  52  52  THR THR B . n 
A 1 37  ASN 37  53  53  ASN ASN B . n 
A 1 38  ILE 38  54  54  ILE ILE B . n 
A 1 39  THR 39  55  55  THR THR B . n 
A 1 40  GLU 40  56  56  GLU GLU B . n 
A 1 41  GLU 41  57  57  GLU GLU B . n 
A 1 42  ASN 42  58  58  ASN ASN B . n 
A 1 43  VAL 43  59  59  VAL VAL B . n 
A 1 44  GLN 44  60  60  GLN GLN B . n 
A 1 45  ASN 45  61  61  ASN ASN B . n 
A 1 46  MET 46  62  62  MET MET B . n 
A 1 47  ASN 47  63  63  ASN ASN B . n 
A 1 48  ASN 48  64  64  ASN ASN B . n 
A 1 49  ALA 49  65  65  ALA ALA B . n 
A 1 50  GLY 50  66  66  GLY GLY B . n 
A 1 51  ASP 51  67  67  ASP ASP B . n 
A 1 52  LYS 52  68  68  LYS LYS B . n 
A 1 53  TRP 53  69  69  TRP TRP B . n 
A 1 54  SER 54  70  70  SER SER B . n 
A 1 55  ALA 55  71  71  ALA ALA B . n 
A 1 56  PHE 56  72  72  PHE PHE B . n 
A 1 57  LEU 57  73  73  LEU LEU B . n 
A 1 58  LYS 58  74  74  LYS LYS B . n 
A 1 59  GLU 59  75  75  GLU GLU B . n 
A 1 60  GLN 60  76  76  GLN GLN B . n 
A 1 61  SER 61  77  77  SER SER B . n 
A 1 62  THR 62  78  78  THR THR B . n 
A 1 63  LEU 63  79  79  LEU LEU B . n 
A 1 64  ALA 64  80  80  ALA ALA B . n 
A 1 65  GLN 65  81  81  GLN GLN B . n 
A 1 66  MET 66  82  82  MET MET B . n 
A 1 67  TYR 67  83  83  TYR TYR B . n 
A 1 68  PRO 68  84  84  PRO PRO B . n 
A 1 69  LEU 69  85  85  LEU LEU B . n 
A 1 70  GLN 70  86  86  GLN GLN B . n 
A 1 71  GLU 71  87  87  GLU GLU B . n 
A 1 72  ILE 72  88  88  ILE ILE B . n 
A 1 73  GLN 73  89  89  GLN GLN B . n 
A 1 74  ASN 74  90  90  ASN ASN B . n 
A 1 75  LEU 75  91  91  LEU LEU B . n 
A 1 76  THR 76  92  92  THR THR B . n 
A 1 77  VAL 77  93  93  VAL VAL B . n 
A 1 78  LYS 78  94  94  LYS LYS B . n 
A 1 79  LEU 79  95  95  LEU LEU B . n 
A 1 80  GLN 80  96  96  GLN GLN B . n 
A 1 81  LEU 81  97  97  LEU LEU B . n 
A 1 82  GLN 82  98  98  GLN GLN B . n 
A 1 83  ALA 83  99  99  ALA ALA B . n 
A 1 84  LEU 84  100 100 LEU LEU B . n 
A 1 85  GLN 85  101 101 GLN GLN B . n 
A 1 86  GLN 86  102 102 GLN GLN B . n 
A 1 87  ASN 87  103 103 ASN ASN B . n 
A 1 88  GLY 88  104 104 GLY GLY B . n 
A 1 89  SER 89  105 105 SER SER B . n 
A 1 90  SER 90  106 106 SER SER B . n 
A 1 91  VAL 91  107 107 VAL VAL B . n 
A 1 92  LEU 92  108 108 LEU LEU B . n 
A 1 93  SER 93  109 109 SER SER B . n 
A 1 94  GLU 94  110 110 GLU GLU B . n 
A 1 95  ASP 95  111 111 ASP ASP B . n 
A 1 96  LYS 96  112 112 LYS LYS B . n 
A 1 97  SER 97  113 113 SER SER B . n 
A 1 98  LYS 98  114 114 LYS LYS B . n 
A 1 99  ARG 99  115 115 ARG ARG B . n 
A 1 100 LEU 100 116 116 LEU LEU B . n 
A 1 101 ASN 101 117 117 ASN ASN B . n 
A 1 102 THR 102 118 118 THR THR B . n 
A 1 103 ILE 103 119 119 ILE ILE B . n 
A 1 104 LEU 104 120 120 LEU LEU B . n 
A 1 105 ASN 105 121 121 ASN ASN B . n 
A 1 106 THR 106 122 122 THR THR B . n 
A 1 107 MET 107 123 123 MET MET B . n 
A 1 108 SER 108 124 124 SER SER B . n 
A 1 109 THR 109 125 125 THR THR B . n 
A 1 110 ILE 110 126 126 ILE ILE B . n 
A 1 111 TYR 111 127 127 TYR TYR B . n 
A 1 112 SER 112 128 128 SER SER B . n 
A 1 113 THR 113 129 129 THR THR B . n 
A 1 114 GLY 114 130 130 GLY GLY B . n 
A 1 115 LYS 115 131 131 LYS LYS B . n 
A 1 116 VAL 116 132 132 VAL VAL B . n 
A 1 117 CYS 117 133 133 CYS CYS B . n 
A 1 118 ASN 118 134 134 ASN ASN B . n 
A 1 119 PRO 119 135 135 PRO PRO B . n 
A 1 120 ASP 120 136 136 ASP ASP B . n 
A 1 121 ASN 121 137 137 ASN ASN B . n 
A 1 122 PRO 122 138 138 PRO PRO B . n 
A 1 123 GLN 123 139 139 GLN GLN B . n 
A 1 124 GLU 124 140 140 GLU GLU B . n 
A 1 125 CYS 125 141 141 CYS CYS B . n 
A 1 126 LEU 126 142 142 LEU LEU B . n 
A 1 127 LEU 127 143 143 LEU LEU B . n 
A 1 128 LEU 128 144 144 LEU LEU B . n 
A 1 129 GLU 129 145 145 GLU GLU B . n 
A 1 130 PRO 130 146 146 PRO PRO B . n 
A 1 131 GLY 131 147 147 GLY GLY B . n 
A 1 132 LEU 132 148 148 LEU LEU B . n 
A 1 133 ASN 133 149 149 ASN ASN B . n 
A 1 134 GLU 134 150 150 GLU GLU B . n 
A 1 135 ILE 135 151 151 ILE ILE B . n 
A 1 136 MET 136 152 152 MET MET B . n 
A 1 137 ALA 137 153 153 ALA ALA B . n 
A 1 138 ASN 138 154 154 ASN ASN B . n 
A 1 139 SER 139 155 155 SER SER B . n 
A 1 140 LEU 140 156 156 LEU LEU B . n 
A 1 141 ASP 141 157 157 ASP ASP B . n 
A 1 142 TYR 142 158 158 TYR TYR B . n 
A 1 143 ASN 143 159 159 ASN ASN B . n 
A 1 144 GLU 144 160 160 GLU GLU B . n 
A 1 145 ARG 145 161 161 ARG ARG B . n 
A 1 146 LEU 146 162 162 LEU LEU B . n 
A 1 147 TRP 147 163 163 TRP TRP B . n 
A 1 148 ALA 148 164 164 ALA ALA B . n 
A 1 149 TRP 149 165 165 TRP TRP B . n 
A 1 150 GLU 150 166 166 GLU GLU B . n 
A 1 151 SER 151 167 167 SER SER B . n 
A 1 152 TRP 152 168 168 TRP TRP B . n 
A 1 153 ARG 153 169 169 ARG ARG B . n 
A 1 154 SER 154 170 170 SER SER B . n 
A 1 155 GLU 155 171 171 GLU GLU B . n 
A 1 156 VAL 156 172 172 VAL VAL B . n 
A 1 157 GLY 157 173 173 GLY GLY B . n 
A 1 158 LYS 158 174 174 LYS LYS B . n 
A 1 159 GLN 159 175 175 GLN GLN B . n 
A 1 160 LEU 160 176 176 LEU LEU B . n 
A 1 161 ARG 161 177 177 ARG ARG B . n 
A 1 162 PRO 162 178 178 PRO PRO B . n 
A 1 163 LEU 163 179 179 LEU LEU B . n 
A 1 164 TYR 164 180 180 TYR TYR B . n 
A 1 165 GLU 165 181 181 GLU GLU B . n 
A 1 166 GLU 166 182 182 GLU GLU B . n 
A 1 167 TYR 167 183 183 TYR TYR B . n 
A 1 168 VAL 168 184 184 VAL VAL B . n 
A 1 169 VAL 169 185 185 VAL VAL B . n 
A 1 170 LEU 170 186 186 LEU LEU B . n 
A 1 171 LYS 171 187 187 LYS LYS B . n 
A 1 172 ASN 172 188 188 ASN ASN B . n 
A 1 173 GLU 173 189 189 GLU GLU B . n 
A 1 174 MET 174 190 190 MET MET B . n 
A 1 175 ALA 175 191 191 ALA ALA B . n 
A 1 176 ARG 176 192 192 ARG ARG B . n 
A 1 177 ALA 177 193 193 ALA ALA B . n 
A 1 178 ASN 178 194 194 ASN ASN B . n 
A 1 179 HIS 179 195 195 HIS HIS B . n 
A 1 180 TYR 180 196 196 TYR TYR B . n 
A 1 181 GLU 181 197 197 GLU GLU B . n 
A 1 182 ASP 182 198 198 ASP ASP B . n 
A 1 183 TYR 183 199 199 TYR TYR B . n 
A 1 184 GLY 184 200 200 GLY GLY B . n 
A 1 185 ASP 185 201 201 ASP ASP B . n 
A 1 186 TYR 186 202 202 TYR TYR B . n 
A 1 187 TRP 187 203 203 TRP TRP B . n 
A 1 188 ARG 188 204 204 ARG ARG B . n 
A 1 189 GLY 189 205 205 GLY GLY B . n 
A 1 190 ASP 190 206 206 ASP ASP B . n 
A 1 191 TYR 191 207 207 TYR TYR B . n 
A 1 192 GLU 192 208 208 GLU GLU B . n 
A 1 193 VAL 193 209 209 VAL VAL B . n 
A 1 194 ASN 194 210 210 ASN ASN B . n 
A 1 195 GLY 195 211 211 GLY GLY B . n 
A 1 196 VAL 196 212 212 VAL VAL B . n 
A 1 197 ASP 197 213 213 ASP ASP B . n 
A 1 198 GLY 198 214 214 GLY GLY B . n 
A 1 199 TYR 199 215 215 TYR TYR B . n 
A 1 200 ASP 200 216 216 ASP ASP B . n 
A 1 201 TYR 201 217 217 TYR TYR B . n 
A 1 202 SER 202 218 218 SER SER B . n 
A 1 203 ARG 203 219 219 ARG ARG B . n 
A 1 204 GLY 204 220 220 GLY GLY B . n 
A 1 205 GLN 205 221 221 GLN GLN B . n 
A 1 206 LEU 206 222 222 LEU LEU B . n 
A 1 207 ILE 207 223 223 ILE ILE B . n 
A 1 208 GLU 208 224 224 GLU GLU B . n 
A 1 209 ASP 209 225 225 ASP ASP B . n 
A 1 210 VAL 210 226 226 VAL VAL B . n 
A 1 211 GLU 211 227 227 GLU GLU B . n 
A 1 212 HIS 212 228 228 HIS HIS B . n 
A 1 213 THR 213 229 229 THR THR B . n 
A 1 214 PHE 214 230 230 PHE PHE B . n 
A 1 215 GLU 215 231 231 GLU GLU B . n 
A 1 216 GLU 216 232 232 GLU GLU B . n 
A 1 217 ILE 217 233 233 ILE ILE B . n 
A 1 218 LYS 218 234 234 LYS LYS B . n 
A 1 219 PRO 219 235 235 PRO PRO B . n 
A 1 220 LEU 220 236 236 LEU LEU B . n 
A 1 221 TYR 221 237 237 TYR TYR B . n 
A 1 222 GLU 222 238 238 GLU GLU B . n 
A 1 223 HIS 223 239 239 HIS HIS B . n 
A 1 224 LEU 224 240 240 LEU LEU B . n 
A 1 225 HIS 225 241 241 HIS HIS B . n 
A 1 226 ALA 226 242 242 ALA ALA B . n 
A 1 227 TYR 227 243 243 TYR TYR B . n 
A 1 228 VAL 228 244 244 VAL VAL B . n 
A 1 229 ARG 229 245 245 ARG ARG B . n 
A 1 230 ALA 230 246 246 ALA ALA B . n 
A 1 231 LYS 231 247 247 LYS LYS B . n 
A 1 232 LEU 232 248 248 LEU LEU B . n 
A 1 233 MET 233 249 249 MET MET B . n 
A 1 234 ASN 234 250 250 ASN ASN B . n 
A 1 235 ALA 235 251 251 ALA ALA B . n 
A 1 236 TYR 236 252 252 TYR TYR B . n 
A 1 237 PRO 237 253 253 PRO PRO B . n 
A 1 238 SER 238 254 254 SER SER B . n 
A 1 239 TYR 239 255 255 TYR TYR B . n 
A 1 240 ILE 240 256 256 ILE ILE B . n 
A 1 241 SER 241 257 257 SER SER B . n 
A 1 242 PRO 242 258 258 PRO PRO B . n 
A 1 243 ILE 243 259 259 ILE ILE B . n 
A 1 244 GLY 244 260 260 GLY GLY B . n 
A 1 245 CYS 245 261 261 CYS CYS B . n 
A 1 246 LEU 246 262 262 LEU LEU B . n 
A 1 247 PRO 247 263 263 PRO PRO B . n 
A 1 248 ALA 248 264 264 ALA ALA B . n 
A 1 249 HIS 249 265 265 HIS HIS B . n 
A 1 250 LEU 250 266 266 LEU LEU B . n 
A 1 251 LEU 251 267 267 LEU LEU B . n 
A 1 252 GLY 252 268 268 GLY GLY B . n 
A 1 253 ASP 253 269 269 ASP ASP B . n 
A 1 254 MET 254 270 270 MET MET B . n 
A 1 255 TRP 255 271 271 TRP TRP B . n 
A 1 256 GLY 256 272 272 GLY GLY B . n 
A 1 257 ARG 257 273 273 ARG ARG B . n 
A 1 258 PHE 258 274 274 PHE PHE B . n 
A 1 259 TRP 259 275 275 TRP TRP B . n 
A 1 260 THR 260 276 276 THR THR B . n 
A 1 261 ASN 261 277 277 ASN ASN B . n 
A 1 262 LEU 262 278 278 LEU LEU B . n 
A 1 263 TYR 263 279 279 TYR TYR B . n 
A 1 264 SER 264 280 280 SER SER B . n 
A 1 265 LEU 265 281 281 LEU LEU B . n 
A 1 266 THR 266 282 282 THR THR B . n 
A 1 267 VAL 267 283 283 VAL VAL B . n 
A 1 268 PRO 268 284 284 PRO PRO B . n 
A 1 269 PHE 269 285 285 PHE PHE B . n 
A 1 270 GLY 270 286 286 GLY GLY B . n 
A 1 271 GLN 271 287 287 GLN GLN B . n 
A 1 272 LYS 272 288 288 LYS LYS B . n 
A 1 273 PRO 273 289 289 PRO PRO B . n 
A 1 274 ASN 274 290 290 ASN ASN B . n 
A 1 275 ILE 275 291 291 ILE ILE B . n 
A 1 276 ASP 276 292 292 ASP ASP B . n 
A 1 277 VAL 277 293 293 VAL VAL B . n 
A 1 278 THR 278 294 294 THR THR B . n 
A 1 279 ASP 279 295 295 ASP ASP B . n 
A 1 280 ALA 280 296 296 ALA ALA B . n 
A 1 281 MET 281 297 297 MET MET B . n 
A 1 282 VAL 282 298 298 VAL VAL B . n 
A 1 283 ASP 283 299 299 ASP ASP B . n 
A 1 284 GLN 284 300 300 GLN GLN B . n 
A 1 285 ALA 285 301 301 ALA ALA B . n 
A 1 286 TRP 286 302 302 TRP TRP B . n 
A 1 287 ASP 287 303 303 ASP ASP B . n 
A 1 288 ALA 288 304 304 ALA ALA B . n 
A 1 289 GLN 289 305 305 GLN GLN B . n 
A 1 290 ARG 290 306 306 ARG ARG B . n 
A 1 291 ILE 291 307 307 ILE ILE B . n 
A 1 292 PHE 292 308 308 PHE PHE B . n 
A 1 293 LYS 293 309 309 LYS LYS B . n 
A 1 294 GLU 294 310 310 GLU GLU B . n 
A 1 295 ALA 295 311 311 ALA ALA B . n 
A 1 296 GLU 296 312 312 GLU GLU B . n 
A 1 297 LYS 297 313 313 LYS LYS B . n 
A 1 298 PHE 298 314 314 PHE PHE B . n 
A 1 299 PHE 299 315 315 PHE PHE B . n 
A 1 300 VAL 300 316 316 VAL VAL B . n 
A 1 301 SER 301 317 317 SER SER B . n 
A 1 302 VAL 302 318 318 VAL VAL B . n 
A 1 303 GLY 303 319 319 GLY GLY B . n 
A 1 304 LEU 304 320 320 LEU LEU B . n 
A 1 305 PRO 305 321 321 PRO PRO B . n 
A 1 306 ASN 306 322 322 ASN ASN B . n 
A 1 307 MET 307 323 323 MET MET B . n 
A 1 308 THR 308 324 324 THR THR B . n 
A 1 309 GLN 309 325 325 GLN GLN B . n 
A 1 310 GLY 310 326 326 GLY GLY B . n 
A 1 311 PHE 311 327 327 PHE PHE B . n 
A 1 312 TRP 312 328 328 TRP TRP B . n 
A 1 313 GLU 313 329 329 GLU GLU B . n 
A 1 314 ASN 314 330 330 ASN ASN B . n 
A 1 315 SER 315 331 331 SER SER B . n 
A 1 316 MET 316 332 332 MET MET B . n 
A 1 317 LEU 317 333 333 LEU LEU B . n 
A 1 318 THR 318 334 334 THR THR B . n 
A 1 319 ASP 319 335 335 ASP ASP B . n 
A 1 320 PRO 320 336 336 PRO PRO B . n 
A 1 321 GLY 321 337 337 GLY GLY B . n 
A 1 322 ASN 322 338 338 ASN ASN B . n 
A 1 323 VAL 323 339 339 VAL VAL B . n 
A 1 324 GLN 324 340 340 GLN GLN B . n 
A 1 325 LYS 325 341 341 LYS LYS B . n 
A 1 326 ALA 326 342 342 ALA ALA B . n 
A 1 327 VAL 327 343 343 VAL VAL B . n 
A 1 328 CYS 328 344 344 CYS CYS B . n 
A 1 329 HIS 329 345 345 HIS HIS B . n 
A 1 330 PRO 330 346 346 PRO PRO B . n 
A 1 331 THR 331 347 347 THR THR B . n 
A 1 332 ALA 332 348 348 ALA ALA B . n 
A 1 333 TRP 333 349 349 TRP TRP B . n 
A 1 334 ASP 334 350 350 ASP ASP B . n 
A 1 335 LEU 335 351 351 LEU LEU B . n 
A 1 336 GLY 336 352 352 GLY GLY B . n 
A 1 337 LYS 337 353 353 LYS LYS B . n 
A 1 338 GLY 338 354 354 GLY GLY B . n 
A 1 339 ASP 339 355 355 ASP ASP B . n 
A 1 340 PHE 340 356 356 PHE PHE B . n 
A 1 341 ARG 341 357 357 ARG ARG B . n 
A 1 342 ILE 342 358 358 ILE ILE B . n 
A 1 343 LEU 343 359 359 LEU LEU B . n 
A 1 344 MET 344 360 360 MET MET B . n 
A 1 345 CYS 345 361 361 CYS CYS B . n 
A 1 346 THR 346 362 362 THR THR B . n 
A 1 347 LYS 347 363 363 LYS LYS B . n 
A 1 348 VAL 348 364 364 VAL VAL B . n 
A 1 349 THR 349 365 365 THR THR B . n 
A 1 350 MET 350 366 366 MET MET B . n 
A 1 351 ASP 351 367 367 ASP ASP B . n 
A 1 352 ASP 352 368 368 ASP ASP B . n 
A 1 353 PHE 353 369 369 PHE PHE B . n 
A 1 354 LEU 354 370 370 LEU LEU B . n 
A 1 355 THR 355 371 371 THR THR B . n 
A 1 356 ALA 356 372 372 ALA ALA B . n 
A 1 357 HIS 357 373 373 HIS HIS B . n 
A 1 358 HIS 358 374 374 HIS HIS B . n 
A 1 359 GLU 359 375 375 GLU GLU B . n 
A 1 360 MET 360 376 376 MET MET B . n 
A 1 361 GLY 361 377 377 GLY GLY B . n 
A 1 362 HIS 362 378 378 HIS HIS B . n 
A 1 363 ILE 363 379 379 ILE ILE B . n 
A 1 364 GLN 364 380 380 GLN GLN B . n 
A 1 365 TYR 365 381 381 TYR TYR B . n 
A 1 366 ASP 366 382 382 ASP ASP B . n 
A 1 367 MET 367 383 383 MET MET B . n 
A 1 368 ALA 368 384 384 ALA ALA B . n 
A 1 369 TYR 369 385 385 TYR TYR B . n 
A 1 370 ALA 370 386 386 ALA ALA B . n 
A 1 371 ALA 371 387 387 ALA ALA B . n 
A 1 372 GLN 372 388 388 GLN GLN B . n 
A 1 373 PRO 373 389 389 PRO PRO B . n 
A 1 374 PHE 374 390 390 PHE PHE B . n 
A 1 375 LEU 375 391 391 LEU LEU B . n 
A 1 376 LEU 376 392 392 LEU LEU B . n 
A 1 377 ARG 377 393 393 ARG ARG B . n 
A 1 378 ASN 378 394 394 ASN ASN B . n 
A 1 379 GLY 379 395 395 GLY GLY B . n 
A 1 380 ALA 380 396 396 ALA ALA B . n 
A 1 381 ASN 381 397 397 ASN ASN B . n 
A 1 382 GLU 382 398 398 GLU GLU B . n 
A 1 383 GLY 383 399 399 GLY GLY B . n 
A 1 384 PHE 384 400 400 PHE PHE B . n 
A 1 385 HIS 385 401 401 HIS HIS B . n 
A 1 386 GLU 386 402 402 GLU GLU B . n 
A 1 387 ALA 387 403 403 ALA ALA B . n 
A 1 388 VAL 388 404 404 VAL VAL B . n 
A 1 389 GLY 389 405 405 GLY GLY B . n 
A 1 390 GLU 390 406 406 GLU GLU B . n 
A 1 391 ILE 391 407 407 ILE ILE B . n 
A 1 392 MET 392 408 408 MET MET B . n 
A 1 393 SER 393 409 409 SER SER B . n 
A 1 394 LEU 394 410 410 LEU LEU B . n 
A 1 395 SER 395 411 411 SER SER B . n 
A 1 396 ALA 396 412 412 ALA ALA B . n 
A 1 397 ALA 397 413 413 ALA ALA B . n 
A 1 398 THR 398 414 414 THR THR B . n 
A 1 399 PRO 399 415 415 PRO PRO B . n 
A 1 400 LYS 400 416 416 LYS LYS B . n 
A 1 401 HIS 401 417 417 HIS HIS B . n 
A 1 402 LEU 402 418 418 LEU LEU B . n 
A 1 403 LYS 403 419 419 LYS LYS B . n 
A 1 404 SER 404 420 420 SER SER B . n 
A 1 405 ILE 405 421 421 ILE ILE B . n 
A 1 406 GLY 406 422 422 GLY GLY B . n 
A 1 407 LEU 407 423 423 LEU LEU B . n 
A 1 408 LEU 408 424 424 LEU LEU B . n 
A 1 409 SER 409 425 425 SER SER B . n 
A 1 410 PRO 410 426 426 PRO PRO B . n 
A 1 411 ASP 411 427 427 ASP ASP B . n 
A 1 412 PHE 412 428 428 PHE PHE B . n 
A 1 413 GLN 413 429 429 GLN GLN B . n 
A 1 414 GLU 414 430 430 GLU GLU B . n 
A 1 415 ASP 415 431 431 ASP ASP B . n 
A 1 416 ASN 416 432 432 ASN ASN B . n 
A 1 417 GLU 417 433 433 GLU GLU B . n 
A 1 418 THR 418 434 434 THR THR B . n 
A 1 419 GLU 419 435 435 GLU GLU B . n 
A 1 420 ILE 420 436 436 ILE ILE B . n 
A 1 421 ASN 421 437 437 ASN ASN B . n 
A 1 422 PHE 422 438 438 PHE PHE B . n 
A 1 423 LEU 423 439 439 LEU LEU B . n 
A 1 424 LEU 424 440 440 LEU LEU B . n 
A 1 425 LYS 425 441 441 LYS LYS B . n 
A 1 426 GLN 426 442 442 GLN GLN B . n 
A 1 427 ALA 427 443 443 ALA ALA B . n 
A 1 428 LEU 428 444 444 LEU LEU B . n 
A 1 429 THR 429 445 445 THR THR B . n 
A 1 430 ILE 430 446 446 ILE ILE B . n 
A 1 431 VAL 431 447 447 VAL VAL B . n 
A 1 432 GLY 432 448 448 GLY GLY B . n 
A 1 433 THR 433 449 449 THR THR B . n 
A 1 434 LEU 434 450 450 LEU LEU B . n 
A 1 435 PRO 435 451 451 PRO PRO B . n 
A 1 436 PHE 436 452 452 PHE PHE B . n 
A 1 437 THR 437 453 453 THR THR B . n 
A 1 438 TYR 438 454 454 TYR TYR B . n 
A 1 439 MET 439 455 455 MET MET B . n 
A 1 440 LEU 440 456 456 LEU LEU B . n 
A 1 441 GLU 441 457 457 GLU GLU B . n 
A 1 442 LYS 442 458 458 LYS LYS B . n 
A 1 443 TRP 443 459 459 TRP TRP B . n 
A 1 444 ARG 444 460 460 ARG ARG B . n 
A 1 445 TRP 445 461 461 TRP TRP B . n 
A 1 446 MET 446 462 462 MET MET B . n 
A 1 447 VAL 447 463 463 VAL VAL B . n 
A 1 448 PHE 448 464 464 PHE PHE B . n 
A 1 449 LYS 449 465 465 LYS LYS B . n 
A 1 450 GLY 450 466 466 GLY GLY B . n 
A 1 451 GLU 451 467 467 GLU GLU B . n 
A 1 452 ILE 452 468 468 ILE ILE B . n 
A 1 453 PRO 453 469 469 PRO PRO B . n 
A 1 454 LYS 454 470 470 LYS LYS B . n 
A 1 455 ASP 455 471 471 ASP ASP B . n 
A 1 456 GLN 456 472 472 GLN GLN B . n 
A 1 457 TRP 457 473 473 TRP TRP B . n 
A 1 458 MET 458 474 474 MET MET B . n 
A 1 459 LYS 459 475 475 LYS LYS B . n 
A 1 460 LYS 460 476 476 LYS LYS B . n 
A 1 461 TRP 461 477 477 TRP TRP B . n 
A 1 462 TRP 462 478 478 TRP TRP B . n 
A 1 463 GLU 463 479 479 GLU GLU B . n 
A 1 464 MET 464 480 480 MET MET B . n 
A 1 465 LYS 465 481 481 LYS LYS B . n 
A 1 466 ARG 466 482 482 ARG ARG B . n 
A 1 467 GLU 467 483 483 GLU GLU B . n 
A 1 468 ILE 468 484 484 ILE ILE B . n 
A 1 469 VAL 469 485 485 VAL VAL B . n 
A 1 470 GLY 470 486 486 GLY GLY B . n 
A 1 471 VAL 471 487 487 VAL VAL B . n 
A 1 472 VAL 472 488 488 VAL VAL B . n 
A 1 473 GLU 473 489 489 GLU GLU B . n 
A 1 474 PRO 474 490 490 PRO PRO B . n 
A 1 475 VAL 475 491 491 VAL VAL B . n 
A 1 476 PRO 476 492 492 PRO PRO B . n 
A 1 477 HIS 477 493 493 HIS HIS B . n 
A 1 478 ASP 478 494 494 ASP ASP B . n 
A 1 479 GLU 479 495 495 GLU GLU B . n 
A 1 480 THR 480 496 496 THR THR B . n 
A 1 481 TYR 481 497 497 TYR TYR B . n 
A 1 482 CYS 482 498 498 CYS CYS B . n 
A 1 483 ASP 483 499 499 ASP ASP B . n 
A 1 484 PRO 484 500 500 PRO PRO B . n 
A 1 485 ALA 485 501 501 ALA ALA B . n 
A 1 486 SER 486 502 502 SER SER B . n 
A 1 487 LEU 487 503 503 LEU LEU B . n 
A 1 488 PHE 488 504 504 PHE PHE B . n 
A 1 489 HIS 489 505 505 HIS HIS B . n 
A 1 490 VAL 490 506 506 VAL VAL B . n 
A 1 491 SER 491 507 507 SER SER B . n 
A 1 492 ASN 492 508 508 ASN ASN B . n 
A 1 493 ASP 493 509 509 ASP ASP B . n 
A 1 494 TYR 494 510 510 TYR TYR B . n 
A 1 495 SER 495 511 511 SER SER B . n 
A 1 496 PHE 496 512 512 PHE PHE B . n 
A 1 497 ILE 497 513 513 ILE ILE B . n 
A 1 498 ARG 498 514 514 ARG ARG B . n 
A 1 499 TYR 499 515 515 TYR TYR B . n 
A 1 500 TYR 500 516 516 TYR TYR B . n 
A 1 501 THR 501 517 517 THR THR B . n 
A 1 502 ARG 502 518 518 ARG ARG B . n 
A 1 503 THR 503 519 519 THR THR B . n 
A 1 504 LEU 504 520 520 LEU LEU B . n 
A 1 505 TYR 505 521 521 TYR TYR B . n 
A 1 506 GLN 506 522 522 GLN GLN B . n 
A 1 507 PHE 507 523 523 PHE PHE B . n 
A 1 508 GLN 508 524 524 GLN GLN B . n 
A 1 509 PHE 509 525 525 PHE PHE B . n 
A 1 510 GLN 510 526 526 GLN GLN B . n 
A 1 511 GLU 511 527 527 GLU GLU B . n 
A 1 512 ALA 512 528 528 ALA ALA B . n 
A 1 513 LEU 513 529 529 LEU LEU B . n 
A 1 514 CYS 514 530 530 CYS CYS B . n 
A 1 515 GLN 515 531 531 GLN GLN B . n 
A 1 516 ALA 516 532 532 ALA ALA B . n 
A 1 517 ALA 517 533 533 ALA ALA B . n 
A 1 518 LYS 518 534 534 LYS LYS B . n 
A 1 519 HIS 519 535 535 HIS HIS B . n 
A 1 520 GLU 520 536 536 GLU GLU B . n 
A 1 521 GLY 521 537 537 GLY GLY B . n 
A 1 522 PRO 522 538 538 PRO PRO B . n 
A 1 523 LEU 523 539 539 LEU LEU B . n 
A 1 524 HIS 524 540 540 HIS HIS B . n 
A 1 525 LYS 525 541 541 LYS LYS B . n 
A 1 526 CYS 526 542 542 CYS CYS B . n 
A 1 527 ASP 527 543 543 ASP ASP B . n 
A 1 528 ILE 528 544 544 ILE ILE B . n 
A 1 529 SER 529 545 545 SER SER B . n 
A 1 530 ASN 530 546 546 ASN ASN B . n 
A 1 531 SER 531 547 547 SER SER B . n 
A 1 532 THR 532 548 548 THR THR B . n 
A 1 533 GLU 533 549 549 GLU GLU B . n 
A 1 534 ALA 534 550 550 ALA ALA B . n 
A 1 535 GLY 535 551 551 GLY GLY B . n 
A 1 536 GLN 536 552 552 GLN GLN B . n 
A 1 537 LYS 537 553 553 LYS LYS B . n 
A 1 538 LEU 538 554 554 LEU LEU B . n 
A 1 539 PHE 539 555 555 PHE PHE B . n 
A 1 540 ASN 540 556 556 ASN ASN B . n 
A 1 541 MET 541 557 557 MET MET B . n 
A 1 542 LEU 542 558 558 LEU LEU B . n 
A 1 543 ARG 543 559 559 ARG ARG B . n 
A 1 544 LEU 544 560 560 LEU LEU B . n 
A 1 545 GLY 545 561 561 GLY GLY B . n 
A 1 546 LYS 546 562 562 LYS LYS B . n 
A 1 547 SER 547 563 563 SER SER B . n 
A 1 548 GLU 548 564 564 GLU GLU B . n 
A 1 549 PRO 549 565 565 PRO PRO B . n 
A 1 550 TRP 550 566 566 TRP TRP B . n 
A 1 551 THR 551 567 567 THR THR B . n 
A 1 552 LEU 552 568 568 LEU LEU B . n 
A 1 553 ALA 553 569 569 ALA ALA B . n 
A 1 554 LEU 554 570 570 LEU LEU B . n 
A 1 555 GLU 555 571 571 GLU GLU B . n 
A 1 556 ASN 556 572 572 ASN ASN B . n 
A 1 557 VAL 557 573 573 VAL VAL B . n 
A 1 558 VAL 558 574 574 VAL VAL B . n 
A 1 559 GLY 559 575 575 GLY GLY B . n 
A 1 560 ALA 560 576 576 ALA ALA B . n 
A 1 561 LYS 561 577 577 LYS LYS B . n 
A 1 562 ASN 562 578 578 ASN ASN B . n 
A 1 563 MET 563 579 579 MET MET B . n 
A 1 564 ASN 564 580 580 ASN ASN B . n 
A 1 565 VAL 565 581 581 VAL VAL B . n 
A 1 566 ARG 566 582 582 ARG ARG B . n 
A 1 567 PRO 567 583 583 PRO PRO B . n 
A 1 568 LEU 568 584 584 LEU LEU B . n 
A 1 569 LEU 569 585 585 LEU LEU B . n 
A 1 570 ASN 570 586 586 ASN ASN B . n 
A 1 571 TYR 571 587 587 TYR TYR B . n 
A 1 572 PHE 572 588 588 PHE PHE B . n 
A 1 573 GLU 573 589 589 GLU GLU B . n 
A 1 574 PRO 574 590 590 PRO PRO B . n 
A 1 575 LEU 575 591 591 LEU LEU B . n 
A 1 576 PHE 576 592 592 PHE PHE B . n 
A 1 577 THR 577 593 593 THR THR B . n 
A 1 578 TRP 578 594 594 TRP TRP B . n 
A 1 579 LEU 579 595 595 LEU LEU B . n 
A 1 580 LYS 580 596 596 LYS LYS B . n 
A 1 581 ASP 581 597 597 ASP ASP B . n 
A 1 582 GLN 582 598 598 GLN GLN B . n 
A 1 583 ASN 583 599 599 ASN ASN B . n 
A 1 584 LYS 584 600 600 LYS LYS B . n 
A 1 585 ASN 585 601 601 ASN ASN B . n 
A 1 586 SER 586 602 602 SER SER B . n 
A 1 587 PHE 587 603 603 PHE PHE B . n 
A 1 588 VAL 588 604 604 VAL VAL B . n 
A 1 589 GLY 589 605 605 GLY GLY B . n 
A 1 590 TRP 590 606 606 TRP TRP B . n 
A 1 591 SER 591 607 607 SER SER B . n 
A 1 592 THR 592 608 608 THR THR B . n 
A 1 593 ASP 593 609 609 ASP ASP B . n 
A 1 594 TRP 594 610 610 TRP TRP B . n 
A 1 595 SER 595 611 611 SER SER B . n 
A 1 596 PRO 596 612 612 PRO PRO B . n 
A 1 597 TYR 597 613 613 TYR TYR B . n 
A 1 598 ALA 598 614 614 ALA ALA B . n 
B 2 1   THR 1   333 333 THR THR C . n 
B 2 2   ASN 2   334 334 ASN ASN C . n 
B 2 3   LEU 3   335 335 LEU LEU C . n 
B 2 4   CYS 4   336 336 CYS CYS C . n 
B 2 5   PRO 5   337 337 PRO PRO C . n 
B 2 6   PHE 6   338 338 PHE PHE C . n 
B 2 7   ASP 7   339 339 ASP ASP C . n 
B 2 8   GLU 8   340 340 GLU GLU C . n 
B 2 9   VAL 9   341 341 VAL VAL C . n 
B 2 10  PHE 10  342 342 PHE PHE C . n 
B 2 11  ASN 11  343 343 ASN ASN C . n 
B 2 12  ALA 12  344 344 ALA ALA C . n 
B 2 13  THR 13  345 345 THR THR C . n 
B 2 14  ARG 14  346 346 ARG ARG C . n 
B 2 15  PHE 15  347 347 PHE PHE C . n 
B 2 16  ALA 16  348 348 ALA ALA C . n 
B 2 17  SER 17  349 349 SER SER C . n 
B 2 18  VAL 18  350 350 VAL VAL C . n 
B 2 19  TYR 19  351 351 TYR TYR C . n 
B 2 20  ALA 20  352 352 ALA ALA C . n 
B 2 21  TRP 21  353 353 TRP TRP C . n 
B 2 22  ASN 22  354 354 ASN ASN C . n 
B 2 23  ARG 23  355 355 ARG ARG C . n 
B 2 24  LYS 24  356 356 LYS LYS C . n 
B 2 25  ARG 25  357 357 ARG ARG C . n 
B 2 26  ILE 26  358 358 ILE ILE C . n 
B 2 27  SER 27  359 359 SER SER C . n 
B 2 28  ASN 28  360 360 ASN ASN C . n 
B 2 29  CYS 29  361 361 CYS CYS C . n 
B 2 30  VAL 30  362 362 VAL VAL C . n 
B 2 31  ALA 31  363 363 ALA ALA C . n 
B 2 32  ASP 32  364 364 ASP ASP C . n 
B 2 33  TYR 33  365 365 TYR TYR C . n 
B 2 34  SER 34  366 366 SER SER C . n 
B 2 35  VAL 35  367 367 VAL VAL C . n 
B 2 36  LEU 36  368 368 LEU LEU C . n 
B 2 37  TYR 37  369 369 TYR TYR C . n 
B 2 38  ASN 38  370 370 ASN ASN C . n 
B 2 39  PHE 39  371 371 PHE PHE C . n 
B 2 40  ALA 40  372 372 ALA ALA C . n 
B 2 41  PRO 41  373 373 PRO PRO C . n 
B 2 42  PHE 42  374 374 PHE PHE C . n 
B 2 43  PHE 43  375 375 PHE PHE C . n 
B 2 44  THR 44  376 376 THR THR C . n 
B 2 45  PHE 45  377 377 PHE PHE C . n 
B 2 46  LYS 46  378 378 LYS LYS C . n 
B 2 47  CYS 47  379 379 CYS CYS C . n 
B 2 48  TYR 48  380 380 TYR TYR C . n 
B 2 49  GLY 49  381 381 GLY GLY C . n 
B 2 50  VAL 50  382 382 VAL VAL C . n 
B 2 51  SER 51  383 383 SER SER C . n 
B 2 52  PRO 52  384 384 PRO PRO C . n 
B 2 53  THR 53  385 385 THR THR C . n 
B 2 54  LYS 54  386 386 LYS LYS C . n 
B 2 55  LEU 55  387 387 LEU LEU C . n 
B 2 56  ASN 56  388 388 ASN ASN C . n 
B 2 57  ASP 57  389 389 ASP ASP C . n 
B 2 58  LEU 58  390 390 LEU LEU C . n 
B 2 59  CYS 59  391 391 CYS CYS C . n 
B 2 60  PHE 60  392 392 PHE PHE C . n 
B 2 61  THR 61  393 393 THR THR C . n 
B 2 62  ASN 62  394 394 ASN ASN C . n 
B 2 63  VAL 63  395 395 VAL VAL C . n 
B 2 64  TYR 64  396 396 TYR TYR C . n 
B 2 65  ALA 65  397 397 ALA ALA C . n 
B 2 66  ASP 66  398 398 ASP ASP C . n 
B 2 67  SER 67  399 399 SER SER C . n 
B 2 68  PHE 68  400 400 PHE PHE C . n 
B 2 69  VAL 69  401 401 VAL VAL C . n 
B 2 70  ILE 70  402 402 ILE ILE C . n 
B 2 71  ARG 71  403 403 ARG ARG C . n 
B 2 72  GLY 72  404 404 GLY GLY C . n 
B 2 73  ASN 73  405 405 ASN ASN C . n 
B 2 74  GLU 74  406 406 GLU GLU C . n 
B 2 75  VAL 75  407 407 VAL VAL C . n 
B 2 76  SER 76  408 408 SER SER C . n 
B 2 77  GLN 77  409 409 GLN GLN C . n 
B 2 78  ILE 78  410 410 ILE ILE C . n 
B 2 79  ALA 79  411 411 ALA ALA C . n 
B 2 80  PRO 80  412 412 PRO PRO C . n 
B 2 81  GLY 81  413 413 GLY GLY C . n 
B 2 82  GLN 82  414 414 GLN GLN C . n 
B 2 83  THR 83  415 415 THR THR C . n 
B 2 84  GLY 84  416 416 GLY GLY C . n 
B 2 85  ASN 85  417 417 ASN ASN C . n 
B 2 86  ILE 86  418 418 ILE ILE C . n 
B 2 87  ALA 87  419 419 ALA ALA C . n 
B 2 88  ASP 88  420 420 ASP ASP C . n 
B 2 89  TYR 89  421 421 TYR TYR C . n 
B 2 90  ASN 90  422 422 ASN ASN C . n 
B 2 91  TYR 91  423 423 TYR TYR C . n 
B 2 92  LYS 92  424 424 LYS LYS C . n 
B 2 93  LEU 93  425 425 LEU LEU C . n 
B 2 94  PRO 94  426 426 PRO PRO C . n 
B 2 95  ASP 95  427 427 ASP ASP C . n 
B 2 96  ASP 96  428 428 ASP ASP C . n 
B 2 97  PHE 97  429 429 PHE PHE C . n 
B 2 98  THR 98  430 430 THR THR C . n 
B 2 99  GLY 99  431 431 GLY GLY C . n 
B 2 100 CYS 100 432 432 CYS CYS C . n 
B 2 101 VAL 101 433 433 VAL VAL C . n 
B 2 102 ILE 102 434 434 ILE ILE C . n 
B 2 103 ALA 103 435 435 ALA ALA C . n 
B 2 104 TRP 104 436 436 TRP TRP C . n 
B 2 105 ASN 105 437 437 ASN ASN C . n 
B 2 106 SER 106 438 438 SER SER C . n 
B 2 107 ASN 107 439 439 ASN ASN C . n 
B 2 108 LYS 108 440 440 LYS LYS C . n 
B 2 109 LEU 109 441 441 LEU LEU C . n 
B 2 110 ASP 110 442 442 ASP ASP C . n 
B 2 111 SER 111 443 443 SER SER C . n 
B 2 112 LYS 112 444 444 LYS LYS C . n 
B 2 113 VAL 113 445 445 VAL VAL C . n 
B 2 114 GLY 114 446 446 GLY GLY C . n 
B 2 115 GLY 115 447 447 GLY GLY C . n 
B 2 116 ASN 116 448 448 ASN ASN C . n 
B 2 117 TYR 117 449 449 TYR TYR C . n 
B 2 118 ASN 118 450 450 ASN ASN C . n 
B 2 119 TYR 119 451 451 TYR TYR C . n 
B 2 120 ARG 120 452 452 ARG ARG C . n 
B 2 121 TYR 121 453 453 TYR TYR C . n 
B 2 122 ARG 122 454 454 ARG ARG C . n 
B 2 123 LEU 123 455 455 LEU LEU C . n 
B 2 124 PHE 124 456 456 PHE PHE C . n 
B 2 125 ARG 125 457 457 ARG ARG C . n 
B 2 126 LYS 126 458 458 LYS LYS C . n 
B 2 127 SER 127 459 459 SER SER C . n 
B 2 128 ASN 128 460 460 ASN ASN C . n 
B 2 129 LEU 129 461 461 LEU LEU C . n 
B 2 130 LYS 130 462 462 LYS LYS C . n 
B 2 131 PRO 131 463 463 PRO PRO C . n 
B 2 132 PHE 132 464 464 PHE PHE C . n 
B 2 133 GLU 133 465 465 GLU GLU C . n 
B 2 134 ARG 134 466 466 ARG ARG C . n 
B 2 135 ASP 135 467 467 ASP ASP C . n 
B 2 136 ILE 136 468 468 ILE ILE C . n 
B 2 137 SER 137 469 469 SER SER C . n 
B 2 138 THR 138 470 470 THR THR C . n 
B 2 139 GLU 139 471 471 GLU GLU C . n 
B 2 140 ILE 140 472 472 ILE ILE C . n 
B 2 141 TYR 141 473 473 TYR TYR C . n 
B 2 142 GLN 142 474 474 GLN GLN C . n 
B 2 143 ALA 143 475 475 ALA ALA C . n 
B 2 144 GLY 144 476 476 GLY GLY C . n 
B 2 145 ASN 145 477 477 ASN ASN C . n 
B 2 146 LYS 146 478 478 LYS LYS C . n 
B 2 147 PRO 147 479 479 PRO PRO C . n 
B 2 148 CYS 148 480 480 CYS CYS C . n 
B 2 149 ASN 149 481 481 ASN ASN C . n 
B 2 150 GLY 150 482 482 GLY GLY C . n 
B 2 151 VAL 151 483 483 VAL VAL C . n 
B 2 152 ALA 152 484 484 ALA ALA C . n 
B 2 153 GLY 153 485 485 GLY GLY C . n 
B 2 154 VAL 154 486 486 VAL VAL C . n 
B 2 155 ASN 155 487 487 ASN ASN C . n 
B 2 156 CYS 156 488 488 CYS CYS C . n 
B 2 157 TYR 157 489 489 TYR TYR C . n 
B 2 158 PHE 158 490 490 PHE PHE C . n 
B 2 159 PRO 159 491 491 PRO PRO C . n 
B 2 160 LEU 160 492 492 LEU LEU C . n 
B 2 161 GLN 161 493 493 GLN GLN C . n 
B 2 162 SER 162 494 494 SER SER C . n 
B 2 163 TYR 163 495 495 TYR TYR C . n 
B 2 164 GLY 164 496 496 GLY GLY C . n 
B 2 165 PHE 165 497 497 PHE PHE C . n 
B 2 166 ARG 166 498 498 ARG ARG C . n 
B 2 167 PRO 167 499 499 PRO PRO C . n 
B 2 168 THR 168 500 500 THR THR C . n 
B 2 169 TYR 169 501 501 TYR TYR C . n 
B 2 170 GLY 170 502 502 GLY GLY C . n 
B 2 171 VAL 171 503 503 VAL VAL C . n 
B 2 172 GLY 172 504 504 GLY GLY C . n 
B 2 173 HIS 173 505 505 HIS HIS C . n 
B 2 174 GLN 174 506 506 GLN GLN C . n 
B 2 175 PRO 175 507 507 PRO PRO C . n 
B 2 176 TYR 176 508 508 TYR TYR C . n 
B 2 177 ARG 177 509 509 ARG ARG C . n 
B 2 178 VAL 178 510 510 VAL VAL C . n 
B 2 179 VAL 179 511 511 VAL VAL C . n 
B 2 180 VAL 180 512 512 VAL VAL C . n 
B 2 181 LEU 181 513 513 LEU LEU C . n 
B 2 182 SER 182 514 514 SER SER C . n 
B 2 183 PHE 183 515 515 PHE PHE C . n 
B 2 184 GLU 184 516 516 GLU GLU C . n 
B 2 185 LEU 185 517 517 LEU LEU C . n 
B 2 186 LEU 186 518 518 LEU LEU C . n 
B 2 187 HIS 187 519 519 HIS HIS C . n 
B 2 188 ALA 188 520 520 ALA ALA C . n 
B 2 189 PRO 189 521 521 PRO PRO C . n 
B 2 190 ALA 190 522 522 ALA ALA C . n 
B 2 191 THR 191 523 523 THR THR C . n 
B 2 192 VAL 192 524 524 VAL VAL C . n 
B 2 193 CYS 193 525 525 CYS CYS C . n 
B 2 194 GLY 194 526 526 GLY GLY C . n 
C 2 1   THR 1   333 333 THR THR D . n 
C 2 2   ASN 2   334 334 ASN ASN D . n 
C 2 3   LEU 3   335 335 LEU LEU D . n 
C 2 4   CYS 4   336 336 CYS CYS D . n 
C 2 5   PRO 5   337 337 PRO PRO D . n 
C 2 6   PHE 6   338 338 PHE PHE D . n 
C 2 7   ASP 7   339 339 ASP ASP D . n 
C 2 8   GLU 8   340 340 GLU GLU D . n 
C 2 9   VAL 9   341 341 VAL VAL D . n 
C 2 10  PHE 10  342 342 PHE PHE D . n 
C 2 11  ASN 11  343 343 ASN ASN D . n 
C 2 12  ALA 12  344 344 ALA ALA D . n 
C 2 13  THR 13  345 345 THR THR D . n 
C 2 14  ARG 14  346 346 ARG ARG D . n 
C 2 15  PHE 15  347 347 PHE PHE D . n 
C 2 16  ALA 16  348 348 ALA ALA D . n 
C 2 17  SER 17  349 349 SER SER D . n 
C 2 18  VAL 18  350 350 VAL VAL D . n 
C 2 19  TYR 19  351 351 TYR TYR D . n 
C 2 20  ALA 20  352 352 ALA ALA D . n 
C 2 21  TRP 21  353 353 TRP TRP D . n 
C 2 22  ASN 22  354 354 ASN ASN D . n 
C 2 23  ARG 23  355 355 ARG ARG D . n 
C 2 24  LYS 24  356 356 LYS LYS D . n 
C 2 25  ARG 25  357 357 ARG ARG D . n 
C 2 26  ILE 26  358 358 ILE ILE D . n 
C 2 27  SER 27  359 359 SER SER D . n 
C 2 28  ASN 28  360 360 ASN ASN D . n 
C 2 29  CYS 29  361 361 CYS CYS D . n 
C 2 30  VAL 30  362 362 VAL VAL D . n 
C 2 31  ALA 31  363 363 ALA ALA D . n 
C 2 32  ASP 32  364 364 ASP ASP D . n 
C 2 33  TYR 33  365 365 TYR TYR D . n 
C 2 34  SER 34  366 366 SER SER D . n 
C 2 35  VAL 35  367 367 VAL VAL D . n 
C 2 36  LEU 36  368 368 LEU LEU D . n 
C 2 37  TYR 37  369 369 TYR TYR D . n 
C 2 38  ASN 38  370 370 ASN ASN D . n 
C 2 39  PHE 39  371 371 PHE PHE D . n 
C 2 40  ALA 40  372 372 ALA ALA D . n 
C 2 41  PRO 41  373 373 PRO PRO D . n 
C 2 42  PHE 42  374 374 PHE PHE D . n 
C 2 43  PHE 43  375 375 PHE PHE D . n 
C 2 44  THR 44  376 376 THR THR D . n 
C 2 45  PHE 45  377 377 PHE PHE D . n 
C 2 46  LYS 46  378 378 LYS LYS D . n 
C 2 47  CYS 47  379 379 CYS CYS D . n 
C 2 48  TYR 48  380 380 TYR TYR D . n 
C 2 49  GLY 49  381 381 GLY GLY D . n 
C 2 50  VAL 50  382 382 VAL VAL D . n 
C 2 51  SER 51  383 383 SER SER D . n 
C 2 52  PRO 52  384 384 PRO PRO D . n 
C 2 53  THR 53  385 385 THR THR D . n 
C 2 54  LYS 54  386 386 LYS LYS D . n 
C 2 55  LEU 55  387 387 LEU LEU D . n 
C 2 56  ASN 56  388 388 ASN ASN D . n 
C 2 57  ASP 57  389 389 ASP ASP D . n 
C 2 58  LEU 58  390 390 LEU LEU D . n 
C 2 59  CYS 59  391 391 CYS CYS D . n 
C 2 60  PHE 60  392 392 PHE PHE D . n 
C 2 61  THR 61  393 393 THR THR D . n 
C 2 62  ASN 62  394 394 ASN ASN D . n 
C 2 63  VAL 63  395 395 VAL VAL D . n 
C 2 64  TYR 64  396 396 TYR TYR D . n 
C 2 65  ALA 65  397 397 ALA ALA D . n 
C 2 66  ASP 66  398 398 ASP ASP D . n 
C 2 67  SER 67  399 399 SER SER D . n 
C 2 68  PHE 68  400 400 PHE PHE D . n 
C 2 69  VAL 69  401 401 VAL VAL D . n 
C 2 70  ILE 70  402 402 ILE ILE D . n 
C 2 71  ARG 71  403 403 ARG ARG D . n 
C 2 72  GLY 72  404 404 GLY GLY D . n 
C 2 73  ASN 73  405 405 ASN ASN D . n 
C 2 74  GLU 74  406 406 GLU GLU D . n 
C 2 75  VAL 75  407 407 VAL VAL D . n 
C 2 76  SER 76  408 408 SER SER D . n 
C 2 77  GLN 77  409 409 GLN GLN D . n 
C 2 78  ILE 78  410 410 ILE ILE D . n 
C 2 79  ALA 79  411 411 ALA ALA D . n 
C 2 80  PRO 80  412 412 PRO PRO D . n 
C 2 81  GLY 81  413 413 GLY GLY D . n 
C 2 82  GLN 82  414 414 GLN GLN D . n 
C 2 83  THR 83  415 415 THR THR D . n 
C 2 84  GLY 84  416 416 GLY GLY D . n 
C 2 85  ASN 85  417 417 ASN ASN D . n 
C 2 86  ILE 86  418 418 ILE ILE D . n 
C 2 87  ALA 87  419 419 ALA ALA D . n 
C 2 88  ASP 88  420 420 ASP ASP D . n 
C 2 89  TYR 89  421 421 TYR TYR D . n 
C 2 90  ASN 90  422 422 ASN ASN D . n 
C 2 91  TYR 91  423 423 TYR TYR D . n 
C 2 92  LYS 92  424 424 LYS LYS D . n 
C 2 93  LEU 93  425 425 LEU LEU D . n 
C 2 94  PRO 94  426 426 PRO PRO D . n 
C 2 95  ASP 95  427 427 ASP ASP D . n 
C 2 96  ASP 96  428 428 ASP ASP D . n 
C 2 97  PHE 97  429 429 PHE PHE D . n 
C 2 98  THR 98  430 430 THR THR D . n 
C 2 99  GLY 99  431 431 GLY GLY D . n 
C 2 100 CYS 100 432 432 CYS CYS D . n 
C 2 101 VAL 101 433 433 VAL VAL D . n 
C 2 102 ILE 102 434 434 ILE ILE D . n 
C 2 103 ALA 103 435 435 ALA ALA D . n 
C 2 104 TRP 104 436 436 TRP TRP D . n 
C 2 105 ASN 105 437 437 ASN ASN D . n 
C 2 106 SER 106 438 438 SER SER D . n 
C 2 107 ASN 107 439 439 ASN ASN D . n 
C 2 108 LYS 108 440 440 LYS LYS D . n 
C 2 109 LEU 109 441 441 LEU LEU D . n 
C 2 110 ASP 110 442 442 ASP ASP D . n 
C 2 111 SER 111 443 443 SER SER D . n 
C 2 112 LYS 112 444 444 LYS LYS D . n 
C 2 113 VAL 113 445 445 VAL VAL D . n 
C 2 114 GLY 114 446 446 GLY GLY D . n 
C 2 115 GLY 115 447 447 GLY GLY D . n 
C 2 116 ASN 116 448 448 ASN ASN D . n 
C 2 117 TYR 117 449 449 TYR TYR D . n 
C 2 118 ASN 118 450 450 ASN ASN D . n 
C 2 119 TYR 119 451 451 TYR TYR D . n 
C 2 120 ARG 120 452 452 ARG ARG D . n 
C 2 121 TYR 121 453 453 TYR TYR D . n 
C 2 122 ARG 122 454 454 ARG ARG D . n 
C 2 123 LEU 123 455 455 LEU LEU D . n 
C 2 124 PHE 124 456 456 PHE PHE D . n 
C 2 125 ARG 125 457 457 ARG ARG D . n 
C 2 126 LYS 126 458 458 LYS LYS D . n 
C 2 127 SER 127 459 459 SER SER D . n 
C 2 128 ASN 128 460 460 ASN ASN D . n 
C 2 129 LEU 129 461 461 LEU LEU D . n 
C 2 130 LYS 130 462 462 LYS LYS D . n 
C 2 131 PRO 131 463 463 PRO PRO D . n 
C 2 132 PHE 132 464 464 PHE PHE D . n 
C 2 133 GLU 133 465 465 GLU GLU D . n 
C 2 134 ARG 134 466 466 ARG ARG D . n 
C 2 135 ASP 135 467 467 ASP ASP D . n 
C 2 136 ILE 136 468 468 ILE ILE D . n 
C 2 137 SER 137 469 469 SER SER D . n 
C 2 138 THR 138 470 470 THR THR D . n 
C 2 139 GLU 139 471 471 GLU GLU D . n 
C 2 140 ILE 140 472 472 ILE ILE D . n 
C 2 141 TYR 141 473 473 TYR TYR D . n 
C 2 142 GLN 142 474 474 GLN GLN D . n 
C 2 143 ALA 143 475 475 ALA ALA D . n 
C 2 144 GLY 144 476 476 GLY GLY D . n 
C 2 145 ASN 145 477 477 ASN ASN D . n 
C 2 146 LYS 146 478 478 LYS LYS D . n 
C 2 147 PRO 147 479 479 PRO PRO D . n 
C 2 148 CYS 148 480 480 CYS CYS D . n 
C 2 149 ASN 149 481 481 ASN ASN D . n 
C 2 150 GLY 150 482 482 GLY GLY D . n 
C 2 151 VAL 151 483 483 VAL VAL D . n 
C 2 152 ALA 152 484 484 ALA ALA D . n 
C 2 153 GLY 153 485 485 GLY GLY D . n 
C 2 154 VAL 154 486 486 VAL VAL D . n 
C 2 155 ASN 155 487 487 ASN ASN D . n 
C 2 156 CYS 156 488 488 CYS CYS D . n 
C 2 157 TYR 157 489 489 TYR TYR D . n 
C 2 158 PHE 158 490 490 PHE PHE D . n 
C 2 159 PRO 159 491 491 PRO PRO D . n 
C 2 160 LEU 160 492 492 LEU LEU D . n 
C 2 161 GLN 161 493 493 GLN GLN D . n 
C 2 162 SER 162 494 494 SER SER D . n 
C 2 163 TYR 163 495 495 TYR TYR D . n 
C 2 164 GLY 164 496 496 GLY GLY D . n 
C 2 165 PHE 165 497 497 PHE PHE D . n 
C 2 166 ARG 166 498 498 ARG ARG D . n 
C 2 167 PRO 167 499 499 PRO PRO D . n 
C 2 168 THR 168 500 500 THR THR D . n 
C 2 169 TYR 169 501 501 TYR TYR D . n 
C 2 170 GLY 170 502 502 GLY GLY D . n 
C 2 171 VAL 171 503 503 VAL VAL D . n 
C 2 172 GLY 172 504 504 GLY GLY D . n 
C 2 173 HIS 173 505 505 HIS HIS D . n 
C 2 174 GLN 174 506 506 GLN GLN D . n 
C 2 175 PRO 175 507 507 PRO PRO D . n 
C 2 176 TYR 176 508 508 TYR TYR D . n 
C 2 177 ARG 177 509 509 ARG ARG D . n 
C 2 178 VAL 178 510 510 VAL VAL D . n 
C 2 179 VAL 179 511 511 VAL VAL D . n 
C 2 180 VAL 180 512 512 VAL VAL D . n 
C 2 181 LEU 181 513 513 LEU LEU D . n 
C 2 182 SER 182 514 514 SER SER D . n 
C 2 183 PHE 183 515 515 PHE PHE D . n 
C 2 184 GLU 184 516 516 GLU GLU D . n 
C 2 185 LEU 185 517 517 LEU LEU D . n 
C 2 186 LEU 186 518 518 LEU LEU D . n 
C 2 187 HIS 187 519 519 HIS HIS D . n 
C 2 188 ALA 188 520 520 ALA ALA D . n 
C 2 189 PRO 189 521 521 PRO PRO D . n 
C 2 190 ALA 190 522 522 ALA ALA D . n 
C 2 191 THR 191 523 523 THR THR D . n 
C 2 192 VAL 192 524 524 VAL VAL D . n 
C 2 193 CYS 193 525 525 CYS CYS D . n 
C 2 194 GLY 194 526 526 GLY GLY D . n 
D 1 1   ASP 1   17  ?   ?   ?   A . n 
D 1 2   PRO 2   18  18  PRO PRO A . n 
D 1 3   SER 3   19  19  SER SER A . n 
D 1 4   THR 4   20  20  THR THR A . n 
D 1 5   ILE 5   21  21  ILE ILE A . n 
D 1 6   GLU 6   22  22  GLU GLU A . n 
D 1 7   GLU 7   23  23  GLU GLU A . n 
D 1 8   GLN 8   24  24  GLN GLN A . n 
D 1 9   ALA 9   25  25  ALA ALA A . n 
D 1 10  LYS 10  26  26  LYS LYS A . n 
D 1 11  THR 11  27  27  THR THR A . n 
D 1 12  PHE 12  28  28  PHE PHE A . n 
D 1 13  LEU 13  29  29  LEU LEU A . n 
D 1 14  ASP 14  30  30  ASP ASP A . n 
D 1 15  LYS 15  31  31  LYS LYS A . n 
D 1 16  PHE 16  32  32  PHE PHE A . n 
D 1 17  ASN 17  33  33  ASN ASN A . n 
D 1 18  HIS 18  34  34  HIS HIS A . n 
D 1 19  GLU 19  35  35  GLU GLU A . n 
D 1 20  ALA 20  36  36  ALA ALA A . n 
D 1 21  GLU 21  37  37  GLU GLU A . n 
D 1 22  ASP 22  38  38  ASP ASP A . n 
D 1 23  LEU 23  39  39  LEU LEU A . n 
D 1 24  PHE 24  40  40  PHE PHE A . n 
D 1 25  TYR 25  41  41  TYR TYR A . n 
D 1 26  GLN 26  42  42  GLN GLN A . n 
D 1 27  SER 27  43  43  SER SER A . n 
D 1 28  SER 28  44  44  SER SER A . n 
D 1 29  LEU 29  45  45  LEU LEU A . n 
D 1 30  ALA 30  46  46  ALA ALA A . n 
D 1 31  SER 31  47  47  SER SER A . n 
D 1 32  TRP 32  48  48  TRP TRP A . n 
D 1 33  ASN 33  49  49  ASN ASN A . n 
D 1 34  TYR 34  50  50  TYR TYR A . n 
D 1 35  ASN 35  51  51  ASN ASN A . n 
D 1 36  THR 36  52  52  THR THR A . n 
D 1 37  ASN 37  53  53  ASN ASN A . n 
D 1 38  ILE 38  54  54  ILE ILE A . n 
D 1 39  THR 39  55  55  THR THR A . n 
D 1 40  GLU 40  56  56  GLU GLU A . n 
D 1 41  GLU 41  57  57  GLU GLU A . n 
D 1 42  ASN 42  58  58  ASN ASN A . n 
D 1 43  VAL 43  59  59  VAL VAL A . n 
D 1 44  GLN 44  60  60  GLN GLN A . n 
D 1 45  ASN 45  61  61  ASN ASN A . n 
D 1 46  MET 46  62  62  MET MET A . n 
D 1 47  ASN 47  63  63  ASN ASN A . n 
D 1 48  ASN 48  64  64  ASN ASN A . n 
D 1 49  ALA 49  65  65  ALA ALA A . n 
D 1 50  GLY 50  66  66  GLY GLY A . n 
D 1 51  ASP 51  67  67  ASP ASP A . n 
D 1 52  LYS 52  68  68  LYS LYS A . n 
D 1 53  TRP 53  69  69  TRP TRP A . n 
D 1 54  SER 54  70  70  SER SER A . n 
D 1 55  ALA 55  71  71  ALA ALA A . n 
D 1 56  PHE 56  72  72  PHE PHE A . n 
D 1 57  LEU 57  73  73  LEU LEU A . n 
D 1 58  LYS 58  74  74  LYS LYS A . n 
D 1 59  GLU 59  75  75  GLU GLU A . n 
D 1 60  GLN 60  76  76  GLN GLN A . n 
D 1 61  SER 61  77  77  SER SER A . n 
D 1 62  THR 62  78  78  THR THR A . n 
D 1 63  LEU 63  79  79  LEU LEU A . n 
D 1 64  ALA 64  80  80  ALA ALA A . n 
D 1 65  GLN 65  81  81  GLN GLN A . n 
D 1 66  MET 66  82  82  MET MET A . n 
D 1 67  TYR 67  83  83  TYR TYR A . n 
D 1 68  PRO 68  84  84  PRO PRO A . n 
D 1 69  LEU 69  85  85  LEU LEU A . n 
D 1 70  GLN 70  86  86  GLN GLN A . n 
D 1 71  GLU 71  87  87  GLU GLU A . n 
D 1 72  ILE 72  88  88  ILE ILE A . n 
D 1 73  GLN 73  89  89  GLN GLN A . n 
D 1 74  ASN 74  90  90  ASN ASN A . n 
D 1 75  LEU 75  91  91  LEU LEU A . n 
D 1 76  THR 76  92  92  THR THR A . n 
D 1 77  VAL 77  93  93  VAL VAL A . n 
D 1 78  LYS 78  94  94  LYS LYS A . n 
D 1 79  LEU 79  95  95  LEU LEU A . n 
D 1 80  GLN 80  96  96  GLN GLN A . n 
D 1 81  LEU 81  97  97  LEU LEU A . n 
D 1 82  GLN 82  98  98  GLN GLN A . n 
D 1 83  ALA 83  99  99  ALA ALA A . n 
D 1 84  LEU 84  100 100 LEU LEU A . n 
D 1 85  GLN 85  101 101 GLN GLN A . n 
D 1 86  GLN 86  102 102 GLN GLN A . n 
D 1 87  ASN 87  103 103 ASN ASN A . n 
D 1 88  GLY 88  104 104 GLY GLY A . n 
D 1 89  SER 89  105 105 SER SER A . n 
D 1 90  SER 90  106 106 SER SER A . n 
D 1 91  VAL 91  107 107 VAL VAL A . n 
D 1 92  LEU 92  108 108 LEU LEU A . n 
D 1 93  SER 93  109 109 SER SER A . n 
D 1 94  GLU 94  110 110 GLU GLU A . n 
D 1 95  ASP 95  111 111 ASP ASP A . n 
D 1 96  LYS 96  112 112 LYS LYS A . n 
D 1 97  SER 97  113 113 SER SER A . n 
D 1 98  LYS 98  114 114 LYS LYS A . n 
D 1 99  ARG 99  115 115 ARG ARG A . n 
D 1 100 LEU 100 116 116 LEU LEU A . n 
D 1 101 ASN 101 117 117 ASN ASN A . n 
D 1 102 THR 102 118 118 THR THR A . n 
D 1 103 ILE 103 119 119 ILE ILE A . n 
D 1 104 LEU 104 120 120 LEU LEU A . n 
D 1 105 ASN 105 121 121 ASN ASN A . n 
D 1 106 THR 106 122 122 THR THR A . n 
D 1 107 MET 107 123 123 MET MET A . n 
D 1 108 SER 108 124 124 SER SER A . n 
D 1 109 THR 109 125 125 THR THR A . n 
D 1 110 ILE 110 126 126 ILE ILE A . n 
D 1 111 TYR 111 127 127 TYR TYR A . n 
D 1 112 SER 112 128 128 SER SER A . n 
D 1 113 THR 113 129 129 THR THR A . n 
D 1 114 GLY 114 130 130 GLY GLY A . n 
D 1 115 LYS 115 131 131 LYS LYS A . n 
D 1 116 VAL 116 132 132 VAL VAL A . n 
D 1 117 CYS 117 133 133 CYS CYS A . n 
D 1 118 ASN 118 134 134 ASN ASN A . n 
D 1 119 PRO 119 135 135 PRO PRO A . n 
D 1 120 ASP 120 136 136 ASP ASP A . n 
D 1 121 ASN 121 137 137 ASN ASN A . n 
D 1 122 PRO 122 138 138 PRO PRO A . n 
D 1 123 GLN 123 139 139 GLN GLN A . n 
D 1 124 GLU 124 140 140 GLU GLU A . n 
D 1 125 CYS 125 141 141 CYS CYS A . n 
D 1 126 LEU 126 142 142 LEU LEU A . n 
D 1 127 LEU 127 143 143 LEU LEU A . n 
D 1 128 LEU 128 144 144 LEU LEU A . n 
D 1 129 GLU 129 145 145 GLU GLU A . n 
D 1 130 PRO 130 146 146 PRO PRO A . n 
D 1 131 GLY 131 147 147 GLY GLY A . n 
D 1 132 LEU 132 148 148 LEU LEU A . n 
D 1 133 ASN 133 149 149 ASN ASN A . n 
D 1 134 GLU 134 150 150 GLU GLU A . n 
D 1 135 ILE 135 151 151 ILE ILE A . n 
D 1 136 MET 136 152 152 MET MET A . n 
D 1 137 ALA 137 153 153 ALA ALA A . n 
D 1 138 ASN 138 154 154 ASN ASN A . n 
D 1 139 SER 139 155 155 SER SER A . n 
D 1 140 LEU 140 156 156 LEU LEU A . n 
D 1 141 ASP 141 157 157 ASP ASP A . n 
D 1 142 TYR 142 158 158 TYR TYR A . n 
D 1 143 ASN 143 159 159 ASN ASN A . n 
D 1 144 GLU 144 160 160 GLU GLU A . n 
D 1 145 ARG 145 161 161 ARG ARG A . n 
D 1 146 LEU 146 162 162 LEU LEU A . n 
D 1 147 TRP 147 163 163 TRP TRP A . n 
D 1 148 ALA 148 164 164 ALA ALA A . n 
D 1 149 TRP 149 165 165 TRP TRP A . n 
D 1 150 GLU 150 166 166 GLU GLU A . n 
D 1 151 SER 151 167 167 SER SER A . n 
D 1 152 TRP 152 168 168 TRP TRP A . n 
D 1 153 ARG 153 169 169 ARG ARG A . n 
D 1 154 SER 154 170 170 SER SER A . n 
D 1 155 GLU 155 171 171 GLU GLU A . n 
D 1 156 VAL 156 172 172 VAL VAL A . n 
D 1 157 GLY 157 173 173 GLY GLY A . n 
D 1 158 LYS 158 174 174 LYS LYS A . n 
D 1 159 GLN 159 175 175 GLN GLN A . n 
D 1 160 LEU 160 176 176 LEU LEU A . n 
D 1 161 ARG 161 177 177 ARG ARG A . n 
D 1 162 PRO 162 178 178 PRO PRO A . n 
D 1 163 LEU 163 179 179 LEU LEU A . n 
D 1 164 TYR 164 180 180 TYR TYR A . n 
D 1 165 GLU 165 181 181 GLU GLU A . n 
D 1 166 GLU 166 182 182 GLU GLU A . n 
D 1 167 TYR 167 183 183 TYR TYR A . n 
D 1 168 VAL 168 184 184 VAL VAL A . n 
D 1 169 VAL 169 185 185 VAL VAL A . n 
D 1 170 LEU 170 186 186 LEU LEU A . n 
D 1 171 LYS 171 187 187 LYS LYS A . n 
D 1 172 ASN 172 188 188 ASN ASN A . n 
D 1 173 GLU 173 189 189 GLU GLU A . n 
D 1 174 MET 174 190 190 MET MET A . n 
D 1 175 ALA 175 191 191 ALA ALA A . n 
D 1 176 ARG 176 192 192 ARG ARG A . n 
D 1 177 ALA 177 193 193 ALA ALA A . n 
D 1 178 ASN 178 194 194 ASN ASN A . n 
D 1 179 HIS 179 195 195 HIS HIS A . n 
D 1 180 TYR 180 196 196 TYR TYR A . n 
D 1 181 GLU 181 197 197 GLU GLU A . n 
D 1 182 ASP 182 198 198 ASP ASP A . n 
D 1 183 TYR 183 199 199 TYR TYR A . n 
D 1 184 GLY 184 200 200 GLY GLY A . n 
D 1 185 ASP 185 201 201 ASP ASP A . n 
D 1 186 TYR 186 202 202 TYR TYR A . n 
D 1 187 TRP 187 203 203 TRP TRP A . n 
D 1 188 ARG 188 204 204 ARG ARG A . n 
D 1 189 GLY 189 205 205 GLY GLY A . n 
D 1 190 ASP 190 206 206 ASP ASP A . n 
D 1 191 TYR 191 207 207 TYR TYR A . n 
D 1 192 GLU 192 208 208 GLU GLU A . n 
D 1 193 VAL 193 209 209 VAL VAL A . n 
D 1 194 ASN 194 210 210 ASN ASN A . n 
D 1 195 GLY 195 211 211 GLY GLY A . n 
D 1 196 VAL 196 212 212 VAL VAL A . n 
D 1 197 ASP 197 213 213 ASP ASP A . n 
D 1 198 GLY 198 214 214 GLY GLY A . n 
D 1 199 TYR 199 215 215 TYR TYR A . n 
D 1 200 ASP 200 216 216 ASP ASP A . n 
D 1 201 TYR 201 217 217 TYR TYR A . n 
D 1 202 SER 202 218 218 SER SER A . n 
D 1 203 ARG 203 219 219 ARG ARG A . n 
D 1 204 GLY 204 220 220 GLY GLY A . n 
D 1 205 GLN 205 221 221 GLN GLN A . n 
D 1 206 LEU 206 222 222 LEU LEU A . n 
D 1 207 ILE 207 223 223 ILE ILE A . n 
D 1 208 GLU 208 224 224 GLU GLU A . n 
D 1 209 ASP 209 225 225 ASP ASP A . n 
D 1 210 VAL 210 226 226 VAL VAL A . n 
D 1 211 GLU 211 227 227 GLU GLU A . n 
D 1 212 HIS 212 228 228 HIS HIS A . n 
D 1 213 THR 213 229 229 THR THR A . n 
D 1 214 PHE 214 230 230 PHE PHE A . n 
D 1 215 GLU 215 231 231 GLU GLU A . n 
D 1 216 GLU 216 232 232 GLU GLU A . n 
D 1 217 ILE 217 233 233 ILE ILE A . n 
D 1 218 LYS 218 234 234 LYS LYS A . n 
D 1 219 PRO 219 235 235 PRO PRO A . n 
D 1 220 LEU 220 236 236 LEU LEU A . n 
D 1 221 TYR 221 237 237 TYR TYR A . n 
D 1 222 GLU 222 238 238 GLU GLU A . n 
D 1 223 HIS 223 239 239 HIS HIS A . n 
D 1 224 LEU 224 240 240 LEU LEU A . n 
D 1 225 HIS 225 241 241 HIS HIS A . n 
D 1 226 ALA 226 242 242 ALA ALA A . n 
D 1 227 TYR 227 243 243 TYR TYR A . n 
D 1 228 VAL 228 244 244 VAL VAL A . n 
D 1 229 ARG 229 245 245 ARG ARG A . n 
D 1 230 ALA 230 246 246 ALA ALA A . n 
D 1 231 LYS 231 247 247 LYS LYS A . n 
D 1 232 LEU 232 248 248 LEU LEU A . n 
D 1 233 MET 233 249 249 MET MET A . n 
D 1 234 ASN 234 250 250 ASN ASN A . n 
D 1 235 ALA 235 251 251 ALA ALA A . n 
D 1 236 TYR 236 252 252 TYR TYR A . n 
D 1 237 PRO 237 253 253 PRO PRO A . n 
D 1 238 SER 238 254 254 SER SER A . n 
D 1 239 TYR 239 255 255 TYR TYR A . n 
D 1 240 ILE 240 256 256 ILE ILE A . n 
D 1 241 SER 241 257 257 SER SER A . n 
D 1 242 PRO 242 258 258 PRO PRO A . n 
D 1 243 ILE 243 259 259 ILE ILE A . n 
D 1 244 GLY 244 260 260 GLY GLY A . n 
D 1 245 CYS 245 261 261 CYS CYS A . n 
D 1 246 LEU 246 262 262 LEU LEU A . n 
D 1 247 PRO 247 263 263 PRO PRO A . n 
D 1 248 ALA 248 264 264 ALA ALA A . n 
D 1 249 HIS 249 265 265 HIS HIS A . n 
D 1 250 LEU 250 266 266 LEU LEU A . n 
D 1 251 LEU 251 267 267 LEU LEU A . n 
D 1 252 GLY 252 268 268 GLY GLY A . n 
D 1 253 ASP 253 269 269 ASP ASP A . n 
D 1 254 MET 254 270 270 MET MET A . n 
D 1 255 TRP 255 271 271 TRP TRP A . n 
D 1 256 GLY 256 272 272 GLY GLY A . n 
D 1 257 ARG 257 273 273 ARG ARG A . n 
D 1 258 PHE 258 274 274 PHE PHE A . n 
D 1 259 TRP 259 275 275 TRP TRP A . n 
D 1 260 THR 260 276 276 THR THR A . n 
D 1 261 ASN 261 277 277 ASN ASN A . n 
D 1 262 LEU 262 278 278 LEU LEU A . n 
D 1 263 TYR 263 279 279 TYR TYR A . n 
D 1 264 SER 264 280 280 SER SER A . n 
D 1 265 LEU 265 281 281 LEU LEU A . n 
D 1 266 THR 266 282 282 THR THR A . n 
D 1 267 VAL 267 283 283 VAL VAL A . n 
D 1 268 PRO 268 284 284 PRO PRO A . n 
D 1 269 PHE 269 285 285 PHE PHE A . n 
D 1 270 GLY 270 286 286 GLY GLY A . n 
D 1 271 GLN 271 287 287 GLN GLN A . n 
D 1 272 LYS 272 288 288 LYS LYS A . n 
D 1 273 PRO 273 289 289 PRO PRO A . n 
D 1 274 ASN 274 290 290 ASN ASN A . n 
D 1 275 ILE 275 291 291 ILE ILE A . n 
D 1 276 ASP 276 292 292 ASP ASP A . n 
D 1 277 VAL 277 293 293 VAL VAL A . n 
D 1 278 THR 278 294 294 THR THR A . n 
D 1 279 ASP 279 295 295 ASP ASP A . n 
D 1 280 ALA 280 296 296 ALA ALA A . n 
D 1 281 MET 281 297 297 MET MET A . n 
D 1 282 VAL 282 298 298 VAL VAL A . n 
D 1 283 ASP 283 299 299 ASP ASP A . n 
D 1 284 GLN 284 300 300 GLN GLN A . n 
D 1 285 ALA 285 301 301 ALA ALA A . n 
D 1 286 TRP 286 302 302 TRP TRP A . n 
D 1 287 ASP 287 303 303 ASP ASP A . n 
D 1 288 ALA 288 304 304 ALA ALA A . n 
D 1 289 GLN 289 305 305 GLN GLN A . n 
D 1 290 ARG 290 306 306 ARG ARG A . n 
D 1 291 ILE 291 307 307 ILE ILE A . n 
D 1 292 PHE 292 308 308 PHE PHE A . n 
D 1 293 LYS 293 309 309 LYS LYS A . n 
D 1 294 GLU 294 310 310 GLU GLU A . n 
D 1 295 ALA 295 311 311 ALA ALA A . n 
D 1 296 GLU 296 312 312 GLU GLU A . n 
D 1 297 LYS 297 313 313 LYS LYS A . n 
D 1 298 PHE 298 314 314 PHE PHE A . n 
D 1 299 PHE 299 315 315 PHE PHE A . n 
D 1 300 VAL 300 316 316 VAL VAL A . n 
D 1 301 SER 301 317 317 SER SER A . n 
D 1 302 VAL 302 318 318 VAL VAL A . n 
D 1 303 GLY 303 319 319 GLY GLY A . n 
D 1 304 LEU 304 320 320 LEU LEU A . n 
D 1 305 PRO 305 321 321 PRO PRO A . n 
D 1 306 ASN 306 322 322 ASN ASN A . n 
D 1 307 MET 307 323 323 MET MET A . n 
D 1 308 THR 308 324 324 THR THR A . n 
D 1 309 GLN 309 325 325 GLN GLN A . n 
D 1 310 GLY 310 326 326 GLY GLY A . n 
D 1 311 PHE 311 327 327 PHE PHE A . n 
D 1 312 TRP 312 328 328 TRP TRP A . n 
D 1 313 GLU 313 329 329 GLU GLU A . n 
D 1 314 ASN 314 330 330 ASN ASN A . n 
D 1 315 SER 315 331 331 SER SER A . n 
D 1 316 MET 316 332 332 MET MET A . n 
D 1 317 LEU 317 333 333 LEU LEU A . n 
D 1 318 THR 318 334 334 THR THR A . n 
D 1 319 ASP 319 335 335 ASP ASP A . n 
D 1 320 PRO 320 336 336 PRO PRO A . n 
D 1 321 GLY 321 337 337 GLY GLY A . n 
D 1 322 ASN 322 338 338 ASN ASN A . n 
D 1 323 VAL 323 339 339 VAL VAL A . n 
D 1 324 GLN 324 340 340 GLN GLN A . n 
D 1 325 LYS 325 341 341 LYS LYS A . n 
D 1 326 ALA 326 342 342 ALA ALA A . n 
D 1 327 VAL 327 343 343 VAL VAL A . n 
D 1 328 CYS 328 344 344 CYS CYS A . n 
D 1 329 HIS 329 345 345 HIS HIS A . n 
D 1 330 PRO 330 346 346 PRO PRO A . n 
D 1 331 THR 331 347 347 THR THR A . n 
D 1 332 ALA 332 348 348 ALA ALA A . n 
D 1 333 TRP 333 349 349 TRP TRP A . n 
D 1 334 ASP 334 350 350 ASP ASP A . n 
D 1 335 LEU 335 351 351 LEU LEU A . n 
D 1 336 GLY 336 352 352 GLY GLY A . n 
D 1 337 LYS 337 353 353 LYS LYS A . n 
D 1 338 GLY 338 354 354 GLY GLY A . n 
D 1 339 ASP 339 355 355 ASP ASP A . n 
D 1 340 PHE 340 356 356 PHE PHE A . n 
D 1 341 ARG 341 357 357 ARG ARG A . n 
D 1 342 ILE 342 358 358 ILE ILE A . n 
D 1 343 LEU 343 359 359 LEU LEU A . n 
D 1 344 MET 344 360 360 MET MET A . n 
D 1 345 CYS 345 361 361 CYS CYS A . n 
D 1 346 THR 346 362 362 THR THR A . n 
D 1 347 LYS 347 363 363 LYS LYS A . n 
D 1 348 VAL 348 364 364 VAL VAL A . n 
D 1 349 THR 349 365 365 THR THR A . n 
D 1 350 MET 350 366 366 MET MET A . n 
D 1 351 ASP 351 367 367 ASP ASP A . n 
D 1 352 ASP 352 368 368 ASP ASP A . n 
D 1 353 PHE 353 369 369 PHE PHE A . n 
D 1 354 LEU 354 370 370 LEU LEU A . n 
D 1 355 THR 355 371 371 THR THR A . n 
D 1 356 ALA 356 372 372 ALA ALA A . n 
D 1 357 HIS 357 373 373 HIS HIS A . n 
D 1 358 HIS 358 374 374 HIS HIS A . n 
D 1 359 GLU 359 375 375 GLU GLU A . n 
D 1 360 MET 360 376 376 MET MET A . n 
D 1 361 GLY 361 377 377 GLY GLY A . n 
D 1 362 HIS 362 378 378 HIS HIS A . n 
D 1 363 ILE 363 379 379 ILE ILE A . n 
D 1 364 GLN 364 380 380 GLN GLN A . n 
D 1 365 TYR 365 381 381 TYR TYR A . n 
D 1 366 ASP 366 382 382 ASP ASP A . n 
D 1 367 MET 367 383 383 MET MET A . n 
D 1 368 ALA 368 384 384 ALA ALA A . n 
D 1 369 TYR 369 385 385 TYR TYR A . n 
D 1 370 ALA 370 386 386 ALA ALA A . n 
D 1 371 ALA 371 387 387 ALA ALA A . n 
D 1 372 GLN 372 388 388 GLN GLN A . n 
D 1 373 PRO 373 389 389 PRO PRO A . n 
D 1 374 PHE 374 390 390 PHE PHE A . n 
D 1 375 LEU 375 391 391 LEU LEU A . n 
D 1 376 LEU 376 392 392 LEU LEU A . n 
D 1 377 ARG 377 393 393 ARG ARG A . n 
D 1 378 ASN 378 394 394 ASN ASN A . n 
D 1 379 GLY 379 395 395 GLY GLY A . n 
D 1 380 ALA 380 396 396 ALA ALA A . n 
D 1 381 ASN 381 397 397 ASN ASN A . n 
D 1 382 GLU 382 398 398 GLU GLU A . n 
D 1 383 GLY 383 399 399 GLY GLY A . n 
D 1 384 PHE 384 400 400 PHE PHE A . n 
D 1 385 HIS 385 401 401 HIS HIS A . n 
D 1 386 GLU 386 402 402 GLU GLU A . n 
D 1 387 ALA 387 403 403 ALA ALA A . n 
D 1 388 VAL 388 404 404 VAL VAL A . n 
D 1 389 GLY 389 405 405 GLY GLY A . n 
D 1 390 GLU 390 406 406 GLU GLU A . n 
D 1 391 ILE 391 407 407 ILE ILE A . n 
D 1 392 MET 392 408 408 MET MET A . n 
D 1 393 SER 393 409 409 SER SER A . n 
D 1 394 LEU 394 410 410 LEU LEU A . n 
D 1 395 SER 395 411 411 SER SER A . n 
D 1 396 ALA 396 412 412 ALA ALA A . n 
D 1 397 ALA 397 413 413 ALA ALA A . n 
D 1 398 THR 398 414 414 THR THR A . n 
D 1 399 PRO 399 415 415 PRO PRO A . n 
D 1 400 LYS 400 416 416 LYS LYS A . n 
D 1 401 HIS 401 417 417 HIS HIS A . n 
D 1 402 LEU 402 418 418 LEU LEU A . n 
D 1 403 LYS 403 419 419 LYS LYS A . n 
D 1 404 SER 404 420 420 SER SER A . n 
D 1 405 ILE 405 421 421 ILE ILE A . n 
D 1 406 GLY 406 422 422 GLY GLY A . n 
D 1 407 LEU 407 423 423 LEU LEU A . n 
D 1 408 LEU 408 424 424 LEU LEU A . n 
D 1 409 SER 409 425 425 SER SER A . n 
D 1 410 PRO 410 426 426 PRO PRO A . n 
D 1 411 ASP 411 427 427 ASP ASP A . n 
D 1 412 PHE 412 428 428 PHE PHE A . n 
D 1 413 GLN 413 429 429 GLN GLN A . n 
D 1 414 GLU 414 430 430 GLU GLU A . n 
D 1 415 ASP 415 431 431 ASP ASP A . n 
D 1 416 ASN 416 432 432 ASN ASN A . n 
D 1 417 GLU 417 433 433 GLU GLU A . n 
D 1 418 THR 418 434 434 THR THR A . n 
D 1 419 GLU 419 435 435 GLU GLU A . n 
D 1 420 ILE 420 436 436 ILE ILE A . n 
D 1 421 ASN 421 437 437 ASN ASN A . n 
D 1 422 PHE 422 438 438 PHE PHE A . n 
D 1 423 LEU 423 439 439 LEU LEU A . n 
D 1 424 LEU 424 440 440 LEU LEU A . n 
D 1 425 LYS 425 441 441 LYS LYS A . n 
D 1 426 GLN 426 442 442 GLN GLN A . n 
D 1 427 ALA 427 443 443 ALA ALA A . n 
D 1 428 LEU 428 444 444 LEU LEU A . n 
D 1 429 THR 429 445 445 THR THR A . n 
D 1 430 ILE 430 446 446 ILE ILE A . n 
D 1 431 VAL 431 447 447 VAL VAL A . n 
D 1 432 GLY 432 448 448 GLY GLY A . n 
D 1 433 THR 433 449 449 THR THR A . n 
D 1 434 LEU 434 450 450 LEU LEU A . n 
D 1 435 PRO 435 451 451 PRO PRO A . n 
D 1 436 PHE 436 452 452 PHE PHE A . n 
D 1 437 THR 437 453 453 THR THR A . n 
D 1 438 TYR 438 454 454 TYR TYR A . n 
D 1 439 MET 439 455 455 MET MET A . n 
D 1 440 LEU 440 456 456 LEU LEU A . n 
D 1 441 GLU 441 457 457 GLU GLU A . n 
D 1 442 LYS 442 458 458 LYS LYS A . n 
D 1 443 TRP 443 459 459 TRP TRP A . n 
D 1 444 ARG 444 460 460 ARG ARG A . n 
D 1 445 TRP 445 461 461 TRP TRP A . n 
D 1 446 MET 446 462 462 MET MET A . n 
D 1 447 VAL 447 463 463 VAL VAL A . n 
D 1 448 PHE 448 464 464 PHE PHE A . n 
D 1 449 LYS 449 465 465 LYS LYS A . n 
D 1 450 GLY 450 466 466 GLY GLY A . n 
D 1 451 GLU 451 467 467 GLU GLU A . n 
D 1 452 ILE 452 468 468 ILE ILE A . n 
D 1 453 PRO 453 469 469 PRO PRO A . n 
D 1 454 LYS 454 470 470 LYS LYS A . n 
D 1 455 ASP 455 471 471 ASP ASP A . n 
D 1 456 GLN 456 472 472 GLN GLN A . n 
D 1 457 TRP 457 473 473 TRP TRP A . n 
D 1 458 MET 458 474 474 MET MET A . n 
D 1 459 LYS 459 475 475 LYS LYS A . n 
D 1 460 LYS 460 476 476 LYS LYS A . n 
D 1 461 TRP 461 477 477 TRP TRP A . n 
D 1 462 TRP 462 478 478 TRP TRP A . n 
D 1 463 GLU 463 479 479 GLU GLU A . n 
D 1 464 MET 464 480 480 MET MET A . n 
D 1 465 LYS 465 481 481 LYS LYS A . n 
D 1 466 ARG 466 482 482 ARG ARG A . n 
D 1 467 GLU 467 483 483 GLU GLU A . n 
D 1 468 ILE 468 484 484 ILE ILE A . n 
D 1 469 VAL 469 485 485 VAL VAL A . n 
D 1 470 GLY 470 486 486 GLY GLY A . n 
D 1 471 VAL 471 487 487 VAL VAL A . n 
D 1 472 VAL 472 488 488 VAL VAL A . n 
D 1 473 GLU 473 489 489 GLU GLU A . n 
D 1 474 PRO 474 490 490 PRO PRO A . n 
D 1 475 VAL 475 491 491 VAL VAL A . n 
D 1 476 PRO 476 492 492 PRO PRO A . n 
D 1 477 HIS 477 493 493 HIS HIS A . n 
D 1 478 ASP 478 494 494 ASP ASP A . n 
D 1 479 GLU 479 495 495 GLU GLU A . n 
D 1 480 THR 480 496 496 THR THR A . n 
D 1 481 TYR 481 497 497 TYR TYR A . n 
D 1 482 CYS 482 498 498 CYS CYS A . n 
D 1 483 ASP 483 499 499 ASP ASP A . n 
D 1 484 PRO 484 500 500 PRO PRO A . n 
D 1 485 ALA 485 501 501 ALA ALA A . n 
D 1 486 SER 486 502 502 SER SER A . n 
D 1 487 LEU 487 503 503 LEU LEU A . n 
D 1 488 PHE 488 504 504 PHE PHE A . n 
D 1 489 HIS 489 505 505 HIS HIS A . n 
D 1 490 VAL 490 506 506 VAL VAL A . n 
D 1 491 SER 491 507 507 SER SER A . n 
D 1 492 ASN 492 508 508 ASN ASN A . n 
D 1 493 ASP 493 509 509 ASP ASP A . n 
D 1 494 TYR 494 510 510 TYR TYR A . n 
D 1 495 SER 495 511 511 SER SER A . n 
D 1 496 PHE 496 512 512 PHE PHE A . n 
D 1 497 ILE 497 513 513 ILE ILE A . n 
D 1 498 ARG 498 514 514 ARG ARG A . n 
D 1 499 TYR 499 515 515 TYR TYR A . n 
D 1 500 TYR 500 516 516 TYR TYR A . n 
D 1 501 THR 501 517 517 THR THR A . n 
D 1 502 ARG 502 518 518 ARG ARG A . n 
D 1 503 THR 503 519 519 THR THR A . n 
D 1 504 LEU 504 520 520 LEU LEU A . n 
D 1 505 TYR 505 521 521 TYR TYR A . n 
D 1 506 GLN 506 522 522 GLN GLN A . n 
D 1 507 PHE 507 523 523 PHE PHE A . n 
D 1 508 GLN 508 524 524 GLN GLN A . n 
D 1 509 PHE 509 525 525 PHE PHE A . n 
D 1 510 GLN 510 526 526 GLN GLN A . n 
D 1 511 GLU 511 527 527 GLU GLU A . n 
D 1 512 ALA 512 528 528 ALA ALA A . n 
D 1 513 LEU 513 529 529 LEU LEU A . n 
D 1 514 CYS 514 530 530 CYS CYS A . n 
D 1 515 GLN 515 531 531 GLN GLN A . n 
D 1 516 ALA 516 532 532 ALA ALA A . n 
D 1 517 ALA 517 533 533 ALA ALA A . n 
D 1 518 LYS 518 534 534 LYS LYS A . n 
D 1 519 HIS 519 535 535 HIS HIS A . n 
D 1 520 GLU 520 536 536 GLU GLU A . n 
D 1 521 GLY 521 537 537 GLY GLY A . n 
D 1 522 PRO 522 538 538 PRO PRO A . n 
D 1 523 LEU 523 539 539 LEU LEU A . n 
D 1 524 HIS 524 540 540 HIS HIS A . n 
D 1 525 LYS 525 541 541 LYS LYS A . n 
D 1 526 CYS 526 542 542 CYS CYS A . n 
D 1 527 ASP 527 543 543 ASP ASP A . n 
D 1 528 ILE 528 544 544 ILE ILE A . n 
D 1 529 SER 529 545 545 SER SER A . n 
D 1 530 ASN 530 546 546 ASN ASN A . n 
D 1 531 SER 531 547 547 SER SER A . n 
D 1 532 THR 532 548 548 THR THR A . n 
D 1 533 GLU 533 549 549 GLU GLU A . n 
D 1 534 ALA 534 550 550 ALA ALA A . n 
D 1 535 GLY 535 551 551 GLY GLY A . n 
D 1 536 GLN 536 552 552 GLN GLN A . n 
D 1 537 LYS 537 553 553 LYS LYS A . n 
D 1 538 LEU 538 554 554 LEU LEU A . n 
D 1 539 PHE 539 555 555 PHE PHE A . n 
D 1 540 ASN 540 556 556 ASN ASN A . n 
D 1 541 MET 541 557 557 MET MET A . n 
D 1 542 LEU 542 558 558 LEU LEU A . n 
D 1 543 ARG 543 559 559 ARG ARG A . n 
D 1 544 LEU 544 560 560 LEU LEU A . n 
D 1 545 GLY 545 561 561 GLY GLY A . n 
D 1 546 LYS 546 562 562 LYS LYS A . n 
D 1 547 SER 547 563 563 SER SER A . n 
D 1 548 GLU 548 564 564 GLU GLU A . n 
D 1 549 PRO 549 565 565 PRO PRO A . n 
D 1 550 TRP 550 566 566 TRP TRP A . n 
D 1 551 THR 551 567 567 THR THR A . n 
D 1 552 LEU 552 568 568 LEU LEU A . n 
D 1 553 ALA 553 569 569 ALA ALA A . n 
D 1 554 LEU 554 570 570 LEU LEU A . n 
D 1 555 GLU 555 571 571 GLU GLU A . n 
D 1 556 ASN 556 572 572 ASN ASN A . n 
D 1 557 VAL 557 573 573 VAL VAL A . n 
D 1 558 VAL 558 574 574 VAL VAL A . n 
D 1 559 GLY 559 575 575 GLY GLY A . n 
D 1 560 ALA 560 576 576 ALA ALA A . n 
D 1 561 LYS 561 577 577 LYS LYS A . n 
D 1 562 ASN 562 578 578 ASN ASN A . n 
D 1 563 MET 563 579 579 MET MET A . n 
D 1 564 ASN 564 580 580 ASN ASN A . n 
D 1 565 VAL 565 581 581 VAL VAL A . n 
D 1 566 ARG 566 582 582 ARG ARG A . n 
D 1 567 PRO 567 583 583 PRO PRO A . n 
D 1 568 LEU 568 584 584 LEU LEU A . n 
D 1 569 LEU 569 585 585 LEU LEU A . n 
D 1 570 ASN 570 586 586 ASN ASN A . n 
D 1 571 TYR 571 587 587 TYR TYR A . n 
D 1 572 PHE 572 588 588 PHE PHE A . n 
D 1 573 GLU 573 589 589 GLU GLU A . n 
D 1 574 PRO 574 590 590 PRO PRO A . n 
D 1 575 LEU 575 591 591 LEU LEU A . n 
D 1 576 PHE 576 592 592 PHE PHE A . n 
D 1 577 THR 577 593 593 THR THR A . n 
D 1 578 TRP 578 594 594 TRP TRP A . n 
D 1 579 LEU 579 595 595 LEU LEU A . n 
D 1 580 LYS 580 596 596 LYS LYS A . n 
D 1 581 ASP 581 597 597 ASP ASP A . n 
D 1 582 GLN 582 598 598 GLN GLN A . n 
D 1 583 ASN 583 599 599 ASN ASN A . n 
D 1 584 LYS 584 600 600 LYS LYS A . n 
D 1 585 ASN 585 601 601 ASN ASN A . n 
D 1 586 SER 586 602 602 SER SER A . n 
D 1 587 PHE 587 603 603 PHE PHE A . n 
D 1 588 VAL 588 604 604 VAL VAL A . n 
D 1 589 GLY 589 605 605 GLY GLY A . n 
D 1 590 TRP 590 606 606 TRP TRP A . n 
D 1 591 SER 591 607 607 SER SER A . n 
D 1 592 THR 592 608 608 THR THR A . n 
D 1 593 ASP 593 609 609 ASP ASP A . n 
D 1 594 TRP 594 610 610 TRP TRP A . n 
D 1 595 SER 595 611 611 SER SER A . n 
D 1 596 PRO 596 612 612 PRO PRO A . n 
D 1 597 TYR 597 613 613 TYR TYR A . n 
D 1 598 ALA 598 614 614 ALA ALA 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 
E 3 NAG 1 E NAG 1 B NAG 907 n 
E 3 NAG 2 E NAG 2 B NAG 908 n 
E 3 BMA 3 E BMA 3 B BMA 909 n 
F 3 NAG 1 F NAG 1 B NAG 910 n 
F 3 NAG 2 F NAG 2 B NAG 911 n 
F 3 BMA 3 F BMA 3 B BMA 912 n 
G 3 NAG 1 G NAG 1 A NAG 907 n 
G 3 NAG 2 G NAG 2 A NAG 908 n 
G 3 BMA 3 G BMA 3 A BMA 909 n 
H 4 NAG 1 H NAG 1 A NAG 912 n 
H 4 NAG 2 H NAG 2 A NAG 913 n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
I 5 NAG 1 701 906 NAG NAG B . 
J 5 NAG 1 702 913 NAG NAG B . 
K 5 NAG 1 703 914 NAG NAG B . 
L 5 NAG 1 704 915 NAG NAG B . 
M 5 NAG 1 701 906 NAG NAG A . 
N 5 NAG 1 702 910 NAG NAG A . 
O 5 NAG 1 703 911 NAG NAG A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.19.1_4122: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   102.18 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XYE 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     84.468 
_cell.length_a_esd                 ? 
_cell.length_b                     165.822 
_cell.length_b_esd                 ? 
_cell.length_c                     98.981 
_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                         8XYE 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_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                   8XYE 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.72 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          66.91 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M BICINE, pH9.0,10% w/v PEG20000,2% v/v 1,4-Dioxane' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-09-12 
_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   0.9798 
_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        0.9798 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XYE 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.32 
_reflns.d_resolution_low                               50 
_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                                     38548 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.976 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.32 
_reflns_shell.d_res_low                                     3.44 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3353 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.725 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8XYE 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.32 
_refine.ls_d_res_low                             31.37 
_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                     38513 
_refine.ls_number_reflns_R_free                  1942 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.34 
_refine.ls_percent_reflns_R_free                 5.04 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1932 
_refine.ls_R_factor_R_free                       0.2421 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1907 
_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                          1.36 
_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                 25.30 
_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                            0.40 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.32 
_refine_hist.d_res_low                        31.37 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               13087 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        13087 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.013 ? 13473 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.511 ? 18318 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.196 ? 1845  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.073 ? 1965  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.012 ? 2352  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.32 3.41  . . 107 2141 80.00  . . . . 0.2978 . . . . . . . . . . . 0.3500 
'X-RAY DIFFRACTION' 3.41 3.50  . . 145 2640 100.00 . . . . 0.2649 . . . . . . . . . . . 0.3045 
'X-RAY DIFFRACTION' 3.50 3.60  . . 132 2664 100.00 . . . . 0.2513 . . . . . . . . . . . 0.2799 
'X-RAY DIFFRACTION' 3.60 3.72  . . 156 2602 100.00 . . . . 0.2301 . . . . . . . . . . . 0.2940 
'X-RAY DIFFRACTION' 3.72 3.85  . . 137 2677 100.00 . . . . 0.2167 . . . . . . . . . . . 0.2830 
'X-RAY DIFFRACTION' 3.85 4.00  . . 134 2626 100.00 . . . . 0.2006 . . . . . . . . . . . 0.2396 
'X-RAY DIFFRACTION' 4.00 4.19  . . 136 2654 100.00 . . . . 0.1956 . . . . . . . . . . . 0.2484 
'X-RAY DIFFRACTION' 4.19 4.41  . . 134 2661 100.00 . . . . 0.1793 . . . . . . . . . . . 0.2408 
'X-RAY DIFFRACTION' 4.41 4.68  . . 133 2669 100.00 . . . . 0.1641 . . . . . . . . . . . 0.2091 
'X-RAY DIFFRACTION' 4.68 5.04  . . 147 2637 100.00 . . . . 0.1567 . . . . . . . . . . . 0.2274 
'X-RAY DIFFRACTION' 5.04 5.55  . . 153 2632 100.00 . . . . 0.1759 . . . . . . . . . . . 0.2126 
'X-RAY DIFFRACTION' 5.55 6.34  . . 128 2664 100.00 . . . . 0.1887 . . . . . . . . . . . 0.2439 
'X-RAY DIFFRACTION' 6.34 7.97  . . 166 2664 100.00 . . . . 0.1821 . . . . . . . . . . . 0.2185 
'X-RAY DIFFRACTION' 7.97 31.37 . . 134 2640 97.00  . . . . 0.1595 . . . . . . . . . . . 0.2185 
# 
_struct.entry_id                     8XYE 
_struct.title                        'Crystal structure of SARS-CoV-2 BA.4 RBD and human ACE2' 
_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        8XYE 
_struct_keywords.text            'SARS-CoV-2 BA.4, human ACE2, VIRAL PROTEIN/HYDROLASE, VIRAL PROTEIN-HYDROLASE complex' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN/HYDROLASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 1 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
K N N 5 ? 
L N N 5 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP ACE2_HUMAN  Q9BYF1 ? 1 
;STIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQ
ALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRP
LYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISP
IGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGN
VQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHL
KSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYC
DPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKN
MNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYA
;
19  
2 UNP SPIKE_SARS2 P0DTC2 ? 2 
;TNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAP
GQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPL
QSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCG
;
333 
# 
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 8XYE B 3 ? 598 ? Q9BYF1 19  ? 614 ? 19  614 
2 2 8XYE C 1 ? 194 ? P0DTC2 333 ? 526 ? 333 526 
3 2 8XYE D 1 ? 194 ? P0DTC2 333 ? 526 ? 333 526 
4 1 8XYE A 3 ? 598 ? Q9BYF1 19  ? 614 ? 19  614 
# 
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 8XYE ASP B 1   ? UNP Q9BYF1 ?   ?   'expression tag' 17  1  
1 8XYE PRO B 2   ? UNP Q9BYF1 ?   ?   'expression tag' 18  2  
2 8XYE ASP C 7   ? UNP P0DTC2 GLY 339 variant          339 3  
2 8XYE PHE C 39  ? UNP P0DTC2 SER 371 variant          371 4  
2 8XYE PRO C 41  ? UNP P0DTC2 SER 373 variant          373 5  
2 8XYE PHE C 43  ? UNP P0DTC2 SER 375 variant          375 6  
2 8XYE ASN C 73  ? UNP P0DTC2 ASP 405 variant          405 7  
2 8XYE SER C 76  ? UNP P0DTC2 ARG 408 variant          408 8  
2 8XYE ASN C 85  ? UNP P0DTC2 LYS 417 variant          417 9  
2 8XYE LYS C 108 ? UNP P0DTC2 ASN 440 variant          440 10 
2 8XYE ARG C 120 ? UNP P0DTC2 LEU 452 variant          452 11 
2 8XYE ASN C 145 ? UNP P0DTC2 SER 477 variant          477 12 
2 8XYE LYS C 146 ? UNP P0DTC2 THR 478 variant          478 13 
2 8XYE ALA C 152 ? UNP P0DTC2 GLU 484 variant          484 14 
2 8XYE VAL C 154 ? UNP P0DTC2 PHE 486 variant          486 15 
2 8XYE ARG C 166 ? UNP P0DTC2 GLN 498 variant          498 16 
2 8XYE TYR C 169 ? UNP P0DTC2 ASN 501 variant          501 17 
2 8XYE HIS C 173 ? UNP P0DTC2 TYR 505 variant          505 18 
3 8XYE ASP D 7   ? UNP P0DTC2 GLY 339 variant          339 19 
3 8XYE PHE D 39  ? UNP P0DTC2 SER 371 variant          371 20 
3 8XYE PRO D 41  ? UNP P0DTC2 SER 373 variant          373 21 
3 8XYE PHE D 43  ? UNP P0DTC2 SER 375 variant          375 22 
3 8XYE ASN D 73  ? UNP P0DTC2 ASP 405 variant          405 23 
3 8XYE SER D 76  ? UNP P0DTC2 ARG 408 variant          408 24 
3 8XYE ASN D 85  ? UNP P0DTC2 LYS 417 variant          417 25 
3 8XYE LYS D 108 ? UNP P0DTC2 ASN 440 variant          440 26 
3 8XYE ARG D 120 ? UNP P0DTC2 LEU 452 variant          452 27 
3 8XYE ASN D 145 ? UNP P0DTC2 SER 477 variant          477 28 
3 8XYE LYS D 146 ? UNP P0DTC2 THR 478 variant          478 29 
3 8XYE ALA D 152 ? UNP P0DTC2 GLU 484 variant          484 30 
3 8XYE VAL D 154 ? UNP P0DTC2 PHE 486 variant          486 31 
3 8XYE ARG D 166 ? UNP P0DTC2 GLN 498 variant          498 32 
3 8XYE TYR D 169 ? UNP P0DTC2 ASN 501 variant          501 33 
3 8XYE HIS D 173 ? UNP P0DTC2 TYR 505 variant          505 34 
4 8XYE ASP A 1   ? UNP Q9BYF1 ?   ?   'expression tag' 17  35 
4 8XYE PRO A 2   ? UNP Q9BYF1 ?   ?   'expression tag' 18  36 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? dimeric 2 
2 author_defined_assembly ? dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E,F,I,J,K,L 
2 1 B,D,G,H,M,N,O   
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 4   ? THR A 36  ? THR B 20  THR B 52  1 ? 33 
HELX_P HELX_P2  AA2 THR A 39  ? GLN A 65  ? THR B 55  GLN B 81  1 ? 27 
HELX_P HELX_P3  AA3 MET A 66  ? TYR A 67  ? MET B 82  TYR B 83  5 ? 2  
HELX_P HELX_P4  AA4 PRO A 68  ? ILE A 72  ? PRO B 84  ILE B 88  5 ? 5  
HELX_P HELX_P5  AA5 ASN A 74  ? GLN A 86  ? ASN B 90  GLN B 102 1 ? 13 
HELX_P HELX_P6  AA6 ASN A 87  ? LEU A 92  ? ASN B 103 LEU B 108 5 ? 6  
HELX_P HELX_P7  AA7 SER A 93  ? THR A 113 ? SER B 109 THR B 129 1 ? 21 
HELX_P HELX_P8  AA8 GLY A 131 ? SER A 139 ? GLY B 147 SER B 155 1 ? 9  
HELX_P HELX_P9  AA9 ASP A 141 ? VAL A 156 ? ASP B 157 VAL B 172 1 ? 16 
HELX_P HELX_P10 AB1 VAL A 156 ? ASN A 178 ? VAL B 172 ASN B 194 1 ? 23 
HELX_P HELX_P11 AB2 ASP A 182 ? GLY A 189 ? ASP B 198 GLY B 205 1 ? 8  
HELX_P HELX_P12 AB3 ASP A 190 ? GLU A 192 ? ASP B 206 GLU B 208 5 ? 3  
HELX_P HELX_P13 AB4 SER A 202 ? ASN A 234 ? SER B 218 ASN B 250 1 ? 33 
HELX_P HELX_P14 AB5 LEU A 262 ? VAL A 267 ? LEU B 278 VAL B 283 1 ? 6  
HELX_P HELX_P15 AB6 VAL A 277 ? GLN A 284 ? VAL B 293 GLN B 300 1 ? 8  
HELX_P HELX_P16 AB7 ASP A 287 ? SER A 301 ? ASP B 303 SER B 317 1 ? 15 
HELX_P HELX_P17 AB8 THR A 308 ? SER A 315 ? THR B 324 SER B 331 1 ? 8  
HELX_P HELX_P18 AB9 PRO A 320 ? GLN A 324 ? PRO B 336 GLN B 340 5 ? 5  
HELX_P HELX_P19 AC1 THR A 349 ? TYR A 369 ? THR B 365 TYR B 385 1 ? 21 
HELX_P HELX_P20 AC2 ALA A 370 ? GLN A 372 ? ALA B 386 GLN B 388 5 ? 3  
HELX_P HELX_P21 AC3 PRO A 373 ? ARG A 377 ? PRO B 389 ARG B 393 5 ? 5  
HELX_P HELX_P22 AC4 GLY A 383 ? THR A 398 ? GLY B 399 THR B 414 1 ? 16 
HELX_P HELX_P23 AC5 THR A 398 ? ILE A 405 ? THR B 414 ILE B 421 1 ? 8  
HELX_P HELX_P24 AC6 ASP A 415 ? GLY A 450 ? ASP B 431 GLY B 466 1 ? 36 
HELX_P HELX_P25 AC7 PRO A 453 ? ASP A 455 ? PRO B 469 ASP B 471 5 ? 3  
HELX_P HELX_P26 AC8 GLN A 456 ? ILE A 468 ? GLN B 472 ILE B 484 1 ? 13 
HELX_P HELX_P27 AC9 ASP A 483 ? SER A 486 ? ASP B 499 SER B 502 5 ? 4  
HELX_P HELX_P28 AD1 LEU A 487 ? ASN A 492 ? LEU B 503 ASN B 508 1 ? 6  
HELX_P HELX_P29 AD2 ILE A 497 ? ALA A 517 ? ILE B 513 ALA B 533 1 ? 21 
HELX_P HELX_P30 AD3 PRO A 522 ? CYS A 526 ? PRO B 538 CYS B 542 5 ? 5  
HELX_P HELX_P31 AD4 SER A 531 ? ARG A 543 ? SER B 547 ARG B 559 1 ? 13 
HELX_P HELX_P32 AD5 PRO A 549 ? GLY A 559 ? PRO B 565 GLY B 575 1 ? 11 
HELX_P HELX_P33 AD6 VAL A 565 ? ASN A 583 ? VAL B 581 ASN B 599 1 ? 19 
HELX_P HELX_P34 AD7 PRO B 5   ? ASN B 11  ? PRO C 337 ASN C 343 1 ? 7  
HELX_P HELX_P35 AD8 SER B 17  ? TRP B 21  ? SER C 349 TRP C 353 5 ? 5  
HELX_P HELX_P36 AD9 VAL B 35  ? PHE B 39  ? VAL C 367 PHE C 371 5 ? 5  
HELX_P HELX_P37 AE1 THR B 53  ? LEU B 58  ? THR C 385 LEU C 390 5 ? 6  
HELX_P HELX_P38 AE2 ARG B 71  ? SER B 76  ? ARG C 403 SER C 408 1 ? 6  
HELX_P HELX_P39 AE3 ASN B 85  ? ASN B 90  ? ASN C 417 ASN C 422 1 ? 6  
HELX_P HELX_P40 AE4 SER B 106 ? SER B 111 ? SER C 438 SER C 443 1 ? 6  
HELX_P HELX_P41 AE5 GLY B 170 ? GLN B 174 ? GLY C 502 GLN C 506 5 ? 5  
HELX_P HELX_P42 AE6 PHE C 6   ? ASN C 11  ? PHE D 338 ASN D 343 1 ? 6  
HELX_P HELX_P43 AE7 SER C 17  ? TRP C 21  ? SER D 349 TRP D 353 5 ? 5  
HELX_P HELX_P44 AE8 ASP C 32  ? TYR C 37  ? ASP D 364 TYR D 369 1 ? 6  
HELX_P HELX_P45 AE9 LYS C 54  ? LEU C 58  ? LYS D 386 LEU D 390 5 ? 5  
HELX_P HELX_P46 AF1 GLY C 72  ? SER C 76  ? GLY D 404 SER D 408 1 ? 5  
HELX_P HELX_P47 AF2 ASN C 85  ? ASN C 90  ? ASN D 417 ASN D 422 1 ? 6  
HELX_P HELX_P48 AF3 SER C 106 ? SER C 111 ? SER D 438 SER D 443 1 ? 6  
HELX_P HELX_P49 AF4 GLY C 170 ? HIS C 173 ? GLY D 502 HIS D 505 5 ? 4  
HELX_P HELX_P50 AF5 THR D 4   ? ASN D 37  ? THR A 20  ASN A 53  1 ? 34 
HELX_P HELX_P51 AF6 THR D 39  ? GLN D 65  ? THR A 55  GLN A 81  1 ? 27 
HELX_P HELX_P52 AF7 MET D 66  ? TYR D 67  ? MET A 82  TYR A 83  5 ? 2  
HELX_P HELX_P53 AF8 PRO D 68  ? ILE D 72  ? PRO A 84  ILE A 88  5 ? 5  
HELX_P HELX_P54 AF9 ASN D 74  ? GLN D 86  ? ASN A 90  GLN A 102 1 ? 13 
HELX_P HELX_P55 AG1 ASN D 87  ? LEU D 92  ? ASN A 103 LEU A 108 5 ? 6  
HELX_P HELX_P56 AG2 SER D 93  ? GLY D 114 ? SER A 109 GLY A 130 1 ? 22 
HELX_P HELX_P57 AG3 GLY D 131 ? SER D 139 ? GLY A 147 SER A 155 1 ? 9  
HELX_P HELX_P58 AG4 ASP D 141 ? ASN D 178 ? ASP A 157 ASN A 194 1 ? 38 
HELX_P HELX_P59 AG5 ASP D 182 ? GLY D 189 ? ASP A 198 GLY A 205 1 ? 8  
HELX_P HELX_P60 AG6 ASP D 190 ? GLU D 192 ? ASP A 206 GLU A 208 5 ? 3  
HELX_P HELX_P61 AG7 GLY D 204 ? TYR D 236 ? GLY A 220 TYR A 252 1 ? 33 
HELX_P HELX_P62 AG8 PRO D 237 ? ILE D 240 ? PRO A 253 ILE A 256 5 ? 4  
HELX_P HELX_P63 AG9 HIS D 249 ? LEU D 251 ? HIS A 265 LEU A 267 5 ? 3  
HELX_P HELX_P64 AH1 LEU D 262 ? VAL D 267 ? LEU A 278 VAL A 283 1 ? 6  
HELX_P HELX_P65 AH2 VAL D 277 ? GLN D 284 ? VAL A 293 GLN A 300 1 ? 8  
HELX_P HELX_P66 AH3 ASP D 287 ? VAL D 302 ? ASP A 303 VAL A 318 1 ? 16 
HELX_P HELX_P67 AH4 THR D 308 ? SER D 315 ? THR A 324 SER A 331 1 ? 8  
HELX_P HELX_P68 AH5 THR D 349 ? TYR D 369 ? THR A 365 TYR A 385 1 ? 21 
HELX_P HELX_P69 AH6 PRO D 373 ? ARG D 377 ? PRO A 389 ARG A 393 5 ? 5  
HELX_P HELX_P70 AH7 PHE D 384 ? THR D 398 ? PHE A 400 THR A 414 1 ? 15 
HELX_P HELX_P71 AH8 THR D 398 ? ILE D 405 ? THR A 414 ILE A 421 1 ? 8  
HELX_P HELX_P72 AH9 ASP D 415 ? VAL D 431 ? ASP A 431 VAL A 447 1 ? 17 
HELX_P HELX_P73 AI1 GLY D 432 ? GLY D 450 ? GLY A 448 GLY A 466 1 ? 19 
HELX_P HELX_P74 AI2 PRO D 453 ? ASP D 455 ? PRO A 469 ASP A 471 5 ? 3  
HELX_P HELX_P75 AI3 GLN D 456 ? ILE D 468 ? GLN A 472 ILE A 484 1 ? 13 
HELX_P HELX_P76 AI4 CYS D 482 ? SER D 486 ? CYS A 498 SER A 502 5 ? 5  
HELX_P HELX_P77 AI5 LEU D 487 ? ASN D 492 ? LEU A 503 ASN A 508 1 ? 6  
HELX_P HELX_P78 AI6 ILE D 497 ? ALA D 517 ? ILE A 513 ALA A 533 1 ? 21 
HELX_P HELX_P79 AI7 PRO D 522 ? CYS D 526 ? PRO A 538 CYS A 542 5 ? 5  
HELX_P HELX_P80 AI8 SER D 531 ? ARG D 543 ? SER A 547 ARG A 559 1 ? 13 
HELX_P HELX_P81 AI9 PRO D 549 ? GLY D 559 ? PRO A 565 GLY A 575 1 ? 11 
HELX_P HELX_P82 AJ1 VAL D 565 ? PHE D 572 ? VAL A 581 PHE A 588 1 ? 8  
HELX_P HELX_P83 AJ2 PHE D 572 ? ASN D 583 ? PHE A 588 ASN A 599 1 ? 12 
HELX_P HELX_P84 AJ3 LYS D 584 ? SER D 586 ? LYS A 600 SER A 602 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 117 SG  ? ? ? 1_555 A CYS 125 SG ? ? B CYS 133 B CYS 141 1_555 ? ? ? ? ? ? ? 2.048 ? ?               
disulf2  disulf ?    ? A CYS 328 SG  ? ? ? 1_555 A CYS 345 SG ? ? B CYS 344 B CYS 361 1_555 ? ? ? ? ? ? ? 2.038 ? ?               
disulf3  disulf ?    ? A CYS 514 SG  ? ? ? 1_555 A CYS 526 SG ? ? B CYS 530 B CYS 542 1_555 ? ? ? ? ? ? ? 2.021 ? ?               
disulf4  disulf ?    ? B CYS 4   SG  ? ? ? 1_555 B CYS 29  SG ? ? C CYS 336 C CYS 361 1_555 ? ? ? ? ? ? ? 2.034 ? ?               
disulf5  disulf ?    ? B CYS 47  SG  ? ? ? 1_555 B CYS 100 SG ? ? C CYS 379 C CYS 432 1_555 ? ? ? ? ? ? ? 2.040 ? ?               
disulf6  disulf ?    ? B CYS 59  SG  ? ? ? 1_555 B CYS 193 SG ? ? C CYS 391 C CYS 525 1_555 ? ? ? ? ? ? ? 2.038 ? ?               
disulf7  disulf ?    ? B CYS 148 SG  ? ? ? 1_555 B CYS 156 SG ? ? C CYS 480 C CYS 488 1_555 ? ? ? ? ? ? ? 2.014 ? ?               
disulf8  disulf ?    ? C CYS 4   SG  ? ? ? 1_555 C CYS 29  SG ? ? D CYS 336 D CYS 361 1_555 ? ? ? ? ? ? ? 2.048 ? ?               
disulf9  disulf ?    ? C CYS 47  SG  ? ? ? 1_555 C CYS 100 SG ? ? D CYS 379 D CYS 432 1_555 ? ? ? ? ? ? ? 2.020 ? ?               
disulf10 disulf ?    ? C CYS 59  SG  ? ? ? 1_555 C CYS 193 SG ? ? D CYS 391 D CYS 525 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf11 disulf ?    ? C CYS 148 SG  ? ? ? 1_555 C CYS 156 SG ? ? D CYS 480 D CYS 488 1_555 ? ? ? ? ? ? ? 2.036 ? ?               
disulf12 disulf ?    ? D CYS 117 SG  ? ? ? 1_555 D CYS 125 SG ? ? A CYS 133 A CYS 141 1_555 ? ? ? ? ? ? ? 2.044 ? ?               
disulf13 disulf ?    ? D CYS 328 SG  ? ? ? 1_555 D CYS 345 SG ? ? A CYS 344 A CYS 361 1_555 ? ? ? ? ? ? ? 2.051 ? ?               
disulf14 disulf ?    ? D CYS 514 SG  ? ? ? 1_555 D CYS 526 SG ? ? A CYS 530 A CYS 542 1_555 ? ? ? ? ? ? ? 2.043 ? ?               
covale1  covale one  ? A ASN 37  ND2 ? ? ? 1_555 I NAG .   C1 ? ? B ASN 53  B NAG 701 1_555 ? ? ? ? ? ? ? 1.430 ? N-Glycosylation 
covale2  covale one  ? A ASN 74  ND2 ? ? ? 1_555 E NAG .   C1 ? ? B ASN 90  E NAG 1   1_555 ? ? ? ? ? ? ? 1.440 ? N-Glycosylation 
covale3  covale one  ? A ASN 87  ND2 ? ? ? 1_555 F NAG .   C1 ? ? B ASN 103 F NAG 1   1_555 ? ? ? ? ? ? ? 1.410 ? N-Glycosylation 
covale4  covale one  ? A ASN 306 ND2 ? ? ? 1_555 J NAG .   C1 ? ? B ASN 322 B NAG 702 1_555 ? ? ? ? ? ? ? 1.455 ? N-Glycosylation 
covale5  covale one  ? A ASN 416 ND2 ? ? ? 1_555 K NAG .   C1 ? ? B ASN 432 B NAG 703 1_555 ? ? ? ? ? ? ? 1.440 ? N-Glycosylation 
covale6  covale one  ? A ASN 530 ND2 ? ? ? 1_555 L NAG .   C1 ? ? B ASN 546 B NAG 704 1_555 ? ? ? ? ? ? ? 1.473 ? N-Glycosylation 
covale7  covale one  ? D ASN 37  ND2 ? ? ? 1_555 M NAG .   C1 ? ? A ASN 53  A NAG 701 1_555 ? ? ? ? ? ? ? 1.423 ? N-Glycosylation 
covale8  covale one  ? D ASN 74  ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 90  G NAG 1   1_555 ? ? ? ? ? ? ? 1.435 ? N-Glycosylation 
covale9  covale one  ? D ASN 87  ND2 ? ? ? 1_555 N NAG .   C1 ? ? A ASN 103 A NAG 702 1_555 ? ? ? ? ? ? ? 1.432 ? N-Glycosylation 
covale10 covale one  ? D ASN 306 ND2 ? ? ? 1_555 O NAG .   C1 ? ? A ASN 322 A NAG 703 1_555 ? ? ? ? ? ? ? 1.468 ? N-Glycosylation 
covale11 covale one  ? D ASN 530 ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 546 H NAG 1   1_555 ? ? ? ? ? ? ? 1.424 ? N-Glycosylation 
covale12 covale both ? E NAG .   O4  ? ? ? 1_555 E NAG .   C1 ? ? E NAG 1   E NAG 2   1_555 ? ? ? ? ? ? ? 1.425 ? ?               
covale13 covale both ? E NAG .   O4  ? ? ? 1_555 E BMA .   C1 ? ? E NAG 2   E BMA 3   1_555 ? ? ? ? ? ? ? 1.475 ? ?               
covale14 covale both ? F NAG .   O4  ? ? ? 1_555 F NAG .   C1 ? ? F NAG 1   F NAG 2   1_555 ? ? ? ? ? ? ? 1.490 ? ?               
covale15 covale both ? F NAG .   O4  ? ? ? 1_555 F BMA .   C1 ? ? F NAG 2   F BMA 3   1_555 ? ? ? ? ? ? ? 1.447 ? ?               
covale16 covale both ? G NAG .   O4  ? ? ? 1_555 G NAG .   C1 ? ? G NAG 1   G NAG 2   1_555 ? ? ? ? ? ? ? 1.448 ? ?               
covale17 covale both ? G NAG .   O4  ? ? ? 1_555 G BMA .   C1 ? ? G NAG 2   G BMA 3   1_555 ? ? ? ? ? ? ? 1.486 ? ?               
covale18 covale both ? H NAG .   O4  ? ? ? 1_555 H NAG .   C1 ? ? H NAG 1   H NAG 2   1_555 ? ? ? ? ? ? ? 1.464 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  NAG E .   ? ASN A 74  ? NAG E 1   ? 1_555 ASN B 90  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG F .   ? ASN A 87  ? NAG F 1   ? 1_555 ASN B 103 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG G .   ? ASN D 74  ? NAG G 1   ? 1_555 ASN A 90  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG H .   ? ASN D 530 ? NAG H 1   ? 1_555 ASN A 546 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG I .   ? ASN A 37  ? NAG B 701 ? 1_555 ASN B 53  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG J .   ? ASN A 306 ? NAG B 702 ? 1_555 ASN B 322 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  NAG K .   ? ASN A 416 ? NAG B 703 ? 1_555 ASN B 432 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
8  NAG L .   ? ASN A 530 ? NAG B 704 ? 1_555 ASN B 546 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
9  NAG M .   ? ASN D 37  ? NAG A 701 ? 1_555 ASN A 53  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
10 NAG N .   ? ASN D 87  ? NAG A 702 ? 1_555 ASN A 103 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
11 NAG O .   ? ASN D 306 ? NAG A 703 ? 1_555 ASN A 322 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
12 CYS A 117 ? CYS A 125 ? CYS B 133 ? 1_555 CYS B 141 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
13 CYS A 328 ? CYS A 345 ? CYS B 344 ? 1_555 CYS B 361 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
14 CYS A 514 ? CYS A 526 ? CYS B 530 ? 1_555 CYS B 542 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
15 CYS B 4   ? CYS B 29  ? CYS C 336 ? 1_555 CYS C 361 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
16 CYS B 47  ? CYS B 100 ? CYS C 379 ? 1_555 CYS C 432 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
17 CYS B 59  ? CYS B 193 ? CYS C 391 ? 1_555 CYS C 525 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
18 CYS B 148 ? CYS B 156 ? CYS C 480 ? 1_555 CYS C 488 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
19 CYS C 4   ? CYS C 29  ? CYS D 336 ? 1_555 CYS D 361 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
20 CYS C 47  ? CYS C 100 ? CYS D 379 ? 1_555 CYS D 432 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
21 CYS C 59  ? CYS C 193 ? CYS D 391 ? 1_555 CYS D 525 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
22 CYS C 148 ? CYS C 156 ? CYS D 480 ? 1_555 CYS D 488 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
23 CYS D 117 ? CYS D 125 ? CYS A 133 ? 1_555 CYS A 141 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
24 CYS D 328 ? CYS D 345 ? CYS A 344 ? 1_555 CYS A 361 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
25 CYS D 514 ? CYS D 526 ? CYS A 530 ? 1_555 CYS A 542 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 129 A . ? GLU 145 B PRO 130 A ? PRO 146 B 1 3.67 
2 GLU 129 D . ? GLU 145 A PRO 130 D ? PRO 146 A 1 7.38 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 5 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
AA8 ? 5 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
AB3 ? 2 ? 
AB4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA9 1 2 ? parallel      
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? parallel      
AB4 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 115 ? CYS A 117 ? LYS B 131 CYS B 133 
AA1 2 CYS A 125 ? LEU A 127 ? CYS B 141 LEU B 143 
AA2 1 LEU A 246 ? PRO A 247 ? LEU B 262 PRO B 263 
AA2 2 VAL A 471 ? VAL A 472 ? VAL B 487 VAL B 488 
AA3 1 THR A 331 ? GLY A 336 ? THR B 347 GLY B 352 
AA3 2 ASP A 339 ? LEU A 343 ? ASP B 355 LEU B 359 
AA4 1 ASN B 22  ? ILE B 26  ? ASN C 354 ILE C 358 
AA4 2 ASN B 62  ? ILE B 70  ? ASN C 394 ILE C 402 
AA4 3 TYR B 176 ? GLU B 184 ? TYR C 508 GLU C 516 
AA4 4 GLY B 99  ? ASN B 105 ? GLY C 431 ASN C 437 
AA4 5 THR B 44  ? CYS B 47  ? THR C 376 CYS C 379 
AA5 1 CYS B 29  ? VAL B 30  ? CYS C 361 VAL C 362 
AA5 2 VAL B 192 ? CYS B 193 ? VAL C 524 CYS C 525 
AA6 1 ARG B 120 ? ARG B 122 ? ARG C 452 ARG C 454 
AA6 2 LEU B 160 ? SER B 162 ? LEU C 492 SER C 494 
AA7 1 TYR B 141 ? GLN B 142 ? TYR C 473 GLN C 474 
AA7 2 CYS B 156 ? TYR B 157 ? CYS C 488 TYR C 489 
AA8 1 ASN C 22  ? ILE C 26  ? ASN D 354 ILE D 358 
AA8 2 ASN C 62  ? ARG C 71  ? ASN D 394 ARG D 403 
AA8 3 PRO C 175 ? GLU C 184 ? PRO D 507 GLU D 516 
AA8 4 CYS C 100 ? ASN C 105 ? CYS D 432 ASN D 437 
AA8 5 THR C 44  ? CYS C 47  ? THR D 376 CYS D 379 
AA9 1 CYS C 29  ? VAL C 30  ? CYS D 361 VAL D 362 
AA9 2 VAL C 192 ? CYS C 193 ? VAL D 524 CYS D 525 
AB1 1 ARG C 120 ? ARG C 122 ? ARG D 452 ARG D 454 
AB1 2 LEU C 160 ? SER C 162 ? LEU D 492 SER D 494 
AB2 1 LYS D 115 ? CYS D 117 ? LYS A 131 CYS A 133 
AB2 2 CYS D 125 ? LEU D 127 ? CYS A 141 LEU A 143 
AB3 1 LEU D 246 ? PRO D 247 ? LEU A 262 PRO A 263 
AB3 2 VAL D 471 ? VAL D 472 ? VAL A 487 VAL A 488 
AB4 1 THR D 331 ? GLY D 336 ? THR A 347 GLY A 352 
AB4 2 ASP D 339 ? LEU D 343 ? ASP A 355 LEU A 359 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 116 ? N VAL B 132 O LEU A 126 ? O LEU B 142 
AA2 1 2 N LEU A 246 ? N LEU B 262 O VAL A 472 ? O VAL B 488 
AA3 1 2 N TRP A 333 ? N TRP B 349 O ARG A 341 ? O ARG B 357 
AA4 1 2 N LYS B 24  ? N LYS C 356 O ALA B 65  ? O ALA C 397 
AA4 2 3 N ILE B 70  ? N ILE C 402 O TYR B 176 ? O TYR C 508 
AA4 3 4 O VAL B 179 ? O VAL C 511 N ILE B 102 ? N ILE C 434 
AA4 4 5 O ALA B 103 ? O ALA C 435 N THR B 44  ? N THR C 376 
AA5 1 2 N CYS B 29  ? N CYS C 361 O CYS B 193 ? O CYS C 525 
AA6 1 2 N TYR B 121 ? N TYR C 453 O GLN B 161 ? O GLN C 493 
AA7 1 2 N TYR B 141 ? N TYR C 473 O TYR B 157 ? O TYR C 489 
AA8 1 2 N LYS C 24  ? N LYS D 356 O ALA C 65  ? O ALA D 397 
AA8 2 3 N ILE C 70  ? N ILE D 402 O TYR C 176 ? O TYR D 508 
AA8 3 4 O VAL C 179 ? O VAL D 511 N ILE C 102 ? N ILE D 434 
AA8 4 5 O VAL C 101 ? O VAL D 433 N LYS C 46  ? N LYS D 378 
AA9 1 2 N CYS C 29  ? N CYS D 361 O CYS C 193 ? O CYS D 525 
AB1 1 2 N TYR C 121 ? N TYR D 453 O GLN C 161 ? O GLN D 493 
AB2 1 2 N VAL D 116 ? N VAL A 132 O LEU D 126 ? O LEU A 142 
AB3 1 2 N LEU D 246 ? N LEU A 262 O VAL D 472 ? O VAL A 488 
AB4 1 2 N THR D 331 ? N THR A 347 O LEU D 343 ? O LEU A 359 
# 
_pdbx_entry_details.entry_id                   8XYE 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD1 D ASP 442 ? ? OH  D TYR 451 ? ? 1.93 
2 1 NE2 A HIS 378 ? ? OE2 A GLU 402 ? ? 2.02 
3 1 OG  D SER 359 ? ? OD1 D ASN 394 ? ? 2.07 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CB A TRP 203 ? ? CG A TRP 203 ? ? 1.390 1.498 -0.108 0.018 N 
2 1 CB A GLU 402 ? ? CG A GLU 402 ? ? 1.665 1.517 0.148  0.019 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB  B ASP 382 ? ? CG B ASP 382 ? ? OD2 B ASP 382 ? ? 123.72 118.30 5.42   0.90 N 
2 1 CB  B LEU 584 ? ? CG B LEU 584 ? ? CD2 B LEU 584 ? ? 100.60 111.00 -10.40 1.70 N 
3 1 N   C PRO 373 ? ? CA C PRO 373 ? ? C   C PRO 373 ? ? 96.24  112.10 -15.86 2.60 N 
4 1 CA  D CYS 361 ? ? CB D CYS 361 ? ? SG  D CYS 361 ? ? 124.41 114.20 10.21  1.10 N 
5 1 CA  D LEU 455 ? ? CB D LEU 455 ? ? CG  D LEU 455 ? ? 132.35 115.30 17.05  2.30 N 
6 1 CB  D LEU 492 ? ? CG D LEU 492 ? ? CD2 D LEU 492 ? ? 97.08  111.00 -13.92 1.70 N 
7 1 OE1 A GLU 402 ? ? CD A GLU 402 ? ? OE2 A GLU 402 ? ? 114.44 123.30 -8.86  1.20 N 
8 1 CG  A GLU 402 ? ? CD A GLU 402 ? ? OE2 A GLU 402 ? ? 130.44 118.30 12.14  2.00 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN B 53  ? ? -161.10 80.44   
2  1 ASN B 90  ? ? -161.71 105.18  
3  1 TRP B 275 ? ? -88.84  32.47   
4  1 LEU B 278 ? ? -67.25  0.22    
5  1 ASP B 292 ? ? -160.79 100.06  
6  1 PRO B 336 ? ? -84.77  49.72   
7  1 PRO B 389 ? ? -47.63  160.16  
8  1 GLU B 398 ? ? -49.43  -17.78  
9  1 ASP B 427 ? ? -85.88  34.41   
10 1 GLN B 472 ? ? -142.94 16.63   
11 1 GLU B 495 ? ? -69.74  1.13    
12 1 CYS B 498 ? ? -150.63 71.53   
13 1 ASN C 343 ? ? -98.05  44.82   
14 1 ASN C 360 ? ? 61.83   65.40   
15 1 TYR C 365 ? ? -66.28  1.98    
16 1 THR C 376 ? ? -171.98 109.30  
17 1 PHE C 377 ? ? -117.47 79.62   
18 1 ASP C 389 ? ? -108.42 44.47   
19 1 ASN C 422 ? ? -135.39 -60.83  
20 1 THR C 470 ? ? -102.43 50.31   
21 1 LEU C 518 ? ? -143.68 -159.69 
22 1 ALA D 352 ? ? -116.80 50.71   
23 1 ASN D 394 ? ? -160.53 107.75  
24 1 ASN D 422 ? ? -130.77 -55.67  
25 1 ASP D 428 ? ? -94.00  36.14   
26 1 THR D 430 ? ? -140.44 18.65   
27 1 GLN D 474 ? ? -100.98 64.74   
28 1 THR D 523 ? ? -145.85 34.28   
29 1 ASN A 53  ? ? -154.69 68.90   
30 1 ASN A 137 ? ? -168.82 87.41   
31 1 PRO A 138 ? ? -64.32  4.26    
32 1 TYR A 215 ? ? -144.27 10.12   
33 1 TYR A 217 ? ? -166.56 107.32  
34 1 TYR A 255 ? ? -140.22 -19.47  
35 1 TRP A 275 ? ? -99.39  36.28   
36 1 ALA A 301 ? ? 60.69   60.25   
37 1 PRO A 336 ? ? -81.71  45.13   
38 1 ASN A 394 ? ? -172.44 -167.67 
39 1 CYS A 498 ? ? -146.59 58.45   
40 1 ASP A 509 ? ? 63.47   69.21   
41 1 ASN A 546 ? ? 74.91   -20.80  
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    TYR 
_pdbx_validate_planes.auth_asym_id    C 
_pdbx_validate_planes.auth_seq_id     495 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.056 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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 2.2084   51.6989 95.0824  0.6301 ? 0.0277  ? -0.0036 ? 0.4351 ? 0.0271  ? 0.4715 ? 1.2137 ? 
0.3814  ? 0.6227  ? 1.6916  ? -0.7820 ? 2.3137  ? -0.2193 ? 0.3252  ? 0.2483  ? -0.6441 ? -0.1079 ? -0.1369 ? -0.4780 ? 0.1640  ? 
-1.0592 ? 
2  'X-RAY DIFFRACTION' ? refined 29.5372  31.2996 92.4073  0.9678 ? 0.4014  ? 0.0625  ? 1.0899 ? -0.0909 ? 0.4773 ? 0.8823 ? 
0.4692  ? 0.0044  ? 0.3784  ? 0.3047  ? 0.0814  ? -0.1352 ? 0.4236  ? -0.2250 ? -0.4466 ? 0.3970  ? 0.0292  ? 0.0179  ? 0.7560  ? 
0.0616  ? 
3  'X-RAY DIFFRACTION' ? refined 22.2501  35.4392 111.3445 0.5341 ? 0.1265  ? 0.0868  ? 0.5468 ? 0.0418  ? 0.4157 ? 0.8791 ? 
-0.1824 ? 0.6820  ? 0.6812  ? -0.7045 ? 0.6968  ? 0.0939  ? -0.1449 ? -0.1374 ? -0.1264 ? -0.1073 ? 0.1558  ? 0.1631  ? 0.4577  ? 
-0.0001 ? 
4  'X-RAY DIFFRACTION' ? refined 10.1556  15.7162 102.4033 0.7642 ? 0.1038  ? -0.0115 ? 0.4377 ? 0.0220  ? 0.6624 ? 0.3763 ? 
0.7178  ? -0.1115 ? 0.5387  ? 0.0031  ? 0.5563  ? -0.2063 ? 0.0928  ? -0.2155 ? -0.3755 ? 0.0633  ? 0.0966  ? 0.3742  ? 0.1412  ? 
0.0001  ? 
5  'X-RAY DIFFRACTION' ? refined 1.4046   24.3551 98.6311  0.8173 ? 0.0308  ? -0.0071 ? 0.5203 ? 0.0500  ? 0.7383 ? 0.4865 ? 
0.1115  ? -0.1098 ? 0.1793  ? -0.3578 ? 0.6119  ? 0.1280  ? -0.0535 ? -0.3700 ? -0.4557 ? -0.2470 ? -0.1198 ? 0.3476  ? -0.0503 ? 
-0.0002 ? 
6  'X-RAY DIFFRACTION' ? refined 13.9406  29.7979 112.7179 0.4314 ? 0.0400  ? 0.0266  ? 0.4303 ? 0.1210  ? 0.4201 ? 0.6892 ? 
-0.5091 ? 0.5944  ? 0.6421  ? 0.1946  ? 0.6607  ? 0.2835  ? -0.0157 ? -0.2464 ? -0.0573 ? -0.2865 ? 0.2094  ? 0.2125  ? 0.2282  ? 
-0.0534 ? 
7  'X-RAY DIFFRACTION' ? refined 22.3124  16.8405 122.2838 0.5966 ? 0.1139  ? -0.0648 ? 0.6791 ? 0.2828  ? 0.9093 ? 0.1230 ? 
0.2299  ? 0.1060  ? 0.5164  ? 0.0168  ? 0.1479  ? 0.5394  ? -0.8235 ? -0.1470 ? -0.4990 ? -0.4046 ? 0.7439  ? 0.5663  ? 0.2884  ? 
0.0086  ? 
8  'X-RAY DIFFRACTION' ? refined -58.2832 43.7390 36.1264  0.5883 ? -0.0522 ? 0.0182  ? 0.4456 ? -0.0036 ? 0.4296 ? 1.3439 ? 
2.2218  ? -1.2145 ? 3.7713  ? -2.7717 ? 2.7372  ? -0.3673 ? -0.1573 ? -0.7122 ? -0.4653 ? -0.3674 ? -0.6078 ? 0.9476  ? 0.4116  ? 
-0.8694 ? 
9  'X-RAY DIFFRACTION' ? refined -61.5429 45.9120 48.4731  0.9004 ? -0.2300 ? 0.2194  ? 0.9659 ? 0.2849  ? 0.9265 ? 0.0795 ? 
-0.0060 ? -0.0697 ? -0.0004 ? 0.1133  ? 0.1170  ? -0.1637 ? -0.9036 ? -0.0201 ? 0.3544  ? -0.2170 ? 0.6051  ? 0.2290  ? -0.4523 ? 
-0.0000 ? 
10 'X-RAY DIFFRACTION' ? refined -66.7668 50.2298 42.8832  0.5426 ? -0.2082 ? 0.1111  ? 0.5429 ? -0.0691 ? 0.5787 ? 0.1240 ? 
-0.2104 ? 0.1857  ? 0.2629  ? -0.2590 ? 0.7877  ? 0.5365  ? -0.9257 ? 0.2574  ? 0.2178  ? -0.1878 ? 0.1511  ? 0.0374  ? 0.5335  ? 
-0.0840 ? 
11 'X-RAY DIFFRACTION' ? refined -51.8838 57.7208 35.0856  0.5098 ? 0.0296  ? -0.0378 ? 0.5730 ? -0.0135 ? 0.4391 ? 0.7326 ? 
0.6575  ? -0.2103 ? 0.5137  ? 0.1778  ? 0.3669  ? 0.0012  ? 0.3853  ? 0.1558  ? -0.1175 ? -0.2388 ? 0.2485  ? -0.2225 ? -0.0509 ? 
-0.0007 ? 
12 'X-RAY DIFFRACTION' ? refined -42.7478 66.8535 15.6105  0.7095 ? -0.1976 ? -0.1028 ? 0.6596 ? 0.2228  ? 0.5527 ? 0.0233 ? 
0.0694  ? -0.0221 ? 0.0853  ? 0.0059  ? -0.0151 ? 0.1914  ? 0.4149  ? 0.1527  ? 0.0526  ? -0.3034 ? 0.5811  ? -0.3080 ? 0.5931  ? 
-0.0011 ? 
13 'X-RAY DIFFRACTION' ? refined -53.8382 52.3374 38.1086  0.4401 ? -0.1065 ? 0.0313  ? 0.4339 ? -0.1279 ? 0.4238 ? 0.2841 ? 
-0.1886 ? 0.1900  ? 0.4141  ? -0.1851 ? 0.6089  ? -0.1989 ? 0.3303  ? 0.1293  ? 0.2083  ? -0.1801 ? 0.0405  ? 0.3356  ? 0.0573  ? 
-0.0907 ? 
14 'X-RAY DIFFRACTION' ? refined -34.1376 43.3428 79.3905  0.6777 ? -0.3129 ? -0.3565 ? 0.5458 ? 0.2317  ? 0.6438 ? 0.4609 ? 
-0.2563 ? 0.1701  ? 1.9319  ? 0.3531  ? 1.2053  ? 0.5206  ? -0.4078 ? -0.7204 ? -0.0258 ? -0.3950 ? -0.5246 ? -0.3189 ? -0.3137 ? 
0.5973  ? 
15 'X-RAY DIFFRACTION' ? refined -24.0129 51.5769 87.7204  0.5748 ? -0.0495 ? -0.0072 ? 0.7711 ? 0.0297  ? 0.6104 ? 0.2540 ? 
0.3962  ? 0.0437  ? 0.3827  ? -0.3874 ? 0.4859  ? -0.1465 ? -0.0506 ? 0.0989  ? -0.0288 ? 0.1066  ? 0.1106  ? 0.1790  ? -0.4793 ? 
-0.0001 ? 
16 'X-RAY DIFFRACTION' ? refined -23.7877 68.3927 30.6152  0.5499 ? -0.0722 ? -0.0282 ? 0.4980 ? 0.0806  ? 0.4003 ? 1.3262 ? 
0.1985  ? 0.4328  ? 0.5501  ? 0.6559  ? 0.7469  ? -0.1878 ? 0.2001  ? -0.0150 ? -0.3464 ? 0.3213  ? 0.1429  ? 0.0106  ? 0.1753  ? 
0.1661  ? 
17 'X-RAY DIFFRACTION' ? refined -4.3169  81.3908 47.1442  0.5658 ? -0.0715 ? 0.0293  ? 0.4879 ? -0.0810 ? 0.5005 ? 2.2590 ? 
0.1831  ? -0.6423 ? 0.8546  ? 0.1529  ? 0.9860  ? -0.2782 ? 0.3905  ? 0.2582  ? -0.2553 ? 0.1576  ? -0.0076 ? -0.1646 ? 0.2913  ? 
-0.0246 ? 
18 'X-RAY DIFFRACTION' ? refined -17.3277 66.6816 60.7424  0.3401 ? 0.0309  ? 0.0436  ? 0.3991 ? -0.0828 ? 0.4484 ? 0.0734 ? 
0.4410  ? 0.4125  ? 0.4085  ? -0.0201 ? 0.7137  ? 0.0723  ? -0.2717 ? -0.0514 ? 0.0761  ? 0.0851  ? 0.0234  ? 0.0924  ? -0.0234 ? 
0.0010  ? 
19 'X-RAY DIFFRACTION' ? refined -26.0105 73.3132 61.1501  0.3905 ? 0.0410  ? 0.0731  ? 0.4567 ? -0.0103 ? 0.3911 ? 0.1635 ? 
-0.2526 ? -0.0454 ? 0.5693  ? 0.0225  ? 0.0246  ? -0.1745 ? 0.0250  ? -0.0321 ? 0.0292  ? 0.2579  ? 0.2908  ? -0.5580 ? -0.0634 ? 
-0.0033 ? 
20 'X-RAY DIFFRACTION' ? refined -2.9718  84.8245 49.1299  0.5893 ? -0.1878 ? 0.0484  ? 0.4831 ? -0.0395 ? 0.4717 ? 0.6379 ? 
-0.2639 ? 0.0654  ? -0.0220 ? -0.1220 ? 0.2079  ? -0.1260 ? 0.1435  ? 0.2383  ? -0.2196 ? 0.0317  ? 0.0924  ? -0.2389 ? 0.0240  ? 
-0.0003 ? 
21 'X-RAY DIFFRACTION' ? refined -21.0563 85.9910 60.0885  0.4931 ? -0.0107 ? -0.0210 ? 0.3662 ? -0.0829 ? 0.5744 ? 0.1324 ? 
0.0996  ? 0.2937  ? 0.2081  ? 0.2449  ? 1.2155  ? -0.2450 ? -0.2493 ? 0.3219  ? -0.1737 ? 0.1301  ? 0.1429  ? -0.5781 ? -0.1199 ? 
-0.0061 ? 
# 
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 'B' and (resid 17 through 109 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 110 through 157 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 158 through 251 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 252 through 330 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 331 through 431 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 432 through 581 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 582 through 614 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 333 through 358 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 359 through 379 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 380 through 402 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 403 through 469 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 470 through 489 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 490 through 526 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 333 through 385 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 386 through 526 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 18 through 129 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 130 through 251 )
;
18 'X-RAY DIFFRACTION' 18 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 252 through 384 )
;
19 'X-RAY DIFFRACTION' 19 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 385 through 431 )
;
20 'X-RAY DIFFRACTION' 20 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 432 through 512 )
;
21 'X-RAY DIFFRACTION' 21 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 513 through 614 )
;
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     ASP 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      17 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    D 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    ASP 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     1 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
BMA C1   C N R 74  
BMA C2   C N S 75  
BMA C3   C N S 76  
BMA C4   C N S 77  
BMA C5   C N R 78  
BMA C6   C N N 79  
BMA O1   O N N 80  
BMA O2   O N N 81  
BMA O3   O N N 82  
BMA O4   O N N 83  
BMA O5   O N N 84  
BMA O6   O N N 85  
BMA H1   H N N 86  
BMA H2   H N N 87  
BMA H3   H N N 88  
BMA H4   H N N 89  
BMA H5   H N N 90  
BMA H61  H N N 91  
BMA H62  H N N 92  
BMA HO1  H N N 93  
BMA HO2  H N N 94  
BMA HO3  H N N 95  
BMA HO4  H N N 96  
BMA HO6  H N N 97  
CYS N    N N N 98  
CYS CA   C N R 99  
CYS C    C N N 100 
CYS O    O N N 101 
CYS CB   C N N 102 
CYS SG   S N N 103 
CYS OXT  O N N 104 
CYS H    H N N 105 
CYS H2   H N N 106 
CYS HA   H N N 107 
CYS HB2  H N N 108 
CYS HB3  H N N 109 
CYS HG   H N N 110 
CYS HXT  H N N 111 
GLN N    N N N 112 
GLN CA   C N S 113 
GLN C    C N N 114 
GLN O    O N N 115 
GLN CB   C N N 116 
GLN CG   C N N 117 
GLN CD   C N N 118 
GLN OE1  O N N 119 
GLN NE2  N N N 120 
GLN OXT  O N N 121 
GLN H    H N N 122 
GLN H2   H N N 123 
GLN HA   H N N 124 
GLN HB2  H N N 125 
GLN HB3  H N N 126 
GLN HG2  H N N 127 
GLN HG3  H N N 128 
GLN HE21 H N N 129 
GLN HE22 H N N 130 
GLN HXT  H N N 131 
GLU N    N N N 132 
GLU CA   C N S 133 
GLU C    C N N 134 
GLU O    O N N 135 
GLU CB   C N N 136 
GLU CG   C N N 137 
GLU CD   C N N 138 
GLU OE1  O N N 139 
GLU OE2  O N N 140 
GLU OXT  O N N 141 
GLU H    H N N 142 
GLU H2   H N N 143 
GLU HA   H N N 144 
GLU HB2  H N N 145 
GLU HB3  H N N 146 
GLU HG2  H N N 147 
GLU HG3  H N N 148 
GLU HE2  H N N 149 
GLU HXT  H N N 150 
GLY N    N N N 151 
GLY CA   C N N 152 
GLY C    C N N 153 
GLY O    O N N 154 
GLY OXT  O N N 155 
GLY H    H N N 156 
GLY H2   H N N 157 
GLY HA2  H N N 158 
GLY HA3  H N N 159 
GLY HXT  H N N 160 
HIS N    N N N 161 
HIS CA   C N S 162 
HIS C    C N N 163 
HIS O    O N N 164 
HIS CB   C N N 165 
HIS CG   C Y N 166 
HIS ND1  N Y N 167 
HIS CD2  C Y N 168 
HIS CE1  C Y N 169 
HIS NE2  N Y N 170 
HIS OXT  O N N 171 
HIS H    H N N 172 
HIS H2   H N N 173 
HIS HA   H N N 174 
HIS HB2  H N N 175 
HIS HB3  H N N 176 
HIS HD1  H N N 177 
HIS HD2  H N N 178 
HIS HE1  H N N 179 
HIS HE2  H N N 180 
HIS HXT  H N N 181 
ILE N    N N N 182 
ILE CA   C N S 183 
ILE C    C N N 184 
ILE O    O N N 185 
ILE CB   C N S 186 
ILE CG1  C N N 187 
ILE CG2  C N N 188 
ILE CD1  C N N 189 
ILE OXT  O N N 190 
ILE H    H N N 191 
ILE H2   H N N 192 
ILE HA   H N N 193 
ILE HB   H N N 194 
ILE HG12 H N N 195 
ILE HG13 H N N 196 
ILE HG21 H N N 197 
ILE HG22 H N N 198 
ILE HG23 H N N 199 
ILE HD11 H N N 200 
ILE HD12 H N N 201 
ILE HD13 H N N 202 
ILE HXT  H N N 203 
LEU N    N N N 204 
LEU CA   C N S 205 
LEU C    C N N 206 
LEU O    O N N 207 
LEU CB   C N N 208 
LEU CG   C N N 209 
LEU CD1  C N N 210 
LEU CD2  C N N 211 
LEU OXT  O N N 212 
LEU H    H N N 213 
LEU H2   H N N 214 
LEU HA   H N N 215 
LEU HB2  H N N 216 
LEU HB3  H N N 217 
LEU HG   H N N 218 
LEU HD11 H N N 219 
LEU HD12 H N N 220 
LEU HD13 H N N 221 
LEU HD21 H N N 222 
LEU HD22 H N N 223 
LEU HD23 H N N 224 
LEU HXT  H N N 225 
LYS N    N N N 226 
LYS CA   C N S 227 
LYS C    C N N 228 
LYS O    O N N 229 
LYS CB   C N N 230 
LYS CG   C N N 231 
LYS CD   C N N 232 
LYS CE   C N N 233 
LYS NZ   N N N 234 
LYS OXT  O N N 235 
LYS H    H N N 236 
LYS H2   H N N 237 
LYS HA   H N N 238 
LYS HB2  H N N 239 
LYS HB3  H N N 240 
LYS HG2  H N N 241 
LYS HG3  H N N 242 
LYS HD2  H N N 243 
LYS HD3  H N N 244 
LYS HE2  H N N 245 
LYS HE3  H N N 246 
LYS HZ1  H N N 247 
LYS HZ2  H N N 248 
LYS HZ3  H N N 249 
LYS HXT  H N N 250 
MET N    N N N 251 
MET CA   C N S 252 
MET C    C N N 253 
MET O    O N N 254 
MET CB   C N N 255 
MET CG   C N N 256 
MET SD   S N N 257 
MET CE   C N N 258 
MET OXT  O N N 259 
MET H    H N N 260 
MET H2   H N N 261 
MET HA   H N N 262 
MET HB2  H N N 263 
MET HB3  H N N 264 
MET HG2  H N N 265 
MET HG3  H N N 266 
MET HE1  H N N 267 
MET HE2  H N N 268 
MET HE3  H N N 269 
MET HXT  H N N 270 
NAG C1   C N R 271 
NAG C2   C N R 272 
NAG C3   C N R 273 
NAG C4   C N S 274 
NAG C5   C N R 275 
NAG C6   C N N 276 
NAG C7   C N N 277 
NAG C8   C N N 278 
NAG N2   N N N 279 
NAG O1   O N N 280 
NAG O3   O N N 281 
NAG O4   O N N 282 
NAG O5   O N N 283 
NAG O6   O N N 284 
NAG O7   O N N 285 
NAG H1   H N N 286 
NAG H2   H N N 287 
NAG H3   H N N 288 
NAG H4   H N N 289 
NAG H5   H N N 290 
NAG H61  H N N 291 
NAG H62  H N N 292 
NAG H81  H N N 293 
NAG H82  H N N 294 
NAG H83  H N N 295 
NAG HN2  H N N 296 
NAG HO1  H N N 297 
NAG HO3  H N N 298 
NAG HO4  H N N 299 
NAG HO6  H N N 300 
PHE N    N N N 301 
PHE CA   C N S 302 
PHE C    C N N 303 
PHE O    O N N 304 
PHE CB   C N N 305 
PHE CG   C Y N 306 
PHE CD1  C Y N 307 
PHE CD2  C Y N 308 
PHE CE1  C Y N 309 
PHE CE2  C Y N 310 
PHE CZ   C Y N 311 
PHE OXT  O N N 312 
PHE H    H N N 313 
PHE H2   H N N 314 
PHE HA   H N N 315 
PHE HB2  H N N 316 
PHE HB3  H N N 317 
PHE HD1  H N N 318 
PHE HD2  H N N 319 
PHE HE1  H N N 320 
PHE HE2  H N N 321 
PHE HZ   H N N 322 
PHE HXT  H N N 323 
PRO N    N N N 324 
PRO CA   C N S 325 
PRO C    C N N 326 
PRO O    O N N 327 
PRO CB   C N N 328 
PRO CG   C N N 329 
PRO CD   C N N 330 
PRO OXT  O N N 331 
PRO H    H N N 332 
PRO HA   H N N 333 
PRO HB2  H N N 334 
PRO HB3  H N N 335 
PRO HG2  H N N 336 
PRO HG3  H N N 337 
PRO HD2  H N N 338 
PRO HD3  H N N 339 
PRO HXT  H N N 340 
SER N    N N N 341 
SER CA   C N S 342 
SER C    C N N 343 
SER O    O N N 344 
SER CB   C N N 345 
SER OG   O N N 346 
SER OXT  O N N 347 
SER H    H N N 348 
SER H2   H N N 349 
SER HA   H N N 350 
SER HB2  H N N 351 
SER HB3  H N N 352 
SER HG   H N N 353 
SER HXT  H N N 354 
THR N    N N N 355 
THR CA   C N S 356 
THR C    C N N 357 
THR O    O N N 358 
THR CB   C N R 359 
THR OG1  O N N 360 
THR CG2  C N N 361 
THR OXT  O N N 362 
THR H    H N N 363 
THR H2   H N N 364 
THR HA   H N N 365 
THR HB   H N N 366 
THR HG1  H N N 367 
THR HG21 H N N 368 
THR HG22 H N N 369 
THR HG23 H N N 370 
THR HXT  H N N 371 
TRP N    N N N 372 
TRP CA   C N S 373 
TRP C    C N N 374 
TRP O    O N N 375 
TRP CB   C N N 376 
TRP CG   C Y N 377 
TRP CD1  C Y N 378 
TRP CD2  C Y N 379 
TRP NE1  N Y N 380 
TRP CE2  C Y N 381 
TRP CE3  C Y N 382 
TRP CZ2  C Y N 383 
TRP CZ3  C Y N 384 
TRP CH2  C Y N 385 
TRP OXT  O N N 386 
TRP H    H N N 387 
TRP H2   H N N 388 
TRP HA   H N N 389 
TRP HB2  H N N 390 
TRP HB3  H N N 391 
TRP HD1  H N N 392 
TRP HE1  H N N 393 
TRP HE3  H N N 394 
TRP HZ2  H N N 395 
TRP HZ3  H N N 396 
TRP HH2  H N N 397 
TRP HXT  H N N 398 
TYR N    N N N 399 
TYR CA   C N S 400 
TYR C    C N N 401 
TYR O    O N N 402 
TYR CB   C N N 403 
TYR CG   C Y N 404 
TYR CD1  C Y N 405 
TYR CD2  C Y N 406 
TYR CE1  C Y N 407 
TYR CE2  C Y N 408 
TYR CZ   C Y N 409 
TYR OH   O N N 410 
TYR OXT  O N N 411 
TYR H    H N N 412 
TYR H2   H N N 413 
TYR HA   H N N 414 
TYR HB2  H N N 415 
TYR HB3  H N N 416 
TYR HD1  H N N 417 
TYR HD2  H N N 418 
TYR HE1  H N N 419 
TYR HE2  H N N 420 
TYR HH   H N N 421 
TYR HXT  H N N 422 
VAL N    N N N 423 
VAL CA   C N S 424 
VAL C    C N N 425 
VAL O    O N N 426 
VAL CB   C N N 427 
VAL CG1  C N N 428 
VAL CG2  C N N 429 
VAL OXT  O N N 430 
VAL H    H N N 431 
VAL H2   H N N 432 
VAL HA   H N N 433 
VAL HB   H N N 434 
VAL HG11 H N N 435 
VAL HG12 H N N 436 
VAL HG13 H N N 437 
VAL HG21 H N N 438 
VAL HG22 H N N 439 
VAL HG23 H N N 440 
VAL HXT  H N N 441 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BMA C1  C2   sing N N 70  
BMA C1  O1   sing N N 71  
BMA C1  O5   sing N N 72  
BMA C1  H1   sing N N 73  
BMA C2  C3   sing N N 74  
BMA C2  O2   sing N N 75  
BMA C2  H2   sing N N 76  
BMA C3  C4   sing N N 77  
BMA C3  O3   sing N N 78  
BMA C3  H3   sing N N 79  
BMA C4  C5   sing N N 80  
BMA C4  O4   sing N N 81  
BMA C4  H4   sing N N 82  
BMA C5  C6   sing N N 83  
BMA C5  O5   sing N N 84  
BMA C5  H5   sing N N 85  
BMA C6  O6   sing N N 86  
BMA C6  H61  sing N N 87  
BMA C6  H62  sing N N 88  
BMA O1  HO1  sing N N 89  
BMA O2  HO2  sing N N 90  
BMA O3  HO3  sing N N 91  
BMA O4  HO4  sing N N 92  
BMA O6  HO6  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
GLN N   CA   sing N N 107 
GLN N   H    sing N N 108 
GLN N   H2   sing N N 109 
GLN CA  C    sing N N 110 
GLN CA  CB   sing N N 111 
GLN CA  HA   sing N N 112 
GLN C   O    doub N N 113 
GLN C   OXT  sing N N 114 
GLN CB  CG   sing N N 115 
GLN CB  HB2  sing N N 116 
GLN CB  HB3  sing N N 117 
GLN CG  CD   sing N N 118 
GLN CG  HG2  sing N N 119 
GLN CG  HG3  sing N N 120 
GLN CD  OE1  doub N N 121 
GLN CD  NE2  sing N N 122 
GLN NE2 HE21 sing N N 123 
GLN NE2 HE22 sing N N 124 
GLN OXT HXT  sing N N 125 
GLU N   CA   sing N N 126 
GLU N   H    sing N N 127 
GLU N   H2   sing N N 128 
GLU CA  C    sing N N 129 
GLU CA  CB   sing N N 130 
GLU CA  HA   sing N N 131 
GLU C   O    doub N N 132 
GLU C   OXT  sing N N 133 
GLU CB  CG   sing N N 134 
GLU CB  HB2  sing N N 135 
GLU CB  HB3  sing N N 136 
GLU CG  CD   sing N N 137 
GLU CG  HG2  sing N N 138 
GLU CG  HG3  sing N N 139 
GLU CD  OE1  doub N N 140 
GLU CD  OE2  sing N N 141 
GLU OE2 HE2  sing N N 142 
GLU OXT HXT  sing N N 143 
GLY N   CA   sing N N 144 
GLY N   H    sing N N 145 
GLY N   H2   sing N N 146 
GLY CA  C    sing N N 147 
GLY CA  HA2  sing N N 148 
GLY CA  HA3  sing N N 149 
GLY C   O    doub N N 150 
GLY C   OXT  sing N N 151 
GLY OXT HXT  sing N N 152 
HIS N   CA   sing N N 153 
HIS N   H    sing N N 154 
HIS N   H2   sing N N 155 
HIS CA  C    sing N N 156 
HIS CA  CB   sing N N 157 
HIS CA  HA   sing N N 158 
HIS C   O    doub N N 159 
HIS C   OXT  sing N N 160 
HIS CB  CG   sing N N 161 
HIS CB  HB2  sing N N 162 
HIS CB  HB3  sing N N 163 
HIS CG  ND1  sing Y N 164 
HIS CG  CD2  doub Y N 165 
HIS ND1 CE1  doub Y N 166 
HIS ND1 HD1  sing N N 167 
HIS CD2 NE2  sing Y N 168 
HIS CD2 HD2  sing N N 169 
HIS CE1 NE2  sing Y N 170 
HIS CE1 HE1  sing N N 171 
HIS NE2 HE2  sing N N 172 
HIS OXT HXT  sing N N 173 
ILE N   CA   sing N N 174 
ILE N   H    sing N N 175 
ILE N   H2   sing N N 176 
ILE CA  C    sing N N 177 
ILE CA  CB   sing N N 178 
ILE CA  HA   sing N N 179 
ILE C   O    doub N N 180 
ILE C   OXT  sing N N 181 
ILE CB  CG1  sing N N 182 
ILE CB  CG2  sing N N 183 
ILE CB  HB   sing N N 184 
ILE CG1 CD1  sing N N 185 
ILE CG1 HG12 sing N N 186 
ILE CG1 HG13 sing N N 187 
ILE CG2 HG21 sing N N 188 
ILE CG2 HG22 sing N N 189 
ILE CG2 HG23 sing N N 190 
ILE CD1 HD11 sing N N 191 
ILE CD1 HD12 sing N N 192 
ILE CD1 HD13 sing N N 193 
ILE OXT HXT  sing N N 194 
LEU N   CA   sing N N 195 
LEU N   H    sing N N 196 
LEU N   H2   sing N N 197 
LEU CA  C    sing N N 198 
LEU CA  CB   sing N N 199 
LEU CA  HA   sing N N 200 
LEU C   O    doub N N 201 
LEU C   OXT  sing N N 202 
LEU CB  CG   sing N N 203 
LEU CB  HB2  sing N N 204 
LEU CB  HB3  sing N N 205 
LEU CG  CD1  sing N N 206 
LEU CG  CD2  sing N N 207 
LEU CG  HG   sing N N 208 
LEU CD1 HD11 sing N N 209 
LEU CD1 HD12 sing N N 210 
LEU CD1 HD13 sing N N 211 
LEU CD2 HD21 sing N N 212 
LEU CD2 HD22 sing N N 213 
LEU CD2 HD23 sing N N 214 
LEU OXT HXT  sing N N 215 
LYS N   CA   sing N N 216 
LYS N   H    sing N N 217 
LYS N   H2   sing N N 218 
LYS CA  C    sing N N 219 
LYS CA  CB   sing N N 220 
LYS CA  HA   sing N N 221 
LYS C   O    doub N N 222 
LYS C   OXT  sing N N 223 
LYS CB  CG   sing N N 224 
LYS CB  HB2  sing N N 225 
LYS CB  HB3  sing N N 226 
LYS CG  CD   sing N N 227 
LYS CG  HG2  sing N N 228 
LYS CG  HG3  sing N N 229 
LYS CD  CE   sing N N 230 
LYS CD  HD2  sing N N 231 
LYS CD  HD3  sing N N 232 
LYS CE  NZ   sing N N 233 
LYS CE  HE2  sing N N 234 
LYS CE  HE3  sing N N 235 
LYS NZ  HZ1  sing N N 236 
LYS NZ  HZ2  sing N N 237 
LYS NZ  HZ3  sing N N 238 
LYS OXT HXT  sing N N 239 
MET N   CA   sing N N 240 
MET N   H    sing N N 241 
MET N   H2   sing N N 242 
MET CA  C    sing N N 243 
MET CA  CB   sing N N 244 
MET CA  HA   sing N N 245 
MET C   O    doub N N 246 
MET C   OXT  sing N N 247 
MET CB  CG   sing N N 248 
MET CB  HB2  sing N N 249 
MET CB  HB3  sing N N 250 
MET CG  SD   sing N N 251 
MET CG  HG2  sing N N 252 
MET CG  HG3  sing N N 253 
MET SD  CE   sing N N 254 
MET CE  HE1  sing N N 255 
MET CE  HE2  sing N N 256 
MET CE  HE3  sing N N 257 
MET OXT HXT  sing N N 258 
NAG C1  C2   sing N N 259 
NAG C1  O1   sing N N 260 
NAG C1  O5   sing N N 261 
NAG C1  H1   sing N N 262 
NAG C2  C3   sing N N 263 
NAG C2  N2   sing N N 264 
NAG C2  H2   sing N N 265 
NAG C3  C4   sing N N 266 
NAG C3  O3   sing N N 267 
NAG C3  H3   sing N N 268 
NAG C4  C5   sing N N 269 
NAG C4  O4   sing N N 270 
NAG C4  H4   sing N N 271 
NAG C5  C6   sing N N 272 
NAG C5  O5   sing N N 273 
NAG C5  H5   sing N N 274 
NAG C6  O6   sing N N 275 
NAG C6  H61  sing N N 276 
NAG C6  H62  sing N N 277 
NAG C7  C8   sing N N 278 
NAG C7  N2   sing N N 279 
NAG C7  O7   doub N N 280 
NAG C8  H81  sing N N 281 
NAG C8  H82  sing N N 282 
NAG C8  H83  sing N N 283 
NAG N2  HN2  sing N N 284 
NAG O1  HO1  sing N N 285 
NAG O3  HO3  sing N N 286 
NAG O4  HO4  sing N N 287 
NAG O6  HO6  sing N N 288 
PHE N   CA   sing N N 289 
PHE N   H    sing N N 290 
PHE N   H2   sing N N 291 
PHE CA  C    sing N N 292 
PHE CA  CB   sing N N 293 
PHE CA  HA   sing N N 294 
PHE C   O    doub N N 295 
PHE C   OXT  sing N N 296 
PHE CB  CG   sing N N 297 
PHE CB  HB2  sing N N 298 
PHE CB  HB3  sing N N 299 
PHE CG  CD1  doub Y N 300 
PHE CG  CD2  sing Y N 301 
PHE CD1 CE1  sing Y N 302 
PHE CD1 HD1  sing N N 303 
PHE CD2 CE2  doub Y N 304 
PHE CD2 HD2  sing N N 305 
PHE CE1 CZ   doub Y N 306 
PHE CE1 HE1  sing N N 307 
PHE CE2 CZ   sing Y N 308 
PHE CE2 HE2  sing N N 309 
PHE CZ  HZ   sing N N 310 
PHE OXT HXT  sing N N 311 
PRO N   CA   sing N N 312 
PRO N   CD   sing N N 313 
PRO N   H    sing N N 314 
PRO CA  C    sing N N 315 
PRO CA  CB   sing N N 316 
PRO CA  HA   sing N N 317 
PRO C   O    doub N N 318 
PRO C   OXT  sing N N 319 
PRO CB  CG   sing N N 320 
PRO CB  HB2  sing N N 321 
PRO CB  HB3  sing N N 322 
PRO CG  CD   sing N N 323 
PRO CG  HG2  sing N N 324 
PRO CG  HG3  sing N N 325 
PRO CD  HD2  sing N N 326 
PRO CD  HD3  sing N N 327 
PRO OXT HXT  sing N N 328 
SER N   CA   sing N N 329 
SER N   H    sing N N 330 
SER N   H2   sing N N 331 
SER CA  C    sing N N 332 
SER CA  CB   sing N N 333 
SER CA  HA   sing N N 334 
SER C   O    doub N N 335 
SER C   OXT  sing N N 336 
SER CB  OG   sing N N 337 
SER CB  HB2  sing N N 338 
SER CB  HB3  sing N N 339 
SER OG  HG   sing N N 340 
SER OXT HXT  sing N N 341 
THR N   CA   sing N N 342 
THR N   H    sing N N 343 
THR N   H2   sing N N 344 
THR CA  C    sing N N 345 
THR CA  CB   sing N N 346 
THR CA  HA   sing N N 347 
THR C   O    doub N N 348 
THR C   OXT  sing N N 349 
THR CB  OG1  sing N N 350 
THR CB  CG2  sing N N 351 
THR CB  HB   sing N N 352 
THR OG1 HG1  sing N N 353 
THR CG2 HG21 sing N N 354 
THR CG2 HG22 sing N N 355 
THR CG2 HG23 sing N N 356 
THR OXT HXT  sing N N 357 
TRP N   CA   sing N N 358 
TRP N   H    sing N N 359 
TRP N   H2   sing N N 360 
TRP CA  C    sing N N 361 
TRP CA  CB   sing N N 362 
TRP CA  HA   sing N N 363 
TRP C   O    doub N N 364 
TRP C   OXT  sing N N 365 
TRP CB  CG   sing N N 366 
TRP CB  HB2  sing N N 367 
TRP CB  HB3  sing N N 368 
TRP CG  CD1  doub Y N 369 
TRP CG  CD2  sing Y N 370 
TRP CD1 NE1  sing Y N 371 
TRP CD1 HD1  sing N N 372 
TRP CD2 CE2  doub Y N 373 
TRP CD2 CE3  sing Y N 374 
TRP NE1 CE2  sing Y N 375 
TRP NE1 HE1  sing N N 376 
TRP CE2 CZ2  sing Y N 377 
TRP CE3 CZ3  doub Y N 378 
TRP CE3 HE3  sing N N 379 
TRP CZ2 CH2  doub Y N 380 
TRP CZ2 HZ2  sing N N 381 
TRP CZ3 CH2  sing Y N 382 
TRP CZ3 HZ3  sing N N 383 
TRP CH2 HH2  sing N N 384 
TRP OXT HXT  sing N N 385 
TYR N   CA   sing N N 386 
TYR N   H    sing N N 387 
TYR N   H2   sing N N 388 
TYR CA  C    sing N N 389 
TYR CA  CB   sing N N 390 
TYR CA  HA   sing N N 391 
TYR C   O    doub N N 392 
TYR C   OXT  sing N N 393 
TYR CB  CG   sing N N 394 
TYR CB  HB2  sing N N 395 
TYR CB  HB3  sing N N 396 
TYR CG  CD1  doub Y N 397 
TYR CG  CD2  sing Y N 398 
TYR CD1 CE1  sing Y N 399 
TYR CD1 HD1  sing N N 400 
TYR CD2 CE2  doub Y N 401 
TYR CD2 HD2  sing N N 402 
TYR CE1 CZ   doub Y N 403 
TYR CE1 HE1  sing N N 404 
TYR CE2 CZ   sing Y N 405 
TYR CE2 HE2  sing N N 406 
TYR CZ  OH   sing N N 407 
TYR OH  HH   sing N N 408 
TYR OXT HXT  sing N N 409 
VAL N   CA   sing N N 410 
VAL N   H    sing N N 411 
VAL N   H2   sing N N 412 
VAL CA  C    sing N N 413 
VAL CA  CB   sing N N 414 
VAL CA  HA   sing N N 415 
VAL C   O    doub N N 416 
VAL C   OXT  sing N N 417 
VAL CB  CG1  sing N N 418 
VAL CB  CG2  sing N N 419 
VAL CB  HB   sing N N 420 
VAL CG1 HG11 sing N N 421 
VAL CG1 HG12 sing N N 422 
VAL CG1 HG13 sing N N 423 
VAL CG2 HG21 sing N N 424 
VAL CG2 HG22 sing N N 425 
VAL CG2 HG23 sing N N 426 
VAL OXT HXT  sing N N 427 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
3 NAG 1 n 
3 NAG 2 n 
3 BMA 3 n 
4 NAG 1 n 
4 NAG 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   6M0J 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8XYE 
_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]   0.011839 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002555 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006031 
_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]   0.010335 
_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  
CL 
N  
O  
S  
ZN 
# 
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   . ASP A 1 1   ? -16.933 72.727  107.632 1.00 83.78  ?  17  ASP B N   1 
ATOM   2     C CA  . ASP A 1 1   ? -16.767 71.424  106.940 1.00 82.71  ?  17  ASP B CA  1 
ATOM   3     C C   . ASP A 1 1   ? -15.505 71.449  106.084 1.00 88.45  ?  17  ASP B C   1 
ATOM   4     O O   . ASP A 1 1   ? -15.617 71.184  104.875 1.00 93.36  ?  17  ASP B O   1 
ATOM   5     C CB  . ASP A 1 1   ? -17.969 71.132  106.055 1.00 89.56  ?  17  ASP B CB  1 
ATOM   6     C CG  . ASP A 1 1   ? -18.199 72.225  105.024 1.00 93.45  ?  17  ASP B CG  1 
ATOM   7     O OD1 . ASP A 1 1   ? -18.226 73.403  105.420 1.00 92.18  ?  17  ASP B OD1 1 
ATOM   8     O OD2 . ASP A 1 1   ? -18.319 71.891  103.829 1.00 88.31  ?  17  ASP B OD2 1 
ATOM   9     N N   . PRO A 1 2   ? -14.313 71.758  106.636 1.00 97.78  ?  18  PRO B N   1 
ATOM   10    C CA  . PRO A 1 2   ? -13.094 71.665  105.861 1.00 93.99  ?  18  PRO B CA  1 
ATOM   11    C C   . PRO A 1 2   ? -12.633 70.203  105.921 1.00 110.44 ?  18  PRO B C   1 
ATOM   12    O O   . PRO A 1 2   ? -13.241 69.418  106.639 1.00 116.06 ?  18  PRO B O   1 
ATOM   13    C CB  . PRO A 1 2   ? -12.158 72.600  106.627 1.00 94.17  ?  18  PRO B CB  1 
ATOM   14    C CG  . PRO A 1 2   ? -12.573 72.421  108.068 1.00 88.55  ?  18  PRO B CG  1 
ATOM   15    C CD  . PRO A 1 2   ? -14.072 72.200  108.016 1.00 95.46  ?  18  PRO B CD  1 
ATOM   16    N N   . SER A 1 3   ? -11.583 69.861  105.173 1.00 93.83  ?  19  SER B N   1 
ATOM   17    C CA  . SER A 1 3   ? -11.087 68.467  105.133 1.00 91.34  ?  19  SER B CA  1 
ATOM   18    C C   . SER A 1 3   ? -9.995  68.287  106.181 1.00 93.09  ?  19  SER B C   1 
ATOM   19    O O   . SER A 1 3   ? -9.168  69.203  106.321 1.00 96.76  ?  19  SER B O   1 
ATOM   20    C CB  . SER A 1 3   ? -10.565 68.152  103.780 1.00 92.58  ?  19  SER B CB  1 
ATOM   21    O OG  . SER A 1 3   ? -9.533  69.066  103.435 1.00 95.66  ?  19  SER B OG  1 
ATOM   22    N N   . THR A 1 4   ? -9.995  67.154  106.878 1.00 85.94  ?  20  THR B N   1 
ATOM   23    C CA  . THR A 1 4   ? -8.960  66.858  107.889 1.00 86.67  ?  20  THR B CA  1 
ATOM   24    C C   . THR A 1 4   ? -7.849  66.094  107.186 1.00 87.72  ?  20  THR B C   1 
ATOM   25    O O   . THR A 1 4   ? -8.128  65.431  106.175 1.00 85.32  ?  20  THR B O   1 
ATOM   26    C CB  . THR A 1 4   ? -9.529  66.058  109.063 1.00 79.92  ?  20  THR B CB  1 
ATOM   27    O OG1 . THR A 1 4   ? -9.518  64.680  108.703 1.00 80.54  ?  20  THR B OG1 1 
ATOM   28    C CG2 . THR A 1 4   ? -10.930 66.482  109.444 1.00 84.51  ?  20  THR B CG2 1 
ATOM   29    N N   . ILE A 1 5   ? -6.637  66.187  107.711 1.00 86.13  ?  21  ILE B N   1 
ATOM   30    C CA  . ILE A 1 5   ? -5.521  65.550  107.016 1.00 80.20  ?  21  ILE B CA  1 
ATOM   31    C C   . ILE A 1 5   ? -5.852  64.085  106.773 1.00 78.85  ?  21  ILE B C   1 
ATOM   32    O O   . ILE A 1 5   ? -5.565  63.525  105.704 1.00 88.52  ?  21  ILE B O   1 
ATOM   33    C CB  . ILE A 1 5   ? -4.216  65.718  107.820 1.00 88.05  ?  21  ILE B CB  1 
ATOM   34    C CG1 . ILE A 1 5   ? -3.850  67.195  107.988 1.00 95.93  ?  21  ILE B CG1 1 
ATOM   35    C CG2 . ILE A 1 5   ? -3.066  65.019  107.142 1.00 88.98  ?  21  ILE B CG2 1 
ATOM   36    C CD1 . ILE A 1 5   ? -3.618  67.937  106.705 1.00 96.70  ?  21  ILE B CD1 1 
ATOM   37    N N   . GLU A 1 6   ? -6.551  63.466  107.722 1.00 77.17  ?  22  GLU B N   1 
ATOM   38    C CA  . GLU A 1 6   ? -6.904  62.057  107.585 1.00 75.81  ?  22  GLU B CA  1 
ATOM   39    C C   . GLU A 1 6   ? -7.906  61.805  106.454 1.00 74.10  ?  22  GLU B C   1 
ATOM   40    O O   . GLU A 1 6   ? -7.839  60.780  105.759 1.00 69.43  ?  22  GLU B O   1 
ATOM   41    C CB  . GLU A 1 6   ? -7.448  61.554  108.909 1.00 77.41  ?  22  GLU B CB  1 
ATOM   42    C CG  . GLU A 1 6   ? -7.938  60.142  108.834 1.00 77.51  ?  22  GLU B CG  1 
ATOM   43    C CD  . GLU A 1 6   ? -8.280  59.578  110.192 1.00 85.11  ?  22  GLU B CD  1 
ATOM   44    O OE1 . GLU A 1 6   ? -7.430  59.693  111.101 1.00 90.25  ?  22  GLU B OE1 1 
ATOM   45    O OE2 . GLU A 1 6   ? -9.382  59.006  110.349 1.00 84.95  -1 22  GLU B OE2 1 
ATOM   46    N N   . GLU A 1 7   ? -8.853  62.709  106.258 1.00 73.95  ?  23  GLU B N   1 
ATOM   47    C CA  . GLU A 1 7   ? -9.809  62.554  105.172 1.00 72.88  ?  23  GLU B CA  1 
ATOM   48    C C   . GLU A 1 7   ? -9.115  62.577  103.820 1.00 71.86  ?  23  GLU B C   1 
ATOM   49    O O   . GLU A 1 7   ? -9.361  61.724  102.950 1.00 72.25  ?  23  GLU B O   1 
ATOM   50    C CB  . GLU A 1 7   ? -10.813 63.679  105.277 1.00 78.60  ?  23  GLU B CB  1 
ATOM   51    C CG  . GLU A 1 7   ? -11.507 63.708  106.599 1.00 78.99  ?  23  GLU B CG  1 
ATOM   52    C CD  . GLU A 1 7   ? -12.364 64.929  106.741 1.00 88.23  ?  23  GLU B CD  1 
ATOM   53    O OE1 . GLU A 1 7   ? -11.860 66.025  106.438 1.00 96.79  ?  23  GLU B OE1 1 
ATOM   54    O OE2 . GLU A 1 7   ? -13.528 64.815  107.149 1.00 96.08  -1 23  GLU B OE2 1 
ATOM   55    N N   . GLN A 1 8   ? -8.277  63.590  103.612 1.00 70.67  ?  24  GLN B N   1 
ATOM   56    C CA  . GLN A 1 8   ? -7.478  63.658  102.406 1.00 70.16  ?  24  GLN B CA  1 
ATOM   57    C C   . GLN A 1 8   ? -6.710  62.364  102.196 1.00 72.20  ?  24  GLN B C   1 
ATOM   58    O O   . GLN A 1 8   ? -6.638  61.846  101.068 1.00 68.85  ?  24  GLN B O   1 
ATOM   59    C CB  . GLN A 1 8   ? -6.538  64.860  102.500 1.00 73.16  ?  24  GLN B CB  1 
ATOM   60    C CG  . GLN A 1 8   ? -7.286  66.161  102.674 1.00 76.48  ?  24  GLN B CG  1 
ATOM   61    C CD  . GLN A 1 8   ? -6.435  67.290  103.188 1.00 82.06  ?  24  GLN B CD  1 
ATOM   62    O OE1 . GLN A 1 8   ? -5.275  67.423  102.822 1.00 84.58  ?  24  GLN B OE1 1 
ATOM   63    N NE2 . GLN A 1 8   ? -7.025  68.149  103.994 1.00 88.32  ?  24  GLN B NE2 1 
ATOM   64    N N   . ALA A 1 9   ? -6.169  61.807  103.287 1.00 70.01  ?  25  ALA B N   1 
ATOM   65    C CA  . ALA A 1 9   ? -5.306  60.640  103.171 1.00 67.34  ?  25  ALA B CA  1 
ATOM   66    C C   . ALA A 1 9   ? -6.118  59.392  102.824 1.00 68.34  ?  25  ALA B C   1 
ATOM   67    O O   . ALA A 1 9   ? -5.650  58.508  102.090 1.00 67.57  ?  25  ALA B O   1 
ATOM   68    C CB  . ALA A 1 9   ? -4.501  60.469  104.465 1.00 68.66  ?  25  ALA B CB  1 
ATOM   69    N N   . LYS A 1 10  ? -7.358  59.317  103.295 1.00 68.35  ?  26  LYS B N   1 
ATOM   70    C CA  . LYS A 1 10  ? -8.206  58.198  102.885 1.00 64.68  ?  26  LYS B CA  1 
ATOM   71    C C   . LYS A 1 10  ? -8.509  58.254  101.391 1.00 67.84  ?  26  LYS B C   1 
ATOM   72    O O   . LYS A 1 10  ? -8.335  57.263  100.670 1.00 65.88  ?  26  LYS B O   1 
ATOM   73    C CB  . LYS A 1 10  ? -9.507  58.184  103.673 1.00 67.28  ?  26  LYS B CB  1 
ATOM   74    C CG  . LYS A 1 10  ? -9.362  57.716  105.078 1.00 65.08  ?  26  LYS B CG  1 
ATOM   75    C CD  . LYS A 1 10  ? -10.691 57.722  105.782 1.00 68.12  ?  26  LYS B CD  1 
ATOM   76    C CE  . LYS A 1 10  ? -10.576 57.342  107.229 1.00 68.67  ?  26  LYS B CE  1 
ATOM   77    N NZ  . LYS A 1 10  ? -11.848 57.563  107.911 1.00 67.85  ?  26  LYS B NZ  1 
ATOM   78    N N   . THR A 1 11  ? -8.973  59.412  100.909 1.00 68.56  ?  27  THR B N   1 
ATOM   79    C CA  . THR A 1 11  ? -9.226  59.539  99.478  1.00 66.09  ?  27  THR B CA  1 
ATOM   80    C C   . THR A 1 11  ? -7.958  59.239  98.684  1.00 67.29  ?  27  THR B C   1 
ATOM   81    O O   . THR A 1 11  ? -8.003  58.550  97.648  1.00 69.04  ?  27  THR B O   1 
ATOM   82    C CB  . THR A 1 11  ? -9.761  60.935  99.166  1.00 68.58  ?  27  THR B CB  1 
ATOM   83    O OG1 . THR A 1 11  ? -10.807 61.247  100.085 1.00 66.10  ?  27  THR B OG1 1 
ATOM   84    C CG2 . THR A 1 11  ? -10.322 60.998  97.803  1.00 64.14  ?  27  THR B CG2 1 
ATOM   85    N N   . PHE A 1 12  ? -6.817  59.747  99.164  1.00 66.68  ?  28  PHE B N   1 
ATOM   86    C CA  . PHE A 1 12  ? -5.537  59.502  98.508  1.00 67.32  ?  28  PHE B CA  1 
ATOM   87    C C   . PHE A 1 12  ? -5.320  58.006  98.316  1.00 61.91  ?  28  PHE B C   1 
ATOM   88    O O   . PHE A 1 12  ? -5.086  57.524  97.196  1.00 60.00  ?  28  PHE B O   1 
ATOM   89    C CB  . PHE A 1 12  ? -4.392  60.125  99.333  1.00 65.56  ?  28  PHE B CB  1 
ATOM   90    C CG  . PHE A 1 12  ? -3.027  59.709  98.867  1.00 62.51  ?  28  PHE B CG  1 
ATOM   91    C CD1 . PHE A 1 12  ? -2.515  60.170  97.667  1.00 63.90  ?  28  PHE B CD1 1 
ATOM   92    C CD2 . PHE A 1 12  ? -2.310  58.768  99.572  1.00 57.29  ?  28  PHE B CD2 1 
ATOM   93    C CE1 . PHE A 1 12  ? -1.282  59.756  97.213  1.00 65.12  ?  28  PHE B CE1 1 
ATOM   94    C CE2 . PHE A 1 12  ? -1.087  58.346  99.120  1.00 61.80  ?  28  PHE B CE2 1 
ATOM   95    C CZ  . PHE A 1 12  ? -0.569  58.838  97.942  1.00 68.64  ?  28  PHE B CZ  1 
ATOM   96    N N   . LEU A 1 13  ? -5.437  57.253  99.408  1.00 64.09  ?  29  LEU B N   1 
ATOM   97    C CA  . LEU A 1 13  ? -5.227  55.814  99.386  1.00 66.58  ?  29  LEU B CA  1 
ATOM   98    C C   . LEU A 1 13  ? -6.267  55.100  98.562  1.00 66.37  ?  29  LEU B C   1 
ATOM   99    O O   . LEU A 1 13  ? -6.021  53.989  98.074  1.00 63.75  ?  29  LEU B O   1 
ATOM   100   C CB  . LEU A 1 13  ? -5.278  55.296  100.805 1.00 66.86  ?  29  LEU B CB  1 
ATOM   101   C CG  . LEU A 1 13  ? -4.140  55.747  101.684 1.00 62.70  ?  29  LEU B CG  1 
ATOM   102   C CD1 . LEU A 1 13  ? -4.615  55.341  103.025 1.00 61.00  ?  29  LEU B CD1 1 
ATOM   103   C CD2 . LEU A 1 13  ? -2.838  55.046  101.272 1.00 58.41  ?  29  LEU B CD2 1 
ATOM   104   N N   . ASP A 1 14  ? -7.425  55.730  98.412  1.00 68.63  ?  30  ASP B N   1 
ATOM   105   C CA  . ASP A 1 14  ? -8.506  55.154  97.634  1.00 67.27  ?  30  ASP B CA  1 
ATOM   106   C C   . ASP A 1 14  ? -8.120  55.116  96.159  1.00 64.24  ?  30  ASP B C   1 
ATOM   107   O O   . ASP A 1 14  ? -8.033  54.043  95.550  1.00 63.54  ?  30  ASP B O   1 
ATOM   108   C CB  . ASP A 1 14  ? -9.741  56.011  97.837  1.00 65.42  ?  30  ASP B CB  1 
ATOM   109   C CG  . ASP A 1 14  ? -10.950 55.202  97.971  1.00 74.86  ?  30  ASP B CG  1 
ATOM   110   O OD1 . ASP A 1 14  ? -10.849 54.018  97.564  1.00 78.74  ?  30  ASP B OD1 1 
ATOM   111   O OD2 . ASP A 1 14  ? -11.995 55.768  98.389  1.00 78.87  -1 30  ASP B OD2 1 
ATOM   112   N N   . LYS A 1 15  ? -7.826  56.300  95.594  1.00 62.07  ?  31  LYS B N   1 
ATOM   113   C CA  . LYS A 1 15  ? -7.248  56.394  94.247  1.00 62.77  ?  31  LYS B CA  1 
ATOM   114   C C   . LYS A 1 15  ? -6.004  55.507  94.086  1.00 66.64  ?  31  LYS B C   1 
ATOM   115   O O   . LYS A 1 15  ? -5.803  54.860  93.034  1.00 69.92  ?  31  LYS B O   1 
ATOM   116   C CB  . LYS A 1 15  ? -6.945  57.867  93.898  1.00 65.66  ?  31  LYS B CB  1 
ATOM   117   C CG  . LYS A 1 15  ? -5.929  58.057  92.743  1.00 75.47  ?  31  LYS B CG  1 
ATOM   118   C CD  . LYS A 1 15  ? -6.439  57.735  91.332  1.00 78.27  ?  31  LYS B CD  1 
ATOM   119   C CE  . LYS A 1 15  ? -5.327  57.985  90.294  1.00 86.28  ?  31  LYS B CE  1 
ATOM   120   N NZ  . LYS A 1 15  ? -5.667  57.488  88.916  1.00 90.85  ?  31  LYS B NZ  1 
ATOM   121   N N   . PHE A 1 16  ? -5.167  55.440  95.129  1.00 66.97  ?  32  PHE B N   1 
ATOM   122   C CA  . PHE A 1 16  ? -3.949  54.642  95.037  1.00 64.54  ?  32  PHE B CA  1 
ATOM   123   C C   . PHE A 1 16  ? -4.240  53.149  94.942  1.00 64.74  ?  32  PHE B C   1 
ATOM   124   O O   . PHE A 1 16  ? -3.551  52.444  94.203  1.00 67.37  ?  32  PHE B O   1 
ATOM   125   C CB  . PHE A 1 16  ? -3.012  54.912  96.218  1.00 63.68  ?  32  PHE B CB  1 
ATOM   126   C CG  . PHE A 1 16  ? -1.872  53.917  96.325  1.00 61.82  ?  32  PHE B CG  1 
ATOM   127   C CD1 . PHE A 1 16  ? -0.709  54.105  95.608  1.00 57.42  ?  32  PHE B CD1 1 
ATOM   128   C CD2 . PHE A 1 16  ? -1.959  52.814  97.149  1.00 61.23  ?  32  PHE B CD2 1 
ATOM   129   C CE1 . PHE A 1 16  ? 0.324   53.212  95.692  1.00 55.33  ?  32  PHE B CE1 1 
ATOM   130   C CE2 . PHE A 1 16  ? -0.904  51.920  97.239  1.00 58.19  ?  32  PHE B CE2 1 
ATOM   131   C CZ  . PHE A 1 16  ? 0.229   52.120  96.510  1.00 58.23  ?  32  PHE B CZ  1 
ATOM   132   N N   . ASN A 1 17  ? -5.224  52.631  95.688  1.00 66.25  ?  33  ASN B N   1 
ATOM   133   C CA  . ASN A 1 17  ? -5.482  51.188  95.634  1.00 67.71  ?  33  ASN B CA  1 
ATOM   134   C C   . ASN A 1 17  ? -5.920  50.735  94.240  1.00 71.69  ?  33  ASN B C   1 
ATOM   135   O O   . ASN A 1 17  ? -5.593  49.619  93.811  1.00 71.53  ?  33  ASN B O   1 
ATOM   136   C CB  . ASN A 1 17  ? -6.535  50.768  96.652  1.00 63.28  ?  33  ASN B CB  1 
ATOM   137   C CG  . ASN A 1 17  ? -6.047  50.856  98.058  1.00 58.81  ?  33  ASN B CG  1 
ATOM   138   O OD1 . ASN A 1 17  ? -4.857  50.776  98.337  1.00 63.53  ?  33  ASN B OD1 1 
ATOM   139   N ND2 . ASN A 1 17  ? -6.972  51.059  98.965  1.00 60.36  ?  33  ASN B ND2 1 
ATOM   140   N N   . HIS A 1 18  ? -6.599  51.588  93.489  1.00 76.37  ?  34  HIS B N   1 
ATOM   141   C CA  . HIS A 1 18  ? -6.990  51.069  92.192  1.00 78.74  ?  34  HIS B CA  1 
ATOM   142   C C   . HIS A 1 18  ? -5.895  51.222  91.148  1.00 81.63  ?  34  HIS B C   1 
ATOM   143   O O   . HIS A 1 18  ? -5.595  50.248  90.426  1.00 89.13  ?  34  HIS B O   1 
ATOM   144   C CB  . HIS A 1 18  ? -8.290  51.718  91.780  1.00 83.17  ?  34  HIS B CB  1 
ATOM   145   C CG  . HIS A 1 18  ? -9.379  51.404  92.756  1.00 90.01  ?  34  HIS B CG  1 
ATOM   146   N ND1 . HIS A 1 18  ? -9.480  52.042  93.976  1.00 87.47  ?  34  HIS B ND1 1 
ATOM   147   C CD2 . HIS A 1 18  ? -10.354 50.463  92.744  1.00 95.17  ?  34  HIS B CD2 1 
ATOM   148   C CE1 . HIS A 1 18  ? -10.506 51.545  94.648  1.00 89.87  ?  34  HIS B CE1 1 
ATOM   149   N NE2 . HIS A 1 18  ? -11.056 50.589  93.921  1.00 91.98  ?  34  HIS B NE2 1 
ATOM   150   N N   . GLU A 1 19  ? -5.273  52.412  91.072  1.00 75.68  ?  35  GLU B N   1 
ATOM   151   C CA  . GLU A 1 19  ? -4.075  52.516  90.240  1.00 75.59  ?  35  GLU B CA  1 
ATOM   152   C C   . GLU A 1 19  ? -3.101  51.369  90.523  1.00 69.78  ?  35  GLU B C   1 
ATOM   153   O O   . GLU A 1 19  ? -2.524  50.762  89.599  1.00 69.71  ?  35  GLU B O   1 
ATOM   154   C CB  . GLU A 1 19  ? -3.421  53.879  90.445  1.00 72.88  ?  35  GLU B CB  1 
ATOM   155   C CG  . GLU A 1 19  ? -3.854  54.966  89.463  1.00 78.83  ?  35  GLU B CG  1 
ATOM   156   C CD  . GLU A 1 19  ? -3.711  54.569  87.964  1.00 103.84 ?  35  GLU B CD  1 
ATOM   157   O OE1 . GLU A 1 19  ? -3.100  53.515  87.614  1.00 97.94  ?  35  GLU B OE1 1 
ATOM   158   O OE2 . GLU A 1 19  ? -4.241  55.326  87.112  1.00 116.97 -1 35  GLU B OE2 1 
ATOM   159   N N   . ALA A 1 20  ? -2.972  51.008  91.795  1.00 70.60  ?  36  ALA B N   1 
ATOM   160   C CA  . ALA A 1 20  ? -2.016  50.007  92.217  1.00 67.46  ?  36  ALA B CA  1 
ATOM   161   C C   . ALA A 1 20  ? -2.420  48.611  91.779  1.00 66.43  ?  36  ALA B C   1 
ATOM   162   O O   . ALA A 1 20  ? -1.591  47.875  91.241  1.00 68.97  ?  36  ALA B O   1 
ATOM   163   C CB  . ALA A 1 20  ? -1.859  50.064  93.731  1.00 68.91  ?  36  ALA B CB  1 
ATOM   164   N N   . GLU A 1 21  ? -3.661  48.186  92.048  1.00 63.92  ?  37  GLU B N   1 
ATOM   165   C CA  . GLU A 1 21  ? -4.012  46.832  91.640  1.00 63.37  ?  37  GLU B CA  1 
ATOM   166   C C   . GLU A 1 21  ? -3.824  46.663  90.146  1.00 62.92  ?  37  GLU B C   1 
ATOM   167   O O   . GLU A 1 21  ? -3.349  45.616  89.693  1.00 61.62  ?  37  GLU B O   1 
ATOM   168   C CB  . GLU A 1 21  ? -5.438  46.473  92.014  1.00 66.55  ?  37  GLU B CB  1 
ATOM   169   C CG  . GLU A 1 21  ? -5.821  46.503  93.475  1.00 65.37  ?  37  GLU B CG  1 
ATOM   170   C CD  . GLU A 1 21  ? -6.835  45.403  93.803  1.00 72.06  ?  37  GLU B CD  1 
ATOM   171   O OE1 . GLU A 1 21  ? -6.711  44.250  93.318  1.00 72.01  ?  37  GLU B OE1 1 
ATOM   172   O OE2 . GLU A 1 21  ? -7.841  45.727  94.462  1.00 79.58  -1 37  GLU B OE2 1 
ATOM   173   N N   . ASP A 1 22  ? -4.119  47.704  89.359  1.00 65.15  ?  38  ASP B N   1 
ATOM   174   C CA  . ASP A 1 22  ? -3.898  47.531  87.927  1.00 62.46  ?  38  ASP B CA  1 
ATOM   175   C C   . ASP A 1 22  ? -2.416  47.386  87.592  1.00 66.20  ?  38  ASP B C   1 
ATOM   176   O O   . ASP A 1 22  ? -2.028  46.453  86.872  1.00 68.00  ?  38  ASP B O   1 
ATOM   177   C CB  . ASP A 1 22  ? -4.495  48.658  87.107  1.00 65.15  ?  38  ASP B CB  1 
ATOM   178   C CG  . ASP A 1 22  ? -4.597  48.267  85.644  1.00 68.21  ?  38  ASP B CG  1 
ATOM   179   O OD1 . ASP A 1 22  ? -5.349  47.290  85.375  1.00 65.30  ?  38  ASP B OD1 1 
ATOM   180   O OD2 . ASP A 1 22  ? -3.913  48.877  84.781  1.00 70.28  -1 38  ASP B OD2 1 
ATOM   181   N N   . LEU A 1 23  ? -1.566  48.300  88.086  1.00 68.68  ?  39  LEU B N   1 
ATOM   182   C CA  . LEU A 1 23  ? -0.147  48.240  87.707  1.00 66.58  ?  39  LEU B CA  1 
ATOM   183   C C   . LEU A 1 23  ? 0.542   46.982  88.224  1.00 69.74  ?  39  LEU B C   1 
ATOM   184   O O   . LEU A 1 23  ? 1.432   46.411  87.567  1.00 73.32  ?  39  LEU B O   1 
ATOM   185   C CB  . LEU A 1 23  ? 0.574   49.475  88.198  1.00 60.85  ?  39  LEU B CB  1 
ATOM   186   C CG  . LEU A 1 23  ? 0.364   50.530  87.165  1.00 58.63  ?  39  LEU B CG  1 
ATOM   187   C CD1 . LEU A 1 23  ? 0.881   51.842  87.647  1.00 63.04  ?  39  LEU B CD1 1 
ATOM   188   C CD2 . LEU A 1 23  ? 1.181   50.005  86.029  1.00 60.47  ?  39  LEU B CD2 1 
ATOM   189   N N   . PHE A 1 24  ? 0.139   46.535  89.399  1.00 67.98  ?  40  PHE B N   1 
ATOM   190   C CA  . PHE A 1 24  ? 0.681   45.323  89.982  1.00 66.98  ?  40  PHE B CA  1 
ATOM   191   C C   . PHE A 1 24  ? 0.234   44.100  89.186  1.00 69.93  ?  40  PHE B C   1 
ATOM   192   O O   . PHE A 1 24  ? 1.017   43.164  89.001  1.00 71.28  ?  40  PHE B O   1 
ATOM   193   C CB  . PHE A 1 24  ? 0.220   45.261  91.436  1.00 64.52  ?  40  PHE B CB  1 
ATOM   194   C CG  . PHE A 1 24  ? 0.744   44.097  92.211  1.00 68.64  ?  40  PHE B CG  1 
ATOM   195   C CD1 . PHE A 1 24  ? 1.998   44.152  92.805  1.00 67.67  ?  40  PHE B CD1 1 
ATOM   196   C CD2 . PHE A 1 24  ? -0.028  42.962  92.373  1.00 68.90  ?  40  PHE B CD2 1 
ATOM   197   C CE1 . PHE A 1 24  ? 2.468   43.104  93.546  1.00 65.53  ?  40  PHE B CE1 1 
ATOM   198   C CE2 . PHE A 1 24  ? 0.442   41.896  93.113  1.00 71.89  ?  40  PHE B CE2 1 
ATOM   199   C CZ  . PHE A 1 24  ? 1.694   41.968  93.695  1.00 72.75  ?  40  PHE B CZ  1 
ATOM   200   N N   . TYR A 1 25  ? -1.013  44.105  88.676  1.00 69.56  ?  41  TYR B N   1 
ATOM   201   C CA  . TYR A 1 25  ? -1.447  43.000  87.832  1.00 68.85  ?  41  TYR B CA  1 
ATOM   202   C C   . TYR A 1 25  ? -0.649  42.994  86.534  1.00 71.52  ?  41  TYR B C   1 
ATOM   203   O O   . TYR A 1 25  ? -0.317  41.926  86.018  1.00 76.11  ?  41  TYR B O   1 
ATOM   204   C CB  . TYR A 1 25  ? -2.935  43.100  87.491  1.00 66.93  ?  41  TYR B CB  1 
ATOM   205   C CG  . TYR A 1 25  ? -3.503  41.783  86.966  1.00 64.46  ?  41  TYR B CG  1 
ATOM   206   C CD1 . TYR A 1 25  ? -3.991  40.831  87.849  1.00 68.63  ?  41  TYR B CD1 1 
ATOM   207   C CD2 . TYR A 1 25  ? -3.393  41.417  85.640  1.00 61.91  ?  41  TYR B CD2 1 
ATOM   208   C CE1 . TYR A 1 25  ? -4.454  39.618  87.405  1.00 68.26  ?  41  TYR B CE1 1 
ATOM   209   C CE2 . TYR A 1 25  ? -3.843  40.190  85.201  1.00 60.51  ?  41  TYR B CE2 1 
ATOM   210   C CZ  . TYR A 1 25  ? -4.370  39.300  86.087  1.00 64.06  ?  41  TYR B CZ  1 
ATOM   211   O OH  . TYR A 1 25  ? -4.820  38.069  85.693  1.00 68.88  ?  41  TYR B OH  1 
ATOM   212   N N   . GLN A 1 26  ? -0.315  44.181  86.015  1.00 70.58  ?  42  GLN B N   1 
ATOM   213   C CA  . GLN A 1 26  ? 0.587   44.296  84.874  1.00 76.67  ?  42  GLN B CA  1 
ATOM   214   C C   . GLN A 1 26  ? 1.889   43.554  85.150  1.00 81.87  ?  42  GLN B C   1 
ATOM   215   O O   . GLN A 1 26  ? 2.280   42.635  84.410  1.00 86.99  ?  42  GLN B O   1 
ATOM   216   C CB  . GLN A 1 26  ? 0.915   45.773  84.610  1.00 82.28  ?  42  GLN B CB  1 
ATOM   217   C CG  . GLN A 1 26  ? -0.219  46.716  84.168  1.00 76.33  ?  42  GLN B CG  1 
ATOM   218   C CD  . GLN A 1 26  ? -0.899  46.339  82.900  1.00 79.71  ?  42  GLN B CD  1 
ATOM   219   O OE1 . GLN A 1 26  ? -0.525  45.377  82.219  1.00 89.71  ?  42  GLN B OE1 1 
ATOM   220   N NE2 . GLN A 1 26  ? -1.925  47.096  82.564  1.00 85.74  ?  42  GLN B NE2 1 
ATOM   221   N N   . SER A 1 27  ? 2.584   43.978  86.215  1.00 78.63  ?  43  SER B N   1 
ATOM   222   C CA  . SER A 1 27  ? 3.885   43.410  86.554  1.00 82.24  ?  43  SER B CA  1 
ATOM   223   C C   . SER A 1 27  ? 3.813   41.914  86.815  1.00 81.48  ?  43  SER B C   1 
ATOM   224   O O   . SER A 1 27  ? 4.708   41.159  86.412  1.00 87.15  ?  43  SER B O   1 
ATOM   225   C CB  . SER A 1 27  ? 4.462   44.106  87.775  1.00 82.22  ?  43  SER B CB  1 
ATOM   226   O OG  . SER A 1 27  ? 5.831   43.795  87.907  1.00 89.67  ?  43  SER B OG  1 
ATOM   227   N N   . SER A 1 28  ? 2.774   41.465  87.503  1.00 77.16  ?  44  SER B N   1 
ATOM   228   C CA  . SER A 1 28  ? 2.759   40.077  87.906  1.00 72.00  ?  44  SER B CA  1 
ATOM   229   C C   . SER A 1 28  ? 2.360   39.163  86.773  1.00 81.51  ?  44  SER B C   1 
ATOM   230   O O   . SER A 1 28  ? 2.869   38.041  86.697  1.00 86.24  ?  44  SER B O   1 
ATOM   231   C CB  . SER A 1 28  ? 1.842   39.905  89.098  1.00 75.88  ?  44  SER B CB  1 
ATOM   232   O OG  . SER A 1 28  ? 2.170   40.882  90.070  1.00 80.95  ?  44  SER B OG  1 
ATOM   233   N N   . LEU A 1 29  ? 1.487   39.605  85.870  1.00 81.14  ?  45  LEU B N   1 
ATOM   234   C CA  . LEU A 1 29  ? 1.243   38.774  84.705  1.00 82.20  ?  45  LEU B CA  1 
ATOM   235   C C   . LEU A 1 29  ? 2.488   38.725  83.845  1.00 87.87  ?  45  LEU B C   1 
ATOM   236   O O   . LEU A 1 29  ? 2.855   37.655  83.352  1.00 94.05  ?  45  LEU B O   1 
ATOM   237   C CB  . LEU A 1 29  ? 0.042   39.284  83.912  1.00 82.19  ?  45  LEU B CB  1 
ATOM   238   C CG  . LEU A 1 29  ? -0.710  38.287  83.003  1.00 83.59  ?  45  LEU B CG  1 
ATOM   239   C CD1 . LEU A 1 29  ? -0.916  36.922  83.673  1.00 84.92  ?  45  LEU B CD1 1 
ATOM   240   C CD2 . LEU A 1 29  ? -2.059  38.839  82.531  1.00 80.50  ?  45  LEU B CD2 1 
ATOM   241   N N   . ALA A 1 30  ? 3.180   39.858  83.694  1.00 84.79  ?  46  ALA B N   1 
ATOM   242   C CA  . ALA A 1 30  ? 4.441   39.842  82.964  1.00 90.37  ?  46  ALA B CA  1 
ATOM   243   C C   . ALA A 1 30  ? 5.412   38.824  83.569  1.00 96.41  ?  46  ALA B C   1 
ATOM   244   O O   . ALA A 1 30  ? 6.032   38.020  82.852  1.00 103.00 ?  46  ALA B O   1 
ATOM   245   C CB  . ALA A 1 30  ? 5.039   41.247  82.951  1.00 93.65  ?  46  ALA B CB  1 
ATOM   246   N N   . SER A 1 31  ? 5.518   38.814  84.899  1.00 94.95  ?  47  SER B N   1 
ATOM   247   C CA  . SER A 1 31  ? 6.470   37.928  85.560  1.00 94.73  ?  47  SER B CA  1 
ATOM   248   C C   . SER A 1 31  ? 6.078   36.459  85.400  1.00 95.16  ?  47  SER B C   1 
ATOM   249   O O   . SER A 1 31  ? 6.932   35.615  85.112  1.00 96.19  ?  47  SER B O   1 
ATOM   250   C CB  . SER A 1 31  ? 6.581   38.307  87.030  1.00 91.54  ?  47  SER B CB  1 
ATOM   251   O OG  . SER A 1 31  ? 7.436   37.423  87.714  1.00 95.69  ?  47  SER B OG  1 
ATOM   252   N N   . TRP A 1 32  ? 4.797   36.133  85.589  1.00 91.18  ?  48  TRP B N   1 
ATOM   253   C CA  . TRP A 1 32  ? 4.351   34.759  85.378  1.00 90.78  ?  48  TRP B CA  1 
ATOM   254   C C   . TRP A 1 32  ? 4.640   34.311  83.959  1.00 102.53 ?  48  TRP B C   1 
ATOM   255   O O   . TRP A 1 32  ? 5.046   33.165  83.740  1.00 107.34 ?  48  TRP B O   1 
ATOM   256   C CB  . TRP A 1 32  ? 2.863   34.630  85.666  1.00 89.88  ?  48  TRP B CB  1 
ATOM   257   C CG  . TRP A 1 32  ? 2.252   33.290  85.341  1.00 90.15  ?  48  TRP B CG  1 
ATOM   258   C CD1 . TRP A 1 32  ? 1.710   32.913  84.149  1.00 96.78  ?  48  TRP B CD1 1 
ATOM   259   C CD2 . TRP A 1 32  ? 1.991   32.208  86.252  1.00 90.99  ?  48  TRP B CD2 1 
ATOM   260   N NE1 . TRP A 1 32  ? 1.191   31.641  84.236  1.00 96.28  ?  48  TRP B NE1 1 
ATOM   261   C CE2 . TRP A 1 32  ? 1.338   31.190  85.518  1.00 91.73  ?  48  TRP B CE2 1 
ATOM   262   C CE3 . TRP A 1 32  ? 2.262   31.991  87.604  1.00 90.75  ?  48  TRP B CE3 1 
ATOM   263   C CZ2 . TRP A 1 32  ? 0.960   29.976  86.088  1.00 91.16  ?  48  TRP B CZ2 1 
ATOM   264   C CZ3 . TRP A 1 32  ? 1.887   30.786  88.169  1.00 92.73  ?  48  TRP B CZ3 1 
ATOM   265   C CH2 . TRP A 1 32  ? 1.239   29.792  87.412  1.00 92.45  ?  48  TRP B CH2 1 
ATOM   266   N N   . ASN A 1 33  ? 4.442   35.205  82.972  1.00 104.83 ?  49  ASN B N   1 
ATOM   267   C CA  . ASN A 1 33  ? 4.701   34.833  81.578  1.00 108.95 ?  49  ASN B CA  1 
ATOM   268   C C   . ASN A 1 33  ? 6.190   34.641  81.324  1.00 114.60 ?  49  ASN B C   1 
ATOM   269   O O   . ASN A 1 33  ? 6.565   33.895  80.410  1.00 115.81 ?  49  ASN B O   1 
ATOM   270   C CB  . ASN A 1 33  ? 4.133   35.869  80.587  1.00 110.40 ?  49  ASN B CB  1 
ATOM   271   C CG  . ASN A 1 33  ? 2.591   35.998  80.634  1.00 108.25 ?  49  ASN B CG  1 
ATOM   272   O OD1 . ASN A 1 33  ? 1.851   35.012  80.768  1.00 111.76 ?  49  ASN B OD1 1 
ATOM   273   N ND2 . ASN A 1 33  ? 2.112   37.227  80.471  1.00 97.64  ?  49  ASN B ND2 1 
ATOM   274   N N   . TYR A 1 34  ? 7.051   35.297  82.112  1.00 107.92 ?  50  TYR B N   1 
ATOM   275   C CA  . TYR A 1 34  ? 8.482   35.007  81.985  1.00 113.66 ?  50  TYR B CA  1 
ATOM   276   C C   . TYR A 1 34  ? 8.880   33.700  82.683  1.00 109.87 ?  50  TYR B C   1 
ATOM   277   O O   . TYR A 1 34  ? 9.681   32.922  82.148  1.00 113.41 ?  50  TYR B O   1 
ATOM   278   C CB  . TYR A 1 34  ? 9.323   36.160  82.524  1.00 113.73 ?  50  TYR B CB  1 
ATOM   279   C CG  . TYR A 1 34  ? 10.775  35.783  82.660  1.00 114.75 ?  50  TYR B CG  1 
ATOM   280   C CD1 . TYR A 1 34  ? 11.542  35.542  81.540  1.00 119.00 ?  50  TYR B CD1 1 
ATOM   281   C CD2 . TYR A 1 34  ? 11.369  35.647  83.904  1.00 114.70 ?  50  TYR B CD2 1 
ATOM   282   C CE1 . TYR A 1 34  ? 12.855  35.173  81.650  1.00 125.51 ?  50  TYR B CE1 1 
ATOM   283   C CE2 . TYR A 1 34  ? 12.690  35.295  84.023  1.00 118.30 ?  50  TYR B CE2 1 
ATOM   284   C CZ  . TYR A 1 34  ? 13.432  35.062  82.888  1.00 124.64 ?  50  TYR B CZ  1 
ATOM   285   O OH  . TYR A 1 34  ? 14.754  34.700  82.973  1.00 129.83 ?  50  TYR B OH  1 
ATOM   286   N N   . ASN A 1 35  ? 8.336   33.440  83.866  1.00 104.84 ?  51  ASN B N   1 
ATOM   287   C CA  . ASN A 1 35  ? 8.699   32.283  84.671  1.00 102.16 ?  51  ASN B CA  1 
ATOM   288   C C   . ASN A 1 35  ? 8.043   30.988  84.200  1.00 102.96 ?  51  ASN B C   1 
ATOM   289   O O   . ASN A 1 35  ? 8.364   29.922  84.728  1.00 104.49 ?  51  ASN B O   1 
ATOM   290   C CB  . ASN A 1 35  ? 8.337   32.553  86.131  1.00 102.33 ?  51  ASN B CB  1 
ATOM   291   C CG  . ASN A 1 35  ? 9.466   33.211  86.901  1.00 100.79 ?  51  ASN B CG  1 
ATOM   292   O OD1 . ASN A 1 35  ? 10.330  32.525  87.443  1.00 104.80 ?  51  ASN B OD1 1 
ATOM   293   N ND2 . ASN A 1 35  ? 9.468   34.539  86.956  1.00 97.71  ?  51  ASN B ND2 1 
ATOM   294   N N   . THR A 1 36  ? 7.139   31.048  83.233  1.00 106.78 ?  52  THR B N   1 
ATOM   295   C CA  . THR A 1 36  ? 6.507   29.870  82.668  1.00 106.22 ?  52  THR B CA  1 
ATOM   296   C C   . THR A 1 36  ? 6.857   29.667  81.196  1.00 112.86 ?  52  THR B C   1 
ATOM   297   O O   . THR A 1 36  ? 6.373   28.711  80.579  1.00 121.65 ?  52  THR B O   1 
ATOM   298   C CB  . THR A 1 36  ? 4.983   29.964  82.834  1.00 102.66 ?  52  THR B CB  1 
ATOM   299   O OG1 . THR A 1 36  ? 4.513   31.166  82.215  1.00 105.67 ?  52  THR B OG1 1 
ATOM   300   C CG2 . THR A 1 36  ? 4.590   29.977  84.302  1.00 99.93  ?  52  THR B CG2 1 
ATOM   301   N N   . ASN A 1 37  ? 7.516   30.654  80.584  1.00 113.63 ?  53  ASN B N   1 
ATOM   302   C CA  . ASN A 1 37  ? 7.778   30.602  79.123  1.00 117.65 ?  53  ASN B CA  1 
ATOM   303   C C   . ASN A 1 37  ? 8.908   31.590  78.911  1.00 119.69 ?  53  ASN B C   1 
ATOM   304   O O   . ASN A 1 37  ? 8.629   32.745  78.579  1.00 121.71 ?  53  ASN B O   1 
ATOM   305   C CB  . ASN A 1 37  ? 6.503   30.905  78.333  1.00 126.57 ?  53  ASN B CB  1 
ATOM   306   C CG  . ASN A 1 37  ? 6.719   31.144  76.854  1.00 135.29 ?  53  ASN B CG  1 
ATOM   307   O OD1 . ASN A 1 37  ? 7.655   30.623  76.246  1.00 129.34 ?  53  ASN B OD1 1 
ATOM   308   N ND2 . ASN A 1 37  ? 5.846   31.943  76.275  1.00 140.86 ?  53  ASN B ND2 1 
ATOM   309   N N   . ILE A 1 38  ? 10.125  31.154  79.193  1.00 118.59 ?  54  ILE B N   1 
ATOM   310   C CA  . ILE A 1 38  ? 11.288  32.067  79.138  1.00 120.84 ?  54  ILE B CA  1 
ATOM   311   C C   . ILE A 1 38  ? 11.618  32.377  77.681  1.00 122.97 ?  54  ILE B C   1 
ATOM   312   O O   . ILE A 1 38  ? 12.126  31.478  76.974  1.00 123.14 ?  54  ILE B O   1 
ATOM   313   C CB  . ILE A 1 38  ? 12.418  31.372  79.908  1.00 122.01 ?  54  ILE B CB  1 
ATOM   314   C CG1 . ILE A 1 38  ? 11.887  30.777  81.208  1.00 121.64 ?  54  ILE B CG1 1 
ATOM   315   C CG2 . ILE A 1 38  ? 13.542  32.338  80.185  1.00 116.73 ?  54  ILE B CG2 1 
ATOM   316   C CD1 . ILE A 1 38  ? 12.875  29.901  81.929  1.00 123.65 ?  54  ILE B CD1 1 
ATOM   317   N N   . THR A 1 39  ? 11.275  33.584  77.239  1.00 124.24 ?  55  THR B N   1 
ATOM   318   C CA  . THR A 1 39  ? 11.644  34.047  75.885  1.00 128.92 ?  55  THR B CA  1 
ATOM   319   C C   . THR A 1 39  ? 12.316  35.401  76.092  1.00 131.84 ?  55  THR B C   1 
ATOM   320   O O   . THR A 1 39  ? 11.798  36.175  76.890  1.00 127.22 ?  55  THR B O   1 
ATOM   321   C CB  . THR A 1 39  ? 10.428  34.211  74.960  1.00 127.71 ?  55  THR B CB  1 
ATOM   322   O OG1 . THR A 1 39  ? 9.569   35.234  75.468  1.00 124.84 ?  55  THR B OG1 1 
ATOM   323   C CG2 . THR A 1 39  ? 9.647   32.932  74.758  1.00 127.01 ?  55  THR B CG2 1 
ATOM   324   N N   . GLU A 1 40  ? 13.469  35.657  75.473  1.00 138.46 ?  56  GLU B N   1 
ATOM   325   C CA  . GLU A 1 40  ? 14.016  37.026  75.650  1.00 139.26 ?  56  GLU B CA  1 
ATOM   326   C C   . GLU A 1 40  ? 12.826  37.970  75.501  1.00 133.10 ?  56  GLU B C   1 
ATOM   327   O O   . GLU A 1 40  ? 12.738  38.943  76.268  1.00 128.97 ?  56  GLU B O   1 
ATOM   328   C CB  . GLU A 1 40  ? 15.068  37.371  74.602  1.00 147.62 ?  56  GLU B CB  1 
ATOM   329   C CG  . GLU A 1 40  ? 15.625  38.769  74.770  1.00 149.64 ?  56  GLU B CG  1 
ATOM   330   C CD  . GLU A 1 40  ? 16.243  39.027  76.131  1.00 145.72 ?  56  GLU B CD  1 
ATOM   331   O OE1 . GLU A 1 40  ? 16.831  38.088  76.702  1.00 146.07 ?  56  GLU B OE1 1 
ATOM   332   O OE2 . GLU A 1 40  ? 16.137  40.169  76.610  1.00 140.37 -1 56  GLU B OE2 1 
ATOM   333   N N   . GLU A 1 41  ? 11.912  37.664  74.569  1.00 133.97 ?  57  GLU B N   1 
ATOM   334   C CA  . GLU A 1 41  ? 10.740  38.533  74.504  1.00 130.43 ?  57  GLU B CA  1 
ATOM   335   C C   . GLU A 1 41  ? 10.092  38.716  75.876  1.00 128.57 ?  57  GLU B C   1 
ATOM   336   O O   . GLU A 1 41  ? 9.760   39.840  76.283  1.00 128.12 ?  57  GLU B O   1 
ATOM   337   C CB  . GLU A 1 41  ? 9.737   37.951  73.505  1.00 132.27 ?  57  GLU B CB  1 
ATOM   338   C CG  . GLU A 1 41  ? 8.361   38.620  73.516  1.00 133.88 ?  57  GLU B CG  1 
ATOM   339   C CD  . GLU A 1 41  ? 7.377   37.961  72.546  1.00 141.53 ?  57  GLU B CD  1 
ATOM   340   O OE1 . GLU A 1 41  ? 7.459   36.724  72.373  1.00 141.79 ?  57  GLU B OE1 1 
ATOM   341   O OE2 . GLU A 1 41  ? 6.493   38.662  71.995  1.00 145.63 -1 57  GLU B OE2 1 
ATOM   342   N N   . ASN A 1 42  ? 9.907   37.621  76.616  1.00 130.78 ?  58  ASN B N   1 
ATOM   343   C CA  . ASN A 1 42  ? 9.162   37.745  77.863  1.00 127.53 ?  58  ASN B CA  1 
ATOM   344   C C   . ASN A 1 42  ? 10.031  38.297  78.993  1.00 126.37 ?  58  ASN B C   1 
ATOM   345   O O   . ASN A 1 42  ? 9.489   38.882  79.944  1.00 120.49 ?  58  ASN B O   1 
ATOM   346   C CB  . ASN A 1 42  ? 8.545   36.397  78.244  1.00 123.99 ?  58  ASN B CB  1 
ATOM   347   C CG  . ASN A 1 42  ? 7.294   36.079  77.436  1.00 125.17 ?  58  ASN B CG  1 
ATOM   348   O OD1 . ASN A 1 42  ? 6.530   36.966  77.051  1.00 127.53 ?  58  ASN B OD1 1 
ATOM   349   N ND2 . ASN A 1 42  ? 7.094   34.805  77.161  1.00 127.01 ?  58  ASN B ND2 1 
ATOM   350   N N   . VAL A 1 43  ? 11.364  38.137  78.897  1.00 128.60 ?  59  VAL B N   1 
ATOM   351   C CA  . VAL A 1 43  ? 12.289  38.923  79.725  1.00 125.54 ?  59  VAL B CA  1 
ATOM   352   C C   . VAL A 1 43  ? 12.033  40.406  79.518  1.00 121.37 ?  59  VAL B C   1 
ATOM   353   O O   . VAL A 1 43  ? 11.950  41.194  80.470  1.00 117.24 ?  59  VAL B O   1 
ATOM   354   C CB  . VAL A 1 43  ? 13.764  38.607  79.392  1.00 127.71 ?  59  VAL B CB  1 
ATOM   355   C CG1 . VAL A 1 43  ? 14.678  39.327  80.361  1.00 119.00 ?  59  VAL B CG1 1 
ATOM   356   C CG2 . VAL A 1 43  ? 14.075  37.133  79.376  1.00 131.90 ?  59  VAL B CG2 1 
ATOM   357   N N   . GLN A 1 44  ? 11.948  40.811  78.255  1.00 122.70 ?  60  GLN B N   1 
ATOM   358   C CA  . GLN A 1 44  ? 11.763  42.221  77.951  1.00 123.01 ?  60  GLN B CA  1 
ATOM   359   C C   . GLN A 1 44  ? 10.450  42.724  78.548  1.00 119.26 ?  60  GLN B C   1 
ATOM   360   O O   . GLN A 1 44  ? 10.408  43.792  79.171  1.00 117.20 ?  60  GLN B O   1 
ATOM   361   C CB  . GLN A 1 44  ? 11.798  42.414  76.429  1.00 129.48 ?  60  GLN B CB  1 
ATOM   362   C CG  . GLN A 1 44  ? 13.185  42.743  75.808  1.00 135.29 ?  60  GLN B CG  1 
ATOM   363   C CD  . GLN A 1 44  ? 13.898  43.943  76.420  1.00 138.91 ?  60  GLN B CD  1 
ATOM   364   O OE1 . GLN A 1 44  ? 14.959  43.805  77.038  1.00 135.89 ?  60  GLN B OE1 1 
ATOM   365   N NE2 . GLN A 1 44  ? 13.340  45.129  76.213  1.00 137.13 ?  60  GLN B NE2 1 
ATOM   366   N N   . ASN A 1 45  ? 9.373   41.939  78.409  1.00 122.20 ?  61  ASN B N   1 
ATOM   367   C CA  . ASN A 1 45  ? 8.076   42.378  78.932  1.00 118.41 ?  61  ASN B CA  1 
ATOM   368   C C   . ASN A 1 45  ? 8.070   42.443  80.456  1.00 115.54 ?  61  ASN B C   1 
ATOM   369   O O   . ASN A 1 45  ? 7.541   43.401  81.037  1.00 113.99 ?  61  ASN B O   1 
ATOM   370   C CB  . ASN A 1 45  ? 6.940   41.482  78.432  1.00 120.07 ?  61  ASN B CB  1 
ATOM   371   C CG  . ASN A 1 45  ? 6.849   41.434  76.923  1.00 123.05 ?  61  ASN B CG  1 
ATOM   372   O OD1 . ASN A 1 45  ? 6.036   42.141  76.331  1.00 116.87 ?  61  ASN B OD1 1 
ATOM   373   N ND2 . ASN A 1 45  ? 7.638   40.566  76.295  1.00 127.20 ?  61  ASN B ND2 1 
ATOM   374   N N   . MET A 1 46  ? 8.626   41.426  81.123  1.00 118.63 ?  62  MET B N   1 
ATOM   375   C CA  . MET A 1 46  ? 8.723   41.463  82.583  1.00 118.44 ?  62  MET B CA  1 
ATOM   376   C C   . MET A 1 46  ? 9.460   42.707  83.058  1.00 116.77 ?  62  MET B C   1 
ATOM   377   O O   . MET A 1 46  ? 9.023   43.381  83.996  1.00 115.22 ?  62  MET B O   1 
ATOM   378   C CB  . MET A 1 46  ? 9.433   40.214  83.097  1.00 115.60 ?  62  MET B CB  1 
ATOM   379   C CG  . MET A 1 46  ? 9.574   40.185  84.590  1.00 109.44 ?  62  MET B CG  1 
ATOM   380   S SD  . MET A 1 46  ? 10.516  38.752  85.077  1.00 114.01 ?  62  MET B SD  1 
ATOM   381   C CE  . MET A 1 46  ? 10.491  38.909  86.874  1.00 119.57 ?  62  MET B CE  1 
ATOM   382   N N   . ASN A 1 47  ? 10.593  43.023  82.428  1.00 116.65 ?  63  ASN B N   1 
ATOM   383   C CA  . ASN A 1 47  ? 11.345  44.200  82.852  1.00 113.68 ?  63  ASN B CA  1 
ATOM   384   C C   . ASN A 1 47  ? 10.556  45.493  82.629  1.00 109.11 ?  63  ASN B C   1 
ATOM   385   O O   . ASN A 1 47  ? 10.532  46.351  83.507  1.00 107.56 ?  63  ASN B O   1 
ATOM   386   C CB  . ASN A 1 47  ? 12.709  44.254  82.149  1.00 120.12 ?  63  ASN B CB  1 
ATOM   387   C CG  . ASN A 1 47  ? 13.725  43.234  82.711  1.00 121.21 ?  63  ASN B CG  1 
ATOM   388   O OD1 . ASN A 1 47  ? 13.778  42.970  83.921  1.00 112.91 ?  63  ASN B OD1 1 
ATOM   389   N ND2 . ASN A 1 47  ? 14.548  42.679  81.821  1.00 121.21 ?  63  ASN B ND2 1 
ATOM   390   N N   . ASN A 1 48  ? 9.895   45.655  81.474  1.00 111.53 ?  64  ASN B N   1 
ATOM   391   C CA  . ASN A 1 48  ? 9.134   46.894  81.225  1.00 107.90 ?  64  ASN B CA  1 
ATOM   392   C C   . ASN A 1 48  ? 7.964   47.066  82.192  1.00 103.49 ?  64  ASN B C   1 
ATOM   393   O O   . ASN A 1 48  ? 7.685   48.185  82.655  1.00 99.16  ?  64  ASN B O   1 
ATOM   394   C CB  . ASN A 1 48  ? 8.627   46.928  79.785  1.00 111.93 ?  64  ASN B CB  1 
ATOM   395   C CG  . ASN A 1 48  ? 9.746   46.813  78.774  1.00 117.78 ?  64  ASN B CG  1 
ATOM   396   O OD1 . ASN A 1 48  ? 10.880  47.210  79.051  1.00 116.81 ?  64  ASN B OD1 1 
ATOM   397   N ND2 . ASN A 1 48  ? 9.446   46.248  77.602  1.00 121.04 ?  64  ASN B ND2 1 
ATOM   398   N N   . ALA A 1 49  ? 7.277   45.970  82.523  1.00 109.60 ?  65  ALA B N   1 
ATOM   399   C CA  . ALA A 1 49  ? 6.156   46.044  83.464  1.00 106.63 ?  65  ALA B CA  1 
ATOM   400   C C   . ALA A 1 49  ? 6.634   46.306  84.894  1.00 100.08 ?  65  ALA B C   1 
ATOM   401   O O   . ALA A 1 49  ? 6.075   47.159  85.612  1.00 95.72  ?  65  ALA B O   1 
ATOM   402   C CB  . ALA A 1 49  ? 5.342   44.751  83.395  1.00 102.03 ?  65  ALA B CB  1 
ATOM   403   N N   . GLY A 1 50  ? 7.664   45.576  85.325  1.00 107.72 ?  66  GLY B N   1 
ATOM   404   C CA  . GLY A 1 50  ? 8.275   45.871  86.603  1.00 105.32 ?  66  GLY B CA  1 
ATOM   405   C C   . GLY A 1 50  ? 8.750   47.306  86.704  1.00 98.79  ?  66  GLY B C   1 
ATOM   406   O O   . GLY A 1 50  ? 8.580   47.948  87.734  1.00 94.86  ?  66  GLY B O   1 
ATOM   407   N N   . ASP A 1 51  ? 9.352   47.826  85.638  1.00 97.71  ?  67  ASP B N   1 
ATOM   408   C CA  . ASP A 1 51  ? 9.803   49.213  85.640  1.00 98.70  ?  67  ASP B CA  1 
ATOM   409   C C   . ASP A 1 51  ? 8.650   50.172  85.904  1.00 90.81  ?  67  ASP B C   1 
ATOM   410   O O   . ASP A 1 51  ? 8.743   51.030  86.793  1.00 85.70  ?  67  ASP B O   1 
ATOM   411   C CB  . ASP A 1 51  ? 10.504  49.536  84.316  1.00 101.20 ?  67  ASP B CB  1 
ATOM   412   C CG  . ASP A 1 51  ? 11.914  48.970  84.243  1.00 110.11 ?  67  ASP B CG  1 
ATOM   413   O OD1 . ASP A 1 51  ? 12.428  48.536  85.299  1.00 116.48 ?  67  ASP B OD1 1 
ATOM   414   O OD2 . ASP A 1 51  ? 12.491  48.930  83.126  1.00 114.55 -1 67  ASP B OD2 1 
ATOM   415   N N   . LYS A 1 52  ? 7.561   50.065  85.122  1.00 93.35  ?  68  LYS B N   1 
ATOM   416   C CA  . LYS A 1 52  ? 6.444   51.004  85.306  1.00 86.97  ?  68  LYS B CA  1 
ATOM   417   C C   . LYS A 1 52  ? 5.909   50.950  86.737  1.00 79.50  ?  68  LYS B C   1 
ATOM   418   O O   . LYS A 1 52  ? 5.584   51.987  87.336  1.00 70.41  ?  68  LYS B O   1 
ATOM   419   C CB  . LYS A 1 52  ? 5.313   50.711  84.308  1.00 87.73  ?  68  LYS B CB  1 
ATOM   420   C CG  . LYS A 1 52  ? 5.674   50.855  82.833  1.00 88.44  ?  68  LYS B CG  1 
ATOM   421   C CD  . LYS A 1 52  ? 4.430   50.820  81.940  1.00 93.44  ?  68  LYS B CD  1 
ATOM   422   C CE  . LYS A 1 52  ? 4.812   50.826  80.442  1.00 97.47  ?  68  LYS B CE  1 
ATOM   423   N NZ  . LYS A 1 52  ? 3.678   51.036  79.473  1.00 90.42  ?  68  LYS B NZ  1 
ATOM   424   N N   . TRP A 1 53  ? 5.816   49.737  87.300  1.00 84.54  ?  69  TRP B N   1 
ATOM   425   C CA  . TRP A 1 53  ? 5.337   49.574  88.675  1.00 78.08  ?  69  TRP B CA  1 
ATOM   426   C C   . TRP A 1 53  ? 6.285   50.187  89.697  1.00 76.62  ?  69  TRP B C   1 
ATOM   427   O O   . TRP A 1 53  ? 5.830   50.840  90.638  1.00 69.92  ?  69  TRP B O   1 
ATOM   428   C CB  . TRP A 1 53  ? 5.117   48.092  88.967  1.00 77.67  ?  69  TRP B CB  1 
ATOM   429   C CG  . TRP A 1 53  ? 4.947   47.705  90.419  1.00 71.84  ?  69  TRP B CG  1 
ATOM   430   C CD1 . TRP A 1 53  ? 5.751   46.881  91.130  1.00 74.61  ?  69  TRP B CD1 1 
ATOM   431   C CD2 . TRP A 1 53  ? 3.894   48.111  91.318  1.00 74.24  ?  69  TRP B CD2 1 
ATOM   432   N NE1 . TRP A 1 53  ? 5.274   46.743  92.411  1.00 75.91  ?  69  TRP B NE1 1 
ATOM   433   C CE2 . TRP A 1 53  ? 4.138   47.491  92.552  1.00 72.35  ?  69  TRP B CE2 1 
ATOM   434   C CE3 . TRP A 1 53  ? 2.768   48.943  91.194  1.00 74.10  ?  69  TRP B CE3 1 
ATOM   435   C CZ2 . TRP A 1 53  ? 3.306   47.670  93.659  1.00 68.97  ?  69  TRP B CZ2 1 
ATOM   436   C CZ3 . TRP A 1 53  ? 1.936   49.124  92.309  1.00 67.51  ?  69  TRP B CZ3 1 
ATOM   437   C CH2 . TRP A 1 53  ? 2.213   48.486  93.519  1.00 66.58  ?  69  TRP B CH2 1 
ATOM   438   N N   . SER A 1 54  ? 7.597   49.969  89.553  1.00 83.18  ?  70  SER B N   1 
ATOM   439   C CA  . SER A 1 54  ? 8.566   50.640  90.425  1.00 76.76  ?  70  SER B CA  1 
ATOM   440   C C   . SER A 1 54  ? 8.387   52.144  90.380  1.00 71.56  ?  70  SER B C   1 
ATOM   441   O O   . SER A 1 54  ? 8.359   52.802  91.424  1.00 69.74  ?  70  SER B O   1 
ATOM   442   C CB  . SER A 1 54  ? 10.002  50.279  90.038  1.00 81.07  ?  70  SER B CB  1 
ATOM   443   O OG  . SER A 1 54  ? 10.341  48.972  90.466  1.00 87.06  ?  70  SER B OG  1 
ATOM   444   N N   . ALA A 1 55  ? 8.258   52.698  89.167  1.00 79.03  ?  71  ALA B N   1 
ATOM   445   C CA  . ALA A 1 55  ? 8.174   54.151  88.985  1.00 75.76  ?  71  ALA B CA  1 
ATOM   446   C C   . ALA A 1 55  ? 6.896   54.724  89.590  1.00 73.76  ?  71  ALA B C   1 
ATOM   447   O O   . ALA A 1 55  ? 6.892   55.838  90.137  1.00 67.82  ?  71  ALA B O   1 
ATOM   448   C CB  . ALA A 1 55  ? 8.264   54.483  87.497  1.00 77.74  ?  71  ALA B CB  1 
ATOM   449   N N   . PHE A 1 56  ? 5.802   53.964  89.498  1.00 75.40  ?  72  PHE B N   1 
ATOM   450   C CA  . PHE A 1 56  ? 4.557   54.330  90.165  1.00 69.73  ?  72  PHE B CA  1 
ATOM   451   C C   . PHE A 1 56  ? 4.673   54.276  91.684  1.00 68.96  ?  72  PHE B C   1 
ATOM   452   O O   . PHE A 1 56  ? 4.125   55.131  92.379  1.00 69.07  ?  72  PHE B O   1 
ATOM   453   C CB  . PHE A 1 56  ? 3.439   53.409  89.695  1.00 66.21  ?  72  PHE B CB  1 
ATOM   454   C CG  . PHE A 1 56  ? 2.203   53.528  90.511  1.00 63.46  ?  72  PHE B CG  1 
ATOM   455   C CD1 . PHE A 1 56  ? 1.402   54.656  90.414  1.00 63.19  ?  72  PHE B CD1 1 
ATOM   456   C CD2 . PHE A 1 56  ? 1.848   52.519  91.400  1.00 63.93  ?  72  PHE B CD2 1 
ATOM   457   C CE1 . PHE A 1 56  ? 0.258   54.775  91.165  1.00 59.33  ?  72  PHE B CE1 1 
ATOM   458   C CE2 . PHE A 1 56  ? 0.707   52.630  92.155  1.00 62.02  ?  72  PHE B CE2 1 
ATOM   459   C CZ  . PHE A 1 56  ? -0.092  53.764  92.039  1.00 62.86  ?  72  PHE B CZ  1 
ATOM   460   N N   . LEU A 1 57  ? 5.316   53.245  92.228  1.00 72.56  ?  73  LEU B N   1 
ATOM   461   C CA  . LEU A 1 57  ? 5.531   53.227  93.673  1.00 72.55  ?  73  LEU B CA  1 
ATOM   462   C C   . LEU A 1 57  ? 6.323   54.439  94.114  1.00 73.13  ?  73  LEU B C   1 
ATOM   463   O O   . LEU A 1 57  ? 5.940   55.114  95.070  1.00 67.98  ?  73  LEU B O   1 
ATOM   464   C CB  . LEU A 1 57  ? 6.239   51.951  94.129  1.00 72.26  ?  73  LEU B CB  1 
ATOM   465   C CG  . LEU A 1 57  ? 5.305   50.772  94.340  1.00 66.26  ?  73  LEU B CG  1 
ATOM   466   C CD1 . LEU A 1 57  ? 6.083   49.516  94.679  1.00 66.26  ?  73  LEU B CD1 1 
ATOM   467   C CD2 . LEU A 1 57  ? 4.331   51.146  95.432  1.00 61.18  ?  73  LEU B CD2 1 
ATOM   468   N N   . LYS A 1 58  ? 7.452   54.702  93.453  1.00 70.10  ?  74  LYS B N   1 
ATOM   469   C CA  . LYS A 1 58  ? 8.254   55.869  93.816  1.00 73.48  ?  74  LYS B CA  1 
ATOM   470   C C   . LYS A 1 58  ? 7.412   57.134  93.747  1.00 72.34  ?  74  LYS B C   1 
ATOM   471   O O   . LYS A 1 58  ? 7.478   57.999  94.631  1.00 73.36  ?  74  LYS B O   1 
ATOM   472   C CB  . LYS A 1 58  ? 9.506   55.961  92.923  1.00 80.26  ?  74  LYS B CB  1 
ATOM   473   C CG  . LYS A 1 58  ? 10.606  56.953  93.408  1.00 95.56  ?  74  LYS B CG  1 
ATOM   474   C CD  . LYS A 1 58  ? 11.950  56.910  92.605  1.00 104.70 ?  74  LYS B CD  1 
ATOM   475   C CE  . LYS A 1 58  ? 12.740  55.591  92.729  1.00 112.41 ?  74  LYS B CE  1 
ATOM   476   N NZ  . LYS A 1 58  ? 13.091  55.232  94.154  1.00 106.72 ?  74  LYS B NZ  1 
ATOM   477   N N   . GLU A 1 59  ? 6.545   57.224  92.746  1.00 77.75  ?  75  GLU B N   1 
ATOM   478   C CA  . GLU A 1 59  ? 5.790   58.460  92.581  1.00 78.68  ?  75  GLU B CA  1 
ATOM   479   C C   . GLU A 1 59  ? 4.683   58.613  93.630  1.00 72.75  ?  75  GLU B C   1 
ATOM   480   O O   . GLU A 1 59  ? 4.477   59.705  94.173  1.00 73.33  ?  75  GLU B O   1 
ATOM   481   C CB  . GLU A 1 59  ? 5.254   58.530  91.147  1.00 84.98  ?  75  GLU B CB  1 
ATOM   482   C CG  . GLU A 1 59  ? 4.210   59.581  90.925  1.00 92.59  ?  75  GLU B CG  1 
ATOM   483   C CD  . GLU A 1 59  ? 4.747   60.995  91.162  1.00 104.59 ?  75  GLU B CD  1 
ATOM   484   O OE1 . GLU A 1 59  ? 5.968   61.171  91.391  1.00 107.10 ?  75  GLU B OE1 1 
ATOM   485   O OE2 . GLU A 1 59  ? 3.946   61.952  91.097  1.00 110.29 -1 75  GLU B OE2 1 
ATOM   486   N N   . GLN A 1 60  ? 4.003   57.526  93.989  1.00 70.84  ?  76  GLN B N   1 
ATOM   487   C CA  . GLN A 1 60  ? 2.987   57.645  95.024  1.00 67.36  ?  76  GLN B CA  1 
ATOM   488   C C   . GLN A 1 60  ? 3.617   57.793  96.388  1.00 73.63  ?  76  GLN B C   1 
ATOM   489   O O   . GLN A 1 60  ? 3.052   58.462  97.254  1.00 77.36  ?  76  GLN B O   1 
ATOM   490   C CB  . GLN A 1 60  ? 2.056   56.442  95.064  1.00 63.13  ?  76  GLN B CB  1 
ATOM   491   C CG  . GLN A 1 60  ? 1.174   56.313  93.862  1.00 65.03  ?  76  GLN B CG  1 
ATOM   492   C CD  . GLN A 1 60  ? 0.119   57.394  93.717  1.00 63.53  ?  76  GLN B CD  1 
ATOM   493   O OE1 . GLN A 1 60  ? -0.725  57.613  94.593  1.00 61.22  ?  76  GLN B OE1 1 
ATOM   494   N NE2 . GLN A 1 60  ? 0.148   58.064  92.569  1.00 68.33  ?  76  GLN B NE2 1 
ATOM   495   N N   . SER A 1 61  ? 4.763   57.143  96.614  1.00 77.18  ?  77  SER B N   1 
ATOM   496   C CA  . SER A 1 61  ? 5.514   57.372  97.839  1.00 73.90  ?  77  SER B CA  1 
ATOM   497   C C   . SER A 1 61  ? 5.763   58.854  98.013  1.00 81.26  ?  77  SER B C   1 
ATOM   498   O O   . SER A 1 61  ? 5.314   59.447  98.993  1.00 83.34  ?  77  SER B O   1 
ATOM   499   C CB  . SER A 1 61  ? 6.827   56.592  97.806  1.00 76.57  ?  77  SER B CB  1 
ATOM   500   O OG  . SER A 1 61  ? 7.538   56.705  99.017  1.00 81.14  ?  77  SER B OG  1 
ATOM   501   N N   . THR A 1 62  ? 6.412   59.487  97.022  1.00 84.86  ?  78  THR B N   1 
ATOM   502   C CA  . THR A 1 62  ? 6.682   60.922  97.131  1.00 85.85  ?  78  THR B CA  1 
ATOM   503   C C   . THR A 1 62  ? 5.397   61.720  97.290  1.00 78.97  ?  78  THR B C   1 
ATOM   504   O O   . THR A 1 62  ? 5.404   62.782  97.929  1.00 82.98  ?  78  THR B O   1 
ATOM   505   C CB  . THR A 1 62  ? 7.476   61.424  95.921  1.00 86.38  ?  78  THR B CB  1 
ATOM   506   O OG1 . THR A 1 62  ? 8.695   60.676  95.802  1.00 96.34  ?  78  THR B OG1 1 
ATOM   507   C CG2 . THR A 1 62  ? 7.838   62.889  96.097  1.00 89.24  ?  78  THR B CG2 1 
ATOM   508   N N   . LEU A 1 63  ? 4.284   61.218  96.751  1.00 81.19  ?  79  LEU B N   1 
ATOM   509   C CA  . LEU A 1 63  ? 3.018   61.924  96.938  1.00 83.96  ?  79  LEU B CA  1 
ATOM   510   C C   . LEU A 1 63  ? 2.467   61.747  98.331  1.00 82.00  ?  79  LEU B C   1 
ATOM   511   O O   . LEU A 1 63  ? 1.650   62.553  98.782  1.00 79.82  ?  79  LEU B O   1 
ATOM   512   C CB  . LEU A 1 63  ? 1.978   61.443  95.940  1.00 73.28  ?  79  LEU B CB  1 
ATOM   513   C CG  . LEU A 1 63  ? 2.025   62.266  94.689  1.00 72.26  ?  79  LEU B CG  1 
ATOM   514   C CD1 . LEU A 1 63  ? 1.281   61.514  93.664  1.00 81.97  ?  79  LEU B CD1 1 
ATOM   515   C CD2 . LEU A 1 63  ? 1.332   63.546  95.008  1.00 71.04  ?  79  LEU B CD2 1 
ATOM   516   N N   . ALA A 1 64  ? 2.780   60.631  98.972  1.00 86.38  ?  80  ALA B N   1 
ATOM   517   C CA  . ALA A 1 64  ? 2.099   60.318  100.249 1.00 88.73  ?  80  ALA B CA  1 
ATOM   518   C C   . ALA A 1 64  ? 2.817   60.903  101.454 1.00 94.36  ?  80  ALA B C   1 
ATOM   519   O O   . ALA A 1 64  ? 2.231   60.890  102.576 1.00 92.60  ?  80  ALA B O   1 
ATOM   520   C CB  . ALA A 1 64  ? 1.993   58.821  100.350 1.00 90.25  ?  80  ALA B CB  1 
ATOM   521   N N   . GLN A 1 65  ? 4.058   61.350  101.255 1.00 102.74 ?  81  GLN B N   1 
ATOM   522   C CA  . GLN A 1 65  ? 4.858   61.913  102.374 1.00 94.44  ?  81  GLN B CA  1 
ATOM   523   C C   . GLN A 1 65  ? 4.362   63.334  102.605 1.00 93.36  ?  81  GLN B C   1 
ATOM   524   O O   . GLN A 1 65  ? 5.076   64.095  103.271 1.00 101.91 ?  81  GLN B O   1 
ATOM   525   C CB  . GLN A 1 65  ? 6.351   61.837  102.044 1.00 89.05  ?  81  GLN B CB  1 
ATOM   526   C CG  . GLN A 1 65  ? 7.001   60.487  102.329 1.00 91.58  ?  81  GLN B CG  1 
ATOM   527   C CD  . GLN A 1 65  ? 8.319   60.246  101.622 1.00 111.22 ?  81  GLN B CD  1 
ATOM   528   O OE1 . GLN A 1 65  ? 9.075   61.167  101.330 1.00 114.81 ?  81  GLN B OE1 1 
ATOM   529   N NE2 . GLN A 1 65  ? 8.603   58.979  101.360 1.00 129.02 ?  81  GLN B NE2 1 
ATOM   530   N N   . MET A 1 66  ? 3.207   63.663  102.023 1.00 108.65 ?  82  MET B N   1 
ATOM   531   C CA  . MET A 1 66  ? 2.604   65.002  102.200 1.00 118.46 ?  82  MET B CA  1 
ATOM   532   C C   . MET A 1 66  ? 1.392   64.866  103.107 1.00 108.97 ?  82  MET B C   1 
ATOM   533   O O   . MET A 1 66  ? 0.620   65.826  103.206 1.00 106.59 ?  82  MET B O   1 
ATOM   534   C CB  . MET A 1 66  ? 2.148   65.563  100.850 1.00 127.80 ?  82  MET B CB  1 
ATOM   535   C CG  . MET A 1 66  ? 3.090   65.221  99.717  1.00 129.75 ?  82  MET B CG  1 
ATOM   536   S SD  . MET A 1 66  ? 2.966   66.357  98.308  1.00 143.76 ?  82  MET B SD  1 
ATOM   537   C CE  . MET A 1 66  ? 4.310   65.757  97.283  1.00 130.68 ?  82  MET B CE  1 
ATOM   538   N N   . TYR A 1 67  ? 1.215   63.688  103.691 1.00 86.72  ?  83  TYR B N   1 
ATOM   539   C CA  . TYR A 1 67  ? 0.108   63.557  104.649 1.00 83.79  ?  83  TYR B CA  1 
ATOM   540   C C   . TYR A 1 67  ? 0.705   62.950  105.906 1.00 85.97  ?  83  TYR B C   1 
ATOM   541   O O   . TYR A 1 67  ? 0.976   61.730  105.927 1.00 84.28  ?  83  TYR B O   1 
ATOM   542   C CB  . TYR A 1 67  ? -1.043  62.646  104.197 1.00 86.65  ?  83  TYR B CB  1 
ATOM   543   C CG  . TYR A 1 67  ? -1.656  62.886  102.829 1.00 84.02  ?  83  TYR B CG  1 
ATOM   544   C CD1 . TYR A 1 67  ? -1.042  62.418  101.684 1.00 83.30  ?  83  TYR B CD1 1 
ATOM   545   C CD2 . TYR A 1 67  ? -2.824  63.601  102.680 1.00 77.18  ?  83  TYR B CD2 1 
ATOM   546   C CE1 . TYR A 1 67  ? -1.578  62.652  100.440 1.00 80.32  ?  83  TYR B CE1 1 
ATOM   547   C CE2 . TYR A 1 67  ? -3.347  63.846  101.439 1.00 77.74  ?  83  TYR B CE2 1 
ATOM   548   C CZ  . TYR A 1 67  ? -2.722  63.363  100.320 1.00 75.17  ?  83  TYR B CZ  1 
ATOM   549   O OH  . TYR A 1 67  ? -3.228  63.575  99.054  1.00 79.40  ?  83  TYR B OH  1 
ATOM   550   N N   . PRO A 1 68  ? 0.885   63.721  106.978 1.00 90.54  ?  84  PRO B N   1 
ATOM   551   C CA  . PRO A 1 68  ? 1.799   63.308  108.059 1.00 83.74  ?  84  PRO B CA  1 
ATOM   552   C C   . PRO A 1 68  ? 1.146   62.357  109.060 1.00 84.76  ?  84  PRO B C   1 
ATOM   553   O O   . PRO A 1 68  ? 0.125   62.688  109.670 1.00 86.36  ?  84  PRO B O   1 
ATOM   554   C CB  . PRO A 1 68  ? 2.167   64.639  108.725 1.00 82.54  ?  84  PRO B CB  1 
ATOM   555   C CG  . PRO A 1 68  ? 0.986   65.475  108.512 1.00 86.62  ?  84  PRO B CG  1 
ATOM   556   C CD  . PRO A 1 68  ? 0.416   65.097  107.164 1.00 91.99  ?  84  PRO B CD  1 
ATOM   557   N N   . LEU A 1 69  ? 1.782   61.190  109.273 1.00 84.69  ?  85  LEU B N   1 
ATOM   558   C CA  . LEU A 1 69  ? 1.239   60.177  110.191 1.00 82.85  ?  85  LEU B CA  1 
ATOM   559   C C   . LEU A 1 69  ? 0.915   60.771  111.547 1.00 87.43  ?  85  LEU B C   1 
ATOM   560   O O   . LEU A 1 69  ? 0.034   60.280  112.259 1.00 88.42  ?  85  LEU B O   1 
ATOM   561   C CB  . LEU A 1 69  ? 2.213   59.011  110.404 1.00 71.03  ?  85  LEU B CB  1 
ATOM   562   C CG  . LEU A 1 69  ? 2.823   58.269  109.229 1.00 73.49  ?  85  LEU B CG  1 
ATOM   563   C CD1 . LEU A 1 69  ? 3.860   57.260  109.646 1.00 75.67  ?  85  LEU B CD1 1 
ATOM   564   C CD2 . LEU A 1 69  ? 1.726   57.551  108.557 1.00 79.66  ?  85  LEU B CD2 1 
ATOM   565   N N   . GLN A 1 70  ? 1.642   61.810  111.932 1.00 93.98  ?  86  GLN B N   1 
ATOM   566   C CA  . GLN A 1 70  ? 1.448   62.417  113.237 1.00 98.66  ?  86  GLN B CA  1 
ATOM   567   C C   . GLN A 1 70  ? 0.001   62.883  113.404 1.00 95.65  ?  86  GLN B C   1 
ATOM   568   O O   . GLN A 1 70  ? -0.609  62.661  114.454 1.00 95.38  ?  86  GLN B O   1 
ATOM   569   C CB  . GLN A 1 70  ? 2.543   63.494  113.393 1.00 99.32  ?  86  GLN B CB  1 
ATOM   570   C CG  . GLN A 1 70  ? 2.753   64.170  114.727 1.00 106.83 ?  86  GLN B CG  1 
ATOM   571   C CD  . GLN A 1 70  ? 2.179   65.591  114.774 1.00 115.05 ?  86  GLN B CD  1 
ATOM   572   O OE1 . GLN A 1 70  ? 1.995   66.224  113.732 1.00 117.16 ?  86  GLN B OE1 1 
ATOM   573   N NE2 . GLN A 1 70  ? 1.913   66.101  115.976 1.00 119.04 ?  86  GLN B NE2 1 
ATOM   574   N N   . GLU A 1 71  ? -0.609  63.386  112.329 1.00 103.34 ?  87  GLU B N   1 
ATOM   575   C CA  . GLU A 1 71  ? -1.971  63.897  112.346 1.00 102.04 ?  87  GLU B CA  1 
ATOM   576   C C   . GLU A 1 71  ? -2.997  62.873  111.894 1.00 97.93  ?  87  GLU B C   1 
ATOM   577   O O   . GLU A 1 71  ? -4.057  63.253  111.377 1.00 97.26  ?  87  GLU B O   1 
ATOM   578   C CB  . GLU A 1 71  ? -2.074  65.126  111.457 1.00 103.89 ?  87  GLU B CB  1 
ATOM   579   C CG  . GLU A 1 71  ? -1.291  66.301  111.920 1.00 113.27 ?  87  GLU B CG  1 
ATOM   580   C CD  . GLU A 1 71  ? -1.308  67.388  110.887 1.00 125.82 ?  87  GLU B CD  1 
ATOM   581   O OE1 . GLU A 1 71  ? -2.282  68.170  110.824 1.00 135.81 ?  87  GLU B OE1 1 
ATOM   582   O OE2 . GLU A 1 71  ? -0.301  67.456  110.139 1.00 127.98 -1 87  GLU B OE2 1 
ATOM   583   N N   . ILE A 1 72  ? -2.714  61.589  112.047 1.00 94.06  ?  88  ILE B N   1 
ATOM   584   C CA  . ILE A 1 72  ? -3.588  60.528  111.570 1.00 88.30  ?  88  ILE B CA  1 
ATOM   585   C C   . ILE A 1 72  ? -3.851  59.560  112.696 1.00 91.85  ?  88  ILE B C   1 
ATOM   586   O O   . ILE A 1 72  ? -2.914  59.027  113.295 1.00 94.04  ?  88  ILE B O   1 
ATOM   587   C CB  . ILE A 1 72  ? -2.990  59.797  110.362 1.00 83.68  ?  88  ILE B CB  1 
ATOM   588   C CG1 . ILE A 1 72  ? -2.636  60.840  109.304 1.00 89.23  ?  88  ILE B CG1 1 
ATOM   589   C CG2 . ILE A 1 72  ? -3.885  58.685  109.919 1.00 81.31  ?  88  ILE B CG2 1 
ATOM   590   C CD1 . ILE A 1 72  ? -2.364  60.300  107.951 1.00 90.73  ?  88  ILE B CD1 1 
ATOM   591   N N   . GLN A 1 73  ? -5.118  59.330  112.978 1.00 88.41  ?  89  GLN B N   1 
ATOM   592   C CA  . GLN A 1 73  ? -5.558  58.523  114.104 1.00 85.66  ?  89  GLN B CA  1 
ATOM   593   C C   . GLN A 1 73  ? -6.512  57.483  113.586 1.00 87.16  ?  89  GLN B C   1 
ATOM   594   O O   . GLN A 1 73  ? -7.705  57.619  113.814 1.00 94.89  ?  89  GLN B O   1 
ATOM   595   C CB  . GLN A 1 73  ? -6.214  59.374  115.132 1.00 90.20  ?  89  GLN B CB  1 
ATOM   596   C CG  . GLN A 1 73  ? -5.445  60.609  115.476 1.00 101.20 ?  89  GLN B CG  1 
ATOM   597   C CD  . GLN A 1 73  ? -5.864  61.812  114.660 1.00 105.07 ?  89  GLN B CD  1 
ATOM   598   O OE1 . GLN A 1 73  ? -5.016  62.509  114.095 1.00 110.21 ?  89  GLN B OE1 1 
ATOM   599   N NE2 . GLN A 1 73  ? -7.170  62.054  114.574 1.00 109.81 ?  89  GLN B NE2 1 
ATOM   600   N N   . ASN A 1 74  ? -5.957  56.515  112.847 1.00 79.35  ?  90  ASN B N   1 
ATOM   601   C CA  . ASN A 1 74  ? -6.717  55.384  112.265 1.00 80.40  ?  90  ASN B CA  1 
ATOM   602   C C   . ASN A 1 74  ? -5.640  54.374  111.952 1.00 78.84  ?  90  ASN B C   1 
ATOM   603   O O   . ASN A 1 74  ? -4.881  54.614  111.004 1.00 84.67  ?  90  ASN B O   1 
ATOM   604   C CB  . ASN A 1 74  ? -7.404  55.705  110.949 1.00 81.23  ?  90  ASN B CB  1 
ATOM   605   C CG  . ASN A 1 74  ? -8.248  54.572  110.417 1.00 75.30  ?  90  ASN B CG  1 
ATOM   606   O OD1 . ASN A 1 74  ? -7.797  53.436  110.273 1.00 71.86  ?  90  ASN B OD1 1 
ATOM   607   N ND2 . ASN A 1 74  ? -9.492  54.876  110.123 1.00 75.40  ?  90  ASN B ND2 1 
ATOM   608   N N   . LEU A 1 75  ? -5.538  53.324  112.747 1.00 81.80  ?  91  LEU B N   1 
ATOM   609   C CA  . LEU A 1 75  ? -4.405  52.392  112.569 1.00 80.05  ?  91  LEU B CA  1 
ATOM   610   C C   . LEU A 1 75  ? -4.396  51.797  111.150 1.00 74.91  ?  91  LEU B C   1 
ATOM   611   O O   . LEU A 1 75  ? -3.299  51.672  110.602 1.00 77.66  ?  91  LEU B O   1 
ATOM   612   C CB  . LEU A 1 75  ? -4.471  51.355  113.693 1.00 81.17  ?  91  LEU B CB  1 
ATOM   613   C CG  . LEU A 1 75  ? -4.694  51.945  115.096 1.00 85.47  ?  91  LEU B CG  1 
ATOM   614   C CD1 . LEU A 1 75  ? -4.753  50.870  116.179 1.00 87.91  ?  91  LEU B CD1 1 
ATOM   615   C CD2 . LEU A 1 75  ? -3.641  52.983  115.455 1.00 74.83  ?  91  LEU B CD2 1 
ATOM   616   N N   . THR A 1 76  ? -5.543  51.492  110.542 1.00 71.27  ?  92  THR B N   1 
ATOM   617   C CA  . THR A 1 76  ? -5.437  50.883  109.192 1.00 68.60  ?  92  THR B CA  1 
ATOM   618   C C   . THR A 1 76  ? -4.812  51.909  108.249 1.00 69.98  ?  92  THR B C   1 
ATOM   619   O O   . THR A 1 76  ? -3.861  51.558  107.526 1.00 74.04  ?  92  THR B O   1 
ATOM   620   C CB  . THR A 1 76  ? -6.784  50.379  108.650 1.00 66.93  ?  92  THR B CB  1 
ATOM   621   O OG1 . THR A 1 76  ? -7.835  50.854  109.487 1.00 75.28  ?  92  THR B OG1 1 
ATOM   622   C CG2 . THR A 1 76  ? -6.848  48.867  108.559 1.00 57.16  ?  92  THR B CG2 1 
ATOM   623   N N   . VAL A 1 77  ? -5.314  53.139  108.278 1.00 71.05  ?  93  VAL B N   1 
ATOM   624   C CA  . VAL A 1 77  ? -4.771  54.212  107.403 1.00 70.86  ?  93  VAL B CA  1 
ATOM   625   C C   . VAL A 1 77  ? -3.300  54.397  107.744 1.00 73.05  ?  93  VAL B C   1 
ATOM   626   O O   . VAL A 1 77  ? -2.458  54.266  106.844 1.00 70.08  ?  93  VAL B O   1 
ATOM   627   C CB  . VAL A 1 77  ? -5.557  55.517  107.623 1.00 66.98  ?  93  VAL B CB  1 
ATOM   628   C CG1 . VAL A 1 77  ? -4.904  56.702  106.934 1.00 69.02  ?  93  VAL B CG1 1 
ATOM   629   C CG2 . VAL A 1 77  ? -7.009  55.370  107.187 1.00 60.76  ?  93  VAL B CG2 1 
ATOM   630   N N   . LYS A 1 78  ? -3.014  54.705  109.001 1.00 73.11  ?  94  LYS B N   1 
ATOM   631   C CA  . LYS A 1 78  ? -1.631  54.920  109.413 1.00 72.61  ?  94  LYS B CA  1 
ATOM   632   C C   . LYS A 1 78  ? -0.725  53.792  108.916 1.00 72.21  ?  94  LYS B C   1 
ATOM   633   O O   . LYS A 1 78  ? 0.396   54.035  108.463 1.00 78.74  ?  94  LYS B O   1 
ATOM   634   C CB  . LYS A 1 78  ? -1.616  55.061  110.931 1.00 75.68  ?  94  LYS B CB  1 
ATOM   635   C CG  . LYS A 1 78  ? -0.816  56.208  111.486 1.00 78.75  ?  94  LYS B CG  1 
ATOM   636   C CD  . LYS A 1 78  ? -0.818  56.056  112.990 1.00 81.74  ?  94  LYS B CD  1 
ATOM   637   C CE  . LYS A 1 78  ? 0.059   57.053  113.671 1.00 93.68  ?  94  LYS B CE  1 
ATOM   638   N NZ  . LYS A 1 78  ? 0.393   56.523  115.024 1.00 100.35 ?  94  LYS B NZ  1 
ATOM   639   N N   . LEU A 1 79  ? -1.214  52.555  108.933 1.00 68.89  ?  95  LEU B N   1 
ATOM   640   C CA  . LEU A 1 79  ? -0.412  51.457  108.414 1.00 69.76  ?  95  LEU B CA  1 
ATOM   641   C C   . LEU A 1 79  ? -0.137  51.640  106.938 1.00 65.76  ?  95  LEU B C   1 
ATOM   642   O O   . LEU A 1 79  ? 0.992   51.456  106.472 1.00 68.69  ?  95  LEU B O   1 
ATOM   643   C CB  . LEU A 1 79  ? -1.126  50.139  108.643 1.00 65.77  ?  95  LEU B CB  1 
ATOM   644   C CG  . LEU A 1 79  ? -1.028  49.641  110.066 1.00 62.39  ?  95  LEU B CG  1 
ATOM   645   C CD1 . LEU A 1 79  ? -1.713  48.309  110.083 1.00 59.34  ?  95  LEU B CD1 1 
ATOM   646   C CD2 . LEU A 1 79  ? 0.418   49.551  110.468 1.00 62.62  ?  95  LEU B CD2 1 
ATOM   647   N N   . GLN A 1 80  ? -1.158  52.012  106.176 1.00 62.69  ?  96  GLN B N   1 
ATOM   648   C CA  . GLN A 1 80  ? -0.906  52.121  104.749 1.00 62.12  ?  96  GLN B CA  1 
ATOM   649   C C   . GLN A 1 80  ? -0.013  53.303  104.451 1.00 64.84  ?  96  GLN B C   1 
ATOM   650   O O   . GLN A 1 80  ? 0.834   53.239  103.558 1.00 66.60  ?  96  GLN B O   1 
ATOM   651   C CB  . GLN A 1 80  ? -2.199  52.274  103.978 1.00 61.85  ?  96  GLN B CB  1 
ATOM   652   C CG  . GLN A 1 80  ? -3.085  51.091  104.085 1.00 61.08  ?  96  GLN B CG  1 
ATOM   653   C CD  . GLN A 1 80  ? -4.450  51.464  103.640 1.00 64.32  ?  96  GLN B CD  1 
ATOM   654   O OE1 . GLN A 1 80  ? -4.744  51.472  102.437 1.00 67.93  ?  96  GLN B OE1 1 
ATOM   655   N NE2 . GLN A 1 80  ? -5.246  51.944  104.579 1.00 61.04  ?  96  GLN B NE2 1 
ATOM   656   N N   . LEU A 1 81  ? -0.195  54.396  105.178 1.00 65.18  ?  97  LEU B N   1 
ATOM   657   C CA  . LEU A 1 81  ? 0.574   55.588  104.873 1.00 67.43  ?  97  LEU B CA  1 
ATOM   658   C C   . LEU A 1 81  ? 2.034   55.386  105.234 1.00 68.14  ?  97  LEU B C   1 
ATOM   659   O O   . LEU A 1 81  ? 2.933   55.793  104.486 1.00 67.71  ?  97  LEU B O   1 
ATOM   660   C CB  . LEU A 1 81  ? -0.044  56.774  105.599 1.00 67.64  ?  97  LEU B CB  1 
ATOM   661   C CG  . LEU A 1 81  ? -0.898  57.507  104.580 1.00 66.00  ?  97  LEU B CG  1 
ATOM   662   C CD1 . LEU A 1 81  ? -1.521  58.733  105.124 1.00 73.69  ?  97  LEU B CD1 1 
ATOM   663   C CD2 . LEU A 1 81  ? -0.000  57.874  103.415 1.00 69.89  ?  97  LEU B CD2 1 
ATOM   664   N N   . GLN A 1 82  ? 2.284   54.702  106.348 1.00 70.47  ?  98  GLN B N   1 
ATOM   665   C CA  . GLN A 1 82  ? 3.638   54.354  106.737 1.00 72.26  ?  98  GLN B CA  1 
ATOM   666   C C   . GLN A 1 82  ? 4.271   53.371  105.771 1.00 71.05  ?  98  GLN B C   1 
ATOM   667   O O   . GLN A 1 82  ? 5.467   53.473  105.480 1.00 74.75  ?  98  GLN B O   1 
ATOM   668   C CB  . GLN A 1 82  ? 3.610   53.772  108.130 1.00 74.07  ?  98  GLN B CB  1 
ATOM   669   C CG  . GLN A 1 82  ? 4.960   53.585  108.698 1.00 88.27  ?  98  GLN B CG  1 
ATOM   670   C CD  . GLN A 1 82  ? 4.844   53.306  110.138 1.00 94.49  ?  98  GLN B CD  1 
ATOM   671   O OE1 . GLN A 1 82  ? 3.912   52.612  110.551 1.00 93.92  ?  98  GLN B OE1 1 
ATOM   672   N NE2 . GLN A 1 82  ? 5.786   53.813  110.930 1.00 95.33  ?  98  GLN B NE2 1 
ATOM   673   N N   . ALA A 1 83  ? 3.499   52.397  105.293 1.00 71.17  ?  99  ALA B N   1 
ATOM   674   C CA  . ALA A 1 83  ? 4.015   51.506  104.274 1.00 70.41  ?  99  ALA B CA  1 
ATOM   675   C C   . ALA A 1 83  ? 4.352   52.277  103.013 1.00 68.23  ?  99  ALA B C   1 
ATOM   676   O O   . ALA A 1 83  ? 5.319   51.957  102.320 1.00 71.86  ?  99  ALA B O   1 
ATOM   677   C CB  . ALA A 1 83  ? 2.991   50.406  104.003 1.00 66.04  ?  99  ALA B CB  1 
ATOM   678   N N   . LEU A 1 84  ? 3.581   53.300  102.706 1.00 66.24  ?  100 LEU B N   1 
ATOM   679   C CA  . LEU A 1 84  ? 3.742   53.935  101.421 1.00 66.02  ?  100 LEU B CA  1 
ATOM   680   C C   . LEU A 1 84  ? 4.861   54.954  101.467 1.00 69.73  ?  100 LEU B C   1 
ATOM   681   O O   . LEU A 1 84  ? 5.382   55.331  100.412 1.00 73.96  ?  100 LEU B O   1 
ATOM   682   C CB  . LEU A 1 84  ? 2.424   54.599  101.013 1.00 63.63  ?  100 LEU B CB  1 
ATOM   683   C CG  . LEU A 1 84  ? 2.140   54.857  99.534  1.00 64.41  ?  100 LEU B CG  1 
ATOM   684   C CD1 . LEU A 1 84  ? 2.418   53.612  98.723  1.00 59.02  ?  100 LEU B CD1 1 
ATOM   685   C CD2 . LEU A 1 84  ? 0.745   55.337  99.317  1.00 65.49  ?  100 LEU B CD2 1 
ATOM   686   N N   . GLN A 1 85  ? 5.167   55.460  102.663 1.00 76.45  ?  101 GLN B N   1 
ATOM   687   C CA  . GLN A 1 85  ? 6.133   56.585  102.796 1.00 77.07  ?  101 GLN B CA  1 
ATOM   688   C C   . GLN A 1 85  ? 7.574   56.117  103.008 1.00 79.67  ?  101 GLN B C   1 
ATOM   689   O O   . GLN A 1 85  ? 8.450   56.976  103.094 1.00 89.15  ?  101 GLN B O   1 
ATOM   690   C CB  . GLN A 1 85  ? 5.718   57.474  103.970 1.00 76.50  ?  101 GLN B CB  1 
ATOM   691   C CG  . GLN A 1 85  ? 4.438   58.261  103.726 1.00 76.28  ?  101 GLN B CG  1 
ATOM   692   C CD  . GLN A 1 85  ? 3.900   58.857  105.003 1.00 73.74  ?  101 GLN B CD  1 
ATOM   693   O OE1 . GLN A 1 85  ? 4.307   58.484  106.100 1.00 75.08  ?  101 GLN B OE1 1 
ATOM   694   N NE2 . GLN A 1 85  ? 2.979   59.796  104.866 1.00 76.54  ?  101 GLN B NE2 1 
ATOM   695   N N   . GLN A 1 86  ? 7.818   54.821  103.140 1.00 84.23  ?  102 GLN B N   1 
ATOM   696   C CA  . GLN A 1 86  ? 9.228   54.379  103.232 1.00 87.08  ?  102 GLN B CA  1 
ATOM   697   C C   . GLN A 1 86  ? 9.901   54.786  101.928 1.00 93.73  ?  102 GLN B C   1 
ATOM   698   O O   . GLN A 1 86  ? 9.516   54.228  100.895 1.00 102.23 ?  102 GLN B O   1 
ATOM   699   C CB  . GLN A 1 86  ? 9.332   52.865  103.425 1.00 92.51  ?  102 GLN B CB  1 
ATOM   700   C CG  . GLN A 1 86  ? 8.170   52.071  102.858 1.00 91.64  ?  102 GLN B CG  1 
ATOM   701   C CD  . GLN A 1 86  ? 8.231   50.620  103.267 1.00 97.97  ?  102 GLN B CD  1 
ATOM   702   O OE1 . GLN A 1 86  ? 8.812   50.269  104.291 1.00 106.95 ?  102 GLN B OE1 1 
ATOM   703   N NE2 . GLN A 1 86  ? 7.631   49.757  102.465 1.00 101.91 ?  102 GLN B NE2 1 
ATOM   704   N N   . ASN A 1 87  ? 10.851  55.717  101.957 1.00 93.70  ?  103 ASN B N   1 
ATOM   705   C CA  . ASN A 1 87  ? 11.529  56.032  100.676 1.00 94.24  ?  103 ASN B CA  1 
ATOM   706   C C   . ASN A 1 87  ? 12.697  55.077  100.446 1.00 93.35  ?  103 ASN B C   1 
ATOM   707   O O   . ASN A 1 87  ? 13.315  55.155  99.374  1.00 91.17  ?  103 ASN B O   1 
ATOM   708   C CB  . ASN A 1 87  ? 11.982  57.483  100.542 1.00 93.90  ?  103 ASN B CB  1 
ATOM   709   C CG  . ASN A 1 87  ? 12.035  58.276  101.820 1.00 99.86  ?  103 ASN B CG  1 
ATOM   710   O OD1 . ASN A 1 87  ? 12.152  57.742  102.920 1.00 110.33 ?  103 ASN B OD1 1 
ATOM   711   N ND2 . ASN A 1 87  ? 11.960  59.578  101.643 1.00 96.56  ?  103 ASN B ND2 1 
ATOM   712   N N   . GLY A 1 88  ? 12.983  54.205  101.407 1.00 83.87  ?  104 GLY B N   1 
ATOM   713   C CA  . GLY A 1 88  ? 14.016  53.216  101.174 1.00 83.88  ?  104 GLY B CA  1 
ATOM   714   C C   . GLY A 1 88  ? 15.195  53.692  100.354 1.00 90.31  ?  104 GLY B C   1 
ATOM   715   O O   . GLY A 1 88  ? 15.778  54.745  100.647 1.00 94.10  ?  104 GLY B O   1 
ATOM   716   N N   . SER A 1 89  ? 15.523  52.954  99.291  1.00 85.54  ?  105 SER B N   1 
ATOM   717   C CA  . SER A 1 89  ? 16.783  53.188  98.606  1.00 85.04  ?  105 SER B CA  1 
ATOM   718   C C   . SER A 1 89  ? 16.889  54.588  98.024  1.00 87.51  ?  105 SER B C   1 
ATOM   719   O O   . SER A 1 89  ? 17.994  55.006  97.672  1.00 86.89  ?  105 SER B O   1 
ATOM   720   C CB  . SER A 1 89  ? 16.983  52.170  97.499  1.00 81.91  ?  105 SER B CB  1 
ATOM   721   O OG  . SER A 1 89  ? 17.766  52.753  96.476  1.00 90.02  ?  105 SER B OG  1 
ATOM   722   N N   . SER A 1 90  ? 15.779  55.319  97.921  1.00 94.77  ?  106 SER B N   1 
ATOM   723   C CA  . SER A 1 90  ? 15.775  56.651  97.325  1.00 89.75  ?  106 SER B CA  1 
ATOM   724   C C   . SER A 1 90  ? 16.296  57.721  98.266  1.00 95.86  ?  106 SER B C   1 
ATOM   725   O O   . SER A 1 90  ? 16.596  58.834  97.819  1.00 98.37  ?  106 SER B O   1 
ATOM   726   C CB  . SER A 1 90  ? 14.360  57.041  96.898  1.00 90.65  ?  106 SER B CB  1 
ATOM   727   O OG  . SER A 1 90  ? 13.625  57.555  97.996  1.00 93.44  ?  106 SER B OG  1 
ATOM   728   N N   . VAL A 1 91  ? 16.381  57.431  99.562  1.00 100.79 ?  107 VAL B N   1 
ATOM   729   C CA  . VAL A 1 91  ? 16.826  58.469  100.473 1.00 97.50  ?  107 VAL B CA  1 
ATOM   730   C C   . VAL A 1 91  ? 18.305  58.741  100.315 1.00 97.53  ?  107 VAL B C   1 
ATOM   731   O O   . VAL A 1 91  ? 18.782  59.789  100.756 1.00 100.59 ?  107 VAL B O   1 
ATOM   732   C CB  . VAL A 1 91  ? 16.396  58.037  101.881 1.00 95.54  ?  107 VAL B CB  1 
ATOM   733   C CG1 . VAL A 1 91  ? 17.354  56.982  102.405 1.00 92.15  ?  107 VAL B CG1 1 
ATOM   734   C CG2 . VAL A 1 91  ? 16.294  59.251  102.778 1.00 97.11  ?  107 VAL B CG2 1 
ATOM   735   N N   . LEU A 1 92  ? 19.024  57.828  99.669  1.00 89.73  ?  108 LEU B N   1 
ATOM   736   C CA  . LEU A 1 92  ? 20.405  58.005  99.263  1.00 93.55  ?  108 LEU B CA  1 
ATOM   737   C C   . LEU A 1 92  ? 20.490  58.947  98.069  1.00 98.27  ?  108 LEU B C   1 
ATOM   738   O O   . LEU A 1 92  ? 19.506  59.203  97.380  1.00 98.64  ?  108 LEU B O   1 
ATOM   739   C CB  . LEU A 1 92  ? 21.023  56.668  98.871  1.00 91.96  ?  108 LEU B CB  1 
ATOM   740   C CG  . LEU A 1 92  ? 21.155  55.541  99.887  1.00 89.70  ?  108 LEU B CG  1 
ATOM   741   C CD1 . LEU A 1 92  ? 21.553  54.260  99.185  1.00 88.41  ?  108 LEU B CD1 1 
ATOM   742   C CD2 . LEU A 1 92  ? 22.172  55.897  100.964 1.00 91.23  ?  108 LEU B CD2 1 
ATOM   743   N N   . SER A 1 93  ? 21.690  59.455  97.817  1.00 104.05 ?  109 SER B N   1 
ATOM   744   C CA  . SER A 1 93  ? 21.908  60.266  96.632  1.00 100.88 ?  109 SER B CA  1 
ATOM   745   C C   . SER A 1 93  ? 22.058  59.361  95.426  1.00 101.68 ?  109 SER B C   1 
ATOM   746   O O   . SER A 1 93  ? 22.346  58.174  95.553  1.00 104.33 ?  109 SER B O   1 
ATOM   747   C CB  . SER A 1 93  ? 23.150  61.130  96.788  1.00 102.85 ?  109 SER B CB  1 
ATOM   748   O OG  . SER A 1 93  ? 24.292  60.363  96.474  1.00 108.74 ?  109 SER B OG  1 
ATOM   749   N N   . GLU A 1 94  ? 21.871  59.938  94.239  1.00 106.28 ?  110 GLU B N   1 
ATOM   750   C CA  . GLU A 1 94  ? 21.739  59.111  93.042  1.00 110.91 ?  110 GLU B CA  1 
ATOM   751   C C   . GLU A 1 94  ? 23.015  58.359  92.741  1.00 114.15 ?  110 GLU B C   1 
ATOM   752   O O   . GLU A 1 94  ? 22.984  57.163  92.445  1.00 117.41 ?  110 GLU B O   1 
ATOM   753   C CB  . GLU A 1 94  ? 21.323  59.935  91.828  1.00 111.77 ?  110 GLU B CB  1 
ATOM   754   C CG  . GLU A 1 94  ? 19.996  60.650  91.991  1.00 119.23 ?  110 GLU B CG  1 
ATOM   755   C CD  . GLU A 1 94  ? 19.764  61.704  90.938  1.00 124.79 ?  110 GLU B CD  1 
ATOM   756   O OE1 . GLU A 1 94  ? 20.287  61.550  89.809  1.00 123.06 ?  110 GLU B OE1 1 
ATOM   757   O OE2 . GLU A 1 94  ? 19.015  62.660  91.223  1.00 126.37 -1 110 GLU B OE2 1 
ATOM   758   N N   . ASP A 1 95  ? 24.145  59.043  92.801  1.00 114.66 ?  111 ASP B N   1 
ATOM   759   C CA  . ASP A 1 95  ? 25.414  58.370  92.583  1.00 118.27 ?  111 ASP B CA  1 
ATOM   760   C C   . ASP A 1 95  ? 25.572  57.162  93.519  1.00 119.21 ?  111 ASP B C   1 
ATOM   761   O O   . ASP A 1 95  ? 25.858  56.042  93.065  1.00 119.30 ?  111 ASP B O   1 
ATOM   762   C CB  . ASP A 1 95  ? 26.528  59.395  92.751  1.00 125.64 ?  111 ASP B CB  1 
ATOM   763   C CG  . ASP A 1 95  ? 27.864  58.824  92.485  1.00 141.67 ?  111 ASP B CG  1 
ATOM   764   O OD1 . ASP A 1 95  ? 28.096  58.480  91.314  1.00 147.94 ?  111 ASP B OD1 1 
ATOM   765   O OD2 . ASP A 1 95  ? 28.677  58.731  93.434  1.00 147.71 -1 111 ASP B OD2 1 
ATOM   766   N N   . LYS A 1 96  ? 25.314  57.360  94.826  1.00 118.13 ?  112 LYS B N   1 
ATOM   767   C CA  . LYS A 1 96  ? 25.482  56.286  95.809  1.00 113.60 ?  112 LYS B CA  1 
ATOM   768   C C   . LYS A 1 96  ? 24.480  55.149  95.585  1.00 112.55 ?  112 LYS B C   1 
ATOM   769   O O   . LYS A 1 96  ? 24.826  53.982  95.775  1.00 109.29 ?  112 LYS B O   1 
ATOM   770   C CB  . LYS A 1 96  ? 25.368  56.832  97.244  1.00 102.56 ?  112 LYS B CB  1 
ATOM   771   C CG  . LYS A 1 96  ? 26.378  57.934  97.670  1.00 99.62  ?  112 LYS B CG  1 
ATOM   772   C CD  . LYS A 1 96  ? 26.696  57.873  99.189  1.00 90.27  ?  112 LYS B CD  1 
ATOM   773   C CE  . LYS A 1 96  ? 27.333  59.158  99.716  1.00 83.87  ?  112 LYS B CE  1 
ATOM   774   N NZ  . LYS A 1 96  ? 28.413  58.852  100.698 1.00 85.98  ?  112 LYS B NZ  1 
ATOM   775   N N   . SER A 1 97  ? 23.242  55.458  95.174  1.00 128.80 ?  113 SER B N   1 
ATOM   776   C CA  . SER A 1 97  ? 22.220  54.414  95.007  1.00 124.52 ?  113 SER B CA  1 
ATOM   777   C C   . SER A 1 97  ? 22.477  53.574  93.761  1.00 115.81 ?  113 SER B C   1 
ATOM   778   O O   . SER A 1 97  ? 22.267  52.352  93.754  1.00 110.87 ?  113 SER B O   1 
ATOM   779   C CB  . SER A 1 97  ? 20.832  55.050  94.928  1.00 128.31 ?  113 SER B CB  1 
ATOM   780   O OG  . SER A 1 97  ? 20.557  55.834  96.073  1.00 135.22 ?  113 SER B OG  1 
ATOM   781   N N   . LYS A 1 98  ? 22.904  54.228  92.690  1.00 109.65 ?  114 LYS B N   1 
ATOM   782   C CA  . LYS A 1 98  ? 23.482  53.534  91.553  1.00 105.90 ?  114 LYS B CA  1 
ATOM   783   C C   . LYS A 1 98  ? 24.597  52.582  91.978  1.00 105.10 ?  114 LYS B C   1 
ATOM   784   O O   . LYS A 1 98  ? 24.602  51.409  91.586  1.00 97.27  ?  114 LYS B O   1 
ATOM   785   C CB  . LYS A 1 98  ? 23.985  54.593  90.581  1.00 121.34 ?  114 LYS B CB  1 
ATOM   786   C CG  . LYS A 1 98  ? 22.850  55.472  90.004  1.00 126.30 ?  114 LYS B CG  1 
ATOM   787   C CD  . LYS A 1 98  ? 23.359  56.456  88.938  1.00 133.80 ?  114 LYS B CD  1 
ATOM   788   C CE  . LYS A 1 98  ? 24.313  57.467  89.590  1.00 139.22 ?  114 LYS B CE  1 
ATOM   789   N NZ  . LYS A 1 98  ? 25.375  58.160  88.779  1.00 140.98 ?  114 LYS B NZ  1 
ATOM   790   N N   . ARG A 1 99  ? 25.575  53.074  92.762  1.00 111.60 ?  115 ARG B N   1 
ATOM   791   C CA  . ARG A 1 99  ? 26.659  52.201  93.232  1.00 102.06 ?  115 ARG B CA  1 
ATOM   792   C C   . ARG A 1 99  ? 26.103  50.968  93.944  1.00 94.37  ?  115 ARG B C   1 
ATOM   793   O O   . ARG A 1 99  ? 26.406  49.829  93.564  1.00 89.62  ?  115 ARG B O   1 
ATOM   794   C CB  . ARG A 1 99  ? 27.620  52.962  94.165  1.00 110.20 ?  115 ARG B CB  1 
ATOM   795   C CG  . ARG A 1 99  ? 28.590  53.968  93.509  1.00 128.20 ?  115 ARG B CG  1 
ATOM   796   C CD  . ARG A 1 99  ? 29.123  54.978  94.559  1.00 140.15 ?  115 ARG B CD  1 
ATOM   797   N NE  . ARG A 1 99  ? 30.556  54.914  94.832  1.00 157.48 ?  115 ARG B NE  1 
ATOM   798   C CZ  . ARG A 1 99  ? 31.385  55.952  94.762  1.00 161.48 ?  115 ARG B CZ  1 
ATOM   799   N NH1 . ARG A 1 99  ? 30.961  57.155  94.403  1.00 159.52 ?  115 ARG B NH1 1 
ATOM   800   N NH2 . ARG A 1 99  ? 32.670  55.784  95.084  1.00 159.45 ?  115 ARG B NH2 1 
ATOM   801   N N   . LEU A 1 100 ? 25.295  51.196  94.993  1.00 96.08  ?  116 LEU B N   1 
ATOM   802   C CA  . LEU A 1 100 ? 24.664  50.119  95.771  1.00 87.39  ?  116 LEU B CA  1 
ATOM   803   C C   . LEU A 1 100 ? 24.062  49.040  94.901  1.00 86.93  ?  116 LEU B C   1 
ATOM   804   O O   . LEU A 1 100 ? 24.237  47.846  95.166  1.00 83.04  ?  116 LEU B O   1 
ATOM   805   C CB  . LEU A 1 100 ? 23.568  50.673  96.677  1.00 85.26  ?  116 LEU B CB  1 
ATOM   806   C CG  . LEU A 1 100 ? 22.858  49.664  97.583  1.00 76.55  ?  116 LEU B CG  1 
ATOM   807   C CD1 . LEU A 1 100 ? 23.777  48.860  98.443  1.00 71.44  ?  116 LEU B CD1 1 
ATOM   808   C CD2 . LEU A 1 100 ? 21.811  50.358  98.428  1.00 78.50  ?  116 LEU B CD2 1 
ATOM   809   N N   . ASN A 1 101 ? 23.276  49.444  93.896  1.00 90.28  ?  117 ASN B N   1 
ATOM   810   C CA  . ASN A 1 101 ? 22.628  48.450  93.042  1.00 88.44  ?  117 ASN B CA  1 
ATOM   811   C C   . ASN A 1 101 ? 23.649  47.679  92.209  1.00 83.24  ?  117 ASN B C   1 
ATOM   812   O O   . ASN A 1 101 ? 23.538  46.450  92.054  1.00 77.79  ?  117 ASN B O   1 
ATOM   813   C CB  . ASN A 1 101 ? 21.585  49.132  92.152  1.00 89.01  ?  117 ASN B CB  1 
ATOM   814   C CG  . ASN A 1 101 ? 20.401  49.665  92.945  1.00 93.65  ?  117 ASN B CG  1 
ATOM   815   O OD1 . ASN A 1 101 ? 20.174  49.271  94.095  1.00 88.71  ?  117 ASN B OD1 1 
ATOM   816   N ND2 . ASN A 1 101 ? 19.666  50.595  92.350  1.00 106.24 ?  117 ASN B ND2 1 
ATOM   817   N N   . THR A 1 102 ? 24.657  48.380  91.674  1.00 85.71  ?  118 THR B N   1 
ATOM   818   C CA  . THR A 1 102 ? 25.684  47.684  90.905  1.00 83.55  ?  118 THR B CA  1 
ATOM   819   C C   . THR A 1 102 ? 26.324  46.606  91.759  1.00 80.92  ?  118 THR B C   1 
ATOM   820   O O   . THR A 1 102 ? 26.592  45.493  91.293  1.00 77.09  ?  118 THR B O   1 
ATOM   821   C CB  . THR A 1 102 ? 26.764  48.652  90.439  1.00 82.24  ?  118 THR B CB  1 
ATOM   822   O OG1 . THR A 1 102 ? 26.189  49.608  89.560  1.00 84.85  ?  118 THR B OG1 1 
ATOM   823   C CG2 . THR A 1 102 ? 27.791  47.889  89.635  1.00 72.53  ?  118 THR B CG2 1 
ATOM   824   N N   . ILE A 1 103 ? 26.554  46.930  93.035  1.00 80.81  ?  119 ILE B N   1 
ATOM   825   C CA  . ILE A 1 103 ? 27.191  45.993  93.955  1.00 78.23  ?  119 ILE B CA  1 
ATOM   826   C C   . ILE A 1 103 ? 26.270  44.808  94.250  1.00 81.53  ?  119 ILE B C   1 
ATOM   827   O O   . ILE A 1 103 ? 26.692  43.648  94.160  1.00 82.26  ?  119 ILE B O   1 
ATOM   828   C CB  . ILE A 1 103 ? 27.625  46.715  95.245  1.00 76.68  ?  119 ILE B CB  1 
ATOM   829   C CG1 . ILE A 1 103 ? 28.793  47.666  94.983  1.00 79.98  ?  119 ILE B CG1 1 
ATOM   830   C CG2 . ILE A 1 103 ? 27.940  45.731  96.352  1.00 76.24  ?  119 ILE B CG2 1 
ATOM   831   C CD1 . ILE A 1 103 ? 28.975  48.679  96.069  1.00 84.99  ?  119 ILE B CD1 1 
ATOM   832   N N   . LEU A 1 104 ? 25.018  45.079  94.656  1.00 82.39  ?  120 LEU B N   1 
ATOM   833   C CA  . LEU A 1 104 ? 24.057  44.001  94.930  1.00 79.39  ?  120 LEU B CA  1 
ATOM   834   C C   . LEU A 1 104 ? 24.002  43.023  93.773  1.00 76.72  ?  120 LEU B C   1 
ATOM   835   O O   . LEU A 1 104 ? 24.073  41.795  93.961  1.00 72.61  ?  120 LEU B O   1 
ATOM   836   C CB  . LEU A 1 104 ? 22.658  44.572  95.202  1.00 76.26  ?  120 LEU B CB  1 
ATOM   837   C CG  . LEU A 1 104 ? 22.337  45.380  96.461  1.00 74.25  ?  120 LEU B CG  1 
ATOM   838   C CD1 . LEU A 1 104 ? 20.964  46.010  96.372  1.00 77.05  ?  120 LEU B CD1 1 
ATOM   839   C CD2 . LEU A 1 104 ? 22.351  44.426  97.661  1.00 68.51  ?  120 LEU B CD2 1 
ATOM   840   N N   . ASN A 1 105 ? 23.929  43.564  92.560  1.00 79.49  ?  121 ASN B N   1 
ATOM   841   C CA  . ASN A 1 105 ? 23.795  42.720  91.392  1.00 79.35  ?  121 ASN B CA  1 
ATOM   842   C C   . ASN A 1 105 ? 25.072  41.944  91.132  1.00 77.60  ?  121 ASN B C   1 
ATOM   843   O O   . ASN A 1 105 ? 25.026  40.753  90.798  1.00 76.39  ?  121 ASN B O   1 
ATOM   844   C CB  . ASN A 1 105 ? 23.433  43.587  90.211  1.00 79.59  ?  121 ASN B CB  1 
ATOM   845   C CG  . ASN A 1 105 ? 21.963  43.656  90.022  1.00 87.15  ?  121 ASN B CG  1 
ATOM   846   O OD1 . ASN A 1 105 ? 21.386  42.872  89.277  1.00 96.35  ?  121 ASN B OD1 1 
ATOM   847   N ND2 . ASN A 1 105 ? 21.324  44.584  90.724  1.00 88.50  ?  121 ASN B ND2 1 
ATOM   848   N N   . THR A 1 106 ? 26.221  42.606  91.283  1.00 74.86  ?  122 THR B N   1 
ATOM   849   C CA  . THR A 1 106 ? 27.492  41.935  91.058  1.00 77.90  ?  122 THR B CA  1 
ATOM   850   C C   . THR A 1 106 ? 27.633  40.730  91.974  1.00 78.64  ?  122 THR B C   1 
ATOM   851   O O   . THR A 1 106 ? 27.965  39.639  91.513  1.00 77.97  ?  122 THR B O   1 
ATOM   852   C CB  . THR A 1 106 ? 28.648  42.913  91.264  1.00 78.24  ?  122 THR B CB  1 
ATOM   853   O OG1 . THR A 1 106 ? 28.550  43.979  90.313  1.00 78.39  ?  122 THR B OG1 1 
ATOM   854   C CG2 . THR A 1 106 ? 29.986  42.206  91.134  1.00 74.81  ?  122 THR B CG2 1 
ATOM   855   N N   . MET A 1 107 ? 27.373  40.916  93.278  1.00 78.86  ?  123 MET B N   1 
ATOM   856   C CA  . MET A 1 107 ? 27.353  39.806  94.235  1.00 75.72  ?  123 MET B CA  1 
ATOM   857   C C   . MET A 1 107 ? 26.406  38.698  93.807  1.00 77.96  ?  123 MET B C   1 
ATOM   858   O O   . MET A 1 107 ? 26.733  37.510  93.936  1.00 75.00  ?  123 MET B O   1 
ATOM   859   C CB  . MET A 1 107 ? 26.953  40.317  95.613  1.00 71.13  ?  123 MET B CB  1 
ATOM   860   C CG  . MET A 1 107 ? 27.967  41.199  96.247  1.00 69.12  ?  123 MET B CG  1 
ATOM   861   S SD  . MET A 1 107 ? 27.604  41.407  97.988  1.00 67.89  ?  123 MET B SD  1 
ATOM   862   C CE  . MET A 1 107 ? 26.048  42.256  97.959  1.00 65.88  ?  123 MET B CE  1 
ATOM   863   N N   . SER A 1 108 ? 25.209  39.052  93.330  1.00 80.87  ?  124 SER B N   1 
ATOM   864   C CA  . SER A 1 108 ? 24.255  37.981  93.072  1.00 78.80  ?  124 SER B CA  1 
ATOM   865   C C   . SER A 1 108 ? 24.666  37.151  91.869  1.00 77.10  ?  124 SER B C   1 
ATOM   866   O O   . SER A 1 108 ? 24.523  35.917  91.875  1.00 77.89  ?  124 SER B O   1 
ATOM   867   C CB  . SER A 1 108 ? 22.859  38.526  92.869  1.00 77.46  ?  124 SER B CB  1 
ATOM   868   O OG  . SER A 1 108 ? 22.034  37.412  92.666  1.00 73.84  ?  124 SER B OG  1 
ATOM   869   N N   . THR A 1 109 ? 25.203  37.798  90.837  1.00 80.08  ?  125 THR B N   1 
ATOM   870   C CA  . THR A 1 109 ? 25.711  37.015  89.715  1.00 82.74  ?  125 THR B CA  1 
ATOM   871   C C   . THR A 1 109 ? 27.011  36.293  90.083  1.00 82.89  ?  125 THR B C   1 
ATOM   872   O O   . THR A 1 109 ? 27.258  35.193  89.587  1.00 86.46  ?  125 THR B O   1 
ATOM   873   C CB  . THR A 1 109 ? 25.912  37.878  88.462  1.00 79.67  ?  125 THR B CB  1 
ATOM   874   O OG1 . THR A 1 109 ? 27.143  38.602  88.558  1.00 86.57  ?  125 THR B OG1 1 
ATOM   875   C CG2 . THR A 1 109 ? 24.758  38.845  88.266  1.00 78.78  ?  125 THR B CG2 1 
ATOM   876   N N   . ILE A 1 110 ? 27.855  36.873  90.948  1.00 84.14  ?  126 ILE B N   1 
ATOM   877   C CA  . ILE A 1 110 ? 29.053  36.157  91.379  1.00 84.45  ?  126 ILE B CA  1 
ATOM   878   C C   . ILE A 1 110 ? 28.656  34.868  92.070  1.00 84.89  ?  126 ILE B C   1 
ATOM   879   O O   . ILE A 1 110 ? 29.293  33.831  91.892  1.00 85.72  ?  126 ILE B O   1 
ATOM   880   C CB  . ILE A 1 110 ? 29.932  37.040  92.284  1.00 83.68  ?  126 ILE B CB  1 
ATOM   881   C CG1 . ILE A 1 110 ? 30.571  38.149  91.460  1.00 84.33  ?  126 ILE B CG1 1 
ATOM   882   C CG2 . ILE A 1 110 ? 31.062  36.230  92.914  1.00 80.57  ?  126 ILE B CG2 1 
ATOM   883   C CD1 . ILE A 1 110 ? 31.491  39.050  92.251  1.00 88.32  ?  126 ILE B CD1 1 
ATOM   884   N N   . TYR A 1 111 ? 27.579  34.906  92.846  1.00 82.82  ?  127 TYR B N   1 
ATOM   885   C CA  . TYR A 1 111 ? 27.123  33.701  93.526  1.00 80.44  ?  127 TYR B CA  1 
ATOM   886   C C   . TYR A 1 111 ? 26.553  32.692  92.563  1.00 84.68  ?  127 TYR B C   1 
ATOM   887   O O   . TYR A 1 111 ? 26.819  31.494  92.673  1.00 84.99  ?  127 TYR B O   1 
ATOM   888   C CB  . TYR A 1 111 ? 26.063  34.052  94.539  1.00 76.51  ?  127 TYR B CB  1 
ATOM   889   C CG  . TYR A 1 111 ? 25.537  32.886  95.335  1.00 77.16  ?  127 TYR B CG  1 
ATOM   890   C CD1 . TYR A 1 111 ? 26.141  32.454  96.504  1.00 81.65  ?  127 TYR B CD1 1 
ATOM   891   C CD2 . TYR A 1 111 ? 24.408  32.222  94.921  1.00 77.06  ?  127 TYR B CD2 1 
ATOM   892   C CE1 . TYR A 1 111 ? 25.598  31.384  97.251  1.00 81.52  ?  127 TYR B CE1 1 
ATOM   893   C CE2 . TYR A 1 111 ? 23.869  31.177  95.644  1.00 77.42  ?  127 TYR B CE2 1 
ATOM   894   C CZ  . TYR A 1 111 ? 24.457  30.754  96.803  1.00 79.26  ?  127 TYR B CZ  1 
ATOM   895   O OH  . TYR A 1 111 ? 23.881  29.698  97.489  1.00 73.29  ?  127 TYR B OH  1 
ATOM   896   N N   . SER A 1 112 ? 25.681  33.145  91.673  1.00 90.65  ?  128 SER B N   1 
ATOM   897   C CA  . SER A 1 112 ? 25.031  32.202  90.768  1.00 90.81  ?  128 SER B CA  1 
ATOM   898   C C   . SER A 1 112 ? 26.023  31.597  89.769  1.00 96.56  ?  128 SER B C   1 
ATOM   899   O O   . SER A 1 112 ? 25.858  30.446  89.344  1.00 96.30  ?  128 SER B O   1 
ATOM   900   C CB  . SER A 1 112 ? 23.858  32.907  90.087  1.00 85.77  ?  128 SER B CB  1 
ATOM   901   O OG  . SER A 1 112 ? 24.301  34.007  89.310  1.00 85.61  ?  128 SER B OG  1 
ATOM   902   N N   . THR A 1 113 ? 27.081  32.325  89.433  1.00 101.72 ?  129 THR B N   1 
ATOM   903   C CA  . THR A 1 113 ? 28.045  31.889  88.432  1.00 105.88 ?  129 THR B CA  1 
ATOM   904   C C   . THR A 1 113 ? 29.395  31.558  89.027  1.00 111.17 ?  129 THR B C   1 
ATOM   905   O O   . THR A 1 113 ? 30.372  31.439  88.284  1.00 121.47 ?  129 THR B O   1 
ATOM   906   C CB  . THR A 1 113 ? 28.250  32.968  87.382  1.00 110.59 ?  129 THR B CB  1 
ATOM   907   O OG1 . THR A 1 113 ? 29.047  34.014  87.960  1.00 112.03 ?  129 THR B OG1 1 
ATOM   908   C CG2 . THR A 1 113 ? 26.913  33.524  86.914  1.00 108.45 ?  129 THR B CG2 1 
ATOM   909   N N   . GLY A 1 114 ? 29.496  31.466  90.340  1.00 106.95 ?  130 GLY B N   1 
ATOM   910   C CA  . GLY A 1 114 ? 30.759  31.071  90.920  1.00 113.22 ?  130 GLY B CA  1 
ATOM   911   C C   . GLY A 1 114 ? 31.018  29.633  90.562  1.00 113.08 ?  130 GLY B C   1 
ATOM   912   O O   . GLY A 1 114 ? 30.139  28.779  90.725  1.00 104.58 ?  130 GLY B O   1 
ATOM   913   N N   . LYS A 1 115 ? 32.215  29.368  90.055  1.00 115.48 ?  131 LYS B N   1 
ATOM   914   C CA  . LYS A 1 115 ? 32.627  28.029  89.674  1.00 118.44 ?  131 LYS B CA  1 
ATOM   915   C C   . LYS A 1 115 ? 34.036  27.787  90.184  1.00 122.52 ?  131 LYS B C   1 
ATOM   916   O O   . LYS A 1 115 ? 34.862  28.705  90.242  1.00 128.75 ?  131 LYS B O   1 
ATOM   917   C CB  . LYS A 1 115 ? 32.603  27.820  88.153  1.00 121.97 ?  131 LYS B CB  1 
ATOM   918   C CG  . LYS A 1 115 ? 33.406  28.841  87.354  1.00 128.46 ?  131 LYS B CG  1 
ATOM   919   C CD  . LYS A 1 115 ? 33.585  28.414  85.887  1.00 134.86 ?  131 LYS B CD  1 
ATOM   920   C CE  . LYS A 1 115 ? 32.267  28.382  85.114  1.00 132.22 ?  131 LYS B CE  1 
ATOM   921   N NZ  . LYS A 1 115 ? 31.720  29.754  84.902  1.00 127.98 ?  131 LYS B NZ  1 
ATOM   922   N N   . VAL A 1 116 ? 34.295  26.541  90.574  1.00 121.43 ?  132 VAL B N   1 
ATOM   923   C CA  . VAL A 1 116 ? 35.609  26.100  91.026  1.00 124.74 ?  132 VAL B CA  1 
ATOM   924   C C   . VAL A 1 116 ? 36.029  24.915  90.177  1.00 125.02 ?  132 VAL B C   1 
ATOM   925   O O   . VAL A 1 116 ? 35.235  23.994  89.946  1.00 122.01 ?  132 VAL B O   1 
ATOM   926   C CB  . VAL A 1 116 ? 35.636  25.730  92.524  1.00 119.64 ?  132 VAL B CB  1 
ATOM   927   C CG1 . VAL A 1 116 ? 35.365  26.952  93.387  1.00 119.33 ?  132 VAL B CG1 1 
ATOM   928   C CG2 . VAL A 1 116 ? 34.635  24.636  92.827  1.00 110.79 ?  132 VAL B CG2 1 
ATOM   929   N N   . CYS A 1 117 ? 37.269  24.953  89.703  1.00 130.06 ?  133 CYS B N   1 
ATOM   930   C CA  . CYS A 1 117 ? 37.823  23.960  88.803  1.00 136.45 ?  133 CYS B CA  1 
ATOM   931   C C   . CYS A 1 117 ? 38.838  23.137  89.576  1.00 149.75 ?  133 CYS B C   1 
ATOM   932   O O   . CYS A 1 117 ? 39.566  23.677  90.417  1.00 152.69 ?  133 CYS B O   1 
ATOM   933   C CB  . CYS A 1 117 ? 38.488  24.649  87.618  1.00 140.37 ?  133 CYS B CB  1 
ATOM   934   S SG  . CYS A 1 117 ? 37.498  26.035  86.985  1.00 142.96 ?  133 CYS B SG  1 
ATOM   935   N N   . ASN A 1 118 ? 38.886  21.832  89.297  1.00 156.79 ?  134 ASN B N   1 
ATOM   936   C CA  . ASN A 1 118 ? 39.670  20.907  90.114  1.00 165.37 ?  134 ASN B CA  1 
ATOM   937   C C   . ASN A 1 118 ? 41.170  21.084  89.870  1.00 179.05 ?  134 ASN B C   1 
ATOM   938   O O   . ASN A 1 118 ? 41.585  21.562  88.810  1.00 182.39 ?  134 ASN B O   1 
ATOM   939   C CB  . ASN A 1 118 ? 39.241  19.466  89.837  1.00 166.02 ?  134 ASN B CB  1 
ATOM   940   C CG  . ASN A 1 118 ? 39.613  19.005  88.451  1.00 174.39 ?  134 ASN B CG  1 
ATOM   941   O OD1 . ASN A 1 118 ? 38.921  19.306  87.476  1.00 170.37 ?  134 ASN B OD1 1 
ATOM   942   N ND2 . ASN A 1 118 ? 40.699  18.256  88.352  1.00 179.24 ?  134 ASN B ND2 1 
ATOM   943   N N   . PRO A 1 119 ? 42.018  20.697  90.851  1.00 171.34 ?  135 PRO B N   1 
ATOM   944   C CA  . PRO A 1 119 ? 43.448  21.033  90.755  1.00 176.76 ?  135 PRO B CA  1 
ATOM   945   C C   . PRO A 1 119 ? 44.221  20.218  89.723  1.00 180.34 ?  135 PRO B C   1 
ATOM   946   O O   . PRO A 1 119 ? 45.456  20.204  89.756  1.00 184.72 ?  135 PRO B O   1 
ATOM   947   C CB  . PRO A 1 119 ? 43.966  20.759  92.176  1.00 175.71 ?  135 PRO B CB  1 
ATOM   948   C CG  . PRO A 1 119 ? 43.046  19.719  92.719  1.00 169.87 ?  135 PRO B CG  1 
ATOM   949   C CD  . PRO A 1 119 ? 41.694  20.037  92.133  1.00 163.16 ?  135 PRO B CD  1 
ATOM   950   N N   . ASP A 1 120 ? 43.519  19.552  88.798  1.00 182.43 ?  136 ASP B N   1 
ATOM   951   C CA  . ASP A 1 120 ? 44.152  18.704  87.790  1.00 178.89 ?  136 ASP B CA  1 
ATOM   952   C C   . ASP A 1 120 ? 43.666  18.974  86.375  1.00 179.69 ?  136 ASP B C   1 
ATOM   953   O O   . ASP A 1 120 ? 44.236  18.414  85.433  1.00 173.70 ?  136 ASP B O   1 
ATOM   954   C CB  . ASP A 1 120 ? 43.906  17.221  88.108  1.00 173.14 ?  136 ASP B CB  1 
ATOM   955   C CG  . ASP A 1 120 ? 44.128  16.902  89.568  1.00 173.32 ?  136 ASP B CG  1 
ATOM   956   O OD1 . ASP A 1 120 ? 45.242  17.150  90.065  1.00 173.76 ?  136 ASP B OD1 1 
ATOM   957   O OD2 . ASP A 1 120 ? 43.176  16.446  90.233  1.00 172.17 -1 136 ASP B OD2 1 
ATOM   958   N N   . ASN A 1 121 ? 42.639  19.799  86.200  1.00 188.92 ?  137 ASN B N   1 
ATOM   959   C CA  . ASN A 1 121 ? 42.045  20.079  84.894  1.00 187.26 ?  137 ASN B CA  1 
ATOM   960   C C   . ASN A 1 121 ? 41.447  21.479  84.970  1.00 186.23 ?  137 ASN B C   1 
ATOM   961   O O   . ASN A 1 121 ? 40.340  21.661  85.500  1.00 179.85 ?  137 ASN B O   1 
ATOM   962   C CB  . ASN A 1 121 ? 40.984  19.042  84.535  1.00 180.79 ?  137 ASN B CB  1 
ATOM   963   C CG  . ASN A 1 121 ? 40.538  19.130  83.089  1.00 180.64 ?  137 ASN B CG  1 
ATOM   964   O OD1 . ASN A 1 121 ? 41.102  19.883  82.296  1.00 180.76 ?  137 ASN B OD1 1 
ATOM   965   N ND2 . ASN A 1 121 ? 39.516  18.359  82.739  1.00 179.04 ?  137 ASN B ND2 1 
ATOM   966   N N   . PRO A 1 122 ? 42.160  22.501  84.481  1.00 184.15 ?  138 PRO B N   1 
ATOM   967   C CA  . PRO A 1 122 ? 41.662  23.887  84.601  1.00 180.12 ?  138 PRO B CA  1 
ATOM   968   C C   . PRO A 1 122 ? 40.459  24.243  83.709  1.00 174.77 ?  138 PRO B C   1 
ATOM   969   O O   . PRO A 1 122 ? 39.957  25.372  83.822  1.00 163.42 ?  138 PRO B O   1 
ATOM   970   C CB  . PRO A 1 122 ? 42.898  24.724  84.225  1.00 181.22 ?  138 PRO B CB  1 
ATOM   971   C CG  . PRO A 1 122 ? 44.081  23.827  84.552  1.00 177.37 ?  138 PRO B CG  1 
ATOM   972   C CD  . PRO A 1 122 ? 43.607  22.449  84.187  1.00 180.85 ?  138 PRO B CD  1 
ATOM   973   N N   . GLN A 1 123 ? 39.965  23.340  82.840  1.00 177.86 ?  139 GLN B N   1 
ATOM   974   C CA  . GLN A 1 123 ? 38.786  23.620  82.021  1.00 179.62 ?  139 GLN B CA  1 
ATOM   975   C C   . GLN A 1 123 ? 37.517  22.928  82.502  1.00 171.81 ?  139 GLN B C   1 
ATOM   976   O O   . GLN A 1 123 ? 36.421  23.350  82.120  1.00 167.96 ?  139 GLN B O   1 
ATOM   977   C CB  . GLN A 1 123 ? 39.017  23.212  80.555  1.00 185.60 ?  139 GLN B CB  1 
ATOM   978   C CG  . GLN A 1 123 ? 39.358  21.746  80.338  1.00 187.66 ?  139 GLN B CG  1 
ATOM   979   C CD  . GLN A 1 123 ? 38.520  21.133  79.234  1.00 193.23 ?  139 GLN B CD  1 
ATOM   980   O OE1 . GLN A 1 123 ? 37.461  21.656  78.891  1.00 189.95 ?  139 GLN B OE1 1 
ATOM   981   N NE2 . GLN A 1 123 ? 38.995  20.033  78.662  1.00 200.40 ?  139 GLN B NE2 1 
ATOM   982   N N   . GLU A 1 124 ? 37.641  21.879  83.308  1.00 168.31 ?  140 GLU B N   1 
ATOM   983   C CA  . GLU A 1 124 ? 36.511  21.128  83.837  1.00 159.89 ?  140 GLU B CA  1 
ATOM   984   C C   . GLU A 1 124 ? 36.177  21.658  85.230  1.00 153.74 ?  140 GLU B C   1 
ATOM   985   O O   . GLU A 1 124 ? 36.910  21.404  86.194  1.00 155.75 ?  140 GLU B O   1 
ATOM   986   C CB  . GLU A 1 124 ? 36.848  19.644  83.882  1.00 157.41 ?  140 GLU B CB  1 
ATOM   987   C CG  . GLU A 1 124 ? 35.963  18.851  84.789  1.00 154.10 ?  140 GLU B CG  1 
ATOM   988   C CD  . GLU A 1 124 ? 36.485  17.464  84.991  1.00 158.88 ?  140 GLU B CD  1 
ATOM   989   O OE1 . GLU A 1 124 ? 37.718  17.298  84.998  1.00 163.30 ?  140 GLU B OE1 1 
ATOM   990   O OE2 . GLU A 1 124 ? 35.669  16.540  85.147  1.00 157.87 -1 140 GLU B OE2 1 
ATOM   991   N N   . CYS A 1 125 ? 35.065  22.379  85.344  1.00 141.70 ?  141 CYS B N   1 
ATOM   992   C CA  . CYS A 1 125 ? 34.742  23.089  86.570  1.00 134.11 ?  141 CYS B CA  1 
ATOM   993   C C   . CYS A 1 125 ? 33.376  22.632  87.088  1.00 123.89 ?  141 CYS B C   1 
ATOM   994   O O   . CYS A 1 125 ? 32.685  21.827  86.446  1.00 115.31 ?  141 CYS B O   1 
ATOM   995   C CB  . CYS A 1 125 ? 34.781  24.610  86.335  1.00 136.34 ?  141 CYS B CB  1 
ATOM   996   S SG  . CYS A 1 125 ? 36.310  25.253  85.511  1.00 154.31 ?  141 CYS B SG  1 
ATOM   997   N N   . LEU A 1 126 ? 33.017  23.125  88.293  1.00 128.02 ?  142 LEU B N   1 
ATOM   998   C CA  . LEU A 1 126 ? 31.677  22.988  88.871  1.00 121.81 ?  142 LEU B CA  1 
ATOM   999   C C   . LEU A 1 126 ? 31.182  24.303  89.461  1.00 124.25 ?  142 LEU B C   1 
ATOM   1000  O O   . LEU A 1 126 ? 31.919  24.979  90.188  1.00 120.33 ?  142 LEU B O   1 
ATOM   1001  C CB  . LEU A 1 126 ? 31.610  21.934  89.977  1.00 113.92 ?  142 LEU B CB  1 
ATOM   1002  C CG  . LEU A 1 126 ? 31.966  20.504  89.599  1.00 110.08 ?  142 LEU B CG  1 
ATOM   1003  C CD1 . LEU A 1 126 ? 32.026  19.602  90.829  1.00 95.76  ?  142 LEU B CD1 1 
ATOM   1004  C CD2 . LEU A 1 126 ? 30.974  20.005  88.576  1.00 117.89 ?  142 LEU B CD2 1 
ATOM   1005  N N   . LEU A 1 127 ? 29.927  24.651  89.139  1.00 127.38 ?  143 LEU B N   1 
ATOM   1006  C CA  . LEU A 1 127 ? 29.174  25.682  89.839  1.00 123.72 ?  143 LEU B CA  1 
ATOM   1007  C C   . LEU A 1 127 ? 28.558  25.093  91.088  1.00 124.79 ?  143 LEU B C   1 
ATOM   1008  O O   . LEU A 1 127 ? 28.342  23.882  91.184  1.00 122.34 ?  143 LEU B O   1 
ATOM   1009  C CB  . LEU A 1 127 ? 28.041  26.262  88.996  1.00 130.00 ?  143 LEU B CB  1 
ATOM   1010  C CG  . LEU A 1 127 ? 28.173  27.130  87.753  1.00 133.87 ?  143 LEU B CG  1 
ATOM   1011  C CD1 . LEU A 1 127 ? 26.772  27.584  87.342  1.00 132.58 ?  143 LEU B CD1 1 
ATOM   1012  C CD2 . LEU A 1 127 ? 29.061  28.339  87.980  1.00 128.32 ?  143 LEU B CD2 1 
ATOM   1013  N N   . LEU A 1 128 ? 28.245  25.976  92.039  1.00 125.50 ?  144 LEU B N   1 
ATOM   1014  C CA  . LEU A 1 128 ? 27.654  25.527  93.295  1.00 119.03 ?  144 LEU B CA  1 
ATOM   1015  C C   . LEU A 1 128 ? 26.490  24.598  93.015  1.00 124.55 ?  144 LEU B C   1 
ATOM   1016  O O   . LEU A 1 128 ? 26.424  23.475  93.524  1.00 117.46 ?  144 LEU B O   1 
ATOM   1017  C CB  . LEU A 1 128 ? 27.196  26.730  94.124  1.00 111.29 ?  144 LEU B CB  1 
ATOM   1018  C CG  . LEU A 1 128 ? 26.534  26.412  95.463  1.00 100.58 ?  144 LEU B CG  1 
ATOM   1019  C CD1 . LEU A 1 128 ? 27.548  25.772  96.353  1.00 104.62 ?  144 LEU B CD1 1 
ATOM   1020  C CD2 . LEU A 1 128 ? 25.988  27.660  96.114  1.00 98.56  ?  144 LEU B CD2 1 
ATOM   1021  N N   . GLU A 1 129 ? 25.604  25.029  92.145  1.00 145.70 ?  145 GLU B N   1 
ATOM   1022  C CA  . GLU A 1 129 ? 24.512  24.190  91.728  1.00 148.24 ?  145 GLU B CA  1 
ATOM   1023  C C   . GLU A 1 129 ? 24.704  23.825  90.265  1.00 152.32 ?  145 GLU B C   1 
ATOM   1024  O O   . GLU A 1 129 ? 24.842  24.726  89.424  1.00 154.96 ?  145 GLU B O   1 
ATOM   1025  C CB  . GLU A 1 129 ? 23.167  24.907  91.929  1.00 145.28 ?  145 GLU B CB  1 
ATOM   1026  C CG  . GLU A 1 129 ? 22.002  24.065  91.483  1.00 149.72 ?  145 GLU B CG  1 
ATOM   1027  C CD  . GLU A 1 129 ? 21.950  22.721  92.211  1.00 151.75 ?  145 GLU B CD  1 
ATOM   1028  O OE1 . GLU A 1 129 ? 22.398  22.634  93.375  1.00 149.30 ?  145 GLU B OE1 1 
ATOM   1029  O OE2 . GLU A 1 129 ? 21.542  21.725  91.582  1.00 154.91 -1 145 GLU B OE2 1 
ATOM   1030  N N   . PRO A 1 130 ? 24.699  22.526  89.910  1.00 139.81 ?  146 PRO B N   1 
ATOM   1031  C CA  . PRO A 1 130 ? 24.452  21.359  90.770  1.00 134.44 ?  146 PRO B CA  1 
ATOM   1032  C C   . PRO A 1 130 ? 25.651  20.491  91.136  1.00 130.13 ?  146 PRO B C   1 
ATOM   1033  O O   . PRO A 1 130 ? 25.425  19.326  91.456  1.00 123.24 ?  146 PRO B O   1 
ATOM   1034  C CB  . PRO A 1 130 ? 23.510  20.523  89.921  1.00 129.58 ?  146 PRO B CB  1 
ATOM   1035  C CG  . PRO A 1 130 ? 24.022  20.769  88.541  1.00 131.80 ?  146 PRO B CG  1 
ATOM   1036  C CD  . PRO A 1 130 ? 24.446  22.212  88.495  1.00 135.99 ?  146 PRO B CD  1 
ATOM   1037  N N   . GLY A 1 131 ? 26.875  21.008  91.085  1.00 131.95 ?  147 GLY B N   1 
ATOM   1038  C CA  . GLY A 1 131 ? 28.021  20.149  91.317  1.00 131.47 ?  147 GLY B CA  1 
ATOM   1039  C C   . GLY A 1 131 ? 28.460  20.057  92.764  1.00 128.73 ?  147 GLY B C   1 
ATOM   1040  O O   . GLY A 1 131 ? 28.280  19.028  93.435  1.00 130.85 ?  147 GLY B O   1 
ATOM   1041  N N   . LEU A 1 132 ? 29.061  21.144  93.247  1.00 113.23 ?  148 LEU B N   1 
ATOM   1042  C CA  . LEU A 1 132 ? 29.557  21.178  94.612  1.00 105.53 ?  148 LEU B CA  1 
ATOM   1043  C C   . LEU A 1 132 ? 28.482  20.740  95.591  1.00 105.27 ?  148 LEU B C   1 
ATOM   1044  O O   . LEU A 1 132 ? 28.726  19.905  96.466  1.00 106.22 ?  148 LEU B O   1 
ATOM   1045  C CB  . LEU A 1 132 ? 30.032  22.584  94.946  1.00 103.08 ?  148 LEU B CB  1 
ATOM   1046  C CG  . LEU A 1 132 ? 31.101  23.170  94.043  1.00 103.90 ?  148 LEU B CG  1 
ATOM   1047  C CD1 . LEU A 1 132 ? 31.464  24.570  94.523  1.00 105.98 ?  148 LEU B CD1 1 
ATOM   1048  C CD2 . LEU A 1 132 ? 32.303  22.255  94.033  1.00 104.03 ?  148 LEU B CD2 1 
ATOM   1049  N N   . ASN A 1 133 ? 27.285  21.315  95.456  1.00 112.84 ?  149 ASN B N   1 
ATOM   1050  C CA  . ASN A 1 133 ? 26.156  20.964  96.315  1.00 107.82 ?  149 ASN B CA  1 
ATOM   1051  C C   . ASN A 1 133 ? 25.949  19.463  96.341  1.00 108.39 ?  149 ASN B C   1 
ATOM   1052  O O   . ASN A 1 133 ? 25.662  18.871  97.392  1.00 101.80 ?  149 ASN B O   1 
ATOM   1053  C CB  . ASN A 1 133 ? 24.906  21.681  95.805  1.00 104.02 ?  149 ASN B CB  1 
ATOM   1054  C CG  . ASN A 1 133 ? 24.892  23.122  96.191  1.00 104.70 ?  149 ASN B CG  1 
ATOM   1055  O OD1 . ASN A 1 133 ? 25.570  23.517  97.133  1.00 97.71  ?  149 ASN B OD1 1 
ATOM   1056  N ND2 . ASN A 1 133 ? 24.192  23.936  95.421  1.00 109.88 ?  149 ASN B ND2 1 
ATOM   1057  N N   . GLU A 1 134 ? 26.143  18.823  95.193  1.00 113.59 ?  150 GLU B N   1 
ATOM   1058  C CA  . GLU A 1 134 ? 25.891  17.398  95.104  1.00 115.29 ?  150 GLU B CA  1 
ATOM   1059  C C   . GLU A 1 134 ? 26.963  16.631  95.872  1.00 116.22 ?  150 GLU B C   1 
ATOM   1060  O O   . GLU A 1 134 ? 26.644  15.705  96.635  1.00 118.55 ?  150 GLU B O   1 
ATOM   1061  C CB  . GLU A 1 134 ? 25.816  17.005  93.624  1.00 120.47 ?  150 GLU B CB  1 
ATOM   1062  C CG  . GLU A 1 134 ? 25.341  15.590  93.302  1.00 124.22 ?  150 GLU B CG  1 
ATOM   1063  C CD  . GLU A 1 134 ? 26.389  14.520  93.567  1.00 128.92 ?  150 GLU B CD  1 
ATOM   1064  O OE1 . GLU A 1 134 ? 27.606  14.805  93.428  1.00 128.22 ?  150 GLU B OE1 1 
ATOM   1065  O OE2 . GLU A 1 134 ? 25.990  13.377  93.887  1.00 126.84 -1 150 GLU B OE2 1 
ATOM   1066  N N   . ILE A 1 135 ? 28.237  17.035  95.722  1.00 113.89 ?  151 ILE B N   1 
ATOM   1067  C CA  . ILE A 1 135 ? 29.300  16.434  96.543  1.00 106.58 ?  151 ILE B CA  1 
ATOM   1068  C C   . ILE A 1 135 ? 28.977  16.553  98.027  1.00 103.10 ?  151 ILE B C   1 
ATOM   1069  O O   . ILE A 1 135 ? 29.021  15.562  98.760  1.00 98.93  ?  151 ILE B O   1 
ATOM   1070  C CB  . ILE A 1 135 ? 30.682  17.051  96.249  1.00 105.84 ?  151 ILE B CB  1 
ATOM   1071  C CG1 . ILE A 1 135 ? 31.182  16.772  94.829  1.00 108.64 ?  151 ILE B CG1 1 
ATOM   1072  C CG2 . ILE A 1 135 ? 31.674  16.603  97.278  1.00 97.45  ?  151 ILE B CG2 1 
ATOM   1073  C CD1 . ILE A 1 135 ? 32.509  17.481  94.546  1.00 104.00 ?  151 ILE B CD1 1 
ATOM   1074  N N   . MET A 1 136 ? 28.673  17.775  98.492  1.00 97.36  ?  152 MET B N   1 
ATOM   1075  C CA  . MET A 1 136 ? 28.435  18.010  99.923  1.00 95.35  ?  152 MET B CA  1 
ATOM   1076  C C   . MET A 1 136 ? 27.244  17.235  100.458 1.00 93.04  ?  152 MET B C   1 
ATOM   1077  O O   . MET A 1 136 ? 27.206  16.895  101.644 1.00 91.21  ?  152 MET B O   1 
ATOM   1078  C CB  . MET A 1 136 ? 28.240  19.500  100.223 1.00 87.85  ?  152 MET B CB  1 
ATOM   1079  C CG  . MET A 1 136 ? 29.393  20.379  99.841  1.00 89.26  ?  152 MET B CG  1 
ATOM   1080  S SD  . MET A 1 136 ? 30.893  19.796  100.672 1.00 94.80  ?  152 MET B SD  1 
ATOM   1081  C CE  . MET A 1 136 ? 30.497  20.113  102.402 1.00 87.96  ?  152 MET B CE  1 
ATOM   1082  N N   . ALA A 1 137 ? 26.263  16.953  99.618  1.00 95.49  ?  153 ALA B N   1 
ATOM   1083  C CA  . ALA A 1 137 ? 25.106  16.229  100.115 1.00 95.28  ?  153 ALA B CA  1 
ATOM   1084  C C   . ALA A 1 137 ? 25.312  14.718  100.125 1.00 94.16  ?  153 ALA B C   1 
ATOM   1085  O O   . ALA A 1 137 ? 24.765  14.026  100.990 1.00 89.58  ?  153 ALA B O   1 
ATOM   1086  C CB  . ALA A 1 137 ? 23.890  16.599  99.268  1.00 104.12 ?  153 ALA B CB  1 
ATOM   1087  N N   . ASN A 1 138 ? 26.077  14.178  99.180  1.00 99.22  ?  154 ASN B N   1 
ATOM   1088  C CA  . ASN A 1 138 ? 26.178  12.725  99.079  1.00 100.34 ?  154 ASN B CA  1 
ATOM   1089  C C   . ASN A 1 138 ? 27.454  12.124  99.679  1.00 94.14  ?  154 ASN B C   1 
ATOM   1090  O O   . ASN A 1 138 ? 27.396  11.045  100.282 1.00 84.30  ?  154 ASN B O   1 
ATOM   1091  C CB  . ASN A 1 138 ? 26.057  12.294  97.606  1.00 111.54 ?  154 ASN B CB  1 
ATOM   1092  C CG  . ASN A 1 138 ? 24.718  12.679  96.966  1.00 111.50 ?  154 ASN B CG  1 
ATOM   1093  O OD1 . ASN A 1 138 ? 23.747  11.924  97.063  1.00 105.55 ?  154 ASN B OD1 1 
ATOM   1094  N ND2 . ASN A 1 138 ? 24.682  13.818  96.265  1.00 114.93 ?  154 ASN B ND2 1 
ATOM   1095  N N   . SER A 1 139 ? 28.601  12.796  99.547  1.00 102.43 ?  155 SER B N   1 
ATOM   1096  C CA  . SER A 1 139 ? 29.898  12.139  99.710  1.00 97.19  ?  155 SER B CA  1 
ATOM   1097  C C   . SER A 1 139 ? 30.138  11.672  101.131 1.00 85.47  ?  155 SER B C   1 
ATOM   1098  O O   . SER A 1 139 ? 29.707  12.298  102.101 1.00 87.64  ?  155 SER B O   1 
ATOM   1099  C CB  . SER A 1 139 ? 31.053  13.066  99.315  1.00 101.72 ?  155 SER B CB  1 
ATOM   1100  O OG  . SER A 1 139 ? 32.318  12.417  99.458  1.00 101.01 ?  155 SER B OG  1 
ATOM   1101  N N   . LEU A 1 140 ? 30.870  10.566  101.233 1.00 92.23  ?  156 LEU B N   1 
ATOM   1102  C CA  . LEU A 1 140 ? 31.452  10.123  102.491 1.00 100.84 ?  156 LEU B CA  1 
ATOM   1103  C C   . LEU A 1 140 ? 32.980  10.128  102.511 1.00 106.31 ?  156 LEU B C   1 
ATOM   1104  O O   . LEU A 1 140 ? 33.567  9.672   103.494 1.00 100.35 ?  156 LEU B O   1 
ATOM   1105  C CB  . LEU A 1 140 ? 30.936  8.724   102.864 1.00 91.79  ?  156 LEU B CB  1 
ATOM   1106  C CG  . LEU A 1 140 ? 29.426  8.702   103.100 1.00 90.94  ?  156 LEU B CG  1 
ATOM   1107  C CD1 . LEU A 1 140 ? 28.945  7.347   103.549 1.00 75.76  ?  156 LEU B CD1 1 
ATOM   1108  C CD2 . LEU A 1 140 ? 29.052  9.761   104.129 1.00 93.37  ?  156 LEU B CD2 1 
ATOM   1109  N N   . ASP A 1 141 ? 33.644  10.653  101.483 1.00 112.48 ?  157 ASP B N   1 
ATOM   1110  C CA  . ASP A 1 141 ? 35.090  10.847  101.530 1.00 111.90 ?  157 ASP B CA  1 
ATOM   1111  C C   . ASP A 1 141 ? 35.379  12.217  102.133 1.00 111.04 ?  157 ASP B C   1 
ATOM   1112  O O   . ASP A 1 141 ? 34.925  13.240  101.610 1.00 112.41 ?  157 ASP B O   1 
ATOM   1113  C CB  . ASP A 1 141 ? 35.720  10.758  100.143 1.00 114.43 ?  157 ASP B CB  1 
ATOM   1114  C CG  . ASP A 1 141 ? 37.216  11.074  100.164 1.00 122.92 ?  157 ASP B CG  1 
ATOM   1115  O OD1 . ASP A 1 141 ? 38.034  10.154  100.397 1.00 124.34 ?  157 ASP B OD1 1 
ATOM   1116  O OD2 . ASP A 1 141 ? 37.571  12.264  100.040 1.00 127.07 -1 157 ASP B OD2 1 
ATOM   1117  N N   . TYR A 1 142 ? 36.154  12.234  103.217 1.00 103.08 ?  158 TYR B N   1 
ATOM   1118  C CA  . TYR A 1 142 ? 36.448  13.476  103.927 1.00 100.31 ?  158 TYR B CA  1 
ATOM   1119  C C   . TYR A 1 142 ? 37.159  14.495  103.055 1.00 100.52 ?  158 TYR B C   1 
ATOM   1120  O O   . TYR A 1 142 ? 36.917  15.701  103.173 1.00 100.20 ?  158 TYR B O   1 
ATOM   1121  C CB  . TYR A 1 142 ? 37.308  13.160  105.132 1.00 99.32  ?  158 TYR B CB  1 
ATOM   1122  C CG  . TYR A 1 142 ? 37.709  14.303  106.044 1.00 96.21  ?  158 TYR B CG  1 
ATOM   1123  C CD1 . TYR A 1 142 ? 38.838  15.070  105.778 1.00 94.68  ?  158 TYR B CD1 1 
ATOM   1124  C CD2 . TYR A 1 142 ? 37.016  14.556  107.225 1.00 97.05  ?  158 TYR B CD2 1 
ATOM   1125  C CE1 . TYR A 1 142 ? 39.243  16.088  106.653 1.00 93.06  ?  158 TYR B CE1 1 
ATOM   1126  C CE2 . TYR A 1 142 ? 37.413  15.569  108.104 1.00 92.71  ?  158 TYR B CE2 1 
ATOM   1127  C CZ  . TYR A 1 142 ? 38.526  16.332  107.818 1.00 90.51  ?  158 TYR B CZ  1 
ATOM   1128  O OH  . TYR A 1 142 ? 38.904  17.330  108.703 1.00 82.54  ?  158 TYR B OH  1 
ATOM   1129  N N   . ASN A 1 143 ? 38.079  14.049  102.218 1.00 104.93 ?  159 ASN B N   1 
ATOM   1130  C CA  . ASN A 1 143 ? 38.893  15.024  101.514 1.00 103.86 ?  159 ASN B CA  1 
ATOM   1131  C C   . ASN A 1 143 ? 38.119  15.691  100.381 1.00 103.06 ?  159 ASN B C   1 
ATOM   1132  O O   . ASN A 1 143 ? 38.324  16.881  100.116 1.00 102.06 ?  159 ASN B O   1 
ATOM   1133  C CB  . ASN A 1 143 ? 40.136  14.350  100.972 1.00 109.98 ?  159 ASN B CB  1 
ATOM   1134  C CG  . ASN A 1 143 ? 41.110  14.032  102.055 1.00 104.97 ?  159 ASN B CG  1 
ATOM   1135  O OD1 . ASN A 1 143 ? 41.082  14.645  103.122 1.00 98.96  ?  159 ASN B OD1 1 
ATOM   1136  N ND2 . ASN A 1 143 ? 41.989  13.081  101.796 1.00 106.38 ?  159 ASN B ND2 1 
ATOM   1137  N N   . GLU A 1 144 ? 37.214  14.946  99.731  1.00 107.88 ?  160 GLU B N   1 
ATOM   1138  C CA  . GLU A 1 144 ? 36.340  15.509  98.702  1.00 110.97 ?  160 GLU B CA  1 
ATOM   1139  C C   . GLU A 1 144 ? 35.435  16.595  99.283  1.00 105.34 ?  160 GLU B C   1 
ATOM   1140  O O   . GLU A 1 144 ? 35.314  17.699  98.720  1.00 107.79 ?  160 GLU B O   1 
ATOM   1141  C CB  . GLU A 1 144 ? 35.528  14.372  98.057  1.00 112.94 ?  160 GLU B CB  1 
ATOM   1142  C CG  . GLU A 1 144 ? 34.756  14.718  96.776  1.00 118.81 ?  160 GLU B CG  1 
ATOM   1143  C CD  . GLU A 1 144 ? 33.815  13.601  96.319  1.00 112.55 ?  160 GLU B CD  1 
ATOM   1144  O OE1 . GLU A 1 144 ? 33.793  12.537  96.971  1.00 106.65 ?  160 GLU B OE1 1 
ATOM   1145  O OE2 . GLU A 1 144 ? 33.080  13.805  95.323  1.00 110.83 -1 160 GLU B OE2 1 
ATOM   1146  N N   . ARG A 1 145 ? 34.796  16.295  100.418 1.00 98.44  ?  161 ARG B N   1 
ATOM   1147  C CA  . ARG A 1 145 ? 33.958  17.273  101.111 1.00 93.60  ?  161 ARG B CA  1 
ATOM   1148  C C   . ARG A 1 145 ? 34.773  18.502  101.491 1.00 93.53  ?  161 ARG B C   1 
ATOM   1149  O O   . ARG A 1 145 ? 34.349  19.644  101.274 1.00 95.74  ?  161 ARG B O   1 
ATOM   1150  C CB  . ARG A 1 145 ? 33.364  16.609  102.346 1.00 91.30  ?  161 ARG B CB  1 
ATOM   1151  C CG  . ARG A 1 145 ? 32.509  15.386  102.042 1.00 92.02  ?  161 ARG B CG  1 
ATOM   1152  C CD  . ARG A 1 145 ? 31.888  14.823  103.317 1.00 93.67  ?  161 ARG B CD  1 
ATOM   1153  N NE  . ARG A 1 145 ? 30.987  15.699  104.053 1.00 88.38  ?  161 ARG B NE  1 
ATOM   1154  C CZ  . ARG A 1 145 ? 29.676  15.719  103.868 1.00 91.17  ?  161 ARG B CZ  1 
ATOM   1155  N NH1 . ARG A 1 145 ? 29.079  14.844  103.077 1.00 90.72  ?  161 ARG B NH1 1 
ATOM   1156  N NH2 . ARG A 1 145 ? 28.940  16.609  104.531 1.00 90.89  ?  161 ARG B NH2 1 
ATOM   1157  N N   . LEU A 1 146 ? 35.958  18.281  102.062 1.00 90.74  ?  162 LEU B N   1 
ATOM   1158  C CA  . LEU A 1 146 ? 36.801  19.405  102.454 1.00 91.90  ?  162 LEU B CA  1 
ATOM   1159  C C   . LEU A 1 146 ? 37.140  20.277  101.257 1.00 93.16  ?  162 LEU B C   1 
ATOM   1160  O O   . LEU A 1 146 ? 37.174  21.508  101.371 1.00 94.73  ?  162 LEU B O   1 
ATOM   1161  C CB  . LEU A 1 146 ? 38.078  18.899  103.129 1.00 91.47  ?  162 LEU B CB  1 
ATOM   1162  C CG  . LEU A 1 146 ? 39.101  19.915  103.629 1.00 85.13  ?  162 LEU B CG  1 
ATOM   1163  C CD1 . LEU A 1 146 ? 38.478  20.929  104.533 1.00 84.03  ?  162 LEU B CD1 1 
ATOM   1164  C CD2 . LEU A 1 146 ? 40.156  19.173  104.376 1.00 90.28  ?  162 LEU B CD2 1 
ATOM   1165  N N   . TRP A 1 147 ? 37.399  19.658  100.101 1.00 93.67  ?  163 TRP B N   1 
ATOM   1166  C CA  . TRP A 1 147 ? 37.773  20.433  98.926  1.00 95.04  ?  163 TRP B CA  1 
ATOM   1167  C C   . TRP A 1 147 ? 36.607  21.266  98.433  1.00 97.49  ?  163 TRP B C   1 
ATOM   1168  O O   . TRP A 1 147 ? 36.771  22.460  98.140  1.00 98.70  ?  163 TRP B O   1 
ATOM   1169  C CB  . TRP A 1 147 ? 38.302  19.518  97.827  1.00 93.22  ?  163 TRP B CB  1 
ATOM   1170  C CG  . TRP A 1 147 ? 38.421  20.174  96.477  1.00 96.11  ?  163 TRP B CG  1 
ATOM   1171  C CD1 . TRP A 1 147 ? 39.414  21.016  96.044  1.00 98.34  ?  163 TRP B CD1 1 
ATOM   1172  C CD2 . TRP A 1 147 ? 37.554  19.974  95.354  1.00 95.07  ?  163 TRP B CD2 1 
ATOM   1173  N NE1 . TRP A 1 147 ? 39.191  21.385  94.732  1.00 102.38 ?  163 TRP B NE1 1 
ATOM   1174  C CE2 . TRP A 1 147 ? 38.059  20.753  94.287  1.00 99.25  ?  163 TRP B CE2 1 
ATOM   1175  C CE3 . TRP A 1 147 ? 36.383  19.229  95.151  1.00 92.88  ?  163 TRP B CE3 1 
ATOM   1176  C CZ2 . TRP A 1 147 ? 37.435  20.803  93.051  1.00 107.64 ?  163 TRP B CZ2 1 
ATOM   1177  C CZ3 . TRP A 1 147 ? 35.764  19.284  93.923  1.00 89.19  ?  163 TRP B CZ3 1 
ATOM   1178  C CH2 . TRP A 1 147 ? 36.289  20.062  92.890  1.00 100.50 ?  163 TRP B CH2 1 
ATOM   1179  N N   . ALA A 1 148 ? 35.422  20.655  98.334  1.00 101.11 ?  164 ALA B N   1 
ATOM   1180  C CA  . ALA A 1 148 ? 34.230  21.423  97.956  1.00 99.72  ?  164 ALA B CA  1 
ATOM   1181  C C   . ALA A 1 148 ? 34.071  22.648  98.854  1.00 95.33  ?  164 ALA B C   1 
ATOM   1182  O O   . ALA A 1 148 ? 33.905  23.781  98.375  1.00 96.32  ?  164 ALA B O   1 
ATOM   1183  C CB  . ALA A 1 148 ? 32.981  20.538  98.017  1.00 94.29  ?  164 ALA B CB  1 
ATOM   1184  N N   . TRP A 1 149 ? 34.208  22.430  100.164 1.00 90.48  ?  165 TRP B N   1 
ATOM   1185  C CA  . TRP A 1 149 ? 33.976  23.468  101.162 1.00 87.85  ?  165 TRP B CA  1 
ATOM   1186  C C   . TRP A 1 149 ? 34.975  24.621  101.010 1.00 91.10  ?  165 TRP B C   1 
ATOM   1187  O O   . TRP A 1 149 ? 34.592  25.783  100.780 1.00 90.83  ?  165 TRP B O   1 
ATOM   1188  C CB  . TRP A 1 149 ? 34.083  22.813  102.539 1.00 88.17  ?  165 TRP B CB  1 
ATOM   1189  C CG  . TRP A 1 149 ? 33.615  23.616  103.707 1.00 86.70  ?  165 TRP B CG  1 
ATOM   1190  C CD1 . TRP A 1 149 ? 32.380  23.576  104.300 1.00 82.24  ?  165 TRP B CD1 1 
ATOM   1191  C CD2 . TRP A 1 149 ? 34.370  24.588  104.423 1.00 83.92  ?  165 TRP B CD2 1 
ATOM   1192  N NE1 . TRP A 1 149 ? 32.338  24.453  105.356 1.00 79.03  ?  165 TRP B NE1 1 
ATOM   1193  C CE2 . TRP A 1 149 ? 33.545  25.095  105.442 1.00 78.99  ?  165 TRP B CE2 1 
ATOM   1194  C CE3 . TRP A 1 149 ? 35.666  25.086  104.296 1.00 84.69  ?  165 TRP B CE3 1 
ATOM   1195  C CZ2 . TRP A 1 149 ? 33.976  26.073  106.323 1.00 78.08  ?  165 TRP B CZ2 1 
ATOM   1196  C CZ3 . TRP A 1 149 ? 36.089  26.060  105.175 1.00 84.06  ?  165 TRP B CZ3 1 
ATOM   1197  C CH2 . TRP A 1 149 ? 35.247  26.544  106.174 1.00 79.97  ?  165 TRP B CH2 1 
ATOM   1198  N N   . GLU A 1 150 ? 36.277  24.308  101.135 1.00 92.64  ?  166 GLU B N   1 
ATOM   1199  C CA  . GLU A 1 150 ? 37.307  25.344  101.106 1.00 93.54  ?  166 GLU B CA  1 
ATOM   1200  C C   . GLU A 1 150 ? 37.343  26.067  99.768  1.00 96.72  ?  166 GLU B C   1 
ATOM   1201  O O   . GLU A 1 150 ? 37.559  27.285  99.717  1.00 100.61 ?  166 GLU B O   1 
ATOM   1202  C CB  . GLU A 1 150 ? 38.683  24.747  101.399 1.00 86.55  ?  166 GLU B CB  1 
ATOM   1203  C CG  . GLU A 1 150 ? 39.840  25.671  101.029 1.00 88.33  ?  166 GLU B CG  1 
ATOM   1204  C CD  . GLU A 1 150 ? 39.874  26.952  101.824 1.00 89.03  ?  166 GLU B CD  1 
ATOM   1205  O OE1 . GLU A 1 150 ? 39.119  27.090  102.806 1.00 85.84  ?  166 GLU B OE1 1 
ATOM   1206  O OE2 . GLU A 1 150 ? 40.627  27.860  101.423 1.00 91.88  -1 166 GLU B OE2 1 
ATOM   1207  N N   . SER A 1 151 ? 37.146  25.343  98.663  1.00 98.15  ?  167 SER B N   1 
ATOM   1208  C CA  . SER A 1 151 ? 37.301  25.999  97.370  1.00 103.15 ?  167 SER B CA  1 
ATOM   1209  C C   . SER A 1 151 ? 36.096  26.871  97.033  1.00 105.47 ?  167 SER B C   1 
ATOM   1210  O O   . SER A 1 151 ? 36.272  27.991  96.534  1.00 108.37 ?  167 SER B O   1 
ATOM   1211  C CB  . SER A 1 151 ? 37.541  24.968  96.273  1.00 95.73  ?  167 SER B CB  1 
ATOM   1212  O OG  . SER A 1 151 ? 36.509  24.016  96.328  1.00 96.46  ?  167 SER B OG  1 
ATOM   1213  N N   . TRP A 1 152 ? 34.869  26.380  97.279  1.00 101.55 ?  168 TRP B N   1 
ATOM   1214  C CA  . TRP A 1 152 ? 33.705  27.255  97.184  1.00 99.75  ?  168 TRP B CA  1 
ATOM   1215  C C   . TRP A 1 152 ? 33.888  28.520  98.011  1.00 100.43 ?  168 TRP B C   1 
ATOM   1216  O O   . TRP A 1 152 ? 33.612  29.624  97.522  1.00 102.99 ?  168 TRP B O   1 
ATOM   1217  C CB  . TRP A 1 152 ? 32.433  26.514  97.605  1.00 93.70  ?  168 TRP B CB  1 
ATOM   1218  C CG  . TRP A 1 152 ? 31.230  27.396  97.552  1.00 91.10  ?  168 TRP B CG  1 
ATOM   1219  C CD1 . TRP A 1 152 ? 30.480  27.803  98.613  1.00 90.85  ?  168 TRP B CD1 1 
ATOM   1220  C CD2 . TRP A 1 152 ? 30.679  28.049  96.404  1.00 94.59  ?  168 TRP B CD2 1 
ATOM   1221  N NE1 . TRP A 1 152 ? 29.480  28.641  98.198  1.00 92.74  ?  168 TRP B NE1 1 
ATOM   1222  C CE2 . TRP A 1 152 ? 29.579  28.808  96.842  1.00 98.46  ?  168 TRP B CE2 1 
ATOM   1223  C CE3 . TRP A 1 152 ? 30.990  28.049  95.047  1.00 96.90  ?  168 TRP B CE3 1 
ATOM   1224  C CZ2 . TRP A 1 152 ? 28.794  29.566  95.967  1.00 94.28  ?  168 TRP B CZ2 1 
ATOM   1225  C CZ3 . TRP A 1 152 ? 30.201  28.795  94.180  1.00 99.80  ?  168 TRP B CZ3 1 
ATOM   1226  C CH2 . TRP A 1 152 ? 29.126  29.549  94.645  1.00 94.22  ?  168 TRP B CH2 1 
ATOM   1227  N N   . ARG A 1 153 ? 34.375  28.394  99.255  1.00 98.12  ?  169 ARG B N   1 
ATOM   1228  C CA  . ARG A 1 153 ? 34.541  29.604  100.052 1.00 96.33  ?  169 ARG B CA  1 
ATOM   1229  C C   . ARG A 1 153 ? 35.730  30.468  99.653  1.00 103.79 ?  169 ARG B C   1 
ATOM   1230  O O   . ARG A 1 153 ? 35.740  31.650  100.015 1.00 101.73 ?  169 ARG B O   1 
ATOM   1231  C CB  . ARG A 1 153 ? 34.635  29.261  101.529 1.00 88.91  ?  169 ARG B CB  1 
ATOM   1232  C CG  . ARG A 1 153 ? 33.336  28.998  102.188 1.00 84.90  ?  169 ARG B CG  1 
ATOM   1233  C CD  . ARG A 1 153 ? 33.542  28.211  103.434 1.00 88.32  ?  169 ARG B CD  1 
ATOM   1234  N NE  . ARG A 1 153 ? 32.296  28.085  104.174 1.00 89.23  ?  169 ARG B NE  1 
ATOM   1235  C CZ  . ARG A 1 153 ? 31.328  27.231  103.893 1.00 85.18  ?  169 ARG B CZ  1 
ATOM   1236  N NH1 . ARG A 1 153 ? 31.373  26.484  102.805 1.00 83.05  ?  169 ARG B NH1 1 
ATOM   1237  N NH2 . ARG A 1 153 ? 30.266  27.166  104.703 1.00 82.61  ?  169 ARG B NH2 1 
ATOM   1238  N N   . SER A 1 154 ? 36.726  29.928  98.947  1.00 117.81 ?  170 SER B N   1 
ATOM   1239  C CA  . SER A 1 154 ? 37.915  30.707  98.619  1.00 116.84 ?  170 SER B CA  1 
ATOM   1240  C C   . SER A 1 154 ? 37.911  31.273  97.210  1.00 118.76 ?  170 SER B C   1 
ATOM   1241  O O   . SER A 1 154 ? 38.581  32.278  96.957  1.00 123.16 ?  170 SER B O   1 
ATOM   1242  C CB  . SER A 1 154 ? 39.180  29.863  98.811  1.00 115.85 ?  170 SER B CB  1 
ATOM   1243  O OG  . SER A 1 154 ? 39.348  28.976  97.728  1.00 124.12 ?  170 SER B OG  1 
ATOM   1244  N N   . GLU A 1 155 ? 37.180  30.665  96.288  1.00 123.24 ?  171 GLU B N   1 
ATOM   1245  C CA  . GLU A 1 155 ? 37.016  31.239  94.956  1.00 130.20 ?  171 GLU B CA  1 
ATOM   1246  C C   . GLU A 1 155 ? 35.935  32.322  94.959  1.00 126.37 ?  171 GLU B C   1 
ATOM   1247  O O   . GLU A 1 155 ? 36.141  33.423  94.445  1.00 128.02 ?  171 GLU B O   1 
ATOM   1248  C CB  . GLU A 1 155 ? 36.693  30.110  93.966  1.00 135.31 ?  171 GLU B CB  1 
ATOM   1249  C CG  . GLU A 1 155 ? 37.540  30.043  92.674  1.00 146.99 ?  171 GLU B CG  1 
ATOM   1250  C CD  . GLU A 1 155 ? 37.297  31.202  91.701  1.00 155.56 ?  171 GLU B CD  1 
ATOM   1251  O OE1 . GLU A 1 155 ? 36.116  31.537  91.443  1.00 148.76 ?  171 GLU B OE1 1 
ATOM   1252  O OE2 . GLU A 1 155 ? 38.284  31.764  91.175  1.00 166.69 -1 171 GLU B OE2 1 
ATOM   1253  N N   . VAL A 1 156 ? 34.797  32.042  95.582  1.00 113.14 ?  172 VAL B N   1 
ATOM   1254  C CA  . VAL A 1 156 ? 33.645  32.931  95.538  1.00 102.37 ?  172 VAL B CA  1 
ATOM   1255  C C   . VAL A 1 156 ? 33.654  33.927  96.680  1.00 95.94  ?  172 VAL B C   1 
ATOM   1256  O O   . VAL A 1 156 ? 33.484  35.129  96.472  1.00 94.10  ?  172 VAL B O   1 
ATOM   1257  C CB  . VAL A 1 156 ? 32.375  32.075  95.547  1.00 96.14  ?  172 VAL B CB  1 
ATOM   1258  C CG1 . VAL A 1 156 ? 31.192  32.903  95.240  1.00 92.40  ?  172 VAL B CG1 1 
ATOM   1259  C CG2 . VAL A 1 156 ? 32.541  31.032  94.521  1.00 102.60 ?  172 VAL B CG2 1 
ATOM   1260  N N   . GLY A 1 157 ? 33.831  33.441  97.899  1.00 88.24  ?  173 GLY B N   1 
ATOM   1261  C CA  . GLY A 1 157 ? 33.969  34.297  99.057  1.00 84.72  ?  173 GLY B CA  1 
ATOM   1262  C C   . GLY A 1 157 ? 35.017  35.375  98.874  1.00 86.16  ?  173 GLY B C   1 
ATOM   1263  O O   . GLY A 1 157 ? 34.709  36.572  98.995  1.00 84.87  ?  173 GLY B O   1 
ATOM   1264  N N   . LYS A 1 158 ? 36.251  34.975  98.549  1.00 90.15  ?  174 LYS B N   1 
ATOM   1265  C CA  . LYS A 1 158 ? 37.312  35.963  98.410  1.00 90.20  ?  174 LYS B CA  1 
ATOM   1266  C C   . LYS A 1 158 ? 36.993  37.019  97.354  1.00 88.11  ?  174 LYS B C   1 
ATOM   1267  O O   . LYS A 1 158 ? 37.607  38.091  97.367  1.00 93.26  ?  174 LYS B O   1 
ATOM   1268  C CB  . LYS A 1 158 ? 38.650  35.278  98.102  1.00 93.95  ?  174 LYS B CB  1 
ATOM   1269  C CG  . LYS A 1 158 ? 39.513  34.795  99.297  1.00 88.95  ?  174 LYS B CG  1 
ATOM   1270  C CD  . LYS A 1 158 ? 40.562  33.778  98.812  1.00 89.90  ?  174 LYS B CD  1 
ATOM   1271  C CE  . LYS A 1 158 ? 41.396  33.157  99.910  1.00 88.29  ?  174 LYS B CE  1 
ATOM   1272  N NZ  . LYS A 1 158 ? 42.558  34.043  100.229 1.00 88.24  ?  174 LYS B NZ  1 
ATOM   1273  N N   . GLN A 1 159 ? 36.045  36.760  96.453  1.00 85.00  ?  175 GLN B N   1 
ATOM   1274  C CA  . GLN A 1 159 ? 35.585  37.825  95.564  1.00 82.03  ?  175 GLN B CA  1 
ATOM   1275  C C   . GLN A 1 159 ? 34.560  38.711  96.233  1.00 84.44  ?  175 GLN B C   1 
ATOM   1276  O O   . GLN A 1 159 ? 34.522  39.920  95.985  1.00 86.62  ?  175 GLN B O   1 
ATOM   1277  C CB  . GLN A 1 159 ? 34.919  37.250  94.337  1.00 87.60  ?  175 GLN B CB  1 
ATOM   1278  C CG  . GLN A 1 159 ? 35.754  36.352  93.560  1.00 100.25 ?  175 GLN B CG  1 
ATOM   1279  C CD  . GLN A 1 159 ? 35.018  35.897  92.352  1.00 105.73 ?  175 GLN B CD  1 
ATOM   1280  O OE1 . GLN A 1 159 ? 34.436  36.699  91.628  1.00 105.99 ?  175 GLN B OE1 1 
ATOM   1281  N NE2 . GLN A 1 159 ? 34.991  34.591  92.143  1.00 113.97 ?  175 GLN B NE2 1 
ATOM   1282  N N   . LEU A 1 160 ? 33.677  38.106  97.031  1.00 86.31  ?  176 LEU B N   1 
ATOM   1283  C CA  . LEU A 1 160 ? 32.583  38.851  97.624  1.00 78.35  ?  176 LEU B CA  1 
ATOM   1284  C C   . LEU A 1 160 ? 33.039  39.798  98.727  1.00 78.13  ?  176 LEU B C   1 
ATOM   1285  O O   . LEU A 1 160 ? 32.384  40.821  98.938  1.00 77.88  ?  176 LEU B O   1 
ATOM   1286  C CB  . LEU A 1 160 ? 31.534  37.875  98.140  1.00 77.24  ?  176 LEU B CB  1 
ATOM   1287  C CG  . LEU A 1 160 ? 30.936  37.073  96.986  1.00 77.18  ?  176 LEU B CG  1 
ATOM   1288  C CD1 . LEU A 1 160 ? 30.136  35.877  97.470  1.00 72.26  ?  176 LEU B CD1 1 
ATOM   1289  C CD2 . LEU A 1 160 ? 30.122  37.972  96.075  1.00 79.26  ?  176 LEU B CD2 1 
ATOM   1290  N N   . ARG A 1 161 ? 34.152  39.510  99.399  1.00 75.81  ?  177 ARG B N   1 
ATOM   1291  C CA  . ARG A 1 161 ? 34.576  40.320  100.543 1.00 76.35  ?  177 ARG B CA  1 
ATOM   1292  C C   . ARG A 1 161 ? 34.572  41.829  100.291 1.00 77.30  ?  177 ARG B C   1 
ATOM   1293  O O   . ARG A 1 161 ? 33.917  42.551  101.063 1.00 80.58  ?  177 ARG B O   1 
ATOM   1294  C CB  . ARG A 1 161 ? 35.949  39.809  100.983 1.00 80.55  ?  177 ARG B CB  1 
ATOM   1295  C CG  . ARG A 1 161 ? 36.606  40.511  102.157 1.00 81.84  ?  177 ARG B CG  1 
ATOM   1296  C CD  . ARG A 1 161 ? 35.763  40.367  103.392 1.00 81.40  ?  177 ARG B CD  1 
ATOM   1297  N NE  . ARG A 1 161 ? 36.268  41.180  104.490 1.00 84.30  ?  177 ARG B NE  1 
ATOM   1298  C CZ  . ARG A 1 161 ? 36.718  40.664  105.625 1.00 78.22  ?  177 ARG B CZ  1 
ATOM   1299  N NH1 . ARG A 1 161 ? 36.698  39.357  105.844 1.00 76.15  ?  177 ARG B NH1 1 
ATOM   1300  N NH2 . ARG A 1 161 ? 37.181  41.478  106.569 1.00 83.90  ?  177 ARG B NH2 1 
ATOM   1301  N N   . PRO A 1 162 ? 35.240  42.374  99.262  1.00 76.09  ?  178 PRO B N   1 
ATOM   1302  C CA  . PRO A 1 162 ? 35.223  43.843  99.097  1.00 77.64  ?  178 PRO B CA  1 
ATOM   1303  C C   . PRO A 1 162 ? 33.842  44.382  98.805  1.00 78.32  ?  178 PRO B C   1 
ATOM   1304  O O   . PRO A 1 162 ? 33.458  45.468  99.295  1.00 80.03  ?  178 PRO B O   1 
ATOM   1305  C CB  . PRO A 1 162 ? 36.175  44.066  97.917  1.00 74.00  ?  178 PRO B CB  1 
ATOM   1306  C CG  . PRO A 1 162 ? 36.083  42.797  97.151  1.00 72.26  ?  178 PRO B CG  1 
ATOM   1307  C CD  . PRO A 1 162 ? 36.019  41.733  98.194  1.00 73.56  ?  178 PRO B CD  1 
ATOM   1308  N N   . LEU A 1 163 ? 33.081  43.637  97.999  1.00 74.20  ?  179 LEU B N   1 
ATOM   1309  C CA  . LEU A 1 163 ? 31.712  44.027  97.706  1.00 72.20  ?  179 LEU B CA  1 
ATOM   1310  C C   . LEU A 1 163 ? 30.875  44.042  98.972  1.00 73.84  ?  179 LEU B C   1 
ATOM   1311  O O   . LEU A 1 163 ? 30.087  44.968  99.190  1.00 74.81  ?  179 LEU B O   1 
ATOM   1312  C CB  . LEU A 1 163 ? 31.109  43.085  96.677  1.00 69.82  ?  179 LEU B CB  1 
ATOM   1313  C CG  . LEU A 1 163 ? 31.833  43.129  95.344  1.00 70.03  ?  179 LEU B CG  1 
ATOM   1314  C CD1 . LEU A 1 163 ? 31.447  41.922  94.496  1.00 72.35  ?  179 LEU B CD1 1 
ATOM   1315  C CD2 . LEU A 1 163 ? 31.513  44.434  94.661  1.00 66.38  ?  179 LEU B CD2 1 
ATOM   1316  N N   . TYR A 1 164 ? 31.047  43.034  99.836  1.00 71.41  ?  180 TYR B N   1 
ATOM   1317  C CA  . TYR A 1 164 ? 30.240  42.984  101.047 1.00 68.68  ?  180 TYR B CA  1 
ATOM   1318  C C   . TYR A 1 164 ? 30.591  44.144  101.976 1.00 72.59  ?  180 TYR B C   1 
ATOM   1319  O O   . TYR A 1 164 ? 29.704  44.721  102.618 1.00 71.53  ?  180 TYR B O   1 
ATOM   1320  C CB  . TYR A 1 164 ? 30.415  41.648  101.774 1.00 65.91  ?  180 TYR B CB  1 
ATOM   1321  C CG  . TYR A 1 164 ? 29.174  41.268  102.551 1.00 64.99  ?  180 TYR B CG  1 
ATOM   1322  C CD1 . TYR A 1 164 ? 28.054  40.821  101.890 1.00 66.60  ?  180 TYR B CD1 1 
ATOM   1323  C CD2 . TYR A 1 164 ? 29.073  41.477  103.919 1.00 62.32  ?  180 TYR B CD2 1 
ATOM   1324  C CE1 . TYR A 1 164 ? 26.891  40.500  102.562 1.00 65.30  ?  180 TYR B CE1 1 
ATOM   1325  C CE2 . TYR A 1 164 ? 27.899  41.166  104.604 1.00 61.69  ?  180 TYR B CE2 1 
ATOM   1326  C CZ  . TYR A 1 164 ? 26.808  40.681  103.912 1.00 63.22  ?  180 TYR B CZ  1 
ATOM   1327  O OH  . TYR A 1 164 ? 25.617  40.372  104.544 1.00 63.21  ?  180 TYR B OH  1 
ATOM   1328  N N   . GLU A 1 165 ? 31.882  44.499  102.057 1.00 76.03  ?  181 GLU B N   1 
ATOM   1329  C CA  . GLU A 1 165 ? 32.289  45.659  102.847 1.00 76.75  ?  181 GLU B CA  1 
ATOM   1330  C C   . GLU A 1 165 ? 31.564  46.925  102.374 1.00 74.73  ?  181 GLU B C   1 
ATOM   1331  O O   . GLU A 1 165 ? 30.953  47.660  103.176 1.00 72.22  ?  181 GLU B O   1 
ATOM   1332  C CB  . GLU A 1 165 ? 33.820  45.816  102.775 1.00 80.11  ?  181 GLU B CB  1 
ATOM   1333  C CG  . GLU A 1 165 ? 34.671  44.588  103.255 1.00 80.86  ?  181 GLU B CG  1 
ATOM   1334  C CD  . GLU A 1 165 ? 36.194  44.874  103.373 1.00 89.83  ?  181 GLU B CD  1 
ATOM   1335  O OE1 . GLU A 1 165 ? 36.637  45.932  102.881 1.00 99.34  ?  181 GLU B OE1 1 
ATOM   1336  O OE2 . GLU A 1 165 ? 36.956  44.039  103.936 1.00 85.24  -1 181 GLU B OE2 1 
ATOM   1337  N N   . GLU A 1 166 ? 31.594  47.184  101.061 1.00 77.49  ?  182 GLU B N   1 
ATOM   1338  C CA  . GLU A 1 166 ? 30.960  48.407  100.573 1.00 81.09  ?  182 GLU B CA  1 
ATOM   1339  C C   . GLU A 1 166 ? 29.440  48.331  100.690 1.00 76.88  ?  182 GLU B C   1 
ATOM   1340  O O   . GLU A 1 166 ? 28.768  49.344  100.941 1.00 75.16  ?  182 GLU B O   1 
ATOM   1341  C CB  . GLU A 1 166 ? 31.385  48.685  99.134  1.00 80.41  ?  182 GLU B CB  1 
ATOM   1342  C CG  . GLU A 1 166 ? 30.955  50.063  98.684  1.00 87.34  ?  182 GLU B CG  1 
ATOM   1343  C CD  . GLU A 1 166 ? 31.484  50.415  97.328  1.00 94.97  ?  182 GLU B CD  1 
ATOM   1344  O OE1 . GLU A 1 166 ? 32.507  49.816  96.937  1.00 102.18 ?  182 GLU B OE1 1 
ATOM   1345  O OE2 . GLU A 1 166 ? 30.874  51.274  96.655  1.00 101.10 -1 182 GLU B OE2 1 
ATOM   1346  N N   . TYR A 1 167 ? 28.888  47.132  100.513 1.00 71.42  ?  183 TYR B N   1 
ATOM   1347  C CA  . TYR A 1 167 ? 27.461  46.895  100.701 1.00 70.24  ?  183 TYR B CA  1 
ATOM   1348  C C   . TYR A 1 167 ? 27.010  47.229  102.117 1.00 68.52  ?  183 TYR B C   1 
ATOM   1349  O O   . TYR A 1 167 ? 25.943  47.827  102.316 1.00 64.42  ?  183 TYR B O   1 
ATOM   1350  C CB  . TYR A 1 167 ? 27.168  45.441  100.336 1.00 68.09  ?  183 TYR B CB  1 
ATOM   1351  C CG  . TYR A 1 167 ? 25.975  44.782  100.977 1.00 65.76  ?  183 TYR B CG  1 
ATOM   1352  C CD1 . TYR A 1 167 ? 24.702  44.814  100.402 1.00 63.10  ?  183 TYR B CD1 1 
ATOM   1353  C CD2 . TYR A 1 167 ? 26.143  44.056  102.133 1.00 70.71  ?  183 TYR B CD2 1 
ATOM   1354  C CE1 . TYR A 1 167 ? 23.609  44.151  101.009 1.00 62.65  ?  183 TYR B CE1 1 
ATOM   1355  C CE2 . TYR A 1 167 ? 25.082  43.394  102.748 1.00 71.45  ?  183 TYR B CE2 1 
ATOM   1356  C CZ  . TYR A 1 167 ? 23.825  43.436  102.193 1.00 66.08  ?  183 TYR B CZ  1 
ATOM   1357  O OH  . TYR A 1 167 ? 22.859  42.734  102.874 1.00 59.67  ?  183 TYR B OH  1 
ATOM   1358  N N   . VAL A 1 168 ? 27.823  46.883  103.114 1.00 69.59  ?  184 VAL B N   1 
ATOM   1359  C CA  . VAL A 1 168 ? 27.457  47.260  104.470 1.00 65.00  ?  184 VAL B CA  1 
ATOM   1360  C C   . VAL A 1 168 ? 27.542  48.769  104.614 1.00 65.84  ?  184 VAL B C   1 
ATOM   1361  O O   . VAL A 1 168 ? 26.655  49.388  105.206 1.00 67.34  ?  184 VAL B O   1 
ATOM   1362  C CB  . VAL A 1 168 ? 28.328  46.547  105.513 1.00 61.30  ?  184 VAL B CB  1 
ATOM   1363  C CG1 . VAL A 1 168 ? 27.985  47.078  106.880 1.00 60.52  ?  184 VAL B CG1 1 
ATOM   1364  C CG2 . VAL A 1 168 ? 28.160  45.059  105.413 1.00 59.87  ?  184 VAL B CG2 1 
ATOM   1365  N N   . VAL A 1 169 ? 28.571  49.394  104.028 1.00 65.23  ?  185 VAL B N   1 
ATOM   1366  C CA  . VAL A 1 169 ? 28.722  50.843  104.181 1.00 67.25  ?  185 VAL B CA  1 
ATOM   1367  C C   . VAL A 1 169 ? 27.490  51.578  103.660 1.00 72.39  ?  185 VAL B C   1 
ATOM   1368  O O   . VAL A 1 169 ? 26.951  52.501  104.304 1.00 74.08  ?  185 VAL B O   1 
ATOM   1369  C CB  . VAL A 1 169 ? 29.965  51.340  103.445 1.00 67.81  ?  185 VAL B CB  1 
ATOM   1370  C CG1 . VAL A 1 169 ? 29.922  52.849  103.427 1.00 67.48  ?  185 VAL B CG1 1 
ATOM   1371  C CG2 . VAL A 1 169 ? 31.212  50.791  104.076 1.00 70.56  ?  185 VAL B CG2 1 
ATOM   1372  N N   . LEU A 1 170 ? 27.024  51.171  102.475 1.00 70.85  ?  186 LEU B N   1 
ATOM   1373  C CA  . LEU A 1 170 ? 25.935  51.878  101.803 1.00 67.67  ?  186 LEU B CA  1 
ATOM   1374  C C   . LEU A 1 170 ? 24.595  51.551  102.435 1.00 66.94  ?  186 LEU B C   1 
ATOM   1375  O O   . LEU A 1 170 ? 23.775  52.450  102.670 1.00 70.44  ?  186 LEU B O   1 
ATOM   1376  C CB  . LEU A 1 170 ? 25.899  51.529  100.317 1.00 64.76  ?  186 LEU B CB  1 
ATOM   1377  C CG  . LEU A 1 170 ? 27.027  52.123  99.507  1.00 69.38  ?  186 LEU B CG  1 
ATOM   1378  C CD1 . LEU A 1 170 ? 27.245  51.310  98.269  1.00 73.10  ?  186 LEU B CD1 1 
ATOM   1379  C CD2 . LEU A 1 170 ? 26.622  53.516  99.170  1.00 76.23  ?  186 LEU B CD2 1 
ATOM   1380  N N   . LYS A 1 171 ? 24.334  50.264  102.678 1.00 66.74  ?  187 LYS B N   1 
ATOM   1381  C CA  . LYS A 1 171 ? 23.096  49.908  103.338 1.00 64.72  ?  187 LYS B CA  1 
ATOM   1382  C C   . LYS A 1 171 ? 22.954  50.674  104.635 1.00 68.83  ?  187 LYS B C   1 
ATOM   1383  O O   . LYS A 1 171 ? 21.859  51.143  104.965 1.00 71.20  ?  187 LYS B O   1 
ATOM   1384  C CB  . LYS A 1 171 ? 23.047  48.412  103.603 1.00 63.51  ?  187 LYS B CB  1 
ATOM   1385  C CG  . LYS A 1 171 ? 22.781  47.592  102.377 1.00 64.98  ?  187 LYS B CG  1 
ATOM   1386  C CD  . LYS A 1 171 ? 21.336  47.637  102.028 1.00 62.43  ?  187 LYS B CD  1 
ATOM   1387  C CE  . LYS A 1 171 ? 21.050  46.859  100.793 1.00 60.40  ?  187 LYS B CE  1 
ATOM   1388  N NZ  . LYS A 1 171 ? 19.574  46.779  100.666 1.00 62.23  ?  187 LYS B NZ  1 
ATOM   1389  N N   . ASN A 1 172 ? 24.059  50.824  105.381 1.00 65.63  ?  188 ASN B N   1 
ATOM   1390  C CA  . ASN A 1 172 ? 23.997  51.531  106.652 1.00 65.60  ?  188 ASN B CA  1 
ATOM   1391  C C   . ASN A 1 172 ? 23.653  52.996  106.433 1.00 69.16  ?  188 ASN B C   1 
ATOM   1392  O O   . ASN A 1 172 ? 22.824  53.564  107.160 1.00 69.99  ?  188 ASN B O   1 
ATOM   1393  C CB  . ASN A 1 172 ? 25.326  51.368  107.391 1.00 67.39  ?  188 ASN B CB  1 
ATOM   1394  C CG  . ASN A 1 172 ? 25.290  50.243  108.390 1.00 66.62  ?  188 ASN B CG  1 
ATOM   1395  O OD1 . ASN A 1 172 ? 24.216  49.798  108.769 1.00 66.18  ?  188 ASN B OD1 1 
ATOM   1396  N ND2 . ASN A 1 172 ? 26.461  49.721  108.762 1.00 62.86  ?  188 ASN B ND2 1 
ATOM   1397  N N   . GLU A 1 173 ? 24.272  53.628  105.427 1.00 75.89  ?  189 GLU B N   1 
ATOM   1398  C CA  . GLU A 1 173 ? 23.899  55.008  105.114 1.00 77.76  ?  189 GLU B CA  1 
ATOM   1399  C C   . GLU A 1 173 ? 22.416  55.117  104.829 1.00 69.65  ?  189 GLU B C   1 
ATOM   1400  O O   . GLU A 1 173 ? 21.741  56.029  105.320 1.00 73.66  ?  189 GLU B O   1 
ATOM   1401  C CB  . GLU A 1 173 ? 24.718  55.521  103.933 1.00 78.37  ?  189 GLU B CB  1 
ATOM   1402  C CG  . GLU A 1 173 ? 26.175  55.700  104.334 1.00 90.44  ?  189 GLU B CG  1 
ATOM   1403  C CD  . GLU A 1 173 ? 26.992  56.305  103.250 1.00 94.91  ?  189 GLU B CD  1 
ATOM   1404  O OE1 . GLU A 1 173 ? 26.375  56.910  102.349 1.00 92.58  ?  189 GLU B OE1 1 
ATOM   1405  O OE2 . GLU A 1 173 ? 28.242  56.238  103.338 1.00 101.42 -1 189 GLU B OE2 1 
ATOM   1406  N N   . MET A 1 174 ? 21.895  54.166  104.067 1.00 68.03  ?  190 MET B N   1 
ATOM   1407  C CA  . MET A 1 174 ? 20.489  54.178  103.681 1.00 68.54  ?  190 MET B CA  1 
ATOM   1408  C C   . MET A 1 174 ? 19.571  53.968  104.881 1.00 68.85  ?  190 MET B C   1 
ATOM   1409  O O   . MET A 1 174 ? 18.524  54.612  104.997 1.00 69.85  ?  190 MET B O   1 
ATOM   1410  C CB  . MET A 1 174 ? 20.291  53.097  102.628 1.00 64.75  ?  190 MET B CB  1 
ATOM   1411  C CG  . MET A 1 174 ? 18.925  52.849  102.074 1.00 67.47  ?  190 MET B CG  1 
ATOM   1412  S SD  . MET A 1 174 ? 18.071  51.646  103.112 1.00 67.49  ?  190 MET B SD  1 
ATOM   1413  C CE  . MET A 1 174 ? 17.185  50.627  101.932 1.00 71.59  ?  190 MET B CE  1 
ATOM   1414  N N   . ALA A 1 175 ? 19.944  53.081  105.789 1.00 73.05  ?  191 ALA B N   1 
ATOM   1415  C CA  . ALA A 1 175 ? 19.040  52.845  106.889 1.00 68.85  ?  191 ALA B CA  1 
ATOM   1416  C C   . ALA A 1 175 ? 19.099  53.986  107.873 1.00 66.63  ?  191 ALA B C   1 
ATOM   1417  O O   . ALA A 1 175 ? 18.091  54.287  108.510 1.00 66.29  ?  191 ALA B O   1 
ATOM   1418  C CB  . ALA A 1 175 ? 19.350  51.520  107.563 1.00 69.83  ?  191 ALA B CB  1 
ATOM   1419  N N   . ARG A 1 176 ? 20.254  54.639  108.001 1.00 59.52  ?  192 ARG B N   1 
ATOM   1420  C CA  . ARG A 1 176 ? 20.325  55.801  108.875 1.00 64.32  ?  192 ARG B CA  1 
ATOM   1421  C C   . ARG A 1 176 ? 19.561  56.965  108.266 1.00 66.68  ?  192 ARG B C   1 
ATOM   1422  O O   . ARG A 1 176 ? 18.889  57.718  108.986 1.00 63.95  ?  192 ARG B O   1 
ATOM   1423  C CB  . ARG A 1 176 ? 21.793  56.157  109.174 1.00 68.14  ?  192 ARG B CB  1 
ATOM   1424  C CG  . ARG A 1 176 ? 22.606  55.076  109.890 1.00 66.08  ?  192 ARG B CG  1 
ATOM   1425  C CD  . ARG A 1 176 ? 24.061  55.496  110.077 1.00 70.20  ?  192 ARG B CD  1 
ATOM   1426  N NE  . ARG A 1 176 ? 24.960  54.346  110.161 1.00 72.12  ?  192 ARG B NE  1 
ATOM   1427  C CZ  . ARG A 1 176 ? 25.136  53.656  111.289 1.00 80.45  ?  192 ARG B CZ  1 
ATOM   1428  N NH1 . ARG A 1 176 ? 24.565  54.040  112.434 1.00 84.94  ?  192 ARG B NH1 1 
ATOM   1429  N NH2 . ARG A 1 176 ? 25.921  52.573  111.283 1.00 76.50  ?  192 ARG B NH2 1 
ATOM   1430  N N   . ALA A 1 177 ? 19.607  57.067  106.943 1.00 71.12  ?  193 ALA B N   1 
ATOM   1431  C CA  . ALA A 1 177 ? 18.894  58.160  106.255 1.00 72.65  ?  193 ALA B CA  1 
ATOM   1432  C C   . ALA A 1 177 ? 17.403  57.868  106.284 1.00 71.65  ?  193 ALA B C   1 
ATOM   1433  O O   . ALA A 1 177 ? 16.619  58.799  106.061 1.00 73.42  ?  193 ALA B O   1 
ATOM   1434  C CB  . ALA A 1 177 ? 19.390  58.262  104.846 1.00 78.21  ?  193 ALA B CB  1 
ATOM   1435  N N   . ASN A 1 178 ? 17.043  56.605  106.504 1.00 68.07  ?  194 ASN B N   1 
ATOM   1436  C CA  . ASN A 1 178 ? 15.608  56.243  106.625 1.00 66.70  ?  194 ASN B CA  1 
ATOM   1437  C C   . ASN A 1 178 ? 15.261  56.296  108.111 1.00 65.20  ?  194 ASN B C   1 
ATOM   1438  O O   . ASN A 1 178 ? 14.239  55.718  108.493 1.00 64.66  ?  194 ASN B O   1 
ATOM   1439  C CB  . ASN A 1 178 ? 15.295  54.926  105.919 1.00 66.47  ?  194 ASN B CB  1 
ATOM   1440  C CG  . ASN A 1 178 ? 15.071  55.110  104.434 1.00 82.40  ?  194 ASN B CG  1 
ATOM   1441  O OD1 . ASN A 1 178 ? 15.684  54.433  103.618 1.00 84.25  ?  194 ASN B OD1 1 
ATOM   1442  N ND2 . ASN A 1 178 ? 14.190  56.030  104.081 1.00 82.80  ?  194 ASN B ND2 1 
ATOM   1443  N N   . HIS A 1 179 ? 16.129  56.921  108.904 1.00 63.16  ?  195 HIS B N   1 
ATOM   1444  C CA  . HIS A 1 179 ? 15.837  57.149  110.343 1.00 64.03  ?  195 HIS B CA  1 
ATOM   1445  C C   . HIS A 1 179 ? 15.988  55.871  111.183 1.00 63.37  ?  195 HIS B C   1 
ATOM   1446  O O   . HIS A 1 179 ? 15.374  55.828  112.258 1.00 61.69  ?  195 HIS B O   1 
ATOM   1447  C CB  . HIS A 1 179 ? 14.486  57.877  110.445 1.00 63.72  ?  195 HIS B CB  1 
ATOM   1448  C CG  . HIS A 1 179 ? 14.411  59.113  109.612 1.00 58.70  ?  195 HIS B CG  1 
ATOM   1449  N ND1 . HIS A 1 179 ? 13.440  59.304  108.650 1.00 61.32  ?  195 HIS B ND1 1 
ATOM   1450  C CD2 . HIS A 1 179 ? 15.179  60.219  109.601 1.00 64.53  ?  195 HIS B CD2 1 
ATOM   1451  C CE1 . HIS A 1 179 ? 13.611  60.480  108.081 1.00 54.26  ?  195 HIS B CE1 1 
ATOM   1452  N NE2 . HIS A 1 179 ? 14.676  61.061  108.651 1.00 53.86  ?  195 HIS B NE2 1 
ATOM   1453  N N   . TYR A 1 180 ? 16.809  54.905  110.756 1.00 58.10  ?  196 TYR B N   1 
ATOM   1454  C CA  . TYR A 1 180 ? 17.086  53.702  111.591 1.00 60.86  ?  196 TYR B CA  1 
ATOM   1455  C C   . TYR A 1 180 ? 18.529  53.794  112.085 1.00 65.22  ?  196 TYR B C   1 
ATOM   1456  O O   . TYR A 1 180 ? 19.290  54.590  111.528 1.00 69.17  ?  196 TYR B O   1 
ATOM   1457  C CB  . TYR A 1 180 ? 16.835  52.415  110.809 1.00 63.80  ?  196 TYR B CB  1 
ATOM   1458  C CG  . TYR A 1 180 ? 15.386  52.099  110.558 1.00 61.70  ?  196 TYR B CG  1 
ATOM   1459  C CD1 . TYR A 1 180 ? 14.732  52.661  109.480 1.00 60.17  ?  196 TYR B CD1 1 
ATOM   1460  C CD2 . TYR A 1 180 ? 14.663  51.266  111.395 1.00 58.50  ?  196 TYR B CD2 1 
ATOM   1461  C CE1 . TYR A 1 180 ? 13.398  52.403  109.229 1.00 54.41  ?  196 TYR B CE1 1 
ATOM   1462  C CE2 . TYR A 1 180 ? 13.326  50.996  111.159 1.00 60.20  ?  196 TYR B CE2 1 
ATOM   1463  C CZ  . TYR A 1 180 ? 12.691  51.567  110.072 1.00 54.97  ?  196 TYR B CZ  1 
ATOM   1464  O OH  . TYR A 1 180 ? 11.375  51.311  109.826 1.00 51.60  ?  196 TYR B OH  1 
ATOM   1465  N N   . GLU A 1 181 ? 18.894  53.036  113.118 1.00 66.22  ?  197 GLU B N   1 
ATOM   1466  C CA  . GLU A 1 181 ? 20.258  53.226  113.689 1.00 74.77  ?  197 GLU B CA  1 
ATOM   1467  C C   . GLU A 1 181 ? 21.266  52.486  112.818 1.00 69.02  ?  197 GLU B C   1 
ATOM   1468  O O   . GLU A 1 181 ? 22.303  53.066  112.505 1.00 69.84  ?  197 GLU B O   1 
ATOM   1469  C CB  . GLU A 1 181 ? 20.316  52.873  115.182 1.00 76.67  ?  197 GLU B CB  1 
ATOM   1470  C CG  . GLU A 1 181 ? 19.676  51.569  115.593 1.00 79.48  ?  197 GLU B CG  1 
ATOM   1471  C CD  . GLU A 1 181 ? 19.753  51.359  117.097 1.00 75.31  ?  197 GLU B CD  1 
ATOM   1472  O OE1 . GLU A 1 181 ? 19.359  52.281  117.836 1.00 65.36  ?  197 GLU B OE1 1 
ATOM   1473  O OE2 . GLU A 1 181 ? 20.232  50.291  117.529 1.00 71.60  -1 197 GLU B OE2 1 
ATOM   1474  N N   . ASP A 1 182 ? 20.960  51.259  112.435 1.00 60.25  ?  198 ASP B N   1 
ATOM   1475  C CA  . ASP A 1 182 ? 21.844  50.562  111.515 1.00 60.37  ?  198 ASP B CA  1 
ATOM   1476  C C   . ASP A 1 182 ? 20.938  49.720  110.629 1.00 62.65  ?  198 ASP B C   1 
ATOM   1477  O O   . ASP A 1 182 ? 19.714  49.712  110.803 1.00 62.83  ?  198 ASP B O   1 
ATOM   1478  C CB  . ASP A 1 182 ? 22.927  49.719  112.249 1.00 63.20  ?  198 ASP B CB  1 
ATOM   1479  C CG  . ASP A 1 182 ? 22.355  48.644  113.232 1.00 65.07  ?  198 ASP B CG  1 
ATOM   1480  O OD1 . ASP A 1 182 ? 21.744  47.669  112.736 1.00 61.67  ?  198 ASP B OD1 1 
ATOM   1481  O OD2 . ASP A 1 182 ? 22.467  48.764  114.488 1.00 66.97  -1 198 ASP B OD2 1 
ATOM   1482  N N   . TYR A 1 183 ? 21.534  49.027  109.658 1.00 60.70  ?  199 TYR B N   1 
ATOM   1483  C CA  . TYR A 1 183 ? 20.737  48.249  108.710 1.00 58.40  ?  199 TYR B CA  1 
ATOM   1484  C C   . TYR A 1 183 ? 20.051  47.059  109.379 1.00 58.31  ?  199 TYR B C   1 
ATOM   1485  O O   . TYR A 1 183 ? 18.926  46.698  109.003 1.00 57.34  ?  199 TYR B O   1 
ATOM   1486  C CB  . TYR A 1 183 ? 21.616  47.813  107.538 1.00 57.18  ?  199 TYR B CB  1 
ATOM   1487  C CG  . TYR A 1 183 ? 20.878  47.146  106.389 1.00 56.25  ?  199 TYR B CG  1 
ATOM   1488  C CD1 . TYR A 1 183 ? 19.691  47.661  105.889 1.00 55.85  ?  199 TYR B CD1 1 
ATOM   1489  C CD2 . TYR A 1 183 ? 21.394  46.007  105.779 1.00 54.54  ?  199 TYR B CD2 1 
ATOM   1490  C CE1 . TYR A 1 183 ? 19.010  47.020  104.822 1.00 59.87  ?  199 TYR B CE1 1 
ATOM   1491  C CE2 . TYR A 1 183 ? 20.738  45.370  104.723 1.00 54.89  ?  199 TYR B CE2 1 
ATOM   1492  C CZ  . TYR A 1 183 ? 19.544  45.866  104.242 1.00 55.04  ?  199 TYR B CZ  1 
ATOM   1493  O OH  . TYR A 1 183 ? 18.890  45.215  103.195 1.00 50.30  ?  199 TYR B OH  1 
ATOM   1494  N N   . GLY A 1 184 ? 20.688  46.456  110.386 1.00 58.39  ?  200 GLY B N   1 
ATOM   1495  C CA  . GLY A 1 184 ? 20.016  45.407  111.135 1.00 56.60  ?  200 GLY B CA  1 
ATOM   1496  C C   . GLY A 1 184 ? 18.770  45.907  111.835 1.00 53.38  ?  200 GLY B C   1 
ATOM   1497  O O   . GLY A 1 184 ? 17.758  45.211  111.892 1.00 53.16  ?  200 GLY B O   1 
ATOM   1498  N N   . ASP A 1 185 ? 18.822  47.129  112.356 1.00 55.39  ?  201 ASP B N   1 
ATOM   1499  C CA  . ASP A 1 185 ? 17.670  47.714  113.013 1.00 53.96  ?  201 ASP B CA  1 
ATOM   1500  C C   . ASP A 1 185 ? 16.530  47.864  112.028 1.00 56.42  ?  201 ASP B C   1 
ATOM   1501  O O   . ASP A 1 185 ? 15.360  47.651  112.371 1.00 58.60  ?  201 ASP B O   1 
ATOM   1502  C CB  . ASP A 1 185 ? 18.064  49.069  113.565 1.00 58.25  ?  201 ASP B CB  1 
ATOM   1503  C CG  . ASP A 1 185 ? 17.028  49.652  114.463 1.00 60.00  ?  201 ASP B CG  1 
ATOM   1504  O OD1 . ASP A 1 185 ? 16.419  48.909  115.281 1.00 57.64  ?  201 ASP B OD1 1 
ATOM   1505  O OD2 . ASP A 1 185 ? 16.820  50.866  114.339 1.00 62.79  -1 201 ASP B OD2 1 
ATOM   1506  N N   . TYR A 1 186 ? 16.873  48.197  110.790 1.00 55.77  ?  202 TYR B N   1 
ATOM   1507  C CA  . TYR A 1 186 ? 15.897  48.305  109.716 1.00 53.75  ?  202 TYR B CA  1 
ATOM   1508  C C   . TYR A 1 186 ? 15.251  46.957  109.419 1.00 51.50  ?  202 TYR B C   1 
ATOM   1509  O O   . TYR A 1 186 ? 14.020  46.861  109.383 1.00 49.84  ?  202 TYR B O   1 
ATOM   1510  C CB  . TYR A 1 186 ? 16.621  48.927  108.529 1.00 54.33  ?  202 TYR B CB  1 
ATOM   1511  C CG  . TYR A 1 186 ? 15.973  49.154  107.177 1.00 55.18  ?  202 TYR B CG  1 
ATOM   1512  C CD1 . TYR A 1 186 ? 15.885  48.136  106.234 1.00 53.56  ?  202 TYR B CD1 1 
ATOM   1513  C CD2 . TYR A 1 186 ? 15.566  50.428  106.798 1.00 54.70  ?  202 TYR B CD2 1 
ATOM   1514  C CE1 . TYR A 1 186 ? 15.373  48.380  104.967 1.00 60.64  ?  202 TYR B CE1 1 
ATOM   1515  C CE2 . TYR A 1 186 ? 15.060  50.681  105.543 1.00 59.53  ?  202 TYR B CE2 1 
ATOM   1516  C CZ  . TYR A 1 186 ? 14.953  49.659  104.633 1.00 63.59  ?  202 TYR B CZ  1 
ATOM   1517  O OH  . TYR A 1 186 ? 14.419  49.928  103.390 1.00 70.71  ?  202 TYR B OH  1 
ATOM   1518  N N   . TRP A 1 187 ? 16.049  45.890  109.257 1.00 51.16  ?  203 TRP B N   1 
ATOM   1519  C CA  . TRP A 1 187 ? 15.431  44.586  109.016 1.00 50.37  ?  203 TRP B CA  1 
ATOM   1520  C C   . TRP A 1 187 ? 14.553  44.173  110.190 1.00 48.99  ?  203 TRP B C   1 
ATOM   1521  O O   . TRP A 1 187 ? 13.558  43.455  110.014 1.00 44.51  ?  203 TRP B O   1 
ATOM   1522  C CB  . TRP A 1 187 ? 16.455  43.484  108.804 1.00 56.13  ?  203 TRP B CB  1 
ATOM   1523  C CG  . TRP A 1 187 ? 16.990  43.343  107.457 1.00 53.67  ?  203 TRP B CG  1 
ATOM   1524  C CD1 . TRP A 1 187 ? 16.522  43.922  106.342 1.00 57.11  ?  203 TRP B CD1 1 
ATOM   1525  C CD2 . TRP A 1 187 ? 18.027  42.449  107.047 1.00 52.72  ?  203 TRP B CD2 1 
ATOM   1526  N NE1 . TRP A 1 187 ? 17.273  43.534  105.254 1.00 57.63  ?  203 TRP B NE1 1 
ATOM   1527  C CE2 . TRP A 1 187 ? 18.191  42.609  105.668 1.00 56.33  ?  203 TRP B CE2 1 
ATOM   1528  C CE3 . TRP A 1 187 ? 18.855  41.556  107.721 1.00 54.06  ?  203 TRP B CE3 1 
ATOM   1529  C CZ2 . TRP A 1 187 ? 19.142  41.910  104.947 1.00 59.44  ?  203 TRP B CZ2 1 
ATOM   1530  C CZ3 . TRP A 1 187 ? 19.807  40.859  107.003 1.00 54.86  ?  203 TRP B CZ3 1 
ATOM   1531  C CH2 . TRP A 1 187 ? 19.939  41.039  105.635 1.00 58.27  ?  203 TRP B CH2 1 
ATOM   1532  N N   . ARG A 1 188 ? 14.878  44.638  111.391 1.00 52.29  ?  204 ARG B N   1 
ATOM   1533  C CA  . ARG A 1 188 ? 14.113  44.178  112.581 1.00 51.68  ?  204 ARG B CA  1 
ATOM   1534  C C   . ARG A 1 188 ? 12.773  44.911  112.654 1.00 47.49  ?  204 ARG B C   1 
ATOM   1535  O O   . ARG A 1 188 ? 11.883  44.436  113.360 1.00 49.99  ?  204 ARG B O   1 
ATOM   1536  C CB  . ARG A 1 188 ? 14.932  44.372  113.859 1.00 48.81  ?  204 ARG B CB  1 
ATOM   1537  C CG  . ARG A 1 188 ? 16.106  43.415  114.005 1.00 49.07  ?  204 ARG B CG  1 
ATOM   1538  C CD  . ARG A 1 188 ? 16.686  43.448  115.406 1.00 58.85  ?  204 ARG B CD  1 
ATOM   1539  N NE  . ARG A 1 188 ? 17.309  44.723  115.728 1.00 56.91  ?  204 ARG B NE  1 
ATOM   1540  C CZ  . ARG A 1 188 ? 18.542  45.064  115.379 1.00 56.69  ?  204 ARG B CZ  1 
ATOM   1541  N NH1 . ARG A 1 188 ? 19.290  44.222  114.689 1.00 56.83  ?  204 ARG B NH1 1 
ATOM   1542  N NH2 . ARG A 1 188 ? 19.025  46.245  115.719 1.00 60.61  ?  204 ARG B NH2 1 
ATOM   1543  N N   . GLY A 1 189 ? 12.635  46.009  111.925 1.00 45.09  ?  205 GLY B N   1 
ATOM   1544  C CA  . GLY A 1 189 ? 11.390  46.789  111.975 1.00 49.61  ?  205 GLY B CA  1 
ATOM   1545  C C   . GLY A 1 189 ? 10.185  45.948  111.629 1.00 48.72  ?  205 GLY B C   1 
ATOM   1546  O O   . GLY A 1 189 ? 9.090   46.280  112.076 1.00 46.18  ?  205 GLY B O   1 
ATOM   1547  N N   . ASP A 1 190 ? 10.379  44.899  110.844 1.00 48.78  ?  206 ASP B N   1 
ATOM   1548  C CA  . ASP A 1 190 ? 9.220   44.093  110.395 1.00 45.99  ?  206 ASP B CA  1 
ATOM   1549  C C   . ASP A 1 190 ? 8.387   43.738  111.615 1.00 43.64  ?  206 ASP B C   1 
ATOM   1550  O O   . ASP A 1 190 ? 7.168   43.605  111.469 1.00 48.64  ?  206 ASP B O   1 
ATOM   1551  C CB  . ASP A 1 190 ? 9.653   42.836  109.642 1.00 49.45  ?  206 ASP B CB  1 
ATOM   1552  C CG  . ASP A 1 190 ? 8.502   42.090  109.003 1.00 48.89  ?  206 ASP B CG  1 
ATOM   1553  O OD1 . ASP A 1 190 ? 8.126   42.453  107.879 1.00 50.65  ?  206 ASP B OD1 1 
ATOM   1554  O OD2 . ASP A 1 190 ? 7.996   41.156  109.636 1.00 49.47  -1 206 ASP B OD2 1 
ATOM   1555  N N   . TYR A 1 191 ? 9.023   43.603  112.778 1.00 48.43  ?  207 TYR B N   1 
ATOM   1556  C CA  . TYR A 1 191 ? 8.239   43.153  113.917 1.00 46.48  ?  207 TYR B CA  1 
ATOM   1557  C C   . TYR A 1 191 ? 7.718   44.304  114.763 1.00 47.70  ?  207 TYR B C   1 
ATOM   1558  O O   . TYR A 1 191 ? 7.156   44.044  115.827 1.00 50.17  ?  207 TYR B O   1 
ATOM   1559  C CB  . TYR A 1 191 ? 9.063   42.203  114.783 1.00 42.82  ?  207 TYR B CB  1 
ATOM   1560  C CG  . TYR A 1 191 ? 9.560   40.998  114.018 1.00 46.45  ?  207 TYR B CG  1 
ATOM   1561  C CD1 . TYR A 1 191 ? 10.734  41.061  113.257 1.00 45.74  ?  207 TYR B CD1 1 
ATOM   1562  C CD2 . TYR A 1 191 ? 8.844   39.804  114.016 1.00 47.01  ?  207 TYR B CD2 1 
ATOM   1563  C CE1 . TYR A 1 191 ? 11.175  39.963  112.536 1.00 47.78  ?  207 TYR B CE1 1 
ATOM   1564  C CE2 . TYR A 1 191 ? 9.288   38.700  113.300 1.00 47.57  ?  207 TYR B CE2 1 
ATOM   1565  C CZ  . TYR A 1 191 ? 10.450  38.785  112.557 1.00 47.94  ?  207 TYR B CZ  1 
ATOM   1566  O OH  . TYR A 1 191 ? 10.881  37.682  111.838 1.00 47.10  ?  207 TYR B OH  1 
ATOM   1567  N N   . GLU A 1 192 ? 7.858   45.553  114.298 1.00 45.25  ?  208 GLU B N   1 
ATOM   1568  C CA  . GLU A 1 192 ? 7.531   46.727  115.103 1.00 46.19  ?  208 GLU B CA  1 
ATOM   1569  C C   . GLU A 1 192 ? 6.030   46.865  115.263 1.00 50.21  ?  208 GLU B C   1 
ATOM   1570  O O   . GLU A 1 192 ? 5.278   46.528  114.343 1.00 52.43  ?  208 GLU B O   1 
ATOM   1571  C CB  . GLU A 1 192 ? 8.094   47.980  114.434 1.00 47.14  ?  208 GLU B CB  1 
ATOM   1572  C CG  . GLU A 1 192 ? 8.156   49.264  115.266 1.00 51.95  ?  208 GLU B CG  1 
ATOM   1573  C CD  . GLU A 1 192 ? 8.961   50.368  114.556 1.00 60.17  ?  208 GLU B CD  1 
ATOM   1574  O OE1 . GLU A 1 192 ? 9.354   50.221  113.367 1.00 60.18  ?  208 GLU B OE1 1 
ATOM   1575  O OE2 . GLU A 1 192 ? 9.204   51.413  115.178 1.00 64.80  -1 208 GLU B OE2 1 
ATOM   1576  N N   . VAL A 1 193 ? 5.593   47.376  116.433 1.00 55.67  ?  209 VAL B N   1 
ATOM   1577  C CA  . VAL A 1 193 ? 4.190   47.754  116.697 1.00 55.81  ?  209 VAL B CA  1 
ATOM   1578  C C   . VAL A 1 193 ? 4.095   48.899  117.721 1.00 63.74  ?  209 VAL B C   1 
ATOM   1579  O O   . VAL A 1 193 ? 4.346   48.692  118.913 1.00 65.74  ?  209 VAL B O   1 
ATOM   1580  C CB  . VAL A 1 193 ? 3.356   46.556  117.215 1.00 52.09  ?  209 VAL B CB  1 
ATOM   1581  C CG1 . VAL A 1 193 ? 2.000   47.014  117.641 1.00 54.78  ?  209 VAL B CG1 1 
ATOM   1582  C CG2 . VAL A 1 193 ? 3.195   45.469  116.203 1.00 52.86  ?  209 VAL B CG2 1 
ATOM   1583  N N   . ASN A 1 194 ? 3.698   50.102  117.302 1.00 73.92  ?  210 ASN B N   1 
ATOM   1584  C CA  . ASN A 1 194 ? 3.283   51.128  118.256 1.00 76.72  ?  210 ASN B CA  1 
ATOM   1585  C C   . ASN A 1 194 ? 1.791   51.386  118.297 1.00 78.84  ?  210 ASN B C   1 
ATOM   1586  O O   . ASN A 1 194 ? 1.083   51.308  117.293 1.00 76.35  ?  210 ASN B O   1 
ATOM   1587  C CB  . ASN A 1 194 ? 3.895   52.509  118.032 1.00 84.20  ?  210 ASN B CB  1 
ATOM   1588  C CG  . ASN A 1 194 ? 5.291   52.620  118.520 1.00 86.79  ?  210 ASN B CG  1 
ATOM   1589  O OD1 . ASN A 1 194 ? 5.537   52.560  119.728 1.00 76.50  ?  210 ASN B OD1 1 
ATOM   1590  N ND2 . ASN A 1 194 ? 6.213   52.872  117.609 1.00 98.19  ?  210 ASN B ND2 1 
ATOM   1591  N N   . GLY A 1 195 ? 1.367   51.822  119.466 1.00 85.35  ?  211 GLY B N   1 
ATOM   1592  C CA  . GLY A 1 195 ? 0.098   52.484  119.576 1.00 86.33  ?  211 GLY B CA  1 
ATOM   1593  C C   . GLY A 1 195 ? -1.059  51.562  119.782 1.00 84.05  ?  211 GLY B C   1 
ATOM   1594  O O   . GLY A 1 195 ? -2.199  52.044  119.872 1.00 91.31  ?  211 GLY B O   1 
ATOM   1595  N N   . VAL A 1 196 ? -0.804  50.267  119.879 1.00 77.35  ?  212 VAL B N   1 
ATOM   1596  C CA  . VAL A 1 196 ? -1.870  49.318  120.093 1.00 80.58  ?  212 VAL B CA  1 
ATOM   1597  C C   . VAL A 1 196 ? -1.781  48.772  121.506 1.00 81.81  ?  212 VAL B C   1 
ATOM   1598  O O   . VAL A 1 196 ? -1.223  47.694  121.724 1.00 79.98  ?  212 VAL B O   1 
ATOM   1599  C CB  . VAL A 1 196 ? -1.805  48.205  119.043 1.00 74.48  ?  212 VAL B CB  1 
ATOM   1600  C CG1 . VAL A 1 196 ? -2.999  47.359  119.156 1.00 75.94  ?  212 VAL B CG1 1 
ATOM   1601  C CG2 . VAL A 1 196 ? -1.751  48.810  117.668 1.00 75.18  ?  212 VAL B CG2 1 
ATOM   1602  N N   . ASP A 1 197 ? -2.353  49.504  122.465 1.00 79.62  ?  213 ASP B N   1 
ATOM   1603  C CA  . ASP A 1 197 ? -2.106  49.249  123.884 1.00 81.79  ?  213 ASP B CA  1 
ATOM   1604  C C   . ASP A 1 197 ? -2.180  47.755  124.184 1.00 80.10  ?  213 ASP B C   1 
ATOM   1605  O O   . ASP A 1 197 ? -3.249  47.152  124.079 1.00 81.81  ?  213 ASP B O   1 
ATOM   1606  C CB  . ASP A 1 197 ? -3.096  49.997  124.785 1.00 81.12  ?  213 ASP B CB  1 
ATOM   1607  C CG  . ASP A 1 197 ? -2.693  51.452  125.017 1.00 83.73  ?  213 ASP B CG  1 
ATOM   1608  O OD1 . ASP A 1 197 ? -1.564  51.682  125.510 1.00 83.75  ?  213 ASP B OD1 1 
ATOM   1609  O OD2 . ASP A 1 197 ? -3.535  52.354  124.784 1.00 87.98  -1 213 ASP B OD2 1 
ATOM   1610  N N   . GLY A 1 198 ? -1.039  47.144  124.515 1.00 86.68  ?  214 GLY B N   1 
ATOM   1611  C CA  . GLY A 1 198 ? -1.007  45.749  124.910 1.00 90.61  ?  214 GLY B CA  1 
ATOM   1612  C C   . GLY A 1 198 ? -0.623  44.809  123.802 1.00 82.94  ?  214 GLY B C   1 
ATOM   1613  O O   . GLY A 1 198 ? -0.539  43.602  124.029 1.00 81.23  ?  214 GLY B O   1 
ATOM   1614  N N   . TYR A 1 199 ? -0.398  45.333  122.617 1.00 70.07  ?  215 TYR B N   1 
ATOM   1615  C CA  . TYR A 1 199 ? 0.036   44.562  121.480 1.00 64.04  ?  215 TYR B CA  1 
ATOM   1616  C C   . TYR A 1 199 ? 1.268   45.187  120.847 1.00 63.85  ?  215 TYR B C   1 
ATOM   1617  O O   . TYR A 1 199 ? 1.722   44.701  119.804 1.00 59.73  ?  215 TYR B O   1 
ATOM   1618  C CB  . TYR A 1 199 ? -1.096  44.484  120.454 1.00 64.94  ?  215 TYR B CB  1 
ATOM   1619  C CG  . TYR A 1 199 ? -2.270  43.637  120.892 1.00 68.95  ?  215 TYR B CG  1 
ATOM   1620  C CD1 . TYR A 1 199 ? -2.223  42.257  120.803 1.00 68.96  ?  215 TYR B CD1 1 
ATOM   1621  C CD2 . TYR A 1 199 ? -3.427  44.215  121.372 1.00 71.52  ?  215 TYR B CD2 1 
ATOM   1622  C CE1 . TYR A 1 199 ? -3.285  41.477  121.189 1.00 66.53  ?  215 TYR B CE1 1 
ATOM   1623  C CE2 . TYR A 1 199 ? -4.486  43.438  121.755 1.00 73.81  ?  215 TYR B CE2 1 
ATOM   1624  C CZ  . TYR A 1 199 ? -4.410  42.074  121.664 1.00 69.58  ?  215 TYR B CZ  1 
ATOM   1625  O OH  . TYR A 1 199 ? -5.476  41.313  122.067 1.00 73.62  ?  215 TYR B OH  1 
ATOM   1626  N N   . ASP A 1 200 ? 1.793   46.267  121.440 1.00 65.22  ?  216 ASP B N   1 
ATOM   1627  C CA  . ASP A 1 200 ? 3.024   46.932  121.036 1.00 58.03  ?  216 ASP B CA  1 
ATOM   1628  C C   . ASP A 1 200 ? 4.237   46.001  121.110 1.00 54.79  ?  216 ASP B C   1 
ATOM   1629  O O   . ASP A 1 200 ? 4.297   45.059  121.892 1.00 52.72  ?  216 ASP B O   1 
ATOM   1630  C CB  . ASP A 1 200 ? 3.274   48.153  121.926 1.00 64.55  ?  216 ASP B CB  1 
ATOM   1631  C CG  . ASP A 1 200 ? 2.251   49.280  121.745 1.00 72.35  ?  216 ASP B CG  1 
ATOM   1632  O OD1 . ASP A 1 200 ? 1.782   49.466  120.609 1.00 74.99  ?  216 ASP B OD1 1 
ATOM   1633  O OD2 . ASP A 1 200 ? 1.881   49.967  122.752 1.00 68.41  -1 216 ASP B OD2 1 
ATOM   1634  N N   . TYR A 1 201 ? 5.231   46.302  120.286 1.00 53.98  ?  217 TYR B N   1 
ATOM   1635  C CA  . TYR A 1 201 ? 6.473   45.545  120.178 1.00 55.49  ?  217 TYR B CA  1 
ATOM   1636  C C   . TYR A 1 201 ? 7.527   46.406  119.500 1.00 55.24  ?  217 TYR B C   1 
ATOM   1637  O O   . TYR A 1 201 ? 7.305   46.901  118.394 1.00 54.42  ?  217 TYR B O   1 
ATOM   1638  C CB  . TYR A 1 201 ? 6.246   44.267  119.389 1.00 56.25  ?  217 TYR B CB  1 
ATOM   1639  C CG  . TYR A 1 201 ? 7.269   43.142  119.512 1.00 54.51  ?  217 TYR B CG  1 
ATOM   1640  C CD1 . TYR A 1 201 ? 8.384   43.099  118.699 1.00 51.83  ?  217 TYR B CD1 1 
ATOM   1641  C CD2 . TYR A 1 201 ? 7.063   42.078  120.367 1.00 57.41  ?  217 TYR B CD2 1 
ATOM   1642  C CE1 . TYR A 1 201 ? 9.279   42.059  118.761 1.00 50.85  ?  217 TYR B CE1 1 
ATOM   1643  C CE2 . TYR A 1 201 ? 7.966   41.029  120.436 1.00 57.85  ?  217 TYR B CE2 1 
ATOM   1644  C CZ  . TYR A 1 201 ? 9.067   41.026  119.627 1.00 54.13  ?  217 TYR B CZ  1 
ATOM   1645  O OH  . TYR A 1 201 ? 9.957   39.980  119.679 1.00 58.89  ?  217 TYR B OH  1 
ATOM   1646  N N   . SER A 1 202 ? 8.667   46.605  120.153 1.00 53.33  ?  218 SER B N   1 
ATOM   1647  C CA  . SER A 1 202 ? 9.740   47.430  119.626 1.00 54.96  ?  218 SER B CA  1 
ATOM   1648  C C   . SER A 1 202 ? 10.826  46.545  119.049 1.00 53.98  ?  218 SER B C   1 
ATOM   1649  O O   . SER A 1 202 ? 10.848  45.331  119.248 1.00 56.64  ?  218 SER B O   1 
ATOM   1650  C CB  . SER A 1 202 ? 10.325  48.326  120.710 1.00 57.66  ?  218 SER B CB  1 
ATOM   1651  O OG  . SER A 1 202 ? 11.150  47.529  121.517 1.00 61.57  ?  218 SER B OG  1 
ATOM   1652  N N   . ARG A 1 203 ? 11.764  47.171  118.358 1.00 55.42  ?  219 ARG B N   1 
ATOM   1653  C CA  . ARG A 1 203 ? 12.633  46.395  117.487 1.00 56.77  ?  219 ARG B CA  1 
ATOM   1654  C C   . ARG A 1 203 ? 13.661  45.621  118.305 1.00 61.68  ?  219 ARG B C   1 
ATOM   1655  O O   . ARG A 1 203 ? 14.003  44.483  117.971 1.00 60.89  ?  219 ARG B O   1 
ATOM   1656  C CB  . ARG A 1 203 ? 13.293  47.351  116.505 1.00 57.14  ?  219 ARG B CB  1 
ATOM   1657  C CG  . ARG A 1 203 ? 12.228  48.130  115.737 1.00 53.00  ?  219 ARG B CG  1 
ATOM   1658  C CD  . ARG A 1 203 ? 12.717  48.880  114.516 1.00 55.61  ?  219 ARG B CD  1 
ATOM   1659  N NE  . ARG A 1 203 ? 13.702  49.940  114.753 1.00 57.23  ?  219 ARG B NE  1 
ATOM   1660  C CZ  . ARG A 1 203 ? 13.413  51.228  114.905 1.00 54.96  ?  219 ARG B CZ  1 
ATOM   1661  N NH1 . ARG A 1 203 ? 12.165  51.644  115.004 1.00 61.16  ?  219 ARG B NH1 1 
ATOM   1662  N NH2 . ARG A 1 203 ? 14.401  52.119  114.988 1.00 54.92  ?  219 ARG B NH2 1 
ATOM   1663  N N   . GLY A 1 204 ? 14.153  46.225  119.394 1.00 69.57  ?  220 GLY B N   1 
ATOM   1664  C CA  . GLY A 1 204 ? 15.114  45.568  120.267 1.00 69.95  ?  220 GLY B CA  1 
ATOM   1665  C C   . GLY A 1 204 ? 14.510  44.443  121.054 1.00 71.89  ?  220 GLY B C   1 
ATOM   1666  O O   . GLY A 1 204 ? 15.233  43.536  121.509 1.00 80.62  ?  220 GLY B O   1 
ATOM   1667  N N   . GLN A 1 205 ? 13.188  44.481  121.216 1.00 61.00  ?  221 GLN B N   1 
ATOM   1668  C CA  . GLN A 1 205 ? 12.470  43.378  121.825 1.00 60.10  ?  221 GLN B CA  1 
ATOM   1669  C C   . GLN A 1 205 ? 12.617  42.126  120.970 1.00 59.43  ?  221 GLN B C   1 
ATOM   1670  O O   . GLN A 1 205 ? 12.522  41.007  121.497 1.00 61.01  ?  221 GLN B O   1 
ATOM   1671  C CB  . GLN A 1 205 ? 10.995  43.789  122.071 1.00 59.88  ?  221 GLN B CB  1 
ATOM   1672  C CG  . GLN A 1 205 ? 10.136  42.803  122.899 1.00 61.15  ?  221 GLN B CG  1 
ATOM   1673  C CD  . GLN A 1 205 ? 10.654  42.512  124.343 1.00 81.55  ?  221 GLN B CD  1 
ATOM   1674  O OE1 . GLN A 1 205 ? 11.055  43.421  125.094 1.00 88.47  ?  221 GLN B OE1 1 
ATOM   1675  N NE2 . GLN A 1 205 ? 10.703  41.222  124.700 1.00 81.37  ?  221 GLN B NE2 1 
ATOM   1676  N N   . LEU A 1 206 ? 12.952  42.280  119.689 1.00 55.97  ?  222 LEU B N   1 
ATOM   1677  C CA  . LEU A 1 206 ? 13.219  41.097  118.882 1.00 58.04  ?  222 LEU B CA  1 
ATOM   1678  C C   . LEU A 1 206 ? 14.522  40.418  119.280 1.00 61.23  ?  222 LEU B C   1 
ATOM   1679  O O   . LEU A 1 206 ? 14.564  39.184  119.372 1.00 61.74  ?  222 LEU B O   1 
ATOM   1680  C CB  . LEU A 1 206 ? 13.218  41.432  117.398 1.00 57.04  ?  222 LEU B CB  1 
ATOM   1681  C CG  . LEU A 1 206 ? 13.526  40.251  116.472 1.00 54.31  ?  222 LEU B CG  1 
ATOM   1682  C CD1 . LEU A 1 206 ? 12.325  39.387  116.354 1.00 55.19  ?  222 LEU B CD1 1 
ATOM   1683  C CD2 . LEU A 1 206 ? 13.861  40.778  115.101 1.00 52.40  ?  222 LEU B CD2 1 
ATOM   1684  N N   . ILE A 1 207 ? 15.600  41.180  119.527 1.00 62.34  ?  223 ILE B N   1 
ATOM   1685  C CA  . ILE A 1 207 ? 16.840  40.518  119.944 1.00 61.15  ?  223 ILE B CA  1 
ATOM   1686  C C   . ILE A 1 207 ? 16.644  39.845  121.302 1.00 64.34  ?  223 ILE B C   1 
ATOM   1687  O O   . ILE A 1 207 ? 17.039  38.682  121.508 1.00 62.81  ?  223 ILE B O   1 
ATOM   1688  C CB  . ILE A 1 207 ? 18.038  41.481  119.952 1.00 55.68  ?  223 ILE B CB  1 
ATOM   1689  C CG1 . ILE A 1 207 ? 18.415  41.904  118.537 1.00 59.68  ?  223 ILE B CG1 1 
ATOM   1690  C CG2 . ILE A 1 207 ? 19.245  40.748  120.434 1.00 51.48  ?  223 ILE B CG2 1 
ATOM   1691  C CD1 . ILE A 1 207 ? 19.590  42.901  118.468 1.00 59.88  ?  223 ILE B CD1 1 
ATOM   1692  N N   . GLU A 1 208 ? 16.012  40.551  122.243 1.00 62.31  ?  224 GLU B N   1 
ATOM   1693  C CA  . GLU A 1 208 ? 15.760  39.879  123.512 1.00 65.95  ?  224 GLU B CA  1 
ATOM   1694  C C   . GLU A 1 208 ? 15.056  38.543  123.306 1.00 67.86  ?  224 GLU B C   1 
ATOM   1695  O O   . GLU A 1 208 ? 15.602  37.499  123.684 1.00 72.01  ?  224 GLU B O   1 
ATOM   1696  C CB  . GLU A 1 208 ? 15.010  40.754  124.525 1.00 74.22  ?  224 GLU B CB  1 
ATOM   1697  C CG  . GLU A 1 208 ? 15.921  41.803  125.128 1.00 84.03  ?  224 GLU B CG  1 
ATOM   1698  C CD  . GLU A 1 208 ? 15.220  43.052  125.580 1.00 87.51  ?  224 GLU B CD  1 
ATOM   1699  O OE1 . GLU A 1 208 ? 14.000  42.975  125.860 1.00 86.39  ?  224 GLU B OE1 1 
ATOM   1700  O OE2 . GLU A 1 208 ? 15.884  44.105  125.666 1.00 90.28  -1 224 GLU B OE2 1 
ATOM   1701  N N   . ASP A 1 209 ? 13.886  38.540  122.658 1.00 66.35  ?  225 ASP B N   1 
ATOM   1702  C CA  . ASP A 1 209 ? 13.105  37.300  122.588 1.00 65.73  ?  225 ASP B CA  1 
ATOM   1703  C C   . ASP A 1 209 ? 13.815  36.219  121.785 1.00 64.86  ?  225 ASP B C   1 
ATOM   1704  O O   . ASP A 1 209 ? 13.717  35.029  122.120 1.00 64.00  ?  225 ASP B O   1 
ATOM   1705  C CB  . ASP A 1 209 ? 11.710  37.544  122.013 1.00 64.42  ?  225 ASP B CB  1 
ATOM   1706  C CG  . ASP A 1 209 ? 10.826  38.384  122.915 1.00 72.18  ?  225 ASP B CG  1 
ATOM   1707  O OD1 . ASP A 1 209 ? 11.068  38.441  124.149 1.00 76.09  ?  225 ASP B OD1 1 
ATOM   1708  O OD2 . ASP A 1 209 ? 9.869   38.986  122.379 1.00 69.87  -1 225 ASP B OD2 1 
ATOM   1709  N N   . VAL A 1 210 ? 14.532  36.592  120.722 1.00 62.13  ?  226 VAL B N   1 
ATOM   1710  C CA  . VAL A 1 210 ? 15.243  35.567  119.966 1.00 60.18  ?  226 VAL B CA  1 
ATOM   1711  C C   . VAL A 1 210 ? 16.220  34.853  120.887 1.00 65.48  ?  226 VAL B C   1 
ATOM   1712  O O   . VAL A 1 210 ? 16.232  33.619  120.967 1.00 68.63  ?  226 VAL B O   1 
ATOM   1713  C CB  . VAL A 1 210 ? 15.951  36.172  118.737 1.00 56.17  ?  226 VAL B CB  1 
ATOM   1714  C CG1 . VAL A 1 210 ? 16.996  35.238  118.243 1.00 56.66  ?  226 VAL B CG1 1 
ATOM   1715  C CG2 . VAL A 1 210 ? 14.970  36.505  117.617 1.00 53.88  ?  226 VAL B CG2 1 
ATOM   1716  N N   . GLU A 1 211 ? 16.999  35.630  121.662 1.00 67.46  ?  227 GLU B N   1 
ATOM   1717  C CA  . GLU A 1 211 ? 18.011  35.053  122.553 1.00 66.57  ?  227 GLU B CA  1 
ATOM   1718  C C   . GLU A 1 211 ? 17.373  34.253  123.690 1.00 68.67  ?  227 GLU B C   1 
ATOM   1719  O O   . GLU A 1 211 ? 17.846  33.165  124.049 1.00 66.96  ?  227 GLU B O   1 
ATOM   1720  C CB  . GLU A 1 211 ? 18.893  36.186  123.083 1.00 65.42  ?  227 GLU B CB  1 
ATOM   1721  C CG  . GLU A 1 211 ? 19.920  36.700  122.031 1.00 63.76  ?  227 GLU B CG  1 
ATOM   1722  C CD  . GLU A 1 211 ? 20.750  37.958  122.436 1.00 70.53  ?  227 GLU B CD  1 
ATOM   1723  O OE1 . GLU A 1 211 ? 20.456  38.645  123.459 1.00 63.22  ?  227 GLU B OE1 1 
ATOM   1724  O OE2 . GLU A 1 211 ? 21.718  38.269  121.687 1.00 72.03  -1 227 GLU B OE2 1 
ATOM   1725  N N   . HIS A 1 212 ? 16.259  34.750  124.210 1.00 77.67  ?  228 HIS B N   1 
ATOM   1726  C CA  A HIS A 1 212 ? 15.583  34.107  125.331 0.18 104.56 ?  228 HIS B CA  1 
ATOM   1727  C CA  B HIS A 1 212 ? 15.600  34.099  125.333 0.82 102.42 ?  228 HIS B CA  1 
ATOM   1728  C C   . HIS A 1 212 ? 15.056  32.734  124.917 1.00 80.16  ?  228 HIS B C   1 
ATOM   1729  O O   . HIS A 1 212 ? 15.229  31.733  125.624 1.00 77.80  ?  228 HIS B O   1 
ATOM   1730  C CB  A HIS A 1 212 ? 14.420  34.997  125.746 0.18 84.11  ?  228 HIS B CB  1 
ATOM   1731  C CB  B HIS A 1 212 ? 14.481  34.997  125.854 0.82 100.26 ?  228 HIS B CB  1 
ATOM   1732  C CG  A HIS A 1 212 ? 14.858  36.305  126.196 0.18 89.97  ?  228 HIS B CG  1 
ATOM   1733  C CG  B HIS A 1 212 ? 13.740  34.435  127.021 0.82 82.97  ?  228 HIS B CG  1 
ATOM   1734  N ND1 A HIS A 1 212 ? 13.980  37.358  126.376 0.18 90.85  ?  228 HIS B ND1 1 
ATOM   1735  N ND1 B HIS A 1 212 ? 13.988  34.836  128.318 0.82 89.28  ?  228 HIS B ND1 1 
ATOM   1736  C CD2 A HIS A 1 212 ? 16.105  36.811  126.337 0.18 91.02  ?  228 HIS B CD2 1 
ATOM   1737  C CD2 B HIS A 1 212 ? 12.775  33.496  127.093 0.82 79.62  ?  228 HIS B CD2 1 
ATOM   1738  C CE1 A HIS A 1 212 ? 14.684  38.426  126.691 0.18 94.03  ?  228 HIS B CE1 1 
ATOM   1739  C CE1 B HIS A 1 212 ? 13.185  34.184  129.136 0.82 86.41  ?  228 HIS B CE1 1 
ATOM   1740  N NE2 A HIS A 1 212 ? 15.959  38.124  126.658 0.18 94.34  ?  228 HIS B NE2 1 
ATOM   1741  N NE2 B HIS A 1 212 ? 12.444  33.360  128.418 0.82 85.48  ?  228 HIS B NE2 1 
ATOM   1742  N N   . THR A 1 213 ? 14.394  32.668  123.753 1.00 82.15  ?  229 THR B N   1 
ATOM   1743  C CA  . THR A 1 213 ? 13.895  31.392  123.260 1.00 75.15  ?  229 THR B CA  1 
ATOM   1744  C C   . THR A 1 213 ? 15.042  30.466  122.868 1.00 70.04  ?  229 THR B C   1 
ATOM   1745  O O   . THR A 1 213 ? 14.957  29.242  123.054 1.00 66.81  ?  229 THR B O   1 
ATOM   1746  C CB  . THR A 1 213 ? 12.886  31.632  122.113 1.00 63.74  ?  229 THR B CB  1 
ATOM   1747  O OG1 . THR A 1 213 ? 13.459  32.398  121.051 1.00 52.27  ?  229 THR B OG1 1 
ATOM   1748  C CG2 . THR A 1 213 ? 11.672  32.310  122.623 1.00 66.87  ?  229 THR B CG2 1 
ATOM   1749  N N   . PHE A 1 214 ? 16.143  31.016  122.377 1.00 61.63  ?  230 PHE B N   1 
ATOM   1750  C CA  . PHE A 1 214 ? 17.230  30.127  122.033 1.00 58.78  ?  230 PHE B CA  1 
ATOM   1751  C C   . PHE A 1 214 ? 17.839  29.508  123.284 1.00 61.41  ?  230 PHE B C   1 
ATOM   1752  O O   . PHE A 1 214 ? 18.330  28.373  123.236 1.00 61.12  ?  230 PHE B O   1 
ATOM   1753  C CB  . PHE A 1 214 ? 18.270  30.882  121.221 1.00 58.12  ?  230 PHE B CB  1 
ATOM   1754  C CG  . PHE A 1 214 ? 19.367  30.026  120.756 1.00 60.77  ?  230 PHE B CG  1 
ATOM   1755  C CD1 . PHE A 1 214 ? 19.145  29.016  119.841 1.00 60.37  ?  230 PHE B CD1 1 
ATOM   1756  C CD2 . PHE A 1 214 ? 20.622  30.184  121.279 1.00 60.12  ?  230 PHE B CD2 1 
ATOM   1757  C CE1 . PHE A 1 214 ? 20.191  28.203  119.424 1.00 59.80  ?  230 PHE B CE1 1 
ATOM   1758  C CE2 . PHE A 1 214 ? 21.648  29.375  120.872 1.00 60.57  ?  230 PHE B CE2 1 
ATOM   1759  C CZ  . PHE A 1 214 ? 21.433  28.386  119.944 1.00 58.67  ?  230 PHE B CZ  1 
ATOM   1760  N N   . GLU A 1 215 ? 17.804  30.229  124.411 1.00 63.92  ?  231 GLU B N   1 
ATOM   1761  C CA  . GLU A 1 215 ? 18.344  29.659  125.643 1.00 61.38  ?  231 GLU B CA  1 
ATOM   1762  C C   . GLU A 1 215 ? 17.623  28.372  126.022 1.00 60.65  ?  231 GLU B C   1 
ATOM   1763  O O   . GLU A 1 215 ? 18.265  27.409  126.468 1.00 64.63  ?  231 GLU B O   1 
ATOM   1764  C CB  . GLU A 1 215 ? 18.287  30.665  126.802 1.00 67.57  ?  231 GLU B CB  1 
ATOM   1765  C CG  . GLU A 1 215 ? 19.457  31.628  126.810 1.00 69.98  ?  231 GLU B CG  1 
ATOM   1766  C CD  . GLU A 1 215 ? 20.754  30.933  127.159 1.00 74.47  ?  231 GLU B CD  1 
ATOM   1767  O OE1 . GLU A 1 215 ? 20.760  30.083  128.077 1.00 72.68  ?  231 GLU B OE1 1 
ATOM   1768  O OE2 . GLU A 1 215 ? 21.763  31.188  126.472 1.00 86.88  -1 231 GLU B OE2 1 
ATOM   1769  N N   . GLU A 1 216 ? 16.290  28.331  125.852 1.00 59.74  ?  232 GLU B N   1 
ATOM   1770  C CA  . GLU A 1 216 ? 15.518  27.145  126.212 1.00 59.62  ?  232 GLU B CA  1 
ATOM   1771  C C   . GLU A 1 216 ? 15.566  26.071  125.124 1.00 56.84  ?  232 GLU B C   1 
ATOM   1772  O O   . GLU A 1 216 ? 15.255  24.893  125.399 1.00 55.69  ?  232 GLU B O   1 
ATOM   1773  C CB  . GLU A 1 216 ? 14.070  27.533  126.482 1.00 61.95  ?  232 GLU B CB  1 
ATOM   1774  C CG  . GLU A 1 216 ? 13.913  28.822  127.275 1.00 66.46  ?  232 GLU B CG  1 
ATOM   1775  C CD  . GLU A 1 216 ? 12.458  29.158  127.573 1.00 75.46  ?  232 GLU B CD  1 
ATOM   1776  O OE1 . GLU A 1 216 ? 11.746  28.315  128.168 1.00 78.92  ?  232 GLU B OE1 1 
ATOM   1777  O OE2 . GLU A 1 216 ? 12.029  30.273  127.181 1.00 77.16  -1 232 GLU B OE2 1 
ATOM   1778  N N   . ILE A 1 217 ? 15.943  26.462  123.896 1.00 58.57  ?  233 ILE B N   1 
ATOM   1779  C CA  . ILE A 1 217 ? 16.186  25.469  122.855 1.00 56.33  ?  233 ILE B CA  1 
ATOM   1780  C C   . ILE A 1 217 ? 17.504  24.729  123.108 1.00 58.72  ?  233 ILE B C   1 
ATOM   1781  O O   . ILE A 1 217 ? 17.610  23.526  122.839 1.00 58.15  ?  233 ILE B O   1 
ATOM   1782  C CB  . ILE A 1 217 ? 16.208  26.153  121.483 1.00 57.95  ?  233 ILE B CB  1 
ATOM   1783  C CG1 . ILE A 1 217 ? 14.816  26.280  120.924 1.00 60.61  ?  233 ILE B CG1 1 
ATOM   1784  C CG2 . ILE A 1 217 ? 16.890  25.257  120.480 1.00 52.27  ?  233 ILE B CG2 1 
ATOM   1785  C CD1 . ILE A 1 217 ? 14.743  27.407  119.913 1.00 61.39  ?  233 ILE B CD1 1 
ATOM   1786  N N   . LYS A 1 218 ? 18.535  25.454  123.608 1.00 62.48  ?  234 LYS B N   1 
ATOM   1787  C CA  . LYS A 1 218 ? 19.900  24.926  123.796 1.00 58.70  ?  234 LYS B CA  1 
ATOM   1788  C C   . LYS A 1 218 ? 19.976  23.507  124.335 1.00 58.10  ?  234 LYS B C   1 
ATOM   1789  O O   . LYS A 1 218 ? 20.739  22.720  123.768 1.00 60.11  ?  234 LYS B O   1 
ATOM   1790  C CB  . LYS A 1 218 ? 20.760  25.815  124.705 1.00 53.20  ?  234 LYS B CB  1 
ATOM   1791  C CG  . LYS A 1 218 ? 21.419  26.940  123.953 1.00 58.63  ?  234 LYS B CG  1 
ATOM   1792  C CD  . LYS A 1 218 ? 22.271  27.784  124.882 1.00 65.34  ?  234 LYS B CD  1 
ATOM   1793  C CE  . LYS A 1 218 ? 22.716  29.113  124.263 1.00 69.52  ?  234 LYS B CE  1 
ATOM   1794  N NZ  . LYS A 1 218 ? 23.537  29.944  125.192 1.00 69.89  ?  234 LYS B NZ  1 
ATOM   1795  N N   . PRO A 1 219 ? 19.248  23.111  125.401 1.00 57.16  ?  235 PRO B N   1 
ATOM   1796  C CA  . PRO A 1 219 ? 19.292  21.703  125.827 1.00 58.13  ?  235 PRO B CA  1 
ATOM   1797  C C   . PRO A 1 219 ? 19.010  20.696  124.723 1.00 61.98  ?  235 PRO B C   1 
ATOM   1798  O O   . PRO A 1 219 ? 19.844  19.805  124.458 1.00 63.82  ?  235 PRO B O   1 
ATOM   1799  C CB  . PRO A 1 219 ? 18.231  21.651  126.924 1.00 52.14  ?  235 PRO B CB  1 
ATOM   1800  C CG  . PRO A 1 219 ? 18.166  23.042  127.411 1.00 51.09  ?  235 PRO B CG  1 
ATOM   1801  C CD  . PRO A 1 219 ? 18.323  23.890  126.243 1.00 55.57  ?  235 PRO B CD  1 
ATOM   1802  N N   . LEU A 1 220 ? 17.844  20.823  124.068 1.00 62.66  ?  236 LEU B N   1 
ATOM   1803  C CA  . LEU A 1 220 ? 17.547  19.918  122.961 1.00 62.81  ?  236 LEU B CA  1 
ATOM   1804  C C   . LEU A 1 220 ? 18.691  19.924  121.945 1.00 61.97  ?  236 LEU B C   1 
ATOM   1805  O O   . LEU A 1 220 ? 19.182  18.864  121.530 1.00 62.80  ?  236 LEU B O   1 
ATOM   1806  C CB  . LEU A 1 220 ? 16.234  20.299  122.275 1.00 61.39  ?  236 LEU B CB  1 
ATOM   1807  C CG  . LEU A 1 220 ? 15.873  19.386  121.089 1.00 58.75  ?  236 LEU B CG  1 
ATOM   1808  C CD1 . LEU A 1 220 ? 15.976  17.910  121.489 1.00 64.15  ?  236 LEU B CD1 1 
ATOM   1809  C CD2 . LEU A 1 220 ? 14.539  19.698  120.451 1.00 53.92  ?  236 LEU B CD2 1 
ATOM   1810  N N   . TYR A 1 221 ? 19.142  21.116  121.545 1.00 57.67  ?  237 TYR B N   1 
ATOM   1811  C CA  . TYR A 1 221 ? 20.175  21.179  120.522 1.00 58.19  ?  237 TYR B CA  1 
ATOM   1812  C C   . TYR A 1 221 ? 21.438  20.467  120.968 1.00 61.46  ?  237 TYR B C   1 
ATOM   1813  O O   . TYR A 1 221 ? 22.051  19.737  120.185 1.00 62.63  ?  237 TYR B O   1 
ATOM   1814  C CB  . TYR A 1 221 ? 20.497  22.620  120.165 1.00 56.18  ?  237 TYR B CB  1 
ATOM   1815  C CG  . TYR A 1 221 ? 21.560  22.690  119.113 1.00 54.99  ?  237 TYR B CG  1 
ATOM   1816  C CD1 . TYR A 1 221 ? 21.318  22.200  117.842 1.00 57.08  ?  237 TYR B CD1 1 
ATOM   1817  C CD2 . TYR A 1 221 ? 22.807  23.218  119.397 1.00 55.45  ?  237 TYR B CD2 1 
ATOM   1818  C CE1 . TYR A 1 221 ? 22.279  22.253  116.875 1.00 59.68  ?  237 TYR B CE1 1 
ATOM   1819  C CE2 . TYR A 1 221 ? 23.776  23.276  118.445 1.00 56.20  ?  237 TYR B CE2 1 
ATOM   1820  C CZ  . TYR A 1 221 ? 23.509  22.794  117.187 1.00 59.35  ?  237 TYR B CZ  1 
ATOM   1821  O OH  . TYR A 1 221 ? 24.461  22.842  116.214 1.00 62.11  ?  237 TYR B OH  1 
ATOM   1822  N N   . GLU A 1 222 ? 21.856  20.701  122.212 1.00 60.30  ?  238 GLU B N   1 
ATOM   1823  C CA  . GLU A 1 222 ? 23.098  20.144  122.723 1.00 59.49  ?  238 GLU B CA  1 
ATOM   1824  C C   . GLU A 1 222 ? 23.036  18.644  122.717 1.00 62.90  ?  238 GLU B C   1 
ATOM   1825  O O   . GLU A 1 222 ? 24.047  17.972  122.479 1.00 68.76  ?  238 GLU B O   1 
ATOM   1826  C CB  . GLU A 1 222 ? 23.333  20.652  124.133 1.00 59.21  ?  238 GLU B CB  1 
ATOM   1827  C CG  . GLU A 1 222 ? 23.795  22.079  124.165 1.00 63.94  ?  238 GLU B CG  1 
ATOM   1828  C CD  . GLU A 1 222 ? 24.197  22.532  125.545 1.00 70.77  ?  238 GLU B CD  1 
ATOM   1829  O OE1 . GLU A 1 222 ? 24.745  21.706  126.309 1.00 73.87  ?  238 GLU B OE1 1 
ATOM   1830  O OE2 . GLU A 1 222 ? 23.957  23.724  125.861 1.00 70.41  -1 238 GLU B OE2 1 
ATOM   1831  N N   . HIS A 1 223 ? 21.849  18.101  122.928 1.00 61.26  ?  239 HIS B N   1 
ATOM   1832  C CA  . HIS A 1 223 ? 21.761  16.653  122.890 1.00 66.42  ?  239 HIS B CA  1 
ATOM   1833  C C   . HIS A 1 223 ? 21.752  16.121  121.465 1.00 71.74  ?  239 HIS B C   1 
ATOM   1834  O O   . HIS A 1 223 ? 22.393  15.096  121.181 1.00 76.14  ?  239 HIS B O   1 
ATOM   1835  C CB  . HIS A 1 223 ? 20.542  16.217  123.665 1.00 66.35  ?  239 HIS B CB  1 
ATOM   1836  C CG  . HIS A 1 223 ? 20.798  16.121  125.128 1.00 67.65  ?  239 HIS B CG  1 
ATOM   1837  N ND1 . HIS A 1 223 ? 21.410  15.027  125.692 1.00 70.54  ?  239 HIS B ND1 1 
ATOM   1838  C CD2 . HIS A 1 223 ? 20.610  17.010  126.130 1.00 66.43  ?  239 HIS B CD2 1 
ATOM   1839  C CE1 . HIS A 1 223 ? 21.539  15.226  126.992 1.00 71.65  ?  239 HIS B CE1 1 
ATOM   1840  N NE2 . HIS A 1 223 ? 21.068  16.425  127.283 1.00 63.47  ?  239 HIS B NE2 1 
ATOM   1841  N N   . LEU A 1 224 ? 21.034  16.800  120.563 1.00 69.06  ?  240 LEU B N   1 
ATOM   1842  C CA  . LEU A 1 224 ? 21.096  16.421  119.154 1.00 68.49  ?  240 LEU B CA  1 
ATOM   1843  C C   . LEU A 1 224 ? 22.541  16.436  118.684 1.00 71.38  ?  240 LEU B C   1 
ATOM   1844  O O   . LEU A 1 224 ? 22.996  15.522  117.986 1.00 71.79  ?  240 LEU B O   1 
ATOM   1845  C CB  . LEU A 1 224 ? 20.263  17.382  118.312 1.00 62.71  ?  240 LEU B CB  1 
ATOM   1846  C CG  . LEU A 1 224 ? 20.190  17.126  116.813 1.00 59.05  ?  240 LEU B CG  1 
ATOM   1847  C CD1 . LEU A 1 224 ? 19.343  15.894  116.504 1.00 59.06  ?  240 LEU B CD1 1 
ATOM   1848  C CD2 . LEU A 1 224 ? 19.687  18.365  116.126 1.00 57.58  ?  240 LEU B CD2 1 
ATOM   1849  N N   . HIS A 1 225 ? 23.278  17.465  119.112 1.00 66.57  ?  241 HIS B N   1 
ATOM   1850  C CA  . HIS A 1 225 ? 24.671  17.657  118.746 1.00 71.60  ?  241 HIS B CA  1 
ATOM   1851  C C   . HIS A 1 225 ? 25.526  16.528  119.295 1.00 73.22  ?  241 HIS B C   1 
ATOM   1852  O O   . HIS A 1 225 ? 26.323  15.933  118.563 1.00 71.34  ?  241 HIS B O   1 
ATOM   1853  C CB  . HIS A 1 225 ? 25.121  19.021  119.281 1.00 69.80  ?  241 HIS B CB  1 
ATOM   1854  C CG  . HIS A 1 225 ? 26.518  19.416  118.911 1.00 66.63  ?  241 HIS B CG  1 
ATOM   1855  N ND1 . HIS A 1 225 ? 27.628  18.840  119.474 1.00 61.18  ?  241 HIS B ND1 1 
ATOM   1856  C CD2 . HIS A 1 225 ? 26.977  20.358  118.052 1.00 63.53  ?  241 HIS B CD2 1 
ATOM   1857  C CE1 . HIS A 1 225 ? 28.711  19.392  118.960 1.00 64.32  ?  241 HIS B CE1 1 
ATOM   1858  N NE2 . HIS A 1 225 ? 28.346  20.314  118.091 1.00 58.30  ?  241 HIS B NE2 1 
ATOM   1859  N N   . ALA A 1 226 ? 25.362  16.215  120.586 1.00 89.09  ?  242 ALA B N   1 
ATOM   1860  C CA  . ALA A 1 226 ? 26.139  15.145  121.196 1.00 90.69  ?  242 ALA B CA  1 
ATOM   1861  C C   . ALA A 1 226 ? 25.915  13.831  120.468 1.00 93.19  ?  242 ALA B C   1 
ATOM   1862  O O   . ALA A 1 226 ? 26.873  13.081  120.199 1.00 92.52  ?  242 ALA B O   1 
ATOM   1863  C CB  . ALA A 1 226 ? 25.764  15.017  122.667 1.00 84.86  ?  242 ALA B CB  1 
ATOM   1864  N N   . TYR A 1 227 ? 24.658  13.563  120.097 1.00 74.49  ?  243 TYR B N   1 
ATOM   1865  C CA  . TYR A 1 227 ? 24.332  12.302  119.454 1.00 74.31  ?  243 TYR B CA  1 
ATOM   1866  C C   . TYR A 1 227 ? 24.840  12.268  118.028 1.00 72.49  ?  243 TYR B C   1 
ATOM   1867  O O   . TYR A 1 227 ? 25.360  11.242  117.553 1.00 72.01  ?  243 TYR B O   1 
ATOM   1868  C CB  . TYR A 1 227 ? 22.835  12.081  119.491 1.00 74.40  ?  243 TYR B CB  1 
ATOM   1869  C CG  . TYR A 1 227 ? 22.367  10.920  118.658 1.00 77.70  ?  243 TYR B CG  1 
ATOM   1870  C CD1 . TYR A 1 227 ? 22.576  9.608   119.048 1.00 77.68  ?  243 TYR B CD1 1 
ATOM   1871  C CD2 . TYR A 1 227 ? 21.692  11.140  117.484 1.00 80.47  ?  243 TYR B CD2 1 
ATOM   1872  C CE1 . TYR A 1 227 ? 22.134  8.549   118.263 1.00 77.92  ?  243 TYR B CE1 1 
ATOM   1873  C CE2 . TYR A 1 227 ? 21.249  10.108  116.701 1.00 79.95  ?  243 TYR B CE2 1 
ATOM   1874  C CZ  . TYR A 1 227 ? 21.463  8.824   117.081 1.00 82.82  ?  243 TYR B CZ  1 
ATOM   1875  O OH  . TYR A 1 227 ? 20.981  7.859   116.226 1.00 91.57  ?  243 TYR B OH  1 
ATOM   1876  N N   . VAL A 1 228 ? 24.730  13.387  117.337 1.00 73.95  ?  244 VAL B N   1 
ATOM   1877  C CA  . VAL A 1 228 ? 25.167  13.389  115.956 1.00 76.85  ?  244 VAL B CA  1 
ATOM   1878  C C   . VAL A 1 228 ? 26.689  13.279  115.906 1.00 74.00  ?  244 VAL B C   1 
ATOM   1879  O O   . VAL A 1 228 ? 27.236  12.566  115.063 1.00 75.55  ?  244 VAL B O   1 
ATOM   1880  C CB  . VAL A 1 228 ? 24.613  14.628  115.213 1.00 72.92  ?  244 VAL B CB  1 
ATOM   1881  C CG1 . VAL A 1 228 ? 25.340  14.870  113.886 1.00 72.25  ?  244 VAL B CG1 1 
ATOM   1882  C CG2 . VAL A 1 228 ? 23.139  14.491  114.979 1.00 70.63  ?  244 VAL B CG2 1 
ATOM   1883  N N   . ARG A 1 229 ? 27.393  13.959  116.818 1.00 73.11  ?  245 ARG B N   1 
ATOM   1884  C CA  . ARG A 1 229 ? 28.846  13.827  116.875 1.00 77.62  ?  245 ARG B CA  1 
ATOM   1885  C C   . ARG A 1 229 ? 29.254  12.397  117.186 1.00 80.95  ?  245 ARG B C   1 
ATOM   1886  O O   . ARG A 1 229 ? 30.246  11.898  116.642 1.00 84.15  ?  245 ARG B O   1 
ATOM   1887  C CB  . ARG A 1 229 ? 29.434  14.753  117.930 1.00 78.78  ?  245 ARG B CB  1 
ATOM   1888  C CG  . ARG A 1 229 ? 30.956  14.650  118.097 1.00 78.48  ?  245 ARG B CG  1 
ATOM   1889  C CD  . ARG A 1 229 ? 31.372  15.674  119.128 1.00 75.65  ?  245 ARG B CD  1 
ATOM   1890  N NE  . ARG A 1 229 ? 30.534  15.505  120.304 1.00 74.72  ?  245 ARG B NE  1 
ATOM   1891  C CZ  . ARG A 1 229 ? 30.397  16.417  121.246 1.00 73.70  ?  245 ARG B CZ  1 
ATOM   1892  N NH1 . ARG A 1 229 ? 31.039  17.573  121.175 1.00 71.36  ?  245 ARG B NH1 1 
ATOM   1893  N NH2 . ARG A 1 229 ? 29.552  16.189  122.249 1.00 69.86  ?  245 ARG B NH2 1 
ATOM   1894  N N   . ALA A 1 230 ? 28.510  11.731  118.072 1.00 78.10  ?  246 ALA B N   1 
ATOM   1895  C CA  . ALA A 1 230 ? 28.724  10.308  118.290 1.00 78.75  ?  246 ALA B CA  1 
ATOM   1896  C C   . ALA A 1 230 ? 28.674  9.530   116.966 1.00 82.82  ?  246 ALA B C   1 
ATOM   1897  O O   . ALA A 1 230 ? 29.622  8.820   116.611 1.00 86.12  ?  246 ALA B O   1 
ATOM   1898  C CB  . ALA A 1 230 ? 27.692  9.790   119.300 1.00 75.20  ?  246 ALA B CB  1 
ATOM   1899  N N   . LYS A 1 231 ? 27.586  9.687   116.197 1.00 81.95  ?  247 LYS B N   1 
ATOM   1900  C CA  . LYS A 1 231 ? 27.411  8.889   114.970 1.00 83.38  ?  247 LYS B CA  1 
ATOM   1901  C C   . LYS A 1 231 ? 28.396  9.275   113.856 1.00 82.57  ?  247 LYS B C   1 
ATOM   1902  O O   . LYS A 1 231 ? 28.851  8.410   113.092 1.00 81.63  ?  247 LYS B O   1 
ATOM   1903  C CB  . LYS A 1 231 ? 25.970  9.024   114.495 1.00 83.21  ?  247 LYS B CB  1 
ATOM   1904  C CG  . LYS A 1 231 ? 24.893  8.463   115.431 1.00 82.07  ?  247 LYS B CG  1 
ATOM   1905  C CD  . LYS A 1 231 ? 25.010  6.970   115.601 1.00 85.09  ?  247 LYS B CD  1 
ATOM   1906  C CE  . LYS A 1 231 ? 24.597  6.336   114.272 1.00 86.58  ?  247 LYS B CE  1 
ATOM   1907  N NZ  . LYS A 1 231 ? 24.458  4.870   114.328 1.00 103.46 ?  247 LYS B NZ  1 
ATOM   1908  N N   . LEU A 1 232 ? 28.722  10.562  113.731 1.00 84.57  ?  248 LEU B N   1 
ATOM   1909  C CA  . LEU A 1 232 ? 29.726  10.992  112.757 1.00 88.70  ?  248 LEU B CA  1 
ATOM   1910  C C   . LEU A 1 232 ? 31.103  10.502  113.133 1.00 95.66  ?  248 LEU B C   1 
ATOM   1911  O O   . LEU A 1 232 ? 31.930  10.202  112.263 1.00 106.38 ?  248 LEU B O   1 
ATOM   1912  C CB  . LEU A 1 232 ? 29.773  12.507  112.651 1.00 85.28  ?  248 LEU B CB  1 
ATOM   1913  C CG  . LEU A 1 232 ? 28.572  13.204  112.072 1.00 79.86  ?  248 LEU B CG  1 
ATOM   1914  C CD1 . LEU A 1 232 ? 28.865  14.675  112.073 1.00 73.97  ?  248 LEU B CD1 1 
ATOM   1915  C CD2 . LEU A 1 232 ? 28.454  12.661  110.676 1.00 81.60  ?  248 LEU B CD2 1 
ATOM   1916  N N   . MET A 1 233 ? 31.385  10.459  114.423 1.00 98.46  ?  249 MET B N   1 
ATOM   1917  C CA  . MET A 1 233 ? 32.642  9.900   114.875 1.00 107.26 ?  249 MET B CA  1 
ATOM   1918  C C   . MET A 1 233 ? 32.728  8.420   114.492 1.00 114.35 ?  249 MET B C   1 
ATOM   1919  O O   . MET A 1 233 ? 33.748  7.971   113.960 1.00 118.25 ?  249 MET B O   1 
ATOM   1920  C CB  . MET A 1 233 ? 32.734  10.165  116.379 1.00 107.33 ?  249 MET B CB  1 
ATOM   1921  C CG  . MET A 1 233 ? 34.061  9.991   117.046 1.00 110.18 ?  249 MET B CG  1 
ATOM   1922  S SD  . MET A 1 233 ? 33.816  10.444  118.768 1.00 103.94 ?  249 MET B SD  1 
ATOM   1923  C CE  . MET A 1 233 ? 32.596  9.214   119.244 1.00 98.60  ?  249 MET B CE  1 
ATOM   1924  N N   . ASN A 1 234 ? 31.631  7.662   114.679 1.00 100.77 ?  250 ASN B N   1 
ATOM   1925  C CA  . ASN A 1 234 ? 31.555  6.295   114.140 1.00 96.89  ?  250 ASN B CA  1 
ATOM   1926  C C   . ASN A 1 234 ? 31.676  6.241   112.626 1.00 97.86  ?  250 ASN B C   1 
ATOM   1927  O O   . ASN A 1 234 ? 31.888  5.155   112.082 1.00 90.25  ?  250 ASN B O   1 
ATOM   1928  C CB  . ASN A 1 234 ? 30.238  5.583   114.506 1.00 94.80  ?  250 ASN B CB  1 
ATOM   1929  C CG  . ASN A 1 234 ? 30.120  5.211   115.987 1.00 101.66 ?  250 ASN B CG  1 
ATOM   1930  O OD1 . ASN A 1 234 ? 31.103  5.152   116.742 1.00 99.33  ?  250 ASN B OD1 1 
ATOM   1931  N ND2 . ASN A 1 234 ? 28.875  4.992   116.416 1.00 103.44 ?  250 ASN B ND2 1 
ATOM   1932  N N   . ALA A 1 235 ? 31.471  7.358   111.924 1.00 104.35 ?  251 ALA B N   1 
ATOM   1933  C CA  . ALA A 1 235 ? 31.609  7.361   110.466 1.00 105.37 ?  251 ALA B CA  1 
ATOM   1934  C C   . ALA A 1 235 ? 32.899  7.999   109.965 1.00 110.88 ?  251 ALA B C   1 
ATOM   1935  O O   . ALA A 1 235 ? 33.192  7.914   108.764 1.00 111.62 ?  251 ALA B O   1 
ATOM   1936  C CB  . ALA A 1 235 ? 30.427  8.083   109.813 1.00 97.44  ?  251 ALA B CB  1 
ATOM   1937  N N   . TYR A 1 236 ? 33.654  8.656   110.837 1.00 117.19 ?  252 TYR B N   1 
ATOM   1938  C CA  . TYR A 1 236 ? 34.930  9.266   110.468 1.00 116.48 ?  252 TYR B CA  1 
ATOM   1939  C C   . TYR A 1 236 ? 35.851  9.215   111.666 1.00 115.18 ?  252 TYR B C   1 
ATOM   1940  O O   . TYR A 1 236 ? 36.090  10.233  112.331 1.00 116.19 ?  252 TYR B O   1 
ATOM   1941  C CB  . TYR A 1 236 ? 34.766  10.713  110.011 1.00 114.13 ?  252 TYR B CB  1 
ATOM   1942  C CG  . TYR A 1 236 ? 33.905  10.953  108.800 1.00 118.42 ?  252 TYR B CG  1 
ATOM   1943  C CD1 . TYR A 1 236 ? 34.403  10.740  107.527 1.00 123.87 ?  252 TYR B CD1 1 
ATOM   1944  C CD2 . TYR A 1 236 ? 32.637  11.505  108.921 1.00 120.05 ?  252 TYR B CD2 1 
ATOM   1945  C CE1 . TYR A 1 236 ? 33.638  11.000  106.403 1.00 124.61 ?  252 TYR B CE1 1 
ATOM   1946  C CE2 . TYR A 1 236 ? 31.863  11.773  107.806 1.00 121.12 ?  252 TYR B CE2 1 
ATOM   1947  C CZ  . TYR A 1 236 ? 32.367  11.521  106.548 1.00 125.61 ?  252 TYR B CZ  1 
ATOM   1948  O OH  . TYR A 1 236 ? 31.599  11.782  105.432 1.00 119.07 ?  252 TYR B OH  1 
ATOM   1949  N N   . PRO A 1 237 ? 36.426  8.049   111.950 1.00 110.86 ?  253 PRO B N   1 
ATOM   1950  C CA  . PRO A 1 237 ? 36.995  7.830   113.290 1.00 106.66 ?  253 PRO B CA  1 
ATOM   1951  C C   . PRO A 1 237 ? 38.101  8.808   113.616 1.00 103.34 ?  253 PRO B C   1 
ATOM   1952  O O   . PRO A 1 237 ? 38.105  9.426   114.693 1.00 105.61 ?  253 PRO B O   1 
ATOM   1953  C CB  . PRO A 1 237 ? 37.509  6.393   113.213 1.00 106.19 ?  253 PRO B CB  1 
ATOM   1954  C CG  . PRO A 1 237 ? 37.609  6.106   111.741 1.00 107.37 ?  253 PRO B CG  1 
ATOM   1955  C CD  . PRO A 1 237 ? 36.540  6.870   111.086 1.00 104.96 ?  253 PRO B CD  1 
ATOM   1956  N N   . SER A 1 238 ? 39.017  9.005   112.682 1.00 97.74  ?  254 SER B N   1 
ATOM   1957  C CA  . SER A 1 238 ? 40.243  9.708   112.987 1.00 96.09  ?  254 SER B CA  1 
ATOM   1958  C C   . SER A 1 238 ? 40.158  11.195  112.732 1.00 98.13  ?  254 SER B C   1 
ATOM   1959  O O   . SER A 1 238 ? 41.203  11.847  112.625 1.00 97.76  ?  254 SER B O   1 
ATOM   1960  C CB  . SER A 1 238 ? 41.372  9.124   112.167 1.00 95.01  ?  254 SER B CB  1 
ATOM   1961  O OG  . SER A 1 238 ? 41.226  9.602   110.851 1.00 96.86  ?  254 SER B OG  1 
ATOM   1962  N N   . TYR A 1 239 ? 38.950  11.751  112.632 1.00 98.40  ?  255 TYR B N   1 
ATOM   1963  C CA  . TYR A 1 239 ? 38.783  13.159  112.287 1.00 96.57  ?  255 TYR B CA  1 
ATOM   1964  C C   . TYR A 1 239 ? 37.977  13.988  113.281 1.00 96.17  ?  255 TYR B C   1 
ATOM   1965  O O   . TYR A 1 239 ? 38.167  15.208  113.329 1.00 89.41  ?  255 TYR B O   1 
ATOM   1966  C CB  . TYR A 1 239 ? 38.132  13.284  110.908 1.00 94.60  ?  255 TYR B CB  1 
ATOM   1967  C CG  . TYR A 1 239 ? 38.985  12.849  109.742 1.00 92.71  ?  255 TYR B CG  1 
ATOM   1968  C CD1 . TYR A 1 239 ? 40.144  13.541  109.411 1.00 89.49  ?  255 TYR B CD1 1 
ATOM   1969  C CD2 . TYR A 1 239 ? 38.619  11.763  108.955 1.00 94.90  ?  255 TYR B CD2 1 
ATOM   1970  C CE1 . TYR A 1 239 ? 40.920  13.164  108.324 1.00 91.01  ?  255 TYR B CE1 1 
ATOM   1971  C CE2 . TYR A 1 239 ? 39.387  11.376  107.864 1.00 90.27  ?  255 TYR B CE2 1 
ATOM   1972  C CZ  . TYR A 1 239 ? 40.539  12.077  107.551 1.00 91.54  ?  255 TYR B CZ  1 
ATOM   1973  O OH  . TYR A 1 239 ? 41.304  11.682  106.466 1.00 88.42  ?  255 TYR B OH  1 
ATOM   1974  N N   . ILE A 1 240 ? 37.100  13.380  114.077 1.00 105.24 ?  256 ILE B N   1 
ATOM   1975  C CA  . ILE A 1 240 ? 36.185  14.110  114.951 1.00 95.22  ?  256 ILE B CA  1 
ATOM   1976  C C   . ILE A 1 240 ? 36.516  13.828  116.415 1.00 98.20  ?  256 ILE B C   1 
ATOM   1977  O O   . ILE A 1 240 ? 36.715  12.667  116.806 1.00 100.10 ?  256 ILE B O   1 
ATOM   1978  C CB  . ILE A 1 240 ? 34.727  13.749  114.634 1.00 92.01  ?  256 ILE B CB  1 
ATOM   1979  C CG1 . ILE A 1 240 ? 34.280  14.505  113.388 1.00 90.72  ?  256 ILE B CG1 1 
ATOM   1980  C CG2 . ILE A 1 240 ? 33.844  13.997  115.843 1.00 91.34  ?  256 ILE B CG2 1 
ATOM   1981  C CD1 . ILE A 1 240 ? 33.193  13.796  112.644 1.00 101.74 ?  256 ILE B CD1 1 
ATOM   1982  N N   . SER A 1 241 ? 36.569  14.905  117.234 1.00 92.20  ?  257 SER B N   1 
ATOM   1983  C CA  . SER A 1 241 ? 36.879  14.687  118.640 1.00 86.80  ?  257 SER B CA  1 
ATOM   1984  C C   . SER A 1 241 ? 35.598  14.552  119.429 1.00 84.54  ?  257 SER B C   1 
ATOM   1985  O O   . SER A 1 241 ? 34.678  15.349  119.243 1.00 83.70  ?  257 SER B O   1 
ATOM   1986  C CB  . SER A 1 241 ? 37.667  15.836  119.235 1.00 82.68  ?  257 SER B CB  1 
ATOM   1987  O OG  . SER A 1 241 ? 37.402  15.895  120.629 1.00 79.52  ?  257 SER B OG  1 
ATOM   1988  N N   . PRO A 1 242 ? 35.551  13.598  120.357 1.00 79.92  ?  258 PRO B N   1 
ATOM   1989  C CA  . PRO A 1 242 ? 34.339  13.399  121.148 1.00 78.50  ?  258 PRO B CA  1 
ATOM   1990  C C   . PRO A 1 242 ? 34.068  14.500  122.145 1.00 78.53  ?  258 PRO B C   1 
ATOM   1991  O O   . PRO A 1 242 ? 33.143  14.358  122.951 1.00 78.11  ?  258 PRO B O   1 
ATOM   1992  C CB  . PRO A 1 242 ? 34.610  12.089  121.880 1.00 81.79  ?  258 PRO B CB  1 
ATOM   1993  C CG  . PRO A 1 242 ? 36.056  12.021  121.964 1.00 86.20  ?  258 PRO B CG  1 
ATOM   1994  C CD  . PRO A 1 242 ? 36.601  12.647  120.726 1.00 84.75  ?  258 PRO B CD  1 
ATOM   1995  N N   . ILE A 1 243 ? 34.836  15.587  122.150 1.00 78.40  ?  259 ILE B N   1 
ATOM   1996  C CA  . ILE A 1 243 ? 34.444  16.745  122.947 1.00 76.48  ?  259 ILE B CA  1 
ATOM   1997  C C   . ILE A 1 243 ? 34.498  18.033  122.137 1.00 77.25  ?  259 ILE B C   1 
ATOM   1998  O O   . ILE A 1 243 ? 34.301  19.127  122.687 1.00 76.42  ?  259 ILE B O   1 
ATOM   1999  C CB  . ILE A 1 243 ? 35.332  16.891  124.182 1.00 73.22  ?  259 ILE B CB  1 
ATOM   2000  C CG1 . ILE A 1 243 ? 36.738  17.256  123.709 1.00 72.38  ?  259 ILE B CG1 1 
ATOM   2001  C CG2 . ILE A 1 243 ? 35.231  15.654  125.034 1.00 75.75  ?  259 ILE B CG2 1 
ATOM   2002  C CD1 . ILE A 1 243 ? 37.582  17.872  124.766 1.00 67.02  ?  259 ILE B CD1 1 
ATOM   2003  N N   . GLY A 1 244 ? 34.759  17.924  120.828 1.00 82.72  ?  260 GLY B N   1 
ATOM   2004  C CA  . GLY A 1 244 ? 34.989  19.089  119.996 1.00 81.70  ?  260 GLY B CA  1 
ATOM   2005  C C   . GLY A 1 244 ? 33.723  19.601  119.330 1.00 77.66  ?  260 GLY B C   1 
ATOM   2006  O O   . GLY A 1 244 ? 32.630  19.064  119.512 1.00 76.08  ?  260 GLY B O   1 
ATOM   2007  N N   . CYS A 1 245 ? 33.888  20.666  118.545 1.00 74.70  ?  261 CYS B N   1 
ATOM   2008  C CA  . CYS A 1 245 ? 32.807  21.022  117.635 1.00 70.21  ?  261 CYS B CA  1 
ATOM   2009  C C   . CYS A 1 245 ? 32.809  20.126  116.404 1.00 65.47  ?  261 CYS B C   1 
ATOM   2010  O O   . CYS A 1 245 ? 33.828  19.537  116.043 1.00 69.67  ?  261 CYS B O   1 
ATOM   2011  C CB  . CYS A 1 245 ? 32.896  22.469  117.171 1.00 70.82  ?  261 CYS B CB  1 
ATOM   2012  S SG  . CYS A 1 245 ? 32.660  23.763  118.386 1.00 77.23  ?  261 CYS B SG  1 
ATOM   2013  N N   . LEU A 1 246 ? 31.660  20.060  115.731 1.00 69.00  ?  262 LEU B N   1 
ATOM   2014  C CA  . LEU A 1 246 ? 31.554  19.277  114.497 1.00 68.38  ?  262 LEU B CA  1 
ATOM   2015  C C   . LEU A 1 246 ? 32.219  19.987  113.316 1.00 67.07  ?  262 LEU B C   1 
ATOM   2016  O O   . LEU A 1 246 ? 31.989  21.182  113.102 1.00 66.23  ?  262 LEU B O   1 
ATOM   2017  C CB  . LEU A 1 246 ? 30.093  19.000  114.195 1.00 66.58  ?  262 LEU B CB  1 
ATOM   2018  C CG  . LEU A 1 246 ? 29.346  18.132  115.192 1.00 63.77  ?  262 LEU B CG  1 
ATOM   2019  C CD1 . LEU A 1 246 ? 27.876  18.191  114.942 1.00 65.39  ?  262 LEU B CD1 1 
ATOM   2020  C CD2 . LEU A 1 246 ? 29.818  16.742  114.943 1.00 65.81  ?  262 LEU B CD2 1 
ATOM   2021  N N   . PRO A 1 247 ? 33.051  19.293  112.537 1.00 66.51  ?  263 PRO B N   1 
ATOM   2022  C CA  . PRO A 1 247 ? 33.719  19.934  111.391 1.00 73.35  ?  263 PRO B CA  1 
ATOM   2023  C C   . PRO A 1 247 ? 32.729  20.510  110.378 1.00 74.28  ?  263 PRO B C   1 
ATOM   2024  O O   . PRO A 1 247 ? 31.890  19.787  109.833 1.00 79.48  ?  263 PRO B O   1 
ATOM   2025  C CB  . PRO A 1 247 ? 34.542  18.789  110.789 1.00 73.56  ?  263 PRO B CB  1 
ATOM   2026  C CG  . PRO A 1 247 ? 34.782  17.864  111.932 1.00 68.86  ?  263 PRO B CG  1 
ATOM   2027  C CD  . PRO A 1 247 ? 33.565  17.940  112.796 1.00 68.32  ?  263 PRO B CD  1 
ATOM   2028  N N   . ALA A 1 248 ? 32.873  21.809  110.086 1.00 73.59  ?  264 ALA B N   1 
ATOM   2029  C CA  . ALA A 1 248 ? 31.878  22.533  109.286 1.00 74.78  ?  264 ALA B CA  1 
ATOM   2030  C C   . ALA A 1 248 ? 31.537  21.849  107.957 1.00 80.80  ?  264 ALA B C   1 
ATOM   2031  O O   . ALA A 1 248 ? 30.463  22.099  107.398 1.00 77.47  ?  264 ALA B O   1 
ATOM   2032  C CB  . ALA A 1 248 ? 32.358  23.960  109.022 1.00 73.90  ?  264 ALA B CB  1 
ATOM   2033  N N   . HIS A 1 249 ? 32.404  20.969  107.453 1.00 80.74  ?  265 HIS B N   1 
ATOM   2034  C CA  . HIS A 1 249 ? 32.218  20.358  106.145 1.00 80.38  ?  265 HIS B CA  1 
ATOM   2035  C C   . HIS A 1 249 ? 31.667  18.950  106.227 1.00 77.46  ?  265 HIS B C   1 
ATOM   2036  O O   . HIS A 1 249 ? 31.780  18.192  105.264 1.00 77.96  ?  265 HIS B O   1 
ATOM   2037  C CB  . HIS A 1 249 ? 33.539  20.332  105.379 1.00 81.24  ?  265 HIS B CB  1 
ATOM   2038  C CG  . HIS A 1 249 ? 34.556  19.370  105.928 1.00 86.61  ?  265 HIS B CG  1 
ATOM   2039  N ND1 . HIS A 1 249 ? 35.134  19.506  107.174 1.00 88.42  ?  265 HIS B ND1 1 
ATOM   2040  C CD2 . HIS A 1 249 ? 35.123  18.270  105.373 1.00 88.63  ?  265 HIS B CD2 1 
ATOM   2041  C CE1 . HIS A 1 249 ? 35.993  18.520  107.372 1.00 86.14  ?  265 HIS B CE1 1 
ATOM   2042  N NE2 . HIS A 1 249 ? 36.010  17.759  106.292 1.00 86.80  ?  265 HIS B NE2 1 
ATOM   2043  N N   . LEU A 1 250 ? 31.117  18.565  107.352 1.00 75.49  ?  266 LEU B N   1 
ATOM   2044  C CA  . LEU A 1 250 ? 30.633  17.206  107.517 1.00 78.09  ?  266 LEU B CA  1 
ATOM   2045  C C   . LEU A 1 250 ? 29.179  17.225  107.951 1.00 81.73  ?  266 LEU B C   1 
ATOM   2046  O O   . LEU A 1 250 ? 28.671  16.279  108.553 1.00 80.15  ?  266 LEU B O   1 
ATOM   2047  C CB  . LEU A 1 250 ? 31.512  16.429  108.499 1.00 79.87  ?  266 LEU B CB  1 
ATOM   2048  C CG  . LEU A 1 250 ? 32.962  16.237  108.023 1.00 89.40  ?  266 LEU B CG  1 
ATOM   2049  C CD1 . LEU A 1 250 ? 33.931  15.493  108.988 1.00 92.93  ?  266 LEU B CD1 1 
ATOM   2050  C CD2 . LEU A 1 250 ? 32.893  15.509  106.698 1.00 97.91  ?  266 LEU B CD2 1 
ATOM   2051  N N   . LEU A 1 251 ? 28.478  18.292  107.620 1.00 81.66  ?  267 LEU B N   1 
ATOM   2052  C CA  . LEU A 1 251 ? 27.161  18.465  108.189 1.00 76.42  ?  267 LEU B CA  1 
ATOM   2053  C C   . LEU A 1 251 ? 26.023  18.073  107.248 1.00 78.81  ?  267 LEU B C   1 
ATOM   2054  O O   . LEU A 1 251 ? 24.891  17.911  107.724 1.00 78.32  ?  267 LEU B O   1 
ATOM   2055  C CB  . LEU A 1 251 ? 27.019  19.914  108.649 1.00 78.00  ?  267 LEU B CB  1 
ATOM   2056  C CG  . LEU A 1 251 ? 28.044  20.103  109.765 1.00 72.30  ?  267 LEU B CG  1 
ATOM   2057  C CD1 . LEU A 1 251 ? 28.126  21.547  110.222 1.00 79.23  ?  267 LEU B CD1 1 
ATOM   2058  C CD2 . LEU A 1 251 ? 27.681  19.176  110.895 1.00 72.88  ?  267 LEU B CD2 1 
ATOM   2059  N N   . GLY A 1 252 ? 26.275  17.899  105.942 1.00 82.49  ?  268 GLY B N   1 
ATOM   2060  C CA  . GLY A 1 252 ? 25.229  17.458  105.016 1.00 84.43  ?  268 GLY B CA  1 
ATOM   2061  C C   . GLY A 1 252 ? 24.834  18.445  103.926 1.00 81.98  ?  268 GLY B C   1 
ATOM   2062  O O   . GLY A 1 252 ? 24.050  18.080  103.040 1.00 78.36  ?  268 GLY B O   1 
ATOM   2063  N N   . ASP A 1 253 ? 25.323  19.681  103.953 1.00 81.29  ?  269 ASP B N   1 
ATOM   2064  C CA  . ASP A 1 253 ? 25.190  20.595  102.832 1.00 76.90  ?  269 ASP B CA  1 
ATOM   2065  C C   . ASP A 1 253 ? 26.349  21.590  102.876 1.00 75.92  ?  269 ASP B C   1 
ATOM   2066  O O   . ASP A 1 253 ? 27.199  21.544  103.764 1.00 75.73  ?  269 ASP B O   1 
ATOM   2067  C CB  . ASP A 1 253 ? 23.795  21.233  102.815 1.00 74.64  ?  269 ASP B CB  1 
ATOM   2068  C CG  . ASP A 1 253 ? 23.556  22.205  103.957 1.00 75.79  ?  269 ASP B CG  1 
ATOM   2069  O OD1 . ASP A 1 253 ? 24.521  22.759  104.536 1.00 77.12  ?  269 ASP B OD1 1 
ATOM   2070  O OD2 . ASP A 1 253 ? 22.360  22.430  104.262 1.00 71.40  -1 269 ASP B OD2 1 
ATOM   2071  N N   . MET A 1 254 ? 26.388  22.478  101.887 1.00 74.33  ?  270 MET B N   1 
ATOM   2072  C CA  . MET A 1 254 ? 27.512  23.374  101.680 1.00 75.25  ?  270 MET B CA  1 
ATOM   2073  C C   . MET A 1 254 ? 27.788  24.297  102.863 1.00 74.47  ?  270 MET B C   1 
ATOM   2074  O O   . MET A 1 254 ? 28.874  24.883  102.919 1.00 75.74  ?  270 MET B O   1 
ATOM   2075  C CB  . MET A 1 254 ? 27.240  24.172  100.394 1.00 81.82  ?  270 MET B CB  1 
ATOM   2076  C CG  . MET A 1 254 ? 28.304  25.180  100.043 1.00 83.24  ?  270 MET B CG  1 
ATOM   2077  S SD  . MET A 1 254 ? 29.886  24.387  99.899  1.00 84.46  ?  270 MET B SD  1 
ATOM   2078  C CE  . MET A 1 254 ? 29.947  23.992  98.166  1.00 91.82  ?  270 MET B CE  1 
ATOM   2079  N N   . TRP A 1 255 ? 26.858  24.446  103.808 1.00 73.29  ?  271 TRP B N   1 
ATOM   2080  C CA  . TRP A 1 255 ? 27.078  25.322  104.958 1.00 75.27  ?  271 TRP B CA  1 
ATOM   2081  C C   . TRP A 1 255 ? 26.806  24.701  106.327 1.00 74.91  ?  271 TRP B C   1 
ATOM   2082  O O   . TRP A 1 255 ? 27.274  25.260  107.330 1.00 72.85  ?  271 TRP B O   1 
ATOM   2083  C CB  . TRP A 1 255 ? 26.235  26.601  104.826 1.00 74.77  ?  271 TRP B CB  1 
ATOM   2084  C CG  . TRP A 1 255 ? 26.354  27.276  103.504 1.00 77.23  ?  271 TRP B CG  1 
ATOM   2085  C CD1 . TRP A 1 255 ? 27.238  28.273  103.149 1.00 79.57  ?  271 TRP B CD1 1 
ATOM   2086  C CD2 . TRP A 1 255 ? 25.682  26.904  102.319 1.00 75.62  ?  271 TRP B CD2 1 
ATOM   2087  N NE1 . TRP A 1 255 ? 27.082  28.593  101.823 1.00 76.88  ?  271 TRP B NE1 1 
ATOM   2088  C CE2 . TRP A 1 255 ? 26.141  27.754  101.288 1.00 76.05  ?  271 TRP B CE2 1 
ATOM   2089  C CE3 . TRP A 1 255 ? 24.724  25.946  102.026 1.00 71.60  ?  271 TRP B CE3 1 
ATOM   2090  C CZ2 . TRP A 1 255 ? 25.669  27.665  100.000 1.00 76.34  ?  271 TRP B CZ2 1 
ATOM   2091  C CZ3 . TRP A 1 255 ? 24.264  25.861  100.760 1.00 74.91  ?  271 TRP B CZ3 1 
ATOM   2092  C CH2 . TRP A 1 255 ? 24.730  26.714  99.755  1.00 76.85  ?  271 TRP B CH2 1 
ATOM   2093  N N   . GLY A 1 256 ? 26.083  23.585  106.412 1.00 80.57  ?  272 GLY B N   1 
ATOM   2094  C CA  . GLY A 1 256 ? 25.601  23.109  107.695 1.00 77.17  ?  272 GLY B CA  1 
ATOM   2095  C C   . GLY A 1 256 ? 24.342  23.793  108.173 1.00 76.49  ?  272 GLY B C   1 
ATOM   2096  O O   . GLY A 1 256 ? 24.073  23.771  109.389 1.00 73.04  ?  272 GLY B O   1 
ATOM   2097  N N   . ARG A 1 257 ? 23.588  24.421  107.242 1.00 71.32  ?  273 ARG B N   1 
ATOM   2098  C CA  . ARG A 1 257 ? 22.297  25.050  107.521 1.00 63.73  ?  273 ARG B CA  1 
ATOM   2099  C C   . ARG A 1 257 ? 21.245  24.023  107.890 1.00 64.41  ?  273 ARG B C   1 
ATOM   2100  O O   . ARG A 1 257 ? 20.383  24.290  108.729 1.00 64.58  ?  273 ARG B O   1 
ATOM   2101  C CB  . ARG A 1 257 ? 21.809  25.814  106.303 1.00 62.25  ?  273 ARG B CB  1 
ATOM   2102  C CG  . ARG A 1 257 ? 20.456  26.500  106.511 1.00 63.97  ?  273 ARG B CG  1 
ATOM   2103  C CD  . ARG A 1 257 ? 20.013  27.314  105.285 1.00 63.41  ?  273 ARG B CD  1 
ATOM   2104  N NE  . ARG A 1 257 ? 18.703  27.928  105.444 1.00 61.09  ?  273 ARG B NE  1 
ATOM   2105  C CZ  . ARG A 1 257 ? 17.900  28.170  104.419 1.00 63.88  ?  273 ARG B CZ  1 
ATOM   2106  N NH1 . ARG A 1 257 ? 18.201  27.750  103.196 1.00 65.67  ?  273 ARG B NH1 1 
ATOM   2107  N NH2 . ARG A 1 257 ? 16.743  28.789  104.634 1.00 61.34  ?  273 ARG B NH2 1 
ATOM   2108  N N   . PHE A 1 258 ? 21.241  22.879  107.223 1.00 65.69  ?  274 PHE B N   1 
ATOM   2109  C CA  . PHE A 1 258 ? 20.327  21.796  107.562 1.00 66.38  ?  274 PHE B CA  1 
ATOM   2110  C C   . PHE A 1 258 ? 21.144  20.522  107.708 1.00 68.75  ?  274 PHE B C   1 
ATOM   2111  O O   . PHE A 1 258 ? 21.960  20.192  106.835 1.00 70.21  ?  274 PHE B O   1 
ATOM   2112  C CB  . PHE A 1 258 ? 19.196  21.603  106.513 1.00 66.62  ?  274 PHE B CB  1 
ATOM   2113  C CG  . PHE A 1 258 ? 18.432  22.869  106.171 1.00 63.33  ?  274 PHE B CG  1 
ATOM   2114  C CD1 . PHE A 1 258 ? 17.425  23.335  107.001 1.00 60.73  ?  274 PHE B CD1 1 
ATOM   2115  C CD2 . PHE A 1 258 ? 18.691  23.561  104.995 1.00 62.34  ?  274 PHE B CD2 1 
ATOM   2116  C CE1 . PHE A 1 258 ? 16.728  24.486  106.688 1.00 58.42  ?  274 PHE B CE1 1 
ATOM   2117  C CE2 . PHE A 1 258 ? 17.983  24.718  104.680 1.00 60.62  ?  274 PHE B CE2 1 
ATOM   2118  C CZ  . PHE A 1 258 ? 17.007  25.177  105.531 1.00 55.17  ?  274 PHE B CZ  1 
ATOM   2119  N N   . TRP A 1 259 ? 20.927  19.809  108.812 1.00 72.19  ?  275 TRP B N   1 
ATOM   2120  C CA  . TRP A 1 259 ? 21.584  18.529  109.039 1.00 70.74  ?  275 TRP B CA  1 
ATOM   2121  C C   . TRP A 1 259 ? 20.784  17.373  108.465 1.00 70.57  ?  275 TRP B C   1 
ATOM   2122  O O   . TRP A 1 259 ? 20.782  16.278  109.037 1.00 71.01  ?  275 TRP B O   1 
ATOM   2123  C CB  . TRP A 1 259 ? 21.821  18.307  110.536 1.00 69.63  ?  275 TRP B CB  1 
ATOM   2124  C CG  . TRP A 1 259 ? 22.788  19.231  111.208 1.00 66.07  ?  275 TRP B CG  1 
ATOM   2125  C CD1 . TRP A 1 259 ? 23.476  20.268  110.646 1.00 68.66  ?  275 TRP B CD1 1 
ATOM   2126  C CD2 . TRP A 1 259 ? 23.117  19.237  112.591 1.00 61.90  ?  275 TRP B CD2 1 
ATOM   2127  N NE1 . TRP A 1 259 ? 24.233  20.913  111.597 1.00 66.51  ?  275 TRP B NE1 1 
ATOM   2128  C CE2 . TRP A 1 259 ? 24.027  20.298  112.803 1.00 64.39  ?  275 TRP B CE2 1 
ATOM   2129  C CE3 . TRP A 1 259 ? 22.730  18.451  113.678 1.00 62.16  ?  275 TRP B CE3 1 
ATOM   2130  C CZ2 . TRP A 1 259 ? 24.563  20.584  114.057 1.00 64.35  ?  275 TRP B CZ2 1 
ATOM   2131  C CZ3 . TRP A 1 259 ? 23.266  18.735  114.923 1.00 65.14  ?  275 TRP B CZ3 1 
ATOM   2132  C CH2 . TRP A 1 259 ? 24.177  19.796  115.102 1.00 62.84  ?  275 TRP B CH2 1 
ATOM   2133  N N   . THR A 1 260 ? 20.067  17.593  107.360 1.00 74.04  ?  276 THR B N   1 
ATOM   2134  C CA  . THR A 1 260 ? 19.109  16.584  106.919 1.00 73.99  ?  276 THR B CA  1 
ATOM   2135  C C   . THR A 1 260 ? 19.798  15.402  106.261 1.00 72.40  ?  276 THR B C   1 
ATOM   2136  O O   . THR A 1 260 ? 19.300  14.276  106.341 1.00 70.00  ?  276 THR B O   1 
ATOM   2137  C CB  . THR A 1 260 ? 18.066  17.165  105.954 1.00 72.30  ?  276 THR B CB  1 
ATOM   2138  O OG1 . THR A 1 260 ? 17.557  18.420  106.433 1.00 67.61  ?  276 THR B OG1 1 
ATOM   2139  C CG2 . THR A 1 260 ? 16.901  16.193  105.818 1.00 76.65  ?  276 THR B CG2 1 
ATOM   2140  N N   . ASN A 1 261 ? 20.940  15.614  105.624 1.00 74.21  ?  277 ASN B N   1 
ATOM   2141  C CA  . ASN A 1 261 ? 21.507  14.473  104.938 1.00 75.81  ?  277 ASN B CA  1 
ATOM   2142  C C   . ASN A 1 261 ? 22.205  13.523  105.888 1.00 75.01  ?  277 ASN B C   1 
ATOM   2143  O O   . ASN A 1 261 ? 22.378  12.348  105.546 1.00 73.93  ?  277 ASN B O   1 
ATOM   2144  C CB  . ASN A 1 261 ? 22.437  14.940  103.852 1.00 80.82  ?  277 ASN B CB  1 
ATOM   2145  C CG  . ASN A 1 261 ? 21.700  15.690  102.808 1.00 80.08  ?  277 ASN B CG  1 
ATOM   2146  O OD1 . ASN A 1 261 ? 20.620  15.271  102.380 1.00 70.16  ?  277 ASN B OD1 1 
ATOM   2147  N ND2 . ASN A 1 261 ? 22.280  16.791  102.360 1.00 83.44  ?  277 ASN B ND2 1 
ATOM   2148  N N   . LEU A 1 262 ? 22.569  13.990  107.081 1.00 76.21  ?  278 LEU B N   1 
ATOM   2149  C CA  . LEU A 1 262 ? 23.178  13.106  108.072 1.00 77.25  ?  278 LEU B CA  1 
ATOM   2150  C C   . LEU A 1 262 ? 22.226  12.040  108.608 1.00 77.28  ?  278 LEU B C   1 
ATOM   2151  O O   . LEU A 1 262 ? 22.661  11.205  109.409 1.00 81.37  ?  278 LEU B O   1 
ATOM   2152  C CB  . LEU A 1 262 ? 23.777  13.928  109.221 1.00 75.38  ?  278 LEU B CB  1 
ATOM   2153  C CG  . LEU A 1 262 ? 24.785  15.004  108.806 1.00 76.13  ?  278 LEU B CG  1 
ATOM   2154  C CD1 . LEU A 1 262 ? 25.437  15.663  110.005 1.00 73.80  ?  278 LEU B CD1 1 
ATOM   2155  C CD2 . LEU A 1 262 ? 25.871  14.360  107.928 1.00 74.96  ?  278 LEU B CD2 1 
ATOM   2156  N N   . TYR A 1 263 ? 20.975  11.992  108.154 1.00 78.93  ?  279 TYR B N   1 
ATOM   2157  C CA  . TYR A 1 263 ? 20.071  10.940  108.613 1.00 82.33  ?  279 TYR B CA  1 
ATOM   2158  C C   . TYR A 1 263 ? 20.583  9.542   108.263 1.00 84.84  ?  279 TYR B C   1 
ATOM   2159  O O   . TYR A 1 263 ? 20.647  8.660   109.137 1.00 83.66  ?  279 TYR B O   1 
ATOM   2160  C CB  . TYR A 1 263 ? 18.679  11.155  108.038 1.00 81.34  ?  279 TYR B CB  1 
ATOM   2161  C CG  . TYR A 1 263 ? 17.704  10.104  108.477 1.00 79.81  ?  279 TYR B CG  1 
ATOM   2162  C CD1 . TYR A 1 263 ? 17.165  10.136  109.747 1.00 80.58  ?  279 TYR B CD1 1 
ATOM   2163  C CD2 . TYR A 1 263 ? 17.264  9.129   107.605 1.00 80.39  ?  279 TYR B CD2 1 
ATOM   2164  C CE1 . TYR A 1 263 ? 16.264  9.184   110.175 1.00 83.09  ?  279 TYR B CE1 1 
ATOM   2165  C CE2 . TYR A 1 263 ? 16.346  8.180   108.015 1.00 87.18  ?  279 TYR B CE2 1 
ATOM   2166  C CZ  . TYR A 1 263 ? 15.850  8.215   109.308 1.00 84.71  ?  279 TYR B CZ  1 
ATOM   2167  O OH  . TYR A 1 263 ? 14.938  7.284   109.744 1.00 87.14  ?  279 TYR B OH  1 
ATOM   2168  N N   . SER A 1 264 ? 20.956  9.319   106.988 1.00 89.33  ?  280 SER B N   1 
ATOM   2169  C CA  . SER A 1 264 ? 21.547  8.035   106.600 1.00 85.77  ?  280 SER B CA  1 
ATOM   2170  C C   . SER A 1 264 ? 22.659  7.619   107.562 1.00 82.08  ?  280 SER B C   1 
ATOM   2171  O O   . SER A 1 264 ? 22.786  6.434   107.859 1.00 75.40  ?  280 SER B O   1 
ATOM   2172  C CB  . SER A 1 264 ? 22.058  8.080   105.140 1.00 86.43  ?  280 SER B CB  1 
ATOM   2173  O OG  . SER A 1 264 ? 23.307  8.745   104.968 1.00 83.17  ?  280 SER B OG  1 
ATOM   2174  N N   . LEU A 1 265 ? 23.423  8.583   108.117 1.00 87.82  ?  281 LEU B N   1 
ATOM   2175  C CA  . LEU A 1 265 ? 24.595  8.305   108.956 1.00 89.17  ?  281 LEU B CA  1 
ATOM   2176  C C   . LEU A 1 265 ? 24.276  8.312   110.449 1.00 87.93  ?  281 LEU B C   1 
ATOM   2177  O O   . LEU A 1 265 ? 25.146  7.966   111.254 1.00 92.48  ?  281 LEU B O   1 
ATOM   2178  C CB  . LEU A 1 265 ? 25.714  9.331   108.683 1.00 87.65  ?  281 LEU B CB  1 
ATOM   2179  C CG  . LEU A 1 265 ? 26.512  9.303   107.367 1.00 99.22  ?  281 LEU B CG  1 
ATOM   2180  C CD1 . LEU A 1 265 ? 27.585  10.374  107.352 1.00 105.91 ?  281 LEU B CD1 1 
ATOM   2181  C CD2 . LEU A 1 265 ? 27.142  7.943   107.076 1.00 93.60  ?  281 LEU B CD2 1 
ATOM   2182  N N   . THR A 1 266 ? 23.057  8.706   110.831 1.00 85.31  ?  282 THR B N   1 
ATOM   2183  C CA  . THR A 1 266 ? 22.665  8.876   112.225 1.00 86.43  ?  282 THR B CA  1 
ATOM   2184  C C   . THR A 1 266 ? 21.265  8.326   112.495 1.00 86.13  ?  282 THR B C   1 
ATOM   2185  O O   . THR A 1 266 ? 20.715  8.553   113.587 1.00 74.74  ?  282 THR B O   1 
ATOM   2186  C CB  . THR A 1 266 ? 22.734  10.367  112.626 1.00 80.72  ?  282 THR B CB  1 
ATOM   2187  O OG1 . THR A 1 266 ? 21.751  11.099  111.885 1.00 87.09  ?  282 THR B OG1 1 
ATOM   2188  C CG2 . THR A 1 266 ? 24.102  10.975  112.365 1.00 80.73  ?  282 THR B CG2 1 
ATOM   2189  N N   . VAL A 1 267 ? 20.679  7.621   111.536 1.00 94.16  ?  283 VAL B N   1 
ATOM   2190  C CA  . VAL A 1 267 ? 19.386  6.968   111.716 1.00 95.04  ?  283 VAL B CA  1 
ATOM   2191  C C   . VAL A 1 267 ? 19.403  6.085   112.960 1.00 96.66  ?  283 VAL B C   1 
ATOM   2192  O O   . VAL A 1 267 ? 20.237  5.170   113.070 1.00 102.05 ?  283 VAL B O   1 
ATOM   2193  C CB  . VAL A 1 267 ? 18.988  6.177   110.461 1.00 98.97  ?  283 VAL B CB  1 
ATOM   2194  C CG1 . VAL A 1 267 ? 20.141  5.318   109.964 1.00 100.46 ?  283 VAL B CG1 1 
ATOM   2195  C CG2 . VAL A 1 267 ? 17.802  5.300   110.782 1.00 105.81 ?  283 VAL B CG2 1 
ATOM   2196  N N   . PRO A 1 268 ? 18.531  6.351   113.922 1.00 93.11  ?  284 PRO B N   1 
ATOM   2197  C CA  . PRO A 1 268 ? 18.457  5.471   115.104 1.00 98.79  ?  284 PRO B CA  1 
ATOM   2198  C C   . PRO A 1 268 ? 18.253  3.993   114.794 1.00 102.94 ?  284 PRO B C   1 
ATOM   2199  O O   . PRO A 1 268 ? 19.055  3.163   115.237 1.00 101.96 ?  284 PRO B O   1 
ATOM   2200  C CB  . PRO A 1 268 ? 17.306  6.081   115.918 1.00 92.86  ?  284 PRO B CB  1 
ATOM   2201  C CG  . PRO A 1 268 ? 17.238  7.484   115.448 1.00 89.50  ?  284 PRO B CG  1 
ATOM   2202  C CD  . PRO A 1 268 ? 17.647  7.519   114.034 1.00 89.28  ?  284 PRO B CD  1 
ATOM   2203  N N   . PHE A 1 269 ? 17.169  3.662   114.085 1.00 101.35 ?  285 PHE B N   1 
ATOM   2204  C CA  . PHE A 1 269 ? 16.844  2.242   113.777 1.00 109.51 ?  285 PHE B CA  1 
ATOM   2205  C C   . PHE A 1 269 ? 16.692  2.067   112.269 1.00 116.32 ?  285 PHE B C   1 
ATOM   2206  O O   . PHE A 1 269 ? 15.575  2.255   111.760 1.00 117.54 ?  285 PHE B O   1 
ATOM   2207  C CB  . PHE A 1 269 ? 15.538  1.838   114.457 1.00 108.41 ?  285 PHE B CB  1 
ATOM   2208  C CG  . PHE A 1 269 ? 15.295  2.522   115.774 1.00 107.53 ?  285 PHE B CG  1 
ATOM   2209  C CD1 . PHE A 1 269 ? 15.809  1.998   116.945 1.00 108.10 ?  285 PHE B CD1 1 
ATOM   2210  C CD2 . PHE A 1 269 ? 14.569  3.695   115.834 1.00 105.70 ?  285 PHE B CD2 1 
ATOM   2211  C CE1 . PHE A 1 269 ? 15.585  2.629   118.158 1.00 108.09 ?  285 PHE B CE1 1 
ATOM   2212  C CE2 . PHE A 1 269 ? 14.347  4.329   117.045 1.00 101.99 ?  285 PHE B CE2 1 
ATOM   2213  C CZ  . PHE A 1 269 ? 14.855  3.793   118.204 1.00 102.47 ?  285 PHE B CZ  1 
ATOM   2214  N N   . GLY A 1 270 ? 17.768  1.701   111.584 1.00 141.63 ?  286 GLY B N   1 
ATOM   2215  C CA  . GLY A 1 270 ? 17.716  1.636   110.114 1.00 144.76 ?  286 GLY B CA  1 
ATOM   2216  C C   . GLY A 1 270 ? 16.752  0.585   109.623 1.00 153.18 ?  286 GLY B C   1 
ATOM   2217  O O   . GLY A 1 270 ? 15.881  0.918   108.804 1.00 158.91 ?  286 GLY B O   1 
ATOM   2218  N N   . GLN A 1 271 ? 16.900  -0.649  110.099 1.00 127.61 ?  287 GLN B N   1 
ATOM   2219  C CA  . GLN A 1 271 ? 16.056  -1.748  109.570 1.00 126.57 ?  287 GLN B CA  1 
ATOM   2220  C C   . GLN A 1 271 ? 14.610  -1.262  109.397 1.00 128.88 ?  287 GLN B C   1 
ATOM   2221  O O   . GLN A 1 271 ? 13.983  -1.634  108.391 1.00 129.37 ?  287 GLN B O   1 
ATOM   2222  C CB  . GLN A 1 271 ? 16.183  -2.970  110.480 1.00 127.27 ?  287 GLN B CB  1 
ATOM   2223  C CG  . GLN A 1 271 ? 17.547  -3.125  111.144 1.00 130.22 ?  287 GLN B CG  1 
ATOM   2224  C CD  . GLN A 1 271 ? 18.678  -3.459  110.201 1.00 134.57 ?  287 GLN B CD  1 
ATOM   2225  O OE1 . GLN A 1 271 ? 19.772  -3.827  110.622 1.00 135.32 ?  287 GLN B OE1 1 
ATOM   2226  N NE2 . GLN A 1 271 ? 18.431  -3.330  108.907 1.00 137.85 ?  287 GLN B NE2 1 
ATOM   2227  N N   . LYS A 1 272 ? 14.106  -0.455  110.328 1.00 130.22 ?  288 LYS B N   1 
ATOM   2228  C CA  . LYS A 1 272 ? 12.689  0.001   110.273 1.00 133.27 ?  288 LYS B CA  1 
ATOM   2229  C C   . LYS A 1 272 ? 12.323  0.524   108.880 1.00 144.51 ?  288 LYS B C   1 
ATOM   2230  O O   . LYS A 1 272 ? 13.120  1.283   108.305 1.00 143.35 ?  288 LYS B O   1 
ATOM   2231  C CB  . LYS A 1 272 ? 12.460  1.104   111.305 1.00 125.49 ?  288 LYS B CB  1 
ATOM   2232  C CG  . LYS A 1 272 ? 12.036  0.607   112.678 1.00 121.65 ?  288 LYS B CG  1 
ATOM   2233  C CD  . LYS A 1 272 ? 11.023  -0.505  112.567 1.00 122.34 ?  288 LYS B CD  1 
ATOM   2234  C CE  . LYS A 1 272 ? 10.916  -1.329  113.831 1.00 121.13 ?  288 LYS B CE  1 
ATOM   2235  N NZ  . LYS A 1 272 ? 9.532   -1.819  114.016 1.00 114.30 ?  288 LYS B NZ  1 
ATOM   2236  N N   . PRO A 1 273 ? 11.152  0.160   108.316 1.00 170.47 ?  289 PRO B N   1 
ATOM   2237  C CA  . PRO A 1 273 ? 10.708  0.705   107.033 1.00 171.87 ?  289 PRO B CA  1 
ATOM   2238  C C   . PRO A 1 273 ? 10.369  2.175   107.170 1.00 161.38 ?  289 PRO B C   1 
ATOM   2239  O O   . PRO A 1 273 ? 9.366   2.523   107.800 1.00 158.82 ?  289 PRO B O   1 
ATOM   2240  C CB  . PRO A 1 273 ? 9.465   -0.131  106.701 1.00 174.50 ?  289 PRO B CB  1 
ATOM   2241  C CG  . PRO A 1 273 ? 8.957   -0.579  108.036 1.00 177.08 ?  289 PRO B CG  1 
ATOM   2242  C CD  . PRO A 1 273 ? 10.179  -0.793  108.884 1.00 171.36 ?  289 PRO B CD  1 
ATOM   2243  N N   . ASN A 1 274 ? 11.196  3.050   106.610 1.00 155.65 ?  290 ASN B N   1 
ATOM   2244  C CA  . ASN A 1 274 ? 10.789  4.440   106.547 1.00 144.57 ?  290 ASN B CA  1 
ATOM   2245  C C   . ASN A 1 274 ? 9.535   4.568   105.685 1.00 141.12 ?  290 ASN B C   1 
ATOM   2246  O O   . ASN A 1 274 ? 9.167   3.667   104.922 1.00 143.34 ?  290 ASN B O   1 
ATOM   2247  C CB  . ASN A 1 274 ? 11.905  5.323   105.991 1.00 143.64 ?  290 ASN B CB  1 
ATOM   2248  C CG  . ASN A 1 274 ? 11.823  6.744   106.513 1.00 140.91 ?  290 ASN B CG  1 
ATOM   2249  O OD1 . ASN A 1 274 ? 10.877  7.480   106.210 1.00 139.52 ?  290 ASN B OD1 1 
ATOM   2250  N ND2 . ASN A 1 274 ? 12.813  7.138   107.310 1.00 133.87 ?  290 ASN B ND2 1 
ATOM   2251  N N   . ILE A 1 275 ? 8.866   5.700   105.820 1.00 132.48 ?  291 ILE B N   1 
ATOM   2252  C CA  . ILE A 1 275 ? 7.603   5.924   105.138 1.00 125.33 ?  291 ILE B CA  1 
ATOM   2253  C C   . ILE A 1 275 ? 7.881   6.683   103.848 1.00 118.02 ?  291 ILE B C   1 
ATOM   2254  O O   . ILE A 1 275 ? 8.610   7.683   103.849 1.00 118.01 ?  291 ILE B O   1 
ATOM   2255  C CB  . ILE A 1 275 ? 6.626   6.684   106.047 1.00 119.23 ?  291 ILE B CB  1 
ATOM   2256  C CG1 . ILE A 1 275 ? 6.303   5.832   107.277 1.00 125.01 ?  291 ILE B CG1 1 
ATOM   2257  C CG2 . ILE A 1 275 ? 5.344   6.987   105.305 1.00 106.74 ?  291 ILE B CG2 1 
ATOM   2258  C CD1 . ILE A 1 275 ? 5.216   6.400   108.158 1.00 116.59 ?  291 ILE B CD1 1 
ATOM   2259  N N   . ASP A 1 276 ? 7.343   6.187   102.738 1.00 112.26 ?  292 ASP B N   1 
ATOM   2260  C CA  . ASP A 1 276 ? 7.476   6.877   101.454 1.00 113.04 ?  292 ASP B CA  1 
ATOM   2261  C C   . ASP A 1 276 ? 6.383   6.333   100.539 1.00 113.73 ?  292 ASP B C   1 
ATOM   2262  O O   . ASP A 1 276 ? 6.551   5.264   99.948  1.00 114.37 ?  292 ASP B O   1 
ATOM   2263  C CB  . ASP A 1 276 ? 8.856   6.688   100.838 1.00 111.01 ?  292 ASP B CB  1 
ATOM   2264  C CG  . ASP A 1 276 ? 8.986   7.380   99.475  1.00 112.23 ?  292 ASP B CG  1 
ATOM   2265  O OD1 . ASP A 1 276 ? 8.037   8.077   99.068  1.00 114.40 ?  292 ASP B OD1 1 
ATOM   2266  O OD2 . ASP A 1 276 ? 10.006  7.199   98.781  1.00 107.53 -1 292 ASP B OD2 1 
ATOM   2267  N N   . VAL A 1 277 ? 5.297   7.086   100.408 1.00 118.47 ?  293 VAL B N   1 
ATOM   2268  C CA  . VAL A 1 277 ? 4.135   6.562   99.703  1.00 130.12 ?  293 VAL B CA  1 
ATOM   2269  C C   . VAL A 1 277 ? 4.242   6.775   98.194  1.00 128.24 ?  293 VAL B C   1 
ATOM   2270  O O   . VAL A 1 277 ? 3.277   6.532   97.463  1.00 129.73 ?  293 VAL B O   1 
ATOM   2271  C CB  . VAL A 1 277 ? 2.834   7.166   100.270 1.00 136.66 ?  293 VAL B CB  1 
ATOM   2272  C CG1 . VAL A 1 277 ? 2.665   6.778   101.727 1.00 130.05 ?  293 VAL B CG1 1 
ATOM   2273  C CG2 . VAL A 1 277 ? 2.860   8.666   100.180 1.00 133.03 ?  293 VAL B CG2 1 
ATOM   2274  N N   . THR A 1 278 ? 5.417   7.205   97.719  1.00 121.04 ?  294 THR B N   1 
ATOM   2275  C CA  . THR A 1 278 ? 5.703   7.389   96.290  1.00 119.36 ?  294 THR B CA  1 
ATOM   2276  C C   . THR A 1 278 ? 5.167   6.218   95.488  1.00 120.47 ?  294 THR B C   1 
ATOM   2277  O O   . THR A 1 278 ? 4.553   6.355   94.409  1.00 118.62 ?  294 THR B O   1 
ATOM   2278  C CB  . THR A 1 278 ? 7.222   7.469   96.030  1.00 113.35 ?  294 THR B CB  1 
ATOM   2279  O OG1 . THR A 1 278 ? 7.825   8.523   96.792  1.00 105.19 ?  294 THR B OG1 1 
ATOM   2280  C CG2 . THR A 1 278 ? 7.474   7.718   94.554  1.00 108.37 ?  294 THR B CG2 1 
ATOM   2281  N N   . ASP A 1 279 ? 5.413   5.045   96.050  1.00 117.49 ?  295 ASP B N   1 
ATOM   2282  C CA  . ASP A 1 279 ? 5.170   3.812   95.348  1.00 117.10 ?  295 ASP B CA  1 
ATOM   2283  C C   . ASP A 1 279 ? 3.680   3.522   95.291  1.00 124.03 ?  295 ASP B C   1 
ATOM   2284  O O   . ASP A 1 279 ? 3.136   3.195   94.223  1.00 123.88 ?  295 ASP B O   1 
ATOM   2285  C CB  . ASP A 1 279 ? 5.944   2.740   96.071  1.00 114.64 ?  295 ASP B CB  1 
ATOM   2286  C CG  . ASP A 1 279 ? 7.394   2.804   95.729  1.00 113.58 ?  295 ASP B CG  1 
ATOM   2287  O OD1 . ASP A 1 279 ? 7.699   3.356   94.644  1.00 108.70 ?  295 ASP B OD1 1 
ATOM   2288  O OD2 . ASP A 1 279 ? 8.209   2.381   96.570  1.00 114.25 -1 295 ASP B OD2 1 
ATOM   2289  N N   . ALA A 1 280 ? 2.996   3.692   96.425  1.00 132.38 ?  296 ALA B N   1 
ATOM   2290  C CA  . ALA A 1 280 ? 1.540   3.671   96.423  1.00 131.06 ?  296 ALA B CA  1 
ATOM   2291  C C   . ALA A 1 280 ? 0.957   4.596   95.357  1.00 129.60 ?  296 ALA B C   1 
ATOM   2292  O O   . ALA A 1 280 ? -0.002  4.225   94.669  1.00 125.83 ?  296 ALA B O   1 
ATOM   2293  C CB  . ALA A 1 280 ? 1.014   4.050   97.809  1.00 131.55 ?  296 ALA B CB  1 
ATOM   2294  N N   . MET A 1 281 ? 1.535   5.797   95.200  1.00 120.02 ?  297 MET B N   1 
ATOM   2295  C CA  . MET A 1 281 ? 0.959   6.807   94.308  1.00 120.62 ?  297 MET B CA  1 
ATOM   2296  C C   . MET A 1 281 ? 1.089   6.422   92.837  1.00 120.22 ?  297 MET B C   1 
ATOM   2297  O O   . MET A 1 281 ? 0.123   6.558   92.064  1.00 117.83 ?  297 MET B O   1 
ATOM   2298  C CB  . MET A 1 281 ? 1.590   8.177   94.549  1.00 117.74 ?  297 MET B CB  1 
ATOM   2299  C CG  . MET A 1 281 ? 1.490   8.668   95.973  1.00 118.59 ?  297 MET B CG  1 
ATOM   2300  S SD  . MET A 1 281 ? 2.605   10.033  96.345  1.00 103.00 ?  297 MET B SD  1 
ATOM   2301  C CE  . MET A 1 281 ? 1.885   11.266  95.264  1.00 110.79 ?  297 MET B CE  1 
ATOM   2302  N N   . VAL A 1 282 ? 2.272   5.967   92.415  1.00 123.44 ?  298 VAL B N   1 
ATOM   2303  C CA  . VAL A 1 282 ? 2.340   5.376   91.083  1.00 119.03 ?  298 VAL B CA  1 
ATOM   2304  C C   . VAL A 1 282 ? 1.311   4.265   90.945  1.00 115.80 ?  298 VAL B C   1 
ATOM   2305  O O   . VAL A 1 282 ? 0.593   4.190   89.946  1.00 114.72 ?  298 VAL B O   1 
ATOM   2306  C CB  . VAL A 1 282 ? 3.756   4.872   90.792  1.00 110.48 ?  298 VAL B CB  1 
ATOM   2307  C CG1 . VAL A 1 282 ? 3.772   4.154   89.468  1.00 101.41 ?  298 VAL B CG1 1 
ATOM   2308  C CG2 . VAL A 1 282 ? 4.705   6.045   90.778  1.00 101.63 ?  298 VAL B CG2 1 
ATOM   2309  N N   . ASP A 1 283 ? 1.169   3.438   91.984  1.00 117.25 ?  299 ASP B N   1 
ATOM   2310  C CA  . ASP A 1 283 ? 0.400   2.209   91.867  1.00 115.98 ?  299 ASP B CA  1 
ATOM   2311  C C   . ASP A 1 283 ? -1.105  2.452   91.825  1.00 112.11 ?  299 ASP B C   1 
ATOM   2312  O O   . ASP A 1 283 ? -1.856  1.563   91.398  1.00 111.01 ?  299 ASP B O   1 
ATOM   2313  C CB  . ASP A 1 283 ? 0.781   1.299   93.026  1.00 123.32 ?  299 ASP B CB  1 
ATOM   2314  C CG  . ASP A 1 283 ? 2.178   0.708   92.856  1.00 126.32 ?  299 ASP B CG  1 
ATOM   2315  O OD1 . ASP A 1 283 ? 2.779   0.909   91.769  1.00 120.82 ?  299 ASP B OD1 1 
ATOM   2316  O OD2 . ASP A 1 283 ? 2.686   0.085   93.817  1.00 135.58 -1 299 ASP B OD2 1 
ATOM   2317  N N   . GLN A 1 284 ? -1.557  3.620   92.264  1.00 113.53 ?  300 GLN B N   1 
ATOM   2318  C CA  . GLN A 1 284 ? -2.945  4.021   92.101  1.00 113.04 ?  300 GLN B CA  1 
ATOM   2319  C C   . GLN A 1 284 ? -3.119  4.976   90.930  1.00 112.39 ?  300 GLN B C   1 
ATOM   2320  O O   . GLN A 1 284 ? -4.234  5.447   90.685  1.00 110.80 ?  300 GLN B O   1 
ATOM   2321  C CB  . GLN A 1 284 ? -3.464  4.644   93.397  1.00 111.16 ?  300 GLN B CB  1 
ATOM   2322  C CG  . GLN A 1 284 ? -3.290  3.747   94.606  1.00 107.82 ?  300 GLN B CG  1 
ATOM   2323  C CD  . GLN A 1 284 ? -3.627  4.444   95.905  1.00 114.79 ?  300 GLN B CD  1 
ATOM   2324  O OE1 . GLN A 1 284 ? -4.440  5.374   95.938  1.00 118.69 ?  300 GLN B OE1 1 
ATOM   2325  N NE2 . GLN A 1 284 ? -2.984  4.014   96.989  1.00 119.25 ?  300 GLN B NE2 1 
ATOM   2326  N N   . ALA A 1 285 ? -2.032  5.259   90.205  1.00 111.02 ?  301 ALA B N   1 
ATOM   2327  C CA  . ALA A 1 285 ? -2.044  6.088   89.005  1.00 109.96 ?  301 ALA B CA  1 
ATOM   2328  C C   . ALA A 1 285 ? -2.414  7.531   89.350  1.00 114.33 ?  301 ALA B C   1 
ATOM   2329  O O   . ALA A 1 285 ? -3.397  8.092   88.850  1.00 111.21 ?  301 ALA B O   1 
ATOM   2330  C CB  . ALA A 1 285 ? -2.986  5.509   87.947  1.00 104.33 ?  301 ALA B CB  1 
ATOM   2331  N N   . TRP A 1 286 ? -1.613  8.117   90.243  1.00 112.72 ?  302 TRP B N   1 
ATOM   2332  C CA  . TRP A 1 286 ? -1.784  9.509   90.639  1.00 111.44 ?  302 TRP B CA  1 
ATOM   2333  C C   . TRP A 1 286 ? -0.980  10.394  89.698  1.00 114.46 ?  302 TRP B C   1 
ATOM   2334  O O   . TRP A 1 286 ? 0.208   10.149  89.467  1.00 112.40 ?  302 TRP B O   1 
ATOM   2335  C CB  . TRP A 1 286 ? -1.359  9.750   92.092  1.00 108.03 ?  302 TRP B CB  1 
ATOM   2336  C CG  . TRP A 1 286 ? -2.355  9.217   93.086  1.00 112.12 ?  302 TRP B CG  1 
ATOM   2337  C CD1 . TRP A 1 286 ? -3.146  8.109   92.936  1.00 115.08 ?  302 TRP B CD1 1 
ATOM   2338  C CD2 . TRP A 1 286 ? -2.726  9.797   94.342  1.00 112.76 ?  302 TRP B CD2 1 
ATOM   2339  N NE1 . TRP A 1 286 ? -3.951  7.936   94.040  1.00 115.13 ?  302 TRP B NE1 1 
ATOM   2340  C CE2 . TRP A 1 286 ? -3.719  8.962   94.915  1.00 111.87 ?  302 TRP B CE2 1 
ATOM   2341  C CE3 . TRP A 1 286 ? -2.311  10.929  95.044  1.00 112.30 ?  302 TRP B CE3 1 
ATOM   2342  C CZ2 . TRP A 1 286 ? -4.300  9.225   96.154  1.00 110.51 ?  302 TRP B CZ2 1 
ATOM   2343  C CZ3 . TRP A 1 286 ? -2.892  11.193  96.278  1.00 113.74 ?  302 TRP B CZ3 1 
ATOM   2344  C CH2 . TRP A 1 286 ? -3.879  10.341  96.819  1.00 112.30 ?  302 TRP B CH2 1 
ATOM   2345  N N   . ASP A 1 287 ? -1.649  11.394  89.130  1.00 118.55 ?  303 ASP B N   1 
ATOM   2346  C CA  . ASP A 1 287 ? -1.044  12.460  88.340  1.00 115.39 ?  303 ASP B CA  1 
ATOM   2347  C C   . ASP A 1 287 ? -1.073  13.779  89.118  1.00 115.16 ?  303 ASP B C   1 
ATOM   2348  O O   . ASP A 1 287 ? -1.666  13.884  90.202  1.00 113.90 ?  303 ASP B O   1 
ATOM   2349  C CB  . ASP A 1 287 ? -1.752  12.598  86.979  1.00 113.82 ?  303 ASP B CB  1 
ATOM   2350  C CG  . ASP A 1 287 ? -3.284  12.769  87.101  1.00 115.13 ?  303 ASP B CG  1 
ATOM   2351  O OD1 . ASP A 1 287 ? -3.823  12.866  88.225  1.00 116.89 ?  303 ASP B OD1 1 
ATOM   2352  O OD2 . ASP A 1 287 ? -3.951  12.829  86.046  1.00 118.71 -1 303 ASP B OD2 1 
ATOM   2353  N N   . ALA A 1 288 ? -0.353  14.787  88.621  1.00 114.63 ?  304 ALA B N   1 
ATOM   2354  C CA  . ALA A 1 288 ? -0.272  16.072  89.358  1.00 107.69 ?  304 ALA B CA  1 
ATOM   2355  C C   . ALA A 1 288 ? -1.671  16.525  89.750  1.00 105.57 ?  304 ALA B C   1 
ATOM   2356  O O   . ALA A 1 288 ? -1.902  16.755  90.939  1.00 100.15 ?  304 ALA B O   1 
ATOM   2357  C CB  . ALA A 1 288 ? 0.403   17.098  88.492  1.00 101.32 ?  304 ALA B CB  1 
ATOM   2358  N N   . GLN A 1 289 ? -2.556  16.645  88.766  1.00 97.47  ?  305 GLN B N   1 
ATOM   2359  C CA  . GLN A 1 289 ? -3.945  17.089  89.032  1.00 99.26  ?  305 GLN B CA  1 
ATOM   2360  C C   . GLN A 1 289 ? -4.482  16.371  90.274  1.00 101.03 ?  305 GLN B C   1 
ATOM   2361  O O   . GLN A 1 289 ? -5.216  16.996  91.049  1.00 97.38  ?  305 GLN B O   1 
ATOM   2362  C CB  . GLN A 1 289 ? -4.805  16.813  87.800  1.00 107.76 ?  305 GLN B CB  1 
ATOM   2363  C CG  . GLN A 1 289 ? -6.235  16.455  88.145  1.00 110.83 ?  305 GLN B CG  1 
ATOM   2364  C CD  . GLN A 1 289 ? -7.171  17.576  87.779  1.00 109.68 ?  305 GLN B CD  1 
ATOM   2365  O OE1 . GLN A 1 289 ? -6.750  18.684  87.464  1.00 99.33  ?  305 GLN B OE1 1 
ATOM   2366  N NE2 . GLN A 1 289 ? -8.460  17.288  87.809  1.00 104.64 ?  305 GLN B NE2 1 
ATOM   2367  N N   . ARG A 1 290 ? -4.133  15.095  90.443  1.00 103.91 ?  306 ARG B N   1 
ATOM   2368  C CA  . ARG A 1 290 ? -4.602  14.344  91.633  1.00 100.89 ?  306 ARG B CA  1 
ATOM   2369  C C   . ARG A 1 290 ? -3.955  14.979  92.857  1.00 96.02  ?  306 ARG B C   1 
ATOM   2370  O O   . ARG A 1 290 ? -4.687  15.432  93.756  1.00 93.22  ?  306 ARG B O   1 
ATOM   2371  C CB  . ARG A 1 290 ? -4.240  12.859  91.535  1.00 104.27 ?  306 ARG B CB  1 
ATOM   2372  C CG  . ARG A 1 290 ? -4.630  12.048  92.763  1.00 103.67 ?  306 ARG B CG  1 
ATOM   2373  C CD  . ARG A 1 290 ? -6.109  12.145  93.047  1.00 100.87 ?  306 ARG B CD  1 
ATOM   2374  N NE  . ARG A 1 290 ? -6.550  11.232  94.096  1.00 104.35 ?  306 ARG B NE  1 
ATOM   2375  C CZ  . ARG A 1 290 ? -6.800  9.941   93.909  1.00 115.29 ?  306 ARG B CZ  1 
ATOM   2376  N NH1 . ARG A 1 290 ? -6.651  9.402   92.712  1.00 115.45 ?  306 ARG B NH1 1 
ATOM   2377  N NH2 . ARG A 1 290 ? -7.198  9.195   94.922  1.00 120.97 ?  306 ARG B NH2 1 
ATOM   2378  N N   . ILE A 1 291 ? -2.633  15.042  92.853  1.00 94.51  ?  307 ILE B N   1 
ATOM   2379  C CA  . ILE A 1 291 ? -1.932  15.631  93.995  1.00 96.02  ?  307 ILE B CA  1 
ATOM   2380  C C   . ILE A 1 291 ? -2.647  16.892  94.462  1.00 94.37  ?  307 ILE B C   1 
ATOM   2381  O O   . ILE A 1 291 ? -3.063  17.017  95.624  1.00 92.33  ?  307 ILE B O   1 
ATOM   2382  C CB  . ILE A 1 291 ? -0.467  15.930  93.639  1.00 93.83  ?  307 ILE B CB  1 
ATOM   2383  C CG1 . ILE A 1 291 ? 0.300   14.639  93.450  1.00 95.48  ?  307 ILE B CG1 1 
ATOM   2384  C CG2 . ILE A 1 291 ? 0.175   16.761  94.695  1.00 92.51  ?  307 ILE B CG2 1 
ATOM   2385  C CD1 . ILE A 1 291 ? 1.658   14.867  92.932  1.00 99.36  ?  307 ILE B CD1 1 
ATOM   2386  N N   . PHE A 1 292 ? -2.811  17.843  93.550  1.00 90.66  ?  308 PHE B N   1 
ATOM   2387  C CA  . PHE A 1 292 ? -3.380  19.120  93.954  1.00 87.86  ?  308 PHE B CA  1 
ATOM   2388  C C   . PHE A 1 292 ? -4.854  18.991  94.287  1.00 85.54  ?  308 PHE B C   1 
ATOM   2389  O O   . PHE A 1 292 ? -5.360  19.756  95.112  1.00 86.47  ?  308 PHE B O   1 
ATOM   2390  C CB  . PHE A 1 292 ? -3.162  20.157  92.858  1.00 91.36  ?  308 PHE B CB  1 
ATOM   2391  C CG  . PHE A 1 292 ? -1.764  20.709  92.833  1.00 91.42  ?  308 PHE B CG  1 
ATOM   2392  C CD1 . PHE A 1 292 ? -0.760  20.043  92.146  1.00 89.66  ?  308 PHE B CD1 1 
ATOM   2393  C CD2 . PHE A 1 292 ? -1.456  21.884  93.482  1.00 88.63  ?  308 PHE B CD2 1 
ATOM   2394  C CE1 . PHE A 1 292 ? 0.503   20.532  92.107  1.00 87.83  ?  308 PHE B CE1 1 
ATOM   2395  C CE2 . PHE A 1 292 ? -0.179  22.372  93.443  1.00 86.47  ?  308 PHE B CE2 1 
ATOM   2396  C CZ  . PHE A 1 292 ? 0.800   21.692  92.756  1.00 85.22  ?  308 PHE B CZ  1 
ATOM   2397  N N   . LYS A 1 293 ? -5.555  18.032  93.681  1.00 87.32  ?  309 LYS B N   1 
ATOM   2398  C CA  . LYS A 1 293 ? -6.925  17.786  94.092  1.00 89.47  ?  309 LYS B CA  1 
ATOM   2399  C C   . LYS A 1 293 ? -6.977  17.307  95.537  1.00 87.02  ?  309 LYS B C   1 
ATOM   2400  O O   . LYS A 1 293 ? -7.846  17.738  96.301  1.00 87.51  ?  309 LYS B O   1 
ATOM   2401  C CB  . LYS A 1 293 ? -7.584  16.771  93.158  1.00 91.27  ?  309 LYS B CB  1 
ATOM   2402  C CG  . LYS A 1 293 ? -8.030  17.270  91.791  1.00 92.63  ?  309 LYS B CG  1 
ATOM   2403  C CD  . LYS A 1 293 ? -9.203  18.219  91.850  1.00 90.86  ?  309 LYS B CD  1 
ATOM   2404  C CE  . LYS A 1 293 ? -9.466  18.811  90.476  1.00 88.65  ?  309 LYS B CE  1 
ATOM   2405  N NZ  . LYS A 1 293 ? -10.579 19.787  90.486  1.00 85.12  ?  309 LYS B NZ  1 
ATOM   2406  N N   . GLU A 1 294 ? -6.071  16.399  95.930  1.00 83.22  ?  310 GLU B N   1 
ATOM   2407  C CA  . GLU A 1 294 ? -6.088  15.929  97.316  1.00 83.34  ?  310 GLU B CA  1 
ATOM   2408  C C   . GLU A 1 294 ? -5.730  17.056  98.272  1.00 83.20  ?  310 GLU B C   1 
ATOM   2409  O O   . GLU A 1 294 ? -6.246  17.112  99.398  1.00 81.51  ?  310 GLU B O   1 
ATOM   2410  C CB  . GLU A 1 294 ? -5.139  14.740  97.515  1.00 86.73  ?  310 GLU B CB  1 
ATOM   2411  C CG  . GLU A 1 294 ? -5.600  13.413  96.910  1.00 95.15  ?  310 GLU B CG  1 
ATOM   2412  C CD  . GLU A 1 294 ? -6.876  12.853  97.556  1.00 97.25  ?  310 GLU B CD  1 
ATOM   2413  O OE1 . GLU A 1 294 ? -7.158  13.181  98.733  1.00 90.96  ?  310 GLU B OE1 1 
ATOM   2414  O OE2 . GLU A 1 294 ? -7.588  12.070  96.879  1.00 100.03 -1 310 GLU B OE2 1 
ATOM   2415  N N   . ALA A 1 295 ? -4.868  17.969  97.824  1.00 83.71  ?  311 ALA B N   1 
ATOM   2416  C CA  . ALA A 1 295 ? -4.583  19.166  98.606  1.00 81.26  ?  311 ALA B CA  1 
ATOM   2417  C C   . ALA A 1 295 ? -5.846  20.019  98.786  1.00 80.26  ?  311 ALA B C   1 
ATOM   2418  O O   . ALA A 1 295 ? -6.214  20.377  99.915  1.00 79.67  ?  311 ALA B O   1 
ATOM   2419  C CB  . ALA A 1 295 ? -3.455  19.946  97.934  1.00 80.09  ?  311 ALA B CB  1 
ATOM   2420  N N   . GLU A 1 296 ? -6.514  20.361  97.676  1.00 77.67  ?  312 GLU B N   1 
ATOM   2421  C CA  . GLU A 1 296 ? -7.797  21.072  97.721  1.00 79.37  ?  312 GLU B CA  1 
ATOM   2422  C C   . GLU A 1 296 ? -8.759  20.413  98.690  1.00 77.36  ?  312 GLU B C   1 
ATOM   2423  O O   . GLU A 1 296 ? -9.430  21.085  99.482  1.00 75.53  ?  312 GLU B O   1 
ATOM   2424  C CB  . GLU A 1 296 ? -8.438  21.113  96.327  1.00 82.06  ?  312 GLU B CB  1 
ATOM   2425  C CG  . GLU A 1 296 ? -9.861  21.704  96.272  1.00 86.09  ?  312 GLU B CG  1 
ATOM   2426  C CD  . GLU A 1 296 ? -10.344 21.907  94.836  1.00 88.42  ?  312 GLU B CD  1 
ATOM   2427  O OE1 . GLU A 1 296 ? -10.376 20.898  94.100  1.00 86.70  ?  312 GLU B OE1 1 
ATOM   2428  O OE2 . GLU A 1 296 ? -10.722 23.044  94.448  1.00 87.21  -1 312 GLU B OE2 1 
ATOM   2429  N N   . LYS A 1 297 ? -8.887  19.095  98.574  1.00 78.92  ?  313 LYS B N   1 
ATOM   2430  C CA  . LYS A 1 297 ? -9.744  18.337  99.467  1.00 77.51  ?  313 LYS B CA  1 
ATOM   2431  C C   . LYS A 1 297 ? -9.359  18.585  100.920 1.00 78.20  ?  313 LYS B C   1 
ATOM   2432  O O   . LYS A 1 297 ? -10.224 18.889  101.751 1.00 75.68  ?  313 LYS B O   1 
ATOM   2433  C CB  . LYS A 1 297 ? -9.667  16.857  99.077  1.00 77.48  ?  313 LYS B CB  1 
ATOM   2434  C CG  . LYS A 1 297 ? -10.816 16.005  99.550  1.00 76.46  ?  313 LYS B CG  1 
ATOM   2435  C CD  . LYS A 1 297 ? -10.662 14.535  99.122  1.00 81.57  ?  313 LYS B CD  1 
ATOM   2436  C CE  . LYS A 1 297 ? -10.533 14.421  97.581  1.00 84.45  ?  313 LYS B CE  1 
ATOM   2437  N NZ  . LYS A 1 297 ? -10.369 13.021  97.045  1.00 88.58  ?  313 LYS B NZ  1 
ATOM   2438  N N   . PHE A 1 298 ? -8.061  18.472  101.237 1.00 77.45  ?  314 PHE B N   1 
ATOM   2439  C CA  . PHE A 1 298 ? -7.594  18.674  102.607 1.00 72.96  ?  314 PHE B CA  1 
ATOM   2440  C C   . PHE A 1 298 ? -8.024  20.036  103.126 1.00 71.73  ?  314 PHE B C   1 
ATOM   2441  O O   . PHE A 1 298 ? -8.609  20.149  104.211 1.00 72.01  ?  314 PHE B O   1 
ATOM   2442  C CB  . PHE A 1 298 ? -6.070  18.520  102.657 1.00 75.08  ?  314 PHE B CB  1 
ATOM   2443  C CG  . PHE A 1 298 ? -5.438  19.072  103.906 1.00 75.49  ?  314 PHE B CG  1 
ATOM   2444  C CD1 . PHE A 1 298 ? -5.550  18.409  105.111 1.00 73.61  ?  314 PHE B CD1 1 
ATOM   2445  C CD2 . PHE A 1 298 ? -4.733  20.264  103.880 1.00 72.75  ?  314 PHE B CD2 1 
ATOM   2446  C CE1 . PHE A 1 298 ? -4.975  18.931  106.278 1.00 68.63  ?  314 PHE B CE1 1 
ATOM   2447  C CE2 . PHE A 1 298 ? -4.156  20.780  105.044 1.00 69.21  ?  314 PHE B CE2 1 
ATOM   2448  C CZ  . PHE A 1 298 ? -4.279  20.111  106.237 1.00 65.50  ?  314 PHE B CZ  1 
ATOM   2449  N N   . PHE A 1 299 ? -7.769  21.079  102.342 1.00 70.52  ?  315 PHE B N   1 
ATOM   2450  C CA  . PHE A 1 299 ? -8.174  22.420  102.760 1.00 69.19  ?  315 PHE B CA  1 
ATOM   2451  C C   . PHE A 1 299 ? -9.682  22.522  102.928 1.00 70.82  ?  315 PHE B C   1 
ATOM   2452  O O   . PHE A 1 299 ? -10.156 23.073  103.926 1.00 72.57  ?  315 PHE B O   1 
ATOM   2453  C CB  . PHE A 1 299 ? -7.665  23.466  101.777 1.00 68.69  ?  315 PHE B CB  1 
ATOM   2454  C CG  . PHE A 1 299 ? -6.202  23.637  101.820 1.00 70.59  ?  315 PHE B CG  1 
ATOM   2455  C CD1 . PHE A 1 299 ? -5.605  24.250  102.919 1.00 73.94  ?  315 PHE B CD1 1 
ATOM   2456  C CD2 . PHE A 1 299 ? -5.403  23.130  100.819 1.00 69.00  ?  315 PHE B CD2 1 
ATOM   2457  C CE1 . PHE A 1 299 ? -4.205  24.401  102.999 1.00 68.28  ?  315 PHE B CE1 1 
ATOM   2458  C CE2 . PHE A 1 299 ? -4.017  23.265  100.895 1.00 73.06  ?  315 PHE B CE2 1 
ATOM   2459  C CZ  . PHE A 1 299 ? -3.416  23.904  101.982 1.00 69.29  ?  315 PHE B CZ  1 
ATOM   2460  N N   . VAL A 1 300 ? -10.420 22.041  101.937 1.00 72.19  ?  316 VAL B N   1 
ATOM   2461  C CA  . VAL A 1 300 ? -11.901 22.061  102.052 1.00 73.18  ?  316 VAL B CA  1 
ATOM   2462  C C   . VAL A 1 300 ? -12.248 21.329  103.340 1.00 72.56  ?  316 VAL B C   1 
ATOM   2463  O O   . VAL A 1 300 ? -13.081 21.836  104.101 1.00 73.74  ?  316 VAL B O   1 
ATOM   2464  C CB  . VAL A 1 300 ? -12.567 21.408  100.831 1.00 70.05  ?  316 VAL B CB  1 
ATOM   2465  C CG1 . VAL A 1 300 ? -14.046 21.160  101.067 1.00 58.65  ?  316 VAL B CG1 1 
ATOM   2466  C CG2 . VAL A 1 300 ? -12.358 22.233  99.572  1.00 74.62  ?  316 VAL B CG2 1 
ATOM   2467  N N   . SER A 1 301 ? -11.570 20.214  103.597 1.00 73.42  ?  317 SER B N   1 
ATOM   2468  C CA  . SER A 1 301 ? -11.886 19.385  104.785 1.00 75.94  ?  317 SER B CA  1 
ATOM   2469  C C   . SER A 1 301 ? -11.920 20.235  106.048 1.00 75.45  ?  317 SER B C   1 
ATOM   2470  O O   . SER A 1 301 ? -12.510 19.778  107.035 1.00 79.73  ?  317 SER B O   1 
ATOM   2471  C CB  . SER A 1 301 ? -10.881 18.290  104.935 1.00 75.35  ?  317 SER B CB  1 
ATOM   2472  O OG  . SER A 1 301 ? -9.919  18.627  105.921 1.00 75.80  ?  317 SER B OG  1 
ATOM   2473  N N   . VAL A 1 302 ? -11.313 21.417  106.023 1.00 70.88  ?  318 VAL B N   1 
ATOM   2474  C CA  . VAL A 1 302 ? -11.218 22.197  107.288 1.00 73.24  ?  318 VAL B CA  1 
ATOM   2475  C C   . VAL A 1 302 ? -11.989 23.512  107.161 1.00 73.15  ?  318 VAL B C   1 
ATOM   2476  O O   . VAL A 1 302 ? -11.664 24.447  107.904 1.00 76.05  ?  318 VAL B O   1 
ATOM   2477  C CB  . VAL A 1 302 ? -9.743  22.414  107.672 1.00 70.94  ?  318 VAL B CB  1 
ATOM   2478  C CG1 . VAL A 1 302 ? -9.028  21.091  107.892 1.00 69.27  ?  318 VAL B CG1 1 
ATOM   2479  C CG2 . VAL A 1 302 ? -9.004  23.252  106.644 1.00 65.73  ?  318 VAL B CG2 1 
ATOM   2480  N N   . GLY A 1 303 ? -12.991 23.577  106.285 1.00 70.17  ?  319 GLY B N   1 
ATOM   2481  C CA  . GLY A 1 303 ? -13.804 24.773  106.191 1.00 70.71  ?  319 GLY B CA  1 
ATOM   2482  C C   . GLY A 1 303 ? -13.195 25.885  105.376 1.00 72.21  ?  319 GLY B C   1 
ATOM   2483  O O   . GLY A 1 303 ? -13.623 27.043  105.487 1.00 73.34  ?  319 GLY B O   1 
ATOM   2484  N N   . LEU A 1 304 ? -12.226 25.584  104.583 1.00 68.24  ?  320 LEU B N   1 
ATOM   2485  C CA  . LEU A 1 304 ? -11.618 26.571  103.726 1.00 69.89  ?  320 LEU B CA  1 
ATOM   2486  C C   . LEU A 1 304 ? -12.042 26.317  102.295 1.00 70.24  ?  320 LEU B C   1 
ATOM   2487  O O   . LEU A 1 304 ? -12.271 25.163  101.920 1.00 73.20  ?  320 LEU B O   1 
ATOM   2488  C CB  . LEU A 1 304 ? -10.095 26.495  103.829 1.00 70.85  ?  320 LEU B CB  1 
ATOM   2489  C CG  . LEU A 1 304 ? -9.506  27.014  105.132 1.00 66.07  ?  320 LEU B CG  1 
ATOM   2490  C CD1 . LEU A 1 304 ? -8.070  26.601  105.178 1.00 62.67  ?  320 LEU B CD1 1 
ATOM   2491  C CD2 . LEU A 1 304 ? -9.626  28.506  105.149 1.00 64.74  ?  320 LEU B CD2 1 
ATOM   2492  N N   . PRO A 1 305 ? -12.156 27.362  101.476 1.00 70.76  ?  321 PRO B N   1 
ATOM   2493  C CA  . PRO A 1 305 ? -12.640 27.176  100.112 1.00 76.10  ?  321 PRO B CA  1 
ATOM   2494  C C   . PRO A 1 305 ? -11.676 26.475  99.170  1.00 79.55  ?  321 PRO B C   1 
ATOM   2495  O O   . PRO A 1 305 ? -10.455 26.419  99.354  1.00 73.79  ?  321 PRO B O   1 
ATOM   2496  C CB  . PRO A 1 305 ? -12.923 28.607  99.651  1.00 71.55  ?  321 PRO B CB  1 
ATOM   2497  C CG  . PRO A 1 305 ? -11.965 29.415  100.356 1.00 63.75  ?  321 PRO B CG  1 
ATOM   2498  C CD  . PRO A 1 305 ? -11.912 28.789  101.748 1.00 68.94  ?  321 PRO B CD  1 
ATOM   2499  N N   . ASN A 1 306 ? -12.292 25.929  98.133  1.00 79.66  ?  322 ASN B N   1 
ATOM   2500  C CA  . ASN A 1 306 ? -11.584 25.252  97.075  1.00 84.45  ?  322 ASN B CA  1 
ATOM   2501  C C   . ASN A 1 306 ? -11.073 26.260  96.055  1.00 81.63  ?  322 ASN B C   1 
ATOM   2502  O O   . ASN A 1 306 ? -11.641 27.340  95.877  1.00 80.74  ?  322 ASN B O   1 
ATOM   2503  C CB  . ASN A 1 306 ? -12.492 24.210  96.426  1.00 89.28  ?  322 ASN B CB  1 
ATOM   2504  C CG  . ASN A 1 306 ? -13.945 24.672  96.307  1.00 100.38 ?  322 ASN B CG  1 
ATOM   2505  O OD1 . ASN A 1 306 ? -14.262 25.841  96.549  1.00 98.15  ?  322 ASN B OD1 1 
ATOM   2506  N ND2 . ASN A 1 306 ? -14.840 23.729  95.939  1.00 107.28 ?  322 ASN B ND2 1 
ATOM   2507  N N   . MET A 1 307 ? -9.965  25.898  95.426  1.00 83.49  ?  323 MET B N   1 
ATOM   2508  C CA  . MET A 1 307 ? -9.245  26.783  94.531  1.00 80.98  ?  323 MET B CA  1 
ATOM   2509  C C   . MET A 1 307 ? -10.198 27.405  93.517  1.00 86.60  ?  323 MET B C   1 
ATOM   2510  O O   . MET A 1 307 ? -11.193 26.788  93.114  1.00 89.93  ?  323 MET B O   1 
ATOM   2511  C CB  . MET A 1 307 ? -8.187  25.989  93.783  1.00 84.32  ?  323 MET B CB  1 
ATOM   2512  C CG  . MET A 1 307 ? -7.131  25.304  94.612  1.00 84.60  ?  323 MET B CG  1 
ATOM   2513  S SD  . MET A 1 307 ? -6.034  26.420  95.466  1.00 84.39  ?  323 MET B SD  1 
ATOM   2514  C CE  . MET A 1 307 ? -6.791  26.447  97.085  1.00 81.06  ?  323 MET B CE  1 
ATOM   2515  N N   . THR A 1 308 ? -9.878  28.619  93.075  1.00 88.00  ?  324 THR B N   1 
ATOM   2516  C CA  . THR A 1 308 ? -10.720 29.264  92.072  1.00 87.60  ?  324 THR B CA  1 
ATOM   2517  C C   . THR A 1 308 ? -10.674 28.481  90.773  1.00 90.07  ?  324 THR B C   1 
ATOM   2518  O O   . THR A 1 308 ? -9.688  27.805  90.465  1.00 88.91  ?  324 THR B O   1 
ATOM   2519  C CB  . THR A 1 308 ? -10.250 30.678  91.763  1.00 87.40  ?  324 THR B CB  1 
ATOM   2520  O OG1 . THR A 1 308 ? -9.019  30.628  91.037  1.00 86.51  ?  324 THR B OG1 1 
ATOM   2521  C CG2 . THR A 1 308 ? -9.954  31.394  93.034  1.00 82.67  ?  324 THR B CG2 1 
ATOM   2522  N N   . GLN A 1 309 ? -11.745 28.591  89.988  1.00 89.61  ?  325 GLN B N   1 
ATOM   2523  C CA  . GLN A 1 309 ? -11.691 28.078  88.625  1.00 89.45  ?  325 GLN B CA  1 
ATOM   2524  C C   . GLN A 1 309 ? -10.491 28.686  87.900  1.00 88.55  ?  325 GLN B C   1 
ATOM   2525  O O   . GLN A 1 309 ? -9.720  27.990  87.228  1.00 87.85  ?  325 GLN B O   1 
ATOM   2526  C CB  . GLN A 1 309 ? -12.992 28.397  87.894  1.00 87.10  ?  325 GLN B CB  1 
ATOM   2527  C CG  . GLN A 1 309 ? -13.080 27.921  86.465  1.00 92.50  ?  325 GLN B CG  1 
ATOM   2528  C CD  . GLN A 1 309 ? -14.383 28.392  85.818  1.00 104.78 ?  325 GLN B CD  1 
ATOM   2529  O OE1 . GLN A 1 309 ? -15.208 29.046  86.478  1.00 105.83 ?  325 GLN B OE1 1 
ATOM   2530  N NE2 . GLN A 1 309 ? -14.557 28.105  84.521  1.00 103.55 ?  325 GLN B NE2 1 
ATOM   2531  N N   . GLY A 1 310 ? -10.308 29.992  88.067  1.00 88.19  ?  326 GLY B N   1 
ATOM   2532  C CA  . GLY A 1 310 ? -9.098  30.672  87.666  1.00 85.08  ?  326 GLY B CA  1 
ATOM   2533  C C   . GLY A 1 310 ? -7.875  29.895  88.077  1.00 86.03  ?  326 GLY B C   1 
ATOM   2534  O O   . GLY A 1 310 ? -7.011  29.658  87.235  1.00 88.39  ?  326 GLY B O   1 
ATOM   2535  N N   . PHE A 1 311 ? -7.795  29.461  89.347  1.00 87.36  ?  327 PHE B N   1 
ATOM   2536  C CA  . PHE A 1 311 ? -6.611  28.739  89.823  1.00 88.53  ?  327 PHE B CA  1 
ATOM   2537  C C   . PHE A 1 311 ? -6.280  27.538  88.958  1.00 86.89  ?  327 PHE B C   1 
ATOM   2538  O O   . PHE A 1 311 ? -5.105  27.286  88.658  1.00 82.81  ?  327 PHE B O   1 
ATOM   2539  C CB  . PHE A 1 311 ? -6.771  28.252  91.263  1.00 81.44  ?  327 PHE B CB  1 
ATOM   2540  C CG  . PHE A 1 311 ? -5.685  27.292  91.681  1.00 77.26  ?  327 PHE B CG  1 
ATOM   2541  C CD1 . PHE A 1 311 ? -5.817  25.929  91.468  1.00 79.38  ?  327 PHE B CD1 1 
ATOM   2542  C CD2 . PHE A 1 311 ? -4.539  27.742  92.268  1.00 81.98  ?  327 PHE B CD2 1 
ATOM   2543  C CE1 . PHE A 1 311 ? -4.846  25.048  91.836  1.00 81.54  ?  327 PHE B CE1 1 
ATOM   2544  C CE2 . PHE A 1 311 ? -3.542  26.848  92.653  1.00 83.77  ?  327 PHE B CE2 1 
ATOM   2545  C CZ  . PHE A 1 311 ? -3.700  25.499  92.434  1.00 82.88  ?  327 PHE B CZ  1 
ATOM   2546  N N   . TRP A 1 312 ? -7.293  26.719  88.643  1.00 87.45  ?  328 TRP B N   1 
ATOM   2547  C CA  . TRP A 1 312 ? -7.026  25.508  87.875  1.00 85.24  ?  328 TRP B CA  1 
ATOM   2548  C C   . TRP A 1 312 ? -6.711  25.847  86.431  1.00 88.23  ?  328 TRP B C   1 
ATOM   2549  O O   . TRP A 1 312 ? -5.708  25.368  85.884  1.00 88.02  ?  328 TRP B O   1 
ATOM   2550  C CB  . TRP A 1 312 ? -8.201  24.545  87.949  1.00 82.27  ?  328 TRP B CB  1 
ATOM   2551  C CG  . TRP A 1 312 ? -8.467  23.988  89.293  1.00 85.47  ?  328 TRP B CG  1 
ATOM   2552  C CD1 . TRP A 1 312 ? -9.523  24.287  90.119  1.00 88.59  ?  328 TRP B CD1 1 
ATOM   2553  C CD2 . TRP A 1 312 ? -7.674  23.014  89.987  1.00 86.69  ?  328 TRP B CD2 1 
ATOM   2554  N NE1 . TRP A 1 312 ? -9.430  23.557  91.288  1.00 92.82  ?  328 TRP B NE1 1 
ATOM   2555  C CE2 . TRP A 1 312 ? -8.303  22.772  91.232  1.00 90.24  ?  328 TRP B CE2 1 
ATOM   2556  C CE3 . TRP A 1 312 ? -6.494  22.330  89.681  1.00 84.33  ?  328 TRP B CE3 1 
ATOM   2557  C CZ2 . TRP A 1 312 ? -7.786  21.877  92.168  1.00 87.77  ?  328 TRP B CZ2 1 
ATOM   2558  C CZ3 . TRP A 1 312 ? -5.984  21.440  90.609  1.00 86.64  ?  328 TRP B CZ3 1 
ATOM   2559  C CH2 . TRP A 1 312 ? -6.631  21.219  91.836  1.00 89.30  ?  328 TRP B CH2 1 
ATOM   2560  N N   . GLU A 1 313 ? -7.539  26.702  85.813  1.00 86.18  ?  329 GLU B N   1 
ATOM   2561  C CA  . GLU A 1 313 ? -7.345  27.078  84.413  1.00 85.72  ?  329 GLU B CA  1 
ATOM   2562  C C   . GLU A 1 313 ? -5.963  27.673  84.156  1.00 85.75  ?  329 GLU B C   1 
ATOM   2563  O O   . GLU A 1 313 ? -5.388  27.442  83.087  1.00 83.25  ?  329 GLU B O   1 
ATOM   2564  C CB  . GLU A 1 313 ? -8.410  28.083  83.969  1.00 87.63  ?  329 GLU B CB  1 
ATOM   2565  C CG  . GLU A 1 313 ? -9.524  27.473  83.145  1.00 94.81  ?  329 GLU B CG  1 
ATOM   2566  C CD  . GLU A 1 313 ? -10.850 28.188  83.297  1.00 97.96  ?  329 GLU B CD  1 
ATOM   2567  O OE1 . GLU A 1 313 ? -10.852 29.369  83.712  1.00 95.93  ?  329 GLU B OE1 1 
ATOM   2568  O OE2 . GLU A 1 313 ? -11.893 27.574  82.986  1.00 104.40 -1 329 GLU B OE2 1 
ATOM   2569  N N   . ASN A 1 314 ? -5.410  28.434  85.117  1.00 88.10  ?  330 ASN B N   1 
ATOM   2570  C CA  . ASN A 1 314 ? -4.239  29.268  84.867  1.00 83.79  ?  330 ASN B CA  1 
ATOM   2571  C C   . ASN A 1 314 ? -2.956  28.785  85.512  1.00 82.29  ?  330 ASN B C   1 
ATOM   2572  O O   . ASN A 1 314 ? -1.886  29.219  85.078  1.00 84.85  ?  330 ASN B O   1 
ATOM   2573  C CB  . ASN A 1 314 ? -4.487  30.715  85.327  1.00 82.24  ?  330 ASN B CB  1 
ATOM   2574  C CG  . ASN A 1 314 ? -5.664  31.360  84.613  1.00 84.21  ?  330 ASN B CG  1 
ATOM   2575  O OD1 . ASN A 1 314 ? -5.796  31.234  83.395  1.00 83.69  ?  330 ASN B OD1 1 
ATOM   2576  N ND2 . ASN A 1 314 ? -6.521  32.059  85.363  1.00 84.37  ?  330 ASN B ND2 1 
ATOM   2577  N N   . SER A 1 315 ? -3.022  27.930  86.532  1.00 84.38  ?  331 SER B N   1 
ATOM   2578  C CA  . SER A 1 315 ? -1.798  27.482  87.194  1.00 84.05  ?  331 SER B CA  1 
ATOM   2579  C C   . SER A 1 315 ? -0.943  26.656  86.233  1.00 85.00  ?  331 SER B C   1 
ATOM   2580  O O   . SER A 1 315 ? -1.413  26.162  85.198  1.00 87.53  ?  331 SER B O   1 
ATOM   2581  C CB  . SER A 1 315 ? -2.111  26.638  88.439  1.00 82.96  ?  331 SER B CB  1 
ATOM   2582  O OG  . SER A 1 315 ? -2.827  27.347  89.434  1.00 80.08  ?  331 SER B OG  1 
ATOM   2583  N N   . MET A 1 316 ? 0.333   26.500  86.594  1.00 85.31  ?  332 MET B N   1 
ATOM   2584  C CA  . MET A 1 316 ? 1.255   25.605  85.897  1.00 90.08  ?  332 MET B CA  1 
ATOM   2585  C C   . MET A 1 316 ? 1.707   24.512  86.853  1.00 90.70  ?  332 MET B C   1 
ATOM   2586  O O   . MET A 1 316 ? 2.639   24.708  87.638  1.00 89.25  ?  332 MET B O   1 
ATOM   2587  C CB  . MET A 1 316 ? 2.456   26.356  85.353  1.00 91.53  ?  332 MET B CB  1 
ATOM   2588  C CG  . MET A 1 316 ? 3.540   25.394  84.966  1.00 96.16  ?  332 MET B CG  1 
ATOM   2589  S SD  . MET A 1 316 ? 4.800   26.173  83.985  1.00 103.80 ?  332 MET B SD  1 
ATOM   2590  C CE  . MET A 1 316 ? 3.885   26.535  82.491  1.00 111.06 ?  332 MET B CE  1 
ATOM   2591  N N   . LEU A 1 317 ? 1.067   23.352  86.762  1.00 95.32  ?  333 LEU B N   1 
ATOM   2592  C CA  . LEU A 1 317 ? 1.253   22.308  87.761  1.00 99.57  ?  333 LEU B CA  1 
ATOM   2593  C C   . LEU A 1 317 ? 2.095   21.124  87.286  1.00 109.85 ?  333 LEU B C   1 
ATOM   2594  O O   . LEU A 1 317 ? 2.370   20.228  88.093  1.00 113.34 ?  333 LEU B O   1 
ATOM   2595  C CB  . LEU A 1 317 ? -0.107  21.780  88.257  1.00 88.30  ?  333 LEU B CB  1 
ATOM   2596  C CG  . LEU A 1 317 ? -1.182  22.758  88.714  1.00 82.74  ?  333 LEU B CG  1 
ATOM   2597  C CD1 . LEU A 1 317 ? -2.424  22.012  89.188  1.00 80.69  ?  333 LEU B CD1 1 
ATOM   2598  C CD2 . LEU A 1 317 ? -0.663  23.702  89.758  1.00 88.00  ?  333 LEU B CD2 1 
ATOM   2599  N N   . THR A 1 318 ? 2.498   21.071  86.013  1.00 111.87 ?  334 THR B N   1 
ATOM   2600  C CA  . THR A 1 318 ? 3.427   20.049  85.551  1.00 117.04 ?  334 THR B CA  1 
ATOM   2601  C C   . THR A 1 318 ? 4.532   20.741  84.788  1.00 128.49 ?  334 THR B C   1 
ATOM   2602  O O   . THR A 1 318 ? 4.329   21.831  84.246  1.00 128.94 ?  334 THR B O   1 
ATOM   2603  C CB  . THR A 1 318 ? 2.788   19.022  84.627  1.00 113.79 ?  334 THR B CB  1 
ATOM   2604  O OG1 . THR A 1 318 ? 2.234   19.701  83.501  1.00 122.00 ?  334 THR B OG1 1 
ATOM   2605  C CG2 . THR A 1 318 ? 1.684   18.275  85.332  1.00 112.16 ?  334 THR B CG2 1 
ATOM   2606  N N   . ASP A 1 319 ? 5.696   20.109  84.734  1.00 138.01 ?  335 ASP B N   1 
ATOM   2607  C CA  . ASP A 1 319 ? 6.718   20.612  83.836  1.00 146.66 ?  335 ASP B CA  1 
ATOM   2608  C C   . ASP A 1 319 ? 6.119   20.674  82.435  1.00 154.29 ?  335 ASP B C   1 
ATOM   2609  O O   . ASP A 1 319 ? 5.461   19.714  82.006  1.00 155.90 ?  335 ASP B O   1 
ATOM   2610  C CB  . ASP A 1 319 ? 7.968   19.728  83.833  1.00 154.30 ?  335 ASP B CB  1 
ATOM   2611  C CG  . ASP A 1 319 ? 9.174   20.416  83.177  1.00 158.94 ?  335 ASP B CG  1 
ATOM   2612  O OD1 . ASP A 1 319 ? 9.033   21.005  82.078  1.00 156.52 ?  335 ASP B OD1 1 
ATOM   2613  O OD2 . ASP A 1 319 ? 10.279  20.336  83.754  1.00 160.25 -1 335 ASP B OD2 1 
ATOM   2614  N N   . PRO A 1 320 ? 6.271   21.789  81.718  1.00 166.49 ?  336 PRO B N   1 
ATOM   2615  C CA  . PRO A 1 320 ? 5.575   21.988  80.439  1.00 175.59 ?  336 PRO B CA  1 
ATOM   2616  C C   . PRO A 1 320 ? 6.306   21.373  79.231  1.00 179.84 ?  336 PRO B C   1 
ATOM   2617  O O   . PRO A 1 320 ? 6.565   22.036  78.236  1.00 180.13 ?  336 PRO B O   1 
ATOM   2618  C CB  . PRO A 1 320 ? 5.507   23.514  80.337  1.00 170.88 ?  336 PRO B CB  1 
ATOM   2619  C CG  . PRO A 1 320 ? 6.753   23.954  81.024  1.00 165.36 ?  336 PRO B CG  1 
ATOM   2620  C CD  . PRO A 1 320 ? 6.910   23.027  82.190  1.00 161.06 ?  336 PRO B CD  1 
ATOM   2621  N N   . GLY A 1 321 ? 6.697   20.104  79.358  1.00 167.13 ?  337 GLY B N   1 
ATOM   2622  C CA  . GLY A 1 321 ? 7.386   19.432  78.244  1.00 155.79 ?  337 GLY B CA  1 
ATOM   2623  C C   . GLY A 1 321 ? 8.745   20.038  77.946  1.00 158.06 ?  337 GLY B C   1 
ATOM   2624  O O   . GLY A 1 321 ? 9.053   21.118  78.483  1.00 158.30 ?  337 GLY B O   1 
ATOM   2625  N N   . ASN A 1 322 ? 9.536   19.365  77.111  1.00 156.54 ?  338 ASN B N   1 
ATOM   2626  C CA  . ASN A 1 322 ? 10.910  19.839  76.770  1.00 161.54 ?  338 ASN B CA  1 
ATOM   2627  C C   . ASN A 1 322 ? 10.804  20.676  75.486  1.00 161.09 ?  338 ASN B C   1 
ATOM   2628  O O   . ASN A 1 322 ? 11.832  20.848  74.792  1.00 151.65 ?  338 ASN B O   1 
ATOM   2629  C CB  . ASN A 1 322 ? 11.861  18.628  76.795  1.00 160.06 ?  338 ASN B CB  1 
ATOM   2630  C CG  . ASN A 1 322 ? 13.050  18.676  75.865  1.00 157.46 ?  338 ASN B CG  1 
ATOM   2631  O OD1 . ASN A 1 322 ? 14.052  19.316  76.168  1.00 155.02 ?  338 ASN B OD1 1 
ATOM   2632  N ND2 . ASN A 1 322 ? 12.956  17.949  74.767  1.00 156.42 ?  338 ASN B ND2 1 
ATOM   2633  N N   . VAL A 1 323 ? 9.602   21.192  75.195  1.00 168.12 ?  339 VAL B N   1 
ATOM   2634  C CA  . VAL A 1 323 ? 9.352   21.990  73.958  1.00 172.44 ?  339 VAL B CA  1 
ATOM   2635  C C   . VAL A 1 323 ? 9.286   23.471  74.344  1.00 172.81 ?  339 VAL B C   1 
ATOM   2636  O O   . VAL A 1 323 ? 8.997   24.294  73.449  1.00 164.05 ?  339 VAL B O   1 
ATOM   2637  C CB  . VAL A 1 323 ? 8.056   21.525  73.263  1.00 172.09 ?  339 VAL B CB  1 
ATOM   2638  C CG1 . VAL A 1 323 ? 8.216   21.388  71.756  1.00 167.10 ?  339 VAL B CG1 1 
ATOM   2639  C CG2 . VAL A 1 323 ? 7.543   20.234  73.876  1.00 168.80 ?  339 VAL B CG2 1 
ATOM   2640  N N   . GLN A 1 324 ? 9.504   23.787  75.622  1.00 193.09 ?  340 GLN B N   1 
ATOM   2641  C CA  . GLN A 1 324 ? 9.504   25.186  76.136  1.00 185.36 ?  340 GLN B CA  1 
ATOM   2642  C C   . GLN A 1 324 ? 10.134  25.094  77.523  1.00 185.84 ?  340 GLN B C   1 
ATOM   2643  O O   . GLN A 1 324 ? 10.008  24.016  78.139  1.00 188.41 ?  340 GLN B O   1 
ATOM   2644  C CB  . GLN A 1 324 ? 8.096   25.769  76.122  1.00 175.83 ?  340 GLN B CB  1 
ATOM   2645  C CG  . GLN A 1 324 ? 7.438   25.836  77.483  1.00 184.68 ?  340 GLN B CG  1 
ATOM   2646  C CD  . GLN A 1 324 ? 6.127   26.570  77.380  1.00 174.26 ?  340 GLN B CD  1 
ATOM   2647  O OE1 . GLN A 1 324 ? 6.047   27.772  77.610  1.00 158.60 ?  340 GLN B OE1 1 
ATOM   2648  N NE2 . GLN A 1 324 ? 5.084   25.852  77.006  1.00 174.95 ?  340 GLN B NE2 1 
ATOM   2649  N N   . LYS A 1 325 ? 10.774  26.154  78.013  1.00 152.90 ?  341 LYS B N   1 
ATOM   2650  C CA  . LYS A 1 325 ? 11.514  25.984  79.259  1.00 140.66 ?  341 LYS B CA  1 
ATOM   2651  C C   . LYS A 1 325 ? 11.006  26.930  80.345  1.00 135.56 ?  341 LYS B C   1 
ATOM   2652  O O   . LYS A 1 325 ? 10.663  28.078  80.063  1.00 131.53 ?  341 LYS B O   1 
ATOM   2653  C CB  . LYS A 1 325 ? 13.021  26.181  79.035  1.00 133.56 ?  341 LYS B CB  1 
ATOM   2654  C CG  . LYS A 1 325 ? 13.681  25.207  78.038  1.00 132.27 ?  341 LYS B CG  1 
ATOM   2655  C CD  . LYS A 1 325 ? 13.172  23.783  78.244  1.00 136.73 ?  341 LYS B CD  1 
ATOM   2656  C CE  . LYS A 1 325 ? 14.148  22.739  77.761  1.00 123.76 ?  341 LYS B CE  1 
ATOM   2657  N NZ  . LYS A 1 325 ? 15.281  22.676  78.707  1.00 112.41 ?  341 LYS B NZ  1 
ATOM   2658  N N   . ALA A 1 326 ? 11.028  26.507  81.624  1.00 134.41 ?  342 ALA B N   1 
ATOM   2659  C CA  . ALA A 1 326 ? 10.484  27.364  82.711  1.00 125.67 ?  342 ALA B CA  1 
ATOM   2660  C C   . ALA A 1 326 ? 11.297  27.218  84.002  1.00 125.27 ?  342 ALA B C   1 
ATOM   2661  O O   . ALA A 1 326 ? 12.007  26.213  84.157  1.00 131.28 ?  342 ALA B O   1 
ATOM   2662  C CB  . ALA A 1 326 ? 9.032   27.035  82.960  1.00 127.41 ?  342 ALA B CB  1 
ATOM   2663  N N   . VAL A 1 327 ? 11.225  28.214  84.887  1.00 121.60 ?  343 VAL B N   1 
ATOM   2664  C CA  . VAL A 1 327 ? 11.924  28.076  86.190  1.00 121.29 ?  343 VAL B CA  1 
ATOM   2665  C C   . VAL A 1 327 ? 11.116  27.110  87.045  1.00 125.68 ?  343 VAL B C   1 
ATOM   2666  O O   . VAL A 1 327 ? 9.921   27.395  87.293  1.00 119.26 ?  343 VAL B O   1 
ATOM   2667  C CB  . VAL A 1 327 ? 12.085  29.440  86.874  1.00 108.74 ?  343 VAL B CB  1 
ATOM   2668  C CG1 . VAL A 1 327 ? 13.279  29.422  87.820  1.00 103.57 ?  343 VAL B CG1 1 
ATOM   2669  C CG2 . VAL A 1 327 ? 12.227  30.558  85.855  1.00 104.25 ?  343 VAL B CG2 1 
ATOM   2670  N N   . CYS A 1 328 ? 11.714  25.971  87.406  1.00 126.70 ?  344 CYS B N   1 
ATOM   2671  C CA  . CYS A 1 328 ? 10.980  24.934  88.176  1.00 123.73 ?  344 CYS B CA  1 
ATOM   2672  C C   . CYS A 1 328 ? 11.272  25.187  89.654  1.00 120.13 ?  344 CYS B C   1 
ATOM   2673  O O   . CYS A 1 328 ? 12.243  24.600  90.174  1.00 119.72 ?  344 CYS B O   1 
ATOM   2674  C CB  . CYS A 1 328 ? 11.369  23.508  87.794  1.00 129.88 ?  344 CYS B CB  1 
ATOM   2675  S SG  . CYS A 1 328 ? 10.677  22.924  86.222  1.00 181.83 ?  344 CYS B SG  1 
ATOM   2676  N N   . HIS A 1 329 ? 10.495  26.057  90.292  1.00 105.16 ?  345 HIS B N   1 
ATOM   2677  C CA  . HIS A 1 329 ? 10.655  26.240  91.749  1.00 99.65  ?  345 HIS B CA  1 
ATOM   2678  C C   . HIS A 1 329 ? 9.280   26.582  92.282  1.00 96.39  ?  345 HIS B C   1 
ATOM   2679  O O   . HIS A 1 329 ? 8.745   27.617  91.866  1.00 96.82  ?  345 HIS B O   1 
ATOM   2680  C CB  . HIS A 1 329 ? 11.664  27.335  92.090  1.00 100.83 ?  345 HIS B CB  1 
ATOM   2681  C CG  . HIS A 1 329 ? 11.643  27.703  93.533  1.00 103.49 ?  345 HIS B CG  1 
ATOM   2682  N ND1 . HIS A 1 329 ? 10.782  28.653  94.045  1.00 103.19 ?  345 HIS B ND1 1 
ATOM   2683  C CD2 . HIS A 1 329 ? 12.389  27.272  94.576  1.00 101.18 ?  345 HIS B CD2 1 
ATOM   2684  C CE1 . HIS A 1 329 ? 10.990  28.784  95.340  1.00 99.16  ?  345 HIS B CE1 1 
ATOM   2685  N NE2 . HIS A 1 329 ? 11.971  27.949  95.690  1.00 98.84  ?  345 HIS B NE2 1 
ATOM   2686  N N   . PRO A 1 330 ? 8.674   25.755  93.143  1.00 97.79  ?  346 PRO B N   1 
ATOM   2687  C CA  . PRO A 1 330 ? 7.322   26.001  93.593  1.00 95.84  ?  346 PRO B CA  1 
ATOM   2688  C C   . PRO A 1 330 ? 7.165   27.486  93.930  1.00 94.83  ?  346 PRO B C   1 
ATOM   2689  O O   . PRO A 1 330 ? 7.968   27.986  94.670  1.00 93.91  ?  346 PRO B O   1 
ATOM   2690  C CB  . PRO A 1 330 ? 7.170   25.145  94.851  1.00 92.45  ?  346 PRO B CB  1 
ATOM   2691  C CG  . PRO A 1 330 ? 8.489   24.405  95.013  1.00 93.22  ?  346 PRO B CG  1 
ATOM   2692  C CD  . PRO A 1 330 ? 9.241   24.543  93.711  1.00 96.96  ?  346 PRO B CD  1 
ATOM   2693  N N   . THR A 1 331 ? 6.169   28.135  93.334  1.00 86.06  ?  347 THR B N   1 
ATOM   2694  C CA  . THR A 1 331 ? 5.903   29.565  93.628  1.00 83.76  ?  347 THR B CA  1 
ATOM   2695  C C   . THR A 1 331 ? 4.390   29.755  93.792  1.00 81.90  ?  347 THR B C   1 
ATOM   2696  O O   . THR A 1 331 ? 3.653   29.375  92.863  1.00 84.49  ?  347 THR B O   1 
ATOM   2697  C CB  . THR A 1 331 ? 6.484   30.474  92.542  1.00 84.56  ?  347 THR B CB  1 
ATOM   2698  O OG1 . THR A 1 331 ? 6.429   29.854  91.254  1.00 86.02  ?  347 THR B OG1 1 
ATOM   2699  C CG2 . THR A 1 331 ? 7.912   30.874  92.833  1.00 89.10  ?  347 THR B CG2 1 
ATOM   2700  N N   . ALA A 1 332 ? 3.944   30.344  94.907  1.00 82.39  ?  348 ALA B N   1 
ATOM   2701  C CA  . ALA A 1 332 ? 2.503   30.582  95.071  1.00 78.81  ?  348 ALA B CA  1 
ATOM   2702  C C   . ALA A 1 332 ? 2.152   32.038  94.764  1.00 77.75  ?  348 ALA B C   1 
ATOM   2703  O O   . ALA A 1 332 ? 2.265   32.926  95.629  1.00 73.27  ?  348 ALA B O   1 
ATOM   2704  C CB  . ALA A 1 332 ? 2.032   30.202  96.467  1.00 75.36  ?  348 ALA B CB  1 
ATOM   2705  N N   . TRP A 1 333 ? 1.649   32.241  93.548  1.00 73.16  ?  349 TRP B N   1 
ATOM   2706  C CA  . TRP A 1 333 ? 1.462   33.557  92.967  1.00 70.09  ?  349 TRP B CA  1 
ATOM   2707  C C   . TRP A 1 333 ? 0.111   34.122  93.356  1.00 70.80  ?  349 TRP B C   1 
ATOM   2708  O O   . TRP A 1 333 ? -0.917  33.511  93.063  1.00 73.86  ?  349 TRP B O   1 
ATOM   2709  C CB  . TRP A 1 333 ? 1.550   33.466  91.454  1.00 71.35  ?  349 TRP B CB  1 
ATOM   2710  C CG  . TRP A 1 333 ? 2.892   33.166  91.009  1.00 72.33  ?  349 TRP B CG  1 
ATOM   2711  C CD1 . TRP A 1 333 ? 3.628   32.065  91.302  1.00 77.09  ?  349 TRP B CD1 1 
ATOM   2712  C CD2 . TRP A 1 333 ? 3.723   34.017  90.246  1.00 70.48  ?  349 TRP B CD2 1 
ATOM   2713  N NE1 . TRP A 1 333 ? 4.868   32.162  90.729  1.00 77.43  ?  349 TRP B NE1 1 
ATOM   2714  C CE2 . TRP A 1 333 ? 4.950   33.361  90.078  1.00 73.37  ?  349 TRP B CE2 1 
ATOM   2715  C CE3 . TRP A 1 333 ? 3.542   35.272  89.672  1.00 73.70  ?  349 TRP B CE3 1 
ATOM   2716  C CZ2 . TRP A 1 333 ? 5.991   33.919  89.364  1.00 79.88  ?  349 TRP B CZ2 1 
ATOM   2717  C CZ3 . TRP A 1 333 ? 4.570   35.824  88.957  1.00 77.56  ?  349 TRP B CZ3 1 
ATOM   2718  C CH2 . TRP A 1 333 ? 5.780   35.151  88.806  1.00 82.39  ?  349 TRP B CH2 1 
ATOM   2719  N N   . ASP A 1 334 ? 0.114   35.298  93.965  1.00 61.42  ?  350 ASP B N   1 
ATOM   2720  C CA  . ASP A 1 334 ? -1.090  36.078  94.213  1.00 60.76  ?  350 ASP B CA  1 
ATOM   2721  C C   . ASP A 1 334 ? -1.066  37.308  93.310  1.00 66.69  ?  350 ASP B C   1 
ATOM   2722  O O   . ASP A 1 334 ? -0.611  38.375  93.728  1.00 69.60  ?  350 ASP B O   1 
ATOM   2723  C CB  . ASP A 1 334 ? -1.142  36.434  95.660  1.00 63.43  ?  350 ASP B CB  1 
ATOM   2724  C CG  . ASP A 1 334 ? -2.329  37.279  96.027  1.00 72.93  ?  350 ASP B CG  1 
ATOM   2725  O OD1 . ASP A 1 334 ? -3.128  37.683  95.141  1.00 74.63  ?  350 ASP B OD1 1 
ATOM   2726  O OD2 . ASP A 1 334 ? -2.454  37.538  97.245  1.00 75.35  -1 350 ASP B OD2 1 
ATOM   2727  N N   . LEU A 1 335 ? -1.609  37.177  92.077  1.00 66.57  ?  351 LEU B N   1 
ATOM   2728  C CA  . LEU A 1 335 ? -1.512  38.260  91.095  1.00 67.91  ?  351 LEU B CA  1 
ATOM   2729  C C   . LEU A 1 335 ? -2.528  39.371  91.341  1.00 69.89  ?  351 LEU B C   1 
ATOM   2730  O O   . LEU A 1 335 ? -2.380  40.470  90.778  1.00 67.65  ?  351 LEU B O   1 
ATOM   2731  C CB  . LEU A 1 335 ? -1.728  37.742  89.672  1.00 65.33  ?  351 LEU B CB  1 
ATOM   2732  C CG  . LEU A 1 335 ? -0.760  36.742  89.048  1.00 65.99  ?  351 LEU B CG  1 
ATOM   2733  C CD1 . LEU A 1 335 ? -1.163  35.331  89.459  1.00 69.87  ?  351 LEU B CD1 1 
ATOM   2734  C CD2 . LEU A 1 335 ? -0.721  36.872  87.553  1.00 69.96  ?  351 LEU B CD2 1 
ATOM   2735  N N   . GLY A 1 336 ? -3.567  39.105  92.142  1.00 65.89  ?  352 GLY B N   1 
ATOM   2736  C CA  . GLY A 1 336 ? -4.585  40.099  92.405  1.00 66.41  ?  352 GLY B CA  1 
ATOM   2737  C C   . GLY A 1 336 ? -5.803  39.974  91.504  1.00 65.45  ?  352 GLY B C   1 
ATOM   2738  O O   . GLY A 1 336 ? -5.866  39.173  90.565  1.00 63.98  ?  352 GLY B O   1 
ATOM   2739  N N   . LYS A 1 337 ? -6.790  40.804  91.828  1.00 70.16  ?  353 LYS B N   1 
ATOM   2740  C CA  . LYS A 1 337 ? -8.109  40.821  91.186  1.00 68.96  ?  353 LYS B CA  1 
ATOM   2741  C C   . LYS A 1 337 ? -8.601  39.403  90.947  1.00 62.07  ?  353 LYS B C   1 
ATOM   2742  O O   . LYS A 1 337 ? -8.950  39.036  89.834  1.00 63.31  ?  353 LYS B O   1 
ATOM   2743  C CB  . LYS A 1 337 ? -8.076  41.618  89.883  1.00 63.12  ?  353 LYS B CB  1 
ATOM   2744  C CG  . LYS A 1 337 ? -7.170  42.796  90.099  1.00 66.59  ?  353 LYS B CG  1 
ATOM   2745  C CD  . LYS A 1 337 ? -7.184  43.934  89.126  1.00 61.22  ?  353 LYS B CD  1 
ATOM   2746  C CE  . LYS A 1 337 ? -8.047  45.028  89.696  1.00 57.60  ?  353 LYS B CE  1 
ATOM   2747  N NZ  . LYS A 1 337 ? -7.800  46.328  89.042  1.00 60.58  ?  353 LYS B NZ  1 
ATOM   2748  N N   . GLY A 1 338 ? -8.543  38.581  91.999  1.00 63.48  ?  354 GLY B N   1 
ATOM   2749  C CA  . GLY A 1 338 ? -9.042  37.218  91.978  1.00 60.26  ?  354 GLY B CA  1 
ATOM   2750  C C   . GLY A 1 338 ? -8.124  36.179  91.373  1.00 59.28  ?  354 GLY B C   1 
ATOM   2751  O O   . GLY A 1 338 ? -8.467  34.988  91.377  1.00 59.59  ?  354 GLY B O   1 
ATOM   2752  N N   . ASP A 1 339 ? -6.977  36.565  90.859  1.00 58.72  ?  355 ASP B N   1 
ATOM   2753  C CA  . ASP A 1 339 ? -6.162  35.633  90.108  1.00 63.58  ?  355 ASP B CA  1 
ATOM   2754  C C   . ASP A 1 339 ? -5.099  35.010  91.024  1.00 69.57  ?  355 ASP B C   1 
ATOM   2755  O O   . ASP A 1 339 ? -4.138  35.681  91.433  1.00 66.39  ?  355 ASP B O   1 
ATOM   2756  C CB  . ASP A 1 339 ? -5.545  36.365  88.936  1.00 64.95  ?  355 ASP B CB  1 
ATOM   2757  C CG  . ASP A 1 339 ? -4.778  35.461  88.056  1.00 66.97  ?  355 ASP B CG  1 
ATOM   2758  O OD1 . ASP A 1 339 ? -4.577  34.278  88.421  1.00 71.54  ?  355 ASP B OD1 1 
ATOM   2759  O OD2 . ASP A 1 339 ? -4.371  35.940  86.984  1.00 65.40  -1 355 ASP B OD2 1 
ATOM   2760  N N   . PHE A 1 340 ? -5.271  33.720  91.336  1.00 71.03  ?  356 PHE B N   1 
ATOM   2761  C CA  . PHE A 1 340 ? -4.323  32.957  92.148  1.00 64.07  ?  356 PHE B CA  1 
ATOM   2762  C C   . PHE A 1 340 ? -3.786  31.763  91.381  1.00 69.10  ?  356 PHE B C   1 
ATOM   2763  O O   . PHE A 1 340 ? -4.560  30.966  90.843  1.00 74.82  ?  356 PHE B O   1 
ATOM   2764  C CB  . PHE A 1 340 ? -4.956  32.458  93.441  1.00 63.38  ?  356 PHE B CB  1 
ATOM   2765  C CG  . PHE A 1 340 ? -5.632  33.519  94.245  1.00 62.03  ?  356 PHE B CG  1 
ATOM   2766  C CD1 . PHE A 1 340 ? -4.938  34.236  95.201  1.00 65.22  ?  356 PHE B CD1 1 
ATOM   2767  C CD2 . PHE A 1 340 ? -6.956  33.785  94.069  1.00 64.54  ?  356 PHE B CD2 1 
ATOM   2768  C CE1 . PHE A 1 340 ? -5.570  35.187  95.948  1.00 65.26  ?  356 PHE B CE1 1 
ATOM   2769  C CE2 . PHE A 1 340 ? -7.577  34.740  94.814  1.00 66.02  ?  356 PHE B CE2 1 
ATOM   2770  C CZ  . PHE A 1 340 ? -6.887  35.443  95.750  1.00 64.38  ?  356 PHE B CZ  1 
ATOM   2771  N N   . ARG A 1 341 ? -2.465  31.620  91.370  1.00 71.27  ?  357 ARG B N   1 
ATOM   2772  C CA  . ARG A 1 341 ? -1.811  30.563  90.618  1.00 72.71  ?  357 ARG B CA  1 
ATOM   2773  C C   . ARG A 1 341 ? -0.755  29.899  91.485  1.00 75.72  ?  357 ARG B C   1 
ATOM   2774  O O   . ARG A 1 341 ? -0.288  30.465  92.476  1.00 75.93  ?  357 ARG B O   1 
ATOM   2775  C CB  . ARG A 1 341 ? -1.164  31.096  89.347  1.00 74.12  ?  357 ARG B CB  1 
ATOM   2776  C CG  . ARG A 1 341 ? -2.144  31.776  88.426  1.00 78.52  ?  357 ARG B CG  1 
ATOM   2777  C CD  . ARG A 1 341 ? -1.479  32.352  87.212  1.00 78.00  ?  357 ARG B CD  1 
ATOM   2778  N NE  . ARG A 1 341 ? -2.341  33.347  86.596  1.00 79.63  ?  357 ARG B NE  1 
ATOM   2779  C CZ  . ARG A 1 341 ? -2.174  33.818  85.370  1.00 81.66  ?  357 ARG B CZ  1 
ATOM   2780  N NH1 . ARG A 1 341 ? -1.286  33.295  84.548  1.00 87.49  ?  357 ARG B NH1 1 
ATOM   2781  N NH2 . ARG A 1 341 ? -2.925  34.833  84.954  1.00 78.84  ?  357 ARG B NH2 1 
ATOM   2782  N N   . ILE A 1 342 ? -0.394  28.673  91.104  1.00 80.66  ?  358 ILE B N   1 
ATOM   2783  C CA  . ILE A 1 342 ? 0.722   27.945  91.699  1.00 79.68  ?  358 ILE B CA  1 
ATOM   2784  C C   . ILE A 1 342 ? 1.597   27.514  90.536  1.00 79.67  ?  358 ILE B C   1 
ATOM   2785  O O   . ILE A 1 342 ? 1.082   27.189  89.462  1.00 83.77  ?  358 ILE B O   1 
ATOM   2786  C CB  . ILE A 1 342 ? 0.266   26.718  92.519  1.00 77.02  ?  358 ILE B CB  1 
ATOM   2787  C CG1 . ILE A 1 342 ? -0.309  27.126  93.877  1.00 75.19  ?  358 ILE B CG1 1 
ATOM   2788  C CG2 . ILE A 1 342 ? 1.456   25.850  92.836  1.00 76.12  ?  358 ILE B CG2 1 
ATOM   2789  C CD1 . ILE A 1 342 ? -0.801  25.945  94.704  1.00 75.68  ?  358 ILE B CD1 1 
ATOM   2790  N N   . LEU A 1 343 ? 2.909   27.550  90.723  1.00 81.53  ?  359 LEU B N   1 
ATOM   2791  C CA  . LEU A 1 343 ? 3.844   27.152  89.678  1.00 86.30  ?  359 LEU B CA  1 
ATOM   2792  C C   . LEU A 1 343 ? 4.815   26.134  90.266  1.00 92.07  ?  359 LEU B C   1 
ATOM   2793  O O   . LEU A 1 343 ? 5.593   26.471  91.163  1.00 93.69  ?  359 LEU B O   1 
ATOM   2794  C CB  . LEU A 1 343 ? 4.570   28.375  89.128  1.00 85.62  ?  359 LEU B CB  1 
ATOM   2795  C CG  . LEU A 1 343 ? 5.352   28.329  87.823  1.00 86.49  ?  359 LEU B CG  1 
ATOM   2796  C CD1 . LEU A 1 343 ? 5.966   29.672  87.634  1.00 88.13  ?  359 LEU B CD1 1 
ATOM   2797  C CD2 . LEU A 1 343 ? 6.449   27.331  87.888  1.00 89.42  ?  359 LEU B CD2 1 
ATOM   2798  N N   . MET A 1 344 ? 4.788   24.904  89.740  1.00 91.23  ?  360 MET B N   1 
ATOM   2799  C CA  . MET A 1 344 ? 5.582   23.793  90.264  1.00 96.98  ?  360 MET B CA  1 
ATOM   2800  C C   . MET A 1 344 ? 5.664   22.681  89.220  1.00 107.58 ?  360 MET B C   1 
ATOM   2801  O O   . MET A 1 344 ? 4.634   22.290  88.666  1.00 110.11 ?  360 MET B O   1 
ATOM   2802  C CB  . MET A 1 344 ? 4.958   23.206  91.528  1.00 93.23  ?  360 MET B CB  1 
ATOM   2803  C CG  . MET A 1 344 ? 5.881   22.203  92.187  1.00 101.29 ?  360 MET B CG  1 
ATOM   2804  S SD  . MET A 1 344 ? 5.177   21.430  93.647  1.00 102.71 ?  360 MET B SD  1 
ATOM   2805  C CE  . MET A 1 344 ? 4.102   22.711  94.230  1.00 92.47  ?  360 MET B CE  1 
ATOM   2806  N N   . CYS A 1 345 ? 6.861   22.134  88.990  1.00 113.26 ?  361 CYS B N   1 
ATOM   2807  C CA  . CYS A 1 345 ? 7.030   21.049  88.019  1.00 119.98 ?  361 CYS B CA  1 
ATOM   2808  C C   . CYS A 1 345 ? 6.874   19.745  88.766  1.00 121.33 ?  361 CYS B C   1 
ATOM   2809  O O   . CYS A 1 345 ? 7.846   19.126  89.190  1.00 124.66 ?  361 CYS B O   1 
ATOM   2810  C CB  . CYS A 1 345 ? 8.377   21.129  87.328  1.00 132.56 ?  361 CYS B CB  1 
ATOM   2811  S SG  . CYS A 1 345 ? 8.672   22.697  86.509  1.00 140.92 ?  361 CYS B SG  1 
ATOM   2812  N N   . THR A 1 346 ? 5.631   19.324  88.912  1.00 125.90 ?  362 THR B N   1 
ATOM   2813  C CA  . THR A 1 346 ? 5.285   18.291  89.870  1.00 130.32 ?  362 THR B CA  1 
ATOM   2814  C C   . THR A 1 346 ? 5.745   16.928  89.379  1.00 129.17 ?  362 THR B C   1 
ATOM   2815  O O   . THR A 1 346 ? 5.616   16.608  88.195  1.00 131.84 ?  362 THR B O   1 
ATOM   2816  C CB  . THR A 1 346 ? 3.774   18.271  90.091  1.00 129.65 ?  362 THR B CB  1 
ATOM   2817  O OG1 . THR A 1 346 ? 3.319   19.596  90.378  1.00 129.19 ?  362 THR B OG1 1 
ATOM   2818  C CG2 . THR A 1 346 ? 3.433   17.385  91.276  1.00 126.94 ?  362 THR B CG2 1 
ATOM   2819  N N   . LYS A 1 347 ? 6.285   16.128  90.290  1.00 125.78 ?  363 LYS B N   1 
ATOM   2820  C CA  . LYS A 1 347 ? 6.584   14.724  90.051  1.00 125.16 ?  363 LYS B CA  1 
ATOM   2821  C C   . LYS A 1 347 ? 5.717   13.888  90.989  1.00 124.25 ?  363 LYS B C   1 
ATOM   2822  O O   . LYS A 1 347 ? 5.377   14.335  92.084  1.00 127.82 ?  363 LYS B O   1 
ATOM   2823  C CB  . LYS A 1 347 ? 8.066   14.435  90.290  1.00 122.21 ?  363 LYS B CB  1 
ATOM   2824  C CG  . LYS A 1 347 ? 8.994   15.364  89.551  1.00 123.05 ?  363 LYS B CG  1 
ATOM   2825  C CD  . LYS A 1 347 ? 8.635   15.478  88.093  1.00 121.60 ?  363 LYS B CD  1 
ATOM   2826  C CE  . LYS A 1 347 ? 9.480   16.553  87.449  1.00 127.32 ?  363 LYS B CE  1 
ATOM   2827  N NZ  . LYS A 1 347 ? 9.104   16.777  86.031  1.00 133.44 ?  363 LYS B NZ  1 
ATOM   2828  N N   . VAL A 1 348 ? 5.337   12.679  90.563  1.00 122.17 ?  364 VAL B N   1 
ATOM   2829  C CA  . VAL A 1 348 ? 4.397   11.892  91.361  1.00 122.43 ?  364 VAL B CA  1 
ATOM   2830  C C   . VAL A 1 348 ? 5.175   11.232  92.507  1.00 120.25 ?  364 VAL B C   1 
ATOM   2831  O O   . VAL A 1 348 ? 5.443   10.024  92.485  1.00 119.95 ?  364 VAL B O   1 
ATOM   2832  C CB  . VAL A 1 348 ? 3.644   10.864  90.491  1.00 123.02 ?  364 VAL B CB  1 
ATOM   2833  C CG1 . VAL A 1 348 ? 2.559   10.161  91.307  1.00 125.30 ?  364 VAL B CG1 1 
ATOM   2834  C CG2 . VAL A 1 348 ? 3.064   11.518  89.243  1.00 118.39 ?  364 VAL B CG2 1 
ATOM   2835  N N   . THR A 1 349 ? 5.551   12.039  93.513  1.00 120.78 ?  365 THR B N   1 
ATOM   2836  C CA  . THR A 1 349 ? 6.474   11.671  94.595  1.00 113.93 ?  365 THR B CA  1 
ATOM   2837  C C   . THR A 1 349 ? 5.850   11.993  95.956  1.00 108.95 ?  365 THR B C   1 
ATOM   2838  O O   . THR A 1 349 ? 4.707   12.441  96.052  1.00 111.92 ?  365 THR B O   1 
ATOM   2839  C CB  . THR A 1 349 ? 7.810   12.408  94.452  1.00 110.06 ?  365 THR B CB  1 
ATOM   2840  O OG1 . THR A 1 349 ? 7.639   13.768  94.860  1.00 108.11 ?  365 THR B OG1 1 
ATOM   2841  C CG2 . THR A 1 349 ? 8.272   12.375  93.014  1.00 108.65 ?  365 THR B CG2 1 
ATOM   2842  N N   . MET A 1 350 ? 6.596   11.756  97.031  1.00 104.48 ?  366 MET B N   1 
ATOM   2843  C CA  . MET A 1 350 ? 6.045   12.131  98.324  1.00 101.52 ?  366 MET B CA  1 
ATOM   2844  C C   . MET A 1 350 ? 6.443   13.539  98.680  1.00 102.91 ?  366 MET B C   1 
ATOM   2845  O O   . MET A 1 350 ? 5.637   14.314  99.212  1.00 101.35 ?  366 MET B O   1 
ATOM   2846  C CB  . MET A 1 350 ? 6.503   11.166  99.418  1.00 104.94 ?  366 MET B CB  1 
ATOM   2847  C CG  . MET A 1 350 ? 5.984   11.565  100.793 1.00 103.41 ?  366 MET B CG  1 
ATOM   2848  S SD  . MET A 1 350 ? 6.464   10.500  102.162 1.00 105.24 ?  366 MET B SD  1 
ATOM   2849  C CE  . MET A 1 350 ? 5.591   11.274  103.532 1.00 91.07  ?  366 MET B CE  1 
ATOM   2850  N N   . ASP A 1 351 ? 7.680   13.874  98.352  1.00 110.78 ?  367 ASP B N   1 
ATOM   2851  C CA  . ASP A 1 351 ? 8.183   15.215  98.589  1.00 114.34 ?  367 ASP B CA  1 
ATOM   2852  C C   . ASP A 1 351 ? 7.322   16.259  97.883  1.00 108.40 ?  367 ASP B C   1 
ATOM   2853  O O   . ASP A 1 351 ? 6.980   17.296  98.468  1.00 104.65 ?  367 ASP B O   1 
ATOM   2854  C CB  . ASP A 1 351 ? 9.631   15.276  98.120  1.00 120.73 ?  367 ASP B CB  1 
ATOM   2855  C CG  . ASP A 1 351 ? 10.606  14.783  99.179  1.00 127.04 ?  367 ASP B CG  1 
ATOM   2856  O OD1 . ASP A 1 351 ? 10.196  14.575  100.344 1.00 122.31 ?  367 ASP B OD1 1 
ATOM   2857  O OD2 . ASP A 1 351 ? 11.775  14.557  98.822  1.00 134.79 -1 367 ASP B OD2 1 
ATOM   2858  N N   . ASP A 1 352 ? 6.920   15.981  96.641  1.00 110.17 ?  368 ASP B N   1 
ATOM   2859  C CA  . ASP A 1 352 ? 6.091   16.940  95.924  1.00 113.21 ?  368 ASP B CA  1 
ATOM   2860  C C   . ASP A 1 352 ? 4.661   16.984  96.462  1.00 109.97 ?  368 ASP B C   1 
ATOM   2861  O O   . ASP A 1 352 ? 4.028   18.038  96.414  1.00 109.59 ?  368 ASP B O   1 
ATOM   2862  C CB  . ASP A 1 352 ? 6.106   16.645  94.416  1.00 119.61 ?  368 ASP B CB  1 
ATOM   2863  C CG  . ASP A 1 352 ? 7.425   17.059  93.732  1.00 121.16 ?  368 ASP B CG  1 
ATOM   2864  O OD1 . ASP A 1 352 ? 8.416   17.278  94.461  1.00 120.63 ?  368 ASP B OD1 1 
ATOM   2865  O OD2 . ASP A 1 352 ? 7.455   17.179  92.474  1.00 121.17 -1 368 ASP B OD2 1 
ATOM   2866  N N   . PHE A 1 353 ? 4.133   15.875  96.982  1.00 100.17 ?  369 PHE B N   1 
ATOM   2867  C CA  . PHE A 1 353 ? 2.810   15.906  97.607  1.00 96.66  ?  369 PHE B CA  1 
ATOM   2868  C C   . PHE A 1 353 ? 2.819   16.853  98.810  1.00 95.71  ?  369 PHE B C   1 
ATOM   2869  O O   . PHE A 1 353 ? 1.976   17.770  98.924  1.00 92.38  ?  369 PHE B O   1 
ATOM   2870  C CB  . PHE A 1 353 ? 2.446   14.476  98.011  1.00 94.39  ?  369 PHE B CB  1 
ATOM   2871  C CG  . PHE A 1 353 ? 1.250   14.325  98.921  1.00 89.31  ?  369 PHE B CG  1 
ATOM   2872  C CD1 . PHE A 1 353 ? -0.030  14.201  98.386  1.00 88.31  ?  369 PHE B CD1 1 
ATOM   2873  C CD2 . PHE A 1 353 ? 1.407   14.235  100.291 1.00 87.74  ?  369 PHE B CD2 1 
ATOM   2874  C CE1 . PHE A 1 353 ? -1.132  13.999  99.199  1.00 86.28  ?  369 PHE B CE1 1 
ATOM   2875  C CE2 . PHE A 1 353 ? 0.306   14.054  101.115 1.00 87.27  ?  369 PHE B CE2 1 
ATOM   2876  C CZ  . PHE A 1 353 ? -0.967  13.936  100.564 1.00 85.52  ?  369 PHE B CZ  1 
ATOM   2877  N N   . LEU A 1 354 ? 3.813   16.673  99.694  1.00 100.02 ?  370 LEU B N   1 
ATOM   2878  C CA  . LEU A 1 354 ? 3.930   17.538  100.861 1.00 93.91  ?  370 LEU B CA  1 
ATOM   2879  C C   . LEU A 1 354 ? 4.174   18.986  100.446 1.00 91.73  ?  370 LEU B C   1 
ATOM   2880  O O   . LEU A 1 354 ? 3.615   19.924  101.044 1.00 93.32  ?  370 LEU B O   1 
ATOM   2881  C CB  . LEU A 1 354 ? 5.040   17.016  101.767 1.00 91.97  ?  370 LEU B CB  1 
ATOM   2882  C CG  . LEU A 1 354 ? 4.737   15.601  102.295 1.00 91.03  ?  370 LEU B CG  1 
ATOM   2883  C CD1 . LEU A 1 354 ? 5.739   15.111  103.309 1.00 89.81  ?  370 LEU B CD1 1 
ATOM   2884  C CD2 . LEU A 1 354 ? 3.343   15.518  102.887 1.00 91.11  ?  370 LEU B CD2 1 
ATOM   2885  N N   . THR A 1 355 ? 4.950   19.191  99.379  1.00 94.93  ?  371 THR B N   1 
ATOM   2886  C CA  . THR A 1 355 ? 5.190   20.547  98.904  1.00 94.18  ?  371 THR B CA  1 
ATOM   2887  C C   . THR A 1 355 ? 3.919   21.194  98.362  1.00 91.57  ?  371 THR B C   1 
ATOM   2888  O O   . THR A 1 355 ? 3.713   22.407  98.510  1.00 85.32  ?  371 THR B O   1 
ATOM   2889  C CB  . THR A 1 355 ? 6.272   20.527  97.841  1.00 91.54  ?  371 THR B CB  1 
ATOM   2890  O OG1 . THR A 1 355 ? 7.489   20.073  98.430  1.00 92.53  ?  371 THR B OG1 1 
ATOM   2891  C CG2 . THR A 1 355 ? 6.489   21.908  97.309  1.00 88.09  ?  371 THR B CG2 1 
ATOM   2892  N N   . ALA A 1 356 ? 3.063   20.414  97.712  1.00 92.69  ?  372 ALA B N   1 
ATOM   2893  C CA  . ALA A 1 356 ? 1.861   21.008  97.157  1.00 94.89  ?  372 ALA B CA  1 
ATOM   2894  C C   . ALA A 1 356 ? 0.920   21.435  98.259  1.00 92.10  ?  372 ALA B C   1 
ATOM   2895  O O   . ALA A 1 356 ? 0.288   22.491  98.149  1.00 92.54  ?  372 ALA B O   1 
ATOM   2896  C CB  . ALA A 1 356 ? 1.171   20.048  96.195  1.00 99.16  ?  372 ALA B CB  1 
ATOM   2897  N N   . HIS A 1 357 ? 0.811   20.641  99.326  1.00 79.79  ?  373 HIS B N   1 
ATOM   2898  C CA  . HIS A 1 357 ? 0.066   21.146  100.478 1.00 77.33  ?  373 HIS B CA  1 
ATOM   2899  C C   . HIS A 1 357 ? 0.637   22.464  100.992 1.00 73.37  ?  373 HIS B C   1 
ATOM   2900  O O   . HIS A 1 357 ? -0.122  23.405  101.265 1.00 73.53  ?  373 HIS B O   1 
ATOM   2901  C CB  . HIS A 1 357 ? 0.007   20.108  101.581 1.00 77.14  ?  373 HIS B CB  1 
ATOM   2902  C CG  . HIS A 1 357 ? -0.867  18.951  101.243 1.00 78.12  ?  373 HIS B CG  1 
ATOM   2903  N ND1 . HIS A 1 357 ? -0.519  18.011  100.300 1.00 79.45  ?  373 HIS B ND1 1 
ATOM   2904  C CD2 . HIS A 1 357 ? -2.056  18.555  101.762 1.00 76.72  ?  373 HIS B CD2 1 
ATOM   2905  C CE1 . HIS A 1 357 ? -1.475  17.106  100.225 1.00 81.04  ?  373 HIS B CE1 1 
ATOM   2906  N NE2 . HIS A 1 357 ? -2.415  17.406  101.106 1.00 78.12  ?  373 HIS B NE2 1 
ATOM   2907  N N   . HIS A 1 358 ? 1.971   22.559  101.103 1.00 76.15  ?  374 HIS B N   1 
ATOM   2908  C CA  . HIS A 1 358 ? 2.621   23.812  101.535 1.00 76.66  ?  374 HIS B CA  1 
ATOM   2909  C C   . HIS A 1 358 ? 2.225   25.007  100.651 1.00 73.56  ?  374 HIS B C   1 
ATOM   2910  O O   . HIS A 1 358 ? 1.759   26.051  101.144 1.00 70.98  ?  374 HIS B O   1 
ATOM   2911  C CB  . HIS A 1 358 ? 4.148   23.582  101.556 1.00 76.65  ?  374 HIS B CB  1 
ATOM   2912  C CG  . HIS A 1 358 ? 4.981   24.747  102.027 1.00 71.39  ?  374 HIS B CG  1 
ATOM   2913  N ND1 . HIS A 1 358 ? 5.706   24.720  103.197 1.00 72.82  ?  374 HIS B ND1 1 
ATOM   2914  C CD2 . HIS A 1 358 ? 5.314   25.911  101.409 1.00 74.97  ?  374 HIS B CD2 1 
ATOM   2915  C CE1 . HIS A 1 358 ? 6.378   25.849  103.320 1.00 77.36  ?  374 HIS B CE1 1 
ATOM   2916  N NE2 . HIS A 1 358 ? 6.164   26.589  102.245 1.00 73.92  ?  374 HIS B NE2 1 
ATOM   2917  N N   . GLU A 1 359 ? 2.441   24.887  99.350  1.00 70.84  ?  375 GLU B N   1 
ATOM   2918  C CA  . GLU A 1 359 ? 2.225   26.041  98.483  1.00 70.19  ?  375 GLU B CA  1 
ATOM   2919  C C   . GLU A 1 359 ? 0.732   26.380  98.367  1.00 70.87  ?  375 GLU B C   1 
ATOM   2920  O O   . GLU A 1 359 ? 0.340   27.562  98.307  1.00 66.23  ?  375 GLU B O   1 
ATOM   2921  C CB  . GLU A 1 359 ? 2.920   25.777  97.139  1.00 70.54  ?  375 GLU B CB  1 
ATOM   2922  C CG  . GLU A 1 359 ? 4.506   25.747  97.210  1.00 69.44  ?  375 GLU B CG  1 
ATOM   2923  C CD  . GLU A 1 359 ? 5.171   27.015  97.859  1.00 78.66  ?  375 GLU B CD  1 
ATOM   2924  O OE1 . GLU A 1 359 ? 4.705   28.136  97.535  1.00 82.95  ?  375 GLU B OE1 1 
ATOM   2925  O OE2 . GLU A 1 359 ? 6.126   26.931  98.700  1.00 78.98  -1 375 GLU B OE2 1 
ATOM   2926  N N   . MET A 1 360 ? -0.133  25.374  98.404  1.00 70.48  ?  376 MET B N   1 
ATOM   2927  C CA  . MET A 1 360 ? -1.543  25.696  98.427  1.00 68.95  ?  376 MET B CA  1 
ATOM   2928  C C   . MET A 1 360 ? -1.926  26.381  99.737  1.00 66.99  ?  376 MET B C   1 
ATOM   2929  O O   . MET A 1 360 ? -2.870  27.172  99.771  1.00 67.36  ?  376 MET B O   1 
ATOM   2930  C CB  . MET A 1 360 ? -2.357  24.432  98.183  1.00 72.78  ?  376 MET B CB  1 
ATOM   2931  C CG  . MET A 1 360 ? -3.824  24.727  97.897  1.00 79.08  ?  376 MET B CG  1 
ATOM   2932  S SD  . MET A 1 360 ? -4.817  23.350  97.277  1.00 70.65  ?  376 MET B SD  1 
ATOM   2933  C CE  . MET A 1 360 ? -4.129  23.095  95.643  1.00 79.39  ?  376 MET B CE  1 
ATOM   2934  N N   . GLY A 1 361 ? -1.199  26.130  100.821 1.00 74.09  ?  377 GLY B N   1 
ATOM   2935  C CA  . GLY A 1 361 ? -1.483  26.872  102.043 1.00 75.16  ?  377 GLY B CA  1 
ATOM   2936  C C   . GLY A 1 361 ? -1.117  28.335  101.924 1.00 68.18  ?  377 GLY B C   1 
ATOM   2937  O O   . GLY A 1 361 ? -1.809  29.211  102.448 1.00 64.95  ?  377 GLY B O   1 
ATOM   2938  N N   . HIS A 1 362 ? -0.010  28.616  101.245 1.00 63.98  ?  378 HIS B N   1 
ATOM   2939  C CA  . HIS A 1 362 ? 0.220   29.975  100.740 1.00 67.58  ?  378 HIS B CA  1 
ATOM   2940  C C   . HIS A 1 362 ? -1.009  30.570  100.040 1.00 68.79  ?  378 HIS B C   1 
ATOM   2941  O O   . HIS A 1 362 ? -1.463  31.673  100.381 1.00 65.42  ?  378 HIS B O   1 
ATOM   2942  C CB  . HIS A 1 362 ? 1.423   29.979  99.794  1.00 68.83  ?  378 HIS B CB  1 
ATOM   2943  C CG  . HIS A 1 362 ? 2.761   29.957  100.462 1.00 63.68  ?  378 HIS B CG  1 
ATOM   2944  N ND1 . HIS A 1 362 ? 3.024   30.680  101.601 1.00 58.77  ?  378 HIS B ND1 1 
ATOM   2945  C CD2 . HIS A 1 362 ? 3.893   29.269  100.178 1.00 67.69  ?  378 HIS B CD2 1 
ATOM   2946  C CE1 . HIS A 1 362 ? 4.279   30.479  101.962 1.00 68.58  ?  378 HIS B CE1 1 
ATOM   2947  N NE2 . HIS A 1 362 ? 4.824   29.613  101.125 1.00 71.59  ?  378 HIS B NE2 1 
ATOM   2948  N N   . ILE A 1 363 ? -1.522  29.877  99.013  1.00 70.87  ?  379 ILE B N   1 
ATOM   2949  C CA  . ILE A 1 363 ? -2.655  30.426  98.249  1.00 69.76  ?  379 ILE B CA  1 
ATOM   2950  C C   . ILE A 1 363 ? -3.854  30.688  99.156  1.00 68.40  ?  379 ILE B C   1 
ATOM   2951  O O   . ILE A 1 363 ? -4.521  31.723  99.049  1.00 69.54  ?  379 ILE B O   1 
ATOM   2952  C CB  . ILE A 1 363 ? -3.033  29.502  97.082  1.00 66.90  ?  379 ILE B CB  1 
ATOM   2953  C CG1 . ILE A 1 363 ? -1.870  29.385  96.117  1.00 66.06  ?  379 ILE B CG1 1 
ATOM   2954  C CG2 . ILE A 1 363 ? -4.270  30.019  96.374  1.00 65.77  ?  379 ILE B CG2 1 
ATOM   2955  C CD1 . ILE A 1 363 ? -1.678  30.618  95.338  1.00 66.18  ?  379 ILE B CD1 1 
ATOM   2956  N N   . GLN A 1 364 ? -4.179  29.719  100.007 1.00 67.64  ?  380 GLN B N   1 
ATOM   2957  C CA  . GLN A 1 364 ? -5.229  29.888  101.007 1.00 65.68  ?  380 GLN B CA  1 
ATOM   2958  C C   . GLN A 1 364 ? -5.051  31.191  101.798 1.00 63.65  ?  380 GLN B C   1 
ATOM   2959  O O   . GLN A 1 364 ? -5.995  31.977  101.938 1.00 63.23  ?  380 GLN B O   1 
ATOM   2960  C CB  . GLN A 1 364 ? -5.207  28.674  101.937 1.00 63.80  ?  380 GLN B CB  1 
ATOM   2961  C CG  . GLN A 1 364 ? -6.529  28.206  102.499 1.00 61.04  ?  380 GLN B CG  1 
ATOM   2962  C CD  . GLN A 1 364 ? -7.448  27.572  101.476 1.00 66.56  ?  380 GLN B CD  1 
ATOM   2963  O OE1 . GLN A 1 364 ? -8.629  27.894  101.414 1.00 66.13  ?  380 GLN B OE1 1 
ATOM   2964  N NE2 . GLN A 1 364 ? -6.913  26.656  100.670 1.00 70.92  ?  380 GLN B NE2 1 
ATOM   2965  N N   . TYR A 1 365 ? -3.840  31.427  102.331 1.00 65.83  ?  381 TYR B N   1 
ATOM   2966  C CA  . TYR A 1 365 ? -3.550  32.686  103.025 1.00 64.94  ?  381 TYR B CA  1 
ATOM   2967  C C   . TYR A 1 365 ? -3.804  33.886  102.113 1.00 67.19  ?  381 TYR B C   1 
ATOM   2968  O O   . TYR A 1 365 ? -4.320  34.917  102.562 1.00 67.63  ?  381 TYR B O   1 
ATOM   2969  C CB  . TYR A 1 365 ? -2.087  32.710  103.514 1.00 60.79  ?  381 TYR B CB  1 
ATOM   2970  C CG  . TYR A 1 365 ? -1.736  33.616  104.732 1.00 59.80  ?  381 TYR B CG  1 
ATOM   2971  C CD1 . TYR A 1 365 ? -2.651  34.523  105.280 1.00 63.80  ?  381 TYR B CD1 1 
ATOM   2972  C CD2 . TYR A 1 365 ? -0.449  33.613  105.290 1.00 58.25  ?  381 TYR B CD2 1 
ATOM   2973  C CE1 . TYR A 1 365 ? -2.300  35.368  106.414 1.00 65.98  ?  381 TYR B CE1 1 
ATOM   2974  C CE2 . TYR A 1 365 ? -0.093  34.460  106.404 1.00 55.83  ?  381 TYR B CE2 1 
ATOM   2975  C CZ  . TYR A 1 365 ? -1.014  35.332  106.967 1.00 56.98  ?  381 TYR B CZ  1 
ATOM   2976  O OH  . TYR A 1 365 ? -0.661  36.155  108.053 1.00 47.88  ?  381 TYR B OH  1 
ATOM   2977  N N   . ASP A 1 366 ? -3.414  33.775  100.834 1.00 67.25  ?  382 ASP B N   1 
ATOM   2978  C CA  . ASP A 1 366 ? -3.568  34.879  99.880  1.00 68.19  ?  382 ASP B CA  1 
ATOM   2979  C C   . ASP A 1 366 ? -5.045  35.207  99.621  1.00 70.97  ?  382 ASP B C   1 
ATOM   2980  O O   . ASP A 1 366 ? -5.428  36.383  99.497  1.00 67.90  ?  382 ASP B O   1 
ATOM   2981  C CB  . ASP A 1 366 ? -2.798  34.530  98.590  1.00 71.00  ?  382 ASP B CB  1 
ATOM   2982  C CG  . ASP A 1 366 ? -1.270  34.428  98.821  1.00 74.43  ?  382 ASP B CG  1 
ATOM   2983  O OD1 . ASP A 1 366 ? -0.838  35.043  99.806  1.00 75.45  ?  382 ASP B OD1 1 
ATOM   2984  O OD2 . ASP A 1 366 ? -0.488  33.758  98.078  1.00 73.14  -1 382 ASP B OD2 1 
ATOM   2985  N N   . MET A 1 367 ? -5.889  34.174  99.562  1.00 69.46  ?  383 MET B N   1 
ATOM   2986  C CA  . MET A 1 367 ? -7.316  34.369  99.325  1.00 64.55  ?  383 MET B CA  1 
ATOM   2987  C C   . MET A 1 367 ? -7.988  34.919  100.562 1.00 65.64  ?  383 MET B C   1 
ATOM   2988  O O   . MET A 1 367 ? -8.879  35.760  100.465 1.00 70.01  ?  383 MET B O   1 
ATOM   2989  C CB  . MET A 1 367 ? -7.945  33.042  98.926  1.00 63.40  ?  383 MET B CB  1 
ATOM   2990  C CG  . MET A 1 367 ? -7.424  32.544  97.620  1.00 63.63  ?  383 MET B CG  1 
ATOM   2991  S SD  . MET A 1 367 ? -7.897  30.842  97.330  1.00 69.59  ?  383 MET B SD  1 
ATOM   2992  C CE  . MET A 1 367 ? -9.673  31.020  97.144  1.00 70.28  ?  383 MET B CE  1 
ATOM   2993  N N   . ALA A 1 368 ? -7.570  34.452  101.737 1.00 74.56  ?  384 ALA B N   1 
ATOM   2994  C CA  . ALA A 1 368 ? -8.196  34.893  102.983 1.00 74.25  ?  384 ALA B CA  1 
ATOM   2995  C C   . ALA A 1 368 ? -8.135  36.408  103.136 1.00 74.07  ?  384 ALA B C   1 
ATOM   2996  O O   . ALA A 1 368 ? -9.155  37.061  103.388 1.00 76.33  ?  384 ALA B O   1 
ATOM   2997  C CB  . ALA A 1 368 ? -7.531  34.215  104.180 1.00 73.67  ?  384 ALA B CB  1 
ATOM   2998  N N   . TYR A 1 369 ? -6.955  36.996  102.959 1.00 67.08  ?  385 TYR B N   1 
ATOM   2999  C CA  . TYR A 1 369 ? -6.834  38.431  103.149 1.00 63.75  ?  385 TYR B CA  1 
ATOM   3000  C C   . TYR A 1 369 ? -6.986  39.218  101.846 1.00 67.03  ?  385 TYR B C   1 
ATOM   3001  O O   . TYR A 1 369 ? -6.520  40.368  101.781 1.00 61.70  ?  385 TYR B O   1 
ATOM   3002  C CB  . TYR A 1 369 ? -5.500  38.774  103.807 1.00 63.48  ?  385 TYR B CB  1 
ATOM   3003  C CG  . TYR A 1 369 ? -4.220  38.344  103.083 1.00 64.59  ?  385 TYR B CG  1 
ATOM   3004  C CD1 . TYR A 1 369 ? -3.975  38.745  101.782 1.00 64.86  ?  385 TYR B CD1 1 
ATOM   3005  C CD2 . TYR A 1 369 ? -3.222  37.606  103.727 1.00 62.39  ?  385 TYR B CD2 1 
ATOM   3006  C CE1 . TYR A 1 369 ? -2.813  38.392  101.122 1.00 64.35  ?  385 TYR B CE1 1 
ATOM   3007  C CE2 . TYR A 1 369 ? -2.042  37.253  103.064 1.00 57.93  ?  385 TYR B CE2 1 
ATOM   3008  C CZ  . TYR A 1 369 ? -1.855  37.657  101.757 1.00 60.42  ?  385 TYR B CZ  1 
ATOM   3009  O OH  . TYR A 1 369 ? -0.733  37.351  101.026 1.00 61.87  ?  385 TYR B OH  1 
ATOM   3010  N N   . ALA A 1 370 ? -7.654  38.670  100.837 1.00 72.87  ?  386 ALA B N   1 
ATOM   3011  C CA  . ALA A 1 370 ? -7.734  39.437  99.577  1.00 64.66  ?  386 ALA B CA  1 
ATOM   3012  C C   . ALA A 1 370 ? -8.582  40.685  99.806  1.00 62.23  ?  386 ALA B C   1 
ATOM   3013  O O   . ALA A 1 370 ? -8.266  41.731  99.220  1.00 51.72  ?  386 ALA B O   1 
ATOM   3014  C CB  . ALA A 1 370 ? -8.311  38.583  98.490  1.00 62.27  ?  386 ALA B CB  1 
ATOM   3015  N N   . ALA A 1 371 ? -9.602  40.574  100.647 1.00 60.93  ?  387 ALA B N   1 
ATOM   3016  C CA  . ALA A 1 371 ? -10.501 41.715  100.921 1.00 59.80  ?  387 ALA B CA  1 
ATOM   3017  C C   . ALA A 1 371 ? -9.711  42.880  101.493 1.00 58.05  ?  387 ALA B C   1 
ATOM   3018  O O   . ALA A 1 371 ? -10.169 44.024  101.370 1.00 53.30  ?  387 ALA B O   1 
ATOM   3019  C CB  . ALA A 1 371 ? -11.539 41.284  101.912 1.00 62.53  ?  387 ALA B CB  1 
ATOM   3020  N N   . GLN A 1 372 ? -8.586  42.585  102.133 1.00 63.19  ?  388 GLN B N   1 
ATOM   3021  C CA  . GLN A 1 372 ? -7.840  43.663  102.815 1.00 54.55  ?  388 GLN B CA  1 
ATOM   3022  C C   . GLN A 1 372 ? -7.296  44.636  101.778 1.00 53.54  ?  388 GLN B C   1 
ATOM   3023  O O   . GLN A 1 372 ? -6.857  44.188  100.719 1.00 56.35  ?  388 GLN B O   1 
ATOM   3024  C CB  . GLN A 1 372 ? -6.722  43.070  103.668 1.00 53.18  ?  388 GLN B CB  1 
ATOM   3025  C CG  . GLN A 1 372 ? -7.215  42.163  104.778 1.00 53.50  ?  388 GLN B CG  1 
ATOM   3026  C CD  . GLN A 1 372 ? -7.683  42.965  105.964 1.00 51.77  ?  388 GLN B CD  1 
ATOM   3027  O OE1 . GLN A 1 372 ? -7.486  44.175  106.037 1.00 45.66  ?  388 GLN B OE1 1 
ATOM   3028  N NE2 . GLN A 1 372 ? -8.310  42.288  106.909 1.00 51.92  ?  388 GLN B NE2 1 
ATOM   3029  N N   . PRO A 1 373 ? -7.329  45.947  102.047 1.00 49.59  ?  389 PRO B N   1 
ATOM   3030  C CA  . PRO A 1 373 ? -6.733  46.950  101.152 1.00 52.99  ?  389 PRO B CA  1 
ATOM   3031  C C   . PRO A 1 373 ? -5.328  46.564  100.725 1.00 54.11  ?  389 PRO B C   1 
ATOM   3032  O O   . PRO A 1 373 ? -4.652  45.764  101.369 1.00 59.36  ?  389 PRO B O   1 
ATOM   3033  C CB  . PRO A 1 373 ? -6.731  48.234  101.990 1.00 47.95  ?  389 PRO B CB  1 
ATOM   3034  C CG  . PRO A 1 373 ? -6.974  47.798  103.345 1.00 48.12  ?  389 PRO B CG  1 
ATOM   3035  C CD  . PRO A 1 373 ? -7.755  46.538  103.310 1.00 49.52  ?  389 PRO B CD  1 
ATOM   3036  N N   . PHE A 1 374 ? -4.880  47.170  99.626  1.00 53.78  ?  390 PHE B N   1 
ATOM   3037  C CA  . PHE A 1 374 ? -3.769  46.596  98.870  1.00 52.50  ?  390 PHE B CA  1 
ATOM   3038  C C   . PHE A 1 374 ? -2.487  46.572  99.688  1.00 54.79  ?  390 PHE B C   1 
ATOM   3039  O O   . PHE A 1 374 ? -1.794  45.540  99.736  1.00 52.83  ?  390 PHE B O   1 
ATOM   3040  C CB  . PHE A 1 374 ? -3.602  47.353  97.547  1.00 55.09  ?  390 PHE B CB  1 
ATOM   3041  C CG  . PHE A 1 374 ? -2.427  46.933  96.728  1.00 49.98  ?  390 PHE B CG  1 
ATOM   3042  C CD1 . PHE A 1 374 ? -2.540  45.887  95.836  1.00 52.19  ?  390 PHE B CD1 1 
ATOM   3043  C CD2 . PHE A 1 374 ? -1.201  47.545  96.876  1.00 53.33  ?  390 PHE B CD2 1 
ATOM   3044  C CE1 . PHE A 1 374 ? -1.464  45.481  95.082  1.00 53.48  ?  390 PHE B CE1 1 
ATOM   3045  C CE2 . PHE A 1 374 ? -0.115  47.150  96.108  1.00 56.66  ?  390 PHE B CE2 1 
ATOM   3046  C CZ  . PHE A 1 374 ? -0.251  46.113  95.211  1.00 56.39  ?  390 PHE B CZ  1 
ATOM   3047  N N   . LEU A 1 375 ? -2.163  47.675  100.371 1.00 56.63  ?  391 LEU B N   1 
ATOM   3048  C CA  . LEU A 1 375 ? -0.889  47.612  101.084 1.00 51.26  ?  391 LEU B CA  1 
ATOM   3049  C C   . LEU A 1 375 ? -0.940  46.704  102.306 1.00 49.33  ?  391 LEU B C   1 
ATOM   3050  O O   . LEU A 1 375 ? 0.083   46.564  102.985 1.00 54.04  ?  391 LEU B O   1 
ATOM   3051  C CB  . LEU A 1 375 ? -0.412  49.009  101.492 1.00 50.41  ?  391 LEU B CB  1 
ATOM   3052  C CG  . LEU A 1 375 ? -0.097  49.973  100.341 1.00 51.20  ?  391 LEU B CG  1 
ATOM   3053  C CD1 . LEU A 1 375 ? 0.094   51.436  100.773 1.00 53.41  ?  391 LEU B CD1 1 
ATOM   3054  C CD2 . LEU A 1 375 ? 1.024   49.461  99.498  1.00 46.99  ?  391 LEU B CD2 1 
ATOM   3055  N N   . LEU A 1 376 ? -2.081  46.070  102.588 1.00 47.94  ?  392 LEU B N   1 
ATOM   3056  C CA  . LEU A 1 376 ? -2.210  45.167  103.722 1.00 50.74  ?  392 LEU B CA  1 
ATOM   3057  C C   . LEU A 1 376 ? -2.371  43.708  103.320 1.00 51.08  ?  392 LEU B C   1 
ATOM   3058  O O   . LEU A 1 376 ? -2.615  42.859  104.180 1.00 54.78  ?  392 LEU B O   1 
ATOM   3059  C CB  . LEU A 1 376 ? -3.370  45.611  104.618 1.00 49.75  ?  392 LEU B CB  1 
ATOM   3060  C CG  . LEU A 1 376 ? -3.208  47.066  105.042 1.00 51.41  ?  392 LEU B CG  1 
ATOM   3061  C CD1 . LEU A 1 376 ? -4.307  47.574  105.967 1.00 48.61  ?  392 LEU B CD1 1 
ATOM   3062  C CD2 . LEU A 1 376 ? -1.871  47.157  105.738 1.00 57.57  ?  392 LEU B CD2 1 
ATOM   3063  N N   . ARG A 1 377 ? -2.167  43.372  102.055 1.00 49.41  ?  393 ARG B N   1 
ATOM   3064  C CA  . ARG A 1 377 ? -2.388  42.001  101.621 1.00 55.37  ?  393 ARG B CA  1 
ATOM   3065  C C   . ARG A 1 377 ? -1.101  41.208  101.800 1.00 55.93  ?  393 ARG B C   1 
ATOM   3066  O O   . ARG A 1 377 ? -0.281  41.064  100.893 1.00 59.47  ?  393 ARG B O   1 
ATOM   3067  C CB  . ARG A 1 377 ? -2.873  41.989  100.188 1.00 54.14  ?  393 ARG B CB  1 
ATOM   3068  C CG  . ARG A 1 377 ? -4.231  42.586  100.085 1.00 54.14  ?  393 ARG B CG  1 
ATOM   3069  C CD  . ARG A 1 377 ? -4.623  42.644  98.691  1.00 54.64  ?  393 ARG B CD  1 
ATOM   3070  N NE  . ARG A 1 377 ? -5.879  43.335  98.515  1.00 57.92  ?  393 ARG B NE  1 
ATOM   3071  C CZ  . ARG A 1 377 ? -6.292  43.792  97.345  1.00 63.49  ?  393 ARG B CZ  1 
ATOM   3072  N NH1 . ARG A 1 377 ? -5.568  43.603  96.239  1.00 59.36  ?  393 ARG B NH1 1 
ATOM   3073  N NH2 . ARG A 1 377 ? -7.473  44.412  97.274  1.00 67.99  ?  393 ARG B NH2 1 
ATOM   3074  N N   . ASN A 1 378 ? -0.921  40.676  103.000 1.00 55.48  ?  394 ASN B N   1 
ATOM   3075  C CA  . ASN A 1 378 ? 0.383   40.111  103.307 1.00 56.74  ?  394 ASN B CA  1 
ATOM   3076  C C   . ASN A 1 378 ? 0.331   39.442  104.658 1.00 54.45  ?  394 ASN B C   1 
ATOM   3077  O O   . ASN A 1 378 ? -0.538  39.743  105.480 1.00 54.77  ?  394 ASN B O   1 
ATOM   3078  C CB  . ASN A 1 378 ? 1.472   41.174  103.315 1.00 53.78  ?  394 ASN B CB  1 
ATOM   3079  C CG  . ASN A 1 378 ? 2.690   40.725  102.568 1.00 64.01  ?  394 ASN B CG  1 
ATOM   3080  O OD1 . ASN A 1 378 ? 3.180   39.587  102.759 1.00 60.12  ?  394 ASN B OD1 1 
ATOM   3081  N ND2 . ASN A 1 378 ? 3.221   41.615  101.724 1.00 74.99  ?  394 ASN B ND2 1 
ATOM   3082  N N   . GLY A 1 379 ? 1.305   38.570  104.893 1.00 48.72  ?  395 GLY B N   1 
ATOM   3083  C CA  . GLY A 1 379 ? 1.377   37.895  106.172 1.00 53.96  ?  395 GLY B CA  1 
ATOM   3084  C C   . GLY A 1 379 ? 1.644   38.874  107.302 1.00 56.05  ?  395 GLY B C   1 
ATOM   3085  O O   . GLY A 1 379 ? 2.224   39.948  107.097 1.00 57.07  ?  395 GLY B O   1 
ATOM   3086  N N   . ALA A 1 380 ? 1.221   38.486  108.518 1.00 56.24  ?  396 ALA B N   1 
ATOM   3087  C CA  . ALA A 1 380 ? 1.236   39.409  109.656 1.00 52.81  ?  396 ALA B CA  1 
ATOM   3088  C C   . ALA A 1 380 ? 2.609   40.039  109.866 1.00 54.60  ?  396 ALA B C   1 
ATOM   3089  O O   . ALA A 1 380 ? 2.712   41.235  110.179 1.00 56.28  ?  396 ALA B O   1 
ATOM   3090  C CB  . ALA A 1 380 ? 0.777   38.680  110.914 1.00 49.83  ?  396 ALA B CB  1 
ATOM   3091  N N   . ASN A 1 381 ? 3.672   39.239  109.723 1.00 51.48  ?  397 ASN B N   1 
ATOM   3092  C CA  . ASN A 1 381 ? 5.059   39.690  109.666 1.00 50.26  ?  397 ASN B CA  1 
ATOM   3093  C C   . ASN A 1 381 ? 5.791   38.712  108.754 1.00 50.79  ?  397 ASN B C   1 
ATOM   3094  O O   . ASN A 1 381 ? 5.238   37.664  108.377 1.00 49.42  ?  397 ASN B O   1 
ATOM   3095  C CB  . ASN A 1 381 ? 5.730   39.764  111.055 1.00 46.30  ?  397 ASN B CB  1 
ATOM   3096  C CG  . ASN A 1 381 ? 5.883   38.382  111.757 1.00 49.50  ?  397 ASN B CG  1 
ATOM   3097  O OD1 . ASN A 1 381 ? 6.168   37.363  111.121 1.00 50.48  ?  397 ASN B OD1 1 
ATOM   3098  N ND2 . ASN A 1 381 ? 5.747   38.375  113.088 1.00 49.56  ?  397 ASN B ND2 1 
ATOM   3099  N N   . GLU A 1 382 ? 7.065   39.029  108.456 1.00 49.89  ?  398 GLU B N   1 
ATOM   3100  C CA  . GLU A 1 382 ? 7.874   38.226  107.530 1.00 49.17  ?  398 GLU B CA  1 
ATOM   3101  C C   . GLU A 1 382 ? 7.839   36.729  107.845 1.00 47.53  ?  398 GLU B C   1 
ATOM   3102  O O   . GLU A 1 382 ? 8.177   35.917  106.968 1.00 49.59  ?  398 GLU B O   1 
ATOM   3103  C CB  . GLU A 1 382 ? 9.332   38.695  107.499 1.00 50.19  ?  398 GLU B CB  1 
ATOM   3104  C CG  . GLU A 1 382 ? 10.111  38.496  108.820 1.00 56.11  ?  398 GLU B CG  1 
ATOM   3105  C CD  . GLU A 1 382 ? 11.485  39.176  108.862 1.00 57.27  ?  398 GLU B CD  1 
ATOM   3106  O OE1 . GLU A 1 382 ? 11.786  40.104  108.071 1.00 60.06  ?  398 GLU B OE1 1 
ATOM   3107  O OE2 . GLU A 1 382 ? 12.323  38.692  109.635 1.00 56.12  -1 398 GLU B OE2 1 
ATOM   3108  N N   . GLY A 1 383 ? 7.430   36.332  109.052 1.00 46.04  ?  399 GLY B N   1 
ATOM   3109  C CA  . GLY A 1 383 ? 7.493   34.925  109.403 1.00 49.11  ?  399 GLY B CA  1 
ATOM   3110  C C   . GLY A 1 383 ? 6.238   34.100  109.181 1.00 60.19  ?  399 GLY B C   1 
ATOM   3111  O O   . GLY A 1 383 ? 6.266   32.867  109.368 1.00 59.62  ?  399 GLY B O   1 
ATOM   3112  N N   . PHE A 1 384 ? 5.134   34.743  108.781 1.00 56.84  ?  400 PHE B N   1 
ATOM   3113  C CA  . PHE A 1 384 ? 3.833   34.099  108.906 1.00 50.52  ?  400 PHE B CA  1 
ATOM   3114  C C   . PHE A 1 384 ? 3.519   33.191  107.742 1.00 55.38  ?  400 PHE B C   1 
ATOM   3115  O O   . PHE A 1 384 ? 3.058   32.067  107.952 1.00 60.25  ?  400 PHE B O   1 
ATOM   3116  C CB  . PHE A 1 384 ? 2.743   35.134  109.058 1.00 51.92  ?  400 PHE B CB  1 
ATOM   3117  C CG  . PHE A 1 384 ? 2.368   35.427  110.476 1.00 51.99  ?  400 PHE B CG  1 
ATOM   3118  C CD1 . PHE A 1 384 ? 3.281   35.922  111.378 1.00 52.75  ?  400 PHE B CD1 1 
ATOM   3119  C CD2 . PHE A 1 384 ? 1.063   35.217  110.902 1.00 54.15  ?  400 PHE B CD2 1 
ATOM   3120  C CE1 . PHE A 1 384 ? 2.891   36.200  112.693 1.00 53.08  ?  400 PHE B CE1 1 
ATOM   3121  C CE2 . PHE A 1 384 ? 0.678   35.481  112.213 1.00 55.44  ?  400 PHE B CE2 1 
ATOM   3122  C CZ  . PHE A 1 384 ? 1.576   35.970  113.106 1.00 51.15  ?  400 PHE B CZ  1 
ATOM   3123  N N   . HIS A 1 385 ? 3.716   33.659  106.511 1.00 57.50  ?  401 HIS B N   1 
ATOM   3124  C CA  . HIS A 1 385 ? 3.399   32.806  105.367 1.00 60.35  ?  401 HIS B CA  1 
ATOM   3125  C C   . HIS A 1 385 ? 4.064   31.443  105.437 1.00 64.53  ?  401 HIS B C   1 
ATOM   3126  O O   . HIS A 1 385 ? 3.385   30.410  105.352 1.00 64.17  ?  401 HIS B O   1 
ATOM   3127  C CB  . HIS A 1 385 ? 3.757   33.476  104.046 1.00 65.78  ?  401 HIS B CB  1 
ATOM   3128  C CG  . HIS A 1 385 ? 2.585   34.064  103.331 1.00 65.08  ?  401 HIS B CG  1 
ATOM   3129  N ND1 . HIS A 1 385 ? 1.772   33.303  102.521 1.00 61.89  ?  401 HIS B ND1 1 
ATOM   3130  C CD2 . HIS A 1 385 ? 2.064   35.309  103.327 1.00 64.58  ?  401 HIS B CD2 1 
ATOM   3131  C CE1 . HIS A 1 385 ? 0.804   34.062  102.044 1.00 63.13  ?  401 HIS B CE1 1 
ATOM   3132  N NE2 . HIS A 1 385 ? 0.966   35.285  102.510 1.00 62.44  ?  401 HIS B NE2 1 
ATOM   3133  N N   . GLU A 1 386 ? 5.392   31.417  105.550 1.00 72.97  ?  402 GLU B N   1 
ATOM   3134  C CA  . GLU A 1 386 ? 6.086   30.133  105.475 1.00 73.30  ?  402 GLU B CA  1 
ATOM   3135  C C   . GLU A 1 386 ? 5.705   29.210  106.642 1.00 74.77  ?  402 GLU B C   1 
ATOM   3136  O O   . GLU A 1 386 ? 5.610   27.986  106.461 1.00 78.08  ?  402 GLU B O   1 
ATOM   3137  C CB  . GLU A 1 386 ? 7.604   30.367  105.328 1.00 74.16  ?  402 GLU B CB  1 
ATOM   3138  C CG  . GLU A 1 386 ? 8.106   30.591  103.838 1.00 81.45  ?  402 GLU B CG  1 
ATOM   3139  C CD  . GLU A 1 386 ? 7.843   29.377  102.874 1.00 81.52  ?  402 GLU B CD  1 
ATOM   3140  O OE1 . GLU A 1 386 ? 8.405   28.313  103.213 1.00 90.27  ?  402 GLU B OE1 1 
ATOM   3141  O OE2 . GLU A 1 386 ? 7.176   29.447  101.793 1.00 68.18  -1 402 GLU B OE2 1 
ATOM   3142  N N   . ALA A 1 387 ? 5.385   29.775  107.809 1.00 62.72  ?  403 ALA B N   1 
ATOM   3143  C CA  . ALA A 1 387 ? 4.859   28.972  108.917 1.00 61.92  ?  403 ALA B CA  1 
ATOM   3144  C C   . ALA A 1 387 ? 3.512   28.332  108.563 1.00 65.01  ?  403 ALA B C   1 
ATOM   3145  O O   . ALA A 1 387 ? 3.282   27.134  108.816 1.00 70.64  ?  403 ALA B O   1 
ATOM   3146  C CB  . ALA A 1 387 ? 4.734   29.840  110.173 1.00 58.54  ?  403 ALA B CB  1 
ATOM   3147  N N   . VAL A 1 388 ? 2.595   29.124  107.992 1.00 66.11  ?  404 VAL B N   1 
ATOM   3148  C CA  . VAL A 1 388 ? 1.305   28.583  107.561 1.00 62.84  ?  404 VAL B CA  1 
ATOM   3149  C C   . VAL A 1 388 ? 1.515   27.441  106.572 1.00 65.51  ?  404 VAL B C   1 
ATOM   3150  O O   . VAL A 1 388 ? 0.870   26.391  106.665 1.00 68.96  ?  404 VAL B O   1 
ATOM   3151  C CB  . VAL A 1 388 ? 0.422   29.693  106.958 1.00 59.94  ?  404 VAL B CB  1 
ATOM   3152  C CG1 . VAL A 1 388 ? -0.717  29.080  106.153 1.00 63.91  ?  404 VAL B CG1 1 
ATOM   3153  C CG2 . VAL A 1 388 ? -0.106  30.652  108.038 1.00 58.66  ?  404 VAL B CG2 1 
ATOM   3154  N N   . GLY A 1 389 ? 2.431   27.623  105.620 1.00 66.15  ?  405 GLY B N   1 
ATOM   3155  C CA  . GLY A 1 389 ? 2.712   26.560  104.663 1.00 68.50  ?  405 GLY B CA  1 
ATOM   3156  C C   . GLY A 1 389 ? 3.296   25.319  105.314 1.00 69.23  ?  405 GLY B C   1 
ATOM   3157  O O   . GLY A 1 389 ? 2.988   24.191  104.910 1.00 70.66  ?  405 GLY B O   1 
ATOM   3158  N N   . GLU A 1 390 ? 4.128   25.506  106.343 1.00 73.18  ?  406 GLU B N   1 
ATOM   3159  C CA  . GLU A 1 390 ? 4.782   24.356  106.965 1.00 79.45  ?  406 GLU B CA  1 
ATOM   3160  C C   . GLU A 1 390 ? 3.788   23.464  107.706 1.00 82.45  ?  406 GLU B C   1 
ATOM   3161  O O   . GLU A 1 390 ? 3.908   22.229  107.663 1.00 86.93  ?  406 GLU B O   1 
ATOM   3162  C CB  . GLU A 1 390 ? 5.872   24.788  107.940 1.00 77.98  ?  406 GLU B CB  1 
ATOM   3163  C CG  . GLU A 1 390 ? 7.031   25.399  107.277 1.00 75.58  ?  406 GLU B CG  1 
ATOM   3164  C CD  . GLU A 1 390 ? 7.851   24.373  106.597 1.00 83.26  ?  406 GLU B CD  1 
ATOM   3165  O OE1 . GLU A 1 390 ? 7.806   23.188  107.015 1.00 92.74  ?  406 GLU B OE1 1 
ATOM   3166  O OE2 . GLU A 1 390 ? 8.521   24.775  105.623 1.00 84.79  -1 406 GLU B OE2 1 
ATOM   3167  N N   . ILE A 1 391 ? 2.832   24.065  108.431 1.00 72.31  ?  407 ILE B N   1 
ATOM   3168  C CA  . ILE A 1 391 ? 1.943   23.231  109.250 1.00 67.66  ?  407 ILE B CA  1 
ATOM   3169  C C   . ILE A 1 391 ? 1.027   22.372  108.384 1.00 70.84  ?  407 ILE B C   1 
ATOM   3170  O O   . ILE A 1 391 ? 0.554   21.313  108.833 1.00 72.26  ?  407 ILE B O   1 
ATOM   3171  C CB  . ILE A 1 391 ? 1.144   24.077  110.262 1.00 62.73  ?  407 ILE B CB  1 
ATOM   3172  C CG1 . ILE A 1 391 ? 0.137   24.983  109.576 1.00 61.87  ?  407 ILE B CG1 1 
ATOM   3173  C CG2 . ILE A 1 391 ? 2.035   24.920  111.100 1.00 65.13  ?  407 ILE B CG2 1 
ATOM   3174  C CD1 . ILE A 1 391 ? -0.609  25.833  110.557 1.00 56.90  ?  407 ILE B CD1 1 
ATOM   3175  N N   . MET A 1 392 ? 0.794   22.780  107.136 1.00 65.33  ?  408 MET B N   1 
ATOM   3176  C CA  . MET A 1 392 ? 0.028   21.939  106.227 1.00 65.43  ?  408 MET B CA  1 
ATOM   3177  C C   . MET A 1 392 ? 0.781   20.659  105.906 1.00 68.81  ?  408 MET B C   1 
ATOM   3178  O O   . MET A 1 392 ? 0.235   19.560  106.055 1.00 69.97  ?  408 MET B O   1 
ATOM   3179  C CB  . MET A 1 392 ? -0.325  22.710  104.951 1.00 67.59  ?  408 MET B CB  1 
ATOM   3180  C CG  . MET A 1 392 ? -0.927  24.075  105.245 1.00 64.52  ?  408 MET B CG  1 
ATOM   3181  S SD  . MET A 1 392 ? -2.253  23.836  106.435 1.00 61.85  ?  408 MET B SD  1 
ATOM   3182  C CE  . MET A 1 392 ? -2.564  25.498  107.027 1.00 58.89  ?  408 MET B CE  1 
ATOM   3183  N N   . SER A 1 393 ? 2.029   20.781  105.453 1.00 71.79  ?  409 SER B N   1 
ATOM   3184  C CA  . SER A 1 393 ? 2.847   19.591  105.228 1.00 75.75  ?  409 SER B CA  1 
ATOM   3185  C C   . SER A 1 393 ? 3.023   18.768  106.515 1.00 75.49  ?  409 SER B C   1 
ATOM   3186  O O   . SER A 1 393 ? 3.181   17.540  106.445 1.00 79.13  ?  409 SER B O   1 
ATOM   3187  C CB  . SER A 1 393 ? 4.186   20.009  104.564 1.00 76.50  ?  409 SER B CB  1 
ATOM   3188  O OG  . SER A 1 393 ? 5.329   20.147  105.413 1.00 71.88  ?  409 SER B OG  1 
ATOM   3189  N N   . LEU A 1 394 ? 2.944   19.394  107.698 1.00 76.33  ?  410 LEU B N   1 
ATOM   3190  C CA  . LEU A 1 394 ? 3.002   18.589  108.927 1.00 75.38  ?  410 LEU B CA  1 
ATOM   3191  C C   . LEU A 1 394 ? 1.788   17.686  109.053 1.00 78.05  ?  410 LEU B C   1 
ATOM   3192  O O   . LEU A 1 394 ? 1.916   16.465  109.201 1.00 79.08  ?  410 LEU B O   1 
ATOM   3193  C CB  . LEU A 1 394 ? 3.111   19.448  110.188 1.00 71.04  ?  410 LEU B CB  1 
ATOM   3194  C CG  . LEU A 1 394 ? 4.385   20.205  110.489 1.00 69.54  ?  410 LEU B CG  1 
ATOM   3195  C CD1 . LEU A 1 394 ? 4.243   20.627  111.923 1.00 68.42  ?  410 LEU B CD1 1 
ATOM   3196  C CD2 . LEU A 1 394 ? 5.637   19.370  110.253 1.00 70.52  ?  410 LEU B CD2 1 
ATOM   3197  N N   . SER A 1 395 ? 0.597   18.286  109.036 1.00 76.88  ?  411 SER B N   1 
ATOM   3198  C CA  . SER A 1 395 ? -0.639  17.507  109.039 1.00 78.01  ?  411 SER B CA  1 
ATOM   3199  C C   . SER A 1 395 ? -0.632  16.453  107.931 1.00 79.60  ?  411 SER B C   1 
ATOM   3200  O O   . SER A 1 395 ? -1.072  15.317  108.136 1.00 83.28  ?  411 SER B O   1 
ATOM   3201  C CB  . SER A 1 395 ? -1.831  18.450  108.869 1.00 74.08  ?  411 SER B CB  1 
ATOM   3202  O OG  . SER A 1 395 ? -2.219  19.019  110.103 1.00 75.21  ?  411 SER B OG  1 
ATOM   3203  N N   . ALA A 1 396 ? -0.107  16.811  106.754 1.00 82.95  ?  412 ALA B N   1 
ATOM   3204  C CA  . ALA A 1 396 ? -0.203  15.998  105.547 1.00 83.84  ?  412 ALA B CA  1 
ATOM   3205  C C   . ALA A 1 396 ? 0.740   14.811  105.524 1.00 86.71  ?  412 ALA B C   1 
ATOM   3206  O O   . ALA A 1 396 ? 0.478   13.865  104.775 1.00 88.49  ?  412 ALA B O   1 
ATOM   3207  C CB  . ALA A 1 396 ? 0.086   16.855  104.311 1.00 82.25  ?  412 ALA B CB  1 
ATOM   3208  N N   . ALA A 1 397 ? 1.853   14.874  106.264 1.00 97.83  ?  413 ALA B N   1 
ATOM   3209  C CA  . ALA A 1 397 ? 2.860   13.821  106.269 1.00 97.29  ?  413 ALA B CA  1 
ATOM   3210  C C   . ALA A 1 397 ? 2.650   12.791  107.372 1.00 101.18 ?  413 ALA B C   1 
ATOM   3211  O O   . ALA A 1 397 ? 3.415   11.825  107.449 1.00 102.18 ?  413 ALA B O   1 
ATOM   3212  C CB  . ALA A 1 397 ? 4.257   14.432  106.402 1.00 96.25  ?  413 ALA B CB  1 
ATOM   3213  N N   . THR A 1 398 ? 1.646   12.963  108.227 1.00 91.69  ?  414 THR B N   1 
ATOM   3214  C CA  . THR A 1 398 ? 1.449   12.012  109.308 1.00 93.16  ?  414 THR B CA  1 
ATOM   3215  C C   . THR A 1 398 ? 0.913   10.695  108.756 1.00 96.23  ?  414 THR B C   1 
ATOM   3216  O O   . THR A 1 398 ? 0.301   10.670  107.687 1.00 97.79  ?  414 THR B O   1 
ATOM   3217  C CB  . THR A 1 398 ? 0.472   12.563  110.332 1.00 90.77  ?  414 THR B CB  1 
ATOM   3218  O OG1 . THR A 1 398 ? -0.814  12.689  109.719 1.00 90.59  ?  414 THR B OG1 1 
ATOM   3219  C CG2 . THR A 1 398 ? 0.931   13.930  110.807 1.00 90.30  ?  414 THR B CG2 1 
ATOM   3220  N N   . PRO A 1 399 ? 1.138   9.578   109.461 1.00 96.70  ?  415 PRO B N   1 
ATOM   3221  C CA  . PRO A 1 399 ? 0.523   8.324   109.011 1.00 99.62  ?  415 PRO B CA  1 
ATOM   3222  C C   . PRO A 1 399 ? -0.993  8.351   109.070 1.00 102.80 ?  415 PRO B C   1 
ATOM   3223  O O   . PRO A 1 399 ? -1.624  7.828   108.145 1.00 105.48 ?  415 PRO B O   1 
ATOM   3224  C CB  . PRO A 1 399 ? 1.106   7.278   109.965 1.00 96.77  ?  415 PRO B CB  1 
ATOM   3225  C CG  . PRO A 1 399 ? 2.335   7.851   110.450 1.00 91.21  ?  415 PRO B CG  1 
ATOM   3226  C CD  . PRO A 1 399 ? 2.133   9.339   110.510 1.00 90.33  ?  415 PRO B CD  1 
ATOM   3227  N N   . LYS A 1 400 ? -1.600  8.929   110.121 1.00 93.39  ?  416 LYS B N   1 
ATOM   3228  C CA  . LYS A 1 400 ? -3.063  9.008   110.189 1.00 94.13  ?  416 LYS B CA  1 
ATOM   3229  C C   . LYS A 1 400 ? -3.636  9.529   108.873 1.00 95.34  ?  416 LYS B C   1 
ATOM   3230  O O   . LYS A 1 400 ? -4.511  8.894   108.257 1.00 97.52  ?  416 LYS B O   1 
ATOM   3231  C CB  . LYS A 1 400 ? -3.492  9.886   111.379 1.00 97.22  ?  416 LYS B CB  1 
ATOM   3232  C CG  . LYS A 1 400 ? -5.020  9.868   111.700 1.00 103.49 ?  416 LYS B CG  1 
ATOM   3233  C CD  . LYS A 1 400 ? -5.546  11.156  112.407 1.00 104.09 ?  416 LYS B CD  1 
ATOM   3234  C CE  . LYS A 1 400 ? -4.974  11.311  113.842 1.00 103.29 ?  416 LYS B CE  1 
ATOM   3235  N NZ  . LYS A 1 400 ? -5.335  12.598  114.537 1.00 95.51  ?  416 LYS B NZ  1 
ATOM   3236  N N   . HIS A 1 401 ? -3.067  10.645  108.387 1.00 93.44  ?  417 HIS B N   1 
ATOM   3237  C CA  . HIS A 1 401 ? -3.467  11.254  107.114 1.00 92.88  ?  417 HIS B CA  1 
ATOM   3238  C C   . HIS A 1 401 ? -3.188  10.352  105.918 1.00 94.72  ?  417 HIS B C   1 
ATOM   3239  O O   . HIS A 1 401 ? -4.049  10.182  105.045 1.00 97.37  ?  417 HIS B O   1 
ATOM   3240  C CB  . HIS A 1 401 ? -2.741  12.587  106.924 1.00 87.49  ?  417 HIS B CB  1 
ATOM   3241  C CG  . HIS A 1 401 ? -3.216  13.368  105.736 1.00 82.45  ?  417 HIS B CG  1 
ATOM   3242  N ND1 . HIS A 1 401 ? -4.297  14.220  105.779 1.00 77.51  ?  417 HIS B ND1 1 
ATOM   3243  C CD2 . HIS A 1 401 ? -2.742  13.424  104.466 1.00 82.33  ?  417 HIS B CD2 1 
ATOM   3244  C CE1 . HIS A 1 401 ? -4.472  14.765  104.586 1.00 77.65  ?  417 HIS B CE1 1 
ATOM   3245  N NE2 . HIS A 1 401 ? -3.541  14.302  103.772 1.00 79.69  ?  417 HIS B NE2 1 
ATOM   3246  N N   . LEU A 1 402 ? -1.964  9.829   105.823 1.00 98.98  ?  418 LEU B N   1 
ATOM   3247  C CA  . LEU A 1 402 ? -1.581  9.019   104.670 1.00 100.74 ?  418 LEU B CA  1 
ATOM   3248  C C   . LEU A 1 402 ? -2.474  7.796   104.524 1.00 104.19 ?  418 LEU B C   1 
ATOM   3249  O O   . LEU A 1 402 ? -2.822  7.396   103.405 1.00 107.36 ?  418 LEU B O   1 
ATOM   3250  C CB  . LEU A 1 402 ? -0.121  8.610   104.812 1.00 105.22 ?  418 LEU B CB  1 
ATOM   3251  C CG  . LEU A 1 402 ? 0.799   9.820   104.814 1.00 97.09  ?  418 LEU B CG  1 
ATOM   3252  C CD1 . LEU A 1 402 ? 2.205   9.397   105.158 1.00 94.24  ?  418 LEU B CD1 1 
ATOM   3253  C CD2 . LEU A 1 402 ? 0.730   10.462  103.421 1.00 92.37  ?  418 LEU B CD2 1 
ATOM   3254  N N   . LYS A 1 403 ? -2.844  7.187   105.649 1.00 109.67 ?  419 LYS B N   1 
ATOM   3255  C CA  . LYS A 1 403 ? -3.820  6.109   105.636 1.00 111.89 ?  419 LYS B CA  1 
ATOM   3256  C C   . LYS A 1 403 ? -5.158  6.611   105.111 1.00 107.32 ?  419 LYS B C   1 
ATOM   3257  O O   . LYS A 1 403 ? -5.676  6.093   104.116 1.00 107.49 ?  419 LYS B O   1 
ATOM   3258  C CB  . LYS A 1 403 ? -3.962  5.529   107.041 1.00 112.37 ?  419 LYS B CB  1 
ATOM   3259  C CG  . LYS A 1 403 ? -2.747  4.730   107.484 1.00 119.14 ?  419 LYS B CG  1 
ATOM   3260  C CD  . LYS A 1 403 ? -2.958  4.093   108.849 1.00 121.59 ?  419 LYS B CD  1 
ATOM   3261  C CE  . LYS A 1 403 ? -1.808  3.169   109.180 1.00 128.31 ?  419 LYS B CE  1 
ATOM   3262  N NZ  . LYS A 1 403 ? -2.119  2.337   110.363 1.00 134.32 ?  419 LYS B NZ  1 
ATOM   3263  N N   . SER A 1 404 ? -5.711  7.663   105.741 1.00 107.66 ?  420 SER B N   1 
ATOM   3264  C CA  . SER A 1 404 ? -7.033  8.139   105.319 1.00 106.85 ?  420 SER B CA  1 
ATOM   3265  C C   . SER A 1 404 ? -7.110  8.385   103.812 1.00 103.40 ?  420 SER B C   1 
ATOM   3266  O O   . SER A 1 404 ? -8.142  8.094   103.195 1.00 109.66 ?  420 SER B O   1 
ATOM   3267  C CB  . SER A 1 404 ? -7.442  9.393   106.119 1.00 106.12 ?  420 SER B CB  1 
ATOM   3268  O OG  . SER A 1 404 ? -8.846  9.618   106.013 1.00 103.22 ?  420 SER B OG  1 
ATOM   3269  N N   . ILE A 1 405 ? -6.041  8.892   103.199 1.00 101.91 ?  421 ILE B N   1 
ATOM   3270  C CA  . ILE A 1 405 ? -6.053  9.124   101.756 1.00 103.59 ?  421 ILE B CA  1 
ATOM   3271  C C   . ILE A 1 405 ? -5.641  7.883   100.990 1.00 110.98 ?  421 ILE B C   1 
ATOM   3272  O O   . ILE A 1 405 ? -5.335  7.965   99.807  1.00 114.27 ?  421 ILE B O   1 
ATOM   3273  C CB  . ILE A 1 405 ? -5.199  10.319  101.341 1.00 98.31  ?  421 ILE B CB  1 
ATOM   3274  C CG1 . ILE A 1 405 ? -3.777  10.182  101.764 1.00 102.50 ?  421 ILE B CG1 1 
ATOM   3275  C CG2 . ILE A 1 405 ? -5.611  11.510  102.122 1.00 95.70  ?  421 ILE B CG2 1 
ATOM   3276  C CD1 . ILE A 1 405 ? -2.884  11.121  100.999 1.00 101.78 ?  421 ILE B CD1 1 
ATOM   3277  N N   . GLY A 1 406 ? -5.582  6.739   101.643 1.00 113.18 ?  422 GLY B N   1 
ATOM   3278  C CA  . GLY A 1 406 ? -5.299  5.500   100.941 1.00 118.91 ?  422 GLY B CA  1 
ATOM   3279  C C   . GLY A 1 406 ? -3.933  5.355   100.288 1.00 120.42 ?  422 GLY B C   1 
ATOM   3280  O O   . GLY A 1 406 ? -3.732  4.422   99.503  1.00 121.16 ?  422 GLY B O   1 
ATOM   3281  N N   . LEU A 1 407 ? -2.981  6.233   100.576 1.00 125.73 ?  423 LEU B N   1 
ATOM   3282  C CA  . LEU A 1 407 ? -1.613  6.004   100.122 1.00 125.13 ?  423 LEU B CA  1 
ATOM   3283  C C   . LEU A 1 407 ? -0.828  5.112   101.063 1.00 131.38 ?  423 LEU B C   1 
ATOM   3284  O O   . LEU A 1 407 ? 0.228   4.597   100.682 1.00 132.01 ?  423 LEU B O   1 
ATOM   3285  C CB  . LEU A 1 407 ? -0.874  7.329   99.953  1.00 121.25 ?  423 LEU B CB  1 
ATOM   3286  C CG  . LEU A 1 407 ? -1.379  8.065   98.724  1.00 123.37 ?  423 LEU B CG  1 
ATOM   3287  C CD1 . LEU A 1 407 ? -0.744  9.435   98.596  1.00 120.48 ?  423 LEU B CD1 1 
ATOM   3288  C CD2 . LEU A 1 407 ? -1.149  7.210   97.500  1.00 124.75 ?  423 LEU B CD2 1 
ATOM   3289  N N   . LEU A 1 408 ? -1.317  4.931   102.283 1.00 128.73 ?  424 LEU B N   1 
ATOM   3290  C CA  . LEU A 1 408 ? -0.746  3.993   103.231 1.00 131.43 ?  424 LEU B CA  1 
ATOM   3291  C C   . LEU A 1 408 ? -1.767  2.901   103.550 1.00 136.86 ?  424 LEU B C   1 
ATOM   3292  O O   . LEU A 1 408 ? -2.984  3.112   103.470 1.00 129.59 ?  424 LEU B O   1 
ATOM   3293  C CB  . LEU A 1 408 ? -0.295  4.710   104.508 1.00 121.38 ?  424 LEU B CB  1 
ATOM   3294  C CG  . LEU A 1 408 ? 0.641   3.845   105.331 1.00 121.99 ?  424 LEU B CG  1 
ATOM   3295  C CD1 . LEU A 1 408 ? 1.718   3.382   104.398 1.00 126.14 ?  424 LEU B CD1 1 
ATOM   3296  C CD2 . LEU A 1 408 ? 1.222   4.649   106.461 1.00 120.66 ?  424 LEU B CD2 1 
ATOM   3297  N N   . SER A 1 409 ? -1.250  1.713   103.889 1.00 140.93 ?  425 SER B N   1 
ATOM   3298  C CA  . SER A 1 409 ? -2.054  0.525   104.139 1.00 144.38 ?  425 SER B CA  1 
ATOM   3299  C C   . SER A 1 409 ? -2.384  0.397   105.620 1.00 147.71 ?  425 SER B C   1 
ATOM   3300  O O   . SER A 1 409 ? -1.452  0.398   106.440 1.00 143.70 ?  425 SER B O   1 
ATOM   3301  C CB  . SER A 1 409 ? -1.292  -0.707  103.672 1.00 146.06 ?  425 SER B CB  1 
ATOM   3302  O OG  . SER A 1 409 ? -2.047  -1.875  103.898 1.00 157.50 ?  425 SER B OG  1 
ATOM   3303  N N   . PRO A 1 410 ? -3.700  0.239   106.017 1.00 154.43 ?  426 PRO B N   1 
ATOM   3304  C CA  . PRO A 1 410 ? -4.043  0.143   107.452 1.00 154.18 ?  426 PRO B CA  1 
ATOM   3305  C C   . PRO A 1 410 ? -3.217  -0.893  108.201 1.00 155.61 ?  426 PRO B C   1 
ATOM   3306  O O   . PRO A 1 410 ? -3.098  -0.835  109.430 1.00 155.18 ?  426 PRO B O   1 
ATOM   3307  C CB  . PRO A 1 410 ? -5.540  -0.223  107.439 1.00 150.47 ?  426 PRO B CB  1 
ATOM   3308  C CG  . PRO A 1 410 ? -6.041  0.272   106.135 1.00 151.18 ?  426 PRO B CG  1 
ATOM   3309  C CD  . PRO A 1 410 ? -4.893  0.066   105.165 1.00 153.03 ?  426 PRO B CD  1 
ATOM   3310  N N   . ASP A 1 411 ? -2.615  -1.833  107.466 1.00 152.50 ?  427 ASP B N   1 
ATOM   3311  C CA  . ASP A 1 411 ? -1.671  -2.789  108.031 1.00 150.85 ?  427 ASP B CA  1 
ATOM   3312  C C   . ASP A 1 411 ? -0.240  -2.247  108.084 1.00 151.56 ?  427 ASP B C   1 
ATOM   3313  O O   . ASP A 1 411 ? 0.711   -3.018  107.904 1.00 151.83 ?  427 ASP B O   1 
ATOM   3314  C CB  . ASP A 1 411 ? -1.705  -4.108  107.250 1.00 147.73 ?  427 ASP B CB  1 
ATOM   3315  C CG  . ASP A 1 411 ? -3.113  -4.533  106.859 1.00 149.04 ?  427 ASP B CG  1 
ATOM   3316  O OD1 . ASP A 1 411 ? -4.065  -4.179  107.579 1.00 150.21 ?  427 ASP B OD1 1 
ATOM   3317  O OD2 . ASP A 1 411 ? -3.272  -5.220  105.824 1.00 145.55 -1 427 ASP B OD2 1 
ATOM   3318  N N   . PHE A 1 412 ? -0.054  -0.948  108.318 1.00 148.20 ?  428 PHE B N   1 
ATOM   3319  C CA  . PHE A 1 412 ? 1.255   -0.384  108.648 1.00 140.37 ?  428 PHE B CA  1 
ATOM   3320  C C   . PHE A 1 412 ? 1.374   -0.167  110.149 1.00 138.44 ?  428 PHE B C   1 
ATOM   3321  O O   . PHE A 1 412 ? 0.525   0.492   110.760 1.00 138.71 ?  428 PHE B O   1 
ATOM   3322  C CB  . PHE A 1 412 ? 1.510   0.937   107.921 1.00 136.25 ?  428 PHE B CB  1 
ATOM   3323  C CG  . PHE A 1 412 ? 2.917   1.455   108.081 1.00 133.89 ?  428 PHE B CG  1 
ATOM   3324  C CD1 . PHE A 1 412 ? 3.249   2.289   109.142 1.00 135.46 ?  428 PHE B CD1 1 
ATOM   3325  C CD2 . PHE A 1 412 ? 3.911   1.087   107.195 1.00 129.05 ?  428 PHE B CD2 1 
ATOM   3326  C CE1 . PHE A 1 412 ? 4.544   2.770   109.289 1.00 131.09 ?  428 PHE B CE1 1 
ATOM   3327  C CE2 . PHE A 1 412 ? 5.209   1.562   107.340 1.00 128.85 ?  428 PHE B CE2 1 
ATOM   3328  C CZ  . PHE A 1 412 ? 5.523   2.402   108.391 1.00 127.61 ?  428 PHE B CZ  1 
ATOM   3329  N N   . GLN A 1 413 ? 2.444   -0.691  110.728 1.00 139.95 ?  429 GLN B N   1 
ATOM   3330  C CA  . GLN A 1 413 ? 2.662   -0.651  112.166 1.00 139.71 ?  429 GLN B CA  1 
ATOM   3331  C C   . GLN A 1 413 ? 3.561   0.530   112.488 1.00 138.21 ?  429 GLN B C   1 
ATOM   3332  O O   . GLN A 1 413 ? 4.755   0.512   112.177 1.00 137.06 ?  429 GLN B O   1 
ATOM   3333  C CB  . GLN A 1 413 ? 3.287   -1.958  112.653 1.00 143.06 ?  429 GLN B CB  1 
ATOM   3334  C CG  . GLN A 1 413 ? 3.574   -2.046  114.164 1.00 148.19 ?  429 GLN B CG  1 
ATOM   3335  C CD  . GLN A 1 413 ? 2.332   -2.122  115.059 1.00 147.17 ?  429 GLN B CD  1 
ATOM   3336  O OE1 . GLN A 1 413 ? 1.251   -1.653  114.706 1.00 143.35 ?  429 GLN B OE1 1 
ATOM   3337  N NE2 . GLN A 1 413 ? 2.505   -2.699  116.245 1.00 142.34 ?  429 GLN B NE2 1 
ATOM   3338  N N   . GLU A 1 414 ? 2.989   1.562   113.094 1.00 149.83 ?  430 GLU B N   1 
ATOM   3339  C CA  . GLU A 1 414 ? 3.807   2.563   113.753 1.00 141.41 ?  430 GLU B CA  1 
ATOM   3340  C C   . GLU A 1 414 ? 4.237   2.031   115.110 1.00 145.62 ?  430 GLU B C   1 
ATOM   3341  O O   . GLU A 1 414 ? 3.495   1.297   115.765 1.00 154.18 ?  430 GLU B O   1 
ATOM   3342  C CB  . GLU A 1 414 ? 3.061   3.890   113.907 1.00 134.13 ?  430 GLU B CB  1 
ATOM   3343  C CG  . GLU A 1 414 ? 2.268   4.322   112.697 1.00 129.88 ?  430 GLU B CG  1 
ATOM   3344  C CD  . GLU A 1 414 ? 1.052   5.140   113.069 1.00 125.63 ?  430 GLU B CD  1 
ATOM   3345  O OE1 . GLU A 1 414 ? 1.146   5.916   114.050 1.00 119.58 ?  430 GLU B OE1 1 
ATOM   3346  O OE2 . GLU A 1 414 ? 0.019   5.021   112.362 1.00 120.47 -1 430 GLU B OE2 1 
ATOM   3347  N N   . ASP A 1 415 ? 5.450   2.387   115.517 1.00 141.97 ?  431 ASP B N   1 
ATOM   3348  C CA  . ASP A 1 415 ? 6.008   1.936   116.781 1.00 135.87 ?  431 ASP B CA  1 
ATOM   3349  C C   . ASP A 1 415 ? 6.894   3.058   117.306 1.00 131.23 ?  431 ASP B C   1 
ATOM   3350  O O   . ASP A 1 415 ? 7.026   4.110   116.670 1.00 125.44 ?  431 ASP B O   1 
ATOM   3351  C CB  . ASP A 1 415 ? 6.704   0.563   116.598 1.00 136.57 ?  431 ASP B CB  1 
ATOM   3352  C CG  . ASP A 1 415 ? 8.021   0.648   115.832 1.00 131.68 ?  431 ASP B CG  1 
ATOM   3353  O OD1 . ASP A 1 415 ? 8.154   1.555   114.985 1.00 134.47 ?  431 ASP B OD1 1 
ATOM   3354  O OD2 . ASP A 1 415 ? 8.904   -0.220  116.026 1.00 133.62 -1 431 ASP B OD2 1 
ATOM   3355  N N   . ASN A 1 416 ? 7.431   2.864   118.514 1.00 134.46 ?  432 ASN B N   1 
ATOM   3356  C CA  . ASN A 1 416 ? 8.432   3.792   119.050 1.00 126.73 ?  432 ASN B CA  1 
ATOM   3357  C C   . ASN A 1 416 ? 9.492   4.086   118.017 1.00 129.01 ?  432 ASN B C   1 
ATOM   3358  O O   . ASN A 1 416 ? 9.867   5.237   117.797 1.00 123.70 ?  432 ASN B O   1 
ATOM   3359  C CB  . ASN A 1 416 ? 9.167   3.205   120.239 1.00 122.53 ?  432 ASN B CB  1 
ATOM   3360  C CG  . ASN A 1 416 ? 8.287   2.431   121.163 1.00 126.31 ?  432 ASN B CG  1 
ATOM   3361  O OD1 . ASN A 1 416 ? 7.069   2.400   121.027 1.00 126.45 ?  432 ASN B OD1 1 
ATOM   3362  N ND2 . ASN A 1 416 ? 8.942   1.739   122.090 1.00 128.85 ?  432 ASN B ND2 1 
ATOM   3363  N N   . GLU A 1 417 ? 9.998   3.028   117.391 1.00 150.33 ?  433 GLU B N   1 
ATOM   3364  C CA  . GLU A 1 417 ? 11.193  3.130   116.576 1.00 144.43 ?  433 GLU B CA  1 
ATOM   3365  C C   . GLU A 1 417 ? 10.960  3.989   115.343 1.00 138.83 ?  433 GLU B C   1 
ATOM   3366  O O   . GLU A 1 417 ? 11.701  4.950   115.102 1.00 132.01 ?  433 GLU B O   1 
ATOM   3367  C CB  . GLU A 1 417 ? 11.692  1.734   116.187 1.00 147.41 ?  433 GLU B CB  1 
ATOM   3368  C CG  . GLU A 1 417 ? 12.126  0.911   117.379 1.00 148.99 ?  433 GLU B CG  1 
ATOM   3369  C CD  . GLU A 1 417 ? 13.025  -0.256  116.988 1.00 154.44 ?  433 GLU B CD  1 
ATOM   3370  O OE1 . GLU A 1 417 ? 13.378  -0.371  115.788 1.00 157.65 ?  433 GLU B OE1 1 
ATOM   3371  O OE2 . GLU A 1 417 ? 13.411  -1.033  117.891 1.00 153.66 -1 433 GLU B OE2 1 
ATOM   3372  N N   . THR A 1 418 ? 9.980   3.629   114.513 1.00 129.92 ?  434 THR B N   1 
ATOM   3373  C CA  . THR A 1 418 ? 9.741   4.420   113.306 1.00 119.87 ?  434 THR B CA  1 
ATOM   3374  C C   . THR A 1 418 ? 9.428   5.858   113.666 1.00 118.39 ?  434 THR B C   1 
ATOM   3375  O O   . THR A 1 418 ? 9.813   6.780   112.941 1.00 117.90 ?  434 THR B O   1 
ATOM   3376  C CB  . THR A 1 418 ? 8.603   3.847   112.459 1.00 117.31 ?  434 THR B CB  1 
ATOM   3377  O OG1 . THR A 1 418 ? 7.488   3.561   113.306 1.00 117.59 ?  434 THR B OG1 1 
ATOM   3378  C CG2 . THR A 1 418 ? 9.043   2.580   111.697 1.00 120.36 ?  434 THR B CG2 1 
ATOM   3379  N N   . GLU A 1 419 ? 8.778   6.069   114.809 1.00 122.58 ?  435 GLU B N   1 
ATOM   3380  C CA  . GLU A 1 419 ? 8.466   7.434   115.204 1.00 113.79 ?  435 GLU B CA  1 
ATOM   3381  C C   . GLU A 1 419 ? 9.682   8.204   115.709 1.00 105.70 ?  435 GLU B C   1 
ATOM   3382  O O   . GLU A 1 419 ? 9.795   9.407   115.435 1.00 99.69  ?  435 GLU B O   1 
ATOM   3383  C CB  . GLU A 1 419 ? 7.320   7.438   116.207 1.00 116.84 ?  435 GLU B CB  1 
ATOM   3384  C CG  . GLU A 1 419 ? 6.035   7.082   115.501 1.00 123.54 ?  435 GLU B CG  1 
ATOM   3385  C CD  . GLU A 1 419 ? 4.850   7.077   116.405 1.00 123.09 ?  435 GLU B CD  1 
ATOM   3386  O OE1 . GLU A 1 419 ? 4.870   7.809   117.417 1.00 122.55 ?  435 GLU B OE1 1 
ATOM   3387  O OE2 . GLU A 1 419 ? 3.881   6.377   116.073 1.00 127.46 -1 435 GLU B OE2 1 
ATOM   3388  N N   . ILE A 1 420 ? 10.608  7.546   116.409 1.00 103.72 ?  436 ILE B N   1 
ATOM   3389  C CA  . ILE A 1 420 ? 11.895  8.178   116.718 1.00 99.36  ?  436 ILE B CA  1 
ATOM   3390  C C   . ILE A 1 420 ? 12.656  8.462   115.435 1.00 95.21  ?  436 ILE B C   1 
ATOM   3391  O O   . ILE A 1 420 ? 13.345  9.482   115.322 1.00 90.09  ?  436 ILE B O   1 
ATOM   3392  C CB  . ILE A 1 420 ? 12.735  7.308   117.675 1.00 98.72  ?  436 ILE B CB  1 
ATOM   3393  C CG1 . ILE A 1 420 ? 12.132  7.250   119.082 1.00 93.87  ?  436 ILE B CG1 1 
ATOM   3394  C CG2 . ILE A 1 420 ? 14.201  7.775   117.724 1.00 90.61  ?  436 ILE B CG2 1 
ATOM   3395  C CD1 . ILE A 1 420 ? 12.249  8.533   119.866 1.00 86.17  ?  436 ILE B CD1 1 
ATOM   3396  N N   . ASN A 1 421 ? 12.559  7.551   114.458 1.00 91.95  ?  437 ASN B N   1 
ATOM   3397  C CA  . ASN A 1 421 ? 13.229  7.749   113.178 1.00 89.17  ?  437 ASN B CA  1 
ATOM   3398  C C   . ASN A 1 421 ? 12.732  9.040   112.546 1.00 88.88  ?  437 ASN B C   1 
ATOM   3399  O O   . ASN A 1 421 ? 13.520  9.923   112.160 1.00 86.06  ?  437 ASN B O   1 
ATOM   3400  C CB  . ASN A 1 421 ? 12.944  6.572   112.226 1.00 95.38  ?  437 ASN B CB  1 
ATOM   3401  C CG  . ASN A 1 421 ? 13.817  5.322   112.484 1.00 95.92  ?  437 ASN B CG  1 
ATOM   3402  O OD1 . ASN A 1 421 ? 14.646  5.293   113.387 1.00 93.99  ?  437 ASN B OD1 1 
ATOM   3403  N ND2 . ASN A 1 421 ? 13.671  4.314   111.620 1.00 104.59 ?  437 ASN B ND2 1 
ATOM   3404  N N   . PHE A 1 422 ? 11.403  9.164   112.481 1.00 90.68  ?  438 PHE B N   1 
ATOM   3405  C CA  . PHE A 1 422 ? 10.737  10.345  111.960 1.00 86.39  ?  438 PHE B CA  1 
ATOM   3406  C C   . PHE A 1 422 ? 11.134  11.607  112.717 1.00 82.13  ?  438 PHE B C   1 
ATOM   3407  O O   . PHE A 1 422 ? 11.641  12.560  112.114 1.00 80.02  ?  438 PHE B O   1 
ATOM   3408  C CB  . PHE A 1 422 ? 9.230   10.103  111.985 1.00 89.30  ?  438 PHE B CB  1 
ATOM   3409  C CG  . PHE A 1 422 ? 8.421   11.331  111.768 1.00 91.52  ?  438 PHE B CG  1 
ATOM   3410  C CD1 . PHE A 1 422 ? 8.332   11.908  110.510 1.00 85.76  ?  438 PHE B CD1 1 
ATOM   3411  C CD2 . PHE A 1 422 ? 7.659   11.850  112.803 1.00 89.63  ?  438 PHE B CD2 1 
ATOM   3412  C CE1 . PHE A 1 422 ? 7.589   13.033  110.315 1.00 84.27  ?  438 PHE B CE1 1 
ATOM   3413  C CE2 . PHE A 1 422 ? 6.891   12.965  112.609 1.00 86.54  ?  438 PHE B CE2 1 
ATOM   3414  C CZ  . PHE A 1 422 ? 6.854   13.560  111.365 1.00 87.81  ?  438 PHE B CZ  1 
ATOM   3415  N N   . LEU A 1 423 ? 10.905  11.635  114.033 1.00 81.16  ?  439 LEU B N   1 
ATOM   3416  C CA  . LEU A 1 423 ? 11.280  12.784  114.860 1.00 80.46  ?  439 LEU B CA  1 
ATOM   3417  C C   . LEU A 1 423 ? 12.767  13.163  114.765 1.00 81.13  ?  439 LEU B C   1 
ATOM   3418  O O   . LEU A 1 423 ? 13.117  14.347  114.867 1.00 80.58  ?  439 LEU B O   1 
ATOM   3419  C CB  . LEU A 1 423 ? 10.909  12.486  116.303 1.00 81.18  ?  439 LEU B CB  1 
ATOM   3420  C CG  . LEU A 1 423 ? 9.454   12.711  116.642 1.00 79.45  ?  439 LEU B CG  1 
ATOM   3421  C CD1 . LEU A 1 423 ? 9.205   12.439  118.105 1.00 78.25  ?  439 LEU B CD1 1 
ATOM   3422  C CD2 . LEU A 1 423 ? 9.219   14.164  116.354 1.00 80.05  ?  439 LEU B CD2 1 
ATOM   3423  N N   . LEU A 1 424 ? 13.663  12.187  114.579 1.00 81.18  ?  440 LEU B N   1 
ATOM   3424  C CA  . LEU A 1 424 ? 15.080  12.505  114.453 1.00 75.37  ?  440 LEU B CA  1 
ATOM   3425  C C   . LEU A 1 424 ? 15.357  13.156  113.107 1.00 73.75  ?  440 LEU B C   1 
ATOM   3426  O O   . LEU A 1 424 ? 16.109  14.132  113.016 1.00 72.38  ?  440 LEU B O   1 
ATOM   3427  C CB  . LEU A 1 424 ? 15.916  11.234  114.626 1.00 76.54  ?  440 LEU B CB  1 
ATOM   3428  C CG  . LEU A 1 424 ? 17.455  11.263  114.774 1.00 72.62  ?  440 LEU B CG  1 
ATOM   3429  C CD1 . LEU A 1 424 ? 18.205  11.229  113.454 1.00 72.89  ?  440 LEU B CD1 1 
ATOM   3430  C CD2 . LEU A 1 424 ? 17.910  12.439  115.617 1.00 67.58  ?  440 LEU B CD2 1 
ATOM   3431  N N   . LYS A 1 425 ? 14.770  12.617  112.040 1.00 73.23  ?  441 LYS B N   1 
ATOM   3432  C CA  . LYS A 1 425 ? 14.882  13.292  110.753 1.00 72.46  ?  441 LYS B CA  1 
ATOM   3433  C C   . LYS A 1 425 ? 14.378  14.727  110.879 1.00 72.01  ?  441 LYS B C   1 
ATOM   3434  O O   . LYS A 1 425 ? 15.044  15.694  110.458 1.00 67.57  ?  441 LYS B O   1 
ATOM   3435  C CB  . LYS A 1 425 ? 14.092  12.526  109.692 1.00 73.26  ?  441 LYS B CB  1 
ATOM   3436  C CG  . LYS A 1 425 ? 14.353  13.047  108.297 1.00 79.18  ?  441 LYS B CG  1 
ATOM   3437  C CD  . LYS A 1 425 ? 13.789  12.128  107.212 1.00 89.12  ?  441 LYS B CD  1 
ATOM   3438  C CE  . LYS A 1 425 ? 14.477  12.361  105.866 1.00 91.91  ?  441 LYS B CE  1 
ATOM   3439  N NZ  . LYS A 1 425 ? 14.390  11.148  105.019 1.00 98.63  ?  441 LYS B NZ  1 
ATOM   3440  N N   . GLN A 1 426 ? 13.203  14.868  111.518 1.00 71.68  ?  442 GLN B N   1 
ATOM   3441  C CA  . GLN A 1 426 ? 12.591  16.174  111.741 1.00 69.82  ?  442 GLN B CA  1 
ATOM   3442  C C   . GLN A 1 426 ? 13.522  17.098  112.492 1.00 70.00  ?  442 GLN B C   1 
ATOM   3443  O O   . GLN A 1 426 ? 13.553  18.293  112.201 1.00 70.36  ?  442 GLN B O   1 
ATOM   3444  C CB  . GLN A 1 426 ? 11.272  16.068  112.517 1.00 71.69  ?  442 GLN B CB  1 
ATOM   3445  C CG  . GLN A 1 426 ? 10.129  15.471  111.744 1.00 76.27  ?  442 GLN B CG  1 
ATOM   3446  C CD  . GLN A 1 426 ? 9.634   16.435  110.704 1.00 74.71  ?  442 GLN B CD  1 
ATOM   3447  O OE1 . GLN A 1 426 ? 10.177  16.458  109.597 1.00 73.35  ?  442 GLN B OE1 1 
ATOM   3448  N NE2 . GLN A 1 426 ? 8.664   17.278  111.054 1.00 76.36  ?  442 GLN B NE2 1 
ATOM   3449  N N   . ALA A 1 427 ? 14.261  16.577  113.484 1.00 74.40  ?  443 ALA B N   1 
ATOM   3450  C CA  . ALA A 1 427 ? 15.144  17.426  114.285 1.00 70.20  ?  443 ALA B CA  1 
ATOM   3451  C C   . ALA A 1 427 ? 16.422  17.778  113.539 1.00 67.82  ?  443 ALA B C   1 
ATOM   3452  O O   . ALA A 1 427 ? 16.874  18.930  113.596 1.00 61.71  ?  443 ALA B O   1 
ATOM   3453  C CB  . ALA A 1 427 ? 15.474  16.748  115.598 1.00 66.75  ?  443 ALA B CB  1 
ATOM   3454  N N   . LEU A 1 428 ? 16.978  16.809  112.809 1.00 67.34  ?  444 LEU B N   1 
ATOM   3455  C CA  . LEU A 1 428 ? 18.105  17.075  111.927 1.00 68.38  ?  444 LEU B CA  1 
ATOM   3456  C C   . LEU A 1 428 ? 17.784  18.206  110.964 1.00 71.86  ?  444 LEU B C   1 
ATOM   3457  O O   . LEU A 1 428 ? 18.683  18.946  110.557 1.00 71.74  ?  444 LEU B O   1 
ATOM   3458  C CB  . LEU A 1 428 ? 18.491  15.795  111.174 1.00 69.59  ?  444 LEU B CB  1 
ATOM   3459  C CG  . LEU A 1 428 ? 19.223  14.694  111.976 1.00 68.28  ?  444 LEU B CG  1 
ATOM   3460  C CD1 . LEU A 1 428 ? 19.606  13.482  111.147 1.00 70.54  ?  444 LEU B CD1 1 
ATOM   3461  C CD2 . LEU A 1 428 ? 20.452  15.246  112.656 1.00 69.59  ?  444 LEU B CD2 1 
ATOM   3462  N N   . THR A 1 429 ? 16.504  18.367  110.614 1.00 82.79  ?  445 THR B N   1 
ATOM   3463  C CA  . THR A 1 429 ? 16.059  19.435  109.714 1.00 82.84  ?  445 THR B CA  1 
ATOM   3464  C C   . THR A 1 429 ? 15.694  20.732  110.444 1.00 79.66  ?  445 THR B C   1 
ATOM   3465  O O   . THR A 1 429 ? 16.192  21.814  110.106 1.00 81.84  ?  445 THR B O   1 
ATOM   3466  C CB  . THR A 1 429 ? 14.858  18.945  108.890 1.00 84.25  ?  445 THR B CB  1 
ATOM   3467  O OG1 . THR A 1 429 ? 15.258  17.840  108.050 1.00 82.53  ?  445 THR B OG1 1 
ATOM   3468  C CG2 . THR A 1 429 ? 14.251  20.090  108.067 1.00 77.57  ?  445 THR B CG2 1 
ATOM   3469  N N   . ILE A 1 430 ? 14.811  20.634  111.430 1.00 70.19  ?  446 ILE B N   1 
ATOM   3470  C CA  . ILE A 1 430 ? 14.260  21.805  112.090 1.00 65.82  ?  446 ILE B CA  1 
ATOM   3471  C C   . ILE A 1 430 ? 15.214  22.326  113.152 1.00 65.86  ?  446 ILE B C   1 
ATOM   3472  O O   . ILE A 1 430 ? 15.576  23.509  113.149 1.00 63.82  ?  446 ILE B O   1 
ATOM   3473  C CB  . ILE A 1 430 ? 12.887  21.467  112.690 1.00 65.48  ?  446 ILE B CB  1 
ATOM   3474  C CG1 . ILE A 1 430 ? 11.912  21.182  111.556 1.00 67.99  ?  446 ILE B CG1 1 
ATOM   3475  C CG2 . ILE A 1 430 ? 12.382  22.592  113.570 1.00 64.83  ?  446 ILE B CG2 1 
ATOM   3476  C CD1 . ILE A 1 430 ? 10.703  20.375  111.940 1.00 70.10  ?  446 ILE B CD1 1 
ATOM   3477  N N   . VAL A 1 431 ? 15.627  21.452  114.083 1.00 67.16  ?  447 VAL B N   1 
ATOM   3478  C CA  . VAL A 1 431 ? 16.378  21.898  115.257 1.00 60.72  ?  447 VAL B CA  1 
ATOM   3479  C C   . VAL A 1 431 ? 17.774  22.290  114.833 1.00 56.84  ?  447 VAL B C   1 
ATOM   3480  O O   . VAL A 1 431 ? 18.308  23.311  115.278 1.00 52.38  ?  447 VAL B O   1 
ATOM   3481  C CB  . VAL A 1 431 ? 16.410  20.796  116.334 1.00 56.37  ?  447 VAL B CB  1 
ATOM   3482  C CG1 . VAL A 1 431 ? 17.172  21.253  117.522 1.00 53.29  ?  447 VAL B CG1 1 
ATOM   3483  C CG2 . VAL A 1 431 ? 15.013  20.388  116.734 1.00 60.95  ?  447 VAL B CG2 1 
ATOM   3484  N N   . GLY A 1 432 ? 18.358  21.505  113.916 1.00 57.49  ?  448 GLY B N   1 
ATOM   3485  C CA  . GLY A 1 432 ? 19.678  21.813  113.390 1.00 53.88  ?  448 GLY B CA  1 
ATOM   3486  C C   . GLY A 1 432 ? 19.793  23.229  112.871 1.00 52.42  ?  448 GLY B C   1 
ATOM   3487  O O   . GLY A 1 432 ? 20.694  23.973  113.257 1.00 58.81  ?  448 GLY B O   1 
ATOM   3488  N N   . THR A 1 433 ? 18.874  23.631  112.003 1.00 59.24  ?  449 THR B N   1 
ATOM   3489  C CA  . THR A 1 433 ? 18.958  24.951  111.399 1.00 57.42  ?  449 THR B CA  1 
ATOM   3490  C C   . THR A 1 433 ? 18.786  26.094  112.386 1.00 57.60  ?  449 THR B C   1 
ATOM   3491  O O   . THR A 1 433 ? 19.216  27.216  112.082 1.00 59.17  ?  449 THR B O   1 
ATOM   3492  C CB  . THR A 1 433 ? 17.936  25.037  110.268 1.00 61.50  ?  449 THR B CB  1 
ATOM   3493  O OG1 . THR A 1 433 ? 18.339  26.083  109.380 1.00 64.58  ?  449 THR B OG1 1 
ATOM   3494  C CG2 . THR A 1 433 ? 16.497  25.241  110.772 1.00 63.69  ?  449 THR B CG2 1 
ATOM   3495  N N   . LEU A 1 434 ? 18.201  25.832  113.565 1.00 53.82  ?  450 LEU B N   1 
ATOM   3496  C CA  . LEU A 1 434 ? 17.904  26.895  114.524 1.00 51.37  ?  450 LEU B CA  1 
ATOM   3497  C C   . LEU A 1 434 ? 19.154  27.638  114.977 1.00 55.36  ?  450 LEU B C   1 
ATOM   3498  O O   . LEU A 1 434 ? 19.261  28.847  114.695 1.00 56.70  ?  450 LEU B O   1 
ATOM   3499  C CB  . LEU A 1 434 ? 17.120  26.303  115.689 1.00 50.43  ?  450 LEU B CB  1 
ATOM   3500  C CG  . LEU A 1 434 ? 15.709  25.871  115.450 1.00 52.74  ?  450 LEU B CG  1 
ATOM   3501  C CD1 . LEU A 1 434 ? 15.154  25.417  116.748 1.00 51.59  ?  450 LEU B CD1 1 
ATOM   3502  C CD2 . LEU A 1 434 ? 15.021  27.146  115.025 1.00 53.85  ?  450 LEU B CD2 1 
ATOM   3503  N N   . PRO A 1 435 ? 20.127  27.006  115.657 1.00 54.10  ?  451 PRO B N   1 
ATOM   3504  C CA  . PRO A 1 435 ? 21.290  27.773  116.097 1.00 52.61  ?  451 PRO B CA  1 
ATOM   3505  C C   . PRO A 1 435 ? 22.038  28.357  114.928 1.00 54.89  ?  451 PRO B C   1 
ATOM   3506  O O   . PRO A 1 435 ? 22.567  29.468  115.030 1.00 57.84  ?  451 PRO B O   1 
ATOM   3507  C CB  . PRO A 1 435 ? 22.141  26.724  116.821 1.00 54.30  ?  451 PRO B CB  1 
ATOM   3508  C CG  . PRO A 1 435 ? 21.240  25.622  117.130 1.00 52.86  ?  451 PRO B CG  1 
ATOM   3509  C CD  . PRO A 1 435 ? 20.318  25.586  115.960 1.00 55.10  ?  451 PRO B CD  1 
ATOM   3510  N N   . PHE A 1 436 ? 22.094  27.622  113.818 1.00 54.64  ?  452 PHE B N   1 
ATOM   3511  C CA  . PHE A 1 436 ? 22.691  28.124  112.585 1.00 58.10  ?  452 PHE B CA  1 
ATOM   3512  C C   . PHE A 1 436 ? 22.146  29.498  112.250 1.00 56.57  ?  452 PHE B C   1 
ATOM   3513  O O   . PHE A 1 436 ? 22.902  30.422  111.900 1.00 57.78  ?  452 PHE B O   1 
ATOM   3514  C CB  . PHE A 1 436 ? 22.403  27.129  111.450 1.00 56.32  ?  452 PHE B CB  1 
ATOM   3515  C CG  . PHE A 1 436 ? 22.930  27.549  110.101 1.00 55.03  ?  452 PHE B CG  1 
ATOM   3516  C CD1 . PHE A 1 436 ? 22.204  28.358  109.277 1.00 56.62  ?  452 PHE B CD1 1 
ATOM   3517  C CD2 . PHE A 1 436 ? 24.162  27.118  109.669 1.00 59.98  ?  452 PHE B CD2 1 
ATOM   3518  C CE1 . PHE A 1 436 ? 22.695  28.732  108.063 1.00 57.42  ?  452 PHE B CE1 1 
ATOM   3519  C CE2 . PHE A 1 436 ? 24.646  27.496  108.458 1.00 61.53  ?  452 PHE B CE2 1 
ATOM   3520  C CZ  . PHE A 1 436 ? 23.910  28.297  107.653 1.00 60.83  ?  452 PHE B CZ  1 
ATOM   3521  N N   . THR A 1 437 ? 20.839  29.658  112.417 1.00 53.65  ?  453 THR B N   1 
ATOM   3522  C CA  . THR A 1 437 ? 20.133  30.804  111.890 1.00 59.26  ?  453 THR B CA  1 
ATOM   3523  C C   . THR A 1 437 ? 20.256  31.971  112.841 1.00 55.72  ?  453 THR B C   1 
ATOM   3524  O O   . THR A 1 437 ? 20.552  33.113  112.440 1.00 54.24  ?  453 THR B O   1 
ATOM   3525  C CB  . THR A 1 437 ? 18.677  30.419  111.702 1.00 61.74  ?  453 THR B CB  1 
ATOM   3526  O OG1 . THR A 1 437 ? 18.585  29.424  110.674 1.00 59.36  ?  453 THR B OG1 1 
ATOM   3527  C CG2 . THR A 1 437 ? 17.872  31.646  111.326 1.00 59.96  ?  453 THR B CG2 1 
ATOM   3528  N N   . TYR A 1 438 ? 20.029  31.676  114.118 1.00 52.70  ?  454 TYR B N   1 
ATOM   3529  C CA  . TYR A 1 438 ? 20.267  32.675  115.140 1.00 56.37  ?  454 TYR B CA  1 
ATOM   3530  C C   . TYR A 1 438 ? 21.686  33.210  115.062 1.00 56.91  ?  454 TYR B C   1 
ATOM   3531  O O   . TYR A 1 438 ? 21.912  34.421  115.214 1.00 56.90  ?  454 TYR B O   1 
ATOM   3532  C CB  . TYR A 1 438 ? 19.948  32.111  116.532 1.00 57.05  ?  454 TYR B CB  1 
ATOM   3533  C CG  . TYR A 1 438 ? 20.596  32.914  117.629 1.00 55.02  ?  454 TYR B CG  1 
ATOM   3534  C CD1 . TYR A 1 438 ? 20.360  34.275  117.741 1.00 54.51  ?  454 TYR B CD1 1 
ATOM   3535  C CD2 . TYR A 1 438 ? 21.349  32.306  118.611 1.00 58.74  ?  454 TYR B CD2 1 
ATOM   3536  C CE1 . TYR A 1 438 ? 20.926  35.028  118.732 1.00 59.77  ?  454 TYR B CE1 1 
ATOM   3537  C CE2 . TYR A 1 438 ? 21.919  33.055  119.637 1.00 61.76  ?  454 TYR B CE2 1 
ATOM   3538  C CZ  . TYR A 1 438 ? 21.694  34.432  119.686 1.00 62.73  ?  454 TYR B CZ  1 
ATOM   3539  O OH  . TYR A 1 438 ? 22.242  35.245  120.668 1.00 65.87  ?  454 TYR B OH  1 
ATOM   3540  N N   . MET A 1 439 ? 22.652  32.336  114.755 1.00 58.33  ?  455 MET B N   1 
ATOM   3541  C CA  . MET A 1 439 ? 24.055  32.744  114.756 1.00 55.20  ?  455 MET B CA  1 
ATOM   3542  C C   . MET A 1 439 ? 24.340  33.654  113.561 1.00 56.34  ?  455 MET B C   1 
ATOM   3543  O O   . MET A 1 439 ? 24.859  34.764  113.719 1.00 57.87  ?  455 MET B O   1 
ATOM   3544  C CB  . MET A 1 439 ? 24.951  31.500  114.711 1.00 54.45  ?  455 MET B CB  1 
ATOM   3545  C CG  . MET A 1 439 ? 26.448  31.699  114.827 1.00 55.90  ?  455 MET B CG  1 
ATOM   3546  S SD  . MET A 1 439 ? 27.195  32.396  113.357 1.00 63.68  ?  455 MET B SD  1 
ATOM   3547  C CE  . MET A 1 439 ? 27.257  30.950  112.349 1.00 65.34  ?  455 MET B CE  1 
ATOM   3548  N N   . LEU A 1 440 ? 24.059  33.171  112.347 1.00 56.22  ?  456 LEU B N   1 
ATOM   3549  C CA  . LEU A 1 440 ? 24.294  33.977  111.155 1.00 57.46  ?  456 LEU B CA  1 
ATOM   3550  C C   . LEU A 1 440 ? 23.691  35.362  111.296 1.00 56.91  ?  456 LEU B C   1 
ATOM   3551  O O   . LEU A 1 440 ? 24.342  36.378  111.001 1.00 56.68  ?  456 LEU B O   1 
ATOM   3552  C CB  . LEU A 1 440 ? 23.691  33.266  109.955 1.00 61.48  ?  456 LEU B CB  1 
ATOM   3553  C CG  . LEU A 1 440 ? 23.866  33.835  108.558 1.00 58.38  ?  456 LEU B CG  1 
ATOM   3554  C CD1 . LEU A 1 440 ? 23.813  32.665  107.569 1.00 56.50  ?  456 LEU B CD1 1 
ATOM   3555  C CD2 . LEU A 1 440 ? 22.776  34.846  108.281 1.00 56.94  ?  456 LEU B CD2 1 
ATOM   3556  N N   . GLU A 1 441 ? 22.421  35.423  111.709 1.00 56.82  ?  457 GLU B N   1 
ATOM   3557  C CA  . GLU A 1 441 ? 21.811  36.736  111.787 1.00 55.44  ?  457 GLU B CA  1 
ATOM   3558  C C   . GLU A 1 441 ? 22.375  37.561  112.954 1.00 61.27  ?  457 GLU B C   1 
ATOM   3559  O O   . GLU A 1 441 ? 22.442  38.792  112.855 1.00 61.99  ?  457 GLU B O   1 
ATOM   3560  C CB  . GLU A 1 441 ? 20.303  36.620  111.899 1.00 51.86  ?  457 GLU B CB  1 
ATOM   3561  C CG  . GLU A 1 441 ? 19.617  37.910  111.502 1.00 54.26  ?  457 GLU B CG  1 
ATOM   3562  C CD  . GLU A 1 441 ? 19.506  38.098  109.996 1.00 55.24  ?  457 GLU B CD  1 
ATOM   3563  O OE1 . GLU A 1 441 ? 20.503  38.002  109.248 1.00 53.82  ?  457 GLU B OE1 1 
ATOM   3564  O OE2 . GLU A 1 441 ? 18.384  38.406  109.563 1.00 53.18  -1 457 GLU B OE2 1 
ATOM   3565  N N   . LYS A 1 442 ? 22.799  36.933  114.061 1.00 60.90  ?  458 LYS B N   1 
ATOM   3566  C CA  . LYS A 1 442 ? 23.463  37.728  115.089 1.00 60.72  ?  458 LYS B CA  1 
ATOM   3567  C C   . LYS A 1 442 ? 24.744  38.341  114.542 1.00 61.85  ?  458 LYS B C   1 
ATOM   3568  O O   . LYS A 1 442 ? 25.068  39.504  114.834 1.00 63.98  ?  458 LYS B O   1 
ATOM   3569  C CB  . LYS A 1 442 ? 23.749  36.882  116.329 1.00 60.64  ?  458 LYS B CB  1 
ATOM   3570  C CG  . LYS A 1 442 ? 23.935  37.711  117.604 1.00 64.16  ?  458 LYS B CG  1 
ATOM   3571  C CD  . LYS A 1 442 ? 24.537  36.918  118.743 1.00 62.00  ?  458 LYS B CD  1 
ATOM   3572  C CE  . LYS A 1 442 ? 24.543  37.760  119.980 1.00 61.87  ?  458 LYS B CE  1 
ATOM   3573  N NZ  . LYS A 1 442 ? 24.630  39.182  119.580 1.00 65.39  ?  458 LYS B NZ  1 
ATOM   3574  N N   . TRP A 1 443 ? 25.464  37.583  113.713 1.00 62.82  ?  459 TRP B N   1 
ATOM   3575  C CA  . TRP A 1 443 ? 26.712  38.092  113.153 1.00 63.60  ?  459 TRP B CA  1 
ATOM   3576  C C   . TRP A 1 443 ? 26.454  39.285  112.254 1.00 62.57  ?  459 TRP B C   1 
ATOM   3577  O O   . TRP A 1 443 ? 27.169  40.291  112.338 1.00 65.82  ?  459 TRP B O   1 
ATOM   3578  C CB  . TRP A 1 443 ? 27.452  37.002  112.381 1.00 62.73  ?  459 TRP B CB  1 
ATOM   3579  C CG  . TRP A 1 443 ? 28.735  37.486  111.765 1.00 63.05  ?  459 TRP B CG  1 
ATOM   3580  C CD1 . TRP A 1 443 ? 29.966  37.477  112.335 1.00 65.73  ?  459 TRP B CD1 1 
ATOM   3581  C CD2 . TRP A 1 443 ? 28.912  38.033  110.449 1.00 64.18  ?  459 TRP B CD2 1 
ATOM   3582  N NE1 . TRP A 1 443 ? 30.900  37.990  111.469 1.00 66.31  ?  459 TRP B NE1 1 
ATOM   3583  C CE2 . TRP A 1 443 ? 30.272  38.340  110.303 1.00 65.99  ?  459 TRP B CE2 1 
ATOM   3584  C CE3 . TRP A 1 443 ? 28.050  38.304  109.383 1.00 63.90  ?  459 TRP B CE3 1 
ATOM   3585  C CZ2 . TRP A 1 443 ? 30.790  38.896  109.131 1.00 68.42  ?  459 TRP B CZ2 1 
ATOM   3586  C CZ3 . TRP A 1 443 ? 28.574  38.861  108.217 1.00 60.30  ?  459 TRP B CZ3 1 
ATOM   3587  C CH2 . TRP A 1 443 ? 29.920  39.147  108.104 1.00 60.42  ?  459 TRP B CH2 1 
ATOM   3588  N N   . ARG A 1 444 ? 25.430  39.196  111.396 1.00 59.94  ?  460 ARG B N   1 
ATOM   3589  C CA  . ARG A 1 444 ? 25.085  40.349  110.562 1.00 58.82  ?  460 ARG B CA  1 
ATOM   3590  C C   . ARG A 1 444 ? 24.585  41.528  111.373 1.00 59.11  ?  460 ARG B C   1 
ATOM   3591  O O   . ARG A 1 444 ? 24.891  42.680  111.055 1.00 58.04  ?  460 ARG B O   1 
ATOM   3592  C CB  . ARG A 1 444 ? 24.014  39.994  109.573 1.00 61.03  ?  460 ARG B CB  1 
ATOM   3593  C CG  . ARG A 1 444 ? 24.467  39.324  108.371 1.00 61.81  ?  460 ARG B CG  1 
ATOM   3594  C CD  . ARG A 1 444 ? 23.241  38.664  107.933 1.00 63.59  ?  460 ARG B CD  1 
ATOM   3595  N NE  . ARG A 1 444 ? 23.012  38.725  106.514 1.00 58.24  ?  460 ARG B NE  1 
ATOM   3596  C CZ  . ARG A 1 444 ? 21.880  38.342  105.955 1.00 58.90  ?  460 ARG B CZ  1 
ATOM   3597  N NH1 . ARG A 1 444 ? 20.837  37.946  106.685 1.00 51.78  ?  460 ARG B NH1 1 
ATOM   3598  N NH2 . ARG A 1 444 ? 21.792  38.358  104.633 1.00 65.82  ?  460 ARG B NH2 1 
ATOM   3599  N N   . TRP A 1 445 ? 23.747  41.272  112.371 1.00 60.54  ?  461 TRP B N   1 
ATOM   3600  C CA  . TRP A 1 445 ? 23.274  42.362  113.211 1.00 60.17  ?  461 TRP B CA  1 
ATOM   3601  C C   . TRP A 1 445 ? 24.428  43.112  113.821 1.00 59.04  ?  461 TRP B C   1 
ATOM   3602  O O   . TRP A 1 445 ? 24.450  44.350  113.793 1.00 60.38  ?  461 TRP B O   1 
ATOM   3603  C CB  . TRP A 1 445 ? 22.332  41.839  114.292 1.00 60.18  ?  461 TRP B CB  1 
ATOM   3604  C CG  . TRP A 1 445 ? 20.983  41.492  113.791 1.00 57.77  ?  461 TRP B CG  1 
ATOM   3605  C CD1 . TRP A 1 445 ? 20.414  41.888  112.623 1.00 56.99  ?  461 TRP B CD1 1 
ATOM   3606  C CD2 . TRP A 1 445 ? 20.025  40.688  114.449 1.00 55.14  ?  461 TRP B CD2 1 
ATOM   3607  N NE1 . TRP A 1 445 ? 19.149  41.378  112.514 1.00 54.48  ?  461 TRP B NE1 1 
ATOM   3608  C CE2 . TRP A 1 445 ? 18.892  40.633  113.630 1.00 54.26  ?  461 TRP B CE2 1 
ATOM   3609  C CE3 . TRP A 1 445 ? 20.017  39.994  115.652 1.00 60.09  ?  461 TRP B CE3 1 
ATOM   3610  C CZ2 . TRP A 1 445 ? 17.776  39.913  113.972 1.00 55.00  ?  461 TRP B CZ2 1 
ATOM   3611  C CZ3 . TRP A 1 445 ? 18.900  39.291  115.992 1.00 56.31  ?  461 TRP B CZ3 1 
ATOM   3612  C CH2 . TRP A 1 445 ? 17.796  39.250  115.157 1.00 51.30  ?  461 TRP B CH2 1 
ATOM   3613  N N   . MET A 1 446 ? 25.406  42.379  114.357 1.00 60.02  ?  462 MET B N   1 
ATOM   3614  C CA  . MET A 1 446 ? 26.602  43.036  114.859 1.00 67.52  ?  462 MET B CA  1 
ATOM   3615  C C   . MET A 1 446 ? 27.362  43.755  113.757 1.00 61.42  ?  462 MET B C   1 
ATOM   3616  O O   . MET A 1 446 ? 27.786  44.902  113.949 1.00 62.74  ?  462 MET B O   1 
ATOM   3617  C CB  . MET A 1 446 ? 27.500  42.045  115.582 1.00 71.25  ?  462 MET B CB  1 
ATOM   3618  C CG  . MET A 1 446 ? 26.883  41.580  116.867 1.00 76.90  ?  462 MET B CG  1 
ATOM   3619  S SD  . MET A 1 446 ? 27.974  40.475  117.744 1.00 74.15  ?  462 MET B SD  1 
ATOM   3620  C CE  . MET A 1 446 ? 27.101  38.975  117.333 1.00 69.06  ?  462 MET B CE  1 
ATOM   3621  N N   . VAL A 1 447 ? 27.575  43.104  112.608 1.00 65.42  ?  463 VAL B N   1 
ATOM   3622  C CA  . VAL A 1 447 ? 28.344  43.767  111.558 1.00 63.25  ?  463 VAL B CA  1 
ATOM   3623  C C   . VAL A 1 447 ? 27.752  45.143  111.319 1.00 62.73  ?  463 VAL B C   1 
ATOM   3624  O O   . VAL A 1 447 ? 28.427  46.167  111.438 1.00 68.25  ?  463 VAL B O   1 
ATOM   3625  C CB  . VAL A 1 447 ? 28.343  42.957  110.254 1.00 60.21  ?  463 VAL B CB  1 
ATOM   3626  C CG1 . VAL A 1 447 ? 28.868  43.829  109.172 1.00 59.68  ?  463 VAL B CG1 1 
ATOM   3627  C CG2 . VAL A 1 447 ? 29.152  41.711  110.364 1.00 63.09  ?  463 VAL B CG2 1 
ATOM   3628  N N   . PHE A 1 448 ? 26.443  45.174  111.098 1.00 59.47  ?  464 PHE B N   1 
ATOM   3629  C CA  . PHE A 1 448 ? 25.752  46.419  110.808 1.00 59.06  ?  464 PHE B CA  1 
ATOM   3630  C C   . PHE A 1 448 ? 25.876  47.415  111.968 1.00 61.71  ?  464 PHE B C   1 
ATOM   3631  O O   . PHE A 1 448 ? 26.221  48.581  111.746 1.00 64.61  ?  464 PHE B O   1 
ATOM   3632  C CB  . PHE A 1 448 ? 24.273  46.122  110.491 1.00 62.50  ?  464 PHE B CB  1 
ATOM   3633  C CG  . PHE A 1 448 ? 24.054  45.269  109.227 1.00 59.93  ?  464 PHE B CG  1 
ATOM   3634  C CD1 . PHE A 1 448 ? 24.821  45.438  108.091 1.00 60.62  ?  464 PHE B CD1 1 
ATOM   3635  C CD2 . PHE A 1 448 ? 23.093  44.284  109.199 1.00 57.91  ?  464 PHE B CD2 1 
ATOM   3636  C CE1 . PHE A 1 448 ? 24.626  44.636  106.965 1.00 55.37  ?  464 PHE B CE1 1 
ATOM   3637  C CE2 . PHE A 1 448 ? 22.908  43.494  108.080 1.00 59.52  ?  464 PHE B CE2 1 
ATOM   3638  C CZ  . PHE A 1 448 ? 23.677  43.669  106.968 1.00 54.59  ?  464 PHE B CZ  1 
ATOM   3639  N N   . LYS A 1 449 ? 25.592  46.981  113.217 1.00 65.07  ?  465 LYS B N   1 
ATOM   3640  C CA  . LYS A 1 449 ? 25.785  47.855  114.380 1.00 64.20  ?  465 LYS B CA  1 
ATOM   3641  C C   . LYS A 1 449 ? 27.193  48.438  114.456 1.00 65.26  ?  465 LYS B C   1 
ATOM   3642  O O   . LYS A 1 449 ? 27.365  49.543  114.981 1.00 67.64  ?  465 LYS B O   1 
ATOM   3643  C CB  . LYS A 1 449 ? 25.333  47.123  115.680 1.00 59.57  ?  465 LYS B CB  1 
ATOM   3644  C CG  . LYS A 1 449 ? 25.073  48.058  116.908 1.00 61.22  ?  465 LYS B CG  1 
ATOM   3645  C CD  . LYS A 1 449 ? 24.149  47.537  118.071 1.00 73.11  ?  465 LYS B CD  1 
ATOM   3646  C CE  . LYS A 1 449 ? 22.675  47.203  117.511 1.00 90.36  ?  465 LYS B CE  1 
ATOM   3647  N NZ  . LYS A 1 449 ? 21.496  46.990  118.485 1.00 75.93  ?  465 LYS B NZ  1 
ATOM   3648  N N   . GLY A 1 450 ? 28.185  47.793  113.847 1.00 63.38  ?  466 GLY B N   1 
ATOM   3649  C CA  . GLY A 1 450 ? 29.560  48.192  114.017 1.00 66.96  ?  466 GLY B CA  1 
ATOM   3650  C C   . GLY A 1 450 ? 30.299  47.509  115.154 1.00 69.48  ?  466 GLY B C   1 
ATOM   3651  O O   . GLY A 1 450 ? 31.443  47.879  115.448 1.00 70.16  ?  466 GLY B O   1 
ATOM   3652  N N   . GLU A 1 451 ? 29.693  46.522  115.803 1.00 68.45  ?  467 GLU B N   1 
ATOM   3653  C CA  . GLU A 1 451 ? 30.343  45.927  116.948 1.00 65.93  ?  467 GLU B CA  1 
ATOM   3654  C C   . GLU A 1 451 ? 31.489  45.010  116.548 1.00 71.39  ?  467 GLU B C   1 
ATOM   3655  O O   . GLU A 1 451 ? 32.282  44.638  117.414 1.00 74.80  ?  467 GLU B O   1 
ATOM   3656  C CB  . GLU A 1 451 ? 29.351  45.132  117.793 1.00 68.49  ?  467 GLU B CB  1 
ATOM   3657  C CG  . GLU A 1 451 ? 28.277  45.956  118.480 1.00 76.37  ?  467 GLU B CG  1 
ATOM   3658  C CD  . GLU A 1 451 ? 27.169  45.093  119.111 1.00 86.57  ?  467 GLU B CD  1 
ATOM   3659  O OE1 . GLU A 1 451 ? 27.263  43.844  119.058 1.00 85.26  ?  467 GLU B OE1 1 
ATOM   3660  O OE2 . GLU A 1 451 ? 26.149  45.666  119.574 1.00 96.09  -1 467 GLU B OE2 1 
ATOM   3661  N N   . ILE A 1 452 ? 31.523  44.577  115.285 1.00 74.45  ?  468 ILE B N   1 
ATOM   3662  C CA  . ILE A 1 452 ? 32.566  43.608  114.828 1.00 74.30  ?  468 ILE B CA  1 
ATOM   3663  C C   . ILE A 1 452 ? 33.387  44.253  113.714 1.00 80.39  ?  468 ILE B C   1 
ATOM   3664  O O   . ILE A 1 452 ? 32.898  44.312  112.577 1.00 80.11  ?  468 ILE B O   1 
ATOM   3665  C CB  . ILE A 1 452 ? 31.943  42.289  114.339 1.00 70.58  ?  468 ILE B CB  1 
ATOM   3666  C CG1 . ILE A 1 452 ? 31.234  41.531  115.463 1.00 74.05  ?  468 ILE B CG1 1 
ATOM   3667  C CG2 . ILE A 1 452 ? 32.988  41.426  113.653 1.00 75.31  ?  468 ILE B CG2 1 
ATOM   3668  C CD1 . ILE A 1 452 ? 30.578  40.251  115.003 1.00 70.16  ?  468 ILE B CD1 1 
ATOM   3669  N N   . PRO A 1 453 ? 34.618  44.726  113.987 1.00 83.20  ?  469 PRO B N   1 
ATOM   3670  C CA  . PRO A 1 453 ? 35.410  45.418  112.982 1.00 81.82  ?  469 PRO B CA  1 
ATOM   3671  C C   . PRO A 1 453 ? 35.840  44.489  111.843 1.00 83.87  ?  469 PRO B C   1 
ATOM   3672  O O   . PRO A 1 453 ? 35.914  43.301  112.066 1.00 85.60  ?  469 PRO B O   1 
ATOM   3673  C CB  . PRO A 1 453 ? 36.648  45.853  113.762 1.00 86.13  ?  469 PRO B CB  1 
ATOM   3674  C CG  . PRO A 1 453 ? 36.218  45.824  115.207 1.00 87.87  ?  469 PRO B CG  1 
ATOM   3675  C CD  . PRO A 1 453 ? 35.284  44.639  115.281 1.00 87.43  ?  469 PRO B CD  1 
ATOM   3676  N N   . LYS A 1 454 ? 36.136  45.056  110.672 1.00 83.71  ?  470 LYS B N   1 
ATOM   3677  C CA  . LYS A 1 454 ? 36.500  44.232  109.490 1.00 84.97  ?  470 LYS B CA  1 
ATOM   3678  C C   . LYS A 1 454 ? 37.742  43.398  109.800 1.00 89.31  ?  470 LYS B C   1 
ATOM   3679  O O   . LYS A 1 454 ? 37.835  42.270  109.293 1.00 88.58  ?  470 LYS B O   1 
ATOM   3680  C CB  . LYS A 1 454 ? 36.748  45.135  108.284 1.00 83.42  ?  470 LYS B CB  1 
ATOM   3681  C CG  . LYS A 1 454 ? 35.502  45.721  107.638 1.00 87.04  ?  470 LYS B CG  1 
ATOM   3682  C CD  . LYS A 1 454 ? 35.767  47.011  106.892 1.00 86.66  ?  470 LYS B CD  1 
ATOM   3683  C CE  . LYS A 1 454 ? 37.073  46.997  106.126 1.00 84.74  ?  470 LYS B CE  1 
ATOM   3684  N NZ  . LYS A 1 454 ? 37.317  48.283  105.432 1.00 87.05  ?  470 LYS B NZ  1 
ATOM   3685  N N   . ASP A 1 455 ? 38.651  43.930  110.614 1.00 94.56  ?  471 ASP B N   1 
ATOM   3686  C CA  . ASP A 1 455 ? 39.913  43.216  110.937 1.00 95.06  ?  471 ASP B CA  1 
ATOM   3687  C C   . ASP A 1 455 ? 39.607  41.953  111.742 1.00 95.70  ?  471 ASP B C   1 
ATOM   3688  O O   . ASP A 1 455 ? 40.555  41.223  112.053 1.00 95.29  ?  471 ASP B O   1 
ATOM   3689  C CB  . ASP A 1 455 ? 40.877  44.128  111.695 1.00 98.90  ?  471 ASP B CB  1 
ATOM   3690  C CG  . ASP A 1 455 ? 40.389  44.526  113.075 1.00 106.69 ?  471 ASP B CG  1 
ATOM   3691  O OD1 . ASP A 1 455 ? 39.213  44.268  113.370 1.00 106.63 ?  471 ASP B OD1 1 
ATOM   3692  O OD2 . ASP A 1 455 ? 41.195  45.089  113.840 1.00 112.31 -1 471 ASP B OD2 1 
ATOM   3693  N N   . GLN A 1 456 ? 38.341  41.702  112.071 1.00 91.45  ?  472 GLN B N   1 
ATOM   3694  C CA  . GLN A 1 456 ? 37.968  40.540  112.916 1.00 88.38  ?  472 GLN B CA  1 
ATOM   3695  C C   . GLN A 1 456 ? 36.648  39.980  112.400 1.00 82.25  ?  472 GLN B C   1 
ATOM   3696  O O   . GLN A 1 456 ? 36.005  39.220  113.137 1.00 77.72  ?  472 GLN B O   1 
ATOM   3697  C CB  . GLN A 1 456 ? 37.819  41.003  114.363 1.00 91.37  ?  472 GLN B CB  1 
ATOM   3698  C CG  . GLN A 1 456 ? 39.121  41.469  114.994 1.00 95.45  ?  472 GLN B CG  1 
ATOM   3699  C CD  . GLN A 1 456 ? 39.009  41.599  116.492 1.00 101.90 ?  472 GLN B CD  1 
ATOM   3700  O OE1 . GLN A 1 456 ? 38.414  42.543  117.009 1.00 102.72 ?  472 GLN B OE1 1 
ATOM   3701  N NE2 . GLN A 1 456 ? 39.592  40.647  117.202 1.00 96.55  ?  472 GLN B NE2 1 
ATOM   3702  N N   . TRP A 1 457 ? 36.276  40.352  111.182 1.00 82.97  ?  473 TRP B N   1 
ATOM   3703  C CA  . TRP A 1 457 ? 34.980  39.921  110.607 1.00 79.95  ?  473 TRP B CA  1 
ATOM   3704  C C   . TRP A 1 457 ? 34.889  38.393  110.592 1.00 80.48  ?  473 TRP B C   1 
ATOM   3705  O O   . TRP A 1 457 ? 33.864  37.862  111.054 1.00 80.91  ?  473 TRP B O   1 
ATOM   3706  C CB  . TRP A 1 457 ? 34.844  40.507  109.201 1.00 77.19  ?  473 TRP B CB  1 
ATOM   3707  C CG  . TRP A 1 457 ? 33.965  41.713  109.093 1.00 79.65  ?  473 TRP B CG  1 
ATOM   3708  C CD1 . TRP A 1 457 ? 33.591  42.560  110.096 1.00 80.60  ?  473 TRP B CD1 1 
ATOM   3709  C CD2 . TRP A 1 457 ? 33.355  42.224  107.896 1.00 74.47  ?  473 TRP B CD2 1 
ATOM   3710  N NE1 . TRP A 1 457 ? 32.790  43.555  109.606 1.00 75.93  ?  473 TRP B NE1 1 
ATOM   3711  C CE2 . TRP A 1 457 ? 32.630  43.373  108.257 1.00 70.91  ?  473 TRP B CE2 1 
ATOM   3712  C CE3 . TRP A 1 457 ? 33.358  41.813  106.560 1.00 68.47  ?  473 TRP B CE3 1 
ATOM   3713  C CZ2 . TRP A 1 457 ? 31.911  44.114  107.323 1.00 74.38  ?  473 TRP B CZ2 1 
ATOM   3714  C CZ3 . TRP A 1 457 ? 32.646  42.546  105.641 1.00 68.61  ?  473 TRP B CZ3 1 
ATOM   3715  C CH2 . TRP A 1 457 ? 31.934  43.679  106.020 1.00 69.75  ?  473 TRP B CH2 1 
ATOM   3716  N N   . MET A 1 458 ? 35.904  37.717  110.050 1.00 80.64  ?  474 MET B N   1 
ATOM   3717  C CA  . MET A 1 458 ? 35.892  36.235  109.963 1.00 75.91  ?  474 MET B CA  1 
ATOM   3718  C C   . MET A 1 458 ? 36.262  35.655  111.328 1.00 74.60  ?  474 MET B C   1 
ATOM   3719  O O   . MET A 1 458 ? 35.634  34.679  111.744 1.00 71.99  ?  474 MET B O   1 
ATOM   3720  C CB  . MET A 1 458 ? 36.871  35.753  108.893 1.00 77.40  ?  474 MET B CB  1 
ATOM   3721  C CG  . MET A 1 458 ? 36.513  36.250  107.505 1.00 82.89  ?  474 MET B CG  1 
ATOM   3722  S SD  . MET A 1 458 ? 34.764  35.949  107.203 1.00 73.86  ?  474 MET B SD  1 
ATOM   3723  C CE  . MET A 1 458 ? 34.720  34.164  107.337 1.00 80.48  ?  474 MET B CE  1 
ATOM   3724  N N   . LYS A 1 459 ? 37.209  36.285  112.023 1.00 78.57  ?  475 LYS B N   1 
ATOM   3725  C CA  . LYS A 1 459 ? 37.535  35.793  113.355 1.00 77.05  ?  475 LYS B CA  1 
ATOM   3726  C C   . LYS A 1 459 ? 36.264  35.706  114.187 1.00 73.97  ?  475 LYS B C   1 
ATOM   3727  O O   . LYS A 1 459 ? 35.864  34.612  114.616 1.00 70.89  ?  475 LYS B O   1 
ATOM   3728  C CB  . LYS A 1 459 ? 38.588  36.697  114.017 1.00 78.75  ?  475 LYS B CB  1 
ATOM   3729  C CG  . LYS A 1 459 ? 39.119  36.219  115.371 1.00 77.95  ?  475 LYS B CG  1 
ATOM   3730  C CD  . LYS A 1 459 ? 40.016  37.268  116.067 1.00 86.69  ?  475 LYS B CD  1 
ATOM   3731  C CE  . LYS A 1 459 ? 40.370  36.792  117.504 1.00 101.07 ?  475 LYS B CE  1 
ATOM   3732  N NZ  . LYS A 1 459 ? 40.911  37.824  118.478 1.00 104.55 ?  475 LYS B NZ  1 
ATOM   3733  N N   . LYS A 1 460 ? 35.529  36.827  114.275 1.00 73.74  ?  476 LYS B N   1 
ATOM   3734  C CA  . LYS A 1 460 ? 34.323  36.844  115.094 1.00 71.05  ?  476 LYS B CA  1 
ATOM   3735  C C   . LYS A 1 460 ? 33.332  35.823  114.570 1.00 70.67  ?  476 LYS B C   1 
ATOM   3736  O O   . LYS A 1 460 ? 32.754  35.042  115.344 1.00 70.62  ?  476 LYS B O   1 
ATOM   3737  C CB  . LYS A 1 460 ? 33.711  38.248  115.126 1.00 71.31  ?  476 LYS B CB  1 
ATOM   3738  C CG  . LYS A 1 460 ? 33.924  39.027  116.442 1.00 76.84  ?  476 LYS B CG  1 
ATOM   3739  C CD  . LYS A 1 460 ? 33.301  38.303  117.677 1.00 85.04  ?  476 LYS B CD  1 
ATOM   3740  C CE  . LYS A 1 460 ? 32.416  39.212  118.584 1.00 81.71  ?  476 LYS B CE  1 
ATOM   3741  N NZ  . LYS A 1 460 ? 31.677  38.449  119.660 1.00 79.13  ?  476 LYS B NZ  1 
ATOM   3742  N N   . TRP A 1 461 ? 33.217  35.737  113.243 1.00 68.60  ?  477 TRP B N   1 
ATOM   3743  C CA  . TRP A 1 461 ? 32.357  34.738  112.629 1.00 67.89  ?  477 TRP B CA  1 
ATOM   3744  C C   . TRP A 1 461 ? 32.643  33.355  113.202 1.00 69.87  ?  477 TRP B C   1 
ATOM   3745  O O   . TRP A 1 461 ? 31.774  32.723  113.826 1.00 67.74  ?  477 TRP B O   1 
ATOM   3746  C CB  . TRP A 1 461 ? 32.553  34.765  111.114 1.00 68.69  ?  477 TRP B CB  1 
ATOM   3747  C CG  . TRP A 1 461 ? 31.771  33.721  110.332 1.00 68.81  ?  477 TRP B CG  1 
ATOM   3748  C CD1 . TRP A 1 461 ? 32.232  32.528  109.846 1.00 71.57  ?  477 TRP B CD1 1 
ATOM   3749  C CD2 . TRP A 1 461 ? 30.399  33.801  109.940 1.00 69.42  ?  477 TRP B CD2 1 
ATOM   3750  N NE1 . TRP A 1 461 ? 31.239  31.872  109.165 1.00 69.13  ?  477 TRP B NE1 1 
ATOM   3751  C CE2 . TRP A 1 461 ? 30.102  32.627  109.211 1.00 67.63  ?  477 TRP B CE2 1 
ATOM   3752  C CE3 . TRP A 1 461 ? 29.390  34.750  110.139 1.00 68.60  ?  477 TRP B CE3 1 
ATOM   3753  C CZ2 . TRP A 1 461 ? 28.851  32.380  108.683 1.00 64.32  ?  477 TRP B CZ2 1 
ATOM   3754  C CZ3 . TRP A 1 461 ? 28.151  34.506  109.609 1.00 66.58  ?  477 TRP B CZ3 1 
ATOM   3755  C CH2 . TRP A 1 461 ? 27.888  33.329  108.886 1.00 65.32  ?  477 TRP B CH2 1 
ATOM   3756  N N   . TRP A 1 462 ? 33.886  32.891  113.053 1.00 69.60  ?  478 TRP B N   1 
ATOM   3757  C CA  . TRP A 1 462 ? 34.133  31.507  113.418 1.00 68.54  ?  478 TRP B CA  1 
ATOM   3758  C C   . TRP A 1 462 ? 34.166  31.300  114.912 1.00 69.96  ?  478 TRP B C   1 
ATOM   3759  O O   . TRP A 1 462 ? 34.041  30.156  115.359 1.00 70.85  ?  478 TRP B O   1 
ATOM   3760  C CB  . TRP A 1 462 ? 35.406  31.011  112.777 1.00 68.52  ?  478 TRP B CB  1 
ATOM   3761  C CG  . TRP A 1 462 ? 35.195  30.699  111.381 1.00 66.76  ?  478 TRP B CG  1 
ATOM   3762  C CD1 . TRP A 1 462 ? 35.685  31.358  110.314 1.00 71.82  ?  478 TRP B CD1 1 
ATOM   3763  C CD2 . TRP A 1 462 ? 34.475  29.584  110.873 1.00 69.98  ?  478 TRP B CD2 1 
ATOM   3764  N NE1 . TRP A 1 462 ? 35.295  30.737  109.146 1.00 69.53  ?  478 TRP B NE1 1 
ATOM   3765  C CE2 . TRP A 1 462 ? 34.550  29.640  109.472 1.00 71.56  ?  478 TRP B CE2 1 
ATOM   3766  C CE3 . TRP A 1 462 ? 33.759  28.544  111.469 1.00 73.45  ?  478 TRP B CE3 1 
ATOM   3767  C CZ2 . TRP A 1 462 ? 33.938  28.700  108.656 1.00 73.95  ?  478 TRP B CZ2 1 
ATOM   3768  C CZ3 . TRP A 1 462 ? 33.142  27.600  110.650 1.00 72.36  ?  478 TRP B CZ3 1 
ATOM   3769  C CH2 . TRP A 1 462 ? 33.241  27.686  109.265 1.00 72.40  ?  478 TRP B CH2 1 
ATOM   3770  N N   . GLU A 1 463 ? 34.305  32.372  115.696 1.00 69.09  ?  479 GLU B N   1 
ATOM   3771  C CA  . GLU A 1 463 ? 34.155  32.224  117.137 1.00 65.39  ?  479 GLU B CA  1 
ATOM   3772  C C   . GLU A 1 463 ? 32.722  31.811  117.442 1.00 66.14  ?  479 GLU B C   1 
ATOM   3773  O O   . GLU A 1 463 ? 32.461  30.841  118.175 1.00 63.54  ?  479 GLU B O   1 
ATOM   3774  C CB  . GLU A 1 463 ? 34.532  33.553  117.793 1.00 68.45  ?  479 GLU B CB  1 
ATOM   3775  C CG  . GLU A 1 463 ? 36.048  33.792  117.754 1.00 77.46  ?  479 GLU B CG  1 
ATOM   3776  C CD  . GLU A 1 463 ? 36.516  35.125  118.351 1.00 82.55  ?  479 GLU B CD  1 
ATOM   3777  O OE1 . GLU A 1 463 ? 35.662  35.990  118.691 1.00 81.22  ?  479 GLU B OE1 1 
ATOM   3778  O OE2 . GLU A 1 463 ? 37.760  35.297  118.464 1.00 81.65  -1 479 GLU B OE2 1 
ATOM   3779  N N   . MET A 1 464 ? 31.792  32.461  116.744 1.00 67.64  ?  480 MET B N   1 
ATOM   3780  C CA  . MET A 1 464 ? 30.373  32.269  116.960 1.00 66.25  ?  480 MET B CA  1 
ATOM   3781  C C   . MET A 1 464 ? 29.927  30.884  116.491 1.00 65.95  ?  480 MET B C   1 
ATOM   3782  O O   . MET A 1 464 ? 29.291  30.143  117.250 1.00 66.91  ?  480 MET B O   1 
ATOM   3783  C CB  . MET A 1 464 ? 29.665  33.417  116.262 1.00 62.93  ?  480 MET B CB  1 
ATOM   3784  C CG  . MET A 1 464 ? 29.987  34.707  116.993 1.00 65.59  ?  480 MET B CG  1 
ATOM   3785  S SD  . MET A 1 464 ? 29.544  36.222  116.156 1.00 62.21  ?  480 MET B SD  1 
ATOM   3786  C CE  . MET A 1 464 ? 27.778  35.895  116.011 1.00 61.28  ?  480 MET B CE  1 
ATOM   3787  N N   . LYS A 1 465 ? 30.304  30.484  115.273 1.00 66.36  ?  481 LYS B N   1 
ATOM   3788  C CA  . LYS A 1 465 ? 30.138  29.085  114.886 1.00 64.83  ?  481 LYS B CA  1 
ATOM   3789  C C   . LYS A 1 465 ? 30.583  28.121  115.995 1.00 65.19  ?  481 LYS B C   1 
ATOM   3790  O O   . LYS A 1 465 ? 29.858  27.178  116.337 1.00 64.03  ?  481 LYS B O   1 
ATOM   3791  C CB  . LYS A 1 465 ? 30.899  28.788  113.587 1.00 66.89  ?  481 LYS B CB  1 
ATOM   3792  C CG  . LYS A 1 465 ? 30.202  29.233  112.332 1.00 63.77  ?  481 LYS B CG  1 
ATOM   3793  C CD  . LYS A 1 465 ? 29.134  28.251  111.871 1.00 60.19  ?  481 LYS B CD  1 
ATOM   3794  C CE  . LYS A 1 465 ? 28.690  28.635  110.453 1.00 63.22  ?  481 LYS B CE  1 
ATOM   3795  N NZ  . LYS A 1 465 ? 27.656  27.726  109.900 1.00 63.93  ?  481 LYS B NZ  1 
ATOM   3796  N N   . ARG A 1 466 ? 31.757  28.348  116.598 1.00 65.54  ?  482 ARG B N   1 
ATOM   3797  C CA  . ARG A 1 466 ? 32.174  27.416  117.637 1.00 66.41  ?  482 ARG B CA  1 
ATOM   3798  C C   . ARG A 1 466 ? 31.302  27.574  118.876 1.00 65.62  ?  482 ARG B C   1 
ATOM   3799  O O   . ARG A 1 466 ? 30.802  26.581  119.432 1.00 61.01  ?  482 ARG B O   1 
ATOM   3800  C CB  . ARG A 1 466 ? 33.646  27.606  117.990 1.00 66.40  ?  482 ARG B CB  1 
ATOM   3801  C CG  . ARG A 1 466 ? 34.597  27.285  116.863 1.00 66.79  ?  482 ARG B CG  1 
ATOM   3802  C CD  . ARG A 1 466 ? 36.029  27.817  117.153 1.00 78.06  ?  482 ARG B CD  1 
ATOM   3803  N NE  . ARG A 1 466 ? 36.922  27.627  116.010 1.00 81.23  ?  482 ARG B NE  1 
ATOM   3804  C CZ  . ARG A 1 466 ? 38.034  26.898  116.000 1.00 82.21  ?  482 ARG B CZ  1 
ATOM   3805  N NH1 . ARG A 1 466 ? 38.497  26.303  117.095 1.00 81.45  ?  482 ARG B NH1 1 
ATOM   3806  N NH2 . ARG A 1 466 ? 38.702  26.764  114.859 1.00 82.80  ?  482 ARG B NH2 1 
ATOM   3807  N N   . GLU A 1 467 ? 31.088  28.821  119.311 1.00 69.33  ?  483 GLU B N   1 
ATOM   3808  C CA  . GLU A 1 467 ? 30.475  29.023  120.618 1.00 73.62  ?  483 GLU B CA  1 
ATOM   3809  C C   . GLU A 1 467 ? 29.000  28.653  120.591 1.00 76.80  ?  483 GLU B C   1 
ATOM   3810  O O   . GLU A 1 467 ? 28.521  27.926  121.471 1.00 79.45  ?  483 GLU B O   1 
ATOM   3811  C CB  . GLU A 1 467 ? 30.639  30.462  121.082 1.00 76.20  ?  483 GLU B CB  1 
ATOM   3812  C CG  . GLU A 1 467 ? 29.936  30.721  122.417 1.00 82.31  ?  483 GLU B CG  1 
ATOM   3813  C CD  . GLU A 1 467 ? 30.225  32.107  122.965 1.00 97.64  ?  483 GLU B CD  1 
ATOM   3814  O OE1 . GLU A 1 467 ? 31.330  32.339  123.504 1.00 106.31 ?  483 GLU B OE1 1 
ATOM   3815  O OE2 . GLU A 1 467 ? 29.323  32.973  122.859 1.00 103.02 -1 483 GLU B OE2 1 
ATOM   3816  N N   . ILE A 1 468 ? 28.265  29.161  119.587 1.00 72.14  ?  484 ILE B N   1 
ATOM   3817  C CA  . ILE A 1 468 ? 26.807  29.065  119.498 1.00 65.83  ?  484 ILE B CA  1 
ATOM   3818  C C   . ILE A 1 468 ? 26.402  27.775  118.814 1.00 62.08  ?  484 ILE B C   1 
ATOM   3819  O O   . ILE A 1 468 ? 25.632  26.982  119.358 1.00 60.71  ?  484 ILE B O   1 
ATOM   3820  C CB  . ILE A 1 468 ? 26.196  30.247  118.729 1.00 63.91  ?  484 ILE B CB  1 
ATOM   3821  C CG1 . ILE A 1 468 ? 26.425  31.578  119.440 1.00 62.67  ?  484 ILE B CG1 1 
ATOM   3822  C CG2 . ILE A 1 468 ? 24.742  29.995  118.581 1.00 67.21  ?  484 ILE B CG2 1 
ATOM   3823  C CD1 . ILE A 1 468 ? 26.038  32.802  118.639 1.00 62.36  ?  484 ILE B CD1 1 
ATOM   3824  N N   . VAL A 1 469 ? 26.906  27.583  117.598 1.00 61.50  ?  485 VAL B N   1 
ATOM   3825  C CA  . VAL A 1 469 ? 26.528  26.452  116.760 1.00 60.44  ?  485 VAL B CA  1 
ATOM   3826  C C   . VAL A 1 469 ? 27.210  25.173  117.189 1.00 59.44  ?  485 VAL B C   1 
ATOM   3827  O O   . VAL A 1 469 ? 26.643  24.093  117.043 1.00 58.35  ?  485 VAL B O   1 
ATOM   3828  C CB  . VAL A 1 469 ? 26.840  26.774  115.291 1.00 61.04  ?  485 VAL B CB  1 
ATOM   3829  C CG1 . VAL A 1 469 ? 26.321  25.703  114.390 1.00 61.78  ?  485 VAL B CG1 1 
ATOM   3830  C CG2 . VAL A 1 469 ? 26.184  28.077  114.936 1.00 60.25  ?  485 VAL B CG2 1 
ATOM   3831  N N   . GLY A 1 470 ? 28.417  25.252  117.726 1.00 60.49  ?  486 GLY B N   1 
ATOM   3832  C CA  . GLY A 1 470 ? 29.108  24.017  118.018 1.00 63.42  ?  486 GLY B CA  1 
ATOM   3833  C C   . GLY A 1 470 ? 29.643  23.394  116.752 1.00 63.03  ?  486 GLY B C   1 
ATOM   3834  O O   . GLY A 1 470 ? 29.603  22.159  116.590 1.00 60.68  ?  486 GLY B O   1 
ATOM   3835  N N   . VAL A 1 471 ? 30.144  24.233  115.847 1.00 66.77  ?  487 VAL B N   1 
ATOM   3836  C CA  . VAL A 1 471 ? 30.670  23.813  114.559 1.00 66.73  ?  487 VAL B CA  1 
ATOM   3837  C C   . VAL A 1 471 ? 31.997  24.539  114.357 1.00 66.89  ?  487 VAL B C   1 
ATOM   3838  O O   . VAL A 1 471 ? 32.134  25.704  114.747 1.00 65.16  ?  487 VAL B O   1 
ATOM   3839  C CB  . VAL A 1 471 ? 29.656  24.127  113.441 1.00 63.23  ?  487 VAL B CB  1 
ATOM   3840  C CG1 . VAL A 1 471 ? 30.295  24.002  112.101 1.00 65.81  ?  487 VAL B CG1 1 
ATOM   3841  C CG2 . VAL A 1 471 ? 28.488  23.214  113.546 1.00 61.97  ?  487 VAL B CG2 1 
ATOM   3842  N N   . VAL A 1 472 ? 32.980  23.858  113.750 1.00 68.96  ?  488 VAL B N   1 
ATOM   3843  C CA  . VAL A 1 472 ? 34.337  24.385  113.617 1.00 70.93  ?  488 VAL B CA  1 
ATOM   3844  C C   . VAL A 1 472 ? 34.854  24.302  112.179 1.00 73.53  ?  488 VAL B C   1 
ATOM   3845  O O   . VAL A 1 472 ? 34.657  23.300  111.483 1.00 74.21  ?  488 VAL B O   1 
ATOM   3846  C CB  . VAL A 1 472 ? 35.287  23.642  114.557 1.00 74.10  ?  488 VAL B CB  1 
ATOM   3847  C CG1 . VAL A 1 472 ? 35.243  22.147  114.235 1.00 74.67  ?  488 VAL B CG1 1 
ATOM   3848  C CG2 . VAL A 1 472 ? 36.688  24.219  114.422 1.00 74.09  ?  488 VAL B CG2 1 
ATOM   3849  N N   . GLU A 1 473 ? 35.554  25.353  111.755 1.00 72.33  ?  489 GLU B N   1 
ATOM   3850  C CA  . GLU A 1 473 ? 36.074  25.432  110.399 1.00 73.47  ?  489 GLU B CA  1 
ATOM   3851  C C   . GLU A 1 473 ? 37.263  24.491  110.259 1.00 82.81  ?  489 GLU B C   1 
ATOM   3852  O O   . GLU A 1 473 ? 38.136  24.468  111.136 1.00 88.21  ?  489 GLU B O   1 
ATOM   3853  C CB  . GLU A 1 473 ? 36.515  26.864  110.077 1.00 73.47  ?  489 GLU B CB  1 
ATOM   3854  C CG  . GLU A 1 473 ? 37.833  27.349  110.740 1.00 76.63  ?  489 GLU B CG  1 
ATOM   3855  C CD  . GLU A 1 473 ? 37.709  27.762  112.210 1.00 77.99  ?  489 GLU B CD  1 
ATOM   3856  O OE1 . GLU A 1 473 ? 36.752  27.325  112.883 1.00 77.14  ?  489 GLU B OE1 1 
ATOM   3857  O OE2 . GLU A 1 473 ? 38.607  28.474  112.727 1.00 78.80  -1 489 GLU B OE2 1 
ATOM   3858  N N   . PRO A 1 474 ? 37.332  23.679  109.203 1.00 91.50  ?  490 PRO B N   1 
ATOM   3859  C CA  . PRO A 1 474 ? 38.498  22.803  109.014 1.00 91.94  ?  490 PRO B CA  1 
ATOM   3860  C C   . PRO A 1 474 ? 39.711  23.462  108.365 1.00 94.65  ?  490 PRO B C   1 
ATOM   3861  O O   . PRO A 1 474 ? 40.694  22.762  108.121 1.00 102.70 ?  490 PRO B O   1 
ATOM   3862  C CB  . PRO A 1 474 ? 37.938  21.677  108.126 1.00 90.67  ?  490 PRO B CB  1 
ATOM   3863  C CG  . PRO A 1 474 ? 36.863  22.308  107.368 1.00 90.36  ?  490 PRO B CG  1 
ATOM   3864  C CD  . PRO A 1 474 ? 36.262  23.381  108.235 1.00 86.76  ?  490 PRO B CD  1 
ATOM   3865  N N   . VAL A 1 475 ? 39.693  24.762  108.084 1.00 87.53  ?  491 VAL B N   1 
ATOM   3866  C CA  . VAL A 1 475 ? 40.854  25.478  107.558 1.00 88.50  ?  491 VAL B CA  1 
ATOM   3867  C C   . VAL A 1 475 ? 40.847  26.878  108.163 1.00 89.39  ?  491 VAL B C   1 
ATOM   3868  O O   . VAL A 1 475 ? 39.786  27.506  108.233 1.00 94.67  ?  491 VAL B O   1 
ATOM   3869  C CB  . VAL A 1 475 ? 40.816  25.560  106.024 1.00 88.79  ?  491 VAL B CB  1 
ATOM   3870  C CG1 . VAL A 1 475 ? 41.973  26.451  105.487 1.00 93.80  ?  491 VAL B CG1 1 
ATOM   3871  C CG2 . VAL A 1 475 ? 40.721  24.178  105.356 1.00 82.52  ?  491 VAL B CG2 1 
ATOM   3872  N N   . PRO A 1 476 ? 41.971  27.423  108.608 1.00 89.24  ?  492 PRO B N   1 
ATOM   3873  C CA  . PRO A 1 476 ? 41.952  28.807  109.099 1.00 93.58  ?  492 PRO B CA  1 
ATOM   3874  C C   . PRO A 1 476 ? 41.753  29.789  107.957 1.00 95.86  ?  492 PRO B C   1 
ATOM   3875  O O   . PRO A 1 476 ? 42.400  29.694  106.908 1.00 96.81  ?  492 PRO B O   1 
ATOM   3876  C CB  . PRO A 1 476 ? 43.328  28.984  109.747 1.00 96.97  ?  492 PRO B CB  1 
ATOM   3877  C CG  . PRO A 1 476 ? 44.165  28.008  109.079 1.00 104.54 ?  492 PRO B CG  1 
ATOM   3878  C CD  . PRO A 1 476 ? 43.298  26.823  108.753 1.00 99.37  ?  492 PRO B CD  1 
ATOM   3879  N N   . HIS A 1 477 ? 40.768  30.672  108.136 1.00 89.12  ?  493 HIS B N   1 
ATOM   3880  C CA  . HIS A 1 477 ? 40.417  31.622  107.054 1.00 85.36  ?  493 HIS B CA  1 
ATOM   3881  C C   . HIS A 1 477 ? 40.808  33.041  107.450 1.00 83.12  ?  493 HIS B C   1 
ATOM   3882  O O   . HIS A 1 477 ? 40.257  33.551  108.433 1.00 83.48  ?  493 HIS B O   1 
ATOM   3883  C CB  . HIS A 1 477 ? 38.923  31.532  106.747 1.00 85.60  ?  493 HIS B CB  1 
ATOM   3884  C CG  . HIS A 1 477 ? 38.530  30.315  105.987 1.00 83.66  ?  493 HIS B CG  1 
ATOM   3885  N ND1 . HIS A 1 477 ? 37.305  30.203  105.370 1.00 84.67  ?  493 HIS B ND1 1 
ATOM   3886  C CD2 . HIS A 1 477 ? 39.186  29.164  105.741 1.00 85.20  ?  493 HIS B CD2 1 
ATOM   3887  C CE1 . HIS A 1 477 ? 37.218  29.032  104.778 1.00 83.62  ?  493 HIS B CE1 1 
ATOM   3888  N NE2 . HIS A 1 477 ? 38.357  28.376  104.995 1.00 81.71  ?  493 HIS B NE2 1 
ATOM   3889  N N   . ASP A 1 478 ? 41.721  33.645  106.695 1.00 84.44  ?  494 ASP B N   1 
ATOM   3890  C CA  . ASP A 1 478 ? 42.123  35.044  106.964 1.00 85.78  ?  494 ASP B CA  1 
ATOM   3891  C C   . ASP A 1 478 ? 41.005  35.964  106.495 1.00 84.76  ?  494 ASP B C   1 
ATOM   3892  O O   . ASP A 1 478 ? 40.009  35.462  105.953 1.00 82.40  ?  494 ASP B O   1 
ATOM   3893  C CB  . ASP A 1 478 ? 43.414  35.397  106.232 1.00 84.09  ?  494 ASP B CB  1 
ATOM   3894  C CG  . ASP A 1 478 ? 43.458  34.809  104.835 1.00 87.74  ?  494 ASP B CG  1 
ATOM   3895  O OD1 . ASP A 1 478 ? 42.422  34.861  104.152 1.00 91.43  ?  494 ASP B OD1 1 
ATOM   3896  O OD2 . ASP A 1 478 ? 44.522  34.294  104.452 1.00 95.37  -1 494 ASP B OD2 1 
ATOM   3897  N N   . GLU A 1 479 ? 41.199  37.266  106.661 1.00 93.33  ?  495 GLU B N   1 
ATOM   3898  C CA  . GLU A 1 479 ? 40.157  38.239  106.267 1.00 89.02  ?  495 GLU B CA  1 
ATOM   3899  C C   . GLU A 1 479 ? 40.028  38.293  104.745 1.00 86.28  ?  495 GLU B C   1 
ATOM   3900  O O   . GLU A 1 479 ? 39.214  39.101  104.273 1.00 82.36  ?  495 GLU B O   1 
ATOM   3901  C CB  . GLU A 1 479 ? 40.518  39.629  106.782 1.00 90.82  ?  495 GLU B CB  1 
ATOM   3902  C CG  . GLU A 1 479 ? 39.734  40.081  108.001 1.00 93.69  ?  495 GLU B CG  1 
ATOM   3903  C CD  . GLU A 1 479 ? 39.029  38.993  108.789 1.00 89.45  ?  495 GLU B CD  1 
ATOM   3904  O OE1 . GLU A 1 479 ? 37.788  39.007  108.818 1.00 90.42  ?  495 GLU B OE1 1 
ATOM   3905  O OE2 . GLU A 1 479 ? 39.725  38.149  109.382 1.00 95.85  -1 495 GLU B OE2 1 
ATOM   3906  N N   . THR A 1 480 ? 40.796  37.497  103.993 1.00 83.66  ?  496 THR B N   1 
ATOM   3907  C CA  . THR A 1 480 ? 40.581  37.626  102.534 1.00 85.22  ?  496 THR B CA  1 
ATOM   3908  C C   . THR A 1 480 ? 39.297  36.854  102.282 1.00 87.20  ?  496 THR B C   1 
ATOM   3909  O O   . THR A 1 480 ? 38.782  36.909  101.165 1.00 83.52  ?  496 THR B O   1 
ATOM   3910  C CB  . THR A 1 480 ? 41.570  36.881  101.640 1.00 85.14  ?  496 THR B CB  1 
ATOM   3911  O OG1 . THR A 1 480 ? 41.480  35.502  101.974 1.00 84.36  ?  496 THR B OG1 1 
ATOM   3912  C CG2 . THR A 1 480 ? 42.990  37.373  101.795 1.00 88.86  ?  496 THR B CG2 1 
ATOM   3913  N N   . TYR A 1 481 ? 38.841  36.115  103.310 1.00 86.96  ?  497 TYR B N   1 
ATOM   3914  C CA  . TYR A 1 481 ? 37.626  35.344  103.089 1.00 84.18  ?  497 TYR B CA  1 
ATOM   3915  C C   . TYR A 1 481 ? 36.370  36.136  103.391 1.00 83.31  ?  497 TYR B C   1 
ATOM   3916  O O   . TYR A 1 481 ? 36.391  37.209  104.008 1.00 83.90  ?  497 TYR B O   1 
ATOM   3917  C CB  . TYR A 1 481 ? 37.609  34.083  103.942 1.00 84.38  ?  497 TYR B CB  1 
ATOM   3918  C CG  . TYR A 1 481 ? 38.576  33.053  103.502 1.00 82.47  ?  497 TYR B CG  1 
ATOM   3919  C CD1 . TYR A 1 481 ? 39.917  33.153  103.793 1.00 82.96  ?  497 TYR B CD1 1 
ATOM   3920  C CD2 . TYR A 1 481 ? 38.134  31.957  102.791 1.00 85.29  ?  497 TYR B CD2 1 
ATOM   3921  C CE1 . TYR A 1 481 ? 40.784  32.193  103.359 1.00 84.95  ?  497 TYR B CE1 1 
ATOM   3922  C CE2 . TYR A 1 481 ? 38.986  31.002  102.371 1.00 83.73  ?  497 TYR B CE2 1 
ATOM   3923  C CZ  . TYR A 1 481 ? 40.302  31.116  102.649 1.00 82.70  ?  497 TYR B CZ  1 
ATOM   3924  O OH  . TYR A 1 481 ? 41.138  30.135  102.200 1.00 85.50  ?  497 TYR B OH  1 
ATOM   3925  N N   . CYS A 1 482 ? 35.245  35.568  102.963 1.00 81.44  ?  498 CYS B N   1 
ATOM   3926  C CA  . CYS A 1 482 ? 33.949  36.084  103.337 1.00 81.71  ?  498 CYS B CA  1 
ATOM   3927  C C   . CYS A 1 482 ? 32.983  34.901  103.346 1.00 83.59  ?  498 CYS B C   1 
ATOM   3928  O O   . CYS A 1 482 ? 32.116  34.744  102.491 1.00 81.41  ?  498 CYS B O   1 
ATOM   3929  C CB  . CYS A 1 482 ? 33.491  37.212  102.414 1.00 77.30  ?  498 CYS B CB  1 
ATOM   3930  S SG  . CYS A 1 482 ? 32.103  38.121  103.087 1.00 72.73  ?  498 CYS B SG  1 
ATOM   3931  N N   . ASP A 1 483 ? 33.136  34.028  104.341 1.00 94.68  ?  499 ASP B N   1 
ATOM   3932  C CA  . ASP A 1 483 ? 32.258  32.865  104.412 1.00 93.60  ?  499 ASP B CA  1 
ATOM   3933  C C   . ASP A 1 483 ? 30.786  33.192  104.620 1.00 90.41  ?  499 ASP B C   1 
ATOM   3934  O O   . ASP A 1 483 ? 29.952  32.541  103.968 1.00 91.41  ?  499 ASP B O   1 
ATOM   3935  C CB  . ASP A 1 483 ? 32.777  31.915  105.482 1.00 92.75  ?  499 ASP B CB  1 
ATOM   3936  C CG  . ASP A 1 483 ? 34.200  31.498  105.217 1.00 95.30  ?  499 ASP B CG  1 
ATOM   3937  O OD1 . ASP A 1 483 ? 34.649  31.634  104.051 1.00 92.71  ?  499 ASP B OD1 1 
ATOM   3938  O OD2 . ASP A 1 483 ? 34.861  31.038  106.177 1.00 96.02  -1 499 ASP B OD2 1 
ATOM   3939  N N   . PRO A 1 484 ? 30.386  34.161  105.472 1.00 85.42  ?  500 PRO B N   1 
ATOM   3940  C CA  . PRO A 1 484 ? 28.978  34.567  105.483 1.00 80.54  ?  500 PRO B CA  1 
ATOM   3941  C C   . PRO A 1 484 ? 28.386  34.652  104.084 1.00 81.54  ?  500 PRO B C   1 
ATOM   3942  O O   . PRO A 1 484 ? 27.467  33.906  103.737 1.00 79.64  ?  500 PRO B O   1 
ATOM   3943  C CB  . PRO A 1 484 ? 29.022  35.940  106.160 1.00 76.22  ?  500 PRO B CB  1 
ATOM   3944  C CG  . PRO A 1 484 ? 30.179  35.907  107.016 1.00 75.72  ?  500 PRO B CG  1 
ATOM   3945  C CD  . PRO A 1 484 ? 31.177  34.948  106.434 1.00 81.99  ?  500 PRO B CD  1 
ATOM   3946  N N   . ALA A 1 485 ? 28.980  35.510  103.260 1.00 76.17  ?  501 ALA B N   1 
ATOM   3947  C CA  . ALA A 1 485 ? 28.523  35.840  101.915 1.00 73.24  ?  501 ALA B CA  1 
ATOM   3948  C C   . ALA A 1 485 ? 28.535  34.655  100.950 1.00 71.69  ?  501 ALA B C   1 
ATOM   3949  O O   . ALA A 1 485 ? 28.157  34.788  99.779  1.00 64.59  ?  501 ALA B O   1 
ATOM   3950  C CB  . ALA A 1 485 ? 29.384  36.985  101.360 1.00 70.53  ?  501 ALA B CB  1 
ATOM   3951  N N   . SER A 1 486 ? 28.973  33.490  101.410 1.00 80.20  ?  502 SER B N   1 
ATOM   3952  C CA  . SER A 1 486 ? 28.978  32.344  100.514 1.00 81.72  ?  502 SER B CA  1 
ATOM   3953  C C   . SER A 1 486 ? 27.647  31.617  100.513 1.00 79.74  ?  502 SER B C   1 
ATOM   3954  O O   . SER A 1 486 ? 27.482  30.644  99.767  1.00 80.59  ?  502 SER B O   1 
ATOM   3955  C CB  . SER A 1 486 ? 30.083  31.350  100.882 1.00 83.30  ?  502 SER B CB  1 
ATOM   3956  O OG  . SER A 1 486 ? 29.649  30.483  101.899 1.00 87.88  ?  502 SER B OG  1 
ATOM   3957  N N   . LEU A 1 487 ? 26.709  32.047  101.346 1.00 77.38  ?  503 LEU B N   1 
ATOM   3958  C CA  . LEU A 1 487 ? 25.374  31.476  101.367 1.00 74.71  ?  503 LEU B CA  1 
ATOM   3959  C C   . LEU A 1 487 ? 24.441  32.441  100.644 1.00 69.22  ?  503 LEU B C   1 
ATOM   3960  O O   . LEU A 1 487 ? 24.613  33.666  100.717 1.00 66.91  ?  503 LEU B O   1 
ATOM   3961  C CB  . LEU A 1 487 ? 24.916  31.214  102.810 1.00 71.02  ?  503 LEU B CB  1 
ATOM   3962  C CG  . LEU A 1 487 ? 23.482  30.738  103.039 1.00 65.90  ?  503 LEU B CG  1 
ATOM   3963  C CD1 . LEU A 1 487 ? 23.360  29.332  102.556 1.00 63.81  ?  503 LEU B CD1 1 
ATOM   3964  C CD2 . LEU A 1 487 ? 23.101  30.799  104.501 1.00 61.77  ?  503 LEU B CD2 1 
ATOM   3965  N N   . PHE A 1 488 ? 23.483  31.873  99.909  1.00 71.21  ?  504 PHE B N   1 
ATOM   3966  C CA  . PHE A 1 488 ? 22.672  32.663  98.988  1.00 70.39  ?  504 PHE B CA  1 
ATOM   3967  C C   . PHE A 1 488 ? 22.048  33.870  99.678  1.00 68.99  ?  504 PHE B C   1 
ATOM   3968  O O   . PHE A 1 488 ? 22.191  35.013  99.216  1.00 69.95  ?  504 PHE B O   1 
ATOM   3969  C CB  . PHE A 1 488 ? 21.593  31.782  98.353  1.00 68.57  ?  504 PHE B CB  1 
ATOM   3970  C CG  . PHE A 1 488 ? 20.519  32.559  97.646  1.00 69.64  ?  504 PHE B CG  1 
ATOM   3971  C CD1 . PHE A 1 488 ? 20.722  33.054  96.363  1.00 73.49  ?  504 PHE B CD1 1 
ATOM   3972  C CD2 . PHE A 1 488 ? 19.288  32.768  98.246  1.00 70.38  ?  504 PHE B CD2 1 
ATOM   3973  C CE1 . PHE A 1 488 ? 19.730  33.771  95.704  1.00 74.43  ?  504 PHE B CE1 1 
ATOM   3974  C CE2 . PHE A 1 488 ? 18.301  33.482  97.596  1.00 73.64  ?  504 PHE B CE2 1 
ATOM   3975  C CZ  . PHE A 1 488 ? 18.521  33.986  96.326  1.00 75.09  ?  504 PHE B CZ  1 
ATOM   3976  N N   . HIS A 1 489 ? 21.362  33.630  100.799 1.00 64.07  ?  505 HIS B N   1 
ATOM   3977  C CA  . HIS A 1 489 ? 20.597  34.687  101.444 1.00 61.06  ?  505 HIS B CA  1 
ATOM   3978  C C   . HIS A 1 489 ? 21.495  35.848  101.840 1.00 62.29  ?  505 HIS B C   1 
ATOM   3979  O O   . HIS A 1 489 ? 21.058  37.000  101.829 1.00 64.51  ?  505 HIS B O   1 
ATOM   3980  C CB  . HIS A 1 489 ? 19.871  34.124  102.659 1.00 55.19  ?  505 HIS B CB  1 
ATOM   3981  C CG  . HIS A 1 489 ? 18.957  32.986  102.341 1.00 62.06  ?  505 HIS B CG  1 
ATOM   3982  N ND1 . HIS A 1 489 ? 19.416  31.765  101.899 1.00 64.08  ?  505 HIS B ND1 1 
ATOM   3983  C CD2 . HIS A 1 489 ? 17.607  32.874  102.410 1.00 65.74  ?  505 HIS B CD2 1 
ATOM   3984  C CE1 . HIS A 1 489 ? 18.391  30.951  101.703 1.00 67.33  ?  505 HIS B CE1 1 
ATOM   3985  N NE2 . HIS A 1 489 ? 17.280  31.599  102.007 1.00 65.77  ?  505 HIS B NE2 1 
ATOM   3986  N N   . VAL A 1 490 ? 22.754  35.568  102.171 1.00 63.19  ?  506 VAL B N   1 
ATOM   3987  C CA  . VAL A 1 490 ? 23.641  36.622  102.636 1.00 66.92  ?  506 VAL B CA  1 
ATOM   3988  C C   . VAL A 1 490 ? 24.030  37.535  101.491 1.00 65.41  ?  506 VAL B C   1 
ATOM   3989  O O   . VAL A 1 490 ? 23.890  38.765  101.582 1.00 63.87  ?  506 VAL B O   1 
ATOM   3990  C CB  . VAL A 1 490 ? 24.871  36.008  103.326 1.00 70.19  ?  506 VAL B CB  1 
ATOM   3991  C CG1 . VAL A 1 490 ? 25.838  37.092  103.754 1.00 67.45  ?  506 VAL B CG1 1 
ATOM   3992  C CG2 . VAL A 1 490 ? 24.399  35.250  104.555 1.00 66.37  ?  506 VAL B CG2 1 
ATOM   3993  N N   . SER A 1 491 ? 24.527  36.940  100.405 1.00 59.32  ?  507 SER B N   1 
ATOM   3994  C CA  . SER A 1 491 ? 24.978  37.637  99.206  1.00 62.98  ?  507 SER B CA  1 
ATOM   3995  C C   . SER A 1 491 ? 23.842  38.095  98.318  1.00 65.91  ?  507 SER B C   1 
ATOM   3996  O O   . SER A 1 491 ? 24.107  38.576  97.213  1.00 69.59  ?  507 SER B O   1 
ATOM   3997  C CB  . SER A 1 491 ? 25.860  36.734  98.363  1.00 65.92  ?  507 SER B CB  1 
ATOM   3998  O OG  . SER A 1 491 ? 25.200  35.499  98.206  1.00 64.75  ?  507 SER B OG  1 
ATOM   3999  N N   . ASN A 1 492 ? 22.597  37.896  98.727  1.00 66.02  ?  508 ASN B N   1 
ATOM   4000  C CA  . ASN A 1 492 ? 21.467  38.380  97.957  1.00 64.66  ?  508 ASN B CA  1 
ATOM   4001  C C   . ASN A 1 492 ? 20.571  39.266  98.813  1.00 61.84  ?  508 ASN B C   1 
ATOM   4002  O O   . ASN A 1 492 ? 19.438  39.548  98.426  1.00 64.89  ?  508 ASN B O   1 
ATOM   4003  C CB  . ASN A 1 492 ? 20.691  37.190  97.358  1.00 68.57  ?  508 ASN B CB  1 
ATOM   4004  C CG  . ASN A 1 492 ? 21.483  36.462  96.250  1.00 71.03  ?  508 ASN B CG  1 
ATOM   4005  O OD1 . ASN A 1 492 ? 21.243  36.622  95.043  1.00 70.79  ?  508 ASN B OD1 1 
ATOM   4006  N ND2 . ASN A 1 492 ? 22.483  35.706  96.677  1.00 70.89  ?  508 ASN B ND2 1 
ATOM   4007  N N   . ASP A 1 493 ? 21.052  39.700  99.974  1.00 61.84  ?  509 ASP B N   1 
ATOM   4008  C CA  . ASP A 1 493 ? 20.414  40.754  100.746 1.00 64.14  ?  509 ASP B CA  1 
ATOM   4009  C C   . ASP A 1 493 ? 18.987  40.368  101.145 1.00 60.66  ?  509 ASP B C   1 
ATOM   4010  O O   . ASP A 1 493 ? 18.032  41.119  100.946 1.00 68.86  ?  509 ASP B O   1 
ATOM   4011  C CB  . ASP A 1 493 ? 20.509  42.067  99.956  1.00 64.54  ?  509 ASP B CB  1 
ATOM   4012  C CG  . ASP A 1 493 ? 20.012  43.258  100.712 1.00 61.27  ?  509 ASP B CG  1 
ATOM   4013  O OD1 . ASP A 1 493 ? 20.224  43.341  101.932 1.00 61.32  ?  509 ASP B OD1 1 
ATOM   4014  O OD2 . ASP A 1 493 ? 19.532  44.197  100.051 1.00 65.03  -1 509 ASP B OD2 1 
ATOM   4015  N N   . TYR A 1 494 ? 18.854  39.174  101.732 1.00 52.34  ?  510 TYR B N   1 
ATOM   4016  C CA  . TYR A 1 494 ? 17.608  38.686  102.321 1.00 58.67  ?  510 TYR B CA  1 
ATOM   4017  C C   . TYR A 1 494 ? 17.708  38.595  103.846 1.00 55.54  ?  510 TYR B C   1 
ATOM   4018  O O   . TYR A 1 494 ? 18.657  38.006  104.367 1.00 58.07  ?  510 TYR B O   1 
ATOM   4019  C CB  . TYR A 1 494 ? 17.256  37.317  101.733 1.00 62.54  ?  510 TYR B CB  1 
ATOM   4020  C CG  . TYR A 1 494 ? 16.749  37.410  100.320 1.00 65.97  ?  510 TYR B CG  1 
ATOM   4021  C CD1 . TYR A 1 494 ? 15.476  37.890  100.054 1.00 67.45  ?  510 TYR B CD1 1 
ATOM   4022  C CD2 . TYR A 1 494 ? 17.554  37.066  99.246  1.00 68.17  ?  510 TYR B CD2 1 
ATOM   4023  C CE1 . TYR A 1 494 ? 15.011  38.013  98.750  1.00 69.64  ?  510 TYR B CE1 1 
ATOM   4024  C CE2 . TYR A 1 494 ? 17.094  37.181  97.940  1.00 69.01  ?  510 TYR B CE2 1 
ATOM   4025  C CZ  . TYR A 1 494 ? 15.823  37.657  97.698  1.00 69.92  ?  510 TYR B CZ  1 
ATOM   4026  O OH  . TYR A 1 494 ? 15.373  37.771  96.399  1.00 65.78  ?  510 TYR B OH  1 
ATOM   4027  N N   . SER A 1 495 ? 16.728  39.143  104.573 1.00 49.91  ?  511 SER B N   1 
ATOM   4028  C CA  . SER A 1 495 ? 16.818  38.979  106.019 1.00 52.13  ?  511 SER B CA  1 
ATOM   4029  C C   . SER A 1 495 ? 16.695  37.493  106.329 1.00 53.90  ?  511 SER B C   1 
ATOM   4030  O O   . SER A 1 495 ? 15.955  36.759  105.670 1.00 57.16  ?  511 SER B O   1 
ATOM   4031  C CB  . SER A 1 495 ? 15.735  39.746  106.793 1.00 52.05  ?  511 SER B CB  1 
ATOM   4032  O OG  . SER A 1 495 ? 14.443  39.190  106.653 1.00 57.55  ?  511 SER B OG  1 
ATOM   4033  N N   . PHE A 1 496 ? 17.453  37.031  107.322 1.00 55.42  ?  512 PHE B N   1 
ATOM   4034  C CA  . PHE A 1 496 ? 17.471  35.616  107.649 1.00 51.16  ?  512 PHE B CA  1 
ATOM   4035  C C   . PHE A 1 496 ? 16.660  35.220  108.879 1.00 51.40  ?  512 PHE B C   1 
ATOM   4036  O O   . PHE A 1 496 ? 16.204  34.071  108.931 1.00 52.91  ?  512 PHE B O   1 
ATOM   4037  C CB  . PHE A 1 496 ? 18.906  35.139  107.853 1.00 52.40  ?  512 PHE B CB  1 
ATOM   4038  C CG  . PHE A 1 496 ? 19.140  33.699  107.468 1.00 51.92  ?  512 PHE B CG  1 
ATOM   4039  C CD1 . PHE A 1 496 ? 19.016  33.283  106.154 1.00 51.45  ?  512 PHE B CD1 1 
ATOM   4040  C CD2 . PHE A 1 496 ? 19.446  32.748  108.450 1.00 52.94  ?  512 PHE B CD2 1 
ATOM   4041  C CE1 . PHE A 1 496 ? 19.239  31.947  105.820 1.00 56.29  ?  512 PHE B CE1 1 
ATOM   4042  C CE2 . PHE A 1 496 ? 19.656  31.421  108.132 1.00 53.69  ?  512 PHE B CE2 1 
ATOM   4043  C CZ  . PHE A 1 496 ? 19.548  31.013  106.812 1.00 58.48  ?  512 PHE B CZ  1 
ATOM   4044  N N   . ILE A 1 497 ? 16.457  36.108  109.865 1.00 52.01  ?  513 ILE B N   1 
ATOM   4045  C CA  . ILE A 1 497 ? 15.818  35.676  111.118 1.00 54.41  ?  513 ILE B CA  1 
ATOM   4046  C C   . ILE A 1 497 ? 14.393  35.145  110.887 1.00 57.80  ?  513 ILE B C   1 
ATOM   4047  O O   . ILE A 1 497 ? 13.876  34.384  111.721 1.00 57.03  ?  513 ILE B O   1 
ATOM   4048  C CB  . ILE A 1 497 ? 15.844  36.804  112.188 1.00 52.10  ?  513 ILE B CB  1 
ATOM   4049  C CG1 . ILE A 1 497 ? 15.875  36.232  113.597 1.00 53.90  ?  513 ILE B CG1 1 
ATOM   4050  C CG2 . ILE A 1 497 ? 14.616  37.666  112.150 1.00 52.07  ?  513 ILE B CG2 1 
ATOM   4051  C CD1 . ILE A 1 497 ? 17.083  35.399  113.885 1.00 54.04  ?  513 ILE B CD1 1 
ATOM   4052  N N   . ARG A 1 498 ? 13.764  35.478  109.743 1.00 58.11  ?  514 ARG B N   1 
ATOM   4053  C CA  . ARG A 1 498 ? 12.412  34.997  109.467 1.00 51.68  ?  514 ARG B CA  1 
ATOM   4054  C C   . ARG A 1 498 ? 12.327  33.480  109.565 1.00 53.11  ?  514 ARG B C   1 
ATOM   4055  O O   . ARG A 1 498 ? 11.240  32.969  109.833 1.00 50.34  ?  514 ARG B O   1 
ATOM   4056  C CB  . ARG A 1 498 ? 11.941  35.426  108.074 1.00 51.60  ?  514 ARG B CB  1 
ATOM   4057  C CG  . ARG A 1 498 ? 12.439  34.544  106.923 1.00 52.02  ?  514 ARG B CG  1 
ATOM   4058  C CD  . ARG A 1 498 ? 12.928  35.342  105.736 1.00 55.93  ?  514 ARG B CD  1 
ATOM   4059  N NE  . ARG A 1 498 ? 11.876  36.088  105.062 1.00 64.76  ?  514 ARG B NE  1 
ATOM   4060  C CZ  . ARG A 1 498 ? 12.106  37.142  104.282 1.00 70.74  ?  514 ARG B CZ  1 
ATOM   4061  N NH1 . ARG A 1 498 ? 13.341  37.545  104.005 1.00 63.62  ?  514 ARG B NH1 1 
ATOM   4062  N NH2 . ARG A 1 498 ? 11.074  37.822  103.781 1.00 77.32  ?  514 ARG B NH2 1 
ATOM   4063  N N   . TYR A 1 499 ? 13.446  32.750  109.370 1.00 54.21  ?  515 TYR B N   1 
ATOM   4064  C CA  . TYR A 1 499 ? 13.427  31.288  109.475 1.00 53.02  ?  515 TYR B CA  1 
ATOM   4065  C C   . TYR A 1 499 ? 13.391  30.816  110.912 1.00 52.39  ?  515 TYR B C   1 
ATOM   4066  O O   . TYR A 1 499 ? 12.721  29.822  111.226 1.00 57.30  ?  515 TYR B O   1 
ATOM   4067  C CB  . TYR A 1 499 ? 14.616  30.683  108.753 1.00 51.16  ?  515 TYR B CB  1 
ATOM   4068  C CG  . TYR A 1 499 ? 14.647  30.990  107.285 1.00 52.70  ?  515 TYR B CG  1 
ATOM   4069  C CD1 . TYR A 1 499 ? 13.765  30.374  106.408 1.00 54.61  ?  515 TYR B CD1 1 
ATOM   4070  C CD2 . TYR A 1 499 ? 15.493  31.957  106.777 1.00 58.14  ?  515 TYR B CD2 1 
ATOM   4071  C CE1 . TYR A 1 499 ? 13.773  30.675  105.024 1.00 59.15  ?  515 TYR B CE1 1 
ATOM   4072  C CE2 . TYR A 1 499 ? 15.508  32.271  105.402 1.00 60.43  ?  515 TYR B CE2 1 
ATOM   4073  C CZ  . TYR A 1 499 ? 14.648  31.632  104.530 1.00 60.08  ?  515 TYR B CZ  1 
ATOM   4074  O OH  . TYR A 1 499 ? 14.676  31.955  103.183 1.00 60.45  ?  515 TYR B OH  1 
ATOM   4075  N N   . TYR A 1 500 ? 14.062  31.539  111.803 1.00 50.89  ?  516 TYR B N   1 
ATOM   4076  C CA  . TYR A 1 500 ? 13.970  31.223  113.228 1.00 52.50  ?  516 TYR B CA  1 
ATOM   4077  C C   . TYR A 1 500 ? 12.539  31.409  113.761 1.00 57.53  ?  516 TYR B C   1 
ATOM   4078  O O   . TYR A 1 500 ? 11.933  30.469  114.319 1.00 58.41  ?  516 TYR B O   1 
ATOM   4079  C CB  . TYR A 1 500 ? 15.022  32.054  113.987 1.00 50.98  ?  516 TYR B CB  1 
ATOM   4080  C CG  . TYR A 1 500 ? 15.088  31.752  115.450 1.00 47.76  ?  516 TYR B CG  1 
ATOM   4081  C CD1 . TYR A 1 500 ? 14.286  32.430  116.318 1.00 50.96  ?  516 TYR B CD1 1 
ATOM   4082  C CD2 . TYR A 1 500 ? 15.828  30.694  115.941 1.00 49.97  ?  516 TYR B CD2 1 
ATOM   4083  C CE1 . TYR A 1 500 ? 14.287  32.146  117.644 1.00 54.05  ?  516 TYR B CE1 1 
ATOM   4084  C CE2 . TYR A 1 500 ? 15.817  30.392  117.287 1.00 52.07  ?  516 TYR B CE2 1 
ATOM   4085  C CZ  . TYR A 1 500 ? 15.033  31.132  118.129 1.00 51.83  ?  516 TYR B CZ  1 
ATOM   4086  O OH  . TYR A 1 500 ? 14.965  30.884  119.478 1.00 56.95  ?  516 TYR B OH  1 
ATOM   4087  N N   . THR A 1 501 ? 11.961  32.602  113.538 1.00 59.86  ?  517 THR B N   1 
ATOM   4088  C CA  . THR A 1 501 ? 10.600  32.915  113.981 1.00 54.85  ?  517 THR B CA  1 
ATOM   4089  C C   . THR A 1 501 ? 9.535   32.083  113.265 1.00 56.12  ?  517 THR B C   1 
ATOM   4090  O O   . THR A 1 501 ? 8.549   31.688  113.894 1.00 55.63  ?  517 THR B O   1 
ATOM   4091  C CB  . THR A 1 501 ? 10.367  34.408  113.816 1.00 54.36  ?  517 THR B CB  1 
ATOM   4092  O OG1 . THR A 1 501 ? 10.555  34.750  112.444 1.00 57.60  ?  517 THR B OG1 1 
ATOM   4093  C CG2 . THR A 1 501 ? 11.312  35.217  114.678 1.00 59.85  ?  517 THR B CG2 1 
ATOM   4094  N N   . ARG A 1 502 ? 9.687   31.830  111.962 1.00 62.79  ?  518 ARG B N   1 
ATOM   4095  C CA  . ARG A 1 502 ? 8.757   30.918  111.286 1.00 62.43  ?  518 ARG B CA  1 
ATOM   4096  C C   . ARG A 1 502 ? 8.759   29.573  111.979 1.00 62.53  ?  518 ARG B C   1 
ATOM   4097  O O   . ARG A 1 502 ? 7.697   29.006  112.261 1.00 64.63  ?  518 ARG B O   1 
ATOM   4098  C CB  . ARG A 1 502 ? 9.140   30.721  109.817 1.00 66.49  ?  518 ARG B CB  1 
ATOM   4099  C CG  . ARG A 1 502 ? 8.544   29.458  109.157 1.00 66.74  ?  518 ARG B CG  1 
ATOM   4100  C CD  . ARG A 1 502 ? 9.356   28.970  107.939 1.00 70.07  ?  518 ARG B CD  1 
ATOM   4101  N NE  . ARG A 1 502 ? 10.622  28.377  108.341 1.00 71.46  ?  518 ARG B NE  1 
ATOM   4102  C CZ  . ARG A 1 502 ? 10.793  27.076  108.521 1.00 78.05  ?  518 ARG B CZ  1 
ATOM   4103  N NH1 . ARG A 1 502 ? 9.841   26.210  108.207 1.00 80.00  ?  518 ARG B NH1 1 
ATOM   4104  N NH2 . ARG A 1 502 ? 11.957  26.632  109.001 1.00 75.68  ?  518 ARG B NH2 1 
ATOM   4105  N N   . THR A 1 503 ? 9.962   29.044  112.255 1.00 61.22  ?  519 THR B N   1 
ATOM   4106  C CA  . THR A 1 503 ? 10.064  27.733  112.881 1.00 58.78  ?  519 THR B CA  1 
ATOM   4107  C C   . THR A 1 503 ? 9.356   27.710  114.239 1.00 57.32  ?  519 THR B C   1 
ATOM   4108  O O   . THR A 1 503 ? 8.636   26.753  114.540 1.00 58.71  ?  519 THR B O   1 
ATOM   4109  C CB  . THR A 1 503 ? 11.542  27.329  112.967 1.00 56.34  ?  519 THR B CB  1 
ATOM   4110  O OG1 . THR A 1 503 ? 12.064  27.186  111.632 1.00 57.06  ?  519 THR B OG1 1 
ATOM   4111  C CG2 . THR A 1 503 ? 11.719  25.991  113.707 1.00 58.66  ?  519 THR B CG2 1 
ATOM   4112  N N   . LEU A 1 504 ? 9.492   28.765  115.048 1.00 56.47  ?  520 LEU B N   1 
ATOM   4113  C CA  . LEU A 1 504 ? 8.775   28.746  116.333 1.00 56.12  ?  520 LEU B CA  1 
ATOM   4114  C C   . LEU A 1 504 ? 7.275   28.972  116.211 1.00 58.82  ?  520 LEU B C   1 
ATOM   4115  O O   . LEU A 1 504 ? 6.496   28.346  116.956 1.00 62.32  ?  520 LEU B O   1 
ATOM   4116  C CB  . LEU A 1 504 ? 9.348   29.757  117.307 1.00 59.84  ?  520 LEU B CB  1 
ATOM   4117  C CG  . LEU A 1 504 ? 10.499  29.300  118.176 1.00 60.03  ?  520 LEU B CG  1 
ATOM   4118  C CD1 . LEU A 1 504 ? 11.668  28.861  117.381 1.00 58.24  ?  520 LEU B CD1 1 
ATOM   4119  C CD2 . LEU A 1 504 ? 10.893  30.520  119.005 1.00 61.43  ?  520 LEU B CD2 1 
ATOM   4120  N N   . TYR A 1 505 ? 6.833   29.848  115.301 1.00 56.67  ?  521 TYR B N   1 
ATOM   4121  C CA  . TYR A 1 505 ? 5.391   30.018  115.105 1.00 57.43  ?  521 TYR B CA  1 
ATOM   4122  C C   . TYR A 1 505 ? 4.744   28.702  114.691 1.00 53.82  ?  521 TYR B C   1 
ATOM   4123  O O   . TYR A 1 505 ? 3.784   28.238  115.321 1.00 51.24  ?  521 TYR B O   1 
ATOM   4124  C CB  . TYR A 1 505 ? 5.085   31.083  114.051 1.00 53.91  ?  521 TYR B CB  1 
ATOM   4125  C CG  . TYR A 1 505 ? 5.544   32.498  114.332 1.00 52.59  ?  521 TYR B CG  1 
ATOM   4126  C CD1 . TYR A 1 505 ? 5.712   32.977  115.626 1.00 55.14  ?  521 TYR B CD1 1 
ATOM   4127  C CD2 . TYR A 1 505 ? 5.837   33.352  113.284 1.00 49.28  ?  521 TYR B CD2 1 
ATOM   4128  C CE1 . TYR A 1 505 ? 6.156   34.287  115.857 1.00 53.02  ?  521 TYR B CE1 1 
ATOM   4129  C CE2 . TYR A 1 505 ? 6.273   34.640  113.507 1.00 52.01  ?  521 TYR B CE2 1 
ATOM   4130  C CZ  . TYR A 1 505 ? 6.435   35.109  114.792 1.00 53.25  ?  521 TYR B CZ  1 
ATOM   4131  O OH  . TYR A 1 505 ? 6.873   36.408  114.977 1.00 50.19  ?  521 TYR B OH  1 
ATOM   4132  N N   . GLN A 1 506 ? 5.292   28.058  113.658 1.00 54.98  ?  522 GLN B N   1 
ATOM   4133  C CA  . GLN A 1 506 ? 4.598   26.915  113.091 1.00 58.01  ?  522 GLN B CA  1 
ATOM   4134  C C   . GLN A 1 506 ? 4.222   25.911  114.172 1.00 58.02  ?  522 GLN B C   1 
ATOM   4135  O O   . GLN A 1 506 ? 3.150   25.313  114.127 1.00 58.15  ?  522 GLN B O   1 
ATOM   4136  C CB  . GLN A 1 506 ? 5.432   26.254  111.994 1.00 59.82  ?  522 GLN B CB  1 
ATOM   4137  C CG  . GLN A 1 506 ? 6.591   25.409  112.445 1.00 61.07  ?  522 GLN B CG  1 
ATOM   4138  C CD  . GLN A 1 506 ? 7.418   24.951  111.266 1.00 64.82  ?  522 GLN B CD  1 
ATOM   4139  O OE1 . GLN A 1 506 ? 7.754   25.734  110.379 1.00 67.10  ?  522 GLN B OE1 1 
ATOM   4140  N NE2 . GLN A 1 506 ? 7.713   23.659  111.225 1.00 67.19  ?  522 GLN B NE2 1 
ATOM   4141  N N   . PHE A 1 507 ? 5.045   25.756  115.196 1.00 59.27  ?  523 PHE B N   1 
ATOM   4142  C CA  . PHE A 1 507 ? 4.589   24.870  116.249 1.00 58.94  ?  523 PHE B CA  1 
ATOM   4143  C C   . PHE A 1 507 ? 3.579   25.567  117.133 1.00 56.78  ?  523 PHE B C   1 
ATOM   4144  O O   . PHE A 1 507 ? 2.639   24.919  117.583 1.00 60.85  ?  523 PHE B O   1 
ATOM   4145  C CB  . PHE A 1 507 ? 5.788   24.278  117.013 1.00 59.66  ?  523 PHE B CB  1 
ATOM   4146  C CG  . PHE A 1 507 ? 6.587   23.344  116.170 1.00 60.57  ?  523 PHE B CG  1 
ATOM   4147  C CD1 . PHE A 1 507 ? 6.102   22.099  115.851 1.00 60.70  ?  523 PHE B CD1 1 
ATOM   4148  C CD2 . PHE A 1 507 ? 7.732   23.787  115.529 1.00 65.32  ?  523 PHE B CD2 1 
ATOM   4149  C CE1 . PHE A 1 507 ? 6.797   21.273  114.988 1.00 64.74  ?  523 PHE B CE1 1 
ATOM   4150  C CE2 . PHE A 1 507 ? 8.433   22.958  114.653 1.00 65.54  ?  523 PHE B CE2 1 
ATOM   4151  C CZ  . PHE A 1 507 ? 7.959   21.700  114.388 1.00 66.71  ?  523 PHE B CZ  1 
ATOM   4152  N N   . GLN A 1 508 ? 3.753   26.856  117.391 1.00 54.63  ?  524 GLN B N   1 
ATOM   4153  C CA  . GLN A 1 508 ? 2.749   27.535  118.233 1.00 56.52  ?  524 GLN B CA  1 
ATOM   4154  C C   . GLN A 1 508 ? 1.376   27.310  117.614 1.00 63.82  ?  524 GLN B C   1 
ATOM   4155  O O   . GLN A 1 508 ? 0.416   27.092  118.367 1.00 65.91  ?  524 GLN B O   1 
ATOM   4156  C CB  . GLN A 1 508 ? 3.075   29.021  118.352 1.00 57.99  ?  524 GLN B CB  1 
ATOM   4157  C CG  . GLN A 1 508 ? 4.389   29.306  119.059 1.00 64.52  ?  524 GLN B CG  1 
ATOM   4158  C CD  . GLN A 1 508 ? 4.522   30.768  119.398 1.00 62.82  ?  524 GLN B CD  1 
ATOM   4159  O OE1 . GLN A 1 508 ? 5.332   31.487  118.821 1.00 59.03  ?  524 GLN B OE1 1 
ATOM   4160  N NE2 . GLN A 1 508 ? 3.712   31.224  120.337 1.00 64.84  ?  524 GLN B NE2 1 
ATOM   4161  N N   . PHE A 1 509 ? 1.304   27.358  116.288 1.00 63.60  ?  525 PHE B N   1 
ATOM   4162  C CA  . PHE A 1 509 ? 0.010   27.166  115.594 1.00 57.68  ?  525 PHE B CA  1 
ATOM   4163  C C   . PHE A 1 509 ? -0.410  25.709  115.722 1.00 61.67  ?  525 PHE B C   1 
ATOM   4164  O O   . PHE A 1 509 ? -1.427  25.430  116.363 1.00 63.16  ?  525 PHE B O   1 
ATOM   4165  C CB  . PHE A 1 509 ? 0.141   27.486  114.110 1.00 53.37  ?  525 PHE B CB  1 
ATOM   4166  C CG  . PHE A 1 509 ? 0.449   28.921  113.774 1.00 50.12  ?  525 PHE B CG  1 
ATOM   4167  C CD1 . PHE A 1 509 ? -0.008  29.957  114.569 1.00 50.33  ?  525 PHE B CD1 1 
ATOM   4168  C CD2 . PHE A 1 509 ? 1.184   29.229  112.644 1.00 49.72  ?  525 PHE B CD2 1 
ATOM   4169  C CE1 . PHE A 1 509 ? 0.272   31.273  114.241 1.00 48.64  ?  525 PHE B CE1 1 
ATOM   4170  C CE2 . PHE A 1 509 ? 1.461   30.545  112.317 1.00 48.10  ?  525 PHE B CE2 1 
ATOM   4171  C CZ  . PHE A 1 509 ? 1.006   31.562  113.118 1.00 45.03  ?  525 PHE B CZ  1 
ATOM   4172  N N   . GLN A 1 510 ? 0.357   24.806  115.120 1.00 64.75  ?  526 GLN B N   1 
ATOM   4173  C CA  . GLN A 1 510 ? -0.081  23.392  115.122 1.00 65.08  ?  526 GLN B CA  1 
ATOM   4174  C C   . GLN A 1 510 ? -0.554  23.046  116.527 1.00 65.97  ?  526 GLN B C   1 
ATOM   4175  O O   . GLN A 1 510 ? -1.663  22.508  116.654 1.00 73.17  ?  526 GLN B O   1 
ATOM   4176  C CB  . GLN A 1 510 ? 1.027   22.450  114.662 1.00 63.92  ?  526 GLN B CB  1 
ATOM   4177  C CG  . GLN A 1 510 ? 0.547   21.021  114.457 1.00 68.04  ?  526 GLN B CG  1 
ATOM   4178  C CD  . GLN A 1 510 ? -0.118  20.829  113.115 1.00 72.73  ?  526 GLN B CD  1 
ATOM   4179  O OE1 . GLN A 1 510 ? -0.445  21.786  112.420 1.00 67.88  ?  526 GLN B OE1 1 
ATOM   4180  N NE2 . GLN A 1 510 ? -0.321  19.578  112.736 1.00 75.02  ?  526 GLN B NE2 1 
ATOM   4181  N N   . GLU A 1 511 ? 0.234   23.361  117.549 1.00 63.47  ?  527 GLU B N   1 
ATOM   4182  C CA  . GLU A 1 511 ? -0.279  22.956  118.849 1.00 65.84  ?  527 GLU B CA  1 
ATOM   4183  C C   . GLU A 1 511 ? -1.665  23.533  119.102 1.00 71.15  ?  527 GLU B C   1 
ATOM   4184  O O   . GLU A 1 511 ? -2.568  22.825  119.583 1.00 74.41  ?  527 GLU B O   1 
ATOM   4185  C CB  . GLU A 1 511 ? 0.670   23.375  119.959 1.00 68.82  ?  527 GLU B CB  1 
ATOM   4186  C CG  . GLU A 1 511 ? 0.228   22.818  121.287 1.00 75.83  ?  527 GLU B CG  1 
ATOM   4187  C CD  . GLU A 1 511 ? 1.137   23.191  122.431 1.00 81.73  ?  527 GLU B CD  1 
ATOM   4188  O OE1 . GLU A 1 511 ? 1.003   24.304  122.991 1.00 77.05  ?  527 GLU B OE1 1 
ATOM   4189  O OE2 . GLU A 1 511 ? 2.000   22.341  122.759 1.00 87.27  -1 527 GLU B OE2 1 
ATOM   4190  N N   . ALA A 1 512 ? -1.862  24.810  118.764 1.00 67.61  ?  528 ALA B N   1 
ATOM   4191  C CA  . ALA A 1 512 ? -3.170  25.433  118.965 1.00 71.37  ?  528 ALA B CA  1 
ATOM   4192  C C   . ALA A 1 512 ? -4.258  24.754  118.126 1.00 70.74  ?  528 ALA B C   1 
ATOM   4193  O O   . ALA A 1 512 ? -5.362  24.479  118.622 1.00 73.70  ?  528 ALA B O   1 
ATOM   4194  C CB  . ALA A 1 512 ? -3.077  26.930  118.645 1.00 67.28  ?  528 ALA B CB  1 
ATOM   4195  N N   . LEU A 1 513 ? -3.969  24.488  116.851 1.00 69.50  ?  529 LEU B N   1 
ATOM   4196  C CA  . LEU A 1 513 ? -4.961  23.858  115.991 1.00 68.54  ?  529 LEU B CA  1 
ATOM   4197  C C   . LEU A 1 513 ? -5.270  22.443  116.452 1.00 75.29  ?  529 LEU B C   1 
ATOM   4198  O O   . LEU A 1 513 ? -6.443  22.036  116.464 1.00 79.03  ?  529 LEU B O   1 
ATOM   4199  C CB  . LEU A 1 513 ? -4.532  23.892  114.517 1.00 65.05  ?  529 LEU B CB  1 
ATOM   4200  C CG  . LEU A 1 513 ? -4.272  25.235  113.822 1.00 63.53  ?  529 LEU B CG  1 
ATOM   4201  C CD1 . LEU A 1 513 ? -4.151  25.044  112.326 1.00 56.95  ?  529 LEU B CD1 1 
ATOM   4202  C CD2 . LEU A 1 513 ? -5.412  26.234  114.124 1.00 62.57  ?  529 LEU B CD2 1 
ATOM   4203  N N   . CYS A 1 514 ? -4.258  21.683  116.869 1.00 74.75  ?  530 CYS B N   1 
ATOM   4204  C CA  . CYS A 1 514 ? -4.553  20.325  117.301 1.00 75.92  ?  530 CYS B CA  1 
ATOM   4205  C C   . CYS A 1 514 ? -5.396  20.340  118.572 1.00 81.71  ?  530 CYS B C   1 
ATOM   4206  O O   . CYS A 1 514 ? -6.304  19.517  118.725 1.00 82.36  ?  530 CYS B O   1 
ATOM   4207  C CB  . CYS A 1 514 ? -3.256  19.553  117.479 1.00 78.17  ?  530 CYS B CB  1 
ATOM   4208  S SG  . CYS A 1 514 ? -2.461  19.276  115.881 1.00 84.00  ?  530 CYS B SG  1 
ATOM   4209  N N   . GLN A 1 515 ? -5.154  21.299  119.477 1.00 82.10  ?  531 GLN B N   1 
ATOM   4210  C CA  . GLN A 1 515 ? -6.075  21.448  120.597 1.00 83.79  ?  531 GLN B CA  1 
ATOM   4211  C C   . GLN A 1 515 ? -7.476  21.760  120.111 1.00 82.89  ?  531 GLN B C   1 
ATOM   4212  O O   . GLN A 1 515 ? -8.457  21.241  120.659 1.00 89.92  ?  531 GLN B O   1 
ATOM   4213  C CB  . GLN A 1 515 ? -5.610  22.538  121.543 1.00 88.34  ?  531 GLN B CB  1 
ATOM   4214  C CG  . GLN A 1 515 ? -6.516  22.702  122.749 1.00 92.33  ?  531 GLN B CG  1 
ATOM   4215  C CD  . GLN A 1 515 ? -5.870  23.575  123.808 1.00 106.74 ?  531 GLN B CD  1 
ATOM   4216  O OE1 . GLN A 1 515 ? -4.762  23.286  124.270 1.00 113.47 ?  531 GLN B OE1 1 
ATOM   4217  N NE2 . GLN A 1 515 ? -6.551  24.652  124.192 1.00 109.77 ?  531 GLN B NE2 1 
ATOM   4218  N N   . ALA A 1 516 ? -7.593  22.618  119.087 1.00 86.41  ?  532 ALA B N   1 
ATOM   4219  C CA  . ALA A 1 516 ? -8.898  22.890  118.490 1.00 86.60  ?  532 ALA B CA  1 
ATOM   4220  C C   . ALA A 1 516 ? -9.476  21.640  117.836 1.00 86.67  ?  532 ALA B C   1 
ATOM   4221  O O   . ALA A 1 516 ? -10.696 21.462  117.785 1.00 85.75  ?  532 ALA B O   1 
ATOM   4222  C CB  . ALA A 1 516 ? -8.774  24.026  117.482 1.00 79.78  ?  532 ALA B CB  1 
ATOM   4223  N N   . ALA A 1 517 ? -8.626  20.745  117.380 1.00 77.45  ?  533 ALA B N   1 
ATOM   4224  C CA  . ALA A 1 517 ? -9.076  19.509  116.763 1.00 81.96  ?  533 ALA B CA  1 
ATOM   4225  C C   . ALA A 1 517 ? -9.364  18.401  117.770 1.00 87.87  ?  533 ALA B C   1 
ATOM   4226  O O   . ALA A 1 517 ? -9.776  17.314  117.357 1.00 91.26  ?  533 ALA B O   1 
ATOM   4227  C CB  . ALA A 1 517 ? -8.022  19.021  115.749 1.00 79.38  ?  533 ALA B CB  1 
ATOM   4228  N N   . LYS A 1 518 ? -9.147  18.638  119.065 1.00 87.37  ?  534 LYS B N   1 
ATOM   4229  C CA  . LYS A 1 518 ? -9.243  17.600  120.093 1.00 91.39  ?  534 LYS B CA  1 
ATOM   4230  C C   . LYS A 1 518 ? -8.376  16.391  119.756 1.00 94.58  ?  534 LYS B C   1 
ATOM   4231  O O   . LYS A 1 518 ? -8.852  15.260  119.683 1.00 97.71  ?  534 LYS B O   1 
ATOM   4232  C CB  . LYS A 1 518 ? -10.688 17.181  120.304 1.00 92.40  ?  534 LYS B CB  1 
ATOM   4233  C CG  . LYS A 1 518 ? -11.493 18.264  120.893 1.00 97.26  ?  534 LYS B CG  1 
ATOM   4234  C CD  . LYS A 1 518 ? -12.949 17.958  120.719 1.00 110.11 ?  534 LYS B CD  1 
ATOM   4235  C CE  . LYS A 1 518 ? -13.755 19.210  120.934 1.00 117.47 ?  534 LYS B CE  1 
ATOM   4236  N NZ  . LYS A 1 518 ? -13.274 19.890  122.179 1.00 122.51 ?  534 LYS B NZ  1 
ATOM   4237  N N   . HIS A 1 519 ? -7.093  16.642  119.541 1.00 94.40  ?  535 HIS B N   1 
ATOM   4238  C CA  . HIS A 1 519 ? -6.162  15.574  119.221 1.00 98.33  ?  535 HIS B CA  1 
ATOM   4239  C C   . HIS A 1 519 ? -5.696  14.916  120.510 1.00 104.36 ?  535 HIS B C   1 
ATOM   4240  O O   . HIS A 1 519 ? -5.463  15.594  121.510 1.00 106.11 ?  535 HIS B O   1 
ATOM   4241  C CB  . HIS A 1 519 ? -4.966  16.129  118.434 1.00 95.28  ?  535 HIS B CB  1 
ATOM   4242  C CG  . HIS A 1 519 ? -3.868  15.136  118.196 1.00 95.05  ?  535 HIS B CG  1 
ATOM   4243  N ND1 . HIS A 1 519 ? -3.943  14.168  117.217 1.00 95.75  ?  535 HIS B ND1 1 
ATOM   4244  C CD2 . HIS A 1 519 ? -2.664  14.974  118.793 1.00 93.49  ?  535 HIS B CD2 1 
ATOM   4245  C CE1 . HIS A 1 519 ? -2.840  13.442  117.235 1.00 98.00  ?  535 HIS B CE1 1 
ATOM   4246  N NE2 . HIS A 1 519 ? -2.044  13.916  118.177 1.00 94.48  ?  535 HIS B NE2 1 
ATOM   4247  N N   . GLU A 1 520 ? -5.587  13.594  120.496 1.00 110.80 ?  536 GLU B N   1 
ATOM   4248  C CA  . GLU A 1 520 ? -5.013  12.860  121.611 1.00 110.84 ?  536 GLU B CA  1 
ATOM   4249  C C   . GLU A 1 520 ? -3.638  12.369  121.190 1.00 108.74 ?  536 GLU B C   1 
ATOM   4250  O O   . GLU A 1 520 ? -3.423  12.040  120.021 1.00 112.40 ?  536 GLU B O   1 
ATOM   4251  C CB  . GLU A 1 520 ? -5.876  11.665  122.036 1.00 121.39 ?  536 GLU B CB  1 
ATOM   4252  C CG  . GLU A 1 520 ? -7.401  11.857  122.060 1.00 129.66 ?  536 GLU B CG  1 
ATOM   4253  C CD  . GLU A 1 520 ? -7.895  12.832  123.131 1.00 137.75 ?  536 GLU B CD  1 
ATOM   4254  O OE1 . GLU A 1 520 ? -7.119  13.194  124.048 1.00 134.09 ?  536 GLU B OE1 1 
ATOM   4255  O OE2 . GLU A 1 520 ? -9.106  13.172  123.075 1.00 139.02 -1 536 GLU B OE2 1 
ATOM   4256  N N   . GLY A 1 521 ? -2.707  12.336  122.133 1.00 102.32 ?  537 GLY B N   1 
ATOM   4257  C CA  . GLY A 1 521 ? -1.414  11.750  121.877 1.00 101.41 ?  537 GLY B CA  1 
ATOM   4258  C C   . GLY A 1 521 ? -0.283  12.752  121.780 1.00 96.91  ?  537 GLY B C   1 
ATOM   4259  O O   . GLY A 1 521 ? -0.393  13.903  122.209 1.00 96.51  ?  537 GLY B O   1 
ATOM   4260  N N   . PRO A 1 522 ? 0.844   12.314  121.235 1.00 92.23  ?  538 PRO B N   1 
ATOM   4261  C CA  . PRO A 1 522 ? 1.937   13.248  120.980 1.00 89.88  ?  538 PRO B CA  1 
ATOM   4262  C C   . PRO A 1 522 ? 1.575   14.168  119.831 1.00 91.48  ?  538 PRO B C   1 
ATOM   4263  O O   . PRO A 1 522 ? 0.840   13.799  118.914 1.00 90.27  ?  538 PRO B O   1 
ATOM   4264  C CB  . PRO A 1 522 ? 3.120   12.342  120.626 1.00 93.20  ?  538 PRO B CB  1 
ATOM   4265  C CG  . PRO A 1 522 ? 2.691   10.944  121.042 1.00 96.01  ?  538 PRO B CG  1 
ATOM   4266  C CD  . PRO A 1 522 ? 1.208   10.926  120.926 1.00 95.87  ?  538 PRO B CD  1 
ATOM   4267  N N   . LEU A 1 523 ? 2.089   15.388  119.906 1.00 84.78  ?  539 LEU B N   1 
ATOM   4268  C CA  . LEU A 1 523 ? 1.705   16.425  118.961 1.00 80.57  ?  539 LEU B CA  1 
ATOM   4269  C C   . LEU A 1 523 ? 2.165   16.137  117.531 1.00 84.62  ?  539 LEU B C   1 
ATOM   4270  O O   . LEU A 1 523 ? 1.565   16.651  116.579 1.00 86.34  ?  539 LEU B O   1 
ATOM   4271  C CB  . LEU A 1 523 ? 2.246   17.756  119.472 1.00 77.98  ?  539 LEU B CB  1 
ATOM   4272  C CG  . LEU A 1 523 ? 2.132   19.032  118.644 1.00 79.86  ?  539 LEU B CG  1 
ATOM   4273  C CD1 . LEU A 1 523 ? 0.682   19.335  118.271 1.00 77.81  ?  539 LEU B CD1 1 
ATOM   4274  C CD2 . LEU A 1 523 ? 2.768   20.184  119.447 1.00 76.63  ?  539 LEU B CD2 1 
ATOM   4275  N N   . HIS A 1 524 ? 3.206   15.318  117.349 1.00 83.36  ?  540 HIS B N   1 
ATOM   4276  C CA  . HIS A 1 524 ? 3.804   15.133  116.027 1.00 81.34  ?  540 HIS B CA  1 
ATOM   4277  C C   . HIS A 1 524 ? 2.997   14.227  115.115 1.00 84.92  ?  540 HIS B C   1 
ATOM   4278  O O   . HIS A 1 524 ? 3.238   14.226  113.897 1.00 84.59  ?  540 HIS B O   1 
ATOM   4279  C CB  . HIS A 1 524 ? 5.236   14.607  116.183 1.00 81.58  ?  540 HIS B CB  1 
ATOM   4280  C CG  . HIS A 1 524 ? 5.317   13.169  116.591 1.00 84.82  ?  540 HIS B CG  1 
ATOM   4281  N ND1 . HIS A 1 524 ? 5.372   12.788  117.917 1.00 81.83  ?  540 HIS B ND1 1 
ATOM   4282  C CD2 . HIS A 1 524 ? 5.391   12.026  115.863 1.00 86.36  ?  540 HIS B CD2 1 
ATOM   4283  C CE1 . HIS A 1 524 ? 5.442   11.471  117.988 1.00 84.01  ?  540 HIS B CE1 1 
ATOM   4284  N NE2 . HIS A 1 524 ? 5.458   10.985  116.758 1.00 89.01  ?  540 HIS B NE2 1 
ATOM   4285  N N   . LYS A 1 525 ? 2.049   13.479  115.679 1.00 86.54  ?  541 LYS B N   1 
ATOM   4286  C CA  . LYS A 1 525 ? 1.155   12.599  114.947 1.00 86.91  ?  541 LYS B CA  1 
ATOM   4287  C C   . LYS A 1 525 ? -0.126  13.294  114.509 1.00 90.62  ?  541 LYS B C   1 
ATOM   4288  O O   . LYS A 1 525 ? -0.964  12.657  113.859 1.00 96.03  ?  541 LYS B O   1 
ATOM   4289  C CB  . LYS A 1 525 ? 0.785   11.369  115.800 1.00 83.02  ?  541 LYS B CB  1 
ATOM   4290  C CG  . LYS A 1 525 ? 1.946   10.464  116.205 1.00 90.19  ?  541 LYS B CG  1 
ATOM   4291  C CD  . LYS A 1 525 ? 1.568   9.499   117.335 1.00 94.40  ?  541 LYS B CD  1 
ATOM   4292  C CE  . LYS A 1 525 ? 0.475   8.543   116.925 1.00 95.88  ?  541 LYS B CE  1 
ATOM   4293  N NZ  . LYS A 1 525 ? 1.009   7.593   115.915 1.00 105.73 ?  541 LYS B NZ  1 
ATOM   4294  N N   . CYS A 1 526 ? -0.311  14.572  114.837 1.00 87.41  ?  542 CYS B N   1 
ATOM   4295  C CA  . CYS A 1 526 ? -1.629  15.182  114.711 1.00 87.86  ?  542 CYS B CA  1 
ATOM   4296  C C   . CYS A 1 526 ? -1.933  15.600  113.279 1.00 85.74  ?  542 CYS B C   1 
ATOM   4297  O O   . CYS A 1 526 ? -1.138  16.297  112.634 1.00 85.57  ?  542 CYS B O   1 
ATOM   4298  C CB  . CYS A 1 526 ? -1.757  16.389  115.631 1.00 88.29  ?  542 CYS B CB  1 
ATOM   4299  S SG  . CYS A 1 526 ? -3.114  17.502  115.167 1.00 86.82  ?  542 CYS B SG  1 
ATOM   4300  N N   . ASP A 1 527 ? -3.101  15.188  112.793 1.00 82.14  ?  543 ASP B N   1 
ATOM   4301  C CA  . ASP A 1 527 ? -3.607  15.630  111.503 1.00 79.42  ?  543 ASP B CA  1 
ATOM   4302  C C   . ASP A 1 527 ? -4.927  16.352  111.743 1.00 79.80  ?  543 ASP B C   1 
ATOM   4303  O O   . ASP A 1 527 ? -5.909  15.727  112.176 1.00 80.53  ?  543 ASP B O   1 
ATOM   4304  C CB  . ASP A 1 527 ? -3.811  14.456  110.551 1.00 82.21  ?  543 ASP B CB  1 
ATOM   4305  C CG  . ASP A 1 527 ? -4.412  14.887  109.217 1.00 81.17  ?  543 ASP B CG  1 
ATOM   4306  O OD1 . ASP A 1 527 ? -4.500  16.112  108.975 1.00 79.85  ?  543 ASP B OD1 1 
ATOM   4307  O OD2 . ASP A 1 527 ? -4.827  14.008  108.425 1.00 84.45  -1 543 ASP B OD2 1 
ATOM   4308  N N   . ILE A 1 528 ? -4.938  17.662  111.437 1.00 78.83  ?  544 ILE B N   1 
ATOM   4309  C CA  . ILE A 1 528 ? -6.078  18.565  111.630 1.00 74.37  ?  544 ILE B CA  1 
ATOM   4310  C C   . ILE A 1 528 ? -7.197  18.376  110.620 1.00 80.94  ?  544 ILE B C   1 
ATOM   4311  O O   . ILE A 1 528 ? -8.206  19.091  110.696 1.00 83.00  ?  544 ILE B O   1 
ATOM   4312  C CB  . ILE A 1 528 ? -5.646  20.035  111.513 1.00 67.72  ?  544 ILE B CB  1 
ATOM   4313  C CG1 . ILE A 1 528 ? -5.311  20.359  110.070 1.00 62.48  ?  544 ILE B CG1 1 
ATOM   4314  C CG2 . ILE A 1 528 ? -4.442  20.290  112.315 1.00 75.90  ?  544 ILE B CG2 1 
ATOM   4315  C CD1 . ILE A 1 528 ? -5.022  21.770  109.891 1.00 58.19  ?  544 ILE B CD1 1 
ATOM   4316  N N   . SER A 1 529 ? -7.041  17.462  109.664 1.00 81.77  ?  545 SER B N   1 
ATOM   4317  C CA  . SER A 1 529 ? -8.068  17.230  108.666 1.00 76.62  ?  545 SER B CA  1 
ATOM   4318  C C   . SER A 1 529 ? -9.426  17.014  109.302 1.00 78.34  ?  545 SER B C   1 
ATOM   4319  O O   . SER A 1 529 ? -9.542  16.432  110.381 1.00 81.73  ?  545 SER B O   1 
ATOM   4320  C CB  . SER A 1 529 ? -7.711  16.016  107.837 1.00 78.04  ?  545 SER B CB  1 
ATOM   4321  O OG  . SER A 1 529 ? -6.496  16.252  107.182 1.00 75.01  ?  545 SER B OG  1 
ATOM   4322  N N   . ASN A 1 530 ? -10.456 17.467  108.607 1.00 82.99  ?  546 ASN B N   1 
ATOM   4323  C CA  . ASN A 1 530 ? -11.806 17.217  109.058 1.00 87.13  ?  546 ASN B CA  1 
ATOM   4324  C C   . ASN A 1 530 ? -12.068 17.939  110.384 1.00 85.18  ?  546 ASN B C   1 
ATOM   4325  O O   . ASN A 1 530 ? -12.707 17.389  111.277 1.00 93.37  ?  546 ASN B O   1 
ATOM   4326  C CB  . ASN A 1 530 ? -12.061 15.700  109.203 1.00 93.29  ?  546 ASN B CB  1 
ATOM   4327  C CG  . ASN A 1 530 ? -12.105 14.945  107.859 1.00 98.90  ?  546 ASN B CG  1 
ATOM   4328  O OD1 . ASN A 1 530 ? -11.616 15.446  106.838 1.00 96.33  ?  546 ASN B OD1 1 
ATOM   4329  N ND2 . ASN A 1 530 ? -12.675 13.702  107.879 1.00 105.29 ?  546 ASN B ND2 1 
ATOM   4330  N N   . SER A 1 531 ? -11.554 19.154  110.558 1.00 80.25  ?  547 SER B N   1 
ATOM   4331  C CA  . SER A 1 531 ? -11.859 19.852  111.814 1.00 83.94  ?  547 SER B CA  1 
ATOM   4332  C C   . SER A 1 531 ? -12.140 21.311  111.526 1.00 83.24  ?  547 SER B C   1 
ATOM   4333  O O   . SER A 1 531 ? -11.221 22.130  111.512 1.00 80.49  ?  547 SER B O   1 
ATOM   4334  C CB  . SER A 1 531 ? -10.752 19.723  112.844 1.00 87.50  ?  547 SER B CB  1 
ATOM   4335  O OG  . SER A 1 531 ? -11.099 20.493  113.985 1.00 87.29  ?  547 SER B OG  1 
ATOM   4336  N N   . THR A 1 532 ? -13.417 21.627  111.354 1.00 82.42  ?  548 THR B N   1 
ATOM   4337  C CA  . THR A 1 532 ? -13.777 22.987  110.994 1.00 79.72  ?  548 THR B CA  1 
ATOM   4338  C C   . THR A 1 532 ? -13.454 23.979  112.105 1.00 82.94  ?  548 THR B C   1 
ATOM   4339  O O   . THR A 1 532 ? -13.134 25.130  111.810 1.00 80.46  ?  548 THR B O   1 
ATOM   4340  C CB  . THR A 1 532 ? -15.253 23.074  110.650 1.00 78.37  ?  548 THR B CB  1 
ATOM   4341  O OG1 . THR A 1 532 ? -16.025 22.607  111.763 1.00 81.00  ?  548 THR B OG1 1 
ATOM   4342  C CG2 . THR A 1 532 ? -15.527 22.186  109.456 1.00 76.08  ?  548 THR B CG2 1 
ATOM   4343  N N   . GLU A 1 533 ? -13.557 23.576  113.379 1.00 88.37  ?  549 GLU B N   1 
ATOM   4344  C CA  . GLU A 1 533 ? -13.106 24.465  114.446 1.00 87.55  ?  549 GLU B CA  1 
ATOM   4345  C C   . GLU A 1 533 ? -11.653 24.861  114.247 1.00 79.75  ?  549 GLU B C   1 
ATOM   4346  O O   . GLU A 1 533 ? -11.290 26.011  114.523 1.00 79.52  ?  549 GLU B O   1 
ATOM   4347  C CB  . GLU A 1 533 ? -13.328 23.842  115.839 1.00 93.87  ?  549 GLU B CB  1 
ATOM   4348  C CG  . GLU A 1 533 ? -14.641 23.066  116.066 1.00 96.02  ?  549 GLU B CG  1 
ATOM   4349  C CD  . GLU A 1 533 ? -14.632 21.623  115.552 1.00 103.38 ?  549 GLU B CD  1 
ATOM   4350  O OE1 . GLU A 1 533 ? -13.830 20.803  116.068 1.00 108.02 ?  549 GLU B OE1 1 
ATOM   4351  O OE2 . GLU A 1 533 ? -15.476 21.303  114.669 1.00 104.98 -1 549 GLU B OE2 1 
ATOM   4352  N N   . ALA A 1 534 ? -10.833 23.954  113.692 1.00 78.64  ?  550 ALA B N   1 
ATOM   4353  C CA  . ALA A 1 534 ? -9.421  24.249  113.435 1.00 74.06  ?  550 ALA B CA  1 
ATOM   4354  C C   . ALA A 1 534 ? -9.258  25.194  112.250 1.00 72.42  ?  550 ALA B C   1 
ATOM   4355  O O   . ALA A 1 534 ? -8.518  26.189  112.330 1.00 72.05  ?  550 ALA B O   1 
ATOM   4356  C CB  . ALA A 1 534 ? -8.642  22.954  113.191 1.00 70.74  ?  550 ALA B CB  1 
ATOM   4357  N N   . GLY A 1 535 ? -9.919  24.892  111.129 1.00 74.55  ?  551 GLY B N   1 
ATOM   4358  C CA  . GLY A 1 535 ? -9.870  25.809  110.003 1.00 70.54  ?  551 GLY B CA  1 
ATOM   4359  C C   . GLY A 1 535 ? -10.382 27.191  110.367 1.00 70.86  ?  551 GLY B C   1 
ATOM   4360  O O   . GLY A 1 535 ? -9.847  28.202  109.919 1.00 64.64  ?  551 GLY B O   1 
ATOM   4361  N N   . GLN A 1 536 ? -11.417 27.249  111.198 1.00 71.20  ?  552 GLN B N   1 
ATOM   4362  C CA  . GLN A 1 536 ? -12.001 28.518  111.609 1.00 68.78  ?  552 GLN B CA  1 
ATOM   4363  C C   . GLN A 1 536 ? -11.035 29.321  112.478 1.00 70.69  ?  552 GLN B C   1 
ATOM   4364  O O   . GLN A 1 536 ? -10.829 30.521  112.242 1.00 70.16  ?  552 GLN B O   1 
ATOM   4365  C CB  . GLN A 1 536 ? -13.318 28.242  112.331 1.00 74.29  ?  552 GLN B CB  1 
ATOM   4366  C CG  . GLN A 1 536 ? -14.026 29.470  112.835 1.00 80.79  ?  552 GLN B CG  1 
ATOM   4367  C CD  . GLN A 1 536 ? -14.463 30.375  111.723 1.00 80.87  ?  552 GLN B CD  1 
ATOM   4368  O OE1 . GLN A 1 536 ? -14.082 31.544  111.691 1.00 78.76  ?  552 GLN B OE1 1 
ATOM   4369  N NE2 . GLN A 1 536 ? -15.268 29.852  110.805 1.00 81.27  ?  552 GLN B NE2 1 
ATOM   4370  N N   . LYS A 1 537 ? -10.429 28.669  113.489 1.00 70.63  ?  553 LYS B N   1 
ATOM   4371  C CA  . LYS A 1 537 ? -9.433  29.331  114.338 1.00 65.90  ?  553 LYS B CA  1 
ATOM   4372  C C   . LYS A 1 537 ? -8.309  29.894  113.494 1.00 60.66  ?  553 LYS B C   1 
ATOM   4373  O O   . LYS A 1 537 ? -7.961  31.071  113.613 1.00 60.18  ?  553 LYS B O   1 
ATOM   4374  C CB  . LYS A 1 537 ? -8.854  28.357  115.373 1.00 64.72  ?  553 LYS B CB  1 
ATOM   4375  C CG  . LYS A 1 537 ? -8.399  28.987  116.688 1.00 63.40  ?  553 LYS B CG  1 
ATOM   4376  C CD  . LYS A 1 537 ? -8.389  27.929  117.797 1.00 69.38  ?  553 LYS B CD  1 
ATOM   4377  C CE  . LYS A 1 537 ? -7.997  28.464  119.187 1.00 76.14  ?  553 LYS B CE  1 
ATOM   4378  N NZ  . LYS A 1 537 ? -8.825  29.658  119.574 1.00 74.68  ?  553 LYS B NZ  1 
ATOM   4379  N N   . LEU A 1 538 ? -7.726  29.055  112.635 1.00 61.69  ?  554 LEU B N   1 
ATOM   4380  C CA  . LEU A 1 538 ? -6.722  29.519  111.684 1.00 61.72  ?  554 LEU B CA  1 
ATOM   4381  C C   . LEU A 1 538 ? -7.215  30.692  110.838 1.00 65.29  ?  554 LEU B C   1 
ATOM   4382  O O   . LEU A 1 538 ? -6.551  31.741  110.766 1.00 59.03  ?  554 LEU B O   1 
ATOM   4383  C CB  . LEU A 1 538 ? -6.281  28.336  110.820 1.00 57.38  ?  554 LEU B CB  1 
ATOM   4384  C CG  . LEU A 1 538 ? -5.277  28.607  109.708 1.00 50.89  ?  554 LEU B CG  1 
ATOM   4385  C CD1 . LEU A 1 538 ? -3.966  29.095  110.221 1.00 55.27  ?  554 LEU B CD1 1 
ATOM   4386  C CD2 . LEU A 1 538 ? -5.071  27.315  108.963 1.00 41.12  ?  554 LEU B CD2 1 
ATOM   4387  N N   . PHE A 1 539 ? -8.369  30.519  110.167 1.00 67.45  ?  555 PHE B N   1 
ATOM   4388  C CA  . PHE A 1 539 ? -8.888  31.504  109.217 1.00 59.72  ?  555 PHE B CA  1 
ATOM   4389  C C   . PHE A 1 539 ? -9.040  32.878  109.839 1.00 58.54  ?  555 PHE B C   1 
ATOM   4390  O O   . PHE A 1 539 ? -8.834  33.892  109.173 1.00 58.46  ?  555 PHE B O   1 
ATOM   4391  C CB  . PHE A 1 539 ? -10.244 31.066  108.678 1.00 57.64  ?  555 PHE B CB  1 
ATOM   4392  C CG  . PHE A 1 539 ? -10.801 32.031  107.674 1.00 58.73  ?  555 PHE B CG  1 
ATOM   4393  C CD1 . PHE A 1 539 ? -10.434 31.969  106.339 1.00 59.62  ?  555 PHE B CD1 1 
ATOM   4394  C CD2 . PHE A 1 539 ? -11.637 33.075  108.099 1.00 60.76  ?  555 PHE B CD2 1 
ATOM   4395  C CE1 . PHE A 1 539 ? -10.933 32.899  105.429 1.00 58.09  ?  555 PHE B CE1 1 
ATOM   4396  C CE2 . PHE A 1 539 ? -12.127 34.005  107.210 1.00 53.94  ?  555 PHE B CE2 1 
ATOM   4397  C CZ  . PHE A 1 539 ? -11.779 33.920  105.876 1.00 56.05  ?  555 PHE B CZ  1 
ATOM   4398  N N   . ASN A 1 540 ? -9.481  32.933  111.089 1.00 58.24  ?  556 ASN B N   1 
ATOM   4399  C CA  . ASN A 1 540 ? -9.701  34.219  111.730 1.00 56.14  ?  556 ASN B CA  1 
ATOM   4400  C C   . ASN A 1 540 ? -8.410  35.045  111.799 1.00 59.32  ?  556 ASN B C   1 
ATOM   4401  O O   . ASN A 1 540 ? -8.465  36.275  111.880 1.00 60.31  ?  556 ASN B O   1 
ATOM   4402  C CB  . ASN A 1 540 ? -10.307 33.948  113.103 1.00 60.45  ?  556 ASN B CB  1 
ATOM   4403  C CG  . ASN A 1 540 ? -11.687 33.347  112.978 1.00 66.75  ?  556 ASN B CG  1 
ATOM   4404  O OD1 . ASN A 1 540 ? -12.232 32.733  113.900 1.00 71.42  ?  556 ASN B OD1 1 
ATOM   4405  N ND2 . ASN A 1 540 ? -12.243 33.472  111.781 1.00 64.45  ?  556 ASN B ND2 1 
ATOM   4406  N N   . MET A 1 541 ? -7.246  34.405  111.716 1.00 54.74  ?  557 MET B N   1 
ATOM   4407  C CA  . MET A 1 541 ? -5.976  35.104  111.575 1.00 55.44  ?  557 MET B CA  1 
ATOM   4408  C C   . MET A 1 541 ? -5.535  35.236  110.133 1.00 56.45  ?  557 MET B C   1 
ATOM   4409  O O   . MET A 1 541 ? -4.897  36.228  109.768 1.00 57.18  ?  557 MET B O   1 
ATOM   4410  C CB  . MET A 1 541 ? -4.885  34.376  112.390 1.00 62.37  ?  557 MET B CB  1 
ATOM   4411  C CG  . MET A 1 541 ? -3.382  34.827  112.254 1.00 50.96  ?  557 MET B CG  1 
ATOM   4412  S SD  . MET A 1 541 ? -2.479  34.057  110.886 1.00 50.05  ?  557 MET B SD  1 
ATOM   4413  C CE  . MET A 1 541 ? -2.463  32.365  111.432 1.00 48.51  ?  557 MET B CE  1 
ATOM   4414  N N   . LEU A 1 542 ? -5.829  34.235  109.316 1.00 57.42  ?  558 LEU B N   1 
ATOM   4415  C CA  . LEU A 1 542 ? -5.544  34.360  107.894 1.00 58.10  ?  558 LEU B CA  1 
ATOM   4416  C C   . LEU A 1 542 ? -6.185  35.615  107.315 1.00 60.69  ?  558 LEU B C   1 
ATOM   4417  O O   . LEU A 1 542 ? -5.503  36.474  106.738 1.00 62.00  ?  558 LEU B O   1 
ATOM   4418  C CB  . LEU A 1 542 ? -6.043  33.125  107.168 1.00 57.50  ?  558 LEU B CB  1 
ATOM   4419  C CG  . LEU A 1 542 ? -5.309  31.921  107.713 1.00 57.91  ?  558 LEU B CG  1 
ATOM   4420  C CD1 . LEU A 1 542 ? -5.818  30.702  106.983 1.00 56.53  ?  558 LEU B CD1 1 
ATOM   4421  C CD2 . LEU A 1 542 ? -3.781  32.115  107.610 1.00 56.73  ?  558 LEU B CD2 1 
ATOM   4422  N N   . ARG A 1 543 ? -7.502  35.746  107.489 1.00 59.84  ?  559 ARG B N   1 
ATOM   4423  C CA  . ARG A 1 543 ? -8.275  36.846  106.919 1.00 59.17  ?  559 ARG B CA  1 
ATOM   4424  C C   . ARG A 1 543 ? -7.690  38.208  107.243 1.00 59.60  ?  559 ARG B C   1 
ATOM   4425  O O   . ARG A 1 543 ? -8.022  39.179  106.559 1.00 66.39  ?  559 ARG B O   1 
ATOM   4426  C CB  . ARG A 1 543 ? -9.732  36.775  107.407 1.00 57.29  ?  559 ARG B CB  1 
ATOM   4427  C CG  . ARG A 1 543 ? -9.935  36.998  108.915 1.00 59.95  ?  559 ARG B CG  1 
ATOM   4428  C CD  . ARG A 1 543 ? -11.328 37.494  109.271 1.00 59.10  ?  559 ARG B CD  1 
ATOM   4429  N NE  . ARG A 1 543 ? -11.679 38.695  108.540 1.00 72.85  ?  559 ARG B NE  1 
ATOM   4430  C CZ  . ARG A 1 543 ? -11.548 39.924  109.015 1.00 78.35  ?  559 ARG B CZ  1 
ATOM   4431  N NH1 . ARG A 1 543 ? -11.104 40.148  110.241 1.00 85.08  ?  559 ARG B NH1 1 
ATOM   4432  N NH2 . ARG A 1 543 ? -11.882 40.957  108.245 1.00 82.90  ?  559 ARG B NH2 1 
ATOM   4433  N N   . LEU A 1 544 ? -6.806  38.304  108.238 1.00 59.98  ?  560 LEU B N   1 
ATOM   4434  C CA  . LEU A 1 544 ? -6.360  39.600  108.739 1.00 60.32  ?  560 LEU B CA  1 
ATOM   4435  C C   . LEU A 1 544 ? -5.391  40.318  107.814 1.00 61.41  ?  560 LEU B C   1 
ATOM   4436  O O   . LEU A 1 544 ? -5.288  41.555  107.888 1.00 60.30  ?  560 LEU B O   1 
ATOM   4437  C CB  . LEU A 1 544 ? -5.715  39.434  110.110 1.00 59.07  ?  560 LEU B CB  1 
ATOM   4438  C CG  . LEU A 1 544 ? -6.707  39.137  111.200 1.00 54.14  ?  560 LEU B CG  1 
ATOM   4439  C CD1 . LEU A 1 544 ? -5.997  39.022  112.516 1.00 55.82  ?  560 LEU B CD1 1 
ATOM   4440  C CD2 . LEU A 1 544 ? -7.571  40.347  111.201 1.00 56.65  ?  560 LEU B CD2 1 
ATOM   4441  N N   . GLY A 1 545 ? -4.683  39.597  106.950 1.00 63.57  ?  561 GLY B N   1 
ATOM   4442  C CA  . GLY A 1 545 ? -3.613  40.277  106.242 1.00 62.04  ?  561 GLY B CA  1 
ATOM   4443  C C   . GLY A 1 545 ? -2.570  40.707  107.235 1.00 54.37  ?  561 GLY B C   1 
ATOM   4444  O O   . GLY A 1 545 ? -2.295  39.996  108.201 1.00 53.65  ?  561 GLY B O   1 
ATOM   4445  N N   . LYS A 1 546 ? -1.981  41.877  107.011 1.00 49.06  ?  562 LYS B N   1 
ATOM   4446  C CA  . LYS A 1 546 ? -1.141  42.486  108.032 1.00 56.81  ?  562 LYS B CA  1 
ATOM   4447  C C   . LYS A 1 546 ? -1.814  43.723  108.618 1.00 58.36  ?  562 LYS B C   1 
ATOM   4448  O O   . LYS A 1 546 ? -1.133  44.663  109.048 1.00 59.43  ?  562 LYS B O   1 
ATOM   4449  C CB  . LYS A 1 546 ? 0.235   42.881  107.507 1.00 53.91  ?  562 LYS B CB  1 
ATOM   4450  C CG  . LYS A 1 546 ? 0.217   43.742  106.275 1.00 53.80  ?  562 LYS B CG  1 
ATOM   4451  C CD  . LYS A 1 546 ? 1.640   44.030  105.836 1.00 61.96  ?  562 LYS B CD  1 
ATOM   4452  C CE  . LYS A 1 546 ? 2.318   45.114  106.685 1.00 67.38  ?  562 LYS B CE  1 
ATOM   4453  N NZ  . LYS A 1 546 ? 3.780   45.186  106.353 1.00 70.27  ?  562 LYS B NZ  1 
ATOM   4454  N N   . SER A 1 547 ? -3.153  43.731  108.616 1.00 54.56  ?  563 SER B N   1 
ATOM   4455  C CA  . SER A 1 547 ? -3.964  44.855  109.082 1.00 54.62  ?  563 SER B CA  1 
ATOM   4456  C C   . SER A 1 547 ? -4.060  44.985  110.603 1.00 55.20  ?  563 SER B C   1 
ATOM   4457  O O   . SER A 1 547 ? -4.450  46.051  111.092 1.00 48.82  ?  563 SER B O   1 
ATOM   4458  C CB  . SER A 1 547 ? -5.374  44.702  108.541 1.00 60.62  ?  563 SER B CB  1 
ATOM   4459  O OG  . SER A 1 547 ? -5.952  43.535  109.097 1.00 58.92  ?  563 SER B OG  1 
ATOM   4460  N N   . GLU A 1 548 ? -3.787  43.914  111.354 1.00 56.59  ?  564 GLU B N   1 
ATOM   4461  C CA  . GLU A 1 548 ? -3.646  43.943  112.803 1.00 54.06  ?  564 GLU B CA  1 
ATOM   4462  C C   . GLU A 1 548 ? -2.211  43.632  113.214 1.00 55.26  ?  564 GLU B C   1 
ATOM   4463  O O   . GLU A 1 548 ? -1.440  43.080  112.422 1.00 52.36  ?  564 GLU B O   1 
ATOM   4464  C CB  . GLU A 1 548 ? -4.597  42.961  113.500 1.00 53.26  ?  564 GLU B CB  1 
ATOM   4465  C CG  . GLU A 1 548 ? -6.103  43.195  113.345 1.00 56.05  ?  564 GLU B CG  1 
ATOM   4466  C CD  . GLU A 1 548 ? -6.627  44.458  114.055 1.00 61.35  ?  564 GLU B CD  1 
ATOM   4467  O OE1 . GLU A 1 548 ? -5.850  45.190  114.722 1.00 58.60  ?  564 GLU B OE1 1 
ATOM   4468  O OE2 . GLU A 1 548 ? -7.872  44.635  114.060 1.00 64.72  -1 564 GLU B OE2 1 
ATOM   4469  N N   . PRO A 1 549 ? -1.802  44.035  114.430 1.00 56.58  ?  565 PRO B N   1 
ATOM   4470  C CA  . PRO A 1 549 ? -0.437  43.772  114.880 1.00 55.55  ?  565 PRO B CA  1 
ATOM   4471  C C   . PRO A 1 549 ? -0.161  42.275  114.957 1.00 57.02  ?  565 PRO B C   1 
ATOM   4472  O O   . PRO A 1 549 ? -1.020  41.496  115.393 1.00 54.71  ?  565 PRO B O   1 
ATOM   4473  C CB  . PRO A 1 549 ? -0.404  44.412  116.272 1.00 56.01  ?  565 PRO B CB  1 
ATOM   4474  C CG  . PRO A 1 549 ? -1.423  45.442  116.256 1.00 52.85  ?  565 PRO B CG  1 
ATOM   4475  C CD  . PRO A 1 549 ? -2.510  44.911  115.383 1.00 55.55  ?  565 PRO B CD  1 
ATOM   4476  N N   . TRP A 1 550 ? 1.070   41.878  114.556 1.00 56.63  ?  566 TRP B N   1 
ATOM   4477  C CA  . TRP A 1 550 ? 1.362   40.447  114.478 1.00 53.21  ?  566 TRP B CA  1 
ATOM   4478  C C   . TRP A 1 550 ? 1.184   39.771  115.827 1.00 53.61  ?  566 TRP B C   1 
ATOM   4479  O O   . TRP A 1 550 ? 0.959   38.551  115.887 1.00 54.75  ?  566 TRP B O   1 
ATOM   4480  C CB  . TRP A 1 550 ? 2.767   40.156  113.937 1.00 51.28  ?  566 TRP B CB  1 
ATOM   4481  C CG  . TRP A 1 550 ? 3.927   40.487  114.812 1.00 56.86  ?  566 TRP B CG  1 
ATOM   4482  C CD1 . TRP A 1 550 ? 4.736   41.602  114.761 1.00 57.19  ?  566 TRP B CD1 1 
ATOM   4483  C CD2 . TRP A 1 550 ? 4.407   39.703  115.914 1.00 62.14  ?  566 TRP B CD2 1 
ATOM   4484  N NE1 . TRP A 1 550 ? 5.720   41.529  115.750 1.00 52.97  ?  566 TRP B NE1 1 
ATOM   4485  C CE2 . TRP A 1 550 ? 5.515   40.382  116.475 1.00 53.64  ?  566 TRP B CE2 1 
ATOM   4486  C CE3 . TRP A 1 550 ? 4.005   38.484  116.486 1.00 58.83  ?  566 TRP B CE3 1 
ATOM   4487  C CZ2 . TRP A 1 550 ? 6.195   39.882  117.577 1.00 53.78  ?  566 TRP B CZ2 1 
ATOM   4488  C CZ3 . TRP A 1 550 ? 4.696   37.997  117.586 1.00 53.94  ?  566 TRP B CZ3 1 
ATOM   4489  C CH2 . TRP A 1 550 ? 5.765   38.688  118.113 1.00 53.46  ?  566 TRP B CH2 1 
ATOM   4490  N N   . THR A 1 551 ? 1.241   40.548  116.909 1.00 57.45  ?  567 THR B N   1 
ATOM   4491  C CA  . THR A 1 551 ? 0.973   40.011  118.235 1.00 59.25  ?  567 THR B CA  1 
ATOM   4492  C C   . THR A 1 551 ? -0.494  39.594  118.366 1.00 59.59  ?  567 THR B C   1 
ATOM   4493  O O   . THR A 1 551 ? -0.796  38.456  118.746 1.00 62.50  ?  567 THR B O   1 
ATOM   4494  C CB  . THR A 1 551 ? 1.400   41.035  119.298 1.00 59.80  ?  567 THR B CB  1 
ATOM   4495  O OG1 . THR A 1 551 ? 0.783   42.299  119.063 1.00 56.68  ?  567 THR B OG1 1 
ATOM   4496  C CG2 . THR A 1 551 ? 2.910   41.250  119.236 1.00 57.66  ?  567 THR B CG2 1 
ATOM   4497  N N   . LEU A 1 552 ? -1.421  40.480  118.012 1.00 58.99  ?  568 LEU B N   1 
ATOM   4498  C CA  . LEU A 1 552 ? -2.834  40.105  118.011 1.00 62.05  ?  568 LEU B CA  1 
ATOM   4499  C C   . LEU A 1 552 ? -3.133  38.981  117.033 1.00 60.07  ?  568 LEU B C   1 
ATOM   4500  O O   . LEU A 1 552 ? -3.919  38.079  117.342 1.00 59.24  ?  568 LEU B O   1 
ATOM   4501  C CB  . LEU A 1 552 ? -3.694  41.331  117.715 1.00 63.84  ?  568 LEU B CB  1 
ATOM   4502  C CG  . LEU A 1 552 ? -5.184  41.095  117.469 1.00 64.05  ?  568 LEU B CG  1 
ATOM   4503  C CD1 . LEU A 1 552 ? -5.930  40.265  118.543 1.00 67.72  ?  568 LEU B CD1 1 
ATOM   4504  C CD2 . LEU A 1 552 ? -5.781  42.483  117.350 1.00 61.90  ?  568 LEU B CD2 1 
ATOM   4505  N N   . ALA A 1 553 ? -2.541  39.037  115.842 1.00 58.31  ?  569 ALA B N   1 
ATOM   4506  C CA  . ALA A 1 553 ? -2.705  37.964  114.867 1.00 57.00  ?  569 ALA B CA  1 
ATOM   4507  C C   . ALA A 1 553 ? -2.377  36.622  115.488 1.00 59.90  ?  569 ALA B C   1 
ATOM   4508  O O   . ALA A 1 553 ? -3.118  35.635  115.337 1.00 55.87  ?  569 ALA B O   1 
ATOM   4509  C CB  . ALA A 1 553 ? -1.785  38.212  113.679 1.00 56.73  ?  569 ALA B CB  1 
ATOM   4510  N N   . LEU A 1 554 ? -1.241  36.576  116.186 1.00 61.37  ?  570 LEU B N   1 
ATOM   4511  C CA  . LEU A 1 554 ? -0.785  35.342  116.807 1.00 58.85  ?  570 LEU B CA  1 
ATOM   4512  C C   . LEU A 1 554 ? -1.767  34.893  117.897 1.00 61.24  ?  570 LEU B C   1 
ATOM   4513  O O   . LEU A 1 554 ? -2.226  33.739  117.910 1.00 63.19  ?  570 LEU B O   1 
ATOM   4514  C CB  . LEU A 1 554 ? 0.626   35.555  117.359 1.00 54.04  ?  570 LEU B CB  1 
ATOM   4515  C CG  . LEU A 1 554 ? 1.196   34.317  118.017 1.00 56.06  ?  570 LEU B CG  1 
ATOM   4516  C CD1 . LEU A 1 554 ? 1.066   33.204  117.015 1.00 55.34  ?  570 LEU B CD1 1 
ATOM   4517  C CD2 . LEU A 1 554 ? 2.637   34.512  118.369 1.00 57.83  ?  570 LEU B CD2 1 
ATOM   4518  N N   . GLU A 1 555 ? -2.141  35.815  118.792 1.00 59.61  ?  571 GLU B N   1 
ATOM   4519  C CA  . GLU A 1 555 ? -3.125  35.516  119.830 1.00 60.29  ?  571 GLU B CA  1 
ATOM   4520  C C   . GLU A 1 555 ? -4.460  35.027  119.240 1.00 63.50  ?  571 GLU B C   1 
ATOM   4521  O O   . GLU A 1 555 ? -5.198  34.281  119.903 1.00 63.97  ?  571 GLU B O   1 
ATOM   4522  C CB  . GLU A 1 555 ? -3.275  36.763  120.714 1.00 58.04  ?  571 GLU B CB  1 
ATOM   4523  C CG  . GLU A 1 555 ? -4.225  36.685  121.889 1.00 64.67  ?  571 GLU B CG  1 
ATOM   4524  C CD  . GLU A 1 555 ? -4.452  38.064  122.525 1.00 70.16  ?  571 GLU B CD  1 
ATOM   4525  O OE1 . GLU A 1 555 ? -5.099  38.926  121.897 1.00 72.22  ?  571 GLU B OE1 1 
ATOM   4526  O OE2 . GLU A 1 555 ? -4.028  38.286  123.671 1.00 76.65  -1 571 GLU B OE2 1 
ATOM   4527  N N   . ASN A 1 556 ? -4.772  35.386  117.988 1.00 63.39  ?  572 ASN B N   1 
ATOM   4528  C CA  . ASN A 1 556 ? -6.017  34.890  117.403 1.00 63.39  ?  572 ASN B CA  1 
ATOM   4529  C C   . ASN A 1 556 ? -5.986  33.385  117.218 1.00 64.87  ?  572 ASN B C   1 
ATOM   4530  O O   . ASN A 1 556 ? -7.040  32.746  117.283 1.00 69.39  ?  572 ASN B O   1 
ATOM   4531  C CB  . ASN A 1 556 ? -6.307  35.562  116.066 1.00 58.31  ?  572 ASN B CB  1 
ATOM   4532  C CG  . ASN A 1 556 ? -7.054  36.859  116.232 1.00 61.80  ?  572 ASN B CG  1 
ATOM   4533  O OD1 . ASN A 1 556 ? -7.035  37.471  117.315 1.00 62.46  ?  572 ASN B OD1 1 
ATOM   4534  N ND2 . ASN A 1 556 ? -7.666  37.325  115.153 1.00 59.97  ?  572 ASN B ND2 1 
ATOM   4535  N N   . VAL A 1 557 ? -4.806  32.814  116.982 1.00 63.32  ?  573 VAL B N   1 
ATOM   4536  C CA  . VAL A 1 557 ? -4.657  31.375  116.763 1.00 61.90  ?  573 VAL B CA  1 
ATOM   4537  C C   . VAL A 1 557 ? -4.332  30.645  118.064 1.00 63.64  ?  573 VAL B C   1 
ATOM   4538  O O   . VAL A 1 557 ? -4.947  29.621  118.374 1.00 62.28  ?  573 VAL B O   1 
ATOM   4539  C CB  . VAL A 1 557 ? -3.573  31.106  115.688 1.00 56.09  ?  573 VAL B CB  1 
ATOM   4540  C CG1 . VAL A 1 557 ? -3.595  29.658  115.173 1.00 51.91  ?  573 VAL B CG1 1 
ATOM   4541  C CG2 . VAL A 1 557 ? -3.680  32.066  114.550 1.00 53.91  ?  573 VAL B CG2 1 
ATOM   4542  N N   . VAL A 1 558 ? -3.394  31.188  118.852 1.00 67.68  ?  574 VAL B N   1 
ATOM   4543  C CA  . VAL A 1 558 ? -2.724  30.470  119.934 1.00 66.11  ?  574 VAL B CA  1 
ATOM   4544  C C   . VAL A 1 558 ? -2.975  31.070  121.312 1.00 64.73  ?  574 VAL B C   1 
ATOM   4545  O O   . VAL A 1 558 ? -2.505  30.515  122.309 1.00 63.49  ?  574 VAL B O   1 
ATOM   4546  C CB  . VAL A 1 558 ? -1.213  30.376  119.666 1.00 62.37  ?  574 VAL B CB  1 
ATOM   4547  C CG1 . VAL A 1 558 ? -0.971  29.913  118.237 1.00 63.69  ?  574 VAL B CG1 1 
ATOM   4548  C CG2 . VAL A 1 558 ? -0.618  31.751  119.872 1.00 60.36  ?  574 VAL B CG2 1 
ATOM   4549  N N   . GLY A 1 559 ? -3.692  32.184  121.405 1.00 71.54  ?  575 GLY B N   1 
ATOM   4550  C CA  . GLY A 1 559 ? -4.083  32.730  122.690 1.00 65.23  ?  575 GLY B CA  1 
ATOM   4551  C C   . GLY A 1 559 ? -2.957  33.337  123.474 1.00 63.81  ?  575 GLY B C   1 
ATOM   4552  O O   . GLY A 1 559 ? -3.027  33.375  124.700 1.00 71.28  ?  575 GLY B O   1 
ATOM   4553  N N   . ALA A 1 560 ? -1.911  33.800  122.796 1.00 59.73  ?  576 ALA B N   1 
ATOM   4554  C CA  . ALA A 1 560 ? -0.746  34.409  123.424 1.00 60.14  ?  576 ALA B CA  1 
ATOM   4555  C C   . ALA A 1 560 ? -0.138  35.395  122.435 1.00 60.82  ?  576 ALA B C   1 
ATOM   4556  O O   . ALA A 1 560 ? -0.135  35.148  121.223 1.00 63.66  ?  576 ALA B O   1 
ATOM   4557  C CB  . ALA A 1 560 ? 0.289   33.361  123.824 1.00 60.28  ?  576 ALA B CB  1 
ATOM   4558  N N   . LYS A 1 561 ? 0.382   36.503  122.943 1.00 61.05  ?  577 LYS B N   1 
ATOM   4559  C CA  . LYS A 1 561 ? 0.751   37.593  122.063 1.00 59.63  ?  577 LYS B CA  1 
ATOM   4560  C C   . LYS A 1 561 ? 2.184   37.503  121.586 1.00 66.30  ?  577 LYS B C   1 
ATOM   4561  O O   . LYS A 1 561 ? 2.615   38.347  120.799 1.00 68.91  ?  577 LYS B O   1 
ATOM   4562  C CB  . LYS A 1 561 ? 0.567   38.903  122.786 1.00 61.64  ?  577 LYS B CB  1 
ATOM   4563  C CG  . LYS A 1 561 ? -0.835  39.136  123.234 1.00 68.20  ?  577 LYS B CG  1 
ATOM   4564  C CD  . LYS A 1 561 ? -0.837  40.393  124.046 1.00 70.35  ?  577 LYS B CD  1 
ATOM   4565  C CE  . LYS A 1 561 ? -2.193  40.823  124.534 1.00 76.33  ?  577 LYS B CE  1 
ATOM   4566  N NZ  . LYS A 1 561 ? -2.009  41.865  125.591 1.00 85.03  ?  577 LYS B NZ  1 
ATOM   4567  N N   . ASN A 1 562 ? 2.937   36.516  122.057 1.00 71.72  ?  578 ASN B N   1 
ATOM   4568  C CA  . ASN A 1 562 ? 4.376   36.517  121.692 1.00 72.87  ?  578 ASN B CA  1 
ATOM   4569  C C   . ASN A 1 562 ? 4.896   35.129  121.348 1.00 71.70  ?  578 ASN B C   1 
ATOM   4570  O O   . ASN A 1 562 ? 4.215   34.145  121.659 1.00 67.78  ?  578 ASN B O   1 
ATOM   4571  C CB  . ASN A 1 562 ? 5.235   37.100  122.811 1.00 79.80  ?  578 ASN B CB  1 
ATOM   4572  C CG  . ASN A 1 562 ? 6.524   37.719  122.318 1.00 87.35  ?  578 ASN B CG  1 
ATOM   4573  O OD1 . ASN A 1 562 ? 6.938   37.496  121.181 1.00 81.65  ?  578 ASN B OD1 1 
ATOM   4574  N ND2 . ASN A 1 562 ? 7.168   38.494  123.172 1.00 95.45  ?  578 ASN B ND2 1 
ATOM   4575  N N   . MET A 1 563 ? 6.089   35.086  120.771 1.00 64.90  ?  579 MET B N   1 
ATOM   4576  C CA  . MET A 1 563 ? 6.717   33.808  120.370 1.00 64.49  ?  579 MET B CA  1 
ATOM   4577  C C   . MET A 1 563 ? 6.900   32.939  121.606 1.00 69.99  ?  579 MET B C   1 
ATOM   4578  O O   . MET A 1 563 ? 6.894   33.489  122.720 1.00 70.71  ?  579 MET B O   1 
ATOM   4579  C CB  . MET A 1 563 ? 8.093   34.089  119.772 1.00 63.78  ?  579 MET B CB  1 
ATOM   4580  C CG  . MET A 1 563 ? 8.364   33.362  118.483 1.00 64.08  ?  579 MET B CG  1 
ATOM   4581  S SD  . MET A 1 563 ? 10.028  33.764  117.898 1.00 56.96  ?  579 MET B SD  1 
ATOM   4582  C CE  . MET A 1 563 ? 10.434  35.140  118.966 1.00 59.44  ?  579 MET B CE  1 
ATOM   4583  N N   . ASN A 1 564 ? 7.096   31.641  121.395 1.00 73.80  ?  580 ASN B N   1 
ATOM   4584  C CA  . ASN A 1 564 ? 7.273   30.699  122.527 1.00 75.01  ?  580 ASN B CA  1 
ATOM   4585  C C   . ASN A 1 564 ? 7.839   29.381  122.006 1.00 71.86  ?  580 ASN B C   1 
ATOM   4586  O O   . ASN A 1 564 ? 7.219   28.776  121.119 1.00 69.93  ?  580 ASN B O   1 
ATOM   4587  C CB  . ASN A 1 564 ? 5.969   30.472  123.287 1.00 74.91  ?  580 ASN B CB  1 
ATOM   4588  C CG  . ASN A 1 564 ? 6.179   29.769  124.607 1.00 81.24  ?  580 ASN B CG  1 
ATOM   4589  O OD1 . ASN A 1 564 ? 6.862   28.755  124.668 1.00 82.26  ?  580 ASN B OD1 1 
ATOM   4590  N ND2 . ASN A 1 564 ? 5.592   30.304  125.664 1.00 89.34  ?  580 ASN B ND2 1 
ATOM   4591  N N   . VAL A 1 565 ? 8.986   28.971  122.535 1.00 69.28  ?  581 VAL B N   1 
ATOM   4592  C CA  . VAL A 1 565 ? 9.562   27.690  122.156 1.00 70.82  ?  581 VAL B CA  1 
ATOM   4593  C C   . VAL A 1 565 ? 8.886   26.480  122.778 1.00 75.99  ?  581 VAL B C   1 
ATOM   4594  O O   . VAL A 1 565 ? 9.137   25.355  122.323 1.00 77.63  ?  581 VAL B O   1 
ATOM   4595  C CB  . VAL A 1 565 ? 11.041  27.673  122.519 1.00 65.46  ?  581 VAL B CB  1 
ATOM   4596  C CG1 . VAL A 1 565 ? 11.780  28.410  121.509 1.00 65.02  ?  581 VAL B CG1 1 
ATOM   4597  C CG2 . VAL A 1 565 ? 11.175  28.405  123.829 1.00 66.51  ?  581 VAL B CG2 1 
ATOM   4598  N N   . ARG A 1 566 ? 8.068   26.662  123.806 1.00 74.31  ?  582 ARG B N   1 
ATOM   4599  C CA  . ARG A 1 566 ? 7.562   25.497  124.516 1.00 75.48  ?  582 ARG B CA  1 
ATOM   4600  C C   . ARG A 1 566 ? 6.866   24.520  123.576 1.00 79.43  ?  582 ARG B C   1 
ATOM   4601  O O   . ARG A 1 566 ? 7.050   23.307  123.762 1.00 79.00  ?  582 ARG B O   1 
ATOM   4602  C CB  . ARG A 1 566 ? 6.652   25.958  125.660 1.00 82.69  ?  582 ARG B CB  1 
ATOM   4603  C CG  . ARG A 1 566 ? 6.376   24.948  126.753 1.00 94.37  ?  582 ARG B CG  1 
ATOM   4604  C CD  . ARG A 1 566 ? 5.120   25.411  127.499 1.00 111.74 ?  582 ARG B CD  1 
ATOM   4605  N NE  . ARG A 1 566 ? 4.151   26.089  126.620 1.00 114.54 ?  582 ARG B NE  1 
ATOM   4606  C CZ  . ARG A 1 566 ? 3.342   25.520  125.712 1.00 107.99 ?  582 ARG B CZ  1 
ATOM   4607  N NH1 . ARG A 1 566 ? 3.140   24.199  125.665 1.00 105.33 ?  582 ARG B NH1 1 
ATOM   4608  N NH2 . ARG A 1 566 ? 2.689   26.304  124.847 1.00 96.08  ?  582 ARG B NH2 1 
ATOM   4609  N N   . PRO A 1 567 ? 6.100   24.956  122.558 1.00 82.71  ?  583 PRO B N   1 
ATOM   4610  C CA  . PRO A 1 567 ? 5.492   23.986  121.634 1.00 76.67  ?  583 PRO B CA  1 
ATOM   4611  C C   . PRO A 1 567 ? 6.487   23.265  120.748 1.00 79.85  ?  583 PRO B C   1 
ATOM   4612  O O   . PRO A 1 567 ? 6.292   22.079  120.465 1.00 80.58  ?  583 PRO B O   1 
ATOM   4613  C CB  . PRO A 1 567 ? 4.530   24.855  120.827 1.00 62.15  ?  583 PRO B CB  1 
ATOM   4614  C CG  . PRO A 1 567 ? 4.183   25.928  121.726 1.00 72.74  ?  583 PRO B CG  1 
ATOM   4615  C CD  . PRO A 1 567 ? 5.433   26.263  122.439 1.00 79.73  ?  583 PRO B CD  1 
ATOM   4616  N N   . LEU A 1 568 ? 7.534   23.946  120.280 1.00 76.30  ?  584 LEU B N   1 
ATOM   4617  C CA  . LEU A 1 568 ? 8.703   23.257  119.729 1.00 73.34  ?  584 LEU B CA  1 
ATOM   4618  C C   . LEU A 1 568 ? 9.172   22.118  120.625 1.00 72.32  ?  584 LEU B C   1 
ATOM   4619  O O   . LEU A 1 568 ? 9.163   20.937  120.238 1.00 75.36  ?  584 LEU B O   1 
ATOM   4620  C CB  . LEU A 1 568 ? 9.835   24.260  119.531 1.00 69.06  ?  584 LEU B CB  1 
ATOM   4621  C CG  . LEU A 1 568 ? 11.110  23.792  118.848 1.00 63.87  ?  584 LEU B CG  1 
ATOM   4622  C CD1 . LEU A 1 568 ? 10.930  23.297  117.431 1.00 64.15  ?  584 LEU B CD1 1 
ATOM   4623  C CD2 . LEU A 1 568 ? 11.894  25.047  118.846 1.00 64.89  ?  584 LEU B CD2 1 
ATOM   4624  N N   . LEU A 1 569 ? 9.612   22.482  121.831 1.00 79.89  ?  585 LEU B N   1 
ATOM   4625  C CA  . LEU A 1 569 ? 10.094  21.512  122.804 1.00 79.72  ?  585 LEU B CA  1 
ATOM   4626  C C   . LEU A 1 569 ? 9.103   20.376  122.980 1.00 79.91  ?  585 LEU B C   1 
ATOM   4627  O O   . LEU A 1 569 ? 9.475   19.201  123.033 1.00 87.90  ?  585 LEU B O   1 
ATOM   4628  C CB  . LEU A 1 569 ? 10.344  22.226  124.138 1.00 74.47  ?  585 LEU B CB  1 
ATOM   4629  C CG  . LEU A 1 569 ? 11.297  23.412  124.054 1.00 61.89  ?  585 LEU B CG  1 
ATOM   4630  C CD1 . LEU A 1 569 ? 11.528  23.944  125.429 1.00 60.37  ?  585 LEU B CD1 1 
ATOM   4631  C CD2 . LEU A 1 569 ? 12.571  22.976  123.423 1.00 58.74  ?  585 LEU B CD2 1 
ATOM   4632  N N   . ASN A 1 570 ? 7.833   20.706  123.047 1.00 73.81  ?  586 ASN B N   1 
ATOM   4633  C CA  . ASN A 1 570 ? 6.859   19.673  123.295 1.00 79.05  ?  586 ASN B CA  1 
ATOM   4634  C C   . ASN A 1 570 ? 6.758   18.738  122.090 1.00 81.46  ?  586 ASN B C   1 
ATOM   4635  O O   . ASN A 1 570 ? 6.726   17.511  122.253 1.00 85.80  ?  586 ASN B O   1 
ATOM   4636  C CB  . ASN A 1 570 ? 5.524   20.326  123.629 1.00 80.98  ?  586 ASN B CB  1 
ATOM   4637  C CG  . ASN A 1 570 ? 4.459   19.319  123.866 1.00 92.12  ?  586 ASN B CG  1 
ATOM   4638  O OD1 . ASN A 1 570 ? 4.746   18.136  124.116 1.00 96.15  ?  586 ASN B OD1 1 
ATOM   4639  N ND2 . ASN A 1 570 ? 3.211   19.743  123.729 1.00 103.71 ?  586 ASN B ND2 1 
ATOM   4640  N N   . TYR A 1 571 ? 6.743   19.302  120.872 1.00 77.21  ?  587 TYR B N   1 
ATOM   4641  C CA  . TYR A 1 571 ? 6.735   18.488  119.659 1.00 76.38  ?  587 TYR B CA  1 
ATOM   4642  C C   . TYR A 1 571 ? 7.878   17.482  119.684 1.00 78.72  ?  587 TYR B C   1 
ATOM   4643  O O   . TYR A 1 571 ? 7.696   16.310  119.333 1.00 79.12  ?  587 TYR B O   1 
ATOM   4644  C CB  . TYR A 1 571 ? 6.810   19.386  118.405 1.00 74.92  ?  587 TYR B CB  1 
ATOM   4645  C CG  . TYR A 1 571 ? 6.766   18.646  117.052 1.00 73.93  ?  587 TYR B CG  1 
ATOM   4646  C CD1 . TYR A 1 571 ? 7.930   18.117  116.474 1.00 72.19  ?  587 TYR B CD1 1 
ATOM   4647  C CD2 . TYR A 1 571 ? 5.573   18.504  116.339 1.00 71.12  ?  587 TYR B CD2 1 
ATOM   4648  C CE1 . TYR A 1 571 ? 7.901   17.437  115.245 1.00 73.00  ?  587 TYR B CE1 1 
ATOM   4649  C CE2 . TYR A 1 571 ? 5.540   17.832  115.100 1.00 74.28  ?  587 TYR B CE2 1 
ATOM   4650  C CZ  . TYR A 1 571 ? 6.706   17.298  114.566 1.00 76.37  ?  587 TYR B CZ  1 
ATOM   4651  O OH  . TYR A 1 571 ? 6.680   16.636  113.356 1.00 77.30  ?  587 TYR B OH  1 
ATOM   4652  N N   . PHE A 1 572 ? 9.056   17.910  120.135 1.00 78.68  ?  588 PHE B N   1 
ATOM   4653  C CA  . PHE A 1 572 ? 10.237  17.056  120.060 1.00 75.08  ?  588 PHE B CA  1 
ATOM   4654  C C   . PHE A 1 572 ? 10.535  16.266  121.331 1.00 81.94  ?  588 PHE B C   1 
ATOM   4655  O O   . PHE A 1 572 ? 11.495  15.487  121.344 1.00 83.50  ?  588 PHE B O   1 
ATOM   4656  C CB  . PHE A 1 572 ? 11.446  17.889  119.682 1.00 66.88  ?  588 PHE B CB  1 
ATOM   4657  C CG  . PHE A 1 572 ? 11.509  18.196  118.238 1.00 71.55  ?  588 PHE B CG  1 
ATOM   4658  C CD1 . PHE A 1 572 ? 11.749  17.184  117.324 1.00 72.10  ?  588 PHE B CD1 1 
ATOM   4659  C CD2 . PHE A 1 572 ? 11.277  19.488  117.773 1.00 73.90  ?  588 PHE B CD2 1 
ATOM   4660  C CE1 . PHE A 1 572 ? 11.805  17.459  115.967 1.00 75.92  ?  588 PHE B CE1 1 
ATOM   4661  C CE2 . PHE A 1 572 ? 11.321  19.779  116.416 1.00 71.85  ?  588 PHE B CE2 1 
ATOM   4662  C CZ  . PHE A 1 572 ? 11.584  18.764  115.512 1.00 73.72  ?  588 PHE B CZ  1 
ATOM   4663  N N   . GLU A 1 573 ? 9.735   16.421  122.381 1.00 96.99  ?  589 GLU B N   1 
ATOM   4664  C CA  . GLU A 1 573 ? 10.093  15.858  123.680 1.00 95.36  ?  589 GLU B CA  1 
ATOM   4665  C C   . GLU A 1 573 ? 10.321  14.341  123.708 1.00 95.64  ?  589 GLU B C   1 
ATOM   4666  O O   . GLU A 1 573 ? 11.234  13.901  124.431 1.00 97.22  ?  589 GLU B O   1 
ATOM   4667  C CB  . GLU A 1 573 ? 9.028   16.279  124.686 1.00 103.16 ?  589 GLU B CB  1 
ATOM   4668  C CG  . GLU A 1 573 ? 9.046   15.491  125.931 1.00 117.07 ?  589 GLU B CG  1 
ATOM   4669  C CD  . GLU A 1 573 ? 8.670   16.356  127.107 1.00 139.10 ?  589 GLU B CD  1 
ATOM   4670  O OE1 . GLU A 1 573 ? 8.136   17.464  126.867 1.00 136.16 ?  589 GLU B OE1 1 
ATOM   4671  O OE2 . GLU A 1 573 ? 8.988   15.975  128.255 1.00 147.52 -1 589 GLU B OE2 1 
ATOM   4672  N N   . PRO A 1 574 ? 9.566   13.496  122.993 1.00 93.23  ?  590 PRO B N   1 
ATOM   4673  C CA  . PRO A 1 574 ? 10.003  12.088  122.848 1.00 89.75  ?  590 PRO B CA  1 
ATOM   4674  C C   . PRO A 1 574 ? 11.456  11.936  122.399 1.00 85.25  ?  590 PRO B C   1 
ATOM   4675  O O   . PRO A 1 574 ? 12.238  11.170  122.983 1.00 82.79  ?  590 PRO B O   1 
ATOM   4676  C CB  . PRO A 1 574 ? 9.020   11.531  121.800 1.00 79.62  ?  590 PRO B CB  1 
ATOM   4677  C CG  . PRO A 1 574 ? 7.864   12.399  121.863 1.00 81.11  ?  590 PRO B CG  1 
ATOM   4678  C CD  . PRO A 1 574 ? 8.356   13.761  122.199 1.00 89.96  ?  590 PRO B CD  1 
ATOM   4679  N N   . LEU A 1 575 ? 11.823  12.652  121.338 1.00 80.08  ?  591 LEU B N   1 
ATOM   4680  C CA  . LEU A 1 575 ? 13.180  12.584  120.836 1.00 75.93  ?  591 LEU B CA  1 
ATOM   4681  C C   . LEU A 1 575 ? 14.140  13.148  121.853 1.00 80.61  ?  591 LEU B C   1 
ATOM   4682  O O   . LEU A 1 575 ? 15.265  12.658  121.980 1.00 86.18  ?  591 LEU B O   1 
ATOM   4683  C CB  . LEU A 1 575 ? 13.294  13.348  119.527 1.00 74.36  ?  591 LEU B CB  1 
ATOM   4684  C CG  . LEU A 1 575 ? 14.658  13.303  118.855 1.00 72.16  ?  591 LEU B CG  1 
ATOM   4685  C CD1 . LEU A 1 575 ? 14.919  11.892  118.403 1.00 75.69  ?  591 LEU B CD1 1 
ATOM   4686  C CD2 . LEU A 1 575 ? 14.670  14.213  117.670 1.00 73.01  ?  591 LEU B CD2 1 
ATOM   4687  N N   . PHE A 1 576 ? 13.697  14.149  122.614 1.00 82.24  ?  592 PHE B N   1 
ATOM   4688  C CA  . PHE A 1 576 ? 14.523  14.713  123.675 1.00 79.90  ?  592 PHE B CA  1 
ATOM   4689  C C   . PHE A 1 576 ? 14.931  13.639  124.675 1.00 79.10  ?  592 PHE B C   1 
ATOM   4690  O O   . PHE A 1 576 ? 16.121  13.442  124.939 1.00 78.72  ?  592 PHE B O   1 
ATOM   4691  C CB  . PHE A 1 576 ? 13.755  15.798  124.415 1.00 81.77  ?  592 PHE B CB  1 
ATOM   4692  C CG  . PHE A 1 576 ? 14.606  16.656  125.287 1.00 74.03  ?  592 PHE B CG  1 
ATOM   4693  C CD1 . PHE A 1 576 ? 15.924  16.885  124.977 1.00 69.64  ?  592 PHE B CD1 1 
ATOM   4694  C CD2 . PHE A 1 576 ? 14.107  17.151  126.468 1.00 75.20  ?  592 PHE B CD2 1 
ATOM   4695  C CE1 . PHE A 1 576 ? 16.690  17.675  125.777 1.00 65.14  ?  592 PHE B CE1 1 
ATOM   4696  C CE2 . PHE A 1 576 ? 14.882  17.921  127.276 1.00 68.76  ?  592 PHE B CE2 1 
ATOM   4697  C CZ  . PHE A 1 576 ? 16.173  18.177  126.932 1.00 63.31  ?  592 PHE B CZ  1 
ATOM   4698  N N   . THR A 1 577 ? 13.941  12.943  125.260 1.00 82.37  ?  593 THR B N   1 
ATOM   4699  C CA  . THR A 1 577 ? 14.266  12.011  126.340 1.00 80.48  ?  593 THR B CA  1 
ATOM   4700  C C   . THR A 1 577 ? 14.983  10.773  125.811 1.00 82.46  ?  593 THR B C   1 
ATOM   4701  O O   . THR A 1 577 ? 15.837  10.213  126.507 1.00 88.38  ?  593 THR B O   1 
ATOM   4702  C CB  . THR A 1 577 ? 13.017  11.583  127.117 1.00 76.00  ?  593 THR B CB  1 
ATOM   4703  O OG1 . THR A 1 577 ? 12.205  10.748  126.300 1.00 74.83  ?  593 THR B OG1 1 
ATOM   4704  C CG2 . THR A 1 577 ? 12.176  12.810  127.538 1.00 77.90  ?  593 THR B CG2 1 
ATOM   4705  N N   . TRP A 1 578 ? 14.689  10.341  124.576 1.00 79.31  ?  594 TRP B N   1 
ATOM   4706  C CA  . TRP A 1 578 ? 15.501  9.277   123.989 1.00 82.05  ?  594 TRP B CA  1 
ATOM   4707  C C   . TRP A 1 578 ? 16.951  9.708   123.770 1.00 85.19  ?  594 TRP B C   1 
ATOM   4708  O O   . TRP A 1 578 ? 17.877  8.922   124.016 1.00 88.07  ?  594 TRP B O   1 
ATOM   4709  C CB  . TRP A 1 578 ? 14.888  8.786   122.686 1.00 81.42  ?  594 TRP B CB  1 
ATOM   4710  C CG  . TRP A 1 578 ? 15.710  7.732   122.059 1.00 83.98  ?  594 TRP B CG  1 
ATOM   4711  C CD1 . TRP A 1 578 ? 15.645  6.398   122.291 1.00 87.00  ?  594 TRP B CD1 1 
ATOM   4712  C CD2 . TRP A 1 578 ? 16.712  7.921   121.053 1.00 83.42  ?  594 TRP B CD2 1 
ATOM   4713  N NE1 . TRP A 1 578 ? 16.565  5.737   121.510 1.00 91.43  ?  594 TRP B NE1 1 
ATOM   4714  C CE2 . TRP A 1 578 ? 17.223  6.652   120.730 1.00 85.90  ?  594 TRP B CE2 1 
ATOM   4715  C CE3 . TRP A 1 578 ? 17.232  9.046   120.401 1.00 82.35  ?  594 TRP B CE3 1 
ATOM   4716  C CZ2 . TRP A 1 578 ? 18.222  6.472   119.774 1.00 86.41  ?  594 TRP B CZ2 1 
ATOM   4717  C CZ3 . TRP A 1 578 ? 18.224  8.866   119.453 1.00 80.07  ?  594 TRP B CZ3 1 
ATOM   4718  C CH2 . TRP A 1 578 ? 18.709  7.589   119.150 1.00 83.72  ?  594 TRP B CH2 1 
ATOM   4719  N N   . LEU A 1 579 ? 17.176  10.937  123.297 1.00 83.38  ?  595 LEU B N   1 
ATOM   4720  C CA  . LEU A 1 579 ? 18.539  11.444  123.186 1.00 78.42  ?  595 LEU B CA  1 
ATOM   4721  C C   . LEU A 1 579 ? 19.217  11.483  124.538 1.00 81.84  ?  595 LEU B C   1 
ATOM   4722  O O   . LEU A 1 579 ? 20.390  11.126  124.672 1.00 92.13  ?  595 LEU B O   1 
ATOM   4723  C CB  . LEU A 1 579 ? 18.536  12.844  122.594 1.00 77.39  ?  595 LEU B CB  1 
ATOM   4724  C CG  . LEU A 1 579 ? 18.260  12.878  121.109 1.00 81.91  ?  595 LEU B CG  1 
ATOM   4725  C CD1 . LEU A 1 579 ? 18.167  14.328  120.652 1.00 79.99  ?  595 LEU B CD1 1 
ATOM   4726  C CD2 . LEU A 1 579 ? 19.335  12.088  120.369 1.00 76.33  ?  595 LEU B CD2 1 
ATOM   4727  N N   . LYS A 1 580 ? 18.505  11.945  125.550 1.00 85.46  ?  596 LYS B N   1 
ATOM   4728  C CA  . LYS A 1 580 ? 19.120  12.076  126.855 1.00 86.71  ?  596 LYS B CA  1 
ATOM   4729  C C   . LYS A 1 580 ? 19.540  10.712  127.395 1.00 97.06  ?  596 LYS B C   1 
ATOM   4730  O O   . LYS A 1 580 ? 20.620  10.571  127.975 1.00 96.50  ?  596 LYS B O   1 
ATOM   4731  C CB  . LYS A 1 580 ? 18.144  12.780  127.772 1.00 80.77  ?  596 LYS B CB  1 
ATOM   4732  C CG  . LYS A 1 580 ? 18.462  14.214  128.028 1.00 75.89  ?  596 LYS B CG  1 
ATOM   4733  C CD  . LYS A 1 580 ? 17.163  14.968  127.972 1.00 73.68  ?  596 LYS B CD  1 
ATOM   4734  C CE  . LYS A 1 580 ? 16.167  14.491  129.009 1.00 73.21  ?  596 LYS B CE  1 
ATOM   4735  N NZ  . LYS A 1 580 ? 14.861  15.181  128.793 1.00 83.94  ?  596 LYS B NZ  1 
ATOM   4736  N N   . ASP A 1 581 ? 18.714  9.681   127.188 1.00 104.90 ?  597 ASP B N   1 
ATOM   4737  C CA  . ASP A 1 581 ? 19.183  8.331   127.487 1.00 113.26 ?  597 ASP B CA  1 
ATOM   4738  C C   . ASP A 1 581 ? 20.437  8.006   126.680 1.00 119.22 ?  597 ASP B C   1 
ATOM   4739  O O   . ASP A 1 581 ? 21.469  7.615   127.235 1.00 126.11 ?  597 ASP B O   1 
ATOM   4740  C CB  . ASP A 1 581 ? 18.077  7.299   127.228 1.00 117.68 ?  597 ASP B CB  1 
ATOM   4741  C CG  . ASP A 1 581 ? 18.542  5.859   127.496 1.00 129.49 ?  597 ASP B CG  1 
ATOM   4742  O OD1 . ASP A 1 581 ? 19.066  5.230   126.550 1.00 132.24 ?  597 ASP B OD1 1 
ATOM   4743  O OD2 . ASP A 1 581 ? 18.424  5.359   128.644 1.00 127.33 -1 597 ASP B OD2 1 
ATOM   4744  N N   . GLN A 1 582 ? 20.383  8.220   125.370 1.00 98.74  ?  598 GLN B N   1 
ATOM   4745  C CA  . GLN A 1 582 ? 21.459  7.780   124.505 1.00 94.21  ?  598 GLN B CA  1 
ATOM   4746  C C   . GLN A 1 582 ? 22.753  8.511   124.798 1.00 93.48  ?  598 GLN B C   1 
ATOM   4747  O O   . GLN A 1 582 ? 23.807  8.072   124.328 1.00 104.07 ?  598 GLN B O   1 
ATOM   4748  C CB  . GLN A 1 582 ? 21.085  8.029   123.059 1.00 91.78  ?  598 GLN B CB  1 
ATOM   4749  C CG  . GLN A 1 582 ? 20.077  7.071   122.467 1.00 92.88  ?  598 GLN B CG  1 
ATOM   4750  C CD  . GLN A 1 582 ? 20.530  5.652   122.356 1.00 93.46  ?  598 GLN B CD  1 
ATOM   4751  O OE1 . GLN A 1 582 ? 21.586  5.353   121.785 1.00 96.06  ?  598 GLN B OE1 1 
ATOM   4752  N NE2 . GLN A 1 582 ? 19.694  4.746   122.842 1.00 91.47  ?  598 GLN B NE2 1 
ATOM   4753  N N   . ASN A 1 583 ? 22.703  9.628   125.539 1.00 95.91  ?  599 ASN B N   1 
ATOM   4754  C CA  . ASN A 1 583 ? 23.896  10.428  125.837 1.00 98.65  ?  599 ASN B CA  1 
ATOM   4755  C C   . ASN A 1 583 ? 24.372  10.339  127.294 1.00 102.71 ?  599 ASN B C   1 
ATOM   4756  O O   . ASN A 1 583 ? 25.107  11.211  127.762 1.00 101.10 ?  599 ASN B O   1 
ATOM   4757  C CB  . ASN A 1 583 ? 23.686  11.888  125.426 1.00 86.29  ?  599 ASN B CB  1 
ATOM   4758  C CG  . ASN A 1 583 ? 23.671  12.072  123.920 1.00 86.62  ?  599 ASN B CG  1 
ATOM   4759  O OD1 . ASN A 1 583 ? 24.178  11.226  123.176 1.00 85.78  ?  599 ASN B OD1 1 
ATOM   4760  N ND2 . ASN A 1 583 ? 23.112  13.194  123.463 1.00 84.53  ?  599 ASN B ND2 1 
ATOM   4761  N N   . LYS A 1 584 ? 23.997  9.286   128.012 1.00 112.50 ?  600 LYS B N   1 
ATOM   4762  C CA  . LYS A 1 584 ? 24.613  8.992   129.300 1.00 108.42 ?  600 LYS B CA  1 
ATOM   4763  C C   . LYS A 1 584 ? 26.128  8.815   129.168 1.00 120.70 ?  600 LYS B C   1 
ATOM   4764  O O   . LYS A 1 584 ? 26.906  9.407   129.927 1.00 114.69 ?  600 LYS B O   1 
ATOM   4765  C CB  . LYS A 1 584 ? 23.874  7.775   129.882 1.00 107.41 ?  600 LYS B CB  1 
ATOM   4766  C CG  . LYS A 1 584 ? 23.936  6.504   128.979 1.00 117.65 ?  600 LYS B CG  1 
ATOM   4767  C CD  . LYS A 1 584 ? 22.856  5.447   129.369 1.00 124.15 ?  600 LYS B CD  1 
ATOM   4768  C CE  . LYS A 1 584 ? 22.739  4.219   128.399 1.00 124.85 ?  600 LYS B CE  1 
ATOM   4769  N NZ  . LYS A 1 584 ? 22.574  4.579   126.940 1.00 110.78 ?  600 LYS B NZ  1 
ATOM   4770  N N   . ASN A 1 585 ? 26.561  8.088   128.153 1.00 145.72 ?  601 ASN B N   1 
ATOM   4771  C CA  . ASN A 1 585 ? 27.936  7.644   128.004 1.00 149.70 ?  601 ASN B CA  1 
ATOM   4772  C C   . ASN A 1 585 ? 28.742  8.612   127.193 1.00 143.17 ?  601 ASN B C   1 
ATOM   4773  O O   . ASN A 1 585 ? 29.825  8.281   126.716 1.00 143.34 ?  601 ASN B O   1 
ATOM   4774  C CB  . ASN A 1 585 ? 27.906  6.288   127.335 1.00 156.59 ?  601 ASN B CB  1 
ATOM   4775  C CG  . ASN A 1 585 ? 27.238  5.294   128.192 1.00 157.32 ?  601 ASN B CG  1 
ATOM   4776  O OD1 . ASN A 1 585 ? 27.372  5.351   129.425 1.00 154.64 ?  601 ASN B OD1 1 
ATOM   4777  N ND2 . ASN A 1 585 ? 26.324  4.527   127.595 1.00 159.61 ?  601 ASN B ND2 1 
ATOM   4778  N N   . SER A 1 586 ? 28.220  9.798   127.004 1.00 113.14 ?  602 SER B N   1 
ATOM   4779  C CA  . SER A 1 586 ? 28.693  10.700  125.980 1.00 102.78 ?  602 SER B CA  1 
ATOM   4780  C C   . SER A 1 586 ? 28.910  12.054  126.616 1.00 91.03  ?  602 SER B C   1 
ATOM   4781  O O   . SER A 1 586 ? 28.401  12.353  127.699 1.00 93.10  ?  602 SER B O   1 
ATOM   4782  C CB  . SER A 1 586 ? 27.685  10.841  124.805 1.00 103.23 ?  602 SER B CB  1 
ATOM   4783  O OG  . SER A 1 586 ? 27.394  9.602   124.163 1.00 106.92 ?  602 SER B OG  1 
ATOM   4784  N N   . PHE A 1 587 ? 29.683  12.873  125.944 1.00 77.57  ?  603 PHE B N   1 
ATOM   4785  C CA  . PHE A 1 587 ? 29.930  14.222  126.403 1.00 73.84  ?  603 PHE B CA  1 
ATOM   4786  C C   . PHE A 1 587 ? 29.017  15.189  125.680 1.00 72.83  ?  603 PHE B C   1 
ATOM   4787  O O   . PHE A 1 587 ? 29.076  15.321  124.451 1.00 76.81  ?  603 PHE B O   1 
ATOM   4788  C CB  . PHE A 1 587 ? 31.396  14.609  126.245 1.00 72.80  ?  603 PHE B CB  1 
ATOM   4789  C CG  . PHE A 1 587 ? 31.689  15.963  126.784 1.00 70.74  ?  603 PHE B CG  1 
ATOM   4790  C CD1 . PHE A 1 587 ? 31.776  16.184  128.133 1.00 69.85  ?  603 PHE B CD1 1 
ATOM   4791  C CD2 . PHE A 1 587 ? 31.911  17.015  125.930 1.00 71.66  ?  603 PHE B CD2 1 
ATOM   4792  C CE1 . PHE A 1 587 ? 32.040  17.445  128.619 1.00 72.11  ?  603 PHE B CE1 1 
ATOM   4793  C CE2 . PHE A 1 587 ? 32.176  18.262  126.405 1.00 69.08  ?  603 PHE B CE2 1 
ATOM   4794  C CZ  . PHE A 1 587 ? 32.243  18.484  127.744 1.00 75.18  ?  603 PHE B CZ  1 
ATOM   4795  N N   . VAL A 1 588 ? 28.223  15.907  126.458 1.00 70.91  ?  604 VAL B N   1 
ATOM   4796  C CA  . VAL A 1 588 ? 27.140  16.737  125.944 1.00 73.48  ?  604 VAL B CA  1 
ATOM   4797  C C   . VAL A 1 588 ? 27.567  18.189  126.024 1.00 69.26  ?  604 VAL B C   1 
ATOM   4798  O O   . VAL A 1 588 ? 27.788  18.714  127.120 1.00 68.49  ?  604 VAL B O   1 
ATOM   4799  C CB  . VAL A 1 588 ? 25.852  16.498  126.740 1.00 70.97  ?  604 VAL B CB  1 
ATOM   4800  C CG1 . VAL A 1 588 ? 24.789  17.493  126.352 1.00 62.51  ?  604 VAL B CG1 1 
ATOM   4801  C CG2 . VAL A 1 588 ? 25.399  15.079  126.530 1.00 74.60  ?  604 VAL B CG2 1 
ATOM   4802  N N   . GLY A 1 589 ? 27.627  18.851  124.879 1.00 70.20  ?  605 GLY B N   1 
ATOM   4803  C CA  . GLY A 1 589 ? 28.181  20.186  124.759 1.00 66.72  ?  605 GLY B CA  1 
ATOM   4804  C C   . GLY A 1 589 ? 29.516  20.097  124.056 1.00 65.69  ?  605 GLY B C   1 
ATOM   4805  O O   . GLY A 1 589 ? 29.941  19.022  123.631 1.00 69.43  ?  605 GLY B O   1 
ATOM   4806  N N   . TRP A 1 590 ? 30.196  21.241  123.940 1.00 61.96  ?  606 TRP B N   1 
ATOM   4807  C CA  . TRP A 1 590 ? 31.434  21.227  123.156 1.00 66.78  ?  606 TRP B CA  1 
ATOM   4808  C C   . TRP A 1 590 ? 32.468  22.242  123.610 1.00 66.89  ?  606 TRP B C   1 
ATOM   4809  O O   . TRP A 1 590 ? 32.133  23.386  123.918 1.00 69.29  ?  606 TRP B O   1 
ATOM   4810  C CB  . TRP A 1 590 ? 31.143  21.487  121.676 1.00 67.38  ?  606 TRP B CB  1 
ATOM   4811  C CG  . TRP A 1 590 ? 30.260  22.690  121.448 1.00 66.05  ?  606 TRP B CG  1 
ATOM   4812  C CD1 . TRP A 1 590 ? 30.644  23.994  121.311 1.00 66.09  ?  606 TRP B CD1 1 
ATOM   4813  C CD2 . TRP A 1 590 ? 28.835  22.684  121.377 1.00 63.86  ?  606 TRP B CD2 1 
ATOM   4814  N NE1 . TRP A 1 590 ? 29.546  24.794  121.140 1.00 62.69  ?  606 TRP B NE1 1 
ATOM   4815  C CE2 . TRP A 1 590 ? 28.423  24.011  121.187 1.00 60.72  ?  606 TRP B CE2 1 
ATOM   4816  C CE3 . TRP A 1 590 ? 27.865  21.676  121.447 1.00 64.09  ?  606 TRP B CE3 1 
ATOM   4817  C CZ2 . TRP A 1 590 ? 27.091  24.353  121.066 1.00 59.77  ?  606 TRP B CZ2 1 
ATOM   4818  C CZ3 . TRP A 1 590 ? 26.557  22.020  121.332 1.00 62.63  ?  606 TRP B CZ3 1 
ATOM   4819  C CH2 . TRP A 1 590 ? 26.176  23.343  121.143 1.00 62.27  ?  606 TRP B CH2 1 
ATOM   4820  N N   . SER A 1 591 ? 33.732  21.845  123.566 1.00 64.11  ?  607 SER B N   1 
ATOM   4821  C CA  . SER A 1 591 ? 34.797  22.802  123.811 1.00 73.18  ?  607 SER B CA  1 
ATOM   4822  C C   . SER A 1 591 ? 35.064  23.607  122.549 1.00 72.98  ?  607 SER B C   1 
ATOM   4823  O O   . SER A 1 591 ? 35.127  23.058  121.442 1.00 75.10  ?  607 SER B O   1 
ATOM   4824  C CB  . SER A 1 591 ? 36.086  22.104  124.245 1.00 83.13  ?  607 SER B CB  1 
ATOM   4825  O OG  . SER A 1 591 ? 36.858  21.691  123.122 1.00 84.40  ?  607 SER B OG  1 
ATOM   4826  N N   . THR A 1 592 ? 35.262  24.911  122.723 1.00 74.28  ?  608 THR B N   1 
ATOM   4827  C CA  . THR A 1 592 ? 35.371  25.785  121.568 1.00 79.26  ?  608 THR B CA  1 
ATOM   4828  C C   . THR A 1 592 ? 36.740  25.759  120.915 1.00 82.81  ?  608 THR B C   1 
ATOM   4829  O O   . THR A 1 592 ? 36.902  26.413  119.883 1.00 83.45  ?  608 THR B O   1 
ATOM   4830  C CB  . THR A 1 592 ? 35.131  27.242  121.924 1.00 74.51  ?  608 THR B CB  1 
ATOM   4831  O OG1 . THR A 1 592 ? 36.147  27.638  122.839 1.00 83.24  ?  608 THR B OG1 1 
ATOM   4832  C CG2 . THR A 1 592 ? 33.813  27.423  122.590 1.00 67.18  ?  608 THR B CG2 1 
ATOM   4833  N N   . ASP A 1 593 ? 37.746  25.093  121.488 1.00 92.09  ?  609 ASP B N   1 
ATOM   4834  C CA  . ASP A 1 593 ? 39.108  25.332  121.022 1.00 91.32  ?  609 ASP B CA  1 
ATOM   4835  C C   . ASP A 1 593 ? 39.725  24.182  120.228 1.00 88.42  ?  609 ASP B C   1 
ATOM   4836  O O   . ASP A 1 593 ? 40.770  24.391  119.609 1.00 91.42  ?  609 ASP B O   1 
ATOM   4837  C CB  . ASP A 1 593 ? 40.014  25.722  122.204 1.00 94.55  ?  609 ASP B CB  1 
ATOM   4838  C CG  . ASP A 1 593 ? 40.038  24.675  123.291 1.00 107.25 ?  609 ASP B CG  1 
ATOM   4839  O OD1 . ASP A 1 593 ? 38.958  24.158  123.657 1.00 102.49 ?  609 ASP B OD1 1 
ATOM   4840  O OD2 . ASP A 1 593 ? 41.142  24.393  123.817 1.00 122.59 -1 609 ASP B OD2 1 
ATOM   4841  N N   . TRP A 1 594 ? 39.108  23.003  120.189 1.00 82.44  ?  610 TRP B N   1 
ATOM   4842  C CA  . TRP A 1 594 ? 39.575  21.953  119.285 1.00 79.73  ?  610 TRP B CA  1 
ATOM   4843  C C   . TRP A 1 594 ? 39.297  22.302  117.834 1.00 80.89  ?  610 TRP B C   1 
ATOM   4844  O O   . TRP A 1 594 ? 38.369  23.051  117.530 1.00 84.64  ?  610 TRP B O   1 
ATOM   4845  C CB  . TRP A 1 594 ? 38.917  20.624  119.631 1.00 80.11  ?  610 TRP B CB  1 
ATOM   4846  C CG  . TRP A 1 594 ? 39.254  19.520  118.695 1.00 81.15  ?  610 TRP B CG  1 
ATOM   4847  C CD1 . TRP A 1 594 ? 40.314  18.710  118.755 1.00 85.96  ?  610 TRP B CD1 1 
ATOM   4848  C CD2 . TRP A 1 594 ? 38.461  19.067  117.579 1.00 83.40  ?  610 TRP B CD2 1 
ATOM   4849  N NE1 . TRP A 1 594 ? 40.280  17.791  117.725 1.00 89.79  ?  610 TRP B NE1 1 
ATOM   4850  C CE2 . TRP A 1 594 ? 39.139  17.989  116.996 1.00 86.09  ?  610 TRP B CE2 1 
ATOM   4851  C CE3 . TRP A 1 594 ? 37.251  19.479  117.016 1.00 86.04  ?  610 TRP B CE3 1 
ATOM   4852  C CZ2 . TRP A 1 594 ? 38.657  17.312  115.878 1.00 87.73  ?  610 TRP B CZ2 1 
ATOM   4853  C CZ3 . TRP A 1 594 ? 36.774  18.802  115.903 1.00 85.20  ?  610 TRP B CZ3 1 
ATOM   4854  C CH2 . TRP A 1 594 ? 37.480  17.733  115.350 1.00 85.79  ?  610 TRP B CH2 1 
ATOM   4855  N N   . SER A 1 595 ? 40.097  21.738  116.927 1.00 81.54  ?  611 SER B N   1 
ATOM   4856  C CA  . SER A 1 595 ? 39.900  21.953  115.497 1.00 88.61  ?  611 SER B CA  1 
ATOM   4857  C C   . SER A 1 595 ? 40.661  20.880  114.742 1.00 91.57  ?  611 SER B C   1 
ATOM   4858  O O   . SER A 1 595 ? 41.655  20.354  115.259 1.00 94.68  ?  611 SER B O   1 
ATOM   4859  C CB  . SER A 1 595 ? 40.380  23.347  115.064 1.00 91.49  ?  611 SER B CB  1 
ATOM   4860  O OG  . SER A 1 595 ? 41.747  23.322  114.673 1.00 95.94  ?  611 SER B OG  1 
ATOM   4861  N N   . PRO A 1 596 ? 40.232  20.532  113.525 1.00 86.06  ?  612 PRO B N   1 
ATOM   4862  C CA  . PRO A 1 596 ? 40.971  19.518  112.768 1.00 86.73  ?  612 PRO B CA  1 
ATOM   4863  C C   . PRO A 1 596 ? 42.359  19.945  112.347 1.00 92.82  ?  612 PRO B C   1 
ATOM   4864  O O   . PRO A 1 596 ? 43.141  19.060  111.981 1.00 98.77  ?  612 PRO B O   1 
ATOM   4865  C CB  . PRO A 1 596 ? 40.070  19.245  111.549 1.00 88.16  ?  612 PRO B CB  1 
ATOM   4866  C CG  . PRO A 1 596 ? 38.708  19.628  112.007 1.00 87.12  ?  612 PRO B CG  1 
ATOM   4867  C CD  . PRO A 1 596 ? 38.931  20.829  112.893 1.00 87.86  ?  612 PRO B CD  1 
ATOM   4868  N N   . TYR A 1 597 ? 42.722  21.235  112.411 1.00 96.37  ?  613 TYR B N   1 
ATOM   4869  C CA  . TYR A 1 597 ? 44.027  21.619  111.877 1.00 102.29 ?  613 TYR B CA  1 
ATOM   4870  C C   . TYR A 1 597 ? 45.107  21.935  112.931 1.00 106.04 ?  613 TYR B C   1 
ATOM   4871  O O   . TYR A 1 597 ? 46.306  21.821  112.627 1.00 105.43 ?  613 TYR B O   1 
ATOM   4872  C CB  . TYR A 1 597 ? 43.876  22.811  110.923 1.00 94.38  ?  613 TYR B CB  1 
ATOM   4873  C CG  . TYR A 1 597 ? 43.240  24.053  111.495 1.00 94.17  ?  613 TYR B CG  1 
ATOM   4874  C CD1 . TYR A 1 597 ? 44.033  25.013  112.106 1.00 97.78  ?  613 TYR B CD1 1 
ATOM   4875  C CD2 . TYR A 1 597 ? 41.888  24.317  111.364 1.00 93.07  ?  613 TYR B CD2 1 
ATOM   4876  C CE1 . TYR A 1 597 ? 43.505  26.177  112.621 1.00 95.85  ?  613 TYR B CE1 1 
ATOM   4877  C CE2 . TYR A 1 597 ? 41.344  25.506  111.877 1.00 93.38  ?  613 TYR B CE2 1 
ATOM   4878  C CZ  . TYR A 1 597 ? 42.172  26.427  112.509 1.00 92.78  ?  613 TYR B CZ  1 
ATOM   4879  O OH  . TYR A 1 597 ? 41.699  27.607  113.038 1.00 89.80  ?  613 TYR B OH  1 
ATOM   4880  N N   . ALA A 1 598 ? 44.734  22.314  114.146 1.00 103.54 ?  614 ALA B N   1 
ATOM   4881  C CA  . ALA A 1 598 ? 45.722  22.492  115.202 1.00 110.23 ?  614 ALA B CA  1 
ATOM   4882  C C   . ALA A 1 598 ? 46.118  21.137  115.760 1.00 128.30 ?  614 ALA B C   1 
ATOM   4883  O O   . ALA A 1 598 ? 45.285  20.440  116.344 1.00 121.72 ?  614 ALA B O   1 
ATOM   4884  C CB  . ALA A 1 598 ? 45.179  23.384  116.307 1.00 108.13 ?  614 ALA B CB  1 
ATOM   4885  N N   . THR B 2 1   ? -74.291 33.741  40.260  1.00 148.69 ?  333 THR C N   1 
ATOM   4886  C CA  . THR B 2 1   ? -73.800 33.705  41.638  1.00 142.22 ?  333 THR C CA  1 
ATOM   4887  C C   . THR B 2 1   ? -72.305 33.437  41.655  1.00 139.99 ?  333 THR C C   1 
ATOM   4888  O O   . THR B 2 1   ? -71.733 33.053  42.677  1.00 135.99 ?  333 THR C O   1 
ATOM   4889  C CB  . THR B 2 1   ? -74.497 32.627  42.454  1.00 143.29 ?  333 THR C CB  1 
ATOM   4890  O OG1 . THR B 2 1   ? -73.841 31.369  42.230  1.00 143.22 ?  333 THR C OG1 1 
ATOM   4891  C CG2 . THR B 2 1   ? -75.940 32.510  42.001  1.00 151.09 ?  333 THR C CG2 1 
ATOM   4892  N N   . ASN B 2 2   ? -71.677 33.621  40.503  1.00 143.38 ?  334 ASN C N   1 
ATOM   4893  C CA  . ASN B 2 2   ? -70.248 33.401  40.389  1.00 144.35 ?  334 ASN C CA  1 
ATOM   4894  C C   . ASN B 2 2   ? -69.523 34.526  41.129  1.00 141.91 ?  334 ASN C C   1 
ATOM   4895  O O   . ASN B 2 2   ? -69.983 35.671  41.127  1.00 139.86 ?  334 ASN C O   1 
ATOM   4896  C CB  . ASN B 2 2   ? -69.873 33.374  38.910  1.00 145.81 ?  334 ASN C CB  1 
ATOM   4897  C CG  . ASN B 2 2   ? -68.625 32.568  38.638  1.00 157.15 ?  334 ASN C CG  1 
ATOM   4898  O OD1 . ASN B 2 2   ? -67.796 32.354  39.526  1.00 161.61 ?  334 ASN C OD1 1 
ATOM   4899  N ND2 . ASN B 2 2   ? -68.479 32.112  37.394  1.00 153.89 ?  334 ASN C ND2 1 
ATOM   4900  N N   . LEU B 2 3   ? -68.400 34.205  41.783  1.00 133.16 ?  335 LEU C N   1 
ATOM   4901  C CA  . LEU B 2 3   ? -67.630 35.232  42.486  1.00 125.61 ?  335 LEU C CA  1 
ATOM   4902  C C   . LEU B 2 3   ? -66.916 36.150  41.488  1.00 125.90 ?  335 LEU C C   1 
ATOM   4903  O O   . LEU B 2 3   ? -66.319 35.688  40.510  1.00 126.81 ?  335 LEU C O   1 
ATOM   4904  C CB  . LEU B 2 3   ? -66.615 34.585  43.436  1.00 123.45 ?  335 LEU C CB  1 
ATOM   4905  C CG  . LEU B 2 3   ? -66.055 35.373  44.645  1.00 125.07 ?  335 LEU C CG  1 
ATOM   4906  C CD1 . LEU B 2 3   ? -65.271 34.442  45.575  1.00 119.60 ?  335 LEU C CD1 1 
ATOM   4907  C CD2 . LEU B 2 3   ? -65.195 36.621  44.292  1.00 131.74 ?  335 LEU C CD2 1 
ATOM   4908  N N   . CYS B 2 4   ? -67.133 37.451  41.689  1.00 120.76 ?  336 CYS C N   1 
ATOM   4909  C CA  . CYS B 2 4   ? -66.570 38.445  40.747  1.00 120.42 ?  336 CYS C CA  1 
ATOM   4910  C C   . CYS B 2 4   ? -65.069 38.222  40.648  1.00 118.99 ?  336 CYS C C   1 
ATOM   4911  O O   . CYS B 2 4   ? -64.419 38.047  41.693  1.00 118.17 ?  336 CYS C O   1 
ATOM   4912  C CB  . CYS B 2 4   ? -66.933 39.854  41.193  1.00 114.51 ?  336 CYS C CB  1 
ATOM   4913  S SG  . CYS B 2 4   ? -68.689 40.223  40.939  1.00 121.68 ?  336 CYS C SG  1 
ATOM   4914  N N   . PRO B 2 5   ? -64.501 38.233  39.432  1.00 133.77 ?  337 PRO C N   1 
ATOM   4915  C CA  . PRO B 2 5   ? -63.097 37.907  39.255  1.00 136.22 ?  337 PRO C CA  1 
ATOM   4916  C C   . PRO B 2 5   ? -62.236 39.096  39.675  1.00 129.66 ?  337 PRO C C   1 
ATOM   4917  O O   . PRO B 2 5   ? -61.543 39.655  38.851  1.00 130.54 ?  337 PRO C O   1 
ATOM   4918  C CB  . PRO B 2 5   ? -63.053 37.660  37.743  1.00 141.46 ?  337 PRO C CB  1 
ATOM   4919  C CG  . PRO B 2 5   ? -64.050 38.641  37.182  1.00 138.37 ?  337 PRO C CG  1 
ATOM   4920  C CD  . PRO B 2 5   ? -65.171 38.646  38.197  1.00 136.07 ?  337 PRO C CD  1 
ATOM   4921  N N   . PHE B 2 6   ? -62.326 39.464  40.949  1.00 116.75 ?  338 PHE C N   1 
ATOM   4922  C CA  . PHE B 2 6   ? -61.484 40.572  41.449  1.00 107.59 ?  338 PHE C CA  1 
ATOM   4923  C C   . PHE B 2 6   ? -60.048 40.069  41.530  1.00 102.59 ?  338 PHE C C   1 
ATOM   4924  O O   . PHE B 2 6   ? -59.157 40.729  40.987  1.00 96.91  ?  338 PHE C O   1 
ATOM   4925  C CB  . PHE B 2 6   ? -61.991 41.052  42.807  1.00 106.76 ?  338 PHE C CB  1 
ATOM   4926  C CG  . PHE B 2 6   ? -63.156 41.998  42.721  1.00 96.95  ?  338 PHE C CG  1 
ATOM   4927  C CD1 . PHE B 2 6   ? -63.336 42.789  41.598  1.00 99.03  ?  338 PHE C CD1 1 
ATOM   4928  C CD2 . PHE B 2 6   ? -64.073 42.091  43.753  1.00 104.40 ?  338 PHE C CD2 1 
ATOM   4929  C CE1 . PHE B 2 6   ? -64.408 43.659  41.513  1.00 95.03  ?  338 PHE C CE1 1 
ATOM   4930  C CE2 . PHE B 2 6   ? -65.146 42.963  43.667  1.00 109.97 ?  338 PHE C CE2 1 
ATOM   4931  C CZ  . PHE B 2 6   ? -65.309 43.743  42.547  1.00 95.70  ?  338 PHE C CZ  1 
ATOM   4932  N N   . ASP B 2 7   ? -59.831 38.993  42.277  1.00 97.23  ?  339 ASP C N   1 
ATOM   4933  C CA  . ASP B 2 7   ? -58.443 38.532  42.527  1.00 105.16 ?  339 ASP C CA  1 
ATOM   4934  C C   . ASP B 2 7   ? -57.615 38.695  41.262  1.00 106.06 ?  339 ASP C C   1 
ATOM   4935  O O   . ASP B 2 7   ? -56.478 39.178  41.364  1.00 107.53 ?  339 ASP C O   1 
ATOM   4936  C CB  . ASP B 2 7   ? -58.416 37.098  43.044  1.00 110.35 ?  339 ASP C CB  1 
ATOM   4937  C CG  . ASP B 2 7   ? -57.100 36.709  43.699  1.00 117.82 ?  339 ASP C CG  1 
ATOM   4938  O OD1 . ASP B 2 7   ? -56.140 36.439  42.956  1.00 119.34 ?  339 ASP C OD1 1 
ATOM   4939  O OD2 . ASP B 2 7   ? -57.051 36.662  44.946  1.00 116.78 -1 339 ASP C OD2 1 
ATOM   4940  N N   . GLU B 2 8   ? -58.173 38.321  40.122  1.00 102.78 ?  340 GLU C N   1 
ATOM   4941  C CA  . GLU B 2 8   ? -57.347 38.363  38.896  1.00 102.98 ?  340 GLU C CA  1 
ATOM   4942  C C   . GLU B 2 8   ? -56.861 39.789  38.692  1.00 91.79  ?  340 GLU C C   1 
ATOM   4943  O O   . GLU B 2 8   ? -55.701 39.945  38.353  1.00 95.41  ?  340 GLU C O   1 
ATOM   4944  C CB  . GLU B 2 8   ? -58.126 37.785  37.717  1.00 114.41 ?  340 GLU C CB  1 
ATOM   4945  C CG  . GLU B 2 8   ? -58.953 38.777  36.933  1.00 115.56 ?  340 GLU C CG  1 
ATOM   4946  C CD  . GLU B 2 8   ? -59.613 38.113  35.740  1.00 125.42 ?  340 GLU C CD  1 
ATOM   4947  O OE1 . GLU B 2 8   ? -58.998 37.178  35.191  1.00 123.50 ?  340 GLU C OE1 1 
ATOM   4948  O OE2 . GLU B 2 8   ? -60.732 38.510  35.373  1.00 135.18 -1 340 GLU C OE2 1 
ATOM   4949  N N   . VAL B 2 9   ? -57.703 40.773  38.981  1.00 94.98  ?  341 VAL C N   1 
ATOM   4950  C CA  . VAL B 2 9   ? -57.330 42.190  38.724  1.00 90.77  ?  341 VAL C CA  1 
ATOM   4951  C C   . VAL B 2 9   ? -56.330 42.697  39.760  1.00 89.91  ?  341 VAL C C   1 
ATOM   4952  O O   . VAL B 2 9   ? -55.572 43.607  39.417  1.00 84.81  ?  341 VAL C O   1 
ATOM   4953  C CB  . VAL B 2 9   ? -58.591 43.068  38.758  1.00 86.05  ?  341 VAL C CB  1 
ATOM   4954  C CG1 . VAL B 2 9   ? -58.241 44.548  38.710  1.00 76.16  ?  341 VAL C CG1 1 
ATOM   4955  C CG2 . VAL B 2 9   ? -59.550 42.702  37.642  1.00 90.13  ?  341 VAL C CG2 1 
ATOM   4956  N N   . PHE B 2 10  ? -56.315 42.137  40.965  1.00 83.37  ?  342 PHE C N   1 
ATOM   4957  C CA  . PHE B 2 10  ? -55.518 42.706  42.043  1.00 81.36  ?  342 PHE C CA  1 
ATOM   4958  C C   . PHE B 2 10  ? -54.213 41.939  42.243  1.00 82.17  ?  342 PHE C C   1 
ATOM   4959  O O   . PHE B 2 10  ? -53.143 42.539  42.400  1.00 77.07  ?  342 PHE C O   1 
ATOM   4960  C CB  . PHE B 2 10  ? -56.331 42.696  43.344  1.00 86.52  ?  342 PHE C CB  1 
ATOM   4961  C CG  . PHE B 2 10  ? -57.335 43.818  43.467  1.00 82.48  ?  342 PHE C CG  1 
ATOM   4962  C CD1 . PHE B 2 10  ? -57.705 44.555  42.385  1.00 82.91  ?  342 PHE C CD1 1 
ATOM   4963  C CD2 . PHE B 2 10  ? -57.921 44.118  44.667  1.00 87.62  ?  342 PHE C CD2 1 
ATOM   4964  C CE1 . PHE B 2 10  ? -58.627 45.570  42.504  1.00 82.73  ?  342 PHE C CE1 1 
ATOM   4965  C CE2 . PHE B 2 10  ? -58.836 45.143  44.764  1.00 85.64  ?  342 PHE C CE2 1 
ATOM   4966  C CZ  . PHE B 2 10  ? -59.183 45.859  43.692  1.00 78.05  ?  342 PHE C CZ  1 
ATOM   4967  N N   . ASN B 2 11  ? -54.299 40.610  42.274  1.00 82.79  ?  343 ASN C N   1 
ATOM   4968  C CA  . ASN B 2 11  ? -53.123 39.748  42.294  1.00 81.11  ?  343 ASN C CA  1 
ATOM   4969  C C   . ASN B 2 11  ? -52.822 39.246  40.889  1.00 77.65  ?  343 ASN C C   1 
ATOM   4970  O O   . ASN B 2 11  ? -52.558 38.054  40.685  1.00 75.36  ?  343 ASN C O   1 
ATOM   4971  C CB  . ASN B 2 11  ? -53.290 38.596  43.297  1.00 84.68  ?  343 ASN C CB  1 
ATOM   4972  C CG  . ASN B 2 11  ? -53.623 39.084  44.727  1.00 92.08  ?  343 ASN C CG  1 
ATOM   4973  O OD1 . ASN B 2 11  ? -53.435 40.259  45.063  1.00 90.39  ?  343 ASN C OD1 1 
ATOM   4974  N ND2 . ASN B 2 11  ? -54.138 38.177  45.562  1.00 97.67  ?  343 ASN C ND2 1 
ATOM   4975  N N   . ALA B 2 12  ? -52.880 40.162  39.909  1.00 75.31  ?  344 ALA C N   1 
ATOM   4976  C CA  . ALA B 2 12  ? -52.449 39.904  38.538  1.00 78.41  ?  344 ALA C CA  1 
ATOM   4977  C C   . ALA B 2 12  ? -50.949 40.159  38.376  1.00 78.47  ?  344 ALA C C   1 
ATOM   4978  O O   . ALA B 2 12  ? -50.390 41.081  38.971  1.00 76.29  ?  344 ALA C O   1 
ATOM   4979  C CB  . ALA B 2 12  ? -53.228 40.781  37.550  1.00 75.00  ?  344 ALA C CB  1 
ATOM   4980  N N   . THR B 2 13  ? -50.299 39.354  37.535  1.00 77.73  ?  345 THR C N   1 
ATOM   4981  C CA  . THR B 2 13  ? -48.843 39.415  37.446  1.00 73.97  ?  345 THR C CA  1 
ATOM   4982  C C   . THR B 2 13  ? -48.368 40.666  36.739  1.00 74.86  ?  345 THR C C   1 
ATOM   4983  O O   . THR B 2 13  ? -47.391 41.294  37.181  1.00 80.20  ?  345 THR C O   1 
ATOM   4984  C CB  . THR B 2 13  ? -48.320 38.180  36.747  1.00 86.74  ?  345 THR C CB  1 
ATOM   4985  O OG1 . THR B 2 13  ? -49.018 37.041  37.247  1.00 86.94  ?  345 THR C OG1 1 
ATOM   4986  C CG2 . THR B 2 13  ? -46.825 38.026  37.008  1.00 88.86  ?  345 THR C CG2 1 
ATOM   4987  N N   . ARG B 2 14  ? -49.023 41.048  35.644  1.00 76.32  ?  346 ARG C N   1 
ATOM   4988  C CA  . ARG B 2 14  ? -48.728 42.316  34.984  1.00 77.13  ?  346 ARG C CA  1 
ATOM   4989  C C   . ARG B 2 14  ? -49.859 43.312  35.139  1.00 67.07  ?  346 ARG C C   1 
ATOM   4990  O O   . ARG B 2 14  ? -51.013 42.963  35.379  1.00 66.86  ?  346 ARG C O   1 
ATOM   4991  C CB  . ARG B 2 14  ? -48.469 42.128  33.519  1.00 98.57  ?  346 ARG C CB  1 
ATOM   4992  C CG  . ARG B 2 14  ? -47.341 41.236  33.396  1.00 113.71 ?  346 ARG C CG  1 
ATOM   4993  C CD  . ARG B 2 14  ? -47.314 40.510  32.027  1.00 117.76 ?  346 ARG C CD  1 
ATOM   4994  N NE  . ARG B 2 14  ? -47.912 39.240  32.380  1.00 131.37 ?  346 ARG C NE  1 
ATOM   4995  C CZ  . ARG B 2 14  ? -47.232 38.150  32.712  1.00 140.62 ?  346 ARG C CZ  1 
ATOM   4996  N NH1 . ARG B 2 14  ? -45.901 38.118  32.572  1.00 133.37 ?  346 ARG C NH1 1 
ATOM   4997  N NH2 . ARG B 2 14  ? -47.917 37.050  33.097  1.00 144.30 ?  346 ARG C NH2 1 
ATOM   4998  N N   . PHE B 2 15  ? -49.487 44.581  35.081  1.00 60.97  ?  347 PHE C N   1 
ATOM   4999  C CA  . PHE B 2 15  ? -50.423 45.678  35.088  1.00 58.15  ?  347 PHE C CA  1 
ATOM   5000  C C   . PHE B 2 15  ? -50.137 46.477  33.839  1.00 55.37  ?  347 PHE C C   1 
ATOM   5001  O O   . PHE B 2 15  ? -48.996 46.538  33.384  1.00 54.09  ?  347 PHE C O   1 
ATOM   5002  C CB  . PHE B 2 15  ? -50.283 46.554  36.346  1.00 60.42  ?  347 PHE C CB  1 
ATOM   5003  C CG  . PHE B 2 15  ? -51.211 46.164  37.488  1.00 54.33  ?  347 PHE C CG  1 
ATOM   5004  C CD1 . PHE B 2 15  ? -51.148 44.917  38.046  1.00 58.83  ?  347 PHE C CD1 1 
ATOM   5005  C CD2 . PHE B 2 15  ? -52.180 47.037  37.952  1.00 55.40  ?  347 PHE C CD2 1 
ATOM   5006  C CE1 . PHE B 2 15  ? -51.982 44.570  39.060  1.00 62.81  ?  347 PHE C CE1 1 
ATOM   5007  C CE2 . PHE B 2 15  ? -53.027 46.679  38.968  1.00 54.63  ?  347 PHE C CE2 1 
ATOM   5008  C CZ  . PHE B 2 15  ? -52.933 45.448  39.507  1.00 60.70  ?  347 PHE C CZ  1 
ATOM   5009  N N   . ALA B 2 16  ? -51.174 47.033  33.244  1.00 50.98  ?  348 ALA C N   1 
ATOM   5010  C CA  . ALA B 2 16  ? -50.937 47.866  32.079  1.00 53.87  ?  348 ALA C CA  1 
ATOM   5011  C C   . ALA B 2 16  ? -50.169 49.102  32.499  1.00 51.91  ?  348 ALA C C   1 
ATOM   5012  O O   . ALA B 2 16  ? -50.166 49.470  33.674  1.00 55.93  ?  348 ALA C O   1 
ATOM   5013  C CB  . ALA B 2 16  ? -52.251 48.272  31.418  1.00 60.14  ?  348 ALA C CB  1 
ATOM   5014  N N   . SER B 2 17  ? -49.480 49.738  31.553  1.00 54.60  ?  349 SER C N   1 
ATOM   5015  C CA  . SER B 2 17  ? -48.918 51.030  31.929  1.00 58.61  ?  349 SER C CA  1 
ATOM   5016  C C   . SER B 2 17  ? -49.970 52.082  31.630  1.00 55.77  ?  349 SER C C   1 
ATOM   5017  O O   . SER B 2 17  ? -50.896 51.853  30.849  1.00 50.11  ?  349 SER C O   1 
ATOM   5018  C CB  . SER B 2 17  ? -47.534 51.337  31.294  1.00 58.95  ?  349 SER C CB  1 
ATOM   5019  O OG  . SER B 2 17  ? -47.380 51.229  29.889  1.00 57.45  ?  349 SER C OG  1 
ATOM   5020  N N   . VAL B 2 18  ? -49.875 53.203  32.347  1.00 53.82  ?  350 VAL C N   1 
ATOM   5021  C CA  . VAL B 2 18  ? -51.060 54.019  32.594  1.00 49.62  ?  350 VAL C CA  1 
ATOM   5022  C C   . VAL B 2 18  ? -51.622 54.572  31.295  1.00 51.77  ?  350 VAL C C   1 
ATOM   5023  O O   . VAL B 2 18  ? -52.840 54.586  31.102  1.00 57.64  ?  350 VAL C O   1 
ATOM   5024  C CB  . VAL B 2 18  ? -50.738 55.136  33.596  1.00 48.34  ?  350 VAL C CB  1 
ATOM   5025  C CG1 . VAL B 2 18  ? -49.581 55.928  33.098  1.00 56.03  ?  350 VAL C CG1 1 
ATOM   5026  C CG2 . VAL B 2 18  ? -51.887 56.024  33.735  1.00 46.44  ?  350 VAL C CG2 1 
ATOM   5027  N N   . TYR B 2 19  ? -50.762 55.001  30.368  1.00 51.92  ?  351 TYR C N   1 
ATOM   5028  C CA  . TYR B 2 19  ? -51.265 55.584  29.131  1.00 51.32  ?  351 TYR C CA  1 
ATOM   5029  C C   . TYR B 2 19  ? -52.192 54.653  28.377  1.00 54.23  ?  351 TYR C C   1 
ATOM   5030  O O   . TYR B 2 19  ? -53.110 55.126  27.693  1.00 59.27  ?  351 TYR C O   1 
ATOM   5031  C CB  . TYR B 2 19  ? -50.123 55.980  28.230  1.00 53.10  ?  351 TYR C CB  1 
ATOM   5032  C CG  . TYR B 2 19  ? -49.631 54.853  27.358  1.00 53.44  ?  351 TYR C CG  1 
ATOM   5033  C CD1 . TYR B 2 19  ? -48.790 53.903  27.875  1.00 55.52  ?  351 TYR C CD1 1 
ATOM   5034  C CD2 . TYR B 2 19  ? -49.975 54.743  26.027  1.00 53.52  ?  351 TYR C CD2 1 
ATOM   5035  C CE1 . TYR B 2 19  ? -48.295 52.887  27.110  1.00 53.08  ?  351 TYR C CE1 1 
ATOM   5036  C CE2 . TYR B 2 19  ? -49.478 53.698  25.248  1.00 50.00  ?  351 TYR C CE2 1 
ATOM   5037  C CZ  . TYR B 2 19  ? -48.632 52.789  25.812  1.00 47.57  ?  351 TYR C CZ  1 
ATOM   5038  O OH  . TYR B 2 19  ? -48.101 51.745  25.110  1.00 51.12  ?  351 TYR C OH  1 
ATOM   5039  N N   . ALA B 2 20  ? -51.973 53.341  28.483  1.00 51.26  ?  352 ALA C N   1 
ATOM   5040  C CA  . ALA B 2 20  ? -52.824 52.316  27.881  1.00 49.71  ?  352 ALA C CA  1 
ATOM   5041  C C   . ALA B 2 20  ? -53.507 51.453  28.942  1.00 50.69  ?  352 ALA C C   1 
ATOM   5042  O O   . ALA B 2 20  ? -53.597 50.220  28.800  1.00 50.15  ?  352 ALA C O   1 
ATOM   5043  C CB  . ALA B 2 20  ? -52.028 51.442  26.911  1.00 49.07  ?  352 ALA C CB  1 
ATOM   5044  N N   . TRP B 2 21  ? -54.008 52.101  30.005  1.00 51.18  ?  353 TRP C N   1 
ATOM   5045  C CA  . TRP B 2 21  ? -54.610 51.406  31.148  1.00 55.96  ?  353 TRP C CA  1 
ATOM   5046  C C   . TRP B 2 21  ? -55.633 50.370  30.720  1.00 57.97  ?  353 TRP C C   1 
ATOM   5047  O O   . TRP B 2 21  ? -56.317 50.551  29.714  1.00 62.32  ?  353 TRP C O   1 
ATOM   5048  C CB  . TRP B 2 21  ? -55.347 52.386  32.069  1.00 59.61  ?  353 TRP C CB  1 
ATOM   5049  C CG  . TRP B 2 21  ? -56.240 53.405  31.411  1.00 52.86  ?  353 TRP C CG  1 
ATOM   5050  C CD1 . TRP B 2 21  ? -55.858 54.533  30.780  1.00 53.60  ?  353 TRP C CD1 1 
ATOM   5051  C CD2 . TRP B 2 21  ? -57.650 53.303  31.230  1.00 57.06  ?  353 TRP C CD2 1 
ATOM   5052  N NE1 . TRP B 2 21  ? -56.936 55.192  30.283  1.00 57.80  ?  353 TRP C NE1 1 
ATOM   5053  C CE2 . TRP B 2 21  ? -58.055 54.445  30.527  1.00 56.56  ?  353 TRP C CE2 1 
ATOM   5054  C CE3 . TRP B 2 21  ? -58.612 52.356  31.608  1.00 58.45  ?  353 TRP C CE3 1 
ATOM   5055  C CZ2 . TRP B 2 21  ? -59.376 54.677  30.184  1.00 58.27  ?  353 TRP C CZ2 1 
ATOM   5056  C CZ3 . TRP B 2 21  ? -59.919 52.583  31.290  1.00 59.71  ?  353 TRP C CZ3 1 
ATOM   5057  C CH2 . TRP B 2 21  ? -60.298 53.737  30.574  1.00 63.49  ?  353 TRP C CH2 1 
ATOM   5058  N N   . ASN B 2 22  ? -55.810 49.289  31.479  1.00 50.70  ?  354 ASN C N   1 
ATOM   5059  C CA  . ASN B 2 22  ? -56.832 48.449  30.879  1.00 62.73  ?  354 ASN C CA  1 
ATOM   5060  C C   . ASN B 2 22  ? -58.014 48.352  31.819  1.00 64.83  ?  354 ASN C C   1 
ATOM   5061  O O   . ASN B 2 22  ? -57.925 48.586  33.026  1.00 58.39  ?  354 ASN C O   1 
ATOM   5062  C CB  . ASN B 2 22  ? -56.370 47.036  30.424  1.00 69.32  ?  354 ASN C CB  1 
ATOM   5063  C CG  . ASN B 2 22  ? -56.074 46.066  31.540  1.00 67.51  ?  354 ASN C CG  1 
ATOM   5064  O OD1 . ASN B 2 22  ? -56.685 46.103  32.606  1.00 69.71  ?  354 ASN C OD1 1 
ATOM   5065  N ND2 . ASN B 2 22  ? -55.108 45.171  31.286  1.00 69.79  ?  354 ASN C ND2 1 
ATOM   5066  N N   . ARG B 2 23  ? -59.144 48.058  31.202  1.00 65.98  ?  355 ARG C N   1 
ATOM   5067  C CA  . ARG B 2 23  ? -60.419 48.144  31.859  1.00 68.37  ?  355 ARG C CA  1 
ATOM   5068  C C   . ARG B 2 23  ? -61.050 46.802  31.672  1.00 68.73  ?  355 ARG C C   1 
ATOM   5069  O O   . ARG B 2 23  ? -60.936 46.221  30.590  1.00 67.58  ?  355 ARG C O   1 
ATOM   5070  C CB  . ARG B 2 23  ? -61.282 49.223  31.256  1.00 70.34  ?  355 ARG C CB  1 
ATOM   5071  C CG  . ARG B 2 23  ? -62.734 48.880  31.198  1.00 74.35  ?  355 ARG C CG  1 
ATOM   5072  C CD  . ARG B 2 23  ? -63.400 50.130  30.813  1.00 76.31  ?  355 ARG C CD  1 
ATOM   5073  N NE  . ARG B 2 23  ? -63.532 50.946  32.011  1.00 70.16  ?  355 ARG C NE  1 
ATOM   5074  C CZ  . ARG B 2 23  ? -64.216 52.074  32.067  1.00 73.40  ?  355 ARG C CZ  1 
ATOM   5075  N NH1 . ARG B 2 23  ? -64.770 52.594  30.992  1.00 79.29  ?  355 ARG C NH1 1 
ATOM   5076  N NH2 . ARG B 2 23  ? -64.318 52.714  33.223  1.00 74.21  ?  355 ARG C NH2 1 
ATOM   5077  N N   . LYS B 2 24  ? -61.631 46.286  32.743  1.00 69.72  ?  356 LYS C N   1 
ATOM   5078  C CA  . LYS B 2 24  ? -62.202 44.957  32.759  1.00 72.51  ?  356 LYS C CA  1 
ATOM   5079  C C   . LYS B 2 24  ? -63.633 45.168  33.177  1.00 76.08  ?  356 LYS C C   1 
ATOM   5080  O O   . LYS B 2 24  ? -63.883 45.882  34.153  1.00 77.48  ?  356 LYS C O   1 
ATOM   5081  C CB  . LYS B 2 24  ? -61.475 44.017  33.734  1.00 74.65  ?  356 LYS C CB  1 
ATOM   5082  C CG  . LYS B 2 24  ? -60.328 43.157  33.055  1.00 91.62  ?  356 LYS C CG  1 
ATOM   5083  C CD  . LYS B 2 24  ? -59.289 44.039  32.204  1.00 87.64  ?  356 LYS C CD  1 
ATOM   5084  C CE  . LYS B 2 24  ? -58.518 43.309  31.057  1.00 78.23  ?  356 LYS C CE  1 
ATOM   5085  N NZ  . LYS B 2 24  ? -57.691 42.139  31.472  1.00 82.79  ?  356 LYS C NZ  1 
ATOM   5086  N N   . ARG B 2 25  ? -64.559 44.623  32.394  1.00 82.28  ?  357 ARG C N   1 
ATOM   5087  C CA  . ARG B 2 25  ? -65.992 44.730  32.662  1.00 87.71  ?  357 ARG C CA  1 
ATOM   5088  C C   . ARG B 2 25  ? -66.355 43.695  33.708  1.00 88.65  ?  357 ARG C C   1 
ATOM   5089  O O   . ARG B 2 25  ? -66.474 42.511  33.410  1.00 93.62  ?  357 ARG C O   1 
ATOM   5090  C CB  . ARG B 2 25  ? -66.788 44.539  31.379  1.00 95.12  ?  357 ARG C CB  1 
ATOM   5091  C CG  . ARG B 2 25  ? -68.202 45.168  31.322  1.00 103.45 ?  357 ARG C CG  1 
ATOM   5092  C CD  . ARG B 2 25  ? -68.972 44.431  30.234  1.00 107.23 ?  357 ARG C CD  1 
ATOM   5093  N NE  . ARG B 2 25  ? -70.282 43.973  30.680  1.00 121.01 ?  357 ARG C NE  1 
ATOM   5094  C CZ  . ARG B 2 25  ? -70.988 43.018  30.073  1.00 133.35 ?  357 ARG C CZ  1 
ATOM   5095  N NH1 . ARG B 2 25  ? -70.533 42.393  28.986  1.00 125.31 ?  357 ARG C NH1 1 
ATOM   5096  N NH2 . ARG B 2 25  ? -72.166 42.652  30.588  1.00 134.21 ?  357 ARG C NH2 1 
ATOM   5097  N N   . ILE B 2 26  ? -66.499 44.141  34.948  1.00 96.51  ?  358 ILE C N   1 
ATOM   5098  C CA  . ILE B 2 26  ? -66.921 43.294  36.053  1.00 98.74  ?  358 ILE C CA  1 
ATOM   5099  C C   . ILE B 2 26  ? -68.438 43.339  36.020  1.00 107.83 ?  358 ILE C C   1 
ATOM   5100  O O   . ILE B 2 26  ? -69.037 44.412  36.195  1.00 111.75 ?  358 ILE C O   1 
ATOM   5101  C CB  . ILE B 2 26  ? -66.372 43.794  37.398  1.00 100.00 ?  358 ILE C CB  1 
ATOM   5102  C CG1 . ILE B 2 26  ? -64.831 43.930  37.385  1.00 105.70 ?  358 ILE C CG1 1 
ATOM   5103  C CG2 . ILE B 2 26  ? -66.813 42.890  38.541  1.00 104.72 ?  358 ILE C CG2 1 
ATOM   5104  C CD1 . ILE B 2 26  ? -64.054 42.971  36.431  1.00 112.21 ?  358 ILE C CD1 1 
ATOM   5105  N N   . SER B 2 27  ? -69.059 42.189  35.744  1.00 117.79 ?  359 SER C N   1 
ATOM   5106  C CA  . SER B 2 27  ? -70.482 42.174  35.442  1.00 120.55 ?  359 SER C CA  1 
ATOM   5107  C C   . SER B 2 27  ? -70.966 40.740  35.466  1.00 127.86 ?  359 SER C C   1 
ATOM   5108  O O   . SER B 2 27  ? -70.225 39.840  35.088  1.00 125.16 ?  359 SER C O   1 
ATOM   5109  C CB  . SER B 2 27  ? -70.757 42.805  34.072  1.00 125.77 ?  359 SER C CB  1 
ATOM   5110  O OG  . SER B 2 27  ? -70.976 44.213  34.175  1.00 129.20 ?  359 SER C OG  1 
ATOM   5111  N N   . ASN B 2 28  ? -72.213 40.542  35.918  1.00 151.85 ?  360 ASN C N   1 
ATOM   5112  C CA  . ASN B 2 28  ? -72.876 39.229  36.001  1.00 156.16 ?  360 ASN C CA  1 
ATOM   5113  C C   . ASN B 2 28  ? -72.125 38.288  36.950  1.00 148.49 ?  360 ASN C C   1 
ATOM   5114  O O   . ASN B 2 28  ? -71.608 37.237  36.569  1.00 146.87 ?  360 ASN C O   1 
ATOM   5115  C CB  . ASN B 2 28  ? -73.067 38.611  34.604  1.00 158.76 ?  360 ASN C CB  1 
ATOM   5116  C CG  . ASN B 2 28  ? -73.491 39.642  33.531  1.00 164.38 ?  360 ASN C CG  1 
ATOM   5117  O OD1 . ASN B 2 28  ? -72.650 40.234  32.834  1.00 163.98 ?  360 ASN C OD1 1 
ATOM   5118  N ND2 . ASN B 2 28  ? -74.809 39.795  33.352  1.00 164.05 ?  360 ASN C ND2 1 
ATOM   5119  N N   . CYS B 2 29  ? -72.128 38.673  38.216  1.00 125.45 ?  361 CYS C N   1 
ATOM   5120  C CA  . CYS B 2 29  ? -71.239 38.120  39.214  1.00 120.60 ?  361 CYS C CA  1 
ATOM   5121  C C   . CYS B 2 29  ? -71.530 38.794  40.548  1.00 119.01 ?  361 CYS C C   1 
ATOM   5122  O O   . CYS B 2 29  ? -72.041 39.920  40.588  1.00 122.48 ?  361 CYS C O   1 
ATOM   5123  C CB  . CYS B 2 29  ? -69.777 38.289  38.788  1.00 120.77 ?  361 CYS C CB  1 
ATOM   5124  S SG  . CYS B 2 29  ? -69.012 39.958  38.948  1.00 123.63 ?  361 CYS C SG  1 
ATOM   5125  N N   . VAL B 2 30  ? -71.240 38.080  41.636  1.00 122.20 ?  362 VAL C N   1 
ATOM   5126  C CA  . VAL B 2 30  ? -71.427 38.582  43.000  1.00 115.10 ?  362 VAL C CA  1 
ATOM   5127  C C   . VAL B 2 30  ? -70.057 38.827  43.618  1.00 123.53 ?  362 VAL C C   1 
ATOM   5128  O O   . VAL B 2 30  ? -69.153 37.996  43.478  1.00 127.01 ?  362 VAL C O   1 
ATOM   5129  C CB  . VAL B 2 30  ? -72.225 37.600  43.865  1.00 109.44 ?  362 VAL C CB  1 
ATOM   5130  C CG1 . VAL B 2 30  ? -71.612 36.188  43.763  1.00 116.65 ?  362 VAL C CG1 1 
ATOM   5131  C CG2 . VAL B 2 30  ? -72.230 38.069  45.278  1.00 105.62 ?  362 VAL C CG2 1 
ATOM   5132  N N   . ALA B 2 31  ? -69.920 39.938  44.352  1.00 126.70 ?  363 ALA C N   1 
ATOM   5133  C CA  . ALA B 2 31  ? -68.625 40.554  44.603  1.00 130.07 ?  363 ALA C CA  1 
ATOM   5134  C C   . ALA B 2 31  ? -68.123 40.400  46.035  1.00 141.74 ?  363 ALA C C   1 
ATOM   5135  O O   . ALA B 2 31  ? -68.898 40.336  46.996  1.00 135.13 ?  363 ALA C O   1 
ATOM   5136  C CB  . ALA B 2 31  ? -68.689 42.034  44.247  1.00 127.05 ?  363 ALA C CB  1 
ATOM   5137  N N   . ASP B 2 32  ? -66.793 40.429  46.153  1.00 170.76 ?  364 ASP C N   1 
ATOM   5138  C CA  . ASP B 2 32  ? -66.094 40.197  47.407  1.00 182.56 ?  364 ASP C CA  1 
ATOM   5139  C C   . ASP B 2 32  ? -65.432 41.455  47.972  1.00 189.88 ?  364 ASP C C   1 
ATOM   5140  O O   . ASP B 2 32  ? -64.499 41.355  48.776  1.00 204.20 ?  364 ASP C O   1 
ATOM   5141  C CB  . ASP B 2 32  ? -65.060 39.090  47.196  1.00 191.58 ?  364 ASP C CB  1 
ATOM   5142  C CG  . ASP B 2 32  ? -64.460 38.586  48.498  1.00 214.69 ?  364 ASP C CG  1 
ATOM   5143  O OD1 . ASP B 2 32  ? -65.170 38.637  49.529  1.00 221.19 ?  364 ASP C OD1 1 
ATOM   5144  O OD2 . ASP B 2 32  ? -63.283 38.165  48.494  1.00 218.68 -1 364 ASP C OD2 1 
ATOM   5145  N N   . TYR B 2 33  ? -65.889 42.649  47.578  1.00 167.12 ?  365 TYR C N   1 
ATOM   5146  C CA  . TYR B 2 33  ? -65.416 43.860  48.278  1.00 163.75 ?  365 TYR C CA  1 
ATOM   5147  C C   . TYR B 2 33  ? -65.878 43.932  49.726  1.00 172.77 ?  365 TYR C C   1 
ATOM   5148  O O   . TYR B 2 33  ? -65.606 44.925  50.403  1.00 170.86 ?  365 TYR C O   1 
ATOM   5149  C CB  . TYR B 2 33  ? -65.816 45.158  47.568  1.00 146.63 ?  365 TYR C CB  1 
ATOM   5150  C CG  . TYR B 2 33  ? -67.210 45.120  47.047  1.00 143.82 ?  365 TYR C CG  1 
ATOM   5151  C CD1 . TYR B 2 33  ? -68.278 45.071  47.918  1.00 147.90 ?  365 TYR C CD1 1 
ATOM   5152  C CD2 . TYR B 2 33  ? -67.466 45.301  45.686  1.00 129.50 ?  365 TYR C CD2 1 
ATOM   5153  C CE1 . TYR B 2 33  ? -69.553 45.033  47.466  1.00 145.09 ?  365 TYR C CE1 1 
ATOM   5154  C CE2 . TYR B 2 33  ? -68.752 45.307  45.211  1.00 127.65 ?  365 TYR C CE2 1 
ATOM   5155  C CZ  . TYR B 2 33  ? -69.802 45.170  46.115  1.00 140.10 ?  365 TYR C CZ  1 
ATOM   5156  O OH  . TYR B 2 33  ? -71.118 45.163  45.708  1.00 142.11 ?  365 TYR C OH  1 
ATOM   5157  N N   . SER B 2 34  ? -66.596 42.925  50.216  1.00 177.37 ?  366 SER C N   1 
ATOM   5158  C CA  . SER B 2 34  ? -66.800 42.823  51.653  1.00 184.41 ?  366 SER C CA  1 
ATOM   5159  C C   . SER B 2 34  ? -65.472 42.600  52.369  1.00 199.25 ?  366 SER C C   1 
ATOM   5160  O O   . SER B 2 34  ? -65.065 43.402  53.219  1.00 195.38 ?  366 SER C O   1 
ATOM   5161  C CB  . SER B 2 34  ? -67.788 41.692  51.949  1.00 184.13 ?  366 SER C CB  1 
ATOM   5162  O OG  . SER B 2 34  ? -67.107 40.484  52.215  1.00 196.71 ?  366 SER C OG  1 
ATOM   5163  N N   . VAL B 2 35  ? -64.751 41.542  51.991  1.00 243.20 ?  367 VAL C N   1 
ATOM   5164  C CA  . VAL B 2 35  ? -63.557 41.120  52.717  1.00 242.43 ?  367 VAL C CA  1 
ATOM   5165  C C   . VAL B 2 35  ? -62.261 41.450  51.985  1.00 234.60 ?  367 VAL C C   1 
ATOM   5166  O O   . VAL B 2 35  ? -61.179 41.237  52.556  1.00 231.42 ?  367 VAL C O   1 
ATOM   5167  C CB  . VAL B 2 35  ? -63.603 39.611  53.049  1.00 239.29 ?  367 VAL C CB  1 
ATOM   5168  C CG1 . VAL B 2 35  ? -63.096 38.788  51.879  1.00 230.22 ?  367 VAL C CG1 1 
ATOM   5169  C CG2 . VAL B 2 35  ? -62.835 39.299  54.332  1.00 238.37 ?  367 VAL C CG2 1 
ATOM   5170  N N   . LEU B 2 36  ? -62.316 41.944  50.750  1.00 191.79 ?  368 LEU C N   1 
ATOM   5171  C CA  . LEU B 2 36  ? -61.082 42.455  50.171  1.00 180.16 ?  368 LEU C CA  1 
ATOM   5172  C C   . LEU B 2 36  ? -60.738 43.850  50.675  1.00 179.96 ?  368 LEU C C   1 
ATOM   5173  O O   . LEU B 2 36  ? -59.592 44.285  50.523  1.00 173.73 ?  368 LEU C O   1 
ATOM   5174  C CB  . LEU B 2 36  ? -61.144 42.438  48.639  1.00 164.65 ?  368 LEU C CB  1 
ATOM   5175  C CG  . LEU B 2 36  ? -59.779 42.680  47.974  1.00 147.38 ?  368 LEU C CG  1 
ATOM   5176  C CD1 . LEU B 2 36  ? -59.503 41.810  46.763  1.00 131.46 ?  368 LEU C CD1 1 
ATOM   5177  C CD2 . LEU B 2 36  ? -59.742 44.121  47.585  1.00 123.98 ?  368 LEU C CD2 1 
ATOM   5178  N N   . TYR B 2 37  ? -61.682 44.547  51.307  1.00 179.54 ?  369 TYR C N   1 
ATOM   5179  C CA  . TYR B 2 37  ? -61.360 45.823  51.931  1.00 175.62 ?  369 TYR C CA  1 
ATOM   5180  C C   . TYR B 2 37  ? -60.428 45.680  53.138  1.00 180.66 ?  369 TYR C C   1 
ATOM   5181  O O   . TYR B 2 37  ? -59.889 46.690  53.608  1.00 178.18 ?  369 TYR C O   1 
ATOM   5182  C CB  . TYR B 2 37  ? -62.664 46.544  52.311  1.00 172.16 ?  369 TYR C CB  1 
ATOM   5183  C CG  . TYR B 2 37  ? -62.547 47.599  53.397  1.00 171.71 ?  369 TYR C CG  1 
ATOM   5184  C CD1 . TYR B 2 37  ? -62.097 48.886  53.098  1.00 165.36 ?  369 TYR C CD1 1 
ATOM   5185  C CD2 . TYR B 2 37  ? -62.931 47.330  54.708  1.00 177.19 ?  369 TYR C CD2 1 
ATOM   5186  C CE1 . TYR B 2 37  ? -61.991 49.865  54.087  1.00 168.14 ?  369 TYR C CE1 1 
ATOM   5187  C CE2 . TYR B 2 37  ? -62.839 48.304  55.700  1.00 174.23 ?  369 TYR C CE2 1 
ATOM   5188  C CZ  . TYR B 2 37  ? -62.370 49.566  55.382  1.00 174.13 ?  369 TYR C CZ  1 
ATOM   5189  O OH  . TYR B 2 37  ? -62.278 50.528  56.360  1.00 172.75 ?  369 TYR C OH  1 
ATOM   5190  N N   . ASN B 2 38  ? -60.246 44.452  53.613  1.00 186.83 ?  370 ASN C N   1 
ATOM   5191  C CA  . ASN B 2 38  ? -59.435 44.246  54.840  1.00 186.76 ?  370 ASN C CA  1 
ATOM   5192  C C   . ASN B 2 38  ? -58.025 43.810  54.445  1.00 187.92 ?  370 ASN C C   1 
ATOM   5193  O O   . ASN B 2 38  ? -57.206 43.582  55.355  1.00 182.83 ?  370 ASN C O   1 
ATOM   5194  C CB  . ASN B 2 38  ? -60.134 43.276  55.790  1.00 187.38 ?  370 ASN C CB  1 
ATOM   5195  C CG  . ASN B 2 38  ? -61.636 43.480  55.800  1.00 187.80 ?  370 ASN C CG  1 
ATOM   5196  O OD1 . ASN B 2 38  ? -62.311 43.194  54.813  1.00 188.90 ?  370 ASN C OD1 1 
ATOM   5197  N ND2 . ASN B 2 38  ? -62.163 43.995  56.899  1.00 185.50 ?  370 ASN C ND2 1 
ATOM   5198  N N   . PHE B 2 39  ? -57.761 43.697  53.142  1.00 199.14 ?  371 PHE C N   1 
ATOM   5199  C CA  . PHE B 2 39  ? -56.383 43.378  52.690  1.00 193.66 ?  371 PHE C CA  1 
ATOM   5200  C C   . PHE B 2 39  ? -55.469 44.464  53.240  1.00 191.99 ?  371 PHE C C   1 
ATOM   5201  O O   . PHE B 2 39  ? -54.431 44.146  53.832  1.00 194.26 ?  371 PHE C O   1 
ATOM   5202  C CB  . PHE B 2 39  ? -56.314 43.352  51.167  1.00 186.10 ?  371 PHE C CB  1 
ATOM   5203  C CG  . PHE B 2 39  ? -56.938 42.116  50.579  1.00 182.46 ?  371 PHE C CG  1 
ATOM   5204  C CD1 . PHE B 2 39  ? -57.971 41.471  51.235  1.00 185.52 ?  371 PHE C CD1 1 
ATOM   5205  C CD2 . PHE B 2 39  ? -56.477 41.587  49.388  1.00 179.78 ?  371 PHE C CD2 1 
ATOM   5206  C CE1 . PHE B 2 39  ? -58.542 40.328  50.706  1.00 184.46 ?  371 PHE C CE1 1 
ATOM   5207  C CE2 . PHE B 2 39  ? -57.049 40.441  48.860  1.00 173.49 ?  371 PHE C CE2 1 
ATOM   5208  C CZ  . PHE B 2 39  ? -58.082 39.816  49.520  1.00 181.22 ?  371 PHE C CZ  1 
ATOM   5209  N N   . ALA B 2 40  ? -55.845 45.715  53.004  1.00 203.23 ?  372 ALA C N   1 
ATOM   5210  C CA  . ALA B 2 40  ? -55.101 46.867  53.560  1.00 199.04 ?  372 ALA C CA  1 
ATOM   5211  C C   . ALA B 2 40  ? -53.582 46.804  53.363  1.00 191.76 ?  372 ALA C C   1 
ATOM   5212  O O   . ALA B 2 40  ? -52.869 47.232  54.296  1.00 192.13 ?  372 ALA C O   1 
ATOM   5213  C CB  . ALA B 2 40  ? -55.439 47.023  55.022  1.00 197.72 ?  372 ALA C CB  1 
ATOM   5214  N N   . PRO B 2 41  ? -53.017 46.316  52.236  1.00 159.13 ?  373 PRO C N   1 
ATOM   5215  C CA  . PRO B 2 41  ? -51.591 46.437  51.994  1.00 146.62 ?  373 PRO C CA  1 
ATOM   5216  C C   . PRO B 2 41  ? -51.677 47.684  51.115  1.00 136.24 ?  373 PRO C C   1 
ATOM   5217  O O   . PRO B 2 41  ? -50.788 47.889  50.310  1.00 126.22 ?  373 PRO C O   1 
ATOM   5218  C CB  . PRO B 2 41  ? -51.289 45.182  51.189  1.00 139.80 ?  373 PRO C CB  1 
ATOM   5219  C CG  . PRO B 2 41  ? -52.529 44.994  50.342  1.00 146.64 ?  373 PRO C CG  1 
ATOM   5220  C CD  . PRO B 2 41  ? -53.664 45.616  51.128  1.00 154.30 ?  373 PRO C CD  1 
ATOM   5221  N N   . PHE B 2 42  ? -52.726 48.496  51.305  1.00 134.52 ?  374 PHE C N   1 
ATOM   5222  C CA  . PHE B 2 42  ? -52.992 49.651  50.411  1.00 123.74 ?  374 PHE C CA  1 
ATOM   5223  C C   . PHE B 2 42  ? -52.429 50.961  50.951  1.00 123.13 ?  374 PHE C C   1 
ATOM   5224  O O   . PHE B 2 42  ? -52.842 51.387  52.039  1.00 121.30 ?  374 PHE C O   1 
ATOM   5225  C CB  . PHE B 2 42  ? -54.499 49.793  50.197  1.00 115.34 ?  374 PHE C CB  1 
ATOM   5226  C CG  . PHE B 2 42  ? -55.207 48.513  49.838  1.00 124.86 ?  374 PHE C CG  1 
ATOM   5227  C CD1 . PHE B 2 42  ? -54.791 47.750  48.760  1.00 114.66 ?  374 PHE C CD1 1 
ATOM   5228  C CD2 . PHE B 2 42  ? -56.294 48.074  50.576  1.00 131.82 ?  374 PHE C CD2 1 
ATOM   5229  C CE1 . PHE B 2 42  ? -55.447 46.576  48.428  1.00 120.94 ?  374 PHE C CE1 1 
ATOM   5230  C CE2 . PHE B 2 42  ? -56.950 46.900  50.245  1.00 145.13 ?  374 PHE C CE2 1 
ATOM   5231  C CZ  . PHE B 2 42  ? -56.525 46.154  49.171  1.00 137.91 ?  374 PHE C CZ  1 
ATOM   5232  N N   . PHE B 2 43  ? -51.511 51.565  50.203  1.00 141.77 ?  375 PHE C N   1 
ATOM   5233  C CA  . PHE B 2 43  ? -50.961 52.879  50.532  1.00 143.74 ?  375 PHE C CA  1 
ATOM   5234  C C   . PHE B 2 43  ? -51.858 54.018  50.032  1.00 143.55 ?  375 PHE C C   1 
ATOM   5235  O O   . PHE B 2 43  ? -51.394 55.174  49.986  1.00 135.21 ?  375 PHE C O   1 
ATOM   5236  C CB  . PHE B 2 43  ? -49.556 53.050  49.922  1.00 126.93 ?  375 PHE C CB  1 
ATOM   5237  C CG  . PHE B 2 43  ? -48.431 52.497  50.777  1.00 128.71 ?  375 PHE C CG  1 
ATOM   5238  C CD1 . PHE B 2 43  ? -48.660 51.428  51.650  1.00 130.69 ?  375 PHE C CD1 1 
ATOM   5239  C CD2 . PHE B 2 43  ? -47.158 53.072  50.736  1.00 124.24 ?  375 PHE C CD2 1 
ATOM   5240  C CE1 . PHE B 2 43  ? -47.631 50.914  52.433  1.00 134.49 ?  375 PHE C CE1 1 
ATOM   5241  C CE2 . PHE B 2 43  ? -46.114 52.576  51.527  1.00 123.06 ?  375 PHE C CE2 1 
ATOM   5242  C CZ  . PHE B 2 43  ? -46.355 51.490  52.381  1.00 134.01 ?  375 PHE C CZ  1 
ATOM   5243  N N   . THR B 2 44  ? -53.085 53.682  49.575  1.00 122.74 ?  376 THR C N   1 
ATOM   5244  C CA  . THR B 2 44  ? -54.220 54.609  49.429  1.00 120.57 ?  376 THR C CA  1 
ATOM   5245  C C   . THR B 2 44  ? -55.480 53.814  49.075  1.00 121.16 ?  376 THR C C   1 
ATOM   5246  O O   . THR B 2 44  ? -55.593 53.283  47.972  1.00 119.48 ?  376 THR C O   1 
ATOM   5247  C CB  . THR B 2 44  ? -53.957 55.699  48.362  1.00 117.61 ?  376 THR C CB  1 
ATOM   5248  O OG1 . THR B 2 44  ? -52.844 56.517  48.753  1.00 129.90 ?  376 THR C OG1 1 
ATOM   5249  C CG2 . THR B 2 44  ? -55.165 56.625  48.169  1.00 108.22 ?  376 THR C CG2 1 
ATOM   5250  N N   . PHE B 2 45  ? -56.433 53.701  49.991  1.00 103.64 ?  377 PHE C N   1 
ATOM   5251  C CA  . PHE B 2 45  ? -57.719 53.082  49.696  1.00 93.81  ?  377 PHE C CA  1 
ATOM   5252  C C   . PHE B 2 45  ? -58.782 54.155  49.888  1.00 93.37  ?  377 PHE C C   1 
ATOM   5253  O O   . PHE B 2 45  ? -59.460 54.198  50.912  1.00 92.58  ?  377 PHE C O   1 
ATOM   5254  C CB  . PHE B 2 45  ? -57.940 51.901  50.611  1.00 98.82  ?  377 PHE C CB  1 
ATOM   5255  C CG  . PHE B 2 45  ? -59.123 51.031  50.249  1.00 100.55 ?  377 PHE C CG  1 
ATOM   5256  C CD1 . PHE B 2 45  ? -60.196 51.521  49.537  1.00 94.02  ?  377 PHE C CD1 1 
ATOM   5257  C CD2 . PHE B 2 45  ? -59.165 49.707  50.656  1.00 111.88 ?  377 PHE C CD2 1 
ATOM   5258  C CE1 . PHE B 2 45  ? -61.272 50.703  49.220  1.00 96.25  ?  377 PHE C CE1 1 
ATOM   5259  C CE2 . PHE B 2 45  ? -60.255 48.891  50.331  1.00 120.34 ?  377 PHE C CE2 1 
ATOM   5260  C CZ  . PHE B 2 45  ? -61.311 49.397  49.611  1.00 104.42 ?  377 PHE C CZ  1 
ATOM   5261  N N   . LYS B 2 46  ? -58.937 55.024  48.895  1.00 83.95  ?  378 LYS C N   1 
ATOM   5262  C CA  . LYS B 2 46  ? -59.825 56.175  49.045  1.00 85.85  ?  378 LYS C CA  1 
ATOM   5263  C C   . LYS B 2 46  ? -61.080 55.989  48.210  1.00 83.91  ?  378 LYS C C   1 
ATOM   5264  O O   . LYS B 2 46  ? -61.018 55.936  46.973  1.00 84.25  ?  378 LYS C O   1 
ATOM   5265  C CB  . LYS B 2 46  ? -59.159 57.497  48.665  1.00 90.39  ?  378 LYS C CB  1 
ATOM   5266  C CG  . LYS B 2 46  ? -58.042 57.936  49.611  1.00 104.63 ?  378 LYS C CG  1 
ATOM   5267  C CD  . LYS B 2 46  ? -58.545 58.064  51.056  1.00 111.02 ?  378 LYS C CD  1 
ATOM   5268  C CE  . LYS B 2 46  ? -59.466 59.264  51.251  1.00 109.96 ?  378 LYS C CE  1 
ATOM   5269  N NZ  . LYS B 2 46  ? -59.152 60.062  52.458  1.00 102.72 ?  378 LYS C NZ  1 
ATOM   5270  N N   . CYS B 2 47  ? -62.217 55.914  48.887  1.00 96.41  ?  379 CYS C N   1 
ATOM   5271  C CA  . CYS B 2 47  ? -63.489 55.531  48.273  1.00 96.60  ?  379 CYS C CA  1 
ATOM   5272  C C   . CYS B 2 47  ? -64.424 56.720  48.041  1.00 103.52 ?  379 CYS C C   1 
ATOM   5273  O O   . CYS B 2 47  ? -65.239 57.043  48.912  1.00 119.70 ?  379 CYS C O   1 
ATOM   5274  C CB  . CYS B 2 47  ? -64.157 54.462  49.132  1.00 85.89  ?  379 CYS C CB  1 
ATOM   5275  S SG  . CYS B 2 47  ? -64.688 53.087  48.135  1.00 101.13 ?  379 CYS C SG  1 
ATOM   5276  N N   . TYR B 2 48  ? -64.331 57.344  46.862  1.00 91.76  ?  380 TYR C N   1 
ATOM   5277  C CA  . TYR B 2 48  ? -65.250 58.381  46.407  1.00 105.06 ?  380 TYR C CA  1 
ATOM   5278  C C   . TYR B 2 48  ? -66.520 57.685  45.923  1.00 119.07 ?  380 TYR C C   1 
ATOM   5279  O O   . TYR B 2 48  ? -66.448 56.603  45.334  1.00 110.91 ?  380 TYR C O   1 
ATOM   5280  C CB  . TYR B 2 48  ? -64.645 59.083  45.200  1.00 94.29  ?  380 TYR C CB  1 
ATOM   5281  C CG  . TYR B 2 48  ? -63.187 59.448  45.283  1.00 85.41  ?  380 TYR C CG  1 
ATOM   5282  C CD1 . TYR B 2 48  ? -62.698 60.515  46.020  1.00 88.58  ?  380 TYR C CD1 1 
ATOM   5283  C CD2 . TYR B 2 48  ? -62.261 58.613  44.691  1.00 86.46  ?  380 TYR C CD2 1 
ATOM   5284  C CE1 . TYR B 2 48  ? -61.299 60.775  46.081  1.00 80.77  ?  380 TYR C CE1 1 
ATOM   5285  C CE2 . TYR B 2 48  ? -60.902 58.846  44.748  1.00 88.03  ?  380 TYR C CE2 1 
ATOM   5286  C CZ  . TYR B 2 48  ? -60.420 59.923  45.440  1.00 79.88  ?  380 TYR C CZ  1 
ATOM   5287  O OH  . TYR B 2 48  ? -59.054 60.084  45.446  1.00 77.17  ?  380 TYR C OH  1 
ATOM   5288  N N   . GLY B 2 49  ? -67.687 58.299  46.092  1.00 135.38 ?  381 GLY C N   1 
ATOM   5289  C CA  . GLY B 2 49  ? -68.958 57.753  45.591  1.00 135.76 ?  381 GLY C CA  1 
ATOM   5290  C C   . GLY B 2 49  ? -69.716 56.621  46.360  1.00 149.16 ?  381 GLY C C   1 
ATOM   5291  O O   . GLY B 2 49  ? -70.918 56.697  46.504  1.00 147.27 ?  381 GLY C O   1 
ATOM   5292  N N   . VAL B 2 50  ? -68.985 55.729  47.026  1.00 132.61 ?  382 VAL C N   1 
ATOM   5293  C CA  . VAL B 2 50  ? -69.642 54.605  47.762  1.00 132.20 ?  382 VAL C CA  1 
ATOM   5294  C C   . VAL B 2 50  ? -68.935 54.364  49.103  1.00 134.61 ?  382 VAL C C   1 
ATOM   5295  O O   . VAL B 2 50  ? -67.897 55.002  49.331  1.00 140.70 ?  382 VAL C O   1 
ATOM   5296  C CB  . VAL B 2 50  ? -69.620 53.328  46.905  1.00 121.19 ?  382 VAL C CB  1 
ATOM   5297  C CG1 . VAL B 2 50  ? -68.241 52.685  46.857  1.00 120.13 ?  382 VAL C CG1 1 
ATOM   5298  C CG2 . VAL B 2 50  ? -70.674 52.318  47.339  1.00 127.20 ?  382 VAL C CG2 1 
ATOM   5299  N N   . SER B 2 51  ? -69.478 53.475  49.943  1.00 148.83 ?  383 SER C N   1 
ATOM   5300  C CA  . SER B 2 51  ? -68.840 53.126  51.241  1.00 152.06 ?  383 SER C CA  1 
ATOM   5301  C C   . SER B 2 51  ? -68.515 51.639  51.245  1.00 149.77 ?  383 SER C C   1 
ATOM   5302  O O   . SER B 2 51  ? -69.364 50.857  50.797  1.00 152.12 ?  383 SER C O   1 
ATOM   5303  C CB  . SER B 2 51  ? -69.733 53.490  52.386  1.00 151.94 ?  383 SER C CB  1 
ATOM   5304  O OG  . SER B 2 51  ? -69.725 52.456  53.359  1.00 149.61 ?  383 SER C OG  1 
ATOM   5305  N N   . PRO B 2 52  ? -67.361 51.198  51.794  1.00 132.43 ?  384 PRO C N   1 
ATOM   5306  C CA  . PRO B 2 52  ? -66.940 49.787  51.704  1.00 134.87 ?  384 PRO C CA  1 
ATOM   5307  C C   . PRO B 2 52  ? -68.010 48.801  52.198  1.00 137.21 ?  384 PRO C C   1 
ATOM   5308  O O   . PRO B 2 52  ? -68.250 47.817  51.527  1.00 139.42 ?  384 PRO C O   1 
ATOM   5309  C CB  . PRO B 2 52  ? -65.674 49.733  52.570  1.00 137.70 ?  384 PRO C CB  1 
ATOM   5310  C CG  . PRO B 2 52  ? -65.767 50.960  53.459  1.00 135.87 ?  384 PRO C CG  1 
ATOM   5311  C CD  . PRO B 2 52  ? -66.432 52.002  52.590  1.00 135.16 ?  384 PRO C CD  1 
ATOM   5312  N N   . THR B 2 53  ? -68.617 49.074  53.359  1.00 144.51 ?  385 THR C N   1 
ATOM   5313  C CA  . THR B 2 53  ? -69.682 48.181  53.871  1.00 141.81 ?  385 THR C CA  1 
ATOM   5314  C C   . THR B 2 53  ? -70.901 48.312  52.976  1.00 149.81 ?  385 THR C C   1 
ATOM   5315  O O   . THR B 2 53  ? -71.476 47.280  52.604  1.00 151.94 ?  385 THR C O   1 
ATOM   5316  C CB  . THR B 2 53  ? -70.172 48.590  55.262  1.00 131.16 ?  385 THR C CB  1 
ATOM   5317  O OG1 . THR B 2 53  ? -70.596 49.953  55.228  1.00 134.43 ?  385 THR C OG1 1 
ATOM   5318  C CG2 . THR B 2 53  ? -69.113 48.390  56.320  1.00 126.31 ?  385 THR C CG2 1 
ATOM   5319  N N   . LYS B 2 54  ? -71.273 49.549  52.666  1.00 172.12 ?  386 LYS C N   1 
ATOM   5320  C CA  . LYS B 2 54  ? -72.473 49.831  51.838  1.00 168.56 ?  386 LYS C CA  1 
ATOM   5321  C C   . LYS B 2 54  ? -72.311 49.305  50.423  1.00 173.26 ?  386 LYS C C   1 
ATOM   5322  O O   . LYS B 2 54  ? -73.325 49.015  49.774  1.00 172.51 ?  386 LYS C O   1 
ATOM   5323  C CB  . LYS B 2 54  ? -72.601 51.347  51.762  1.00 161.62 ?  386 LYS C CB  1 
ATOM   5324  C CG  . LYS B 2 54  ? -72.971 52.014  53.081  1.00 162.61 ?  386 LYS C CG  1 
ATOM   5325  C CD  . LYS B 2 54  ? -74.392 51.707  53.471  1.00 172.88 ?  386 LYS C CD  1 
ATOM   5326  C CE  . LYS B 2 54  ? -74.647 51.879  54.948  1.00 173.67 ?  386 LYS C CE  1 
ATOM   5327  N NZ  . LYS B 2 54  ? -74.523 50.595  55.672  1.00 173.23 ?  386 LYS C NZ  1 
ATOM   5328  N N   . LEU B 2 55  ? -71.078 49.260  49.941  1.00 165.06 ?  387 LEU C N   1 
ATOM   5329  C CA  . LEU B 2 55  ? -70.834 48.821  48.555  1.00 157.64 ?  387 LEU C CA  1 
ATOM   5330  C C   . LEU B 2 55  ? -71.423 47.426  48.436  1.00 158.59 ?  387 LEU C C   1 
ATOM   5331  O O   . LEU B 2 55  ? -71.740 46.991  47.321  1.00 160.36 ?  387 LEU C O   1 
ATOM   5332  C CB  . LEU B 2 55  ? -69.315 48.799  48.396  1.00 157.03 ?  387 LEU C CB  1 
ATOM   5333  C CG  . LEU B 2 55  ? -68.804 48.181  47.113  1.00 154.01 ?  387 LEU C CG  1 
ATOM   5334  C CD1 . LEU B 2 55  ? -69.681 48.597  45.955  1.00 150.07 ?  387 LEU C CD1 1 
ATOM   5335  C CD2 . LEU B 2 55  ? -67.360 48.613  46.917  1.00 144.81 ?  387 LEU C CD2 1 
ATOM   5336  N N   . ASN B 2 56  ? -71.515 46.747  49.584  1.00 148.21 ?  388 ASN C N   1 
ATOM   5337  C CA  . ASN B 2 56  ? -71.951 45.329  49.602  1.00 145.15 ?  388 ASN C CA  1 
ATOM   5338  C C   . ASN B 2 56  ? -73.451 45.233  49.827  1.00 141.38 ?  388 ASN C C   1 
ATOM   5339  O O   . ASN B 2 56  ? -74.002 44.142  49.697  1.00 137.28 ?  388 ASN C O   1 
ATOM   5340  C CB  . ASN B 2 56  ? -71.286 44.558  50.738  1.00 145.12 ?  388 ASN C CB  1 
ATOM   5341  C CG  . ASN B 2 56  ? -69.791 44.393  50.578  1.00 151.56 ?  388 ASN C CG  1 
ATOM   5342  O OD1 . ASN B 2 56  ? -69.333 43.492  49.880  1.00 153.93 ?  388 ASN C OD1 1 
ATOM   5343  N ND2 . ASN B 2 56  ? -69.023 45.239  51.244  1.00 154.25 ?  388 ASN C ND2 1 
ATOM   5344  N N   . ASP B 2 57  ? -74.076 46.331  50.204  1.00 140.96 ?  389 ASP C N   1 
ATOM   5345  C CA  . ASP B 2 57  ? -75.546 46.282  50.340  1.00 134.25 ?  389 ASP C CA  1 
ATOM   5346  C C   . ASP B 2 57  ? -76.084 47.092  49.176  1.00 131.69 ?  389 ASP C C   1 
ATOM   5347  O O   . ASP B 2 57  ? -77.013 47.889  49.407  1.00 130.28 ?  389 ASP C O   1 
ATOM   5348  C CB  . ASP B 2 57  ? -75.961 46.769  51.728  1.00 136.18 ?  389 ASP C CB  1 
ATOM   5349  C CG  . ASP B 2 57  ? -74.809 46.722  52.718  1.00 140.07 ?  389 ASP C CG  1 
ATOM   5350  O OD1 . ASP B 2 57  ? -74.323 45.607  53.001  1.00 141.86 -1 389 ASP C OD1 1 
ATOM   5351  O OD2 . ASP B 2 57  ? -74.400 47.799  53.194  1.00 137.19 ?  389 ASP C OD2 1 
ATOM   5352  N N   . LEU B 2 58  ? -75.517 46.871  47.988  1.00 136.16 ?  390 LEU C N   1 
ATOM   5353  C CA  . LEU B 2 58  ? -75.908 47.688  46.815  1.00 138.94 ?  390 LEU C CA  1 
ATOM   5354  C C   . LEU B 2 58  ? -75.498 47.000  45.515  1.00 140.59 ?  390 LEU C C   1 
ATOM   5355  O O   . LEU B 2 58  ? -74.300 46.709  45.370  1.00 140.51 ?  390 LEU C O   1 
ATOM   5356  C CB  . LEU B 2 58  ? -75.172 49.024  46.938  1.00 135.86 ?  390 LEU C CB  1 
ATOM   5357  C CG  . LEU B 2 58  ? -75.559 50.092  45.919  1.00 134.49 ?  390 LEU C CG  1 
ATOM   5358  C CD1 . LEU B 2 58  ? -77.021 49.947  45.520  1.00 128.60 ?  390 LEU C CD1 1 
ATOM   5359  C CD2 . LEU B 2 58  ? -75.293 51.473  46.485  1.00 124.71 ?  390 LEU C CD2 1 
ATOM   5360  N N   . CYS B 2 59  ? -76.444 46.739  44.608  1.00 151.03 ?  391 CYS C N   1 
ATOM   5361  C CA  . CYS B 2 59  ? -76.074 46.236  43.295  1.00 153.06 ?  391 CYS C CA  1 
ATOM   5362  C C   . CYS B 2 59  ? -75.926 47.375  42.301  1.00 148.63 ?  391 CYS C C   1 
ATOM   5363  O O   . CYS B 2 59  ? -76.501 48.455  42.470  1.00 148.90 ?  391 CYS C O   1 
ATOM   5364  C CB  . CYS B 2 59  ? -77.108 45.236  42.785  1.00 156.07 ?  391 CYS C CB  1 
ATOM   5365  S SG  . CYS B 2 59  ? -77.543 43.976  43.970  1.00 178.49 ?  391 CYS C SG  1 
ATOM   5366  N N   . PHE B 2 60  ? -75.162 47.117  41.246  1.00 132.37 ?  392 PHE C N   1 
ATOM   5367  C CA  . PHE B 2 60  ? -74.907 48.102  40.214  1.00 131.88 ?  392 PHE C CA  1 
ATOM   5368  C C   . PHE B 2 60  ? -75.079 47.474  38.846  1.00 133.06 ?  392 PHE C C   1 
ATOM   5369  O O   . PHE B 2 60  ? -75.188 46.254  38.708  1.00 132.51 ?  392 PHE C O   1 
ATOM   5370  C CB  . PHE B 2 60  ? -73.506 48.681  40.357  1.00 130.19 ?  392 PHE C CB  1 
ATOM   5371  C CG  . PHE B 2 60  ? -73.349 49.541  41.551  1.00 125.77 ?  392 PHE C CG  1 
ATOM   5372  C CD1 . PHE B 2 60  ? -73.867 50.824  41.557  1.00 125.35 ?  392 PHE C CD1 1 
ATOM   5373  C CD2 . PHE B 2 60  ? -72.737 49.053  42.691  1.00 121.40 ?  392 PHE C CD2 1 
ATOM   5374  C CE1 . PHE B 2 60  ? -73.743 51.633  42.655  1.00 121.64 ?  392 PHE C CE1 1 
ATOM   5375  C CE2 . PHE B 2 60  ? -72.611 49.849  43.800  1.00 121.72 ?  392 PHE C CE2 1 
ATOM   5376  C CZ  . PHE B 2 60  ? -73.115 51.149  43.782  1.00 119.30 ?  392 PHE C CZ  1 
ATOM   5377  N N   . THR B 2 61  ? -75.070 48.329  37.823  1.00 134.58 ?  393 THR C N   1 
ATOM   5378  C CA  . THR B 2 61  ? -75.394 47.899  36.469  1.00 137.79 ?  393 THR C CA  1 
ATOM   5379  C C   . THR B 2 61  ? -74.179 47.428  35.664  1.00 133.92 ?  393 THR C C   1 
ATOM   5380  O O   . THR B 2 61  ? -74.278 46.427  34.944  1.00 132.24 ?  393 THR C O   1 
ATOM   5381  C CB  . THR B 2 61  ? -76.134 49.023  35.744  1.00 146.36 ?  393 THR C CB  1 
ATOM   5382  O OG1 . THR B 2 61  ? -76.483 48.620  34.421  1.00 149.27 ?  393 THR C OG1 1 
ATOM   5383  C CG2 . THR B 2 61  ? -75.294 50.208  35.661  1.00 146.00 ?  393 THR C CG2 1 
ATOM   5384  N N   . ASN B 2 62  ? -73.033 48.105  35.763  1.00 133.77 ?  394 ASN C N   1 
ATOM   5385  C CA  . ASN B 2 62  ? -71.809 47.601  35.144  1.00 128.79 ?  394 ASN C CA  1 
ATOM   5386  C C   . ASN B 2 62  ? -70.645 48.144  35.961  1.00 120.51 ?  394 ASN C C   1 
ATOM   5387  O O   . ASN B 2 62  ? -70.416 49.357  35.977  1.00 118.51 ?  394 ASN C O   1 
ATOM   5388  C CB  . ASN B 2 62  ? -71.687 48.021  33.664  1.00 127.47 ?  394 ASN C CB  1 
ATOM   5389  C CG  . ASN B 2 62  ? -71.818 46.831  32.672  1.00 124.55 ?  394 ASN C CG  1 
ATOM   5390  O OD1 . ASN B 2 62  ? -72.169 45.705  33.052  1.00 126.20 ?  394 ASN C OD1 1 
ATOM   5391  N ND2 . ASN B 2 62  ? -71.502 47.090  31.401  1.00 114.13 ?  394 ASN C ND2 1 
ATOM   5392  N N   . VAL B 2 63  ? -69.922 47.275  36.655  1.00 108.84 ?  395 VAL C N   1 
ATOM   5393  C CA  . VAL B 2 63  ? -68.715 47.721  37.321  1.00 101.89 ?  395 VAL C CA  1 
ATOM   5394  C C   . VAL B 2 63  ? -67.546 47.679  36.355  1.00 98.85  ?  395 VAL C C   1 
ATOM   5395  O O   . VAL B 2 63  ? -67.446 46.779  35.515  1.00 99.03  ?  395 VAL C O   1 
ATOM   5396  C CB  . VAL B 2 63  ? -68.457 46.851  38.544  1.00 97.81  ?  395 VAL C CB  1 
ATOM   5397  C CG1 . VAL B 2 63  ? -67.316 47.426  39.292  1.00 96.29  ?  395 VAL C CG1 1 
ATOM   5398  C CG2 . VAL B 2 63  ? -69.676 46.864  39.374  1.00 98.33  ?  395 VAL C CG2 1 
ATOM   5399  N N   . TYR B 2 64  ? -66.642 48.635  36.489  1.00 91.69  ?  396 TYR C N   1 
ATOM   5400  C CA  . TYR B 2 64  ? -65.477 48.747  35.621  1.00 80.91  ?  396 TYR C CA  1 
ATOM   5401  C C   . TYR B 2 64  ? -64.214 48.751  36.479  1.00 78.12  ?  396 TYR C C   1 
ATOM   5402  O O   . TYR B 2 64  ? -63.972 49.703  37.230  1.00 77.01  ?  396 TYR C O   1 
ATOM   5403  C CB  . TYR B 2 64  ? -65.595 50.013  34.776  1.00 82.49  ?  396 TYR C CB  1 
ATOM   5404  C CG  . TYR B 2 64  ? -66.486 49.866  33.566  1.00 85.66  ?  396 TYR C CG  1 
ATOM   5405  C CD1 . TYR B 2 64  ? -66.410 48.731  32.765  1.00 84.85  ?  396 TYR C CD1 1 
ATOM   5406  C CD2 . TYR B 2 64  ? -67.431 50.836  33.244  1.00 85.45  ?  396 TYR C CD2 1 
ATOM   5407  C CE1 . TYR B 2 64  ? -67.229 48.580  31.642  1.00 89.38  ?  396 TYR C CE1 1 
ATOM   5408  C CE2 . TYR B 2 64  ? -68.252 50.694  32.123  1.00 92.63  ?  396 TYR C CE2 1 
ATOM   5409  C CZ  . TYR B 2 64  ? -68.146 49.560  31.326  1.00 92.54  ?  396 TYR C CZ  1 
ATOM   5410  O OH  . TYR B 2 64  ? -68.946 49.396  30.215  1.00 95.99  ?  396 TYR C OH  1 
ATOM   5411  N N   . ALA B 2 65  ? -63.409 47.697  36.396  1.00 82.14  ?  397 ALA C N   1 
ATOM   5412  C CA  . ALA B 2 65  ? -62.157 47.662  37.139  1.00 71.55  ?  397 ALA C CA  1 
ATOM   5413  C C   . ALA B 2 65  ? -61.036 48.022  36.161  1.00 70.46  ?  397 ALA C C   1 
ATOM   5414  O O   . ALA B 2 65  ? -60.635 47.207  35.326  1.00 72.79  ?  397 ALA C O   1 
ATOM   5415  C CB  . ALA B 2 65  ? -61.976 46.307  37.807  1.00 72.95  ?  397 ALA C CB  1 
ATOM   5416  N N   . ASP B 2 66  ? -60.588 49.279  36.221  1.00 61.99  ?  398 ASP C N   1 
ATOM   5417  C CA  . ASP B 2 66  ? -59.432 49.766  35.474  1.00 61.57  ?  398 ASP C CA  1 
ATOM   5418  C C   . ASP B 2 66  ? -58.182 49.614  36.322  1.00 62.57  ?  398 ASP C C   1 
ATOM   5419  O O   . ASP B 2 66  ? -58.158 50.051  37.472  1.00 60.01  ?  398 ASP C O   1 
ATOM   5420  C CB  . ASP B 2 66  ? -59.567 51.252  35.135  1.00 62.30  ?  398 ASP C CB  1 
ATOM   5421  C CG  . ASP B 2 66  ? -60.905 51.623  34.576  1.00 63.03  ?  398 ASP C CG  1 
ATOM   5422  O OD1 . ASP B 2 66  ? -61.485 50.853  33.813  1.00 68.64  ?  398 ASP C OD1 1 
ATOM   5423  O OD2 . ASP B 2 66  ? -61.421 52.682  34.961  1.00 58.24  -1 398 ASP C OD2 1 
ATOM   5424  N N   . SER B 2 67  ? -57.122 49.062  35.746  1.00 69.39  ?  399 SER C N   1 
ATOM   5425  C CA  . SER B 2 67  ? -55.852 48.949  36.460  1.00 62.97  ?  399 SER C CA  1 
ATOM   5426  C C   . SER B 2 67  ? -54.703 49.467  35.596  1.00 61.64  ?  399 SER C C   1 
ATOM   5427  O O   . SER B 2 67  ? -54.739 49.363  34.361  1.00 65.45  ?  399 SER C O   1 
ATOM   5428  C CB  . SER B 2 67  ? -55.550 47.513  36.860  1.00 67.59  ?  399 SER C CB  1 
ATOM   5429  O OG  . SER B 2 67  ? -55.666 46.606  35.774  1.00 65.12  ?  399 SER C OG  1 
ATOM   5430  N N   . PHE B 2 68  ? -53.682 50.016  36.267  1.00 55.83  ?  400 PHE C N   1 
ATOM   5431  C CA  . PHE B 2 68  ? -52.462 50.514  35.608  1.00 54.44  ?  400 PHE C CA  1 
ATOM   5432  C C   . PHE B 2 68  ? -51.414 50.764  36.688  1.00 52.88  ?  400 PHE C C   1 
ATOM   5433  O O   . PHE B 2 68  ? -51.594 50.352  37.842  1.00 55.00  ?  400 PHE C O   1 
ATOM   5434  C CB  . PHE B 2 68  ? -52.790 51.744  34.770  1.00 52.06  ?  400 PHE C CB  1 
ATOM   5435  C CG  . PHE B 2 68  ? -53.467 52.845  35.535  1.00 54.34  ?  400 PHE C CG  1 
ATOM   5436  C CD1 . PHE B 2 68  ? -54.848 52.795  35.766  1.00 54.78  ?  400 PHE C CD1 1 
ATOM   5437  C CD2 . PHE B 2 68  ? -52.726 53.837  36.163  1.00 54.74  ?  400 PHE C CD2 1 
ATOM   5438  C CE1 . PHE B 2 68  ? -55.485 53.780  36.518  1.00 53.49  ?  400 PHE C CE1 1 
ATOM   5439  C CE2 . PHE B 2 68  ? -53.378 54.857  36.893  1.00 54.65  ?  400 PHE C CE2 1 
ATOM   5440  C CZ  . PHE B 2 68  ? -54.743 54.810  37.092  1.00 51.41  ?  400 PHE C CZ  1 
ATOM   5441  N N   . VAL B 2 69  ? -50.303 51.380  36.299  1.00 52.74  ?  401 VAL C N   1 
ATOM   5442  C CA  . VAL B 2 69  ? -49.202 51.608  37.274  1.00 53.38  ?  401 VAL C CA  1 
ATOM   5443  C C   . VAL B 2 69  ? -48.774 53.069  37.207  1.00 54.28  ?  401 VAL C C   1 
ATOM   5444  O O   . VAL B 2 69  ? -48.826 53.658  36.110  1.00 54.42  ?  401 VAL C O   1 
ATOM   5445  C CB  . VAL B 2 69  ? -47.999 50.694  37.024  1.00 48.40  ?  401 VAL C CB  1 
ATOM   5446  C CG1 . VAL B 2 69  ? -46.874 51.484  36.362  1.00 51.46  ?  401 VAL C CG1 1 
ATOM   5447  C CG2 . VAL B 2 69  ? -47.515 50.088  38.331  1.00 49.46  ?  401 VAL C CG2 1 
ATOM   5448  N N   . ILE B 2 70  ? -48.340 53.610  38.330  1.00 51.62  ?  402 ILE C N   1 
ATOM   5449  C CA  . ILE B 2 70  ? -47.902 55.025  38.401  1.00 51.96  ?  402 ILE C CA  1 
ATOM   5450  C C   . ILE B 2 70  ? -46.975 55.113  39.611  1.00 57.10  ?  402 ILE C C   1 
ATOM   5451  O O   . ILE B 2 70  ? -46.868 54.093  40.350  1.00 61.33  ?  402 ILE C O   1 
ATOM   5452  C CB  . ILE B 2 70  ? -49.113 55.967  38.513  1.00 50.38  ?  402 ILE C CB  1 
ATOM   5453  C CG1 . ILE B 2 70  ? -50.336 55.247  39.076  1.00 51.17  ?  402 ILE C CG1 1 
ATOM   5454  C CG2 . ILE B 2 70  ? -49.433 56.635  37.186  1.00 50.28  ?  402 ILE C CG2 1 
ATOM   5455  C CD1 . ILE B 2 70  ? -51.159 56.101  39.998  1.00 50.00  ?  402 ILE C CD1 1 
ATOM   5456  N N   . ARG B 2 71  ? -46.326 56.271  39.790  1.00 53.76  ?  403 ARG C N   1 
ATOM   5457  C CA  . ARG B 2 71  ? -45.380 56.464  40.916  1.00 51.75  ?  403 ARG C CA  1 
ATOM   5458  C C   . ARG B 2 71  ? -46.096 57.213  42.035  1.00 54.53  ?  403 ARG C C   1 
ATOM   5459  O O   . ARG B 2 71  ? -47.235 57.654  41.838  1.00 60.00  ?  403 ARG C O   1 
ATOM   5460  C CB  . ARG B 2 71  ? -44.120 57.207  40.465  1.00 47.98  ?  403 ARG C CB  1 
ATOM   5461  C CG  . ARG B 2 71  ? -44.229 57.921  39.127  1.00 52.43  ?  403 ARG C CG  1 
ATOM   5462  C CD  . ARG B 2 71  ? -43.074 58.893  38.971  1.00 58.51  ?  403 ARG C CD  1 
ATOM   5463  N NE  . ARG B 2 71  ? -43.239 60.105  39.758  1.00 67.93  ?  403 ARG C NE  1 
ATOM   5464  C CZ  . ARG B 2 71  ? -42.872 61.314  39.349  1.00 73.13  ?  403 ARG C CZ  1 
ATOM   5465  N NH1 . ARG B 2 71  ? -42.309 61.471  38.163  1.00 68.42  ?  403 ARG C NH1 1 
ATOM   5466  N NH2 . ARG B 2 71  ? -43.065 62.366  40.122  1.00 69.81  ?  403 ARG C NH2 1 
ATOM   5467  N N   . GLY B 2 72  ? -45.425 57.376  43.168  1.00 56.03  ?  404 GLY C N   1 
ATOM   5468  C CA  . GLY B 2 72  ? -46.054 58.139  44.237  1.00 63.82  ?  404 GLY C CA  1 
ATOM   5469  C C   . GLY B 2 72  ? -46.735 59.457  43.893  1.00 64.45  ?  404 GLY C C   1 
ATOM   5470  O O   . GLY B 2 72  ? -47.936 59.617  44.139  1.00 60.88  ?  404 GLY C O   1 
ATOM   5471  N N   . ASN B 2 73  ? -45.978 60.410  43.336  1.00 69.71  ?  405 ASN C N   1 
ATOM   5472  C CA  . ASN B 2 73  ? -46.518 61.739  43.056  1.00 72.22  ?  405 ASN C CA  1 
ATOM   5473  C C   . ASN B 2 73  ? -47.769 61.671  42.168  1.00 73.72  ?  405 ASN C C   1 
ATOM   5474  O O   . ASN B 2 73  ? -48.639 62.543  42.249  1.00 76.97  ?  405 ASN C O   1 
ATOM   5475  C CB  . ASN B 2 73  ? -45.482 62.600  42.321  1.00 78.37  ?  405 ASN C CB  1 
ATOM   5476  C CG  . ASN B 2 73  ? -44.083 62.466  42.873  1.00 79.61  ?  405 ASN C CG  1 
ATOM   5477  O OD1 . ASN B 2 73  ? -43.474 61.414  42.728  1.00 74.72  ?  405 ASN C OD1 1 
ATOM   5478  N ND2 . ASN B 2 73  ? -43.559 63.527  43.501  1.00 91.08  ?  405 ASN C ND2 1 
ATOM   5479  N N   . GLU B 2 74  ? -47.820 60.683  41.257  1.00 63.26  ?  406 GLU C N   1 
ATOM   5480  C CA  . GLU B 2 74  ? -48.973 60.422  40.398  1.00 61.12  ?  406 GLU C CA  1 
ATOM   5481  C C   . GLU B 2 74  ? -50.245 60.030  41.165  1.00 60.21  ?  406 GLU C C   1 
ATOM   5482  O O   . GLU B 2 74  ? -51.326 60.498  40.799  1.00 62.10  ?  406 GLU C O   1 
ATOM   5483  C CB  . GLU B 2 74  ? -48.588 59.343  39.376  1.00 63.22  ?  406 GLU C CB  1 
ATOM   5484  C CG  . GLU B 2 74  ? -47.970 59.702  37.970  1.00 58.31  ?  406 GLU C CG  1 
ATOM   5485  C CD  . GLU B 2 74  ? -46.784 60.545  37.947  1.00 62.94  ?  406 GLU C CD  1 
ATOM   5486  O OE1 . GLU B 2 74  ? -45.975 60.355  38.829  1.00 92.33  ?  406 GLU C OE1 1 
ATOM   5487  O OE2 . GLU B 2 74  ? -46.563 61.166  36.895  1.00 69.12  -1 406 GLU C OE2 1 
ATOM   5488  N N   . VAL B 2 75  ? -50.165 59.137  42.144  1.00 59.00  ?  407 VAL C N   1 
ATOM   5489  C CA  . VAL B 2 75  ? -51.414 58.631  42.793  1.00 57.12  ?  407 VAL C CA  1 
ATOM   5490  C C   . VAL B 2 75  ? -52.336 59.793  43.159  1.00 59.53  ?  407 VAL C C   1 
ATOM   5491  O O   . VAL B 2 75  ? -53.555 59.625  43.048  1.00 59.18  ?  407 VAL C O   1 
ATOM   5492  C CB  . VAL B 2 75  ? -51.090 57.752  44.014  1.00 56.31  ?  407 VAL C CB  1 
ATOM   5493  C CG1 . VAL B 2 75  ? -52.325 57.464  44.850  1.00 60.87  ?  407 VAL C CG1 1 
ATOM   5494  C CG2 . VAL B 2 75  ? -50.414 56.455  43.600  1.00 52.92  ?  407 VAL C CG2 1 
ATOM   5495  N N   . SER B 2 76  ? -51.776 60.935  43.547  1.00 59.58  ?  408 SER C N   1 
ATOM   5496  C CA  . SER B 2 76  ? -52.602 62.077  44.018  1.00 56.80  ?  408 SER C CA  1 
ATOM   5497  C C   . SER B 2 76  ? -53.528 62.573  42.914  1.00 56.10  ?  408 SER C C   1 
ATOM   5498  O O   . SER B 2 76  ? -54.389 63.410  43.207  1.00 54.79  ?  408 SER C O   1 
ATOM   5499  C CB  . SER B 2 76  ? -51.723 63.188  44.504  1.00 64.63  ?  408 SER C CB  1 
ATOM   5500  O OG  . SER B 2 76  ? -50.475 62.687  44.960  1.00 66.91  ?  408 SER C OG  1 
ATOM   5501  N N   . GLN B 2 77  ? -53.336 62.088  41.693  1.00 58.16  ?  409 GLN C N   1 
ATOM   5502  C CA  . GLN B 2 77  ? -54.150 62.568  40.555  1.00 56.02  ?  409 GLN C CA  1 
ATOM   5503  C C   . GLN B 2 77  ? -55.185 61.511  40.206  1.00 57.02  ?  409 GLN C C   1 
ATOM   5504  O O   . GLN B 2 77  ? -55.999 61.770  39.316  1.00 58.87  ?  409 GLN C O   1 
ATOM   5505  C CB  . GLN B 2 77  ? -53.279 62.797  39.325  1.00 57.64  ?  409 GLN C CB  1 
ATOM   5506  C CG  . GLN B 2 77  ? -52.168 63.809  39.528  1.00 64.05  ?  409 GLN C CG  1 
ATOM   5507  C CD  . GLN B 2 77  ? -51.119 63.662  38.456  1.00 65.59  ?  409 GLN C CD  1 
ATOM   5508  O OE1 . GLN B 2 77  ? -51.427 63.521  37.276  1.00 67.06  ?  409 GLN C OE1 1 
ATOM   5509  N NE2 . GLN B 2 77  ? -49.863 63.695  38.865  1.00 70.53  ?  409 GLN C NE2 1 
ATOM   5510  N N   . ILE B 2 78  ? -55.146 60.350  40.857  1.00 54.98  ?  410 ILE C N   1 
ATOM   5511  C CA  . ILE B 2 78  ? -56.130 59.377  40.427  1.00 50.82  ?  410 ILE C CA  1 
ATOM   5512  C C   . ILE B 2 78  ? -57.315 59.666  41.337  1.00 54.39  ?  410 ILE C C   1 
ATOM   5513  O O   . ILE B 2 78  ? -57.580 58.950  42.307  1.00 59.88  ?  410 ILE C O   1 
ATOM   5514  C CB  . ILE B 2 78  ? -55.591 57.941  40.544  1.00 51.32  ?  410 ILE C CB  1 
ATOM   5515  C CG1 . ILE B 2 78  ? -54.354 57.736  39.676  1.00 53.73  ?  410 ILE C CG1 1 
ATOM   5516  C CG2 . ILE B 2 78  ? -56.592 56.970  40.027  1.00 52.74  ?  410 ILE C CG2 1 
ATOM   5517  C CD1 . ILE B 2 78  ? -54.486 58.170  38.241  1.00 52.00  ?  410 ILE C CD1 1 
ATOM   5518  N N   . ALA B 2 79  ? -57.993 60.772  41.066  1.00 54.64  ?  411 ALA C N   1 
ATOM   5519  C CA  . ALA B 2 79  ? -58.932 61.380  41.995  1.00 57.55  ?  411 ALA C CA  1 
ATOM   5520  C C   . ALA B 2 79  ? -59.754 62.421  41.251  1.00 61.73  ?  411 ALA C C   1 
ATOM   5521  O O   . ALA B 2 79  ? -59.260 63.045  40.304  1.00 64.26  ?  411 ALA C O   1 
ATOM   5522  C CB  . ALA B 2 79  ? -58.197 62.030  43.171  1.00 61.97  ?  411 ALA C CB  1 
ATOM   5523  N N   . PRO B 2 80  ? -60.994 62.651  41.661  1.00 67.77  ?  412 PRO C N   1 
ATOM   5524  C CA  . PRO B 2 80  ? -61.850 63.538  40.881  1.00 68.63  ?  412 PRO C CA  1 
ATOM   5525  C C   . PRO B 2 80  ? -61.376 64.972  40.984  1.00 72.17  ?  412 PRO C C   1 
ATOM   5526  O O   . PRO B 2 80  ? -61.086 65.467  42.071  1.00 68.16  ?  412 PRO C O   1 
ATOM   5527  C CB  . PRO B 2 80  ? -63.229 63.333  41.506  1.00 69.18  ?  412 PRO C CB  1 
ATOM   5528  C CG  . PRO B 2 80  ? -62.941 62.971  42.894  1.00 70.54  ?  412 PRO C CG  1 
ATOM   5529  C CD  . PRO B 2 80  ? -61.633 62.248  42.921  1.00 70.22  ?  412 PRO C CD  1 
ATOM   5530  N N   . GLY B 2 81  ? -61.271 65.620  39.826  1.00 87.14  ?  413 GLY C N   1 
ATOM   5531  C CA  . GLY B 2 81  ? -60.972 67.029  39.767  1.00 87.34  ?  413 GLY C CA  1 
ATOM   5532  C C   . GLY B 2 81  ? -59.513 67.379  39.863  1.00 87.55  ?  413 GLY C C   1 
ATOM   5533  O O   . GLY B 2 81  ? -59.179 68.564  39.788  1.00 90.14  ?  413 GLY C O   1 
ATOM   5534  N N   . GLN B 2 82  ? -58.642 66.386  40.025  1.00 78.12  ?  414 GLN C N   1 
ATOM   5535  C CA  . GLN B 2 82  ? -57.206 66.608  39.969  1.00 72.74  ?  414 GLN C CA  1 
ATOM   5536  C C   . GLN B 2 82  ? -56.756 66.749  38.521  1.00 73.72  ?  414 GLN C C   1 
ATOM   5537  O O   . GLN B 2 82  ? -57.112 65.943  37.665  1.00 75.19  ?  414 GLN C O   1 
ATOM   5538  C CB  . GLN B 2 82  ? -56.479 65.445  40.644  1.00 68.21  ?  414 GLN C CB  1 
ATOM   5539  C CG  . GLN B 2 82  ? -56.640 65.534  42.100  1.00 68.16  ?  414 GLN C CG  1 
ATOM   5540  C CD  . GLN B 2 82  ? -55.971 66.787  42.595  1.00 78.40  ?  414 GLN C CD  1 
ATOM   5541  O OE1 . GLN B 2 82  ? -54.920 67.185  42.075  1.00 81.17  ?  414 GLN C OE1 1 
ATOM   5542  N NE2 . GLN B 2 82  ? -56.620 67.481  43.534  1.00 82.79  ?  414 GLN C NE2 1 
ATOM   5543  N N   . THR B 2 83  ? -55.992 67.785  38.225  1.00 78.78  ?  415 THR C N   1 
ATOM   5544  C CA  . THR B 2 83  ? -55.229 67.799  36.976  1.00 77.21  ?  415 THR C CA  1 
ATOM   5545  C C   . THR B 2 83  ? -53.775 67.909  37.368  1.00 74.41  ?  415 THR C C   1 
ATOM   5546  O O   . THR B 2 83  ? -53.299 69.003  37.671  1.00 70.11  ?  415 THR C O   1 
ATOM   5547  C CB  . THR B 2 83  ? -55.572 68.934  36.000  1.00 78.24  ?  415 THR C CB  1 
ATOM   5548  O OG1 . THR B 2 83  ? -54.842 70.123  36.376  1.00 73.20  ?  415 THR C OG1 1 
ATOM   5549  C CG2 . THR B 2 83  ? -57.135 69.160  35.806  1.00 83.23  ?  415 THR C CG2 1 
ATOM   5550  N N   . GLY B 2 84  ? -53.094 66.776  37.377  1.00 71.43  ?  416 GLY C N   1 
ATOM   5551  C CA  . GLY B 2 84  ? -51.671 66.780  37.212  1.00 74.08  ?  416 GLY C CA  1 
ATOM   5552  C C   . GLY B 2 84  ? -51.274 66.598  35.756  1.00 73.62  ?  416 GLY C C   1 
ATOM   5553  O O   . GLY B 2 84  ? -51.656 67.381  34.887  1.00 70.44  ?  416 GLY C O   1 
ATOM   5554  N N   . ASN B 2 85  ? -50.491 65.558  35.501  1.00 68.70  ?  417 ASN C N   1 
ATOM   5555  C CA  . ASN B 2 85  ? -49.904 65.208  34.215  1.00 63.79  ?  417 ASN C CA  1 
ATOM   5556  C C   . ASN B 2 85  ? -50.460 63.895  33.721  1.00 64.08  ?  417 ASN C C   1 
ATOM   5557  O O   . ASN B 2 85  ? -50.540 63.631  32.517  1.00 57.71  ?  417 ASN C O   1 
ATOM   5558  C CB  . ASN B 2 85  ? -48.387 65.037  34.382  1.00 67.36  ?  417 ASN C CB  1 
ATOM   5559  C CG  . ASN B 2 85  ? -47.613 65.269  33.094  1.00 67.15  ?  417 ASN C CG  1 
ATOM   5560  O OD1 . ASN B 2 85  ? -48.180 65.615  32.060  1.00 61.66  ?  417 ASN C OD1 1 
ATOM   5561  N ND2 . ASN B 2 85  ? -46.303 65.052  33.152  1.00 74.08  ?  417 ASN C ND2 1 
ATOM   5562  N N   . ILE B 2 86  ? -50.762 63.005  34.663  1.00 68.80  ?  418 ILE C N   1 
ATOM   5563  C CA  . ILE B 2 86  ? -51.358 61.697  34.282  1.00 63.34  ?  418 ILE C CA  1 
ATOM   5564  C C   . ILE B 2 86  ? -52.829 61.970  33.998  1.00 71.03  ?  418 ILE C C   1 
ATOM   5565  O O   . ILE B 2 86  ? -53.334 61.523  32.968  1.00 71.49  ?  418 ILE C O   1 
ATOM   5566  C CB  . ILE B 2 86  ? -51.168 60.663  35.406  1.00 58.87  ?  418 ILE C CB  1 
ATOM   5567  C CG1 . ILE B 2 86  ? -49.953 59.766  35.159  1.00 62.11  ?  418 ILE C CG1 1 
ATOM   5568  C CG2 . ILE B 2 86  ? -52.428 59.842  35.608  1.00 61.84  ?  418 ILE C CG2 1 
ATOM   5569  C CD1 . ILE B 2 86  ? -48.758 60.487  34.590  1.00 59.55  ?  418 ILE C CD1 1 
ATOM   5570  N N   . ALA B 2 87  ? -53.468 62.744  34.867  1.00 82.63  ?  419 ALA C N   1 
ATOM   5571  C CA  . ALA B 2 87  ? -54.911 63.018  34.710  1.00 77.93  ?  419 ALA C CA  1 
ATOM   5572  C C   . ALA B 2 87  ? -55.171 63.795  33.426  1.00 84.27  ?  419 ALA C C   1 
ATOM   5573  O O   . ALA B 2 87  ? -56.235 63.594  32.836  1.00 92.12  ?  419 ALA C O   1 
ATOM   5574  C CB  . ALA B 2 87  ? -55.390 63.801  35.894  1.00 82.77  ?  419 ALA C CB  1 
ATOM   5575  N N   . ASP B 2 88  ? -54.310 64.746  33.095  1.00 72.47  ?  420 ASP C N   1 
ATOM   5576  C CA  . ASP B 2 88  ? -54.621 65.609  31.930  1.00 73.40  ?  420 ASP C CA  1 
ATOM   5577  C C   . ASP B 2 88  ? -54.315 64.858  30.633  1.00 65.44  ?  420 ASP C C   1 
ATOM   5578  O O   . ASP B 2 88  ? -55.007 65.142  29.655  1.00 62.46  ?  420 ASP C O   1 
ATOM   5579  C CB  . ASP B 2 88  ? -54.009 67.015  32.082  1.00 76.91  ?  420 ASP C CB  1 
ATOM   5580  C CG  . ASP B 2 88  ? -52.490 67.106  31.985  1.00 70.05  ?  420 ASP C CG  1 
ATOM   5581  O OD1 . ASP B 2 88  ? -51.850 66.052  32.000  1.00 74.08  ?  420 ASP C OD1 1 
ATOM   5582  O OD2 . ASP B 2 88  ? -51.953 68.246  31.921  1.00 59.83  -1 420 ASP C OD2 1 
ATOM   5583  N N   . TYR B 2 89  ? -53.368 63.928  30.641  1.00 60.01  ?  421 TYR C N   1 
ATOM   5584  C CA  . TYR B 2 89  ? -52.969 63.257  29.375  1.00 60.88  ?  421 TYR C CA  1 
ATOM   5585  C C   . TYR B 2 89  ? -52.937 61.731  29.469  1.00 61.25  ?  421 TYR C C   1 
ATOM   5586  O O   . TYR B 2 89  ? -52.474 61.119  28.504  1.00 60.94  ?  421 TYR C O   1 
ATOM   5587  C CB  . TYR B 2 89  ? -51.532 63.645  29.037  1.00 63.43  ?  421 TYR C CB  1 
ATOM   5588  C CG  . TYR B 2 89  ? -51.295 65.073  28.631  1.00 63.41  ?  421 TYR C CG  1 
ATOM   5589  C CD1 . TYR B 2 89  ? -52.118 65.693  27.710  1.00 64.77  ?  421 TYR C CD1 1 
ATOM   5590  C CD2 . TYR B 2 89  ? -50.228 65.789  29.138  1.00 65.83  ?  421 TYR C CD2 1 
ATOM   5591  C CE1 . TYR B 2 89  ? -51.893 66.995  27.310  1.00 69.28  ?  421 TYR C CE1 1 
ATOM   5592  C CE2 . TYR B 2 89  ? -49.989 67.095  28.753  1.00 61.00  ?  421 TYR C CE2 1 
ATOM   5593  C CZ  . TYR B 2 89  ? -50.824 67.699  27.834  1.00 58.63  ?  421 TYR C CZ  1 
ATOM   5594  O OH  . TYR B 2 89  ? -50.606 68.984  27.440  1.00 62.88  ?  421 TYR C OH  1 
ATOM   5595  N N   . ASN B 2 90  ? -53.393 61.126  30.560  1.00 62.07  ?  422 ASN C N   1 
ATOM   5596  C CA  . ASN B 2 90  ? -53.240 59.649  30.675  1.00 59.21  ?  422 ASN C CA  1 
ATOM   5597  C C   . ASN B 2 90  ? -54.525 58.958  31.187  1.00 57.43  ?  422 ASN C C   1 
ATOM   5598  O O   . ASN B 2 90  ? -55.015 58.090  30.451  1.00 59.49  ?  422 ASN C O   1 
ATOM   5599  C CB  . ASN B 2 90  ? -52.005 59.273  31.491  1.00 56.71  ?  422 ASN C CB  1 
ATOM   5600  C CG  . ASN B 2 90  ? -50.731 59.248  30.681  1.00 55.22  ?  422 ASN C CG  1 
ATOM   5601  O OD1 . ASN B 2 90  ? -50.701 58.727  29.572  1.00 58.03  ?  422 ASN C OD1 1 
ATOM   5602  N ND2 . ASN B 2 90  ? -49.665 59.798  31.237  1.00 63.12  ?  422 ASN C ND2 1 
ATOM   5603  N N   . TYR B 2 91  ? -55.019 59.268  32.395  1.00 57.23  ?  423 TYR C N   1 
ATOM   5604  C CA  . TYR B 2 91  ? -56.216 58.598  32.944  1.00 58.72  ?  423 TYR C CA  1 
ATOM   5605  C C   . TYR B 2 91  ? -56.986 59.604  33.816  1.00 60.98  ?  423 TYR C C   1 
ATOM   5606  O O   . TYR B 2 91  ? -56.700 59.755  35.009  1.00 64.41  ?  423 TYR C O   1 
ATOM   5607  C CB  . TYR B 2 91  ? -55.807 57.393  33.769  1.00 53.34  ?  423 TYR C CB  1 
ATOM   5608  C CG  . TYR B 2 91  ? -56.933 56.589  34.402  1.00 51.33  ?  423 TYR C CG  1 
ATOM   5609  C CD1 . TYR B 2 91  ? -57.708 55.718  33.670  1.00 54.83  ?  423 TYR C CD1 1 
ATOM   5610  C CD2 . TYR B 2 91  ? -57.337 56.854  35.707  1.00 51.20  ?  423 TYR C CD2 1 
ATOM   5611  C CE1 . TYR B 2 91  ? -58.750 55.012  34.273  1.00 54.58  ?  423 TYR C CE1 1 
ATOM   5612  C CE2 . TYR B 2 91  ? -58.386 56.177  36.300  1.00 49.28  ?  423 TYR C CE2 1 
ATOM   5613  C CZ  . TYR B 2 91  ? -59.085 55.270  35.585  1.00 51.08  ?  423 TYR C CZ  1 
ATOM   5614  O OH  . TYR B 2 91  ? -60.115 54.633  36.220  1.00 55.04  ?  423 TYR C OH  1 
ATOM   5615  N N   . LYS B 2 92  ? -57.971 60.278  33.240  1.00 60.92  ?  424 LYS C N   1 
ATOM   5616  C CA  . LYS B 2 92  ? -58.689 61.314  33.972  1.00 63.36  ?  424 LYS C CA  1 
ATOM   5617  C C   . LYS B 2 92  ? -60.014 60.745  34.459  1.00 60.59  ?  424 LYS C C   1 
ATOM   5618  O O   . LYS B 2 92  ? -60.754 60.148  33.681  1.00 60.39  ?  424 LYS C O   1 
ATOM   5619  C CB  . LYS B 2 92  ? -58.915 62.559  33.102  1.00 64.66  ?  424 LYS C CB  1 
ATOM   5620  C CG  . LYS B 2 92  ? -60.055 63.486  33.526  1.00 57.80  ?  424 LYS C CG  1 
ATOM   5621  C CD  . LYS B 2 92  ? -59.683 64.384  34.693  1.00 60.74  ?  424 LYS C CD  1 
ATOM   5622  C CE  . LYS B 2 92  ? -59.379 65.797  34.213  1.00 64.41  ?  424 LYS C CE  1 
ATOM   5623  N NZ  . LYS B 2 92  ? -59.364 66.803  35.332  1.00 66.53  ?  424 LYS C NZ  1 
ATOM   5624  N N   . LEU B 2 93  ? -60.272 60.879  35.741  1.00 65.55  ?  425 LEU C N   1 
ATOM   5625  C CA  . LEU B 2 93  ? -61.542 60.589  36.380  1.00 61.64  ?  425 LEU C CA  1 
ATOM   5626  C C   . LEU B 2 93  ? -62.494 61.760  36.214  1.00 67.88  ?  425 LEU C C   1 
ATOM   5627  O O   . LEU B 2 93  ? -62.067 62.896  35.980  1.00 72.20  ?  425 LEU C O   1 
ATOM   5628  C CB  . LEU B 2 93  ? -61.323 60.333  37.849  1.00 59.92  ?  425 LEU C CB  1 
ATOM   5629  C CG  . LEU B 2 93  ? -60.662 59.043  38.223  1.00 59.71  ?  425 LEU C CG  1 
ATOM   5630  C CD1 . LEU B 2 93  ? -61.007 58.772  39.657  1.00 64.09  ?  425 LEU C CD1 1 
ATOM   5631  C CD2 . LEU B 2 93  ? -61.173 57.980  37.294  1.00 57.05  ?  425 LEU C CD2 1 
ATOM   5632  N N   . PRO B 2 94  ? -63.791 61.529  36.341  1.00 67.08  ?  426 PRO C N   1 
ATOM   5633  C CA  . PRO B 2 94  ? -64.755 62.598  36.105  1.00 70.75  ?  426 PRO C CA  1 
ATOM   5634  C C   . PRO B 2 94  ? -64.987 63.336  37.401  1.00 72.92  ?  426 PRO C C   1 
ATOM   5635  O O   . PRO B 2 94  ? -64.792 62.806  38.496  1.00 71.90  ?  426 PRO C O   1 
ATOM   5636  C CB  . PRO B 2 94  ? -66.028 61.848  35.713  1.00 74.44  ?  426 PRO C CB  1 
ATOM   5637  C CG  . PRO B 2 94  ? -65.868 60.536  36.380  1.00 74.75  ?  426 PRO C CG  1 
ATOM   5638  C CD  . PRO B 2 94  ? -64.419 60.210  36.306  1.00 68.35  ?  426 PRO C CD  1 
ATOM   5639  N N   . ASP B 2 95  ? -65.446 64.577  37.277  1.00 75.81  ?  427 ASP C N   1 
ATOM   5640  C CA  . ASP B 2 95  ? -65.722 65.324  38.489  1.00 74.76  ?  427 ASP C CA  1 
ATOM   5641  C C   . ASP B 2 95  ? -66.820 64.639  39.294  1.00 78.53  ?  427 ASP C C   1 
ATOM   5642  O O   . ASP B 2 95  ? -66.755 64.606  40.523  1.00 76.61  ?  427 ASP C O   1 
ATOM   5643  C CB  . ASP B 2 95  ? -66.087 66.753  38.139  1.00 68.80  ?  427 ASP C CB  1 
ATOM   5644  C CG  . ASP B 2 95  ? -65.055 67.388  37.262  1.00 75.14  ?  427 ASP C CG  1 
ATOM   5645  O OD1 . ASP B 2 95  ? -63.874 67.337  37.633  1.00 79.26  ?  427 ASP C OD1 1 
ATOM   5646  O OD2 . ASP B 2 95  ? -65.414 67.947  36.203  1.00 77.97  -1 427 ASP C OD2 1 
ATOM   5647  N N   . ASP B 2 96  ? -67.800 64.031  38.615  1.00 90.88  ?  428 ASP C N   1 
ATOM   5648  C CA  . ASP B 2 96  ? -68.939 63.386  39.260  1.00 92.13  ?  428 ASP C CA  1 
ATOM   5649  C C   . ASP B 2 96  ? -68.682 61.918  39.578  1.00 92.95  ?  428 ASP C C   1 
ATOM   5650  O O   . ASP B 2 96  ? -69.631 61.124  39.625  1.00 94.80  ?  428 ASP C O   1 
ATOM   5651  C CB  . ASP B 2 96  ? -70.191 63.518  38.393  1.00 93.65  ?  428 ASP C CB  1 
ATOM   5652  C CG  . ASP B 2 96  ? -69.984 62.972  36.968  1.00 107.86 ?  428 ASP C CG  1 
ATOM   5653  O OD1 . ASP B 2 96  ? -69.568 63.773  36.102  1.00 108.53 ?  428 ASP C OD1 1 
ATOM   5654  O OD2 . ASP B 2 96  ? -70.228 61.748  36.725  1.00 105.86 -1 428 ASP C OD2 1 
ATOM   5655  N N   . PHE B 2 97  ? -67.427 61.540  39.815  1.00 77.56  ?  429 PHE C N   1 
ATOM   5656  C CA  . PHE B 2 97  ? -67.038 60.160  40.106  1.00 74.78  ?  429 PHE C CA  1 
ATOM   5657  C C   . PHE B 2 97  ? -67.776 59.519  41.266  1.00 75.93  ?  429 PHE C C   1 
ATOM   5658  O O   . PHE B 2 97  ? -68.105 60.160  42.269  1.00 77.68  ?  429 PHE C O   1 
ATOM   5659  C CB  . PHE B 2 97  ? -65.535 60.121  40.344  1.00 74.30  ?  429 PHE C CB  1 
ATOM   5660  C CG  . PHE B 2 97  ? -64.915 58.767  40.231  1.00 73.44  ?  429 PHE C CG  1 
ATOM   5661  C CD1 . PHE B 2 97  ? -64.601 58.238  39.002  1.00 74.69  ?  429 PHE C CD1 1 
ATOM   5662  C CD2 . PHE B 2 97  ? -64.761 57.974  41.349  1.00 74.65  ?  429 PHE C CD2 1 
ATOM   5663  C CE1 . PHE B 2 97  ? -64.029 56.957  38.914  1.00 75.46  ?  429 PHE C CE1 1 
ATOM   5664  C CE2 . PHE B 2 97  ? -64.175 56.749  41.270  1.00 74.60  ?  429 PHE C CE2 1 
ATOM   5665  C CZ  . PHE B 2 97  ? -63.829 56.221  40.079  1.00 71.75  ?  429 PHE C CZ  1 
ATOM   5666  N N   . THR B 2 98  ? -68.011 58.221  41.119  1.00 78.16  ?  430 THR C N   1 
ATOM   5667  C CA  . THR B 2 98  ? -68.647 57.409  42.135  1.00 82.73  ?  430 THR C CA  1 
ATOM   5668  C C   . THR B 2 98  ? -68.060 56.003  42.093  1.00 85.43  ?  430 THR C C   1 
ATOM   5669  O O   . THR B 2 98  ? -68.705 55.054  41.691  1.00 86.79  ?  430 THR C O   1 
ATOM   5670  C CB  . THR B 2 98  ? -70.159 57.316  41.951  1.00 80.61  ?  430 THR C CB  1 
ATOM   5671  O OG1 . THR B 2 98  ? -70.397 56.697  40.690  1.00 93.15  ?  430 THR C OG1 1 
ATOM   5672  C CG2 . THR B 2 98  ? -70.853 58.673  41.981  1.00 79.21  ?  430 THR C CG2 1 
ATOM   5673  N N   . GLY B 2 99  ? -66.816 55.857  42.527  1.00 91.85  ?  431 GLY C N   1 
ATOM   5674  C CA  . GLY B 2 99  ? -66.239 54.548  42.742  1.00 88.70  ?  431 GLY C CA  1 
ATOM   5675  C C   . GLY B 2 99  ? -65.035 54.592  43.656  1.00 84.18  ?  431 GLY C C   1 
ATOM   5676  O O   . GLY B 2 99  ? -64.637 55.642  44.146  1.00 87.67  ?  431 GLY C O   1 
ATOM   5677  N N   . CYS B 2 100 ? -64.397 53.463  43.837  1.00 80.12  ?  432 CYS C N   1 
ATOM   5678  C CA  . CYS B 2 100 ? -63.215 53.413  44.679  1.00 80.22  ?  432 CYS C CA  1 
ATOM   5679  C C   . CYS B 2 100 ? -61.907 53.535  43.912  1.00 77.28  ?  432 CYS C C   1 
ATOM   5680  O O   . CYS B 2 100 ? -61.798 53.063  42.783  1.00 78.34  ?  432 CYS C O   1 
ATOM   5681  C CB  . CYS B 2 100 ? -63.227 52.111  45.452  1.00 87.27  ?  432 CYS C CB  1 
ATOM   5682  S SG  . CYS B 2 100 ? -63.026 52.332  47.225  1.00 114.49 ?  432 CYS C SG  1 
ATOM   5683  N N   . VAL B 2 101 ? -60.892 54.127  44.554  1.00 77.40  ?  433 VAL C N   1 
ATOM   5684  C CA  . VAL B 2 101 ? -59.529 54.152  44.023  1.00 75.79  ?  433 VAL C CA  1 
ATOM   5685  C C   . VAL B 2 101 ? -58.626 53.441  45.022  1.00 73.43  ?  433 VAL C C   1 
ATOM   5686  O O   . VAL B 2 101 ? -58.563 53.838  46.193  1.00 79.80  ?  433 VAL C O   1 
ATOM   5687  C CB  . VAL B 2 101 ? -59.020 55.586  43.798  1.00 71.58  ?  433 VAL C CB  1 
ATOM   5688  C CG1 . VAL B 2 101 ? -57.545 55.550  43.496  1.00 67.44  ?  433 VAL C CG1 1 
ATOM   5689  C CG2 . VAL B 2 101 ? -59.794 56.314  42.726  1.00 70.97  ?  433 VAL C CG2 1 
ATOM   5690  N N   . ILE B 2 102 ? -57.892 52.426  44.558  1.00 67.48  ?  434 ILE C N   1 
ATOM   5691  C CA  . ILE B 2 102 ? -57.110 51.542  45.422  1.00 68.88  ?  434 ILE C CA  1 
ATOM   5692  C C   . ILE B 2 102 ? -55.685 51.504  44.888  1.00 69.86  ?  434 ILE C C   1 
ATOM   5693  O O   . ILE B 2 102 ? -55.489 51.282  43.689  1.00 67.24  ?  434 ILE C O   1 
ATOM   5694  C CB  . ILE B 2 102 ? -57.706 50.124  45.439  1.00 66.12  ?  434 ILE C CB  1 
ATOM   5695  C CG1 . ILE B 2 102 ? -59.149 50.196  45.897  1.00 69.19  ?  434 ILE C CG1 1 
ATOM   5696  C CG2 . ILE B 2 102 ? -56.904 49.231  46.355  1.00 74.82  ?  434 ILE C CG2 1 
ATOM   5697  C CD1 . ILE B 2 102 ? -59.726 48.907  46.258  1.00 72.26  ?  434 ILE C CD1 1 
ATOM   5698  N N   . ALA B 2 103 ? -54.695 51.735  45.755  1.00 83.56  ?  435 ALA C N   1 
ATOM   5699  C CA  . ALA B 2 103 ? -53.300 51.845  45.332  1.00 77.21  ?  435 ALA C CA  1 
ATOM   5700  C C   . ALA B 2 103 ? -52.398 51.185  46.356  1.00 84.05  ?  435 ALA C C   1 
ATOM   5701  O O   . ALA B 2 103 ? -52.540 51.454  47.553  1.00 97.64  ?  435 ALA C O   1 
ATOM   5702  C CB  . ALA B 2 103 ? -52.869 53.300  45.182  1.00 80.40  ?  435 ALA C CB  1 
ATOM   5703  N N   . TRP B 2 104 ? -51.443 50.386  45.894  1.00 69.21  ?  436 TRP C N   1 
ATOM   5704  C CA  . TRP B 2 104 ? -50.439 49.842  46.801  1.00 68.45  ?  436 TRP C CA  1 
ATOM   5705  C C   . TRP B 2 104 ? -49.034 49.980  46.188  1.00 65.36  ?  436 TRP C C   1 
ATOM   5706  O O   . TRP B 2 104 ? -48.896 50.156  44.963  1.00 63.77  ?  436 TRP C O   1 
ATOM   5707  C CB  . TRP B 2 104 ? -50.760 48.392  47.135  1.00 64.22  ?  436 TRP C CB  1 
ATOM   5708  C CG  . TRP B 2 104 ? -50.910 47.516  45.981  1.00 59.57  ?  436 TRP C CG  1 
ATOM   5709  C CD1 . TRP B 2 104 ? -50.027 46.578  45.582  1.00 59.81  ?  436 TRP C CD1 1 
ATOM   5710  C CD2 . TRP B 2 104 ? -52.024 47.406  45.104  1.00 62.30  ?  436 TRP C CD2 1 
ATOM   5711  N NE1 . TRP B 2 104 ? -50.485 45.908  44.479  1.00 60.50  ?  436 TRP C NE1 1 
ATOM   5712  C CE2 . TRP B 2 104 ? -51.715 46.395  44.164  1.00 56.88  ?  436 TRP C CE2 1 
ATOM   5713  C CE3 . TRP B 2 104 ? -53.249 48.061  45.007  1.00 65.04  ?  436 TRP C CE3 1 
ATOM   5714  C CZ2 . TRP B 2 104 ? -52.570 46.028  43.158  1.00 57.59  ?  436 TRP C CZ2 1 
ATOM   5715  C CZ3 . TRP B 2 104 ? -54.109 47.693  43.990  1.00 63.44  ?  436 TRP C CZ3 1 
ATOM   5716  C CH2 . TRP B 2 104 ? -53.763 46.688  43.078  1.00 62.52  ?  436 TRP C CH2 1 
ATOM   5717  N N   . ASN B 2 105 ? -47.988 49.764  46.983  1.00 63.92  ?  437 ASN C N   1 
ATOM   5718  C CA  . ASN B 2 105 ? -46.597 49.924  46.475  1.00 58.21  ?  437 ASN C CA  1 
ATOM   5719  C C   . ASN B 2 105 ? -46.166 48.637  45.778  1.00 58.82  ?  437 ASN C C   1 
ATOM   5720  O O   . ASN B 2 105 ? -46.442 47.569  46.329  1.00 59.91  ?  437 ASN C O   1 
ATOM   5721  C CB  . ASN B 2 105 ? -45.636 50.302  47.601  1.00 52.37  ?  437 ASN C CB  1 
ATOM   5722  C CG  . ASN B 2 105 ? -44.419 51.073  47.140  1.00 56.47  ?  437 ASN C CG  1 
ATOM   5723  O OD1 . ASN B 2 105 ? -44.279 52.256  47.434  1.00 62.36  ?  437 ASN C OD1 1 
ATOM   5724  N ND2 . ASN B 2 105 ? -43.521 50.401  46.440  1.00 51.41  ?  437 ASN C ND2 1 
ATOM   5725  N N   . SER B 2 106 ? -45.472 48.745  44.647  1.00 53.09  ?  438 SER C N   1 
ATOM   5726  C CA  . SER B 2 106 ? -45.095 47.543  43.865  1.00 55.38  ?  438 SER C CA  1 
ATOM   5727  C C   . SER B 2 106 ? -43.588 47.499  43.647  1.00 58.04  ?  438 SER C C   1 
ATOM   5728  O O   . SER B 2 106 ? -43.145 46.798  42.730  1.00 60.01  ?  438 SER C O   1 
ATOM   5729  C CB  . SER B 2 106 ? -45.792 47.569  42.559  1.00 51.44  ?  438 SER C CB  1 
ATOM   5730  O OG  . SER B 2 106 ? -45.018 48.254  41.597  1.00 50.49  ?  438 SER C OG  1 
ATOM   5731  N N   . ASN B 2 107 ? -42.829 48.213  44.466  1.00 52.11  ?  439 ASN C N   1 
ATOM   5732  C CA  . ASN B 2 107 ? -41.370 48.285  44.220  1.00 52.24  ?  439 ASN C CA  1 
ATOM   5733  C C   . ASN B 2 107 ? -40.792 46.881  44.117  1.00 52.45  ?  439 ASN C C   1 
ATOM   5734  O O   . ASN B 2 107 ? -39.947 46.662  43.242  1.00 47.56  ?  439 ASN C O   1 
ATOM   5735  C CB  . ASN B 2 107 ? -40.651 49.101  45.291  1.00 49.73  ?  439 ASN C CB  1 
ATOM   5736  C CG  . ASN B 2 107 ? -39.476 49.879  44.747  1.00 50.75  ?  439 ASN C CG  1 
ATOM   5737  O OD1 . ASN B 2 107 ? -39.426 50.177  43.560  1.00 53.68  ?  439 ASN C OD1 1 
ATOM   5738  N ND2 . ASN B 2 107 ? -38.527 50.205  45.608  1.00 52.73  ?  439 ASN C ND2 1 
ATOM   5739  N N   . LYS B 2 108 ? -41.228 45.965  44.976  1.00 52.54  ?  440 LYS C N   1 
ATOM   5740  C CA  . LYS B 2 108 ? -40.590 44.658  44.962  1.00 55.08  ?  440 LYS C CA  1 
ATOM   5741  C C   . LYS B 2 108 ? -40.692 44.017  43.600  1.00 51.90  ?  440 LYS C C   1 
ATOM   5742  O O   . LYS B 2 108 ? -39.738 43.393  43.131  1.00 51.59  ?  440 LYS C O   1 
ATOM   5743  C CB  . LYS B 2 108 ? -41.169 43.736  46.039  1.00 61.90  ?  440 LYS C CB  1 
ATOM   5744  C CG  . LYS B 2 108 ? -40.534 43.975  47.435  1.00 74.98  ?  440 LYS C CG  1 
ATOM   5745  C CD  . LYS B 2 108 ? -41.474 43.777  48.648  1.00 88.57  ?  440 LYS C CD  1 
ATOM   5746  C CE  . LYS B 2 108 ? -40.658 43.592  49.961  1.00 89.85  ?  440 LYS C CE  1 
ATOM   5747  N NZ  . LYS B 2 108 ? -41.021 42.327  50.722  1.00 91.11  ?  440 LYS C NZ  1 
ATOM   5748  N N   . LEU B 2 109 ? -41.820 44.164  42.926  1.00 52.75  ?  441 LEU C N   1 
ATOM   5749  C CA  . LEU B 2 109 ? -41.977 43.351  41.745  1.00 53.77  ?  441 LEU C CA  1 
ATOM   5750  C C   . LEU B 2 109 ? -42.170 44.141  40.469  1.00 55.45  ?  441 LEU C C   1 
ATOM   5751  O O   . LEU B 2 109 ? -42.142 43.538  39.392  1.00 61.99  ?  441 LEU C O   1 
ATOM   5752  C CB  . LEU B 2 109 ? -43.119 42.337  41.940  1.00 55.50  ?  441 LEU C CB  1 
ATOM   5753  C CG  . LEU B 2 109 ? -44.594 42.701  41.970  1.00 56.63  ?  441 LEU C CG  1 
ATOM   5754  C CD1 . LEU B 2 109 ? -45.448 41.436  42.052  1.00 57.77  ?  441 LEU C CD1 1 
ATOM   5755  C CD2 . LEU B 2 109 ? -44.915 43.664  43.082  1.00 59.01  ?  441 LEU C CD2 1 
ATOM   5756  N N   . ASP B 2 110 ? -42.317 45.458  40.528  1.00 53.31  ?  442 ASP C N   1 
ATOM   5757  C CA  . ASP B 2 110 ? -42.396 46.205  39.279  1.00 52.89  ?  442 ASP C CA  1 
ATOM   5758  C C   . ASP B 2 110 ? -41.199 47.083  38.997  1.00 52.21  ?  442 ASP C C   1 
ATOM   5759  O O   . ASP B 2 110 ? -41.134 47.685  37.929  1.00 53.55  ?  442 ASP C O   1 
ATOM   5760  C CB  . ASP B 2 110 ? -43.669 47.052  39.200  1.00 58.00  ?  442 ASP C CB  1 
ATOM   5761  C CG  . ASP B 2 110 ? -44.873 46.226  38.814  1.00 60.58  ?  442 ASP C CG  1 
ATOM   5762  O OD1 . ASP B 2 110 ? -44.808 45.645  37.714  1.00 60.55  ?  442 ASP C OD1 1 
ATOM   5763  O OD2 . ASP B 2 110 ? -45.884 46.195  39.556  1.00 63.93  -1 442 ASP C OD2 1 
ATOM   5764  N N   . SER B 2 111 ? -40.247 47.169  39.882  1.00 54.18  ?  443 SER C N   1 
ATOM   5765  C CA  . SER B 2 111 ? -39.056 47.943  39.601  1.00 53.81  ?  443 SER C CA  1 
ATOM   5766  C C   . SER B 2 111 ? -37.839 47.036  39.721  1.00 49.82  ?  443 SER C C   1 
ATOM   5767  O O   . SER B 2 111 ? -37.747 46.232  40.651  1.00 47.21  ?  443 SER C O   1 
ATOM   5768  C CB  . SER B 2 111 ? -39.030 49.164  40.508  1.00 52.75  ?  443 SER C CB  1 
ATOM   5769  O OG  . SER B 2 111 ? -38.322 48.878  41.676  1.00 55.36  ?  443 SER C OG  1 
ATOM   5770  N N   . LYS B 2 112 ? -36.974 47.084  38.720  1.00 54.70  ?  444 LYS C N   1 
ATOM   5771  C CA  . LYS B 2 112 ? -35.865 46.156  38.633  1.00 64.05  ?  444 LYS C CA  1 
ATOM   5772  C C   . LYS B 2 112 ? -34.544 46.921  38.616  1.00 66.01  ?  444 LYS C C   1 
ATOM   5773  O O   . LYS B 2 112 ? -34.447 48.036  38.083  1.00 65.05  ?  444 LYS C O   1 
ATOM   5774  C CB  . LYS B 2 112 ? -35.982 45.254  37.378  1.00 67.24  ?  444 LYS C CB  1 
ATOM   5775  C CG  . LYS B 2 112 ? -35.377 45.900  36.125  1.00 74.20  ?  444 LYS C CG  1 
ATOM   5776  C CD  . LYS B 2 112 ? -34.928 44.963  34.994  1.00 78.82  ?  444 LYS C CD  1 
ATOM   5777  C CE  . LYS B 2 112 ? -34.546 45.802  33.746  1.00 84.97  ?  444 LYS C CE  1 
ATOM   5778  N NZ  . LYS B 2 112 ? -33.178 45.557  33.195  1.00 81.36  ?  444 LYS C NZ  1 
ATOM   5779  N N   . VAL B 2 113 ? -33.531 46.324  39.231  1.00 63.75  ?  445 VAL C N   1 
ATOM   5780  C CA  . VAL B 2 113 ? -32.222 46.944  39.268  1.00 62.64  ?  445 VAL C CA  1 
ATOM   5781  C C   . VAL B 2 113 ? -31.791 47.244  37.849  1.00 66.67  ?  445 VAL C C   1 
ATOM   5782  O O   . VAL B 2 113 ? -31.804 46.361  36.986  1.00 69.58  ?  445 VAL C O   1 
ATOM   5783  C CB  . VAL B 2 113 ? -31.217 46.030  39.949  1.00 58.31  ?  445 VAL C CB  1 
ATOM   5784  C CG1 . VAL B 2 113 ? -29.998 46.815  40.176  1.00 48.53  ?  445 VAL C CG1 1 
ATOM   5785  C CG2 . VAL B 2 113 ? -31.782 45.460  41.250  1.00 59.64  ?  445 VAL C CG2 1 
ATOM   5786  N N   . GLY B 2 114 ? -31.419 48.479  37.591  1.00 70.34  ?  446 GLY C N   1 
ATOM   5787  C CA  . GLY B 2 114 ? -30.975 48.831  36.267  1.00 72.46  ?  446 GLY C CA  1 
ATOM   5788  C C   . GLY B 2 114 ? -32.033 49.380  35.358  1.00 79.32  ?  446 GLY C C   1 
ATOM   5789  O O   . GLY B 2 114 ? -31.753 49.583  34.179  1.00 80.05  ?  446 GLY C O   1 
ATOM   5790  N N   . GLY B 2 115 ? -33.238 49.615  35.870  1.00 107.60 ?  447 GLY C N   1 
ATOM   5791  C CA  . GLY B 2 115 ? -34.221 50.424  35.172  1.00 104.15 ?  447 GLY C CA  1 
ATOM   5792  C C   . GLY B 2 115 ? -35.278 49.665  34.402  1.00 99.84  ?  447 GLY C C   1 
ATOM   5793  O O   . GLY B 2 115 ? -35.006 49.066  33.356  1.00 101.95 ?  447 GLY C O   1 
ATOM   5794  N N   . ASN B 2 116 ? -36.493 49.687  34.895  1.00 75.12  ?  448 ASN C N   1 
ATOM   5795  C CA  . ASN B 2 116 ? -37.567 48.962  34.245  1.00 73.65  ?  448 ASN C CA  1 
ATOM   5796  C C   . ASN B 2 116 ? -38.332 49.954  33.378  1.00 69.49  ?  448 ASN C C   1 
ATOM   5797  O O   . ASN B 2 116 ? -39.041 50.818  33.889  1.00 71.67  ?  448 ASN C O   1 
ATOM   5798  C CB  . ASN B 2 116 ? -38.475 48.298  35.268  1.00 69.97  ?  448 ASN C CB  1 
ATOM   5799  C CG  . ASN B 2 116 ? -39.735 47.826  34.649  1.00 66.50  ?  448 ASN C CG  1 
ATOM   5800  O OD1 . ASN B 2 116 ? -39.743 47.459  33.474  1.00 67.08  ?  448 ASN C OD1 1 
ATOM   5801  N ND2 . ASN B 2 116 ? -40.797 47.752  35.429  1.00 61.85  ?  448 ASN C ND2 1 
ATOM   5802  N N   . TYR B 2 117 ? -38.177 49.860  32.070  1.00 64.72  ?  449 TYR C N   1 
ATOM   5803  C CA  . TYR B 2 117 ? -38.820 50.844  31.225  1.00 64.15  ?  449 TYR C CA  1 
ATOM   5804  C C   . TYR B 2 117 ? -40.097 50.335  30.587  1.00 68.66  ?  449 TYR C C   1 
ATOM   5805  O O   . TYR B 2 117 ? -40.725 51.063  29.816  1.00 73.37  ?  449 TYR C O   1 
ATOM   5806  C CB  . TYR B 2 117 ? -37.847 51.305  30.155  1.00 65.65  ?  449 TYR C CB  1 
ATOM   5807  C CG  . TYR B 2 117 ? -36.580 51.911  30.696  1.00 70.26  ?  449 TYR C CG  1 
ATOM   5808  C CD1 . TYR B 2 117 ? -36.620 52.844  31.710  1.00 72.38  ?  449 TYR C CD1 1 
ATOM   5809  C CD2 . TYR B 2 117 ? -35.331 51.541  30.189  1.00 70.76  ?  449 TYR C CD2 1 
ATOM   5810  C CE1 . TYR B 2 117 ? -35.458 53.410  32.201  1.00 69.23  ?  449 TYR C CE1 1 
ATOM   5811  C CE2 . TYR B 2 117 ? -34.165 52.103  30.683  1.00 68.08  ?  449 TYR C CE2 1 
ATOM   5812  C CZ  . TYR B 2 117 ? -34.247 53.038  31.690  1.00 65.18  ?  449 TYR C CZ  1 
ATOM   5813  O OH  . TYR B 2 117 ? -33.131 53.618  32.207  1.00 61.18  ?  449 TYR C OH  1 
ATOM   5814  N N   . ASN B 2 118 ? -40.523 49.121  30.913  1.00 64.48  ?  450 ASN C N   1 
ATOM   5815  C CA  . ASN B 2 118 ? -41.711 48.565  30.292  1.00 65.20  ?  450 ASN C CA  1 
ATOM   5816  C C   . ASN B 2 118 ? -42.959 49.400  30.585  1.00 65.27  ?  450 ASN C C   1 
ATOM   5817  O O   . ASN B 2 118 ? -43.895 49.434  29.785  1.00 72.31  ?  450 ASN C O   1 
ATOM   5818  C CB  . ASN B 2 118 ? -41.894 47.155  30.807  1.00 72.70  ?  450 ASN C CB  1 
ATOM   5819  C CG  . ASN B 2 118 ? -41.230 46.157  29.919  1.00 85.22  ?  450 ASN C CG  1 
ATOM   5820  O OD1 . ASN B 2 118 ? -40.331 46.523  29.149  1.00 85.15  ?  450 ASN C OD1 1 
ATOM   5821  N ND2 . ASN B 2 118 ? -41.659 44.904  29.985  1.00 100.25 ?  450 ASN C ND2 1 
ATOM   5822  N N   . TYR B 2 119 ? -42.994 50.082  31.721  1.00 60.95  ?  451 TYR C N   1 
ATOM   5823  C CA  . TYR B 2 119 ? -44.143 50.869  32.154  1.00 59.21  ?  451 TYR C CA  1 
ATOM   5824  C C   . TYR B 2 119 ? -43.928 52.326  31.756  1.00 58.92  ?  451 TYR C C   1 
ATOM   5825  O O   . TYR B 2 119 ? -42.980 52.956  32.224  1.00 57.45  ?  451 TYR C O   1 
ATOM   5826  C CB  . TYR B 2 119 ? -44.338 50.716  33.667  1.00 54.21  ?  451 TYR C CB  1 
ATOM   5827  C CG  . TYR B 2 119 ? -44.646 49.312  34.182  1.00 56.12  ?  451 TYR C CG  1 
ATOM   5828  C CD1 . TYR B 2 119 ? -43.773 48.261  34.068  1.00 68.05  ?  451 TYR C CD1 1 
ATOM   5829  C CD2 . TYR B 2 119 ? -45.825 49.061  34.793  1.00 61.21  ?  451 TYR C CD2 1 
ATOM   5830  C CE1 . TYR B 2 119 ? -44.126 46.988  34.563  1.00 72.49  ?  451 TYR C CE1 1 
ATOM   5831  C CE2 . TYR B 2 119 ? -46.184 47.863  35.307  1.00 61.91  ?  451 TYR C CE2 1 
ATOM   5832  C CZ  . TYR B 2 119 ? -45.363 46.824  35.183  1.00 68.11  ?  451 TYR C CZ  1 
ATOM   5833  O OH  . TYR B 2 119 ? -45.798 45.627  35.696  1.00 76.56  ?  451 TYR C OH  1 
ATOM   5834  N N   . ARG B 2 120 ? -44.833 52.879  30.939  1.00 60.50  ?  452 ARG C N   1 
ATOM   5835  C CA  . ARG B 2 120 ? -44.620 54.189  30.341  1.00 56.87  ?  452 ARG C CA  1 
ATOM   5836  C C   . ARG B 2 120 ? -45.825 55.084  30.622  1.00 53.42  ?  452 ARG C C   1 
ATOM   5837  O O   . ARG B 2 120 ? -46.926 54.580  30.821  1.00 53.94  ?  452 ARG C O   1 
ATOM   5838  C CB  . ARG B 2 120 ? -44.504 54.046  28.861  1.00 55.65  ?  452 ARG C CB  1 
ATOM   5839  C CG  . ARG B 2 120 ? -43.274 53.439  28.321  1.00 56.34  ?  452 ARG C CG  1 
ATOM   5840  C CD  . ARG B 2 120 ? -43.476 53.615  26.845  1.00 56.35  ?  452 ARG C CD  1 
ATOM   5841  N NE  . ARG B 2 120 ? -43.675 52.343  26.175  1.00 55.90  ?  452 ARG C NE  1 
ATOM   5842  C CZ  . ARG B 2 120 ? -44.043 52.229  24.904  1.00 58.17  ?  452 ARG C CZ  1 
ATOM   5843  N NH1 . ARG B 2 120 ? -44.139 53.284  24.104  1.00 58.70  ?  452 ARG C NH1 1 
ATOM   5844  N NH2 . ARG B 2 120 ? -44.381 51.037  24.434  1.00 67.32  ?  452 ARG C NH2 1 
ATOM   5845  N N   . TYR B 2 121 ? -45.636 56.410  30.626  1.00 53.27  ?  453 TYR C N   1 
ATOM   5846  C CA  . TYR B 2 121 ? -46.739 57.372  30.574  1.00 55.65  ?  453 TYR C CA  1 
ATOM   5847  C C   . TYR B 2 121 ? -46.727 58.138  29.250  1.00 61.14  ?  453 TYR C C   1 
ATOM   5848  O O   . TYR B 2 121 ? -45.749 58.119  28.488  1.00 66.40  ?  453 TYR C O   1 
ATOM   5849  C CB  . TYR B 2 121 ? -46.712 58.436  31.698  1.00 56.25  ?  453 TYR C CB  1 
ATOM   5850  C CG  . TYR B 2 121 ? -45.409 59.240  31.862  1.00 62.11  ?  453 TYR C CG  1 
ATOM   5851  C CD1 . TYR B 2 121 ? -44.944 60.097  30.896  1.00 70.39  ?  453 TYR C CD1 1 
ATOM   5852  C CD2 . TYR B 2 121 ? -44.796 59.303  33.059  1.00 67.33  ?  453 TYR C CD2 1 
ATOM   5853  C CE1 . TYR B 2 121 ? -43.787 60.851  31.094  1.00 72.55  ?  453 TYR C CE1 1 
ATOM   5854  C CE2 . TYR B 2 121 ? -43.660 60.009  33.292  1.00 71.37  ?  453 TYR C CE2 1 
ATOM   5855  C CZ  . TYR B 2 121 ? -43.143 60.789  32.315  1.00 68.26  ?  453 TYR C CZ  1 
ATOM   5856  O OH  . TYR B 2 121 ? -42.003 61.504  32.566  1.00 71.10  ?  453 TYR C OH  1 
ATOM   5857  N N   . ARG B 2 122 ? -47.790 58.885  28.989  1.00 58.54  ?  454 ARG C N   1 
ATOM   5858  C CA  . ARG B 2 122 ? -47.791 59.933  27.969  1.00 59.07  ?  454 ARG C CA  1 
ATOM   5859  C C   . ARG B 2 122 ? -47.377 61.227  28.650  1.00 62.66  ?  454 ARG C C   1 
ATOM   5860  O O   . ARG B 2 122 ? -48.035 61.622  29.632  1.00 62.60  ?  454 ARG C O   1 
ATOM   5861  C CB  . ARG B 2 122 ? -49.209 60.164  27.441  1.00 65.90  ?  454 ARG C CB  1 
ATOM   5862  C CG  . ARG B 2 122 ? -49.400 60.488  25.988  1.00 61.79  ?  454 ARG C CG  1 
ATOM   5863  C CD  . ARG B 2 122 ? -50.846 60.332  25.556  1.00 57.04  ?  454 ARG C CD  1 
ATOM   5864  N NE  . ARG B 2 122 ? -50.846 59.092  24.800  1.00 56.17  ?  454 ARG C NE  1 
ATOM   5865  C CZ  . ARG B 2 122 ? -50.341 58.982  23.588  1.00 55.51  ?  454 ARG C CZ  1 
ATOM   5866  N NH1 . ARG B 2 122 ? -49.861 60.042  22.951  1.00 58.71  ?  454 ARG C NH1 1 
ATOM   5867  N NH2 . ARG B 2 122 ? -50.204 57.769  23.058  1.00 50.36  ?  454 ARG C NH2 1 
ATOM   5868  N N   . LEU B 2 123 ? -46.370 61.958  28.116  1.00 60.45  ?  455 LEU C N   1 
ATOM   5869  C CA  . LEU B 2 123 ? -46.241 63.314  28.665  1.00 68.43  ?  455 LEU C CA  1 
ATOM   5870  C C   . LEU B 2 123 ? -46.585 64.460  27.700  1.00 67.97  ?  455 LEU C C   1 
ATOM   5871  O O   . LEU B 2 123 ? -46.646 65.612  28.152  1.00 72.87  ?  455 LEU C O   1 
ATOM   5872  C CB  . LEU B 2 123 ? -44.852 63.598  29.252  1.00 63.34  ?  455 LEU C CB  1 
ATOM   5873  C CG  . LEU B 2 123 ? -43.699 64.123  28.428  1.00 63.14  ?  455 LEU C CG  1 
ATOM   5874  C CD1 . LEU B 2 123 ? -42.600 64.423  29.359  1.00 63.56  ?  455 LEU C CD1 1 
ATOM   5875  C CD2 . LEU B 2 123 ? -43.243 63.088  27.485  1.00 74.30  ?  455 LEU C CD2 1 
ATOM   5876  N N   . PHE B 2 124 ? -46.862 64.208  26.421  1.00 61.94  ?  456 PHE C N   1 
ATOM   5877  C CA  . PHE B 2 124 ? -47.200 65.287  25.493  1.00 63.01  ?  456 PHE C CA  1 
ATOM   5878  C C   . PHE B 2 124 ? -48.481 64.958  24.726  1.00 63.92  ?  456 PHE C C   1 
ATOM   5879  O O   . PHE B 2 124 ? -48.659 63.830  24.239  1.00 67.48  ?  456 PHE C O   1 
ATOM   5880  C CB  . PHE B 2 124 ? -46.072 65.500  24.488  1.00 66.34  ?  456 PHE C CB  1 
ATOM   5881  C CG  . PHE B 2 124 ? -44.797 66.004  25.076  1.00 63.50  ?  456 PHE C CG  1 
ATOM   5882  C CD1 . PHE B 2 124 ? -44.799 66.759  26.213  1.00 66.38  ?  456 PHE C CD1 1 
ATOM   5883  C CD2 . PHE B 2 124 ? -43.585 65.694  24.471  1.00 64.58  ?  456 PHE C CD2 1 
ATOM   5884  C CE1 . PHE B 2 124 ? -43.625 67.194  26.743  1.00 70.06  ?  456 PHE C CE1 1 
ATOM   5885  C CE2 . PHE B 2 124 ? -42.405 66.127  24.989  1.00 65.73  ?  456 PHE C CE2 1 
ATOM   5886  C CZ  . PHE B 2 124 ? -42.419 66.873  26.130  1.00 67.15  ?  456 PHE C CZ  1 
ATOM   5887  N N   . ARG B 2 125 ? -49.357 65.934  24.567  1.00 66.22  ?  457 ARG C N   1 
ATOM   5888  C CA  . ARG B 2 125 ? -50.590 65.639  23.845  1.00 67.77  ?  457 ARG C CA  1 
ATOM   5889  C C   . ARG B 2 125 ? -51.282 66.952  23.568  1.00 70.20  ?  457 ARG C C   1 
ATOM   5890  O O   . ARG B 2 125 ? -51.231 67.873  24.391  1.00 67.69  ?  457 ARG C O   1 
ATOM   5891  C CB  . ARG B 2 125 ? -51.524 64.692  24.617  1.00 62.04  ?  457 ARG C CB  1 
ATOM   5892  C CG  . ARG B 2 125 ? -52.749 64.193  23.878  1.00 68.81  ?  457 ARG C CG  1 
ATOM   5893  C CD  . ARG B 2 125 ? -53.494 63.123  24.688  1.00 66.06  ?  457 ARG C CD  1 
ATOM   5894  N NE  . ARG B 2 125 ? -54.632 62.529  23.994  1.00 54.03  ?  457 ARG C NE  1 
ATOM   5895  C CZ  . ARG B 2 125 ? -55.864 62.992  24.077  1.00 63.09  ?  457 ARG C CZ  1 
ATOM   5896  N NH1 . ARG B 2 125 ? -56.165 64.001  24.873  1.00 65.71  ?  457 ARG C NH1 1 
ATOM   5897  N NH2 . ARG B 2 125 ? -56.817 62.440  23.332  1.00 72.57  ?  457 ARG C NH2 1 
ATOM   5898  N N   . LYS B 2 126 ? -51.905 67.040  22.398  1.00 69.52  ?  458 LYS C N   1 
ATOM   5899  C CA  . LYS B 2 126 ? -52.420 68.334  21.979  1.00 69.31  ?  458 LYS C CA  1 
ATOM   5900  C C   . LYS B 2 126 ? -53.458 68.877  22.967  1.00 65.40  ?  458 LYS C C   1 
ATOM   5901  O O   . LYS B 2 126 ? -53.596 70.097  23.102  1.00 67.66  ?  458 LYS C O   1 
ATOM   5902  C CB  . LYS B 2 126 ? -53.004 68.263  20.555  1.00 73.33  ?  458 LYS C CB  1 
ATOM   5903  C CG  . LYS B 2 126 ? -52.484 67.186  19.567  1.00 77.65  ?  458 LYS C CG  1 
ATOM   5904  C CD  . LYS B 2 126 ? -52.972 67.562  18.126  1.00 73.85  ?  458 LYS C CD  1 
ATOM   5905  C CE  . LYS B 2 126 ? -52.580 66.573  17.008  1.00 85.97  ?  458 LYS C CE  1 
ATOM   5906  N NZ  . LYS B 2 126 ? -51.111 66.489  16.734  1.00 107.60 ?  458 LYS C NZ  1 
ATOM   5907  N N   . SER B 2 127 ? -54.147 68.001  23.708  1.00 64.47  ?  459 SER C N   1 
ATOM   5908  C CA  . SER B 2 127 ? -55.324 68.380  24.487  1.00 64.35  ?  459 SER C CA  1 
ATOM   5909  C C   . SER B 2 127 ? -55.514 67.407  25.639  1.00 65.26  ?  459 SER C C   1 
ATOM   5910  O O   . SER B 2 127 ? -55.129 66.243  25.539  1.00 67.04  ?  459 SER C O   1 
ATOM   5911  C CB  . SER B 2 127 ? -56.577 68.348  23.626  1.00 74.07  ?  459 SER C CB  1 
ATOM   5912  O OG  . SER B 2 127 ? -56.678 67.089  22.962  1.00 77.79  ?  459 SER C OG  1 
ATOM   5913  N N   . ASN B 2 128 ? -56.164 67.875  26.705  1.00 64.91  ?  460 ASN C N   1 
ATOM   5914  C CA  . ASN B 2 128 ? -56.380 67.054  27.895  1.00 64.30  ?  460 ASN C CA  1 
ATOM   5915  C C   . ASN B 2 128 ? -57.394 65.954  27.599  1.00 68.64  ?  460 ASN C C   1 
ATOM   5916  O O   . ASN B 2 128 ? -58.273 66.089  26.736  1.00 67.28  ?  460 ASN C O   1 
ATOM   5917  C CB  . ASN B 2 128 ? -56.889 67.931  29.035  1.00 62.58  ?  460 ASN C CB  1 
ATOM   5918  C CG  . ASN B 2 128 ? -55.870 68.950  29.477  1.00 65.97  ?  460 ASN C CG  1 
ATOM   5919  O OD1 . ASN B 2 128 ? -55.490 68.989  30.644  1.00 69.72  ?  460 ASN C OD1 1 
ATOM   5920  N ND2 . ASN B 2 128 ? -55.317 69.701  28.517  1.00 67.78  ?  460 ASN C ND2 1 
ATOM   5921  N N   . LEU B 2 129 ? -57.284 64.859  28.340  1.00 68.37  ?  461 LEU C N   1 
ATOM   5922  C CA  . LEU B 2 129 ? -58.171 63.733  28.093  1.00 65.88  ?  461 LEU C CA  1 
ATOM   5923  C C   . LEU B 2 129 ? -59.556 64.021  28.662  1.00 72.11  ?  461 LEU C C   1 
ATOM   5924  O O   . LEU B 2 129 ? -59.702 64.713  29.670  1.00 78.14  ?  461 LEU C O   1 
ATOM   5925  C CB  . LEU B 2 129 ? -57.633 62.462  28.740  1.00 61.11  ?  461 LEU C CB  1 
ATOM   5926  C CG  . LEU B 2 129 ? -56.713 61.500  28.007  1.00 55.56  ?  461 LEU C CG  1 
ATOM   5927  C CD1 . LEU B 2 129 ? -56.651 60.205  28.786  1.00 57.61  ?  461 LEU C CD1 1 
ATOM   5928  C CD2 . LEU B 2 129 ? -57.154 61.257  26.610  1.00 53.97  ?  461 LEU C CD2 1 
ATOM   5929  N N   . LYS B 2 130 ? -60.577 63.473  28.012  1.00 80.45  ?  462 LYS C N   1 
ATOM   5930  C CA  . LYS B 2 130 ? -61.947 63.469  28.512  1.00 75.29  ?  462 LYS C CA  1 
ATOM   5931  C C   . LYS B 2 130 ? -62.129 62.280  29.458  1.00 72.51  ?  462 LYS C C   1 
ATOM   5932  O O   . LYS B 2 130 ? -61.503 61.237  29.254  1.00 73.16  ?  462 LYS C O   1 
ATOM   5933  C CB  . LYS B 2 130 ? -62.933 63.381  27.360  1.00 81.66  ?  462 LYS C CB  1 
ATOM   5934  C CG  . LYS B 2 130 ? -62.953 64.625  26.473  1.00 94.04  ?  462 LYS C CG  1 
ATOM   5935  C CD  . LYS B 2 130 ? -64.382 65.121  26.197  1.00 105.86 ?  462 LYS C CD  1 
ATOM   5936  C CE  . LYS B 2 130 ? -64.683 66.392  27.038  1.00 109.12 ?  462 LYS C CE  1 
ATOM   5937  N NZ  . LYS B 2 130 ? -65.887 67.173  26.596  1.00 110.73 ?  462 LYS C NZ  1 
ATOM   5938  N N   . PRO B 2 131 ? -62.954 62.397  30.506  1.00 65.14  ?  463 PRO C N   1 
ATOM   5939  C CA  . PRO B 2 131 ? -62.988 61.342  31.522  1.00 61.63  ?  463 PRO C CA  1 
ATOM   5940  C C   . PRO B 2 131 ? -63.149 59.978  30.887  1.00 60.96  ?  463 PRO C C   1 
ATOM   5941  O O   . PRO B 2 131 ? -63.901 59.801  29.929  1.00 67.34  ?  463 PRO C O   1 
ATOM   5942  C CB  . PRO B 2 131 ? -64.190 61.724  32.394  1.00 57.55  ?  463 PRO C CB  1 
ATOM   5943  C CG  . PRO B 2 131 ? -64.188 63.145  32.352  1.00 58.71  ?  463 PRO C CG  1 
ATOM   5944  C CD  . PRO B 2 131 ? -63.695 63.575  30.966  1.00 68.83  ?  463 PRO C CD  1 
ATOM   5945  N N   . PHE B 2 132 ? -62.334 59.051  31.340  1.00 57.05  ?  464 PHE C N   1 
ATOM   5946  C CA  . PHE B 2 132 ? -62.415 57.657  31.000  1.00 57.89  ?  464 PHE C CA  1 
ATOM   5947  C C   . PHE B 2 132 ? -62.023 57.398  29.541  1.00 60.28  ?  464 PHE C C   1 
ATOM   5948  O O   . PHE B 2 132 ? -62.244 56.286  29.039  1.00 57.01  ?  464 PHE C O   1 
ATOM   5949  C CB  . PHE B 2 132 ? -63.813 57.142  31.299  1.00 58.82  ?  464 PHE C CB  1 
ATOM   5950  C CG  . PHE B 2 132 ? -63.958 56.687  32.696  1.00 58.75  ?  464 PHE C CG  1 
ATOM   5951  C CD1 . PHE B 2 132 ? -63.155 55.709  33.208  1.00 62.39  ?  464 PHE C CD1 1 
ATOM   5952  C CD2 . PHE B 2 132 ? -64.873 57.282  33.524  1.00 62.21  ?  464 PHE C CD2 1 
ATOM   5953  C CE1 . PHE B 2 132 ? -63.286 55.326  34.522  1.00 66.71  ?  464 PHE C CE1 1 
ATOM   5954  C CE2 . PHE B 2 132 ? -65.017 56.893  34.825  1.00 66.15  ?  464 PHE C CE2 1 
ATOM   5955  C CZ  . PHE B 2 132 ? -64.238 55.928  35.331  1.00 65.62  ?  464 PHE C CZ  1 
ATOM   5956  N N   . GLU B 2 133 ? -61.434 58.382  28.856  1.00 56.37  ?  465 GLU C N   1 
ATOM   5957  C CA  . GLU B 2 133 ? -60.814 58.219  27.539  1.00 54.84  ?  465 GLU C CA  1 
ATOM   5958  C C   . GLU B 2 133 ? -59.479 57.467  27.669  1.00 58.60  ?  465 GLU C C   1 
ATOM   5959  O O   . GLU B 2 133 ? -58.867 57.394  28.756  1.00 58.42  ?  465 GLU C O   1 
ATOM   5960  C CB  . GLU B 2 133 ? -60.543 59.588  26.922  1.00 59.49  ?  465 GLU C CB  1 
ATOM   5961  C CG  . GLU B 2 133 ? -60.838 59.786  25.417  1.00 66.50  ?  465 GLU C CG  1 
ATOM   5962  C CD  . GLU B 2 133 ? -60.123 61.008  24.762  1.00 65.24  ?  465 GLU C CD  1 
ATOM   5963  O OE1 . GLU B 2 133 ? -60.525 62.177  25.064  1.00 62.93  ?  465 GLU C OE1 1 
ATOM   5964  O OE2 . GLU B 2 133 ? -59.298 60.799  23.832  1.00 58.08  -1 465 GLU C OE2 1 
ATOM   5965  N N   . ARG B 2 134 ? -59.030 56.894  26.546  1.00 56.49  ?  466 ARG C N   1 
ATOM   5966  C CA  . ARG B 2 134 ? -57.723 56.230  26.439  1.00 57.43  ?  466 ARG C CA  1 
ATOM   5967  C C   . ARG B 2 134 ? -57.073 56.625  25.127  1.00 60.72  ?  466 ARG C C   1 
ATOM   5968  O O   . ARG B 2 134 ? -57.654 56.404  24.058  1.00 65.37  ?  466 ARG C O   1 
ATOM   5969  C CB  . ARG B 2 134 ? -57.802 54.701  26.528  1.00 53.11  ?  466 ARG C CB  1 
ATOM   5970  C CG  . ARG B 2 134 ? -56.586 54.057  27.144  1.00 52.21  ?  466 ARG C CG  1 
ATOM   5971  C CD  . ARG B 2 134 ? -56.565 52.549  26.854  1.00 51.37  ?  466 ARG C CD  1 
ATOM   5972  N NE  . ARG B 2 134 ? -57.686 51.880  27.497  1.00 50.13  ?  466 ARG C NE  1 
ATOM   5973  C CZ  . ARG B 2 134 ? -58.740 51.390  26.865  1.00 62.68  ?  466 ARG C CZ  1 
ATOM   5974  N NH1 . ARG B 2 134 ? -58.862 51.477  25.541  1.00 75.21  ?  466 ARG C NH1 1 
ATOM   5975  N NH2 . ARG B 2 134 ? -59.736 50.865  27.583  1.00 70.93  ?  466 ARG C NH2 1 
ATOM   5976  N N   . ASP B 2 135 ? -55.881 57.212  25.226  1.00 60.38  ?  467 ASP C N   1 
ATOM   5977  C CA  . ASP B 2 135 ? -55.038 57.523  24.082  1.00 59.07  ?  467 ASP C CA  1 
ATOM   5978  C C   . ASP B 2 135 ? -53.871 56.573  24.064  1.00 61.05  ?  467 ASP C C   1 
ATOM   5979  O O   . ASP B 2 135 ? -53.052 56.570  24.987  1.00 58.09  ?  467 ASP C O   1 
ATOM   5980  C CB  . ASP B 2 135 ? -54.506 58.946  24.103  1.00 59.92  ?  467 ASP C CB  1 
ATOM   5981  C CG  . ASP B 2 135 ? -54.386 59.521  22.717  1.00 66.16  ?  467 ASP C CG  1 
ATOM   5982  O OD1 . ASP B 2 135 ? -55.215 59.172  21.837  1.00 81.56  ?  467 ASP C OD1 1 
ATOM   5983  O OD2 . ASP B 2 135 ? -53.410 60.266  22.487  1.00 62.62  -1 467 ASP C OD2 1 
ATOM   5984  N N   . ILE B 2 136 ? -53.774 55.816  22.988  1.00 59.53  ?  468 ILE C N   1 
ATOM   5985  C CA  . ILE B 2 136 ? -52.712 54.844  22.846  1.00 56.35  ?  468 ILE C CA  1 
ATOM   5986  C C   . ILE B 2 136 ? -51.967 55.193  21.574  1.00 52.10  ?  468 ILE C C   1 
ATOM   5987  O O   . ILE B 2 136 ? -51.342 54.330  20.955  1.00 52.72  ?  468 ILE C O   1 
ATOM   5988  C CB  . ILE B 2 136 ? -53.262 53.412  22.815  1.00 52.84  ?  468 ILE C CB  1 
ATOM   5989  C CG1 . ILE B 2 136 ? -54.409 53.296  21.823  1.00 55.13  ?  468 ILE C CG1 1 
ATOM   5990  C CG2 . ILE B 2 136 ? -53.790 53.029  24.183  1.00 52.82  ?  468 ILE C CG2 1 
ATOM   5991  C CD1 . ILE B 2 136 ? -54.508 51.910  21.256  1.00 61.72  ?  468 ILE C CD1 1 
ATOM   5992  N N   . SER B 2 137 ? -51.993 56.463  21.203  1.00 55.14  ?  469 SER C N   1 
ATOM   5993  C CA  . SER B 2 137 ? -51.466 56.901  19.923  1.00 54.06  ?  469 SER C CA  1 
ATOM   5994  C C   . SER B 2 137 ? -49.990 57.295  20.009  1.00 58.11  ?  469 SER C C   1 
ATOM   5995  O O   . SER B 2 137 ? -49.590 58.126  20.824  1.00 63.20  ?  469 SER C O   1 
ATOM   5996  C CB  . SER B 2 137 ? -52.333 58.044  19.404  1.00 60.87  ?  469 SER C CB  1 
ATOM   5997  O OG  . SER B 2 137 ? -51.878 59.326  19.809  1.00 57.04  ?  469 SER C OG  1 
ATOM   5998  N N   . THR B 2 138 ? -49.178 56.715  19.151  1.00 54.58  ?  470 THR C N   1 
ATOM   5999  C CA  . THR B 2 138 ? -47.754 57.003  19.199  1.00 59.27  ?  470 THR C CA  1 
ATOM   6000  C C   . THR B 2 138 ? -47.376 57.983  18.080  1.00 62.07  ?  470 THR C C   1 
ATOM   6001  O O   . THR B 2 138 ? -46.429 57.806  17.302  1.00 69.63  ?  470 THR C O   1 
ATOM   6002  C CB  . THR B 2 138 ? -46.965 55.704  19.114  1.00 59.95  ?  470 THR C CB  1 
ATOM   6003  O OG1 . THR B 2 138 ? -47.054 55.211  17.782  1.00 64.84  ?  470 THR C OG1 1 
ATOM   6004  C CG2 . THR B 2 138 ? -47.548 54.663  20.034  1.00 56.34  ?  470 THR C CG2 1 
ATOM   6005  N N   . GLU B 2 139 ? -48.128 59.062  18.009  1.00 64.67  ?  471 GLU C N   1 
ATOM   6006  C CA  . GLU B 2 139 ? -47.922 60.057  16.968  1.00 62.34  ?  471 GLU C CA  1 
ATOM   6007  C C   . GLU B 2 139 ? -46.887 61.019  17.508  1.00 63.94  ?  471 GLU C C   1 
ATOM   6008  O O   . GLU B 2 139 ? -47.053 61.517  18.627  1.00 68.27  ?  471 GLU C O   1 
ATOM   6009  C CB  . GLU B 2 139 ? -49.243 60.777  16.700  1.00 67.42  ?  471 GLU C CB  1 
ATOM   6010  C CG  . GLU B 2 139 ? -49.420 61.568  15.415  1.00 68.83  ?  471 GLU C CG  1 
ATOM   6011  C CD  . GLU B 2 139 ? -50.313 62.769  15.576  1.00 76.43  ?  471 GLU C CD  1 
ATOM   6012  O OE1 . GLU B 2 139 ? -51.546 62.594  15.784  1.00 82.89  ?  471 GLU C OE1 1 
ATOM   6013  O OE2 . GLU B 2 139 ? -49.801 63.894  15.401  1.00 83.92  -1 471 GLU C OE2 1 
ATOM   6014  N N   . ILE B 2 140 ? -45.808 61.255  16.757  1.00 63.58  ?  472 ILE C N   1 
ATOM   6015  C CA  . ILE B 2 140 ? -44.758 62.177  17.222  1.00 63.28  ?  472 ILE C CA  1 
ATOM   6016  C C   . ILE B 2 140 ? -45.421 63.493  17.634  1.00 62.95  ?  472 ILE C C   1 
ATOM   6017  O O   . ILE B 2 140 ? -46.468 63.841  17.090  1.00 69.45  ?  472 ILE C O   1 
ATOM   6018  C CB  . ILE B 2 140 ? -43.727 62.420  16.109  1.00 63.28  ?  472 ILE C CB  1 
ATOM   6019  C CG1 . ILE B 2 140 ? -42.826 61.216  15.906  1.00 66.69  ?  472 ILE C CG1 1 
ATOM   6020  C CG2 . ILE B 2 140 ? -42.897 63.628  16.393  1.00 72.24  ?  472 ILE C CG2 1 
ATOM   6021  C CD1 . ILE B 2 140 ? -42.171 60.804  17.089  1.00 70.17  ?  472 ILE C CD1 1 
ATOM   6022  N N   . TYR B 2 141 ? -44.853 64.245  18.568  1.00 60.72  ?  473 TYR C N   1 
ATOM   6023  C CA  . TYR B 2 141 ? -45.495 65.486  19.004  1.00 60.03  ?  473 TYR C CA  1 
ATOM   6024  C C   . TYR B 2 141 ? -45.038 66.698  18.177  1.00 67.28  ?  473 TYR C C   1 
ATOM   6025  O O   . TYR B 2 141 ? -43.846 66.908  17.960  1.00 72.19  ?  473 TYR C O   1 
ATOM   6026  C CB  . TYR B 2 141 ? -45.245 65.737  20.485  1.00 62.21  ?  473 TYR C CB  1 
ATOM   6027  C CG  . TYR B 2 141 ? -46.073 66.854  21.058  1.00 59.18  ?  473 TYR C CG  1 
ATOM   6028  C CD1 . TYR B 2 141 ? -45.690 68.173  20.938  1.00 61.73  ?  473 TYR C CD1 1 
ATOM   6029  C CD2 . TYR B 2 141 ? -47.268 66.591  21.687  1.00 62.28  ?  473 TYR C CD2 1 
ATOM   6030  C CE1 . TYR B 2 141 ? -46.480 69.208  21.460  1.00 62.61  ?  473 TYR C CE1 1 
ATOM   6031  C CE2 . TYR B 2 141 ? -48.063 67.615  22.217  1.00 65.78  ?  473 TYR C CE2 1 
ATOM   6032  C CZ  . TYR B 2 141 ? -47.670 68.918  22.094  1.00 64.54  ?  473 TYR C CZ  1 
ATOM   6033  O OH  . TYR B 2 141 ? -48.468 69.916  22.613  1.00 68.59  ?  473 TYR C OH  1 
ATOM   6034  N N   . GLN B 2 142 ? -46.006 67.508  17.743  1.00 71.65  ?  474 GLN C N   1 
ATOM   6035  C CA  . GLN B 2 142 ? -45.808 68.687  16.885  1.00 71.12  ?  474 GLN C CA  1 
ATOM   6036  C C   . GLN B 2 142 ? -45.616 69.923  17.756  1.00 75.57  ?  474 GLN C C   1 
ATOM   6037  O O   . GLN B 2 142 ? -46.533 70.725  17.937  1.00 78.95  ?  474 GLN C O   1 
ATOM   6038  C CB  . GLN B 2 142 ? -47.037 68.843  15.982  1.00 91.43  ?  474 GLN C CB  1 
ATOM   6039  C CG  . GLN B 2 142 ? -47.155 70.036  14.977  1.00 94.76  ?  474 GLN C CG  1 
ATOM   6040  C CD  . GLN B 2 142 ? -46.454 69.825  13.664  1.00 97.63  ?  474 GLN C CD  1 
ATOM   6041  O OE1 . GLN B 2 142 ? -45.250 69.637  13.620  1.00 101.76 ?  474 GLN C OE1 1 
ATOM   6042  N NE2 . GLN B 2 142 ? -47.226 69.789  12.586  1.00 107.16 ?  474 GLN C NE2 1 
ATOM   6043  N N   . ALA B 2 143 ? -44.397 70.107  18.290  1.00 84.27  ?  475 ALA C N   1 
ATOM   6044  C CA  . ALA B 2 143 ? -44.154 71.223  19.211  1.00 81.81  ?  475 ALA C CA  1 
ATOM   6045  C C   . ALA B 2 143 ? -43.761 72.523  18.505  1.00 86.16  ?  475 ALA C C   1 
ATOM   6046  O O   . ALA B 2 143 ? -44.190 73.606  18.917  1.00 86.81  ?  475 ALA C O   1 
ATOM   6047  C CB  . ALA B 2 143 ? -43.088 70.852  20.241  1.00 79.31  ?  475 ALA C CB  1 
ATOM   6048  N N   . GLY B 2 144 ? -42.942 72.445  17.463  1.00 77.04  ?  476 GLY C N   1 
ATOM   6049  C CA  . GLY B 2 144 ? -42.742 73.586  16.599  1.00 94.15  ?  476 GLY C CA  1 
ATOM   6050  C C   . GLY B 2 144 ? -43.597 73.465  15.363  1.00 114.80 ?  476 GLY C C   1 
ATOM   6051  O O   . GLY B 2 144 ? -44.027 72.374  15.011  1.00 116.24 ?  476 GLY C O   1 
ATOM   6052  N N   . ASN B 2 145 ? -43.851 74.581  14.679  1.00 138.91 ?  477 ASN C N   1 
ATOM   6053  C CA  . ASN B 2 145 ? -44.839 74.482  13.615  1.00 147.08 ?  477 ASN C CA  1 
ATOM   6054  C C   . ASN B 2 145 ? -44.341 73.684  12.402  1.00 144.26 ?  477 ASN C C   1 
ATOM   6055  O O   . ASN B 2 145 ? -45.168 73.219  11.603  1.00 151.56 ?  477 ASN C O   1 
ATOM   6056  C CB  . ASN B 2 145 ? -45.286 75.848  13.147  1.00 150.05 ?  477 ASN C CB  1 
ATOM   6057  C CG  . ASN B 2 145 ? -46.586 75.759  12.369  1.00 168.47 ?  477 ASN C CG  1 
ATOM   6058  O OD1 . ASN B 2 145 ? -46.578 75.722  11.141  1.00 170.38 ?  477 ASN C OD1 1 
ATOM   6059  N ND2 . ASN B 2 145 ? -47.714 75.739  13.079  1.00 165.45 ?  477 ASN C ND2 1 
ATOM   6060  N N   . LYS B 2 146 ? -43.035 73.522  12.245  1.00 118.90 ?  478 LYS C N   1 
ATOM   6061  C CA  . LYS B 2 146 ? -42.489 72.735  11.136  1.00 113.76 ?  478 LYS C CA  1 
ATOM   6062  C C   . LYS B 2 146 ? -43.047 71.311  11.179  1.00 114.46 ?  478 LYS C C   1 
ATOM   6063  O O   . LYS B 2 146 ? -43.266 70.766  12.261  1.00 116.44 ?  478 LYS C O   1 
ATOM   6064  C CB  . LYS B 2 146 ? -40.972 72.685  11.257  1.00 111.80 ?  478 LYS C CB  1 
ATOM   6065  C CG  . LYS B 2 146 ? -40.290 74.032  11.055  1.00 109.15 ?  478 LYS C CG  1 
ATOM   6066  C CD  . LYS B 2 146 ? -38.877 73.892  10.521  1.00 95.82  ?  478 LYS C CD  1 
ATOM   6067  C CE  . LYS B 2 146 ? -38.393 75.198  9.932   1.00 83.87  ?  478 LYS C CE  1 
ATOM   6068  N NZ  . LYS B 2 146 ? -37.660 74.986  8.669   1.00 85.07  ?  478 LYS C NZ  1 
ATOM   6069  N N   . PRO B 2 147 ? -43.445 70.731  10.026  1.00 114.41 ?  479 PRO C N   1 
ATOM   6070  C CA  . PRO B 2 147 ? -44.087 69.432  10.026  1.00 109.51 ?  479 PRO C CA  1 
ATOM   6071  C C   . PRO B 2 147 ? -43.030 68.352  10.245  1.00 112.14 ?  479 PRO C C   1 
ATOM   6072  O O   . PRO B 2 147 ? -42.104 68.281  9.478   1.00 112.62 ?  479 PRO C O   1 
ATOM   6073  C CB  . PRO B 2 147 ? -44.660 69.290  8.612   1.00 108.52 ?  479 PRO C CB  1 
ATOM   6074  C CG  . PRO B 2 147 ? -44.497 70.647  7.961   1.00 117.05 ?  479 PRO C CG  1 
ATOM   6075  C CD  . PRO B 2 147 ? -43.308 71.259  8.661   1.00 121.89 ?  479 PRO C CD  1 
ATOM   6076  N N   . CYS B 2 148 ? -43.196 67.559  11.298  1.00 123.60 ?  480 CYS C N   1 
ATOM   6077  C CA  . CYS B 2 148 ? -42.261 66.433  11.519  1.00 119.48 ?  480 CYS C CA  1 
ATOM   6078  C C   . CYS B 2 148 ? -42.897 65.189  10.914  1.00 116.94 ?  480 CYS C C   1 
ATOM   6079  O O   . CYS B 2 148 ? -44.005 64.825  11.342  1.00 120.80 ?  480 CYS C O   1 
ATOM   6080  C CB  . CYS B 2 148 ? -41.956 66.262  12.999  1.00 118.52 ?  480 CYS C CB  1 
ATOM   6081  S SG  . CYS B 2 148 ? -40.387 67.055  13.443  1.00 152.35 ?  480 CYS C SG  1 
ATOM   6082  N N   . ASN B 2 149 ? -42.235 64.600  9.928   1.00 109.08 ?  481 ASN C N   1 
ATOM   6083  C CA  . ASN B 2 149 ? -42.840 63.464  9.198   1.00 104.62 ?  481 ASN C CA  1 
ATOM   6084  C C   . ASN B 2 149 ? -42.277 62.174  9.765   1.00 91.84  ?  481 ASN C C   1 
ATOM   6085  O O   . ASN B 2 149 ? -41.436 61.556  9.100   1.00 88.83  ?  481 ASN C O   1 
ATOM   6086  C CB  . ASN B 2 149 ? -42.557 63.593  7.705   1.00 105.39 ?  481 ASN C CB  1 
ATOM   6087  C CG  . ASN B 2 149 ? -43.129 64.868  7.126   1.00 113.27 ?  481 ASN C CG  1 
ATOM   6088  O OD1 . ASN B 2 149 ? -42.743 65.971  7.513   1.00 114.55 ?  481 ASN C OD1 1 
ATOM   6089  N ND2 . ASN B 2 149 ? -44.057 64.722  6.195   1.00 113.75 ?  481 ASN C ND2 1 
ATOM   6090  N N   . GLY B 2 150 ? -42.726 61.811  10.958  1.00 94.44  ?  482 GLY C N   1 
ATOM   6091  C CA  . GLY B 2 150 ? -42.178 60.614  11.610  1.00 92.80  ?  482 GLY C CA  1 
ATOM   6092  C C   . GLY B 2 150 ? -40.742 60.872  11.991  1.00 100.06 ?  482 GLY C C   1 
ATOM   6093  O O   . GLY B 2 150 ? -40.012 59.901  12.233  1.00 93.87  ?  482 GLY C O   1 
ATOM   6094  N N   . VAL B 2 151 ? -40.359 62.148  12.036  1.00 113.87 ?  483 VAL C N   1 
ATOM   6095  C CA  . VAL B 2 151 ? -38.956 62.517  12.364  1.00 102.37 ?  483 VAL C CA  1 
ATOM   6096  C C   . VAL B 2 151 ? -38.884 62.885  13.837  1.00 100.29 ?  483 VAL C C   1 
ATOM   6097  O O   . VAL B 2 151 ? -39.430 63.933  14.212  1.00 107.93 ?  483 VAL C O   1 
ATOM   6098  C CB  . VAL B 2 151 ? -38.465 63.681  11.493  1.00 105.26 ?  483 VAL C CB  1 
ATOM   6099  C CG1 . VAL B 2 151 ? -37.120 64.204  11.970  1.00 100.35 ?  483 VAL C CG1 1 
ATOM   6100  C CG2 . VAL B 2 151 ? -38.408 63.296  10.025  1.00 118.44 ?  483 VAL C CG2 1 
ATOM   6101  N N   . ALA B 2 152 ? -38.257 62.031  14.633  1.00 89.36  ?  484 ALA C N   1 
ATOM   6102  C CA  . ALA B 2 152 ? -38.064 62.310  16.047  1.00 87.41  ?  484 ALA C CA  1 
ATOM   6103  C C   . ALA B 2 152 ? -36.850 63.225  16.130  1.00 91.33  ?  484 ALA C C   1 
ATOM   6104  O O   . ALA B 2 152 ? -35.736 62.828  15.766  1.00 91.50  ?  484 ALA C O   1 
ATOM   6105  C CB  . ALA B 2 152 ? -37.896 61.021  16.837  1.00 77.12  ?  484 ALA C CB  1 
ATOM   6106  N N   . GLY B 2 153 ? -37.071 64.470  16.543  1.00 92.69  ?  485 GLY C N   1 
ATOM   6107  C CA  . GLY B 2 153 ? -36.070 65.496  16.297  1.00 92.89  ?  485 GLY C CA  1 
ATOM   6108  C C   . GLY B 2 153 ? -36.321 66.800  17.019  1.00 89.60  ?  485 GLY C C   1 
ATOM   6109  O O   . GLY B 2 153 ? -36.724 66.768  18.191  1.00 90.86  ?  485 GLY C O   1 
ATOM   6110  N N   . VAL B 2 154 ? -36.074 67.949  16.368  1.00 78.53  ?  486 VAL C N   1 
ATOM   6111  C CA  . VAL B 2 154 ? -36.317 69.193  17.081  1.00 78.04  ?  486 VAL C CA  1 
ATOM   6112  C C   . VAL B 2 154 ? -37.799 69.447  17.138  1.00 82.96  ?  486 VAL C C   1 
ATOM   6113  O O   . VAL B 2 154 ? -38.533 69.205  16.179  1.00 86.05  ?  486 VAL C O   1 
ATOM   6114  C CB  . VAL B 2 154 ? -35.644 70.422  16.469  1.00 63.82  ?  486 VAL C CB  1 
ATOM   6115  C CG1 . VAL B 2 154 ? -34.220 70.142  16.103  1.00 59.85  ?  486 VAL C CG1 1 
ATOM   6116  C CG2 . VAL B 2 154 ? -36.481 70.978  15.384  1.00 74.01  ?  486 VAL C CG2 1 
ATOM   6117  N N   . ASN B 2 155 ? -38.234 69.930  18.289  1.00 78.45  ?  487 ASN C N   1 
ATOM   6118  C CA  . ASN B 2 155 ? -39.606 70.322  18.522  1.00 80.83  ?  487 ASN C CA  1 
ATOM   6119  C C   . ASN B 2 155 ? -40.582 69.178  18.168  1.00 72.71  ?  487 ASN C C   1 
ATOM   6120  O O   . ASN B 2 155 ? -41.744 69.407  17.848  1.00 78.71  ?  487 ASN C O   1 
ATOM   6121  C CB  . ASN B 2 155 ? -39.850 71.626  17.757  1.00 86.29  ?  487 ASN C CB  1 
ATOM   6122  C CG  . ASN B 2 155 ? -39.261 72.832  18.498  1.00 87.33  ?  487 ASN C CG  1 
ATOM   6123  O OD1 . ASN B 2 155 ? -39.234 72.871  19.730  1.00 89.66  ?  487 ASN C OD1 1 
ATOM   6124  N ND2 . ASN B 2 155 ? -38.735 73.778  17.746  1.00 89.58  ?  487 ASN C ND2 1 
ATOM   6125  N N   . CYS B 2 156 ? -40.105 67.928  18.296  1.00 70.16  ?  488 CYS C N   1 
ATOM   6126  C CA  . CYS B 2 156 ? -40.701 66.727  17.707  1.00 72.93  ?  488 CYS C CA  1 
ATOM   6127  C C   . CYS B 2 156 ? -40.334 65.502  18.549  1.00 74.08  ?  488 CYS C C   1 
ATOM   6128  O O   . CYS B 2 156 ? -39.279 64.884  18.335  1.00 78.71  ?  488 CYS C O   1 
ATOM   6129  C CB  . CYS B 2 156 ? -40.195 66.571  16.291  1.00 79.84  ?  488 CYS C CB  1 
ATOM   6130  S SG  . CYS B 2 156 ? -40.755 67.881  15.243  1.00 102.30 ?  488 CYS C SG  1 
ATOM   6131  N N   . TYR B 2 157 ? -41.209 65.133  19.484  1.00 62.62  ?  489 TYR C N   1 
ATOM   6132  C CA  . TYR B 2 157 ? -40.759 64.181  20.497  1.00 68.77  ?  489 TYR C CA  1 
ATOM   6133  C C   . TYR B 2 157 ? -41.706 62.994  20.580  1.00 63.97  ?  489 TYR C C   1 
ATOM   6134  O O   . TYR B 2 157 ? -42.920 63.180  20.687  1.00 64.31  ?  489 TYR C O   1 
ATOM   6135  C CB  . TYR B 2 157 ? -40.591 64.827  21.902  1.00 64.51  ?  489 TYR C CB  1 
ATOM   6136  C CG  . TYR B 2 157 ? -40.062 66.246  21.859  1.00 65.20  ?  489 TYR C CG  1 
ATOM   6137  C CD1 . TYR B 2 157 ? -38.731 66.499  21.561  1.00 63.35  ?  489 TYR C CD1 1 
ATOM   6138  C CD2 . TYR B 2 157 ? -40.873 67.328  22.217  1.00 64.84  ?  489 TYR C CD2 1 
ATOM   6139  C CE1 . TYR B 2 157 ? -38.233 67.812  21.520  1.00 68.55  ?  489 TYR C CE1 1 
ATOM   6140  C CE2 . TYR B 2 157 ? -40.388 68.638  22.200  1.00 65.31  ?  489 TYR C CE2 1 
ATOM   6141  C CZ  . TYR B 2 157 ? -39.067 68.881  21.860  1.00 68.64  ?  489 TYR C CZ  1 
ATOM   6142  O OH  . TYR B 2 157 ? -38.594 70.188  21.844  1.00 65.97  ?  489 TYR C OH  1 
ATOM   6143  N N   . PHE B 2 158 ? -41.138 61.767  20.502  1.00 58.75  ?  490 PHE C N   1 
ATOM   6144  C CA  . PHE B 2 158 ? -41.909 60.580  20.835  1.00 58.09  ?  490 PHE C CA  1 
ATOM   6145  C C   . PHE B 2 158 ? -42.711 60.810  22.109  1.00 59.92  ?  490 PHE C C   1 
ATOM   6146  O O   . PHE B 2 158 ? -42.149 60.989  23.178  1.00 60.09  ?  490 PHE C O   1 
ATOM   6147  C CB  . PHE B 2 158 ? -41.010 59.375  20.987  1.00 53.83  ?  490 PHE C CB  1 
ATOM   6148  C CG  . PHE B 2 158 ? -41.751 58.080  20.984  1.00 60.65  ?  490 PHE C CG  1 
ATOM   6149  C CD1 . PHE B 2 158 ? -42.772 57.843  20.106  1.00 65.73  ?  490 PHE C CD1 1 
ATOM   6150  C CD2 . PHE B 2 158 ? -41.498 57.127  21.963  1.00 67.87  ?  490 PHE C CD2 1 
ATOM   6151  C CE1 . PHE B 2 158 ? -43.490 56.627  20.144  1.00 68.43  ?  490 PHE C CE1 1 
ATOM   6152  C CE2 . PHE B 2 158 ? -42.199 55.924  22.009  1.00 72.61  ?  490 PHE C CE2 1 
ATOM   6153  C CZ  . PHE B 2 158 ? -43.196 55.672  21.100  1.00 71.09  ?  490 PHE C CZ  1 
ATOM   6154  N N   . PRO B 2 159 ? -44.032 60.803  22.045  1.00 59.02  ?  491 PRO C N   1 
ATOM   6155  C CA  . PRO B 2 159 ? -44.819 61.376  23.134  1.00 61.47  ?  491 PRO C CA  1 
ATOM   6156  C C   . PRO B 2 159 ? -44.864 60.529  24.396  1.00 62.12  ?  491 PRO C C   1 
ATOM   6157  O O   . PRO B 2 159 ? -45.378 61.013  25.423  1.00 63.03  ?  491 PRO C O   1 
ATOM   6158  C CB  . PRO B 2 159 ? -46.211 61.512  22.511  1.00 66.57  ?  491 PRO C CB  1 
ATOM   6159  C CG  . PRO B 2 159 ? -46.233 60.470  21.452  1.00 64.81  ?  491 PRO C CG  1 
ATOM   6160  C CD  . PRO B 2 159 ? -44.853 60.414  20.901  1.00 59.38  ?  491 PRO C CD  1 
ATOM   6161  N N   . LEU B 2 160 ? -44.359 59.300  24.380  1.00 60.60  ?  492 LEU C N   1 
ATOM   6162  C CA  . LEU B 2 160 ? -44.372 58.470  25.577  1.00 63.76  ?  492 LEU C CA  1 
ATOM   6163  C C   . LEU B 2 160 ? -43.007 58.453  26.250  1.00 67.19  ?  492 LEU C C   1 
ATOM   6164  O O   . LEU B 2 160 ? -41.972 58.371  25.593  1.00 72.34  ?  492 LEU C O   1 
ATOM   6165  C CB  . LEU B 2 160 ? -44.837 57.050  25.259  1.00 63.60  ?  492 LEU C CB  1 
ATOM   6166  C CG  . LEU B 2 160 ? -46.338 56.948  25.021  1.00 56.17  ?  492 LEU C CG  1 
ATOM   6167  C CD1 . LEU B 2 160 ? -46.443 57.161  23.603  1.00 66.04  ?  492 LEU C CD1 1 
ATOM   6168  C CD2 . LEU B 2 160 ? -46.847 55.578  25.285  1.00 49.85  ?  492 LEU C CD2 1 
ATOM   6169  N N   . GLN B 2 161 ? -43.017 58.587  27.564  1.00 68.06  ?  493 GLN C N   1 
ATOM   6170  C CA  . GLN B 2 161 ? -41.829 58.427  28.380  1.00 67.18  ?  493 GLN C CA  1 
ATOM   6171  C C   . GLN B 2 161 ? -41.988 57.198  29.250  1.00 65.94  ?  493 GLN C C   1 
ATOM   6172  O O   . GLN B 2 161 ? -43.105 56.777  29.567  1.00 59.45  ?  493 GLN C O   1 
ATOM   6173  C CB  . GLN B 2 161 ? -41.575 59.619  29.296  1.00 68.48  ?  493 GLN C CB  1 
ATOM   6174  C CG  . GLN B 2 161 ? -40.151 59.729  29.762  1.00 78.50  ?  493 GLN C CG  1 
ATOM   6175  C CD  . GLN B 2 161 ? -39.274 60.391  28.737  1.00 90.34  ?  493 GLN C CD  1 
ATOM   6176  O OE1 . GLN B 2 161 ? -39.711 60.645  27.580  1.00 83.70  ?  493 GLN C OE1 1 
ATOM   6177  N NE2 . GLN B 2 161 ? -38.001 60.640  29.125  1.00 85.48  ?  493 GLN C NE2 1 
ATOM   6178  N N   . SER B 2 162 ? -40.859 56.622  29.632  1.00 64.93  ?  494 SER C N   1 
ATOM   6179  C CA  . SER B 2 162 ? -40.872 55.433  30.461  1.00 59.70  ?  494 SER C CA  1 
ATOM   6180  C C   . SER B 2 162 ? -40.364 55.789  31.837  1.00 59.45  ?  494 SER C C   1 
ATOM   6181  O O   . SER B 2 162 ? -39.392 56.545  31.972  1.00 59.86  ?  494 SER C O   1 
ATOM   6182  C CB  . SER B 2 162 ? -40.066 54.292  29.853  1.00 62.95  ?  494 SER C CB  1 
ATOM   6183  O OG  . SER B 2 162 ? -38.848 54.730  29.308  1.00 62.83  ?  494 SER C OG  1 
ATOM   6184  N N   . TYR B 2 163 ? -41.075 55.289  32.852  1.00 63.33  ?  495 TYR C N   1 
ATOM   6185  C CA  . TYR B 2 163 ? -40.649 55.528  34.213  1.00 60.45  ?  495 TYR C CA  1 
ATOM   6186  C C   . TYR B 2 163 ? -39.348 54.763  34.355  1.00 66.35  ?  495 TYR C C   1 
ATOM   6187  O O   . TYR B 2 163 ? -39.227 53.643  33.856  1.00 69.39  ?  495 TYR C O   1 
ATOM   6188  C CB  . TYR B 2 163 ? -41.636 55.039  35.277  1.00 56.39  ?  495 TYR C CB  1 
ATOM   6189  C CG  . TYR B 2 163 ? -43.073 55.540  35.241  1.00 54.53  ?  495 TYR C CG  1 
ATOM   6190  C CD1 . TYR B 2 163 ? -43.495 56.508  34.396  1.00 56.19  ?  495 TYR C CD1 1 
ATOM   6191  C CD2 . TYR B 2 163 ? -43.867 55.388  36.360  1.00 59.51  ?  495 TYR C CD2 1 
ATOM   6192  C CE1 . TYR B 2 163 ? -44.781 56.974  34.459  1.00 56.53  ?  495 TYR C CE1 1 
ATOM   6193  C CE2 . TYR B 2 163 ? -45.133 55.971  36.471  1.00 55.67  ?  495 TYR C CE2 1 
ATOM   6194  C CZ  . TYR B 2 163 ? -45.563 56.796  35.496  1.00 52.64  ?  495 TYR C CZ  1 
ATOM   6195  O OH  . TYR B 2 163 ? -46.802 57.409  35.512  1.00 56.83  ?  495 TYR C OH  1 
ATOM   6196  N N   . GLY B 2 164 ? -38.350 55.380  34.977  1.00 78.56  ?  496 GLY C N   1 
ATOM   6197  C CA  . GLY B 2 164 ? -37.068 54.691  35.008  1.00 80.18  ?  496 GLY C CA  1 
ATOM   6198  C C   . GLY B 2 164 ? -36.962 53.663  36.120  1.00 81.79  ?  496 GLY C C   1 
ATOM   6199  O O   . GLY B 2 164 ? -35.937 53.640  36.802  1.00 89.81  ?  496 GLY C O   1 
ATOM   6200  N N   . PHE B 2 165 ? -37.985 52.816  36.316  1.00 65.72  ?  497 PHE C N   1 
ATOM   6201  C CA  . PHE B 2 165 ? -38.237 52.247  37.639  1.00 61.10  ?  497 PHE C CA  1 
ATOM   6202  C C   . PHE B 2 165 ? -37.081 51.381  38.117  1.00 67.37  ?  497 PHE C C   1 
ATOM   6203  O O   . PHE B 2 165 ? -36.643 50.472  37.414  1.00 71.55  ?  497 PHE C O   1 
ATOM   6204  C CB  . PHE B 2 165 ? -39.502 51.412  37.661  1.00 61.83  ?  497 PHE C CB  1 
ATOM   6205  C CG  . PHE B 2 165 ? -40.773 52.204  37.899  1.00 60.04  ?  497 PHE C CG  1 
ATOM   6206  C CD1 . PHE B 2 165 ? -40.838 53.143  38.901  1.00 57.74  ?  497 PHE C CD1 1 
ATOM   6207  C CD2 . PHE B 2 165 ? -41.962 51.856  37.251  1.00 56.58  ?  497 PHE C CD2 1 
ATOM   6208  C CE1 . PHE B 2 165 ? -42.012 53.820  39.161  1.00 51.37  ?  497 PHE C CE1 1 
ATOM   6209  C CE2 . PHE B 2 165 ? -43.132 52.501  37.521  1.00 50.55  ?  497 PHE C CE2 1 
ATOM   6210  C CZ  . PHE B 2 165 ? -43.149 53.477  38.498  1.00 52.42  ?  497 PHE C CZ  1 
ATOM   6211  N N   . ARG B 2 166 ? -36.617 51.660  39.347  1.00 61.82  ?  498 ARG C N   1 
ATOM   6212  C CA  . ARG B 2 166 ? -35.381 51.147  40.010  1.00 58.78  ?  498 ARG C CA  1 
ATOM   6213  C C   . ARG B 2 166 ? -35.591 51.010  41.516  1.00 55.41  ?  498 ARG C C   1 
ATOM   6214  O O   . ARG B 2 166 ? -35.904 52.018  42.169  1.00 55.82  ?  498 ARG C O   1 
ATOM   6215  C CB  . ARG B 2 166 ? -34.200 52.091  39.751  1.00 59.63  ?  498 ARG C CB  1 
ATOM   6216  C CG  . ARG B 2 166 ? -33.423 51.897  38.444  1.00 64.50  ?  498 ARG C CG  1 
ATOM   6217  C CD  . ARG B 2 166 ? -32.332 52.965  38.261  1.00 62.06  ?  498 ARG C CD  1 
ATOM   6218  N NE  . ARG B 2 166 ? -32.453 53.644  36.975  1.00 69.47  ?  498 ARG C NE  1 
ATOM   6219  C CZ  . ARG B 2 166 ? -32.021 53.159  35.815  1.00 70.73  ?  498 ARG C CZ  1 
ATOM   6220  N NH1 . ARG B 2 166 ? -31.249 52.084  35.757  1.00 71.13  ?  498 ARG C NH1 1 
ATOM   6221  N NH2 . ARG B 2 166 ? -32.349 53.788  34.687  1.00 65.49  ?  498 ARG C NH2 1 
ATOM   6222  N N   . PRO B 2 167 ? -35.343 49.838  42.112  1.00 51.35  ?  499 PRO C N   1 
ATOM   6223  C CA  . PRO B 2 167 ? -35.828 49.589  43.485  1.00 49.86  ?  499 PRO C CA  1 
ATOM   6224  C C   . PRO B 2 167 ? -35.359 50.595  44.520  1.00 53.14  ?  499 PRO C C   1 
ATOM   6225  O O   . PRO B 2 167 ? -35.996 50.723  45.574  1.00 54.14  ?  499 PRO C O   1 
ATOM   6226  C CB  . PRO B 2 167 ? -35.287 48.188  43.791  1.00 47.87  ?  499 PRO C CB  1 
ATOM   6227  C CG  . PRO B 2 167 ? -34.145 48.023  42.894  1.00 51.46  ?  499 PRO C CG  1 
ATOM   6228  C CD  . PRO B 2 167 ? -34.517 48.729  41.629  1.00 51.64  ?  499 PRO C CD  1 
ATOM   6229  N N   . THR B 2 168 ? -34.278 51.329  44.239  1.00 56.13  ?  500 THR C N   1 
ATOM   6230  C CA  . THR B 2 168 ? -33.542 52.163  45.186  1.00 48.83  ?  500 THR C CA  1 
ATOM   6231  C C   . THR B 2 168 ? -34.000 53.637  45.160  1.00 52.15  ?  500 THR C C   1 
ATOM   6232  O O   . THR B 2 168 ? -33.306 54.508  45.700  1.00 51.58  ?  500 THR C O   1 
ATOM   6233  C CB  . THR B 2 168 ? -32.045 52.039  44.874  1.00 39.53  ?  500 THR C CB  1 
ATOM   6234  O OG1 . THR B 2 168 ? -31.685 52.924  43.811  1.00 40.40  ?  500 THR C OG1 1 
ATOM   6235  C CG2 . THR B 2 168 ? -31.728 50.649  44.385  1.00 41.94  ?  500 THR C CG2 1 
ATOM   6236  N N   . TYR B 2 169 ? -35.161 53.917  44.552  1.00 50.45  ?  501 TYR C N   1 
ATOM   6237  C CA  . TYR B 2 169 ? -35.727 55.239  44.326  1.00 47.35  ?  501 TYR C CA  1 
ATOM   6238  C C   . TYR B 2 169 ? -36.423 55.746  45.578  1.00 47.22  ?  501 TYR C C   1 
ATOM   6239  O O   . TYR B 2 169 ? -36.736 54.980  46.488  1.00 49.81  ?  501 TYR C O   1 
ATOM   6240  C CB  . TYR B 2 169 ? -36.728 55.172  43.190  1.00 48.33  ?  501 TYR C CB  1 
ATOM   6241  C CG  . TYR B 2 169 ? -36.142 55.403  41.825  1.00 49.42  ?  501 TYR C CG  1 
ATOM   6242  C CD1 . TYR B 2 169 ? -34.788 55.257  41.593  1.00 52.30  ?  501 TYR C CD1 1 
ATOM   6243  C CD2 . TYR B 2 169 ? -36.958 55.573  40.731  1.00 50.00  ?  501 TYR C CD2 1 
ATOM   6244  C CE1 . TYR B 2 169 ? -34.248 55.433  40.306  1.00 55.45  ?  501 TYR C CE1 1 
ATOM   6245  C CE2 . TYR B 2 169 ? -36.434 55.720  39.457  1.00 54.84  ?  501 TYR C CE2 1 
ATOM   6246  C CZ  . TYR B 2 169 ? -35.092 55.646  39.229  1.00 52.57  ?  501 TYR C CZ  1 
ATOM   6247  O OH  . TYR B 2 169 ? -34.649 55.803  37.912  1.00 51.19  ?  501 TYR C OH  1 
ATOM   6248  N N   . GLY B 2 170 ? -36.665 57.052  45.624  1.00 47.18  ?  502 GLY C N   1 
ATOM   6249  C CA  . GLY B 2 170 ? -37.519 57.587  46.664  1.00 47.81  ?  502 GLY C CA  1 
ATOM   6250  C C   . GLY B 2 170 ? -38.848 56.873  46.636  1.00 48.38  ?  502 GLY C C   1 
ATOM   6251  O O   . GLY B 2 170 ? -39.185 56.245  45.645  1.00 52.77  ?  502 GLY C O   1 
ATOM   6252  N N   . VAL B 2 171 ? -39.581 56.897  47.753  1.00 50.92  ?  503 VAL C N   1 
ATOM   6253  C CA  . VAL B 2 171 ? -40.950 56.390  47.681  1.00 49.59  ?  503 VAL C CA  1 
ATOM   6254  C C   . VAL B 2 171 ? -41.775 57.245  46.736  1.00 50.85  ?  503 VAL C C   1 
ATOM   6255  O O   . VAL B 2 171 ? -42.669 56.735  46.032  1.00 49.37  ?  503 VAL C O   1 
ATOM   6256  C CB  . VAL B 2 171 ? -41.580 56.275  49.082  1.00 47.26  ?  503 VAL C CB  1 
ATOM   6257  C CG1 . VAL B 2 171 ? -43.036 56.136  48.968  1.00 52.50  ?  503 VAL C CG1 1 
ATOM   6258  C CG2 . VAL B 2 171 ? -41.095 54.993  49.750  1.00 55.82  ?  503 VAL C CG2 1 
ATOM   6259  N N   . GLY B 2 172 ? -41.444 58.538  46.645  1.00 44.46  ?  504 GLY C N   1 
ATOM   6260  C CA  . GLY B 2 172 ? -42.111 59.363  45.675  1.00 51.93  ?  504 GLY C CA  1 
ATOM   6261  C C   . GLY B 2 172 ? -42.056 58.804  44.271  1.00 50.03  ?  504 GLY C C   1 
ATOM   6262  O O   . GLY B 2 172 ? -42.958 59.039  43.473  1.00 59.33  ?  504 GLY C O   1 
ATOM   6263  N N   . HIS B 2 173 ? -41.074 57.996  43.964  1.00 46.17  ?  505 HIS C N   1 
ATOM   6264  C CA  . HIS B 2 173 ? -40.748 57.730  42.575  1.00 46.26  ?  505 HIS C CA  1 
ATOM   6265  C C   . HIS B 2 173 ? -40.889 56.251  42.267  1.00 48.61  ?  505 HIS C C   1 
ATOM   6266  O O   . HIS B 2 173 ? -40.439 55.808  41.218  1.00 50.46  ?  505 HIS C O   1 
ATOM   6267  C CB  . HIS B 2 173 ? -39.332 58.202  42.322  1.00 53.98  ?  505 HIS C CB  1 
ATOM   6268  C CG  . HIS B 2 173 ? -39.169 59.630  41.942  1.00 56.67  ?  505 HIS C CG  1 
ATOM   6269  N ND1 . HIS B 2 173 ? -38.946 60.041  40.638  1.00 47.41  ?  505 HIS C ND1 1 
ATOM   6270  C CD2 . HIS B 2 173 ? -39.008 60.727  42.717  1.00 62.27  ?  505 HIS C CD2 1 
ATOM   6271  C CE1 . HIS B 2 173 ? -38.702 61.338  40.619  1.00 52.72  ?  505 HIS C CE1 1 
ATOM   6272  N NE2 . HIS B 2 173 ? -38.776 61.784  41.859  1.00 54.96  ?  505 HIS C NE2 1 
ATOM   6273  N N   . GLN B 2 174 ? -41.393 55.467  43.183  1.00 44.36  ?  506 GLN C N   1 
ATOM   6274  C CA  . GLN B 2 174 ? -41.473 54.012  43.155  1.00 46.04  ?  506 GLN C CA  1 
ATOM   6275  C C   . GLN B 2 174 ? -42.744 53.550  42.417  1.00 56.47  ?  506 GLN C C   1 
ATOM   6276  O O   . GLN B 2 174 ? -43.761 54.260  42.388  1.00 55.70  ?  506 GLN C O   1 
ATOM   6277  C CB  . GLN B 2 174 ? -41.495 53.506  44.585  1.00 50.19  ?  506 GLN C CB  1 
ATOM   6278  C CG  . GLN B 2 174 ? -40.115 53.435  45.198  1.00 57.57  ?  506 GLN C CG  1 
ATOM   6279  C CD  . GLN B 2 174 ? -40.056 52.841  46.609  1.00 54.33  ?  506 GLN C CD  1 
ATOM   6280  O OE1 . GLN B 2 174 ? -41.023 52.282  47.126  1.00 56.11  ?  506 GLN C OE1 1 
ATOM   6281  N NE2 . GLN B 2 174 ? -38.924 53.040  47.260  1.00 52.63  ?  506 GLN C NE2 1 
ATOM   6282  N N   . PRO B 2 175 ? -42.763 52.369  41.792  1.00 53.29  ?  507 PRO C N   1 
ATOM   6283  C CA  . PRO B 2 175 ? -44.012 51.903  41.179  1.00 48.98  ?  507 PRO C CA  1 
ATOM   6284  C C   . PRO B 2 175 ? -45.117 51.708  42.216  1.00 52.63  ?  507 PRO C C   1 
ATOM   6285  O O   . PRO B 2 175 ? -44.924 51.098  43.266  1.00 56.70  ?  507 PRO C O   1 
ATOM   6286  C CB  . PRO B 2 175 ? -43.606 50.585  40.503  1.00 49.25  ?  507 PRO C CB  1 
ATOM   6287  C CG  . PRO B 2 175 ? -42.368 50.123  41.191  1.00 48.00  ?  507 PRO C CG  1 
ATOM   6288  C CD  . PRO B 2 175 ? -41.666 51.399  41.573  1.00 52.91  ?  507 PRO C CD  1 
ATOM   6289  N N   . TYR B 2 176 ? -46.283 52.266  41.927  1.00 54.61  ?  508 TYR C N   1 
ATOM   6290  C CA  . TYR B 2 176 ? -47.491 51.922  42.653  1.00 54.94  ?  508 TYR C CA  1 
ATOM   6291  C C   . TYR B 2 176 ? -48.510 51.407  41.658  1.00 55.88  ?  508 TYR C C   1 
ATOM   6292  O O   . TYR B 2 176 ? -48.798 52.089  40.665  1.00 51.87  ?  508 TYR C O   1 
ATOM   6293  C CB  . TYR B 2 176 ? -48.087 53.114  43.328  1.00 57.24  ?  508 TYR C CB  1 
ATOM   6294  C CG  . TYR B 2 176 ? -47.431 53.554  44.573  1.00 57.68  ?  508 TYR C CG  1 
ATOM   6295  C CD1 . TYR B 2 176 ? -46.233 54.235  44.538  1.00 55.96  ?  508 TYR C CD1 1 
ATOM   6296  C CD2 . TYR B 2 176 ? -48.037 53.311  45.806  1.00 60.45  ?  508 TYR C CD2 1 
ATOM   6297  C CE1 . TYR B 2 176 ? -45.654 54.672  45.721  1.00 63.22  ?  508 TYR C CE1 1 
ATOM   6298  C CE2 . TYR B 2 176 ? -47.474 53.731  46.981  1.00 67.52  ?  508 TYR C CE2 1 
ATOM   6299  C CZ  . TYR B 2 176 ? -46.284 54.421  46.940  1.00 67.09  ?  508 TYR C CZ  1 
ATOM   6300  O OH  . TYR B 2 176 ? -45.741 54.820  48.137  1.00 62.36  ?  508 TYR C OH  1 
ATOM   6301  N N   . ARG B 2 177 ? -49.082 50.227  41.935  1.00 56.76  ?  509 ARG C N   1 
ATOM   6302  C CA  . ARG B 2 177 ? -50.144 49.709  41.067  1.00 50.05  ?  509 ARG C CA  1 
ATOM   6303  C C   . ARG B 2 177 ? -51.446 50.263  41.624  1.00 53.61  ?  509 ARG C C   1 
ATOM   6304  O O   . ARG B 2 177 ? -51.598 50.409  42.851  1.00 59.39  ?  509 ARG C O   1 
ATOM   6305  C CB  . ARG B 2 177 ? -50.185 48.168  40.971  1.00 48.00  ?  509 ARG C CB  1 
ATOM   6306  C CG  . ARG B 2 177 ? -48.854 47.535  41.306  1.00 50.04  ?  509 ARG C CG  1 
ATOM   6307  C CD  . ARG B 2 177 ? -48.592 46.022  41.228  1.00 52.30  ?  509 ARG C CD  1 
ATOM   6308  N NE  . ARG B 2 177 ? -48.203 45.501  39.922  1.00 52.05  ?  509 ARG C NE  1 
ATOM   6309  C CZ  . ARG B 2 177 ? -48.090 44.214  39.619  1.00 55.10  ?  509 ARG C CZ  1 
ATOM   6310  N NH1 . ARG B 2 177 ? -48.549 43.265  40.416  1.00 64.47  ?  509 ARG C NH1 1 
ATOM   6311  N NH2 . ARG B 2 177 ? -47.424 43.867  38.534  1.00 53.18  ?  509 ARG C NH2 1 
ATOM   6312  N N   . VAL B 2 178 ? -52.335 50.681  40.709  1.00 50.71  ?  510 VAL C N   1 
ATOM   6313  C CA  . VAL B 2 178 ? -53.619 51.250  41.104  1.00 53.49  ?  510 VAL C CA  1 
ATOM   6314  C C   . VAL B 2 178 ? -54.715 50.541  40.341  1.00 55.22  ?  510 VAL C C   1 
ATOM   6315  O O   . VAL B 2 178 ? -54.548 50.146  39.177  1.00 58.02  ?  510 VAL C O   1 
ATOM   6316  C CB  . VAL B 2 178 ? -53.772 52.767  40.854  1.00 48.48  ?  510 VAL C CB  1 
ATOM   6317  C CG1 . VAL B 2 178 ? -53.083 53.549  41.885  1.00 51.03  ?  510 VAL C CG1 1 
ATOM   6318  C CG2 . VAL B 2 178 ? -53.215 53.110  39.567  1.00 54.33  ?  510 VAL C CG2 1 
ATOM   6319  N N   . VAL B 2 179 ? -55.850 50.413  41.023  1.00 57.01  ?  511 VAL C N   1 
ATOM   6320  C CA  . VAL B 2 179 ? -57.081 49.878  40.473  1.00 59.59  ?  511 VAL C CA  1 
ATOM   6321  C C   . VAL B 2 179 ? -58.223 50.790  40.893  1.00 62.45  ?  511 VAL C C   1 
ATOM   6322  O O   . VAL B 2 179 ? -58.390 51.074  42.085  1.00 65.04  ?  511 VAL C O   1 
ATOM   6323  C CB  . VAL B 2 179 ? -57.341 48.447  40.947  1.00 57.93  ?  511 VAL C CB  1 
ATOM   6324  C CG1 . VAL B 2 179 ? -58.545 47.922  40.231  1.00 62.38  ?  511 VAL C CG1 1 
ATOM   6325  C CG2 . VAL B 2 179 ? -56.128 47.592  40.665  1.00 58.24  ?  511 VAL C CG2 1 
ATOM   6326  N N   . VAL B 2 180 ? -58.998 51.242  39.906  1.00 61.68  ?  512 VAL C N   1 
ATOM   6327  C CA  . VAL B 2 180 ? -60.148 52.112  40.075  1.00 61.45  ?  512 VAL C CA  1 
ATOM   6328  C C   . VAL B 2 180 ? -61.391 51.316  39.724  1.00 68.69  ?  512 VAL C C   1 
ATOM   6329  O O   . VAL B 2 180 ? -61.540 50.857  38.578  1.00 69.83  ?  512 VAL C O   1 
ATOM   6330  C CB  . VAL B 2 180 ? -60.047 53.350  39.184  1.00 59.88  ?  512 VAL C CB  1 
ATOM   6331  C CG1 . VAL B 2 180 ? -61.180 54.276  39.459  1.00 64.26  ?  512 VAL C CG1 1 
ATOM   6332  C CG2 . VAL B 2 180 ? -58.754 54.043  39.419  1.00 64.18  ?  512 VAL C CG2 1 
ATOM   6333  N N   . LEU B 2 181 ? -62.274 51.154  40.715  1.00 71.49  ?  513 LEU C N   1 
ATOM   6334  C CA  . LEU B 2 181 ? -63.598 50.566  40.542  1.00 71.16  ?  513 LEU C CA  1 
ATOM   6335  C C   . LEU B 2 181 ? -64.582 51.672  40.223  1.00 79.09  ?  513 LEU C C   1 
ATOM   6336  O O   . LEU B 2 181 ? -64.858 52.530  41.071  1.00 82.00  ?  513 LEU C O   1 
ATOM   6337  C CB  . LEU B 2 181 ? -64.026 49.823  41.795  1.00 69.33  ?  513 LEU C CB  1 
ATOM   6338  C CG  . LEU B 2 181 ? -62.961 48.840  42.167  1.00 64.14  ?  513 LEU C CG  1 
ATOM   6339  C CD1 . LEU B 2 181 ? -63.443 48.155  43.357  1.00 67.39  ?  513 LEU C CD1 1 
ATOM   6340  C CD2 . LEU B 2 181 ? -62.843 47.881  41.009  1.00 66.83  ?  513 LEU C CD2 1 
ATOM   6341  N N   . SER B 2 182 ? -65.088 51.647  38.992  1.00 82.79  ?  514 SER C N   1 
ATOM   6342  C CA  . SER B 2 182 ? -66.154 52.516  38.523  1.00 86.28  ?  514 SER C CA  1 
ATOM   6343  C C   . SER B 2 182 ? -67.475 51.791  38.764  1.00 90.89  ?  514 SER C C   1 
ATOM   6344  O O   . SER B 2 182 ? -67.743 50.742  38.169  1.00 87.69  ?  514 SER C O   1 
ATOM   6345  C CB  . SER B 2 182 ? -65.914 52.859  37.050  1.00 88.79  ?  514 SER C CB  1 
ATOM   6346  O OG  . SER B 2 182 ? -67.093 53.287  36.394  1.00 101.28 ?  514 SER C OG  1 
ATOM   6347  N N   . PHE B 2 183 ? -68.267 52.330  39.683  1.00 94.70  ?  515 PHE C N   1 
ATOM   6348  C CA  . PHE B 2 183 ? -69.586 51.829  40.042  1.00 100.82 ?  515 PHE C CA  1 
ATOM   6349  C C   . PHE B 2 183 ? -70.640 52.707  39.403  1.00 110.88 ?  515 PHE C C   1 
ATOM   6350  O O   . PHE B 2 183 ? -71.156 53.627  40.033  1.00 109.46 ?  515 PHE C O   1 
ATOM   6351  C CB  . PHE B 2 183 ? -69.746 51.854  41.546  1.00 97.69  ?  515 PHE C CB  1 
ATOM   6352  C CG  . PHE B 2 183 ? -69.064 50.777  42.223  1.00 96.74  ?  515 PHE C CG  1 
ATOM   6353  C CD1 . PHE B 2 183 ? -68.835 49.598  41.576  1.00 98.08  ?  515 PHE C CD1 1 
ATOM   6354  C CD2 . PHE B 2 183 ? -68.545 50.977  43.482  1.00 96.92  ?  515 PHE C CD2 1 
ATOM   6355  C CE1 . PHE B 2 183 ? -68.194 48.571  42.220  1.00 101.72 ?  515 PHE C CE1 1 
ATOM   6356  C CE2 . PHE B 2 183 ? -67.876 49.972  44.117  1.00 103.49 ?  515 PHE C CE2 1 
ATOM   6357  C CZ  . PHE B 2 183 ? -67.691 48.760  43.486  1.00 102.42 ?  515 PHE C CZ  1 
ATOM   6358  N N   . GLU B 2 184 ? -70.988 52.429  38.162  1.00 118.48 ?  516 GLU C N   1 
ATOM   6359  C CA  . GLU B 2 184 ? -72.147 53.114  37.626  1.00 131.24 ?  516 GLU C CA  1 
ATOM   6360  C C   . GLU B 2 184 ? -73.395 52.340  38.029  1.00 137.21 ?  516 GLU C C   1 
ATOM   6361  O O   . GLU B 2 184 ? -73.344 51.137  38.290  1.00 135.59 ?  516 GLU C O   1 
ATOM   6362  C CB  . GLU B 2 184 ? -72.083 53.234  36.107  1.00 134.64 ?  516 GLU C CB  1 
ATOM   6363  C CG  . GLU B 2 184 ? -72.542 51.976  35.410  1.00 136.48 ?  516 GLU C CG  1 
ATOM   6364  C CD  . GLU B 2 184 ? -72.315 51.961  33.907  1.00 139.08 ?  516 GLU C CD  1 
ATOM   6365  O OE1 . GLU B 2 184 ? -72.808 52.887  33.234  1.00 144.16 ?  516 GLU C OE1 1 
ATOM   6366  O OE2 . GLU B 2 184 ? -71.741 50.971  33.392  1.00 134.70 -1 516 GLU C OE2 1 
ATOM   6367  N N   . LEU B 2 185 ? -74.522 53.050  38.099  1.00 150.61 ?  517 LEU C N   1 
ATOM   6368  C CA  . LEU B 2 185 ? -75.805 52.387  38.331  1.00 156.74 ?  517 LEU C CA  1 
ATOM   6369  C C   . LEU B 2 185 ? -76.855 53.155  37.548  1.00 158.18 ?  517 LEU C C   1 
ATOM   6370  O O   . LEU B 2 185 ? -77.119 54.322  37.851  1.00 160.53 ?  517 LEU C O   1 
ATOM   6371  C CB  . LEU B 2 185 ? -76.160 52.325  39.819  1.00 155.76 ?  517 LEU C CB  1 
ATOM   6372  C CG  . LEU B 2 185 ? -77.604 52.045  40.259  1.00 155.08 ?  517 LEU C CG  1 
ATOM   6373  C CD1 . LEU B 2 185 ? -77.968 50.579  40.028  1.00 155.00 ?  517 LEU C CD1 1 
ATOM   6374  C CD2 . LEU B 2 185 ? -77.764 52.385  41.728  1.00 146.95 ?  517 LEU C CD2 1 
ATOM   6375  N N   . LEU B 2 186 ? -77.440 52.514  36.544  1.00 151.81 ?  518 LEU C N   1 
ATOM   6376  C CA  . LEU B 2 186 ? -78.555 53.121  35.829  1.00 156.51 ?  518 LEU C CA  1 
ATOM   6377  C C   . LEU B 2 186 ? -79.544 52.016  35.457  1.00 162.23 ?  518 LEU C C   1 
ATOM   6378  O O   . LEU B 2 186 ? -79.528 50.934  36.054  1.00 165.56 ?  518 LEU C O   1 
ATOM   6379  C CB  . LEU B 2 186 ? -78.048 53.943  34.628  1.00 152.24 ?  518 LEU C CB  1 
ATOM   6380  C CG  . LEU B 2 186 ? -77.483 53.346  33.338  1.00 145.40 ?  518 LEU C CG  1 
ATOM   6381  C CD1 . LEU B 2 186 ? -77.291 54.476  32.351  1.00 134.11 ?  518 LEU C CD1 1 
ATOM   6382  C CD2 . LEU B 2 186 ? -76.201 52.619  33.547  1.00 140.17 ?  518 LEU C CD2 1 
ATOM   6383  N N   . HIS B 2 187 ? -80.402 52.281  34.459  1.00 164.39 ?  519 HIS C N   1 
ATOM   6384  C CA  . HIS B 2 187 ? -81.568 51.443  34.171  1.00 165.77 ?  519 HIS C CA  1 
ATOM   6385  C C   . HIS B 2 187 ? -81.220 50.104  33.542  1.00 173.86 ?  519 HIS C C   1 
ATOM   6386  O O   . HIS B 2 187 ? -82.092 49.231  33.469  1.00 166.59 ?  519 HIS C O   1 
ATOM   6387  C CB  . HIS B 2 187 ? -82.539 52.202  33.263  1.00 158.88 ?  519 HIS C CB  1 
ATOM   6388  C CG  . HIS B 2 187 ? -83.295 53.287  33.970  1.00 158.24 ?  519 HIS C CG  1 
ATOM   6389  N ND1 . HIS B 2 187 ? -83.820 53.123  35.235  1.00 156.22 ?  519 HIS C ND1 1 
ATOM   6390  C CD2 . HIS B 2 187 ? -83.612 54.550  33.596  1.00 157.44 ?  519 HIS C CD2 1 
ATOM   6391  C CE1 . HIS B 2 187 ? -84.424 54.236  35.611  1.00 151.32 ?  519 HIS C CE1 1 
ATOM   6392  N NE2 . HIS B 2 187 ? -84.312 55.119  34.635  1.00 152.97 ?  519 HIS C NE2 1 
ATOM   6393  N N   . ALA B 2 188 ? -79.989 49.913  33.085  1.00 211.74 ?  520 ALA C N   1 
ATOM   6394  C CA  . ALA B 2 188 ? -79.608 48.599  32.600  1.00 207.47 ?  520 ALA C CA  1 
ATOM   6395  C C   . ALA B 2 188 ? -79.665 47.589  33.752  1.00 212.82 ?  520 ALA C C   1 
ATOM   6396  O O   . ALA B 2 188 ? -79.567 47.964  34.923  1.00 215.35 ?  520 ALA C O   1 
ATOM   6397  C CB  . ALA B 2 188 ? -78.217 48.641  31.978  1.00 197.96 ?  520 ALA C CB  1 
ATOM   6398  N N   . PRO B 2 189 ? -79.878 46.308  33.440  1.00 182.34 ?  521 PRO C N   1 
ATOM   6399  C CA  . PRO B 2 189 ? -80.076 45.287  34.486  1.00 173.95 ?  521 PRO C CA  1 
ATOM   6400  C C   . PRO B 2 189 ? -78.884 45.180  35.435  1.00 165.01 ?  521 PRO C C   1 
ATOM   6401  O O   . PRO B 2 189 ? -77.755 44.881  35.021  1.00 161.74 ?  521 PRO C O   1 
ATOM   6402  C CB  . PRO B 2 189 ? -80.265 44.000  33.679  1.00 170.16 ?  521 PRO C CB  1 
ATOM   6403  C CG  . PRO B 2 189 ? -80.835 44.460  32.383  1.00 169.14 ?  521 PRO C CG  1 
ATOM   6404  C CD  . PRO B 2 189 ? -80.242 45.813  32.102  1.00 174.88 ?  521 PRO C CD  1 
ATOM   6405  N N   . ALA B 2 190 ? -79.149 45.376  36.728  1.00 162.50 ?  522 ALA C N   1 
ATOM   6406  C CA  . ALA B 2 190 ? -78.111 45.420  37.761  1.00 152.42 ?  522 ALA C CA  1 
ATOM   6407  C C   . ALA B 2 190 ? -77.795 44.008  38.259  1.00 148.97 ?  522 ALA C C   1 
ATOM   6408  O O   . ALA B 2 190 ? -78.646 43.374  38.890  1.00 150.93 ?  522 ALA C O   1 
ATOM   6409  C CB  . ALA B 2 190 ? -78.558 46.304  38.924  1.00 148.14 ?  522 ALA C CB  1 
ATOM   6410  N N   . THR B 2 191 ? -76.562 43.526  38.006  1.00 139.19 ?  523 THR C N   1 
ATOM   6411  C CA  . THR B 2 191 ? -76.194 42.133  38.256  1.00 134.19 ?  523 THR C CA  1 
ATOM   6412  C C   . THR B 2 191 ? -74.911 41.966  39.072  1.00 128.54 ?  523 THR C C   1 
ATOM   6413  O O   . THR B 2 191 ? -74.354 40.861  39.098  1.00 124.66 ?  523 THR C O   1 
ATOM   6414  C CB  . THR B 2 191 ? -76.048 41.376  36.932  1.00 136.68 ?  523 THR C CB  1 
ATOM   6415  O OG1 . THR B 2 191 ? -75.169 42.103  36.065  1.00 137.52 ?  523 THR C OG1 1 
ATOM   6416  C CG2 . THR B 2 191 ? -77.394 41.215  36.256  1.00 139.12 ?  523 THR C CG2 1 
ATOM   6417  N N   . VAL B 2 192 ? -74.424 43.015  39.737  1.00 134.75 ?  524 VAL C N   1 
ATOM   6418  C CA  . VAL B 2 192 ? -73.214 42.940  40.549  1.00 127.03 ?  524 VAL C CA  1 
ATOM   6419  C C   . VAL B 2 192 ? -73.622 43.272  41.973  1.00 137.43 ?  524 VAL C C   1 
ATOM   6420  O O   . VAL B 2 192 ? -73.960 44.426  42.268  1.00 136.97 ?  524 VAL C O   1 
ATOM   6421  C CB  . VAL B 2 192 ? -72.129 43.909  40.066  1.00 117.32 ?  524 VAL C CB  1 
ATOM   6422  C CG1 . VAL B 2 192 ? -70.812 43.601  40.749  1.00 114.28 ?  524 VAL C CG1 1 
ATOM   6423  C CG2 . VAL B 2 192 ? -71.980 43.876  38.560  1.00 119.88 ?  524 VAL C CG2 1 
ATOM   6424  N N   . CYS B 2 193 ? -73.578 42.281  42.864  1.00 150.43 ?  525 CYS C N   1 
ATOM   6425  C CA  . CYS B 2 193 ? -74.176 42.426  44.185  1.00 149.75 ?  525 CYS C CA  1 
ATOM   6426  C C   . CYS B 2 193 ? -73.229 41.920  45.268  1.00 148.10 ?  525 CYS C C   1 
ATOM   6427  O O   . CYS B 2 193 ? -72.289 41.171  44.995  1.00 143.49 ?  525 CYS C O   1 
ATOM   6428  C CB  . CYS B 2 193 ? -75.504 41.669  44.247  1.00 159.58 ?  525 CYS C CB  1 
ATOM   6429  S SG  . CYS B 2 193 ? -76.774 42.301  43.101  1.00 175.17 ?  525 CYS C SG  1 
ATOM   6430  N N   . GLY B 2 194 ? -73.496 42.334  46.511  1.00 135.36 ?  526 GLY C N   1 
ATOM   6431  C CA  . GLY B 2 194 ? -72.754 41.861  47.675  1.00 129.94 ?  526 GLY C CA  1 
ATOM   6432  C C   . GLY B 2 194 ? -73.601 41.635  48.923  1.00 120.70 ?  526 GLY C C   1 
ATOM   6433  O O   . GLY B 2 194 ? -73.578 40.567  49.547  1.00 102.08 ?  526 GLY C O   1 
ATOM   6434  N N   . THR C 2 1   ? -49.437 45.122  69.072  1.00 112.16 ?  333 THR D N   1 
ATOM   6435  C CA  . THR C 2 1   ? -49.372 43.669  68.930  1.00 125.03 ?  333 THR D CA  1 
ATOM   6436  C C   . THR C 2 1   ? -48.092 43.207  68.217  1.00 135.65 ?  333 THR D C   1 
ATOM   6437  O O   . THR C 2 1   ? -48.099 42.283  67.396  1.00 128.91 ?  333 THR D O   1 
ATOM   6438  C CB  . THR C 2 1   ? -50.608 43.136  68.171  1.00 126.21 ?  333 THR D CB  1 
ATOM   6439  O OG1 . THR C 2 1   ? -50.502 43.474  66.781  1.00 130.97 ?  333 THR D OG1 1 
ATOM   6440  C CG2 . THR C 2 1   ? -51.906 43.707  68.754  1.00 116.55 ?  333 THR D CG2 1 
ATOM   6441  N N   . ASN C 2 2   ? -46.981 43.853  68.566  1.00 149.94 ?  334 ASN D N   1 
ATOM   6442  C CA  . ASN C 2 2   ? -45.664 43.515  68.039  1.00 149.38 ?  334 ASN D CA  1 
ATOM   6443  C C   . ASN C 2 2   ? -44.664 43.508  69.188  1.00 145.96 ?  334 ASN D C   1 
ATOM   6444  O O   . ASN C 2 2   ? -44.685 44.418  70.026  1.00 142.34 ?  334 ASN D O   1 
ATOM   6445  C CB  . ASN C 2 2   ? -45.231 44.507  66.949  1.00 149.34 ?  334 ASN D CB  1 
ATOM   6446  C CG  . ASN C 2 2   ? -44.411 43.853  65.868  1.00 152.79 ?  334 ASN D CG  1 
ATOM   6447  O OD1 . ASN C 2 2   ? -44.860 42.899  65.231  1.00 153.43 ?  334 ASN D OD1 1 
ATOM   6448  N ND2 . ASN C 2 2   ? -43.203 44.356  65.653  1.00 152.13 ?  334 ASN D ND2 1 
ATOM   6449  N N   . LEU C 2 3   ? -43.808 42.480  69.217  1.00 137.71 ?  335 LEU D N   1 
ATOM   6450  C CA  . LEU C 2 3   ? -42.926 42.208  70.343  1.00 135.50 ?  335 LEU D CA  1 
ATOM   6451  C C   . LEU C 2 3   ? -42.157 43.447  70.784  1.00 141.92 ?  335 LEU D C   1 
ATOM   6452  O O   . LEU C 2 3   ? -41.833 44.321  69.969  1.00 143.51 ?  335 LEU D O   1 
ATOM   6453  C CB  . LEU C 2 3   ? -41.972 41.068  69.978  1.00 128.91 ?  335 LEU D CB  1 
ATOM   6454  C CG  . LEU C 2 3   ? -40.868 40.590  70.923  1.00 143.43 ?  335 LEU D CG  1 
ATOM   6455  C CD1 . LEU C 2 3   ? -40.533 39.137  70.661  1.00 144.96 ?  335 LEU D CD1 1 
ATOM   6456  C CD2 . LEU C 2 3   ? -39.619 41.416  70.636  1.00 135.98 ?  335 LEU D CD2 1 
ATOM   6457  N N   . CYS C 2 4   ? -41.853 43.519  72.078  1.00 138.65 ?  336 CYS D N   1 
ATOM   6458  C CA  . CYS C 2 4   ? -41.067 44.626  72.625  1.00 132.66 ?  336 CYS D CA  1 
ATOM   6459  C C   . CYS C 2 4   ? -39.583 44.422  72.365  1.00 123.65 ?  336 CYS D C   1 
ATOM   6460  O O   . CYS C 2 4   ? -39.037 43.392  72.756  1.00 118.19 ?  336 CYS D O   1 
ATOM   6461  C CB  . CYS C 2 4   ? -41.264 44.775  74.128  1.00 131.63 ?  336 CYS D CB  1 
ATOM   6462  S SG  . CYS C 2 4   ? -42.735 45.709  74.623  1.00 152.81 ?  336 CYS D SG  1 
ATOM   6463  N N   . PRO C 2 5   ? -38.886 45.403  71.776  1.00 124.78 ?  337 PRO D N   1 
ATOM   6464  C CA  . PRO C 2 5   ? -37.486 45.210  71.398  1.00 118.99 ?  337 PRO D CA  1 
ATOM   6465  C C   . PRO C 2 5   ? -36.655 44.898  72.613  1.00 115.20 ?  337 PRO D C   1 
ATOM   6466  O O   . PRO C 2 5   ? -36.388 45.771  73.439  1.00 118.19 ?  337 PRO D O   1 
ATOM   6467  C CB  . PRO C 2 5   ? -37.087 46.559  70.792  1.00 121.58 ?  337 PRO D CB  1 
ATOM   6468  C CG  . PRO C 2 5   ? -38.064 47.521  71.329  1.00 120.69 ?  337 PRO D CG  1 
ATOM   6469  C CD  . PRO C 2 5   ? -39.345 46.766  71.482  1.00 129.27 ?  337 PRO D CD  1 
ATOM   6470  N N   . PHE C 2 6   ? -36.282 43.645  72.761  1.00 119.04 ?  338 PHE D N   1 
ATOM   6471  C CA  . PHE C 2 6   ? -35.454 43.267  73.882  1.00 110.48 ?  338 PHE D CA  1 
ATOM   6472  C C   . PHE C 2 6   ? -34.070 42.890  73.454  1.00 107.44 ?  338 PHE D C   1 
ATOM   6473  O O   . PHE C 2 6   ? -33.111 43.209  74.151  1.00 111.42 ?  338 PHE D O   1 
ATOM   6474  C CB  . PHE C 2 6   ? -36.063 42.108  74.654  1.00 105.85 ?  338 PHE D CB  1 
ATOM   6475  C CG  . PHE C 2 6   ? -37.019 42.552  75.698  1.00 108.06 ?  338 PHE D CG  1 
ATOM   6476  C CD1 . PHE C 2 6   ? -37.162 43.902  75.989  1.00 108.73 ?  338 PHE D CD1 1 
ATOM   6477  C CD2 . PHE C 2 6   ? -37.788 41.638  76.384  1.00 120.35 ?  338 PHE D CD2 1 
ATOM   6478  C CE1 . PHE C 2 6   ? -38.054 44.333  76.954  1.00 110.69 ?  338 PHE D CE1 1 
ATOM   6479  C CE2 . PHE C 2 6   ? -38.685 42.062  77.357  1.00 127.29 ?  338 PHE D CE2 1 
ATOM   6480  C CZ  . PHE C 2 6   ? -38.817 43.410  77.640  1.00 121.07 ?  338 PHE D CZ  1 
ATOM   6481  N N   . ASP C 2 7   ? -33.938 42.213  72.327  1.00 109.94 ?  339 ASP D N   1 
ATOM   6482  C CA  . ASP C 2 7   ? -32.601 41.940  71.846  1.00 116.02 ?  339 ASP D CA  1 
ATOM   6483  C C   . ASP C 2 7   ? -31.842 43.258  71.739  1.00 115.75 ?  339 ASP D C   1 
ATOM   6484  O O   . ASP C 2 7   ? -30.683 43.366  72.167  1.00 116.69 ?  339 ASP D O   1 
ATOM   6485  C CB  . ASP C 2 7   ? -32.676 41.238  70.497  1.00 118.13 ?  339 ASP D CB  1 
ATOM   6486  C CG  . ASP C 2 7   ? -31.571 40.206  70.301  1.00 123.53 ?  339 ASP D CG  1 
ATOM   6487  O OD1 . ASP C 2 7   ? -31.223 39.481  71.273  1.00 125.09 ?  339 ASP D OD1 1 
ATOM   6488  O OD2 . ASP C 2 7   ? -31.011 40.174  69.186  1.00 126.50 -1 339 ASP D OD2 1 
ATOM   6489  N N   . GLU C 2 8   ? -32.535 44.302  71.270  1.00 107.74 ?  340 GLU D N   1 
ATOM   6490  C CA  . GLU C 2 8   ? -31.921 45.610  71.067  1.00 105.53 ?  340 GLU D CA  1 
ATOM   6491  C C   . GLU C 2 8   ? -31.214 46.102  72.327  1.00 99.73  ?  340 GLU D C   1 
ATOM   6492  O O   . GLU C 2 8   ? -30.257 46.880  72.237  1.00 93.78  ?  340 GLU D O   1 
ATOM   6493  C CB  . GLU C 2 8   ? -32.998 46.595  70.636  1.00 107.04 ?  340 GLU D CB  1 
ATOM   6494  C CG  . GLU C 2 8   ? -32.514 48.012  70.561  1.00 107.92 ?  340 GLU D CG  1 
ATOM   6495  C CD  . GLU C 2 8   ? -33.620 48.967  70.295  1.00 108.59 ?  340 GLU D CD  1 
ATOM   6496  O OE1 . GLU C 2 8   ? -33.917 49.219  69.113  1.00 101.72 ?  340 GLU D OE1 1 
ATOM   6497  O OE2 . GLU C 2 8   ? -34.129 49.534  71.279  1.00 111.46 -1 340 GLU D OE2 1 
ATOM   6498  N N   . VAL C 2 9   ? -31.688 45.672  73.497  1.00 101.26 ?  341 VAL D N   1 
ATOM   6499  C CA  . VAL C 2 9   ? -31.045 45.938  74.787  1.00 97.02  ?  341 VAL D CA  1 
ATOM   6500  C C   . VAL C 2 9   ? -30.143 44.799  75.216  1.00 91.63  ?  341 VAL D C   1 
ATOM   6501  O O   . VAL C 2 9   ? -28.988 45.026  75.570  1.00 91.27  ?  341 VAL D O   1 
ATOM   6502  C CB  . VAL C 2 9   ? -32.102 46.249  75.870  1.00 93.36  ?  341 VAL D CB  1 
ATOM   6503  C CG1 . VAL C 2 9   ? -31.513 46.076  77.229  1.00 86.00  ?  341 VAL D CG1 1 
ATOM   6504  C CG2 . VAL C 2 9   ? -32.545 47.696  75.746  1.00 97.48  ?  341 VAL D CG2 1 
ATOM   6505  N N   . PHE C 2 10  ? -30.639 43.564  75.189  1.00 87.30  ?  342 PHE D N   1 
ATOM   6506  C CA  . PHE C 2 10  ? -29.801 42.551  75.810  1.00 91.83  ?  342 PHE D CA  1 
ATOM   6507  C C   . PHE C 2 10  ? -28.616 42.193  74.924  1.00 94.58  ?  342 PHE D C   1 
ATOM   6508  O O   . PHE C 2 10  ? -27.474 42.112  75.403  1.00 97.20  ?  342 PHE D O   1 
ATOM   6509  C CB  . PHE C 2 10  ? -30.552 41.267  76.148  1.00 92.88  ?  342 PHE D CB  1 
ATOM   6510  C CG  . PHE C 2 10  ? -31.405 41.383  77.344  1.00 90.39  ?  342 PHE D CG  1 
ATOM   6511  C CD1 . PHE C 2 10  ? -31.861 42.626  77.767  1.00 91.93  ?  342 PHE D CD1 1 
ATOM   6512  C CD2 . PHE C 2 10  ? -31.497 40.331  78.211  1.00 87.35  ?  342 PHE D CD2 1 
ATOM   6513  C CE1 . PHE C 2 10  ? -32.613 42.741  78.905  1.00 93.48  ?  342 PHE D CE1 1 
ATOM   6514  C CE2 . PHE C 2 10  ? -32.205 40.449  79.387  1.00 92.67  ?  342 PHE D CE2 1 
ATOM   6515  C CZ  . PHE C 2 10  ? -32.764 41.664  79.738  1.00 92.36  ?  342 PHE D CZ  1 
ATOM   6516  N N   . ASN C 2 11  ? -28.855 41.960  73.640  1.00 94.91  ?  343 ASN D N   1 
ATOM   6517  C CA  . ASN C 2 11  ? -27.769 41.548  72.768  1.00 91.89  ?  343 ASN D CA  1 
ATOM   6518  C C   . ASN C 2 11  ? -27.178 42.726  72.010  1.00 85.31  ?  343 ASN D C   1 
ATOM   6519  O O   . ASN C 2 11  ? -26.528 42.532  70.993  1.00 87.47  ?  343 ASN D O   1 
ATOM   6520  C CB  . ASN C 2 11  ? -28.226 40.415  71.846  1.00 97.44  ?  343 ASN D CB  1 
ATOM   6521  C CG  . ASN C 2 11  ? -28.576 39.131  72.637  1.00 111.79 ?  343 ASN D CG  1 
ATOM   6522  O OD1 . ASN C 2 11  ? -28.402 39.083  73.862  1.00 109.62 ?  343 ASN D OD1 1 
ATOM   6523  N ND2 . ASN C 2 11  ? -29.045 38.082  71.931  1.00 120.93 ?  343 ASN D ND2 1 
ATOM   6524  N N   . ALA C 2 12  ? -27.346 43.933  72.544  1.00 94.30  ?  344 ALA D N   1 
ATOM   6525  C CA  . ALA C 2 12  ? -26.750 45.125  71.957  1.00 95.80  ?  344 ALA D CA  1 
ATOM   6526  C C   . ALA C 2 12  ? -25.239 45.017  71.931  1.00 98.42  ?  344 ALA D C   1 
ATOM   6527  O O   . ALA C 2 12  ? -24.622 44.416  72.809  1.00 97.55  ?  344 ALA D O   1 
ATOM   6528  C CB  . ALA C 2 12  ? -27.142 46.370  72.742  1.00 97.50  ?  344 ALA D CB  1 
ATOM   6529  N N   . THR C 2 13  ? -24.644 45.628  70.911  1.00 90.63  ?  345 THR D N   1 
ATOM   6530  C CA  . THR C 2 13  ? -23.237 45.387  70.628  1.00 93.81  ?  345 THR D CA  1 
ATOM   6531  C C   . THR C 2 13  ? -22.378 45.759  71.813  1.00 97.01  ?  345 THR D C   1 
ATOM   6532  O O   . THR C 2 13  ? -21.523 44.978  72.243  1.00 100.75 ?  345 THR D O   1 
ATOM   6533  C CB  . THR C 2 13  ? -22.798 46.166  69.401  1.00 95.21  ?  345 THR D CB  1 
ATOM   6534  O OG1 . THR C 2 13  ? -23.774 45.999  68.374  1.00 103.65 ?  345 THR D OG1 1 
ATOM   6535  C CG2 . THR C 2 13  ? -21.471 45.651  68.914  1.00 95.48  ?  345 THR D CG2 1 
ATOM   6536  N N   . ARG C 2 14  ? -22.606 46.941  72.371  1.00 102.30 ?  346 ARG D N   1 
ATOM   6537  C CA  . ARG C 2 14  ? -21.844 47.363  73.526  1.00 103.39 ?  346 ARG D CA  1 
ATOM   6538  C C   . ARG C 2 14  ? -22.786 47.899  74.588  1.00 97.10  ?  346 ARG D C   1 
ATOM   6539  O O   . ARG C 2 14  ? -23.954 48.200  74.339  1.00 95.03  ?  346 ARG D O   1 
ATOM   6540  C CB  . ARG C 2 14  ? -20.798 48.412  73.167  1.00 118.20 ?  346 ARG D CB  1 
ATOM   6541  C CG  . ARG C 2 14  ? -19.620 47.768  72.439  1.00 129.08 ?  346 ARG D CG  1 
ATOM   6542  C CD  . ARG C 2 14  ? -18.388 48.679  72.280  1.00 134.62 ?  346 ARG D CD  1 
ATOM   6543  N NE  . ARG C 2 14  ? -17.339 48.130  71.412  1.00 142.38 ?  346 ARG D NE  1 
ATOM   6544  C CZ  . ARG C 2 14  ? -16.196 48.748  71.119  1.00 135.95 ?  346 ARG D CZ  1 
ATOM   6545  N NH1 . ARG C 2 14  ? -15.873 49.907  71.693  1.00 120.06 ?  346 ARG D NH1 1 
ATOM   6546  N NH2 . ARG C 2 14  ? -15.329 48.159  70.281  1.00 133.08 ?  346 ARG D NH2 1 
ATOM   6547  N N   . PHE C 2 15  ? -22.256 48.026  75.783  1.00 87.21  ?  347 PHE D N   1 
ATOM   6548  C CA  . PHE C 2 15  ? -23.030 48.446  76.931  1.00 82.71  ?  347 PHE D CA  1 
ATOM   6549  C C   . PHE C 2 15  ? -22.440 49.728  77.484  1.00 77.78  ?  347 PHE D C   1 
ATOM   6550  O O   . PHE C 2 15  ? -21.282 50.057  77.237  1.00 75.98  ?  347 PHE D O   1 
ATOM   6551  C CB  . PHE C 2 15  ? -23.004 47.376  78.013  1.00 82.82  ?  347 PHE D CB  1 
ATOM   6552  C CG  . PHE C 2 15  ? -24.105 46.351  77.915  1.00 79.24  ?  347 PHE D CG  1 
ATOM   6553  C CD1 . PHE C 2 15  ? -24.156 45.461  76.863  1.00 80.15  ?  347 PHE D CD1 1 
ATOM   6554  C CD2 . PHE C 2 15  ? -25.033 46.225  78.937  1.00 75.25  ?  347 PHE D CD2 1 
ATOM   6555  C CE1 . PHE C 2 15  ? -25.129 44.492  76.813  1.00 81.45  ?  347 PHE D CE1 1 
ATOM   6556  C CE2 . PHE C 2 15  ? -26.004 45.269  78.889  1.00 71.90  ?  347 PHE D CE2 1 
ATOM   6557  C CZ  . PHE C 2 15  ? -26.052 44.399  77.830  1.00 77.06  ?  347 PHE D CZ  1 
ATOM   6558  N N   . ALA C 2 16  ? -23.233 50.438  78.267  1.00 65.75  ?  348 ALA D N   1 
ATOM   6559  C CA  . ALA C 2 16  ? -22.804 51.722  78.812  1.00 70.66  ?  348 ALA D CA  1 
ATOM   6560  C C   . ALA C 2 16  ? -22.023 51.554  80.115  1.00 73.04  ?  348 ALA D C   1 
ATOM   6561  O O   . ALA C 2 16  ? -22.447 50.813  81.012  1.00 74.70  ?  348 ALA D O   1 
ATOM   6562  C CB  . ALA C 2 16  ? -24.011 52.623  79.061  1.00 79.97  ?  348 ALA D CB  1 
ATOM   6563  N N   . SER C 2 17  ? -20.908 52.270  80.251  1.00 72.62  ?  349 SER D N   1 
ATOM   6564  C CA  . SER C 2 17  ? -20.215 52.197  81.531  1.00 70.55  ?  349 SER D CA  1 
ATOM   6565  C C   . SER C 2 17  ? -21.112 52.821  82.602  1.00 68.26  ?  349 SER D C   1 
ATOM   6566  O O   . SER C 2 17  ? -21.798 53.816  82.363  1.00 69.41  ?  349 SER D O   1 
ATOM   6567  C CB  . SER C 2 17  ? -18.806 52.830  81.472  1.00 68.99  ?  349 SER D CB  1 
ATOM   6568  O OG  . SER C 2 17  ? -18.726 54.169  81.009  1.00 63.88  ?  349 SER D OG  1 
ATOM   6569  N N   . VAL C 2 18  ? -21.171 52.165  83.760  1.00 68.29  ?  350 VAL D N   1 
ATOM   6570  C CA  . VAL C 2 18  ? -22.255 52.360  84.727  1.00 70.64  ?  350 VAL D CA  1 
ATOM   6571  C C   . VAL C 2 18  ? -22.459 53.817  85.139  1.00 68.99  ?  350 VAL D C   1 
ATOM   6572  O O   . VAL C 2 18  ? -23.565 54.216  85.501  1.00 74.48  ?  350 VAL D O   1 
ATOM   6573  C CB  . VAL C 2 18  ? -22.002 51.467  85.961  1.00 68.78  ?  350 VAL D CB  1 
ATOM   6574  C CG1 . VAL C 2 18  ? -20.607 51.684  86.479  1.00 65.96  ?  350 VAL D CG1 1 
ATOM   6575  C CG2 . VAL C 2 18  ? -23.002 51.778  87.063  1.00 69.11  ?  350 VAL D CG2 1 
ATOM   6576  N N   . TYR C 2 19  ? -21.426 54.637  85.111  1.00 69.99  ?  351 TYR D N   1 
ATOM   6577  C CA  . TYR C 2 19  ? -21.628 55.989  85.627  1.00 71.28  ?  351 TYR D CA  1 
ATOM   6578  C C   . TYR C 2 19  ? -22.488 56.827  84.722  1.00 70.53  ?  351 TYR D C   1 
ATOM   6579  O O   . TYR C 2 19  ? -23.044 57.825  85.183  1.00 75.54  ?  351 TYR D O   1 
ATOM   6580  C CB  . TYR C 2 19  ? -20.302 56.683  85.804  1.00 70.53  ?  351 TYR D CB  1 
ATOM   6581  C CG  . TYR C 2 19  ? -19.812 57.272  84.536  1.00 59.93  ?  351 TYR D CG  1 
ATOM   6582  C CD1 . TYR C 2 19  ? -19.207 56.466  83.600  1.00 59.31  ?  351 TYR D CD1 1 
ATOM   6583  C CD2 . TYR C 2 19  ? -19.874 58.627  84.308  1.00 59.79  ?  351 TYR D CD2 1 
ATOM   6584  C CE1 . TYR C 2 19  ? -18.725 56.970  82.465  1.00 58.80  ?  351 TYR D CE1 1 
ATOM   6585  C CE2 . TYR C 2 19  ? -19.379 59.153  83.164  1.00 62.04  ?  351 TYR D CE2 1 
ATOM   6586  C CZ  . TYR C 2 19  ? -18.800 58.318  82.245  1.00 60.43  ?  351 TYR D CZ  1 
ATOM   6587  O OH  . TYR C 2 19  ? -18.278 58.854  81.096  1.00 72.23  ?  351 TYR D OH  1 
ATOM   6588  N N   . ALA C 2 20  ? -22.539 56.467  83.439  1.00 72.96  ?  352 ALA D N   1 
ATOM   6589  C CA  . ALA C 2 20  ? -23.411 57.050  82.427  1.00 70.51  ?  352 ALA D CA  1 
ATOM   6590  C C   . ALA C 2 20  ? -24.372 55.985  81.908  1.00 75.78  ?  352 ALA D C   1 
ATOM   6591  O O   . ALA C 2 20  ? -24.477 55.777  80.694  1.00 75.13  ?  352 ALA D O   1 
ATOM   6592  C CB  . ALA C 2 20  ? -22.582 57.639  81.276  1.00 60.41  ?  352 ALA D CB  1 
ATOM   6593  N N   . TRP C 2 21  ? -25.044 55.291  82.820  1.00 73.19  ?  353 TRP D N   1 
ATOM   6594  C CA  . TRP C 2 21  ? -25.941 54.227  82.419  1.00 83.02  ?  353 TRP D CA  1 
ATOM   6595  C C   . TRP C 2 21  ? -27.053 54.801  81.560  1.00 94.14  ?  353 TRP D C   1 
ATOM   6596  O O   . TRP C 2 21  ? -27.625 55.845  81.897  1.00 94.40  ?  353 TRP D O   1 
ATOM   6597  C CB  . TRP C 2 21  ? -26.565 53.557  83.637  1.00 81.98  ?  353 TRP D CB  1 
ATOM   6598  C CG  . TRP C 2 21  ? -27.155 54.509  84.656  1.00 81.23  ?  353 TRP D CG  1 
ATOM   6599  C CD1 . TRP C 2 21  ? -26.484 55.287  85.531  1.00 81.34  ?  353 TRP D CD1 1 
ATOM   6600  C CD2 . TRP C 2 21  ? -28.545 54.813  84.841  1.00 86.02  ?  353 TRP D CD2 1 
ATOM   6601  N NE1 . TRP C 2 21  ? -27.359 56.027  86.292  1.00 81.92  ?  353 TRP D NE1 1 
ATOM   6602  C CE2 . TRP C 2 21  ? -28.633 55.760  85.877  1.00 82.32  ?  353 TRP D CE2 1 
ATOM   6603  C CE3 . TRP C 2 21  ? -29.722 54.369  84.232  1.00 89.00  ?  353 TRP D CE3 1 
ATOM   6604  C CZ2 . TRP C 2 21  ? -29.848 56.270  86.325  1.00 85.25  ?  353 TRP D CZ2 1 
ATOM   6605  C CZ3 . TRP C 2 21  ? -30.931 54.875  84.679  1.00 88.81  ?  353 TRP D CZ3 1 
ATOM   6606  C CH2 . TRP C 2 21  ? -30.984 55.816  85.719  1.00 88.02  ?  353 TRP D CH2 1 
ATOM   6607  N N   . ASN C 2 22  ? -27.369 54.123  80.456  1.00 97.73  ?  354 ASN D N   1 
ATOM   6608  C CA  . ASN C 2 22  ? -28.492 54.554  79.641  1.00 98.84  ?  354 ASN D CA  1 
ATOM   6609  C C   . ASN C 2 22  ? -29.694 53.666  79.890  1.00 101.58 ?  354 ASN D C   1 
ATOM   6610  O O   . ASN C 2 22  ? -29.623 52.605  80.531  1.00 93.91  ?  354 ASN D O   1 
ATOM   6611  C CB  . ASN C 2 22  ? -28.165 54.615  78.136  1.00 101.25 ?  354 ASN D CB  1 
ATOM   6612  C CG  . ASN C 2 22  ? -27.766 53.276  77.546  1.00 112.19 ?  354 ASN D CG  1 
ATOM   6613  O OD1 . ASN C 2 22  ? -28.159 52.206  78.016  1.00 118.07 ?  354 ASN D OD1 1 
ATOM   6614  N ND2 . ASN C 2 22  ? -26.969 53.338  76.492  1.00 101.57 ?  354 ASN D ND2 1 
ATOM   6615  N N   . ARG C 2 23  ? -30.805 54.121  79.324  1.00 103.66 ?  355 ARG D N   1 
ATOM   6616  C CA  . ARG C 2 23  ? -32.146 53.739  79.737  1.00 100.67 ?  355 ARG D CA  1 
ATOM   6617  C C   . ARG C 2 23  ? -33.016 53.837  78.502  1.00 101.95 ?  355 ARG D C   1 
ATOM   6618  O O   . ARG C 2 23  ? -33.091 54.910  77.898  1.00 106.10 ?  355 ARG D O   1 
ATOM   6619  C CB  . ARG C 2 23  ? -32.650 54.671  80.855  1.00 99.87  ?  355 ARG D CB  1 
ATOM   6620  C CG  . ARG C 2 23  ? -34.124 55.042  80.824  1.00 97.38  ?  355 ARG D CG  1 
ATOM   6621  C CD  . ARG C 2 23  ? -34.527 55.831  82.068  1.00 94.98  ?  355 ARG D CD  1 
ATOM   6622  N NE  . ARG C 2 23  ? -34.772 54.941  83.196  1.00 95.49  ?  355 ARG D NE  1 
ATOM   6623  C CZ  . ARG C 2 23  ? -35.314 55.301  84.353  1.00 96.03  ?  355 ARG D CZ  1 
ATOM   6624  N NH1 . ARG C 2 23  ? -35.635 56.561  84.608  1.00 101.60 ?  355 ARG D NH1 1 
ATOM   6625  N NH2 . ARG C 2 23  ? -35.527 54.374  85.283  1.00 93.40  ?  355 ARG D NH2 1 
ATOM   6626  N N   . LYS C 2 24  ? -33.621 52.722  78.098  1.00 103.69 ?  356 LYS D N   1 
ATOM   6627  C CA  . LYS C 2 24  ? -34.569 52.726  76.991  1.00 107.86 ?  356 LYS D CA  1 
ATOM   6628  C C   . LYS C 2 24  ? -35.984 52.641  77.529  1.00 112.49 ?  356 LYS D C   1 
ATOM   6629  O O   . LYS C 2 24  ? -36.283 51.801  78.380  1.00 114.81 ?  356 LYS D O   1 
ATOM   6630  C CB  . LYS C 2 24  ? -34.288 51.614  75.977  1.00 103.37 ?  356 LYS D CB  1 
ATOM   6631  C CG  . LYS C 2 24  ? -33.564 52.194  74.744  1.00 115.30 ?  356 LYS D CG  1 
ATOM   6632  C CD  . LYS C 2 24  ? -32.347 53.100  75.165  1.00 124.31 ?  356 LYS D CD  1 
ATOM   6633  C CE  . LYS C 2 24  ? -31.932 54.205  74.143  1.00 124.73 ?  356 LYS D CE  1 
ATOM   6634  N NZ  . LYS C 2 24  ? -31.551 53.802  72.739  1.00 121.80 ?  356 LYS D NZ  1 
ATOM   6635  N N   . ARG C 2 25  ? -36.822 53.568  77.079  1.00 114.09 ?  357 ARG D N   1 
ATOM   6636  C CA  . ARG C 2 25  ? -38.248 53.595  77.382  1.00 120.64 ?  357 ARG D CA  1 
ATOM   6637  C C   . ARG C 2 25  ? -38.914 52.451  76.635  1.00 123.26 ?  357 ARG D C   1 
ATOM   6638  O O   . ARG C 2 25  ? -39.244 52.571  75.457  1.00 122.60 ?  357 ARG D O   1 
ATOM   6639  C CB  . ARG C 2 25  ? -38.844 54.936  76.968  1.00 131.22 ?  357 ARG D CB  1 
ATOM   6640  C CG  . ARG C 2 25  ? -40.103 55.370  77.723  1.00 143.80 ?  357 ARG D CG  1 
ATOM   6641  C CD  . ARG C 2 25  ? -40.886 56.377  76.872  1.00 154.32 ?  357 ARG D CD  1 
ATOM   6642  N NE  . ARG C 2 25  ? -42.300 56.020  76.773  1.00 161.00 ?  357 ARG D NE  1 
ATOM   6643  C CZ  . ARG C 2 25  ? -43.141 56.487  75.856  1.00 160.58 ?  357 ARG D CZ  1 
ATOM   6644  N NH1 . ARG C 2 25  ? -42.752 57.352  74.929  1.00 157.14 ?  357 ARG D NH1 1 
ATOM   6645  N NH2 . ARG C 2 25  ? -44.396 56.046  75.847  1.00 154.89 ?  357 ARG D NH2 1 
ATOM   6646  N N   . ILE C 2 26  ? -39.091 51.318  77.306  1.00 126.89 ?  358 ILE D N   1 
ATOM   6647  C CA  . ILE C 2 26  ? -39.831 50.187  76.756  1.00 126.30 ?  358 ILE D CA  1 
ATOM   6648  C C   . ILE C 2 26  ? -41.313 50.491  76.986  1.00 135.02 ?  358 ILE D C   1 
ATOM   6649  O O   . ILE C 2 26  ? -41.805 50.403  78.122  1.00 139.09 ?  358 ILE D O   1 
ATOM   6650  C CB  . ILE C 2 26  ? -39.405 48.864  77.404  1.00 126.45 ?  358 ILE D CB  1 
ATOM   6651  C CG1 . ILE C 2 26  ? -37.884 48.631  77.281  1.00 129.62 ?  358 ILE D CG1 1 
ATOM   6652  C CG2 . ILE C 2 26  ? -40.153 47.693  76.812  1.00 124.84 ?  358 ILE D CG2 1 
ATOM   6653  C CD1 . ILE C 2 26  ? -37.184 49.261  76.039  1.00 127.60 ?  358 ILE D CD1 1 
ATOM   6654  N N   . SER C 2 27  ? -42.027 50.875  75.913  1.00 140.68 ?  359 SER D N   1 
ATOM   6655  C CA  . SER C 2 27  ? -43.427 51.299  75.987  1.00 138.05 ?  359 SER D CA  1 
ATOM   6656  C C   . SER C 2 27  ? -44.141 51.037  74.661  1.00 131.98 ?  359 SER D C   1 
ATOM   6657  O O   . SER C 2 27  ? -43.502 50.832  73.623  1.00 128.92 ?  359 SER D O   1 
ATOM   6658  C CB  . SER C 2 27  ? -43.541 52.786  76.348  1.00 143.60 ?  359 SER D CB  1 
ATOM   6659  O OG  . SER C 2 27  ? -43.664 52.970  77.746  1.00 157.65 ?  359 SER D OG  1 
ATOM   6660  N N   . ASN C 2 28  ? -45.489 51.057  74.723  1.00 140.55 ?  360 ASN D N   1 
ATOM   6661  C CA  . ASN C 2 28  ? -46.437 50.964  73.577  1.00 134.44 ?  360 ASN D CA  1 
ATOM   6662  C C   . ASN C 2 28  ? -46.130 49.801  72.632  1.00 124.79 ?  360 ASN D C   1 
ATOM   6663  O O   . ASN C 2 28  ? -45.968 49.968  71.420  1.00 108.81 ?  360 ASN D O   1 
ATOM   6664  C CB  . ASN C 2 28  ? -46.519 52.281  72.795  1.00 129.45 ?  360 ASN D CB  1 
ATOM   6665  C CG  . ASN C 2 28  ? -46.533 53.501  73.698  1.00 139.74 ?  360 ASN D CG  1 
ATOM   6666  O OD1 . ASN C 2 28  ? -45.488 54.089  73.993  1.00 149.97 ?  360 ASN D OD1 1 
ATOM   6667  N ND2 . ASN C 2 28  ? -47.725 53.903  74.128  1.00 133.86 ?  360 ASN D ND2 1 
ATOM   6668  N N   . CYS C 2 29  ? -46.166 48.603  73.206  1.00 130.20 ?  361 CYS D N   1 
ATOM   6669  C CA  . CYS C 2 29  ? -45.618 47.364  72.653  1.00 135.21 ?  361 CYS D CA  1 
ATOM   6670  C C   . CYS C 2 29  ? -45.934 46.232  73.627  1.00 140.47 ?  361 CYS D C   1 
ATOM   6671  O O   . CYS C 2 29  ? -46.449 46.465  74.724  1.00 142.74 ?  361 CYS D O   1 
ATOM   6672  C CB  . CYS C 2 29  ? -44.105 47.518  72.332  1.00 140.65 ?  361 CYS D CB  1 
ATOM   6673  S SG  . CYS C 2 29  ? -42.728 47.501  73.632  1.00 136.15 ?  361 CYS D SG  1 
ATOM   6674  N N   . VAL C 2 30  ? -45.658 44.997  73.196  1.00 138.41 ?  362 VAL D N   1 
ATOM   6675  C CA  . VAL C 2 30  ? -45.980 43.790  73.964  1.00 145.40 ?  362 VAL D CA  1 
ATOM   6676  C C   . VAL C 2 30  ? -44.715 42.970  74.192  1.00 145.62 ?  362 VAL D C   1 
ATOM   6677  O O   . VAL C 2 30  ? -43.954 42.721  73.252  1.00 144.20 ?  362 VAL D O   1 
ATOM   6678  C CB  . VAL C 2 30  ? -47.056 42.949  73.264  1.00 153.68 ?  362 VAL D CB  1 
ATOM   6679  C CG1 . VAL C 2 30  ? -46.704 42.746  71.806  1.00 150.47 ?  362 VAL D CG1 1 
ATOM   6680  C CG2 . VAL C 2 30  ? -47.181 41.602  73.962  1.00 156.29 ?  362 VAL D CG2 1 
ATOM   6681  N N   . ALA C 2 31  ? -44.521 42.514  75.428  1.00 153.54 ?  363 ALA D N   1 
ATOM   6682  C CA  . ALA C 2 31  ? -43.207 42.131  75.925  1.00 157.78 ?  363 ALA D CA  1 
ATOM   6683  C C   . ALA C 2 31  ? -42.979 40.624  75.904  1.00 162.25 ?  363 ALA D C   1 
ATOM   6684  O O   . ALA C 2 31  ? -43.873 39.828  76.200  1.00 156.10 ?  363 ALA D O   1 
ATOM   6685  C CB  . ALA C 2 31  ? -43.012 42.660  77.344  1.00 153.25 ?  363 ALA D CB  1 
ATOM   6686  N N   . ASP C 2 32  ? -41.737 40.251  75.587  1.00 175.91 ?  364 ASP D N   1 
ATOM   6687  C CA  . ASP C 2 32  ? -41.299 38.862  75.538  1.00 189.19 ?  364 ASP D CA  1 
ATOM   6688  C C   . ASP C 2 32  ? -40.420 38.474  76.725  1.00 190.73 ?  364 ASP D C   1 
ATOM   6689  O O   . ASP C 2 32  ? -39.571 37.586  76.615  1.00 198.48 ?  364 ASP D O   1 
ATOM   6690  C CB  . ASP C 2 32  ? -40.556 38.595  74.236  1.00 191.83 ?  364 ASP D CB  1 
ATOM   6691  C CG  . ASP C 2 32  ? -40.295 37.118  74.007  1.00 210.37 ?  364 ASP D CG  1 
ATOM   6692  O OD1 . ASP C 2 32  ? -41.127 36.312  74.470  1.00 216.07 ?  364 ASP D OD1 1 
ATOM   6693  O OD2 . ASP C 2 32  ? -39.256 36.765  73.413  1.00 216.85 -1 364 ASP D OD2 1 
ATOM   6694  N N   . TYR C 2 33  ? -40.606 39.112  77.885  1.00 182.53 ?  365 TYR D N   1 
ATOM   6695  C CA  . TYR C 2 33  ? -39.981 38.563  79.103  1.00 176.72 ?  365 TYR D CA  1 
ATOM   6696  C C   . TYR C 2 33  ? -40.566 37.202  79.450  1.00 198.15 ?  365 TYR D C   1 
ATOM   6697  O O   . TYR C 2 33  ? -40.143 36.570  80.418  1.00 198.15 ?  365 TYR D O   1 
ATOM   6698  C CB  . TYR C 2 33  ? -40.060 39.502  80.331  1.00 155.82 ?  365 TYR D CB  1 
ATOM   6699  C CG  . TYR C 2 33  ? -41.367 40.241  80.527  1.00 153.49 ?  365 TYR D CG  1 
ATOM   6700  C CD1 . TYR C 2 33  ? -42.539 39.573  80.846  1.00 164.38 ?  365 TYR D CD1 1 
ATOM   6701  C CD2 . TYR C 2 33  ? -41.391 41.632  80.568  1.00 141.30 ?  365 TYR D CD2 1 
ATOM   6702  C CE1 . TYR C 2 33  ? -43.749 40.264  81.046  1.00 163.39 ?  365 TYR D CE1 1 
ATOM   6703  C CE2 . TYR C 2 33  ? -42.581 42.336  80.795  1.00 148.80 ?  365 TYR D CE2 1 
ATOM   6704  C CZ  . TYR C 2 33  ? -43.765 41.650  81.033  1.00 161.67 ?  365 TYR D CZ  1 
ATOM   6705  O OH  . TYR C 2 33  ? -44.958 42.338  81.253  1.00 161.65 ?  365 TYR D OH  1 
ATOM   6706  N N   . SER C 2 34  ? -41.534 36.741  78.662  1.00 238.76 ?  366 SER D N   1 
ATOM   6707  C CA  . SER C 2 34  ? -42.095 35.415  78.875  1.00 254.59 ?  366 SER D CA  1 
ATOM   6708  C C   . SER C 2 34  ? -41.075 34.318  78.571  1.00 267.74 ?  366 SER D C   1 
ATOM   6709  O O   . SER C 2 34  ? -40.795 33.465  79.425  1.00 265.49 ?  366 SER D O   1 
ATOM   6710  C CB  . SER C 2 34  ? -43.354 35.237  78.023  1.00 245.37 ?  366 SER D CB  1 
ATOM   6711  O OG  . SER C 2 34  ? -43.046 34.611  76.797  1.00 255.56 ?  366 SER D OG  1 
ATOM   6712  N N   . VAL C 2 35  ? -40.480 34.339  77.373  1.00 224.97 ?  367 VAL D N   1 
ATOM   6713  C CA  . VAL C 2 35  ? -39.566 33.280  76.941  1.00 223.77 ?  367 VAL D CA  1 
ATOM   6714  C C   . VAL C 2 35  ? -38.101 33.696  77.025  1.00 217.79 ?  367 VAL D C   1 
ATOM   6715  O O   . VAL C 2 35  ? -37.215 32.878  76.749  1.00 215.35 ?  367 VAL D O   1 
ATOM   6716  C CB  . VAL C 2 35  ? -39.901 32.805  75.511  1.00 225.31 ?  367 VAL D CB  1 
ATOM   6717  C CG1 . VAL C 2 35  ? -39.261 33.723  74.478  1.00 219.96 ?  367 VAL D CG1 1 
ATOM   6718  C CG2 . VAL C 2 35  ? -39.503 31.334  75.306  1.00 225.86 ?  367 VAL D CG2 1 
ATOM   6719  N N   . LEU C 2 36  ? -37.817 34.941  77.388  1.00 203.62 ?  368 LEU D N   1 
ATOM   6720  C CA  . LEU C 2 36  ? -36.440 35.331  77.668  1.00 187.62 ?  368 LEU D CA  1 
ATOM   6721  C C   . LEU C 2 36  ? -35.972 34.953  79.073  1.00 190.85 ?  368 LEU D C   1 
ATOM   6722  O O   . LEU C 2 36  ? -34.760 34.910  79.316  1.00 176.54 ?  368 LEU D O   1 
ATOM   6723  C CB  . LEU C 2 36  ? -36.278 36.831  77.440  1.00 165.70 ?  368 LEU D CB  1 
ATOM   6724  C CG  . LEU C 2 36  ? -34.854 37.358  77.433  1.00 139.15 ?  368 LEU D CG  1 
ATOM   6725  C CD1 . LEU C 2 36  ? -34.653 38.397  76.356  1.00 127.04 ?  368 LEU D CD1 1 
ATOM   6726  C CD2 . LEU C 2 36  ? -34.667 37.963  78.796  1.00 117.51 ?  368 LEU D CD2 1 
ATOM   6727  N N   . TYR C 2 37  ? -36.902 34.684  79.998  1.00 229.49 ?  369 TYR D N   1 
ATOM   6728  C CA  . TYR C 2 37  ? -36.573 34.226  81.347  1.00 227.42 ?  369 TYR D CA  1 
ATOM   6729  C C   . TYR C 2 37  ? -35.944 32.838  81.339  1.00 227.63 ?  369 TYR D C   1 
ATOM   6730  O O   . TYR C 2 37  ? -35.428 32.392  82.373  1.00 214.81 ?  369 TYR D O   1 
ATOM   6731  C CB  . TYR C 2 37  ? -37.849 34.241  82.215  1.00 227.42 ?  369 TYR D CB  1 
ATOM   6732  C CG  . TYR C 2 37  ? -37.861 33.401  83.491  1.00 223.97 ?  369 TYR D CG  1 
ATOM   6733  C CD1 . TYR C 2 37  ? -37.316 33.895  84.679  1.00 214.92 ?  369 TYR D CD1 1 
ATOM   6734  C CD2 . TYR C 2 37  ? -38.452 32.141  83.519  1.00 227.62 ?  369 TYR D CD2 1 
ATOM   6735  C CE1 . TYR C 2 37  ? -37.339 33.154  85.846  1.00 219.33 ?  369 TYR D CE1 1 
ATOM   6736  C CE2 . TYR C 2 37  ? -38.482 31.393  84.687  1.00 225.04 ?  369 TYR D CE2 1 
ATOM   6737  C CZ  . TYR C 2 37  ? -37.923 31.906  85.844  1.00 227.22 ?  369 TYR D CZ  1 
ATOM   6738  O OH  . TYR C 2 37  ? -37.948 31.166  87.002  1.00 230.06 ?  369 TYR D OH  1 
ATOM   6739  N N   . ASN C 2 38  ? -36.036 32.184  80.185  1.00 210.14 ?  370 ASN D N   1 
ATOM   6740  C CA  . ASN C 2 38  ? -35.541 30.793  80.081  1.00 213.83 ?  370 ASN D CA  1 
ATOM   6741  C C   . ASN C 2 38  ? -34.250 30.769  79.261  1.00 205.91 ?  370 ASN D C   1 
ATOM   6742  O O   . ASN C 2 38  ? -33.746 29.664  79.015  1.00 206.10 ?  370 ASN D O   1 
ATOM   6743  C CB  . ASN C 2 38  ? -36.617 29.887  79.491  1.00 219.56 ?  370 ASN D CB  1 
ATOM   6744  C CG  . ASN C 2 38  ? -38.007 30.413  79.779  1.00 220.80 ?  370 ASN D CG  1 
ATOM   6745  O OD1 . ASN C 2 38  ? -38.408 31.436  79.233  1.00 223.55 ?  370 ASN D OD1 1 
ATOM   6746  N ND2 . ASN C 2 38  ? -38.727 29.746  80.668  1.00 216.56 ?  370 ASN D ND2 1 
ATOM   6747  N N   . PHE C 2 39  ? -33.847 31.950  78.774  1.00 197.96 ?  371 PHE D N   1 
ATOM   6748  C CA  . PHE C 2 39  ? -32.579 32.047  78.010  1.00 195.37 ?  371 PHE D CA  1 
ATOM   6749  C C   . PHE C 2 39  ? -31.569 31.225  78.815  1.00 201.51 ?  371 PHE D C   1 
ATOM   6750  O O   . PHE C 2 39  ? -30.632 30.694  78.198  1.00 202.78 ?  371 PHE D O   1 
ATOM   6751  C CB  . PHE C 2 39  ? -32.181 33.512  77.785  1.00 184.71 ?  371 PHE D CB  1 
ATOM   6752  C CG  . PHE C 2 39  ? -32.777 34.238  76.595  1.00 186.57 ?  371 PHE D CG  1 
ATOM   6753  C CD1 . PHE C 2 39  ? -33.975 33.848  76.016  1.00 189.87 ?  371 PHE D CD1 1 
ATOM   6754  C CD2 . PHE C 2 39  ? -32.136 35.350  76.066  1.00 186.14 ?  371 PHE D CD2 1 
ATOM   6755  C CE1 . PHE C 2 39  ? -34.507 34.546  74.942  1.00 182.55 ?  371 PHE D CE1 1 
ATOM   6756  C CE2 . PHE C 2 39  ? -32.666 36.043  74.989  1.00 178.75 ?  371 PHE D CE2 1 
ATOM   6757  C CZ  . PHE C 2 39  ? -33.855 35.643  74.426  1.00 175.18 ?  371 PHE D CZ  1 
ATOM   6758  N N   . ALA C 2 40  ? -31.736 31.155  80.143  1.00 208.56 ?  372 ALA D N   1 
ATOM   6759  C CA  . ALA C 2 40  ? -30.912 30.270  81.009  1.00 198.20 ?  372 ALA D CA  1 
ATOM   6760  C C   . ALA C 2 40  ? -29.406 30.538  80.981  1.00 189.03 ?  372 ALA D C   1 
ATOM   6761  O O   . ALA C 2 40  ? -28.665 29.538  80.840  1.00 182.98 ?  372 ALA D O   1 
ATOM   6762  C CB  . ALA C 2 40  ? -31.203 28.830  80.671  1.00 196.49 ?  372 ALA D CB  1 
ATOM   6763  N N   . PRO C 2 41  ? -28.900 31.784  81.066  1.00 190.43 ?  373 PRO D N   1 
ATOM   6764  C CA  . PRO C 2 41  ? -27.485 32.065  81.213  1.00 183.41 ?  373 PRO D CA  1 
ATOM   6765  C C   . PRO C 2 41  ? -27.313 33.209  82.224  1.00 174.70 ?  373 PRO D C   1 
ATOM   6766  O O   . PRO C 2 41  ? -26.456 34.044  81.994  1.00 172.58 ?  373 PRO D O   1 
ATOM   6767  C CB  . PRO C 2 41  ? -27.261 32.579  79.788  1.00 190.35 ?  373 PRO D CB  1 
ATOM   6768  C CG  . PRO C 2 41  ? -28.524 33.390  79.498  1.00 183.22 ?  373 PRO D CG  1 
ATOM   6769  C CD  . PRO C 2 41  ? -29.488 33.021  80.607  1.00 187.02 ?  373 PRO D CD  1 
ATOM   6770  N N   . PHE C 2 42  ? -28.133 33.262  83.286  1.00 160.45 ?  374 PHE D N   1 
ATOM   6771  C CA  . PHE C 2 42  ? -28.114 34.428  84.206  1.00 145.76 ?  374 PHE D CA  1 
ATOM   6772  C C   . PHE C 2 42  ? -27.433 34.101  85.527  1.00 143.73 ?  374 PHE D C   1 
ATOM   6773  O O   . PHE C 2 42  ? -27.986 33.342  86.336  1.00 131.58 ?  374 PHE D O   1 
ATOM   6774  C CB  . PHE C 2 42  ? -29.526 34.948  84.446  1.00 139.23 ?  374 PHE D CB  1 
ATOM   6775  C CG  . PHE C 2 42  ? -30.326 35.130  83.182  1.00 141.53 ?  374 PHE D CG  1 
ATOM   6776  C CD1 . PHE C 2 42  ? -30.130 36.238  82.381  1.00 129.49 ?  374 PHE D CD1 1 
ATOM   6777  C CD2 . PHE C 2 42  ? -31.262 34.191  82.793  1.00 142.53 ?  374 PHE D CD2 1 
ATOM   6778  C CE1 . PHE C 2 42  ? -30.870 36.413  81.225  1.00 134.93 ?  374 PHE D CE1 1 
ATOM   6779  C CE2 . PHE C 2 42  ? -32.002 34.367  81.636  1.00 159.83 ?  374 PHE D CE2 1 
ATOM   6780  C CZ  . PHE C 2 42  ? -31.805 35.479  80.854  1.00 150.95 ?  374 PHE D CZ  1 
ATOM   6781  N N   . PHE C 2 43  ? -26.274 34.717  85.745  1.00 162.89 ?  375 PHE D N   1 
ATOM   6782  C CA  . PHE C 2 43  ? -25.579 34.527  87.039  1.00 165.20 ?  375 PHE D CA  1 
ATOM   6783  C C   . PHE C 2 43  ? -26.402 35.222  88.123  1.00 171.20 ?  375 PHE D C   1 
ATOM   6784  O O   . PHE C 2 43  ? -26.261 34.838  89.296  1.00 171.99 ?  375 PHE D O   1 
ATOM   6785  C CB  . PHE C 2 43  ? -24.136 35.028  86.969  1.00 153.18 ?  375 PHE D CB  1 
ATOM   6786  C CG  . PHE C 2 43  ? -23.200 34.132  86.196  1.00 154.54 ?  375 PHE D CG  1 
ATOM   6787  C CD1 . PHE C 2 43  ? -23.603 33.543  85.010  1.00 157.27 ?  375 PHE D CD1 1 
ATOM   6788  C CD2 . PHE C 2 43  ? -21.919 33.874  86.654  1.00 148.10 ?  375 PHE D CD2 1 
ATOM   6789  C CE1 . PHE C 2 43  ? -22.742 32.731  84.291  1.00 157.17 ?  375 PHE D CE1 1 
ATOM   6790  C CE2 . PHE C 2 43  ? -21.058 33.060  85.936  1.00 141.93 ?  375 PHE D CE2 1 
ATOM   6791  C CZ  . PHE C 2 43  ? -21.473 32.489  84.757  1.00 154.50 ?  375 PHE D CZ  1 
ATOM   6792  N N   . THR C 2 44  ? -27.239 36.198  87.753  1.00 147.95 ?  376 THR D N   1 
ATOM   6793  C CA  . THR C 2 44  ? -28.103 36.763  88.803  1.00 145.08 ?  376 THR D CA  1 
ATOM   6794  C C   . THR C 2 44  ? -29.367 37.293  88.133  1.00 143.39 ?  376 THR D C   1 
ATOM   6795  O O   . THR C 2 44  ? -29.346 38.347  87.497  1.00 141.76 ?  376 THR D O   1 
ATOM   6796  C CB  . THR C 2 44  ? -27.408 37.857  89.628  1.00 134.83 ?  376 THR D CB  1 
ATOM   6797  O OG1 . THR C 2 44  ? -26.289 37.313  90.342  1.00 142.89 ?  376 THR D OG1 1 
ATOM   6798  C CG2 . THR C 2 44  ? -28.377 38.488  90.661  1.00 134.19 ?  376 THR D CG2 1 
ATOM   6799  N N   . PHE C 2 45  ? -30.462 36.565  88.285  1.00 128.43 ?  377 PHE D N   1 
ATOM   6800  C CA  . PHE C 2 45  ? -31.757 36.895  87.707  1.00 120.76 ?  377 PHE D CA  1 
ATOM   6801  C C   . PHE C 2 45  ? -32.728 37.037  88.876  1.00 116.84 ?  377 PHE D C   1 
ATOM   6802  O O   . PHE C 2 45  ? -33.426 36.089  89.233  1.00 115.02 ?  377 PHE D O   1 
ATOM   6803  C CB  . PHE C 2 45  ? -32.183 35.791  86.746  1.00 128.48 ?  377 PHE D CB  1 
ATOM   6804  C CG  . PHE C 2 45  ? -33.366 36.140  85.883  1.00 133.35 ?  377 PHE D CG  1 
ATOM   6805  C CD1 . PHE C 2 45  ? -34.300 37.087  86.287  1.00 128.31 ?  377 PHE D CD1 1 
ATOM   6806  C CD2 . PHE C 2 45  ? -33.547 35.509  84.666  1.00 144.09 ?  377 PHE D CD2 1 
ATOM   6807  C CE1 . PHE C 2 45  ? -35.378 37.406  85.490  1.00 133.02 ?  377 PHE D CE1 1 
ATOM   6808  C CE2 . PHE C 2 45  ? -34.622 35.823  83.864  1.00 156.95 ?  377 PHE D CE2 1 
ATOM   6809  C CZ  . PHE C 2 45  ? -35.540 36.775  84.278  1.00 153.05 ?  377 PHE D CZ  1 
ATOM   6810  N N   . LYS C 2 46  ? -32.794 38.215  89.483  1.00 113.00 ?  378 LYS D N   1 
ATOM   6811  C CA  . LYS C 2 46  ? -33.611 38.384  90.675  1.00 114.65 ?  378 LYS D CA  1 
ATOM   6812  C C   . LYS C 2 46  ? -34.541 39.570  90.474  1.00 113.43 ?  378 LYS D C   1 
ATOM   6813  O O   . LYS C 2 46  ? -34.075 40.698  90.277  1.00 111.09 ?  378 LYS D O   1 
ATOM   6814  C CB  . LYS C 2 46  ? -32.725 38.577  91.916  1.00 119.04 ?  378 LYS D CB  1 
ATOM   6815  C CG  . LYS C 2 46  ? -32.204 37.269  92.543  1.00 118.70 ?  378 LYS D CG  1 
ATOM   6816  C CD  . LYS C 2 46  ? -33.152 36.700  93.607  1.00 118.02 ?  378 LYS D CD  1 
ATOM   6817  C CE  . LYS C 2 46  ? -32.385 36.022  94.737  1.00 111.63 ?  378 LYS D CE  1 
ATOM   6818  N NZ  . LYS C 2 46  ? -33.032 34.747  95.145  1.00 103.95 ?  378 LYS D NZ  1 
ATOM   6819  N N   . CYS C 2 47  ? -35.850 39.300  90.518  1.00 118.31 ?  379 CYS D N   1 
ATOM   6820  C CA  . CYS C 2 47  ? -36.837 40.402  90.461  1.00 125.22 ?  379 CYS D CA  1 
ATOM   6821  C C   . CYS C 2 47  ? -37.022 40.857  91.909  1.00 132.87 ?  379 CYS D C   1 
ATOM   6822  O O   . CYS C 2 47  ? -37.417 40.018  92.747  1.00 126.67 ?  379 CYS D O   1 
ATOM   6823  C CB  . CYS C 2 47  ? -38.161 39.965  89.841  1.00 120.96 ?  379 CYS D CB  1 
ATOM   6824  S SG  . CYS C 2 47  ? -38.624 40.854  88.330  1.00 129.25 ?  379 CYS D SG  1 
ATOM   6825  N N   . TYR C 2 48  ? -36.881 42.154  92.205  1.00 150.82 ?  380 TYR D N   1 
ATOM   6826  C CA  . TYR C 2 48  ? -37.184 42.597  93.592  1.00 151.50 ?  380 TYR D CA  1 
ATOM   6827  C C   . TYR C 2 48  ? -38.506 43.352  93.580  1.00 152.80 ?  380 TYR D C   1 
ATOM   6828  O O   . TYR C 2 48  ? -38.460 44.593  93.546  1.00 150.55 ?  380 TYR D O   1 
ATOM   6829  C CB  . TYR C 2 48  ? -36.105 43.506  94.201  1.00 134.24 ?  380 TYR D CB  1 
ATOM   6830  C CG  . TYR C 2 48  ? -34.686 43.090  93.927  1.00 126.54 ?  380 TYR D CG  1 
ATOM   6831  C CD1 . TYR C 2 48  ? -34.269 41.792  94.157  1.00 124.70 ?  380 TYR D CD1 1 
ATOM   6832  C CD2 . TYR C 2 48  ? -33.768 43.989  93.413  1.00 123.35 ?  380 TYR D CD2 1 
ATOM   6833  C CE1 . TYR C 2 48  ? -32.974 41.395  93.873  1.00 133.55 ?  380 TYR D CE1 1 
ATOM   6834  C CE2 . TYR C 2 48  ? -32.471 43.605  93.127  1.00 123.58 ?  380 TYR D CE2 1 
ATOM   6835  C CZ  . TYR C 2 48  ? -32.070 42.304  93.355  1.00 128.46 ?  380 TYR D CZ  1 
ATOM   6836  O OH  . TYR C 2 48  ? -30.783 41.963  93.059  1.00 114.58 ?  380 TYR D OH  1 
ATOM   6837  N N   . GLY C 2 49  ? -39.629 42.635  93.621  1.00 131.36 ?  381 GLY D N   1 
ATOM   6838  C CA  . GLY C 2 49  ? -40.899 43.372  93.742  1.00 136.77 ?  381 GLY D CA  1 
ATOM   6839  C C   . GLY C 2 49  ? -42.040 42.776  92.943  1.00 149.62 ?  381 GLY D C   1 
ATOM   6840  O O   . GLY C 2 49  ? -43.196 43.151  93.206  1.00 150.92 ?  381 GLY D O   1 
ATOM   6841  N N   . VAL C 2 50  ? -41.775 41.840  92.027  1.00 147.86 ?  382 VAL D N   1 
ATOM   6842  C CA  . VAL C 2 50  ? -42.916 41.200  91.302  1.00 146.34 ?  382 VAL D CA  1 
ATOM   6843  C C   . VAL C 2 50  ? -42.579 39.744  90.962  1.00 152.36 ?  382 VAL D C   1 
ATOM   6844  O O   . VAL C 2 50  ? -41.432 39.480  90.558  1.00 157.99 ?  382 VAL D O   1 
ATOM   6845  C CB  . VAL C 2 50  ? -43.280 41.999  90.037  1.00 141.78 ?  382 VAL D CB  1 
ATOM   6846  C CG1 . VAL C 2 50  ? -42.045 42.560  89.350  1.00 135.92 ?  382 VAL D CG1 1 
ATOM   6847  C CG2 . VAL C 2 50  ? -44.103 41.171  89.062  1.00 151.43 ?  382 VAL D CG2 1 
ATOM   6848  N N   . SER C 2 51  ? -43.551 38.842  91.112  1.00 152.41 ?  383 SER D N   1 
ATOM   6849  C CA  . SER C 2 51  ? -43.334 37.407  90.797  1.00 159.19 ?  383 SER D CA  1 
ATOM   6850  C C   . SER C 2 51  ? -42.622 37.291  89.454  1.00 163.92 ?  383 SER D C   1 
ATOM   6851  O O   . SER C 2 51  ? -42.976 38.047  88.545  1.00 166.31 ?  383 SER D O   1 
ATOM   6852  C CB  . SER C 2 51  ? -44.638 36.657  90.787  1.00 167.39 ?  383 SER D CB  1 
ATOM   6853  O OG  . SER C 2 51  ? -44.728 35.789  89.666  1.00 171.29 ?  383 SER D OG  1 
ATOM   6854  N N   . PRO C 2 52  ? -41.688 36.342  89.270  1.00 169.42 ?  384 PRO D N   1 
ATOM   6855  C CA  . PRO C 2 52  ? -40.899 36.287  88.034  1.00 174.49 ?  384 PRO D CA  1 
ATOM   6856  C C   . PRO C 2 52  ? -41.616 35.776  86.777  1.00 174.17 ?  384 PRO D C   1 
ATOM   6857  O O   . PRO C 2 52  ? -41.413 36.355  85.723  1.00 170.52 ?  384 PRO D O   1 
ATOM   6858  C CB  . PRO C 2 52  ? -39.809 35.267  88.384  1.00 181.63 ?  384 PRO D CB  1 
ATOM   6859  C CG  . PRO C 2 52  ? -40.460 34.367  89.413  1.00 179.70 ?  384 PRO D CG  1 
ATOM   6860  C CD  . PRO C 2 52  ? -41.352 35.284  90.222  1.00 170.77 ?  384 PRO D CD  1 
ATOM   6861  N N   . THR C 2 53  ? -42.410 34.714  86.896  1.00 175.82 ?  385 THR D N   1 
ATOM   6862  C CA  . THR C 2 53  ? -43.014 34.116  85.676  1.00 176.16 ?  385 THR D CA  1 
ATOM   6863  C C   . THR C 2 53  ? -44.315 34.821  85.310  1.00 171.16 ?  385 THR D C   1 
ATOM   6864  O O   . THR C 2 53  ? -44.719 34.742  84.139  1.00 166.66 ?  385 THR D O   1 
ATOM   6865  C CB  . THR C 2 53  ? -43.289 32.628  85.893  1.00 177.76 ?  385 THR D CB  1 
ATOM   6866  O OG1 . THR C 2 53  ? -43.194 32.367  87.294  1.00 175.25 ?  385 THR D OG1 1 
ATOM   6867  C CG2 . THR C 2 53  ? -42.329 31.739  85.131  1.00 190.28 ?  385 THR D CG2 1 
ATOM   6868  N N   . LYS C 2 54  ? -44.933 35.493  86.270  1.00 170.03 ?  386 LYS D N   1 
ATOM   6869  C CA  . LYS C 2 54  ? -46.266 36.095  86.024  1.00 167.95 ?  386 LYS D CA  1 
ATOM   6870  C C   . LYS C 2 54  ? -46.191 37.582  85.674  1.00 173.16 ?  386 LYS D C   1 
ATOM   6871  O O   . LYS C 2 54  ? -47.260 38.213  85.684  1.00 177.74 ?  386 LYS D O   1 
ATOM   6872  C CB  . LYS C 2 54  ? -47.148 35.957  87.263  1.00 159.60 ?  386 LYS D CB  1 
ATOM   6873  C CG  . LYS C 2 54  ? -47.414 34.530  87.714  1.00 156.66 ?  386 LYS D CG  1 
ATOM   6874  C CD  . LYS C 2 54  ? -48.451 34.421  88.842  1.00 148.11 ?  386 LYS D CD  1 
ATOM   6875  C CE  . LYS C 2 54  ? -49.854 34.814  88.426  1.00 143.41 ?  386 LYS D CE  1 
ATOM   6876  N NZ  . LYS C 2 54  ? -50.890 33.943  89.030  1.00 135.30 ?  386 LYS D NZ  1 
ATOM   6877  N N   . LEU C 2 55  ? -45.012 38.134  85.398  1.00 181.69 ?  387 LEU D N   1 
ATOM   6878  C CA  . LEU C 2 55  ? -45.043 39.560  84.982  1.00 183.09 ?  387 LEU D CA  1 
ATOM   6879  C C   . LEU C 2 55  ? -45.734 39.605  83.623  1.00 182.75 ?  387 LEU D C   1 
ATOM   6880  O O   . LEU C 2 55  ? -45.881 40.718  83.108  1.00 186.94 ?  387 LEU D O   1 
ATOM   6881  C CB  . LEU C 2 55  ? -43.659 40.196  84.862  1.00 173.55 ?  387 LEU D CB  1 
ATOM   6882  C CG  . LEU C 2 55  ? -42.442 39.283  84.978  1.00 167.19 ?  387 LEU D CG  1 
ATOM   6883  C CD1 . LEU C 2 55  ? -41.436 39.603  83.883  1.00 167.15 ?  387 LEU D CD1 1 
ATOM   6884  C CD2 . LEU C 2 55  ? -41.791 39.493  86.336  1.00 159.27 ?  387 LEU D CD2 1 
ATOM   6885  N N   . ASN C 2 56  ? -46.157 38.459  83.079  1.00 172.85 ?  388 ASN D N   1 
ATOM   6886  C CA  . ASN C 2 56  ? -46.874 38.558  81.804  1.00 167.25 ?  388 ASN D CA  1 
ATOM   6887  C C   . ASN C 2 56  ? -48.276 39.112  81.988  1.00 167.31 ?  388 ASN D C   1 
ATOM   6888  O O   . ASN C 2 56  ? -48.722 39.983  81.231  1.00 158.95 ?  388 ASN D O   1 
ATOM   6889  C CB  . ASN C 2 56  ? -46.978 37.188  81.137  1.00 156.70 ?  388 ASN D CB  1 
ATOM   6890  C CG  . ASN C 2 56  ? -45.665 36.685  80.649  1.00 152.36 ?  388 ASN D CG  1 
ATOM   6891  O OD1 . ASN C 2 56  ? -45.154 37.153  79.636  1.00 156.87 ?  388 ASN D OD1 1 
ATOM   6892  N ND2 . ASN C 2 56  ? -45.078 35.757  81.385  1.00 153.74 ?  388 ASN D ND2 1 
ATOM   6893  N N   . ASP C 2 57  ? -48.981 38.614  82.998  1.00 179.95 ?  389 ASP D N   1 
ATOM   6894  C CA  . ASP C 2 57  ? -50.410 38.832  83.141  1.00 188.93 ?  389 ASP D CA  1 
ATOM   6895  C C   . ASP C 2 57  ? -50.753 40.181  83.786  1.00 189.93 ?  389 ASP D C   1 
ATOM   6896  O O   . ASP C 2 57  ? -51.888 40.359  84.258  1.00 193.46 ?  389 ASP D O   1 
ATOM   6897  C CB  . ASP C 2 57  ? -51.018 37.664  83.928  1.00 190.57 ?  389 ASP D CB  1 
ATOM   6898  C CG  . ASP C 2 57  ? -50.504 36.301  83.447  1.00 184.10 ?  389 ASP D CG  1 
ATOM   6899  O OD1 . ASP C 2 57  ? -50.244 36.161  82.232  1.00 184.81 ?  389 ASP D OD1 1 
ATOM   6900  O OD2 . ASP C 2 57  ? -50.347 35.377  84.275  1.00 181.22 -1 389 ASP D OD2 1 
ATOM   6901  N N   . LEU C 2 58  ? -49.810 41.128  83.807  1.00 169.57 ?  390 LEU D N   1 
ATOM   6902  C CA  . LEU C 2 58  ? -50.062 42.469  84.325  1.00 164.85 ?  390 LEU D CA  1 
ATOM   6903  C C   . LEU C 2 58  ? -49.390 43.462  83.389  1.00 161.90 ?  390 LEU D C   1 
ATOM   6904  O O   . LEU C 2 58  ? -48.201 43.325  83.083  1.00 158.88 ?  390 LEU D O   1 
ATOM   6905  C CB  . LEU C 2 58  ? -49.549 42.625  85.768  1.00 159.07 ?  390 LEU D CB  1 
ATOM   6906  C CG  . LEU C 2 58  ? -49.813 43.929  86.551  1.00 155.59 ?  390 LEU D CG  1 
ATOM   6907  C CD1 . LEU C 2 58  ? -51.299 44.296  86.628  1.00 151.16 ?  390 LEU D CD1 1 
ATOM   6908  C CD2 . LEU C 2 58  ? -49.217 43.863  87.948  1.00 144.42 ?  390 LEU D CD2 1 
ATOM   6909  N N   . CYS C 2 59  ? -50.161 44.435  82.912  1.00 159.19 ?  391 CYS D N   1 
ATOM   6910  C CA  . CYS C 2 59  ? -49.645 45.506  82.075  1.00 162.47 ?  391 CYS D CA  1 
ATOM   6911  C C   . CYS C 2 59  ? -49.186 46.685  82.909  1.00 158.50 ?  391 CYS D C   1 
ATOM   6912  O O   . CYS C 2 59  ? -49.783 47.029  83.934  1.00 158.21 ?  391 CYS D O   1 
ATOM   6913  C CB  . CYS C 2 59  ? -50.686 45.972  81.059  1.00 164.87 ?  391 CYS D CB  1 
ATOM   6914  S SG  . CYS C 2 59  ? -51.448 44.643  80.127  1.00 173.61 ?  391 CYS D SG  1 
ATOM   6915  N N   . PHE C 2 60  ? -48.125 47.317  82.439  1.00 157.55 ?  392 PHE D N   1 
ATOM   6916  C CA  . PHE C 2 60  ? -47.473 48.382  83.165  1.00 161.70 ?  392 PHE D CA  1 
ATOM   6917  C C   . PHE C 2 60  ? -47.531 49.644  82.325  1.00 162.43 ?  392 PHE D C   1 
ATOM   6918  O O   . PHE C 2 60  ? -47.597 49.580  81.095  1.00 160.76 ?  392 PHE D O   1 
ATOM   6919  C CB  . PHE C 2 60  ? -46.037 47.989  83.483  1.00 159.71 ?  392 PHE D CB  1 
ATOM   6920  C CG  . PHE C 2 60  ? -45.944 46.862  84.463  1.00 154.92 ?  392 PHE D CG  1 
ATOM   6921  C CD1 . PHE C 2 60  ? -46.193 47.075  85.811  1.00 157.00 ?  392 PHE D CD1 1 
ATOM   6922  C CD2 . PHE C 2 60  ? -45.641 45.579  84.030  1.00 147.39 ?  392 PHE D CD2 1 
ATOM   6923  C CE1 . PHE C 2 60  ? -46.134 46.030  86.714  1.00 153.08 ?  392 PHE D CE1 1 
ATOM   6924  C CE2 . PHE C 2 60  ? -45.569 44.532  84.926  1.00 148.31 ?  392 PHE D CE2 1 
ATOM   6925  C CZ  . PHE C 2 60  ? -45.816 44.754  86.270  1.00 151.49 ?  392 PHE D CZ  1 
ATOM   6926  N N   . THR C 2 61  ? -47.516 50.793  83.000  1.00 170.20 ?  393 THR D N   1 
ATOM   6927  C CA  . THR C 2 61  ? -47.684 52.056  82.290  1.00 176.45 ?  393 THR D CA  1 
ATOM   6928  C C   . THR C 2 61  ? -46.446 52.423  81.466  1.00 184.79 ?  393 THR D C   1 
ATOM   6929  O O   . THR C 2 61  ? -46.571 52.966  80.361  1.00 177.86 ?  393 THR D O   1 
ATOM   6930  C CB  . THR C 2 61  ? -48.054 53.167  83.278  1.00 182.71 ?  393 THR D CB  1 
ATOM   6931  O OG1 . THR C 2 61  ? -48.248 54.393  82.570  1.00 189.08 ?  393 THR D OG1 1 
ATOM   6932  C CG2 . THR C 2 61  ? -46.984 53.373  84.293  1.00 180.96 ?  393 THR D CG2 1 
ATOM   6933  N N   . ASN C 2 62  ? -45.248 52.122  81.968  1.00 218.38 ?  394 ASN D N   1 
ATOM   6934  C CA  . ASN C 2 62  ? -44.016 52.468  81.262  1.00 210.66 ?  394 ASN D CA  1 
ATOM   6935  C C   . ASN C 2 62  ? -42.917 51.584  81.830  1.00 202.58 ?  394 ASN D C   1 
ATOM   6936  O O   . ASN C 2 62  ? -42.501 51.793  82.972  1.00 202.46 ?  394 ASN D O   1 
ATOM   6937  C CB  . ASN C 2 62  ? -43.664 53.949  81.449  1.00 209.44 ?  394 ASN D CB  1 
ATOM   6938  C CG  . ASN C 2 62  ? -43.819 54.778  80.170  1.00 210.99 ?  394 ASN D CG  1 
ATOM   6939  O OD1 . ASN C 2 62  ? -44.360 54.311  79.164  1.00 207.92 ?  394 ASN D OD1 1 
ATOM   6940  N ND2 . ASN C 2 62  ? -43.324 56.015  80.210  1.00 208.62 ?  394 ASN D ND2 1 
ATOM   6941  N N   . VAL C 2 63  ? -42.452 50.594  81.068  1.00 157.95 ?  395 VAL D N   1 
ATOM   6942  C CA  . VAL C 2 63  ? -41.282 49.843  81.489  1.00 140.91 ?  395 VAL D CA  1 
ATOM   6943  C C   . VAL C 2 63  ? -40.030 50.623  81.111  1.00 138.02 ?  395 VAL D C   1 
ATOM   6944  O O   . VAL C 2 63  ? -39.933 51.162  80.006  1.00 140.59 ?  395 VAL D O   1 
ATOM   6945  C CB  . VAL C 2 63  ? -41.292 48.447  80.864  1.00 129.17 ?  395 VAL D CB  1 
ATOM   6946  C CG1 . VAL C 2 63  ? -40.150 47.657  81.407  1.00 122.93 ?  395 VAL D CG1 1 
ATOM   6947  C CG2 . VAL C 2 63  ? -42.547 47.774  81.247  1.00 130.10 ?  395 VAL D CG2 1 
ATOM   6948  N N   . TYR C 2 64  ? -39.089 50.729  82.040  1.00 118.07 ?  396 TYR D N   1 
ATOM   6949  C CA  . TYR C 2 64  ? -37.822 51.401  81.790  1.00 113.77 ?  396 TYR D CA  1 
ATOM   6950  C C   . TYR C 2 64  ? -36.727 50.341  81.867  1.00 105.80 ?  396 TYR D C   1 
ATOM   6951  O O   . TYR C 2 64  ? -36.664 49.596  82.850  1.00 104.87 ?  396 TYR D O   1 
ATOM   6952  C CB  . TYR C 2 64  ? -37.595 52.512  82.817  1.00 114.23 ?  396 TYR D CB  1 
ATOM   6953  C CG  . TYR C 2 64  ? -38.346 53.821  82.565  1.00 120.73 ?  396 TYR D CG  1 
ATOM   6954  C CD1 . TYR C 2 64  ? -38.448 54.361  81.289  1.00 122.71 ?  396 TYR D CD1 1 
ATOM   6955  C CD2 . TYR C 2 64  ? -38.973 54.505  83.614  1.00 127.39 ?  396 TYR D CD2 1 
ATOM   6956  C CE1 . TYR C 2 64  ? -39.134 55.559  81.065  1.00 138.29 ?  396 TYR D CE1 1 
ATOM   6957  C CE2 . TYR C 2 64  ? -39.658 55.702  83.397  1.00 133.61 ?  396 TYR D CE2 1 
ATOM   6958  C CZ  . TYR C 2 64  ? -39.734 56.219  82.120  1.00 141.72 ?  396 TYR D CZ  1 
ATOM   6959  O OH  . TYR C 2 64  ? -40.411 57.394  81.883  1.00 147.85 ?  396 TYR D OH  1 
ATOM   6960  N N   . ALA C 2 65  ? -35.887 50.229  80.827  1.00 105.63 ?  397 ALA D N   1 
ATOM   6961  C CA  . ALA C 2 65  ? -34.822 49.218  80.815  1.00 101.16 ?  397 ALA D CA  1 
ATOM   6962  C C   . ALA C 2 65  ? -33.457 49.912  80.897  1.00 99.65  ?  397 ALA D C   1 
ATOM   6963  O O   . ALA C 2 65  ? -32.987 50.496  79.909  1.00 101.33 ?  397 ALA D O   1 
ATOM   6964  C CB  . ALA C 2 65  ? -34.922 48.325  79.581  1.00 100.94 ?  397 ALA D CB  1 
ATOM   6965  N N   . ASP C 2 66  ? -32.830 49.866  82.080  1.00 97.44  ?  398 ASP D N   1 
ATOM   6966  C CA  . ASP C 2 66  ? -31.484 50.374  82.243  1.00 87.66  ?  398 ASP D CA  1 
ATOM   6967  C C   . ASP C 2 66  ? -30.471 49.280  81.983  1.00 87.35  ?  398 ASP D C   1 
ATOM   6968  O O   . ASP C 2 66  ? -30.608 48.160  82.474  1.00 84.75  ?  398 ASP D O   1 
ATOM   6969  C CB  . ASP C 2 66  ? -31.294 50.927  83.638  1.00 87.90  ?  398 ASP D CB  1 
ATOM   6970  C CG  . ASP C 2 66  ? -32.407 51.792  84.046  1.00 92.94  ?  398 ASP D CG  1 
ATOM   6971  O OD1 . ASP C 2 66  ? -32.940 52.480  83.174  1.00 96.36  ?  398 ASP D OD1 1 
ATOM   6972  O OD2 . ASP C 2 66  ? -32.769 51.774  85.226  1.00 95.91  -1 398 ASP D OD2 1 
ATOM   6973  N N   . SER C 2 67  ? -29.440 49.613  81.224  1.00 84.28  ?  399 SER D N   1 
ATOM   6974  C CA  . SER C 2 67  ? -28.386 48.641  80.975  1.00 78.97  ?  399 SER D CA  1 
ATOM   6975  C C   . SER C 2 67  ? -27.026 49.265  81.266  1.00 78.78  ?  399 SER D C   1 
ATOM   6976  O O   . SER C 2 67  ? -26.778 50.424  80.906  1.00 80.92  ?  399 SER D O   1 
ATOM   6977  C CB  . SER C 2 67  ? -28.470 48.092  79.522  1.00 81.92  ?  399 SER D CB  1 
ATOM   6978  O OG  . SER C 2 67  ? -28.637 49.105  78.544  1.00 81.63  ?  399 SER D OG  1 
ATOM   6979  N N   . PHE C 2 68  ? -26.145 48.478  81.887  1.00 74.80  ?  400 PHE D N   1 
ATOM   6980  C CA  . PHE C 2 68  ? -24.768 48.954  82.175  1.00 75.35  ?  400 PHE D CA  1 
ATOM   6981  C C   . PHE C 2 68  ? -23.853 47.746  82.377  1.00 73.26  ?  400 PHE D C   1 
ATOM   6982  O O   . PHE C 2 68  ? -24.282 46.610  82.134  1.00 75.03  ?  400 PHE D O   1 
ATOM   6983  C CB  . PHE C 2 68  ? -24.723 49.883  83.386  1.00 72.82  ?  400 PHE D CB  1 
ATOM   6984  C CG  . PHE C 2 68  ? -25.439 49.417  84.629  1.00 74.74  ?  400 PHE D CG  1 
ATOM   6985  C CD1 . PHE C 2 68  ? -26.788 49.672  84.800  1.00 77.55  ?  400 PHE D CD1 1 
ATOM   6986  C CD2 . PHE C 2 68  ? -24.754 48.773  85.644  1.00 66.94  ?  400 PHE D CD2 1 
ATOM   6987  C CE1 . PHE C 2 68  ? -27.444 49.259  85.947  1.00 74.36  ?  400 PHE D CE1 1 
ATOM   6988  C CE2 . PHE C 2 68  ? -25.415 48.363  86.791  1.00 63.65  ?  400 PHE D CE2 1 
ATOM   6989  C CZ  . PHE C 2 68  ? -26.758 48.606  86.938  1.00 67.54  ?  400 PHE D CZ  1 
ATOM   6990  N N   . VAL C 2 69  ? -22.609 47.994  82.777  1.00 75.49  ?  401 VAL D N   1 
ATOM   6991  C CA  . VAL C 2 69  ? -21.656 46.884  83.040  1.00 74.73  ?  401 VAL D CA  1 
ATOM   6992  C C   . VAL C 2 69  ? -21.058 47.116  84.423  1.00 71.17  ?  401 VAL D C   1 
ATOM   6993  O O   . VAL C 2 69  ? -20.745 48.276  84.742  1.00 72.27  ?  401 VAL D O   1 
ATOM   6994  C CB  . VAL C 2 69  ? -20.580 46.791  81.948  1.00 70.67  ?  401 VAL D CB  1 
ATOM   6995  C CG1 . VAL C 2 69  ? -19.229 47.284  82.435  1.00 76.36  ?  401 VAL D CG1 1 
ATOM   6996  C CG2 . VAL C 2 69  ? -20.471 45.384  81.377  1.00 68.53  ?  401 VAL D CG2 1 
ATOM   6997  N N   . ILE C 2 70  ? -20.814 46.043  85.166  1.00 74.28  ?  402 ILE D N   1 
ATOM   6998  C CA  . ILE C 2 70  ? -20.123 46.176  86.478  1.00 69.09  ?  402 ILE D CA  1 
ATOM   6999  C C   . ILE C 2 70  ? -19.276 44.925  86.694  1.00 69.69  ?  402 ILE D C   1 
ATOM   7000  O O   . ILE C 2 70  ? -19.325 44.018  85.842  1.00 71.21  ?  402 ILE D O   1 
ATOM   7001  C CB  . ILE C 2 70  ? -21.137 46.389  87.614  1.00 64.52  ?  402 ILE D CB  1 
ATOM   7002  C CG1 . ILE C 2 70  ? -22.240 45.330  87.622  1.00 67.53  ?  402 ILE D CG1 1 
ATOM   7003  C CG2 . ILE C 2 70  ? -21.728 47.784  87.553  1.00 57.10  ?  402 ILE D CG2 1 
ATOM   7004  C CD1 . ILE C 2 70  ? -23.304 45.610  88.653  1.00 65.97  ?  402 ILE D CD1 1 
ATOM   7005  N N   . ARG C 2 71  ? -18.500 44.888  87.768  1.00 61.98  ?  403 ARG D N   1 
ATOM   7006  C CA  . ARG C 2 71  ? -17.755 43.651  88.092  1.00 64.39  ?  403 ARG D CA  1 
ATOM   7007  C C   . ARG C 2 71  ? -18.623 42.807  89.018  1.00 69.71  ?  403 ARG D C   1 
ATOM   7008  O O   . ARG C 2 71  ? -19.470 43.384  89.712  1.00 73.35  ?  403 ARG D O   1 
ATOM   7009  C CB  . ARG C 2 71  ? -16.465 43.944  88.858  1.00 70.06  ?  403 ARG D CB  1 
ATOM   7010  C CG  . ARG C 2 71  ? -15.684 45.170  88.415  1.00 77.27  ?  403 ARG D CG  1 
ATOM   7011  C CD  . ARG C 2 71  ? -14.572 45.406  89.417  1.00 76.93  ?  403 ARG D CD  1 
ATOM   7012  N NE  . ARG C 2 71  ? -14.945 45.016  90.771  1.00 85.10  ?  403 ARG D NE  1 
ATOM   7013  C CZ  . ARG C 2 71  ? -14.202 45.203  91.858  1.00 88.72  ?  403 ARG D CZ  1 
ATOM   7014  N NH1 . ARG C 2 71  ? -13.017 45.780  91.764  1.00 93.79  ?  403 ARG D NH1 1 
ATOM   7015  N NH2 . ARG C 2 71  ? -14.646 44.814  93.041  1.00 82.94  ?  403 ARG D NH2 1 
ATOM   7016  N N   . GLY C 2 72  ? -18.449 41.491  88.994  1.00 74.82  ?  404 GLY D N   1 
ATOM   7017  C CA  . GLY C 2 72  ? -19.325 40.628  89.805  1.00 76.07  ?  404 GLY D CA  1 
ATOM   7018  C C   . GLY C 2 72  ? -19.433 41.151  91.219  1.00 76.86  ?  404 GLY D C   1 
ATOM   7019  O O   . GLY C 2 72  ? -20.561 41.316  91.705  1.00 77.47  ?  404 GLY D O   1 
ATOM   7020  N N   . ASN C 2 73  ? -18.293 41.412  91.854  1.00 81.97  ?  405 ASN D N   1 
ATOM   7021  C CA  . ASN C 2 73  ? -18.297 41.880  93.258  1.00 89.26  ?  405 ASN D CA  1 
ATOM   7022  C C   . ASN C 2 73  ? -19.279 43.035  93.413  1.00 91.03  ?  405 ASN D C   1 
ATOM   7023  O O   . ASN C 2 73  ? -19.682 43.293  94.549  1.00 92.73  ?  405 ASN D O   1 
ATOM   7024  C CB  . ASN C 2 73  ? -16.931 42.390  93.715  1.00 96.14  ?  405 ASN D CB  1 
ATOM   7025  C CG  . ASN C 2 73  ? -15.766 41.476  93.402  1.00 103.44 ?  405 ASN D CG  1 
ATOM   7026  O OD1 . ASN C 2 73  ? -14.762 41.913  92.845  1.00 105.05 ?  405 ASN D OD1 1 
ATOM   7027  N ND2 . ASN C 2 73  ? -15.874 40.215  93.777  1.00 107.19 ?  405 ASN D ND2 1 
ATOM   7028  N N   . GLU C 2 74  ? -19.621 43.722  92.328  1.00 76.32  ?  406 GLU D N   1 
ATOM   7029  C CA  . GLU C 2 74  ? -20.469 44.931  92.476  1.00 69.35  ?  406 GLU D CA  1 
ATOM   7030  C C   . GLU C 2 74  ? -21.938 44.574  92.278  1.00 67.56  ?  406 GLU D C   1 
ATOM   7031  O O   . GLU C 2 74  ? -22.790 45.306  92.789  1.00 64.52  ?  406 GLU D O   1 
ATOM   7032  C CB  . GLU C 2 74  ? -20.035 45.986  91.461  1.00 73.19  ?  406 GLU D CB  1 
ATOM   7033  C CG  . GLU C 2 74  ? -19.463 47.230  92.100  1.00 68.74  ?  406 GLU D CG  1 
ATOM   7034  C CD  . GLU C 2 74  ? -18.049 47.545  91.652  1.00 74.14  ?  406 GLU D CD  1 
ATOM   7035  O OE1 . GLU C 2 74  ? -17.508 46.783  90.830  1.00 90.63  ?  406 GLU D OE1 1 
ATOM   7036  O OE2 . GLU C 2 74  ? -17.494 48.549  92.130  1.00 78.07  -1 406 GLU D OE2 1 
ATOM   7037  N N   . VAL C 2 75  ? -22.215 43.473  91.592  1.00 67.19  ?  407 VAL D N   1 
ATOM   7038  C CA  . VAL C 2 75  ? -23.605 43.125  91.268  1.00 68.76  ?  407 VAL D CA  1 
ATOM   7039  C C   . VAL C 2 75  ? -24.478 43.123  92.522  1.00 72.23  ?  407 VAL D C   1 
ATOM   7040  O O   . VAL C 2 75  ? -25.617 43.607  92.506  1.00 74.26  ?  407 VAL D O   1 
ATOM   7041  C CB  . VAL C 2 75  ? -23.664 41.781  90.546  1.00 65.44  ?  407 VAL D CB  1 
ATOM   7042  C CG1 . VAL C 2 75  ? -25.005 41.126  90.769  1.00 65.15  ?  407 VAL D CG1 1 
ATOM   7043  C CG2 . VAL C 2 75  ? -23.432 41.993  89.096  1.00 72.25  ?  407 VAL D CG2 1 
ATOM   7044  N N   . SER C 2 76  ? -23.941 42.596  93.634  1.00 68.32  ?  408 SER D N   1 
ATOM   7045  C CA  . SER C 2 76  ? -24.603 42.582  94.940  1.00 64.58  ?  408 SER D CA  1 
ATOM   7046  C C   . SER C 2 76  ? -25.265 43.911  95.271  1.00 67.65  ?  408 SER D C   1 
ATOM   7047  O O   . SER C 2 76  ? -26.243 43.947  96.020  1.00 70.83  ?  408 SER D O   1 
ATOM   7048  C CB  . SER C 2 76  ? -23.564 42.276  96.018  1.00 68.83  ?  408 SER D CB  1 
ATOM   7049  O OG  . SER C 2 76  ? -22.773 41.141  95.679  1.00 77.00  ?  408 SER D OG  1 
ATOM   7050  N N   . GLN C 2 77  ? -24.721 45.007  94.748  1.00 70.09  ?  409 GLN D N   1 
ATOM   7051  C CA  . GLN C 2 77  ? -25.227 46.331  95.057  1.00 73.59  ?  409 GLN D CA  1 
ATOM   7052  C C   . GLN C 2 77  ? -26.410 46.729  94.190  1.00 75.78  ?  409 GLN D C   1 
ATOM   7053  O O   . GLN C 2 77  ? -27.119 47.690  94.524  1.00 76.91  ?  409 GLN D O   1 
ATOM   7054  C CB  . GLN C 2 77  ? -24.140 47.394  94.879  1.00 71.75  ?  409 GLN D CB  1 
ATOM   7055  C CG  . GLN C 2 77  ? -23.036 47.406  95.911  1.00 70.69  ?  409 GLN D CG  1 
ATOM   7056  C CD  . GLN C 2 77  ? -21.723 47.868  95.311  1.00 69.11  ?  409 GLN D CD  1 
ATOM   7057  O OE1 . GLN C 2 77  ? -21.651 49.007  94.845  1.00 70.23  ?  409 GLN D OE1 1 
ATOM   7058  N NE2 . GLN C 2 77  ? -20.704 47.006  95.278  1.00 68.62  ?  409 GLN D NE2 1 
ATOM   7059  N N   . ILE C 2 78  ? -26.626 46.052  93.068  1.00 71.47  ?  410 ILE D N   1 
ATOM   7060  C CA  . ILE C 2 78  ? -27.737 46.458  92.224  1.00 70.50  ?  410 ILE D CA  1 
ATOM   7061  C C   . ILE C 2 78  ? -28.956 45.803  92.839  1.00 80.39  ?  410 ILE D C   1 
ATOM   7062  O O   . ILE C 2 78  ? -29.427 44.751  92.393  1.00 83.53  ?  410 ILE D O   1 
ATOM   7063  C CB  . ILE C 2 78  ? -27.521 46.072  90.762  1.00 69.43  ?  410 ILE D CB  1 
ATOM   7064  C CG1 . ILE C 2 78  ? -26.241 46.737  90.252  1.00 70.86  ?  410 ILE D CG1 1 
ATOM   7065  C CG2 . ILE C 2 78  ? -28.688 46.516  89.932  1.00 73.55  ?  410 ILE D CG2 1 
ATOM   7066  C CD1 . ILE C 2 78  ? -26.138 48.220  90.536  1.00 71.15  ?  410 ILE D CD1 1 
ATOM   7067  N N   . ALA C 2 79  ? -29.428 46.412  93.907  1.00 82.20  ?  411 ALA D N   1 
ATOM   7068  C CA  . ALA C 2 79  ? -30.392 45.838  94.823  1.00 86.66  ?  411 ALA D CA  1 
ATOM   7069  C C   . ALA C 2 79  ? -30.904 46.972  95.694  1.00 88.95  ?  411 ALA D C   1 
ATOM   7070  O O   . ALA C 2 79  ? -30.164 47.931  95.961  1.00 86.92  ?  411 ALA D O   1 
ATOM   7071  C CB  . ALA C 2 79  ? -29.754 44.729  95.665  1.00 92.42  ?  411 ALA D CB  1 
ATOM   7072  N N   . PRO C 2 80  ? -32.158 46.912  96.146  1.00 95.75  ?  412 PRO D N   1 
ATOM   7073  C CA  . PRO C 2 80  ? -32.686 48.010  96.961  1.00 96.94  ?  412 PRO D CA  1 
ATOM   7074  C C   . PRO C 2 80  ? -31.976 48.048  98.303  1.00 95.24  ?  412 PRO D C   1 
ATOM   7075  O O   . PRO C 2 80  ? -31.777 47.016  98.945  1.00 91.44  ?  412 PRO D O   1 
ATOM   7076  C CB  . PRO C 2 80  ? -34.173 47.667  97.100  1.00 95.63  ?  412 PRO D CB  1 
ATOM   7077  C CG  . PRO C 2 80  ? -34.207 46.171  97.041  1.00 98.49  ?  412 PRO D CG  1 
ATOM   7078  C CD  . PRO C 2 80  ? -33.061 45.741  96.153  1.00 101.71 ?  412 PRO D CD  1 
ATOM   7079  N N   . GLY C 2 81  ? -31.563 49.234  98.693  1.00 97.24  ?  413 GLY D N   1 
ATOM   7080  C CA  . GLY C 2 81  ? -30.964 49.425  100.005 1.00 100.07 ?  413 GLY D CA  1 
ATOM   7081  C C   . GLY C 2 81  ? -29.465 49.266  100.074 1.00 99.86  ?  413 GLY D C   1 
ATOM   7082  O O   . GLY C 2 81  ? -28.793 50.048  100.748 1.00 94.94  ?  413 GLY D O   1 
ATOM   7083  N N   . GLN C 2 82  ? -28.939 48.243  99.394  1.00 101.02 ?  414 GLN D N   1 
ATOM   7084  C CA  . GLN C 2 82  ? -27.502 48.023  99.242  1.00 98.93  ?  414 GLN D CA  1 
ATOM   7085  C C   . GLN C 2 82  ? -26.773 49.330  98.961  1.00 97.09  ?  414 GLN D C   1 
ATOM   7086  O O   . GLN C 2 82  ? -27.139 50.077  98.054  1.00 103.31 ?  414 GLN D O   1 
ATOM   7087  C CB  . GLN C 2 82  ? -27.235 47.023  98.104  1.00 90.71  ?  414 GLN D CB  1 
ATOM   7088  C CG  . GLN C 2 82  ? -27.530 45.613  98.494  1.00 90.14  ?  414 GLN D CG  1 
ATOM   7089  C CD  . GLN C 2 82  ? -26.582 45.163  99.568  1.00 101.13 ?  414 GLN D CD  1 
ATOM   7090  O OE1 . GLN C 2 82  ? -25.407 45.536  99.555  1.00 103.24 ?  414 GLN D OE1 1 
ATOM   7091  N NE2 . GLN C 2 82  ? -27.097 44.443  100.560 1.00 106.55 ?  414 GLN D NE2 1 
ATOM   7092  N N   . THR C 2 83  ? -25.755 49.633  99.762  1.00 93.96  ?  415 THR D N   1 
ATOM   7093  C CA  . THR C 2 83  ? -24.864 50.768  99.501  1.00 90.59  ?  415 THR D CA  1 
ATOM   7094  C C   . THR C 2 83  ? -23.461 50.233  99.605  1.00 80.04  ?  415 THR D C   1 
ATOM   7095  O O   . THR C 2 83  ? -22.898 50.191  100.699 1.00 73.59  ?  415 THR D O   1 
ATOM   7096  C CB  . THR C 2 83  ? -25.008 51.947  100.439 1.00 89.58  ?  415 THR D CB  1 
ATOM   7097  O OG1 . THR C 2 83  ? -24.243 51.692  101.638 1.00 76.11  ?  415 THR D OG1 1 
ATOM   7098  C CG2 . THR C 2 83  ? -26.514 52.295  100.699 1.00 88.92  ?  415 THR D CG2 1 
ATOM   7099  N N   . GLY C 2 84  ? -22.944 49.802  98.474  1.00 82.89  ?  416 GLY D N   1 
ATOM   7100  C CA  . GLY C 2 84  ? -21.534 49.734  98.240  1.00 82.52  ?  416 GLY D CA  1 
ATOM   7101  C C   . GLY C 2 84  ? -21.023 51.042  97.669  1.00 80.78  ?  416 GLY D C   1 
ATOM   7102  O O   . GLY C 2 84  ? -21.521 52.120  97.998  1.00 77.11  ?  416 GLY D O   1 
ATOM   7103  N N   . ASN C 2 85  ? -19.984 50.921  96.841  1.00 79.29  ?  417 ASN D N   1 
ATOM   7104  C CA  . ASN C 2 85  ? -19.386 52.029  96.107  1.00 74.82  ?  417 ASN D CA  1 
ATOM   7105  C C   . ASN C 2 85  ? -20.214 52.424  94.904  1.00 72.22  ?  417 ASN D C   1 
ATOM   7106  O O   . ASN C 2 85  ? -20.157 53.571  94.452  1.00 74.30  ?  417 ASN D O   1 
ATOM   7107  C CB  . ASN C 2 85  ? -17.999 51.624  95.614  1.00 77.30  ?  417 ASN D CB  1 
ATOM   7108  C CG  . ASN C 2 85  ? -17.122 52.812  95.272  1.00 80.33  ?  417 ASN D CG  1 
ATOM   7109  O OD1 . ASN C 2 85  ? -17.513 53.977  95.417  1.00 73.23  ?  417 ASN D OD1 1 
ATOM   7110  N ND2 . ASN C 2 85  ? -15.942 52.517  94.747  1.00 84.46  ?  417 ASN D ND2 1 
ATOM   7111  N N   . ILE C 2 86  ? -20.950 51.490  94.332  1.00 75.02  ?  418 ILE D N   1 
ATOM   7112  C CA  . ILE C 2 86  ? -21.524 51.818  93.062  1.00 76.48  ?  418 ILE D CA  1 
ATOM   7113  C C   . ILE C 2 86  ? -22.960 52.281  93.268  1.00 77.96  ?  418 ILE D C   1 
ATOM   7114  O O   . ILE C 2 86  ? -23.414 53.197  92.591  1.00 79.28  ?  418 ILE D O   1 
ATOM   7115  C CB  . ILE C 2 86  ? -21.407 50.600  92.159  1.00 71.24  ?  418 ILE D CB  1 
ATOM   7116  C CG1 . ILE C 2 86  ? -21.238 51.068  90.759  1.00 74.31  ?  418 ILE D CG1 1 
ATOM   7117  C CG2 . ILE C 2 86  ? -22.725 49.873  92.065  1.00 69.44  ?  418 ILE D CG2 1 
ATOM   7118  C CD1 . ILE C 2 86  ? -20.741 50.037  89.888  1.00 74.94  ?  418 ILE D CD1 1 
ATOM   7119  N N   . ALA C 2 87  ? -23.624 51.715  94.267  1.00 75.44  ?  419 ALA D N   1 
ATOM   7120  C CA  . ALA C 2 87  ? -25.048 52.040  94.480  1.00 75.99  ?  419 ALA D CA  1 
ATOM   7121  C C   . ALA C 2 87  ? -25.189 53.365  95.221  1.00 79.82  ?  419 ALA D C   1 
ATOM   7122  O O   . ALA C 2 87  ? -26.312 53.694  95.607  1.00 85.17  ?  419 ALA D O   1 
ATOM   7123  C CB  . ALA C 2 87  ? -25.691 50.934  95.263  1.00 76.76  ?  419 ALA D CB  1 
ATOM   7124  N N   . ASP C 2 88  ? -24.104 54.105  95.400  1.00 81.86  ?  420 ASP D N   1 
ATOM   7125  C CA  . ASP C 2 88  ? -24.262 55.422  96.058  1.00 85.92  ?  420 ASP D CA  1 
ATOM   7126  C C   . ASP C 2 88  ? -23.550 56.474  95.220  1.00 85.60  ?  420 ASP D C   1 
ATOM   7127  O O   . ASP C 2 88  ? -23.769 57.670  95.462  1.00 89.37  ?  420 ASP D O   1 
ATOM   7128  C CB  . ASP C 2 88  ? -23.725 55.383  97.485  1.00 92.35  ?  420 ASP D CB  1 
ATOM   7129  C CG  . ASP C 2 88  ? -22.304 54.870  97.573  1.00 88.07  ?  420 ASP D CG  1 
ATOM   7130  O OD1 . ASP C 2 88  ? -21.728 54.550  96.516  1.00 86.29  ?  420 ASP D OD1 1 
ATOM   7131  O OD2 . ASP C 2 88  ? -21.797 54.773  98.701  1.00 90.54  -1 420 ASP D OD2 1 
ATOM   7132  N N   . TYR C 2 89  ? -22.725 56.028  94.282  1.00 74.35  ?  421 TYR D N   1 
ATOM   7133  C CA  . TYR C 2 89  ? -21.945 56.984  93.470  1.00 73.56  ?  421 TYR D CA  1 
ATOM   7134  C C   . TYR C 2 89  ? -22.193 56.708  91.987  1.00 75.62  ?  421 TYR D C   1 
ATOM   7135  O O   . TYR C 2 89  ? -21.687 57.485  91.167  1.00 76.47  ?  421 TYR D O   1 
ATOM   7136  C CB  . TYR C 2 89  ? -20.458 56.858  93.790  1.00 78.25  ?  421 TYR D CB  1 
ATOM   7137  C CG  . TYR C 2 89  ? -19.994 57.563  95.038  1.00 79.92  ?  421 TYR D CG  1 
ATOM   7138  C CD1 . TYR C 2 89  ? -20.752 58.559  95.626  1.00 80.51  ?  421 TYR D CD1 1 
ATOM   7139  C CD2 . TYR C 2 89  ? -18.787 57.237  95.631  1.00 79.05  ?  421 TYR D CD2 1 
ATOM   7140  C CE1 . TYR C 2 89  ? -20.328 59.209  96.772  1.00 79.15  ?  421 TYR D CE1 1 
ATOM   7141  C CE2 . TYR C 2 89  ? -18.347 57.877  96.777  1.00 78.51  ?  421 TYR D CE2 1 
ATOM   7142  C CZ  . TYR C 2 89  ? -19.120 58.867  97.349  1.00 81.90  ?  421 TYR D CZ  1 
ATOM   7143  O OH  . TYR C 2 89  ? -18.703 59.509  98.479  1.00 90.05  ?  421 TYR D OH  1 
ATOM   7144  N N   . ASN C 2 90  ? -22.930 55.647  91.647  1.00 83.11  ?  422 ASN D N   1 
ATOM   7145  C CA  . ASN C 2 90  ? -23.121 55.422  90.215  1.00 80.55  ?  422 ASN D CA  1 
ATOM   7146  C C   . ASN C 2 90  ? -24.582 55.191  89.852  1.00 81.64  ?  422 ASN D C   1 
ATOM   7147  O O   . ASN C 2 90  ? -25.116 55.897  88.996  1.00 87.22  ?  422 ASN D O   1 
ATOM   7148  C CB  . ASN C 2 90  ? -22.300 54.227  89.770  1.00 81.87  ?  422 ASN D CB  1 
ATOM   7149  C CG  . ASN C 2 90  ? -20.877 54.596  89.469  1.00 81.18  ?  422 ASN D CG  1 
ATOM   7150  O OD1 . ASN C 2 90  ? -20.567 55.765  89.340  1.00 84.55  ?  422 ASN D OD1 1 
ATOM   7151  N ND2 . ASN C 2 90  ? -20.004 53.611  89.346  1.00 83.85  ?  422 ASN D ND2 1 
ATOM   7152  N N   . TYR C 2 91  ? -25.227 54.203  90.484  1.00 80.73  ?  423 TYR D N   1 
ATOM   7153  C CA  . TYR C 2 91  ? -26.578 53.786  90.090  1.00 76.92  ?  423 TYR D CA  1 
ATOM   7154  C C   . TYR C 2 91  ? -27.317 53.228  91.305  1.00 76.25  ?  423 TYR D C   1 
ATOM   7155  O O   . TYR C 2 91  ? -27.078 52.082  91.700  1.00 75.27  ?  423 TYR D O   1 
ATOM   7156  C CB  . TYR C 2 91  ? -26.506 52.735  88.995  1.00 71.63  ?  423 TYR D CB  1 
ATOM   7157  C CG  . TYR C 2 91  ? -27.855 52.189  88.626  1.00 79.14  ?  423 TYR D CG  1 
ATOM   7158  C CD1 . TYR C 2 91  ? -28.796 52.986  87.963  1.00 84.49  ?  423 TYR D CD1 1 
ATOM   7159  C CD2 . TYR C 2 91  ? -28.229 50.905  89.012  1.00 76.97  ?  423 TYR D CD2 1 
ATOM   7160  C CE1 . TYR C 2 91  ? -30.050 52.490  87.635  1.00 85.52  ?  423 TYR D CE1 1 
ATOM   7161  C CE2 . TYR C 2 91  ? -29.479 50.400  88.702  1.00 79.53  ?  423 TYR D CE2 1 
ATOM   7162  C CZ  . TYR C 2 91  ? -30.386 51.193  88.015  1.00 84.15  ?  423 TYR D CZ  1 
ATOM   7163  O OH  . TYR C 2 91  ? -31.623 50.667  87.715  1.00 89.97  ?  423 TYR D OH  1 
ATOM   7164  N N   . LYS C 2 92  ? -28.240 54.003  91.875  1.00 78.77  ?  424 LYS D N   1 
ATOM   7165  C CA  . LYS C 2 92  ? -28.867 53.650  93.141  1.00 79.20  ?  424 LYS D CA  1 
ATOM   7166  C C   . LYS C 2 92  ? -30.328 53.296  92.909  1.00 82.35  ?  424 LYS D C   1 
ATOM   7167  O O   . LYS C 2 92  ? -31.030 54.001  92.178  1.00 82.18  ?  424 LYS D O   1 
ATOM   7168  C CB  . LYS C 2 92  ? -28.752 54.801  94.146  1.00 80.98  ?  424 LYS D CB  1 
ATOM   7169  C CG  . LYS C 2 92  ? -29.766 54.803  95.289  1.00 80.19  ?  424 LYS D CG  1 
ATOM   7170  C CD  . LYS C 2 92  ? -29.352 53.768  96.334  1.00 82.04  ?  424 LYS D CD  1 
ATOM   7171  C CE  . LYS C 2 92  ? -28.745 54.410  97.591  1.00 87.53  ?  424 LYS D CE  1 
ATOM   7172  N NZ  . LYS C 2 92  ? -28.616 53.437  98.735  1.00 90.31  ?  424 LYS D NZ  1 
ATOM   7173  N N   . LEU C 2 93  ? -30.777 52.206  93.525  1.00 89.79  ?  425 LEU D N   1 
ATOM   7174  C CA  . LEU C 2 93  ? -32.157 51.738  93.476  1.00 92.60  ?  425 LEU D CA  1 
ATOM   7175  C C   . LEU C 2 93  ? -32.940 52.293  94.659  1.00 96.40  ?  425 LEU D C   1 
ATOM   7176  O O   . LEU C 2 93  ? -32.419 52.329  95.781  1.00 100.48 ?  425 LEU D O   1 
ATOM   7177  C CB  . LEU C 2 93  ? -32.215 50.220  93.517  1.00 91.08  ?  425 LEU D CB  1 
ATOM   7178  C CG  . LEU C 2 93  ? -31.717 49.527  92.256  1.00 86.32  ?  425 LEU D CG  1 
ATOM   7179  C CD1 . LEU C 2 93  ? -32.301 48.144  92.116  1.00 87.55  ?  425 LEU D CD1 1 
ATOM   7180  C CD2 . LEU C 2 93  ? -32.038 50.384  91.061  1.00 86.05  ?  425 LEU D CD2 1 
ATOM   7181  N N   . PRO C 2 94  ? -34.185 52.711  94.408  1.00 104.97 ?  426 PRO D N   1 
ATOM   7182  C CA  . PRO C 2 94  ? -35.028 53.225  95.492  1.00 106.28 ?  426 PRO D CA  1 
ATOM   7183  C C   . PRO C 2 94  ? -35.362 52.097  96.445  1.00 112.75 ?  426 PRO D C   1 
ATOM   7184  O O   . PRO C 2 94  ? -35.552 50.950  96.035  1.00 114.98 ?  426 PRO D O   1 
ATOM   7185  C CB  . PRO C 2 94  ? -36.285 53.714  94.770  1.00 106.41 ?  426 PRO D CB  1 
ATOM   7186  C CG  . PRO C 2 94  ? -36.312 52.917  93.522  1.00 106.41 ?  426 PRO D CG  1 
ATOM   7187  C CD  . PRO C 2 94  ? -34.885 52.743  93.119  1.00 105.36 ?  426 PRO D CD  1 
ATOM   7188  N N   . ASP C 2 95  ? -35.440 52.424  97.731  1.00 109.35 ?  427 ASP D N   1 
ATOM   7189  C CA  . ASP C 2 95  ? -35.688 51.363  98.694  1.00 108.31 ?  427 ASP D CA  1 
ATOM   7190  C C   . ASP C 2 95  ? -37.072 50.758  98.513  1.00 115.23 ?  427 ASP D C   1 
ATOM   7191  O O   . ASP C 2 95  ? -37.306 49.643  98.990  1.00 114.63 ?  427 ASP D O   1 
ATOM   7192  C CB  . ASP C 2 95  ? -35.488 51.867  100.126 1.00 105.27 ?  427 ASP D CB  1 
ATOM   7193  C CG  . ASP C 2 95  ? -34.079 52.419  100.364 1.00 106.88 ?  427 ASP D CG  1 
ATOM   7194  O OD1 . ASP C 2 95  ? -33.113 51.696  100.060 1.00 108.28 ?  427 ASP D OD1 1 
ATOM   7195  O OD2 . ASP C 2 95  ? -33.931 53.541  100.906 1.00 105.39 -1 427 ASP D OD2 1 
ATOM   7196  N N   . ASP C 2 96  ? -37.979 51.452  97.815  1.00 119.24 ?  428 ASP D N   1 
ATOM   7197  C CA  . ASP C 2 96  ? -39.270 50.898  97.412  1.00 122.20 ?  428 ASP D CA  1 
ATOM   7198  C C   . ASP C 2 96  ? -39.234 50.302  96.005  1.00 125.97 ?  428 ASP D C   1 
ATOM   7199  O O   . ASP C 2 96  ? -40.230 50.402  95.260  1.00 133.76 ?  428 ASP D O   1 
ATOM   7200  C CB  . ASP C 2 96  ? -40.365 51.966  97.524  1.00 118.57 ?  428 ASP D CB  1 
ATOM   7201  C CG  . ASP C 2 96  ? -40.012 53.254  96.794  1.00 122.88 ?  428 ASP D CG  1 
ATOM   7202  O OD1 . ASP C 2 96  ? -40.309 53.365  95.573  1.00 125.17 -1 428 ASP D OD1 1 
ATOM   7203  O OD2 . ASP C 2 96  ? -39.403 54.132  97.444  1.00 121.37 ?  428 ASP D OD2 1 
ATOM   7204  N N   . PHE C 2 97  ? -38.115 49.681  95.626  1.00 120.79 ?  429 PHE D N   1 
ATOM   7205  C CA  . PHE C 2 97  ? -37.970 49.089  94.298  1.00 118.43 ?  429 PHE D CA  1 
ATOM   7206  C C   . PHE C 2 97  ? -38.985 47.992  94.026  1.00 122.71 ?  429 PHE D C   1 
ATOM   7207  O O   . PHE C 2 97  ? -39.389 47.248  94.923  1.00 129.02 ?  429 PHE D O   1 
ATOM   7208  C CB  . PHE C 2 97  ? -36.551 48.549  94.103  1.00 114.03 ?  429 PHE D CB  1 
ATOM   7209  C CG  . PHE C 2 97  ? -36.147 48.412  92.657  1.00 105.91 ?  429 PHE D CG  1 
ATOM   7210  C CD1 . PHE C 2 97  ? -36.407 47.239  91.959  1.00 108.42 ?  429 PHE D CD1 1 
ATOM   7211  C CD2 . PHE C 2 97  ? -35.603 49.477  91.970  1.00 103.46 ?  429 PHE D CD2 1 
ATOM   7212  C CE1 . PHE C 2 97  ? -36.052 47.094  90.635  1.00 100.00 ?  429 PHE D CE1 1 
ATOM   7213  C CE2 . PHE C 2 97  ? -35.267 49.342  90.623  1.00 101.49 ?  429 PHE D CE2 1 
ATOM   7214  C CZ  . PHE C 2 97  ? -35.501 48.132  89.963  1.00 98.73  ?  429 PHE D CZ  1 
ATOM   7215  N N   . THR C 2 98  ? -39.418 47.919  92.763  1.00 119.89 ?  430 THR D N   1 
ATOM   7216  C CA  . THR C 2 98  ? -40.483 46.960  92.385  1.00 118.80 ?  430 THR D CA  1 
ATOM   7217  C C   . THR C 2 98  ? -40.207 46.318  91.025  1.00 117.65 ?  430 THR D C   1 
ATOM   7218  O O   . THR C 2 98  ? -41.157 45.786  90.446  1.00 120.15 ?  430 THR D O   1 
ATOM   7219  C CB  . THR C 2 98  ? -41.803 47.710  92.217  1.00 114.80 ?  430 THR D CB  1 
ATOM   7220  O OG1 . THR C 2 98  ? -41.641 48.641  91.146  1.00 115.36 ?  430 THR D OG1 1 
ATOM   7221  C CG2 . THR C 2 98  ? -42.232 48.449  93.467  1.00 115.22 ?  430 THR D CG2 1 
ATOM   7222  N N   . GLY C 2 99  ? -38.972 46.354  90.527  1.00 122.84 ?  431 GLY D N   1 
ATOM   7223  C CA  . GLY C 2 99  ? -38.707 45.845  89.169  1.00 119.53 ?  431 GLY D CA  1 
ATOM   7224  C C   . GLY C 2 99  ? -37.870 44.587  89.159  1.00 124.38 ?  431 GLY D C   1 
ATOM   7225  O O   . GLY C 2 99  ? -38.030 43.764  90.078  1.00 127.51 ?  431 GLY D O   1 
ATOM   7226  N N   . CYS C 2 100 ? -37.003 44.443  88.153  1.00 121.45 ?  432 CYS D N   1 
ATOM   7227  C CA  . CYS C 2 100 ? -36.179 43.216  88.013  1.00 123.63 ?  432 CYS D CA  1 
ATOM   7228  C C   . CYS C 2 100 ? -34.700 43.577  87.864  1.00 118.39 ?  432 CYS D C   1 
ATOM   7229  O O   . CYS C 2 100 ? -34.417 44.723  87.482  1.00 116.14 ?  432 CYS D O   1 
ATOM   7230  C CB  . CYS C 2 100 ? -36.614 42.432  86.785  1.00 122.84 ?  432 CYS D CB  1 
ATOM   7231  S SG  . CYS C 2 100 ? -37.007 40.699  87.130  1.00 131.15 ?  432 CYS D SG  1 
ATOM   7232  N N   . VAL C 2 101 ? -33.805 42.631  88.131  1.00 105.72 ?  433 VAL D N   1 
ATOM   7233  C CA  . VAL C 2 101 ? -32.361 42.845  88.050  1.00 97.26  ?  433 VAL D CA  1 
ATOM   7234  C C   . VAL C 2 101 ? -31.698 41.605  87.466  1.00 96.57  ?  433 VAL D C   1 
ATOM   7235  O O   . VAL C 2 101 ? -31.715 40.532  88.089  1.00 104.16 ?  433 VAL D O   1 
ATOM   7236  C CB  . VAL C 2 101 ? -31.761 43.183  89.416  1.00 93.28  ?  433 VAL D CB  1 
ATOM   7237  C CG1 . VAL C 2 101 ? -30.299 42.993  89.362  1.00 87.38  ?  433 VAL D CG1 1 
ATOM   7238  C CG2 . VAL C 2 101 ? -32.073 44.614  89.775  1.00 90.46  ?  433 VAL D CG2 1 
ATOM   7239  N N   . ILE C 2 102 ? -31.079 41.749  86.291  1.00 84.93  ?  434 ILE D N   1 
ATOM   7240  C CA  . ILE C 2 102 ? -30.652 40.602  85.494  1.00 85.69  ?  434 ILE D CA  1 
ATOM   7241  C C   . ILE C 2 102 ? -29.200 40.802  85.082  1.00 83.58  ?  434 ILE D C   1 
ATOM   7242  O O   . ILE C 2 102 ? -28.832 41.874  84.583  1.00 78.03  ?  434 ILE D O   1 
ATOM   7243  C CB  . ILE C 2 102 ? -31.517 40.460  84.231  1.00 89.07  ?  434 ILE D CB  1 
ATOM   7244  C CG1 . ILE C 2 102 ? -32.993 40.383  84.618  1.00 102.14 ?  434 ILE D CG1 1 
ATOM   7245  C CG2 . ILE C 2 102 ? -31.083 39.207  83.457  1.00 92.24  ?  434 ILE D CG2 1 
ATOM   7246  C CD1 . ILE C 2 102 ? -33.908 39.954  83.501  1.00 106.36 ?  434 ILE D CD1 1 
ATOM   7247  N N   . ALA C 2 103 ? -28.385 39.761  85.228  1.00 102.02 ?  435 ALA D N   1 
ATOM   7248  C CA  . ALA C 2 103 ? -26.943 39.923  85.118  1.00 91.66  ?  435 ALA D CA  1 
ATOM   7249  C C   . ALA C 2 103 ? -26.277 38.656  84.640  1.00 94.23  ?  435 ALA D C   1 
ATOM   7250  O O   . ALA C 2 103 ? -26.577 37.575  85.146  1.00 106.61 ?  435 ALA D O   1 
ATOM   7251  C CB  . ALA C 2 103 ? -26.343 40.280  86.464  1.00 98.46  ?  435 ALA D CB  1 
ATOM   7252  N N   . TRP C 2 104 ? -25.325 38.818  83.722  1.00 76.21  ?  436 TRP D N   1 
ATOM   7253  C CA  . TRP C 2 104 ? -24.625 37.643  83.152  1.00 84.94  ?  436 TRP D CA  1 
ATOM   7254  C C   . TRP C 2 104 ? -23.143 37.942  82.933  1.00 80.25  ?  436 TRP D C   1 
ATOM   7255  O O   . TRP C 2 104 ? -22.793 39.120  82.791  1.00 75.64  ?  436 TRP D O   1 
ATOM   7256  C CB  . TRP C 2 104 ? -25.294 37.211  81.844  1.00 87.54  ?  436 TRP D CB  1 
ATOM   7257  C CG  . TRP C 2 104 ? -25.329 38.256  80.773  1.00 72.93  ?  436 TRP D CG  1 
ATOM   7258  C CD1 . TRP C 2 104 ? -24.504 38.363  79.692  1.00 66.20  ?  436 TRP D CD1 1 
ATOM   7259  C CD2 . TRP C 2 104 ? -26.278 39.327  80.656  1.00 71.47  ?  436 TRP D CD2 1 
ATOM   7260  N NE1 . TRP C 2 104 ? -24.864 39.437  78.922  1.00 63.33  ?  436 TRP D NE1 1 
ATOM   7261  C CE2 . TRP C 2 104 ? -25.950 40.047  79.490  1.00 66.79  ?  436 TRP D CE2 1 
ATOM   7262  C CE3 . TRP C 2 104 ? -27.363 39.750  81.429  1.00 77.41  ?  436 TRP D CE3 1 
ATOM   7263  C CZ2 . TRP C 2 104 ? -26.674 41.165  79.082  1.00 71.75  ?  436 TRP D CZ2 1 
ATOM   7264  C CZ3 . TRP C 2 104 ? -28.076 40.855  81.026  1.00 74.21  ?  436 TRP D CZ3 1 
ATOM   7265  C CH2 . TRP C 2 104 ? -27.734 41.551  79.867  1.00 73.05  ?  436 TRP D CH2 1 
ATOM   7266  N N   . ASN C 2 105 ? -22.313 36.899  82.892  1.00 92.28  ?  437 ASN D N   1 
ATOM   7267  C CA  . ASN C 2 105 ? -20.864 37.073  82.626  1.00 83.23  ?  437 ASN D CA  1 
ATOM   7268  C C   . ASN C 2 105 ? -20.686 37.828  81.318  1.00 80.67  ?  437 ASN D C   1 
ATOM   7269  O O   . ASN C 2 105 ? -21.605 37.800  80.493  1.00 83.39  ?  437 ASN D O   1 
ATOM   7270  C CB  . ASN C 2 105 ? -20.139 35.735  82.509  1.00 87.76  ?  437 ASN D CB  1 
ATOM   7271  C CG  . ASN C 2 105 ? -19.012 35.571  83.507  1.00 90.39  ?  437 ASN D CG  1 
ATOM   7272  O OD1 . ASN C 2 105 ? -19.218 35.737  84.705  1.00 92.53  ?  437 ASN D OD1 1 
ATOM   7273  N ND2 . ASN C 2 105 ? -17.822 35.244  83.027  1.00 83.55  ?  437 ASN D ND2 1 
ATOM   7274  N N   . SER C 2 106 ? -19.539 38.470  81.143  1.00 77.35  ?  438 SER D N   1 
ATOM   7275  C CA  . SER C 2 106 ? -19.250 39.137  79.855  1.00 73.45  ?  438 SER D CA  1 
ATOM   7276  C C   . SER C 2 106 ? -17.765 38.956  79.571  1.00 73.50  ?  438 SER D C   1 
ATOM   7277  O O   . SER C 2 106 ? -17.287 39.489  78.559  1.00 72.14  ?  438 SER D O   1 
ATOM   7278  C CB  . SER C 2 106 ? -19.634 40.575  79.897  1.00 69.25  ?  438 SER D CB  1 
ATOM   7279  O OG  . SER C 2 106 ? -18.644 41.343  80.549  1.00 70.27  ?  438 SER D OG  1 
ATOM   7280  N N   . ASN C 2 107 ? -17.070 38.216  80.437  1.00 72.47  ?  439 ASN D N   1 
ATOM   7281  C CA  . ASN C 2 107 ? -15.630 38.113  80.229  1.00 71.17  ?  439 ASN D CA  1 
ATOM   7282  C C   . ASN C 2 107 ? -15.256 37.894  78.767  1.00 75.44  ?  439 ASN D C   1 
ATOM   7283  O O   . ASN C 2 107 ? -14.218 38.394  78.306  1.00 75.27  ?  439 ASN D O   1 
ATOM   7284  C CB  . ASN C 2 107 ? -15.054 36.993  81.071  1.00 70.40  ?  439 ASN D CB  1 
ATOM   7285  C CG  . ASN C 2 107 ? -13.646 37.268  81.454  1.00 69.58  ?  439 ASN D CG  1 
ATOM   7286  O OD1 . ASN C 2 107 ? -13.323 38.339  81.960  1.00 71.97  ?  439 ASN D OD1 1 
ATOM   7287  N ND2 . ASN C 2 107 ? -12.761 36.344  81.111  1.00 71.24  ?  439 ASN D ND2 1 
ATOM   7288  N N   . LYS C 2 108 ? -16.079 37.135  78.030  1.00 75.70  ?  440 LYS D N   1 
ATOM   7289  C CA  . LYS C 2 108 ? -15.746 36.793  76.655  1.00 74.99  ?  440 LYS D CA  1 
ATOM   7290  C C   . LYS C 2 108 ? -15.709 38.030  75.763  1.00 70.43  ?  440 LYS D C   1 
ATOM   7291  O O   . LYS C 2 108 ? -14.708 38.287  75.081  1.00 69.43  ?  440 LYS D O   1 
ATOM   7292  C CB  . LYS C 2 108 ? -16.732 35.751  76.131  1.00 72.32  ?  440 LYS D CB  1 
ATOM   7293  C CG  . LYS C 2 108 ? -16.399 34.331  76.577  1.00 71.48  ?  440 LYS D CG  1 
ATOM   7294  C CD  . LYS C 2 108 ? -17.643 33.509  76.807  1.00 83.76  ?  440 LYS D CD  1 
ATOM   7295  C CE  . LYS C 2 108 ? -17.350 32.003  76.802  1.00 85.99  ?  440 LYS D CE  1 
ATOM   7296  N NZ  . LYS C 2 108 ? -18.227 31.251  75.817  1.00 84.77  ?  440 LYS D NZ  1 
ATOM   7297  N N   . LEU C 2 109 ? -16.771 38.829  75.779  1.00 70.81  ?  441 LEU D N   1 
ATOM   7298  C CA  . LEU C 2 109 ? -16.851 39.971  74.880  1.00 71.29  ?  441 LEU D CA  1 
ATOM   7299  C C   . LEU C 2 109 ? -16.455 41.314  75.510  1.00 72.70  ?  441 LEU D C   1 
ATOM   7300  O O   . LEU C 2 109 ? -15.923 42.173  74.793  1.00 74.99  ?  441 LEU D O   1 
ATOM   7301  C CB  . LEU C 2 109 ? -18.255 40.043  74.227  1.00 67.97  ?  441 LEU D CB  1 
ATOM   7302  C CG  . LEU C 2 109 ? -19.609 40.343  74.900  1.00 69.54  ?  441 LEU D CG  1 
ATOM   7303  C CD1 . LEU C 2 109 ? -20.685 40.571  73.877  1.00 71.73  ?  441 LEU D CD1 1 
ATOM   7304  C CD2 . LEU C 2 109 ? -20.054 39.197  75.793  1.00 70.97  ?  441 LEU D CD2 1 
ATOM   7305  N N   . ASP C 2 110 ? -16.635 41.534  76.820  1.00 67.85  ?  442 ASP D N   1 
ATOM   7306  C CA  . ASP C 2 110 ? -16.329 42.863  77.355  1.00 68.96  ?  442 ASP D CA  1 
ATOM   7307  C C   . ASP C 2 110 ? -14.895 43.024  77.845  1.00 70.28  ?  442 ASP D C   1 
ATOM   7308  O O   . ASP C 2 110 ? -14.439 44.160  78.028  1.00 68.33  ?  442 ASP D O   1 
ATOM   7309  C CB  . ASP C 2 110 ? -17.259 43.238  78.509  1.00 69.11  ?  442 ASP D CB  1 
ATOM   7310  C CG  . ASP C 2 110 ? -18.619 43.687  78.033  1.00 74.42  ?  442 ASP D CG  1 
ATOM   7311  O OD1 . ASP C 2 110 ? -18.662 44.667  77.276  1.00 74.92  ?  442 ASP D OD1 1 
ATOM   7312  O OD2 . ASP C 2 110 ? -19.650 43.099  78.449  1.00 79.32  -1 442 ASP D OD2 1 
ATOM   7313  N N   . SER C 2 111 ? -14.209 41.895  78.026  1.00 72.75  ?  443 SER D N   1 
ATOM   7314  C CA  . SER C 2 111 ? -12.817 41.905  78.536  1.00 71.05  ?  443 SER D CA  1 
ATOM   7315  C C   . SER C 2 111 ? -11.835 41.653  77.397  1.00 74.94  ?  443 SER D C   1 
ATOM   7316  O O   . SER C 2 111 ? -12.255 41.134  76.351  1.00 75.19  ?  443 SER D O   1 
ATOM   7317  C CB  . SER C 2 111 ? -12.642 40.870  79.587  1.00 67.60  ?  443 SER D CB  1 
ATOM   7318  O OG  . SER C 2 111 ? -12.078 39.687  79.044  1.00 70.49  ?  443 SER D OG  1 
ATOM   7319  N N   . LYS C 2 112 ? -10.561 41.985  77.615  1.00 76.86  ?  444 LYS D N   1 
ATOM   7320  C CA  . LYS C 2 112 ? -9.543  41.847  76.546  1.00 78.75  ?  444 LYS D CA  1 
ATOM   7321  C C   . LYS C 2 112 ? -8.148  41.765  77.164  1.00 78.67  ?  444 LYS D C   1 
ATOM   7322  O O   . LYS C 2 112 ? -7.879  42.509  78.125  1.00 79.23  ?  444 LYS D O   1 
ATOM   7323  C CB  . LYS C 2 112 ? -9.631  43.046  75.600  1.00 77.65  ?  444 LYS D CB  1 
ATOM   7324  C CG  . LYS C 2 112 ? -8.761  44.245  75.952  1.00 80.52  ?  444 LYS D CG  1 
ATOM   7325  C CD  . LYS C 2 112 ? -8.252  44.984  74.736  1.00 86.15  ?  444 LYS D CD  1 
ATOM   7326  C CE  . LYS C 2 112 ? -7.302  46.113  75.072  1.00 82.73  ?  444 LYS D CE  1 
ATOM   7327  N NZ  . LYS C 2 112 ? -6.828  46.817  73.859  1.00 84.31  ?  444 LYS D NZ  1 
ATOM   7328  N N   . VAL C 2 113 ? -7.303  40.874  76.648  1.00 78.55  ?  445 VAL D N   1 
ATOM   7329  C CA  . VAL C 2 113 ? -5.897  40.807  77.134  1.00 79.96  ?  445 VAL D CA  1 
ATOM   7330  C C   . VAL C 2 113 ? -5.267  42.163  76.856  1.00 77.45  ?  445 VAL D C   1 
ATOM   7331  O O   . VAL C 2 113 ? -5.244  42.559  75.684  1.00 73.51  ?  445 VAL D O   1 
ATOM   7332  C CB  . VAL C 2 113 ? -5.104  39.688  76.437  1.00 82.04  ?  445 VAL D CB  1 
ATOM   7333  C CG1 . VAL C 2 113 ? -4.290  38.879  77.436  1.00 72.74  ?  445 VAL D CG1 1 
ATOM   7334  C CG2 . VAL C 2 113 ? -6.011  38.771  75.632  1.00 88.26  ?  445 VAL D CG2 1 
ATOM   7335  N N   . GLY C 2 114 ? -4.809  42.854  77.894  1.00 84.61  ?  446 GLY D N   1 
ATOM   7336  C CA  . GLY C 2 114 ? -4.280  44.209  77.676  1.00 81.44  ?  446 GLY D CA  1 
ATOM   7337  C C   . GLY C 2 114 ? -5.176  45.250  78.304  1.00 85.91  ?  446 GLY D C   1 
ATOM   7338  O O   . GLY C 2 114 ? -4.867  46.441  78.182  1.00 85.78  ?  446 GLY D O   1 
ATOM   7339  N N   . GLY C 2 115 ? -6.257  44.823  78.946  1.00 101.60 ?  447 GLY D N   1 
ATOM   7340  C CA  . GLY C 2 115 ? -7.098  45.779  79.681  1.00 97.71  ?  447 GLY D CA  1 
ATOM   7341  C C   . GLY C 2 115 ? -8.074  46.523  78.803  1.00 93.33  ?  447 GLY D C   1 
ATOM   7342  O O   . GLY C 2 115 ? -7.614  47.260  77.927  1.00 94.70  ?  447 GLY D O   1 
ATOM   7343  N N   . ASN C 2 116 ? -9.373  46.339  79.029  1.00 74.80  ?  448 ASN D N   1 
ATOM   7344  C CA  . ASN C 2 116 ? -10.393 47.119  78.295  1.00 68.71  ?  448 ASN D CA  1 
ATOM   7345  C C   . ASN C 2 116 ? -10.747 48.284  79.211  1.00 67.09  ?  448 ASN D C   1 
ATOM   7346  O O   . ASN C 2 116 ? -11.550 48.088  80.136  1.00 66.07  ?  448 ASN D O   1 
ATOM   7347  C CB  . ASN C 2 116 ? -11.608 46.281  77.916  1.00 73.03  ?  448 ASN D CB  1 
ATOM   7348  C CG  . ASN C 2 116 ? -12.904 47.059  77.974  1.00 75.25  ?  448 ASN D CG  1 
ATOM   7349  O OD1 . ASN C 2 116 ? -13.057 48.081  77.309  1.00 77.46  ?  448 ASN D OD1 1 
ATOM   7350  N ND2 . ASN C 2 116 ? -13.827 46.587  78.792  1.00 70.35  ?  448 ASN D ND2 1 
ATOM   7351  N N   . TYR C 2 117 ? -10.090 49.425  79.027  1.00 69.58  ?  449 TYR D N   1 
ATOM   7352  C CA  . TYR C 2 117 ? -10.322 50.551  79.962  1.00 68.19  ?  449 TYR D CA  1 
ATOM   7353  C C   . TYR C 2 117 ? -11.418 51.455  79.409  1.00 69.03  ?  449 TYR D C   1 
ATOM   7354  O O   . TYR C 2 117 ? -11.398 52.658  79.710  1.00 68.24  ?  449 TYR D O   1 
ATOM   7355  C CB  . TYR C 2 117 ? -9.052  51.365  80.169  1.00 69.29  ?  449 TYR D CB  1 
ATOM   7356  C CG  . TYR C 2 117 ? -7.858  50.626  80.711  1.00 71.30  ?  449 TYR D CG  1 
ATOM   7357  C CD1 . TYR C 2 117 ? -7.957  49.779  81.802  1.00 70.84  ?  449 TYR D CD1 1 
ATOM   7358  C CD2 . TYR C 2 117 ? -6.610  50.799  80.140  1.00 70.30  ?  449 TYR D CD2 1 
ATOM   7359  C CE1 . TYR C 2 117 ? -6.847  49.120  82.303  1.00 69.79  ?  449 TYR D CE1 1 
ATOM   7360  C CE2 . TYR C 2 117 ? -5.490  50.146  80.627  1.00 72.05  ?  449 TYR D CE2 1 
ATOM   7361  C CZ  . TYR C 2 117 ? -5.609  49.302  81.713  1.00 71.67  ?  449 TYR D CZ  1 
ATOM   7362  O OH  . TYR C 2 117 ? -4.502  48.665  82.193  1.00 73.09  ?  449 TYR D OH  1 
ATOM   7363  N N   . ASN C 2 118 ? -12.351 50.888  78.648  1.00 63.62  ?  450 ASN D N   1 
ATOM   7364  C CA  . ASN C 2 118 ? -13.416 51.666  78.059  1.00 64.59  ?  450 ASN D CA  1 
ATOM   7365  C C   . ASN C 2 118 ? -14.629 51.757  78.953  1.00 61.46  ?  450 ASN D C   1 
ATOM   7366  O O   . ASN C 2 118 ? -15.409 52.716  78.818  1.00 62.98  ?  450 ASN D O   1 
ATOM   7367  C CB  . ASN C 2 118 ? -13.785 51.084  76.693  1.00 65.46  ?  450 ASN D CB  1 
ATOM   7368  C CG  . ASN C 2 118 ? -13.152 51.863  75.530  1.00 71.31  ?  450 ASN D CG  1 
ATOM   7369  O OD1 . ASN C 2 118 ? -12.199 52.656  75.689  1.00 71.74  ?  450 ASN D OD1 1 
ATOM   7370  N ND2 . ASN C 2 118 ? -13.669 51.603  74.332  1.00 77.52  ?  450 ASN D ND2 1 
ATOM   7371  N N   . TYR C 2 119 ? -14.807 50.807  79.873  1.00 66.42  ?  451 TYR D N   1 
ATOM   7372  C CA  . TYR C 2 119 ? -15.909 50.921  80.817  1.00 67.10  ?  451 TYR D CA  1 
ATOM   7373  C C   . TYR C 2 119 ? -15.329 51.495  82.107  1.00 63.41  ?  451 TYR D C   1 
ATOM   7374  O O   . TYR C 2 119 ? -14.199 51.165  82.490  1.00 60.12  ?  451 TYR D O   1 
ATOM   7375  C CB  . TYR C 2 119 ? -16.617 49.587  81.127  1.00 64.25  ?  451 TYR D CB  1 
ATOM   7376  C CG  . TYR C 2 119 ? -17.109 48.735  79.959  1.00 66.51  ?  451 TYR D CG  1 
ATOM   7377  C CD1 . TYR C 2 119 ? -16.224 48.080  79.121  1.00 70.92  ?  451 TYR D CD1 1 
ATOM   7378  C CD2 . TYR C 2 119 ? -18.444 48.700  79.614  1.00 68.35  ?  451 TYR D CD2 1 
ATOM   7379  C CE1 . TYR C 2 119 ? -16.689 47.306  78.063  1.00 73.17  ?  451 TYR D CE1 1 
ATOM   7380  C CE2 . TYR C 2 119 ? -18.926 47.920  78.588  1.00 69.56  ?  451 TYR D CE2 1 
ATOM   7381  C CZ  . TYR C 2 119 ? -18.037 47.254  77.802  1.00 72.81  ?  451 TYR D CZ  1 
ATOM   7382  O OH  . TYR C 2 119 ? -18.512 46.521  76.751  1.00 78.71  ?  451 TYR D OH  1 
ATOM   7383  N N   . ARG C 2 120 ? -16.098 52.377  82.752  1.00 60.96  ?  452 ARG D N   1 
ATOM   7384  C CA  . ARG C 2 120 ? -15.607 53.184  83.853  1.00 60.17  ?  452 ARG D CA  1 
ATOM   7385  C C   . ARG C 2 120 ? -16.622 53.205  84.985  1.00 63.88  ?  452 ARG D C   1 
ATOM   7386  O O   . ARG C 2 120 ? -17.804 52.931  84.765  1.00 68.97  ?  452 ARG D O   1 
ATOM   7387  C CB  . ARG C 2 120 ? -15.340 54.608  83.419  1.00 59.81  ?  452 ARG D CB  1 
ATOM   7388  C CG  . ARG C 2 120 ? -14.096 54.772  82.657  1.00 58.24  ?  452 ARG D CG  1 
ATOM   7389  C CD  . ARG C 2 120 ? -13.789 56.232  82.534  1.00 61.52  ?  452 ARG D CD  1 
ATOM   7390  N NE  . ARG C 2 120 ? -13.715 56.722  81.171  1.00 68.83  ?  452 ARG D NE  1 
ATOM   7391  C CZ  . ARG C 2 120 ? -13.506 57.994  80.866  1.00 68.35  ?  452 ARG D CZ  1 
ATOM   7392  N NH1 . ARG C 2 120 ? -13.346 58.906  81.808  1.00 61.51  ?  452 ARG D NH1 1 
ATOM   7393  N NH2 . ARG C 2 120 ? -13.376 58.347  79.587  1.00 73.98  ?  452 ARG D NH2 1 
ATOM   7394  N N   . TYR C 2 121 ? -16.154 53.531  86.199  1.00 61.69  ?  453 TYR D N   1 
ATOM   7395  C CA  . TYR C 2 121 ? -17.047 53.933  87.282  1.00 62.43  ?  453 TYR D CA  1 
ATOM   7396  C C   . TYR C 2 121 ? -16.662 55.306  87.821  1.00 64.14  ?  453 TYR D C   1 
ATOM   7397  O O   . TYR C 2 121 ? -15.588 55.858  87.530  1.00 62.89  ?  453 TYR D O   1 
ATOM   7398  C CB  . TYR C 2 121 ? -17.088 52.941  88.462  1.00 65.53  ?  453 TYR D CB  1 
ATOM   7399  C CG  . TYR C 2 121 ? -15.750 52.583  89.096  1.00 68.22  ?  453 TYR D CG  1 
ATOM   7400  C CD1 . TYR C 2 121 ? -14.861 53.553  89.498  1.00 68.65  ?  453 TYR D CD1 1 
ATOM   7401  C CD2 . TYR C 2 121 ? -15.429 51.279  89.413  1.00 73.60  ?  453 TYR D CD2 1 
ATOM   7402  C CE1 . TYR C 2 121 ? -13.662 53.221  90.095  1.00 70.68  ?  453 TYR D CE1 1 
ATOM   7403  C CE2 . TYR C 2 121 ? -14.214 50.931  89.984  1.00 72.17  ?  453 TYR D CE2 1 
ATOM   7404  C CZ  . TYR C 2 121 ? -13.337 51.919  90.323  1.00 71.46  ?  453 TYR D CZ  1 
ATOM   7405  O OH  . TYR C 2 121 ? -12.133 51.629  90.900  1.00 81.46  ?  453 TYR D OH  1 
ATOM   7406  N N   . ARG C 2 122 ? -17.571 55.847  88.631  1.00 64.98  ?  454 ARG D N   1 
ATOM   7407  C CA  . ARG C 2 122 ? -17.273 56.945  89.538  1.00 64.12  ?  454 ARG D CA  1 
ATOM   7408  C C   . ARG C 2 122 ? -16.753 56.307  90.799  1.00 69.82  ?  454 ARG D C   1 
ATOM   7409  O O   . ARG C 2 122 ? -17.367 55.341  91.272  1.00 70.02  ?  454 ARG D O   1 
ATOM   7410  C CB  . ARG C 2 122 ? -18.527 57.705  89.934  1.00 66.98  ?  454 ARG D CB  1 
ATOM   7411  C CG  . ARG C 2 122 ? -18.381 59.161  90.005  1.00 70.37  ?  454 ARG D CG  1 
ATOM   7412  C CD  . ARG C 2 122 ? -19.715 59.798  90.056  1.00 74.79  ?  454 ARG D CD  1 
ATOM   7413  N NE  . ARG C 2 122 ? -19.960 60.357  88.740  1.00 76.74  ?  454 ARG D NE  1 
ATOM   7414  C CZ  . ARG C 2 122 ? -19.392 61.454  88.278  1.00 77.62  ?  454 ARG D CZ  1 
ATOM   7415  N NH1 . ARG C 2 122 ? -18.382 62.033  88.924  1.00 73.20  ?  454 ARG D NH1 1 
ATOM   7416  N NH2 . ARG C 2 122 ? -19.795 61.933  87.102  1.00 79.77  ?  454 ARG D NH2 1 
ATOM   7417  N N   . LEU C 2 123 ? -15.643 56.839  91.371  1.00 69.35  ?  455 LEU D N   1 
ATOM   7418  C CA  . LEU C 2 123 ? -15.367 56.500  92.762  1.00 68.65  ?  455 LEU D CA  1 
ATOM   7419  C C   . LEU C 2 123 ? -15.441 57.670  93.724  1.00 69.21  ?  455 LEU D C   1 
ATOM   7420  O O   . LEU C 2 123 ? -15.711 57.431  94.905  1.00 74.33  ?  455 LEU D O   1 
ATOM   7421  C CB  . LEU C 2 123 ? -14.025 55.771  92.937  1.00 65.69  ?  455 LEU D CB  1 
ATOM   7422  C CG  . LEU C 2 123 ? -12.598 56.268  93.019  1.00 67.58  ?  455 LEU D CG  1 
ATOM   7423  C CD1 . LEU C 2 123 ? -11.739 55.101  93.411  1.00 60.87  ?  455 LEU D CD1 1 
ATOM   7424  C CD2 . LEU C 2 123 ? -12.167 56.757  91.674  1.00 72.51  ?  455 LEU D CD2 1 
ATOM   7425  N N   . PHE C 2 124 ? -15.319 58.916  93.265  1.00 64.35  ?  456 PHE D N   1 
ATOM   7426  C CA  . PHE C 2 124 ? -15.340 60.070  94.161  1.00 66.22  ?  456 PHE D CA  1 
ATOM   7427  C C   . PHE C 2 124 ? -16.533 60.979  93.860  1.00 66.46  ?  456 PHE D C   1 
ATOM   7428  O O   . PHE C 2 124 ? -16.692 61.438  92.723  1.00 69.57  ?  456 PHE D O   1 
ATOM   7429  C CB  . PHE C 2 124 ? -14.021 60.834  94.019  1.00 67.98  ?  456 PHE D CB  1 
ATOM   7430  C CG  . PHE C 2 124 ? -12.829 60.077  94.515  1.00 64.00  ?  456 PHE D CG  1 
ATOM   7431  C CD1 . PHE C 2 124 ? -12.962 59.158  95.526  1.00 66.45  ?  456 PHE D CD1 1 
ATOM   7432  C CD2 . PHE C 2 124 ? -11.592 60.250  93.929  1.00 62.93  ?  456 PHE D CD2 1 
ATOM   7433  C CE1 . PHE C 2 124 ? -11.884 58.437  95.969  1.00 69.19  ?  456 PHE D CE1 1 
ATOM   7434  C CE2 . PHE C 2 124 ? -10.501 59.538  94.362  1.00 67.59  ?  456 PHE D CE2 1 
ATOM   7435  C CZ  . PHE C 2 124 ? -10.643 58.626  95.382  1.00 71.22  ?  456 PHE D CZ  1 
ATOM   7436  N N   . ARG C 2 125 ? -17.354 61.265  94.872  1.00 68.25  ?  457 ARG D N   1 
ATOM   7437  C CA  . ARG C 2 125 ? -18.444 62.234  94.711  1.00 76.94  ?  457 ARG D CA  1 
ATOM   7438  C C   . ARG C 2 125 ? -18.764 62.872  96.059  1.00 78.09  ?  457 ARG D C   1 
ATOM   7439  O O   . ARG C 2 125 ? -18.648 62.218  97.101  1.00 80.50  ?  457 ARG D O   1 
ATOM   7440  C CB  . ARG C 2 125 ? -19.712 61.587  94.107  1.00 75.62  ?  457 ARG D CB  1 
ATOM   7441  C CG  . ARG C 2 125 ? -20.846 62.522  93.660  1.00 77.61  ?  457 ARG D CG  1 
ATOM   7442  C CD  . ARG C 2 125 ? -21.911 61.694  92.906  1.00 81.68  ?  457 ARG D CD  1 
ATOM   7443  N NE  . ARG C 2 125 ? -22.974 62.474  92.279  1.00 78.51  ?  457 ARG D NE  1 
ATOM   7444  C CZ  . ARG C 2 125 ? -24.115 62.783  92.870  1.00 81.61  ?  457 ARG D CZ  1 
ATOM   7445  N NH1 . ARG C 2 125 ? -24.402 62.352  94.084  1.00 82.81  ?  457 ARG D NH1 1 
ATOM   7446  N NH2 . ARG C 2 125 ? -24.995 63.537  92.225  1.00 83.73  ?  457 ARG D NH2 1 
ATOM   7447  N N   . LYS C 2 126 ? -19.164 64.151  96.035  1.00 78.42  ?  458 LYS D N   1 
ATOM   7448  C CA  . LYS C 2 126 ? -19.467 64.850  97.279  1.00 76.15  ?  458 LYS D CA  1 
ATOM   7449  C C   . LYS C 2 126 ? -20.649 64.251  98.039  1.00 75.33  ?  458 LYS D C   1 
ATOM   7450  O O   . LYS C 2 126 ? -20.786 64.506  99.235  1.00 77.09  ?  458 LYS D O   1 
ATOM   7451  C CB  . LYS C 2 126 ? -19.718 66.335  97.009  1.00 74.41  ?  458 LYS D CB  1 
ATOM   7452  C CG  . LYS C 2 126 ? -19.039 66.916  95.760  1.00 79.60  ?  458 LYS D CG  1 
ATOM   7453  C CD  . LYS C 2 126 ? -19.144 68.478  95.768  1.00 83.61  ?  458 LYS D CD  1 
ATOM   7454  C CE  . LYS C 2 126 ? -18.491 69.146  94.549  1.00 92.13  ?  458 LYS D CE  1 
ATOM   7455  N NZ  . LYS C 2 126 ? -16.984 68.973  94.559  1.00 104.00 ?  458 LYS D NZ  1 
ATOM   7456  N N   . SER C 2 127 ? -21.497 63.453  97.405  1.00 77.52  ?  459 SER D N   1 
ATOM   7457  C CA  . SER C 2 127 ? -22.733 63.086  98.087  1.00 84.00  ?  459 SER D CA  1 
ATOM   7458  C C   . SER C 2 127 ? -23.408 61.947  97.337  1.00 86.70  ?  459 SER D C   1 
ATOM   7459  O O   . SER C 2 127 ? -23.195 61.754  96.133  1.00 85.68  ?  459 SER D O   1 
ATOM   7460  C CB  . SER C 2 127 ? -23.697 64.279  98.202  1.00 88.27  ?  459 SER D CB  1 
ATOM   7461  O OG  . SER C 2 127 ? -23.892 64.902  96.946  1.00 94.26  ?  459 SER D OG  1 
ATOM   7462  N N   . ASN C 2 128 ? -24.264 61.227  98.057  1.00 83.31  ?  460 ASN D N   1 
ATOM   7463  C CA  . ASN C 2 128 ? -24.819 59.988  97.547  1.00 80.96  ?  460 ASN D CA  1 
ATOM   7464  C C   . ASN C 2 128 ? -25.833 60.251  96.462  1.00 86.22  ?  460 ASN D C   1 
ATOM   7465  O O   . ASN C 2 128 ? -26.477 61.304  96.419  1.00 89.37  ?  460 ASN D O   1 
ATOM   7466  C CB  . ASN C 2 128 ? -25.472 59.193  98.669  1.00 84.36  ?  460 ASN D CB  1 
ATOM   7467  C CG  . ASN C 2 128 ? -24.474 58.605  99.627  1.00 90.01  ?  460 ASN D CG  1 
ATOM   7468  O OD1 . ASN C 2 128 ? -24.417 57.383  99.792  1.00 91.20  ?  460 ASN D OD1 1 
ATOM   7469  N ND2 . ASN C 2 128 ? -23.654 59.452  100.241 1.00 99.43  ?  460 ASN D ND2 1 
ATOM   7470  N N   . LEU C 2 129 ? -26.000 59.263  95.594  1.00 88.75  ?  461 LEU D N   1 
ATOM   7471  C CA  . LEU C 2 129 ? -26.917 59.402  94.474  1.00 86.68  ?  461 LEU D CA  1 
ATOM   7472  C C   . LEU C 2 129 ? -28.334 59.183  94.939  1.00 88.02  ?  461 LEU D C   1 
ATOM   7473  O O   . LEU C 2 129 ? -28.613 58.216  95.651  1.00 88.49  ?  461 LEU D O   1 
ATOM   7474  C CB  . LEU C 2 129 ? -26.590 58.402  93.370  1.00 84.07  ?  461 LEU D CB  1 
ATOM   7475  C CG  . LEU C 2 129 ? -25.670 58.974  92.318  1.00 81.05  ?  461 LEU D CG  1 
ATOM   7476  C CD1 . LEU C 2 129 ? -25.642 58.084  91.120  1.00 67.47  ?  461 LEU D CD1 1 
ATOM   7477  C CD2 . LEU C 2 129 ? -26.185 60.326  92.024  1.00 80.67  ?  461 LEU D CD2 1 
ATOM   7478  N N   . LYS C 2 130 ? -29.235 60.070  94.519  1.00 89.99  ?  462 LYS D N   1 
ATOM   7479  C CA  . LYS C 2 130 ? -30.653 59.862  94.785  1.00 85.75  ?  462 LYS D CA  1 
ATOM   7480  C C   . LYS C 2 130 ? -31.151 58.737  93.881  1.00 81.94  ?  462 LYS D C   1 
ATOM   7481  O O   . LYS C 2 130 ? -30.519 58.438  92.867  1.00 83.31  ?  462 LYS D O   1 
ATOM   7482  C CB  . LYS C 2 130 ? -31.442 61.159  94.607  1.00 82.46  ?  462 LYS D CB  1 
ATOM   7483  C CG  . LYS C 2 130 ? -31.028 62.167  95.652  1.00 87.13  ?  462 LYS D CG  1 
ATOM   7484  C CD  . LYS C 2 130 ? -32.199 62.738  96.408  1.00 90.25  ?  462 LYS D CD  1 
ATOM   7485  C CE  . LYS C 2 130 ? -32.183 62.047  97.814  1.00 96.87  ?  462 LYS D CE  1 
ATOM   7486  N NZ  . LYS C 2 130 ? -32.961 62.615  98.971  1.00 96.44  ?  462 LYS D NZ  1 
ATOM   7487  N N   . PRO C 2 131 ? -32.231 58.044  94.261  1.00 84.64  ?  463 PRO D N   1 
ATOM   7488  C CA  . PRO C 2 131 ? -32.626 56.851  93.498  1.00 82.93  ?  463 PRO D CA  1 
ATOM   7489  C C   . PRO C 2 131 ? -32.754 57.161  92.013  1.00 79.61  ?  463 PRO D C   1 
ATOM   7490  O O   . PRO C 2 131 ? -33.204 58.240  91.622  1.00 76.57  ?  463 PRO D O   1 
ATOM   7491  C CB  . PRO C 2 131 ? -33.979 56.463  94.111  1.00 84.51  ?  463 PRO D CB  1 
ATOM   7492  C CG  . PRO C 2 131 ? -33.895 56.910  95.507  1.00 85.39  ?  463 PRO D CG  1 
ATOM   7493  C CD  . PRO C 2 131 ? -33.025 58.174  95.500  1.00 85.80  ?  463 PRO D CD  1 
ATOM   7494  N N   . PHE C 2 132 ? -32.258 56.244  91.188  1.00 78.94  ?  464 PHE D N   1 
ATOM   7495  C CA  . PHE C 2 132 ? -32.428 56.304  89.748  1.00 79.84  ?  464 PHE D CA  1 
ATOM   7496  C C   . PHE C 2 132 ? -31.799 57.554  89.144  1.00 78.86  ?  464 PHE D C   1 
ATOM   7497  O O   . PHE C 2 132 ? -32.168 57.958  88.031  1.00 79.76  ?  464 PHE D O   1 
ATOM   7498  C CB  . PHE C 2 132 ? -33.904 56.252  89.408  1.00 77.16  ?  464 PHE D CB  1 
ATOM   7499  C CG  . PHE C 2 132 ? -34.403 54.885  89.206  1.00 81.49  ?  464 PHE D CG  1 
ATOM   7500  C CD1 . PHE C 2 132 ? -33.857 54.075  88.237  1.00 85.72  ?  464 PHE D CD1 1 
ATOM   7501  C CD2 . PHE C 2 132 ? -35.398 54.378  90.028  1.00 82.41  ?  464 PHE D CD2 1 
ATOM   7502  C CE1 . PHE C 2 132 ? -34.322 52.787  88.068  1.00 90.57  ?  464 PHE D CE1 1 
ATOM   7503  C CE2 . PHE C 2 132 ? -35.864 53.103  89.867  1.00 87.04  ?  464 PHE D CE2 1 
ATOM   7504  C CZ  . PHE C 2 132 ? -35.332 52.302  88.891  1.00 91.69  ?  464 PHE D CZ  1 
ATOM   7505  N N   . GLU C 2 133 ? -30.877 58.193  89.873  1.00 75.64  ?  465 GLU D N   1 
ATOM   7506  C CA  . GLU C 2 133 ? -30.207 59.401  89.406  1.00 74.20  ?  465 GLU D CA  1 
ATOM   7507  C C   . GLU C 2 133 ? -29.068 59.017  88.457  1.00 77.24  ?  465 GLU D C   1 
ATOM   7508  O O   . GLU C 2 133 ? -28.573 57.883  88.472  1.00 78.76  ?  465 GLU D O   1 
ATOM   7509  C CB  . GLU C 2 133 ? -29.666 60.183  90.603  1.00 74.64  ?  465 GLU D CB  1 
ATOM   7510  C CG  . GLU C 2 133 ? -29.766 61.706  90.574  1.00 77.02  ?  465 GLU D CG  1 
ATOM   7511  C CD  . GLU C 2 133 ? -28.838 62.396  91.588  1.00 88.46  ?  465 GLU D CD  1 
ATOM   7512  O OE1 . GLU C 2 133 ? -29.139 62.396  92.822  1.00 89.89  ?  465 GLU D OE1 1 
ATOM   7513  O OE2 . GLU C 2 133 ? -27.846 63.007  91.162  1.00 94.35  -1 465 GLU D OE2 1 
ATOM   7514  N N   . ARG C 2 134 ? -28.691 59.956  87.585  1.00 80.42  ?  466 ARG D N   1 
ATOM   7515  C CA  . ARG C 2 134 ? -27.484 59.831  86.780  1.00 82.67  ?  466 ARG D CA  1 
ATOM   7516  C C   . ARG C 2 134 ? -26.642 61.086  86.949  1.00 88.14  ?  466 ARG D C   1 
ATOM   7517  O O   . ARG C 2 134 ? -27.176 62.195  87.091  1.00 89.09  ?  466 ARG D O   1 
ATOM   7518  C CB  . ARG C 2 134 ? -27.778 59.589  85.284  1.00 80.14  ?  466 ARG D CB  1 
ATOM   7519  C CG  . ARG C 2 134 ? -26.748 58.672  84.563  1.00 81.11  ?  466 ARG D CG  1 
ATOM   7520  C CD  . ARG C 2 134 ? -26.798 58.730  83.011  1.00 78.34  ?  466 ARG D CD  1 
ATOM   7521  N NE  . ARG C 2 134 ? -28.072 58.233  82.516  1.00 84.43  ?  466 ARG D NE  1 
ATOM   7522  C CZ  . ARG C 2 134 ? -29.018 58.993  81.985  1.00 82.32  ?  466 ARG D CZ  1 
ATOM   7523  N NH1 . ARG C 2 134 ? -28.822 60.292  81.771  1.00 82.34  ?  466 ARG D NH1 1 
ATOM   7524  N NH2 . ARG C 2 134 ? -30.207 58.451  81.718  1.00 77.52  ?  466 ARG D NH2 1 
ATOM   7525  N N   . ASP C 2 135 ? -25.325 60.885  86.950  1.00 93.24  ?  467 ASP D N   1 
ATOM   7526  C CA  . ASP C 2 135 ? -24.329 61.951  86.946  1.00 93.89  ?  467 ASP D CA  1 
ATOM   7527  C C   . ASP C 2 135 ? -23.255 61.630  85.924  1.00 85.57  ?  467 ASP D C   1 
ATOM   7528  O O   . ASP C 2 135 ? -22.549 60.622  86.044  1.00 86.50  ?  467 ASP D O   1 
ATOM   7529  C CB  . ASP C 2 135 ? -23.683 62.150  88.319  1.00 97.81  ?  467 ASP D CB  1 
ATOM   7530  C CG  . ASP C 2 135 ? -23.416 63.618  88.633  1.00 102.76 ?  467 ASP D CG  1 
ATOM   7531  O OD1 . ASP C 2 135 ? -24.205 64.503  88.217  1.00 102.76 ?  467 ASP D OD1 1 
ATOM   7532  O OD2 . ASP C 2 135 ? -22.395 63.878  89.298  1.00 103.62 -1 467 ASP D OD2 1 
ATOM   7533  N N   . ILE C 2 136 ? -23.112 62.502  84.938  1.00 81.00  ?  468 ILE D N   1 
ATOM   7534  C CA  . ILE C 2 136 ? -22.071 62.295  83.957  1.00 77.36  ?  468 ILE D CA  1 
ATOM   7535  C C   . ILE C 2 136 ? -21.145 63.496  83.988  1.00 78.84  ?  468 ILE D C   1 
ATOM   7536  O O   . ILE C 2 136 ? -20.675 63.947  82.935  1.00 76.51  ?  468 ILE D O   1 
ATOM   7537  C CB  . ILE C 2 136 ? -22.652 62.104  82.559  1.00 72.87  ?  468 ILE D CB  1 
ATOM   7538  C CG1 . ILE C 2 136 ? -23.685 63.186  82.285  1.00 72.70  ?  468 ILE D CG1 1 
ATOM   7539  C CG2 . ILE C 2 136 ? -23.268 60.743  82.460  1.00 72.52  ?  468 ILE D CG2 1 
ATOM   7540  C CD1 . ILE C 2 136 ? -23.844 63.542  80.787  1.00 68.12  ?  468 ILE D CD1 1 
ATOM   7541  N N   . SER C 2 137 ? -20.882 64.029  85.182  1.00 78.03  ?  469 SER D N   1 
ATOM   7542  C CA  . SER C 2 137 ? -20.021 65.196  85.308  1.00 78.69  ?  469 SER D CA  1 
ATOM   7543  C C   . SER C 2 137 ? -18.576 64.740  85.444  1.00 72.34  ?  469 SER D C   1 
ATOM   7544  O O   . SER C 2 137 ? -18.283 63.820  86.202  1.00 76.36  ?  469 SER D O   1 
ATOM   7545  C CB  . SER C 2 137 ? -20.442 66.056  86.503  1.00 84.48  ?  469 SER D CB  1 
ATOM   7546  O OG  . SER C 2 137 ? -19.753 65.707  87.680  1.00 84.66  ?  469 SER D OG  1 
ATOM   7547  N N   . THR C 2 138 ? -17.677 65.358  84.688  1.00 66.73  ?  470 THR D N   1 
ATOM   7548  C CA  . THR C 2 138 ? -16.257 65.076  84.833  1.00 72.54  ?  470 THR D CA  1 
ATOM   7549  C C   . THR C 2 138 ? -15.537 66.161  85.614  1.00 77.31  ?  470 THR D C   1 
ATOM   7550  O O   . THR C 2 138 ? -14.341 66.407  85.412  1.00 77.67  ?  470 THR D O   1 
ATOM   7551  C CB  . THR C 2 138 ? -15.600 64.866  83.477  1.00 73.14  ?  470 THR D CB  1 
ATOM   7552  O OG1 . THR C 2 138 ? -15.529 66.121  82.794  1.00 79.14  ?  470 THR D OG1 1 
ATOM   7553  C CG2 . THR C 2 138 ? -16.394 63.854  82.673  1.00 74.96  ?  470 THR D CG2 1 
ATOM   7554  N N   . GLU C 2 139 ? -16.257 66.817  86.505  1.00 76.84  ?  471 GLU D N   1 
ATOM   7555  C CA  . GLU C 2 139 ? -15.679 67.828  87.364  1.00 74.88  ?  471 GLU D CA  1 
ATOM   7556  C C   . GLU C 2 139 ? -14.742 67.210  88.386  1.00 75.56  ?  471 GLU D C   1 
ATOM   7557  O O   . GLU C 2 139 ? -15.038 66.176  88.993  1.00 77.34  ?  471 GLU D O   1 
ATOM   7558  C CB  . GLU C 2 139 ? -16.812 68.583  88.029  1.00 79.63  ?  471 GLU D CB  1 
ATOM   7559  C CG  . GLU C 2 139 ? -16.445 69.822  88.763  1.00 85.47  ?  471 GLU D CG  1 
ATOM   7560  C CD  . GLU C 2 139 ? -17.409 70.033  89.922  1.00 99.38  ?  471 GLU D CD  1 
ATOM   7561  O OE1 . GLU C 2 139 ? -18.562 70.412  89.631  1.00 117.97 ?  471 GLU D OE1 1 
ATOM   7562  O OE2 . GLU C 2 139 ? -17.059 69.783  91.099  1.00 98.67  -1 471 GLU D OE2 1 
ATOM   7563  N N   . ILE C 2 140 ? -13.605 67.872  88.585  1.00 84.65  ?  472 ILE D N   1 
ATOM   7564  C CA  . ILE C 2 140 ? -12.505 67.307  89.357  1.00 78.86  ?  472 ILE D CA  1 
ATOM   7565  C C   . ILE C 2 140 ? -12.883 67.234  90.827  1.00 74.91  ?  472 ILE D C   1 
ATOM   7566  O O   . ILE C 2 140 ? -13.471 68.170  91.371  1.00 80.39  ?  472 ILE D O   1 
ATOM   7567  C CB  . ILE C 2 140 ? -11.276 68.200  89.178  1.00 80.20  ?  472 ILE D CB  1 
ATOM   7568  C CG1 . ILE C 2 140 ? -10.726 67.972  87.769  1.00 80.36  ?  472 ILE D CG1 1 
ATOM   7569  C CG2 . ILE C 2 140 ? -10.333 67.971  90.317  1.00 80.36  ?  472 ILE D CG2 1 
ATOM   7570  C CD1 . ILE C 2 140 ? -10.482 66.530  87.437  1.00 77.32  ?  472 ILE D CD1 1 
ATOM   7571  N N   . TYR C 2 141 ? -12.546 66.139  91.495  1.00 68.84  ?  473 TYR D N   1 
ATOM   7572  C CA  . TYR C 2 141 ? -12.987 66.013  92.882  1.00 73.66  ?  473 TYR D CA  1 
ATOM   7573  C C   . TYR C 2 141 ? -12.156 66.897  93.796  1.00 79.54  ?  473 TYR D C   1 
ATOM   7574  O O   . TYR C 2 141 ? -10.945 67.033  93.618  1.00 81.33  ?  473 TYR D O   1 
ATOM   7575  C CB  . TYR C 2 141 ? -12.932 64.560  93.334  1.00 72.70  ?  473 TYR D CB  1 
ATOM   7576  C CG  . TYR C 2 141 ? -13.522 64.267  94.705  1.00 67.14  ?  473 TYR D CG  1 
ATOM   7577  C CD1 . TYR C 2 141 ? -12.779 64.427  95.848  1.00 74.46  ?  473 TYR D CD1 1 
ATOM   7578  C CD2 . TYR C 2 141 ? -14.842 63.884  94.852  1.00 71.42  ?  473 TYR D CD2 1 
ATOM   7579  C CE1 . TYR C 2 141 ? -13.307 64.151  97.105  1.00 75.29  ?  473 TYR D CE1 1 
ATOM   7580  C CE2 . TYR C 2 141 ? -15.386 63.609  96.101  1.00 72.50  ?  473 TYR D CE2 1 
ATOM   7581  C CZ  . TYR C 2 141 ? -14.610 63.750  97.225  1.00 73.91  ?  473 TYR D CZ  1 
ATOM   7582  O OH  . TYR C 2 141 ? -15.119 63.493  98.477  1.00 74.71  ?  473 TYR D OH  1 
ATOM   7583  N N   . GLN C 2 142 ? -12.820 67.498  94.784  1.00 80.63  ?  474 GLN D N   1 
ATOM   7584  C CA  . GLN C 2 142 ? -12.198 68.488  95.675  1.00 82.99  ?  474 GLN D CA  1 
ATOM   7585  C C   . GLN C 2 142 ? -11.843 67.814  97.002  1.00 83.69  ?  474 GLN D C   1 
ATOM   7586  O O   . GLN C 2 142 ? -12.413 68.117  98.048  1.00 88.28  ?  474 GLN D O   1 
ATOM   7587  C CB  . GLN C 2 142 ? -13.160 69.660  95.918  1.00 99.11  ?  474 GLN D CB  1 
ATOM   7588  C CG  . GLN C 2 142 ? -12.626 70.819  96.813  1.00 99.59  ?  474 GLN D CG  1 
ATOM   7589  C CD  . GLN C 2 142 ? -11.826 71.846  96.024  1.00 102.70 ?  474 GLN D CD  1 
ATOM   7590  O OE1 . GLN C 2 142 ? -10.839 71.524  95.371  1.00 106.45 ?  474 GLN D OE1 1 
ATOM   7591  N NE2 . GLN C 2 142 ? -12.229 73.110  96.137  1.00 100.16 ?  474 GLN D NE2 1 
ATOM   7592  N N   . ALA C 2 143 ? -10.917 66.848  96.960  1.00 87.36  ?  475 ALA D N   1 
ATOM   7593  C CA  . ALA C 2 143 ? -10.674 66.071  98.173  1.00 83.69  ?  475 ALA D CA  1 
ATOM   7594  C C   . ALA C 2 143 ? -9.981  66.884  99.251  1.00 84.87  ?  475 ALA D C   1 
ATOM   7595  O O   . ALA C 2 143 ? -10.093 66.539  100.430 1.00 89.13  ?  475 ALA D O   1 
ATOM   7596  C CB  . ALA C 2 143 ? -9.876  64.807  97.862  1.00 81.45  ?  475 ALA D CB  1 
ATOM   7597  N N   . GLY C 2 144 ? -9.320  67.983  98.884  1.00 82.47  ?  476 GLY D N   1 
ATOM   7598  C CA  . GLY C 2 144 ? -8.566  68.782  99.818  1.00 84.37  ?  476 GLY D CA  1 
ATOM   7599  C C   . GLY C 2 144 ? -9.308  70.009  100.309 1.00 94.64  ?  476 GLY D C   1 
ATOM   7600  O O   . GLY C 2 144 ? -10.532 70.117  100.239 1.00 94.33  ?  476 GLY D O   1 
ATOM   7601  N N   . ASN C 2 145 ? -8.527  70.945  100.824 1.00 94.67  ?  477 ASN D N   1 
ATOM   7602  C CA  . ASN C 2 145 ? -9.020  72.163  101.429 1.00 92.18  ?  477 ASN D CA  1 
ATOM   7603  C C   . ASN C 2 145 ? -8.751  73.375  100.552 1.00 88.93  ?  477 ASN D C   1 
ATOM   7604  O O   . ASN C 2 145 ? -9.070  74.500  100.939 1.00 91.37  ?  477 ASN D O   1 
ATOM   7605  C CB  . ASN C 2 145 ? -8.349  72.338  102.779 1.00 95.30  ?  477 ASN D CB  1 
ATOM   7606  C CG  . ASN C 2 145 ? -9.147  73.178  103.695 1.00 103.26 ?  477 ASN D CG  1 
ATOM   7607  O OD1 . ASN C 2 145 ? -10.370 73.085  103.714 1.00 94.33  ?  477 ASN D OD1 1 
ATOM   7608  N ND2 . ASN C 2 145 ? -8.474  74.005  104.476 1.00 122.91 ?  477 ASN D ND2 1 
ATOM   7609  N N   . LYS C 2 146 ? -8.173  73.158  99.382  1.00 87.48  ?  478 LYS D N   1 
ATOM   7610  C CA  . LYS C 2 146 ? -7.674  74.152  98.459  1.00 89.43  ?  478 LYS D CA  1 
ATOM   7611  C C   . LYS C 2 146 ? -8.458  74.061  97.157  1.00 100.66 ?  478 LYS D C   1 
ATOM   7612  O O   . LYS C 2 146 ? -8.979  72.993  96.838  1.00 105.30 ?  478 LYS D O   1 
ATOM   7613  C CB  . LYS C 2 146 ? -6.192  73.894  98.189  1.00 88.12  ?  478 LYS D CB  1 
ATOM   7614  C CG  . LYS C 2 146 ? -5.293  74.795  98.967  1.00 86.21  ?  478 LYS D CG  1 
ATOM   7615  C CD  . LYS C 2 146 ? -3.824  74.603  98.661  1.00 82.57  ?  478 LYS D CD  1 
ATOM   7616  C CE  . LYS C 2 146 ? -3.031  75.592  99.508  1.00 84.73  ?  478 LYS D CE  1 
ATOM   7617  N NZ  . LYS C 2 146 ? -3.370  77.019  99.187  1.00 83.74  ?  478 LYS D NZ  1 
ATOM   7618  N N   . PRO C 2 147 ? -8.574  75.157  96.395  1.00 103.05 ?  479 PRO D N   1 
ATOM   7619  C CA  . PRO C 2 147 ? -9.363  75.138  95.144  1.00 103.40 ?  479 PRO D CA  1 
ATOM   7620  C C   . PRO C 2 147 ? -8.636  74.444  93.996  1.00 109.69 ?  479 PRO D C   1 
ATOM   7621  O O   . PRO C 2 147 ? -7.447  74.691  93.759  1.00 109.37 ?  479 PRO D O   1 
ATOM   7622  C CB  . PRO C 2 147 ? -9.568  76.625  94.833  1.00 101.20 ?  479 PRO D CB  1 
ATOM   7623  C CG  . PRO C 2 147 ? -9.383  77.316  96.132  1.00 100.32 ?  479 PRO D CG  1 
ATOM   7624  C CD  . PRO C 2 147 ? -8.366  76.529  96.893  1.00 104.35 ?  479 PRO D CD  1 
ATOM   7625  N N   . CYS C 2 148 ? -9.363  73.584  93.265  1.00 118.58 ?  480 CYS D N   1 
ATOM   7626  C CA  . CYS C 2 148 ? -8.840  72.936  92.059  1.00 111.41 ?  480 CYS D CA  1 
ATOM   7627  C C   . CYS C 2 148 ? -9.591  73.388  90.839  1.00 112.39 ?  480 CYS D C   1 
ATOM   7628  O O   . CYS C 2 148 ? -10.675 72.879  90.549  1.00 116.98 ?  480 CYS D O   1 
ATOM   7629  C CB  . CYS C 2 148 ? -8.893  71.425  92.164  1.00 107.58 ?  480 CYS D CB  1 
ATOM   7630  S SG  . CYS C 2 148 ? -7.374  70.877  92.880  1.00 136.97 ?  480 CYS D SG  1 
ATOM   7631  N N   . ASN C 2 149 ? -8.976  74.282  90.081  1.00 108.55 ?  481 ASN D N   1 
ATOM   7632  C CA  . ASN C 2 149 ? -9.637  74.868  88.925  1.00 108.11 ?  481 ASN D CA  1 
ATOM   7633  C C   . ASN C 2 149 ? -9.363  73.996  87.707  1.00 104.68 ?  481 ASN D C   1 
ATOM   7634  O O   . ASN C 2 149 ? -8.558  74.329  86.840  1.00 103.55 ?  481 ASN D O   1 
ATOM   7635  C CB  . ASN C 2 149 ? -9.145  76.288  88.695  1.00 108.59 ?  481 ASN D CB  1 
ATOM   7636  C CG  . ASN C 2 149 ? -9.344  77.172  89.897  1.00 112.11 ?  481 ASN D CG  1 
ATOM   7637  O OD1 . ASN C 2 149 ? -9.220  76.720  91.034  1.00 112.51 ?  481 ASN D OD1 1 
ATOM   7638  N ND2 . ASN C 2 149 ? -9.704  78.433  89.658  1.00 120.66 ?  481 ASN D ND2 1 
ATOM   7639  N N   . GLY C 2 150 ? -10.053 72.858  87.633  1.00 102.34 ?  482 GLY D N   1 
ATOM   7640  C CA  . GLY C 2 150 ? -9.712  71.878  86.619  1.00 98.67  ?  482 GLY D CA  1 
ATOM   7641  C C   . GLY C 2 150 ? -8.291  71.358  86.806  1.00 107.46 ?  482 GLY D C   1 
ATOM   7642  O O   . GLY C 2 150 ? -7.724  70.686  85.940  1.00 107.92 ?  482 GLY D O   1 
ATOM   7643  N N   . VAL C 2 151 ? -7.681  71.692  87.938  1.00 109.30 ?  483 VAL D N   1 
ATOM   7644  C CA  . VAL C 2 151 ? -6.470  71.004  88.341  1.00 106.52 ?  483 VAL D CA  1 
ATOM   7645  C C   . VAL C 2 151 ? -6.738  69.512  88.382  1.00 103.49 ?  483 VAL D C   1 
ATOM   7646  O O   . VAL C 2 151 ? -7.816  69.060  88.779  1.00 108.97 ?  483 VAL D O   1 
ATOM   7647  C CB  . VAL C 2 151 ? -6.022  71.489  89.730  1.00 117.03 ?  483 VAL D CB  1 
ATOM   7648  C CG1 . VAL C 2 151 ? -4.619  70.942  90.100  1.00 115.50 ?  483 VAL D CG1 1 
ATOM   7649  C CG2 . VAL C 2 151 ? -6.084  73.008  89.815  1.00 120.02 ?  483 VAL D CG2 1 
ATOM   7650  N N   . ALA C 2 152 ? -5.761  68.729  88.018  1.00 99.49  ?  484 ALA D N   1 
ATOM   7651  C CA  . ALA C 2 152 ? -5.796  67.330  88.397  1.00 87.73  ?  484 ALA D CA  1 
ATOM   7652  C C   . ALA C 2 152 ? -4.470  67.135  89.112  1.00 86.63  ?  484 ALA D C   1 
ATOM   7653  O O   . ALA C 2 152 ? -3.426  66.997  88.467  1.00 80.47  ?  484 ALA D O   1 
ATOM   7654  C CB  . ALA C 2 152 ? -5.990  66.428  87.185  1.00 86.38  ?  484 ALA D CB  1 
ATOM   7655  N N   . GLY C 2 153 ? -4.497  67.194  90.442  1.00 83.08  ?  485 GLY D N   1 
ATOM   7656  C CA  . GLY C 2 153 ? -3.247  67.236  91.189  1.00 78.83  ?  485 GLY D CA  1 
ATOM   7657  C C   . GLY C 2 153 ? -3.317  66.751  92.617  1.00 72.02  ?  485 GLY D C   1 
ATOM   7658  O O   . GLY C 2 153 ? -3.876  65.680  92.860  1.00 77.47  ?  485 GLY D O   1 
ATOM   7659  N N   . VAL C 2 154 ? -2.756  67.493  93.574  1.00 77.40  ?  486 VAL D N   1 
ATOM   7660  C CA  . VAL C 2 154 ? -2.826  67.035  94.959  1.00 79.32  ?  486 VAL D CA  1 
ATOM   7661  C C   . VAL C 2 154 ? -4.231  67.202  95.485  1.00 80.77  ?  486 VAL D C   1 
ATOM   7662  O O   . VAL C 2 154 ? -4.873  68.239  95.286  1.00 82.81  ?  486 VAL D O   1 
ATOM   7663  C CB  . VAL C 2 154 ? -1.825  67.753  95.868  1.00 74.51  ?  486 VAL D CB  1 
ATOM   7664  C CG1 . VAL C 2 154 ? -0.453  67.722  95.274  1.00 67.87  ?  486 VAL D CG1 1 
ATOM   7665  C CG2 . VAL C 2 154 ? -2.283  69.175  96.105  1.00 80.67  ?  486 VAL D CG2 1 
ATOM   7666  N N   . ASN C 2 155 ? -4.709  66.157  96.146  1.00 77.51  ?  487 ASN D N   1 
ATOM   7667  C CA  . ASN C 2 155 ? -5.994  66.148  96.807  1.00 81.25  ?  487 ASN D CA  1 
ATOM   7668  C C   . ASN C 2 155 ? -7.112  66.534  95.851  1.00 79.95  ?  487 ASN D C   1 
ATOM   7669  O O   . ASN C 2 155 ? -8.133  67.095  96.266  1.00 82.05  ?  487 ASN D O   1 
ATOM   7670  C CB  . ASN C 2 155 ? -5.942  67.070  98.001  1.00 81.88  ?  487 ASN D CB  1 
ATOM   7671  C CG  . ASN C 2 155 ? -5.230  66.434  99.119  1.00 81.69  ?  487 ASN D CG  1 
ATOM   7672  O OD1 . ASN C 2 155 ? -5.329  65.222  99.316  1.00 89.95  ?  487 ASN D OD1 1 
ATOM   7673  N ND2 . ASN C 2 155 ? -4.429  67.207  99.810  1.00 85.58  ?  487 ASN D ND2 1 
ATOM   7674  N N   . CYS C 2 156 ? -6.886  66.231  94.563  1.00 83.63  ?  488 CYS D N   1 
ATOM   7675  C CA  . CYS C 2 156 ? -7.793  66.552  93.464  1.00 79.67  ?  488 CYS D CA  1 
ATOM   7676  C C   . CYS C 2 156 ? -7.684  65.470  92.408  1.00 73.95  ?  488 CYS D C   1 
ATOM   7677  O O   . CYS C 2 156 ? -6.672  65.388  91.702  1.00 70.61  ?  488 CYS D O   1 
ATOM   7678  C CB  . CYS C 2 156 ? -7.478  67.911  92.870  1.00 83.64  ?  488 CYS D CB  1 
ATOM   7679  S SG  . CYS C 2 156 ? -7.812  69.231  93.996  1.00 98.37  ?  488 CYS D SG  1 
ATOM   7680  N N   . TYR C 2 157 ? -8.743  64.688  92.280  1.00 77.05  ?  489 TYR D N   1 
ATOM   7681  C CA  . TYR C 2 157 ? -8.736  63.537  91.408  1.00 77.69  ?  489 TYR D CA  1 
ATOM   7682  C C   . TYR C 2 157 ? -9.858  63.633  90.382  1.00 71.75  ?  489 TYR D C   1 
ATOM   7683  O O   . TYR C 2 157 ? -10.933 64.184  90.653  1.00 68.91  ?  489 TYR D O   1 
ATOM   7684  C CB  . TYR C 2 157 ? -8.824  62.253  92.249  1.00 78.41  ?  489 TYR D CB  1 
ATOM   7685  C CG  . TYR C 2 157 ? -7.989  62.334  93.512  1.00 78.39  ?  489 TYR D CG  1 
ATOM   7686  C CD1 . TYR C 2 157 ? -6.601  62.176  93.466  1.00 82.52  ?  489 TYR D CD1 1 
ATOM   7687  C CD2 . TYR C 2 157 ? -8.573  62.599  94.740  1.00 76.91  ?  489 TYR D CD2 1 
ATOM   7688  C CE1 . TYR C 2 157 ? -5.813  62.277  94.626  1.00 76.94  ?  489 TYR D CE1 1 
ATOM   7689  C CE2 . TYR C 2 157 ? -7.799  62.696  95.898  1.00 78.85  ?  489 TYR D CE2 1 
ATOM   7690  C CZ  . TYR C 2 157 ? -6.425  62.537  95.838  1.00 76.05  ?  489 TYR D CZ  1 
ATOM   7691  O OH  . TYR C 2 157 ? -5.695  62.643  97.003  1.00 89.36  ?  489 TYR D OH  1 
ATOM   7692  N N   . PHE C 2 158 ? -9.545  63.157  89.177  1.00 64.21  ?  490 PHE D N   1 
ATOM   7693  C CA  . PHE C 2 158 ? -10.551 62.855  88.187  1.00 67.04  ?  490 PHE D CA  1 
ATOM   7694  C C   . PHE C 2 158 ? -11.533 61.846  88.758  1.00 67.59  ?  490 PHE D C   1 
ATOM   7695  O O   . PHE C 2 158 ? -11.116 60.748  89.146  1.00 66.52  ?  490 PHE D O   1 
ATOM   7696  C CB  . PHE C 2 158 ? -9.928  62.266  86.943  1.00 69.18  ?  490 PHE D CB  1 
ATOM   7697  C CG  . PHE C 2 158 ? -10.837 62.298  85.778  1.00 67.28  ?  490 PHE D CG  1 
ATOM   7698  C CD1 . PHE C 2 158 ? -11.594 63.429  85.510  1.00 66.82  ?  490 PHE D CD1 1 
ATOM   7699  C CD2 . PHE C 2 158 ? -11.038 61.152  85.026  1.00 66.33  ?  490 PHE D CD2 1 
ATOM   7700  C CE1 . PHE C 2 158 ? -12.472 63.442  84.447  1.00 69.06  ?  490 PHE D CE1 1 
ATOM   7701  C CE2 . PHE C 2 158 ? -11.915 61.148  83.976  1.00 68.84  ?  490 PHE D CE2 1 
ATOM   7702  C CZ  . PHE C 2 158 ? -12.640 62.296  83.679  1.00 69.02  ?  490 PHE D CZ  1 
ATOM   7703  N N   . PRO C 2 159 ? -12.830 62.141  88.792  1.00 64.81  ?  491 PRO D N   1 
ATOM   7704  C CA  . PRO C 2 159 ? -13.746 61.271  89.528  1.00 65.37  ?  491 PRO D CA  1 
ATOM   7705  C C   . PRO C 2 159 ? -13.953 59.911  88.896  1.00 65.93  ?  491 PRO D C   1 
ATOM   7706  O O   . PRO C 2 159 ? -14.472 59.017  89.577  1.00 67.69  ?  491 PRO D O   1 
ATOM   7707  C CB  . PRO C 2 159 ? -15.048 62.093  89.579  1.00 69.45  ?  491 PRO D CB  1 
ATOM   7708  C CG  . PRO C 2 159 ? -14.964 62.997  88.456  1.00 70.05  ?  491 PRO D CG  1 
ATOM   7709  C CD  . PRO C 2 159 ? -13.503 63.349  88.303  1.00 68.67  ?  491 PRO D CD  1 
ATOM   7710  N N   . LEU C 2 160 ? -13.521 59.690  87.664  1.00 63.58  ?  492 LEU D N   1 
ATOM   7711  C CA  . LEU C 2 160 ? -13.838 58.467  86.931  1.00 64.63  ?  492 LEU D CA  1 
ATOM   7712  C C   . LEU C 2 160 ? -12.628 57.585  86.720  1.00 59.34  ?  492 LEU D C   1 
ATOM   7713  O O   . LEU C 2 160 ? -11.657 58.005  86.102  1.00 60.34  ?  492 LEU D O   1 
ATOM   7714  C CB  . LEU C 2 160 ? -14.479 58.797  85.587  1.00 67.19  ?  492 LEU D CB  1 
ATOM   7715  C CG  . LEU C 2 160 ? -15.938 59.191  85.423  1.00 63.26  ?  492 LEU D CG  1 
ATOM   7716  C CD1 . LEU C 2 160 ? -16.261 60.648  85.542  1.00 65.50  ?  492 LEU D CD1 1 
ATOM   7717  C CD2 . LEU C 2 160 ? -16.064 58.833  83.982  1.00 64.95  ?  492 LEU D CD2 1 
ATOM   7718  N N   . GLN C 2 161 ? -12.740 56.346  87.166  1.00 61.08  ?  493 GLN D N   1 
ATOM   7719  C CA  . GLN C 2 161 ? -11.710 55.335  87.034  1.00 63.23  ?  493 GLN D CA  1 
ATOM   7720  C C   . GLN C 2 161 ? -12.209 54.305  86.036  1.00 61.92  ?  493 GLN D C   1 
ATOM   7721  O O   . GLN C 2 161 ? -13.413 54.166  85.847  1.00 66.63  ?  493 GLN D O   1 
ATOM   7722  C CB  . GLN C 2 161 ? -11.469 54.665  88.385  1.00 69.09  ?  493 GLN D CB  1 
ATOM   7723  C CG  . GLN C 2 161 ? -10.140 54.072  88.578  1.00 72.44  ?  493 GLN D CG  1 
ATOM   7724  C CD  . GLN C 2 161 ? -9.178  55.169  88.945  1.00 82.08  ?  493 GLN D CD  1 
ATOM   7725  O OE1 . GLN C 2 161 ? -9.511  56.379  88.864  1.00 67.77  ?  493 GLN D OE1 1 
ATOM   7726  N NE2 . GLN C 2 161 ? -7.973  54.771  89.354  1.00 93.25  ?  493 GLN D NE2 1 
ATOM   7727  N N   . SER C 2 162 ? -11.312 53.555  85.406  1.00 59.95  ?  494 SER D N   1 
ATOM   7728  C CA  . SER C 2 162 ? -11.805 52.520  84.507  1.00 63.97  ?  494 SER D CA  1 
ATOM   7729  C C   . SER C 2 162 ? -11.428 51.124  84.992  1.00 62.30  ?  494 SER D C   1 
ATOM   7730  O O   . SER C 2 162 ? -10.369 50.912  85.574  1.00 65.90  ?  494 SER D O   1 
ATOM   7731  C CB  . SER C 2 162 ? -11.338 52.726  83.053  1.00 66.24  ?  494 SER D CB  1 
ATOM   7732  O OG  . SER C 2 162 ? -9.987  53.103  82.949  1.00 66.21  ?  494 SER D OG  1 
ATOM   7733  N N   . TYR C 2 163 ? -12.324 50.173  84.746  1.00 61.34  ?  495 TYR D N   1 
ATOM   7734  C CA  . TYR C 2 163 ? -12.108 48.792  85.166  1.00 61.12  ?  495 TYR D CA  1 
ATOM   7735  C C   . TYR C 2 163 ? -11.014 48.180  84.293  1.00 59.88  ?  495 TYR D C   1 
ATOM   7736  O O   . TYR C 2 163 ? -11.104 48.174  83.064  1.00 64.94  ?  495 TYR D O   1 
ATOM   7737  C CB  . TYR C 2 163 ? -13.369 47.919  85.025  1.00 60.81  ?  495 TYR D CB  1 
ATOM   7738  C CG  . TYR C 2 163 ? -14.622 48.361  85.733  1.00 55.49  ?  495 TYR D CG  1 
ATOM   7739  C CD1 . TYR C 2 163 ? -14.620 49.384  86.635  1.00 61.85  ?  495 TYR D CD1 1 
ATOM   7740  C CD2 . TYR C 2 163 ? -15.678 47.493  85.810  1.00 59.17  ?  495 TYR D CD2 1 
ATOM   7741  C CE1 . TYR C 2 163 ? -15.743 49.700  87.314  1.00 61.42  ?  495 TYR D CE1 1 
ATOM   7742  C CE2 . TYR C 2 163 ? -16.783 47.746  86.560  1.00 64.94  ?  495 TYR D CE2 1 
ATOM   7743  C CZ  . TYR C 2 163 ? -16.811 48.849  87.333  1.00 61.09  ?  495 TYR D CZ  1 
ATOM   7744  O OH  . TYR C 2 163 ? -17.942 49.086  88.079  1.00 60.46  ?  495 TYR D OH  1 
ATOM   7745  N N   . GLY C 2 164 ? -9.993  47.631  84.901  1.00 53.39  ?  496 GLY D N   1 
ATOM   7746  C CA  . GLY C 2 164 ? -8.965  47.211  83.974  1.00 62.69  ?  496 GLY D CA  1 
ATOM   7747  C C   . GLY C 2 164 ? -9.230  45.891  83.290  1.00 63.25  ?  496 GLY D C   1 
ATOM   7748  O O   . GLY C 2 164 ? -8.397  44.989  83.396  1.00 71.31  ?  496 GLY D O   1 
ATOM   7749  N N   . PHE C 2 165 ? -10.355 45.729  82.609  1.00 62.68  ?  497 PHE D N   1 
ATOM   7750  C CA  . PHE C 2 165 ? -10.855 44.373  82.433  1.00 64.27  ?  497 PHE D CA  1 
ATOM   7751  C C   . PHE C 2 165 ? -9.920  43.544  81.579  1.00 67.72  ?  497 PHE D C   1 
ATOM   7752  O O   . PHE C 2 165 ? -9.411  44.007  80.559  1.00 71.16  ?  497 PHE D O   1 
ATOM   7753  C CB  . PHE C 2 165 ? -12.212 44.360  81.799  1.00 67.28  ?  497 PHE D CB  1 
ATOM   7754  C CG  . PHE C 2 165 ? -13.309 44.604  82.756  1.00 65.28  ?  497 PHE D CG  1 
ATOM   7755  C CD1 . PHE C 2 165 ? -13.329 43.939  83.960  1.00 62.89  ?  497 PHE D CD1 1 
ATOM   7756  C CD2 . PHE C 2 165 ? -14.387 45.406  82.405  1.00 64.36  ?  497 PHE D CD2 1 
ATOM   7757  C CE1 . PHE C 2 165 ? -14.351 44.121  84.829  1.00 63.43  ?  497 PHE D CE1 1 
ATOM   7758  C CE2 . PHE C 2 165 ? -15.415 45.584  83.266  1.00 65.05  ?  497 PHE D CE2 1 
ATOM   7759  C CZ  . PHE C 2 165 ? -15.406 44.922  84.479  1.00 65.93  ?  497 PHE D CZ  1 
ATOM   7760  N N   . ARG C 2 166 ? -9.718  42.302  82.017  1.00 65.61  ?  498 ARG D N   1 
ATOM   7761  C CA  . ARG C 2 166 ? -8.754  41.335  81.497  1.00 70.08  ?  498 ARG D CA  1 
ATOM   7762  C C   . ARG C 2 166 ? -9.328  39.944  81.688  1.00 71.35  ?  498 ARG D C   1 
ATOM   7763  O O   . ARG C 2 166 ? -9.966  39.687  82.716  1.00 72.12  ?  498 ARG D O   1 
ATOM   7764  C CB  . ARG C 2 166 ? -7.397  41.441  82.197  1.00 69.40  ?  498 ARG D CB  1 
ATOM   7765  C CG  . ARG C 2 166 ? -6.492  42.509  81.635  1.00 73.44  ?  498 ARG D CG  1 
ATOM   7766  C CD  . ARG C 2 166 ? -5.243  42.653  82.464  1.00 67.13  ?  498 ARG D CD  1 
ATOM   7767  N NE  . ARG C 2 166 ? -5.086  44.029  82.913  1.00 68.18  ?  498 ARG D NE  1 
ATOM   7768  C CZ  . ARG C 2 166 ? -4.599  45.017  82.174  1.00 74.04  ?  498 ARG D CZ  1 
ATOM   7769  N NH1 . ARG C 2 166 ? -3.956  44.783  81.033  1.00 77.83  ?  498 ARG D NH1 1 
ATOM   7770  N NH2 . ARG C 2 166 ? -4.729  46.270  82.606  1.00 73.04  ?  498 ARG D NH2 1 
ATOM   7771  N N   . PRO C 2 167 ? -9.131  39.036  80.731  1.00 70.43  ?  499 PRO D N   1 
ATOM   7772  C CA  . PRO C 2 167 ? -9.822  37.733  80.814  1.00 72.26  ?  499 PRO D CA  1 
ATOM   7773  C C   . PRO C 2 167 ? -9.368  36.857  81.987  1.00 74.20  ?  499 PRO D C   1 
ATOM   7774  O O   . PRO C 2 167 ? -10.157 36.033  82.495  1.00 69.70  ?  499 PRO D O   1 
ATOM   7775  C CB  . PRO C 2 167 ? -9.499  37.096  79.449  1.00 72.49  ?  499 PRO D CB  1 
ATOM   7776  C CG  . PRO C 2 167 ? -8.234  37.810  78.976  1.00 70.34  ?  499 PRO D CG  1 
ATOM   7777  C CD  . PRO C 2 167 ? -8.400  39.209  79.457  1.00 70.12  ?  499 PRO D CD  1 
ATOM   7778  N N   . THR C 2 168 ? -8.119  37.017  82.438  1.00 76.00  ?  500 THR D N   1 
ATOM   7779  C CA  . THR C 2 168 ? -7.535  36.176  83.482  1.00 73.92  ?  500 THR D CA  1 
ATOM   7780  C C   . THR C 2 168 ? -7.861  36.661  84.896  1.00 73.62  ?  500 THR D C   1 
ATOM   7781  O O   . THR C 2 168 ? -7.221  36.230  85.870  1.00 74.30  ?  500 THR D O   1 
ATOM   7782  C CB  . THR C 2 168 ? -6.026  36.044  83.243  1.00 70.97  ?  500 THR D CB  1 
ATOM   7783  O OG1 . THR C 2 168 ? -5.380  37.252  83.633  1.00 76.46  ?  500 THR D OG1 1 
ATOM   7784  C CG2 . THR C 2 168 ? -5.748  35.820  81.811  1.00 70.70  ?  500 THR D CG2 1 
ATOM   7785  N N   . TYR C 2 169 ? -8.858  37.529  85.034  1.00 73.23  ?  501 TYR D N   1 
ATOM   7786  C CA  . TYR C 2 169 ? -9.277  38.046  86.311  1.00 68.07  ?  501 TYR D CA  1 
ATOM   7787  C C   . TYR C 2 169 ? -10.125 36.988  86.986  1.00 65.63  ?  501 TYR D C   1 
ATOM   7788  O O   . TYR C 2 169 ? -10.511 35.995  86.381  1.00 69.10  ?  501 TYR D O   1 
ATOM   7789  C CB  . TYR C 2 169 ? -10.066 39.332  86.104  1.00 66.13  ?  501 TYR D CB  1 
ATOM   7790  C CG  . TYR C 2 169 ? -9.205  40.583  86.006  1.00 63.61  ?  501 TYR D CG  1 
ATOM   7791  C CD1 . TYR C 2 169 ? -7.847  40.513  85.661  1.00 66.34  ?  501 TYR D CD1 1 
ATOM   7792  C CD2 . TYR C 2 169 ? -9.778  41.841  86.086  1.00 63.09  ?  501 TYR D CD2 1 
ATOM   7793  C CE1 . TYR C 2 169 ? -7.051  41.692  85.525  1.00 67.86  ?  501 TYR D CE1 1 
ATOM   7794  C CE2 . TYR C 2 169 ? -9.011  43.014  85.935  1.00 65.33  ?  501 TYR D CE2 1 
ATOM   7795  C CZ  . TYR C 2 169 ? -7.651  42.951  85.650  1.00 66.06  ?  501 TYR D CZ  1 
ATOM   7796  O OH  . TYR C 2 169 ? -6.947  44.158  85.515  1.00 56.09  ?  501 TYR D OH  1 
ATOM   7797  N N   . GLY C 2 170 ? -10.374 37.175  88.247  1.00 68.34  ?  502 GLY D N   1 
ATOM   7798  C CA  . GLY C 2 170 ? -11.177 36.227  88.977  1.00 71.42  ?  502 GLY D CA  1 
ATOM   7799  C C   . GLY C 2 170 ? -12.627 36.532  88.827  1.00 77.26  ?  502 GLY D C   1 
ATOM   7800  O O   . GLY C 2 170 ? -12.999 37.657  88.519  1.00 75.33  ?  502 GLY D O   1 
ATOM   7801  N N   . VAL C 2 171 ? -13.445 35.504  89.047  1.00 86.01  ?  503 VAL D N   1 
ATOM   7802  C CA  . VAL C 2 171 ? -14.853 35.609  88.705  1.00 87.51  ?  503 VAL D CA  1 
ATOM   7803  C C   . VAL C 2 171 ? -15.534 36.806  89.364  1.00 89.69  ?  503 VAL D C   1 
ATOM   7804  O O   . VAL C 2 171 ? -16.470 37.385  88.793  1.00 88.82  ?  503 VAL D O   1 
ATOM   7805  C CB  . VAL C 2 171 ? -15.526 34.264  89.016  1.00 87.81  ?  503 VAL D CB  1 
ATOM   7806  C CG1 . VAL C 2 171 ? -17.025 34.404  89.038  1.00 91.65  ?  503 VAL D CG1 1 
ATOM   7807  C CG2 . VAL C 2 171 ? -15.098 33.243  87.951  1.00 91.61  ?  503 VAL D CG2 1 
ATOM   7808  N N   . GLY C 2 172 ? -15.034 37.254  90.510  1.00 82.01  ?  504 GLY D N   1 
ATOM   7809  C CA  . GLY C 2 172 ? -15.545 38.488  91.062  1.00 79.13  ?  504 GLY D CA  1 
ATOM   7810  C C   . GLY C 2 172 ? -15.055 39.758  90.394  1.00 75.19  ?  504 GLY D C   1 
ATOM   7811  O O   . GLY C 2 172 ? -15.684 40.805  90.577  1.00 79.54  ?  504 GLY D O   1 
ATOM   7812  N N   . HIS C 2 173 ? -13.943 39.707  89.650  1.00 67.37  ?  505 HIS D N   1 
ATOM   7813  C CA  . HIS C 2 173 ? -13.354 40.909  89.065  1.00 66.89  ?  505 HIS D CA  1 
ATOM   7814  C C   . HIS C 2 173 ? -13.515 40.956  87.557  1.00 69.88  ?  505 HIS D C   1 
ATOM   7815  O O   . HIS C 2 173 ? -12.867 41.774  86.898  1.00 67.53  ?  505 HIS D O   1 
ATOM   7816  C CB  . HIS C 2 173 ? -11.869 41.027  89.367  1.00 68.02  ?  505 HIS D CB  1 
ATOM   7817  C CG  . HIS C 2 173 ? -11.571 41.714  90.648  1.00 71.34  ?  505 HIS D CG  1 
ATOM   7818  N ND1 . HIS C 2 173 ? -11.484 41.037  91.844  1.00 70.48  ?  505 HIS D ND1 1 
ATOM   7819  C CD2 . HIS C 2 173 ? -11.427 43.024  90.940  1.00 73.38  ?  505 HIS D CD2 1 
ATOM   7820  C CE1 . HIS C 2 173 ? -11.246 41.900  92.815  1.00 75.40  ?  505 HIS D CE1 1 
ATOM   7821  N NE2 . HIS C 2 173 ? -11.210 43.114  92.293  1.00 77.12  ?  505 HIS D NE2 1 
ATOM   7822  N N   . GLN C 2 174 ? -14.311 40.079  87.009  1.00 71.52  ?  506 GLN D N   1 
ATOM   7823  C CA  . GLN C 2 174 ? -14.710 39.846  85.636  1.00 64.87  ?  506 GLN D CA  1 
ATOM   7824  C C   . GLN C 2 174 ? -15.913 40.711  85.305  1.00 65.20  ?  506 GLN D C   1 
ATOM   7825  O O   . GLN C 2 174 ? -16.742 40.989  86.178  1.00 64.05  ?  506 GLN D O   1 
ATOM   7826  C CB  . GLN C 2 174 ? -15.059 38.371  85.428  1.00 65.95  ?  506 GLN D CB  1 
ATOM   7827  C CG  . GLN C 2 174 ? -13.848 37.508  85.113  1.00 66.77  ?  506 GLN D CG  1 
ATOM   7828  C CD  . GLN C 2 174 ? -14.198 36.076  84.767  1.00 70.90  ?  506 GLN D CD  1 
ATOM   7829  O OE1 . GLN C 2 174 ? -15.364 35.732  84.640  1.00 80.69  ?  506 GLN D OE1 1 
ATOM   7830  N NE2 . GLN C 2 174 ? -13.184 35.240  84.586  1.00 68.15  ?  506 GLN D NE2 1 
ATOM   7831  N N   . PRO C 2 175 ? -16.009 41.131  84.047  1.00 72.73  ?  507 PRO D N   1 
ATOM   7832  C CA  . PRO C 2 175 ? -17.079 42.052  83.654  1.00 71.74  ?  507 PRO D CA  1 
ATOM   7833  C C   . PRO C 2 175 ? -18.426 41.346  83.595  1.00 70.04  ?  507 PRO D C   1 
ATOM   7834  O O   . PRO C 2 175 ? -18.530 40.208  83.149  1.00 73.88  ?  507 PRO D O   1 
ATOM   7835  C CB  . PRO C 2 175 ? -16.632 42.530  82.270  1.00 69.98  ?  507 PRO D CB  1 
ATOM   7836  C CG  . PRO C 2 175 ? -15.762 41.462  81.769  1.00 70.32  ?  507 PRO D CG  1 
ATOM   7837  C CD  . PRO C 2 175 ? -15.055 40.895  82.955  1.00 71.54  ?  507 PRO D CD  1 
ATOM   7838  N N   . TYR C 2 176 ? -19.457 42.028  84.068  1.00 62.43  ?  508 TYR D N   1 
ATOM   7839  C CA  . TYR C 2 176 ? -20.825 41.526  84.045  1.00 69.16  ?  508 TYR D CA  1 
ATOM   7840  C C   . TYR C 2 176 ? -21.758 42.551  83.418  1.00 71.83  ?  508 TYR D C   1 
ATOM   7841  O O   . TYR C 2 176 ? -21.856 43.677  83.921  1.00 72.55  ?  508 TYR D O   1 
ATOM   7842  C CB  . TYR C 2 176 ? -21.331 41.201  85.452  1.00 69.64  ?  508 TYR D CB  1 
ATOM   7843  C CG  . TYR C 2 176 ? -20.972 39.831  85.916  1.00 73.13  ?  508 TYR D CG  1 
ATOM   7844  C CD1 . TYR C 2 176 ? -19.654 39.494  86.201  1.00 76.65  ?  508 TYR D CD1 1 
ATOM   7845  C CD2 . TYR C 2 176 ? -21.958 38.868  86.086  1.00 76.15  ?  508 TYR D CD2 1 
ATOM   7846  C CE1 . TYR C 2 176 ? -19.323 38.212  86.626  1.00 80.66  ?  508 TYR D CE1 1 
ATOM   7847  C CE2 . TYR C 2 176 ? -21.648 37.596  86.511  1.00 87.69  ?  508 TYR D CE2 1 
ATOM   7848  C CZ  . TYR C 2 176 ? -20.331 37.264  86.783  1.00 88.87  ?  508 TYR D CZ  1 
ATOM   7849  O OH  . TYR C 2 176 ? -20.007 35.984  87.200  1.00 90.73  ?  508 TYR D OH  1 
ATOM   7850  N N   . ARG C 2 177 ? -22.481 42.160  82.356  1.00 70.80  ?  509 ARG D N   1 
ATOM   7851  C CA  . ARG C 2 177 ? -23.489 43.084  81.833  1.00 68.19  ?  509 ARG D CA  1 
ATOM   7852  C C   . ARG C 2 177 ? -24.778 42.879  82.615  1.00 69.17  ?  509 ARG D C   1 
ATOM   7853  O O   . ARG C 2 177 ? -25.056 41.782  83.120  1.00 71.44  ?  509 ARG D O   1 
ATOM   7854  C CB  . ARG C 2 177 ? -23.698 42.952  80.310  1.00 65.73  ?  509 ARG D CB  1 
ATOM   7855  C CG  . ARG C 2 177 ? -22.544 42.234  79.662  1.00 67.93  ?  509 ARG D CG  1 
ATOM   7856  C CD  . ARG C 2 177 ? -22.475 41.995  78.148  1.00 72.64  ?  509 ARG D CD  1 
ATOM   7857  N NE  . ARG C 2 177 ? -22.051 43.140  77.347  1.00 72.58  ?  509 ARG D NE  1 
ATOM   7858  C CZ  . ARG C 2 177 ? -22.219 43.258  76.034  1.00 78.97  ?  509 ARG D CZ  1 
ATOM   7859  N NH1 . ARG C 2 177 ? -22.832 42.321  75.321  1.00 85.11  ?  509 ARG D NH1 1 
ATOM   7860  N NH2 . ARG C 2 177 ? -21.721 44.324  75.414  1.00 79.94  ?  509 ARG D NH2 1 
ATOM   7861  N N   . VAL C 2 178 ? -25.530 43.973  82.773  1.00 70.09  ?  510 VAL D N   1 
ATOM   7862  C CA  . VAL C 2 178 ? -26.723 44.002  83.620  1.00 71.46  ?  510 VAL D CA  1 
ATOM   7863  C C   . VAL C 2 178 ? -27.824 44.858  83.008  1.00 74.36  ?  510 VAL D C   1 
ATOM   7864  O O   . VAL C 2 178 ? -27.569 45.890  82.367  1.00 73.30  ?  510 VAL D O   1 
ATOM   7865  C CB  . VAL C 2 178 ? -26.404 44.551  85.016  1.00 69.47  ?  510 VAL D CB  1 
ATOM   7866  C CG1 . VAL C 2 178 ? -25.789 43.514  85.838  1.00 69.78  ?  510 VAL D CG1 1 
ATOM   7867  C CG2 . VAL C 2 178 ? -25.422 45.598  84.843  1.00 68.15  ?  510 VAL D CG2 1 
ATOM   7868  N N   . VAL C 2 179 ? -29.063 44.452  83.291  1.00 76.59  ?  511 VAL D N   1 
ATOM   7869  C CA  . VAL C 2 179 ? -30.274 45.143  82.859  1.00 75.21  ?  511 VAL D CA  1 
ATOM   7870  C C   . VAL C 2 179 ? -31.240 45.203  84.034  1.00 78.27  ?  511 VAL D C   1 
ATOM   7871  O O   . VAL C 2 179 ? -31.534 44.181  84.664  1.00 83.73  ?  511 VAL D O   1 
ATOM   7872  C CB  . VAL C 2 179 ? -30.952 44.424  81.686  1.00 76.89  ?  511 VAL D CB  1 
ATOM   7873  C CG1 . VAL C 2 179 ? -32.104 45.252  81.205  1.00 82.74  ?  511 VAL D CG1 1 
ATOM   7874  C CG2 . VAL C 2 179 ? -29.972 44.098  80.586  1.00 77.59  ?  511 VAL D CG2 1 
ATOM   7875  N N   . VAL C 2 180 ? -31.738 46.388  84.319  1.00 72.91  ?  512 VAL D N   1 
ATOM   7876  C CA  . VAL C 2 180 ? -32.676 46.617  85.409  1.00 82.65  ?  512 VAL D CA  1 
ATOM   7877  C C   . VAL C 2 180 ? -33.976 47.079  84.781  1.00 87.60  ?  512 VAL D C   1 
ATOM   7878  O O   . VAL C 2 180 ? -34.038 48.183  84.219  1.00 91.23  ?  512 VAL D O   1 
ATOM   7879  C CB  . VAL C 2 180 ? -32.159 47.646  86.424  1.00 80.51  ?  512 VAL D CB  1 
ATOM   7880  C CG1 . VAL C 2 180 ? -33.138 47.772  87.555  1.00 86.16  ?  512 VAL D CG1 1 
ATOM   7881  C CG2 . VAL C 2 180 ? -30.820 47.215  86.975  1.00 77.57  ?  512 VAL D CG2 1 
ATOM   7882  N N   . LEU C 2 181 ? -35.005 46.234  84.865  1.00 94.20  ?  513 LEU D N   1 
ATOM   7883  C CA  . LEU C 2 181 ? -36.327 46.531  84.312  1.00 97.01  ?  513 LEU D CA  1 
ATOM   7884  C C   . LEU C 2 181 ? -37.179 47.147  85.409  1.00 105.67 ?  513 LEU D C   1 
ATOM   7885  O O   . LEU C 2 181 ? -37.763 46.440  86.226  1.00 111.00 ?  513 LEU D O   1 
ATOM   7886  C CB  . LEU C 2 181 ? -36.974 45.277  83.747  1.00 96.53  ?  513 LEU D CB  1 
ATOM   7887  C CG  . LEU C 2 181 ? -36.157 44.528  82.714  1.00 86.25  ?  513 LEU D CG  1 
ATOM   7888  C CD1 . LEU C 2 181 ? -36.894 43.312  82.263  1.00 76.47  ?  513 LEU D CD1 1 
ATOM   7889  C CD2 . LEU C 2 181 ? -35.894 45.460  81.556  1.00 84.81  ?  513 LEU D CD2 1 
ATOM   7890  N N   . SER C 2 182 ? -37.237 48.482  85.428  1.00 106.49 ?  514 SER D N   1 
ATOM   7891  C CA  . SER C 2 182 ? -38.133 49.221  86.314  1.00 112.79 ?  514 SER D CA  1 
ATOM   7892  C C   . SER C 2 182 ? -39.545 49.135  85.763  1.00 121.38 ?  514 SER D C   1 
ATOM   7893  O O   . SER C 2 182 ? -39.848 49.732  84.723  1.00 125.50 ?  514 SER D O   1 
ATOM   7894  C CB  . SER C 2 182 ? -37.693 50.681  86.444  1.00 109.13 ?  514 SER D CB  1 
ATOM   7895  O OG  . SER C 2 182 ? -38.757 51.521  86.889  1.00 112.34 ?  514 SER D OG  1 
ATOM   7896  N N   . PHE C 2 183 ? -40.395 48.361  86.448  1.00 129.35 ?  515 PHE D N   1 
ATOM   7897  C CA  . PHE C 2 183 ? -41.820 48.243  86.144  1.00 131.05 ?  515 PHE D CA  1 
ATOM   7898  C C   . PHE C 2 183 ? -42.561 49.295  86.950  1.00 140.07 ?  515 PHE D C   1 
ATOM   7899  O O   . PHE C 2 183 ? -42.726 49.145  88.164  1.00 138.77 ?  515 PHE D O   1 
ATOM   7900  C CB  . PHE C 2 183 ? -42.345 46.863  86.522  1.00 123.40 ?  515 PHE D CB  1 
ATOM   7901  C CG  . PHE C 2 183 ? -41.906 45.776  85.622  1.00 118.96 ?  515 PHE D CG  1 
ATOM   7902  C CD1 . PHE C 2 183 ? -41.558 46.037  84.312  1.00 120.70 ?  515 PHE D CD1 1 
ATOM   7903  C CD2 . PHE C 2 183 ? -41.787 44.490  86.110  1.00 118.16 ?  515 PHE D CD2 1 
ATOM   7904  C CE1 . PHE C 2 183 ? -41.141 45.015  83.483  1.00 121.44 ?  515 PHE D CE1 1 
ATOM   7905  C CE2 . PHE C 2 183 ? -41.363 43.473  85.306  1.00 125.93 ?  515 PHE D CE2 1 
ATOM   7906  C CZ  . PHE C 2 183 ? -41.039 43.730  83.982  1.00 128.32 ?  515 PHE D CZ  1 
ATOM   7907  N N   . GLU C 2 184 ? -43.008 50.355  86.301  1.00 149.69 ?  516 GLU D N   1 
ATOM   7908  C CA  . GLU C 2 184 ? -43.894 51.301  86.954  1.00 161.64 ?  516 GLU D CA  1 
ATOM   7909  C C   . GLU C 2 184 ? -45.311 51.083  86.440  1.00 171.48 ?  516 GLU D C   1 
ATOM   7910  O O   . GLU C 2 184 ? -45.507 50.742  85.267  1.00 173.58 ?  516 GLU D O   1 
ATOM   7911  C CB  . GLU C 2 184 ? -43.447 52.751  86.734  1.00 169.10 ?  516 GLU D CB  1 
ATOM   7912  C CG  . GLU C 2 184 ? -43.836 53.349  85.395  1.00 174.79 ?  516 GLU D CG  1 
ATOM   7913  C CD  . GLU C 2 184 ? -43.246 54.723  85.155  1.00 172.80 ?  516 GLU D CD  1 
ATOM   7914  O OE1 . GLU C 2 184 ? -43.519 55.624  85.978  1.00 169.19 ?  516 GLU D OE1 1 
ATOM   7915  O OE2 . GLU C 2 184 ? -42.547 54.917  84.138  1.00 172.17 -1 516 GLU D OE2 1 
ATOM   7916  N N   . LEU C 2 185 ? -46.307 51.315  87.302  1.00 181.69 ?  517 LEU D N   1 
ATOM   7917  C CA  . LEU C 2 185 ? -47.731 51.172  86.878  1.00 183.86 ?  517 LEU D CA  1 
ATOM   7918  C C   . LEU C 2 185 ? -48.618 52.193  87.604  1.00 184.49 ?  517 LEU D C   1 
ATOM   7919  O O   . LEU C 2 185 ? -49.043 51.895  88.739  1.00 182.79 ?  517 LEU D O   1 
ATOM   7920  C CB  . LEU C 2 185 ? -48.185 49.742  87.174  1.00 182.71 ?  517 LEU D CB  1 
ATOM   7921  C CG  . LEU C 2 185 ? -49.617 49.405  86.766  1.00 184.32 ?  517 LEU D CG  1 
ATOM   7922  C CD1 . LEU C 2 185 ? -49.940 49.978  85.393  1.00 182.48 ?  517 LEU D CD1 1 
ATOM   7923  C CD2 . LEU C 2 185 ? -49.838 47.900  86.795  1.00 181.51 ?  517 LEU D CD2 1 
ATOM   7924  N N   . LEU C 2 186 ? -48.904 53.335  86.965  1.00 186.89 ?  518 LEU D N   1 
ATOM   7925  C CA  . LEU C 2 186 ? -49.742 54.403  87.588  1.00 186.16 ?  518 LEU D CA  1 
ATOM   7926  C C   . LEU C 2 186 ? -50.966 54.702  86.711  1.00 197.02 ?  518 LEU D C   1 
ATOM   7927  O O   . LEU C 2 186 ? -51.189 53.961  85.731  1.00 195.54 ?  518 LEU D O   1 
ATOM   7928  C CB  . LEU C 2 186 ? -48.906 55.671  87.773  1.00 175.88 ?  518 LEU D CB  1 
ATOM   7929  C CG  . LEU C 2 186 ? -48.319 56.268  86.497  1.00 174.16 ?  518 LEU D CG  1 
ATOM   7930  C CD1 . LEU C 2 186 ? -48.718 57.727  86.359  1.00 155.04 ?  518 LEU D CD1 1 
ATOM   7931  C CD2 . LEU C 2 186 ? -46.806 56.140  86.510  1.00 172.64 ?  518 LEU D CD2 1 
ATOM   7932  N N   . HIS C 2 187 ? -51.707 55.766  87.038  1.00 200.47 ?  519 HIS D N   1 
ATOM   7933  C CA  . HIS C 2 187 ? -52.939 56.128  86.284  1.00 204.14 ?  519 HIS D CA  1 
ATOM   7934  C C   . HIS C 2 187 ? -52.627 56.309  84.796  1.00 218.21 ?  519 HIS D C   1 
ATOM   7935  O O   . HIS C 2 187 ? -53.564 56.181  83.991  1.00 214.83 ?  519 HIS D O   1 
ATOM   7936  C CB  . HIS C 2 187 ? -53.567 57.398  86.874  1.00 194.90 ?  519 HIS D CB  1 
ATOM   7937  C CG  . HIS C 2 187 ? -53.981 57.230  88.296  1.00 193.42 ?  519 HIS D CG  1 
ATOM   7938  N ND1 . HIS C 2 187 ? -54.043 55.989  88.903  1.00 194.46 ?  519 HIS D ND1 1 
ATOM   7939  C CD2 . HIS C 2 187 ? -54.350 58.130  89.233  1.00 187.82 ?  519 HIS D CD2 1 
ATOM   7940  C CE1 . HIS C 2 187 ? -54.434 56.132  90.152  1.00 184.10 ?  519 HIS D CE1 1 
ATOM   7941  N NE2 . HIS C 2 187 ? -54.629 57.437  90.380  1.00 183.77 ?  519 HIS D NE2 1 
ATOM   7942  N N   . ALA C 2 188 ? -51.367 56.593  84.455  1.00 263.12 ?  520 ALA D N   1 
ATOM   7943  C CA  . ALA C 2 188 ? -50.962 56.808  83.042  1.00 258.23 ?  520 ALA D CA  1 
ATOM   7944  C C   . ALA C 2 188 ? -51.367 55.610  82.168  1.00 263.55 ?  520 ALA D C   1 
ATOM   7945  O O   . ALA C 2 188 ? -51.365 54.477  82.686  1.00 266.27 ?  520 ALA D O   1 
ATOM   7946  C CB  . ALA C 2 188 ? -49.483 57.078  82.985  1.00 247.96 ?  520 ALA D CB  1 
ATOM   7947  N N   . PRO C 2 189 ? -51.707 55.804  80.871  1.00 226.05 ?  521 PRO D N   1 
ATOM   7948  C CA  . PRO C 2 189 ? -52.214 54.714  80.012  1.00 209.47 ?  521 PRO D CA  1 
ATOM   7949  C C   . PRO C 2 189 ? -51.324 53.481  79.920  1.00 199.52 ?  521 PRO D C   1 
ATOM   7950  O O   . PRO C 2 189 ? -50.262 53.530  79.293  1.00 196.29 ?  521 PRO D O   1 
ATOM   7951  C CB  . PRO C 2 189 ? -52.322 55.387  78.637  1.00 208.74 ?  521 PRO D CB  1 
ATOM   7952  C CG  . PRO C 2 189 ? -52.571 56.812  78.937  1.00 211.26 ?  521 PRO D CG  1 
ATOM   7953  C CD  . PRO C 2 189 ? -51.831 57.120  80.214  1.00 221.54 ?  521 PRO D CD  1 
ATOM   7954  N N   . ALA C 2 190 ? -51.758 52.361  80.494  1.00 180.50 ?  522 ALA D N   1 
ATOM   7955  C CA  . ALA C 2 190 ? -50.939 51.154  80.507  1.00 170.68 ?  522 ALA D CA  1 
ATOM   7956  C C   . ALA C 2 190 ? -50.900 50.526  79.116  1.00 162.17 ?  522 ALA D C   1 
ATOM   7957  O O   . ALA C 2 190 ? -51.958 50.240  78.543  1.00 151.27 ?  522 ALA D O   1 
ATOM   7958  C CB  . ALA C 2 190 ? -51.482 50.164  81.534  1.00 160.03 ?  522 ALA D CB  1 
ATOM   7959  N N   . THR C 2 191 ? -49.672 50.314  78.568  1.00 161.43 ?  523 THR D N   1 
ATOM   7960  C CA  . THR C 2 191 ? -49.539 49.764  77.218  1.00 157.48 ?  523 THR D CA  1 
ATOM   7961  C C   . THR C 2 191 ? -48.323 48.863  77.065  1.00 153.65 ?  523 THR D C   1 
ATOM   7962  O O   . THR C 2 191 ? -47.703 48.854  75.997  1.00 146.54 ?  523 THR D O   1 
ATOM   7963  C CB  . THR C 2 191 ? -49.410 50.864  76.149  1.00 153.39 ?  523 THR D CB  1 
ATOM   7964  O OG1 . THR C 2 191 ? -48.311 51.728  76.489  1.00 150.71 ?  523 THR D OG1 1 
ATOM   7965  C CG2 . THR C 2 191 ? -50.685 51.687  76.072  1.00 160.38 ?  523 THR D CG2 1 
ATOM   7966  N N   . VAL C 2 192 ? -47.951 48.120  78.106  1.00 157.95 ?  524 VAL D N   1 
ATOM   7967  C CA  . VAL C 2 192 ? -46.859 47.157  78.049  1.00 157.81 ?  524 VAL D CA  1 
ATOM   7968  C C   . VAL C 2 192 ? -47.374 45.867  78.670  1.00 165.97 ?  524 VAL D C   1 
ATOM   7969  O O   . VAL C 2 192 ? -47.387 45.734  79.899  1.00 164.96 ?  524 VAL D O   1 
ATOM   7970  C CB  . VAL C 2 192 ? -45.612 47.641  78.784  1.00 153.75 ?  524 VAL D CB  1 
ATOM   7971  C CG1 . VAL C 2 192 ? -44.438 46.718  78.460  1.00 151.45 ?  524 VAL D CG1 1 
ATOM   7972  C CG2 . VAL C 2 192 ? -45.297 49.080  78.428  1.00 154.65 ?  524 VAL D CG2 1 
ATOM   7973  N N   . CYS C 2 193 ? -47.759 44.903  77.834  1.00 182.19 ?  525 CYS D N   1 
ATOM   7974  C CA  . CYS C 2 193 ? -48.495 43.718  78.265  1.00 179.01 ?  525 CYS D CA  1 
ATOM   7975  C C   . CYS C 2 193 ? -47.760 42.448  77.847  1.00 170.09 ?  525 CYS D C   1 
ATOM   7976  O O   . CYS C 2 193 ? -46.685 42.487  77.253  1.00 172.85 ?  525 CYS D O   1 
ATOM   7977  C CB  . CYS C 2 193 ? -49.905 43.720  77.676  1.00 180.32 ?  525 CYS D CB  1 
ATOM   7978  S SG  . CYS C 2 193 ? -50.914 45.104  78.222  1.00 198.25 ?  525 CYS D SG  1 
ATOM   7979  N N   . GLY C 2 194 ? -48.361 41.307  78.153  1.00 144.15 ?  526 GLY D N   1 
ATOM   7980  C CA  . GLY C 2 194 ? -47.751 40.047  77.787  1.00 134.78 ?  526 GLY D CA  1 
ATOM   7981  C C   . GLY C 2 194 ? -48.651 38.839  77.908  1.00 126.93 ?  526 GLY D C   1 
ATOM   7982  O O   . GLY C 2 194 ? -48.572 37.919  77.091  1.00 117.87 ?  526 GLY D O   1 
ATOM   7983  N N   . PRO D 1 2   ? -50.312 79.679  15.997  1.00 87.01  ?  18  PRO A N   1 
ATOM   7984  C CA  . PRO D 1 2   ? -49.105 78.862  15.810  1.00 97.05  ?  18  PRO A CA  1 
ATOM   7985  C C   . PRO D 1 2   ? -48.293 78.672  17.092  1.00 97.58  ?  18  PRO A C   1 
ATOM   7986  O O   . PRO D 1 2   ? -48.914 78.660  18.145  1.00 104.22 ?  18  PRO A O   1 
ATOM   7987  C CB  . PRO D 1 2   ? -48.316 79.650  14.743  1.00 89.66  ?  18  PRO A CB  1 
ATOM   7988  C CG  . PRO D 1 2   ? -48.623 81.080  15.072  1.00 76.30  ?  18  PRO A CG  1 
ATOM   7989  C CD  . PRO D 1 2   ? -50.043 81.099  15.683  1.00 82.35  ?  18  PRO A CD  1 
ATOM   7990  N N   . SER D 1 3   ? -46.969 78.502  17.039  1.00 111.73 ?  19  SER A N   1 
ATOM   7991  C CA  . SER D 1 3   ? -46.202 78.096  18.225  1.00 114.10 ?  19  SER A CA  1 
ATOM   7992  C C   . SER D 1 3   ? -45.107 79.100  18.560  1.00 118.28 ?  19  SER A C   1 
ATOM   7993  O O   . SER D 1 3   ? -44.246 79.373  17.724  1.00 121.19 ?  19  SER A O   1 
ATOM   7994  C CB  . SER D 1 3   ? -45.593 76.706  18.032  1.00 115.93 ?  19  SER A CB  1 
ATOM   7995  O OG  . SER D 1 3   ? -44.776 76.719  16.872  1.00 126.84 ?  19  SER A OG  1 
ATOM   7996  N N   . THR D 1 4   ? -45.120 79.619  19.791  1.00 98.84  ?  20  THR A N   1 
ATOM   7997  C CA  . THR D 1 4   ? -44.166 80.653  20.173  1.00 94.18  ?  20  THR A CA  1 
ATOM   7998  C C   . THR D 1 4   ? -42.797 80.040  20.492  1.00 96.35  ?  20  THR A C   1 
ATOM   7999  O O   . THR D 1 4   ? -42.674 78.840  20.764  1.00 96.60  ?  20  THR A O   1 
ATOM   8000  C CB  . THR D 1 4   ? -44.693 81.475  21.364  1.00 85.29  ?  20  THR A CB  1 
ATOM   8001  O OG1 . THR D 1 4   ? -44.350 80.857  22.600  1.00 86.06  ?  20  THR A OG1 1 
ATOM   8002  C CG2 . THR D 1 4   ? -46.163 81.585  21.317  1.00 88.07  ?  20  THR A CG2 1 
ATOM   8003  N N   . ILE D 1 5   ? -41.750 80.870  20.412  1.00 89.99  ?  21  ILE A N   1 
ATOM   8004  C CA  . ILE D 1 5   ? -40.420 80.384  20.780  1.00 85.07  ?  21  ILE A CA  1 
ATOM   8005  C C   . ILE D 1 5   ? -40.417 79.908  22.224  1.00 80.68  ?  21  ILE A C   1 
ATOM   8006  O O   . ILE D 1 5   ? -39.895 78.829  22.527  1.00 83.35  ?  21  ILE A O   1 
ATOM   8007  C CB  . ILE D 1 5   ? -39.336 81.449  20.527  1.00 89.79  ?  21  ILE A CB  1 
ATOM   8008  C CG1 . ILE D 1 5   ? -39.054 81.593  19.027  1.00 96.67  ?  21  ILE A CG1 1 
ATOM   8009  C CG2 . ILE D 1 5   ? -38.065 81.063  21.229  1.00 87.81  ?  21  ILE A CG2 1 
ATOM   8010  C CD1 . ILE D 1 5   ? -38.100 80.541  18.497  1.00 91.19  ?  21  ILE A CD1 1 
ATOM   8011  N N   . GLU D 1 6   ? -41.027 80.687  23.133  1.00 79.15  ?  22  GLU A N   1 
ATOM   8012  C CA  . GLU D 1 6   ? -41.075 80.307  24.552  1.00 81.63  ?  22  GLU A CA  1 
ATOM   8013  C C   . GLU D 1 6   ? -41.817 78.992  24.776  1.00 77.05  ?  22  GLU A C   1 
ATOM   8014  O O   . GLU D 1 6   ? -41.466 78.221  25.680  1.00 76.93  ?  22  GLU A O   1 
ATOM   8015  C CB  . GLU D 1 6   ? -41.715 81.423  25.401  1.00 85.21  ?  22  GLU A CB  1 
ATOM   8016  C CG  . GLU D 1 6   ? -41.922 81.056  26.900  1.00 84.12  ?  22  GLU A CG  1 
ATOM   8017  C CD  . GLU D 1 6   ? -42.357 82.228  27.818  1.00 88.58  ?  22  GLU A CD  1 
ATOM   8018  O OE1 . GLU D 1 6   ? -41.705 83.292  27.790  1.00 91.81  ?  22  GLU A OE1 1 
ATOM   8019  O OE2 . GLU D 1 6   ? -43.349 82.083  28.585  1.00 86.20  -1 22  GLU A OE2 1 
ATOM   8020  N N   . GLU D 1 7   ? -42.820 78.690  23.958  1.00 75.23  ?  23  GLU A N   1 
ATOM   8021  C CA  . GLU D 1 7   ? -43.522 77.436  24.162  1.00 72.88  ?  23  GLU A CA  1 
ATOM   8022  C C   . GLU D 1 7   ? -42.667 76.264  23.705  1.00 72.05  ?  23  GLU A C   1 
ATOM   8023  O O   . GLU D 1 7   ? -42.560 75.244  24.409  1.00 73.00  ?  23  GLU A O   1 
ATOM   8024  C CB  . GLU D 1 7   ? -44.857 77.459  23.436  1.00 78.70  ?  23  GLU A CB  1 
ATOM   8025  C CG  . GLU D 1 7   ? -45.787 78.571  23.862  1.00 80.11  ?  23  GLU A CG  1 
ATOM   8026  C CD  . GLU D 1 7   ? -47.031 78.633  22.999  1.00 90.32  ?  23  GLU A CD  1 
ATOM   8027  O OE1 . GLU D 1 7   ? -46.913 78.597  21.748  1.00 97.54  ?  23  GLU A OE1 1 
ATOM   8028  O OE2 . GLU D 1 7   ? -48.137 78.701  23.574  1.00 88.16  -1 23  GLU A OE2 1 
ATOM   8029  N N   . GLN D 1 8   ? -42.041 76.393  22.527  1.00 73.51  ?  24  GLN A N   1 
ATOM   8030  C CA  . GLN D 1 8   ? -41.127 75.346  22.084  1.00 78.99  ?  24  GLN A CA  1 
ATOM   8031  C C   . GLN D 1 8   ? -40.070 75.099  23.146  1.00 77.83  ?  24  GLN A C   1 
ATOM   8032  O O   . GLN D 1 8   ? -39.746 73.943  23.458  1.00 75.55  ?  24  GLN A O   1 
ATOM   8033  C CB  . GLN D 1 8   ? -40.458 75.706  20.752  1.00 79.29  ?  24  GLN A CB  1 
ATOM   8034  C CG  . GLN D 1 8   ? -41.401 75.967  19.607  1.00 85.45  ?  24  GLN A CG  1 
ATOM   8035  C CD  . GLN D 1 8   ? -40.733 76.695  18.460  1.00 89.79  ?  24  GLN A CD  1 
ATOM   8036  O OE1 . GLN D 1 8   ? -39.573 76.432  18.138  1.00 86.34  ?  24  GLN A OE1 1 
ATOM   8037  N NE2 . GLN D 1 8   ? -41.467 77.599  17.823  1.00 96.51  ?  24  GLN A NE2 1 
ATOM   8038  N N   . ALA D 1 9   ? -39.562 76.188  23.738  1.00 82.98  ?  25  ALA A N   1 
ATOM   8039  C CA  . ALA D 1 9   ? -38.519 76.121  24.753  1.00 74.15  ?  25  ALA A CA  1 
ATOM   8040  C C   . ALA D 1 9   ? -39.008 75.390  26.002  1.00 68.31  ?  25  ALA A C   1 
ATOM   8041  O O   . ALA D 1 9   ? -38.295 74.546  26.557  1.00 70.31  ?  25  ALA A O   1 
ATOM   8042  C CB  . ALA D 1 9   ? -38.063 77.541  25.083  1.00 74.53  ?  25  ALA A CB  1 
ATOM   8043  N N   . LYS D 1 10  ? -40.229 75.696  26.458  1.00 63.52  ?  26  LYS A N   1 
ATOM   8044  C CA  . LYS D 1 10  ? -40.781 74.995  27.621  1.00 63.34  ?  26  LYS A CA  1 
ATOM   8045  C C   . LYS D 1 10  ? -40.893 73.494  27.384  1.00 67.05  ?  26  LYS A C   1 
ATOM   8046  O O   . LYS D 1 10  ? -40.564 72.680  28.266  1.00 66.93  ?  26  LYS A O   1 
ATOM   8047  C CB  . LYS D 1 10  ? -42.160 75.533  27.995  1.00 62.63  ?  26  LYS A CB  1 
ATOM   8048  C CG  . LYS D 1 10  ? -42.172 76.846  28.712  1.00 68.84  ?  26  LYS A CG  1 
ATOM   8049  C CD  . LYS D 1 10  ? -43.578 77.277  29.051  1.00 76.90  ?  26  LYS A CD  1 
ATOM   8050  C CE  . LYS D 1 10  ? -43.601 78.645  29.692  1.00 84.77  ?  26  LYS A CE  1 
ATOM   8051  N NZ  . LYS D 1 10  ? -44.991 79.156  29.818  1.00 83.52  ?  26  LYS A NZ  1 
ATOM   8052  N N   . THR D 1 11  ? -41.378 73.101  26.209  1.00 66.50  ?  27  THR A N   1 
ATOM   8053  C CA  . THR D 1 11  ? -41.449 71.674  25.933  1.00 64.34  ?  27  THR A CA  1 
ATOM   8054  C C   . THR D 1 11  ? -40.067 71.053  25.819  1.00 65.29  ?  27  THR A C   1 
ATOM   8055  O O   . THR D 1 11  ? -39.843 69.934  26.306  1.00 64.24  ?  27  THR A O   1 
ATOM   8056  C CB  . THR D 1 11  ? -42.268 71.434  24.686  1.00 69.62  ?  27  THR A CB  1 
ATOM   8057  O OG1 . THR D 1 11  ? -43.490 72.166  24.815  1.00 72.51  ?  27  THR A OG1 1 
ATOM   8058  C CG2 . THR D 1 11  ? -42.562 69.975  24.528  1.00 65.89  ?  27  THR A CG2 1 
ATOM   8059  N N   . PHE D 1 12  ? -39.141 71.740  25.156  1.00 67.80  ?  28  PHE A N   1 
ATOM   8060  C CA  . PHE D 1 12  ? -37.767 71.254  25.104  1.00 65.21  ?  28  PHE A CA  1 
ATOM   8061  C C   . PHE D 1 12  ? -37.262 70.928  26.484  1.00 64.90  ?  28  PHE A C   1 
ATOM   8062  O O   . PHE D 1 12  ? -36.690 69.854  26.720  1.00 63.35  ?  28  PHE A O   1 
ATOM   8063  C CB  . PHE D 1 12  ? -36.852 72.281  24.461  1.00 66.76  ?  28  PHE A CB  1 
ATOM   8064  C CG  . PHE D 1 12  ? -35.427 71.961  24.645  1.00 66.14  ?  28  PHE A CG  1 
ATOM   8065  C CD1 . PHE D 1 12  ? -34.890 70.842  24.026  1.00 69.14  ?  28  PHE A CD1 1 
ATOM   8066  C CD2 . PHE D 1 12  ? -34.609 72.783  25.386  1.00 66.75  ?  28  PHE A CD2 1 
ATOM   8067  C CE1 . PHE D 1 12  ? -33.572 70.533  24.167  1.00 70.69  ?  28  PHE A CE1 1 
ATOM   8068  C CE2 . PHE D 1 12  ? -33.278 72.486  25.530  1.00 68.36  ?  28  PHE A CE2 1 
ATOM   8069  C CZ  . PHE D 1 12  ? -32.755 71.358  24.916  1.00 72.63  ?  28  PHE A CZ  1 
ATOM   8070  N N   . LEU D 1 13  ? -37.463 71.869  27.410  1.00 66.12  ?  29  LEU A N   1 
ATOM   8071  C CA  . LEU D 1 13  ? -37.015 71.666  28.775  1.00 63.46  ?  29  LEU A CA  1 
ATOM   8072  C C   . LEU D 1 13  ? -37.746 70.520  29.427  1.00 63.40  ?  29  LEU A C   1 
ATOM   8073  O O   . LEU D 1 13  ? -37.184 69.835  30.286  1.00 62.74  ?  29  LEU A O   1 
ATOM   8074  C CB  . LEU D 1 13  ? -37.215 72.924  29.598  1.00 64.78  ?  29  LEU A CB  1 
ATOM   8075  C CG  . LEU D 1 13  ? -36.308 74.020  29.065  1.00 63.46  ?  29  LEU A CG  1 
ATOM   8076  C CD1 . LEU D 1 13  ? -36.699 75.276  29.747  1.00 67.91  ?  29  LEU A CD1 1 
ATOM   8077  C CD2 . LEU D 1 13  ? -34.845 73.730  29.231  1.00 62.39  ?  29  LEU A CD2 1 
ATOM   8078  N N   . ASP D 1 14  ? -38.993 70.297  29.027  1.00 65.82  ?  30  ASP A N   1 
ATOM   8079  C CA  . ASP D 1 14  ? -39.756 69.220  29.648  1.00 67.57  ?  30  ASP A CA  1 
ATOM   8080  C C   . ASP D 1 14  ? -39.235 67.833  29.247  1.00 65.92  ?  30  ASP A C   1 
ATOM   8081  O O   . ASP D 1 14  ? -39.071 66.944  30.097  1.00 58.89  ?  30  ASP A O   1 
ATOM   8082  C CB  . ASP D 1 14  ? -41.221 69.363  29.290  1.00 66.33  ?  30  ASP A CB  1 
ATOM   8083  C CG  . ASP D 1 14  ? -42.096 69.028  30.447  1.00 71.33  ?  30  ASP A CG  1 
ATOM   8084  O OD1 . ASP D 1 14  ? -41.590 68.354  31.396  1.00 67.39  ?  30  ASP A OD1 1 
ATOM   8085  O OD2 . ASP D 1 14  ? -43.292 69.374  30.377  1.00 76.46  -1 30  ASP A OD2 1 
ATOM   8086  N N   . LYS D 1 15  ? -38.985 67.634  27.950  1.00 65.92  ?  31  LYS A N   1 
ATOM   8087  C CA  . LYS D 1 15  ? -38.288 66.429  27.501  1.00 64.29  ?  31  LYS A CA  1 
ATOM   8088  C C   . LYS D 1 15  ? -36.908 66.324  28.153  1.00 66.58  ?  31  LYS A C   1 
ATOM   8089  O O   . LYS D 1 15  ? -36.499 65.230  28.590  1.00 68.68  ?  31  LYS A O   1 
ATOM   8090  C CB  . LYS D 1 15  ? -38.204 66.419  25.965  1.00 61.52  ?  31  LYS A CB  1 
ATOM   8091  C CG  . LYS D 1 15  ? -37.176 65.481  25.369  1.00 64.66  ?  31  LYS A CG  1 
ATOM   8092  C CD  . LYS D 1 15  ? -37.624 64.065  25.490  1.00 71.82  ?  31  LYS A CD  1 
ATOM   8093  C CE  . LYS D 1 15  ? -36.609 63.159  24.869  1.00 86.06  ?  31  LYS A CE  1 
ATOM   8094  N NZ  . LYS D 1 15  ? -36.956 61.750  25.189  1.00 89.22  ?  31  LYS A NZ  1 
ATOM   8095  N N   . PHE D 1 16  ? -36.182 67.455  28.235  1.00 66.92  ?  32  PHE A N   1 
ATOM   8096  C CA  . PHE D 1 16  ? -34.845 67.445  28.820  1.00 63.91  ?  32  PHE A CA  1 
ATOM   8097  C C   . PHE D 1 16  ? -34.881 66.962  30.255  1.00 64.13  ?  32  PHE A C   1 
ATOM   8098  O O   . PHE D 1 16  ? -34.103 66.088  30.635  1.00 65.03  ?  32  PHE A O   1 
ATOM   8099  C CB  . PHE D 1 16  ? -34.184 68.824  28.760  1.00 62.30  ?  32  PHE A CB  1 
ATOM   8100  C CG  . PHE D 1 16  ? -32.944 68.923  29.619  1.00 59.56  ?  32  PHE A CG  1 
ATOM   8101  C CD1 . PHE D 1 16  ? -31.713 68.497  29.145  1.00 63.23  ?  32  PHE A CD1 1 
ATOM   8102  C CD2 . PHE D 1 16  ? -32.996 69.445  30.889  1.00 58.96  ?  32  PHE A CD2 1 
ATOM   8103  C CE1 . PHE D 1 16  ? -30.548 68.572  29.941  1.00 60.64  ?  32  PHE A CE1 1 
ATOM   8104  C CE2 . PHE D 1 16  ? -31.832 69.518  31.687  1.00 58.91  ?  32  PHE A CE2 1 
ATOM   8105  C CZ  . PHE D 1 16  ? -30.616 69.092  31.209  1.00 58.13  ?  32  PHE A CZ  1 
ATOM   8106  N N   . ASN D 1 17  ? -35.742 67.554  31.078  1.00 59.23  ?  33  ASN A N   1 
ATOM   8107  C CA  . ASN D 1 17  ? -35.805 67.163  32.481  1.00 60.55  ?  33  ASN A CA  1 
ATOM   8108  C C   . ASN D 1 17  ? -35.866 65.643  32.647  1.00 63.02  ?  33  ASN A C   1 
ATOM   8109  O O   . ASN D 1 17  ? -35.116 65.069  33.436  1.00 66.67  ?  33  ASN A O   1 
ATOM   8110  C CB  . ASN D 1 17  ? -36.990 67.852  33.158  1.00 60.68  ?  33  ASN A CB  1 
ATOM   8111  C CG  . ASN D 1 17  ? -36.792 69.359  33.332  1.00 60.98  ?  33  ASN A CG  1 
ATOM   8112  O OD1 . ASN D 1 17  ? -35.667 69.867  33.443  1.00 59.16  ?  33  ASN A OD1 1 
ATOM   8113  N ND2 . ASN D 1 17  ? -37.901 70.091  33.281  1.00 65.59  ?  33  ASN A ND2 1 
ATOM   8114  N N   . HIS D 1 18  ? -36.710 64.960  31.883  1.00 65.98  ?  34  HIS A N   1 
ATOM   8115  C CA  . HIS D 1 18  ? -36.907 63.538  32.162  1.00 65.60  ?  34  HIS A CA  1 
ATOM   8116  C C   . HIS D 1 18  ? -35.755 62.695  31.638  1.00 69.09  ?  34  HIS A C   1 
ATOM   8117  O O   . HIS D 1 18  ? -35.223 61.824  32.355  1.00 70.64  ?  34  HIS A O   1 
ATOM   8118  C CB  . HIS D 1 18  ? -38.234 63.112  31.578  1.00 66.65  ?  34  HIS A CB  1 
ATOM   8119  C CG  . HIS D 1 18  ? -39.371 63.857  32.184  1.00 70.26  ?  34  HIS A CG  1 
ATOM   8120  N ND1 . HIS D 1 18  ? -39.653 65.169  31.861  1.00 70.60  ?  34  HIS A ND1 1 
ATOM   8121  C CD2 . HIS D 1 18  ? -40.291 63.492  33.104  1.00 68.52  ?  34  HIS A CD2 1 
ATOM   8122  C CE1 . HIS D 1 18  ? -40.707 65.577  32.547  1.00 68.62  ?  34  HIS A CE1 1 
ATOM   8123  N NE2 . HIS D 1 18  ? -41.122 64.574  33.301  1.00 68.61  ?  34  HIS A NE2 1 
ATOM   8124  N N   . GLU D 1 19  ? -35.342 62.963  30.396  1.00 81.63  ?  35  GLU A N   1 
ATOM   8125  C CA  . GLU D 1 19  ? -34.120 62.343  29.887  1.00 81.43  ?  35  GLU A CA  1 
ATOM   8126  C C   . GLU D 1 19  ? -32.979 62.505  30.877  1.00 75.60  ?  35  GLU A C   1 
ATOM   8127  O O   . GLU D 1 19  ? -32.232 61.562  31.166  1.00 75.18  ?  35  GLU A O   1 
ATOM   8128  C CB  . GLU D 1 19  ? -33.734 62.964  28.535  1.00 81.54  ?  35  GLU A CB  1 
ATOM   8129  C CG  . GLU D 1 19  ? -34.220 62.237  27.292  1.00 87.58  ?  35  GLU A CG  1 
ATOM   8130  C CD  . GLU D 1 19  ? -34.043 60.718  27.338  1.00 102.54 ?  35  GLU A CD  1 
ATOM   8131  O OE1 . GLU D 1 19  ? -33.232 60.183  28.158  1.00 96.59  ?  35  GLU A OE1 1 
ATOM   8132  O OE2 . GLU D 1 19  ? -34.756 60.064  26.539  1.00 109.44 -1 35  GLU A OE2 1 
ATOM   8133  N N   . ALA D 1 20  ? -32.856 63.692  31.439  1.00 67.36  ?  36  ALA A N   1 
ATOM   8134  C CA  . ALA D 1 20  ? -31.690 63.978  32.236  1.00 67.01  ?  36  ALA A CA  1 
ATOM   8135  C C   . ALA D 1 20  ? -31.778 63.338  33.610  1.00 67.40  ?  36  ALA A C   1 
ATOM   8136  O O   . ALA D 1 20  ? -30.765 62.853  34.100  1.00 68.12  ?  36  ALA A O   1 
ATOM   8137  C CB  . ALA D 1 20  ? -31.496 65.484  32.359  1.00 67.79  ?  36  ALA A CB  1 
ATOM   8138  N N   . GLU D 1 21  ? -32.944 63.354  34.277  1.00 61.25  ?  37  GLU A N   1 
ATOM   8139  C CA  . GLU D 1 21  ? -33.039 62.659  35.564  1.00 56.96  ?  37  GLU A CA  1 
ATOM   8140  C C   . GLU D 1 21  ? -32.684 61.197  35.419  1.00 57.99  ?  37  GLU A C   1 
ATOM   8141  O O   . GLU D 1 21  ? -32.006 60.636  36.284  1.00 58.68  ?  37  GLU A O   1 
ATOM   8142  C CB  . GLU D 1 21  ? -34.417 62.774  36.192  1.00 59.07  ?  37  GLU A CB  1 
ATOM   8143  C CG  . GLU D 1 21  ? -34.881 64.164  36.508  1.00 67.15  ?  37  GLU A CG  1 
ATOM   8144  C CD  . GLU D 1 21  ? -35.756 64.205  37.774  1.00 80.75  ?  37  GLU A CD  1 
ATOM   8145  O OE1 . GLU D 1 21  ? -35.460 63.488  38.781  1.00 74.48  ?  37  GLU A OE1 1 
ATOM   8146  O OE2 . GLU D 1 21  ? -36.756 64.974  37.741  1.00 81.22  -1 37  GLU A OE2 1 
ATOM   8147  N N   . ASP D 1 22  ? -33.076 60.557  34.313  1.00 61.93  ?  38  ASP A N   1 
ATOM   8148  C CA  . ASP D 1 22  ? -32.697 59.147  34.252  1.00 61.60  ?  38  ASP A CA  1 
ATOM   8149  C C   . ASP D 1 22  ? -31.204 58.991  33.948  1.00 59.68  ?  38  ASP A C   1 
ATOM   8150  O O   . ASP D 1 22  ? -30.520 58.179  34.589  1.00 58.51  ?  38  ASP A O   1 
ATOM   8151  C CB  . ASP D 1 22  ? -33.548 58.369  33.255  1.00 62.64  ?  38  ASP A CB  1 
ATOM   8152  C CG  . ASP D 1 22  ? -33.443 56.870  33.481  1.00 65.89  ?  38  ASP A CG  1 
ATOM   8153  O OD1 . ASP D 1 22  ? -33.875 56.417  34.588  1.00 62.75  ?  38  ASP A OD1 1 
ATOM   8154  O OD2 . ASP D 1 22  ? -32.883 56.176  32.590  1.00 69.70  -1 38  ASP A OD2 1 
ATOM   8155  N N   . LEU D 1 23  ? -30.660 59.801  33.028  1.00 61.72  ?  39  LEU A N   1 
ATOM   8156  C CA  . LEU D 1 23  ? -29.222 59.731  32.774  1.00 60.11  ?  39  LEU A CA  1 
ATOM   8157  C C   . LEU D 1 23  ? -28.408 60.077  34.008  1.00 63.92  ?  39  LEU A C   1 
ATOM   8158  O O   . LEU D 1 23  ? -27.320 59.527  34.238  1.00 65.21  ?  39  LEU A O   1 
ATOM   8159  C CB  . LEU D 1 23  ? -28.846 60.664  31.649  1.00 56.91  ?  39  LEU A CB  1 
ATOM   8160  C CG  . LEU D 1 23  ? -29.145 59.829  30.444  1.00 62.09  ?  39  LEU A CG  1 
ATOM   8161  C CD1 . LEU D 1 23  ? -28.987 60.665  29.205  1.00 70.54  ?  39  LEU A CD1 1 
ATOM   8162  C CD2 . LEU D 1 23  ? -28.186 58.684  30.493  1.00 64.78  ?  39  LEU A CD2 1 
ATOM   8163  N N   . PHE D 1 24  ? -28.910 60.991  34.816  1.00 59.93  ?  40  PHE A N   1 
ATOM   8164  C CA  . PHE D 1 24  ? -28.104 61.488  35.906  1.00 56.21  ?  40  PHE A CA  1 
ATOM   8165  C C   . PHE D 1 24  ? -28.152 60.512  37.074  1.00 56.94  ?  40  PHE A C   1 
ATOM   8166  O O   . PHE D 1 24  ? -27.138 60.296  37.746  1.00 57.84  ?  40  PHE A O   1 
ATOM   8167  C CB  . PHE D 1 24  ? -28.570 62.891  36.290  1.00 55.64  ?  40  PHE A CB  1 
ATOM   8168  C CG  . PHE D 1 24  ? -27.775 63.487  37.396  1.00 59.75  ?  40  PHE A CG  1 
ATOM   8169  C CD1 . PHE D 1 24  ? -26.548 64.106  37.129  1.00 56.98  ?  40  PHE A CD1 1 
ATOM   8170  C CD2 . PHE D 1 24  ? -28.227 63.419  38.704  1.00 56.41  ?  40  PHE A CD2 1 
ATOM   8171  C CE1 . PHE D 1 24  ? -25.801 64.631  38.142  1.00 48.43  ?  40  PHE A CE1 1 
ATOM   8172  C CE2 . PHE D 1 24  ? -27.480 63.953  39.715  1.00 52.85  ?  40  PHE A CE2 1 
ATOM   8173  C CZ  . PHE D 1 24  ? -26.263 64.553  39.428  1.00 50.69  ?  40  PHE A CZ  1 
ATOM   8174  N N   . TYR D 1 25  ? -29.284 59.862  37.318  1.00 53.49  ?  41  TYR A N   1 
ATOM   8175  C CA  . TYR D 1 25  ? -29.276 58.831  38.387  1.00 50.85  ?  41  TYR A CA  1 
ATOM   8176  C C   . TYR D 1 25  ? -28.254 57.759  38.024  1.00 54.83  ?  41  TYR A C   1 
ATOM   8177  O O   . TYR D 1 25  ? -27.441 57.375  38.876  1.00 57.93  ?  41  TYR A O   1 
ATOM   8178  C CB  . TYR D 1 25  ? -30.632 58.149  38.536  1.00 52.70  ?  41  TYR A CB  1 
ATOM   8179  C CG  . TYR D 1 25  ? -30.843 57.384  39.818  1.00 52.51  ?  41  TYR A CG  1 
ATOM   8180  C CD1 . TYR D 1 25  ? -31.262 58.027  40.967  1.00 55.29  ?  41  TYR A CD1 1 
ATOM   8181  C CD2 . TYR D 1 25  ? -30.649 56.017  39.877  1.00 52.52  ?  41  TYR A CD2 1 
ATOM   8182  C CE1 . TYR D 1 25  ? -31.477 57.333  42.144  1.00 55.10  ?  41  TYR A CE1 1 
ATOM   8183  C CE2 . TYR D 1 25  ? -30.859 55.307  41.046  1.00 53.97  ?  41  TYR A CE2 1 
ATOM   8184  C CZ  . TYR D 1 25  ? -31.273 55.969  42.184  1.00 52.35  ?  41  TYR A CZ  1 
ATOM   8185  O OH  . TYR D 1 25  ? -31.483 55.285  43.343  1.00 51.93  ?  41  TYR A OH  1 
ATOM   8186  N N   . GLN D 1 26  ? -28.321 57.272  36.789  1.00 55.44  ?  42  GLN A N   1 
ATOM   8187  C CA  . GLN D 1 26  ? -27.384 56.210  36.359  1.00 58.22  ?  42  GLN A CA  1 
ATOM   8188  C C   . GLN D 1 26  ? -25.979 56.622  36.774  1.00 57.58  ?  42  GLN A C   1 
ATOM   8189  O O   . GLN D 1 26  ? -25.332 55.874  37.509  1.00 56.16  ?  42  GLN A O   1 
ATOM   8190  C CB  . GLN D 1 26  ? -27.408 56.043  34.844  1.00 68.19  ?  42  GLN A CB  1 
ATOM   8191  C CG  . GLN D 1 26  ? -28.796 55.886  34.256  1.00 64.38  ?  42  GLN A CG  1 
ATOM   8192  C CD  . GLN D 1 26  ? -29.028 54.510  33.691  1.00 63.07  ?  42  GLN A CD  1 
ATOM   8193  O OE1 . GLN D 1 26  ? -28.289 53.570  33.966  1.00 71.46  ?  42  GLN A OE1 1 
ATOM   8194  N NE2 . GLN D 1 26  ? -30.071 54.390  32.887  1.00 69.20  ?  42  GLN A NE2 1 
ATOM   8195  N N   . SER D 1 27  ? -25.531 57.775  36.296  1.00 61.30  ?  43  SER A N   1 
ATOM   8196  C CA  . SER D 1 27  ? -24.149 58.200  36.598  1.00 62.81  ?  43  SER A CA  1 
ATOM   8197  C C   . SER D 1 27  ? -23.967 58.227  38.103  1.00 56.28  ?  43  SER A C   1 
ATOM   8198  O O   . SER D 1 27  ? -23.007 57.611  38.588  1.00 54.68  ?  43  SER A O   1 
ATOM   8199  C CB  . SER D 1 27  ? -23.873 59.547  36.032  1.00 65.80  ?  43  SER A CB  1 
ATOM   8200  O OG  . SER D 1 27  ? -22.575 59.978  36.407  1.00 66.92  ?  43  SER A OG  1 
ATOM   8201  N N   . SER D 1 28  ? -24.848 58.930  38.812  1.00 54.75  ?  44  SER A N   1 
ATOM   8202  C CA  . SER D 1 28  ? -24.582 59.053  40.245  1.00 55.10  ?  44  SER A CA  1 
ATOM   8203  C C   . SER D 1 28  ? -24.521 57.689  40.929  1.00 53.73  ?  44  SER A C   1 
ATOM   8204  O O   . SER D 1 28  ? -23.682 57.480  41.812  1.00 57.82  ?  44  SER A O   1 
ATOM   8205  C CB  . SER D 1 28  ? -25.596 59.981  40.932  1.00 51.81  ?  44  SER A CB  1 
ATOM   8206  O OG  . SER D 1 28  ? -25.736 61.210  40.262  1.00 50.60  ?  44  SER A OG  1 
ATOM   8207  N N   . LEU D 1 29  ? -25.376 56.748  40.549  1.00 51.44  ?  45  LEU A N   1 
ATOM   8208  C CA  . LEU D 1 29  ? -25.233 55.412  41.127  1.00 53.45  ?  45  LEU A CA  1 
ATOM   8209  C C   . LEU D 1 29  ? -23.923 54.745  40.711  1.00 55.08  ?  45  LEU A C   1 
ATOM   8210  O O   . LEU D 1 29  ? -23.277 54.083  41.532  1.00 57.32  ?  45  LEU A O   1 
ATOM   8211  C CB  . LEU D 1 29  ? -26.445 54.550  40.775  1.00 53.15  ?  45  LEU A CB  1 
ATOM   8212  C CG  . LEU D 1 29  ? -26.756 53.318  41.614  1.00 50.22  ?  45  LEU A CG  1 
ATOM   8213  C CD1 . LEU D 1 29  ? -26.535 53.567  43.072  1.00 54.69  ?  45  LEU A CD1 1 
ATOM   8214  C CD2 . LEU D 1 29  ? -28.228 53.051  41.417  1.00 49.91  ?  45  LEU A CD2 1 
ATOM   8215  N N   . ALA D 1 30  ? -23.497 54.907  39.450  1.00 55.72  ?  46  ALA A N   1 
ATOM   8216  C CA  . ALA D 1 30  ? -22.177 54.383  39.075  1.00 56.80  ?  46  ALA A CA  1 
ATOM   8217  C C   . ALA D 1 30  ? -21.067 54.985  39.945  1.00 60.47  ?  46  ALA A C   1 
ATOM   8218  O O   . ALA D 1 30  ? -20.152 54.277  40.409  1.00 58.73  ?  46  ALA A O   1 
ATOM   8219  C CB  . ALA D 1 30  ? -21.910 54.668  37.596  1.00 62.63  ?  46  ALA A CB  1 
ATOM   8220  N N   . SER D 1 31  ? -21.155 56.301  40.171  1.00 61.40  ?  47  SER A N   1 
ATOM   8221  C CA  . SER D 1 31  ? -20.173 57.032  40.948  1.00 56.53  ?  47  SER A CA  1 
ATOM   8222  C C   . SER D 1 31  ? -20.189 56.568  42.386  1.00 56.45  ?  47  SER A C   1 
ATOM   8223  O O   . SER D 1 31  ? -19.140 56.332  42.985  1.00 62.39  ?  47  SER A O   1 
ATOM   8224  C CB  . SER D 1 31  ? -20.471 58.521  40.873  1.00 54.26  ?  47  SER A CB  1 
ATOM   8225  O OG  . SER D 1 31  ? -19.587 59.247  41.694  1.00 57.79  ?  47  SER A OG  1 
ATOM   8226  N N   . TRP D 1 32  ? -21.374 56.453  42.961  1.00 52.33  ?  48  TRP A N   1 
ATOM   8227  C CA  . TRP D 1 32  ? -21.510 55.926  44.308  1.00 53.63  ?  48  TRP A CA  1 
ATOM   8228  C C   . TRP D 1 32  ? -20.942 54.523  44.430  1.00 58.76  ?  48  TRP A C   1 
ATOM   8229  O O   . TRP D 1 32  ? -20.366 54.163  45.462  1.00 66.13  ?  48  TRP A O   1 
ATOM   8230  C CB  . TRP D 1 32  ? -22.963 55.882  44.698  1.00 53.22  ?  48  TRP A CB  1 
ATOM   8231  C CG  . TRP D 1 32  ? -23.191 55.230  45.984  1.00 50.36  ?  48  TRP A CG  1 
ATOM   8232  C CD1 . TRP D 1 32  ? -23.386 53.906  46.184  1.00 51.73  ?  48  TRP A CD1 1 
ATOM   8233  C CD2 . TRP D 1 32  ? -23.412 55.865  47.250  1.00 51.24  ?  48  TRP A CD2 1 
ATOM   8234  N NE1 . TRP D 1 32  ? -23.636 53.656  47.511  1.00 52.56  ?  48  TRP A NE1 1 
ATOM   8235  C CE2 . TRP D 1 32  ? -23.679 54.846  48.183  1.00 50.69  ?  48  TRP A CE2 1 
ATOM   8236  C CE3 . TRP D 1 32  ? -23.382 57.191  47.693  1.00 49.58  ?  48  TRP A CE3 1 
ATOM   8237  C CZ2 . TRP D 1 32  ? -23.918 55.106  49.520  1.00 50.16  ?  48  TRP A CZ2 1 
ATOM   8238  C CZ3 . TRP D 1 32  ? -23.619 57.442  49.025  1.00 47.58  ?  48  TRP A CZ3 1 
ATOM   8239  C CH2 . TRP D 1 32  ? -23.886 56.404  49.922  1.00 48.38  ?  48  TRP A CH2 1 
ATOM   8240  N N   . ASN D 1 33  ? -21.133 53.689  43.420  1.00 55.70  ?  49  ASN A N   1 
ATOM   8241  C CA  . ASN D 1 33  ? -20.610 52.336  43.559  1.00 57.42  ?  49  ASN A CA  1 
ATOM   8242  C C   . ASN D 1 33  ? -19.093 52.311  43.493  1.00 63.12  ?  49  ASN A C   1 
ATOM   8243  O O   . ASN D 1 33  ? -18.476 51.472  44.145  1.00 71.90  ?  49  ASN A O   1 
ATOM   8244  C CB  . ASN D 1 33  ? -21.168 51.403  42.497  1.00 62.18  ?  49  ASN A CB  1 
ATOM   8245  C CG  . ASN D 1 33  ? -22.679 51.268  42.560  1.00 56.13  ?  49  ASN A CG  1 
ATOM   8246  O OD1 . ASN D 1 33  ? -23.287 51.223  43.640  1.00 52.48  ?  49  ASN A OD1 1 
ATOM   8247  N ND2 . ASN D 1 33  ? -23.286 51.109  41.389  1.00 54.05  ?  49  ASN A ND2 1 
ATOM   8248  N N   . TYR D 1 34  ? -18.463 53.195  42.709  1.00 64.68  ?  50  TYR A N   1 
ATOM   8249  C CA  . TYR D 1 34  ? -17.007 53.284  42.812  1.00 65.45  ?  50  TYR A CA  1 
ATOM   8250  C C   . TYR D 1 34  ? -16.597 53.823  44.159  1.00 60.41  ?  50  TYR A C   1 
ATOM   8251  O O   . TYR D 1 34  ? -15.735 53.255  44.821  1.00 64.60  ?  50  TYR A O   1 
ATOM   8252  C CB  . TYR D 1 34  ? -16.389 54.166  41.739  1.00 67.80  ?  50  TYR A CB  1 
ATOM   8253  C CG  . TYR D 1 34  ? -14.921 54.437  42.025  1.00 71.29  ?  50  TYR A CG  1 
ATOM   8254  C CD1 . TYR D 1 34  ? -13.993 53.402  41.968  1.00 77.60  ?  50  TYR A CD1 1 
ATOM   8255  C CD2 . TYR D 1 34  ? -14.439 55.722  42.271  1.00 68.87  ?  50  TYR A CD2 1 
ATOM   8256  C CE1 . TYR D 1 34  ? -12.636 53.613  42.220  1.00 77.41  ?  50  TYR A CE1 1 
ATOM   8257  C CE2 . TYR D 1 34  ? -13.053 55.947  42.504  1.00 74.21  ?  50  TYR A CE2 1 
ATOM   8258  C CZ  . TYR D 1 34  ? -12.163 54.873  42.480  1.00 77.70  ?  50  TYR A CZ  1 
ATOM   8259  O OH  . TYR D 1 34  ? -10.806 55.012  42.710  1.00 75.20  ?  50  TYR A OH  1 
ATOM   8260  N N   . ASN D 1 35  ? -17.188 54.936  44.565  1.00 58.64  ?  51  ASN A N   1 
ATOM   8261  C CA  . ASN D 1 35  ? -16.828 55.607  45.798  1.00 56.16  ?  51  ASN A CA  1 
ATOM   8262  C C   . ASN D 1 35  ? -17.194 54.819  47.046  1.00 61.27  ?  51  ASN A C   1 
ATOM   8263  O O   . ASN D 1 35  ? -16.850 55.269  48.133  1.00 65.88  ?  51  ASN A O   1 
ATOM   8264  C CB  . ASN D 1 35  ? -17.498 56.967  45.826  1.00 52.66  ?  51  ASN A CB  1 
ATOM   8265  C CG  . ASN D 1 35  ? -16.641 58.040  45.173  1.00 57.22  ?  51  ASN A CG  1 
ATOM   8266  O OD1 . ASN D 1 35  ? -15.791 58.656  45.814  1.00 56.49  ?  51  ASN A OD1 1 
ATOM   8267  N ND2 . ASN D 1 35  ? -16.772 58.174  43.858  1.00 55.44  ?  51  ASN A ND2 1 
ATOM   8268  N N   . THR D 1 36  ? -17.877 53.682  46.939  1.00 66.56  ?  52  THR A N   1 
ATOM   8269  C CA  . THR D 1 36  ? -18.098 52.815  48.096  1.00 66.61  ?  52  THR A CA  1 
ATOM   8270  C C   . THR D 1 36  ? -17.551 51.420  47.904  1.00 70.58  ?  52  THR A C   1 
ATOM   8271  O O   . THR D 1 36  ? -17.732 50.575  48.785  1.00 72.15  ?  52  THR A O   1 
ATOM   8272  C CB  . THR D 1 36  ? -19.574 52.718  48.447  1.00 65.55  ?  52  THR A CB  1 
ATOM   8273  O OG1 . THR D 1 36  ? -20.319 52.224  47.327  1.00 66.69  ?  52  THR A OG1 1 
ATOM   8274  C CG2 . THR D 1 36  ? -20.086 54.022  48.900  1.00 62.96  ?  52  THR A CG2 1 
ATOM   8275  N N   . ASN D 1 37  ? -17.063 51.099  46.721  1.00 74.95  ?  53  ASN A N   1 
ATOM   8276  C CA  . ASN D 1 37  ? -16.657 49.696  46.499  1.00 79.80  ?  53  ASN A CA  1 
ATOM   8277  C C   . ASN D 1 37  ? -15.611 49.733  45.408  1.00 86.24  ?  53  ASN A C   1 
ATOM   8278  O O   . ASN D 1 37  ? -15.868 49.252  44.297  1.00 94.81  ?  53  ASN A O   1 
ATOM   8279  C CB  . ASN D 1 37  ? -17.850 48.853  46.080  1.00 77.87  ?  53  ASN A CB  1 
ATOM   8280  C CG  . ASN D 1 37  ? -17.539 47.379  45.975  1.00 86.46  ?  53  ASN A CG  1 
ATOM   8281  O OD1 . ASN D 1 37  ? -16.971 46.786  46.891  1.00 92.47  ?  53  ASN A OD1 1 
ATOM   8282  N ND2 . ASN D 1 37  ? -17.921 46.782  44.863  1.00 101.77 ?  53  ASN A ND2 1 
ATOM   8283  N N   . ILE D 1 38  ? -14.462 50.283  45.748  1.00 78.30  ?  54  ILE A N   1 
ATOM   8284  C CA  . ILE D 1 38  ? -13.450 50.475  44.676  1.00 79.71  ?  54  ILE A CA  1 
ATOM   8285  C C   . ILE D 1 38  ? -13.121 49.134  44.014  1.00 86.36  ?  54  ILE A C   1 
ATOM   8286  O O   . ILE D 1 38  ? -12.642 48.230  44.717  1.00 91.63  ?  54  ILE A O   1 
ATOM   8287  C CB  . ILE D 1 38  ? -12.234 51.236  45.234  1.00 75.08  ?  54  ILE A CB  1 
ATOM   8288  C CG1 . ILE D 1 38  ? -12.690 52.572  45.830  1.00 78.92  ?  54  ILE A CG1 1 
ATOM   8289  C CG2 . ILE D 1 38  ? -11.128 51.385  44.189  1.00 68.78  ?  54  ILE A CG2 1 
ATOM   8290  C CD1 . ILE D 1 38  ? -11.587 53.360  46.519  1.00 72.37  ?  54  ILE A CD1 1 
ATOM   8291  N N   . THR D 1 39  ? -13.383 49.052  42.718  1.00 88.20  ?  55  THR A N   1 
ATOM   8292  C CA  . THR D 1 39  ? -13.028 47.863  41.924  1.00 89.55  ?  55  THR A CA  1 
ATOM   8293  C C   . THR D 1 39  ? -12.801 48.434  40.531  1.00 97.36  ?  55  THR A C   1 
ATOM   8294  O O   . THR D 1 39  ? -13.659 49.211  40.101  1.00 97.25  ?  55  THR A O   1 
ATOM   8295  C CB  . THR D 1 39  ? -14.159 46.833  41.920  1.00 89.98  ?  55  THR A CB  1 
ATOM   8296  O OG1 . THR D 1 39  ? -15.294 47.443  41.306  1.00 92.43  ?  55  THR A OG1 1 
ATOM   8297  C CG2 . THR D 1 39  ? -14.533 46.335  43.298  1.00 85.81  ?  55  THR A CG2 1 
ATOM   8298  N N   . GLU D 1 40  ? -11.674 48.156  39.882  1.00 118.90 ?  56  GLU A N   1 
ATOM   8299  C CA  . GLU D 1 40  ? -11.460 48.800  38.560  1.00 124.48 ?  56  GLU A CA  1 
ATOM   8300  C C   . GLU D 1 40  ? -12.772 48.705  37.788  1.00 117.07 ?  56  GLU A C   1 
ATOM   8301  O O   . GLU D 1 40  ? -13.121 49.665  37.082  1.00 115.49 ?  56  GLU A O   1 
ATOM   8302  C CB  . GLU D 1 40  ? -10.338 48.117  37.782  1.00 126.38 ?  56  GLU A CB  1 
ATOM   8303  C CG  . GLU D 1 40  ? -10.002 48.819  36.484  1.00 129.72 ?  56  GLU A CG  1 
ATOM   8304  C CD  . GLU D 1 40  ? -9.348  50.174  36.677  1.00 133.62 ?  56  GLU A CD  1 
ATOM   8305  O OE1 . GLU D 1 40  ? -8.682  50.364  37.714  1.00 125.94 ?  56  GLU A OE1 1 
ATOM   8306  O OE2 . GLU D 1 40  ? -9.503  51.033  35.790  1.00 137.08 -1 56  GLU A OE2 1 
ATOM   8307  N N   . GLU D 1 41  ? -13.475 47.585  37.944  1.00 98.16  ?  57  GLU A N   1 
ATOM   8308  C CA  . GLU D 1 41  ? -14.787 47.427  37.283  1.00 95.90  ?  57  GLU A CA  1 
ATOM   8309  C C   . GLU D 1 41  ? -15.627 48.667  37.551  1.00 92.55  ?  57  GLU A C   1 
ATOM   8310  O O   . GLU D 1 41  ? -16.117 49.268  36.583  1.00 89.32  ?  57  GLU A O   1 
ATOM   8311  C CB  . GLU D 1 41  ? -15.507 46.202  37.840  1.00 89.15  ?  57  GLU A CB  1 
ATOM   8312  C CG  . GLU D 1 41  ? -17.011 46.246  37.664  1.00 87.46  ?  57  GLU A CG  1 
ATOM   8313  C CD  . GLU D 1 41  ? -17.674 44.884  37.749  1.00 97.24  ?  57  GLU A CD  1 
ATOM   8314  O OE1 . GLU D 1 41  ? -17.141 44.015  38.464  1.00 107.34 ?  57  GLU A OE1 1 
ATOM   8315  O OE2 . GLU D 1 41  ? -18.715 44.692  37.095  1.00 91.52  -1 57  GLU A OE2 1 
ATOM   8316  N N   . ASN D 1 42  ? -15.721 49.079  38.811  1.00 88.34  ?  58  ASN A N   1 
ATOM   8317  C CA  . ASN D 1 42  ? -16.646 50.162  39.112  1.00 80.93  ?  58  ASN A CA  1 
ATOM   8318  C C   . ASN D 1 42  ? -16.125 51.487  38.574  1.00 84.48  ?  58  ASN A C   1 
ATOM   8319  O O   . ASN D 1 42  ? -16.922 52.366  38.230  1.00 83.95  ?  58  ASN A O   1 
ATOM   8320  C CB  . ASN D 1 42  ? -16.850 50.277  40.608  1.00 78.09  ?  58  ASN A CB  1 
ATOM   8321  C CG  . ASN D 1 42  ? -17.744 49.193  41.135  1.00 78.64  ?  58  ASN A CG  1 
ATOM   8322  O OD1 . ASN D 1 42  ? -18.639 48.717  40.455  1.00 86.59  ?  58  ASN A OD1 1 
ATOM   8323  N ND2 . ASN D 1 42  ? -17.506 48.800  42.365  1.00 82.42  ?  58  ASN A ND2 1 
ATOM   8324  N N   . VAL D 1 43  ? -14.793 51.629  38.474  1.00 96.54  ?  59  VAL A N   1 
ATOM   8325  C CA  . VAL D 1 43  ? -14.192 52.751  37.761  1.00 95.20  ?  59  VAL A CA  1 
ATOM   8326  C C   . VAL D 1 43  ? -14.671 52.761  36.325  1.00 94.72  ?  59  VAL A C   1 
ATOM   8327  O O   . VAL D 1 43  ? -14.995 53.821  35.774  1.00 93.64  ?  59  VAL A O   1 
ATOM   8328  C CB  . VAL D 1 43  ? -12.651 52.688  37.813  1.00 91.19  ?  59  VAL A CB  1 
ATOM   8329  C CG1 . VAL D 1 43  ? -12.031 53.962  37.213  1.00 85.83  ?  59  VAL A CG1 1 
ATOM   8330  C CG2 . VAL D 1 43  ? -12.183 52.496  39.196  1.00 95.18  ?  59  VAL A CG2 1 
ATOM   8331  N N   . GLN D 1 44  ? -14.708 51.586  35.687  1.00 92.76  ?  60  GLN A N   1 
ATOM   8332  C CA  . GLN D 1 44  ? -15.131 51.561  34.287  1.00 93.87  ?  60  GLN A CA  1 
ATOM   8333  C C   . GLN D 1 44  ? -16.600 51.944  34.142  1.00 96.75  ?  60  GLN A C   1 
ATOM   8334  O O   . GLN D 1 44  ? -16.955 52.762  33.284  1.00 97.85  ?  60  GLN A O   1 
ATOM   8335  C CB  . GLN D 1 44  ? -14.843 50.196  33.651  1.00 93.85  ?  60  GLN A CB  1 
ATOM   8336  C CG  . GLN D 1 44  ? -13.493 50.175  32.913  1.00 109.22 ?  60  GLN A CG  1 
ATOM   8337  C CD  . GLN D 1 44  ? -13.361 51.295  31.861  1.00 108.09 ?  60  GLN A CD  1 
ATOM   8338  O OE1 . GLN D 1 44  ? -12.537 52.214  32.001  1.00 108.66 ?  60  GLN A OE1 1 
ATOM   8339  N NE2 . GLN D 1 44  ? -14.123 51.175  30.770  1.00 104.97 ?  60  GLN A NE2 1 
ATOM   8340  N N   . ASN D 1 45  ? -17.473 51.368  34.972  1.00 90.07  ?  61  ASN A N   1 
ATOM   8341  C CA  . ASN D 1 45  ? -18.891 51.722  34.860  1.00 83.15  ?  61  ASN A CA  1 
ATOM   8342  C C   . ASN D 1 45  ? -19.127 53.182  35.211  1.00 82.63  ?  61  ASN A C   1 
ATOM   8343  O O   . ASN D 1 45  ? -19.892 53.873  34.530  1.00 87.03  ?  61  ASN A O   1 
ATOM   8344  C CB  . ASN D 1 45  ? -19.777 50.831  35.720  1.00 81.29  ?  61  ASN A CB  1 
ATOM   8345  C CG  . ASN D 1 45  ? -19.618 49.366  35.392  1.00 85.64  ?  61  ASN A CG  1 
ATOM   8346  O OD1 . ASN D 1 45  ? -20.419 48.797  34.651  1.00 84.18  ?  61  ASN A OD1 1 
ATOM   8347  N ND2 . ASN D 1 45  ? -18.632 48.724  36.001  1.00 91.16  ?  61  ASN A ND2 1 
ATOM   8348  N N   . MET D 1 46  ? -18.490 53.669  36.275  1.00 78.39  ?  62  MET A N   1 
ATOM   8349  C CA  . MET D 1 46  ? -18.528 55.089  36.600  1.00 80.22  ?  62  MET A CA  1 
ATOM   8350  C C   . MET D 1 46  ? -18.151 55.950  35.400  1.00 80.75  ?  62  MET A C   1 
ATOM   8351  O O   . MET D 1 46  ? -18.878 56.884  35.045  1.00 83.65  ?  62  MET A O   1 
ATOM   8352  C CB  . MET D 1 46  ? -17.593 55.376  37.776  1.00 77.18  ?  62  MET A CB  1 
ATOM   8353  C CG  . MET D 1 46  ? -17.561 56.830  38.210  1.00 73.97  ?  62  MET A CG  1 
ATOM   8354  S SD  . MET D 1 46  ? -16.358 57.049  39.514  1.00 71.99  ?  62  MET A SD  1 
ATOM   8355  C CE  . MET D 1 46  ? -16.538 58.812  39.885  1.00 73.08  ?  62  MET A CE  1 
ATOM   8356  N N   . ASN D 1 47  ? -17.006 55.663  34.773  1.00 82.55  ?  63  ASN A N   1 
ATOM   8357  C CA  . ASN D 1 47  ? -16.567 56.456  33.630  1.00 86.74  ?  63  ASN A CA  1 
ATOM   8358  C C   . ASN D 1 47  ? -17.552 56.376  32.470  1.00 87.16  ?  63  ASN A C   1 
ATOM   8359  O O   . ASN D 1 47  ? -17.838 57.396  31.842  1.00 88.99  ?  63  ASN A O   1 
ATOM   8360  C CB  . ASN D 1 47  ? -15.169 56.031  33.171  1.00 92.72  ?  63  ASN A CB  1 
ATOM   8361  C CG  . ASN D 1 47  ? -14.073 56.517  34.076  1.00 88.04  ?  63  ASN A CG  1 
ATOM   8362  O OD1 . ASN D 1 47  ? -14.129 57.626  34.610  1.00 86.20  ?  63  ASN A OD1 1 
ATOM   8363  N ND2 . ASN D 1 47  ? -13.056 55.685  34.250  1.00 88.42  ?  63  ASN A ND2 1 
ATOM   8364  N N   . ASN D 1 48  ? -18.044 55.178  32.130  1.00 86.96  ?  64  ASN A N   1 
ATOM   8365  C CA  . ASN D 1 48  ? -19.018 55.093  31.032  1.00 89.63  ?  64  ASN A CA  1 
ATOM   8366  C C   . ASN D 1 48  ? -20.261 55.925  31.314  1.00 89.29  ?  64  ASN A C   1 
ATOM   8367  O O   . ASN D 1 48  ? -20.708 56.698  30.457  1.00 89.79  ?  64  ASN A O   1 
ATOM   8368  C CB  . ASN D 1 48  ? -19.423 53.652  30.704  1.00 86.76  ?  64  ASN A CB  1 
ATOM   8369  C CG  . ASN D 1 48  ? -18.269 52.784  30.294  1.00 89.25  ?  64  ASN A CG  1 
ATOM   8370  O OD1 . ASN D 1 48  ? -17.272 53.273  29.767  1.00 92.21  ?  64  ASN A OD1 1 
ATOM   8371  N ND2 . ASN D 1 48  ? -18.446 51.470  30.419  1.00 88.51  ?  64  ASN A ND2 1 
ATOM   8372  N N   . ALA D 1 49  ? -20.861 55.742  32.484  1.00 86.81  ?  65  ALA A N   1 
ATOM   8373  C CA  . ALA D 1 49  ? -22.059 56.510  32.800  1.00 83.47  ?  65  ALA A CA  1 
ATOM   8374  C C   . ALA D 1 49  ? -21.772 58.007  32.780  1.00 83.15  ?  65  ALA A C   1 
ATOM   8375  O O   . ALA D 1 49  ? -22.551 58.789  32.220  1.00 90.21  ?  65  ALA A O   1 
ATOM   8376  C CB  . ALA D 1 49  ? -22.613 56.079  34.152  1.00 78.02  ?  65  ALA A CB  1 
ATOM   8377  N N   . GLY D 1 50  ? -20.648 58.424  33.367  1.00 89.46  ?  66  GLY A N   1 
ATOM   8378  C CA  . GLY D 1 50  ? -20.290 59.828  33.336  1.00 91.60  ?  66  GLY A CA  1 
ATOM   8379  C C   . GLY D 1 50  ? -20.067 60.334  31.930  1.00 90.75  ?  66  GLY A C   1 
ATOM   8380  O O   . GLY D 1 50  ? -20.390 61.484  31.620  1.00 92.80  ?  66  GLY A O   1 
ATOM   8381  N N   . ASP D 1 51  ? -19.569 59.470  31.045  1.00 85.44  ?  67  ASP A N   1 
ATOM   8382  C CA  . ASP D 1 51  ? -19.335 59.868  29.662  1.00 85.04  ?  67  ASP A CA  1 
ATOM   8383  C C   . ASP D 1 51  ? -20.643 60.035  28.910  1.00 79.82  ?  67  ASP A C   1 
ATOM   8384  O O   . ASP D 1 51  ? -20.813 61.015  28.179  1.00 80.53  ?  67  ASP A O   1 
ATOM   8385  C CB  . ASP D 1 51  ? -18.451 58.836  28.965  1.00 90.12  ?  67  ASP A CB  1 
ATOM   8386  C CG  . ASP D 1 51  ? -16.997 58.923  29.391  1.00 89.61  ?  67  ASP A CG  1 
ATOM   8387  O OD1 . ASP D 1 51  ? -16.627 59.912  30.075  1.00 90.13  ?  67  ASP A OD1 1 
ATOM   8388  O OD2 . ASP D 1 51  ? -16.247 57.971  29.076  1.00 92.74  -1 67  ASP A OD2 1 
ATOM   8389  N N   . LYS D 1 52  ? -21.564 59.077  29.072  1.00 81.33  ?  68  LYS A N   1 
ATOM   8390  C CA  . LYS D 1 52  ? -22.895 59.153  28.461  1.00 80.28  ?  68  LYS A CA  1 
ATOM   8391  C C   . LYS D 1 52  ? -23.654 60.384  28.935  1.00 76.13  ?  68  LYS A C   1 
ATOM   8392  O O   . LYS D 1 52  ? -24.367 61.029  28.160  1.00 75.81  ?  68  LYS A O   1 
ATOM   8393  C CB  . LYS D 1 52  ? -23.680 57.897  28.820  1.00 79.81  ?  68  LYS A CB  1 
ATOM   8394  C CG  . LYS D 1 52  ? -23.018 56.622  28.311  1.00 89.51  ?  68  LYS A CG  1 
ATOM   8395  C CD  . LYS D 1 52  ? -23.915 55.399  28.453  1.00 91.46  ?  68  LYS A CD  1 
ATOM   8396  C CE  . LYS D 1 52  ? -23.153 54.127  28.064  1.00 86.84  ?  68  LYS A CE  1 
ATOM   8397  N NZ  . LYS D 1 52  ? -24.044 52.937  27.960  1.00 87.31  ?  68  LYS A NZ  1 
ATOM   8398  N N   . TRP D 1 53  ? -23.486 60.742  30.200  1.00 74.16  ?  69  TRP A N   1 
ATOM   8399  C CA  . TRP D 1 53  ? -24.107 61.948  30.713  1.00 70.40  ?  69  TRP A CA  1 
ATOM   8400  C C   . TRP D 1 53  ? -23.482 63.190  30.088  1.00 71.27  ?  69  TRP A C   1 
ATOM   8401  O O   . TRP D 1 53  ? -24.198 64.056  29.585  1.00 71.08  ?  69  TRP A O   1 
ATOM   8402  C CB  . TRP D 1 53  ? -23.943 61.978  32.218  1.00 69.32  ?  69  TRP A CB  1 
ATOM   8403  C CG  . TRP D 1 53  ? -24.278 63.263  32.838  1.00 66.79  ?  69  TRP A CG  1 
ATOM   8404  C CD1 . TRP D 1 53  ? -23.432 64.088  33.480  1.00 67.32  ?  69  TRP A CD1 1 
ATOM   8405  C CD2 . TRP D 1 53  ? -25.596 63.798  33.039  1.00 65.17  ?  69  TRP A CD2 1 
ATOM   8406  N NE1 . TRP D 1 53  ? -24.115 65.161  33.994  1.00 66.11  ?  69  TRP A NE1 1 
ATOM   8407  C CE2 . TRP D 1 53  ? -25.450 64.998  33.749  1.00 58.31  ?  69  TRP A CE2 1 
ATOM   8408  C CE3 . TRP D 1 53  ? -26.877 63.393  32.658  1.00 65.68  ?  69  TRP A CE3 1 
ATOM   8409  C CZ2 . TRP D 1 53  ? -26.526 65.808  34.081  1.00 57.22  ?  69  TRP A CZ2 1 
ATOM   8410  C CZ3 . TRP D 1 53  ? -27.955 64.203  32.991  1.00 64.68  ?  69  TRP A CZ3 1 
ATOM   8411  C CH2 . TRP D 1 53  ? -27.768 65.400  33.694  1.00 59.06  ?  69  TRP A CH2 1 
ATOM   8412  N N   . SER D 1 54  ? -22.144 63.317  30.137  1.00 72.05  ?  70  SER A N   1 
ATOM   8413  C CA  . SER D 1 54  ? -21.481 64.461  29.509  1.00 70.26  ?  70  SER A CA  1 
ATOM   8414  C C   . SER D 1 54  ? -21.844 64.574  28.038  1.00 72.27  ?  70  SER A C   1 
ATOM   8415  O O   . SER D 1 54  ? -21.957 65.682  27.493  1.00 74.88  ?  70  SER A O   1 
ATOM   8416  C CB  . SER D 1 54  ? -19.964 64.348  29.632  1.00 71.88  ?  70  SER A CB  1 
ATOM   8417  O OG  . SER D 1 54  ? -19.493 64.642  30.935  1.00 81.86  ?  70  SER A OG  1 
ATOM   8418  N N   . ALA D 1 55  ? -22.004 63.432  27.370  1.00 75.73  ?  71  ALA A N   1 
ATOM   8419  C CA  . ALA D 1 55  ? -22.367 63.434  25.962  1.00 76.38  ?  71  ALA A CA  1 
ATOM   8420  C C   . ALA D 1 55  ? -23.770 63.978  25.787  1.00 77.87  ?  71  ALA A C   1 
ATOM   8421  O O   . ALA D 1 55  ? -24.010 64.850  24.938  1.00 80.13  ?  71  ALA A O   1 
ATOM   8422  C CB  . ALA D 1 55  ? -22.249 62.020  25.392  1.00 73.82  ?  71  ALA A CB  1 
ATOM   8423  N N   . PHE D 1 56  ? -24.699 63.477  26.606  1.00 72.04  ?  72  PHE A N   1 
ATOM   8424  C CA  . PHE D 1 56  ? -26.067 63.978  26.633  1.00 74.46  ?  72  PHE A CA  1 
ATOM   8425  C C   . PHE D 1 56  ? -26.090 65.484  26.854  1.00 74.62  ?  72  PHE A C   1 
ATOM   8426  O O   . PHE D 1 56  ? -26.949 66.193  26.322  1.00 75.06  ?  72  PHE A O   1 
ATOM   8427  C CB  . PHE D 1 56  ? -26.848 63.274  27.750  1.00 71.23  ?  72  PHE A CB  1 
ATOM   8428  C CG  . PHE D 1 56  ? -28.223 63.849  27.994  1.00 65.64  ?  72  PHE A CG  1 
ATOM   8429  C CD1 . PHE D 1 56  ? -29.239 63.618  27.125  1.00 66.97  ?  72  PHE A CD1 1 
ATOM   8430  C CD2 . PHE D 1 56  ? -28.457 64.704  29.045  1.00 67.17  ?  72  PHE A CD2 1 
ATOM   8431  C CE1 . PHE D 1 56  ? -30.465 64.145  27.349  1.00 70.56  ?  72  PHE A CE1 1 
ATOM   8432  C CE2 . PHE D 1 56  ? -29.688 65.247  29.258  1.00 62.20  ?  72  PHE A CE2 1 
ATOM   8433  C CZ  . PHE D 1 56  ? -30.683 64.968  28.414  1.00 66.36  ?  72  PHE A CZ  1 
ATOM   8434  N N   . LEU D 1 57  ? -25.151 65.990  27.636  1.00 73.58  ?  73  LEU A N   1 
ATOM   8435  C CA  . LEU D 1 57  ? -25.179 67.411  27.929  1.00 76.74  ?  73  LEU A CA  1 
ATOM   8436  C C   . LEU D 1 57  ? -24.598 68.219  26.789  1.00 82.03  ?  73  LEU A C   1 
ATOM   8437  O O   . LEU D 1 57  ? -25.138 69.280  26.463  1.00 82.20  ?  73  LEU A O   1 
ATOM   8438  C CB  . LEU D 1 57  ? -24.466 67.694  29.248  1.00 73.73  ?  73  LEU A CB  1 
ATOM   8439  C CG  . LEU D 1 57  ? -25.405 67.481  30.435  1.00 68.49  ?  73  LEU A CG  1 
ATOM   8440  C CD1 . LEU D 1 57  ? -24.715 67.602  31.712  1.00 68.45  ?  73  LEU A CD1 1 
ATOM   8441  C CD2 . LEU D 1 57  ? -26.364 68.586  30.408  1.00 69.15  ?  73  LEU A CD2 1 
ATOM   8442  N N   . LYS D 1 58  ? -23.520 67.749  26.164  1.00 91.60  ?  74  LYS A N   1 
ATOM   8443  C CA  . LYS D 1 58  ? -23.038 68.465  24.989  1.00 98.06  ?  74  LYS A CA  1 
ATOM   8444  C C   . LYS D 1 58  ? -24.144 68.537  23.952  1.00 97.48  ?  74  LYS A C   1 
ATOM   8445  O O   . LYS D 1 58  ? -24.431 69.613  23.391  1.00 97.06  ?  74  LYS A O   1 
ATOM   8446  C CB  . LYS D 1 58  ? -21.772 67.813  24.420  1.00 100.05 ?  74  LYS A CB  1 
ATOM   8447  C CG  . LYS D 1 58  ? -21.048 68.726  23.388  1.00 108.60 ?  74  LYS A CG  1 
ATOM   8448  C CD  . LYS D 1 58  ? -19.657 68.232  22.958  1.00 113.66 ?  74  LYS A CD  1 
ATOM   8449  C CE  . LYS D 1 58  ? -18.655 68.218  24.136  1.00 120.11 ?  74  LYS A CE  1 
ATOM   8450  N NZ  . LYS D 1 58  ? -18.518 69.557  24.816  1.00 111.83 ?  74  LYS A NZ  1 
ATOM   8451  N N   . GLU D 1 59  ? -24.839 67.405  23.764  1.00 101.34 ?  75  GLU A N   1 
ATOM   8452  C CA  . GLU D 1 59  ? -25.919 67.320  22.778  1.00 99.75  ?  75  GLU A CA  1 
ATOM   8453  C C   . GLU D 1 59  ? -27.064 68.275  23.092  1.00 98.20  ?  75  GLU A C   1 
ATOM   8454  O O   . GLU D 1 59  ? -27.517 69.028  22.221  1.00 95.55  ?  75  GLU A O   1 
ATOM   8455  C CB  . GLU D 1 59  ? -26.439 65.888  22.678  1.00 94.87  ?  75  GLU A CB  1 
ATOM   8456  C CG  . GLU D 1 59  ? -27.739 65.861  21.941  1.00 103.58 ?  75  GLU A CG  1 
ATOM   8457  C CD  . GLU D 1 59  ? -27.621 66.324  20.461  1.00 120.57 ?  75  GLU A CD  1 
ATOM   8458  O OE1 . GLU D 1 59  ? -26.485 66.539  19.963  1.00 126.48 ?  75  GLU A OE1 1 
ATOM   8459  O OE2 . GLU D 1 59  ? -28.685 66.536  19.816  1.00 120.83 -1 75  GLU A OE2 1 
ATOM   8460  N N   . GLN D 1 60  ? -27.534 68.268  24.338  1.00 81.77  ?  76  GLN A N   1 
ATOM   8461  C CA  . GLN D 1 60  ? -28.654 69.120  24.718  1.00 77.90  ?  76  GLN A CA  1 
ATOM   8462  C C   . GLN D 1 60  ? -28.260 70.588  24.812  1.00 77.13  ?  76  GLN A C   1 
ATOM   8463  O O   . GLN D 1 60  ? -29.102 71.461  24.609  1.00 74.84  ?  76  GLN A O   1 
ATOM   8464  C CB  . GLN D 1 60  ? -29.215 68.648  26.046  1.00 72.84  ?  76  GLN A CB  1 
ATOM   8465  C CG  . GLN D 1 60  ? -29.854 67.289  25.961  1.00 72.80  ?  76  GLN A CG  1 
ATOM   8466  C CD  . GLN D 1 60  ? -31.137 67.290  25.150  1.00 73.03  ?  76  GLN A CD  1 
ATOM   8467  O OE1 . GLN D 1 60  ? -32.075 68.019  25.475  1.00 71.52  ?  76  GLN A OE1 1 
ATOM   8468  N NE2 . GLN D 1 60  ? -31.204 66.439  24.116  1.00 75.67  ?  76  GLN A NE2 1 
ATOM   8469  N N   . SER D 1 61  ? -26.996 70.890  25.118  1.00 85.43  ?  77  SER A N   1 
ATOM   8470  C CA  . SER D 1 61  ? -26.517 72.256  24.981  1.00 84.83  ?  77  SER A CA  1 
ATOM   8471  C C   . SER D 1 61  ? -26.701 72.748  23.556  1.00 89.18  ?  77  SER A C   1 
ATOM   8472  O O   . SER D 1 61  ? -27.331 73.792  23.317  1.00 90.51  ?  77  SER A O   1 
ATOM   8473  C CB  . SER D 1 61  ? -25.049 72.338  25.370  1.00 89.49  ?  77  SER A CB  1 
ATOM   8474  O OG  . SER D 1 61  ? -24.629 73.688  25.336  1.00 99.36  ?  77  SER A OG  1 
ATOM   8475  N N   . THR D 1 62  ? -26.110 72.014  22.600  1.00 86.59  ?  78  THR A N   1 
ATOM   8476  C CA  . THR D 1 62  ? -26.300 72.300  21.177  1.00 86.71  ?  78  THR A CA  1 
ATOM   8477  C C   . THR D 1 62  ? -27.776 72.522  20.846  1.00 84.95  ?  78  THR A C   1 
ATOM   8478  O O   . THR D 1 62  ? -28.161 73.554  20.291  1.00 85.86  ?  78  THR A O   1 
ATOM   8479  C CB  . THR D 1 62  ? -25.739 71.142  20.361  1.00 83.08  ?  78  THR A CB  1 
ATOM   8480  O OG1 . THR D 1 62  ? -24.383 70.941  20.745  1.00 90.02  ?  78  THR A OG1 1 
ATOM   8481  C CG2 . THR D 1 62  ? -25.758 71.458  18.898  1.00 76.60  ?  78  THR A CG2 1 
ATOM   8482  N N   . LEU D 1 63  ? -28.625 71.566  21.216  1.00 86.24  ?  79  LEU A N   1 
ATOM   8483  C CA  . LEU D 1 63  ? -30.051 71.690  20.950  1.00 85.17  ?  79  LEU A CA  1 
ATOM   8484  C C   . LEU D 1 63  ? -30.645 72.943  21.573  1.00 88.72  ?  79  LEU A C   1 
ATOM   8485  O O   . LEU D 1 63  ? -31.536 73.556  20.989  1.00 93.04  ?  79  LEU A O   1 
ATOM   8486  C CB  . LEU D 1 63  ? -30.770 70.464  21.488  1.00 81.70  ?  79  LEU A CB  1 
ATOM   8487  C CG  . LEU D 1 63  ? -30.818 69.385  20.437  1.00 75.77  ?  79  LEU A CG  1 
ATOM   8488  C CD1 . LEU D 1 63  ? -31.172 68.138  21.140  1.00 78.79  ?  79  LEU A CD1 1 
ATOM   8489  C CD2 . LEU D 1 63  ? -31.859 69.738  19.397  1.00 76.42  ?  79  LEU A CD2 1 
ATOM   8490  N N   . ALA D 1 64  ? -30.186 73.308  22.769  1.00 88.85  ?  80  ALA A N   1 
ATOM   8491  C CA  . ALA D 1 64  ? -30.835 74.412  23.515  1.00 87.48  ?  80  ALA A CA  1 
ATOM   8492  C C   . ALA D 1 64  ? -30.656 75.760  22.821  1.00 88.99  ?  80  ALA A C   1 
ATOM   8493  O O   . ALA D 1 64  ? -31.583 76.593  22.885  1.00 90.32  ?  80  ALA A O   1 
ATOM   8494  C CB  . ALA D 1 64  ? -30.267 74.450  24.906  1.00 88.10  ?  80  ALA A CB  1 
ATOM   8495  N N   . GLN D 1 65  ? -29.546 75.931  22.110  1.00 84.98  ?  81  GLN A N   1 
ATOM   8496  C CA  . GLN D 1 65  ? -29.246 77.245  21.482  1.00 90.60  ?  81  GLN A CA  1 
ATOM   8497  C C   . GLN D 1 65  ? -30.260 77.600  20.391  1.00 90.74  ?  81  GLN A C   1 
ATOM   8498  O O   . GLN D 1 65  ? -30.145 78.703  19.844  1.00 89.59  ?  81  GLN A O   1 
ATOM   8499  C CB  . GLN D 1 65  ? -27.838 77.227  20.891  1.00 92.68  ?  81  GLN A CB  1 
ATOM   8500  C CG  . GLN D 1 65  ? -26.782 77.756  21.848  1.00 98.99  ?  81  GLN A CG  1 
ATOM   8501  C CD  . GLN D 1 65  ? -25.562 76.871  21.887  1.00 110.62 ?  81  GLN A CD  1 
ATOM   8502  O OE1 . GLN D 1 65  ? -25.417 75.943  21.094  1.00 114.86 ?  81  GLN A OE1 1 
ATOM   8503  N NE2 . GLN D 1 65  ? -24.666 77.158  22.817  1.00 110.85 ?  81  GLN A NE2 1 
ATOM   8504  N N   . MET D 1 66  ? -31.203 76.713  20.074  1.00 103.38 ?  82  MET A N   1 
ATOM   8505  C CA  . MET D 1 66  ? -32.143 76.997  18.957  1.00 105.79 ?  82  MET A CA  1 
ATOM   8506  C C   . MET D 1 66  ? -33.228 77.940  19.469  1.00 100.45 ?  82  MET A C   1 
ATOM   8507  O O   . MET D 1 66  ? -34.032 78.413  18.655  1.00 101.68 ?  82  MET A O   1 
ATOM   8508  C CB  . MET D 1 66  ? -32.792 75.717  18.425  1.00 104.08 ?  82  MET A CB  1 
ATOM   8509  C CG  . MET D 1 66  ? -31.818 74.563  18.299  1.00 113.62 ?  82  MET A CG  1 
ATOM   8510  S SD  . MET D 1 66  ? -31.723 73.835  16.648  1.00 137.34 ?  82  MET A SD  1 
ATOM   8511  C CE  . MET D 1 66  ? -30.486 72.569  16.929  1.00 123.44 ?  82  MET A CE  1 
ATOM   8512  N N   . TYR D 1 67  ? -33.234 78.195  20.773  1.00 91.63  ?  83  TYR A N   1 
ATOM   8513  C CA  . TYR D 1 67  ? -34.249 79.093  21.368  1.00 91.55  ?  83  TYR A CA  1 
ATOM   8514  C C   . TYR D 1 67  ? -33.545 80.355  21.853  1.00 96.24  ?  83  TYR A C   1 
ATOM   8515  O O   . TYR D 1 67  ? -32.877 80.289  22.889  1.00 101.33 ?  83  TYR A O   1 
ATOM   8516  C CB  . TYR D 1 67  ? -34.958 78.384  22.518  1.00 84.05  ?  83  TYR A CB  1 
ATOM   8517  C CG  . TYR D 1 67  ? -35.398 76.978  22.203  1.00 86.94  ?  83  TYR A CG  1 
ATOM   8518  C CD1 . TYR D 1 67  ? -34.535 75.908  22.360  1.00 88.94  ?  83  TYR A CD1 1 
ATOM   8519  C CD2 . TYR D 1 67  ? -36.675 76.719  21.739  1.00 83.06  ?  83  TYR A CD2 1 
ATOM   8520  C CE1 . TYR D 1 67  ? -34.930 74.615  22.065  1.00 88.68  ?  83  TYR A CE1 1 
ATOM   8521  C CE2 . TYR D 1 67  ? -37.087 75.433  21.441  1.00 81.29  ?  83  TYR A CE2 1 
ATOM   8522  C CZ  . TYR D 1 67  ? -36.211 74.376  21.604  1.00 85.47  ?  83  TYR A CZ  1 
ATOM   8523  O OH  . TYR D 1 67  ? -36.605 73.104  21.314  1.00 85.32  ?  83  TYR A OH  1 
ATOM   8524  N N   . PRO D 1 68  ? -33.652 81.502  21.151  1.00 93.68  ?  84  PRO A N   1 
ATOM   8525  C CA  . PRO D 1 68  ? -32.930 82.716  21.551  1.00 94.35  ?  84  PRO A CA  1 
ATOM   8526  C C   . PRO D 1 68  ? -33.508 83.300  22.833  1.00 100.94 ?  84  PRO A C   1 
ATOM   8527  O O   . PRO D 1 68  ? -34.724 83.502  22.938  1.00 101.19 ?  84  PRO A O   1 
ATOM   8528  C CB  . PRO D 1 68  ? -33.157 83.660  20.371  1.00 100.46 ?  84  PRO A CB  1 
ATOM   8529  C CG  . PRO D 1 68  ? -34.467 83.254  19.835  1.00 98.69  ?  84  PRO A CG  1 
ATOM   8530  C CD  . PRO D 1 68  ? -34.548 81.757  20.019  1.00 101.26 ?  84  PRO A CD  1 
ATOM   8531  N N   . LEU D 1 69  ? -32.625 83.599  23.802  1.00 98.34  ?  85  LEU A N   1 
ATOM   8532  C CA  . LEU D 1 69  ? -33.097 84.095  25.094  1.00 98.21  ?  85  LEU A CA  1 
ATOM   8533  C C   . LEU D 1 69  ? -33.776 85.443  24.959  1.00 104.94 ?  85  LEU A C   1 
ATOM   8534  O O   . LEU D 1 69  ? -34.563 85.822  25.834  1.00 106.45 ?  85  LEU A O   1 
ATOM   8535  C CB  . LEU D 1 69  ? -31.949 84.228  26.090  1.00 90.92  ?  85  LEU A CB  1 
ATOM   8536  C CG  . LEU D 1 69  ? -31.022 83.054  26.332  1.00 85.57  ?  85  LEU A CG  1 
ATOM   8537  C CD1 . LEU D 1 69  ? -29.877 83.468  27.240  1.00 82.97  ?  85  LEU A CD1 1 
ATOM   8538  C CD2 . LEU D 1 69  ? -31.812 81.962  26.951  1.00 90.21  ?  85  LEU A CD2 1 
ATOM   8539  N N   . GLN D 1 70  ? -33.470 86.174  23.880  1.00 111.93 ?  86  GLN A N   1 
ATOM   8540  C CA  . GLN D 1 70  ? -34.030 87.503  23.664  1.00 116.60 ?  86  GLN A CA  1 
ATOM   8541  C C   . GLN D 1 70  ? -35.558 87.462  23.525  1.00 116.32 ?  86  GLN A C   1 
ATOM   8542  O O   . GLN D 1 70  ? -36.242 88.399  23.950  1.00 123.79 ?  86  GLN A O   1 
ATOM   8543  C CB  . GLN D 1 70  ? -33.361 88.113  22.425  1.00 121.98 ?  86  GLN A CB  1 
ATOM   8544  C CG  . GLN D 1 70  ? -33.596 89.612  22.163  1.00 129.78 ?  86  GLN A CG  1 
ATOM   8545  C CD  . GLN D 1 70  ? -34.682 89.894  21.114  1.00 136.90 ?  86  GLN A CD  1 
ATOM   8546  O OE1 . GLN D 1 70  ? -35.025 89.026  20.301  1.00 139.72 ?  86  GLN A OE1 1 
ATOM   8547  N NE2 . GLN D 1 70  ? -35.166 91.138  21.080  1.00 135.05 ?  86  GLN A NE2 1 
ATOM   8548  N N   . GLU D 1 71  ? -36.111 86.377  22.971  1.00 110.94 ?  87  GLU A N   1 
ATOM   8549  C CA  . GLU D 1 71  ? -37.546 86.221  22.752  1.00 111.87 ?  87  GLU A CA  1 
ATOM   8550  C C   . GLU D 1 71  ? -38.241 85.380  23.831  1.00 104.65 ?  87  GLU A C   1 
ATOM   8551  O O   . GLU D 1 71  ? -39.273 84.761  23.548  1.00 94.60  ?  87  GLU A O   1 
ATOM   8552  C CB  . GLU D 1 71  ? -37.790 85.582  21.387  1.00 117.14 ?  87  GLU A CB  1 
ATOM   8553  C CG  . GLU D 1 71  ? -37.362 86.408  20.207  1.00 120.84 ?  87  GLU A CG  1 
ATOM   8554  C CD  . GLU D 1 71  ? -37.491 85.623  18.914  1.00 128.49 ?  87  GLU A CD  1 
ATOM   8555  O OE1 . GLU D 1 71  ? -38.606 85.562  18.348  1.00 135.25 ?  87  GLU A OE1 1 
ATOM   8556  O OE2 . GLU D 1 71  ? -36.470 85.043  18.480  1.00 126.70 -1 87  GLU A OE2 1 
ATOM   8557  N N   . ILE D 1 72  ? -37.695 85.335  25.055  1.00 105.17 ?  88  ILE A N   1 
ATOM   8558  C CA  . ILE D 1 72  ? -38.222 84.519  26.151  1.00 99.95  ?  88  ILE A CA  1 
ATOM   8559  C C   . ILE D 1 72  ? -38.392 85.390  27.393  1.00 97.05  ?  88  ILE A C   1 
ATOM   8560  O O   . ILE D 1 72  ? -37.505 86.182  27.731  1.00 101.10 ?  88  ILE A O   1 
ATOM   8561  C CB  . ILE D 1 72  ? -37.305 83.317  26.458  1.00 96.23  ?  88  ILE A CB  1 
ATOM   8562  C CG1 . ILE D 1 72  ? -37.042 82.550  25.168  1.00 99.09  ?  88  ILE A CG1 1 
ATOM   8563  C CG2 . ILE D 1 72  ? -37.923 82.407  27.531  1.00 88.28  ?  88  ILE A CG2 1 
ATOM   8564  C CD1 . ILE D 1 72  ? -36.466 81.212  25.360  1.00 94.56  ?  88  ILE A CD1 1 
ATOM   8565  N N   . GLN D 1 73  ? -39.526 85.221  28.092  1.00 95.28  ?  89  GLN A N   1 
ATOM   8566  C CA  . GLN D 1 73  ? -39.963 86.186  29.095  1.00 92.32  ?  89  GLN A CA  1 
ATOM   8567  C C   . GLN D 1 73  ? -40.251 85.538  30.440  1.00 90.68  ?  89  GLN A C   1 
ATOM   8568  O O   . GLN D 1 73  ? -40.207 86.198  31.481  1.00 93.87  ?  89  GLN A O   1 
ATOM   8569  C CB  . GLN D 1 73  ? -41.218 86.931  28.631  1.00 98.35  ?  89  GLN A CB  1 
ATOM   8570  C CG  . GLN D 1 73  ? -41.045 87.872  27.402  1.00 105.45 ?  89  GLN A CG  1 
ATOM   8571  C CD  . GLN D 1 73  ? -40.839 87.172  26.049  1.00 105.36 ?  89  GLN A CD  1 
ATOM   8572  O OE1 . GLN D 1 73  ? -40.030 87.618  25.230  1.00 104.43 ?  89  GLN A OE1 1 
ATOM   8573  N NE2 . GLN D 1 73  ? -41.635 86.134  25.778  1.00 101.38 ?  89  GLN A NE2 1 
ATOM   8574  N N   . ASN D 1 74  ? -40.587 84.256  30.420  1.00 91.71  ?  90  ASN A N   1 
ATOM   8575  C CA  . ASN D 1 74  ? -40.655 83.462  31.640  1.00 89.36  ?  90  ASN A CA  1 
ATOM   8576  C C   . ASN D 1 74  ? -39.257 83.343  32.236  1.00 84.04  ?  90  ASN A C   1 
ATOM   8577  O O   . ASN D 1 74  ? -38.374 82.726  31.628  1.00 77.65  ?  90  ASN A O   1 
ATOM   8578  C CB  . ASN D 1 74  ? -41.267 82.095  31.317  1.00 88.94  ?  90  ASN A CB  1 
ATOM   8579  C CG  . ASN D 1 74  ? -41.578 81.260  32.554  1.00 84.40  ?  90  ASN A CG  1 
ATOM   8580  O OD1 . ASN D 1 74  ? -40.749 81.115  33.446  1.00 81.25  ?  90  ASN A OD1 1 
ATOM   8581  N ND2 . ASN D 1 74  ? -42.785 80.702  32.593  1.00 86.13  ?  90  ASN A ND2 1 
ATOM   8582  N N   . LEU D 1 75  ? -39.040 83.940  33.411  1.00 87.45  ?  91  LEU A N   1 
ATOM   8583  C CA  . LEU D 1 75  ? -37.679 84.025  33.940  1.00 83.32  ?  91  LEU A CA  1 
ATOM   8584  C C   . LEU D 1 75  ? -37.109 82.653  34.294  1.00 71.89  ?  91  LEU A C   1 
ATOM   8585  O O   . LEU D 1 75  ? -35.933 82.415  34.037  1.00 65.57  ?  91  LEU A O   1 
ATOM   8586  C CB  . LEU D 1 75  ? -37.619 84.953  35.154  1.00 87.89  ?  91  LEU A CB  1 
ATOM   8587  C CG  . LEU D 1 75  ? -37.879 86.456  34.987  1.00 87.57  ?  91  LEU A CG  1 
ATOM   8588  C CD1 . LEU D 1 75  ? -37.542 87.162  36.298  1.00 86.37  ?  91  LEU A CD1 1 
ATOM   8589  C CD2 . LEU D 1 75  ? -37.122 87.037  33.816  1.00 81.82  ?  91  LEU A CD2 1 
ATOM   8590  N N   . THR D 1 76  ? -37.900 81.749  34.900  1.00 74.10  ?  92  THR A N   1 
ATOM   8591  C CA  . THR D 1 76  ? -37.355 80.433  35.249  1.00 68.29  ?  92  THR A CA  1 
ATOM   8592  C C   . THR D 1 76  ? -37.051 79.615  34.003  1.00 69.00  ?  92  THR A C   1 
ATOM   8593  O O   . THR D 1 76  ? -36.101 78.819  33.976  1.00 68.98  ?  92  THR A O   1 
ATOM   8594  C CB  . THR D 1 76  ? -38.315 79.664  36.153  1.00 69.52  ?  92  THR A CB  1 
ATOM   8595  O OG1 . THR D 1 76  ? -39.617 79.702  35.590  1.00 85.53  ?  92  THR A OG1 1 
ATOM   8596  C CG2 . THR D 1 76  ? -38.443 80.319  37.492  1.00 62.70  ?  92  THR A CG2 1 
ATOM   8597  N N   . VAL D 1 77  ? -37.812 79.831  32.940  1.00 74.81  ?  93  VAL A N   1 
ATOM   8598  C CA  . VAL D 1 77  ? -37.444 79.247  31.659  1.00 74.56  ?  93  VAL A CA  1 
ATOM   8599  C C   . VAL D 1 77  ? -36.159 79.870  31.159  1.00 72.02  ?  93  VAL A C   1 
ATOM   8600  O O   . VAL D 1 77  ? -35.278 79.184  30.622  1.00 71.22  ?  93  VAL A O   1 
ATOM   8601  C CB  . VAL D 1 77  ? -38.585 79.433  30.647  1.00 76.97  ?  93  VAL A CB  1 
ATOM   8602  C CG1 . VAL D 1 77  ? -38.152 78.936  29.286  1.00 77.43  ?  93  VAL A CG1 1 
ATOM   8603  C CG2 . VAL D 1 77  ? -39.852 78.713  31.130  1.00 73.61  ?  93  VAL A CG2 1 
ATOM   8604  N N   . LYS D 1 78  ? -36.014 81.176  31.372  1.00 70.14  ?  94  LYS A N   1 
ATOM   8605  C CA  . LYS D 1 78  ? -34.814 81.878  30.935  1.00 70.47  ?  94  LYS A CA  1 
ATOM   8606  C C   . LYS D 1 78  ? -33.599 81.355  31.689  1.00 68.18  ?  94  LYS A C   1 
ATOM   8607  O O   . LYS D 1 78  ? -32.536 81.134  31.101  1.00 70.30  ?  94  LYS A O   1 
ATOM   8608  C CB  . LYS D 1 78  ? -35.030 83.384  31.127  1.00 77.88  ?  94  LYS A CB  1 
ATOM   8609  C CG  . LYS D 1 78  ? -34.610 84.251  29.914  1.00 84.15  ?  94  LYS A CG  1 
ATOM   8610  C CD  . LYS D 1 78  ? -34.671 85.775  30.175  1.00 86.50  ?  94  LYS A CD  1 
ATOM   8611  C CE  . LYS D 1 78  ? -34.092 86.540  28.971  1.00 90.80  ?  94  LYS A CE  1 
ATOM   8612  N NZ  . LYS D 1 78  ? -33.639 87.932  29.284  1.00 95.89  ?  94  LYS A NZ  1 
ATOM   8613  N N   . LEU D 1 79  ? -33.790 81.035  32.974  1.00 72.85  ?  95  LEU A N   1 
ATOM   8614  C CA  . LEU D 1 79  ? -32.716 80.541  33.838  1.00 70.32  ?  95  LEU A CA  1 
ATOM   8615  C C   . LEU D 1 79  ? -32.248 79.179  33.390  1.00 69.32  ?  95  LEU A C   1 
ATOM   8616  O O   . LEU D 1 79  ? -31.043 78.920  33.343  1.00 70.78  ?  95  LEU A O   1 
ATOM   8617  C CB  . LEU D 1 79  ? -33.194 80.432  35.280  1.00 64.86  ?  95  LEU A CB  1 
ATOM   8618  C CG  . LEU D 1 79  ? -33.259 81.757  35.978  1.00 63.11  ?  95  LEU A CG  1 
ATOM   8619  C CD1 . LEU D 1 79  ? -33.665 81.467  37.388  1.00 60.35  ?  95  LEU A CD1 1 
ATOM   8620  C CD2 . LEU D 1 79  ? -31.927 82.460  35.827  1.00 58.43  ?  95  LEU A CD2 1 
ATOM   8621  N N   . GLN D 1 80  ? -33.199 78.280  33.082  1.00 66.02  ?  96  GLN A N   1 
ATOM   8622  C CA  . GLN D 1 80  ? -32.814 76.936  32.670  1.00 64.20  ?  96  GLN A CA  1 
ATOM   8623  C C   . GLN D 1 80  ? -32.158 76.953  31.301  1.00 67.93  ?  96  GLN A C   1 
ATOM   8624  O O   . GLN D 1 80  ? -31.196 76.215  31.038  1.00 70.63  ?  96  GLN A O   1 
ATOM   8625  C CB  . GLN D 1 80  ? -34.030 76.033  32.653  1.00 60.85  ?  96  GLN A CB  1 
ATOM   8626  C CG  . GLN D 1 80  ? -34.581 75.869  34.014  1.00 60.88  ?  96  GLN A CG  1 
ATOM   8627  C CD  . GLN D 1 80  ? -35.955 75.312  33.988  1.00 62.74  ?  96  GLN A CD  1 
ATOM   8628  O OE1 . GLN D 1 80  ? -36.131 74.090  33.870  1.00 67.95  ?  96  GLN A OE1 1 
ATOM   8629  N NE2 . GLN D 1 80  ? -36.951 76.190  34.051  1.00 60.65  ?  96  GLN A NE2 1 
ATOM   8630  N N   . LEU D 1 81  ? -32.651 77.797  30.414  1.00 72.95  ?  97  LEU A N   1 
ATOM   8631  C CA  . LEU D 1 81  ? -32.073 77.808  29.087  1.00 77.65  ?  97  LEU A CA  1 
ATOM   8632  C C   . LEU D 1 81  ? -30.664 78.383  29.148  1.00 77.83  ?  97  LEU A C   1 
ATOM   8633  O O   . LEU D 1 81  ? -29.737 77.847  28.541  1.00 78.76  ?  97  LEU A O   1 
ATOM   8634  C CB  . LEU D 1 81  ? -33.004 78.609  28.184  1.00 77.41  ?  97  LEU A CB  1 
ATOM   8635  C CG  . LEU D 1 81  ? -33.966 77.748  27.353  1.00 72.20  ?  97  LEU A CG  1 
ATOM   8636  C CD1 . LEU D 1 81  ? -34.736 78.649  26.497  1.00 81.88  ?  97  LEU A CD1 1 
ATOM   8637  C CD2 . LEU D 1 81  ? -33.292 76.695  26.512  1.00 73.57  ?  97  LEU A CD2 1 
ATOM   8638  N N   . GLN D 1 82  ? -30.488 79.444  29.942  1.00 83.78  ?  98  GLN A N   1 
ATOM   8639  C CA  . GLN D 1 82  ? -29.185 80.059  30.173  1.00 87.98  ?  98  GLN A CA  1 
ATOM   8640  C C   . GLN D 1 82  ? -28.215 79.068  30.801  1.00 86.62  ?  98  GLN A C   1 
ATOM   8641  O O   . GLN D 1 82  ? -27.025 79.029  30.452  1.00 89.78  ?  98  GLN A O   1 
ATOM   8642  C CB  . GLN D 1 82  ? -29.403 81.279  31.081  1.00 88.00  ?  98  GLN A CB  1 
ATOM   8643  C CG  . GLN D 1 82  ? -28.256 82.261  31.293  1.00 96.00  ?  98  GLN A CG  1 
ATOM   8644  C CD  . GLN D 1 82  ? -28.744 83.557  31.943  1.00 98.54  ?  98  GLN A CD  1 
ATOM   8645  O OE1 . GLN D 1 82  ? -28.277 84.660  31.608  1.00 104.82 ?  98  GLN A OE1 1 
ATOM   8646  N NE2 . GLN D 1 82  ? -29.714 83.431  32.848  1.00 85.96  ?  98  GLN A NE2 1 
ATOM   8647  N N   . ALA D 1 83  ? -28.713 78.287  31.762  1.00 82.03  ?  99  ALA A N   1 
ATOM   8648  C CA  . ALA D 1 83  ? -27.994 77.149  32.318  1.00 79.95  ?  99  ALA A CA  1 
ATOM   8649  C C   . ALA D 1 83  ? -27.438 76.258  31.229  1.00 79.70  ?  99  ALA A C   1 
ATOM   8650  O O   . ALA D 1 83  ? -26.239 75.973  31.178  1.00 82.09  ?  99  ALA A O   1 
ATOM   8651  C CB  . ALA D 1 83  ? -28.945 76.341  33.199  1.00 73.21  ?  99  ALA A CB  1 
ATOM   8652  N N   . LEU D 1 84  ? -28.308 75.804  30.352  1.00 80.08  ?  100 LEU A N   1 
ATOM   8653  C CA  . LEU D 1 84  ? -27.955 74.722  29.455  1.00 80.47  ?  100 LEU A CA  1 
ATOM   8654  C C   . LEU D 1 84  ? -27.269 75.228  28.184  1.00 83.25  ?  100 LEU A C   1 
ATOM   8655  O O   . LEU D 1 84  ? -26.740 74.422  27.412  1.00 80.09  ?  100 LEU A O   1 
ATOM   8656  C CB  . LEU D 1 84  ? -29.238 73.937  29.152  1.00 74.45  ?  100 LEU A CB  1 
ATOM   8657  C CG  . LEU D 1 84  ? -29.346 72.487  28.695  1.00 67.56  ?  100 LEU A CG  1 
ATOM   8658  C CD1 . LEU D 1 84  ? -28.487 71.597  29.537  1.00 61.23  ?  100 LEU A CD1 1 
ATOM   8659  C CD2 . LEU D 1 84  ? -30.810 72.057  28.791  1.00 65.22  ?  100 LEU A CD2 1 
ATOM   8660  N N   . GLN D 1 85  ? -27.242 76.541  27.962  1.00 89.06  ?  101 GLN A N   1 
ATOM   8661  C CA  . GLN D 1 85  ? -26.652 77.081  26.745  1.00 90.09  ?  101 GLN A CA  1 
ATOM   8662  C C   . GLN D 1 85  ? -25.158 77.350  26.863  1.00 98.17  ?  101 GLN A C   1 
ATOM   8663  O O   . GLN D 1 85  ? -24.478 77.327  25.835  1.00 108.26 ?  101 GLN A O   1 
ATOM   8664  C CB  . GLN D 1 85  ? -27.327 78.387  26.329  1.00 84.97  ?  101 GLN A CB  1 
ATOM   8665  C CG  . GLN D 1 85  ? -28.605 78.203  25.604  1.00 88.15  ?  101 GLN A CG  1 
ATOM   8666  C CD  . GLN D 1 85  ? -29.269 79.520  25.305  1.00 92.53  ?  101 GLN A CD  1 
ATOM   8667  O OE1 . GLN D 1 85  ? -28.829 80.560  25.778  1.00 96.45  ?  101 GLN A OE1 1 
ATOM   8668  N NE2 . GLN D 1 85  ? -30.376 79.479  24.570  1.00 92.50  ?  101 GLN A NE2 1 
ATOM   8669  N N   . GLN D 1 86  ? -24.638 77.637  28.063  1.00 95.47  ?  102 GLN A N   1 
ATOM   8670  C CA  . GLN D 1 86  ? -23.221 77.945  28.220  1.00 96.69  ?  102 GLN A CA  1 
ATOM   8671  C C   . GLN D 1 86  ? -22.378 76.863  27.561  1.00 99.53  ?  102 GLN A C   1 
ATOM   8672  O O   . GLN D 1 86  ? -22.537 75.677  27.859  1.00 98.01  ?  102 GLN A O   1 
ATOM   8673  C CB  . GLN D 1 86  ? -22.843 78.042  29.701  1.00 99.10  ?  102 GLN A CB  1 
ATOM   8674  C CG  . GLN D 1 86  ? -23.254 76.811  30.510  1.00 100.84 ?  102 GLN A CG  1 
ATOM   8675  C CD  . GLN D 1 86  ? -23.071 76.950  32.011  1.00 102.08 ?  102 GLN A CD  1 
ATOM   8676  O OE1 . GLN D 1 86  ? -22.430 77.887  32.486  1.00 108.19 ?  102 GLN A OE1 1 
ATOM   8677  N NE2 . GLN D 1 86  ? -23.625 75.998  32.767  1.00 102.60 ?  102 GLN A NE2 1 
ATOM   8678  N N   . ASN D 1 87  ? -21.496 77.258  26.651  1.00 106.66 ?  103 ASN A N   1 
ATOM   8679  C CA  . ASN D 1 87  ? -20.662 76.276  25.970  1.00 109.05 ?  103 ASN A CA  1 
ATOM   8680  C C   . ASN D 1 87  ? -19.215 76.311  26.426  1.00 112.62 ?  103 ASN A C   1 
ATOM   8681  O O   . ASN D 1 87  ? -18.405 75.559  25.880  1.00 114.38 ?  103 ASN A O   1 
ATOM   8682  C CB  . ASN D 1 87  ? -20.701 76.428  24.440  1.00 114.01 ?  103 ASN A CB  1 
ATOM   8683  C CG  . ASN D 1 87  ? -20.992 77.844  23.976  1.00 119.06 ?  103 ASN A CG  1 
ATOM   8684  O OD1 . ASN D 1 87  ? -20.875 78.805  24.743  1.00 121.46 ?  103 ASN A OD1 1 
ATOM   8685  N ND2 . ASN D 1 87  ? -21.375 77.974  22.698  1.00 110.97 ?  103 ASN A ND2 1 
ATOM   8686  N N   . GLY D 1 88  ? -18.878 77.151  27.401  1.00 114.76 ?  104 GLY A N   1 
ATOM   8687  C CA  . GLY D 1 88  ? -17.558 77.194  28.007  1.00 106.87 ?  104 GLY A CA  1 
ATOM   8688  C C   . GLY D 1 88  ? -16.396 77.042  27.051  1.00 112.97 ?  104 GLY A C   1 
ATOM   8689  O O   . GLY D 1 88  ? -16.320 77.704  26.009  1.00 112.54 ?  104 GLY A O   1 
ATOM   8690  N N   . SER D 1 89  ? -15.484 76.133  27.384  1.00 108.76 ?  105 SER A N   1 
ATOM   8691  C CA  . SER D 1 89  ? -14.283 75.978  26.575  1.00 114.01 ?  105 SER A CA  1 
ATOM   8692  C C   . SER D 1 89  ? -14.579 75.448  25.174  1.00 114.80 ?  105 SER A C   1 
ATOM   8693  O O   . SER D 1 89  ? -13.752 75.622  24.272  1.00 117.53 ?  105 SER A O   1 
ATOM   8694  C CB  . SER D 1 89  ? -13.287 75.077  27.310  1.00 114.45 ?  105 SER A CB  1 
ATOM   8695  O OG  . SER D 1 89  ? -12.455 74.349  26.422  1.00 115.92 ?  105 SER A OG  1 
ATOM   8696  N N   . SER D 1 90  ? -15.749 74.849  24.948  1.00 111.95 ?  106 SER A N   1 
ATOM   8697  C CA  . SER D 1 90  ? -16.099 74.404  23.603  1.00 110.68 ?  106 SER A CA  1 
ATOM   8698  C C   . SER D 1 90  ? -16.199 75.584  22.630  1.00 108.50 ?  106 SER A C   1 
ATOM   8699  O O   . SER D 1 90  ? -16.344 75.373  21.423  1.00 112.04 ?  106 SER A O   1 
ATOM   8700  C CB  . SER D 1 90  ? -17.395 73.563  23.652  1.00 110.65 ?  106 SER A CB  1 
ATOM   8701  O OG  . SER D 1 90  ? -18.573 74.342  23.676  1.00 110.85 ?  106 SER A OG  1 
ATOM   8702  N N   . VAL D 1 91  ? -16.057 76.826  23.118  1.00 111.83 ?  107 VAL A N   1 
ATOM   8703  C CA  . VAL D 1 91  ? -16.057 77.974  22.208  1.00 106.36 ?  107 VAL A CA  1 
ATOM   8704  C C   . VAL D 1 91  ? -14.675 78.296  21.649  1.00 106.94 ?  107 VAL A C   1 
ATOM   8705  O O   . VAL D 1 91  ? -14.569 79.109  20.719  1.00 100.81 ?  107 VAL A O   1 
ATOM   8706  C CB  . VAL D 1 91  ? -16.606 79.253  22.871  1.00 106.57 ?  107 VAL A CB  1 
ATOM   8707  C CG1 . VAL D 1 91  ? -15.547 79.907  23.746  1.00 106.21 ?  107 VAL A CG1 1 
ATOM   8708  C CG2 . VAL D 1 91  ? -17.148 80.216  21.822  1.00 110.29 ?  107 VAL A CG2 1 
ATOM   8709  N N   . LEU D 1 92  ? -13.615 77.723  22.205  1.00 104.99 ?  108 LEU A N   1 
ATOM   8710  C CA  . LEU D 1 92  ? -12.315 77.781  21.561  1.00 103.15 ?  108 LEU A CA  1 
ATOM   8711  C C   . LEU D 1 92  ? -12.275 76.786  20.419  1.00 101.65 ?  108 LEU A C   1 
ATOM   8712  O O   . LEU D 1 92  ? -12.996 75.783  20.424  1.00 104.28 ?  108 LEU A O   1 
ATOM   8713  C CB  . LEU D 1 92  ? -11.191 77.444  22.538  1.00 106.23 ?  108 LEU A CB  1 
ATOM   8714  C CG  . LEU D 1 92  ? -10.932 78.319  23.759  1.00 107.00 ?  108 LEU A CG  1 
ATOM   8715  C CD1 . LEU D 1 92  ? -9.950  77.616  24.673  1.00 107.19 ?  108 LEU A CD1 1 
ATOM   8716  C CD2 . LEU D 1 92  ? -10.358 79.657  23.323  1.00 106.85 ?  108 LEU A CD2 1 
ATOM   8717  N N   . SER D 1 93  ? -11.404 77.055  19.447  1.00 104.60 ?  109 SER A N   1 
ATOM   8718  C CA  . SER D 1 93  ? -11.145 76.074  18.406  1.00 111.47 ?  109 SER A CA  1 
ATOM   8719  C C   . SER D 1 93  ? -10.840 74.722  19.037  1.00 121.62 ?  109 SER A C   1 
ATOM   8720  O O   . SER D 1 93  ? -10.335 74.651  20.158  1.00 126.14 ?  109 SER A O   1 
ATOM   8721  C CB  . SER D 1 93  ? -9.986  76.537  17.534  1.00 108.56 ?  109 SER A CB  1 
ATOM   8722  O OG  . SER D 1 93  ? -8.759  76.217  18.139  1.00 112.83 ?  109 SER A OG  1 
ATOM   8723  N N   . GLU D 1 94  ? -11.196 73.637  18.336  1.00 136.89 ?  110 GLU A N   1 
ATOM   8724  C CA  . GLU D 1 94  ? -11.011 72.306  18.917  1.00 133.96 ?  110 GLU A CA  1 
ATOM   8725  C C   . GLU D 1 94  ? -9.557  72.083  19.310  1.00 132.63 ?  110 GLU A C   1 
ATOM   8726  O O   . GLU D 1 94  ? -9.263  71.392  20.298  1.00 134.30 ?  110 GLU A O   1 
ATOM   8727  C CB  . GLU D 1 94  ? -11.480 71.227  17.936  1.00 144.22 ?  110 GLU A CB  1 
ATOM   8728  C CG  . GLU D 1 94  ? -12.950 71.333  17.529  1.00 150.70 ?  110 GLU A CG  1 
ATOM   8729  C CD  . GLU D 1 94  ? -13.279 70.480  16.314  1.00 168.08 ?  110 GLU A CD  1 
ATOM   8730  O OE1 . GLU D 1 94  ? -12.613 69.439  16.126  1.00 170.41 ?  110 GLU A OE1 1 
ATOM   8731  O OE2 . GLU D 1 94  ? -14.190 70.857  15.537  1.00 173.89 -1 110 GLU A OE2 1 
ATOM   8732  N N   . ASP D 1 95  ? -8.648  72.732  18.590  1.00 142.22 ?  111 ASP A N   1 
ATOM   8733  C CA  . ASP D 1 95  ? -7.222  72.607  18.843  1.00 138.50 ?  111 ASP A CA  1 
ATOM   8734  C C   . ASP D 1 95  ? -6.823  73.270  20.169  1.00 135.45 ?  111 ASP A C   1 
ATOM   8735  O O   . ASP D 1 95  ? -6.153  72.656  21.014  1.00 131.33 ?  111 ASP A O   1 
ATOM   8736  C CB  . ASP D 1 95  ? -6.501  73.229  17.659  1.00 138.07 ?  111 ASP A CB  1 
ATOM   8737  C CG  . ASP D 1 95  ? -5.040  73.114  17.763  1.00 150.38 ?  111 ASP A CG  1 
ATOM   8738  O OD1 . ASP D 1 95  ? -4.540  71.975  17.673  1.00 154.55 ?  111 ASP A OD1 1 
ATOM   8739  O OD2 . ASP D 1 95  ? -4.399  74.160  17.977  1.00 161.32 -1 111 ASP A OD2 1 
ATOM   8740  N N   . LYS D 1 96  ? -7.237  74.525  20.373  1.00 127.99 ?  112 LYS A N   1 
ATOM   8741  C CA  . LYS D 1 96  ? -7.006  75.206  21.643  1.00 117.77 ?  112 LYS A CA  1 
ATOM   8742  C C   . LYS D 1 96  ? -7.730  74.526  22.802  1.00 115.01 ?  112 LYS A C   1 
ATOM   8743  O O   . LYS D 1 96  ? -7.216  74.522  23.917  1.00 113.08 ?  112 LYS A O   1 
ATOM   8744  C CB  . LYS D 1 96  ? -7.462  76.653  21.530  1.00 106.75 ?  112 LYS A CB  1 
ATOM   8745  C CG  . LYS D 1 96  ? -6.786  77.419  20.430  1.00 100.26 ?  112 LYS A CG  1 
ATOM   8746  C CD  . LYS D 1 96  ? -6.687  78.874  20.776  1.00 93.97  ?  112 LYS A CD  1 
ATOM   8747  C CE  . LYS D 1 96  ? -6.411  79.678  19.536  1.00 94.89  ?  112 LYS A CE  1 
ATOM   8748  N NZ  . LYS D 1 96  ? -5.436  80.778  19.780  1.00 92.61  ?  112 LYS A NZ  1 
ATOM   8749  N N   . SER D 1 97  ? -8.940  73.992  22.566  1.00 112.89 ?  113 SER A N   1 
ATOM   8750  C CA  . SER D 1 97  ? -9.640  73.190  23.570  1.00 112.00 ?  113 SER A CA  1 
ATOM   8751  C C   . SER D 1 97  ? -8.777  72.031  24.042  1.00 120.33 ?  113 SER A C   1 
ATOM   8752  O O   . SER D 1 97  ? -8.619  71.804  25.252  1.00 119.53 ?  113 SER A O   1 
ATOM   8753  C CB  . SER D 1 97  ? -10.951 72.643  22.999  1.00 113.81 ?  113 SER A CB  1 
ATOM   8754  O OG  . SER D 1 97  ? -11.825 73.654  22.530  1.00 115.81 ?  113 SER A OG  1 
ATOM   8755  N N   . LYS D 1 98  ? -8.229  71.267  23.091  1.00 137.03 ?  114 LYS A N   1 
ATOM   8756  C CA  . LYS D 1 98  ? -7.337  70.171  23.453  1.00 133.44 ?  114 LYS A CA  1 
ATOM   8757  C C   . LYS D 1 98  ? -6.103  70.681  24.194  1.00 125.90 ?  114 LYS A C   1 
ATOM   8758  O O   . LYS D 1 98  ? -5.674  70.066  25.178  1.00 124.16 ?  114 LYS A O   1 
ATOM   8759  C CB  . LYS D 1 98  ? -6.979  69.356  22.200  1.00 137.99 ?  114 LYS A CB  1 
ATOM   8760  C CG  . LYS D 1 98  ? -8.241  68.674  21.614  1.00 146.12 ?  114 LYS A CG  1 
ATOM   8761  C CD  . LYS D 1 98  ? -8.055  67.670  20.459  1.00 148.16 ?  114 LYS A CD  1 
ATOM   8762  C CE  . LYS D 1 98  ? -7.529  68.292  19.180  1.00 145.04 ?  114 LYS A CE  1 
ATOM   8763  N NZ  . LYS D 1 98  ? -6.829  67.290  18.327  1.00 137.30 ?  114 LYS A NZ  1 
ATOM   8764  N N   . ARG D 1 99  ? -5.548  71.825  23.778  1.00 113.13 ?  115 ARG A N   1 
ATOM   8765  C CA  . ARG D 1 99  ? -4.380  72.371  24.478  1.00 107.56 ?  115 ARG A CA  1 
ATOM   8766  C C   . ARG D 1 99  ? -4.699  72.737  25.916  1.00 100.43 ?  115 ARG A C   1 
ATOM   8767  O O   . ARG D 1 99  ? -3.919  72.445  26.830  1.00 97.89  ?  115 ARG A O   1 
ATOM   8768  C CB  . ARG D 1 99  ? -3.837  73.594  23.761  1.00 114.08 ?  115 ARG A CB  1 
ATOM   8769  C CG  . ARG D 1 99  ? -3.104  73.250  22.515  1.00 129.68 ?  115 ARG A CG  1 
ATOM   8770  C CD  . ARG D 1 99  ? -2.985  74.439  21.582  1.00 138.79 ?  115 ARG A CD  1 
ATOM   8771  N NE  . ARG D 1 99  ? -1.605  74.882  21.430  1.00 144.72 ?  115 ARG A NE  1 
ATOM   8772  C CZ  . ARG D 1 99  ? -0.983  75.006  20.268  1.00 145.71 ?  115 ARG A CZ  1 
ATOM   8773  N NH1 . ARG D 1 99  ? -1.555  74.631  19.135  1.00 146.14 ?  115 ARG A NH1 1 
ATOM   8774  N NH2 . ARG D 1 99  ? 0.255   75.494  20.245  1.00 147.19 ?  115 ARG A NH2 1 
ATOM   8775  N N   . LEU D 1 100 ? -5.805  73.444  26.129  1.00 102.61 ?  116 LEU A N   1 
ATOM   8776  C CA  . LEU D 1 100 ? -6.146  73.878  27.474  1.00 95.73  ?  116 LEU A CA  1 
ATOM   8777  C C   . LEU D 1 100 ? -6.358  72.677  28.376  1.00 91.80  ?  116 LEU A C   1 
ATOM   8778  O O   . LEU D 1 100 ? -5.818  72.632  29.486  1.00 89.27  ?  116 LEU A O   1 
ATOM   8779  C CB  . LEU D 1 100 ? -7.385  74.767  27.444  1.00 94.63  ?  116 LEU A CB  1 
ATOM   8780  C CG  . LEU D 1 100 ? -7.848  75.420  28.748  1.00 89.22  ?  116 LEU A CG  1 
ATOM   8781  C CD1 . LEU D 1 100 ? -6.711  76.199  29.384  1.00 83.13  ?  116 LEU A CD1 1 
ATOM   8782  C CD2 . LEU D 1 100 ? -9.063  76.312  28.506  1.00 88.25  ?  116 LEU A CD2 1 
ATOM   8783  N N   . ASN D 1 101 ? -7.126  71.675  27.902  1.00 92.09  ?  117 ASN A N   1 
ATOM   8784  C CA  . ASN D 1 101 ? -7.329  70.466  28.710  1.00 92.88  ?  117 ASN A CA  1 
ATOM   8785  C C   . ASN D 1 101 ? -6.009  69.748  28.986  1.00 92.87  ?  117 ASN A C   1 
ATOM   8786  O O   . ASN D 1 101 ? -5.822  69.183  30.074  1.00 90.26  ?  117 ASN A O   1 
ATOM   8787  C CB  . ASN D 1 101 ? -8.331  69.511  28.041  1.00 99.64  ?  117 ASN A CB  1 
ATOM   8788  C CG  . ASN D 1 101 ? -9.774  70.040  28.057  1.00 100.34 ?  117 ASN A CG  1 
ATOM   8789  O OD1 . ASN D 1 101 ? -10.115 70.959  28.807  1.00 98.13  ?  117 ASN A OD1 1 
ATOM   8790  N ND2 . ASN D 1 101 ? -10.628 69.447  27.225  1.00 111.83 ?  117 ASN A ND2 1 
ATOM   8791  N N   . THR D 1 102 ? -5.066  69.797  28.036  1.00 96.05  ?  118 THR A N   1 
ATOM   8792  C CA  . THR D 1 102 ? -3.740  69.221  28.257  1.00 90.99  ?  118 THR A CA  1 
ATOM   8793  C C   . THR D 1 102 ? -3.014  69.930  29.387  1.00 85.41  ?  118 THR A C   1 
ATOM   8794  O O   . THR D 1 102 ? -2.545  69.296  30.340  1.00 84.42  ?  118 THR A O   1 
ATOM   8795  C CB  . THR D 1 102 ? -2.898  69.313  26.988  1.00 92.37  ?  118 THR A CB  1 
ATOM   8796  O OG1 . THR D 1 102 ? -3.478  68.499  25.964  1.00 97.87  ?  118 THR A OG1 1 
ATOM   8797  C CG2 . THR D 1 102 ? -1.491  68.840  27.279  1.00 83.45  ?  118 THR A CG2 1 
ATOM   8798  N N   . ILE D 1 103 ? -2.849  71.245  29.253  1.00 84.81  ?  119 ILE A N   1 
ATOM   8799  C CA  . ILE D 1 103 ? -2.197  72.015  30.303  1.00 81.32  ?  119 ILE A CA  1 
ATOM   8800  C C   . ILE D 1 103 ? -2.830  71.712  31.644  1.00 82.89  ?  119 ILE A C   1 
ATOM   8801  O O   . ILE D 1 103 ? -2.140  71.488  32.648  1.00 83.70  ?  119 ILE A O   1 
ATOM   8802  C CB  . ILE D 1 103 ? -2.274  73.519  30.015  1.00 82.85  ?  119 ILE A CB  1 
ATOM   8803  C CG1 . ILE D 1 103 ? -1.426  73.930  28.846  1.00 83.32  ?  119 ILE A CG1 1 
ATOM   8804  C CG2 . ILE D 1 103 ? -1.856  74.319  31.221  1.00 87.17  ?  119 ILE A CG2 1 
ATOM   8805  C CD1 . ILE D 1 103 ? -1.875  75.241  28.389  1.00 86.83  ?  119 ILE A CD1 1 
ATOM   8806  N N   . LEU D 1 104 ? -4.157  71.770  31.691  1.00 83.62  ?  120 LEU A N   1 
ATOM   8807  C CA  . LEU D 1 104 ? -4.852  71.575  32.955  1.00 86.02  ?  120 LEU A CA  1 
ATOM   8808  C C   . LEU D 1 104 ? -4.463  70.233  33.565  1.00 82.08  ?  120 LEU A C   1 
ATOM   8809  O O   . LEU D 1 104 ? -4.116  70.150  34.749  1.00 77.08  ?  120 LEU A O   1 
ATOM   8810  C CB  . LEU D 1 104 ? -6.368  71.656  32.728  1.00 84.03  ?  120 LEU A CB  1 
ATOM   8811  C CG  . LEU D 1 104 ? -7.103  72.936  32.299  1.00 76.52  ?  120 LEU A CG  1 
ATOM   8812  C CD1 . LEU D 1 104 ? -8.519  72.522  32.001  1.00 83.23  ?  120 LEU A CD1 1 
ATOM   8813  C CD2 . LEU D 1 104 ? -7.080  74.065  33.305  1.00 71.21  ?  120 LEU A CD2 1 
ATOM   8814  N N   . ASN D 1 105 ? -4.495  69.171  32.745  1.00 85.00  ?  121 ASN A N   1 
ATOM   8815  C CA  . ASN D 1 105 ? -4.113  67.840  33.203  1.00 81.26  ?  121 ASN A CA  1 
ATOM   8816  C C   . ASN D 1 105 ? -2.695  67.825  33.732  1.00 77.25  ?  121 ASN A C   1 
ATOM   8817  O O   . ASN D 1 105 ? -2.415  67.176  34.748  1.00 76.86  ?  121 ASN A O   1 
ATOM   8818  C CB  . ASN D 1 105 ? -4.265  66.829  32.062  1.00 85.63  ?  121 ASN A CB  1 
ATOM   8819  C CG  . ASN D 1 105 ? -5.580  66.090  32.104  1.00 92.51  ?  121 ASN A CG  1 
ATOM   8820  O OD1 . ASN D 1 105 ? -5.661  65.006  32.684  1.00 98.59  ?  121 ASN A OD1 1 
ATOM   8821  N ND2 . ASN D 1 105 ? -6.626  66.676  31.516  1.00 100.85 ?  121 ASN A ND2 1 
ATOM   8822  N N   . THR D 1 106 ? -1.787  68.523  33.046  1.00 76.25  ?  122 THR A N   1 
ATOM   8823  C CA  . THR D 1 106 ? -0.378  68.539  33.442  1.00 78.11  ?  122 THR A CA  1 
ATOM   8824  C C   . THR D 1 106 ? -0.187  69.197  34.806  1.00 76.79  ?  122 THR A C   1 
ATOM   8825  O O   . THR D 1 106 ? 0.455   68.626  35.699  1.00 71.12  ?  122 THR A O   1 
ATOM   8826  C CB  . THR D 1 106 ? 0.463   69.268  32.400  1.00 73.01  ?  122 THR A CB  1 
ATOM   8827  O OG1 . THR D 1 106 ? 0.385   68.584  31.146  1.00 72.66  ?  122 THR A OG1 1 
ATOM   8828  C CG2 . THR D 1 106 ? 1.904   69.309  32.875  1.00 68.77  ?  122 THR A CG2 1 
ATOM   8829  N N   . MET D 1 107 ? -0.697  70.425  34.957  1.00 73.89  ?  123 MET A N   1 
ATOM   8830  C CA  . MET D 1 107 ? -0.715  71.089  36.256  1.00 69.24  ?  123 MET A CA  1 
ATOM   8831  C C   . MET D 1 107 ? -1.306  70.181  37.350  1.00 71.17  ?  123 MET A C   1 
ATOM   8832  O O   . MET D 1 107 ? -0.733  70.055  38.441  1.00 73.94  ?  123 MET A O   1 
ATOM   8833  C CB  . MET D 1 107 ? -1.476  72.422  36.146  1.00 68.64  ?  123 MET A CB  1 
ATOM   8834  C CG  . MET D 1 107 ? -0.785  73.505  35.284  1.00 69.70  ?  123 MET A CG  1 
ATOM   8835  S SD  . MET D 1 107 ? -1.426  75.218  35.459  1.00 67.67  ?  123 MET A SD  1 
ATOM   8836  C CE  . MET D 1 107 ? -3.092  75.066  34.848  1.00 78.56  ?  123 MET A CE  1 
ATOM   8837  N N   . SER D 1 108 ? -2.435  69.513  37.068  1.00 72.41  ?  124 SER A N   1 
ATOM   8838  C CA  . SER D 1 108 ? -3.064  68.655  38.075  1.00 70.11  ?  124 SER A CA  1 
ATOM   8839  C C   . SER D 1 108 ? -2.130  67.537  38.502  1.00 70.58  ?  124 SER A C   1 
ATOM   8840  O O   . SER D 1 108 ? -1.905  67.314  39.708  1.00 71.51  ?  124 SER A O   1 
ATOM   8841  C CB  . SER D 1 108 ? -4.366  68.069  37.530  1.00 73.68  ?  124 SER A CB  1 
ATOM   8842  O OG  . SER D 1 108 ? -5.019  67.242  38.484  1.00 71.62  ?  124 SER A OG  1 
ATOM   8843  N N   . THR D 1 109 ? -1.557  66.829  37.524  1.00 70.56  ?  125 THR A N   1 
ATOM   8844  C CA  . THR D 1 109 ? -0.714  65.709  37.904  1.00 72.86  ?  125 THR A CA  1 
ATOM   8845  C C   . THR D 1 109 ? 0.603   66.190  38.513  1.00 72.51  ?  125 THR A C   1 
ATOM   8846  O O   . THR D 1 109 ? 1.186   65.474  39.330  1.00 73.47  ?  125 THR A O   1 
ATOM   8847  C CB  . THR D 1 109 ? -0.486  64.753  36.728  1.00 71.30  ?  125 THR A CB  1 
ATOM   8848  O OG1 . THR D 1 109 ? 0.516   65.286  35.865  1.00 69.46  ?  125 THR A OG1 1 
ATOM   8849  C CG2 . THR D 1 109 ? -1.814  64.507  35.942  1.00 71.40  ?  125 THR A CG2 1 
ATOM   8850  N N   . ILE D 1 110 ? 1.062   67.405  38.193  1.00 75.68  ?  126 ILE A N   1 
ATOM   8851  C CA  . ILE D 1 110 ? 2.248   67.954  38.868  1.00 76.70  ?  126 ILE A CA  1 
ATOM   8852  C C   . ILE D 1 110 ? 1.961   68.104  40.346  1.00 73.14  ?  126 ILE A C   1 
ATOM   8853  O O   . ILE D 1 110 ? 2.613   67.467  41.176  1.00 75.63  ?  126 ILE A O   1 
ATOM   8854  C CB  . ILE D 1 110 ? 2.726   69.309  38.296  1.00 73.59  ?  126 ILE A CB  1 
ATOM   8855  C CG1 . ILE D 1 110 ? 3.367   69.164  36.921  1.00 72.11  ?  126 ILE A CG1 1 
ATOM   8856  C CG2 . ILE D 1 110 ? 3.730   69.957  39.206  1.00 76.62  ?  126 ILE A CG2 1 
ATOM   8857  C CD1 . ILE D 1 110 ? 3.901   70.454  36.372  1.00 72.17  ?  126 ILE A CD1 1 
ATOM   8858  N N   . TYR D 1 111 ? 1.000   68.968  40.680  1.00 66.64  ?  127 TYR A N   1 
ATOM   8859  C CA  . TYR D 1 111 ? 0.651   69.206  42.079  1.00 65.24  ?  127 TYR A CA  1 
ATOM   8860  C C   . TYR D 1 111 ? 0.492   67.898  42.846  1.00 72.56  ?  127 TYR A C   1 
ATOM   8861  O O   . TYR D 1 111 ? 0.955   67.780  43.992  1.00 69.71  ?  127 TYR A O   1 
ATOM   8862  C CB  . TYR D 1 111 ? -0.654  69.996  42.176  1.00 62.43  ?  127 TYR A CB  1 
ATOM   8863  C CG  . TYR D 1 111 ? -1.086  70.440  43.568  1.00 57.68  ?  127 TYR A CG  1 
ATOM   8864  C CD1 . TYR D 1 111 ? -0.688  71.655  44.089  1.00 58.86  ?  127 TYR A CD1 1 
ATOM   8865  C CD2 . TYR D 1 111 ? -1.855  69.608  44.386  1.00 60.28  ?  127 TYR A CD2 1 
ATOM   8866  C CE1 . TYR D 1 111 ? -1.091  72.064  45.380  1.00 60.14  ?  127 TYR A CE1 1 
ATOM   8867  C CE2 . TYR D 1 111 ? -2.257  69.998  45.681  1.00 54.12  ?  127 TYR A CE2 1 
ATOM   8868  C CZ  . TYR D 1 111 ? -1.869  71.233  46.171  1.00 60.81  ?  127 TYR A CZ  1 
ATOM   8869  O OH  . TYR D 1 111 ? -2.242  71.636  47.446  1.00 60.50  ?  127 TYR A OH  1 
ATOM   8870  N N   . SER D 1 112 ? -0.173  66.899  42.242  1.00 69.59  ?  128 SER A N   1 
ATOM   8871  C CA  . SER D 1 112 ? -0.409  65.689  43.024  1.00 72.02  ?  128 SER A CA  1 
ATOM   8872  C C   . SER D 1 112 ? 0.829   64.808  43.139  1.00 75.13  ?  128 SER A C   1 
ATOM   8873  O O   . SER D 1 112 ? 1.021   64.168  44.175  1.00 80.47  ?  128 SER A O   1 
ATOM   8874  C CB  . SER D 1 112 ? -1.556  64.879  42.443  1.00 72.06  ?  128 SER A CB  1 
ATOM   8875  O OG  . SER D 1 112 ? -1.203  64.382  41.175  1.00 76.58  ?  128 SER A OG  1 
ATOM   8876  N N   . THR D 1 113 ? 1.683   64.744  42.114  1.00 76.79  ?  129 THR A N   1 
ATOM   8877  C CA  . THR D 1 113 ? 2.840   63.860  42.189  1.00 78.81  ?  129 THR A CA  1 
ATOM   8878  C C   . THR D 1 113 ? 4.156   64.610  42.166  1.00 82.18  ?  129 THR A C   1 
ATOM   8879  O O   . THR D 1 113 ? 5.206   63.972  42.020  1.00 84.39  ?  129 THR A O   1 
ATOM   8880  C CB  . THR D 1 113 ? 2.854   62.842  41.051  1.00 77.41  ?  129 THR A CB  1 
ATOM   8881  O OG1 . THR D 1 113 ? 3.249   63.499  39.832  1.00 69.70  ?  129 THR A OG1 1 
ATOM   8882  C CG2 . THR D 1 113 ? 1.466   62.185  40.903  1.00 79.44  ?  129 THR A CG2 1 
ATOM   8883  N N   . GLY D 1 114 ? 4.128   65.940  42.256  1.00 79.68  ?  130 GLY A N   1 
ATOM   8884  C CA  . GLY D 1 114 ? 5.308   66.695  42.633  1.00 83.05  ?  130 GLY A CA  1 
ATOM   8885  C C   . GLY D 1 114 ? 5.827   66.244  43.990  1.00 87.58  ?  130 GLY A C   1 
ATOM   8886  O O   . GLY D 1 114 ? 5.077   66.168  44.972  1.00 86.17  ?  130 GLY A O   1 
ATOM   8887  N N   . LYS D 1 115 ? 7.111   65.918  44.058  1.00 90.94  ?  131 LYS A N   1 
ATOM   8888  C CA  . LYS D 1 115 ? 7.681   65.431  45.302  1.00 92.98  ?  131 LYS A CA  1 
ATOM   8889  C C   . LYS D 1 115 ? 9.054   66.033  45.498  1.00 93.64  ?  131 LYS A C   1 
ATOM   8890  O O   . LYS D 1 115 ? 9.769   66.290  44.530  1.00 93.70  ?  131 LYS A O   1 
ATOM   8891  C CB  . LYS D 1 115 ? 7.755   63.902  45.340  1.00 102.55 ?  131 LYS A CB  1 
ATOM   8892  C CG  . LYS D 1 115 ? 8.465   63.216  44.178  1.00 106.71 ?  131 LYS A CG  1 
ATOM   8893  C CD  . LYS D 1 115 ? 8.679   61.715  44.484  1.00 112.75 ?  131 LYS A CD  1 
ATOM   8894  C CE  . LYS D 1 115 ? 7.331   60.928  44.597  1.00 111.44 ?  131 LYS A CE  1 
ATOM   8895  N NZ  . LYS D 1 115 ? 6.540   60.762  43.322  1.00 95.96  ?  131 LYS A NZ  1 
ATOM   8896  N N   . VAL D 1 116 ? 9.396   66.282  46.777  1.00 95.52  ?  132 VAL A N   1 
ATOM   8897  C CA  . VAL D 1 116 ? 10.695  66.833  47.169  1.00 95.84  ?  132 VAL A CA  1 
ATOM   8898  C C   . VAL D 1 116 ? 11.367  65.877  48.133  1.00 102.89 ?  132 VAL A C   1 
ATOM   8899  O O   . VAL D 1 116 ? 10.712  65.298  49.002  1.00 104.35 ?  132 VAL A O   1 
ATOM   8900  C CB  . VAL D 1 116 ? 10.620  68.225  47.827  1.00 89.70  ?  132 VAL A CB  1 
ATOM   8901  C CG1 . VAL D 1 116 ? 10.136  69.217  46.863  1.00 92.94  ?  132 VAL A CG1 1 
ATOM   8902  C CG2 . VAL D 1 116 ? 9.711   68.194  49.038  1.00 87.47  ?  132 VAL A CG2 1 
ATOM   8903  N N   . CYS D 1 117 ? 12.689  65.751  48.014  1.00 108.40 ?  133 CYS A N   1 
ATOM   8904  C CA  . CYS D 1 117 ? 13.439  64.787  48.801  1.00 123.27 ?  133 CYS A CA  1 
ATOM   8905  C C   . CYS D 1 117 ? 14.382  65.500  49.758  1.00 124.80 ?  133 CYS A C   1 
ATOM   8906  O O   . CYS D 1 117 ? 14.900  66.574  49.446  1.00 118.06 ?  133 CYS A O   1 
ATOM   8907  C CB  . CYS D 1 117 ? 14.200  63.838  47.898  1.00 134.12 ?  133 CYS A CB  1 
ATOM   8908  S SG  . CYS D 1 117 ? 13.245  63.261  46.508  1.00 133.43 ?  133 CYS A SG  1 
ATOM   8909  N N   . ASN D 1 118 ? 14.611  64.918  50.933  1.00 131.75 ?  134 ASN A N   1 
ATOM   8910  C CA  . ASN D 1 118 ? 15.393  65.639  51.974  1.00 141.58 ?  134 ASN A CA  1 
ATOM   8911  C C   . ASN D 1 118 ? 16.863  65.751  51.573  1.00 157.93 ?  134 ASN A C   1 
ATOM   8912  O O   . ASN D 1 118 ? 17.471  64.726  51.255  1.00 163.03 ?  134 ASN A O   1 
ATOM   8913  C CB  . ASN D 1 118 ? 15.151  65.007  53.348  1.00 149.75 ?  134 ASN A CB  1 
ATOM   8914  C CG  . ASN D 1 118 ? 16.399  64.782  54.172  1.00 158.53 ?  134 ASN A CG  1 
ATOM   8915  O OD1 . ASN D 1 118 ? 17.216  65.682  54.343  1.00 157.02 ?  134 ASN A OD1 1 
ATOM   8916  N ND2 . ASN D 1 118 ? 16.525  63.588  54.724  1.00 160.86 ?  134 ASN A ND2 1 
ATOM   8917  N N   . PRO D 1 119 ? 17.456  66.962  51.603  1.00 136.99 ?  135 PRO A N   1 
ATOM   8918  C CA  . PRO D 1 119 ? 18.836  67.145  51.179  1.00 129.88 ?  135 PRO A CA  1 
ATOM   8919  C C   . PRO D 1 119 ? 19.770  66.473  52.182  1.00 138.37 ?  135 PRO A C   1 
ATOM   8920  O O   . PRO D 1 119 ? 20.762  65.916  51.775  1.00 129.73 ?  135 PRO A O   1 
ATOM   8921  C CB  . PRO D 1 119 ? 19.041  68.654  51.255  1.00 107.63 ?  135 PRO A CB  1 
ATOM   8922  C CG  . PRO D 1 119 ? 18.023  69.114  52.270  1.00 122.20 ?  135 PRO A CG  1 
ATOM   8923  C CD  . PRO D 1 119 ? 16.833  68.204  52.056  1.00 126.82 ?  135 PRO A CD  1 
ATOM   8924  N N   . ASP D 1 120 ? 19.422  66.544  53.464  1.00 145.14 ?  136 ASP A N   1 
ATOM   8925  C CA  . ASP D 1 120 ? 20.281  65.946  54.516  1.00 146.35 ?  136 ASP A CA  1 
ATOM   8926  C C   . ASP D 1 120 ? 20.187  64.425  54.413  1.00 142.63 ?  136 ASP A C   1 
ATOM   8927  O O   . ASP D 1 120 ? 20.946  63.747  55.126  1.00 152.29 ?  136 ASP A O   1 
ATOM   8928  C CB  . ASP D 1 120 ? 19.910  66.474  55.902  1.00 142.36 ?  136 ASP A CB  1 
ATOM   8929  C CG  . ASP D 1 120 ? 20.080  67.978  56.024  1.00 140.58 ?  136 ASP A CG  1 
ATOM   8930  O OD1 . ASP D 1 120 ? 20.874  68.542  55.244  1.00 144.19 ?  136 ASP A OD1 1 
ATOM   8931  O OD2 . ASP D 1 120 ? 19.419  68.572  56.898  1.00 137.82 -1 136 ASP A OD2 1 
ATOM   8932  N N   . ASN D 1 121 ? 19.290  63.916  53.568  1.00 152.26 ?  137 ASN A N   1 
ATOM   8933  C CA  . ASN D 1 121 ? 19.215  62.449  53.338  1.00 161.40 ?  137 ASN A CA  1 
ATOM   8934  C C   . ASN D 1 121 ? 18.308  62.209  52.139  1.00 172.99 ?  137 ASN A C   1 
ATOM   8935  O O   . ASN D 1 121 ? 17.094  62.033  52.338  1.00 182.02 ?  137 ASN A O   1 
ATOM   8936  C CB  . ASN D 1 121 ? 18.731  61.679  54.567  1.00 162.18 ?  137 ASN A CB  1 
ATOM   8937  C CG  . ASN D 1 121 ? 18.337  60.255  54.243  1.00 162.47 ?  137 ASN A CG  1 
ATOM   8938  O OD1 . ASN D 1 121 ? 19.167  59.462  53.805  1.00 161.26 ?  137 ASN A OD1 1 
ATOM   8939  N ND2 . ASN D 1 121 ? 17.073  59.928  54.448  1.00 153.99 ?  137 ASN A ND2 1 
ATOM   8940  N N   . PRO D 1 122 ? 18.840  62.223  50.903  1.00 182.83 ?  138 PRO A N   1 
ATOM   8941  C CA  . PRO D 1 122 ? 18.001  62.081  49.718  1.00 183.86 ?  138 PRO A CA  1 
ATOM   8942  C C   . PRO D 1 122 ? 17.329  60.706  49.678  1.00 188.02 ?  138 PRO A C   1 
ATOM   8943  O O   . PRO D 1 122 ? 16.652  60.417  48.717  1.00 185.51 ?  138 PRO A O   1 
ATOM   8944  C CB  . PRO D 1 122 ? 18.987  62.240  48.559  1.00 176.23 ?  138 PRO A CB  1 
ATOM   8945  C CG  . PRO D 1 122 ? 20.330  61.897  49.159  1.00 176.29 ?  138 PRO A CG  1 
ATOM   8946  C CD  . PRO D 1 122 ? 20.255  62.375  50.593  1.00 177.31 ?  138 PRO A CD  1 
ATOM   8947  N N   . GLN D 1 123 ? 17.524  59.909  50.725  1.00 243.71 ?  139 GLN A N   1 
ATOM   8948  C CA  . GLN D 1 123 ? 16.877  58.582  50.797  1.00 239.97 ?  139 GLN A CA  1 
ATOM   8949  C C   . GLN D 1 123 ? 15.368  58.778  50.902  1.00 240.80 ?  139 GLN A C   1 
ATOM   8950  O O   . GLN D 1 123 ? 14.630  57.860  50.496  1.00 241.47 ?  139 GLN A O   1 
ATOM   8951  C CB  . GLN D 1 123 ? 17.361  57.825  52.030  1.00 237.19 ?  139 GLN A CB  1 
ATOM   8952  C CG  . GLN D 1 123 ? 17.885  56.428  51.733  1.00 244.82 ?  139 GLN A CG  1 
ATOM   8953  C CD  . GLN D 1 123 ? 19.242  56.205  52.354  1.00 254.26 ?  139 GLN A CD  1 
ATOM   8954  O OE1 . GLN D 1 123 ? 20.274  56.386  51.714  1.00 254.49 ?  139 GLN A OE1 1 
ATOM   8955  N NE2 . GLN D 1 123 ? 19.249  55.801  53.615  1.00 265.00 ?  139 GLN A NE2 1 
ATOM   8956  N N   . GLU D 1 124 ? 14.921  59.930  51.409  1.00 196.22 ?  140 GLU A N   1 
ATOM   8957  C CA  . GLU D 1 124 ? 13.465  60.094  51.654  1.00 175.60 ?  140 GLU A CA  1 
ATOM   8958  C C   . GLU D 1 124 ? 12.883  61.263  50.866  1.00 159.01 ?  140 GLU A C   1 
ATOM   8959  O O   . GLU D 1 124 ? 13.568  62.288  50.744  1.00 145.65 ?  140 GLU A O   1 
ATOM   8960  C CB  . GLU D 1 124 ? 13.213  60.310  53.143  1.00 169.57 ?  140 GLU A CB  1 
ATOM   8961  C CG  . GLU D 1 124 ? 13.889  61.546  53.707  1.00 155.08 ?  140 GLU A CG  1 
ATOM   8962  C CD  . GLU D 1 124 ? 13.318  61.939  55.058  1.00 159.97 ?  140 GLU A CD  1 
ATOM   8963  O OE1 . GLU D 1 124 ? 13.035  63.141  55.261  1.00 165.13 ?  140 GLU A OE1 1 
ATOM   8964  O OE2 . GLU D 1 124 ? 13.141  61.033  55.899  1.00 161.66 -1 140 GLU A OE2 1 
ATOM   8965  N N   . CYS D 1 125 ? 11.668  61.092  50.344  1.00 149.77 ?  141 CYS A N   1 
ATOM   8966  C CA  . CYS D 1 125 ? 10.973  62.203  49.645  1.00 129.67 ?  141 CYS A CA  1 
ATOM   8967  C C   . CYS D 1 125 ? 9.555   62.333  50.216  1.00 117.28 ?  141 CYS A C   1 
ATOM   8968  O O   . CYS D 1 125 ? 8.987   61.289  50.570  1.00 120.61 ?  141 CYS A O   1 
ATOM   8969  C CB  . CYS D 1 125 ? 10.924  61.999  48.133  1.00 127.72 ?  141 CYS A CB  1 
ATOM   8970  S SG  . CYS D 1 125 ? 12.495  61.552  47.341  1.00 146.40 ?  141 CYS A SG  1 
ATOM   8971  N N   . LEU D 1 126 ? 9.020   63.547  50.331  1.00 105.84 ?  142 LEU A N   1 
ATOM   8972  C CA  . LEU D 1 126 ? 7.707   63.858  50.839  1.00 102.75 ?  142 LEU A CA  1 
ATOM   8973  C C   . LEU D 1 126 ? 6.897   64.387  49.668  1.00 94.51  ?  142 LEU A C   1 
ATOM   8974  O O   . LEU D 1 126 ? 7.400   65.207  48.884  1.00 100.61 ?  142 LEU A O   1 
ATOM   8975  C CB  . LEU D 1 126 ? 7.834   64.861  51.977  1.00 95.10  ?  142 LEU A CB  1 
ATOM   8976  C CG  . LEU D 1 126 ? 8.719   64.176  53.028  1.00 93.58  ?  142 LEU A CG  1 
ATOM   8977  C CD1 . LEU D 1 126 ? 9.097   65.095  54.142  1.00 89.41  ?  142 LEU A CD1 1 
ATOM   8978  C CD2 . LEU D 1 126 ? 8.082   62.896  53.559  1.00 106.69 ?  142 LEU A CD2 1 
ATOM   8979  N N   . LEU D 1 127 ? 5.709   63.823  49.480  1.00 87.01  ?  143 LEU A N   1 
ATOM   8980  C CA  . LEU D 1 127 ? 4.687   64.473  48.690  1.00 83.59  ?  143 LEU A CA  1 
ATOM   8981  C C   . LEU D 1 127 ? 4.100   65.606  49.529  1.00 80.86  ?  143 LEU A C   1 
ATOM   8982  O O   . LEU D 1 127 ? 4.311   65.669  50.741  1.00 83.87  ?  143 LEU A O   1 
ATOM   8983  C CB  . LEU D 1 127 ? 3.597   63.474  48.317  1.00 86.04  ?  143 LEU A CB  1 
ATOM   8984  C CG  . LEU D 1 127 ? 3.878   62.295  47.387  1.00 85.16  ?  143 LEU A CG  1 
ATOM   8985  C CD1 . LEU D 1 127 ? 2.549   61.583  47.099  1.00 92.60  ?  143 LEU A CD1 1 
ATOM   8986  C CD2 . LEU D 1 127 ? 4.543   62.749  46.114  1.00 85.97  ?  143 LEU A CD2 1 
ATOM   8987  N N   . LEU D 1 128 ? 3.356   66.515  48.902  1.00 77.43  ?  144 LEU A N   1 
ATOM   8988  C CA  . LEU D 1 128 ? 2.685   67.534  49.705  1.00 77.10  ?  144 LEU A CA  1 
ATOM   8989  C C   . LEU D 1 128 ? 1.765   66.887  50.736  1.00 83.02  ?  144 LEU A C   1 
ATOM   8990  O O   . LEU D 1 128 ? 1.722   67.312  51.897  1.00 81.22  ?  144 LEU A O   1 
ATOM   8991  C CB  . LEU D 1 128 ? 1.917   68.504  48.812  1.00 73.34  ?  144 LEU A CB  1 
ATOM   8992  C CG  . LEU D 1 128 ? 1.131   69.576  49.567  1.00 70.46  ?  144 LEU A CG  1 
ATOM   8993  C CD1 . LEU D 1 128 ? 2.082   70.432  50.320  1.00 73.04  ?  144 LEU A CD1 1 
ATOM   8994  C CD2 . LEU D 1 128 ? 0.393   70.454  48.613  1.00 66.89  ?  144 LEU A CD2 1 
ATOM   8995  N N   . GLU D 1 129 ? 1.029   65.842  50.326  1.00 83.73  ?  145 GLU A N   1 
ATOM   8996  C CA  . GLU D 1 129 ? 0.232   64.977  51.201  1.00 83.23  ?  145 GLU A CA  1 
ATOM   8997  C C   . GLU D 1 129 ? 0.761   63.555  51.115  1.00 84.42  ?  145 GLU A C   1 
ATOM   8998  O O   . GLU D 1 129 ? 0.825   63.006  50.004  1.00 88.72  ?  145 GLU A O   1 
ATOM   8999  C CB  . GLU D 1 129 ? -1.244  65.014  50.802  1.00 82.44  ?  145 GLU A CB  1 
ATOM   9000  C CG  . GLU D 1 129 ? -2.135  64.080  51.602  1.00 89.73  ?  145 GLU A CG  1 
ATOM   9001  C CD  . GLU D 1 129 ? -2.135  64.332  53.102  1.00 89.32  ?  145 GLU A CD  1 
ATOM   9002  O OE1 . GLU D 1 129 ? -1.937  65.487  53.556  1.00 87.04  ?  145 GLU A OE1 1 
ATOM   9003  O OE2 . GLU D 1 129 ? -2.344  63.347  53.839  1.00 94.25  -1 145 GLU A OE2 1 
ATOM   9004  N N   . PRO D 1 130 ? 1.121   62.889  52.238  1.00 84.43  ?  146 PRO A N   1 
ATOM   9005  C CA  . PRO D 1 130 ? 0.955   63.274  53.642  1.00 82.02  ?  146 PRO A CA  1 
ATOM   9006  C C   . PRO D 1 130 ? 2.202   63.841  54.301  1.00 81.58  ?  146 PRO A C   1 
ATOM   9007  O O   . PRO D 1 130 ? 2.193   64.016  55.518  1.00 82.13  ?  146 PRO A O   1 
ATOM   9008  C CB  . PRO D 1 130 ? 0.626   61.949  54.310  1.00 81.44  ?  146 PRO A CB  1 
ATOM   9009  C CG  . PRO D 1 130 ? 1.480   61.001  53.562  1.00 83.37  ?  146 PRO A CG  1 
ATOM   9010  C CD  . PRO D 1 130 ? 1.476   61.465  52.128  1.00 87.85  ?  146 PRO A CD  1 
ATOM   9011  N N   . GLY D 1 131 ? 3.255   64.094  53.527  1.00 82.95  ?  147 GLY A N   1 
ATOM   9012  C CA  . GLY D 1 131 ? 4.563   64.370  54.093  1.00 85.27  ?  147 GLY A CA  1 
ATOM   9013  C C   . GLY D 1 131 ? 4.841   65.792  54.526  1.00 79.93  ?  147 GLY A C   1 
ATOM   9014  O O   . GLY D 1 131 ? 5.029   66.065  55.716  1.00 78.17  ?  147 GLY A O   1 
ATOM   9015  N N   . LEU D 1 132 ? 4.888   66.709  53.553  1.00 80.64  ?  148 LEU A N   1 
ATOM   9016  C CA  . LEU D 1 132 ? 5.204   68.106  53.851  1.00 77.96  ?  148 LEU A CA  1 
ATOM   9017  C C   . LEU D 1 132 ? 4.094   68.762  54.658  1.00 77.87  ?  148 LEU A C   1 
ATOM   9018  O O   . LEU D 1 132 ? 4.372   69.502  55.610  1.00 77.87  ?  148 LEU A O   1 
ATOM   9019  C CB  . LEU D 1 132 ? 5.437   68.920  52.570  1.00 67.76  ?  148 LEU A CB  1 
ATOM   9020  C CG  . LEU D 1 132 ? 6.492   68.515  51.541  1.00 68.25  ?  148 LEU A CG  1 
ATOM   9021  C CD1 . LEU D 1 132 ? 6.495   69.515  50.436  1.00 60.82  ?  148 LEU A CD1 1 
ATOM   9022  C CD2 . LEU D 1 132 ? 7.846   68.354  52.136  1.00 76.82  ?  148 LEU A CD2 1 
ATOM   9023  N N   . ASN D 1 133 ? 2.831   68.531  54.277  1.00 76.67  ?  149 ASN A N   1 
ATOM   9024  C CA  . ASN D 1 133 ? 1.711   69.054  55.060  1.00 77.81  ?  149 ASN A CA  1 
ATOM   9025  C C   . ASN D 1 133 ? 1.833   68.650  56.526  1.00 76.54  ?  149 ASN A C   1 
ATOM   9026  O O   . ASN D 1 133 ? 1.521   69.440  57.436  1.00 71.92  ?  149 ASN A O   1 
ATOM   9027  C CB  . ASN D 1 133 ? 0.394   68.563  54.455  1.00 74.60  ?  149 ASN A CB  1 
ATOM   9028  C CG  . ASN D 1 133 ? -0.007  69.347  53.218  1.00 69.36  ?  149 ASN A CG  1 
ATOM   9029  O OD1 . ASN D 1 133 ? 0.449   70.470  52.980  1.00 62.53  ?  149 ASN A OD1 1 
ATOM   9030  N ND2 . ASN D 1 133 ? -0.810  68.717  52.382  1.00 75.45  ?  149 ASN A ND2 1 
ATOM   9031  N N   . GLU D 1 134 ? 2.345   67.436  56.768  1.00 83.20  ?  150 GLU A N   1 
ATOM   9032  C CA  . GLU D 1 134 ? 2.483   66.949  58.133  1.00 84.45  ?  150 GLU A CA  1 
ATOM   9033  C C   . GLU D 1 134 ? 3.520   67.788  58.875  1.00 79.58  ?  150 GLU A C   1 
ATOM   9034  O O   . GLU D 1 134 ? 3.318   68.157  60.040  1.00 81.66  ?  150 GLU A O   1 
ATOM   9035  C CB  . GLU D 1 134 ? 2.807   65.444  58.080  1.00 86.96  ?  150 GLU A CB  1 
ATOM   9036  C CG  . GLU D 1 134 ? 2.784   64.706  59.396  1.00 93.32  ?  150 GLU A CG  1 
ATOM   9037  C CD  . GLU D 1 134 ? 3.991   64.973  60.223  1.00 99.16  ?  150 GLU A CD  1 
ATOM   9038  O OE1 . GLU D 1 134 ? 5.074   65.190  59.617  1.00 99.42  ?  150 GLU A OE1 1 
ATOM   9039  O OE2 . GLU D 1 134 ? 3.832   65.027  61.469  1.00 103.04 -1 150 GLU A OE2 1 
ATOM   9040  N N   . ILE D 1 135 ? 4.586   68.176  58.168  1.00 77.00  ?  151 ILE A N   1 
ATOM   9041  C CA  . ILE D 1 135 ? 5.590   69.090  58.715  1.00 76.34  ?  151 ILE A CA  1 
ATOM   9042  C C   . ILE D 1 135 ? 4.977   70.453  59.023  1.00 71.97  ?  151 ILE A C   1 
ATOM   9043  O O   . ILE D 1 135 ? 4.957   70.887  60.182  1.00 73.48  ?  151 ILE A O   1 
ATOM   9044  C CB  . ILE D 1 135 ? 6.810   69.236  57.776  1.00 76.14  ?  151 ILE A CB  1 
ATOM   9045  C CG1 . ILE D 1 135 ? 7.602   67.925  57.666  1.00 76.65  ?  151 ILE A CG1 1 
ATOM   9046  C CG2 . ILE D 1 135 ? 7.645   70.438  58.172  1.00 66.70  ?  151 ILE A CG2 1 
ATOM   9047  C CD1 . ILE D 1 135 ? 8.768   68.005  56.686  1.00 73.94  ?  151 ILE A CD1 1 
ATOM   9048  N N   . MET D 1 136 ? 4.495   71.159  57.997  1.00 72.96  ?  152 MET A N   1 
ATOM   9049  C CA  . MET D 1 136 ? 3.990   72.519  58.200  1.00 69.41  ?  152 MET A CA  1 
ATOM   9050  C C   . MET D 1 136 ? 2.922   72.577  59.281  1.00 68.23  ?  152 MET A C   1 
ATOM   9051  O O   . MET D 1 136 ? 2.787   73.592  59.968  1.00 61.75  ?  152 MET A O   1 
ATOM   9052  C CB  . MET D 1 136 ? 3.393   73.061  56.917  1.00 67.27  ?  152 MET A CB  1 
ATOM   9053  C CG  . MET D 1 136 ? 4.314   73.073  55.772  1.00 65.87  ?  152 MET A CG  1 
ATOM   9054  S SD  . MET D 1 136 ? 5.806   73.981  56.048  1.00 62.28  ?  152 MET A SD  1 
ATOM   9055  C CE  . MET D 1 136 ? 5.187   75.656  56.199  1.00 69.09  ?  152 MET A CE  1 
ATOM   9056  N N   . ALA D 1 137 ? 2.148   71.504  59.445  1.00 69.86  ?  153 ALA A N   1 
ATOM   9057  C CA  . ALA D 1 137 ? 1.115   71.513  60.468  1.00 67.41  ?  153 ALA A CA  1 
ATOM   9058  C C   . ALA D 1 137 ? 1.691   71.251  61.842  1.00 68.32  ?  153 ALA A C   1 
ATOM   9059  O O   . ALA D 1 137 ? 1.262   71.873  62.813  1.00 67.17  ?  153 ALA A O   1 
ATOM   9060  C CB  . ALA D 1 137 ? 0.038   70.477  60.153  1.00 72.81  ?  153 ALA A CB  1 
ATOM   9061  N N   . ASN D 1 138 ? 2.659   70.342  61.959  1.00 69.20  ?  154 ASN A N   1 
ATOM   9062  C CA  . ASN D 1 138 ? 3.123   69.982  63.290  1.00 70.38  ?  154 ASN A CA  1 
ATOM   9063  C C   . ASN D 1 138 ? 4.452   70.625  63.702  1.00 70.87  ?  154 ASN A C   1 
ATOM   9064  O O   . ASN D 1 138 ? 4.619   70.954  64.886  1.00 69.25  ?  154 ASN A O   1 
ATOM   9065  C CB  . ASN D 1 138 ? 3.231   68.462  63.418  1.00 73.31  ?  154 ASN A CB  1 
ATOM   9066  C CG  . ASN D 1 138 ? 1.916   67.787  63.220  1.00 77.63  ?  154 ASN A CG  1 
ATOM   9067  O OD1 . ASN D 1 138 ? 1.131   67.611  64.160  1.00 84.37  ?  154 ASN A OD1 1 
ATOM   9068  N ND2 . ASN D 1 138 ? 1.667   67.370  61.988  1.00 82.19  ?  154 ASN A ND2 1 
ATOM   9069  N N   . SER D 1 139 ? 5.399   70.823  62.788  1.00 70.06  ?  155 SER A N   1 
ATOM   9070  C CA  . SER D 1 139 ? 6.764   71.112  63.221  1.00 72.63  ?  155 SER A CA  1 
ATOM   9071  C C   . SER D 1 139 ? 6.919   72.503  63.811  1.00 73.20  ?  155 SER A C   1 
ATOM   9072  O O   . SER D 1 139 ? 6.423   73.493  63.259  1.00 70.47  ?  155 SER A O   1 
ATOM   9073  C CB  . SER D 1 139 ? 7.766   70.985  62.092  1.00 75.61  ?  155 SER A CB  1 
ATOM   9074  O OG  . SER D 1 139 ? 9.052   71.288  62.621  1.00 71.59  ?  155 SER A OG  1 
ATOM   9075  N N   . LEU D 1 140 ? 7.640   72.567  64.939  1.00 76.39  ?  156 LEU A N   1 
ATOM   9076  C CA  . LEU D 1 140 ? 8.051   73.812  65.566  1.00 72.86  ?  156 LEU A CA  1 
ATOM   9077  C C   . LEU D 1 140 ? 9.456   74.221  65.206  1.00 74.60  ?  156 LEU A C   1 
ATOM   9078  O O   . LEU D 1 140 ? 9.878   75.307  65.608  1.00 75.93  ?  156 LEU A O   1 
ATOM   9079  C CB  . LEU D 1 140 ? 7.960   73.752  67.100  1.00 63.92  ?  156 LEU A CB  1 
ATOM   9080  C CG  . LEU D 1 140 ? 6.625   73.567  67.791  1.00 60.18  ?  156 LEU A CG  1 
ATOM   9081  C CD1 . LEU D 1 140 ? 6.743   73.608  69.288  1.00 61.52  ?  156 LEU A CD1 1 
ATOM   9082  C CD2 . LEU D 1 140 ? 5.790   74.714  67.355  1.00 62.21  ?  156 LEU A CD2 1 
ATOM   9083  N N   . ASP D 1 141 ? 10.201  73.397  64.485  1.00 86.19  ?  157 ASP A N   1 
ATOM   9084  C CA  . ASP D 1 141 ? 11.571  73.771  64.151  1.00 87.26  ?  157 ASP A CA  1 
ATOM   9085  C C   . ASP D 1 141 ? 11.585  74.661  62.929  1.00 80.29  ?  157 ASP A C   1 
ATOM   9086  O O   . ASP D 1 141 ? 11.046  74.296  61.886  1.00 78.80  ?  157 ASP A O   1 
ATOM   9087  C CB  . ASP D 1 141 ? 12.457  72.557  63.886  1.00 86.95  ?  157 ASP A CB  1 
ATOM   9088  C CG  . ASP D 1 141 ? 13.839  72.963  63.430  1.00 81.07  ?  157 ASP A CG  1 
ATOM   9089  O OD1 . ASP D 1 141 ? 14.702  73.219  64.290  1.00 94.83  ?  157 ASP A OD1 1 
ATOM   9090  O OD2 . ASP D 1 141 ? 14.054  73.084  62.215  1.00 73.58  -1 157 ASP A OD2 1 
ATOM   9091  N N   . TYR D 1 142 ? 12.253  75.804  63.052  1.00 72.51  ?  158 TYR A N   1 
ATOM   9092  C CA  . TYR D 1 142 ? 12.172  76.839  62.032  1.00 74.13  ?  158 TYR A CA  1 
ATOM   9093  C C   . TYR D 1 142 ? 12.805  76.411  60.725  1.00 70.60  ?  158 TYR A C   1 
ATOM   9094  O O   . TYR D 1 142 ? 12.314  76.760  59.651  1.00 69.37  ?  158 TYR A O   1 
ATOM   9095  C CB  . TYR D 1 142 ? 12.883  78.082  62.501  1.00 73.19  ?  158 TYR A CB  1 
ATOM   9096  C CG  . TYR D 1 142 ? 12.837  79.266  61.539  1.00 72.59  ?  158 TYR A CG  1 
ATOM   9097  C CD1 . TYR D 1 142 ? 13.726  79.387  60.482  1.00 72.03  ?  158 TYR A CD1 1 
ATOM   9098  C CD2 . TYR D 1 142 ? 12.022  80.350  61.798  1.00 73.77  ?  158 TYR A CD2 1 
ATOM   9099  C CE1 . TYR D 1 142 ? 13.726  80.516  59.653  1.00 68.82  ?  158 TYR A CE1 1 
ATOM   9100  C CE2 . TYR D 1 142 ? 12.031  81.484  60.979  1.00 70.63  ?  158 TYR A CE2 1 
ATOM   9101  C CZ  . TYR D 1 142 ? 12.883  81.569  59.909  1.00 65.58  ?  158 TYR A CZ  1 
ATOM   9102  O OH  . TYR D 1 142 ? 12.877  82.707  59.109  1.00 53.74  ?  158 TYR A OH  1 
ATOM   9103  N N   . ASN D 1 143 ? 13.956  75.768  60.784  1.00 72.93  ?  159 ASN A N   1 
ATOM   9104  C CA  . ASN D 1 143 ? 14.639  75.460  59.538  1.00 72.56  ?  159 ASN A CA  1 
ATOM   9105  C C   . ASN D 1 143 ? 13.914  74.355  58.798  1.00 70.37  ?  159 ASN A C   1 
ATOM   9106  O O   . ASN D 1 143 ? 13.888  74.353  57.566  1.00 69.03  ?  159 ASN A O   1 
ATOM   9107  C CB  . ASN D 1 143 ? 16.090  75.087  59.833  1.00 77.23  ?  159 ASN A CB  1 
ATOM   9108  C CG  . ASN D 1 143 ? 16.940  76.290  60.196  1.00 72.48  ?  159 ASN A CG  1 
ATOM   9109  O OD1 . ASN D 1 143 ? 16.669  77.409  59.800  1.00 61.97  ?  159 ASN A OD1 1 
ATOM   9110  N ND2 . ASN D 1 143 ? 17.920  76.065  61.049  1.00 87.78  ?  159 ASN A ND2 1 
ATOM   9111  N N   . GLU D 1 144 ? 13.303  73.426  59.542  1.00 73.53  ?  160 GLU A N   1 
ATOM   9112  C CA  . GLU D 1 144 ? 12.536  72.353  58.919  1.00 71.08  ?  160 GLU A CA  1 
ATOM   9113  C C   . GLU D 1 144 ? 11.377  72.957  58.144  1.00 69.51  ?  160 GLU A C   1 
ATOM   9114  O O   . GLU D 1 144 ? 11.191  72.675  56.950  1.00 68.71  ?  160 GLU A O   1 
ATOM   9115  C CB  . GLU D 1 144 ? 12.080  71.363  60.013  1.00 72.21  ?  160 GLU A CB  1 
ATOM   9116  C CG  . GLU D 1 144 ? 11.525  70.002  59.575  1.00 68.35  ?  160 GLU A CG  1 
ATOM   9117  C CD  . GLU D 1 144 ? 10.929  69.193  60.741  1.00 78.20  ?  160 GLU A CD  1 
ATOM   9118  O OE1 . GLU D 1 144 ? 10.965  69.654  61.913  1.00 79.87  ?  160 GLU A OE1 1 
ATOM   9119  O OE2 . GLU D 1 144 ? 10.449  68.065  60.486  1.00 90.40  -1 160 GLU A OE2 1 
ATOM   9120  N N   . ARG D 1 145 ? 10.646  73.866  58.805  1.00 69.91  ?  161 ARG A N   1 
ATOM   9121  C CA  . ARG D 1 145 ? 9.496   74.543  58.215  1.00 68.47  ?  161 ARG A CA  1 
ATOM   9122  C C   . ARG D 1 145 ? 9.909   75.369  57.006  1.00 68.10  ?  161 ARG A C   1 
ATOM   9123  O O   . ARG D 1 145 ? 9.215   75.384  55.984  1.00 72.71  ?  161 ARG A O   1 
ATOM   9124  C CB  . ARG D 1 145 ? 8.838   75.427  59.280  1.00 67.24  ?  161 ARG A CB  1 
ATOM   9125  C CG  . ARG D 1 145 ? 8.308   74.668  60.489  1.00 68.46  ?  161 ARG A CG  1 
ATOM   9126  C CD  . ARG D 1 145 ? 7.586   75.630  61.356  1.00 68.21  ?  161 ARG A CD  1 
ATOM   9127  N NE  . ARG D 1 145 ? 6.518   76.197  60.564  1.00 67.64  ?  161 ARG A NE  1 
ATOM   9128  C CZ  . ARG D 1 145 ? 5.316   75.657  60.472  1.00 68.91  ?  161 ARG A CZ  1 
ATOM   9129  N NH1 . ARG D 1 145 ? 4.992   74.580  61.169  1.00 68.80  ?  161 ARG A NH1 1 
ATOM   9130  N NH2 . ARG D 1 145 ? 4.422   76.202  59.652  1.00 68.97  ?  161 ARG A NH2 1 
ATOM   9131  N N   . LEU D 1 146 ? 11.048  76.053  57.098  1.00 67.11  ?  162 LEU A N   1 
ATOM   9132  C CA  . LEU D 1 146 ? 11.542  76.831  55.965  1.00 67.44  ?  162 LEU A CA  1 
ATOM   9133  C C   . LEU D 1 146 ? 11.858  75.934  54.773  1.00 66.81  ?  162 LEU A C   1 
ATOM   9134  O O   . LEU D 1 146 ? 11.511  76.253  53.632  1.00 67.44  ?  162 LEU A O   1 
ATOM   9135  C CB  . LEU D 1 146 ? 12.791  77.620  56.366  1.00 68.73  ?  162 LEU A CB  1 
ATOM   9136  C CG  . LEU D 1 146 ? 13.365  78.452  55.221  1.00 63.71  ?  162 LEU A CG  1 
ATOM   9137  C CD1 . LEU D 1 146 ? 12.301  79.327  54.642  1.00 66.30  ?  162 LEU A CD1 1 
ATOM   9138  C CD2 . LEU D 1 146 ? 14.509  79.255  55.671  1.00 59.72  ?  162 LEU A CD2 1 
ATOM   9139  N N   . TRP D 1 147 ? 12.571  74.833  55.002  1.00 67.68  ?  163 TRP A N   1 
ATOM   9140  C CA  . TRP D 1 147 ? 12.844  73.935  53.891  1.00 69.52  ?  163 TRP A CA  1 
ATOM   9141  C C   . TRP D 1 147 ? 11.551  73.469  53.245  1.00 69.15  ?  163 TRP A C   1 
ATOM   9142  O O   . TRP D 1 147 ? 11.347  73.652  52.040  1.00 69.87  ?  163 TRP A O   1 
ATOM   9143  C CB  . TRP D 1 147 ? 13.725  72.765  54.333  1.00 71.79  ?  163 TRP A CB  1 
ATOM   9144  C CG  . TRP D 1 147 ? 13.741  71.685  53.334  1.00 76.54  ?  163 TRP A CG  1 
ATOM   9145  C CD1 . TRP D 1 147 ? 14.443  71.638  52.169  1.00 79.34  ?  163 TRP A CD1 1 
ATOM   9146  C CD2 . TRP D 1 147 ? 13.102  70.413  53.474  1.00 78.60  ?  163 TRP A CD2 1 
ATOM   9147  N NE1 . TRP D 1 147 ? 14.215  70.443  51.528  1.00 80.65  ?  163 TRP A NE1 1 
ATOM   9148  C CE2 . TRP D 1 147 ? 13.404  69.667  52.319  1.00 80.39  ?  163 TRP A CE2 1 
ATOM   9149  C CE3 . TRP D 1 147 ? 12.287  69.841  54.457  1.00 75.55  ?  163 TRP A CE3 1 
ATOM   9150  C CZ2 . TRP D 1 147 ? 12.920  68.383  52.120  1.00 87.23  ?  163 TRP A CZ2 1 
ATOM   9151  C CZ3 . TRP D 1 147 ? 11.809  68.575  54.258  1.00 78.81  ?  163 TRP A CZ3 1 
ATOM   9152  C CH2 . TRP D 1 147 ? 12.122  67.859  53.099  1.00 86.35  ?  163 TRP A CH2 1 
ATOM   9153  N N   . ALA D 1 148 ? 10.650  72.888  54.030  1.00 70.24  ?  164 ALA A N   1 
ATOM   9154  C CA  . ALA D 1 148 ? 9.402   72.390  53.447  1.00 68.81  ?  164 ALA A CA  1 
ATOM   9155  C C   . ALA D 1 148 ? 8.782   73.438  52.531  1.00 67.18  ?  164 ALA A C   1 
ATOM   9156  O O   . ALA D 1 148 ? 8.540   73.199  51.337  1.00 72.85  ?  164 ALA A O   1 
ATOM   9157  C CB  . ALA D 1 148 ? 8.419   71.997  54.555  1.00 70.80  ?  164 ALA A CB  1 
ATOM   9158  N N   . TRP D 1 149 ? 8.590   74.633  53.091  1.00 67.36  ?  165 TRP A N   1 
ATOM   9159  C CA  . TRP D 1 149 ? 7.953   75.740  52.386  1.00 63.09  ?  165 TRP A CA  1 
ATOM   9160  C C   . TRP D 1 149 ? 8.683   76.057  51.078  1.00 66.00  ?  165 TRP A C   1 
ATOM   9161  O O   . TRP D 1 149 ? 8.099   76.010  49.980  1.00 73.58  ?  165 TRP A O   1 
ATOM   9162  C CB  . TRP D 1 149 ? 7.941   76.953  53.317  1.00 63.39  ?  165 TRP A CB  1 
ATOM   9163  C CG  . TRP D 1 149 ? 7.101   78.131  52.929  1.00 63.01  ?  165 TRP A CG  1 
ATOM   9164  C CD1 . TRP D 1 149 ? 5.829   78.409  53.347  1.00 61.18  ?  165 TRP A CD1 1 
ATOM   9165  C CD2 . TRP D 1 149 ? 7.455   79.176  52.015  1.00 64.80  ?  165 TRP A CD2 1 
ATOM   9166  N NE1 . TRP D 1 149 ? 5.385   79.587  52.778  1.00 58.58  ?  165 TRP A NE1 1 
ATOM   9167  C CE2 . TRP D 1 149 ? 6.362   80.071  51.950  1.00 60.89  ?  165 TRP A CE2 1 
ATOM   9168  C CE3 . TRP D 1 149 ? 8.597   79.453  51.251  1.00 64.84  ?  165 TRP A CE3 1 
ATOM   9169  C CZ2 . TRP D 1 149 ? 6.384   81.222  51.149  1.00 60.65  ?  165 TRP A CZ2 1 
ATOM   9170  C CZ3 . TRP D 1 149 ? 8.604   80.605  50.444  1.00 64.09  ?  165 TRP A CZ3 1 
ATOM   9171  C CH2 . TRP D 1 149 ? 7.505   81.465  50.403  1.00 60.41  ?  165 TRP A CH2 1 
ATOM   9172  N N   . GLU D 1 150 ? 9.980   76.347  51.168  1.00 64.77  ?  166 GLU A N   1 
ATOM   9173  C CA  . GLU D 1 150 ? 10.695  76.863  50.007  1.00 72.85  ?  166 GLU A CA  1 
ATOM   9174  C C   . GLU D 1 150 ? 10.836  75.791  48.925  1.00 74.71  ?  166 GLU A C   1 
ATOM   9175  O O   . GLU D 1 150 ? 10.700  76.082  47.723  1.00 75.53  ?  166 GLU A O   1 
ATOM   9176  C CB  . GLU D 1 150 ? 12.092  77.346  50.392  1.00 73.90  ?  166 GLU A CB  1 
ATOM   9177  C CG  . GLU D 1 150 ? 13.005  77.603  49.177  1.00 71.86  ?  166 GLU A CG  1 
ATOM   9178  C CD  . GLU D 1 150 ? 12.536  78.770  48.296  1.00 74.94  ?  166 GLU A CD  1 
ATOM   9179  O OE1 . GLU D 1 150 ? 11.635  79.520  48.715  1.00 75.12  ?  166 GLU A OE1 1 
ATOM   9180  O OE2 . GLU D 1 150 ? 12.994  78.899  47.140  1.00 79.16  -1 166 GLU A OE2 1 
ATOM   9181  N N   . SER D 1 151 ? 11.162  74.556  49.316  1.00 82.02  ?  167 SER A N   1 
ATOM   9182  C CA  . SER D 1 151 ? 11.393  73.541  48.298  1.00 81.98  ?  167 SER A CA  1 
ATOM   9183  C C   . SER D 1 151 ? 10.088  73.075  47.663  1.00 83.54  ?  167 SER A C   1 
ATOM   9184  O O   . SER D 1 151 ? 10.117  72.644  46.511  1.00 88.89  ?  167 SER A O   1 
ATOM   9185  C CB  . SER D 1 151 ? 12.204  72.370  48.857  1.00 86.12  ?  167 SER A CB  1 
ATOM   9186  O OG  . SER D 1 151 ? 11.638  71.820  50.028  1.00 92.13  ?  167 SER A OG  1 
ATOM   9187  N N   . TRP D 1 152 ? 8.934   73.188  48.347  1.00 73.04  ?  168 TRP A N   1 
ATOM   9188  C CA  . TRP D 1 152 ? 7.672   73.030  47.617  1.00 72.62  ?  168 TRP A CA  1 
ATOM   9189  C C   . TRP D 1 152 ? 7.560   74.068  46.514  1.00 73.07  ?  168 TRP A C   1 
ATOM   9190  O O   . TRP D 1 152 ? 7.392   73.727  45.335  1.00 79.70  ?  168 TRP A O   1 
ATOM   9191  C CB  . TRP D 1 152 ? 6.460   73.115  48.553  1.00 71.10  ?  168 TRP A CB  1 
ATOM   9192  C CG  . TRP D 1 152 ? 5.068   72.952  47.859  1.00 69.49  ?  168 TRP A CG  1 
ATOM   9193  C CD1 . TRP D 1 152 ? 4.092   73.920  47.713  1.00 67.24  ?  168 TRP A CD1 1 
ATOM   9194  C CD2 . TRP D 1 152 ? 4.549   71.781  47.219  1.00 66.69  ?  168 TRP A CD2 1 
ATOM   9195  N NE1 . TRP D 1 152 ? 3.009   73.414  47.043  1.00 60.98  ?  168 TRP A NE1 1 
ATOM   9196  C CE2 . TRP D 1 152 ? 3.263   72.104  46.729  1.00 66.48  ?  168 TRP A CE2 1 
ATOM   9197  C CE3 . TRP D 1 152 ? 5.038   70.491  47.022  1.00 64.45  ?  168 TRP A CE3 1 
ATOM   9198  C CZ2 . TRP D 1 152 ? 2.470   71.181  46.051  1.00 67.80  ?  168 TRP A CZ2 1 
ATOM   9199  C CZ3 . TRP D 1 152 ? 4.245   69.571  46.358  1.00 70.01  ?  168 TRP A CZ3 1 
ATOM   9200  C CH2 . TRP D 1 152 ? 2.978   69.921  45.875  1.00 71.03  ?  168 TRP A CH2 1 
ATOM   9201  N N   . ARG D 1 153 ? 7.697   75.342  46.871  1.00 73.29  ?  169 ARG A N   1 
ATOM   9202  C CA  . ARG D 1 153 ? 7.501   76.350  45.836  1.00 76.29  ?  169 ARG A CA  1 
ATOM   9203  C C   . ARG D 1 153 ? 8.580   76.348  44.757  1.00 79.99  ?  169 ARG A C   1 
ATOM   9204  O O   . ARG D 1 153 ? 8.392   77.007  43.729  1.00 78.39  ?  169 ARG A O   1 
ATOM   9205  C CB  . ARG D 1 153 ? 7.421   77.732  46.467  1.00 74.27  ?  169 ARG A CB  1 
ATOM   9206  C CG  . ARG D 1 153 ? 6.084   78.007  47.065  1.00 66.95  ?  169 ARG A CG  1 
ATOM   9207  C CD  . ARG D 1 153 ? 6.183   79.100  48.044  1.00 64.85  ?  169 ARG A CD  1 
ATOM   9208  N NE  . ARG D 1 153 ? 4.878   79.478  48.571  1.00 67.11  ?  169 ARG A NE  1 
ATOM   9209  C CZ  . ARG D 1 153 ? 4.241   78.826  49.538  1.00 65.04  ?  169 ARG A CZ  1 
ATOM   9210  N NH1 . ARG D 1 153 ? 4.707   77.664  50.019  1.00 55.34  ?  169 ARG A NH1 1 
ATOM   9211  N NH2 . ARG D 1 153 ? 3.115   79.359  50.042  1.00 61.44  ?  169 ARG A NH2 1 
ATOM   9212  N N   . SER D 1 154 ? 9.703   75.660  44.958  1.00 80.88  ?  170 SER A N   1 
ATOM   9213  C CA  . SER D 1 154 ? 10.727  75.651  43.914  1.00 84.28  ?  170 SER A CA  1 
ATOM   9214  C C   . SER D 1 154 ? 10.775  74.363  43.078  1.00 90.60  ?  170 SER A C   1 
ATOM   9215  O O   . SER D 1 154 ? 10.939  74.447  41.862  1.00 89.26  ?  170 SER A O   1 
ATOM   9216  C CB  . SER D 1 154 ? 12.102  75.936  44.524  1.00 86.92  ?  170 SER A CB  1 
ATOM   9217  O OG  . SER D 1 154 ? 12.623  74.800  45.170  1.00 97.85  ?  170 SER A OG  1 
ATOM   9218  N N   . GLU D 1 155 ? 10.669  73.166  43.664  1.00 105.14 ?  171 GLU A N   1 
ATOM   9219  C CA  . GLU D 1 155 ? 10.480  71.966  42.848  1.00 113.15 ?  171 GLU A CA  1 
ATOM   9220  C C   . GLU D 1 155 ? 9.136   72.001  42.117  1.00 107.87 ?  171 GLU A C   1 
ATOM   9221  O O   . GLU D 1 155 ? 9.078   71.904  40.888  1.00 109.03 ?  171 GLU A O   1 
ATOM   9222  C CB  . GLU D 1 155 ? 10.620  70.717  43.732  1.00 117.21 ?  171 GLU A CB  1 
ATOM   9223  C CG  . GLU D 1 155 ? 11.539  69.552  43.234  1.00 123.72 ?  171 GLU A CG  1 
ATOM   9224  C CD  . GLU D 1 155 ? 10.970  68.768  42.030  1.00 131.36 ?  171 GLU A CD  1 
ATOM   9225  O OE1 . GLU D 1 155 ? 9.766   68.401  42.076  1.00 124.93 ?  171 GLU A OE1 1 
ATOM   9226  O OE2 . GLU D 1 155 ? 11.719  68.499  41.061  1.00 135.47 -1 171 GLU A OE2 1 
ATOM   9227  N N   . VAL D 1 156 ? 8.037   72.143  42.848  1.00 92.25  ?  172 VAL A N   1 
ATOM   9228  C CA  . VAL D 1 156 ? 6.749   71.992  42.197  1.00 88.71  ?  172 VAL A CA  1 
ATOM   9229  C C   . VAL D 1 156 ? 6.265   73.282  41.534  1.00 82.77  ?  172 VAL A C   1 
ATOM   9230  O O   . VAL D 1 156 ? 5.634   73.238  40.475  1.00 78.96  ?  172 VAL A O   1 
ATOM   9231  C CB  . VAL D 1 156 ? 5.762   71.448  43.236  1.00 83.96  ?  172 VAL A CB  1 
ATOM   9232  C CG1 . VAL D 1 156 ? 4.487   71.022  42.594  1.00 77.46  ?  172 VAL A CG1 1 
ATOM   9233  C CG2 . VAL D 1 156 ? 6.413   70.241  43.873  1.00 88.52  ?  172 VAL A CG2 1 
ATOM   9234  N N   . GLY D 1 157 ? 6.586   74.445  42.083  1.00 81.14  ?  173 GLY A N   1 
ATOM   9235  C CA  . GLY D 1 157 ? 6.011   75.655  41.534  1.00 78.93  ?  173 GLY A CA  1 
ATOM   9236  C C   . GLY D 1 157 ? 6.692   76.194  40.304  1.00 81.07  ?  173 GLY A C   1 
ATOM   9237  O O   . GLY D 1 157 ? 6.096   76.981  39.567  1.00 79.92  ?  173 GLY A O   1 
ATOM   9238  N N   . LYS D 1 158 ? 7.944   75.827  40.080  1.00 80.50  ?  174 LYS A N   1 
ATOM   9239  C CA  . LYS D 1 158 ? 8.660   76.376  38.942  1.00 81.88  ?  174 LYS A CA  1 
ATOM   9240  C C   . LYS D 1 158 ? 8.201   75.670  37.683  1.00 80.95  ?  174 LYS A C   1 
ATOM   9241  O O   . LYS D 1 158 ? 7.973   76.304  36.647  1.00 80.41  ?  174 LYS A O   1 
ATOM   9242  C CB  . LYS D 1 158 ? 10.166  76.195  39.136  1.00 90.61  ?  174 LYS A CB  1 
ATOM   9243  C CG  . LYS D 1 158 ? 10.834  77.258  39.980  1.00 86.84  ?  174 LYS A CG  1 
ATOM   9244  C CD  . LYS D 1 158 ? 12.185  76.755  40.498  1.00 91.42  ?  174 LYS A CD  1 
ATOM   9245  C CE  . LYS D 1 158 ? 12.810  77.728  41.490  1.00 93.33  ?  174 LYS A CE  1 
ATOM   9246  N NZ  . LYS D 1 158 ? 13.602  78.824  40.882  1.00 90.04  ?  174 LYS A NZ  1 
ATOM   9247  N N   . GLN D 1 159 ? 8.077   74.342  37.767  1.00 76.45  ?  175 GLN A N   1 
ATOM   9248  C CA  . GLN D 1 159 ? 7.375   73.579  36.756  1.00 78.97  ?  175 GLN A CA  1 
ATOM   9249  C C   . GLN D 1 159 ? 6.115   74.315  36.310  1.00 79.24  ?  175 GLN A C   1 
ATOM   9250  O O   . GLN D 1 159 ? 5.928   74.582  35.116  1.00 77.74  ?  175 GLN A O   1 
ATOM   9251  C CB  . GLN D 1 159 ? 7.045   72.185  37.306  1.00 78.47  ?  175 GLN A CB  1 
ATOM   9252  C CG  . GLN D 1 159 ? 8.231   71.331  37.721  1.00 77.73  ?  175 GLN A CG  1 
ATOM   9253  C CD  . GLN D 1 159 ? 7.822   69.924  38.173  1.00 85.69  ?  175 GLN A CD  1 
ATOM   9254  O OE1 . GLN D 1 159 ? 7.023   69.246  37.521  1.00 85.76  ?  175 GLN A OE1 1 
ATOM   9255  N NE2 . GLN D 1 159 ? 8.404   69.469  39.272  1.00 99.24  ?  175 GLN A NE2 1 
ATOM   9256  N N   . LEU D 1 160 ? 5.273   74.719  37.269  1.00 78.24  ?  176 LEU A N   1 
ATOM   9257  C CA  . LEU D 1 160 ? 3.932   75.209  36.960  1.00 73.64  ?  176 LEU A CA  1 
ATOM   9258  C C   . LEU D 1 160 ? 3.913   76.592  36.334  1.00 73.70  ?  176 LEU A C   1 
ATOM   9259  O O   . LEU D 1 160 ? 2.834   77.038  35.945  1.00 74.81  ?  176 LEU A O   1 
ATOM   9260  C CB  . LEU D 1 160 ? 3.065   75.278  38.213  1.00 72.80  ?  176 LEU A CB  1 
ATOM   9261  C CG  . LEU D 1 160 ? 2.739   73.989  38.956  1.00 71.81  ?  176 LEU A CG  1 
ATOM   9262  C CD1 . LEU D 1 160 ? 2.153   74.317  40.326  1.00 64.62  ?  176 LEU A CD1 1 
ATOM   9263  C CD2 . LEU D 1 160 ? 1.854   73.090  38.138  1.00 72.04  ?  176 LEU A CD2 1 
ATOM   9264  N N   . ARG D 1 161 ? 5.060   77.281  36.232  1.00 77.18  ?  177 ARG A N   1 
ATOM   9265  C CA  . ARG D 1 161 ? 5.037   78.694  35.845  1.00 79.92  ?  177 ARG A CA  1 
ATOM   9266  C C   . ARG D 1 161 ? 4.633   78.926  34.395  1.00 83.46  ?  177 ARG A C   1 
ATOM   9267  O O   . ARG D 1 161 ? 3.640   79.643  34.148  1.00 84.20  ?  177 ARG A O   1 
ATOM   9268  C CB  . ARG D 1 161 ? 6.385   79.337  36.168  1.00 83.67  ?  177 ARG A CB  1 
ATOM   9269  C CG  . ARG D 1 161 ? 6.520   80.778  35.698  1.00 85.38  ?  177 ARG A CG  1 
ATOM   9270  C CD  . ARG D 1 161 ? 5.489   81.724  36.309  1.00 84.99  ?  177 ARG A CD  1 
ATOM   9271  N NE  . ARG D 1 161 ? 5.510   83.016  35.625  1.00 85.37  ?  177 ARG A NE  1 
ATOM   9272  C CZ  . ARG D 1 161 ? 5.830   84.181  36.171  1.00 82.57  ?  177 ARG A CZ  1 
ATOM   9273  N NH1 . ARG D 1 161 ? 6.166   84.282  37.444  1.00 80.41  ?  177 ARG A NH1 1 
ATOM   9274  N NH2 . ARG D 1 161 ? 5.795   85.275  35.419  1.00 85.27  ?  177 ARG A NH2 1 
ATOM   9275  N N   . PRO D 1 162 ? 5.348   78.400  33.396  1.00 88.13  ?  178 PRO A N   1 
ATOM   9276  C CA  . PRO D 1 162 ? 4.883   78.601  32.013  1.00 89.77  ?  178 PRO A CA  1 
ATOM   9277  C C   . PRO D 1 162 ? 3.504   78.012  31.758  1.00 87.15  ?  178 PRO A C   1 
ATOM   9278  O O   . PRO D 1 162 ? 2.709   78.609  31.016  1.00 89.16  ?  178 PRO A O   1 
ATOM   9279  C CB  . PRO D 1 162 ? 5.974   77.905  31.184  1.00 94.13  ?  178 PRO A CB  1 
ATOM   9280  C CG  . PRO D 1 162 ? 6.515   76.865  32.106  1.00 91.76  ?  178 PRO A CG  1 
ATOM   9281  C CD  . PRO D 1 162 ? 6.549   77.543  33.435  1.00 86.32  ?  178 PRO A CD  1 
ATOM   9282  N N   . LEU D 1 163 ? 3.208   76.841  32.338  1.00 80.39  ?  179 LEU A N   1 
ATOM   9283  C CA  . LEU D 1 163 ? 1.884   76.252  32.190  1.00 78.51  ?  179 LEU A CA  1 
ATOM   9284  C C   . LEU D 1 163 ? 0.805   77.233  32.634  1.00 80.46  ?  179 LEU A C   1 
ATOM   9285  O O   . LEU D 1 163 ? -0.229  77.364  31.972  1.00 83.31  ?  179 LEU A O   1 
ATOM   9286  C CB  . LEU D 1 163 ? 1.801   74.951  32.987  1.00 73.87  ?  179 LEU A CB  1 
ATOM   9287  C CG  . LEU D 1 163 ? 2.773   73.879  32.495  1.00 71.61  ?  179 LEU A CG  1 
ATOM   9288  C CD1 . LEU D 1 163 ? 2.950   72.760  33.533  1.00 71.59  ?  179 LEU A CD1 1 
ATOM   9289  C CD2 . LEU D 1 163 ? 2.356   73.342  31.146  1.00 67.62  ?  179 LEU A CD2 1 
ATOM   9290  N N   . TYR D 1 164 ? 1.042   77.972  33.729  1.00 81.25  ?  180 TYR A N   1 
ATOM   9291  C CA  . TYR D 1 164 ? 0.028   78.918  34.185  1.00 78.43  ?  180 TYR A CA  1 
ATOM   9292  C C   . TYR D 1 164 ? -0.024  80.146  33.304  1.00 78.23  ?  180 TYR A C   1 
ATOM   9293  O O   . TYR D 1 164 ? -1.084  80.768  33.173  1.00 76.92  ?  180 TYR A O   1 
ATOM   9294  C CB  . TYR D 1 164 ? 0.291   79.373  35.606  1.00 75.72  ?  180 TYR A CB  1 
ATOM   9295  C CG  . TYR D 1 164 ? -0.954  79.830  36.356  1.00 74.73  ?  180 TYR A CG  1 
ATOM   9296  C CD1 . TYR D 1 164 ? -1.900  78.911  36.790  1.00 75.62  ?  180 TYR A CD1 1 
ATOM   9297  C CD2 . TYR D 1 164 ? -1.213  81.187  36.571  1.00 71.35  ?  180 TYR A CD2 1 
ATOM   9298  C CE1 . TYR D 1 164 ? -3.031  79.322  37.481  1.00 74.52  ?  180 TYR A CE1 1 
ATOM   9299  C CE2 . TYR D 1 164 ? -2.337  81.606  37.249  1.00 67.83  ?  180 TYR A CE2 1 
ATOM   9300  C CZ  . TYR D 1 164 ? -3.249  80.666  37.703  1.00 71.47  ?  180 TYR A CZ  1 
ATOM   9301  O OH  . TYR D 1 164 ? -4.399  81.040  38.376  1.00 71.91  ?  180 TYR A OH  1 
ATOM   9302  N N   . GLU D 1 165 ? 1.108   80.530  32.720  1.00 79.35  ?  181 GLU A N   1 
ATOM   9303  C CA  . GLU D 1 165 ? 1.077   81.600  31.727  1.00 85.19  ?  181 GLU A CA  1 
ATOM   9304  C C   . GLU D 1 165 ? 0.149   81.227  30.559  1.00 86.24  ?  181 GLU A C   1 
ATOM   9305  O O   . GLU D 1 165 ? -0.794  81.959  30.213  1.00 84.48  ?  181 GLU A O   1 
ATOM   9306  C CB  . GLU D 1 165 ? 2.499   81.870  31.225  1.00 88.47  ?  181 GLU A CB  1 
ATOM   9307  C CG  . GLU D 1 165 ? 3.538   82.214  32.295  1.00 87.37  ?  181 GLU A CG  1 
ATOM   9308  C CD  . GLU D 1 165 ? 4.875   82.677  31.694  1.00 95.68  ?  181 GLU A CD  1 
ATOM   9309  O OE1 . GLU D 1 165 ? 5.052   82.515  30.464  1.00 102.55 ?  181 GLU A OE1 1 
ATOM   9310  O OE2 . GLU D 1 165 ? 5.754   83.185  32.436  1.00 94.94  -1 181 GLU A OE2 1 
ATOM   9311  N N   . GLU D 1 166 ? 0.422   80.076  29.931  1.00 86.45  ?  182 GLU A N   1 
ATOM   9312  C CA  . GLU D 1 166 ? -0.386  79.617  28.806  1.00 87.83  ?  182 GLU A CA  1 
ATOM   9313  C C   . GLU D 1 166 ? -1.837  79.418  29.226  1.00 86.97  ?  182 GLU A C   1 
ATOM   9314  O O   . GLU D 1 166 ? -2.760  79.628  28.425  1.00 87.34  ?  182 GLU A O   1 
ATOM   9315  C CB  . GLU D 1 166 ? 0.201   78.318  28.231  1.00 91.49  ?  182 GLU A CB  1 
ATOM   9316  C CG  . GLU D 1 166 ? -0.399  77.854  26.880  1.00 103.41 ?  182 GLU A CG  1 
ATOM   9317  C CD  . GLU D 1 166 ? 0.286   76.608  26.275  1.00 109.58 ?  182 GLU A CD  1 
ATOM   9318  O OE1 . GLU D 1 166 ? 1.459   76.365  26.621  1.00 102.05 ?  182 GLU A OE1 1 
ATOM   9319  O OE2 . GLU D 1 166 ? -0.362  75.857  25.488  1.00 116.62 -1 182 GLU A OE2 1 
ATOM   9320  N N   . TYR D 1 167 ? -2.052  79.037  30.487  1.00 85.14  ?  183 TYR A N   1 
ATOM   9321  C CA  . TYR D 1 167 ? -3.399  78.848  31.006  1.00 82.67  ?  183 TYR A CA  1 
ATOM   9322  C C   . TYR D 1 167 ? -4.140  80.174  31.120  1.00 82.47  ?  183 TYR A C   1 
ATOM   9323  O O   . TYR D 1 167 ? -5.336  80.247  30.805  1.00 87.13  ?  183 TYR A O   1 
ATOM   9324  C CB  . TYR D 1 167 ? -3.301  78.133  32.350  1.00 78.29  ?  183 TYR A CB  1 
ATOM   9325  C CG  . TYR D 1 167 ? -4.443  78.318  33.314  1.00 76.06  ?  183 TYR A CG  1 
ATOM   9326  C CD1 . TYR D 1 167 ? -4.446  79.384  34.206  1.00 75.37  ?  183 TYR A CD1 1 
ATOM   9327  C CD2 . TYR D 1 167 ? -5.448  77.386  33.420  1.00 79.31  ?  183 TYR A CD2 1 
ATOM   9328  C CE1 . TYR D 1 167 ? -5.451  79.564  35.117  1.00 70.88  ?  183 TYR A CE1 1 
ATOM   9329  C CE2 . TYR D 1 167 ? -6.461  77.554  34.348  1.00 77.09  ?  183 TYR A CE2 1 
ATOM   9330  C CZ  . TYR D 1 167 ? -6.444  78.650  35.191  1.00 69.58  ?  183 TYR A CZ  1 
ATOM   9331  O OH  . TYR D 1 167 ? -7.427  78.838  36.119  1.00 71.53  ?  183 TYR A OH  1 
ATOM   9332  N N   . VAL D 1 168 ? -3.456  81.241  31.539  1.00 86.38  ?  184 VAL A N   1 
ATOM   9333  C CA  . VAL D 1 168 ? -4.133  82.531  31.572  1.00 86.37  ?  184 VAL A CA  1 
ATOM   9334  C C   . VAL D 1 168 ? -4.465  82.980  30.158  1.00 91.16  ?  184 VAL A C   1 
ATOM   9335  O O   . VAL D 1 168 ? -5.553  83.504  29.899  1.00 94.88  ?  184 VAL A O   1 
ATOM   9336  C CB  . VAL D 1 168 ? -3.283  83.575  32.298  1.00 85.08  ?  184 VAL A CB  1 
ATOM   9337  C CG1 . VAL D 1 168 ? -3.955  84.927  32.187  1.00 83.33  ?  184 VAL A CG1 1 
ATOM   9338  C CG2 . VAL D 1 168 ? -3.073  83.177  33.736  1.00 82.93  ?  184 VAL A CG2 1 
ATOM   9339  N N   . VAL D 1 169 ? -3.545  82.748  29.216  1.00 89.79  ?  185 VAL A N   1 
ATOM   9340  C CA  . VAL D 1 169 ? -3.785  83.104  27.811  1.00 94.04  ?  185 VAL A CA  1 
ATOM   9341  C C   . VAL D 1 169 ? -5.045  82.424  27.267  1.00 96.72  ?  185 VAL A C   1 
ATOM   9342  O O   . VAL D 1 169 ? -5.975  83.081  26.764  1.00 98.58  ?  185 VAL A O   1 
ATOM   9343  C CB  . VAL D 1 169 ? -2.561  82.749  26.951  1.00 92.65  ?  185 VAL A CB  1 
ATOM   9344  C CG1 . VAL D 1 169 ? -2.922  82.838  25.483  1.00 102.29 ?  185 VAL A CG1 1 
ATOM   9345  C CG2 . VAL D 1 169 ? -1.414  83.682  27.268  1.00 91.40  ?  185 VAL A CG2 1 
ATOM   9346  N N   . LEU D 1 170 ? -5.084  81.090  27.340  1.00 90.61  ?  186 LEU A N   1 
ATOM   9347  C CA  . LEU D 1 170 ? -6.222  80.361  26.786  1.00 93.30  ?  186 LEU A CA  1 
ATOM   9348  C C   . LEU D 1 170 ? -7.519  80.703  27.501  1.00 94.81  ?  186 LEU A C   1 
ATOM   9349  O O   . LEU D 1 170 ? -8.541  80.949  26.846  1.00 96.06  ?  186 LEU A O   1 
ATOM   9350  C CB  . LEU D 1 170 ? -5.967  78.863  26.827  1.00 90.25  ?  186 LEU A CB  1 
ATOM   9351  C CG  . LEU D 1 170 ? -4.949  78.465  25.781  1.00 86.91  ?  186 LEU A CG  1 
ATOM   9352  C CD1 . LEU D 1 170 ? -4.266  77.188  26.139  1.00 93.74  ?  186 LEU A CD1 1 
ATOM   9353  C CD2 . LEU D 1 170 ? -5.743  78.266  24.542  1.00 87.53  ?  186 LEU A CD2 1 
ATOM   9354  N N   . LYS D 1 171 ? -7.520  80.663  28.840  1.00 92.32  ?  187 LYS A N   1 
ATOM   9355  C CA  . LYS D 1 171 ? -8.744  80.969  29.570  1.00 87.93  ?  187 LYS A CA  1 
ATOM   9356  C C   . LYS D 1 171 ? -9.244  82.364  29.239  1.00 91.38  ?  187 LYS A C   1 
ATOM   9357  O O   . LYS D 1 171 ? -10.455 82.596  29.165  1.00 93.82  ?  187 LYS A O   1 
ATOM   9358  C CB  . LYS D 1 171 ? -8.507  80.821  31.067  1.00 83.75  ?  187 LYS A CB  1 
ATOM   9359  C CG  . LYS D 1 171 ? -8.461  79.401  31.585  1.00 77.67  ?  187 LYS A CG  1 
ATOM   9360  C CD  . LYS D 1 171 ? -9.869  78.855  31.724  1.00 77.06  ?  187 LYS A CD  1 
ATOM   9361  C CE  . LYS D 1 171 ? -9.928  77.412  32.223  1.00 72.91  ?  187 LYS A CE  1 
ATOM   9362  N NZ  . LYS D 1 171 ? -11.332 76.984  32.574  1.00 69.97  ?  187 LYS A NZ  1 
ATOM   9363  N N   . ASN D 1 172 ? -8.333  83.304  29.012  1.00 90.61  ?  188 ASN A N   1 
ATOM   9364  C CA  . ASN D 1 172 ? -8.782  84.632  28.631  1.00 97.69  ?  188 ASN A CA  1 
ATOM   9365  C C   . ASN D 1 172 ? -9.434  84.628  27.253  1.00 102.69 ?  188 ASN A C   1 
ATOM   9366  O O   . ASN D 1 172 ? -10.496 85.234  27.072  1.00 106.33 ?  188 ASN A O   1 
ATOM   9367  C CB  . ASN D 1 172 ? -7.626  85.629  28.712  1.00 98.62  ?  188 ASN A CB  1 
ATOM   9368  C CG  . ASN D 1 172 ? -7.644  86.432  30.006  1.00 92.94  ?  188 ASN A CG  1 
ATOM   9369  O OD1 . ASN D 1 172 ? -8.672  86.519  30.695  1.00 87.59  ?  188 ASN A OD1 1 
ATOM   9370  N ND2 . ASN D 1 172 ? -6.504  87.025  30.341  1.00 98.07  ?  188 ASN A ND2 1 
ATOM   9371  N N   . GLU D 1 173 ? -8.845  83.950  26.266  1.00 103.24 ?  189 GLU A N   1 
ATOM   9372  C CA  . GLU D 1 173 ? -9.558  83.873  24.987  1.00 107.53 ?  189 GLU A CA  1 
ATOM   9373  C C   . GLU D 1 173 ? -10.942 83.253  25.170  1.00 104.36 ?  189 GLU A C   1 
ATOM   9374  O O   . GLU D 1 173 ? -11.951 83.819  24.729  1.00 106.78 ?  189 GLU A O   1 
ATOM   9375  C CB  . GLU D 1 173 ? -8.755  83.099  23.946  1.00 111.50 ?  189 GLU A CB  1 
ATOM   9376  C CG  . GLU D 1 173 ? -7.505  83.808  23.495  1.00 118.75 ?  189 GLU A CG  1 
ATOM   9377  C CD  . GLU D 1 173 ? -6.830  83.073  22.374  1.00 123.14 ?  189 GLU A CD  1 
ATOM   9378  O OE1 . GLU D 1 173 ? -7.534  82.269  21.707  1.00 119.67 ?  189 GLU A OE1 1 
ATOM   9379  O OE2 . GLU D 1 173 ? -5.608  83.283  22.185  1.00 125.88 -1 189 GLU A OE2 1 
ATOM   9380  N N   . MET D 1 174 ? -11.000 82.099  25.846  1.00 102.43 ?  190 MET A N   1 
ATOM   9381  C CA  . MET D 1 174 ? -12.259 81.405  26.111  1.00 99.81  ?  190 MET A CA  1 
ATOM   9382  C C   . MET D 1 174 ? -13.318 82.349  26.661  1.00 101.44 ?  190 MET A C   1 
ATOM   9383  O O   . MET D 1 174 ? -14.448 82.379  26.171  1.00 104.59 ?  190 MET A O   1 
ATOM   9384  C CB  . MET D 1 174 ? -11.992 80.259  27.090  1.00 96.12  ?  190 MET A CB  1 
ATOM   9385  C CG  . MET D 1 174 ? -13.170 79.386  27.540  1.00 97.18  ?  190 MET A CG  1 
ATOM   9386  S SD  . MET D 1 174 ? -14.056 80.036  28.982  1.00 96.17  ?  190 MET A SD  1 
ATOM   9387  C CE  . MET D 1 174 ? -14.405 78.513  29.884  1.00 92.85  ?  190 MET A CE  1 
ATOM   9388  N N   . ALA D 1 175 ? -12.969 83.130  27.683  1.00 103.50 ?  191 ALA A N   1 
ATOM   9389  C CA  . ALA D 1 175 ? -13.948 84.027  28.292  1.00 101.39 ?  191 ALA A CA  1 
ATOM   9390  C C   . ALA D 1 175 ? -14.317 85.170  27.359  1.00 110.30 ?  191 ALA A C   1 
ATOM   9391  O O   . ALA D 1 175 ? -15.499 85.524  27.251  1.00 110.07 ?  191 ALA A O   1 
ATOM   9392  C CB  . ALA D 1 175 ? -13.412 84.577  29.607  1.00 97.87  ?  191 ALA A CB  1 
ATOM   9393  N N   . ARG D 1 176 ? -13.321 85.781  26.698  1.00 118.39 ?  192 ARG A N   1 
ATOM   9394  C CA  . ARG D 1 176 ? -13.610 86.888  25.789  1.00 116.30 ?  192 ARG A CA  1 
ATOM   9395  C C   . ARG D 1 176 ? -14.598 86.464  24.704  1.00 116.61 ?  192 ARG A C   1 
ATOM   9396  O O   . ARG D 1 176 ? -15.456 87.260  24.302  1.00 117.00 ?  192 ARG A O   1 
ATOM   9397  C CB  . ARG D 1 176 ? -12.307 87.437  25.174  1.00 115.52 ?  192 ARG A CB  1 
ATOM   9398  C CG  . ARG D 1 176 ? -11.283 87.981  26.198  1.00 114.19 ?  192 ARG A CG  1 
ATOM   9399  C CD  . ARG D 1 176 ? -9.960  88.490  25.585  1.00 115.32 ?  192 ARG A CD  1 
ATOM   9400  N NE  . ARG D 1 176 ? -8.809  88.410  26.490  1.00 117.99 ?  192 ARG A NE  1 
ATOM   9401  C CZ  . ARG D 1 176 ? -8.516  89.286  27.453  1.00 117.90 ?  192 ARG A CZ  1 
ATOM   9402  N NH1 . ARG D 1 176 ? -9.340  90.273  27.770  1.00 119.46 ?  192 ARG A NH1 1 
ATOM   9403  N NH2 . ARG D 1 176 ? -7.368  89.166  28.123  1.00 111.42 ?  192 ARG A NH2 1 
ATOM   9404  N N   . ALA D 1 177 ? -14.518 85.204  24.252  1.00 113.84 ?  193 ALA A N   1 
ATOM   9405  C CA  . ALA D 1 177 ? -15.419 84.714  23.212  1.00 110.16 ?  193 ALA A CA  1 
ATOM   9406  C C   . ALA D 1 177 ? -16.842 84.517  23.723  1.00 114.04 ?  193 ALA A C   1 
ATOM   9407  O O   . ALA D 1 177 ? -17.791 84.609  22.936  1.00 115.99 ?  193 ALA A O   1 
ATOM   9408  C CB  . ALA D 1 177 ? -14.894 83.404  22.631  1.00 106.24 ?  193 ALA A CB  1 
ATOM   9409  N N   . ASN D 1 178 ? -17.016 84.223  25.013  1.00 110.04 ?  194 ASN A N   1 
ATOM   9410  C CA  . ASN D 1 178 ? -18.345 84.119  25.608  1.00 110.20 ?  194 ASN A CA  1 
ATOM   9411  C C   . ASN D 1 178 ? -18.886 85.455  26.104  1.00 111.85 ?  194 ASN A C   1 
ATOM   9412  O O   . ASN D 1 178 ? -19.901 85.479  26.815  1.00 109.61 ?  194 ASN A O   1 
ATOM   9413  C CB  . ASN D 1 178 ? -18.344 83.103  26.746  1.00 100.96 ?  194 ASN A CB  1 
ATOM   9414  C CG  . ASN D 1 178 ? -18.404 81.686  26.244  1.00 104.45 ?  194 ASN A CG  1 
ATOM   9415  O OD1 . ASN D 1 178 ? -17.456 80.918  26.392  1.00 107.62 ?  194 ASN A OD1 1 
ATOM   9416  N ND2 . ASN D 1 178 ? -19.527 81.329  25.632  1.00 107.15 ?  194 ASN A ND2 1 
ATOM   9417  N N   . HIS D 1 179 ? -18.232 86.559  25.734  1.00 116.30 ?  195 HIS A N   1 
ATOM   9418  C CA  . HIS D 1 179 ? -18.717 87.910  25.987  1.00 114.87 ?  195 HIS A CA  1 
ATOM   9419  C C   . HIS D 1 179 ? -18.608 88.294  27.445  1.00 106.29 ?  195 HIS A C   1 
ATOM   9420  O O   . HIS D 1 179 ? -19.399 89.088  27.957  1.00 106.89 ?  195 HIS A O   1 
ATOM   9421  C CB  . HIS D 1 179 ? -20.147 88.096  25.481  1.00 119.97 ?  195 HIS A CB  1 
ATOM   9422  C CG  . HIS D 1 179 ? -20.329 87.661  24.066  1.00 118.95 ?  195 HIS A CG  1 
ATOM   9423  N ND1 . HIS D 1 179 ? -21.025 86.524  23.723  1.00 122.76 ?  195 HIS A ND1 1 
ATOM   9424  C CD2 . HIS D 1 179 ? -19.925 88.225  22.904  1.00 122.62 ?  195 HIS A CD2 1 
ATOM   9425  C CE1 . HIS D 1 179 ? -21.029 86.396  22.411  1.00 128.36 ?  195 HIS A CE1 1 
ATOM   9426  N NE2 . HIS D 1 179 ? -20.372 87.416  21.890  1.00 128.73 ?  195 HIS A NE2 1 
ATOM   9427  N N   . TYR D 1 180 ? -17.627 87.728  28.123  1.00 102.31 ?  196 TYR A N   1 
ATOM   9428  C CA  . TYR D 1 180 ? -17.161 88.283  29.373  1.00 98.26  ?  196 TYR A CA  1 
ATOM   9429  C C   . TYR D 1 180 ? -15.855 89.016  29.071  1.00 97.98  ?  196 TYR A C   1 
ATOM   9430  O O   . TYR D 1 180 ? -15.218 88.756  28.046  1.00 102.11 ?  196 TYR A O   1 
ATOM   9431  C CB  . TYR D 1 180 ? -16.956 87.195  30.437  1.00 90.69  ?  196 TYR A CB  1 
ATOM   9432  C CG  . TYR D 1 180 ? -18.188 86.405  30.916  1.00 83.63  ?  196 TYR A CG  1 
ATOM   9433  C CD1 . TYR D 1 180 ? -18.599 85.227  30.288  1.00 81.91  ?  196 TYR A CD1 1 
ATOM   9434  C CD2 . TYR D 1 180 ? -18.955 86.872  31.983  1.00 80.97  ?  196 TYR A CD2 1 
ATOM   9435  C CE1 . TYR D 1 180 ? -19.699 84.501  30.764  1.00 74.75  ?  196 TYR A CE1 1 
ATOM   9436  C CE2 . TYR D 1 180 ? -20.070 86.172  32.448  1.00 77.17  ?  196 TYR A CE2 1 
ATOM   9437  C CZ  . TYR D 1 180 ? -20.435 84.989  31.840  1.00 74.13  ?  196 TYR A CZ  1 
ATOM   9438  O OH  . TYR D 1 180 ? -21.524 84.307  32.332  1.00 67.62  ?  196 TYR A OH  1 
ATOM   9439  N N   . GLU D 1 181 ? -15.468 89.969  29.939  1.00 92.82  ?  197 GLU A N   1 
ATOM   9440  C CA  . GLU D 1 181 ? -14.302 90.779  29.584  1.00 91.18  ?  197 GLU A CA  1 
ATOM   9441  C C   . GLU D 1 181 ? -12.983 90.064  29.848  1.00 95.17  ?  197 GLU A C   1 
ATOM   9442  O O   . GLU D 1 181 ? -11.988 90.378  29.187  1.00 96.67  ?  197 GLU A O   1 
ATOM   9443  C CB  . GLU D 1 181 ? -14.318 92.154  30.271  1.00 89.97  ?  197 GLU A CB  1 
ATOM   9444  C CG  . GLU D 1 181 ? -14.377 92.190  31.783  1.00 98.37  ?  197 GLU A CG  1 
ATOM   9445  C CD  . GLU D 1 181 ? -14.986 93.490  32.312  1.00 102.11 ?  197 GLU A CD  1 
ATOM   9446  O OE1 . GLU D 1 181 ? -15.866 94.050  31.627  1.00 98.45  ?  197 GLU A OE1 1 
ATOM   9447  O OE2 . GLU D 1 181 ? -14.572 93.963  33.400  1.00 105.87 -1 197 GLU A OE2 1 
ATOM   9448  N N   . ASP D 1 182 ? -12.964 89.093  30.764  1.00 97.12  ?  198 ASP A N   1 
ATOM   9449  C CA  . ASP D 1 182 ? -11.782 88.291  31.090  1.00 93.69  ?  198 ASP A CA  1 
ATOM   9450  C C   . ASP D 1 182 ? -12.246 87.060  31.857  1.00 88.99  ?  198 ASP A C   1 
ATOM   9451  O O   . ASP D 1 182 ? -13.435 86.895  32.133  1.00 89.30  ?  198 ASP A O   1 
ATOM   9452  C CB  . ASP D 1 182 ? -10.736 89.105  31.871  1.00 92.43  ?  198 ASP A CB  1 
ATOM   9453  C CG  . ASP D 1 182 ? -11.301 89.751  33.142  1.00 91.96  ?  198 ASP A CG  1 
ATOM   9454  O OD1 . ASP D 1 182 ? -11.642 89.019  34.099  1.00 91.17  ?  198 ASP A OD1 1 
ATOM   9455  O OD2 . ASP D 1 182 ? -11.367 91.010  33.187  1.00 92.20  -1 198 ASP A OD2 1 
ATOM   9456  N N   . TYR D 1 183 ? -11.301 86.179  32.183  1.00 78.77  ?  199 TYR A N   1 
ATOM   9457  C CA  . TYR D 1 183 ? -11.680 84.970  32.906  1.00 75.11  ?  199 TYR A CA  1 
ATOM   9458  C C   . TYR D 1 183 ? -12.117 85.279  34.331  1.00 76.29  ?  199 TYR A C   1 
ATOM   9459  O O   . TYR D 1 183 ? -12.999 84.595  34.865  1.00 75.46  ?  199 TYR A O   1 
ATOM   9460  C CB  . TYR D 1 183 ? -10.529 83.981  32.900  1.00 73.95  ?  199 TYR A CB  1 
ATOM   9461  C CG  . TYR D 1 183 ? -10.838 82.604  33.422  1.00 71.69  ?  199 TYR A CG  1 
ATOM   9462  C CD1 . TYR D 1 183 ? -11.989 81.933  33.046  1.00 71.58  ?  199 TYR A CD1 1 
ATOM   9463  C CD2 . TYR D 1 183 ? -9.932  81.942  34.240  1.00 73.02  ?  199 TYR A CD2 1 
ATOM   9464  C CE1 . TYR D 1 183 ? -12.247 80.651  33.503  1.00 68.88  ?  199 TYR A CE1 1 
ATOM   9465  C CE2 . TYR D 1 183 ? -10.170 80.671  34.699  1.00 70.37  ?  199 TYR A CE2 1 
ATOM   9466  C CZ  . TYR D 1 183 ? -11.327 80.029  34.332  1.00 70.33  ?  199 TYR A CZ  1 
ATOM   9467  O OH  . TYR D 1 183 ? -11.543 78.754  34.793  1.00 71.19  ?  199 TYR A OH  1 
ATOM   9468  N N   . GLY D 1 184 ? -11.541 86.314  34.955  1.00 73.26  ?  200 GLY A N   1 
ATOM   9469  C CA  . GLY D 1 184 ? -12.045 86.755  36.249  1.00 72.59  ?  200 GLY A CA  1 
ATOM   9470  C C   . GLY D 1 184 ? -13.509 87.157  36.195  1.00 73.46  ?  200 GLY A C   1 
ATOM   9471  O O   . GLY D 1 184 ? -14.306 86.808  37.076  1.00 68.81  ?  200 GLY A O   1 
ATOM   9472  N N   . ASP D 1 185 ? -13.889 87.873  35.142  1.00 78.31  ?  201 ASP A N   1 
ATOM   9473  C CA  . ASP D 1 185 ? -15.270 88.304  34.985  1.00 75.83  ?  201 ASP A CA  1 
ATOM   9474  C C   . ASP D 1 185 ? -16.174 87.090  34.766  1.00 72.70  ?  201 ASP A C   1 
ATOM   9475  O O   . ASP D 1 185 ? -17.245 86.979  35.381  1.00 71.77  ?  201 ASP A O   1 
ATOM   9476  C CB  . ASP D 1 185 ? -15.315 89.320  33.825  1.00 80.92  ?  201 ASP A CB  1 
ATOM   9477  C CG  . ASP D 1 185 ? -16.665 90.033  33.658  1.00 82.74  ?  201 ASP A CG  1 
ATOM   9478  O OD1 . ASP D 1 185 ? -17.318 90.353  34.678  1.00 83.39  ?  201 ASP A OD1 1 
ATOM   9479  O OD2 . ASP D 1 185 ? -17.016 90.374  32.502  1.00 81.76  -1 201 ASP A OD2 1 
ATOM   9480  N N   . TYR D 1 186 ? -15.731 86.150  33.923  1.00 70.94  ?  202 TYR A N   1 
ATOM   9481  C CA  . TYR D 1 186 ? -16.428 84.879  33.764  1.00 67.15  ?  202 TYR A CA  1 
ATOM   9482  C C   . TYR D 1 186 ? -16.739 84.262  35.124  1.00 68.98  ?  202 TYR A C   1 
ATOM   9483  O O   . TYR D 1 186 ? -17.902 83.975  35.422  1.00 70.65  ?  202 TYR A O   1 
ATOM   9484  C CB  . TYR D 1 186 ? -15.593 83.935  32.883  1.00 71.02  ?  202 TYR A CB  1 
ATOM   9485  C CG  . TYR D 1 186 ? -16.148 82.533  32.635  1.00 72.66  ?  202 TYR A CG  1 
ATOM   9486  C CD1 . TYR D 1 186 ? -15.985 81.531  33.583  1.00 75.31  ?  202 TYR A CD1 1 
ATOM   9487  C CD2 . TYR D 1 186 ? -16.778 82.196  31.437  1.00 79.35  ?  202 TYR A CD2 1 
ATOM   9488  C CE1 . TYR D 1 186 ? -16.473 80.252  33.379  1.00 81.08  ?  202 TYR A CE1 1 
ATOM   9489  C CE2 . TYR D 1 186 ? -17.265 80.908  31.217  1.00 83.72  ?  202 TYR A CE2 1 
ATOM   9490  C CZ  . TYR D 1 186 ? -17.109 79.940  32.198  1.00 85.91  ?  202 TYR A CZ  1 
ATOM   9491  O OH  . TYR D 1 186 ? -17.582 78.654  32.014  1.00 87.07  ?  202 TYR A OH  1 
ATOM   9492  N N   . TRP D 1 187 ? -15.726 84.087  35.985  1.00 67.96  ?  203 TRP A N   1 
ATOM   9493  C CA  . TRP D 1 187 ? -15.998 83.452  37.270  1.00 63.89  ?  203 TRP A CA  1 
ATOM   9494  C C   . TRP D 1 187 ? -16.980 84.244  38.090  1.00 64.46  ?  203 TRP A C   1 
ATOM   9495  O O   . TRP D 1 187 ? -17.847 83.668  38.748  1.00 65.93  ?  203 TRP A O   1 
ATOM   9496  C CB  . TRP D 1 187 ? -14.763 83.314  38.108  1.00 66.93  ?  203 TRP A CB  1 
ATOM   9497  C CG  . TRP D 1 187 ? -14.010 82.187  37.802  1.00 69.12  ?  203 TRP A CG  1 
ATOM   9498  C CD1 . TRP D 1 187 ? -14.384 81.143  37.035  1.00 68.72  ?  203 TRP A CD1 1 
ATOM   9499  C CD2 . TRP D 1 187 ? -12.753 81.863  38.372  1.00 70.84  ?  203 TRP A CD2 1 
ATOM   9500  N NE1 . TRP D 1 187 ? -13.384 80.206  37.014  1.00 69.50  ?  203 TRP A NE1 1 
ATOM   9501  C CE2 . TRP D 1 187 ? -12.373 80.621  37.843  1.00 69.58  ?  203 TRP A CE2 1 
ATOM   9502  C CE3 . TRP D 1 187 ? -11.892 82.524  39.259  1.00 69.56  ?  203 TRP A CE3 1 
ATOM   9503  C CZ2 . TRP D 1 187 ? -11.166 80.013  38.166  1.00 69.94  ?  203 TRP A CZ2 1 
ATOM   9504  C CZ3 . TRP D 1 187 ? -10.685 81.929  39.580  1.00 69.94  ?  203 TRP A CZ3 1 
ATOM   9505  C CH2 . TRP D 1 187 ? -10.336 80.680  39.034  1.00 72.32  ?  203 TRP A CH2 1 
ATOM   9506  N N   . ARG D 1 188 ? -16.807 85.563  38.136  1.00 68.09  ?  204 ARG A N   1 
ATOM   9507  C CA  . ARG D 1 188 ? -17.710 86.377  38.933  1.00 66.26  ?  204 ARG A CA  1 
ATOM   9508  C C   . ARG D 1 188 ? -19.124 86.288  38.378  1.00 65.73  ?  204 ARG A C   1 
ATOM   9509  O O   . ARG D 1 188 ? -20.080 86.685  39.045  1.00 66.40  ?  204 ARG A O   1 
ATOM   9510  C CB  . ARG D 1 188 ? -17.235 87.832  38.964  1.00 68.53  ?  204 ARG A CB  1 
ATOM   9511  C CG  . ARG D 1 188 ? -15.863 88.062  39.596  1.00 63.41  ?  204 ARG A CG  1 
ATOM   9512  C CD  . ARG D 1 188 ? -15.555 89.556  39.794  1.00 62.89  ?  204 ARG A CD  1 
ATOM   9513  N NE  . ARG D 1 188 ? -15.359 90.282  38.538  1.00 68.53  ?  204 ARG A NE  1 
ATOM   9514  C CZ  . ARG D 1 188 ? -14.261 90.266  37.789  1.00 72.08  ?  204 ARG A CZ  1 
ATOM   9515  N NH1 . ARG D 1 188 ? -13.211 89.530  38.109  1.00 72.61  ?  204 ARG A NH1 1 
ATOM   9516  N NH2 . ARG D 1 188 ? -14.208 91.018  36.691  1.00 76.49  ?  204 ARG A NH2 1 
ATOM   9517  N N   . GLY D 1 189 ? -19.297 85.582  37.274  1.00 64.96  ?  205 GLY A N   1 
ATOM   9518  C CA  . GLY D 1 189 ? -20.658 85.549  36.712  1.00 68.23  ?  205 GLY A CA  1 
ATOM   9519  C C   . GLY D 1 189 ? -21.645 84.822  37.610  1.00 68.38  ?  205 GLY A C   1 
ATOM   9520  O O   . GLY D 1 189 ? -22.837 85.112  37.554  1.00 68.16  ?  205 GLY A O   1 
ATOM   9521  N N   . ASP D 1 190 ? -21.168 83.864  38.385  1.00 64.60  ?  206 ASP A N   1 
ATOM   9522  C CA  . ASP D 1 190 ? -22.050 83.041  39.247  1.00 64.22  ?  206 ASP A CA  1 
ATOM   9523  C C   . ASP D 1 190 ? -22.958 83.938  40.071  1.00 62.63  ?  206 ASP A C   1 
ATOM   9524  O O   . ASP D 1 190 ? -24.086 83.512  40.388  1.00 64.32  ?  206 ASP A O   1 
ATOM   9525  C CB  . ASP D 1 190 ? -21.216 82.194  40.203  1.00 65.64  ?  206 ASP A CB  1 
ATOM   9526  C CG  . ASP D 1 190 ? -21.998 81.219  41.069  1.00 68.29  ?  206 ASP A CG  1 
ATOM   9527  O OD1 . ASP D 1 190 ? -22.581 81.668  42.081  1.00 64.38  -1 206 ASP A OD1 1 
ATOM   9528  O OD2 . ASP D 1 190 ? -21.996 80.028  40.742  1.00 72.58  ?  206 ASP A OD2 1 
ATOM   9529  N N   . TYR D 1 191 ? -22.466 85.099  40.488  1.00 61.75  ?  207 TYR A N   1 
ATOM   9530  C CA  . TYR D 1 191 ? -23.307 85.917  41.395  1.00 63.43  ?  207 TYR A CA  1 
ATOM   9531  C C   . TYR D 1 191 ? -24.113 86.925  40.583  1.00 64.20  ?  207 TYR A C   1 
ATOM   9532  O O   . TYR D 1 191 ? -24.500 87.946  41.175  1.00 66.64  ?  207 TYR A O   1 
ATOM   9533  C CB  . TYR D 1 191 ? -22.468 86.689  42.413  1.00 64.77  ?  207 TYR A CB  1 
ATOM   9534  C CG  . TYR D 1 191 ? -21.612 85.860  43.329  1.00 65.33  ?  207 TYR A CG  1 
ATOM   9535  C CD1 . TYR D 1 191 ? -20.318 85.541  42.969  1.00 64.55  ?  207 TYR A CD1 1 
ATOM   9536  C CD2 . TYR D 1 191 ? -22.089 85.404  44.546  1.00 61.27  ?  207 TYR A CD2 1 
ATOM   9537  C CE1 . TYR D 1 191 ? -19.512 84.783  43.793  1.00 62.36  ?  207 TYR A CE1 1 
ATOM   9538  C CE2 . TYR D 1 191 ? -21.295 84.643  45.386  1.00 60.18  ?  207 TYR A CE2 1 
ATOM   9539  C CZ  . TYR D 1 191 ? -20.000 84.334  45.006  1.00 60.93  ?  207 TYR A CZ  1 
ATOM   9540  O OH  . TYR D 1 191 ? -19.185 83.590  45.813  1.00 60.51  ?  207 TYR A OH  1 
ATOM   9541  N N   . GLU D 1 192 ? -24.297 86.687  39.280  1.00 63.77  ?  208 GLU A N   1 
ATOM   9542  C CA  . GLU D 1 192 ? -24.997 87.681  38.473  1.00 63.30  ?  208 GLU A CA  1 
ATOM   9543  C C   . GLU D 1 192 ? -26.513 87.509  38.529  1.00 63.51  ?  208 GLU A C   1 
ATOM   9544  O O   . GLU D 1 192 ? -27.012 86.388  38.625  1.00 65.82  ?  208 GLU A O   1 
ATOM   9545  C CB  . GLU D 1 192 ? -24.499 87.599  37.030  1.00 69.23  ?  208 GLU A CB  1 
ATOM   9546  C CG  . GLU D 1 192 ? -24.875 88.759  36.129  1.00 73.00  ?  208 GLU A CG  1 
ATOM   9547  C CD  . GLU D 1 192 ? -24.122 88.757  34.794  1.00 73.65  ?  208 GLU A CD  1 
ATOM   9548  O OE1 . GLU D 1 192 ? -23.384 87.779  34.479  1.00 69.08  ?  208 GLU A OE1 1 
ATOM   9549  O OE2 . GLU D 1 192 ? -24.334 89.725  34.034  1.00 79.08  -1 208 GLU A OE2 1 
ATOM   9550  N N   . VAL D 1 193 ? -27.245 88.630  38.497  1.00 70.38  ?  209 VAL A N   1 
ATOM   9551  C CA  . VAL D 1 193 ? -28.709 88.628  38.492  1.00 72.28  ?  209 VAL A CA  1 
ATOM   9552  C C   . VAL D 1 193 ? -29.204 89.748  37.581  1.00 81.21  ?  209 VAL A C   1 
ATOM   9553  O O   . VAL D 1 193 ? -28.895 90.924  37.816  1.00 81.83  ?  209 VAL A O   1 
ATOM   9554  C CB  . VAL D 1 193 ? -29.305 88.804  39.894  1.00 72.08  ?  209 VAL A CB  1 
ATOM   9555  C CG1 . VAL D 1 193 ? -30.785 88.984  39.803  1.00 73.68  ?  209 VAL A CG1 1 
ATOM   9556  C CG2 . VAL D 1 193 ? -29.007 87.600  40.740  1.00 75.44  ?  209 VAL A CG2 1 
ATOM   9557  N N   . ASN D 1 194 ? -30.023 89.394  36.576  1.00 76.60  ?  210 ASN A N   1 
ATOM   9558  C CA  . ASN D 1 194 ? -30.437 90.304  35.517  1.00 73.42  ?  210 ASN A CA  1 
ATOM   9559  C C   . ASN D 1 194 ? -31.959 90.399  35.407  1.00 80.81  ?  210 ASN A C   1 
ATOM   9560  O O   . ASN D 1 194 ? -32.670 89.393  35.507  1.00 78.99  ?  210 ASN A O   1 
ATOM   9561  C CB  . ASN D 1 194 ? -29.872 89.844  34.192  1.00 70.13  ?  210 ASN A CB  1 
ATOM   9562  C CG  . ASN D 1 194 ? -28.394 90.076  34.093  1.00 74.30  ?  210 ASN A CG  1 
ATOM   9563  O OD1 . ASN D 1 194 ? -27.933 91.216  34.080  1.00 78.00  ?  210 ASN A OD1 1 
ATOM   9564  N ND2 . ASN D 1 194 ? -27.635 88.992  33.979  1.00 76.54  ?  210 ASN A ND2 1 
ATOM   9565  N N   . GLY D 1 195 ? -32.452 91.621  35.185  1.00 85.51  ?  211 GLY A N   1 
ATOM   9566  C CA  . GLY D 1 195 ? -33.864 91.858  34.974  1.00 83.10  ?  211 GLY A CA  1 
ATOM   9567  C C   . GLY D 1 195 ? -34.777 91.212  35.993  1.00 86.56  ?  211 GLY A C   1 
ATOM   9568  O O   . GLY D 1 195 ? -35.657 90.424  35.634  1.00 85.77  ?  211 GLY A O   1 
ATOM   9569  N N   . VAL D 1 196 ? -34.550 91.502  37.271  1.00 90.03  ?  212 VAL A N   1 
ATOM   9570  C CA  . VAL D 1 196 ? -35.544 91.325  38.332  1.00 90.59  ?  212 VAL A CA  1 
ATOM   9571  C C   . VAL D 1 196 ? -35.525 92.630  39.116  1.00 98.36  ?  212 VAL A C   1 
ATOM   9572  O O   . VAL D 1 196 ? -34.614 92.855  39.916  1.00 95.39  ?  212 VAL A O   1 
ATOM   9573  C CB  . VAL D 1 196 ? -35.250 90.130  39.241  1.00 83.41  ?  212 VAL A CB  1 
ATOM   9574  C CG1 . VAL D 1 196 ? -36.417 89.875  40.165  1.00 83.86  ?  212 VAL A CG1 1 
ATOM   9575  C CG2 . VAL D 1 196 ? -34.981 88.891  38.426  1.00 83.11  ?  212 VAL A CG2 1 
ATOM   9576  N N   . ASP D 1 197 ? -36.501 93.512  38.879  1.00 101.91 ?  213 ASP A N   1 
ATOM   9577  C CA  . ASP D 1 197 ? -36.412 94.827  39.514  1.00 105.84 ?  213 ASP A CA  1 
ATOM   9578  C C   . ASP D 1 197 ? -36.276 94.729  41.023  1.00 106.73 ?  213 ASP A C   1 
ATOM   9579  O O   . ASP D 1 197 ? -37.197 94.260  41.694  1.00 104.53 ?  213 ASP A O   1 
ATOM   9580  C CB  . ASP D 1 197 ? -37.610 95.731  39.188  1.00 114.17 ?  213 ASP A CB  1 
ATOM   9581  C CG  . ASP D 1 197 ? -37.427 96.498  37.893  1.00 125.70 ?  213 ASP A CG  1 
ATOM   9582  O OD1 . ASP D 1 197 ? -36.432 97.262  37.818  1.00 124.81 ?  213 ASP A OD1 1 
ATOM   9583  O OD2 . ASP D 1 197 ? -38.281 96.372  36.984  1.00 133.36 -1 213 ASP A OD2 1 
ATOM   9584  N N   . GLY D 1 198 ? -35.135 95.173  41.557  1.00 109.08 ?  214 GLY A N   1 
ATOM   9585  C CA  . GLY D 1 198 ? -34.907 95.215  42.982  1.00 103.33 ?  214 GLY A CA  1 
ATOM   9586  C C   . GLY D 1 198 ? -34.020 94.124  43.512  1.00 102.35 ?  214 GLY A C   1 
ATOM   9587  O O   . GLY D 1 198 ? -33.817 94.050  44.726  1.00 102.09 ?  214 GLY A O   1 
ATOM   9588  N N   . TYR D 1 199 ? -33.470 93.290  42.647  1.00 91.39  ?  215 TYR A N   1 
ATOM   9589  C CA  . TYR D 1 199 ? -32.686 92.139  43.068  1.00 86.00  ?  215 TYR A CA  1 
ATOM   9590  C C   . TYR D 1 199 ? -31.526 91.874  42.122  1.00 83.34  ?  215 TYR A C   1 
ATOM   9591  O O   . TYR D 1 199 ? -30.906 90.815  42.218  1.00 79.81  ?  215 TYR A O   1 
ATOM   9592  C CB  . TYR D 1 199 ? -33.585 90.900  43.148  1.00 82.74  ?  215 TYR A CB  1 
ATOM   9593  C CG  . TYR D 1 199 ? -34.601 90.917  44.274  1.00 82.09  ?  215 TYR A CG  1 
ATOM   9594  C CD1 . TYR D 1 199 ? -34.239 90.617  45.579  1.00 82.37  ?  215 TYR A CD1 1 
ATOM   9595  C CD2 . TYR D 1 199 ? -35.898 91.286  44.042  1.00 82.17  ?  215 TYR A CD2 1 
ATOM   9596  C CE1 . TYR D 1 199 ? -35.161 90.636  46.594  1.00 80.33  ?  215 TYR A CE1 1 
ATOM   9597  C CE2 . TYR D 1 199 ? -36.813 91.315  45.049  1.00 82.78  ?  215 TYR A CE2 1 
ATOM   9598  C CZ  . TYR D 1 199 ? -36.442 90.994  46.312  1.00 79.35  ?  215 TYR A CZ  1 
ATOM   9599  O OH  . TYR D 1 199 ? -37.393 91.039  47.285  1.00 85.86  ?  215 TYR A OH  1 
ATOM   9600  N N   . ASP D 1 200 ? -31.239 92.786  41.196  1.00 90.50  ?  216 ASP A N   1 
ATOM   9601  C CA  . ASP D 1 200 ? -30.179 92.595  40.223  1.00 83.71  ?  216 ASP A CA  1 
ATOM   9602  C C   . ASP D 1 200 ? -28.830 92.728  40.917  1.00 81.42  ?  216 ASP A C   1 
ATOM   9603  O O   . ASP D 1 200 ? -28.730 93.219  42.044  1.00 81.49  ?  216 ASP A O   1 
ATOM   9604  C CB  . ASP D 1 200 ? -30.261 93.634  39.101  1.00 95.70  ?  216 ASP A CB  1 
ATOM   9605  C CG  . ASP D 1 200 ? -31.543 93.529  38.259  1.00 104.21 ?  216 ASP A CG  1 
ATOM   9606  O OD1 . ASP D 1 200 ? -32.065 92.406  38.072  1.00 106.88 ?  216 ASP A OD1 1 
ATOM   9607  O OD2 . ASP D 1 200 ? -32.016 94.583  37.757  1.00 113.80 -1 216 ASP A OD2 1 
ATOM   9608  N N   . TYR D 1 201 ? -27.782 92.305  40.218  1.00 79.14  ?  217 TYR A N   1 
ATOM   9609  C CA  . TYR D 1 201 ? -26.434 92.291  40.784  1.00 78.83  ?  217 TYR A CA  1 
ATOM   9610  C C   . TYR D 1 201 ? -25.377 92.083  39.699  1.00 76.99  ?  217 TYR A C   1 
ATOM   9611  O O   . TYR D 1 201 ? -25.229 90.978  39.167  1.00 75.56  ?  217 TYR A O   1 
ATOM   9612  C CB  . TYR D 1 201 ? -26.327 91.213  41.870  1.00 76.05  ?  217 TYR A CB  1 
ATOM   9613  C CG  . TYR D 1 201 ? -25.127 91.341  42.818  1.00 75.55  ?  217 TYR A CG  1 
ATOM   9614  C CD1 . TYR D 1 201 ? -23.905 90.750  42.512  1.00 74.09  ?  217 TYR A CD1 1 
ATOM   9615  C CD2 . TYR D 1 201 ? -25.224 92.036  44.022  1.00 77.67  ?  217 TYR A CD2 1 
ATOM   9616  C CE1 . TYR D 1 201 ? -22.823 90.858  43.361  1.00 76.42  ?  217 TYR A CE1 1 
ATOM   9617  C CE2 . TYR D 1 201 ? -24.138 92.137  44.882  1.00 76.56  ?  217 TYR A CE2 1 
ATOM   9618  C CZ  . TYR D 1 201 ? -22.941 91.549  44.544  1.00 75.79  ?  217 TYR A CZ  1 
ATOM   9619  O OH  . TYR D 1 201 ? -21.866 91.653  45.403  1.00 73.67  ?  217 TYR A OH  1 
ATOM   9620  N N   . SER D 1 202 ? -24.636 93.146  39.377  1.00 76.82  ?  218 SER A N   1 
ATOM   9621  C CA  . SER D 1 202 ? -23.605 93.184  38.349  1.00 72.79  ?  218 SER A CA  1 
ATOM   9622  C C   . SER D 1 202 ? -22.352 92.419  38.776  1.00 76.14  ?  218 SER A C   1 
ATOM   9623  O O   . SER D 1 202 ? -22.061 92.267  39.964  1.00 78.45  ?  218 SER A O   1 
ATOM   9624  C CB  . SER D 1 202 ? -23.311 94.651  37.995  1.00 77.05  ?  218 SER A CB  1 
ATOM   9625  O OG  . SER D 1 202 ? -22.539 95.321  38.974  1.00 78.81  ?  218 SER A OG  1 
ATOM   9626  N N   . ARG D 1 203 ? -21.613 91.907  37.779  1.00 78.18  ?  219 ARG A N   1 
ATOM   9627  C CA  . ARG D 1 203 ? -20.406 91.122  38.064  1.00 74.97  ?  219 ARG A CA  1 
ATOM   9628  C C   . ARG D 1 203 ? -19.267 91.963  38.603  1.00 72.87  ?  219 ARG A C   1 
ATOM   9629  O O   . ARG D 1 203 ? -18.275 91.422  39.084  1.00 72.53  ?  219 ARG A O   1 
ATOM   9630  C CB  . ARG D 1 203 ? -19.925 90.423  36.813  1.00 73.93  ?  219 ARG A CB  1 
ATOM   9631  C CG  . ARG D 1 203 ? -20.937 89.500  36.224  1.00 73.65  ?  219 ARG A CG  1 
ATOM   9632  C CD  . ARG D 1 203 ? -20.198 88.655  35.237  1.00 78.84  ?  219 ARG A CD  1 
ATOM   9633  N NE  . ARG D 1 203 ? -19.627 89.450  34.151  1.00 82.68  ?  219 ARG A NE  1 
ATOM   9634  C CZ  . ARG D 1 203 ? -20.204 89.629  32.970  1.00 82.64  ?  219 ARG A CZ  1 
ATOM   9635  N NH1 . ARG D 1 203 ? -21.275 88.941  32.618  1.00 85.14  ?  219 ARG A NH1 1 
ATOM   9636  N NH2 . ARG D 1 203 ? -19.658 90.473  32.099  1.00 85.62  ?  219 ARG A NH2 1 
ATOM   9637  N N   . GLY D 1 204 ? -19.361 93.267  38.475  1.00 75.98  ?  220 GLY A N   1 
ATOM   9638  C CA  . GLY D 1 204 ? -18.418 94.118  39.137  1.00 75.35  ?  220 GLY A CA  1 
ATOM   9639  C C   . GLY D 1 204 ? -18.937 94.475  40.502  1.00 79.55  ?  220 GLY A C   1 
ATOM   9640  O O   . GLY D 1 204 ? -18.164 94.866  41.369  1.00 90.33  ?  220 GLY A O   1 
ATOM   9641  N N   . GLN D 1 205 ? -20.240 94.351  40.719  1.00 76.12  ?  221 GLN A N   1 
ATOM   9642  C CA  . GLN D 1 205 ? -20.771 94.688  42.030  1.00 79.99  ?  221 GLN A CA  1 
ATOM   9643  C C   . GLN D 1 205 ? -20.198 93.754  43.089  1.00 81.84  ?  221 GLN A C   1 
ATOM   9644  O O   . GLN D 1 205 ? -20.068 94.136  44.263  1.00 84.10  ?  221 GLN A O   1 
ATOM   9645  C CB  . GLN D 1 205 ? -22.300 94.620  42.007  1.00 84.09  ?  221 GLN A CB  1 
ATOM   9646  C CG  . GLN D 1 205 ? -22.959 95.138  43.257  1.00 89.58  ?  221 GLN A CG  1 
ATOM   9647  C CD  . GLN D 1 205 ? -22.580 96.580  43.514  1.00 94.57  ?  221 GLN A CD  1 
ATOM   9648  O OE1 . GLN D 1 205 ? -22.570 97.384  42.583  1.00 104.56 ?  221 GLN A OE1 1 
ATOM   9649  N NE2 . GLN D 1 205 ? -22.241 96.913  44.766  1.00 88.55  ?  221 GLN A NE2 1 
ATOM   9650  N N   . LEU D 1 206 ? -19.808 92.545  42.682  1.00 79.57  ?  222 LEU A N   1 
ATOM   9651  C CA  . LEU D 1 206 ? -19.118 91.647  43.605  1.00 78.98  ?  222 LEU A CA  1 
ATOM   9652  C C   . LEU D 1 206 ? -17.775 92.215  44.057  1.00 80.51  ?  222 LEU A C   1 
ATOM   9653  O O   . LEU D 1 206 ? -17.432 92.126  45.238  1.00 85.53  ?  222 LEU A O   1 
ATOM   9654  C CB  . LEU D 1 206 ? -18.943 90.264  42.981  1.00 74.68  ?  222 LEU A CB  1 
ATOM   9655  C CG  . LEU D 1 206 ? -18.223 89.222  43.827  1.00 66.88  ?  222 LEU A CG  1 
ATOM   9656  C CD1 . LEU D 1 206 ? -19.159 88.701  44.857  1.00 65.71  ?  222 LEU A CD1 1 
ATOM   9657  C CD2 . LEU D 1 206 ? -17.823 88.089  42.906  1.00 68.59  ?  222 LEU A CD2 1 
ATOM   9658  N N   . ILE D 1 207 ? -17.003 92.813  43.155  1.00 82.37  ?  223 ILE A N   1 
ATOM   9659  C CA  . ILE D 1 207 ? -15.727 93.359  43.608  1.00 80.01  ?  223 ILE A CA  1 
ATOM   9660  C C   . ILE D 1 207 ? -15.945 94.510  44.592  1.00 82.62  ?  223 ILE A C   1 
ATOM   9661  O O   . ILE D 1 207 ? -15.308 94.558  45.656  1.00 83.05  ?  223 ILE A O   1 
ATOM   9662  C CB  . ILE D 1 207 ? -14.851 93.776  42.418  1.00 80.75  ?  223 ILE A CB  1 
ATOM   9663  C CG1 . ILE D 1 207 ? -14.358 92.547  41.646  1.00 77.17  ?  223 ILE A CG1 1 
ATOM   9664  C CG2 . ILE D 1 207 ? -13.683 94.558  42.914  1.00 78.07  ?  223 ILE A CG2 1 
ATOM   9665  C CD1 . ILE D 1 207 ? -13.527 92.891  40.415  1.00 71.51  ?  223 ILE A CD1 1 
ATOM   9666  N N   . GLU D 1 208 ? -16.851 95.442  44.277  1.00 91.62  ?  224 GLU A N   1 
ATOM   9667  C CA  . GLU D 1 208 ? -17.095 96.533  45.218  1.00 96.95  ?  224 GLU A CA  1 
ATOM   9668  C C   . GLU D 1 208 ? -17.522 96.000  46.573  1.00 100.75 ?  224 GLU A C   1 
ATOM   9669  O O   . GLU D 1 208 ? -16.978 96.427  47.598  1.00 105.35 ?  224 GLU A O   1 
ATOM   9670  C CB  . GLU D 1 208 ? -18.135 97.543  44.711  1.00 101.79 ?  224 GLU A CB  1 
ATOM   9671  C CG  . GLU D 1 208 ? -17.654 98.486  43.615  1.00 113.61 ?  224 GLU A CG  1 
ATOM   9672  C CD  . GLU D 1 208 ? -18.769 98.947  42.675  1.00 123.24 ?  224 GLU A CD  1 
ATOM   9673  O OE1 . GLU D 1 208 ? -19.954 98.918  43.090  1.00 124.03 ?  224 GLU A OE1 1 
ATOM   9674  O OE2 . GLU D 1 208 ? -18.466 99.328  41.520  1.00 131.44 -1 224 GLU A OE2 1 
ATOM   9675  N N   . ASP D 1 209 ? -18.487 95.064  46.607  1.00 85.95  ?  225 ASP A N   1 
ATOM   9676  C CA  . ASP D 1 209 ? -18.977 94.586  47.906  1.00 83.49  ?  225 ASP A CA  1 
ATOM   9677  C C   . ASP D 1 209 ? -17.930 93.776  48.670  1.00 82.48  ?  225 ASP A C   1 
ATOM   9678  O O   . ASP D 1 209 ? -17.813 93.910  49.896  1.00 83.36  ?  225 ASP A O   1 
ATOM   9679  C CB  . ASP D 1 209 ? -20.249 93.764  47.765  1.00 75.84  ?  225 ASP A CB  1 
ATOM   9680  C CG  . ASP D 1 209 ? -21.417 94.561  47.296  1.00 83.06  ?  225 ASP A CG  1 
ATOM   9681  O OD1 . ASP D 1 209 ? -21.434 95.799  47.458  1.00 84.56  ?  225 ASP A OD1 1 
ATOM   9682  O OD2 . ASP D 1 209 ? -22.382 93.913  46.852  1.00 94.13  -1 225 ASP A OD2 1 
ATOM   9683  N N   . VAL D 1 210 ? -17.179 92.911  47.992  1.00 79.03  ?  226 VAL A N   1 
ATOM   9684  C CA  . VAL D 1 210 ? -16.171 92.139  48.706  1.00 77.20  ?  226 VAL A CA  1 
ATOM   9685  C C   . VAL D 1 210 ? -15.128 93.074  49.302  1.00 76.63  ?  226 VAL A C   1 
ATOM   9686  O O   . VAL D 1 210 ? -14.722 92.917  50.463  1.00 74.53  ?  226 VAL A O   1 
ATOM   9687  C CB  . VAL D 1 210 ? -15.536 91.103  47.768  1.00 76.40  ?  226 VAL A CB  1 
ATOM   9688  C CG1 . VAL D 1 210 ? -14.203 90.582  48.345  1.00 69.98  ?  226 VAL A CG1 1 
ATOM   9689  C CG2 . VAL D 1 210 ? -16.528 90.005  47.447  1.00 72.45  ?  226 VAL A CG2 1 
ATOM   9690  N N   . GLU D 1 211 ? -14.706 94.089  48.534  1.00 75.52  ?  227 GLU A N   1 
ATOM   9691  C CA  . GLU D 1 211 ? -13.743 95.039  49.076  1.00 78.07  ?  227 GLU A CA  1 
ATOM   9692  C C   . GLU D 1 211 ? -14.349 95.855  50.218  1.00 76.87  ?  227 GLU A C   1 
ATOM   9693  O O   . GLU D 1 211 ? -13.731 96.014  51.280  1.00 77.29  ?  227 GLU A O   1 
ATOM   9694  C CB  . GLU D 1 211 ? -13.191 95.945  47.966  1.00 78.64  ?  227 GLU A CB  1 
ATOM   9695  C CG  . GLU D 1 211 ? -12.131 95.255  47.088  1.00 75.85  ?  227 GLU A CG  1 
ATOM   9696  C CD  . GLU D 1 211 ? -11.650 96.094  45.884  1.00 79.15  ?  227 GLU A CD  1 
ATOM   9697  O OE1 . GLU D 1 211 ? -12.274 97.139  45.574  1.00 78.84  ?  227 GLU A OE1 1 
ATOM   9698  O OE2 . GLU D 1 211 ? -10.643 95.690  45.240  1.00 77.33  -1 227 GLU A OE2 1 
ATOM   9699  N N   . HIS D 1 212 ? -15.556 96.375  50.036  1.00 82.49  ?  228 HIS A N   1 
ATOM   9700  C CA  A HIS D 1 212 ? -16.124 97.205  51.084  0.38 99.28  ?  228 HIS A CA  1 
ATOM   9701  C CA  B HIS D 1 212 ? -16.169 97.191  51.079  0.62 121.03 ?  228 HIS A CA  1 
ATOM   9702  C C   . HIS D 1 212 ? -16.366 96.405  52.364  1.00 79.64  ?  228 HIS A C   1 
ATOM   9703  O O   . HIS D 1 212 ? -16.319 96.975  53.451  1.00 82.47  ?  228 HIS A O   1 
ATOM   9704  C CB  A HIS D 1 212 ? -17.400 97.889  50.579  0.38 76.61  ?  228 HIS A CB  1 
ATOM   9705  C CB  B HIS D 1 212 ? -17.509 97.764  50.617  0.62 83.82  ?  228 HIS A CB  1 
ATOM   9706  C CG  A HIS D 1 212 ? -17.152 98.939  49.529  0.38 85.28  ?  228 HIS A CG  1 
ATOM   9707  C CG  B HIS D 1 212 ? -18.231 98.531  51.684  0.62 83.52  ?  228 HIS A CG  1 
ATOM   9708  N ND1 A HIS D 1 212 ? -18.159 99.456  48.740  0.38 82.17  ?  228 HIS A ND1 1 
ATOM   9709  N ND1 B HIS D 1 212 ? -18.168 99.903  51.792  0.62 79.09  ?  228 HIS A ND1 1 
ATOM   9710  C CD2 A HIS D 1 212 ? -16.015 99.566  49.139  0.38 81.81  ?  228 HIS A CD2 1 
ATOM   9711  C CD2 B HIS D 1 212 ? -19.018 98.112  52.703  0.62 78.50  ?  228 HIS A CD2 1 
ATOM   9712  C CE1 A HIS D 1 212 ? -17.654 100.349 47.908  0.38 81.23  ?  228 HIS A CE1 1 
ATOM   9713  C CE1 B HIS D 1 212 ? -18.889 100.295 52.827  0.62 74.70  ?  228 HIS A CE1 1 
ATOM   9714  N NE2 A HIS D 1 212 ? -16.355 100.437 48.132  0.38 77.57  ?  228 HIS A NE2 1 
ATOM   9715  N NE2 B HIS D 1 212 ? -19.413 99.226  53.399  0.62 73.44  ?  228 HIS A NE2 1 
ATOM   9716  N N   . THR D 1 213 ? -16.597 95.090  52.276  1.00 82.86  ?  229 THR A N   1 
ATOM   9717  C CA  . THR D 1 213 ? -16.797 94.349  53.531  1.00 80.98  ?  229 THR A CA  1 
ATOM   9718  C C   . THR D 1 213 ? -15.465 93.947  54.165  1.00 77.79  ?  229 THR A C   1 
ATOM   9719  O O   . THR D 1 213 ? -15.345 93.906  55.401  1.00 76.75  ?  229 THR A O   1 
ATOM   9720  C CB  . THR D 1 213 ? -17.741 93.121  53.354  1.00 74.44  ?  229 THR A CB  1 
ATOM   9721  O OG1 . THR D 1 213 ? -17.274 92.212  52.348  1.00 71.98  ?  229 THR A OG1 1 
ATOM   9722  C CG2 . THR D 1 213 ? -19.132 93.542  53.035  1.00 72.20  ?  229 THR A CG2 1 
ATOM   9723  N N   . PHE D 1 214 ? -14.442 93.701  53.352  1.00 77.80  ?  230 PHE A N   1 
ATOM   9724  C CA  . PHE D 1 214 ? -13.141 93.384  53.923  1.00 70.50  ?  230 PHE A CA  1 
ATOM   9725  C C   . PHE D 1 214 ? -12.528 94.587  54.624  1.00 70.90  ?  230 PHE A C   1 
ATOM   9726  O O   . PHE D 1 214 ? -11.794 94.422  55.608  1.00 67.55  ?  230 PHE A O   1 
ATOM   9727  C CB  . PHE D 1 214 ? -12.220 92.873  52.831  1.00 71.60  ?  230 PHE A CB  1 
ATOM   9728  C CG  . PHE D 1 214 ? -10.920 92.478  53.329  1.00 71.83  ?  230 PHE A CG  1 
ATOM   9729  C CD1 . PHE D 1 214 ? -10.823 91.407  54.187  1.00 69.01  ?  230 PHE A CD1 1 
ATOM   9730  C CD2 . PHE D 1 214 ? -9.789  93.171  52.966  1.00 73.57  ?  230 PHE A CD2 1 
ATOM   9731  C CE1 . PHE D 1 214 ? -9.605  91.022  54.687  1.00 68.96  ?  230 PHE A CE1 1 
ATOM   9732  C CE2 . PHE D 1 214 ? -8.556  92.799  53.458  1.00 74.41  ?  230 PHE A CE2 1 
ATOM   9733  C CZ  . PHE D 1 214 ? -8.460  91.718  54.318  1.00 74.25  ?  230 PHE A CZ  1 
ATOM   9734  N N   . GLU D 1 215 ? -12.816 95.796  54.131  1.00 71.19  ?  231 GLU A N   1 
ATOM   9735  C CA  . GLU D 1 215 ? -12.425 96.993  54.870  1.00 70.92  ?  231 GLU A CA  1 
ATOM   9736  C C   . GLU D 1 215 ? -12.925 96.951  56.302  1.00 68.65  ?  231 GLU A C   1 
ATOM   9737  O O   . GLU D 1 215 ? -12.214 97.380  57.211  1.00 73.64  ?  231 GLU A O   1 
ATOM   9738  C CB  . GLU D 1 215 ? -12.938 98.260  54.194  1.00 73.31  ?  231 GLU A CB  1 
ATOM   9739  C CG  . GLU D 1 215 ? -12.068 98.768  53.061  1.00 80.92  ?  231 GLU A CG  1 
ATOM   9740  C CD  . GLU D 1 215 ? -10.740 99.322  53.524  1.00 84.00  ?  231 GLU A CD  1 
ATOM   9741  O OE1 . GLU D 1 215 ? -10.702 100.034 54.561  1.00 81.59  ?  231 GLU A OE1 1 
ATOM   9742  O OE2 . GLU D 1 215 ? -9.734  99.033  52.835  1.00 95.99  -1 231 GLU A OE2 1 
ATOM   9743  N N   . GLU D 1 216 ? -14.150 96.467  56.533  1.00 67.41  ?  232 GLU A N   1 
ATOM   9744  C CA  . GLU D 1 216 ? -14.636 96.363  57.910  1.00 72.79  ?  232 GLU A CA  1 
ATOM   9745  C C   . GLU D 1 216 ? -14.080 95.145  58.648  1.00 67.04  ?  232 GLU A C   1 
ATOM   9746  O O   . GLU D 1 216 ? -14.008 95.154  59.885  1.00 68.08  ?  232 GLU A O   1 
ATOM   9747  C CB  . GLU D 1 216 ? -16.174 96.340  57.976  1.00 78.53  ?  232 GLU A CB  1 
ATOM   9748  C CG  . GLU D 1 216 ? -16.894 97.345  57.073  1.00 83.06  ?  232 GLU A CG  1 
ATOM   9749  C CD  . GLU D 1 216 ? -18.426 97.337  57.251  1.00 90.98  ?  232 GLU A CD  1 
ATOM   9750  O OE1 . GLU D 1 216 ? -18.893 97.512  58.413  1.00 94.07  ?  232 GLU A OE1 1 
ATOM   9751  O OE2 . GLU D 1 216 ? -19.153 97.191  56.227  1.00 89.31  -1 232 GLU A OE2 1 
ATOM   9752  N N   . ILE D 1 217 ? -13.688 94.093  57.937  1.00 70.59  ?  233 ILE A N   1 
ATOM   9753  C CA  . ILE D 1 217 ? -12.995 93.043  58.670  1.00 64.46  ?  233 ILE A CA  1 
ATOM   9754  C C   . ILE D 1 217 ? -11.662 93.552  59.194  1.00 64.79  ?  233 ILE A C   1 
ATOM   9755  O O   . ILE D 1 217 ? -11.236 93.167  60.289  1.00 66.86  ?  233 ILE A O   1 
ATOM   9756  C CB  . ILE D 1 217 ? -12.836 91.783  57.810  1.00 64.02  ?  233 ILE A CB  1 
ATOM   9757  C CG1 . ILE D 1 217 ? -14.113 90.979  57.887  1.00 70.16  ?  233 ILE A CG1 1 
ATOM   9758  C CG2 . ILE D 1 217 ? -11.775 90.913  58.317  1.00 60.33  ?  233 ILE A CG2 1 
ATOM   9759  C CD1 . ILE D 1 217 ? -14.217 89.947  56.834  1.00 72.51  ?  233 ILE A CD1 1 
ATOM   9760  N N   . LYS D 1 218 ? -11.011 94.459  58.461  1.00 66.56  ?  234 LYS A N   1 
ATOM   9761  C CA  . LYS D 1 218 ? -9.588  94.756  58.699  1.00 66.31  ?  234 LYS A CA  1 
ATOM   9762  C C   . LYS D 1 218 ? -9.196  94.935  60.160  1.00 63.65  ?  234 LYS A C   1 
ATOM   9763  O O   . LYS D 1 218 ? -8.190  94.346  60.556  1.00 63.84  ?  234 LYS A O   1 
ATOM   9764  C CB  . LYS D 1 218 ? -9.123  95.997  57.920  1.00 65.56  ?  234 LYS A CB  1 
ATOM   9765  C CG  . LYS D 1 218 ? -8.726  95.720  56.480  1.00 65.03  ?  234 LYS A CG  1 
ATOM   9766  C CD  . LYS D 1 218 ? -8.286  97.004  55.855  1.00 69.91  ?  234 LYS A CD  1 
ATOM   9767  C CE  . LYS D 1 218 ? -8.183  96.913  54.368  1.00 76.96  ?  234 LYS A CE  1 
ATOM   9768  N NZ  . LYS D 1 218 ? -7.759  98.256  53.907  1.00 81.87  ?  234 LYS A NZ  1 
ATOM   9769  N N   . PRO D 1 219 ? -9.915  95.696  61.000  1.00 61.81  ?  235 PRO A N   1 
ATOM   9770  C CA  . PRO D 1 219 ? -9.447  95.864  62.392  1.00 62.16  ?  235 PRO A CA  1 
ATOM   9771  C C   . PRO D 1 219 ? -9.478  94.595  63.223  1.00 64.24  ?  235 PRO A C   1 
ATOM   9772  O O   . PRO D 1 219 ? -8.489  94.313  63.925  1.00 61.38  ?  235 PRO A O   1 
ATOM   9773  C CB  . PRO D 1 219 ? -10.394 96.931  62.955  1.00 59.78  ?  235 PRO A CB  1 
ATOM   9774  C CG  . PRO D 1 219 ? -10.867 97.650  61.774  1.00 61.29  ?  235 PRO A CG  1 
ATOM   9775  C CD  . PRO D 1 219 ? -11.030 96.606  60.716  1.00 63.07  ?  235 PRO A CD  1 
ATOM   9776  N N   . LEU D 1 220 ? -10.593 93.843  63.214  1.00 64.09  ?  236 LEU A N   1 
ATOM   9777  C CA  . LEU D 1 220 ? -10.570 92.530  63.859  1.00 62.24  ?  236 LEU A CA  1 
ATOM   9778  C C   . LEU D 1 220 ? -9.373  91.727  63.372  1.00 62.00  ?  236 LEU A C   1 
ATOM   9779  O O   . LEU D 1 220 ? -8.675  91.067  64.166  1.00 59.30  ?  236 LEU A O   1 
ATOM   9780  C CB  . LEU D 1 220 ? -11.833 91.730  63.561  1.00 60.50  ?  236 LEU A CB  1 
ATOM   9781  C CG  . LEU D 1 220 ? -11.751 90.369  64.279  1.00 52.64  ?  236 LEU A CG  1 
ATOM   9782  C CD1 . LEU D 1 220 ? -11.405 90.591  65.748  1.00 56.69  ?  236 LEU A CD1 1 
ATOM   9783  C CD2 . LEU D 1 220 ? -12.910 89.398  64.065  1.00 41.34  ?  236 LEU A CD2 1 
ATOM   9784  N N   . TYR D 1 221 ? -9.120  91.775  62.056  1.00 57.97  ?  237 TYR A N   1 
ATOM   9785  C CA  . TYR D 1 221 ? -8.006  91.012  61.521  1.00 58.89  ?  237 TYR A CA  1 
ATOM   9786  C C   . TYR D 1 221 ? -6.678  91.491  62.109  1.00 63.60  ?  237 TYR A C   1 
ATOM   9787  O O   . TYR D 1 221 ? -5.887  90.674  62.598  1.00 67.74  ?  237 TYR A O   1 
ATOM   9788  C CB  . TYR D 1 221 ? -7.990  91.055  59.994  1.00 55.95  ?  237 TYR A CB  1 
ATOM   9789  C CG  . TYR D 1 221 ? -6.829  90.242  59.478  1.00 56.71  ?  237 TYR A CG  1 
ATOM   9790  C CD1 . TYR D 1 221 ? -6.777  88.887  59.701  1.00 52.95  ?  237 TYR A CD1 1 
ATOM   9791  C CD2 . TYR D 1 221 ? -5.771  90.837  58.806  1.00 57.52  ?  237 TYR A CD2 1 
ATOM   9792  C CE1 . TYR D 1 221 ? -5.725  88.148  59.277  1.00 55.75  ?  237 TYR A CE1 1 
ATOM   9793  C CE2 . TYR D 1 221 ? -4.718  90.093  58.372  1.00 56.04  ?  237 TYR A CE2 1 
ATOM   9794  C CZ  . TYR D 1 221 ? -4.703  88.753  58.610  1.00 55.96  ?  237 TYR A CZ  1 
ATOM   9795  O OH  . TYR D 1 221 ? -3.644  88.005  58.182  1.00 56.49  ?  237 TYR A OH  1 
ATOM   9796  N N   . GLU D 1 222 ? -6.419  92.809  62.063  1.00 67.06  ?  238 GLU A N   1 
ATOM   9797  C CA  . GLU D 1 222 ? -5.228  93.395  62.680  1.00 68.77  ?  238 GLU A CA  1 
ATOM   9798  C C   . GLU D 1 222 ? -5.019  92.924  64.103  1.00 65.96  ?  238 GLU A C   1 
ATOM   9799  O O   . GLU D 1 222 ? -3.890  92.641  64.507  1.00 66.84  ?  238 GLU A O   1 
ATOM   9800  C CB  . GLU D 1 222 ? -5.286  94.924  62.675  1.00 73.29  ?  238 GLU A CB  1 
ATOM   9801  C CG  . GLU D 1 222 ? -4.959  95.597  61.364  1.00 75.67  ?  238 GLU A CG  1 
ATOM   9802  C CD  . GLU D 1 222 ? -4.860  97.115  61.519  1.00 88.10  ?  238 GLU A CD  1 
ATOM   9803  O OE1 . GLU D 1 222 ? -4.413  97.568  62.585  1.00 86.35  ?  238 GLU A OE1 1 
ATOM   9804  O OE2 . GLU D 1 222 ? -5.197  97.862  60.569  1.00 103.67 -1 238 GLU A OE2 1 
ATOM   9805  N N   . HIS D 1 223 ? -6.070  92.868  64.891  1.00 61.64  ?  239 HIS A N   1 
ATOM   9806  C CA  . HIS D 1 223 ? -5.820  92.514  66.280  1.00 63.33  ?  239 HIS A CA  1 
ATOM   9807  C C   . HIS D 1 223 ? -5.544  91.027  66.444  1.00 61.61  ?  239 HIS A C   1 
ATOM   9808  O O   . HIS D 1 223 ? -4.646  90.642  67.202  1.00 65.96  ?  239 HIS A O   1 
ATOM   9809  C CB  . HIS D 1 223 ? -6.978  92.967  67.136  1.00 62.03  ?  239 HIS A CB  1 
ATOM   9810  C CG  . HIS D 1 223 ? -6.893  94.410  67.494  1.00 61.64  ?  239 HIS A CG  1 
ATOM   9811  N ND1 . HIS D 1 223 ? -6.124  94.870  68.533  1.00 66.88  ?  239 HIS A ND1 1 
ATOM   9812  C CD2 . HIS D 1 223 ? -7.359  95.508  66.859  1.00 63.18  ?  239 HIS A CD2 1 
ATOM   9813  C CE1 . HIS D 1 223 ? -6.208  96.187  68.589  1.00 67.78  ?  239 HIS A CE1 1 
ATOM   9814  N NE2 . HIS D 1 223 ? -6.944  96.601  67.576  1.00 62.93  ?  239 HIS A NE2 1 
ATOM   9815  N N   . LEU D 1 224 ? -6.276  90.171  65.735  1.00 60.58  ?  240 LEU A N   1 
ATOM   9816  C CA  . LEU D 1 224 ? -5.890  88.761  65.750  1.00 63.41  ?  240 LEU A CA  1 
ATOM   9817  C C   . LEU D 1 224 ? -4.424  88.603  65.395  1.00 62.34  ?  240 LEU A C   1 
ATOM   9818  O O   . LEU D 1 224 ? -3.698  87.812  66.008  1.00 60.39  ?  240 LEU A O   1 
ATOM   9819  C CB  . LEU D 1 224 ? -6.742  87.954  64.776  1.00 59.29  ?  240 LEU A CB  1 
ATOM   9820  C CG  . LEU D 1 224 ? -6.290  86.494  64.783  1.00 53.45  ?  240 LEU A CG  1 
ATOM   9821  C CD1 . LEU D 1 224 ? -6.602  85.815  66.094  1.00 54.55  ?  240 LEU A CD1 1 
ATOM   9822  C CD2 . LEU D 1 224 ? -6.979  85.779  63.671  1.00 55.41  ?  240 LEU A CD2 1 
ATOM   9823  N N   . HIS D 1 225 ? -3.990  89.385  64.410  1.00 63.24  ?  241 HIS A N   1 
ATOM   9824  C CA  . HIS D 1 225 ? -2.625  89.374  63.904  1.00 63.40  ?  241 HIS A CA  1 
ATOM   9825  C C   . HIS D 1 225 ? -1.617  89.846  64.940  1.00 64.36  ?  241 HIS A C   1 
ATOM   9826  O O   . HIS D 1 225 ? -0.603  89.182  65.171  1.00 62.17  ?  241 HIS A O   1 
ATOM   9827  C CB  . HIS D 1 225 ? -2.624  90.231  62.655  1.00 63.51  ?  241 HIS A CB  1 
ATOM   9828  C CG  . HIS D 1 225 ? -1.313  90.350  61.983  1.00 62.36  ?  241 HIS A CG  1 
ATOM   9829  N ND1 . HIS D 1 225 ? -0.318  91.156  62.480  1.00 63.37  ?  241 HIS A ND1 1 
ATOM   9830  C CD2 . HIS D 1 225 ? -0.821  89.775  60.862  1.00 60.77  ?  241 HIS A CD2 1 
ATOM   9831  C CE1 . HIS D 1 225 ? 0.730   91.083  61.676  1.00 63.58  ?  241 HIS A CE1 1 
ATOM   9832  N NE2 . HIS D 1 225 ? 0.454   90.244  60.693  1.00 58.27  ?  241 HIS A NE2 1 
ATOM   9833  N N   . ALA D 1 226 ? -1.851  91.007  65.535  1.00 71.84  ?  242 ALA A N   1 
ATOM   9834  C CA  . ALA D 1 226 ? -0.947  91.484  66.573  1.00 71.91  ?  242 ALA A CA  1 
ATOM   9835  C C   . ALA D 1 226 ? -0.775  90.440  67.663  1.00 69.64  ?  242 ALA A C   1 
ATOM   9836  O O   . ALA D 1 226 ? 0.346   90.205  68.142  1.00 72.91  ?  242 ALA A O   1 
ATOM   9837  C CB  . ALA D 1 226 ? -1.462  92.793  67.159  1.00 73.30  ?  242 ALA A CB  1 
ATOM   9838  N N   . TYR D 1 227 ? -1.868  89.768  68.029  1.00 59.57  ?  243 TYR A N   1 
ATOM   9839  C CA  . TYR D 1 227 ? -1.814  88.805  69.120  1.00 57.05  ?  243 TYR A CA  1 
ATOM   9840  C C   . TYR D 1 227 ? -1.067  87.548  68.707  1.00 55.46  ?  243 TYR A C   1 
ATOM   9841  O O   . TYR D 1 227 ? -0.268  86.999  69.473  1.00 52.81  ?  243 TYR A O   1 
ATOM   9842  C CB  . TYR D 1 227 ? -3.222  88.427  69.507  1.00 61.42  ?  243 TYR A CB  1 
ATOM   9843  C CG  . TYR D 1 227 ? -3.382  87.313  70.530  1.00 59.10  ?  243 TYR A CG  1 
ATOM   9844  C CD1 . TYR D 1 227 ? -3.185  87.536  71.879  1.00 61.43  ?  243 TYR A CD1 1 
ATOM   9845  C CD2 . TYR D 1 227 ? -3.678  86.021  70.135  1.00 61.74  ?  243 TYR A CD2 1 
ATOM   9846  C CE1 . TYR D 1 227 ? -3.353  86.517  72.812  1.00 58.45  ?  243 TYR A CE1 1 
ATOM   9847  C CE2 . TYR D 1 227 ? -3.835  84.998  71.062  1.00 59.52  ?  243 TYR A CE2 1 
ATOM   9848  C CZ  . TYR D 1 227 ? -3.669  85.250  72.390  1.00 59.34  ?  243 TYR A CZ  1 
ATOM   9849  O OH  . TYR D 1 227 ? -3.832  84.214  73.275  1.00 63.15  ?  243 TYR A OH  1 
ATOM   9850  N N   . VAL D 1 228 ? -1.331  87.063  67.499  1.00 57.81  ?  244 VAL A N   1 
ATOM   9851  C CA  . VAL D 1 228 ? -0.658  85.857  67.054  1.00 58.46  ?  244 VAL A CA  1 
ATOM   9852  C C   . VAL D 1 228 ? 0.821   86.138  66.858  1.00 60.75  ?  244 VAL A C   1 
ATOM   9853  O O   . VAL D 1 228 ? 1.665   85.272  67.108  1.00 63.34  ?  244 VAL A O   1 
ATOM   9854  C CB  . VAL D 1 228 ? -1.328  85.318  65.773  1.00 54.98  ?  244 VAL A CB  1 
ATOM   9855  C CG1 . VAL D 1 228 ? -0.439  84.312  65.056  1.00 55.37  ?  244 VAL A CG1 1 
ATOM   9856  C CG2 . VAL D 1 228 ? -2.637  84.692  66.119  1.00 54.94  ?  244 VAL A CG2 1 
ATOM   9857  N N   . ARG D 1 229 ? 1.158   87.357  66.431  1.00 64.60  ?  245 ARG A N   1 
ATOM   9858  C CA  . ARG D 1 229 ? 2.557   87.721  66.246  1.00 65.27  ?  245 ARG A CA  1 
ATOM   9859  C C   . ARG D 1 229 ? 3.293   87.746  67.574  1.00 62.56  ?  245 ARG A C   1 
ATOM   9860  O O   . ARG D 1 229 ? 4.405   87.238  67.675  1.00 61.40  ?  245 ARG A O   1 
ATOM   9861  C CB  . ARG D 1 229 ? 2.665   89.075  65.561  1.00 64.56  ?  245 ARG A CB  1 
ATOM   9862  C CG  . ARG D 1 229 ? 4.076   89.511  65.416  1.00 64.97  ?  245 ARG A CG  1 
ATOM   9863  C CD  . ARG D 1 229 ? 4.177   90.775  64.651  1.00 64.74  ?  245 ARG A CD  1 
ATOM   9864  N NE  . ARG D 1 229 ? 3.266   91.762  65.194  1.00 64.74  ?  245 ARG A NE  1 
ATOM   9865  C CZ  . ARG D 1 229 ? 2.924   92.858  64.541  1.00 68.41  ?  245 ARG A CZ  1 
ATOM   9866  N NH1 . ARG D 1 229 ? 3.525   93.198  63.416  1.00 68.19  ?  245 ARG A NH1 1 
ATOM   9867  N NH2 . ARG D 1 229 ? 1.962   93.633  65.032  1.00 74.14  ?  245 ARG A NH2 1 
ATOM   9868  N N   . ALA D 1 230 ? 2.691   88.353  68.600  1.00 63.14  ?  246 ALA A N   1 
ATOM   9869  C CA  . ALA D 1 230 ? 3.240   88.252  69.951  1.00 63.90  ?  246 ALA A CA  1 
ATOM   9870  C C   . ALA D 1 230 ? 3.507   86.799  70.337  1.00 64.36  ?  246 ALA A C   1 
ATOM   9871  O O   . ALA D 1 230 ? 4.600   86.456  70.798  1.00 68.22  ?  246 ALA A O   1 
ATOM   9872  C CB  . ALA D 1 230 ? 2.279   88.900  70.941  1.00 59.11  ?  246 ALA A CB  1 
ATOM   9873  N N   . LYS D 1 231 ? 2.533   85.915  70.110  1.00 62.77  ?  247 LYS A N   1 
ATOM   9874  C CA  . LYS D 1 231 ? 2.680   84.529  70.567  1.00 59.55  ?  247 LYS A CA  1 
ATOM   9875  C C   . LYS D 1 231 ? 3.764   83.781  69.777  1.00 61.52  ?  247 LYS A C   1 
ATOM   9876  O O   . LYS D 1 231 ? 4.576   83.047  70.358  1.00 57.86  ?  247 LYS A O   1 
ATOM   9877  C CB  . LYS D 1 231 ? 1.334   83.831  70.441  1.00 52.36  ?  247 LYS A CB  1 
ATOM   9878  C CG  . LYS D 1 231 ? 0.181   84.438  71.276  1.00 59.02  ?  247 LYS A CG  1 
ATOM   9879  C CD  . LYS D 1 231 ? 0.248   84.459  72.783  1.00 55.16  ?  247 LYS A CD  1 
ATOM   9880  C CE  . LYS D 1 231 ? 0.090   83.065  73.318  1.00 57.72  ?  247 LYS A CE  1 
ATOM   9881  N NZ  . LYS D 1 231 ? -0.056  83.116  74.789  1.00 69.16  ?  247 LYS A NZ  1 
ATOM   9882  N N   . LEU D 1 232 ? 3.798   83.947  68.437  1.00 60.51  ?  248 LEU A N   1 
ATOM   9883  C CA  . LEU D 1 232 ? 4.838   83.291  67.637  1.00 64.51  ?  248 LEU A CA  1 
ATOM   9884  C C   . LEU D 1 232 ? 6.205   83.857  67.963  1.00 75.08  ?  248 LEU A C   1 
ATOM   9885  O O   . LEU D 1 232 ? 7.195   83.120  68.054  1.00 83.99  ?  248 LEU A O   1 
ATOM   9886  C CB  . LEU D 1 232 ? 4.602   83.445  66.136  1.00 62.91  ?  248 LEU A CB  1 
ATOM   9887  C CG  . LEU D 1 232 ? 3.422   82.776  65.458  1.00 61.14  ?  248 LEU A CG  1 
ATOM   9888  C CD1 . LEU D 1 232 ? 3.475   83.112  63.988  1.00 56.34  ?  248 LEU A CD1 1 
ATOM   9889  C CD2 . LEU D 1 232 ? 3.376   81.246  65.668  1.00 57.27  ?  248 LEU A CD2 1 
ATOM   9890  N N   . MET D 1 233 ? 6.279   85.167  68.135  1.00 77.02  ?  249 MET A N   1 
ATOM   9891  C CA  . MET D 1 233 ? 7.522   85.817  68.479  1.00 74.11  ?  249 MET A CA  1 
ATOM   9892  C C   . MET D 1 233 ? 8.071   85.222  69.768  1.00 75.21  ?  249 MET A C   1 
ATOM   9893  O O   . MET D 1 233 ? 9.279   85.056  69.904  1.00 80.58  ?  249 MET A O   1 
ATOM   9894  C CB  . MET D 1 233 ? 7.200   87.309  68.539  1.00 79.43  ?  249 MET A CB  1 
ATOM   9895  C CG  . MET D 1 233 ? 8.302   88.293  68.547  1.00 81.43  ?  249 MET A CG  1 
ATOM   9896  S SD  . MET D 1 233 ? 7.502   89.926  68.521  1.00 72.97  ?  249 MET A SD  1 
ATOM   9897  C CE  . MET D 1 233 ? 6.584   89.854  70.066  1.00 67.08  ?  249 MET A CE  1 
ATOM   9898  N N   . ASN D 1 234 ? 7.195   84.831  70.703  1.00 67.50  ?  250 ASN A N   1 
ATOM   9899  C CA  . ASN D 1 234 ? 7.705   84.035  71.817  1.00 63.64  ?  250 ASN A CA  1 
ATOM   9900  C C   . ASN D 1 234 ? 8.073   82.635  71.390  1.00 68.98  ?  250 ASN A C   1 
ATOM   9901  O O   . ASN D 1 234 ? 8.879   81.998  72.051  1.00 70.88  ?  250 ASN A O   1 
ATOM   9902  C CB  . ASN D 1 234 ? 6.720   83.887  72.974  1.00 60.32  ?  250 ASN A CB  1 
ATOM   9903  C CG  . ASN D 1 234 ? 6.502   85.162  73.722  1.00 64.62  ?  250 ASN A CG  1 
ATOM   9904  O OD1 . ASN D 1 234 ? 7.278   86.115  73.622  1.00 66.66  ?  250 ASN A OD1 1 
ATOM   9905  N ND2 . ASN D 1 234 ? 5.427   85.197  74.485  1.00 67.00  ?  250 ASN A ND2 1 
ATOM   9906  N N   . ALA D 1 235 ? 7.465   82.082  70.369  1.00 73.42  ?  251 ALA A N   1 
ATOM   9907  C CA  . ALA D 1 235 ? 7.832   80.696  70.120  1.00 77.01  ?  251 ALA A CA  1 
ATOM   9908  C C   . ALA D 1 235 ? 8.966   80.555  69.115  1.00 80.74  ?  251 ALA A C   1 
ATOM   9909  O O   . ALA D 1 235 ? 9.511   79.459  68.960  1.00 76.94  ?  251 ALA A O   1 
ATOM   9910  C CB  . ALA D 1 235 ? 6.612   79.893  69.673  1.00 72.28  ?  251 ALA A CB  1 
ATOM   9911  N N   . TYR D 1 236 ? 9.323   81.631  68.431  1.00 80.91  ?  252 TYR A N   1 
ATOM   9912  C CA  . TYR D 1 236 ? 10.489  81.687  67.553  1.00 88.52  ?  252 TYR A CA  1 
ATOM   9913  C C   . TYR D 1 236 ? 11.181  82.996  67.874  1.00 101.44 ?  252 TYR A C   1 
ATOM   9914  O O   . TYR D 1 236 ? 11.114  83.947  67.083  1.00 104.10 ?  252 TYR A O   1 
ATOM   9915  C CB  . TYR D 1 236 ? 10.113  81.687  66.079  1.00 79.46  ?  252 TYR A CB  1 
ATOM   9916  C CG  . TYR D 1 236 ? 9.361   80.491  65.598  1.00 80.26  ?  252 TYR A CG  1 
ATOM   9917  C CD1 . TYR D 1 236 ? 10.008  79.311  65.319  1.00 82.64  ?  252 TYR A CD1 1 
ATOM   9918  C CD2 . TYR D 1 236 ? 7.989   80.549  65.405  1.00 82.97  ?  252 TYR A CD2 1 
ATOM   9919  C CE1 . TYR D 1 236 ? 9.310   78.225  64.852  1.00 86.46  ?  252 TYR A CE1 1 
ATOM   9920  C CE2 . TYR D 1 236 ? 7.290   79.466  64.952  1.00 84.17  ?  252 TYR A CE2 1 
ATOM   9921  C CZ  . TYR D 1 236 ? 7.949   78.312  64.677  1.00 88.12  ?  252 TYR A CZ  1 
ATOM   9922  O OH  . TYR D 1 236 ? 7.222   77.251  64.227  1.00 81.67  ?  252 TYR A OH  1 
ATOM   9923  N N   . PRO D 1 237 ? 11.853  83.083  69.027  1.00 118.76 ?  253 PRO A N   1 
ATOM   9924  C CA  . PRO D 1 237 ? 12.183  84.408  69.566  1.00 121.44 ?  253 PRO A CA  1 
ATOM   9925  C C   . PRO D 1 237 ? 13.112  85.140  68.644  1.00 116.65 ?  253 PRO A C   1 
ATOM   9926  O O   . PRO D 1 237 ? 12.940  86.339  68.368  1.00 117.18 ?  253 PRO A O   1 
ATOM   9927  C CB  . PRO D 1 237 ? 12.870  84.087  70.899  1.00 121.29 ?  253 PRO A CB  1 
ATOM   9928  C CG  . PRO D 1 237 ? 13.277  82.696  70.758  1.00 116.27 ?  253 PRO A CG  1 
ATOM   9929  C CD  . PRO D 1 237 ? 12.296  82.011  69.917  1.00 110.08 ?  253 PRO A CD  1 
ATOM   9930  N N   . SER D 1 238 ? 14.080  84.403  68.134  1.00 106.13 ?  254 SER A N   1 
ATOM   9931  C CA  . SER D 1 238 ? 15.174  84.964  67.375  1.00 108.29 ?  254 SER A CA  1 
ATOM   9932  C C   . SER D 1 238 ? 14.830  85.177  65.898  1.00 109.28 ?  254 SER A C   1 
ATOM   9933  O O   . SER D 1 238 ? 15.756  85.282  65.083  1.00 114.80 ?  254 SER A O   1 
ATOM   9934  C CB  . SER D 1 238 ? 16.410  84.070  67.560  1.00 120.42 ?  254 SER A CB  1 
ATOM   9935  O OG  . SER D 1 238 ? 16.288  82.866  66.821  1.00 118.51 ?  254 SER A OG  1 
ATOM   9936  N N   . TYR D 1 239 ? 13.540  85.299  65.527  1.00 104.08 ?  255 TYR A N   1 
ATOM   9937  C CA  . TYR D 1 239 ? 13.142  85.283  64.111  1.00 95.06  ?  255 TYR A CA  1 
ATOM   9938  C C   . TYR D 1 239 ? 12.042  86.256  63.666  1.00 90.13  ?  255 TYR A C   1 
ATOM   9939  O O   . TYR D 1 239 ? 11.902  86.461  62.457  1.00 88.59  ?  255 TYR A O   1 
ATOM   9940  C CB  . TYR D 1 239 ? 12.689  83.876  63.718  1.00 86.87  ?  255 TYR A CB  1 
ATOM   9941  C CG  . TYR D 1 239 ? 13.726  82.766  63.610  1.00 82.44  ?  255 TYR A CG  1 
ATOM   9942  C CD1 . TYR D 1 239 ? 14.701  82.779  62.614  1.00 71.93  ?  255 TYR A CD1 1 
ATOM   9943  C CD2 . TYR D 1 239 ? 13.733  81.703  64.512  1.00 82.35  ?  255 TYR A CD2 1 
ATOM   9944  C CE1 . TYR D 1 239 ? 15.635  81.742  62.513  1.00 71.70  ?  255 TYR A CE1 1 
ATOM   9945  C CE2 . TYR D 1 239 ? 14.669  80.675  64.421  1.00 75.63  ?  255 TYR A CE2 1 
ATOM   9946  C CZ  . TYR D 1 239 ? 15.617  80.704  63.422  1.00 73.35  ?  255 TYR A CZ  1 
ATOM   9947  O OH  . TYR D 1 239 ? 16.535  79.680  63.327  1.00 75.68  ?  255 TYR A OH  1 
ATOM   9948  N N   . ILE D 1 240 ? 11.204  86.806  64.543  1.00 88.99  ?  256 ILE A N   1 
ATOM   9949  C CA  . ILE D 1 240 ? 10.008  87.534  64.102  1.00 82.20  ?  256 ILE A CA  1 
ATOM   9950  C C   . ILE D 1 240 ? 10.030  88.947  64.673  1.00 82.70  ?  256 ILE A C   1 
ATOM   9951  O O   . ILE D 1 240 ? 10.117  89.126  65.897  1.00 85.19  ?  256 ILE A O   1 
ATOM   9952  C CB  . ILE D 1 240 ? 8.717   86.824  64.538  1.00 79.00  ?  256 ILE A CB  1 
ATOM   9953  C CG1 . ILE D 1 240 ? 8.407   85.626  63.647  1.00 73.61  ?  256 ILE A CG1 1 
ATOM   9954  C CG2 . ILE D 1 240 ? 7.566   87.800  64.489  1.00 75.74  ?  256 ILE A CG2 1 
ATOM   9955  C CD1 . ILE D 1 240 ? 7.613   84.570  64.367  1.00 71.73  ?  256 ILE A CD1 1 
ATOM   9956  N N   . SER D 1 241 ? 9.881   89.962  63.777  1.00 77.00  ?  257 SER A N   1 
ATOM   9957  C CA  . SER D 1 241 ? 9.961   91.346  64.248  1.00 80.10  ?  257 SER A CA  1 
ATOM   9958  C C   . SER D 1 241 ? 8.640   91.789  64.855  1.00 76.22  ?  257 SER A C   1 
ATOM   9959  O O   . SER D 1 241 ? 7.581   91.406  64.369  1.00 76.54  ?  257 SER A O   1 
ATOM   9960  C CB  . SER D 1 241 ? 10.303  92.308  63.123  1.00 78.85  ?  257 SER A CB  1 
ATOM   9961  O OG  . SER D 1 241 ? 9.779   93.598  63.407  1.00 68.91  ?  257 SER A OG  1 
ATOM   9962  N N   . PRO D 1 242 ? 8.676   92.644  65.873  1.00 69.36  ?  258 PRO A N   1 
ATOM   9963  C CA  . PRO D 1 242 ? 7.445   93.060  66.551  1.00 69.37  ?  258 PRO A CA  1 
ATOM   9964  C C   . PRO D 1 242 ? 6.660   94.086  65.775  1.00 72.60  ?  258 PRO A C   1 
ATOM   9965  O O   . PRO D 1 242 ? 5.560   94.469  66.207  1.00 74.76  ?  258 PRO A O   1 
ATOM   9966  C CB  . PRO D 1 242 ? 7.954   93.689  67.839  1.00 70.82  ?  258 PRO A CB  1 
ATOM   9967  C CG  . PRO D 1 242 ? 9.284   94.155  67.489  1.00 79.97  ?  258 PRO A CG  1 
ATOM   9968  C CD  . PRO D 1 242 ? 9.864   93.191  66.514  1.00 79.58  ?  258 PRO A CD  1 
ATOM   9969  N N   . ILE D 1 243 ? 7.220   94.574  64.673  1.00 74.03  ?  259 ILE A N   1 
ATOM   9970  C CA  . ILE D 1 243 ? 6.547   95.480  63.749  1.00 71.89  ?  259 ILE A CA  1 
ATOM   9971  C C   . ILE D 1 243 ? 6.321   94.857  62.403  1.00 71.92  ?  259 ILE A C   1 
ATOM   9972  O O   . ILE D 1 243 ? 5.801   95.527  61.500  1.00 72.09  ?  259 ILE A O   1 
ATOM   9973  C CB  . ILE D 1 243 ? 7.337   96.792  63.612  1.00 68.34  ?  259 ILE A CB  1 
ATOM   9974  C CG1 . ILE D 1 243 ? 8.735   96.497  63.022  1.00 67.98  ?  259 ILE A CG1 1 
ATOM   9975  C CG2 . ILE D 1 243 ? 7.354   97.506  64.917  1.00 70.83  ?  259 ILE A CG2 1 
ATOM   9976  C CD1 . ILE D 1 243 ? 9.466   97.677  62.447  1.00 58.60  ?  259 ILE A CD1 1 
ATOM   9977  N N   . GLY D 1 244 ? 6.689   93.587  62.234  1.00 75.60  ?  260 GLY A N   1 
ATOM   9978  C CA  . GLY D 1 244 ? 6.799   92.988  60.928  1.00 76.38  ?  260 GLY A CA  1 
ATOM   9979  C C   . GLY D 1 244 ? 5.601   92.134  60.554  1.00 75.53  ?  260 GLY A C   1 
ATOM   9980  O O   . GLY D 1 244 ? 4.676   91.900  61.333  1.00 72.16  ?  260 GLY A O   1 
ATOM   9981  N N   . CYS D 1 245 ? 5.639   91.675  59.310  1.00 76.60  ?  261 CYS A N   1 
ATOM   9982  C CA  . CYS D 1 245 ? 4.695   90.691  58.826  1.00 69.05  ?  261 CYS A CA  1 
ATOM   9983  C C   . CYS D 1 245 ? 5.048   89.309  59.383  1.00 68.70  ?  261 CYS A C   1 
ATOM   9984  O O   . CYS D 1 245 ? 6.054   89.111  60.076  1.00 70.78  ?  261 CYS A O   1 
ATOM   9985  C CB  . CYS D 1 245 ? 4.710   90.658  57.308  1.00 65.54  ?  261 CYS A CB  1 
ATOM   9986  S SG  . CYS D 1 245 ? 4.164   92.149  56.561  1.00 68.58  ?  261 CYS A SG  1 
ATOM   9987  N N   . LEU D 1 246 ? 4.229   88.339  59.046  1.00 64.29  ?  262 LEU A N   1 
ATOM   9988  C CA  . LEU D 1 246 ? 4.573   87.049  59.596  1.00 61.32  ?  262 LEU A CA  1 
ATOM   9989  C C   . LEU D 1 246 ? 5.294   86.221  58.539  1.00 61.91  ?  262 LEU A C   1 
ATOM   9990  O O   . LEU D 1 246 ? 4.974   86.317  57.355  1.00 61.66  ?  262 LEU A O   1 
ATOM   9991  C CB  . LEU D 1 246 ? 3.295   86.356  60.056  1.00 61.48  ?  262 LEU A CB  1 
ATOM   9992  C CG  . LEU D 1 246 ? 2.574   87.140  61.168  1.00 58.64  ?  262 LEU A CG  1 
ATOM   9993  C CD1 . LEU D 1 246 ? 1.182   86.628  61.400  1.00 59.89  ?  262 LEU A CD1 1 
ATOM   9994  C CD2 . LEU D 1 246 ? 3.343   87.056  62.473  1.00 60.11  ?  262 LEU A CD2 1 
ATOM   9995  N N   . PRO D 1 247 ? 6.337   85.470  58.866  1.00 64.79  ?  263 PRO A N   1 
ATOM   9996  C CA  . PRO D 1 247 ? 6.952   84.597  57.860  1.00 69.15  ?  263 PRO A CA  1 
ATOM   9997  C C   . PRO D 1 247 ? 6.006   83.484  57.435  1.00 64.93  ?  263 PRO A C   1 
ATOM   9998  O O   . PRO D 1 247 ? 5.498   82.740  58.269  1.00 66.30  ?  263 PRO A O   1 
ATOM   9999  C CB  . PRO D 1 247 ? 8.190   84.052  58.577  1.00 66.97  ?  263 PRO A CB  1 
ATOM   10000 C CG  . PRO D 1 247 ? 8.507   85.091  59.574  1.00 66.74  ?  263 PRO A CG  1 
ATOM   10001 C CD  . PRO D 1 247 ? 7.214   85.667  60.024  1.00 66.29  ?  263 PRO A CD  1 
ATOM   10002 N N   . ALA D 1 248 ? 5.806   83.359  56.116  1.00 66.19  ?  264 ALA A N   1 
ATOM   10003 C CA  . ALA D 1 248 ? 4.740   82.511  55.579  1.00 71.13  ?  264 ALA A CA  1 
ATOM   10004 C C   . ALA D 1 248 ? 4.880   81.045  56.016  1.00 76.26  ?  264 ALA A C   1 
ATOM   10005 O O   . ALA D 1 248 ? 3.868   80.361  56.267  1.00 76.20  ?  264 ALA A O   1 
ATOM   10006 C CB  . ALA D 1 248 ? 4.710   82.642  54.051  1.00 67.64  ?  264 ALA A CB  1 
ATOM   10007 N N   . HIS D 1 249 ? 6.107   80.552  56.142  1.00 62.71  ?  265 HIS A N   1 
ATOM   10008 C CA  . HIS D 1 249 ? 6.329   79.173  56.539  1.00 65.33  ?  265 HIS A CA  1 
ATOM   10009 C C   . HIS D 1 249 ? 6.046   78.909  57.998  1.00 64.41  ?  265 HIS A C   1 
ATOM   10010 O O   . HIS D 1 249 ? 6.321   77.810  58.479  1.00 66.40  ?  265 HIS A O   1 
ATOM   10011 C CB  . HIS D 1 249 ? 7.768   78.808  56.215  1.00 65.72  ?  265 HIS A CB  1 
ATOM   10012 C CG  . HIS D 1 249 ? 8.772   79.567  57.027  1.00 71.26  ?  265 HIS A CG  1 
ATOM   10013 N ND1 . HIS D 1 249 ? 8.928   80.933  56.918  1.00 68.10  ?  265 HIS A ND1 1 
ATOM   10014 C CD2 . HIS D 1 249 ? 9.707   79.157  57.914  1.00 71.72  ?  265 HIS A CD2 1 
ATOM   10015 C CE1 . HIS D 1 249 ? 9.891   81.338  57.724  1.00 64.10  ?  265 HIS A CE1 1 
ATOM   10016 N NE2 . HIS D 1 249 ? 10.384  80.278  58.337  1.00 71.38  ?  265 HIS A NE2 1 
ATOM   10017 N N   . LEU D 1 250 ? 5.534   79.891  58.720  1.00 64.50  ?  266 LEU A N   1 
ATOM   10018 C CA  . LEU D 1 250 ? 5.316   79.751  60.149  1.00 67.05  ?  266 LEU A CA  1 
ATOM   10019 C C   . LEU D 1 250 ? 3.842   79.855  60.496  1.00 63.54  ?  266 LEU A C   1 
ATOM   10020 O O   . LEU D 1 250 ? 3.499   80.086  61.660  1.00 64.89  ?  266 LEU A O   1 
ATOM   10021 C CB  . LEU D 1 250 ? 6.128   80.800  60.920  1.00 72.63  ?  266 LEU A CB  1 
ATOM   10022 C CG  . LEU D 1 250 ? 7.651   80.690  60.778  1.00 68.67  ?  266 LEU A CG  1 
ATOM   10023 C CD1 . LEU D 1 250 ? 8.369   81.796  61.531  1.00 74.95  ?  266 LEU A CD1 1 
ATOM   10024 C CD2 . LEU D 1 250 ? 8.109   79.307  61.234  1.00 79.89  ?  266 LEU A CD2 1 
ATOM   10025 N N   . LEU D 1 251 ? 2.965   79.704  59.509  1.00 65.69  ?  267 LEU A N   1 
ATOM   10026 C CA  . LEU D 1 251 ? 1.550   79.943  59.720  1.00 59.95  ?  267 LEU A CA  1 
ATOM   10027 C C   . LEU D 1 251 ? 0.748   78.691  59.951  1.00 57.87  ?  267 LEU A C   1 
ATOM   10028 O O   . LEU D 1 251 ? -0.434  78.795  60.271  1.00 62.97  ?  267 LEU A O   1 
ATOM   10029 C CB  . LEU D 1 251 ? 0.971   80.729  58.561  1.00 58.36  ?  267 LEU A CB  1 
ATOM   10030 C CG  . LEU D 1 251 ? 1.594   82.105  58.554  1.00 57.86  ?  267 LEU A CG  1 
ATOM   10031 C CD1 . LEU D 1 251 ? 1.164   82.839  57.323  1.00 57.85  ?  267 LEU A CD1 1 
ATOM   10032 C CD2 . LEU D 1 251 ? 1.078   82.804  59.798  1.00 50.08  ?  267 LEU A CD2 1 
ATOM   10033 N N   . GLY D 1 252 ? 1.343   77.523  59.843  1.00 57.24  ?  268 GLY A N   1 
ATOM   10034 C CA  . GLY D 1 252 ? 0.695   76.351  60.370  1.00 60.00  ?  268 GLY A CA  1 
ATOM   10035 C C   . GLY D 1 252 ? 0.077   75.460  59.330  1.00 60.47  ?  268 GLY A C   1 
ATOM   10036 O O   . GLY D 1 252 ? -0.530  74.445  59.695  1.00 63.15  ?  268 GLY A O   1 
ATOM   10037 N N   . ASP D 1 253 ? 0.171   75.832  58.057  1.00 60.15  ?  269 ASP A N   1 
ATOM   10038 C CA  . ASP D 1 253 ? 0.014   74.913  56.942  1.00 56.54  ?  269 ASP A CA  1 
ATOM   10039 C C   . ASP D 1 253 ? 0.925   75.417  55.832  1.00 54.93  ?  269 ASP A C   1 
ATOM   10040 O O   . ASP D 1 253 ? 1.703   76.352  56.027  1.00 60.25  ?  269 ASP A O   1 
ATOM   10041 C CB  . ASP D 1 253 ? -1.472  74.747  56.572  1.00 60.18  ?  269 ASP A CB  1 
ATOM   10042 C CG  . ASP D 1 253 ? -2.098  75.994  55.916  1.00 60.43  ?  269 ASP A CG  1 
ATOM   10043 O OD1 . ASP D 1 253 ? -1.358  76.849  55.354  1.00 60.40  ?  269 ASP A OD1 1 
ATOM   10044 O OD2 . ASP D 1 253 ? -3.358  76.116  55.985  1.00 56.49  -1 269 ASP A OD2 1 
ATOM   10045 N N   . MET D 1 254 ? 0.843   74.788  54.669  1.00 51.52  ?  270 MET A N   1 
ATOM   10046 C CA  . MET D 1 254 ? 1.775   75.078  53.589  1.00 52.37  ?  270 MET A CA  1 
ATOM   10047 C C   . MET D 1 254 ? 1.645   76.470  52.995  1.00 52.97  ?  270 MET A C   1 
ATOM   10048 O O   . MET D 1 254 ? 2.591   76.947  52.365  1.00 55.82  ?  270 MET A O   1 
ATOM   10049 C CB  . MET D 1 254 ? 1.620   74.016  52.502  1.00 56.38  ?  270 MET A CB  1 
ATOM   10050 C CG  . MET D 1 254 ? 2.489   74.231  51.271  1.00 59.14  ?  270 MET A CG  1 
ATOM   10051 S SD  . MET D 1 254 ? 4.224   74.389  51.668  1.00 50.13  ?  270 MET A SD  1 
ATOM   10052 C CE  . MET D 1 254 ? 4.697   72.662  51.573  1.00 57.61  ?  270 MET A CE  1 
ATOM   10053 N N   . TRP D 1 255 ? 0.513   77.143  53.145  1.00 52.62  ?  271 TRP A N   1 
ATOM   10054 C CA  . TRP D 1 255 ? 0.371   78.428  52.489  1.00 54.31  ?  271 TRP A CA  1 
ATOM   10055 C C   . TRP D 1 255 ? -0.124  79.473  53.451  1.00 57.19  ?  271 TRP A C   1 
ATOM   10056 O O   . TRP D 1 255 ? -0.304  80.632  53.058  1.00 57.54  ?  271 TRP A O   1 
ATOM   10057 C CB  . TRP D 1 255 ? -0.610  78.349  51.317  1.00 55.82  ?  271 TRP A CB  1 
ATOM   10058 C CG  . TRP D 1 255 ? -0.379  77.168  50.450  1.00 57.39  ?  271 TRP A CG  1 
ATOM   10059 C CD1 . TRP D 1 255 ? 0.438   77.070  49.366  1.00 55.20  ?  271 TRP A CD1 1 
ATOM   10060 C CD2 . TRP D 1 255 ? -0.984  75.892  50.617  1.00 54.31  ?  271 TRP A CD2 1 
ATOM   10061 N NE1 . TRP D 1 255 ? 0.376   75.804  48.850  1.00 54.49  ?  271 TRP A NE1 1 
ATOM   10062 C CE2 . TRP D 1 255 ? -0.495  75.063  49.606  1.00 56.42  ?  271 TRP A CE2 1 
ATOM   10063 C CE3 . TRP D 1 255 ? -1.892  75.377  51.529  1.00 51.86  ?  271 TRP A CE3 1 
ATOM   10064 C CZ2 . TRP D 1 255 ? -0.887  73.744  49.482  1.00 57.47  ?  271 TRP A CZ2 1 
ATOM   10065 C CZ3 . TRP D 1 255 ? -2.263  74.092  51.416  1.00 55.82  ?  271 TRP A CZ3 1 
ATOM   10066 C CH2 . TRP D 1 255 ? -1.771  73.277  50.400  1.00 58.45  ?  271 TRP A CH2 1 
ATOM   10067 N N   . GLY D 1 256 ? -0.376  79.095  54.695  1.00 66.62  ?  272 GLY A N   1 
ATOM   10068 C CA  . GLY D 1 256 ? -1.009  80.007  55.615  1.00 65.80  ?  272 GLY A CA  1 
ATOM   10069 C C   . GLY D 1 256 ? -2.431  80.301  55.235  1.00 67.44  ?  272 GLY A C   1 
ATOM   10070 O O   . GLY D 1 256 ? -2.911  81.422  55.473  1.00 68.85  ?  272 GLY A O   1 
ATOM   10071 N N   . ARG D 1 257 ? -3.096  79.325  54.596  1.00 59.53  ?  273 ARG A N   1 
ATOM   10072 C CA  . ARG D 1 257 ? -4.487  79.478  54.209  1.00 53.69  ?  273 ARG A CA  1 
ATOM   10073 C C   . ARG D 1 257 ? -5.359  79.658  55.432  1.00 56.67  ?  273 ARG A C   1 
ATOM   10074 O O   . ARG D 1 257 ? -6.222  80.545  55.478  1.00 57.00  ?  273 ARG A O   1 
ATOM   10075 C CB  . ARG D 1 257 ? -4.938  78.265  53.422  1.00 54.97  ?  273 ARG A CB  1 
ATOM   10076 C CG  . ARG D 1 257 ? -6.385  78.410  52.942  1.00 61.28  ?  273 ARG A CG  1 
ATOM   10077 C CD  . ARG D 1 257 ? -6.836  77.259  52.044  1.00 59.96  ?  273 ARG A CD  1 
ATOM   10078 N NE  . ARG D 1 257 ? -8.215  77.408  51.602  1.00 58.22  ?  273 ARG A NE  1 
ATOM   10079 C CZ  . ARG D 1 257 ? -8.988  76.388  51.272  1.00 57.52  ?  273 ARG A CZ  1 
ATOM   10080 N NH1 . ARG D 1 257 ? -8.550  75.141  51.349  1.00 65.05  ?  273 ARG A NH1 1 
ATOM   10081 N NH2 . ARG D 1 257 ? -10.223 76.624  50.844  1.00 55.26  ?  273 ARG A NH2 1 
ATOM   10082 N N   . PHE D 1 258 ? -5.138  78.821  56.436  1.00 56.80  ?  274 PHE A N   1 
ATOM   10083 C CA  . PHE D 1 258 ? -5.792  78.933  57.723  1.00 57.73  ?  274 PHE A CA  1 
ATOM   10084 C C   . PHE D 1 258 ? -4.722  78.987  58.798  1.00 60.42  ?  274 PHE A C   1 
ATOM   10085 O O   . PHE D 1 258 ? -3.646  78.399  58.659  1.00 59.83  ?  274 PHE A O   1 
ATOM   10086 C CB  . PHE D 1 258 ? -6.721  77.733  58.006  1.00 60.48  ?  274 PHE A CB  1 
ATOM   10087 C CG  . PHE D 1 258 ? -7.670  77.409  56.888  1.00 58.34  ?  274 PHE A CG  1 
ATOM   10088 C CD1 . PHE D 1 258 ? -8.847  78.123  56.717  1.00 54.76  ?  274 PHE A CD1 1 
ATOM   10089 C CD2 . PHE D 1 258 ? -7.370  76.378  56.000  1.00 61.41  ?  274 PHE A CD2 1 
ATOM   10090 C CE1 . PHE D 1 258 ? -9.705  77.810  55.675  1.00 58.58  ?  274 PHE A CE1 1 
ATOM   10091 C CE2 . PHE D 1 258 ? -8.228  76.052  54.950  1.00 59.03  ?  274 PHE A CE2 1 
ATOM   10092 C CZ  . PHE D 1 258 ? -9.396  76.771  54.785  1.00 58.99  ?  274 PHE A CZ  1 
ATOM   10093 N N   . TRP D 1 259 ? -5.030  79.662  59.896  1.00 61.42  ?  275 TRP A N   1 
ATOM   10094 C CA  . TRP D 1 259 ? -4.156  79.683  61.070  1.00 58.01  ?  275 TRP A CA  1 
ATOM   10095 C C   . TRP D 1 259 ? -4.628  78.710  62.123  1.00 58.61  ?  275 TRP A C   1 
ATOM   10096 O O   . TRP D 1 259 ? -4.572  79.007  63.310  1.00 58.94  ?  275 TRP A O   1 
ATOM   10097 C CB  . TRP D 1 259 ? -4.096  81.090  61.652  1.00 55.28  ?  275 TRP A CB  1 
ATOM   10098 C CG  . TRP D 1 259 ? -3.393  82.082  60.794  1.00 51.57  ?  275 TRP A CG  1 
ATOM   10099 C CD1 . TRP D 1 259 ? -2.810  81.861  59.574  1.00 49.62  ?  275 TRP A CD1 1 
ATOM   10100 C CD2 . TRP D 1 259 ? -3.337  83.491  61.013  1.00 49.40  ?  275 TRP A CD2 1 
ATOM   10101 N NE1 . TRP D 1 259 ? -2.322  83.036  59.064  1.00 50.83  ?  275 TRP A NE1 1 
ATOM   10102 C CE2 . TRP D 1 259 ? -2.640  84.054  59.925  1.00 48.39  ?  275 TRP A CE2 1 
ATOM   10103 C CE3 . TRP D 1 259 ? -3.782  84.327  62.039  1.00 50.06  ?  275 TRP A CE3 1 
ATOM   10104 C CZ2 . TRP D 1 259 ? -2.375  85.416  59.835  1.00 50.91  ?  275 TRP A CZ2 1 
ATOM   10105 C CZ3 . TRP D 1 259 ? -3.525  85.673  61.946  1.00 52.33  ?  275 TRP A CZ3 1 
ATOM   10106 C CH2 . TRP D 1 259 ? -2.828  86.207  60.848  1.00 52.92  ?  275 TRP A CH2 1 
ATOM   10107 N N   . THR D 1 260 ? -5.150  77.562  61.709  1.00 67.74  ?  276 THR A N   1 
ATOM   10108 C CA  . THR D 1 260 ? -5.707  76.647  62.693  1.00 68.46  ?  276 THR A CA  1 
ATOM   10109 C C   . THR D 1 260 ? -4.617  76.020  63.530  1.00 71.62  ?  276 THR A C   1 
ATOM   10110 O O   . THR D 1 260 ? -4.692  76.019  64.765  1.00 74.77  ?  276 THR A O   1 
ATOM   10111 C CB  . THR D 1 260 ? -6.567  75.570  62.042  1.00 65.92  ?  276 THR A CB  1 
ATOM   10112 O OG1 . THR D 1 260 ? -7.466  76.179  61.093  1.00 65.17  ?  276 THR A OG1 1 
ATOM   10113 C CG2 . THR D 1 260 ? -7.327  74.825  63.123  1.00 71.39  ?  276 THR A CG2 1 
ATOM   10114 N N   . ASN D 1 261 ? -3.569  75.543  62.892  1.00 61.88  ?  277 ASN A N   1 
ATOM   10115 C CA  . ASN D 1 261 ? -2.624  74.793  63.691  1.00 61.89  ?  277 ASN A CA  1 
ATOM   10116 C C   . ASN D 1 261 ? -1.812  75.661  64.637  1.00 59.66  ?  277 ASN A C   1 
ATOM   10117 O O   . ASN D 1 261 ? -1.123  75.115  65.517  1.00 54.14  ?  277 ASN A O   1 
ATOM   10118 C CB  . ASN D 1 261 ? -1.752  73.988  62.770  1.00 62.58  ?  277 ASN A CB  1 
ATOM   10119 C CG  . ASN D 1 261 ? -2.565  72.987  62.066  1.00 62.19  ?  277 ASN A CG  1 
ATOM   10120 O OD1 . ASN D 1 261 ? -3.400  72.343  62.695  1.00 61.74  ?  277 ASN A OD1 1 
ATOM   10121 N ND2 . ASN D 1 261 ? -2.346  72.822  60.772  1.00 65.70  ?  277 ASN A ND2 1 
ATOM   10122 N N   . LEU D 1 262 ? -1.934  76.980  64.533  1.00 55.20  ?  278 LEU A N   1 
ATOM   10123 C CA  . LEU D 1 262 ? -1.285  77.811  65.527  1.00 53.24  ?  278 LEU A CA  1 
ATOM   10124 C C   . LEU D 1 262 ? -1.991  77.801  66.875  1.00 54.83  ?  278 LEU A C   1 
ATOM   10125 O O   . LEU D 1 262 ? -1.507  78.489  67.782  1.00 57.60  ?  278 LEU A O   1 
ATOM   10126 C CB  . LEU D 1 262 ? -1.150  79.254  65.045  1.00 50.25  ?  278 LEU A CB  1 
ATOM   10127 C CG  . LEU D 1 262 ? -0.486  79.465  63.693  1.00 52.31  ?  278 LEU A CG  1 
ATOM   10128 C CD1 . LEU D 1 262 ? -0.260  80.937  63.508  1.00 52.25  ?  278 LEU A CD1 1 
ATOM   10129 C CD2 . LEU D 1 262 ? 0.777   78.672  63.520  1.00 57.24  ?  278 LEU A CD2 1 
ATOM   10130 N N   . TYR D 1 263 ? -3.084  77.041  67.069  1.00 55.39  ?  279 TYR A N   1 
ATOM   10131 C CA  . TYR D 1 263 ? -3.772  77.098  68.370  1.00 56.46  ?  279 TYR A CA  1 
ATOM   10132 C C   . TYR D 1 263 ? -2.904  76.583  69.511  1.00 55.83  ?  279 TYR A C   1 
ATOM   10133 O O   . TYR D 1 263 ? -2.858  77.209  70.588  1.00 54.81  ?  279 TYR A O   1 
ATOM   10134 C CB  . TYR D 1 263 ? -5.099  76.354  68.339  1.00 56.77  ?  279 TYR A CB  1 
ATOM   10135 C CG  . TYR D 1 263 ? -5.898  76.352  69.650  1.00 52.96  ?  279 TYR A CG  1 
ATOM   10136 C CD1 . TYR D 1 263 ? -6.623  77.477  70.064  1.00 53.77  ?  279 TYR A CD1 1 
ATOM   10137 C CD2 . TYR D 1 263 ? -6.062  75.173  70.381  1.00 50.93  ?  279 TYR A CD2 1 
ATOM   10138 C CE1 . TYR D 1 263 ? -7.404  77.462  71.253  1.00 57.16  ?  279 TYR A CE1 1 
ATOM   10139 C CE2 . TYR D 1 263 ? -6.858  75.136  71.550  1.00 59.37  ?  279 TYR A CE2 1 
ATOM   10140 C CZ  . TYR D 1 263 ? -7.524  76.281  71.990  1.00 61.74  ?  279 TYR A CZ  1 
ATOM   10141 O OH  . TYR D 1 263 ? -8.293  76.232  73.157  1.00 63.53  ?  279 TYR A OH  1 
ATOM   10142 N N   . SER D 1 264 ? -2.185  75.463  69.288  1.00 57.02  ?  280 SER A N   1 
ATOM   10143 C CA  . SER D 1 264 ? -1.164  75.015  70.244  1.00 54.08  ?  280 SER A CA  1 
ATOM   10144 C C   . SER D 1 264 ? -0.283  76.168  70.712  1.00 56.39  ?  280 SER A C   1 
ATOM   10145 O O   . SER D 1 264 ? -0.078  76.348  71.915  1.00 57.89  ?  280 SER A O   1 
ATOM   10146 C CB  . SER D 1 264 ? -0.297  73.914  69.634  1.00 52.61  ?  280 SER A CB  1 
ATOM   10147 O OG  . SER D 1 264 ? 0.678   74.422  68.745  1.00 52.78  ?  280 SER A OG  1 
ATOM   10148 N N   . LEU D 1 265 ? 0.204   76.993  69.775  1.00 53.25  ?  281 LEU A N   1 
ATOM   10149 C CA  . LEU D 1 265 ? 1.152   78.064  70.052  1.00 47.61  ?  281 LEU A CA  1 
ATOM   10150 C C   . LEU D 1 265 ? 0.501   79.360  70.529  1.00 54.40  ?  281 LEU A C   1 
ATOM   10151 O O   . LEU D 1 265 ? 1.234   80.290  70.913  1.00 53.05  ?  281 LEU A O   1 
ATOM   10152 C CB  . LEU D 1 265 ? 1.963   78.376  68.801  1.00 45.98  ?  281 LEU A CB  1 
ATOM   10153 C CG  . LEU D 1 265 ? 3.018   77.383  68.329  1.00 51.30  ?  281 LEU A CG  1 
ATOM   10154 C CD1 . LEU D 1 265 ? 3.710   77.978  67.124  1.00 57.03  ?  281 LEU A CD1 1 
ATOM   10155 C CD2 . LEU D 1 265 ? 4.041   77.022  69.423  1.00 55.42  ?  281 LEU A CD2 1 
ATOM   10156 N N   . THR D 1 266 ? -0.832  79.462  70.417  1.00 56.83  ?  282 THR A N   1 
ATOM   10157 C CA  . THR D 1 266 ? -1.522  80.752  70.707  1.00 56.38  ?  282 THR A CA  1 
ATOM   10158 C C   . THR D 1 266 ? -2.711  80.615  71.663  1.00 56.93  ?  282 THR A C   1 
ATOM   10159 O O   . THR D 1 266 ? -3.423  81.609  71.816  1.00 58.44  ?  282 THR A O   1 
ATOM   10160 C CB  . THR D 1 266 ? -2.058  81.349  69.404  1.00 47.94  ?  282 THR A CB  1 
ATOM   10161 O OG1 . THR D 1 266 ? -2.987  80.417  68.860  1.00 52.84  ?  282 THR A OG1 1 
ATOM   10162 C CG2 . THR D 1 266 ? -0.976  81.636  68.386  1.00 54.90  ?  282 THR A CG2 1 
ATOM   10163 N N   . VAL D 1 267 ? -2.909  79.468  72.300  1.00 58.32  ?  283 VAL A N   1 
ATOM   10164 C CA  . VAL D 1 267 ? -4.117  79.263  73.146  1.00 63.01  ?  283 VAL A CA  1 
ATOM   10165 C C   . VAL D 1 267 ? -4.203  80.371  74.196  1.00 66.59  ?  283 VAL A C   1 
ATOM   10166 O O   . VAL D 1 267 ? -3.190  80.646  74.837  1.00 73.86  ?  283 VAL A O   1 
ATOM   10167 C CB  . VAL D 1 267 ? -4.118  77.854  73.766  1.00 64.96  ?  283 VAL A CB  1 
ATOM   10168 C CG1 . VAL D 1 267 ? -2.767  77.486  74.354  1.00 66.45  ?  283 VAL A CG1 1 
ATOM   10169 C CG2 . VAL D 1 267 ? -5.220  77.710  74.795  1.00 66.95  ?  283 VAL A CG2 1 
ATOM   10170 N N   . PRO D 1 268 ? -5.358  81.040  74.373  1.00 63.80  ?  284 PRO A N   1 
ATOM   10171 C CA  . PRO D 1 268 ? -5.478  82.179  75.298  1.00 65.84  ?  284 PRO A CA  1 
ATOM   10172 C C   . PRO D 1 268 ? -5.479  81.795  76.788  1.00 69.25  ?  284 PRO A C   1 
ATOM   10173 O O   . PRO D 1 268 ? -4.965  82.570  77.566  1.00 75.07  ?  284 PRO A O   1 
ATOM   10174 C CB  . PRO D 1 268 ? -6.836  82.778  74.913  1.00 63.28  ?  284 PRO A CB  1 
ATOM   10175 C CG  . PRO D 1 268 ? -7.128  82.214  73.544  1.00 64.67  ?  284 PRO A CG  1 
ATOM   10176 C CD  . PRO D 1 268 ? -6.570  80.810  73.605  1.00 64.20  ?  284 PRO A CD  1 
ATOM   10177 N N   . PHE D 1 269 ? -6.100  80.673  77.161  1.00 63.62  ?  285 PHE A N   1 
ATOM   10178 C CA  . PHE D 1 269 ? -6.086  80.177  78.568  1.00 67.54  ?  285 PHE A CA  1 
ATOM   10179 C C   . PHE D 1 269 ? -5.698  78.710  78.422  1.00 71.83  ?  285 PHE A C   1 
ATOM   10180 O O   . PHE D 1 269 ? -6.565  77.835  78.468  1.00 75.32  ?  285 PHE A O   1 
ATOM   10181 C CB  . PHE D 1 269 ? -7.422  80.536  79.221  1.00 67.99  ?  285 PHE A CB  1 
ATOM   10182 C CG  . PHE D 1 269 ? -7.673  82.021  79.363  1.00 67.22  ?  285 PHE A CG  1 
ATOM   10183 C CD1 . PHE D 1 269 ? -7.078  82.739  80.383  1.00 69.72  ?  285 PHE A CD1 1 
ATOM   10184 C CD2 . PHE D 1 269 ? -8.493  82.699  78.476  1.00 69.14  ?  285 PHE A CD2 1 
ATOM   10185 C CE1 . PHE D 1 269 ? -7.307  84.098  80.528  1.00 71.99  ?  285 PHE A CE1 1 
ATOM   10186 C CE2 . PHE D 1 269 ? -8.724  84.057  78.615  1.00 67.63  ?  285 PHE A CE2 1 
ATOM   10187 C CZ  . PHE D 1 269 ? -8.129  84.755  79.642  1.00 70.61  ?  285 PHE A CZ  1 
ATOM   10188 N N   . GLY D 1 270 ? -4.400  78.457  78.347  1.00 72.43  ?  286 GLY A N   1 
ATOM   10189 C CA  . GLY D 1 270 ? -3.916  77.153  77.928  1.00 74.63  ?  286 GLY A CA  1 
ATOM   10190 C C   . GLY D 1 270 ? -4.227  76.011  78.869  1.00 74.87  ?  286 GLY A C   1 
ATOM   10191 O O   . GLY D 1 270 ? -4.152  74.847  78.453  1.00 69.89  ?  286 GLY A O   1 
ATOM   10192 N N   . GLN D 1 271 ? -4.583  76.306  80.115  1.00 73.95  ?  287 GLN A N   1 
ATOM   10193 C CA  . GLN D 1 271 ? -4.829  75.254  81.085  1.00 79.72  ?  287 GLN A CA  1 
ATOM   10194 C C   . GLN D 1 271 ? -6.293  74.889  81.243  1.00 86.03  ?  287 GLN A C   1 
ATOM   10195 O O   . GLN D 1 271 ? -6.583  73.860  81.861  1.00 94.66  ?  287 GLN A O   1 
ATOM   10196 C CB  . GLN D 1 271 ? -4.266  75.656  82.441  1.00 88.07  ?  287 GLN A CB  1 
ATOM   10197 C CG  . GLN D 1 271 ? -2.849  76.172  82.355  1.00 96.04  ?  287 GLN A CG  1 
ATOM   10198 C CD  . GLN D 1 271 ? -2.167  76.137  83.691  1.00 102.50 ?  287 GLN A CD  1 
ATOM   10199 O OE1 . GLN D 1 271 ? -1.710  77.163  84.192  1.00 105.98 ?  287 GLN A OE1 1 
ATOM   10200 N NE2 . GLN D 1 271 ? -2.122  74.955  84.299  1.00 101.64 ?  287 GLN A NE2 1 
ATOM   10201 N N   . LYS D 1 272 ? -7.211  75.694  80.699  1.00 91.45  ?  288 LYS A N   1 
ATOM   10202 C CA  . LYS D 1 272 ? -8.633  75.414  80.817  1.00 91.43  ?  288 LYS A CA  1 
ATOM   10203 C C   . LYS D 1 272 ? -9.009  74.234  79.924  1.00 100.95 ?  288 LYS A C   1 
ATOM   10204 O O   . LYS D 1 272 ? -8.541  74.131  78.784  1.00 91.40  ?  288 LYS A O   1 
ATOM   10205 C CB  . LYS D 1 272 ? -9.460  76.630  80.417  1.00 87.33  ?  288 LYS A CB  1 
ATOM   10206 C CG  . LYS D 1 272 ? -9.593  77.720  81.473  1.00 89.07  ?  288 LYS A CG  1 
ATOM   10207 C CD  . LYS D 1 272 ? -10.556 77.465  82.635  1.00 89.40  ?  288 LYS A CD  1 
ATOM   10208 C CE  . LYS D 1 272 ? -10.605 78.751  83.476  1.00 86.96  ?  288 LYS A CE  1 
ATOM   10209 N NZ  . LYS D 1 272 ? -11.708 78.867  84.453  1.00 96.88  ?  288 LYS A NZ  1 
ATOM   10210 N N   . PRO D 1 273 ? -9.872  73.345  80.398  1.00 123.37 ?  289 PRO A N   1 
ATOM   10211 C CA  . PRO D 1 273 ? -10.235 72.190  79.582  1.00 124.66 ?  289 PRO A CA  1 
ATOM   10212 C C   . PRO D 1 273 ? -10.911 72.648  78.300  1.00 114.88 ?  289 PRO A C   1 
ATOM   10213 O O   . PRO D 1 273 ? -11.613 73.661  78.265  1.00 112.27 ?  289 PRO A O   1 
ATOM   10214 C CB  . PRO D 1 273 ? -11.186 71.402  80.489  1.00 127.35 ?  289 PRO A CB  1 
ATOM   10215 C CG  . PRO D 1 273 ? -11.782 72.451  81.415  1.00 130.54 ?  289 PRO A CG  1 
ATOM   10216 C CD  . PRO D 1 273 ? -10.674 73.439  81.638  1.00 124.55 ?  289 PRO A CD  1 
ATOM   10217 N N   . ASN D 1 274 ? -10.684 71.897  77.238  1.00 107.04 ?  290 ASN A N   1 
ATOM   10218 C CA  . ASN D 1 274 ? -11.305 72.140  75.944  1.00 97.45  ?  290 ASN A CA  1 
ATOM   10219 C C   . ASN D 1 274 ? -12.429 71.126  75.729  1.00 90.61  ?  290 ASN A C   1 
ATOM   10220 O O   . ASN D 1 274 ? -12.183 69.924  75.829  1.00 94.68  ?  290 ASN A O   1 
ATOM   10221 C CB  . ASN D 1 274 ? -10.230 72.018  74.868  1.00 98.56  ?  290 ASN A CB  1 
ATOM   10222 C CG  . ASN D 1 274 ? -10.660 72.569  73.542  1.00 105.34 ?  290 ASN A CG  1 
ATOM   10223 O OD1 . ASN D 1 274 ? -10.874 73.779  73.399  1.00 112.11 ?  290 ASN A OD1 1 
ATOM   10224 N ND2 . ASN D 1 274 ? -10.731 71.697  72.534  1.00 100.68 ?  290 ASN A ND2 1 
ATOM   10225 N N   . ILE D 1 275 ? -13.645 71.603  75.411  1.00 78.62  ?  291 ILE A N   1 
ATOM   10226 C CA  . ILE D 1 275 ? -14.881 70.792  75.468  1.00 68.54  ?  291 ILE A CA  1 
ATOM   10227 C C   . ILE D 1 275 ? -14.857 69.675  74.434  1.00 62.84  ?  291 ILE A C   1 
ATOM   10228 O O   . ILE D 1 275 ? -14.875 69.928  73.222  1.00 63.03  ?  291 ILE A O   1 
ATOM   10229 C CB  . ILE D 1 275 ? -16.149 71.639  75.246  1.00 65.42  ?  291 ILE A CB  1 
ATOM   10230 C CG1 . ILE D 1 275 ? -16.417 72.643  76.360  1.00 59.26  ?  291 ILE A CG1 1 
ATOM   10231 C CG2 . ILE D 1 275 ? -17.365 70.717  75.102  1.00 59.82  ?  291 ILE A CG2 1 
ATOM   10232 C CD1 . ILE D 1 275 ? -17.757 73.357  76.250  1.00 56.01  ?  291 ILE A CD1 1 
ATOM   10233 N N   . ASP D 1 276 ? -14.747 68.426  74.897  1.00 52.93  ?  292 ASP A N   1 
ATOM   10234 C CA  . ASP D 1 276 ? -14.739 67.255  73.978  1.00 51.42  ?  292 ASP A CA  1 
ATOM   10235 C C   . ASP D 1 276 ? -15.613 66.156  74.573  1.00 53.98  ?  292 ASP A C   1 
ATOM   10236 O O   . ASP D 1 276 ? -15.242 65.613  75.618  1.00 52.10  ?  292 ASP A O   1 
ATOM   10237 C CB  . ASP D 1 276 ? -13.332 66.733  73.693  1.00 55.90  ?  292 ASP A CB  1 
ATOM   10238 C CG  . ASP D 1 276 ? -13.292 65.530  72.769  1.00 54.10  ?  292 ASP A CG  1 
ATOM   10239 O OD1 . ASP D 1 276 ? -14.342 65.191  72.199  1.00 52.15  ?  292 ASP A OD1 1 
ATOM   10240 O OD2 . ASP D 1 276 ? -12.205 64.946  72.623  1.00 60.43  -1 292 ASP A OD2 1 
ATOM   10241 N N   . VAL D 1 277 ? -16.709 65.820  73.901  1.00 56.55  ?  293 VAL A N   1 
ATOM   10242 C CA  . VAL D 1 277 ? -17.680 64.834  74.444  1.00 53.88  ?  293 VAL A CA  1 
ATOM   10243 C C   . VAL D 1 277 ? -17.377 63.456  73.870  1.00 54.16  ?  293 VAL A C   1 
ATOM   10244 O O   . VAL D 1 277 ? -18.232 62.575  73.984  1.00 57.24  ?  293 VAL A O   1 
ATOM   10245 C CB  . VAL D 1 277 ? -19.104 65.288  74.093  1.00 49.85  ?  293 VAL A CB  1 
ATOM   10246 C CG1 . VAL D 1 277 ? -19.439 66.628  74.728  1.00 52.02  ?  293 VAL A CG1 1 
ATOM   10247 C CG2 . VAL D 1 277 ? -19.302 65.356  72.590  1.00 51.71  ?  293 VAL A CG2 1 
ATOM   10248 N N   . THR D 1 278 ? -16.198 63.275  73.284  1.00 54.57  ?  294 THR A N   1 
ATOM   10249 C CA  . THR D 1 278 ? -15.904 61.976  72.632  1.00 54.04  ?  294 THR A CA  1 
ATOM   10250 C C   . THR D 1 278 ? -15.965 60.879  73.692  1.00 57.39  ?  294 THR A C   1 
ATOM   10251 O O   . THR D 1 278 ? -16.632 59.863  73.448  1.00 54.73  ?  294 THR A O   1 
ATOM   10252 C CB  . THR D 1 278 ? -14.558 61.995  71.907  1.00 51.97  ?  294 THR A CB  1 
ATOM   10253 O OG1 . THR D 1 278 ? -14.653 62.946  70.848  1.00 58.75  ?  294 THR A OG1 1 
ATOM   10254 C CG2 . THR D 1 278 ? -14.180 60.643  71.349  1.00 48.24  ?  294 THR A CG2 1 
ATOM   10255 N N   . ASP D 1 279 ? -15.315 61.095  74.835  1.00 58.26  ?  295 ASP A N   1 
ATOM   10256 C CA  . ASP D 1 279 ? -15.377 60.077  75.868  1.00 57.29  ?  295 ASP A CA  1 
ATOM   10257 C C   . ASP D 1 279 ? -16.811 59.891  76.341  1.00 55.50  ?  295 ASP A C   1 
ATOM   10258 O O   . ASP D 1 279 ? -17.213 58.789  76.727  1.00 53.84  ?  295 ASP A O   1 
ATOM   10259 C CB  . ASP D 1 279 ? -14.492 60.480  77.043  1.00 65.11  ?  295 ASP A CB  1 
ATOM   10260 C CG  . ASP D 1 279 ? -13.026 60.192  76.810  1.00 65.31  ?  295 ASP A CG  1 
ATOM   10261 O OD1 . ASP D 1 279 ? -12.668 59.329  75.978  1.00 64.97  ?  295 ASP A OD1 1 
ATOM   10262 O OD2 . ASP D 1 279 ? -12.228 60.810  77.522  1.00 70.95  -1 295 ASP A OD2 1 
ATOM   10263 N N   . ALA D 1 280 ? -17.592 60.972  76.335  1.00 56.17  ?  296 ALA A N   1 
ATOM   10264 C CA  . ALA D 1 280 ? -18.972 60.899  76.800  1.00 55.45  ?  296 ALA A CA  1 
ATOM   10265 C C   . ALA D 1 280 ? -19.798 59.988  75.900  1.00 59.10  ?  296 ALA A C   1 
ATOM   10266 O O   . ALA D 1 280 ? -20.497 59.083  76.377  1.00 66.20  ?  296 ALA A O   1 
ATOM   10267 C CB  . ALA D 1 280 ? -19.587 62.299  76.835  1.00 50.09  ?  296 ALA A CB  1 
ATOM   10268 N N   . MET D 1 281 ? -19.743 60.237  74.582  1.00 63.13  ?  297 MET A N   1 
ATOM   10269 C CA  . MET D 1 281 ? -20.353 59.371  73.571  1.00 61.11  ?  297 MET A CA  1 
ATOM   10270 C C   . MET D 1 281 ? -19.905 57.925  73.718  1.00 63.84  ?  297 MET A C   1 
ATOM   10271 O O   . MET D 1 281 ? -20.741 57.016  73.756  1.00 62.12  ?  297 MET A O   1 
ATOM   10272 C CB  . MET D 1 281 ? -20.013 59.913  72.182  1.00 57.63  ?  297 MET A CB  1 
ATOM   10273 C CG  . MET D 1 281 ? -20.506 61.332  71.919  1.00 54.82  ?  297 MET A CG  1 
ATOM   10274 S SD  . MET D 1 281 ? -19.623 62.051  70.542  1.00 50.49  ?  297 MET A SD  1 
ATOM   10275 C CE  . MET D 1 281 ? -20.086 60.942  69.211  1.00 53.67  ?  297 MET A CE  1 
ATOM   10276 N N   . VAL D 1 282 ? -18.592 57.682  73.808  1.00 61.10  ?  298 VAL A N   1 
ATOM   10277 C CA  . VAL D 1 282 ? -18.116 56.298  73.916  1.00 59.06  ?  298 VAL A CA  1 
ATOM   10278 C C   . VAL D 1 282 ? -18.618 55.626  75.195  1.00 60.06  ?  298 VAL A C   1 
ATOM   10279 O O   . VAL D 1 282 ? -19.109 54.484  75.170  1.00 62.77  ?  298 VAL A O   1 
ATOM   10280 C CB  . VAL D 1 282 ? -16.590 56.250  73.797  1.00 53.74  ?  298 VAL A CB  1 
ATOM   10281 C CG1 . VAL D 1 282 ? -16.124 54.875  74.033  1.00 53.82  ?  298 VAL A CG1 1 
ATOM   10282 C CG2 . VAL D 1 282 ? -16.208 56.660  72.346  1.00 54.16  ?  298 VAL A CG2 1 
ATOM   10283 N N   . ASP D 1 283 ? -18.516 56.337  76.313  1.00 56.67  ?  299 ASP A N   1 
ATOM   10284 C CA  . ASP D 1 283 ? -18.908 55.745  77.617  1.00 61.29  ?  299 ASP A CA  1 
ATOM   10285 C C   . ASP D 1 283 ? -20.414 55.482  77.643  1.00 60.90  ?  299 ASP A C   1 
ATOM   10286 O O   . ASP D 1 283 ? -20.835 54.612  78.413  1.00 60.33  ?  299 ASP A O   1 
ATOM   10287 C CB  . ASP D 1 283 ? -18.460 56.646  78.770  1.00 65.04  ?  299 ASP A CB  1 
ATOM   10288 C CG  . ASP D 1 283 ? -16.980 56.548  79.092  1.00 68.66  ?  299 ASP A CG  1 
ATOM   10289 O OD1 . ASP D 1 283 ? -16.284 55.758  78.428  1.00 69.59  ?  299 ASP A OD1 1 
ATOM   10290 O OD2 . ASP D 1 283 ? -16.537 57.264  80.006  1.00 67.83  -1 299 ASP A OD2 1 
ATOM   10291 N N   . GLN D 1 284 ? -21.185 56.208  76.832  1.00 62.46  ?  300 GLN A N   1 
ATOM   10292 C CA  . GLN D 1 284 ? -22.666 56.054  76.841  1.00 61.63  ?  300 GLN A CA  1 
ATOM   10293 C C   . GLN D 1 284 ? -23.085 55.018  75.791  1.00 61.16  ?  300 GLN A C   1 
ATOM   10294 O O   . GLN D 1 284 ? -24.277 54.881  75.523  1.00 61.55  ?  300 GLN A O   1 
ATOM   10295 C CB  . GLN D 1 284 ? -23.328 57.415  76.643  1.00 60.31  ?  300 GLN A CB  1 
ATOM   10296 C CG  . GLN D 1 284 ? -23.231 58.335  77.852  1.00 60.02  ?  300 GLN A CG  1 
ATOM   10297 C CD  . GLN D 1 284 ? -23.818 59.696  77.572  1.00 62.50  ?  300 GLN A CD  1 
ATOM   10298 O OE1 . GLN D 1 284 ? -24.897 59.814  77.002  1.00 68.34  ?  300 GLN A OE1 1 
ATOM   10299 N NE2 . GLN D 1 284 ? -23.099 60.738  77.956  1.00 64.20  ?  300 GLN A NE2 1 
ATOM   10300 N N   . ALA D 1 285 ? -22.127 54.266  75.270  1.00 67.81  ?  301 ALA A N   1 
ATOM   10301 C CA  . ALA D 1 285 ? -22.484 53.172  74.340  1.00 65.88  ?  301 ALA A CA  1 
ATOM   10302 C C   . ALA D 1 285 ? -23.194 53.728  73.112  1.00 63.10  ?  301 ALA A C   1 
ATOM   10303 O O   . ALA D 1 285 ? -24.348 53.347  72.861  1.00 68.49  ?  301 ALA A O   1 
ATOM   10304 C CB  . ALA D 1 285 ? -23.346 52.153  75.031  1.00 75.38  ?  301 ALA A CB  1 
ATOM   10305 N N   . TRP D 1 286 ? -22.521 54.597  72.372  1.00 55.64  ?  302 TRP A N   1 
ATOM   10306 C CA  . TRP D 1 286 ? -23.181 55.208  71.199  1.00 49.02  ?  302 TRP A CA  1 
ATOM   10307 C C   . TRP D 1 286 ? -22.704 54.515  69.934  1.00 52.98  ?  302 TRP A C   1 
ATOM   10308 O O   . TRP D 1 286 ? -21.793 53.673  70.044  1.00 55.19  ?  302 TRP A O   1 
ATOM   10309 C CB  . TRP D 1 286 ? -22.891 56.693  71.131  1.00 49.38  ?  302 TRP A CB  1 
ATOM   10310 C CG  . TRP D 1 286 ? -23.893 57.570  71.805  1.00 48.10  ?  302 TRP A CG  1 
ATOM   10311 C CD1 . TRP D 1 286 ? -24.654 57.316  72.906  1.00 50.76  ?  302 TRP A CD1 1 
ATOM   10312 C CD2 . TRP D 1 286 ? -24.196 58.906  71.399  1.00 48.02  ?  302 TRP A CD2 1 
ATOM   10313 N NE1 . TRP D 1 286 ? -25.419 58.411  73.208  1.00 43.45  ?  302 TRP A NE1 1 
ATOM   10314 C CE2 . TRP D 1 286 ? -25.155 59.402  72.300  1.00 47.81  ?  302 TRP A CE2 1 
ATOM   10315 C CE3 . TRP D 1 286 ? -23.736 59.715  70.356  1.00 48.94  ?  302 TRP A CE3 1 
ATOM   10316 C CZ2 . TRP D 1 286 ? -25.668 60.691  72.179  1.00 51.99  ?  302 TRP A CZ2 1 
ATOM   10317 C CZ3 . TRP D 1 286 ? -24.243 60.985  70.239  1.00 48.97  ?  302 TRP A CZ3 1 
ATOM   10318 C CH2 . TRP D 1 286 ? -25.195 61.459  71.140  1.00 51.89  ?  302 TRP A CH2 1 
ATOM   10319 N N   . ASP D 1 287 ? -23.260 54.892  68.784  1.00 59.88  ?  303 ASP A N   1 
ATOM   10320 C CA  . ASP D 1 287 ? -22.732 54.252  67.558  1.00 59.62  ?  303 ASP A CA  1 
ATOM   10321 C C   . ASP D 1 287 ? -22.994 55.204  66.397  1.00 58.01  ?  303 ASP A C   1 
ATOM   10322 O O   . ASP D 1 287 ? -23.733 56.177  66.597  1.00 58.33  ?  303 ASP A O   1 
ATOM   10323 C CB  . ASP D 1 287 ? -23.391 52.899  67.313  1.00 63.22  ?  303 ASP A CB  1 
ATOM   10324 C CG  . ASP D 1 287 ? -24.906 52.922  67.384  1.00 69.09  ?  303 ASP A CG  1 
ATOM   10325 O OD1 . ASP D 1 287 ? -25.466 54.016  67.502  1.00 64.76  ?  303 ASP A OD1 1 
ATOM   10326 O OD2 . ASP D 1 287 ? -25.511 51.837  67.323  1.00 78.05  -1 303 ASP A OD2 1 
ATOM   10327 N N   . ALA D 1 288 ? -22.402 54.991  65.229  1.00 52.66  ?  304 ALA A N   1 
ATOM   10328 C CA  . ALA D 1 288 ? -22.649 55.965  64.150  1.00 49.85  ?  304 ALA A CA  1 
ATOM   10329 C C   . ALA D 1 288 ? -24.148 56.220  64.036  1.00 54.09  ?  304 ALA A C   1 
ATOM   10330 O O   . ALA D 1 288 ? -24.553 57.385  64.011  1.00 55.20  ?  304 ALA A O   1 
ATOM   10331 C CB  . ALA D 1 288 ? -22.110 55.421  62.862  1.00 46.35  ?  304 ALA A CB  1 
ATOM   10332 N N   . GLN D 1 289 ? -24.937 55.149  63.953  1.00 53.52  ?  305 GLN A N   1 
ATOM   10333 C CA  . GLN D 1 289 ? -26.404 55.304  63.807  1.00 50.61  ?  305 GLN A CA  1 
ATOM   10334 C C   . GLN D 1 289 ? -26.866 56.355  64.803  1.00 51.93  ?  305 GLN A C   1 
ATOM   10335 O O   . GLN D 1 289 ? -27.423 57.374  64.375  1.00 55.38  ?  305 GLN A O   1 
ATOM   10336 C CB  . GLN D 1 289 ? -27.108 53.975  64.053  1.00 58.74  ?  305 GLN A CB  1 
ATOM   10337 C CG  . GLN D 1 289 ? -28.572 54.117  64.424  1.00 62.70  ?  305 GLN A CG  1 
ATOM   10338 C CD  . GLN D 1 289 ? -29.442 53.294  63.508  1.00 55.25  ?  305 GLN A CD  1 
ATOM   10339 O OE1 . GLN D 1 289 ? -29.184 53.179  62.313  1.00 55.48  ?  305 GLN A OE1 1 
ATOM   10340 N NE2 . GLN D 1 289 ? -30.490 52.717  64.065  1.00 53.49  ?  305 GLN A NE2 1 
ATOM   10341 N N   . ARG D 1 290 ? -26.630 56.110  66.091  1.00 52.55  ?  306 ARG A N   1 
ATOM   10342 C CA  . ARG D 1 290 ? -27.127 57.079  67.088  1.00 50.14  ?  306 ARG A CA  1 
ATOM   10343 C C   . ARG D 1 290 ? -26.647 58.447  66.633  1.00 50.18  ?  306 ARG A C   1 
ATOM   10344 O O   . ARG D 1 290 ? -27.448 59.389  66.657  1.00 53.32  ?  306 ARG A O   1 
ATOM   10345 C CB  . ARG D 1 290 ? -26.614 56.798  68.497  1.00 50.41  ?  306 ARG A CB  1 
ATOM   10346 C CG  . ARG D 1 290 ? -26.829 57.950  69.466  1.00 46.72  ?  306 ARG A CG  1 
ATOM   10347 C CD  . ARG D 1 290 ? -28.305 58.241  69.651  1.00 47.54  ?  306 ARG A CD  1 
ATOM   10348 N NE  . ARG D 1 290 ? -28.577 58.895  70.918  1.00 43.23  ?  306 ARG A NE  1 
ATOM   10349 C CZ  . ARG D 1 290 ? -28.478 58.301  72.099  1.00 48.50  ?  306 ARG A CZ  1 
ATOM   10350 N NH1 . ARG D 1 290 ? -28.108 57.036  72.170  1.00 45.40  ?  306 ARG A NH1 1 
ATOM   10351 N NH2 . ARG D 1 290 ? -28.745 58.974  73.201  1.00 54.36  ?  306 ARG A NH2 1 
ATOM   10352 N N   . ILE D 1 291 ? -25.396 58.543  66.190  1.00 50.23  ?  307 ILE A N   1 
ATOM   10353 C CA  . ILE D 1 291 ? -25.025 59.904  65.789  1.00 52.40  ?  307 ILE A CA  1 
ATOM   10354 C C   . ILE D 1 291 ? -26.002 60.453  64.737  1.00 55.41  ?  307 ILE A C   1 
ATOM   10355 O O   . ILE D 1 291 ? -26.581 61.545  64.903  1.00 52.66  ?  307 ILE A O   1 
ATOM   10356 C CB  . ILE D 1 291 ? -23.561 59.963  65.331  1.00 52.23  ?  307 ILE A CB  1 
ATOM   10357 C CG1 . ILE D 1 291 ? -22.638 59.765  66.519  1.00 50.04  ?  307 ILE A CG1 1 
ATOM   10358 C CG2 . ILE D 1 291 ? -23.212 61.313  64.743  1.00 51.71  ?  307 ILE A CG2 1 
ATOM   10359 C CD1 . ILE D 1 291 ? -21.231 59.668  66.131  1.00 46.68  ?  307 ILE A CD1 1 
ATOM   10360 N N   . PHE D 1 292 ? -26.249 59.681  63.667  1.00 54.01  ?  308 PHE A N   1 
ATOM   10361 C CA  . PHE D 1 292 ? -27.113 60.185  62.594  1.00 49.16  ?  308 PHE A CA  1 
ATOM   10362 C C   . PHE D 1 292 ? -28.561 60.308  63.038  1.00 48.08  ?  308 PHE A C   1 
ATOM   10363 O O   . PHE D 1 292 ? -29.288 61.174  62.544  1.00 47.05  ?  308 PHE A O   1 
ATOM   10364 C CB  . PHE D 1 292 ? -27.009 59.298  61.363  1.00 44.14  ?  308 PHE A CB  1 
ATOM   10365 C CG  . PHE D 1 292 ? -25.774 59.544  60.603  1.00 45.53  ?  308 PHE A CG  1 
ATOM   10366 C CD1 . PHE D 1 292 ? -24.616 58.878  60.916  1.00 46.11  ?  308 PHE A CD1 1 
ATOM   10367 C CD2 . PHE D 1 292 ? -25.723 60.575  59.689  1.00 46.96  ?  308 PHE A CD2 1 
ATOM   10368 C CE1 . PHE D 1 292 ? -23.440 59.152  60.242  1.00 48.10  ?  308 PHE A CE1 1 
ATOM   10369 C CE2 . PHE D 1 292 ? -24.554 60.869  59.027  1.00 48.73  ?  308 PHE A CE2 1 
ATOM   10370 C CZ  . PHE D 1 292 ? -23.401 60.151  59.309  1.00 47.16  ?  308 PHE A CZ  1 
ATOM   10371 N N   . LYS D 1 293 ? -28.971 59.475  63.984  1.00 47.17  ?  309 LYS A N   1 
ATOM   10372 C CA  . LYS D 1 293 ? -30.285 59.602  64.586  1.00 49.60  ?  309 LYS A CA  1 
ATOM   10373 C C   . LYS D 1 293 ? -30.419 60.920  65.363  1.00 54.40  ?  309 LYS A C   1 
ATOM   10374 O O   . LYS D 1 293 ? -31.490 61.553  65.364  1.00 53.36  ?  309 LYS A O   1 
ATOM   10375 C CB  . LYS D 1 293 ? -30.493 58.426  65.527  1.00 53.15  ?  309 LYS A CB  1 
ATOM   10376 C CG  . LYS D 1 293 ? -30.767 57.082  64.883  1.00 54.51  ?  309 LYS A CG  1 
ATOM   10377 C CD  . LYS D 1 293 ? -32.104 57.000  64.194  1.00 54.71  ?  309 LYS A CD  1 
ATOM   10378 C CE  . LYS D 1 293 ? -32.192 55.682  63.427  1.00 56.25  ?  309 LYS A CE  1 
ATOM   10379 N NZ  . LYS D 1 293 ? -33.433 55.447  62.619  1.00 54.76  ?  309 LYS A NZ  1 
ATOM   10380 N N   . GLU D 1 294 ? -29.347 61.330  66.068  1.00 51.73  ?  310 GLU A N   1 
ATOM   10381 C CA  . GLU D 1 294 ? -29.391 62.601  66.792  1.00 51.99  ?  310 GLU A CA  1 
ATOM   10382 C C   . GLU D 1 294 ? -29.371 63.784  65.844  1.00 51.83  ?  310 GLU A C   1 
ATOM   10383 O O   . GLU D 1 294 ? -30.004 64.814  66.117  1.00 53.14  ?  310 GLU A O   1 
ATOM   10384 C CB  . GLU D 1 294 ? -28.246 62.714  67.790  1.00 50.21  ?  310 GLU A CB  1 
ATOM   10385 C CG  . GLU D 1 294 ? -28.396 61.862  69.036  1.00 49.10  ?  310 GLU A CG  1 
ATOM   10386 C CD  . GLU D 1 294 ? -29.594 62.304  69.900  1.00 58.76  ?  310 GLU A CD  1 
ATOM   10387 O OE1 . GLU D 1 294 ? -30.041 63.503  69.808  1.00 57.07  ?  310 GLU A OE1 1 
ATOM   10388 O OE2 . GLU D 1 294 ? -30.060 61.433  70.683  1.00 60.00  -1 310 GLU A OE2 1 
ATOM   10389 N N   . ALA D 1 295 ? -28.666 63.653  64.728  1.00 54.77  ?  311 ALA A N   1 
ATOM   10390 C CA  . ALA D 1 295 ? -28.735 64.677  63.681  1.00 53.24  ?  311 ALA A CA  1 
ATOM   10391 C C   . ALA D 1 295 ? -30.152 64.790  63.082  1.00 54.99  ?  311 ALA A C   1 
ATOM   10392 O O   . ALA D 1 295 ? -30.695 65.899  62.900  1.00 54.63  ?  311 ALA A O   1 
ATOM   10393 C CB  . ALA D 1 295 ? -27.704 64.360  62.597  1.00 50.93  ?  311 ALA A CB  1 
ATOM   10394 N N   . GLU D 1 296 ? -30.739 63.648  62.719  1.00 56.30  ?  312 GLU A N   1 
ATOM   10395 C CA  . GLU D 1 296 ? -32.120 63.617  62.269  1.00 60.84  ?  312 GLU A CA  1 
ATOM   10396 C C   . GLU D 1 296 ? -33.045 64.311  63.271  1.00 63.68  ?  312 GLU A C   1 
ATOM   10397 O O   . GLU D 1 296 ? -33.841 65.185  62.882  1.00 59.19  ?  312 GLU A O   1 
ATOM   10398 C CB  . GLU D 1 296 ? -32.544 62.166  62.058  1.00 59.16  ?  312 GLU A CB  1 
ATOM   10399 C CG  . GLU D 1 296 ? -34.004 61.950  61.701  1.00 63.64  ?  312 GLU A CG  1 
ATOM   10400 C CD  . GLU D 1 296 ? -34.286 60.500  61.274  1.00 74.34  ?  312 GLU A CD  1 
ATOM   10401 O OE1 . GLU D 1 296 ? -34.010 59.596  62.104  1.00 77.23  ?  312 GLU A OE1 1 
ATOM   10402 O OE2 . GLU D 1 296 ? -34.783 60.262  60.135  1.00 74.00  -1 312 GLU A OE2 1 
ATOM   10403 N N   . LYS D 1 297 ? -32.962 63.911  64.564  1.00 55.76  ?  313 LYS A N   1 
ATOM   10404 C CA  . LYS D 1 297 ? -33.759 64.517  65.641  1.00 54.73  ?  313 LYS A CA  1 
ATOM   10405 C C   . LYS D 1 297 ? -33.591 66.036  65.687  1.00 50.69  ?  313 LYS A C   1 
ATOM   10406 O O   . LYS D 1 297 ? -34.567 66.776  65.900  1.00 44.88  ?  313 LYS A O   1 
ATOM   10407 C CB  . LYS D 1 297 ? -33.374 63.891  67.000  1.00 60.48  ?  313 LYS A CB  1 
ATOM   10408 C CG  . LYS D 1 297 ? -34.442 64.047  68.161  1.00 60.93  ?  313 LYS A CG  1 
ATOM   10409 C CD  . LYS D 1 297 ? -34.035 63.436  69.561  1.00 58.36  ?  313 LYS A CD  1 
ATOM   10410 C CE  . LYS D 1 297 ? -33.674 61.907  69.473  1.00 68.33  ?  313 LYS A CE  1 
ATOM   10411 N NZ  . LYS D 1 297 ? -33.231 61.129  70.728  1.00 59.06  ?  313 LYS A NZ  1 
ATOM   10412 N N   . PHE D 1 298 ? -32.352 66.513  65.496  1.00 52.00  ?  314 PHE A N   1 
ATOM   10413 C CA  . PHE D 1 298 ? -32.067 67.947  65.538  1.00 51.82  ?  314 PHE A CA  1 
ATOM   10414 C C   . PHE D 1 298 ? -32.811 68.693  64.449  1.00 48.93  ?  314 PHE A C   1 
ATOM   10415 O O   . PHE D 1 298 ? -33.514 69.675  64.713  1.00 49.52  ?  314 PHE A O   1 
ATOM   10416 C CB  . PHE D 1 298 ? -30.559 68.197  65.411  1.00 52.44  ?  314 PHE A CB  1 
ATOM   10417 C CG  . PHE D 1 298 ? -30.203 69.619  65.064  1.00 48.42  ?  314 PHE A CG  1 
ATOM   10418 C CD1 . PHE D 1 298 ? -30.273 70.616  66.009  1.00 46.54  ?  314 PHE A CD1 1 
ATOM   10419 C CD2 . PHE D 1 298 ? -29.740 69.938  63.791  1.00 46.99  ?  314 PHE A CD2 1 
ATOM   10420 C CE1 . PHE D 1 298 ? -29.945 71.924  65.685  1.00 45.11  ?  314 PHE A CE1 1 
ATOM   10421 C CE2 . PHE D 1 298 ? -29.398 71.244  63.467  1.00 46.44  ?  314 PHE A CE2 1 
ATOM   10422 C CZ  . PHE D 1 298 ? -29.499 72.238  64.419  1.00 43.79  ?  314 PHE A CZ  1 
ATOM   10423 N N   . PHE D 1 299 ? -32.650 68.257  63.207  1.00 49.27  ?  315 PHE A N   1 
ATOM   10424 C CA  . PHE D 1 299 ? -33.359 68.960  62.137  1.00 49.36  ?  315 PHE A CA  1 
ATOM   10425 C C   . PHE D 1 299 ? -34.877 68.886  62.326  1.00 49.38  ?  315 PHE A C   1 
ATOM   10426 O O   . PHE D 1 299 ? -35.572 69.906  62.185  1.00 47.19  ?  315 PHE A O   1 
ATOM   10427 C CB  . PHE D 1 299 ? -32.965 68.408  60.782  1.00 49.47  ?  315 PHE A CB  1 
ATOM   10428 C CG  . PHE D 1 299 ? -31.562 68.715  60.423  1.00 45.22  ?  315 PHE A CG  1 
ATOM   10429 C CD1 . PHE D 1 299 ? -31.190 70.011  60.143  1.00 44.49  ?  315 PHE A CD1 1 
ATOM   10430 C CD2 . PHE D 1 299 ? -30.605 67.705  60.381  1.00 42.47  ?  315 PHE A CD2 1 
ATOM   10431 C CE1 . PHE D 1 299 ? -29.892 70.312  59.797  1.00 43.45  ?  315 PHE A CE1 1 
ATOM   10432 C CE2 . PHE D 1 299 ? -29.329 67.986  60.029  1.00 41.09  ?  315 PHE A CE2 1 
ATOM   10433 C CZ  . PHE D 1 299 ? -28.962 69.303  59.733  1.00 43.83  ?  315 PHE A CZ  1 
ATOM   10434 N N   . VAL D 1 300 ? -35.404 67.701  62.682  1.00 47.90  ?  316 VAL A N   1 
ATOM   10435 C CA  . VAL D 1 300 ? -36.831 67.589  62.989  1.00 45.10  ?  316 VAL A CA  1 
ATOM   10436 C C   . VAL D 1 300 ? -37.243 68.604  64.040  1.00 48.42  ?  316 VAL A C   1 
ATOM   10437 O O   . VAL D 1 300 ? -38.350 69.139  63.987  1.00 52.33  ?  316 VAL A O   1 
ATOM   10438 C CB  . VAL D 1 300 ? -37.208 66.171  63.451  1.00 44.75  ?  316 VAL A CB  1 
ATOM   10439 C CG1 . VAL D 1 300 ? -38.607 66.181  63.992  1.00 42.66  ?  316 VAL A CG1 1 
ATOM   10440 C CG2 . VAL D 1 300 ? -37.093 65.127  62.319  1.00 52.94  ?  316 VAL A CG2 1 
ATOM   10441 N N   . SER D 1 301 ? -36.379 68.888  65.014  1.00 51.36  ?  317 SER A N   1 
ATOM   10442 C CA  . SER D 1 301 ? -36.836 69.786  66.062  1.00 51.65  ?  317 SER A CA  1 
ATOM   10443 C C   . SER D 1 301 ? -37.171 71.186  65.551  1.00 53.82  ?  317 SER A C   1 
ATOM   10444 O O   . SER D 1 301 ? -37.971 71.873  66.190  1.00 55.18  ?  317 SER A O   1 
ATOM   10445 C CB  . SER D 1 301 ? -35.811 69.909  67.162  1.00 52.15  ?  317 SER A CB  1 
ATOM   10446 O OG  . SER D 1 301 ? -34.799 70.793  66.775  1.00 54.83  ?  317 SER A OG  1 
ATOM   10447 N N   . VAL D 1 302 ? -36.601 71.636  64.426  1.00 49.36  ?  318 VAL A N   1 
ATOM   10448 C CA  . VAL D 1 302 ? -36.959 72.947  63.874  1.00 53.22  ?  318 VAL A CA  1 
ATOM   10449 C C   . VAL D 1 302 ? -38.033 72.858  62.776  1.00 55.18  ?  318 VAL A C   1 
ATOM   10450 O O   . VAL D 1 302 ? -38.314 73.859  62.105  1.00 57.26  ?  318 VAL A O   1 
ATOM   10451 C CB  . VAL D 1 302 ? -35.726 73.719  63.374  1.00 52.21  ?  318 VAL A CB  1 
ATOM   10452 C CG1 . VAL D 1 302 ? -34.726 73.880  64.455  1.00 50.86  ?  318 VAL A CG1 1 
ATOM   10453 C CG2 . VAL D 1 302 ? -35.079 72.973  62.218  1.00 52.67  ?  318 VAL A CG2 1 
ATOM   10454 N N   . GLY D 1 303 ? -38.646 71.703  62.581  1.00 50.79  ?  319 GLY A N   1 
ATOM   10455 C CA  . GLY D 1 303 ? -39.748 71.604  61.653  1.00 52.08  ?  319 GLY A CA  1 
ATOM   10456 C C   . GLY D 1 303 ? -39.428 70.938  60.325  1.00 57.02  ?  319 GLY A C   1 
ATOM   10457 O O   . GLY D 1 303 ? -40.364 70.580  59.590  1.00 61.80  ?  319 GLY A O   1 
ATOM   10458 N N   . LEU D 1 304 ? -38.150 70.766  59.987  1.00 45.04  ?  320 LEU A N   1 
ATOM   10459 C CA  . LEU D 1 304 ? -37.749 70.088  58.760  1.00 46.13  ?  320 LEU A CA  1 
ATOM   10460 C C   . LEU D 1 304 ? -38.129 68.595  58.837  1.00 46.55  ?  320 LEU A C   1 
ATOM   10461 O O   . LEU D 1 304 ? -38.493 68.100  59.912  1.00 45.10  ?  320 LEU A O   1 
ATOM   10462 C CB  . LEU D 1 304 ? -36.253 70.315  58.570  1.00 49.81  ?  320 LEU A CB  1 
ATOM   10463 C CG  . LEU D 1 304 ? -35.935 71.734  58.133  1.00 47.69  ?  320 LEU A CG  1 
ATOM   10464 C CD1 . LEU D 1 304 ? -34.466 72.043  58.299  1.00 47.53  ?  320 LEU A CD1 1 
ATOM   10465 C CD2 . LEU D 1 304 ? -36.247 71.829  56.685  1.00 44.13  ?  320 LEU A CD2 1 
ATOM   10466 N N   . PRO D 1 305 ? -38.066 67.850  57.723  1.00 44.46  ?  321 PRO A N   1 
ATOM   10467 C CA  . PRO D 1 305 ? -38.458 66.425  57.739  1.00 48.91  ?  321 PRO A CA  1 
ATOM   10468 C C   . PRO D 1 305 ? -37.411 65.446  58.263  1.00 50.82  ?  321 PRO A C   1 
ATOM   10469 O O   . PRO D 1 305 ? -36.207 65.735  58.337  1.00 55.43  ?  321 PRO A O   1 
ATOM   10470 C CB  . PRO D 1 305 ? -38.706 66.140  56.263  1.00 50.62  ?  321 PRO A CB  1 
ATOM   10471 C CG  . PRO D 1 305 ? -37.702 67.027  55.560  1.00 46.64  ?  321 PRO A CG  1 
ATOM   10472 C CD  . PRO D 1 305 ? -37.706 68.305  56.365  1.00 45.20  ?  321 PRO A CD  1 
ATOM   10473 N N   . ASN D 1 306 ? -37.886 64.229  58.575  1.00 51.27  ?  322 ASN A N   1 
ATOM   10474 C CA  . ASN D 1 306 ? -36.915 63.194  58.918  1.00 62.72  ?  322 ASN A CA  1 
ATOM   10475 C C   . ASN D 1 306 ? -36.296 62.618  57.645  1.00 57.87  ?  322 ASN A C   1 
ATOM   10476 O O   . ASN D 1 306 ? -36.815 62.771  56.544  1.00 55.30  ?  322 ASN A O   1 
ATOM   10477 C CB  . ASN D 1 306 ? -37.478 62.052  59.781  1.00 67.15  ?  322 ASN A CB  1 
ATOM   10478 C CG  . ASN D 1 306 ? -39.029 61.969  59.811  1.00 85.69  ?  322 ASN A CG  1 
ATOM   10479 O OD1 . ASN D 1 306 ? -39.731 62.284  58.836  1.00 95.89  ?  322 ASN A OD1 1 
ATOM   10480 N ND2 . ASN D 1 306 ? -39.555 61.529  60.976  1.00 102.23 ?  322 ASN A ND2 1 
ATOM   10481 N N   . MET D 1 307 ? -35.134 62.007  57.802  1.00 54.06  ?  323 MET A N   1 
ATOM   10482 C CA  . MET D 1 307 ? -34.482 61.388  56.663  1.00 51.64  ?  323 MET A CA  1 
ATOM   10483 C C   . MET D 1 307 ? -35.362 60.280  56.097  1.00 54.32  ?  323 MET A C   1 
ATOM   10484 O O   . MET D 1 307 ? -36.119 59.619  56.823  1.00 53.16  ?  323 MET A O   1 
ATOM   10485 C CB  . MET D 1 307 ? -33.124 60.820  57.082  1.00 48.51  ?  323 MET A CB  1 
ATOM   10486 C CG  . MET D 1 307 ? -32.087 61.791  57.583  1.00 46.74  ?  323 MET A CG  1 
ATOM   10487 S SD  . MET D 1 307 ? -31.469 62.872  56.289  1.00 47.33  ?  323 MET A SD  1 
ATOM   10488 C CE  . MET D 1 307 ? -32.497 64.330  56.563  1.00 49.80  ?  323 MET A CE  1 
ATOM   10489 N N   . THR D 1 308 ? -35.238 60.072  54.791  1.00 54.27  ?  324 THR A N   1 
ATOM   10490 C CA  . THR D 1 308 ? -35.998 59.042  54.103  1.00 50.12  ?  324 THR A CA  1 
ATOM   10491 C C   . THR D 1 308 ? -35.512 57.645  54.461  1.00 51.16  ?  324 THR A C   1 
ATOM   10492 O O   . THR D 1 308 ? -34.315 57.397  54.606  1.00 51.46  ?  324 THR A O   1 
ATOM   10493 C CB  . THR D 1 308 ? -35.875 59.222  52.603  1.00 50.20  ?  324 THR A CB  1 
ATOM   10494 O OG1 . THR D 1 308 ? -34.538 58.915  52.185  1.00 48.34  ?  324 THR A OG1 1 
ATOM   10495 C CG2 . THR D 1 308 ? -36.185 60.643  52.242  1.00 54.35  ?  324 THR A CG2 1 
ATOM   10496 N N   . GLN D 1 309 ? -36.462 56.714  54.567  1.00 51.86  ?  325 GLN A N   1 
ATOM   10497 C CA  . GLN D 1 309 ? -36.135 55.299  54.728  1.00 55.77  ?  325 GLN A CA  1 
ATOM   10498 C C   . GLN D 1 309 ? -35.039 54.872  53.759  1.00 55.53  ?  325 GLN A C   1 
ATOM   10499 O O   . GLN D 1 309 ? -34.218 53.999  54.067  1.00 57.30  ?  325 GLN A O   1 
ATOM   10500 C CB  . GLN D 1 309 ? -37.353 54.461  54.450  1.00 57.10  ?  325 GLN A CB  1 
ATOM   10501 C CG  . GLN D 1 309 ? -37.159 52.998  54.587  1.00 64.79  ?  325 GLN A CG  1 
ATOM   10502 C CD  . GLN D 1 309 ? -38.392 52.260  54.075  1.00 87.60  ?  325 GLN A CD  1 
ATOM   10503 O OE1 . GLN D 1 309 ? -39.386 52.884  53.641  1.00 85.39  ?  325 GLN A OE1 1 
ATOM   10504 N NE2 . GLN D 1 309 ? -38.329 50.930  54.086  1.00 101.30 ?  325 GLN A NE2 1 
ATOM   10505 N N   . GLY D 1 310 ? -35.043 55.443  52.560  1.00 52.69  ?  326 GLY A N   1 
ATOM   10506 C CA  . GLY D 1 310 ? -33.992 55.130  51.615  1.00 49.82  ?  326 GLY A CA  1 
ATOM   10507 C C   . GLY D 1 310 ? -32.656 55.604  52.114  1.00 51.15  ?  326 GLY A C   1 
ATOM   10508 O O   . GLY D 1 310 ? -31.649 54.943  51.906  1.00 55.73  ?  326 GLY A O   1 
ATOM   10509 N N   . PHE D 1 311 ? -32.632 56.763  52.772  1.00 53.33  ?  327 PHE A N   1 
ATOM   10510 C CA  . PHE D 1 311 ? -31.386 57.270  53.324  1.00 50.05  ?  327 PHE A CA  1 
ATOM   10511 C C   . PHE D 1 311 ? -30.786 56.277  54.291  1.00 50.49  ?  327 PHE A C   1 
ATOM   10512 O O   . PHE D 1 311 ? -29.581 55.998  54.250  1.00 49.04  ?  327 PHE A O   1 
ATOM   10513 C CB  . PHE D 1 311 ? -31.643 58.603  54.000  1.00 50.45  ?  327 PHE A CB  1 
ATOM   10514 C CG  . PHE D 1 311 ? -30.501 59.094  54.792  1.00 53.62  ?  327 PHE A CG  1 
ATOM   10515 C CD1 . PHE D 1 311 ? -29.466 59.789  54.180  1.00 54.31  ?  327 PHE A CD1 1 
ATOM   10516 C CD2 . PHE D 1 311 ? -30.484 58.918  56.162  1.00 50.48  ?  327 PHE A CD2 1 
ATOM   10517 C CE1 . PHE D 1 311 ? -28.421 60.260  54.913  1.00 48.78  ?  327 PHE A CE1 1 
ATOM   10518 C CE2 . PHE D 1 311 ? -29.467 59.391  56.898  1.00 47.32  ?  327 PHE A CE2 1 
ATOM   10519 C CZ  . PHE D 1 311 ? -28.424 60.062  56.279  1.00 50.66  ?  327 PHE A CZ  1 
ATOM   10520 N N   . TRP D 1 312 ? -31.628 55.706  55.149  1.00 51.38  ?  328 TRP A N   1 
ATOM   10521 C CA  . TRP D 1 312 ? -31.149 54.735  56.125  1.00 51.35  ?  328 TRP A CA  1 
ATOM   10522 C C   . TRP D 1 312 ? -30.740 53.428  55.454  1.00 52.49  ?  328 TRP A C   1 
ATOM   10523 O O   . TRP D 1 312 ? -29.661 52.887  55.726  1.00 55.99  ?  328 TRP A O   1 
ATOM   10524 C CB  . TRP D 1 312 ? -32.207 54.486  57.202  1.00 50.23  ?  328 TRP A CB  1 
ATOM   10525 C CG  . TRP D 1 312 ? -32.505 55.683  58.080  1.00 52.71  ?  328 TRP A CG  1 
ATOM   10526 C CD1 . TRP D 1 312 ? -33.655 56.422  58.114  1.00 55.69  ?  328 TRP A CD1 1 
ATOM   10527 C CD2 . TRP D 1 312 ? -31.597 56.329  58.968  1.00 51.69  ?  328 TRP A CD2 1 
ATOM   10528 N NE1 . TRP D 1 312 ? -33.539 57.443  59.027  1.00 56.42  ?  328 TRP A NE1 1 
ATOM   10529 C CE2 . TRP D 1 312 ? -32.275 57.413  59.550  1.00 53.06  ?  328 TRP A CE2 1 
ATOM   10530 C CE3 . TRP D 1 312 ? -30.283 56.077  59.347  1.00 50.34  ?  328 TRP A CE3 1 
ATOM   10531 C CZ2 . TRP D 1 312 ? -31.681 58.238  60.487  1.00 52.76  ?  328 TRP A CZ2 1 
ATOM   10532 C CZ3 . TRP D 1 312 ? -29.697 56.897  60.271  1.00 50.88  ?  328 TRP A CZ3 1 
ATOM   10533 C CH2 . TRP D 1 312 ? -30.391 57.966  60.835  1.00 52.78  ?  328 TRP A CH2 1 
ATOM   10534 N N   . GLU D 1 313 ? -31.572 52.910  54.558  1.00 52.01  ?  329 GLU A N   1 
ATOM   10535 C CA  . GLU D 1 313 ? -31.208 51.670  53.891  1.00 54.69  ?  329 GLU A CA  1 
ATOM   10536 C C   . GLU D 1 313 ? -29.881 51.803  53.134  1.00 55.70  ?  329 GLU A C   1 
ATOM   10537 O O   . GLU D 1 313 ? -29.026 50.915  53.213  1.00 60.04  ?  329 GLU A O   1 
ATOM   10538 C CB  . GLU D 1 313 ? -32.334 51.239  52.959  1.00 62.11  ?  329 GLU A CB  1 
ATOM   10539 C CG  . GLU D 1 313 ? -33.186 50.128  53.558  1.00 68.87  ?  329 GLU A CG  1 
ATOM   10540 C CD  . GLU D 1 313 ? -34.641 50.177  53.088  1.00 73.76  ?  329 GLU A CD  1 
ATOM   10541 O OE1 . GLU D 1 313 ? -34.913 50.793  52.034  1.00 72.62  ?  329 GLU A OE1 1 
ATOM   10542 O OE2 . GLU D 1 313 ? -35.524 49.625  53.780  1.00 77.32  -1 329 GLU A OE2 1 
ATOM   10543 N N   . ASN D 1 314 ? -29.654 52.941  52.472  1.00 54.89  ?  330 ASN A N   1 
ATOM   10544 C CA  . ASN D 1 314 ? -28.655 53.025  51.412  1.00 54.48  ?  330 ASN A CA  1 
ATOM   10545 C C   . ASN D 1 314 ? -27.404 53.809  51.771  1.00 53.85  ?  330 ASN A C   1 
ATOM   10546 O O   . ASN D 1 314 ? -26.377 53.640  51.098  1.00 54.59  ?  330 ASN A O   1 
ATOM   10547 C CB  . ASN D 1 314 ? -29.238 53.692  50.160  1.00 57.48  ?  330 ASN A CB  1 
ATOM   10548 C CG  . ASN D 1 314 ? -30.426 52.977  49.622  1.00 54.33  ?  330 ASN A CG  1 
ATOM   10549 O OD1 . ASN D 1 314 ? -31.411 53.607  49.278  1.00 54.70  ?  330 ASN A OD1 1 
ATOM   10550 N ND2 . ASN D 1 314 ? -30.369 51.657  49.587  1.00 53.89  ?  330 ASN A ND2 1 
ATOM   10551 N N   . SER D 1 315 ? -27.468 54.734  52.724  1.00 53.81  ?  331 SER A N   1 
ATOM   10552 C CA  . SER D 1 315 ? -26.248 55.456  53.029  1.00 48.12  ?  331 SER A CA  1 
ATOM   10553 C C   . SER D 1 315 ? -25.202 54.453  53.483  1.00 51.38  ?  331 SER A C   1 
ATOM   10554 O O   . SER D 1 315 ? -25.515 53.306  53.817  1.00 52.16  ?  331 SER A O   1 
ATOM   10555 C CB  . SER D 1 315 ? -26.495 56.530  54.089  1.00 47.76  ?  331 SER A CB  1 
ATOM   10556 O OG  . SER D 1 315 ? -27.383 57.524  53.610  1.00 47.48  ?  331 SER A OG  1 
ATOM   10557 N N   . MET D 1 316 ? -23.943 54.870  53.403  1.00 53.72  ?  332 MET A N   1 
ATOM   10558 C CA  . MET D 1 316 ? -22.814 54.168  54.017  1.00 51.16  ?  332 MET A CA  1 
ATOM   10559 C C   . MET D 1 316 ? -22.356 55.028  55.185  1.00 49.52  ?  332 MET A C   1 
ATOM   10560 O O   . MET D 1 316 ? -21.639 56.018  54.983  1.00 50.07  ?  332 MET A O   1 
ATOM   10561 C CB  . MET D 1 316 ? -21.669 53.957  53.034  1.00 50.64  ?  332 MET A CB  1 
ATOM   10562 C CG  . MET D 1 316 ? -20.375 53.531  53.718  1.00 58.26  ?  332 MET A CG  1 
ATOM   10563 S SD  . MET D 1 316 ? -19.117 52.977  52.587  1.00 65.21  ?  332 MET A SD  1 
ATOM   10564 C CE  . MET D 1 316 ? -19.943 51.490  51.982  1.00 58.54  ?  332 MET A CE  1 
ATOM   10565 N N   . LEU D 1 317 ? -22.774 54.659  56.397  1.00 49.69  ?  333 LEU A N   1 
ATOM   10566 C CA  . LEU D 1 317 ? -22.476 55.474  57.571  1.00 56.14  ?  333 LEU A CA  1 
ATOM   10567 C C   . LEU D 1 317 ? -21.284 54.977  58.417  1.00 56.43  ?  333 LEU A C   1 
ATOM   10568 O O   . LEU D 1 317 ? -21.054 55.513  59.510  1.00 52.67  ?  333 LEU A O   1 
ATOM   10569 C CB  . LEU D 1 317 ? -23.741 55.639  58.416  1.00 51.98  ?  333 LEU A CB  1 
ATOM   10570 C CG  . LEU D 1 317 ? -24.982 56.163  57.699  1.00 45.09  ?  333 LEU A CG  1 
ATOM   10571 C CD1 . LEU D 1 317 ? -26.057 56.227  58.687  1.00 47.14  ?  333 LEU A CD1 1 
ATOM   10572 C CD2 . LEU D 1 317 ? -24.758 57.579  57.208  1.00 44.36  ?  333 LEU A CD2 1 
ATOM   10573 N N   . THR D 1 318 ? -20.499 54.009  57.928  1.00 56.94  ?  334 THR A N   1 
ATOM   10574 C CA  . THR D 1 318 ? -19.320 53.507  58.625  1.00 56.23  ?  334 THR A CA  1 
ATOM   10575 C C   . THR D 1 318 ? -18.390 52.844  57.614  1.00 63.33  ?  334 THR A C   1 
ATOM   10576 O O   . THR D 1 318 ? -18.857 52.143  56.708  1.00 60.51  ?  334 THR A O   1 
ATOM   10577 C CB  . THR D 1 318 ? -19.633 52.425  59.658  1.00 56.58  ?  334 THR A CB  1 
ATOM   10578 O OG1 . THR D 1 318 ? -20.288 51.351  58.996  1.00 52.53  ?  334 THR A OG1 1 
ATOM   10579 C CG2 . THR D 1 318 ? -20.551 52.907  60.724  1.00 52.65  ?  334 THR A CG2 1 
ATOM   10580 N N   . ASP D 1 319 ? -17.067 52.984  57.841  1.00 70.10  ?  335 ASP A N   1 
ATOM   10581 C CA  . ASP D 1 319 ? -16.019 52.325  57.067  1.00 70.78  ?  335 ASP A CA  1 
ATOM   10582 C C   . ASP D 1 319 ? -16.296 50.820  56.927  1.00 74.96  ?  335 ASP A C   1 
ATOM   10583 O O   . ASP D 1 319 ? -16.334 50.101  57.936  1.00 72.30  ?  335 ASP A O   1 
ATOM   10584 C CB  . ASP D 1 319 ? -14.670 52.547  57.731  1.00 73.03  ?  335 ASP A CB  1 
ATOM   10585 C CG  . ASP D 1 319 ? -13.520 52.197  56.828  1.00 79.77  ?  335 ASP A CG  1 
ATOM   10586 O OD1 . ASP D 1 319 ? -13.568 51.103  56.210  1.00 81.07  ?  335 ASP A OD1 1 
ATOM   10587 O OD2 . ASP D 1 319 ? -12.551 52.998  56.766  1.00 91.23  -1 335 ASP A OD2 1 
ATOM   10588 N N   . PRO D 1 320 ? -16.482 50.321  55.724  1.00 81.43  ?  336 PRO A N   1 
ATOM   10589 C CA  . PRO D 1 320 ? -16.944 48.945  55.514  1.00 79.84  ?  336 PRO A CA  1 
ATOM   10590 C C   . PRO D 1 320 ? -15.826 47.924  55.607  1.00 85.50  ?  336 PRO A C   1 
ATOM   10591 O O   . PRO D 1 320 ? -15.709 47.025  54.775  1.00 91.37  ?  336 PRO A O   1 
ATOM   10592 C CB  . PRO D 1 320 ? -17.521 48.998  54.097  1.00 79.26  ?  336 PRO A CB  1 
ATOM   10593 C CG  . PRO D 1 320 ? -16.668 50.005  53.418  1.00 77.25  ?  336 PRO A CG  1 
ATOM   10594 C CD  . PRO D 1 320 ? -16.420 51.068  54.456  1.00 80.56  ?  336 PRO A CD  1 
ATOM   10595 N N   . GLY D 1 321 ? -15.005 48.061  56.597  1.00 87.10  ?  337 GLY A N   1 
ATOM   10596 C CA  . GLY D 1 321 ? -14.008 47.047  56.785  1.00 106.85 ?  337 GLY A CA  1 
ATOM   10597 C C   . GLY D 1 321 ? -12.824 47.221  55.860  1.00 116.18 ?  337 GLY A C   1 
ATOM   10598 O O   . GLY D 1 321 ? -12.681 48.204  55.108  1.00 105.10 ?  337 GLY A O   1 
ATOM   10599 N N   . ASN D 1 322 ? -11.941 46.233  55.939  1.00 138.37 ?  338 ASN A N   1 
ATOM   10600 C CA  . ASN D 1 322 ? -10.698 46.277  55.200  1.00 147.70 ?  338 ASN A CA  1 
ATOM   10601 C C   . ASN D 1 322 ? -10.799 45.558  53.865  1.00 145.44 ?  338 ASN A C   1 
ATOM   10602 O O   . ASN D 1 322 ? -9.921  45.739  53.015  1.00 145.80 ?  338 ASN A O   1 
ATOM   10603 C CB  . ASN D 1 322 ? -9.575  45.683  56.058  1.00 151.91 ?  338 ASN A CB  1 
ATOM   10604 C CG  . ASN D 1 322 ? -8.195  46.080  55.568  1.00 160.26 ?  338 ASN A CG  1 
ATOM   10605 O OD1 . ASN D 1 322 ? -8.051  47.023  54.784  1.00 159.82 ?  338 ASN A OD1 1 
ATOM   10606 N ND2 . ASN D 1 322 ? -7.169  45.377  56.042  1.00 163.76 ?  338 ASN A ND2 1 
ATOM   10607 N N   . VAL D 1 323 ? -11.856 44.772  53.660  1.00 126.47 ?  339 VAL A N   1 
ATOM   10608 C CA  . VAL D 1 323 ? -12.014 44.035  52.408  1.00 119.35 ?  339 VAL A CA  1 
ATOM   10609 C C   . VAL D 1 323 ? -12.165 44.999  51.238  1.00 116.01 ?  339 VAL A C   1 
ATOM   10610 O O   . VAL D 1 323 ? -11.362 44.980  50.298  1.00 108.90 ?  339 VAL A O   1 
ATOM   10611 C CB  . VAL D 1 323 ? -13.206 43.068  52.495  1.00 118.63 ?  339 VAL A CB  1 
ATOM   10612 C CG1 . VAL D 1 323 ? -13.374 42.334  51.180  1.00 111.07 ?  339 VAL A CG1 1 
ATOM   10613 C CG2 . VAL D 1 323 ? -13.003 42.086  53.622  1.00 115.92 ?  339 VAL A CG2 1 
ATOM   10614 N N   . GLN D 1 324 ? -13.207 45.844  51.276  1.00 107.73 ?  340 GLN A N   1 
ATOM   10615 C CA  . GLN D 1 324 ? -13.478 46.838  50.241  1.00 96.33  ?  340 GLN A CA  1 
ATOM   10616 C C   . GLN D 1 324 ? -12.993 48.214  50.670  1.00 96.59  ?  340 GLN A C   1 
ATOM   10617 O O   . GLN D 1 324 ? -13.283 48.654  51.783  1.00 99.88  ?  340 GLN A O   1 
ATOM   10618 C CB  . GLN D 1 324 ? -14.967 46.934  49.950  1.00 91.31  ?  340 GLN A CB  1 
ATOM   10619 C CG  . GLN D 1 324 ? -15.876 47.024  51.179  1.00 87.81  ?  340 GLN A CG  1 
ATOM   10620 C CD  . GLN D 1 324 ? -17.358 47.210  50.782  1.00 87.49  ?  340 GLN A CD  1 
ATOM   10621 O OE1 . GLN D 1 324 ? -17.670 48.024  49.897  1.00 76.86  ?  340 GLN A OE1 1 
ATOM   10622 N NE2 . GLN D 1 324 ? -18.264 46.487  51.443  1.00 82.29  ?  340 GLN A NE2 1 
ATOM   10623 N N   . LYS D 1 325 ? -12.295 48.915  49.787  1.00 90.43  ?  341 LYS A N   1 
ATOM   10624 C CA  . LYS D 1 325 ? -11.891 50.265  50.148  1.00 91.25  ?  341 LYS A CA  1 
ATOM   10625 C C   . LYS D 1 325 ? -12.954 51.236  49.638  1.00 82.22  ?  341 LYS A C   1 
ATOM   10626 O O   . LYS D 1 325 ? -13.642 50.956  48.658  1.00 75.48  ?  341 LYS A O   1 
ATOM   10627 C CB  . LYS D 1 325 ? -10.505 50.617  49.594  1.00 95.72  ?  341 LYS A CB  1 
ATOM   10628 C CG  . LYS D 1 325 ? -9.335  49.670  50.021  1.00 103.87 ?  341 LYS A CG  1 
ATOM   10629 C CD  . LYS D 1 325 ? -9.327  49.244  51.506  1.00 111.81 ?  341 LYS A CD  1 
ATOM   10630 C CE  . LYS D 1 325 ? -7.940  48.768  52.031  1.00 109.00 ?  341 LYS A CE  1 
ATOM   10631 N NZ  . LYS D 1 325 ? -6.891  49.796  52.253  1.00 95.06  ?  341 LYS A NZ  1 
ATOM   10632 N N   . ALA D 1 326 ? -13.098 52.370  50.332  1.00 80.99  ?  342 ALA A N   1 
ATOM   10633 C CA  . ALA D 1 326 ? -14.147 53.347  50.052  1.00 69.50  ?  342 ALA A CA  1 
ATOM   10634 C C   . ALA D 1 326 ? -13.646 54.762  50.268  1.00 68.18  ?  342 ALA A C   1 
ATOM   10635 O O   . ALA D 1 326 ? -12.983 55.038  51.266  1.00 72.69  ?  342 ALA A O   1 
ATOM   10636 C CB  . ALA D 1 326 ? -15.345 53.141  50.967  1.00 72.15  ?  342 ALA A CB  1 
ATOM   10637 N N   . VAL D 1 327 ? -14.010 55.671  49.379  1.00 64.91  ?  343 VAL A N   1 
ATOM   10638 C CA  . VAL D 1 327 ? -13.547 57.040  49.536  1.00 65.83  ?  343 VAL A CA  1 
ATOM   10639 C C   . VAL D 1 327 ? -14.249 57.724  50.711  1.00 70.15  ?  343 VAL A C   1 
ATOM   10640 O O   . VAL D 1 327 ? -15.406 58.157  50.612  1.00 67.73  ?  343 VAL A O   1 
ATOM   10641 C CB  . VAL D 1 327 ? -13.720 57.793  48.215  1.00 60.95  ?  343 VAL A CB  1 
ATOM   10642 C CG1 . VAL D 1 327 ? -13.388 59.269  48.370  1.00 61.64  ?  343 VAL A CG1 1 
ATOM   10643 C CG2 . VAL D 1 327 ? -12.829 57.152  47.216  1.00 59.49  ?  343 VAL A CG2 1 
ATOM   10644 N N   . CYS D 1 328 ? -13.519 57.870  51.826  1.00 69.83  ?  344 CYS A N   1 
ATOM   10645 C CA  . CYS D 1 328 ? -14.089 58.233  53.121  1.00 70.25  ?  344 CYS A CA  1 
ATOM   10646 C C   . CYS D 1 328 ? -14.222 59.723  53.377  1.00 70.53  ?  344 CYS A C   1 
ATOM   10647 O O   . CYS D 1 328 ? -14.580 60.084  54.510  1.00 69.50  ?  344 CYS A O   1 
ATOM   10648 C CB  . CYS D 1 328 ? -13.274 57.648  54.269  1.00 67.94  ?  344 CYS A CB  1 
ATOM   10649 S SG  . CYS D 1 328 ? -13.530 55.907  54.505  1.00 93.55  ?  344 CYS A SG  1 
ATOM   10650 N N   . HIS D 1 329 ? -13.946 60.600  52.405  1.00 68.93  ?  345 HIS A N   1 
ATOM   10651 C CA  . HIS D 1 329 ? -14.315 61.993  52.613  1.00 62.79  ?  345 HIS A CA  1 
ATOM   10652 C C   . HIS D 1 329 ? -15.820 62.067  52.878  1.00 61.29  ?  345 HIS A C   1 
ATOM   10653 O O   . HIS D 1 329 ? -16.599 61.413  52.166  1.00 65.71  ?  345 HIS A O   1 
ATOM   10654 C CB  . HIS D 1 329 ? -13.901 62.861  51.429  1.00 61.14  ?  345 HIS A CB  1 
ATOM   10655 C CG  . HIS D 1 329 ? -14.187 64.327  51.617  1.00 67.94  ?  345 HIS A CG  1 
ATOM   10656 N ND1 . HIS D 1 329 ? -15.321 64.942  51.118  1.00 70.49  ?  345 HIS A ND1 1 
ATOM   10657 C CD2 . HIS D 1 329 ? -13.498 65.296  52.260  1.00 77.16  ?  345 HIS A CD2 1 
ATOM   10658 C CE1 . HIS D 1 329 ? -15.310 66.224  51.428  1.00 67.89  ?  345 HIS A CE1 1 
ATOM   10659 N NE2 . HIS D 1 329 ? -14.218 66.464  52.129  1.00 80.10  ?  345 HIS A NE2 1 
ATOM   10660 N N   . PRO D 1 330 ? -16.266 62.753  53.933  1.00 61.77  ?  346 PRO A N   1 
ATOM   10661 C CA  . PRO D 1 330 ? -17.704 62.787  54.216  1.00 60.36  ?  346 PRO A CA  1 
ATOM   10662 C C   . PRO D 1 330 ? -18.420 63.606  53.154  1.00 61.23  ?  346 PRO A C   1 
ATOM   10663 O O   . PRO D 1 330 ? -18.192 64.814  53.020  1.00 61.67  ?  346 PRO A O   1 
ATOM   10664 C CB  . PRO D 1 330 ? -17.782 63.452  55.598  1.00 58.89  ?  346 PRO A CB  1 
ATOM   10665 C CG  . PRO D 1 330 ? -16.480 63.304  56.156  1.00 59.18  ?  346 PRO A CG  1 
ATOM   10666 C CD  . PRO D 1 330 ? -15.515 63.389  55.017  1.00 64.68  ?  346 PRO A CD  1 
ATOM   10667 N N   . THR D 1 331 ? -19.302 62.941  52.408  1.00 57.53  ?  347 THR A N   1 
ATOM   10668 C CA  . THR D 1 331 ? -19.959 63.582  51.281  1.00 56.50  ?  347 THR A CA  1 
ATOM   10669 C C   . THR D 1 331 ? -21.449 63.237  51.238  1.00 54.52  ?  347 THR A C   1 
ATOM   10670 O O   . THR D 1 331 ? -21.872 62.132  51.589  1.00 55.39  ?  347 THR A O   1 
ATOM   10671 C CB  . THR D 1 331 ? -19.236 63.200  49.981  1.00 57.55  ?  347 THR A CB  1 
ATOM   10672 O OG1 . THR D 1 331 ? -19.027 61.783  49.937  1.00 58.47  ?  347 THR A OG1 1 
ATOM   10673 C CG2 . THR D 1 331 ? -17.910 63.920  49.863  1.00 54.31  ?  347 THR A CG2 1 
ATOM   10674 N N   . ALA D 1 332 ? -22.250 64.199  50.803  1.00 51.46  ?  348 ALA A N   1 
ATOM   10675 C CA  . ALA D 1 332 ? -23.706 64.105  50.924  1.00 49.84  ?  348 ALA A CA  1 
ATOM   10676 C C   . ALA D 1 332 ? -24.383 64.063  49.548  1.00 51.77  ?  348 ALA A C   1 
ATOM   10677 O O   . ALA D 1 332 ? -24.658 65.113  48.953  1.00 49.76  ?  348 ALA A O   1 
ATOM   10678 C CB  . ALA D 1 332 ? -24.228 65.271  51.766  1.00 49.03  ?  348 ALA A CB  1 
ATOM   10679 N N   . TRP D 1 333 ? -24.735 62.847  49.100  1.00 51.05  ?  349 TRP A N   1 
ATOM   10680 C CA  . TRP D 1 333 ? -25.184 62.545  47.747  1.00 46.77  ?  349 TRP A CA  1 
ATOM   10681 C C   . TRP D 1 333 ? -26.675 62.813  47.593  1.00 52.72  ?  349 TRP A C   1 
ATOM   10682 O O   . TRP D 1 333 ? -27.486 62.272  48.362  1.00 52.08  ?  349 TRP A O   1 
ATOM   10683 C CB  . TRP D 1 333 ? -24.920 61.085  47.424  1.00 45.69  ?  349 TRP A CB  1 
ATOM   10684 C CG  . TRP D 1 333 ? -23.477 60.758  47.428  1.00 52.44  ?  349 TRP A CG  1 
ATOM   10685 C CD1 . TRP D 1 333 ? -22.631 60.850  48.500  1.00 52.25  ?  349 TRP A CD1 1 
ATOM   10686 C CD2 . TRP D 1 333 ? -22.686 60.294  46.338  1.00 53.01  ?  349 TRP A CD2 1 
ATOM   10687 N NE1 . TRP D 1 333 ? -21.385 60.451  48.145  1.00 48.64  ?  349 TRP A NE1 1 
ATOM   10688 C CE2 . TRP D 1 333 ? -21.391 60.111  46.817  1.00 50.58  ?  349 TRP A CE2 1 
ATOM   10689 C CE3 . TRP D 1 333 ? -22.952 60.001  45.000  1.00 53.21  ?  349 TRP A CE3 1 
ATOM   10690 C CZ2 . TRP D 1 333 ? -20.366 59.659  46.001  1.00 53.79  ?  349 TRP A CZ2 1 
ATOM   10691 C CZ3 . TRP D 1 333 ? -21.930 59.550  44.197  1.00 52.38  ?  349 TRP A CZ3 1 
ATOM   10692 C CH2 . TRP D 1 333 ? -20.664 59.382  44.694  1.00 53.50  ?  349 TRP A CH2 1 
ATOM   10693 N N   . ASP D 1 334 ? -27.011 63.652  46.597  1.00 59.45  ?  350 ASP A N   1 
ATOM   10694 C CA  . ASP D 1 334 ? -28.356 63.866  46.049  1.00 57.41  ?  350 ASP A CA  1 
ATOM   10695 C C   . ASP D 1 334 ? -28.380 63.188  44.678  1.00 63.27  ?  350 ASP A C   1 
ATOM   10696 O O   . ASP D 1 334 ? -27.913 63.764  43.686  1.00 65.83  ?  350 ASP A O   1 
ATOM   10697 C CB  . ASP D 1 334 ? -28.653 65.372  45.983  1.00 56.27  ?  350 ASP A CB  1 
ATOM   10698 C CG  . ASP D 1 334 ? -30.013 65.743  45.302  1.00 69.77  ?  350 ASP A CG  1 
ATOM   10699 O OD1 . ASP D 1 334 ? -30.770 64.887  44.764  1.00 65.93  ?  350 ASP A OD1 1 
ATOM   10700 O OD2 . ASP D 1 334 ? -30.355 66.945  45.341  1.00 75.55  -1 350 ASP A OD2 1 
ATOM   10701 N N   . LEU D 1 335 ? -28.782 61.916  44.627  1.00 58.30  ?  351 LEU A N   1 
ATOM   10702 C CA  . LEU D 1 335 ? -28.687 61.143  43.356  1.00 58.13  ?  351 LEU A CA  1 
ATOM   10703 C C   . LEU D 1 335 ? -29.900 61.413  42.469  1.00 57.89  ?  351 LEU A C   1 
ATOM   10704 O O   . LEU D 1 335 ? -29.775 61.322  41.244  1.00 54.77  ?  351 LEU A O   1 
ATOM   10705 C CB  . LEU D 1 335 ? -28.590 59.651  43.689  1.00 56.32  ?  351 LEU A CB  1 
ATOM   10706 C CG  . LEU D 1 335 ? -27.304 59.180  44.359  1.00 57.03  ?  351 LEU A CG  1 
ATOM   10707 C CD1 . LEU D 1 335 ? -27.485 59.094  45.865  1.00 56.59  ?  351 LEU A CD1 1 
ATOM   10708 C CD2 . LEU D 1 335 ? -26.893 57.828  43.807  1.00 60.07  ?  351 LEU A CD2 1 
ATOM   10709 N N   . GLY D 1 336 ? -31.032 61.731  43.077  1.00 56.96  ?  352 GLY A N   1 
ATOM   10710 C CA  . GLY D 1 336 ? -32.236 62.032  42.290  1.00 57.52  ?  352 GLY A CA  1 
ATOM   10711 C C   . GLY D 1 336 ? -33.299 60.970  42.445  1.00 54.67  ?  352 GLY A C   1 
ATOM   10712 O O   . GLY D 1 336 ? -33.064 59.992  43.167  1.00 53.39  ?  352 GLY A O   1 
ATOM   10713 N N   . LYS D 1 337 ? -34.445 61.179  41.812  1.00 52.62  ?  353 LYS A N   1 
ATOM   10714 C CA  . LYS D 1 337 ? -35.553 60.203  41.897  1.00 51.94  ?  353 LYS A CA  1 
ATOM   10715 C C   . LYS D 1 337 ? -35.779 59.841  43.364  1.00 50.90  ?  353 LYS A C   1 
ATOM   10716 O O   . LYS D 1 337 ? -36.058 58.670  43.638  1.00 48.90  ?  353 LYS A O   1 
ATOM   10717 C CB  . LYS D 1 337 ? -35.256 59.009  40.989  1.00 50.19  ?  353 LYS A CB  1 
ATOM   10718 C CG  . LYS D 1 337 ? -34.741 59.373  39.604  1.00 55.54  ?  353 LYS A CG  1 
ATOM   10719 C CD  . LYS D 1 337 ? -35.602 58.840  38.490  1.00 59.26  ?  353 LYS A CD  1 
ATOM   10720 C CE  . LYS D 1 337 ? -36.556 59.876  37.943  1.00 61.46  ?  353 LYS A CE  1 
ATOM   10721 N NZ  . LYS D 1 337 ? -36.991 59.551  36.564  1.00 64.14  ?  353 LYS A NZ  1 
ATOM   10722 N N   . GLY D 1 338 ? -35.632 60.808  44.268  1.00 49.13  ?  354 GLY A N   1 
ATOM   10723 C CA  . GLY D 1 338 ? -35.960 60.578  45.687  1.00 47.82  ?  354 GLY A CA  1 
ATOM   10724 C C   . GLY D 1 338 ? -34.865 59.875  46.445  1.00 50.49  ?  354 GLY A C   1 
ATOM   10725 O O   . GLY D 1 338 ? -35.137 59.365  47.540  1.00 54.46  ?  354 GLY A O   1 
ATOM   10726 N N   . ASP D 1 339 ? -33.658 59.861  45.901  1.00 52.51  ?  355 ASP A N   1 
ATOM   10727 C CA  . ASP D 1 339 ? -32.618 59.091  46.565  1.00 56.77  ?  355 ASP A CA  1 
ATOM   10728 C C   . ASP D 1 339 ? -31.597 60.053  47.199  1.00 59.73  ?  355 ASP A C   1 
ATOM   10729 O O   . ASP D 1 339 ? -30.894 60.815  46.504  1.00 57.37  ?  355 ASP A O   1 
ATOM   10730 C CB  . ASP D 1 339 ? -31.982 58.153  45.543  1.00 59.00  ?  355 ASP A CB  1 
ATOM   10731 C CG  . ASP D 1 339 ? -30.918 57.235  46.146  1.00 64.34  ?  355 ASP A CG  1 
ATOM   10732 O OD1 . ASP D 1 339 ? -30.537 57.425  47.340  1.00 65.63  ?  355 ASP A OD1 1 
ATOM   10733 O OD2 . ASP D 1 339 ? -30.413 56.361  45.381  1.00 60.20  -1 355 ASP A OD2 1 
ATOM   10734 N N   . PHE D 1 340 ? -31.521 60.023  48.521  1.00 55.79  ?  356 PHE A N   1 
ATOM   10735 C CA  . PHE D 1 340 ? -30.507 60.783  49.230  1.00 51.40  ?  356 PHE A CA  1 
ATOM   10736 C C   . PHE D 1 340 ? -29.684 59.855  50.114  1.00 51.33  ?  356 PHE A C   1 
ATOM   10737 O O   . PHE D 1 340 ? -30.213 58.887  50.671  1.00 50.62  ?  356 PHE A O   1 
ATOM   10738 C CB  . PHE D 1 340 ? -31.127 61.835  50.077  1.00 50.40  ?  356 PHE A CB  1 
ATOM   10739 C CG  . PHE D 1 340 ? -32.091 62.699  49.373  1.00 48.72  ?  356 PHE A CG  1 
ATOM   10740 C CD1 . PHE D 1 340 ? -31.674 63.860  48.766  1.00 56.75  ?  356 PHE A CD1 1 
ATOM   10741 C CD2 . PHE D 1 340 ? -33.403 62.382  49.334  1.00 47.49  ?  356 PHE A CD2 1 
ATOM   10742 C CE1 . PHE D 1 340 ? -32.581 64.726  48.155  1.00 54.35  ?  356 PHE A CE1 1 
ATOM   10743 C CE2 . PHE D 1 340 ? -34.285 63.214  48.707  1.00 52.27  ?  356 PHE A CE2 1 
ATOM   10744 C CZ  . PHE D 1 340 ? -33.866 64.396  48.115  1.00 52.27  ?  356 PHE A CZ  1 
ATOM   10745 N N   . ARG D 1 341 ? -28.393 60.168  50.250  1.00 48.15  ?  357 ARG A N   1 
ATOM   10746 C CA  . ARG D 1 341 ? -27.411 59.307  50.903  1.00 46.25  ?  357 ARG A CA  1 
ATOM   10747 C C   . ARG D 1 341 ? -26.255 60.139  51.425  1.00 48.48  ?  357 ARG A C   1 
ATOM   10748 O O   . ARG D 1 341 ? -25.937 61.183  50.868  1.00 49.11  ?  357 ARG A O   1 
ATOM   10749 C CB  . ARG D 1 341 ? -26.843 58.248  49.962  1.00 50.57  ?  357 ARG A CB  1 
ATOM   10750 C CG  . ARG D 1 341 ? -27.876 57.274  49.369  1.00 54.30  ?  357 ARG A CG  1 
ATOM   10751 C CD  . ARG D 1 341 ? -27.237 56.299  48.385  1.00 54.10  ?  357 ARG A CD  1 
ATOM   10752 N NE  . ARG D 1 341 ? -28.192 55.624  47.520  1.00 51.76  ?  357 ARG A NE  1 
ATOM   10753 C CZ  . ARG D 1 341 ? -27.883 54.555  46.803  1.00 54.17  ?  357 ARG A CZ  1 
ATOM   10754 N NH1 . ARG D 1 341 ? -26.635 54.135  46.702  1.00 58.11  ?  357 ARG A NH1 1 
ATOM   10755 N NH2 . ARG D 1 341 ? -28.847 53.881  46.186  1.00 56.98  ?  357 ARG A NH2 1 
ATOM   10756 N N   . ILE D 1 342 ? -25.630 59.671  52.500  1.00 49.88  ?  358 ILE A N   1 
ATOM   10757 C CA  . ILE D 1 342 ? -24.402 60.264  53.011  1.00 46.74  ?  358 ILE A CA  1 
ATOM   10758 C C   . ILE D 1 342 ? -23.383 59.149  53.095  1.00 51.41  ?  358 ILE A C   1 
ATOM   10759 O O   . ILE D 1 342 ? -23.693 58.064  53.596  1.00 52.79  ?  358 ILE A O   1 
ATOM   10760 C CB  . ILE D 1 342 ? -24.584 60.897  54.396  1.00 47.16  ?  358 ILE A CB  1 
ATOM   10761 C CG1 . ILE D 1 342 ? -25.254 62.268  54.322  1.00 49.67  ?  358 ILE A CG1 1 
ATOM   10762 C CG2 . ILE D 1 342 ? -23.248 61.103  54.983  1.00 52.63  ?  358 ILE A CG2 1 
ATOM   10763 C CD1 . ILE D 1 342 ? -25.473 62.912  55.699  1.00 43.23  ?  358 ILE A CD1 1 
ATOM   10764 N N   . LEU D 1 343 ? -22.181 59.403  52.587  1.00 54.20  ?  359 LEU A N   1 
ATOM   10765 C CA  . LEU D 1 343 ? -21.077 58.448  52.605  1.00 48.95  ?  359 LEU A CA  1 
ATOM   10766 C C   . LEU D 1 343 ? -20.085 59.030  53.603  1.00 53.90  ?  359 LEU A C   1 
ATOM   10767 O O   . LEU D 1 343 ? -19.521 60.117  53.369  1.00 55.63  ?  359 LEU A O   1 
ATOM   10768 C CB  . LEU D 1 343 ? -20.428 58.321  51.232  1.00 45.20  ?  359 LEU A CB  1 
ATOM   10769 C CG  . LEU D 1 343 ? -19.501 57.159  50.898  1.00 48.86  ?  359 LEU A CG  1 
ATOM   10770 C CD1 . LEU D 1 343 ? -18.947 57.385  49.492  1.00 50.27  ?  359 LEU A CD1 1 
ATOM   10771 C CD2 . LEU D 1 343 ? -18.377 56.886  51.904  1.00 57.91  ?  359 LEU A CD2 1 
ATOM   10772 N N   . MET D 1 344 ? -19.888 58.335  54.719  1.00 50.49  ?  360 MET A N   1 
ATOM   10773 C CA  . MET D 1 344 ? -19.018 58.869  55.749  1.00 51.60  ?  360 MET A CA  1 
ATOM   10774 C C   . MET D 1 344 ? -18.575 57.699  56.599  1.00 55.63  ?  360 MET A C   1 
ATOM   10775 O O   . MET D 1 344 ? -19.437 56.935  57.044  1.00 52.68  ?  360 MET A O   1 
ATOM   10776 C CB  . MET D 1 344 ? -19.743 59.896  56.617  1.00 50.78  ?  360 MET A CB  1 
ATOM   10777 C CG  . MET D 1 344 ? -18.807 60.638  57.534  1.00 58.76  ?  360 MET A CG  1 
ATOM   10778 S SD  . MET D 1 344 ? -19.616 61.862  58.605  1.00 68.54  ?  360 MET A SD  1 
ATOM   10779 C CE  . MET D 1 344 ? -21.006 62.342  57.563  1.00 50.84  ?  360 MET A CE  1 
ATOM   10780 N N   . CYS D 1 345 ? -17.248 57.558  56.809  1.00 60.18  ?  361 CYS A N   1 
ATOM   10781 C CA  . CYS D 1 345 ? -16.669 56.451  57.591  1.00 56.79  ?  361 CYS A CA  1 
ATOM   10782 C C   . CYS D 1 345 ? -16.621 56.883  59.043  1.00 57.81  ?  361 CYS A C   1 
ATOM   10783 O O   . CYS D 1 345 ? -15.571 57.187  59.599  1.00 63.34  ?  361 CYS A O   1 
ATOM   10784 C CB  . CYS D 1 345 ? -15.292 56.063  57.076  1.00 59.25  ?  361 CYS A CB  1 
ATOM   10785 S SG  . CYS D 1 345 ? -15.357 55.600  55.384  1.00 60.87  ?  361 CYS A SG  1 
ATOM   10786 N N   . THR D 1 346 ? -17.798 56.907  59.652  1.00 57.19  ?  362 THR A N   1 
ATOM   10787 C CA  . THR D 1 346 ? -18.012 57.636  60.884  1.00 53.13  ?  362 THR A CA  1 
ATOM   10788 C C   . THR D 1 346 ? -17.333 56.917  62.036  1.00 55.47  ?  362 THR A C   1 
ATOM   10789 O O   . THR D 1 346 ? -17.564 55.721  62.254  1.00 57.27  ?  362 THR A O   1 
ATOM   10790 C CB  . THR D 1 346 ? -19.503 57.779  61.142  1.00 52.15  ?  362 THR A CB  1 
ATOM   10791 O OG1 . THR D 1 346 ? -20.135 58.315  59.978  1.00 55.15  ?  362 THR A OG1 1 
ATOM   10792 C CG2 . THR D 1 346 ? -19.740 58.708  62.287  1.00 55.07  ?  362 THR A CG2 1 
ATOM   10793 N N   . LYS D 1 347 ? -16.464 57.632  62.745  1.00 52.16  ?  363 LYS A N   1 
ATOM   10794 C CA  . LYS D 1 347 ? -15.946 57.250  64.058  1.00 49.24  ?  363 LYS A CA  1 
ATOM   10795 C C   . LYS D 1 347 ? -16.879 57.806  65.140  1.00 50.47  ?  363 LYS A C   1 
ATOM   10796 O O   . LYS D 1 347 ? -17.763 58.601  64.849  1.00 54.92  ?  363 LYS A O   1 
ATOM   10797 C CB  . LYS D 1 347 ? -14.512 57.785  64.222  1.00 55.18  ?  363 LYS A CB  1 
ATOM   10798 C CG  . LYS D 1 347 ? -13.542 57.408  63.094  1.00 57.68  ?  363 LYS A CG  1 
ATOM   10799 C CD  . LYS D 1 347 ? -13.591 55.914  62.806  1.00 55.43  ?  363 LYS A CD  1 
ATOM   10800 C CE  . LYS D 1 347 ? -12.780 55.575  61.578  1.00 61.79  ?  363 LYS A CE  1 
ATOM   10801 N NZ  . LYS D 1 347 ? -12.898 54.129  61.262  1.00 67.73  ?  363 LYS A NZ  1 
ATOM   10802 N N   . VAL D 1 348 ? -16.698 57.394  66.390  1.00 47.20  ?  364 VAL A N   1 
ATOM   10803 C CA  . VAL D 1 348 ? -17.496 57.956  67.497  1.00 49.52  ?  364 VAL A CA  1 
ATOM   10804 C C   . VAL D 1 348 ? -16.635 59.001  68.178  1.00 52.67  ?  364 VAL A C   1 
ATOM   10805 O O   . VAL D 1 348 ? -16.074 58.793  69.247  1.00 60.57  ?  364 VAL A O   1 
ATOM   10806 C CB  . VAL D 1 348 ? -17.992 56.879  68.447  1.00 48.71  ?  364 VAL A CB  1 
ATOM   10807 C CG1 . VAL D 1 348 ? -18.862 57.477  69.524  1.00 52.75  ?  364 VAL A CG1 1 
ATOM   10808 C CG2 . VAL D 1 348 ? -18.836 55.944  67.644  1.00 47.34  ?  364 VAL A CG2 1 
ATOM   10809 N N   . THR D 1 349 ? -16.589 60.175  67.570  1.00 49.55  ?  365 THR A N   1 
ATOM   10810 C CA  . THR D 1 349 ? -15.885 61.329  68.119  1.00 50.04  ?  365 THR A CA  1 
ATOM   10811 C C   . THR D 1 349 ? -16.857 62.494  68.077  1.00 50.87  ?  365 THR A C   1 
ATOM   10812 O O   . THR D 1 349 ? -17.924 62.417  67.470  1.00 53.66  ?  365 THR A O   1 
ATOM   10813 C CB  . THR D 1 349 ? -14.616 61.642  67.307  1.00 52.29  ?  365 THR A CB  1 
ATOM   10814 O OG1 . THR D 1 349 ? -14.996 62.305  66.105  1.00 59.22  ?  365 THR A OG1 1 
ATOM   10815 C CG2 . THR D 1 349 ? -13.968 60.345  66.874  1.00 56.51  ?  365 THR A CG2 1 
ATOM   10816 N N   . MET D 1 350 ? -16.506 63.577  68.744  1.00 48.74  ?  366 MET A N   1 
ATOM   10817 C CA  . MET D 1 350 ? -17.300 64.779  68.592  1.00 48.43  ?  366 MET A CA  1 
ATOM   10818 C C   . MET D 1 350 ? -17.089 65.399  67.214  1.00 55.46  ?  366 MET A C   1 
ATOM   10819 O O   . MET D 1 350 ? -17.993 66.032  66.677  1.00 56.36  ?  366 MET A O   1 
ATOM   10820 C CB  . MET D 1 350 ? -16.945 65.732  69.712  1.00 45.89  ?  366 MET A CB  1 
ATOM   10821 C CG  . MET D 1 350 ? -17.650 67.041  69.649  1.00 44.35  ?  366 MET A CG  1 
ATOM   10822 S SD  . MET D 1 350 ? -17.089 68.048  71.000  1.00 46.49  ?  366 MET A SD  1 
ATOM   10823 C CE  . MET D 1 350 ? -18.043 69.580  70.878  1.00 54.10  ?  366 MET A CE  1 
ATOM   10824 N N   . ASP D 1 351 ? -15.906 65.244  66.632  1.00 63.01  ?  367 ASP A N   1 
ATOM   10825 C CA  . ASP D 1 351 ? -15.674 65.741  65.282  1.00 63.07  ?  367 ASP A CA  1 
ATOM   10826 C C   . ASP D 1 351 ? -16.629 65.079  64.293  1.00 61.64  ?  367 ASP A C   1 
ATOM   10827 O O   . ASP D 1 351 ? -17.215 65.743  63.436  1.00 62.87  ?  367 ASP A O   1 
ATOM   10828 C CB  . ASP D 1 351 ? -14.212 65.478  64.902  1.00 75.01  ?  367 ASP A CB  1 
ATOM   10829 C CG  . ASP D 1 351 ? -13.278 66.571  65.365  1.00 77.83  ?  367 ASP A CG  1 
ATOM   10830 O OD1 . ASP D 1 351 ? -13.807 67.613  65.787  1.00 84.73  ?  367 ASP A OD1 1 
ATOM   10831 O OD2 . ASP D 1 351 ? -12.040 66.350  65.399  1.00 84.13  -1 367 ASP A OD2 1 
ATOM   10832 N N   . ASP D 1 352 ? -16.818 63.773  64.399  1.00 48.77  ?  368 ASP A N   1 
ATOM   10833 C CA  . ASP D 1 352 ? -17.735 63.155  63.460  1.00 52.52  ?  368 ASP A CA  1 
ATOM   10834 C C   . ASP D 1 352 ? -19.177 63.431  63.824  1.00 52.72  ?  368 ASP A C   1 
ATOM   10835 O O   . ASP D 1 352 ? -20.024 63.557  62.936  1.00 51.53  ?  368 ASP A O   1 
ATOM   10836 C CB  . ASP D 1 352 ? -17.426 61.670  63.348  1.00 52.06  ?  368 ASP A CB  1 
ATOM   10837 C CG  . ASP D 1 352 ? -16.230 61.433  62.471  1.00 60.02  ?  368 ASP A CG  1 
ATOM   10838 O OD1 . ASP D 1 352 ? -15.532 62.440  62.196  1.00 61.05  ?  368 ASP A OD1 1 
ATOM   10839 O OD2 . ASP D 1 352 ? -15.983 60.271  62.037  1.00 57.23  -1 368 ASP A OD2 1 
ATOM   10840 N N   . PHE D 1 353 ? -19.475 63.566  65.117  1.00 52.69  ?  369 PHE A N   1 
ATOM   10841 C CA  . PHE D 1 353 ? -20.817 63.974  65.523  1.00 47.58  ?  369 PHE A CA  1 
ATOM   10842 C C   . PHE D 1 353 ? -21.173 65.315  64.908  1.00 47.87  ?  369 PHE A C   1 
ATOM   10843 O O   . PHE D 1 353 ? -22.320 65.522  64.499  1.00 49.49  ?  369 PHE A O   1 
ATOM   10844 C CB  . PHE D 1 353 ? -20.909 64.042  67.054  1.00 48.43  ?  369 PHE A CB  1 
ATOM   10845 C CG  . PHE D 1 353 ? -22.156 64.725  67.600  1.00 48.35  ?  369 PHE A CG  1 
ATOM   10846 C CD1 . PHE D 1 353 ? -23.327 63.999  67.824  1.00 46.48  ?  369 PHE A CD1 1 
ATOM   10847 C CD2 . PHE D 1 353 ? -22.140 66.075  67.939  1.00 48.18  ?  369 PHE A CD2 1 
ATOM   10848 C CE1 . PHE D 1 353 ? -24.467 64.620  68.363  1.00 46.53  ?  369 PHE A CE1 1 
ATOM   10849 C CE2 . PHE D 1 353 ? -23.293 66.705  68.476  1.00 47.28  ?  369 PHE A CE2 1 
ATOM   10850 C CZ  . PHE D 1 353 ? -24.451 65.976  68.683  1.00 43.77  ?  369 PHE A CZ  1 
ATOM   10851 N N   . LEU D 1 354 ? -20.203 66.225  64.786  1.00 45.79  ?  370 LEU A N   1 
ATOM   10852 C CA  . LEU D 1 354 ? -20.528 67.498  64.157  1.00 43.98  ?  370 LEU A CA  1 
ATOM   10853 C C   . LEU D 1 354 ? -20.548 67.395  62.636  1.00 47.20  ?  370 LEU A C   1 
ATOM   10854 O O   . LEU D 1 354 ? -21.405 68.009  61.975  1.00 52.53  ?  370 LEU A O   1 
ATOM   10855 C CB  . LEU D 1 354 ? -19.564 68.601  64.587  1.00 49.65  ?  370 LEU A CB  1 
ATOM   10856 C CG  . LEU D 1 354 ? -19.441 69.022  66.050  1.00 48.20  ?  370 LEU A CG  1 
ATOM   10857 C CD1 . LEU D 1 354 ? -18.572 70.234  66.051  1.00 43.54  ?  370 LEU A CD1 1 
ATOM   10858 C CD2 . LEU D 1 354 ? -20.747 69.314  66.763  1.00 46.94  ?  370 LEU A CD2 1 
ATOM   10859 N N   . THR D 1 355 ? -19.615 66.650  62.051  1.00 46.15  ?  371 THR A N   1 
ATOM   10860 C CA  . THR D 1 355 ? -19.702 66.452  60.610  1.00 47.90  ?  371 THR A CA  1 
ATOM   10861 C C   . THR D 1 355 ? -21.037 65.824  60.183  1.00 50.31  ?  371 THR A C   1 
ATOM   10862 O O   . THR D 1 355 ? -21.537 66.118  59.087  1.00 50.07  ?  371 THR A O   1 
ATOM   10863 C CB  . THR D 1 355 ? -18.492 65.655  60.156  1.00 48.24  ?  371 THR A CB  1 
ATOM   10864 O OG1 . THR D 1 355 ? -17.354 66.472  60.414  1.00 50.28  ?  371 THR A OG1 1 
ATOM   10865 C CG2 . THR D 1 355 ? -18.529 65.311  58.676  1.00 48.88  ?  371 THR A CG2 1 
ATOM   10866 N N   . ALA D 1 356 ? -21.659 65.000  61.024  1.00 48.13  ?  372 ALA A N   1 
ATOM   10867 C CA  . ALA D 1 356 ? -22.947 64.461  60.620  1.00 42.26  ?  372 ALA A CA  1 
ATOM   10868 C C   . ALA D 1 356 ? -23.948 65.585  60.445  1.00 45.69  ?  372 ALA A C   1 
ATOM   10869 O O   . ALA D 1 356 ? -24.634 65.658  59.427  1.00 52.06  ?  372 ALA A O   1 
ATOM   10870 C CB  . ALA D 1 356 ? -23.453 63.427  61.614  1.00 42.43  ?  372 ALA A CB  1 
ATOM   10871 N N   . HIS D 1 357 ? -24.037 66.495  61.408  1.00 43.79  ?  373 HIS A N   1 
ATOM   10872 C CA  . HIS D 1 357 ? -24.960 67.613  61.245  1.00 43.83  ?  373 HIS A CA  1 
ATOM   10873 C C   . HIS D 1 357 ? -24.638 68.459  59.997  1.00 44.15  ?  373 HIS A C   1 
ATOM   10874 O O   . HIS D 1 357 ? -25.547 68.892  59.289  1.00 47.35  ?  373 HIS A O   1 
ATOM   10875 C CB  . HIS D 1 357 ? -24.968 68.467  62.509  1.00 43.27  ?  373 HIS A CB  1 
ATOM   10876 C CG  . HIS D 1 357 ? -25.575 67.807  63.715  1.00 43.50  ?  373 HIS A CG  1 
ATOM   10877 N ND1 . HIS D 1 357 ? -24.970 66.772  64.388  1.00 42.96  ?  373 HIS A ND1 1 
ATOM   10878 C CD2 . HIS D 1 357 ? -26.673 68.128  64.446  1.00 49.19  ?  373 HIS A CD2 1 
ATOM   10879 C CE1 . HIS D 1 357 ? -25.693 66.445  65.448  1.00 48.53  ?  373 HIS A CE1 1 
ATOM   10880 N NE2 . HIS D 1 357 ? -26.739 67.247  65.504  1.00 47.52  ?  373 HIS A NE2 1 
ATOM   10881 N N   . HIS D 1 358 ? -23.361 68.686  59.681  1.00 46.66  ?  374 HIS A N   1 
ATOM   10882 C CA  . HIS D 1 358 ? -23.035 69.404  58.430  1.00 46.76  ?  374 HIS A CA  1 
ATOM   10883 C C   . HIS D 1 358 ? -23.537 68.664  57.176  1.00 45.44  ?  374 HIS A C   1 
ATOM   10884 O O   . HIS D 1 358 ? -24.263 69.223  56.336  1.00 41.90  ?  374 HIS A O   1 
ATOM   10885 C CB  . HIS D 1 358 ? -21.519 69.649  58.357  1.00 43.58  ?  374 HIS A CB  1 
ATOM   10886 C CG  . HIS D 1 358 ? -21.045 70.376  57.116  1.00 45.18  ?  374 HIS A CG  1 
ATOM   10887 N ND1 . HIS D 1 358 ? -20.511 71.649  57.166  1.00 46.84  ?  374 HIS A ND1 1 
ATOM   10888 C CD2 . HIS D 1 358 ? -20.867 69.944  55.829  1.00 43.89  ?  374 HIS A CD2 1 
ATOM   10889 C CE1 . HIS D 1 358 ? -20.112 72.003  55.957  1.00 44.99  ?  374 HIS A CE1 1 
ATOM   10890 N NE2 . HIS D 1 358 ? -20.304 70.984  55.126  1.00 41.27  ?  374 HIS A NE2 1 
ATOM   10891 N N   . GLU D 1 359 ? -23.115 67.428  57.011  1.00 45.58  ?  375 GLU A N   1 
ATOM   10892 C CA  . GLU D 1 359 ? -23.426 66.703  55.792  1.00 41.88  ?  375 GLU A CA  1 
ATOM   10893 C C   . GLU D 1 359 ? -24.937 66.444  55.676  1.00 46.96  ?  375 GLU A C   1 
ATOM   10894 O O   . GLU D 1 359 ? -25.517 66.547  54.578  1.00 51.87  ?  375 GLU A O   1 
ATOM   10895 C CB  . GLU D 1 359 ? -22.561 65.437  55.775  1.00 39.65  ?  375 GLU A CB  1 
ATOM   10896 C CG  . GLU D 1 359 ? -21.076 65.750  55.578  1.00 38.87  ?  375 GLU A CG  1 
ATOM   10897 C CD  . GLU D 1 359 ? -20.826 66.602  54.342  1.00 48.54  ?  375 GLU A CD  1 
ATOM   10898 O OE1 . GLU D 1 359 ? -21.464 66.275  53.300  1.00 54.73  ?  375 GLU A OE1 1 
ATOM   10899 O OE2 . GLU D 1 359 ? -20.076 67.624  54.384  1.00 49.48  -1 375 GLU A OE2 1 
ATOM   10900 N N   . MET D 1 360 ? -25.614 66.153  56.810  1.00 47.96  ?  376 MET A N   1 
ATOM   10901 C CA  . MET D 1 360 ? -27.082 66.040  56.815  1.00 44.79  ?  376 MET A CA  1 
ATOM   10902 C C   . MET D 1 360 ? -27.773 67.353  56.490  1.00 42.22  ?  376 MET A C   1 
ATOM   10903 O O   . MET D 1 360 ? -28.860 67.343  55.919  1.00 45.94  ?  376 MET A O   1 
ATOM   10904 C CB  . MET D 1 360 ? -27.624 65.540  58.155  1.00 41.47  ?  376 MET A CB  1 
ATOM   10905 C CG  . MET D 1 360 ? -29.120 65.210  58.106  1.00 42.38  ?  376 MET A CG  1 
ATOM   10906 S SD  . MET D 1 360 ? -29.904 64.307  59.492  1.00 44.50  ?  376 MET A SD  1 
ATOM   10907 C CE  . MET D 1 360 ? -29.159 62.712  59.261  1.00 49.63  ?  376 MET A CE  1 
ATOM   10908 N N   . GLY D 1 361 ? -27.189 68.488  56.862  1.00 43.78  ?  377 GLY A N   1 
ATOM   10909 C CA  . GLY D 1 361 ? -27.740 69.748  56.400  1.00 42.33  ?  377 GLY A CA  1 
ATOM   10910 C C   . GLY D 1 361 ? -27.644 69.879  54.897  1.00 41.39  ?  377 GLY A C   1 
ATOM   10911 O O   . GLY D 1 361 ? -28.549 70.408  54.253  1.00 44.21  ?  377 GLY A O   1 
ATOM   10912 N N   . HIS D 1 362 ? -26.542 69.408  54.319  1.00 44.58  ?  378 HIS A N   1 
ATOM   10913 C CA  . HIS D 1 362 ? -26.481 69.352  52.860  1.00 44.84  ?  378 HIS A CA  1 
ATOM   10914 C C   . HIS D 1 362 ? -27.685 68.584  52.334  1.00 45.79  ?  378 HIS A C   1 
ATOM   10915 O O   . HIS D 1 362 ? -28.398 69.065  51.447  1.00 49.15  ?  378 HIS A O   1 
ATOM   10916 C CB  . HIS D 1 362 ? -25.158 68.709  52.377  1.00 48.95  ?  378 HIS A CB  1 
ATOM   10917 C CG  . HIS D 1 362 ? -23.933 69.602  52.445  1.00 48.08  ?  378 HIS A CG  1 
ATOM   10918 N ND1 . HIS D 1 362 ? -23.950 70.952  52.141  1.00 46.45  ?  378 HIS A ND1 1 
ATOM   10919 C CD2 . HIS D 1 362 ? -22.652 69.319  52.807  1.00 47.73  ?  378 HIS A CD2 1 
ATOM   10920 C CE1 . HIS D 1 362 ? -22.738 71.458  52.310  1.00 47.26  ?  378 HIS A CE1 1 
ATOM   10921 N NE2 . HIS D 1 362 ? -21.934 70.490  52.726  1.00 49.71  ?  378 HIS A NE2 1 
ATOM   10922 N N   . ILE D 1 363 ? -27.952 67.401  52.910  1.00 46.17  ?  379 ILE A N   1 
ATOM   10923 C CA  . ILE D 1 363 ? -29.114 66.602  52.481  1.00 50.87  ?  379 ILE A CA  1 
ATOM   10924 C C   . ILE D 1 363 ? -30.412 67.339  52.735  1.00 48.79  ?  379 ILE A C   1 
ATOM   10925 O O   . ILE D 1 363 ? -31.397 67.173  52.010  1.00 51.61  ?  379 ILE A O   1 
ATOM   10926 C CB  . ILE D 1 363 ? -29.131 65.234  53.166  1.00 48.62  ?  379 ILE A CB  1 
ATOM   10927 C CG1 . ILE D 1 363 ? -27.919 64.410  52.758  1.00 54.04  ?  379 ILE A CG1 1 
ATOM   10928 C CG2 . ILE D 1 363 ? -30.435 64.548  52.917  1.00 43.98  ?  379 ILE A CG2 1 
ATOM   10929 C CD1 . ILE D 1 363 ? -27.983 63.882  51.369  1.00 54.03  ?  379 ILE A CD1 1 
ATOM   10930 N N   . GLN D 1 364 ? -30.449 68.136  53.784  1.00 48.91  ?  380 GLN A N   1 
ATOM   10931 C CA  . GLN D 1 364 ? -31.665 68.861  54.113  1.00 44.09  ?  380 GLN A CA  1 
ATOM   10932 C C   . GLN D 1 364 ? -31.985 69.886  53.034  1.00 48.45  ?  380 GLN A C   1 
ATOM   10933 O O   . GLN D 1 364 ? -33.136 70.006  52.584  1.00 54.22  ?  380 GLN A O   1 
ATOM   10934 C CB  . GLN D 1 364 ? -31.484 69.508  55.476  1.00 42.73  ?  380 GLN A CB  1 
ATOM   10935 C CG  . GLN D 1 364 ? -32.721 69.617  56.296  1.00 42.13  ?  380 GLN A CG  1 
ATOM   10936 C CD  . GLN D 1 364 ? -33.190 68.277  56.739  1.00 42.41  ?  380 GLN A CD  1 
ATOM   10937 O OE1 . GLN D 1 364 ? -34.355 67.956  56.623  1.00 48.52  ?  380 GLN A OE1 1 
ATOM   10938 N NE2 . GLN D 1 364 ? -32.271 67.443  57.124  1.00 43.31  ?  380 GLN A NE2 1 
ATOM   10939 N N   . TYR D 1 365 ? -30.957 70.608  52.584  1.00 50.44  ?  381 TYR A N   1 
ATOM   10940 C CA  . TYR D 1 365 ? -31.089 71.489  51.423  1.00 52.81  ?  381 TYR A CA  1 
ATOM   10941 C C   . TYR D 1 365 ? -31.551 70.683  50.211  1.00 52.49  ?  381 TYR A C   1 
ATOM   10942 O O   . TYR D 1 365 ? -32.524 71.047  49.547  1.00 56.44  ?  381 TYR A O   1 
ATOM   10943 C CB  . TYR D 1 365 ? -29.740 72.158  51.115  1.00 54.28  ?  381 TYR A CB  1 
ATOM   10944 C CG  . TYR D 1 365 ? -29.729 73.505  50.392  1.00 51.90  ?  381 TYR A CG  1 
ATOM   10945 C CD1 . TYR D 1 365 ? -30.868 74.038  49.820  1.00 51.46  ?  381 TYR A CD1 1 
ATOM   10946 C CD2 . TYR D 1 365 ? -28.556 74.260  50.330  1.00 49.28  ?  381 TYR A CD2 1 
ATOM   10947 C CE1 . TYR D 1 365 ? -30.837 75.300  49.195  1.00 54.33  ?  381 TYR A CE1 1 
ATOM   10948 C CE2 . TYR D 1 365 ? -28.515 75.518  49.707  1.00 49.10  ?  381 TYR A CE2 1 
ATOM   10949 C CZ  . TYR D 1 365 ? -29.659 76.042  49.134  1.00 50.73  ?  381 TYR A CZ  1 
ATOM   10950 O OH  . TYR D 1 365 ? -29.631 77.290  48.507  1.00 45.90  ?  381 TYR A OH  1 
ATOM   10951 N N   . ASP D 1 366 ? -30.885 69.556  49.936  1.00 58.08  ?  382 ASP A N   1 
ATOM   10952 C CA  . ASP D 1 366 ? -31.204 68.776  48.737  1.00 61.63  ?  382 ASP A CA  1 
ATOM   10953 C C   . ASP D 1 366 ? -32.691 68.415  48.676  1.00 60.71  ?  382 ASP A C   1 
ATOM   10954 O O   . ASP D 1 366 ? -33.374 68.704  47.684  1.00 59.39  ?  382 ASP A O   1 
ATOM   10955 C CB  . ASP D 1 366 ? -30.331 67.512  48.664  1.00 61.66  ?  382 ASP A CB  1 
ATOM   10956 C CG  . ASP D 1 366 ? -28.853 67.825  48.483  1.00 64.01  ?  382 ASP A CG  1 
ATOM   10957 O OD1 . ASP D 1 366 ? -28.546 68.933  47.998  1.00 69.77  ?  382 ASP A OD1 1 
ATOM   10958 O OD2 . ASP D 1 366 ? -27.987 66.963  48.785  1.00 65.59  -1 382 ASP A OD2 1 
ATOM   10959 N N   . MET D 1 367 ? -33.201 67.765  49.728  1.00 56.43  ?  383 MET A N   1 
ATOM   10960 C CA  . MET D 1 367 ? -34.627 67.498  49.852  1.00 50.74  ?  383 MET A CA  1 
ATOM   10961 C C   . MET D 1 367 ? -35.474 68.755  49.757  1.00 51.80  ?  383 MET A C   1 
ATOM   10962 O O   . MET D 1 367 ? -36.641 68.694  49.359  1.00 52.81  ?  383 MET A O   1 
ATOM   10963 C CB  . MET D 1 367 ? -34.889 66.810  51.178  1.00 50.11  ?  383 MET A CB  1 
ATOM   10964 C CG  . MET D 1 367 ? -34.320 65.444  51.258  1.00 44.90  ?  383 MET A CG  1 
ATOM   10965 S SD  . MET D 1 367 ? -34.360 64.808  52.934  1.00 40.94  ?  383 MET A SD  1 
ATOM   10966 C CE  . MET D 1 367 ? -36.085 64.588  53.396  1.00 44.01  ?  383 MET A CE  1 
ATOM   10967 N N   . ALA D 1 368 ? -34.934 69.902  50.142  1.00 52.69  ?  384 ALA A N   1 
ATOM   10968 C CA  . ALA D 1 368 ? -35.796 71.079  50.192  1.00 55.17  ?  384 ALA A CA  1 
ATOM   10969 C C   . ALA D 1 368 ? -36.156 71.589  48.797  1.00 53.56  ?  384 ALA A C   1 
ATOM   10970 O O   . ALA D 1 368 ? -37.279 72.040  48.572  1.00 51.47  ?  384 ALA A O   1 
ATOM   10971 C CB  . ALA D 1 368 ? -35.129 72.178  51.015  1.00 58.77  ?  384 ALA A CB  1 
ATOM   10972 N N   . TYR D 1 369 ? -35.224 71.520  47.845  1.00 55.74  ?  385 TYR A N   1 
ATOM   10973 C CA  . TYR D 1 369 ? -35.423 72.075  46.511  1.00 54.14  ?  385 TYR A CA  1 
ATOM   10974 C C   . TYR D 1 369 ? -35.588 70.982  45.463  1.00 55.27  ?  385 TYR A C   1 
ATOM   10975 O O   . TYR D 1 369 ? -35.328 71.217  44.279  1.00 59.13  ?  385 TYR A O   1 
ATOM   10976 C CB  . TYR D 1 369 ? -34.269 73.007  46.100  1.00 55.25  ?  385 TYR A CB  1 
ATOM   10977 C CG  . TYR D 1 369 ? -32.856 72.416  46.081  1.00 56.27  ?  385 TYR A CG  1 
ATOM   10978 C CD1 . TYR D 1 369 ? -32.546 71.314  45.296  1.00 56.72  ?  385 TYR A CD1 1 
ATOM   10979 C CD2 . TYR D 1 369 ? -31.829 72.975  46.842  1.00 55.83  ?  385 TYR A CD2 1 
ATOM   10980 C CE1 . TYR D 1 369 ? -31.289 70.787  45.279  1.00 58.23  ?  385 TYR A CE1 1 
ATOM   10981 C CE2 . TYR D 1 369 ? -30.542 72.445  46.825  1.00 52.24  ?  385 TYR A CE2 1 
ATOM   10982 C CZ  . TYR D 1 369 ? -30.288 71.354  46.029  1.00 52.52  ?  385 TYR A CZ  1 
ATOM   10983 O OH  . TYR D 1 369 ? -29.051 70.785  45.950  1.00 51.85  ?  385 TYR A OH  1 
ATOM   10984 N N   . ALA D 1 370 ? -35.979 69.781  45.861  1.00 59.80  ?  386 ALA A N   1 
ATOM   10985 C CA  . ALA D 1 370 ? -36.047 68.743  44.849  1.00 62.35  ?  386 ALA A CA  1 
ATOM   10986 C C   . ALA D 1 370 ? -37.337 68.808  44.032  1.00 64.24  ?  386 ALA A C   1 
ATOM   10987 O O   . ALA D 1 370 ? -37.448 68.092  43.036  1.00 67.04  ?  386 ALA A O   1 
ATOM   10988 C CB  . ALA D 1 370 ? -35.855 67.370  45.503  1.00 64.46  ?  386 ALA A CB  1 
ATOM   10989 N N   . ALA D 1 371 ? -38.237 69.730  44.349  1.00 56.38  ?  387 ALA A N   1 
ATOM   10990 C CA  . ALA D 1 371 ? -39.421 69.889  43.478  1.00 53.45  ?  387 ALA A CA  1 
ATOM   10991 C C   . ALA D 1 371 ? -39.030 70.766  42.295  1.00 52.21  ?  387 ALA A C   1 
ATOM   10992 O O   . ALA D 1 371 ? -39.594 70.591  41.214  1.00 54.34  ?  387 ALA A O   1 
ATOM   10993 C CB  . ALA D 1 371 ? -40.538 70.512  44.255  1.00 58.08  ?  387 ALA A CB  1 
ATOM   10994 N N   . GLN D 1 372 ? -38.078 71.662  42.512  1.00 48.23  ?  388 GLN A N   1 
ATOM   10995 C CA  . GLN D 1 372 ? -37.667 72.603  41.451  1.00 50.76  ?  388 GLN A CA  1 
ATOM   10996 C C   . GLN D 1 372 ? -37.140 71.820  40.253  1.00 56.05  ?  388 GLN A C   1 
ATOM   10997 O O   . GLN D 1 372 ? -36.730 70.666  40.433  1.00 57.34  ?  388 GLN A O   1 
ATOM   10998 C CB  . GLN D 1 372 ? -36.607 73.545  42.013  1.00 49.79  ?  388 GLN A CB  1 
ATOM   10999 C CG  . GLN D 1 372 ? -37.087 74.311  43.228  1.00 50.74  ?  388 GLN A CG  1 
ATOM   11000 C CD  . GLN D 1 372 ? -37.581 75.666  42.799  1.00 54.30  ?  388 GLN A CD  1 
ATOM   11001 O OE1 . GLN D 1 372 ? -37.580 75.997  41.618  1.00 57.26  ?  388 GLN A OE1 1 
ATOM   11002 N NE2 . GLN D 1 372 ? -38.006 76.469  43.759  1.00 52.95  ?  388 GLN A NE2 1 
ATOM   11003 N N   . PRO D 1 373 ? -37.152 72.402  39.043  1.00 52.69  ?  389 PRO A N   1 
ATOM   11004 C CA  . PRO D 1 373 ? -36.624 71.736  37.873  1.00 53.90  ?  389 PRO A CA  1 
ATOM   11005 C C   . PRO D 1 373 ? -35.208 71.205  38.083  1.00 55.24  ?  389 PRO A C   1 
ATOM   11006 O O   . PRO D 1 373 ? -34.463 71.787  38.829  1.00 57.01  ?  389 PRO A O   1 
ATOM   11007 C CB  . PRO D 1 373 ? -36.551 72.832  36.808  1.00 54.65  ?  389 PRO A CB  1 
ATOM   11008 C CG  . PRO D 1 373 ? -36.991 74.112  37.480  1.00 52.09  ?  389 PRO A CG  1 
ATOM   11009 C CD  . PRO D 1 373 ? -37.715 73.707  38.742  1.00 47.66  ?  389 PRO A CD  1 
ATOM   11010 N N   . PHE D 1 374 ? -34.864 70.146  37.360  1.00 56.59  ?  390 PHE A N   1 
ATOM   11011 C CA  . PHE D 1 374 ? -33.546 69.526  37.514  1.00 53.63  ?  390 PHE A CA  1 
ATOM   11012 C C   . PHE D 1 374 ? -32.433 70.552  37.435  1.00 56.62  ?  390 PHE A C   1 
ATOM   11013 O O   . PHE D 1 374 ? -31.461 70.477  38.195  1.00 58.16  ?  390 PHE A O   1 
ATOM   11014 C CB  . PHE D 1 374 ? -33.359 68.462  36.430  1.00 55.41  ?  390 PHE A CB  1 
ATOM   11015 C CG  . PHE D 1 374 ? -32.024 67.777  36.430  1.00 50.08  ?  390 PHE A CG  1 
ATOM   11016 C CD1 . PHE D 1 374 ? -30.921 68.339  35.788  1.00 53.35  ?  390 PHE A CD1 1 
ATOM   11017 C CD2 . PHE D 1 374 ? -31.902 66.500  36.936  1.00 55.55  ?  390 PHE A CD2 1 
ATOM   11018 C CE1 . PHE D 1 374 ? -29.687 67.679  35.760  1.00 49.23  ?  390 PHE A CE1 1 
ATOM   11019 C CE2 . PHE D 1 374 ? -30.657 65.843  36.887  1.00 57.16  ?  390 PHE A CE2 1 
ATOM   11020 C CZ  . PHE D 1 374 ? -29.564 66.439  36.300  1.00 48.99  ?  390 PHE A CZ  1 
ATOM   11021 N N   . LEU D 1 375 ? -32.540 71.518  36.517  1.00 57.04  ?  391 LEU A N   1 
ATOM   11022 C CA  . LEU D 1 375 ? -31.465 72.500  36.365  1.00 55.11  ?  391 LEU A CA  1 
ATOM   11023 C C   . LEU D 1 375 ? -31.552 73.640  37.381  1.00 50.87  ?  391 LEU A C   1 
ATOM   11024 O O   . LEU D 1 375 ? -30.706 74.525  37.368  1.00 52.55  ?  391 LEU A O   1 
ATOM   11025 C CB  . LEU D 1 375 ? -31.473 73.093  34.956  1.00 51.27  ?  391 LEU A CB  1 
ATOM   11026 C CG  . LEU D 1 375 ? -31.235 72.214  33.727  1.00 48.35  ?  391 LEU A CG  1 
ATOM   11027 C CD1 . LEU D 1 375 ? -31.620 72.995  32.500  1.00 57.14  ?  391 LEU A CD1 1 
ATOM   11028 C CD2 . LEU D 1 375 ? -29.888 71.780  33.593  1.00 43.61  ?  391 LEU A CD2 1 
ATOM   11029 N N   . LEU D 1 376 ? -32.551 73.670  38.250  1.00 48.73  ?  392 LEU A N   1 
ATOM   11030 C CA  . LEU D 1 376 ? -32.553 74.650  39.321  1.00 54.26  ?  392 LEU A CA  1 
ATOM   11031 C C   . LEU D 1 376 ? -32.352 74.019  40.697  1.00 61.42  ?  392 LEU A C   1 
ATOM   11032 O O   . LEU D 1 376 ? -32.503 74.700  41.732  1.00 63.51  ?  392 LEU A O   1 
ATOM   11033 C CB  . LEU D 1 376 ? -33.824 75.490  39.276  1.00 54.03  ?  392 LEU A CB  1 
ATOM   11034 C CG  . LEU D 1 376 ? -34.078 76.203  37.951  1.00 53.71  ?  392 LEU A CG  1 
ATOM   11035 C CD1 . LEU D 1 376 ? -35.333 77.032  38.084  1.00 55.41  ?  392 LEU A CD1 1 
ATOM   11036 C CD2 . LEU D 1 376 ? -32.922 77.047  37.478  1.00 56.85  ?  392 LEU A CD2 1 
ATOM   11037 N N   . ARG D 1 377 ? -32.031 72.731  40.706  1.00 57.92  ?  393 ARG A N   1 
ATOM   11038 C CA  . ARG D 1 377 ? -31.789 72.034  41.987  1.00 55.67  ?  393 ARG A CA  1 
ATOM   11039 C C   . ARG D 1 377 ? -30.335 72.259  42.388  1.00 58.77  ?  393 ARG A C   1 
ATOM   11040 O O   . ARG D 1 377 ? -29.498 71.412  42.053  1.00 61.32  ?  393 ARG A O   1 
ATOM   11041 C CB  . ARG D 1 377 ? -32.129 70.551  41.850  1.00 53.24  ?  393 ARG A CB  1 
ATOM   11042 C CG  . ARG D 1 377 ? -33.584 70.280  41.500  1.00 55.50  ?  393 ARG A CG  1 
ATOM   11043 C CD  . ARG D 1 377 ? -33.808 68.794  41.322  1.00 58.71  ?  393 ARG A CD  1 
ATOM   11044 N NE  . ARG D 1 377 ? -35.158 68.462  40.902  1.00 53.56  ?  393 ARG A NE  1 
ATOM   11045 C CZ  . ARG D 1 377 ? -35.461 67.423  40.138  1.00 60.50  ?  393 ARG A CZ  1 
ATOM   11046 N NH1 . ARG D 1 377 ? -34.505 66.618  39.708  1.00 58.07  ?  393 ARG A NH1 1 
ATOM   11047 N NH2 . ARG D 1 377 ? -36.716 67.191  39.804  1.00 66.17  ?  393 ARG A NH2 1 
ATOM   11048 N N   . ASN D 1 378 ? -30.060 73.369  43.065  1.00 57.96  ?  394 ASN A N   1 
ATOM   11049 C CA  . ASN D 1 378 ? -28.696 73.643  43.580  1.00 58.82  ?  394 ASN A CA  1 
ATOM   11050 C C   . ASN D 1 378 ? -28.774 74.889  44.460  1.00 60.66  ?  394 ASN A C   1 
ATOM   11051 O O   . ASN D 1 378 ? -29.894 75.307  44.777  1.00 65.00  ?  394 ASN A O   1 
ATOM   11052 C CB  . ASN D 1 378 ? -27.667 73.772  42.459  1.00 64.13  ?  394 ASN A CB  1 
ATOM   11053 C CG  . ASN D 1 378 ? -26.278 73.350  42.882  1.00 71.08  ?  394 ASN A CG  1 
ATOM   11054 O OD1 . ASN D 1 378 ? -25.886 73.546  44.029  1.00 64.79  ?  394 ASN A OD1 1 
ATOM   11055 N ND2 . ASN D 1 378 ? -25.526 72.770  41.962  1.00 72.19  ?  394 ASN A ND2 1 
ATOM   11056 N N   . GLY D 1 379 ? -27.633 75.462  44.824  1.00 55.57  ?  395 GLY A N   1 
ATOM   11057 C CA  . GLY D 1 379 ? -27.628 76.615  45.740  1.00 53.30  ?  395 GLY A CA  1 
ATOM   11058 C C   . GLY D 1 379 ? -27.835 77.925  45.015  1.00 55.40  ?  395 GLY A C   1 
ATOM   11059 O O   . GLY D 1 379 ? -27.470 78.012  43.836  1.00 55.63  ?  395 GLY A O   1 
ATOM   11060 N N   . ALA D 1 380 ? -28.388 78.915  45.707  1.00 54.33  ?  396 ALA A N   1 
ATOM   11061 C CA  . ALA D 1 380 ? -28.690 80.202  45.060  1.00 54.28  ?  396 ALA A CA  1 
ATOM   11062 C C   . ALA D 1 380 ? -27.410 80.714  44.428  1.00 56.07  ?  396 ALA A C   1 
ATOM   11063 O O   . ALA D 1 380 ? -27.449 81.119  43.260  1.00 54.88  ?  396 ALA A O   1 
ATOM   11064 C CB  . ALA D 1 380 ? -29.202 81.163  46.088  1.00 54.60  ?  396 ALA A CB  1 
ATOM   11065 N N   . ASN D 1 381 ? -26.330 80.725  45.203  1.00 56.67  ?  397 ASN A N   1 
ATOM   11066 C CA  . ASN D 1 381 ? -25.016 81.132  44.649  1.00 55.56  ?  397 ASN A CA  1 
ATOM   11067 C C   . ASN D 1 381 ? -24.005 80.076  45.043  1.00 55.40  ?  397 ASN A C   1 
ATOM   11068 O O   . ASN D 1 381 ? -24.340 79.191  45.842  1.00 53.92  ?  397 ASN A O   1 
ATOM   11069 C CB  . ASN D 1 381 ? -24.587 82.558  45.003  1.00 57.28  ?  397 ASN A CB  1 
ATOM   11070 C CG  . ASN D 1 381 ? -24.299 82.814  46.462  1.00 57.61  ?  397 ASN A CG  1 
ATOM   11071 O OD1 . ASN D 1 381 ? -23.615 82.039  47.122  1.00 55.97  ?  397 ASN A OD1 1 
ATOM   11072 N ND2 . ASN D 1 381 ? -24.777 83.943  46.953  1.00 56.95  ?  397 ASN A ND2 1 
ATOM   11073 N N   . GLU D 1 382 ? -22.804 80.209  44.525  1.00 58.47  ?  398 GLU A N   1 
ATOM   11074 C CA  . GLU D 1 382 ? -21.843 79.104  44.727  1.00 59.30  ?  398 GLU A CA  1 
ATOM   11075 C C   . GLU D 1 382 ? -21.581 78.889  46.206  1.00 52.07  ?  398 GLU A C   1 
ATOM   11076 O O   . GLU D 1 382 ? -21.068 77.813  46.560  1.00 48.79  ?  398 GLU A O   1 
ATOM   11077 C CB  . GLU D 1 382 ? -20.536 79.446  44.041  1.00 61.70  ?  398 GLU A CB  1 
ATOM   11078 C CG  . GLU D 1 382 ? -20.155 80.901  44.128  1.00 60.87  ?  398 GLU A CG  1 
ATOM   11079 C CD  . GLU D 1 382 ? -18.740 80.967  43.599  1.00 62.15  ?  398 GLU A CD  1 
ATOM   11080 O OE1 . GLU D 1 382 ? -18.444 80.234  42.636  1.00 63.27  ?  398 GLU A OE1 1 
ATOM   11081 O OE2 . GLU D 1 382 ? -17.918 81.694  44.180  1.00 64.76  -1 398 GLU A OE2 1 
ATOM   11082 N N   . GLY D 1 383 ? -21.997 79.840  47.029  1.00 50.64  ?  399 GLY A N   1 
ATOM   11083 C CA  . GLY D 1 383 ? -21.648 79.711  48.447  1.00 48.42  ?  399 GLY A CA  1 
ATOM   11084 C C   . GLY D 1 383 ? -22.821 79.419  49.341  1.00 51.37  ?  399 GLY A C   1 
ATOM   11085 O O   . GLY D 1 383 ? -22.676 79.658  50.548  1.00 51.68  ?  399 GLY A O   1 
ATOM   11086 N N   . PHE D 1 384 ? -23.927 78.898  48.809  1.00 50.95  ?  400 PHE A N   1 
ATOM   11087 C CA  . PHE D 1 384 ? -25.022 78.701  49.751  1.00 47.50  ?  400 PHE A CA  1 
ATOM   11088 C C   . PHE D 1 384 ? -24.946 77.359  50.465  1.00 47.02  ?  400 PHE A C   1 
ATOM   11089 O O   . PHE D 1 384 ? -25.171 77.309  51.680  1.00 46.87  ?  400 PHE A O   1 
ATOM   11090 C CB  . PHE D 1 384 ? -26.353 78.862  49.045  1.00 54.97  ?  400 PHE A CB  1 
ATOM   11091 C CG  . PHE D 1 384 ? -26.913 80.235  49.144  1.00 51.10  ?  400 PHE A CG  1 
ATOM   11092 C CD1 . PHE D 1 384 ? -26.198 81.309  48.658  1.00 50.72  ?  400 PHE A CD1 1 
ATOM   11093 C CD2 . PHE D 1 384 ? -28.167 80.439  49.680  1.00 48.54  ?  400 PHE A CD2 1 
ATOM   11094 C CE1 . PHE D 1 384 ? -26.716 82.564  48.720  1.00 51.99  ?  400 PHE A CE1 1 
ATOM   11095 C CE2 . PHE D 1 384 ? -28.694 81.680  49.751  1.00 50.89  ?  400 PHE A CE2 1 
ATOM   11096 C CZ  . PHE D 1 384 ? -27.974 82.752  49.270  1.00 53.06  ?  400 PHE A CZ  1 
ATOM   11097 N N   . HIS D 1 385 ? -24.642 76.265  49.744  1.00 46.94  ?  401 HIS A N   1 
ATOM   11098 C CA  . HIS D 1 385 ? -24.689 74.936  50.367  1.00 48.69  ?  401 HIS A CA  1 
ATOM   11099 C C   . HIS D 1 385 ? -23.786 74.810  51.596  1.00 49.14  ?  401 HIS A C   1 
ATOM   11100 O O   . HIS D 1 385 ? -24.210 74.300  52.649  1.00 43.66  ?  401 HIS A O   1 
ATOM   11101 C CB  . HIS D 1 385 ? -24.322 73.825  49.392  1.00 48.58  ?  401 HIS A CB  1 
ATOM   11102 C CG  . HIS D 1 385 ? -25.488 73.076  48.838  1.00 50.45  ?  401 HIS A CG  1 
ATOM   11103 N ND1 . HIS D 1 385 ? -26.102 72.072  49.559  1.00 47.50  ?  401 HIS A ND1 1 
ATOM   11104 C CD2 . HIS D 1 385 ? -26.007 73.013  47.592  1.00 52.38  ?  401 HIS A CD2 1 
ATOM   11105 C CE1 . HIS D 1 385 ? -27.040 71.517  48.820  1.00 49.05  ?  401 HIS A CE1 1 
ATOM   11106 N NE2 . HIS D 1 385 ? -26.997 72.063  47.618  1.00 52.45  ?  401 HIS A NE2 1 
ATOM   11107 N N   . GLU D 1 386 ? -22.501 75.154  51.442  1.00 53.49  ?  402 GLU A N   1 
ATOM   11108 C CA  . GLU D 1 386 ? -21.607 74.916  52.562  1.00 50.85  ?  402 GLU A CA  1 
ATOM   11109 C C   . GLU D 1 386 ? -21.807 75.959  53.670  1.00 51.50  ?  402 GLU A C   1 
ATOM   11110 O O   . GLU D 1 386 ? -21.493 75.673  54.832  1.00 56.71  ?  402 GLU A O   1 
ATOM   11111 C CB  . GLU D 1 386 ? -20.150 74.744  52.050  1.00 42.19  ?  402 GLU A CB  1 
ATOM   11112 C CG  . GLU D 1 386 ? -19.626 73.229  51.599  1.00 40.22  ?  402 GLU A CG  1 
ATOM   11113 C CD  . GLU D 1 386 ? -19.614 72.102  52.738  1.00 39.11  ?  402 GLU A CD  1 
ATOM   11114 O OE1 . GLU D 1 386 ? -18.961 72.405  53.713  1.00 49.41  ?  402 GLU A OE1 1 
ATOM   11115 O OE2 . GLU D 1 386 ? -19.950 70.872  52.689  1.00 29.90  -1 402 GLU A OE2 1 
ATOM   11116 N N   . ALA D 1 387 ? -22.529 77.043  53.411  1.00 48.55  ?  403 ALA A N   1 
ATOM   11117 C CA  . ALA D 1 387 ? -22.981 77.884  54.524  1.00 49.96  ?  403 ALA A CA  1 
ATOM   11118 C C   . ALA D 1 387 ? -24.118 77.219  55.300  1.00 44.45  ?  403 ALA A C   1 
ATOM   11119 O O   . ALA D 1 387 ? -24.148 77.256  56.545  1.00 44.64  ?  403 ALA A O   1 
ATOM   11120 C CB  . ALA D 1 387 ? -23.413 79.254  54.001  1.00 52.62  ?  403 ALA A CB  1 
ATOM   11121 N N   . VAL D 1 388 ? -25.067 76.618  54.573  1.00 48.03  ?  404 VAL A N   1 
ATOM   11122 C CA  . VAL D 1 388 ? -26.160 75.886  55.215  1.00 47.06  ?  404 VAL A CA  1 
ATOM   11123 C C   . VAL D 1 388 ? -25.611 74.755  56.068  1.00 46.61  ?  404 VAL A C   1 
ATOM   11124 O O   . VAL D 1 388 ? -26.068 74.534  57.199  1.00 47.12  ?  404 VAL A O   1 
ATOM   11125 C CB  . VAL D 1 388 ? -27.156 75.356  54.164  1.00 42.38  ?  404 VAL A CB  1 
ATOM   11126 C CG1 . VAL D 1 388 ? -28.037 74.256  54.735  1.00 39.83  ?  404 VAL A CG1 1 
ATOM   11127 C CG2 . VAL D 1 388 ? -28.021 76.450  53.697  1.00 42.39  ?  404 VAL A CG2 1 
ATOM   11128 N N   . GLY D 1 389 ? -24.631 74.014  55.538  1.00 42.42  ?  405 GLY A N   1 
ATOM   11129 C CA  . GLY D 1 389 ? -24.026 72.948  56.326  1.00 45.22  ?  405 GLY A CA  1 
ATOM   11130 C C   . GLY D 1 389 ? -23.305 73.451  57.576  1.00 49.25  ?  405 GLY A C   1 
ATOM   11131 O O   . GLY D 1 389 ? -23.354 72.800  58.631  1.00 46.56  ?  405 GLY A O   1 
ATOM   11132 N N   . GLU D 1 390 ? -22.621 74.618  57.471  1.00 51.35  ?  406 GLU A N   1 
ATOM   11133 C CA  . GLU D 1 390 ? -21.822 75.138  58.580  1.00 49.67  ?  406 GLU A CA  1 
ATOM   11134 C C   . GLU D 1 390 ? -22.679 75.574  59.768  1.00 50.90  ?  406 GLU A C   1 
ATOM   11135 O O   . GLU D 1 390 ? -22.301 75.366  60.932  1.00 55.12  ?  406 GLU A O   1 
ATOM   11136 C CB  . GLU D 1 390 ? -20.998 76.323  58.098  1.00 50.19  ?  406 GLU A CB  1 
ATOM   11137 C CG  . GLU D 1 390 ? -19.901 75.951  57.188  1.00 53.96  ?  406 GLU A CG  1 
ATOM   11138 C CD  . GLU D 1 390 ? -18.771 75.335  57.950  1.00 67.69  ?  406 GLU A CD  1 
ATOM   11139 O OE1 . GLU D 1 390 ? -18.660 75.655  59.173  1.00 70.31  ?  406 GLU A OE1 1 
ATOM   11140 O OE2 . GLU D 1 390 ? -18.025 74.535  57.327  1.00 67.62  -1 406 GLU A OE2 1 
ATOM   11141 N N   . ILE D 1 391 ? -23.791 76.259  59.504  1.00 45.64  ?  407 ILE A N   1 
ATOM   11142 C CA  . ILE D 1 391 ? -24.581 76.779  60.624  1.00 46.88  ?  407 ILE A CA  1 
ATOM   11143 C C   . ILE D 1 391 ? -25.135 75.650  61.480  1.00 46.47  ?  407 ILE A C   1 
ATOM   11144 O O   . ILE D 1 391 ? -25.436 75.847  62.676  1.00 47.42  ?  407 ILE A O   1 
ATOM   11145 C CB  . ILE D 1 391 ? -25.721 77.688  60.116  1.00 50.01  ?  407 ILE A CB  1 
ATOM   11146 C CG1 . ILE D 1 391 ? -26.761 76.881  59.336  1.00 47.25  ?  407 ILE A CG1 1 
ATOM   11147 C CG2 . ILE D 1 391 ? -25.203 78.839  59.223  1.00 48.07  ?  407 ILE A CG2 1 
ATOM   11148 C CD1 . ILE D 1 391 ? -27.808 77.744  58.797  1.00 45.74  ?  407 ILE A CD1 1 
ATOM   11149 N N   . MET D 1 392 ? -25.276 74.460  60.889  1.00 45.03  ?  408 MET A N   1 
ATOM   11150 C CA  . MET D 1 392 ? -25.670 73.288  61.657  1.00 45.53  ?  408 MET A CA  1 
ATOM   11151 C C   . MET D 1 392 ? -24.632 72.961  62.729  1.00 47.31  ?  408 MET A C   1 
ATOM   11152 O O   . MET D 1 392 ? -24.951 72.887  63.922  1.00 49.17  ?  408 MET A O   1 
ATOM   11153 C CB  . MET D 1 392 ? -25.905 72.097  60.718  1.00 45.79  ?  408 MET A CB  1 
ATOM   11154 C CG  . MET D 1 392 ? -26.784 72.425  59.545  1.00 48.67  ?  408 MET A CG  1 
ATOM   11155 S SD  . MET D 1 392 ? -28.349 73.238  60.058  1.00 50.75  ?  408 MET A SD  1 
ATOM   11156 C CE  . MET D 1 392 ? -28.955 73.881  58.475  1.00 44.01  ?  408 MET A CE  1 
ATOM   11157 N N   . SER D 1 393 ? -23.379 72.772  62.334  1.00 47.86  ?  409 SER A N   1 
ATOM   11158 C CA  . SER D 1 393 ? -22.391 72.413  63.333  1.00 45.87  ?  409 SER A CA  1 
ATOM   11159 C C   . SER D 1 393 ? -22.194 73.548  64.344  1.00 48.40  ?  409 SER A C   1 
ATOM   11160 O O   . SER D 1 393 ? -21.879 73.286  65.522  1.00 51.59  ?  409 SER A O   1 
ATOM   11161 C CB  . SER D 1 393 ? -21.123 71.952  62.608  1.00 52.64  ?  409 SER A CB  1 
ATOM   11162 O OG  . SER D 1 393 ? -20.151 72.975  62.512  1.00 72.04  ?  409 SER A OG  1 
ATOM   11163 N N   . LEU D 1 394 ? -22.456 74.802  63.947  1.00 48.99  ?  410 LEU A N   1 
ATOM   11164 C CA  . LEU D 1 394 ? -22.435 75.869  64.956  1.00 47.15  ?  410 LEU A CA  1 
ATOM   11165 C C   . LEU D 1 394 ? -23.463 75.595  66.042  1.00 49.58  ?  410 LEU A C   1 
ATOM   11166 O O   . LEU D 1 394 ? -23.158 75.648  67.236  1.00 51.27  ?  410 LEU A O   1 
ATOM   11167 C CB  . LEU D 1 394 ? -22.706 77.254  64.362  1.00 45.43  ?  410 LEU A CB  1 
ATOM   11168 C CG  . LEU D 1 394 ? -21.755 78.034  63.447  1.00 47.64  ?  410 LEU A CG  1 
ATOM   11169 C CD1 . LEU D 1 394 ? -22.261 79.446  63.365  1.00 46.43  ?  410 LEU A CD1 1 
ATOM   11170 C CD2 . LEU D 1 394 ? -20.290 78.002  63.845  1.00 51.39  ?  410 LEU A CD2 1 
ATOM   11171 N N   . SER D 1 395 ? -24.696 75.279  65.639  1.00 54.25  ?  411 SER A N   1 
ATOM   11172 C CA  . SER D 1 395 ? -25.754 75.098  66.632  1.00 54.06  ?  411 SER A CA  1 
ATOM   11173 C C   . SER D 1 395 ? -25.521 73.830  67.458  1.00 48.99  ?  411 SER A C   1 
ATOM   11174 O O   . SER D 1 395 ? -25.923 73.752  68.621  1.00 50.92  ?  411 SER A O   1 
ATOM   11175 C CB  . SER D 1 395 ? -27.118 75.064  65.925  1.00 49.74  ?  411 SER A CB  1 
ATOM   11176 O OG  . SER D 1 395 ? -27.604 76.368  65.678  1.00 50.40  ?  411 SER A OG  1 
ATOM   11177 N N   . ALA D 1 396 ? -24.870 72.836  66.871  1.00 47.83  ?  412 ALA A N   1 
ATOM   11178 C CA  . ALA D 1 396 ? -24.773 71.529  67.500  1.00 51.25  ?  412 ALA A CA  1 
ATOM   11179 C C   . ALA D 1 396 ? -23.657 71.457  68.519  1.00 57.98  ?  412 ALA A C   1 
ATOM   11180 O O   . ALA D 1 396 ? -23.770 70.697  69.488  1.00 57.93  ?  412 ALA A O   1 
ATOM   11181 C CB  . ALA D 1 396 ? -24.566 70.446  66.439  1.00 48.45  ?  412 ALA A CB  1 
ATOM   11182 N N   . ALA D 1 397 ? -22.583 72.235  68.309  1.00 55.64  ?  413 ALA A N   1 
ATOM   11183 C CA  . ALA D 1 397 ? -21.406 72.230  69.172  1.00 50.17  ?  413 ALA A CA  1 
ATOM   11184 C C   . ALA D 1 397 ? -21.567 73.054  70.459  1.00 50.93  ?  413 ALA A C   1 
ATOM   11185 O O   . ALA D 1 397 ? -20.751 72.913  71.367  1.00 51.66  ?  413 ALA A O   1 
ATOM   11186 C CB  . ALA D 1 397 ? -20.218 72.737  68.350  1.00 55.11  ?  413 ALA A CB  1 
ATOM   11187 N N   . THR D 1 398 ? -22.587 73.899  70.560  1.00 52.77  ?  414 THR A N   1 
ATOM   11188 C CA  . THR D 1 398 ? -22.778 74.730  71.733  1.00 54.96  ?  414 THR A CA  1 
ATOM   11189 C C   . THR D 1 398 ? -22.873 73.846  72.966  1.00 57.09  ?  414 THR A C   1 
ATOM   11190 O O   . THR D 1 398 ? -23.318 72.692  72.889  1.00 55.29  ?  414 THR A O   1 
ATOM   11191 C CB  . THR D 1 398 ? -24.080 75.535  71.674  1.00 58.24  ?  414 THR A CB  1 
ATOM   11192 O OG1 . THR D 1 398 ? -25.207 74.642  71.769  1.00 58.14  ?  414 THR A OG1 1 
ATOM   11193 C CG2 . THR D 1 398 ? -24.176 76.283  70.363  1.00 55.03  ?  414 THR A CG2 1 
ATOM   11194 N N   . PRO D 1 399 ? -22.475 74.375  74.124  1.00 60.42  ?  415 PRO A N   1 
ATOM   11195 C CA  . PRO D 1 399 ? -22.738 73.657  75.367  1.00 57.94  ?  415 PRO A CA  1 
ATOM   11196 C C   . PRO D 1 399 ? -24.209 73.473  75.581  1.00 58.32  ?  415 PRO A C   1 
ATOM   11197 O O   . PRO D 1 399 ? -24.628 72.388  75.993  1.00 56.82  ?  415 PRO A O   1 
ATOM   11198 C CB  . PRO D 1 399 ? -22.123 74.560  76.434  1.00 62.41  ?  415 PRO A CB  1 
ATOM   11199 C CG  . PRO D 1 399 ? -21.129 75.382  75.730  1.00 64.59  ?  415 PRO A CG  1 
ATOM   11200 C CD  . PRO D 1 399 ? -21.666 75.580  74.344  1.00 60.95  ?  415 PRO A CD  1 
ATOM   11201 N N   . LYS D 1 400 ? -25.008 74.503  75.291  1.00 60.15  ?  416 LYS A N   1 
ATOM   11202 C CA  . LYS D 1 400 ? -26.450 74.386  75.476  1.00 59.13  ?  416 LYS A CA  1 
ATOM   11203 C C   . LYS D 1 400 ? -26.988 73.103  74.851  1.00 57.61  ?  416 LYS A C   1 
ATOM   11204 O O   . LYS D 1 400 ? -27.599 72.268  75.535  1.00 56.68  ?  416 LYS A O   1 
ATOM   11205 C CB  . LYS D 1 400 ? -27.158 75.619  74.910  1.00 56.29  ?  416 LYS A CB  1 
ATOM   11206 C CG  . LYS D 1 400 ? -28.605 75.569  75.301  1.00 58.92  ?  416 LYS A CG  1 
ATOM   11207 C CD  . LYS D 1 400 ? -29.620 76.323  74.419  1.00 58.89  ?  416 LYS A CD  1 
ATOM   11208 C CE  . LYS D 1 400 ? -29.453 77.848  74.510  1.00 57.28  ?  416 LYS A CE  1 
ATOM   11209 N NZ  . LYS D 1 400 ? -30.349 78.626  73.591  1.00 61.84  ?  416 LYS A NZ  1 
ATOM   11210 N N   . HIS D 1 401 ? -26.701 72.910  73.558  1.00 54.46  ?  417 HIS A N   1 
ATOM   11211 C CA  . HIS D 1 401 ? -27.132 71.723  72.825  1.00 54.32  ?  417 HIS A CA  1 
ATOM   11212 C C   . HIS D 1 401 ? -26.593 70.435  73.429  1.00 54.37  ?  417 HIS A C   1 
ATOM   11213 O O   . HIS D 1 401 ? -27.340 69.460  73.590  1.00 53.81  ?  417 HIS A O   1 
ATOM   11214 C CB  . HIS D 1 401 ? -26.706 71.861  71.364  1.00 53.50  ?  417 HIS A CB  1 
ATOM   11215 C CG  . HIS D 1 401 ? -27.222 70.768  70.488  1.00 54.14  ?  417 HIS A CG  1 
ATOM   11216 N ND1 . HIS D 1 401 ? -28.473 70.800  69.928  1.00 50.05  ?  417 HIS A ND1 1 
ATOM   11217 C CD2 . HIS D 1 401 ? -26.632 69.628  70.038  1.00 54.52  ?  417 HIS A CD2 1 
ATOM   11218 C CE1 . HIS D 1 401 ? -28.651 69.711  69.201  1.00 55.74  ?  417 HIS A CE1 1 
ATOM   11219 N NE2 . HIS D 1 401 ? -27.548 68.984  69.242  1.00 48.85  ?  417 HIS A NE2 1 
ATOM   11220 N N   . LEU D 1 402 ? -25.293 70.405  73.718  1.00 56.99  ?  418 LEU A N   1 
ATOM   11221 C CA  . LEU D 1 402 ? -24.663 69.193  74.230  1.00 56.45  ?  418 LEU A CA  1 
ATOM   11222 C C   . LEU D 1 402 ? -25.244 68.786  75.574  1.00 57.80  ?  418 LEU A C   1 
ATOM   11223 O O   . LEU D 1 402 ? -25.462 67.591  75.834  1.00 56.88  ?  418 LEU A O   1 
ATOM   11224 C CB  . LEU D 1 402 ? -23.150 69.386  74.331  1.00 52.94  ?  418 LEU A CB  1 
ATOM   11225 C CG  . LEU D 1 402 ? -22.604 69.595  72.933  1.00 53.52  ?  418 LEU A CG  1 
ATOM   11226 C CD1 . LEU D 1 402 ? -21.149 69.980  72.913  1.00 54.74  ?  418 LEU A CD1 1 
ATOM   11227 C CD2 . LEU D 1 402 ? -22.801 68.227  72.303  1.00 50.89  ?  418 LEU A CD2 1 
ATOM   11228 N N   . LYS D 1 403 ? -25.480 69.761  76.450  1.00 57.37  ?  419 LYS A N   1 
ATOM   11229 C CA  . LYS D 1 403 ? -26.210 69.480  77.673  1.00 58.31  ?  419 LYS A CA  1 
ATOM   11230 C C   . LYS D 1 403 ? -27.540 68.854  77.318  1.00 62.76  ?  419 LYS A C   1 
ATOM   11231 O O   . LYS D 1 403 ? -27.858 67.751  77.772  1.00 62.14  ?  419 LYS A O   1 
ATOM   11232 C CB  . LYS D 1 403 ? -26.426 70.763  78.465  1.00 60.24  ?  419 LYS A CB  1 
ATOM   11233 C CG  . LYS D 1 403 ? -25.190 71.349  79.123  1.00 64.72  ?  419 LYS A CG  1 
ATOM   11234 C CD  . LYS D 1 403 ? -25.534 72.574  79.971  1.00 67.88  ?  419 LYS A CD  1 
ATOM   11235 C CE  . LYS D 1 403 ? -24.326 73.071  80.760  1.00 77.33  ?  419 LYS A CE  1 
ATOM   11236 N NZ  . LYS D 1 403 ? -24.672 74.087  81.796  1.00 84.37  ?  419 LYS A NZ  1 
ATOM   11237 N N   . SER D 1 404 ? -28.293 69.527  76.433  1.00 67.82  ?  420 SER A N   1 
ATOM   11238 C CA  . SER D 1 404 ? -29.633 69.079  76.074  1.00 62.44  ?  420 SER A CA  1 
ATOM   11239 C C   . SER D 1 404 ? -29.668 67.631  75.636  1.00 62.98  ?  420 SER A C   1 
ATOM   11240 O O   . SER D 1 404 ? -30.581 66.905  76.025  1.00 62.35  ?  420 SER A O   1 
ATOM   11241 C CB  . SER D 1 404 ? -30.208 69.943  74.971  1.00 71.24  ?  420 SER A CB  1 
ATOM   11242 O OG  . SER D 1 404 ? -31.604 69.750  74.907  1.00 89.08  ?  420 SER A OG  1 
ATOM   11243 N N   . ILE D 1 405 ? -28.705 67.182  74.818  1.00 59.45  ?  421 ILE A N   1 
ATOM   11244 C CA  . ILE D 1 405 ? -28.806 65.807  74.330  1.00 56.20  ?  421 ILE A CA  1 
ATOM   11245 C C   . ILE D 1 405 ? -28.166 64.794  75.262  1.00 56.29  ?  421 ILE A C   1 
ATOM   11246 O O   . ILE D 1 405 ? -28.236 63.590  74.980  1.00 54.14  ?  421 ILE A O   1 
ATOM   11247 C CB  . ILE D 1 405 ? -28.195 65.605  72.936  1.00 51.74  ?  421 ILE A CB  1 
ATOM   11248 C CG1 . ILE D 1 405 ? -26.762 66.050  72.880  1.00 51.97  ?  421 ILE A CG1 1 
ATOM   11249 C CG2 . ILE D 1 405 ? -28.891 66.512  71.969  1.00 59.73  ?  421 ILE A CG2 1 
ATOM   11250 C CD1 . ILE D 1 405 ? -26.045 65.534  71.675  1.00 49.69  ?  421 ILE A CD1 1 
ATOM   11251 N N   . GLY D 1 406 ? -27.547 65.231  76.355  1.00 56.90  ?  422 GLY A N   1 
ATOM   11252 C CA  . GLY D 1 406 ? -26.979 64.317  77.325  1.00 58.37  ?  422 GLY A CA  1 
ATOM   11253 C C   . GLY D 1 406 ? -25.520 63.986  77.158  1.00 59.65  ?  422 GLY A C   1 
ATOM   11254 O O   . GLY D 1 406 ? -25.036 63.036  77.785  1.00 60.78  ?  422 GLY A O   1 
ATOM   11255 N N   . LEU D 1 407 ? -24.801 64.719  76.338  1.00 53.48  ?  423 LEU A N   1 
ATOM   11256 C CA  . LEU D 1 407 ? -23.388 64.421  76.227  1.00 55.77  ?  423 LEU A CA  1 
ATOM   11257 C C   . LEU D 1 407 ? -22.546 65.301  77.150  1.00 59.83  ?  423 LEU A C   1 
ATOM   11258 O O   . LEU D 1 407 ? -21.311 65.189  77.176  1.00 60.73  ?  423 LEU A O   1 
ATOM   11259 C CB  . LEU D 1 407 ? -22.887 64.590  74.790  1.00 54.10  ?  423 LEU A CB  1 
ATOM   11260 C CG  . LEU D 1 407 ? -23.331 63.571  73.757  1.00 45.97  ?  423 LEU A CG  1 
ATOM   11261 C CD1 . LEU D 1 407 ? -22.764 63.966  72.386  1.00 44.52  ?  423 LEU A CD1 1 
ATOM   11262 C CD2 . LEU D 1 407 ? -23.044 62.172  74.206  1.00 53.34  ?  423 LEU A CD2 1 
ATOM   11263 N N   . LEU D 1 408 ? -23.187 66.166  77.915  1.00 55.88  ?  424 LEU A N   1 
ATOM   11264 C CA  . LEU D 1 408 ? -22.456 67.130  78.711  1.00 56.97  ?  424 LEU A CA  1 
ATOM   11265 C C   . LEU D 1 408 ? -23.253 67.314  79.985  1.00 64.64  ?  424 LEU A C   1 
ATOM   11266 O O   . LEU D 1 408 ? -24.471 67.492  79.930  1.00 68.11  ?  424 LEU A O   1 
ATOM   11267 C CB  . LEU D 1 408 ? -22.317 68.440  77.948  1.00 57.56  ?  424 LEU A CB  1 
ATOM   11268 C CG  . LEU D 1 408 ? -21.280 69.370  78.504  1.00 62.23  ?  424 LEU A CG  1 
ATOM   11269 C CD1 . LEU D 1 408 ? -20.074 68.505  78.593  1.00 69.58  ?  424 LEU A CD1 1 
ATOM   11270 C CD2 . LEU D 1 408 ? -21.070 70.511  77.546  1.00 64.19  ?  424 LEU A CD2 1 
ATOM   11271 N N   . SER D 1 409 ? -22.626 67.218  81.095  1.00 70.64  ?  425 SER A N   1 
ATOM   11272 C CA  . SER D 1 409 ? -23.522 67.284  82.231  1.00 71.79  ?  425 SER A CA  1 
ATOM   11273 C C   . SER D 1 409 ? -23.978 68.718  82.463  1.00 77.59  ?  425 SER A C   1 
ATOM   11274 O O   . SER D 1 409 ? -23.272 69.661  82.091  1.00 82.01  ?  425 SER A O   1 
ATOM   11275 C CB  . SER D 1 409 ? -22.838 66.761  83.475  1.00 80.85  ?  425 SER A CB  1 
ATOM   11276 O OG  . SER D 1 409 ? -23.719 66.822  84.570  1.00 83.79  ?  425 SER A OG  1 
ATOM   11277 N N   . PRO D 1 410 ? -25.226 68.925  82.966  1.00 85.53  ?  426 PRO A N   1 
ATOM   11278 C CA  . PRO D 1 410 ? -25.759 70.267  83.213  1.00 90.17  ?  426 PRO A CA  1 
ATOM   11279 C C   . PRO D 1 410 ? -24.825 71.043  84.135  1.00 106.58 ?  426 PRO A C   1 
ATOM   11280 O O   . PRO D 1 410 ? -25.055 72.206  84.370  1.00 102.41 ?  426 PRO A O   1 
ATOM   11281 C CB  . PRO D 1 410 ? -27.053 70.005  83.979  1.00 83.77  ?  426 PRO A CB  1 
ATOM   11282 C CG  . PRO D 1 410 ? -27.531 68.695  83.437  1.00 78.00  ?  426 PRO A CG  1 
ATOM   11283 C CD  . PRO D 1 410 ? -26.249 67.909  83.279  1.00 79.16  ?  426 PRO A CD  1 
ATOM   11284 N N   . ASP D 1 411 ? -23.864 70.348  84.728  1.00 122.98 ?  427 ASP A N   1 
ATOM   11285 C CA  . ASP D 1 411 ? -22.992 71.004  85.731  1.00 132.22 ?  427 ASP A CA  1 
ATOM   11286 C C   . ASP D 1 411 ? -21.904 71.799  85.013  1.00 135.11 ?  427 ASP A C   1 
ATOM   11287 O O   . ASP D 1 411 ? -21.239 72.615  85.672  1.00 131.76 ?  427 ASP A O   1 
ATOM   11288 C CB  . ASP D 1 411 ? -22.429 69.953  86.693  1.00 132.31 ?  427 ASP A CB  1 
ATOM   11289 C CG  . ASP D 1 411 ? -21.339 70.469  87.614  1.00 134.47 ?  427 ASP A CG  1 
ATOM   11290 O OD1 . ASP D 1 411 ? -21.524 71.554  88.203  1.00 134.61 ?  427 ASP A OD1 1 
ATOM   11291 O OD2 . ASP D 1 411 ? -20.314 69.775  87.735  1.00 135.10 -1 427 ASP A OD2 1 
ATOM   11292 N N   . PHE D 1 412 ? -21.731 71.586  83.713  1.00 110.79 ?  428 PHE A N   1 
ATOM   11293 C CA  . PHE D 1 412 ? -20.600 72.281  83.048  1.00 109.69 ?  428 PHE A CA  1 
ATOM   11294 C C   . PHE D 1 412 ? -20.666 73.776  83.375  1.00 114.68 ?  428 PHE A C   1 
ATOM   11295 O O   . PHE D 1 412 ? -21.742 74.378  83.259  1.00 110.22 ?  428 PHE A O   1 
ATOM   11296 C CB  . PHE D 1 412 ? -20.578 72.021  81.541  1.00 97.18  ?  428 PHE A CB  1 
ATOM   11297 C CG  . PHE D 1 412 ? -19.287 72.446  80.892  1.00 94.28  ?  428 PHE A CG  1 
ATOM   11298 C CD1 . PHE D 1 412 ? -19.070 73.767  80.538  1.00 99.09  ?  428 PHE A CD1 1 
ATOM   11299 C CD2 . PHE D 1 412 ? -18.277 71.529  80.663  1.00 84.02  ?  428 PHE A CD2 1 
ATOM   11300 C CE1 . PHE D 1 412 ? -17.877 74.158  79.957  1.00 94.81  ?  428 PHE A CE1 1 
ATOM   11301 C CE2 . PHE D 1 412 ? -17.084 71.921  80.080  1.00 82.46  ?  428 PHE A CE2 1 
ATOM   11302 C CZ  . PHE D 1 412 ? -16.887 73.234  79.730  1.00 85.85  ?  428 PHE A CZ  1 
ATOM   11303 N N   . GLN D 1 413 ? -19.537 74.350  83.782  1.00 138.42 ?  429 GLN A N   1 
ATOM   11304 C CA  . GLN D 1 413 ? -19.490 75.799  84.098  1.00 133.73 ?  429 GLN A CA  1 
ATOM   11305 C C   . GLN D 1 413 ? -18.716 76.534  83.008  1.00 130.74 ?  429 GLN A C   1 
ATOM   11306 O O   . GLN D 1 413 ? -17.481 76.413  82.969  1.00 133.41 ?  429 GLN A O   1 
ATOM   11307 C CB  . GLN D 1 413 ? -18.891 76.044  85.483  1.00 142.46 ?  429 GLN A CB  1 
ATOM   11308 C CG  . GLN D 1 413 ? -18.386 77.467  85.685  1.00 145.91 ?  429 GLN A CG  1 
ATOM   11309 C CD  . GLN D 1 413 ? -19.480 78.415  86.109  1.00 150.75 ?  429 GLN A CD  1 
ATOM   11310 O OE1 . GLN D 1 413 ? -20.667 78.132  85.961  1.00 147.22 ?  429 GLN A OE1 1 
ATOM   11311 N NE2 . GLN D 1 413 ? -19.083 79.555  86.646  1.00 153.38 ?  429 GLN A NE2 1 
ATOM   11312 N N   . GLU D 1 414 ? -19.424 77.235  82.140  1.00 112.23 ?  430 GLU A N   1 
ATOM   11313 C CA  . GLU D 1 414 ? -18.854 78.040  81.091  1.00 109.98 ?  430 GLU A CA  1 
ATOM   11314 C C   . GLU D 1 414 ? -18.362 79.320  81.727  1.00 111.54 ?  430 GLU A C   1 
ATOM   11315 O O   . GLU D 1 414 ? -19.086 79.931  82.521  1.00 116.47 ?  430 GLU A O   1 
ATOM   11316 C CB  . GLU D 1 414 ? -19.896 78.294  80.016  1.00 113.82 ?  430 GLU A CB  1 
ATOM   11317 C CG  . GLU D 1 414 ? -20.684 77.040  79.755  1.00 108.47 ?  430 GLU A CG  1 
ATOM   11318 C CD  . GLU D 1 414 ? -22.083 77.314  79.306  1.00 101.19 ?  430 GLU A CD  1 
ATOM   11319 O OE1 . GLU D 1 414 ? -22.282 78.299  78.562  1.00 100.56 ?  430 GLU A OE1 1 
ATOM   11320 O OE2 . GLU D 1 414 ? -22.980 76.538  79.699  1.00 100.21 -1 430 GLU A OE2 1 
ATOM   11321 N N   . ASP D 1 415 ? -17.125 79.659  81.346  1.00 106.83 ?  431 ASP A N   1 
ATOM   11322 C CA  . ASP D 1 415 ? -16.448 80.841  81.915  1.00 105.29 ?  431 ASP A CA  1 
ATOM   11323 C C   . ASP D 1 415 ? -15.770 81.670  80.824  1.00 98.16  ?  431 ASP A C   1 
ATOM   11324 O O   . ASP D 1 415 ? -15.466 81.122  79.750  1.00 93.37  ?  431 ASP A O   1 
ATOM   11325 C CB  . ASP D 1 415 ? -15.350 80.395  82.876  1.00 105.45 ?  431 ASP A CB  1 
ATOM   11326 C CG  . ASP D 1 415 ? -14.354 79.400  82.305  1.00 99.80  ?  431 ASP A CG  1 
ATOM   11327 O OD1 . ASP D 1 415 ? -13.644 79.748  81.342  1.00 97.06  ?  431 ASP A OD1 1 
ATOM   11328 O OD2 . ASP D 1 415 ? -14.267 78.283  82.847  1.00 99.90  -1 431 ASP A OD2 1 
ATOM   11329 N N   . ASN D 1 416 ? -15.534 82.949  81.104  1.00 95.59  ?  432 ASN A N   1 
ATOM   11330 C CA  . ASN D 1 416 ? -14.795 83.814  80.155  1.00 94.82  ?  432 ASN A CA  1 
ATOM   11331 C C   . ASN D 1 416 ? -13.705 83.008  79.472  1.00 88.70  ?  432 ASN A C   1 
ATOM   11332 O O   . ASN D 1 416 ? -13.692 82.980  78.238  1.00 84.86  ?  432 ASN A O   1 
ATOM   11333 C CB  . ASN D 1 416 ? -13.997 84.886  80.888  1.00 100.22 ?  432 ASN A CB  1 
ATOM   11334 C CG  . ASN D 1 416 ? -14.817 86.097  81.250  1.00 102.47 ?  432 ASN A CG  1 
ATOM   11335 O OD1 . ASN D 1 416 ? -15.977 86.205  80.872  1.00 106.15 ?  432 ASN A OD1 1 
ATOM   11336 N ND2 . ASN D 1 416 ? -14.214 87.015  81.986  1.00 99.55  ?  432 ASN A ND2 1 
ATOM   11337 N N   . GLU D 1 417 ? -12.827 82.382  80.255  1.00 87.93  ?  433 GLU A N   1 
ATOM   11338 C CA  . GLU D 1 417 ? -11.653 81.714  79.647  1.00 76.24  ?  433 GLU A CA  1 
ATOM   11339 C C   . GLU D 1 417 ? -12.104 80.726  78.590  1.00 74.40  ?  433 GLU A C   1 
ATOM   11340 O O   . GLU D 1 417 ? -11.909 81.019  77.401  1.00 71.84  ?  433 GLU A O   1 
ATOM   11341 C CB  . GLU D 1 417 ? -10.819 81.013  80.720  1.00 77.34  ?  433 GLU A CB  1 
ATOM   11342 C CG  . GLU D 1 417 ? -10.689 81.824  81.999  1.00 82.99  ?  433 GLU A CG  1 
ATOM   11343 C CD  . GLU D 1 417 ? -9.314  81.879  82.654  1.00 80.83  ?  433 GLU A CD  1 
ATOM   11344 O OE1 . GLU D 1 417 ? -8.557  80.897  82.552  1.00 77.64  ?  433 GLU A OE1 1 
ATOM   11345 O OE2 . GLU D 1 417 ? -9.007  82.912  83.288  1.00 80.60  -1 433 GLU A OE2 1 
ATOM   11346 N N   . THR D 1 418 ? -12.750 79.640  79.004  1.00 82.13  ?  434 THR A N   1 
ATOM   11347 C CA  . THR D 1 418 ? -13.022 78.591  78.020  1.00 80.84  ?  434 THR A CA  1 
ATOM   11348 C C   . THR D 1 418 ? -13.628 79.181  76.768  1.00 75.38  ?  434 THR A C   1 
ATOM   11349 O O   . THR D 1 418 ? -13.261 78.790  75.651  1.00 70.39  ?  434 THR A O   1 
ATOM   11350 C CB  . THR D 1 418 ? -13.960 77.521  78.566  1.00 82.56  ?  434 THR A CB  1 
ATOM   11351 O OG1 . THR D 1 418 ? -15.083 78.142  79.208  1.00 92.07  ?  434 THR A OG1 1 
ATOM   11352 C CG2 . THR D 1 418 ? -13.245 76.570  79.498  1.00 87.21  ?  434 THR A CG2 1 
ATOM   11353 N N   . GLU D 1 419 ? -14.566 80.116  76.938  1.00 78.97  ?  435 GLU A N   1 
ATOM   11354 C CA  . GLU D 1 419 ? -15.174 80.761  75.779  1.00 73.83  ?  435 GLU A CA  1 
ATOM   11355 C C   . GLU D 1 419 ? -14.144 81.506  74.944  1.00 66.59  ?  435 GLU A C   1 
ATOM   11356 O O   . GLU D 1 419 ? -14.206 81.472  73.709  1.00 63.08  ?  435 GLU A O   1 
ATOM   11357 C CB  . GLU D 1 419 ? -16.309 81.686  76.205  1.00 77.13  ?  435 GLU A CB  1 
ATOM   11358 C CG  . GLU D 1 419 ? -17.508 80.933  76.671  1.00 79.54  ?  435 GLU A CG  1 
ATOM   11359 C CD  . GLU D 1 419 ? -18.607 81.856  77.096  1.00 87.14  ?  435 GLU A CD  1 
ATOM   11360 O OE1 . GLU D 1 419 ? -18.661 82.997  76.578  1.00 85.73  ?  435 GLU A OE1 1 
ATOM   11361 O OE2 . GLU D 1 419 ? -19.463 81.409  77.893  1.00 97.01  -1 435 GLU A OE2 1 
ATOM   11362 N N   . ILE D 1 420 ? -13.198 82.191  75.581  1.00 69.41  ?  436 ILE A N   1 
ATOM   11363 C CA  . ILE D 1 420 ? -12.224 82.916  74.778  1.00 64.94  ?  436 ILE A CA  1 
ATOM   11364 C C   . ILE D 1 420 ? -11.299 81.953  74.055  1.00 61.80  ?  436 ILE A C   1 
ATOM   11365 O O   . ILE D 1 420 ? -10.950 82.173  72.894  1.00 59.15  ?  436 ILE A O   1 
ATOM   11366 C CB  . ILE D 1 420 ? -11.475 83.922  75.647  1.00 67.25  ?  436 ILE A CB  1 
ATOM   11367 C CG1 . ILE D 1 420 ? -12.466 85.007  76.032  1.00 65.60  ?  436 ILE A CG1 1 
ATOM   11368 C CG2 . ILE D 1 420 ? -10.305 84.499  74.905  1.00 66.48  ?  436 ILE A CG2 1 
ATOM   11369 C CD1 . ILE D 1 420 ? -12.881 85.893  74.883  1.00 64.01  ?  436 ILE A CD1 1 
ATOM   11370 N N   . ASN D 1 421 ? -10.901 80.869  74.717  1.00 62.32  ?  437 ASN A N   1 
ATOM   11371 C CA  . ASN D 1 421 ? -10.183 79.799  74.026  1.00 60.04  ?  437 ASN A CA  1 
ATOM   11372 C C   . ASN D 1 421 ? -10.906 79.418  72.761  1.00 58.01  ?  437 ASN A C   1 
ATOM   11373 O O   . ASN D 1 421 ? -10.316 79.389  71.673  1.00 56.47  ?  437 ASN A O   1 
ATOM   11374 C CB  . ASN D 1 421 ? -10.074 78.561  74.907  1.00 62.46  ?  437 ASN A CB  1 
ATOM   11375 C CG  . ASN D 1 421 ? -8.956  78.628  75.876  1.00 65.48  ?  437 ASN A CG  1 
ATOM   11376 O OD1 . ASN D 1 421 ? -8.196  79.592  75.911  1.00 66.39  ?  437 ASN A OD1 1 
ATOM   11377 N ND2 . ASN D 1 421 ? -8.884  77.616  76.744  1.00 68.10  ?  437 ASN A ND2 1 
ATOM   11378 N N   . PHE D 1 422 ? -12.197 79.092  72.916  1.00 58.85  ?  438 PHE A N   1 
ATOM   11379 C CA  . PHE D 1 422 ? -13.039 78.642  71.812  1.00 56.04  ?  438 PHE A CA  1 
ATOM   11380 C C   . PHE D 1 422 ? -13.063 79.688  70.695  1.00 55.08  ?  438 PHE A C   1 
ATOM   11381 O O   . PHE D 1 422 ? -12.787 79.389  69.527  1.00 49.66  ?  438 PHE A O   1 
ATOM   11382 C CB  . PHE D 1 422 ? -14.467 78.398  72.326  1.00 56.45  ?  438 PHE A CB  1 
ATOM   11383 C CG  . PHE D 1 422 ? -15.459 78.146  71.228  1.00 56.10  ?  438 PHE A CG  1 
ATOM   11384 C CD1 . PHE D 1 422 ? -15.535 76.903  70.626  1.00 55.91  ?  438 PHE A CD1 1 
ATOM   11385 C CD2 . PHE D 1 422 ? -16.158 79.192  70.661  1.00 58.04  ?  438 PHE A CD2 1 
ATOM   11386 C CE1 . PHE D 1 422 ? -16.382 76.674  69.583  1.00 54.51  ?  438 PHE A CE1 1 
ATOM   11387 C CE2 . PHE D 1 422 ? -17.002 78.969  69.580  1.00 57.03  ?  438 PHE A CE2 1 
ATOM   11388 C CZ  . PHE D 1 422 ? -17.118 77.713  69.048  1.00 54.85  ?  438 PHE A CZ  1 
ATOM   11389 N N   . LEU D 1 423 ? -13.425 80.927  71.045  1.00 56.86  ?  439 LEU A N   1 
ATOM   11390 C CA  . LEU D 1 423 ? -13.555 81.984  70.051  1.00 54.61  ?  439 LEU A CA  1 
ATOM   11391 C C   . LEU D 1 423 ? -12.244 82.202  69.332  1.00 53.12  ?  439 LEU A C   1 
ATOM   11392 O O   . LEU D 1 423 ? -12.213 82.483  68.136  1.00 53.31  ?  439 LEU A O   1 
ATOM   11393 C CB  . LEU D 1 423 ? -14.031 83.270  70.722  1.00 57.48  ?  439 LEU A CB  1 
ATOM   11394 C CG  . LEU D 1 423 ? -15.544 83.276  70.954  1.00 62.40  ?  439 LEU A CG  1 
ATOM   11395 C CD1 . LEU D 1 423 ? -16.000 84.567  71.583  1.00 63.84  ?  439 LEU A CD1 1 
ATOM   11396 C CD2 . LEU D 1 423 ? -16.233 83.116  69.622  1.00 61.93  ?  439 LEU A CD2 1 
ATOM   11397 N N   . LEU D 1 424 ? -11.144 82.018  70.036  1.00 58.13  ?  440 LEU A N   1 
ATOM   11398 C CA  . LEU D 1 424 ? -9.840  82.201  69.425  1.00 57.68  ?  440 LEU A CA  1 
ATOM   11399 C C   . LEU D 1 424 ? -9.577  81.110  68.387  1.00 53.01  ?  440 LEU A C   1 
ATOM   11400 O O   . LEU D 1 424 ? -9.141  81.390  67.266  1.00 51.31  ?  440 LEU A O   1 
ATOM   11401 C CB  . LEU D 1 424 ? -8.766  82.207  70.521  1.00 54.34  ?  440 LEU A CB  1 
ATOM   11402 C CG  . LEU D 1 424 ? -7.378  82.620  70.042  1.00 48.13  ?  440 LEU A CG  1 
ATOM   11403 C CD1 . LEU D 1 424 ? -6.635  81.397  69.520  1.00 51.85  ?  440 LEU A CD1 1 
ATOM   11404 C CD2 . LEU D 1 424 ? -7.424  83.754  69.013  1.00 47.61  ?  440 LEU A CD2 1 
ATOM   11405 N N   . LYS D 1 425 ? -9.788  79.851  68.767  1.00 51.79  ?  441 LYS A N   1 
ATOM   11406 C CA  . LYS D 1 425 ? -9.649  78.754  67.815  1.00 49.00  ?  441 LYS A CA  1 
ATOM   11407 C C   . LYS D 1 425 ? -10.524 78.986  66.576  1.00 53.65  ?  441 LYS A C   1 
ATOM   11408 O O   . LYS D 1 425 ? -10.089 78.797  65.413  1.00 55.67  ?  441 LYS A O   1 
ATOM   11409 C CB  . LYS D 1 425 ? -10.007 77.444  68.518  1.00 49.33  ?  441 LYS A CB  1 
ATOM   11410 C CG  . LYS D 1 425 ? -9.725  76.245  67.689  1.00 53.68  ?  441 LYS A CG  1 
ATOM   11411 C CD  . LYS D 1 425 ? -9.824  74.959  68.454  1.00 59.43  ?  441 LYS A CD  1 
ATOM   11412 C CE  . LYS D 1 425 ? -9.027  73.906  67.692  1.00 63.35  ?  441 LYS A CE  1 
ATOM   11413 N NZ  . LYS D 1 425 ? -8.554  72.847  68.611  1.00 82.29  ?  441 LYS A NZ  1 
ATOM   11414 N N   . GLN D 1 426 ? -11.755 79.439  66.812  1.00 52.11  ?  442 GLN A N   1 
ATOM   11415 C CA  . GLN D 1 426 ? -12.636 79.799  65.712  1.00 48.61  ?  442 GLN A CA  1 
ATOM   11416 C C   . GLN D 1 426 ? -12.013 80.883  64.849  1.00 47.82  ?  442 GLN A C   1 
ATOM   11417 O O   . GLN D 1 426 ? -11.840 80.698  63.645  1.00 48.76  ?  442 GLN A O   1 
ATOM   11418 C CB  . GLN D 1 426 ? -13.993 80.233  66.259  1.00 49.95  ?  442 GLN A CB  1 
ATOM   11419 C CG  . GLN D 1 426 ? -14.781 79.057  66.787  1.00 50.04  ?  442 GLN A CG  1 
ATOM   11420 C CD  . GLN D 1 426 ? -15.340 78.188  65.659  1.00 54.30  ?  442 GLN A CD  1 
ATOM   11421 O OE1 . GLN D 1 426 ? -14.647 77.300  65.137  1.00 54.37  ?  442 GLN A OE1 1 
ATOM   11422 N NE2 . GLN D 1 426 ? -16.619 78.389  65.330  1.00 56.41  ?  442 GLN A NE2 1 
ATOM   11423 N N   . ALA D 1 427 ? -11.605 81.989  65.456  1.00 49.87  ?  443 ALA A N   1 
ATOM   11424 C CA  . ALA D 1 427 ? -11.095 83.110  64.680  1.00 52.24  ?  443 ALA A CA  1 
ATOM   11425 C C   . ALA D 1 427 ? -9.821  82.762  63.925  1.00 52.55  ?  443 ALA A C   1 
ATOM   11426 O O   . ALA D 1 427 ? -9.550  83.366  62.878  1.00 51.92  ?  443 ALA A O   1 
ATOM   11427 C CB  . ALA D 1 427 ? -10.847 84.294  65.594  1.00 52.05  ?  443 ALA A CB  1 
ATOM   11428 N N   . LEU D 1 428 ? -9.025  81.820  64.448  1.00 54.62  ?  444 LEU A N   1 
ATOM   11429 C CA  . LEU D 1 428 ? -7.815  81.378  63.758  1.00 56.21  ?  444 LEU A CA  1 
ATOM   11430 C C   . LEU D 1 428 ? -8.166  80.682  62.462  1.00 56.62  ?  444 LEU A C   1 
ATOM   11431 O O   . LEU D 1 428 ? -7.482  80.855  61.440  1.00 51.57  ?  444 LEU A O   1 
ATOM   11432 C CB  . LEU D 1 428 ? -7.017  80.441  64.653  1.00 55.92  ?  444 LEU A CB  1 
ATOM   11433 C CG  . LEU D 1 428 ? -6.240  81.059  65.811  1.00 56.20  ?  444 LEU A CG  1 
ATOM   11434 C CD1 . LEU D 1 428 ? -5.499  79.963  66.557  1.00 53.49  ?  444 LEU A CD1 1 
ATOM   11435 C CD2 . LEU D 1 428 ? -5.300  82.100  65.243  1.00 54.60  ?  444 LEU A CD2 1 
ATOM   11436 N N   . THR D 1 429 ? -9.242  79.888  62.493  1.00 57.39  ?  445 THR A N   1 
ATOM   11437 C CA  . THR D 1 429 ? -9.645  79.164  61.291  1.00 57.26  ?  445 THR A CA  1 
ATOM   11438 C C   . THR D 1 429 ? -10.458 80.030  60.326  1.00 53.54  ?  445 THR A C   1 
ATOM   11439 O O   . THR D 1 429 ? -10.263 79.972  59.101  1.00 55.54  ?  445 THR A O   1 
ATOM   11440 C CB  . THR D 1 429 ? -10.477 77.952  61.673  1.00 59.66  ?  445 THR A CB  1 
ATOM   11441 O OG1 . THR D 1 429 ? -9.715  77.071  62.507  1.00 60.36  ?  445 THR A OG1 1 
ATOM   11442 C CG2 . THR D 1 429 ? -10.794 77.221  60.409  1.00 58.60  ?  445 THR A CG2 1 
ATOM   11443 N N   . ILE D 1 430 ? -11.346 80.854  60.871  1.00 54.32  ?  446 ILE A N   1 
ATOM   11444 C CA  . ILE D 1 430 ? -12.419 81.494  60.126  1.00 53.58  ?  446 ILE A CA  1 
ATOM   11445 C C   . ILE D 1 430 ? -12.052 82.915  59.719  1.00 56.27  ?  446 ILE A C   1 
ATOM   11446 O O   . ILE D 1 430 ? -12.318 83.328  58.588  1.00 56.44  ?  446 ILE A O   1 
ATOM   11447 C CB  . ILE D 1 430 ? -13.698 81.474  60.989  1.00 49.24  ?  446 ILE A CB  1 
ATOM   11448 C CG1 . ILE D 1 430 ? -14.164 80.036  61.186  1.00 48.51  ?  446 ILE A CG1 1 
ATOM   11449 C CG2 . ILE D 1 430 ? -14.771 82.338  60.372  1.00 52.86  ?  446 ILE A CG2 1 
ATOM   11450 C CD1 . ILE D 1 430 ? -15.068 79.815  62.359  1.00 47.58  ?  446 ILE A CD1 1 
ATOM   11451 N N   . VAL D 1 431 ? -11.474 83.676  60.653  1.00 59.82  ?  447 VAL A N   1 
ATOM   11452 C CA  . VAL D 1 431 ? -11.029 85.031  60.355  1.00 56.99  ?  447 VAL A CA  1 
ATOM   11453 C C   . VAL D 1 431 ? -9.722  85.003  59.599  1.00 53.25  ?  447 VAL A C   1 
ATOM   11454 O O   . VAL D 1 431 ? -9.554  85.714  58.605  1.00 52.21  ?  447 VAL A O   1 
ATOM   11455 C CB  . VAL D 1 431 ? -10.914 85.873  61.636  1.00 46.45  ?  447 VAL A CB  1 
ATOM   11456 C CG1 . VAL D 1 431 ? -10.404 87.211  61.291  1.00 43.76  ?  447 VAL A CG1 1 
ATOM   11457 C CG2 . VAL D 1 431 ? -12.283 86.059  62.229  1.00 49.22  ?  447 VAL A CG2 1 
ATOM   11458 N N   . GLY D 1 432 ? -8.787  84.176  60.046  1.00 51.58  ?  448 GLY A N   1 
ATOM   11459 C CA  . GLY D 1 432 ? -7.504  84.066  59.374  1.00 53.28  ?  448 GLY A CA  1 
ATOM   11460 C C   . GLY D 1 432 ? -7.617  83.888  57.868  1.00 57.04  ?  448 GLY A C   1 
ATOM   11461 O O   . GLY D 1 432 ? -7.033  84.649  57.086  1.00 56.51  ?  448 GLY A O   1 
ATOM   11462 N N   . THR D 1 433 ? -8.402  82.893  57.458  1.00 56.54  ?  449 THR A N   1 
ATOM   11463 C CA  . THR D 1 433 ? -8.566  82.593  56.041  1.00 54.30  ?  449 THR A CA  1 
ATOM   11464 C C   . THR D 1 433 ? -9.076  83.769  55.217  1.00 56.04  ?  449 THR A C   1 
ATOM   11465 O O   . THR D 1 433 ? -8.798  83.836  54.017  1.00 55.93  ?  449 THR A O   1 
ATOM   11466 C CB  . THR D 1 433 ? -9.509  81.403  55.902  1.00 52.54  ?  449 THR A CB  1 
ATOM   11467 O OG1 . THR D 1 433 ? -9.313  80.793  54.623  1.00 57.37  ?  449 THR A OG1 1 
ATOM   11468 C CG2 . THR D 1 433 ? -10.947 81.792  56.116  1.00 50.28  ?  449 THR A CG2 1 
ATOM   11469 N N   . LEU D 1 434 ? -9.854  84.680  55.815  1.00 57.72  ?  450 LEU A N   1 
ATOM   11470 C CA  . LEU D 1 434 ? -10.573 85.683  55.027  1.00 57.47  ?  450 LEU A CA  1 
ATOM   11471 C C   . LEU D 1 434 ? -9.628  86.607  54.261  1.00 56.71  ?  450 LEU A C   1 
ATOM   11472 O O   . LEU D 1 434 ? -9.802  86.752  53.033  1.00 57.72  ?  450 LEU A O   1 
ATOM   11473 C CB  . LEU D 1 434 ? -11.526 86.445  55.953  1.00 55.21  ?  450 LEU A CB  1 
ATOM   11474 C CG  . LEU D 1 434 ? -12.697 85.613  56.460  1.00 52.04  ?  450 LEU A CG  1 
ATOM   11475 C CD1 . LEU D 1 434 ? -13.606 86.460  57.283  1.00 51.46  ?  450 LEU A CD1 1 
ATOM   11476 C CD2 . LEU D 1 434 ? -13.432 85.036  55.288  1.00 49.47  ?  450 LEU A CD2 1 
ATOM   11477 N N   . PRO D 1 435 ? -8.636  87.282  54.904  1.00 58.82  ?  451 PRO A N   1 
ATOM   11478 C CA  . PRO D 1 435 ? -7.697  88.089  54.112  1.00 58.95  ?  451 PRO A CA  1 
ATOM   11479 C C   . PRO D 1 435 ? -6.872  87.256  53.149  1.00 57.88  ?  451 PRO A C   1 
ATOM   11480 O O   . PRO D 1 435 ? -6.602  87.713  52.032  1.00 61.07  ?  451 PRO A O   1 
ATOM   11481 C CB  . PRO D 1 435 ? -6.830  88.779  55.184  1.00 59.76  ?  451 PRO A CB  1 
ATOM   11482 C CG  . PRO D 1 435 ? -7.594  88.739  56.415  1.00 57.35  ?  451 PRO A CG  1 
ATOM   11483 C CD  . PRO D 1 435 ? -8.308  87.414  56.340  1.00 59.82  ?  451 PRO A CD  1 
ATOM   11484 N N   . PHE D 1 436 ? -6.480  86.039  53.535  1.00 51.63  ?  452 PHE A N   1 
ATOM   11485 C CA  . PHE D 1 436 ? -5.739  85.194  52.606  1.00 52.22  ?  452 PHE A CA  1 
ATOM   11486 C C   . PHE D 1 436 ? -6.510  85.012  51.324  1.00 61.16  ?  452 PHE A C   1 
ATOM   11487 O O   . PHE D 1 436 ? -5.980  85.215  50.219  1.00 64.80  ?  452 PHE A O   1 
ATOM   11488 C CB  . PHE D 1 436 ? -5.420  83.846  53.253  1.00 49.92  ?  452 PHE A CB  1 
ATOM   11489 C CG  . PHE D 1 436 ? -4.755  82.869  52.335  1.00 51.09  ?  452 PHE A CG  1 
ATOM   11490 C CD1 . PHE D 1 436 ? -5.494  82.020  51.555  1.00 58.65  ?  452 PHE A CD1 1 
ATOM   11491 C CD2 . PHE D 1 436 ? -3.407  82.919  52.128  1.00 55.19  ?  452 PHE A CD2 1 
ATOM   11492 C CE1 . PHE D 1 436 ? -4.889  81.134  50.682  1.00 57.56  ?  452 PHE A CE1 1 
ATOM   11493 C CE2 . PHE D 1 436 ? -2.792  82.051  51.251  1.00 55.53  ?  452 PHE A CE2 1 
ATOM   11494 C CZ  . PHE D 1 436 ? -3.539  81.155  50.527  1.00 55.98  ?  452 PHE A CZ  1 
ATOM   11495 N N   . THR D 1 437 ? -7.787  84.670  51.473  1.00 63.05  ?  453 THR A N   1 
ATOM   11496 C CA  . THR D 1 437 ? -8.645  84.317  50.354  1.00 55.87  ?  453 THR A CA  1 
ATOM   11497 C C   . THR D 1 437 ? -8.897  85.527  49.493  1.00 59.22  ?  453 THR A C   1 
ATOM   11498 O O   . THR D 1 437 ? -8.701  85.493  48.266  1.00 63.72  ?  453 THR A O   1 
ATOM   11499 C CB  . THR D 1 437 ? -9.961  83.800  50.896  1.00 55.26  ?  453 THR A CB  1 
ATOM   11500 O OG1 . THR D 1 437 ? -9.739  82.569  51.578  1.00 54.51  ?  453 THR A OG1 1 
ATOM   11501 C CG2 . THR D 1 437 ? -10.916 83.574  49.759  1.00 59.76  ?  453 THR A CG2 1 
ATOM   11502 N N   . TYR D 1 438 ? -9.402  86.595  50.124  1.00 57.92  ?  454 TYR A N   1 
ATOM   11503 C CA  . TYR D 1 438 ? -9.636  87.826  49.384  1.00 60.40  ?  454 TYR A CA  1 
ATOM   11504 C C   . TYR D 1 438 ? -8.414  88.220  48.577  1.00 60.87  ?  454 TYR A C   1 
ATOM   11505 O O   . TYR D 1 438 ? -8.537  88.588  47.395  1.00 62.67  ?  454 TYR A O   1 
ATOM   11506 C CB  . TYR D 1 438 ? -10.080 88.963  50.311  1.00 61.21  ?  454 TYR A CB  1 
ATOM   11507 C CG  . TYR D 1 438 ? -9.848  90.298  49.641  1.00 65.51  ?  454 TYR A CG  1 
ATOM   11508 C CD1 . TYR D 1 438 ? -10.420 90.581  48.393  1.00 66.56  ?  454 TYR A CD1 1 
ATOM   11509 C CD2 . TYR D 1 438 ? -9.090  91.290  50.261  1.00 69.27  ?  454 TYR A CD2 1 
ATOM   11510 C CE1 . TYR D 1 438 ? -10.184 91.785  47.744  1.00 69.74  ?  454 TYR A CE1 1 
ATOM   11511 C CE2 . TYR D 1 438 ? -8.864  92.512  49.632  1.00 72.20  ?  454 TYR A CE2 1 
ATOM   11512 C CZ  . TYR D 1 438 ? -9.417  92.752  48.363  1.00 72.37  ?  454 TYR A CZ  1 
ATOM   11513 O OH  . TYR D 1 438 ? -9.212  93.956  47.723  1.00 72.45  ?  454 TYR A OH  1 
ATOM   11514 N N   . MET D 1 439 ? -7.218  88.079  49.166  1.00 58.93  ?  455 MET A N   1 
ATOM   11515 C CA  . MET D 1 439 ? -6.006  88.501  48.468  1.00 61.87  ?  455 MET A CA  1 
ATOM   11516 C C   . MET D 1 439 ? -5.729  87.596  47.255  1.00 62.18  ?  455 MET A C   1 
ATOM   11517 O O   . MET D 1 439 ? -5.467  88.087  46.144  1.00 60.80  ?  455 MET A O   1 
ATOM   11518 C CB  . MET D 1 439 ? -4.829  88.476  49.456  1.00 58.05  ?  455 MET A CB  1 
ATOM   11519 C CG  . MET D 1 439 ? -3.442  88.963  48.997  1.00 58.04  ?  455 MET A CG  1 
ATOM   11520 S SD  . MET D 1 439 ? -2.547  87.843  47.874  1.00 64.77  ?  455 MET A SD  1 
ATOM   11521 C CE  . MET D 1 439 ? -1.998  86.684  49.085  1.00 64.63  ?  455 MET A CE  1 
ATOM   11522 N N   . LEU D 1 440 ? -5.741  86.269  47.454  1.00 58.03  ?  456 LEU A N   1 
ATOM   11523 C CA  . LEU D 1 440 ? -5.421  85.384  46.342  1.00 59.65  ?  456 LEU A CA  1 
ATOM   11524 C C   . LEU D 1 440 ? -6.352  85.656  45.185  1.00 64.40  ?  456 LEU A C   1 
ATOM   11525 O O   . LEU D 1 440 ? -5.903  85.830  44.044  1.00 67.72  ?  456 LEU A O   1 
ATOM   11526 C CB  . LEU D 1 440 ? -5.506  83.924  46.770  1.00 57.51  ?  456 LEU A CB  1 
ATOM   11527 C CG  . LEU D 1 440 ? -5.108  82.859  45.750  1.00 56.57  ?  456 LEU A CG  1 
ATOM   11528 C CD1 . LEU D 1 440 ? -4.584  81.677  46.495  1.00 56.54  ?  456 LEU A CD1 1 
ATOM   11529 C CD2 . LEU D 1 440 ? -6.325  82.438  44.958  1.00 55.31  ?  456 LEU A CD2 1 
ATOM   11530 N N   . GLU D 1 441 ? -7.660  85.688  45.461  1.00 65.65  ?  457 GLU A N   1 
ATOM   11531 C CA  . GLU D 1 441 ? -8.608  85.931  44.385  1.00 64.33  ?  457 GLU A CA  1 
ATOM   11532 C C   . GLU D 1 441 ? -8.361  87.276  43.723  1.00 63.85  ?  457 GLU A C   1 
ATOM   11533 O O   . GLU D 1 441 ? -8.510  87.408  42.502  1.00 64.11  ?  457 GLU A O   1 
ATOM   11534 C CB  . GLU D 1 441 ? -10.034 85.833  44.903  1.00 65.22  ?  457 GLU A CB  1 
ATOM   11535 C CG  . GLU D 1 441 ? -11.019 85.650  43.758  1.00 63.51  ?  457 GLU A CG  1 
ATOM   11536 C CD  . GLU D 1 441 ? -11.067 84.252  43.202  1.00 63.03  ?  457 GLU A CD  1 
ATOM   11537 O OE1 . GLU D 1 441 ? -10.009 83.701  42.823  1.00 61.41  ?  457 GLU A OE1 1 
ATOM   11538 O OE2 . GLU D 1 441 ? -12.188 83.736  43.061  1.00 69.38  -1 457 GLU A OE2 1 
ATOM   11539 N N   . LYS D 1 442 ? -7.958  88.283  44.506  1.00 66.18  ?  458 LYS A N   1 
ATOM   11540 C CA  . LYS D 1 442 ? -7.714  89.607  43.937  1.00 69.90  ?  458 LYS A CA  1 
ATOM   11541 C C   . LYS D 1 442 ? -6.566  89.561  42.949  1.00 68.62  ?  458 LYS A C   1 
ATOM   11542 O O   . LYS D 1 442 ? -6.629  90.136  41.849  1.00 68.68  ?  458 LYS A O   1 
ATOM   11543 C CB  . LYS D 1 442 ? -7.392  90.598  45.049  1.00 71.72  ?  458 LYS A CB  1 
ATOM   11544 C CG  . LYS D 1 442 ? -7.706  92.007  44.636  1.00 81.06  ?  458 LYS A CG  1 
ATOM   11545 C CD  . LYS D 1 442 ? -7.119  93.069  45.527  1.00 81.91  ?  458 LYS A CD  1 
ATOM   11546 C CE  . LYS D 1 442 ? -7.692  94.405  45.069  1.00 91.70  ?  458 LYS A CE  1 
ATOM   11547 N NZ  . LYS D 1 442 ? -8.061  94.351  43.607  1.00 88.88  ?  458 LYS A NZ  1 
ATOM   11548 N N   . TRP D 1 443 ? -5.492  88.891  43.350  1.00 70.23  ?  459 TRP A N   1 
ATOM   11549 C CA  . TRP D 1 443 ? -4.348  88.739  42.474  1.00 70.65  ?  459 TRP A CA  1 
ATOM   11550 C C   . TRP D 1 443 ? -4.765  88.079  41.160  1.00 69.62  ?  459 TRP A C   1 
ATOM   11551 O O   . TRP D 1 443 ? -4.386  88.544  40.077  1.00 70.22  ?  459 TRP A O   1 
ATOM   11552 C CB  . TRP D 1 443 ? -3.272  87.949  43.209  1.00 67.37  ?  459 TRP A CB  1 
ATOM   11553 C CG  . TRP D 1 443 ? -2.071  87.745  42.405  1.00 68.91  ?  459 TRP A CG  1 
ATOM   11554 C CD1 . TRP D 1 443 ? -0.957  88.538  42.356  1.00 69.81  ?  459 TRP A CD1 1 
ATOM   11555 C CD2 . TRP D 1 443 ? -1.852  86.683  41.489  1.00 70.33  ?  459 TRP A CD2 1 
ATOM   11556 N NE1 . TRP D 1 443 ? -0.048  88.020  41.464  1.00 68.01  ?  459 TRP A NE1 1 
ATOM   11557 C CE2 . TRP D 1 443 ? -0.575  86.879  40.919  1.00 70.14  ?  459 TRP A CE2 1 
ATOM   11558 C CE3 . TRP D 1 443 ? -2.618  85.582  41.086  1.00 69.42  ?  459 TRP A CE3 1 
ATOM   11559 C CZ2 . TRP D 1 443 ? -0.045  86.014  39.979  1.00 73.08  ?  459 TRP A CZ2 1 
ATOM   11560 C CZ3 . TRP D 1 443 ? -2.094  84.725  40.151  1.00 68.94  ?  459 TRP A CZ3 1 
ATOM   11561 C CH2 . TRP D 1 443 ? -0.814  84.943  39.606  1.00 71.62  ?  459 TRP A CH2 1 
ATOM   11562 N N   . ARG D 1 444 ? -5.589  87.021  41.235  1.00 66.11  ?  460 ARG A N   1 
ATOM   11563 C CA  . ARG D 1 444 ? -6.064  86.358  40.015  1.00 63.45  ?  460 ARG A CA  1 
ATOM   11564 C C   . ARG D 1 444 ? -6.959  87.257  39.163  1.00 67.60  ?  460 ARG A C   1 
ATOM   11565 O O   . ARG D 1 444 ? -6.849  87.259  37.933  1.00 69.77  ?  460 ARG A O   1 
ATOM   11566 C CB  . ARG D 1 444 ? -6.842  85.111  40.356  1.00 59.39  ?  460 ARG A CB  1 
ATOM   11567 C CG  . ARG D 1 444 ? -6.048  83.903  40.660  1.00 61.02  ?  460 ARG A CG  1 
ATOM   11568 C CD  . ARG D 1 444 ? -7.031  83.085  41.434  1.00 64.36  ?  460 ARG A CD  1 
ATOM   11569 N NE  . ARG D 1 444 ? -7.029  81.665  41.132  1.00 66.85  ?  460 ARG A NE  1 
ATOM   11570 C CZ  . ARG D 1 444 ? -7.957  80.828  41.572  1.00 61.60  ?  460 ARG A CZ  1 
ATOM   11571 N NH1 . ARG D 1 444 ? -9.001  81.258  42.265  1.00 62.09  ?  460 ARG A NH1 1 
ATOM   11572 N NH2 . ARG D 1 444 ? -7.855  79.535  41.275  1.00 61.27  ?  460 ARG A NH2 1 
ATOM   11573 N N   . TRP D 1 445 ? -7.888  87.990  39.782  1.00 67.94  ?  461 TRP A N   1 
ATOM   11574 C CA  . TRP D 1 445 ? -8.775  88.833  38.990  1.00 67.83  ?  461 TRP A CA  1 
ATOM   11575 C C   . TRP D 1 445 ? -7.979  89.889  38.237  1.00 74.05  ?  461 TRP A C   1 
ATOM   11576 O O   . TRP D 1 445 ? -8.339  90.251  37.111  1.00 77.60  ?  461 TRP A O   1 
ATOM   11577 C CB  . TRP D 1 445 ? -9.796  89.530  39.871  1.00 65.63  ?  461 TRP A CB  1 
ATOM   11578 C CG  . TRP D 1 445 ? -10.829 88.673  40.390  1.00 61.77  ?  461 TRP A CG  1 
ATOM   11579 C CD1 . TRP D 1 445 ? -11.179 87.448  39.940  1.00 63.60  ?  461 TRP A CD1 1 
ATOM   11580 C CD2 . TRP D 1 445 ? -11.663 88.953  41.515  1.00 60.97  ?  461 TRP A CD2 1 
ATOM   11581 N NE1 . TRP D 1 445 ? -12.193 86.927  40.721  1.00 62.74  ?  461 TRP A NE1 1 
ATOM   11582 C CE2 . TRP D 1 445 ? -12.504 87.839  41.698  1.00 60.91  ?  461 TRP A CE2 1 
ATOM   11583 C CE3 . TRP D 1 445 ? -11.776 90.037  42.391  1.00 60.27  ?  461 TRP A CE3 1 
ATOM   11584 C CZ2 . TRP D 1 445 ? -13.446 87.777  42.724  1.00 60.62  ?  461 TRP A CZ2 1 
ATOM   11585 C CZ3 . TRP D 1 445 ? -12.718 89.976  43.405  1.00 61.68  ?  461 TRP A CZ3 1 
ATOM   11586 C CH2 . TRP D 1 445 ? -13.540 88.854  43.562  1.00 59.82  ?  461 TRP A CH2 1 
ATOM   11587 N N   . MET D 1 446 ? -6.907  90.424  38.857  1.00 73.28  ?  462 MET A N   1 
ATOM   11588 C CA  . MET D 1 446 ? -6.041  91.360  38.132  1.00 77.46  ?  462 MET A CA  1 
ATOM   11589 C C   . MET D 1 446 ? -5.241  90.682  37.025  1.00 81.00  ?  462 MET A C   1 
ATOM   11590 O O   . MET D 1 446 ? -5.201  91.182  35.894  1.00 81.73  ?  462 MET A O   1 
ATOM   11591 C CB  . MET D 1 446 ? -5.082  92.108  39.054  1.00 78.34  ?  462 MET A CB  1 
ATOM   11592 C CG  . MET D 1 446 ? -5.737  93.103  39.966  1.00 84.67  ?  462 MET A CG  1 
ATOM   11593 S SD  . MET D 1 446 ? -4.457  93.953  40.894  1.00 88.08  ?  462 MET A SD  1 
ATOM   11594 C CE  . MET D 1 446 ? -4.665  93.147  42.461  1.00 88.65  ?  462 MET A CE  1 
ATOM   11595 N N   . VAL D 1 447 ? -4.534  89.589  37.341  1.00 81.07  ?  463 VAL A N   1 
ATOM   11596 C CA  . VAL D 1 447 ? -3.792  88.877  36.299  1.00 81.43  ?  463 VAL A CA  1 
ATOM   11597 C C   . VAL D 1 447 ? -4.692  88.647  35.096  1.00 81.36  ?  463 VAL A C   1 
ATOM   11598 O O   . VAL D 1 447 ? -4.311  88.908  33.948  1.00 86.84  ?  463 VAL A O   1 
ATOM   11599 C CB  . VAL D 1 447 ? -3.208  87.558  36.849  1.00 73.40  ?  463 VAL A CB  1 
ATOM   11600 C CG1 . VAL D 1 447 ? -2.714  86.638  35.716  1.00 77.15  ?  463 VAL A CG1 1 
ATOM   11601 C CG2 . VAL D 1 447 ? -2.078  87.870  37.824  1.00 72.46  ?  463 VAL A CG2 1 
ATOM   11602 N N   . PHE D 1 448 ? -5.931  88.235  35.350  1.00 80.19  ?  464 PHE A N   1 
ATOM   11603 C CA  . PHE D 1 448 ? -6.850  87.970  34.256  1.00 83.51  ?  464 PHE A CA  1 
ATOM   11604 C C   . PHE D 1 448 ? -7.281  89.254  33.542  1.00 87.98  ?  464 PHE A C   1 
ATOM   11605 O O   . PHE D 1 448 ? -7.402  89.266  32.310  1.00 91.71  ?  464 PHE A O   1 
ATOM   11606 C CB  . PHE D 1 448 ? -8.060  87.199  34.781  1.00 80.18  ?  464 PHE A CB  1 
ATOM   11607 C CG  . PHE D 1 448 ? -7.722  85.838  35.283  1.00 71.07  ?  464 PHE A CG  1 
ATOM   11608 C CD1 . PHE D 1 448 ? -6.765  85.074  34.619  1.00 72.00  ?  464 PHE A CD1 1 
ATOM   11609 C CD2 . PHE D 1 448 ? -8.399  85.286  36.357  1.00 66.99  ?  464 PHE A CD2 1 
ATOM   11610 C CE1 . PHE D 1 448 ? -6.454  83.803  35.044  1.00 67.56  ?  464 PHE A CE1 1 
ATOM   11611 C CE2 . PHE D 1 448 ? -8.093  84.007  36.800  1.00 67.62  ?  464 PHE A CE2 1 
ATOM   11612 C CZ  . PHE D 1 448 ? -7.116  83.261  36.140  1.00 66.00  ?  464 PHE A CZ  1 
ATOM   11613 N N   . LYS D 1 449 ? -7.553  90.335  34.291  1.00 89.04  ?  465 LYS A N   1 
ATOM   11614 C CA  . LYS D 1 449 ? -7.889  91.623  33.678  1.00 85.36  ?  465 LYS A CA  1 
ATOM   11615 C C   . LYS D 1 449 ? -6.678  92.260  33.018  1.00 87.48  ?  465 LYS A C   1 
ATOM   11616 O O   . LYS D 1 449 ? -6.845  93.217  32.262  1.00 91.21  ?  465 LYS A O   1 
ATOM   11617 C CB  . LYS D 1 449 ? -8.477  92.591  34.724  1.00 83.35  ?  465 LYS A CB  1 
ATOM   11618 C CG  . LYS D 1 449 ? -9.310  93.769  34.182  1.00 86.44  ?  465 LYS A CG  1 
ATOM   11619 C CD  . LYS D 1 449 ? -10.194 94.396  35.281  1.00 92.38  ?  465 LYS A CD  1 
ATOM   11620 C CE  . LYS D 1 449 ? -11.162 93.377  35.922  1.00 93.04  ?  465 LYS A CE  1 
ATOM   11621 N NZ  . LYS D 1 449 ? -12.228 94.045  36.751  1.00 80.71  ?  465 LYS A NZ  1 
ATOM   11622 N N   . GLY D 1 450 ? -5.474  91.757  33.291  1.00 92.40  ?  466 GLY A N   1 
ATOM   11623 C CA  . GLY D 1 450 ? -4.266  92.277  32.681  1.00 92.18  ?  466 GLY A CA  1 
ATOM   11624 C C   . GLY D 1 450 ? -3.555  93.370  33.440  1.00 86.06  ?  466 GLY A C   1 
ATOM   11625 O O   . GLY D 1 450 ? -2.748  94.089  32.845  1.00 86.15  ?  466 GLY A O   1 
ATOM   11626 N N   . GLU D 1 451 ? -3.823  93.526  34.732  1.00 83.40  ?  467 GLU A N   1 
ATOM   11627 C CA  . GLU D 1 451 ? -3.220  94.596  35.507  1.00 83.96  ?  467 GLU A CA  1 
ATOM   11628 C C   . GLU D 1 451 ? -1.916  94.178  36.172  1.00 80.94  ?  467 GLU A C   1 
ATOM   11629 O O   . GLU D 1 451 ? -1.406  94.886  37.043  1.00 78.41  ?  467 GLU A O   1 
ATOM   11630 C CB  . GLU D 1 451 ? -4.218  95.122  36.535  1.00 85.22  ?  467 GLU A CB  1 
ATOM   11631 C CG  . GLU D 1 451 ? -5.412  95.773  35.853  1.00 87.65  ?  467 GLU A CG  1 
ATOM   11632 C CD  . GLU D 1 451 ? -6.546  96.111  36.798  1.00 88.76  ?  467 GLU A CD  1 
ATOM   11633 O OE1 . GLU D 1 451 ? -6.390  95.879  38.020  1.00 90.40  ?  467 GLU A OE1 1 
ATOM   11634 O OE2 . GLU D 1 451 ? -7.592  96.605  36.310  1.00 86.07  -1 467 GLU A OE2 1 
ATOM   11635 N N   . ILE D 1 452 ? -1.362  93.047  35.769  1.00 81.85  ?  468 ILE A N   1 
ATOM   11636 C CA  . ILE D 1 452 ? -0.076  92.596  36.271  1.00 81.82  ?  468 ILE A CA  1 
ATOM   11637 C C   . ILE D 1 452 ? 0.658   91.962  35.093  1.00 83.26  ?  468 ILE A C   1 
ATOM   11638 O O   . ILE D 1 452 ? 0.247   90.903  34.592  1.00 84.42  ?  468 ILE A O   1 
ATOM   11639 C CB  . ILE D 1 452 ? -0.257  91.640  37.466  1.00 85.16  ?  468 ILE A CB  1 
ATOM   11640 C CG1 . ILE D 1 452 ? -1.101  92.313  38.557  1.00 83.27  ?  468 ILE A CG1 1 
ATOM   11641 C CG2 . ILE D 1 452 ? 1.081   91.221  38.056  1.00 86.16  ?  468 ILE A CG2 1 
ATOM   11642 C CD1 . ILE D 1 452 ? -1.389  91.464  39.745  1.00 81.03  ?  468 ILE A CD1 1 
ATOM   11643 N N   . PRO D 1 453 ? 1.707   92.600  34.582  1.00 85.58  ?  469 PRO A N   1 
ATOM   11644 C CA  . PRO D 1 453 ? 2.504   91.971  33.527  1.00 88.68  ?  469 PRO A CA  1 
ATOM   11645 C C   . PRO D 1 453 ? 3.232   90.751  34.059  1.00 94.15  ?  469 PRO A C   1 
ATOM   11646 O O   . PRO D 1 453 ? 3.543   90.655  35.248  1.00 93.64  ?  469 PRO A O   1 
ATOM   11647 C CB  . PRO D 1 453 ? 3.489   93.069  33.110  1.00 90.18  ?  469 PRO A CB  1 
ATOM   11648 C CG  . PRO D 1 453 ? 2.933   94.338  33.647  1.00 91.19  ?  469 PRO A CG  1 
ATOM   11649 C CD  . PRO D 1 453 ? 2.108   93.990  34.843  1.00 88.48  ?  469 PRO A CD  1 
ATOM   11650 N N   . LYS D 1 454 ? 3.501   89.813  33.144  1.00 97.43  ?  470 LYS A N   1 
ATOM   11651 C CA  . LYS D 1 454 ? 4.087   88.518  33.495  1.00 98.98  ?  470 LYS A CA  1 
ATOM   11652 C C   . LYS D 1 454 ? 5.308   88.681  34.405  1.00 97.16  ?  470 LYS A C   1 
ATOM   11653 O O   . LYS D 1 454 ? 5.400   88.052  35.468  1.00 95.90  ?  470 LYS A O   1 
ATOM   11654 C CB  . LYS D 1 454 ? 4.447   87.775  32.201  1.00 100.05 ?  470 LYS A CB  1 
ATOM   11655 C CG  . LYS D 1 454 ? 3.354   86.852  31.663  1.00 96.91  ?  470 LYS A CG  1 
ATOM   11656 C CD  . LYS D 1 454 ? 3.569   86.465  30.191  1.00 99.19  ?  470 LYS A CD  1 
ATOM   11657 C CE  . LYS D 1 454 ? 4.943   85.877  29.934  1.00 98.21  ?  470 LYS A CE  1 
ATOM   11658 N NZ  . LYS D 1 454 ? 5.054   85.263  28.590  1.00 96.83  ?  470 LYS A NZ  1 
ATOM   11659 N N   . ASP D 1 455 ? 6.224   89.576  34.027  1.00 95.01  ?  471 ASP A N   1 
ATOM   11660 C CA  . ASP D 1 455 ? 7.466   89.806  34.764  1.00 100.37 ?  471 ASP A CA  1 
ATOM   11661 C C   . ASP D 1 455 ? 7.288   90.349  36.187  1.00 100.06 ?  471 ASP A C   1 
ATOM   11662 O O   . ASP D 1 455 ? 8.275   90.441  36.929  1.00 100.84 ?  471 ASP A O   1 
ATOM   11663 C CB  . ASP D 1 455 ? 8.350   90.760  33.952  1.00 107.91 ?  471 ASP A CB  1 
ATOM   11664 C CG  . ASP D 1 455 ? 7.759   92.155  33.847  1.00 103.36 ?  471 ASP A CG  1 
ATOM   11665 O OD1 . ASP D 1 455 ? 6.614   92.354  34.304  1.00 101.01 ?  471 ASP A OD1 1 
ATOM   11666 O OD2 . ASP D 1 455 ? 8.463   93.064  33.360  1.00 100.94 -1 471 ASP A OD2 1 
ATOM   11667 N N   . GLN D 1 456 ? 6.084   90.757  36.574  1.00 93.21  ?  472 GLN A N   1 
ATOM   11668 C CA  . GLN D 1 456 ? 5.831   91.328  37.926  1.00 90.35  ?  472 GLN A CA  1 
ATOM   11669 C C   . GLN D 1 456 ? 4.843   90.419  38.653  1.00 87.87  ?  472 GLN A C   1 
ATOM   11670 O O   . GLN D 1 456 ? 4.279   90.836  39.680  1.00 85.86  ?  472 GLN A O   1 
ATOM   11671 C CB  . GLN D 1 456 ? 5.283   92.750  37.811  1.00 90.54  ?  472 GLN A CB  1 
ATOM   11672 C CG  . GLN D 1 456 ? 6.315   93.754  37.323  1.00 96.17  ?  472 GLN A CG  1 
ATOM   11673 C CD  . GLN D 1 456 ? 5.844   95.171  37.532  1.00 96.75  ?  472 GLN A CD  1 
ATOM   11674 O OE1 . GLN D 1 456 ? 6.327   95.883  38.409  1.00 95.39  ?  472 GLN A OE1 1 
ATOM   11675 N NE2 . GLN D 1 456 ? 4.898   95.597  36.712  1.00 92.83  ?  472 GLN A NE2 1 
ATOM   11676 N N   . TRP D 1 457 ? 4.611   89.240  38.094  1.00 86.88  ?  473 TRP A N   1 
ATOM   11677 C CA  . TRP D 1 457 ? 3.617   88.307  38.664  1.00 84.49  ?  473 TRP A CA  1 
ATOM   11678 C C   . TRP D 1 457 ? 3.957   88.020  40.128  1.00 82.79  ?  473 TRP A C   1 
ATOM   11679 O O   . TRP D 1 457 ? 3.151   88.386  41.000  1.00 80.30  ?  473 TRP A O   1 
ATOM   11680 C CB  . TRP D 1 457 ? 3.612   87.046  37.794  1.00 84.08  ?  473 TRP A CB  1 
ATOM   11681 C CG  . TRP D 1 457 ? 2.507   86.996  36.784  1.00 84.98  ?  473 TRP A CG  1 
ATOM   11682 C CD1 . TRP D 1 457 ? 1.741   88.030  36.329  1.00 84.85  ?  473 TRP A CD1 1 
ATOM   11683 C CD2 . TRP D 1 457 ? 2.050   85.828  36.080  1.00 81.71  ?  473 TRP A CD2 1 
ATOM   11684 N NE1 . TRP D 1 457 ? 0.838   87.583  35.404  1.00 84.62  ?  473 TRP A NE1 1 
ATOM   11685 C CE2 . TRP D 1 457 ? 1.005   86.235  35.229  1.00 83.83  ?  473 TRP A CE2 1 
ATOM   11686 C CE3 . TRP D 1 457 ? 2.420   84.478  36.088  1.00 81.29  ?  473 TRP A CE3 1 
ATOM   11687 C CZ2 . TRP D 1 457 ? 0.329   85.345  34.401  1.00 85.52  ?  473 TRP A CZ2 1 
ATOM   11688 C CZ3 . TRP D 1 457 ? 1.750   83.596  35.266  1.00 82.35  ?  473 TRP A CZ3 1 
ATOM   11689 C CH2 . TRP D 1 457 ? 0.718   84.029  34.436  1.00 85.31  ?  473 TRP A CH2 1 
ATOM   11690 N N   . MET D 1 458 ? 5.092   87.363  40.383  1.00 85.27  ?  474 MET A N   1 
ATOM   11691 C CA  . MET D 1 458 ? 5.469   87.016  41.776  1.00 81.36  ?  474 MET A CA  1 
ATOM   11692 C C   . MET D 1 458 ? 5.717   88.328  42.518  1.00 81.06  ?  474 MET A C   1 
ATOM   11693 O O   . MET D 1 458 ? 5.318   88.454  43.682  1.00 80.38  ?  474 MET A O   1 
ATOM   11694 C CB  . MET D 1 458 ? 6.712   86.122  41.814  1.00 73.29  ?  474 MET A CB  1 
ATOM   11695 C CG  . MET D 1 458 ? 6.553   84.856  41.010  1.00 79.07  ?  474 MET A CG  1 
ATOM   11696 S SD  . MET D 1 458 ? 5.036   84.029  41.516  1.00 74.07  ?  474 MET A SD  1 
ATOM   11697 C CE  . MET D 1 458 ? 5.243   84.066  43.295  1.00 74.99  ?  474 MET A CE  1 
ATOM   11698 N N   . LYS D 1 459 ? 6.343   89.284  41.841  1.00 85.47  ?  475 LYS A N   1 
ATOM   11699 C CA  . LYS D 1 459 ? 6.621   90.549  42.510  1.00 85.86  ?  475 LYS A CA  1 
ATOM   11700 C C   . LYS D 1 459 ? 5.357   91.196  43.050  1.00 81.83  ?  475 LYS A C   1 
ATOM   11701 O O   . LYS D 1 459 ? 5.370   91.752  44.150  1.00 79.02  ?  475 LYS A O   1 
ATOM   11702 C CB  . LYS D 1 459 ? 7.330   91.508  41.564  1.00 88.16  ?  475 LYS A CB  1 
ATOM   11703 C CG  . LYS D 1 459 ? 7.729   92.811  42.212  1.00 81.11  ?  475 LYS A CG  1 
ATOM   11704 C CD  . LYS D 1 459 ? 8.219   93.758  41.140  1.00 87.19  ?  475 LYS A CD  1 
ATOM   11705 C CE  . LYS D 1 459 ? 8.449   95.157  41.674  1.00 86.88  ?  475 LYS A CE  1 
ATOM   11706 N NZ  . LYS D 1 459 ? 8.549   96.177  40.592  1.00 87.91  ?  475 LYS A NZ  1 
ATOM   11707 N N   . LYS D 1 460 ? 4.262   91.159  42.293  1.00 79.57  ?  476 LYS A N   1 
ATOM   11708 C CA  . LYS D 1 460 ? 3.014   91.671  42.846  1.00 80.91  ?  476 LYS A CA  1 
ATOM   11709 C C   . LYS D 1 460 ? 2.449   90.736  43.897  1.00 79.85  ?  476 LYS A C   1 
ATOM   11710 O O   . LYS D 1 460 ? 1.935   91.197  44.931  1.00 78.38  ?  476 LYS A O   1 
ATOM   11711 C CB  . LYS D 1 460 ? 1.996   91.911  41.737  1.00 89.71  ?  476 LYS A CB  1 
ATOM   11712 C CG  . LYS D 1 460 ? 1.711   93.367  41.392  1.00 93.81  ?  476 LYS A CG  1 
ATOM   11713 C CD  . LYS D 1 460 ? 1.112   94.120  42.586  1.00 87.46  ?  476 LYS A CD  1 
ATOM   11714 C CE  . LYS D 1 460 ? -0.138  94.872  42.093  1.00 87.32  ?  476 LYS A CE  1 
ATOM   11715 N NZ  . LYS D 1 460 ? -0.987  95.522  43.133  1.00 80.14  ?  476 LYS A NZ  1 
ATOM   11716 N N   . TRP D 1 461 ? 2.555   89.426  43.661  1.00 86.75  ?  477 TRP A N   1 
ATOM   11717 C CA  . TRP D 1 461 ? 1.991   88.464  44.604  1.00 80.56  ?  477 TRP A CA  1 
ATOM   11718 C C   . TRP D 1 461 ? 2.419   88.811  46.013  1.00 79.71  ?  477 TRP A C   1 
ATOM   11719 O O   . TRP D 1 461 ? 1.596   89.196  46.855  1.00 81.22  ?  477 TRP A O   1 
ATOM   11720 C CB  . TRP D 1 461 ? 2.409   87.039  44.224  1.00 76.75  ?  477 TRP A CB  1 
ATOM   11721 C CG  . TRP D 1 461 ? 1.966   85.975  45.196  1.00 75.97  ?  477 TRP A CG  1 
ATOM   11722 C CD1 . TRP D 1 461 ? 2.738   85.375  46.143  1.00 76.90  ?  477 TRP A CD1 1 
ATOM   11723 C CD2 . TRP D 1 461 ? 0.638   85.440  45.363  1.00 76.04  ?  477 TRP A CD2 1 
ATOM   11724 N NE1 . TRP D 1 461 ? 1.991   84.463  46.850  1.00 79.28  ?  477 TRP A NE1 1 
ATOM   11725 C CE2 . TRP D 1 461 ? 0.699   84.490  46.396  1.00 73.92  ?  477 TRP A CE2 1 
ATOM   11726 C CE3 . TRP D 1 461 ? -0.589  85.665  44.728  1.00 74.46  ?  477 TRP A CE3 1 
ATOM   11727 C CZ2 . TRP D 1 461 ? -0.412  83.767  46.813  1.00 68.53  ?  477 TRP A CZ2 1 
ATOM   11728 C CZ3 . TRP D 1 461 ? -1.690  84.938  45.139  1.00 71.13  ?  477 TRP A CZ3 1 
ATOM   11729 C CH2 . TRP D 1 461 ? -1.594  84.001  46.169  1.00 70.16  ?  477 TRP A CH2 1 
ATOM   11730 N N   . TRP D 1 462 ? 3.733   88.807  46.236  1.00 78.51  ?  478 TRP A N   1 
ATOM   11731 C CA  . TRP D 1 462 ? 4.263   89.015  47.576  1.00 74.15  ?  478 TRP A CA  1 
ATOM   11732 C C   . TRP D 1 462 ? 4.003   90.424  48.079  1.00 70.95  ?  478 TRP A C   1 
ATOM   11733 O O   . TRP D 1 462 ? 3.714   90.591  49.269  1.00 69.37  ?  478 TRP A O   1 
ATOM   11734 C CB  . TRP D 1 462 ? 5.739   88.620  47.599  1.00 70.88  ?  478 TRP A CB  1 
ATOM   11735 C CG  . TRP D 1 462 ? 5.826   87.119  47.627  1.00 69.30  ?  478 TRP A CG  1 
ATOM   11736 C CD1 . TRP D 1 462 ? 6.279   86.296  46.635  1.00 69.92  ?  478 TRP A CD1 1 
ATOM   11737 C CD2 . TRP D 1 462 ? 5.417   86.267  48.695  1.00 64.37  ?  478 TRP A CD2 1 
ATOM   11738 N NE1 . TRP D 1 462 ? 6.183   84.983  47.027  1.00 66.29  ?  478 TRP A NE1 1 
ATOM   11739 C CE2 . TRP D 1 462 ? 5.659   84.944  48.291  1.00 65.47  ?  478 TRP A CE2 1 
ATOM   11740 C CE3 . TRP D 1 462 ? 4.888   86.498  49.966  1.00 65.08  ?  478 TRP A CE3 1 
ATOM   11741 C CZ2 . TRP D 1 462 ? 5.389   83.862  49.109  1.00 66.09  ?  478 TRP A CZ2 1 
ATOM   11742 C CZ3 . TRP D 1 462 ? 4.617   85.426  50.776  1.00 63.47  ?  478 TRP A CZ3 1 
ATOM   11743 C CH2 . TRP D 1 462 ? 4.868   84.124  50.347  1.00 65.58  ?  478 TRP A CH2 1 
ATOM   11744 N N   . GLU D 1 463 ? 3.992   91.432  47.200  1.00 72.80  ?  479 GLU A N   1 
ATOM   11745 C CA  . GLU D 1 463 ? 3.681   92.769  47.695  1.00 71.07  ?  479 GLU A CA  1 
ATOM   11746 C C   . GLU D 1 463 ? 2.322   92.766  48.364  1.00 72.31  ?  479 GLU A C   1 
ATOM   11747 O O   . GLU D 1 463 ? 2.163   93.287  49.476  1.00 72.06  ?  479 GLU A O   1 
ATOM   11748 C CB  . GLU D 1 463 ? 3.698   93.778  46.563  1.00 73.07  ?  479 GLU A CB  1 
ATOM   11749 C CG  . GLU D 1 463 ? 5.078   94.085  46.071  1.00 80.29  ?  479 GLU A CG  1 
ATOM   11750 C CD  . GLU D 1 463 ? 5.091   95.088  44.950  1.00 87.77  ?  479 GLU A CD  1 
ATOM   11751 O OE1 . GLU D 1 463 ? 4.001   95.471  44.462  1.00 91.54  ?  479 GLU A OE1 1 
ATOM   11752 O OE2 . GLU D 1 463 ? 6.208   95.435  44.510  1.00 88.19  -1 479 GLU A OE2 1 
ATOM   11753 N N   . MET D 1 464 ? 1.361   92.065  47.736  1.00 73.81  ?  480 MET A N   1 
ATOM   11754 C CA  . MET D 1 464 ? 0.012   91.899  48.259  1.00 71.01  ?  480 MET A CA  1 
ATOM   11755 C C   . MET D 1 464 ? -0.062  90.882  49.411  1.00 70.86  ?  480 MET A C   1 
ATOM   11756 O O   . MET D 1 464 ? -0.925  91.011  50.287  1.00 69.57  ?  480 MET A O   1 
ATOM   11757 C CB  . MET D 1 464 ? -0.910  91.500  47.117  1.00 71.51  ?  480 MET A CB  1 
ATOM   11758 C CG  . MET D 1 464 ? -1.086  92.595  46.103  1.00 70.51  ?  480 MET A CG  1 
ATOM   11759 S SD  . MET D 1 464 ? -1.899  92.004  44.606  1.00 78.90  ?  480 MET A SD  1 
ATOM   11760 C CE  . MET D 1 464 ? -3.451  91.444  45.310  1.00 66.26  ?  480 MET A CE  1 
ATOM   11761 N N   . LYS D 1 465 ? 0.818   89.876  49.464  1.00 69.28  ?  481 LYS A N   1 
ATOM   11762 C CA  . LYS D 1 465 ? 0.911   89.128  50.711  1.00 67.51  ?  481 LYS A CA  1 
ATOM   11763 C C   . LYS D 1 465 ? 1.346   90.021  51.870  1.00 71.51  ?  481 LYS A C   1 
ATOM   11764 O O   . LYS D 1 465 ? 0.959   89.770  53.014  1.00 74.08  ?  481 LYS A O   1 
ATOM   11765 C CB  . LYS D 1 465 ? 1.857   87.934  50.577  1.00 68.53  ?  481 LYS A CB  1 
ATOM   11766 C CG  . LYS D 1 465 ? 1.308   86.677  49.938  1.00 65.27  ?  481 LYS A CG  1 
ATOM   11767 C CD  . LYS D 1 465 ? 0.520   85.854  50.967  1.00 61.80  ?  481 LYS A CD  1 
ATOM   11768 C CE  . LYS D 1 465 ? 0.194   84.448  50.463  1.00 57.98  ?  481 LYS A CE  1 
ATOM   11769 N NZ  . LYS D 1 465 ? -0.530  83.680  51.498  1.00 54.08  ?  481 LYS A NZ  1 
ATOM   11770 N N   . ARG D 1 466 ? 2.147   91.064  51.614  1.00 67.99  ?  482 ARG A N   1 
ATOM   11771 C CA  . ARG D 1 466 ? 2.641   91.853  52.743  1.00 68.23  ?  482 ARG A CA  1 
ATOM   11772 C C   . ARG D 1 466 ? 1.634   92.925  53.157  1.00 71.60  ?  482 ARG A C   1 
ATOM   11773 O O   . ARG D 1 466 ? 1.503   93.254  54.345  1.00 67.69  ?  482 ARG A O   1 
ATOM   11774 C CB  . ARG D 1 466 ? 3.971   92.525  52.393  1.00 72.42  ?  482 ARG A CB  1 
ATOM   11775 C CG  . ARG D 1 466 ? 5.170   91.620  52.132  1.00 71.41  ?  482 ARG A CG  1 
ATOM   11776 C CD  . ARG D 1 466 ? 6.250   92.449  51.415  1.00 71.76  ?  482 ARG A CD  1 
ATOM   11777 N NE  . ARG D 1 466 ? 7.392   91.649  51.002  1.00 75.49  ?  482 ARG A NE  1 
ATOM   11778 C CZ  . ARG D 1 466 ? 8.636   91.859  51.395  1.00 81.23  ?  482 ARG A CZ  1 
ATOM   11779 N NH1 . ARG D 1 466 ? 8.942   92.860  52.194  1.00 86.02  ?  482 ARG A NH1 1 
ATOM   11780 N NH2 . ARG D 1 466 ? 9.596   91.037  50.979  1.00 85.09  ?  482 ARG A NH2 1 
ATOM   11781 N N   . GLU D 1 467 ? 0.923   93.487  52.186  1.00 70.70  ?  483 GLU A N   1 
ATOM   11782 C CA  . GLU D 1 467 ? 0.067   94.635  52.436  1.00 70.87  ?  483 GLU A CA  1 
ATOM   11783 C C   . GLU D 1 467 ? -1.332  94.232  52.890  1.00 72.23  ?  483 GLU A C   1 
ATOM   11784 O O   . GLU D 1 467 ? -1.899  94.885  53.770  1.00 72.10  ?  483 GLU A O   1 
ATOM   11785 C CB  . GLU D 1 467 ? -0.034  95.511  51.186  1.00 74.39  ?  483 GLU A CB  1 
ATOM   11786 C CG  . GLU D 1 467 ? -0.983  96.680  51.352  1.00 80.25  ?  483 GLU A CG  1 
ATOM   11787 C CD  . GLU D 1 467 ? -0.952  97.650  50.187  1.00 100.00 ?  483 GLU A CD  1 
ATOM   11788 O OE1 . GLU D 1 467 ? 0.005   98.439  50.096  1.00 112.17 ?  483 GLU A OE1 1 
ATOM   11789 O OE2 . GLU D 1 467 ? -1.899  97.634  49.358  1.00 109.05 -1 483 GLU A OE2 1 
ATOM   11790 N N   . ILE D 1 468 ? -1.919  93.184  52.321  1.00 69.54  ?  484 ILE A N   1 
ATOM   11791 C CA  . ILE D 1 468 ? -3.290  92.805  52.662  1.00 69.57  ?  484 ILE A CA  1 
ATOM   11792 C C   . ILE D 1 468 ? -3.321  91.734  53.739  1.00 68.67  ?  484 ILE A C   1 
ATOM   11793 O O   . ILE D 1 468 ? -4.122  91.831  54.666  1.00 69.45  ?  484 ILE A O   1 
ATOM   11794 C CB  . ILE D 1 468 ? -4.048  92.346  51.402  1.00 64.40  ?  484 ILE A CB  1 
ATOM   11795 C CG1 . ILE D 1 468 ? -4.160  93.495  50.425  1.00 61.34  ?  484 ILE A CG1 1 
ATOM   11796 C CG2 . ILE D 1 468 ? -5.454  91.894  51.753  1.00 63.37  ?  484 ILE A CG2 1 
ATOM   11797 C CD1 . ILE D 1 468 ? -4.658  93.038  49.136  1.00 67.72  ?  484 ILE A CD1 1 
ATOM   11798 N N   . VAL D 1 469 ? -2.451  90.719  53.631  1.00 63.12  ?  485 VAL A N   1 
ATOM   11799 C CA  . VAL D 1 469 ? -2.498  89.596  54.561  1.00 61.72  ?  485 VAL A CA  1 
ATOM   11800 C C   . VAL D 1 469 ? -1.703  89.904  55.838  1.00 65.17  ?  485 VAL A C   1 
ATOM   11801 O O   . VAL D 1 469 ? -2.011  89.376  56.916  1.00 63.54  ?  485 VAL A O   1 
ATOM   11802 C CB  . VAL D 1 469 ? -1.972  88.317  53.878  1.00 59.98  ?  485 VAL A CB  1 
ATOM   11803 C CG1 . VAL D 1 469 ? -2.190  87.098  54.753  1.00 59.62  ?  485 VAL A CG1 1 
ATOM   11804 C CG2 . VAL D 1 469 ? -2.605  88.096  52.532  1.00 62.24  ?  485 VAL A CG2 1 
ATOM   11805 N N   . GLY D 1 470 ? -0.690  90.764  55.748  1.00 64.84  ?  486 GLY A N   1 
ATOM   11806 C CA  . GLY D 1 470 ? 0.288   90.889  56.814  1.00 61.26  ?  486 GLY A CA  1 
ATOM   11807 C C   . GLY D 1 470 ? 1.173   89.667  56.909  1.00 61.06  ?  486 GLY A C   1 
ATOM   11808 O O   . GLY D 1 470 ? 1.431   89.179  58.016  1.00 64.40  ?  486 GLY A O   1 
ATOM   11809 N N   . VAL D 1 471 ? 1.621   89.138  55.772  1.00 62.24  ?  487 VAL A N   1 
ATOM   11810 C CA  . VAL D 1 471 ? 2.505   87.985  55.737  1.00 64.15  ?  487 VAL A CA  1 
ATOM   11811 C C   . VAL D 1 471 ? 3.624   88.262  54.736  1.00 70.35  ?  487 VAL A C   1 
ATOM   11812 O O   . VAL D 1 471 ? 3.402   88.925  53.714  1.00 66.96  ?  487 VAL A O   1 
ATOM   11813 C CB  . VAL D 1 471 ? 1.717   86.703  55.398  1.00 60.81  ?  487 VAL A CB  1 
ATOM   11814 C CG1 . VAL D 1 471 ? 2.638   85.535  55.020  1.00 60.78  ?  487 VAL A CG1 1 
ATOM   11815 C CG2 . VAL D 1 471 ? 0.848   86.328  56.576  1.00 58.02  ?  487 VAL A CG2 1 
ATOM   11816 N N   . VAL D 1 472 ? 4.844   87.790  55.060  1.00 69.77  ?  488 VAL A N   1 
ATOM   11817 C CA  . VAL D 1 472 ? 6.053   88.076  54.290  1.00 69.41  ?  488 VAL A CA  1 
ATOM   11818 C C   . VAL D 1 472 ? 6.798   86.778  53.999  1.00 66.91  ?  488 VAL A C   1 
ATOM   11819 O O   . VAL D 1 472 ? 6.681   85.785  54.726  1.00 65.96  ?  488 VAL A O   1 
ATOM   11820 C CB  . VAL D 1 472 ? 6.956   89.077  55.030  1.00 65.31  ?  488 VAL A CB  1 
ATOM   11821 C CG1 . VAL D 1 472 ? 7.340   88.528  56.397  1.00 67.66  ?  488 VAL A CG1 1 
ATOM   11822 C CG2 . VAL D 1 472 ? 8.153   89.464  54.195  1.00 70.21  ?  488 VAL A CG2 1 
ATOM   11823 N N   . GLU D 1 473 ? 7.566   86.792  52.927  1.00 60.06  ?  489 GLU A N   1 
ATOM   11824 C CA  . GLU D 1 473 ? 8.176   85.563  52.465  1.00 62.34  ?  489 GLU A CA  1 
ATOM   11825 C C   . GLU D 1 473 ? 9.556   85.404  53.056  1.00 71.24  ?  489 GLU A C   1 
ATOM   11826 O O   . GLU D 1 473 ? 10.313  86.369  53.122  1.00 78.27  ?  489 GLU A O   1 
ATOM   11827 C CB  . GLU D 1 473 ? 8.274   85.573  50.953  1.00 65.85  ?  489 GLU A CB  1 
ATOM   11828 C CG  . GLU D 1 473 ? 9.297   86.524  50.296  1.00 68.30  ?  489 GLU A CG  1 
ATOM   11829 C CD  . GLU D 1 473 ? 8.823   87.980  50.240  1.00 70.57  ?  489 GLU A CD  1 
ATOM   11830 O OE1 . GLU D 1 473 ? 7.987   88.337  51.098  1.00 69.66  ?  489 GLU A OE1 1 
ATOM   11831 O OE2 . GLU D 1 473 ? 9.140   88.713  49.260  1.00 72.20  -1 489 GLU A OE2 1 
ATOM   11832 N N   . PRO D 1 474 ? 9.910   84.207  53.504  1.00 72.33  ?  490 PRO A N   1 
ATOM   11833 C CA  . PRO D 1 474 ? 11.220  84.034  54.127  1.00 77.21  ?  490 PRO A CA  1 
ATOM   11834 C C   . PRO D 1 474 ? 12.403  84.092  53.168  1.00 77.94  ?  490 PRO A C   1 
ATOM   11835 O O   . PRO D 1 474 ? 13.518  84.281  53.650  1.00 84.91  ?  490 PRO A O   1 
ATOM   11836 C CB  . PRO D 1 474 ? 11.096  82.658  54.789  1.00 77.99  ?  490 PRO A CB  1 
ATOM   11837 C CG  . PRO D 1 474 ? 10.138  81.938  53.939  1.00 70.37  ?  490 PRO A CG  1 
ATOM   11838 C CD  . PRO D 1 474 ? 9.177   82.946  53.381  1.00 69.66  ?  490 PRO A CD  1 
ATOM   11839 N N   . VAL D 1 475 ? 12.210  83.946  51.855  1.00 71.42  ?  491 VAL A N   1 
ATOM   11840 C CA  . VAL D 1 475 ? 13.264  83.901  50.833  1.00 70.86  ?  491 VAL A CA  1 
ATOM   11841 C C   . VAL D 1 475 ? 12.753  84.740  49.662  1.00 80.28  ?  491 VAL A C   1 
ATOM   11842 O O   . VAL D 1 475 ? 11.542  84.730  49.409  1.00 75.83  ?  491 VAL A O   1 
ATOM   11843 C CB  . VAL D 1 475 ? 13.569  82.451  50.396  1.00 72.85  ?  491 VAL A CB  1 
ATOM   11844 C CG1 . VAL D 1 475 ? 14.534  82.400  49.219  1.00 77.48  ?  491 VAL A CG1 1 
ATOM   11845 C CG2 . VAL D 1 475 ? 14.128  81.637  51.526  1.00 72.74  ?  491 VAL A CG2 1 
ATOM   11846 N N   . PRO D 1 476 ? 13.605  85.531  48.966  1.00 79.86  ?  492 PRO A N   1 
ATOM   11847 C CA  . PRO D 1 476 ? 13.157  86.327  47.832  1.00 77.84  ?  492 PRO A CA  1 
ATOM   11848 C C   . PRO D 1 476 ? 12.769  85.429  46.658  1.00 79.56  ?  492 PRO A C   1 
ATOM   11849 O O   . PRO D 1 476 ? 13.363  84.388  46.505  1.00 81.48  ?  492 PRO A O   1 
ATOM   11850 C CB  . PRO D 1 476 ? 14.383  87.160  47.456  1.00 77.26  ?  492 PRO A CB  1 
ATOM   11851 C CG  . PRO D 1 476 ? 15.545  86.343  47.944  1.00 78.90  ?  492 PRO A CG  1 
ATOM   11852 C CD  . PRO D 1 476 ? 15.036  85.750  49.237  1.00 80.73  ?  492 PRO A CD  1 
ATOM   11853 N N   . HIS D 1 477 ? 11.800  85.859  45.849  1.00 85.53  ?  493 HIS A N   1 
ATOM   11854 C CA  . HIS D 1 477 ? 11.320  84.969  44.764  1.00 81.55  ?  493 HIS A CA  1 
ATOM   11855 C C   . HIS D 1 477 ? 11.308  85.686  43.415  1.00 78.75  ?  493 HIS A C   1 
ATOM   11856 O O   . HIS D 1 477 ? 10.561  86.661  43.265  1.00 77.89  ?  493 HIS A O   1 
ATOM   11857 C CB  . HIS D 1 477 ? 9.957   84.381  45.139  1.00 78.10  ?  493 HIS A CB  1 
ATOM   11858 C CG  . HIS D 1 477 ? 10.070  83.152  45.974  1.00 78.59  ?  493 HIS A CG  1 
ATOM   11859 N ND1 . HIS D 1 477 ? 8.968   82.499  46.477  1.00 75.36  ?  493 HIS A ND1 1 
ATOM   11860 C CD2 . HIS D 1 477 ? 11.147  82.463  46.402  1.00 79.05  ?  493 HIS A CD2 1 
ATOM   11861 C CE1 . HIS D 1 477 ? 9.359   81.457  47.177  1.00 74.85  ?  493 HIS A CE1 1 
ATOM   11862 N NE2 . HIS D 1 477 ? 10.691  81.413  47.146  1.00 76.49  ?  493 HIS A NE2 1 
ATOM   11863 N N   . ASP D 1 478 ? 12.107  85.215  42.462  1.00 87.19  ?  494 ASP A N   1 
ATOM   11864 C CA  . ASP D 1 478 ? 12.067  85.801  41.100  1.00 89.29  ?  494 ASP A CA  1 
ATOM   11865 C C   . ASP D 1 478 ? 10.852  85.236  40.379  1.00 90.97  ?  494 ASP A C   1 
ATOM   11866 O O   . ASP D 1 478 ? 10.148  84.409  40.984  1.00 94.52  ?  494 ASP A O   1 
ATOM   11867 C CB  . ASP D 1 478 ? 13.327  85.476  40.307  1.00 93.87  ?  494 ASP A CB  1 
ATOM   11868 C CG  . ASP D 1 478 ? 13.851  84.080  40.570  1.00 96.56  ?  494 ASP A CG  1 
ATOM   11869 O OD1 . ASP D 1 478 ? 13.107  83.276  41.159  1.00 97.21  ?  494 ASP A OD1 1 
ATOM   11870 O OD2 . ASP D 1 478 ? 15.001  83.807  40.178  1.00 105.24 -1 494 ASP A OD2 1 
ATOM   11871 N N   . GLU D 1 479 ? 10.636  85.636  39.130  1.00 86.02  ?  495 GLU A N   1 
ATOM   11872 C CA  . GLU D 1 479 ? 9.410   85.183  38.428  1.00 83.76  ?  495 GLU A CA  1 
ATOM   11873 C C   . GLU D 1 479 ? 9.555   83.712  38.040  1.00 82.30  ?  495 GLU A C   1 
ATOM   11874 O O   . GLU D 1 479 ? 8.573   83.143  37.547  1.00 85.53  ?  495 GLU A O   1 
ATOM   11875 C CB  . GLU D 1 479 ? 9.132   86.066  37.218  1.00 82.87  ?  495 GLU A CB  1 
ATOM   11876 C CG  . GLU D 1 479 ? 8.821   87.501  37.588  1.00 88.70  ?  495 GLU A CG  1 
ATOM   11877 C CD  . GLU D 1 479 ? 7.524   87.672  38.360  1.00 87.67  ?  495 GLU A CD  1 
ATOM   11878 O OE1 . GLU D 1 479 ? 6.579   86.912  38.090  1.00 85.11  ?  495 GLU A OE1 1 
ATOM   11879 O OE2 . GLU D 1 479 ? 7.463   88.559  39.232  1.00 88.52  -1 495 GLU A OE2 1 
ATOM   11880 N N   . THR D 1 480 ? 10.729  83.125  38.259  1.00 80.22  ?  496 THR A N   1 
ATOM   11881 C CA  . THR D 1 480 ? 10.882  81.674  38.003  1.00 82.25  ?  496 THR A CA  1 
ATOM   11882 C C   . THR D 1 480 ? 9.805   80.950  38.800  1.00 86.23  ?  496 THR A C   1 
ATOM   11883 O O   . THR D 1 480 ? 9.425   79.844  38.393  1.00 83.70  ?  496 THR A O   1 
ATOM   11884 C CB  . THR D 1 480 ? 12.272  81.197  38.424  1.00 84.26  ?  496 THR A CB  1 
ATOM   11885 O OG1 . THR D 1 480 ? 12.321  81.160  39.850  1.00 87.56  ?  496 THR A OG1 1 
ATOM   11886 C CG2 . THR D 1 480 ? 13.377  82.088  37.900  1.00 80.47  ?  496 THR A CG2 1 
ATOM   11887 N N   . TYR D 1 481 ? 9.341   81.553  39.891  1.00 80.12  ?  497 TYR A N   1 
ATOM   11888 C CA  . TYR D 1 481 ? 8.345   80.968  40.760  1.00 79.59  ?  497 TYR A CA  1 
ATOM   11889 C C   . TYR D 1 481 ? 6.935   81.233  40.245  1.00 79.90  ?  497 TYR A C   1 
ATOM   11890 O O   . TYR D 1 481 ? 6.697   82.103  39.402  1.00 81.84  ?  497 TYR A O   1 
ATOM   11891 C CB  . TYR D 1 481 ? 8.482   81.516  42.169  1.00 76.89  ?  497 TYR A CB  1 
ATOM   11892 C CG  . TYR D 1 481 ? 9.722   81.094  42.884  1.00 78.93  ?  497 TYR A CG  1 
ATOM   11893 C CD1 . TYR D 1 481 ? 10.933  81.718  42.674  1.00 79.30  ?  497 TYR A CD1 1 
ATOM   11894 C CD2 . TYR D 1 481 ? 9.678   80.021  43.752  1.00 81.34  ?  497 TYR A CD2 1 
ATOM   11895 C CE1 . TYR D 1 481 ? 12.066  81.309  43.367  1.00 78.06  ?  497 TYR A CE1 1 
ATOM   11896 C CE2 . TYR D 1 481 ? 10.790  79.601  44.437  1.00 81.46  ?  497 TYR A CE2 1 
ATOM   11897 C CZ  . TYR D 1 481 ? 11.978  80.238  44.247  1.00 78.22  ?  497 TYR A CZ  1 
ATOM   11898 O OH  . TYR D 1 481 ? 13.045  79.762  44.964  1.00 77.42  ?  497 TYR A OH  1 
ATOM   11899 N N   . CYS D 1 482 ? 5.995   80.455  40.773  1.00 75.18  ?  498 CYS A N   1 
ATOM   11900 C CA  . CYS D 1 482 ? 4.593   80.704  40.510  1.00 71.58  ?  498 CYS A CA  1 
ATOM   11901 C C   . CYS D 1 482 ? 3.820   80.309  41.761  1.00 68.32  ?  498 CYS A C   1 
ATOM   11902 O O   . CYS D 1 482 ? 2.933   79.459  41.733  1.00 69.01  ?  498 CYS A O   1 
ATOM   11903 C CB  . CYS D 1 482 ? 4.124   79.943  39.268  1.00 73.27  ?  498 CYS A CB  1 
ATOM   11904 S SG  . CYS D 1 482 ? 2.550   80.544  38.574  1.00 72.25  ?  498 CYS A SG  1 
ATOM   11905 N N   . ASP D 1 483 ? 4.151   80.933  42.880  1.00 68.97  ?  499 ASP A N   1 
ATOM   11906 C CA  . ASP D 1 483 ? 3.629   80.468  44.158  1.00 68.30  ?  499 ASP A CA  1 
ATOM   11907 C C   . ASP D 1 483 ? 2.112   80.365  44.222  1.00 63.57  ?  499 ASP A C   1 
ATOM   11908 O O   . ASP D 1 483 ? 1.633   79.378  44.800  1.00 64.78  ?  499 ASP A O   1 
ATOM   11909 C CB  . ASP D 1 483 ? 4.215   81.346  45.273  1.00 76.97  ?  499 ASP A CB  1 
ATOM   11910 C CG  . ASP D 1 483 ? 5.743   81.337  45.255  1.00 71.92  ?  499 ASP A CG  1 
ATOM   11911 O OD1 . ASP D 1 483 ? 6.313   80.384  44.673  1.00 72.40  ?  499 ASP A OD1 1 
ATOM   11912 O OD2 . ASP D 1 483 ? 6.371   82.292  45.772  1.00 65.75  -1 499 ASP A OD2 1 
ATOM   11913 N N   . PRO D 1 484 ? 1.303   81.278  43.639  1.00 68.71  ?  500 PRO A N   1 
ATOM   11914 C CA  . PRO D 1 484 ? -0.140  81.011  43.537  1.00 69.86  ?  500 PRO A CA  1 
ATOM   11915 C C   . PRO D 1 484 ? -0.468  79.575  43.118  1.00 66.30  ?  500 PRO A C   1 
ATOM   11916 O O   . PRO D 1 484 ? -1.178  78.852  43.828  1.00 63.43  ?  500 PRO A O   1 
ATOM   11917 C CB  . PRO D 1 484 ? -0.601  82.034  42.490  1.00 68.85  ?  500 PRO A CB  1 
ATOM   11918 C CG  . PRO D 1 484 ? 0.322   83.128  42.607  1.00 67.66  ?  500 PRO A CG  1 
ATOM   11919 C CD  . PRO D 1 484 ? 1.633   82.608  43.112  1.00 70.58  ?  500 PRO A CD  1 
ATOM   11920 N N   . ALA D 1 485 ? 0.123   79.134  42.002  1.00 63.69  ?  501 ALA A N   1 
ATOM   11921 C CA  . ALA D 1 485 ? -0.068  77.802  41.423  1.00 61.28  ?  501 ALA A CA  1 
ATOM   11922 C C   . ALA D 1 485 ? 0.217   76.666  42.394  1.00 59.00  ?  501 ALA A C   1 
ATOM   11923 O O   . ALA D 1 485 ? -0.083  75.512  42.083  1.00 58.58  ?  501 ALA A O   1 
ATOM   11924 C CB  . ALA D 1 485 ? 0.839   77.637  40.192  1.00 59.16  ?  501 ALA A CB  1 
ATOM   11925 N N   . SER D 1 486 ? 0.819   76.954  43.529  1.00 57.57  ?  502 SER A N   1 
ATOM   11926 C CA  . SER D 1 486 ? 1.240   75.924  44.452  1.00 57.58  ?  502 SER A CA  1 
ATOM   11927 C C   . SER D 1 486 ? 0.141   75.543  45.406  1.00 60.20  ?  502 SER A C   1 
ATOM   11928 O O   . SER D 1 486 ? 0.342   74.655  46.243  1.00 63.21  ?  502 SER A O   1 
ATOM   11929 C CB  . SER D 1 486 ? 2.439   76.408  45.241  1.00 53.14  ?  502 SER A CB  1 
ATOM   11930 O OG  . SER D 1 486 ? 1.943   77.205  46.285  1.00 57.07  ?  502 SER A OG  1 
ATOM   11931 N N   . LEU D 1 487 ? -0.990  76.219  45.327  1.00 55.89  ?  503 LEU A N   1 
ATOM   11932 C CA  . LEU D 1 487 ? -2.151  75.879  46.124  1.00 56.52  ?  503 LEU A CA  1 
ATOM   11933 C C   . LEU D 1 487 ? -3.125  75.156  45.213  1.00 56.44  ?  503 LEU A C   1 
ATOM   11934 O O   . LEU D 1 487 ? -3.365  75.594  44.087  1.00 58.16  ?  503 LEU A O   1 
ATOM   11935 C CB  . LEU D 1 487 ? -2.772  77.137  46.724  1.00 56.44  ?  503 LEU A CB  1 
ATOM   11936 C CG  . LEU D 1 487 ? -4.079  77.005  47.477  1.00 50.76  ?  503 LEU A CG  1 
ATOM   11937 C CD1 . LEU D 1 487 ? -3.784  76.287  48.766  1.00 50.23  ?  503 LEU A CD1 1 
ATOM   11938 C CD2 . LEU D 1 487 ? -4.606  78.393  47.760  1.00 51.52  ?  503 LEU A CD2 1 
ATOM   11939 N N   . PHE D 1 488 ? -3.633  74.025  45.680  1.00 55.14  ?  504 PHE A N   1 
ATOM   11940 C CA  . PHE D 1 488 ? -4.505  73.202  44.859  1.00 55.14  ?  504 PHE A CA  1 
ATOM   11941 C C   . PHE D 1 488 ? -5.473  74.001  43.988  1.00 59.56  ?  504 PHE A C   1 
ATOM   11942 O O   . PHE D 1 488 ? -5.528  73.823  42.761  1.00 60.40  ?  504 PHE A O   1 
ATOM   11943 C CB  . PHE D 1 488 ? -5.283  72.270  45.768  1.00 56.09  ?  504 PHE A CB  1 
ATOM   11944 C CG  . PHE D 1 488 ? -6.378  71.589  45.076  1.00 58.07  ?  504 PHE A CG  1 
ATOM   11945 C CD1 . PHE D 1 488 ? -6.138  70.450  44.350  1.00 59.01  ?  504 PHE A CD1 1 
ATOM   11946 C CD2 . PHE D 1 488 ? -7.655  72.114  45.111  1.00 58.52  ?  504 PHE A CD2 1 
ATOM   11947 C CE1 . PHE D 1 488 ? -7.142  69.832  43.693  1.00 61.80  ?  504 PHE A CE1 1 
ATOM   11948 C CE2 . PHE D 1 488 ? -8.672  71.504  44.448  1.00 61.68  ?  504 PHE A CE2 1 
ATOM   11949 C CZ  . PHE D 1 488 ? -8.428  70.355  43.741  1.00 63.49  ?  504 PHE A CZ  1 
ATOM   11950 N N   . HIS D 1 489 ? -6.237  74.900  44.618  1.00 59.57  ?  505 HIS A N   1 
ATOM   11951 C CA  . HIS D 1 489 ? -7.354  75.569  43.951  1.00 56.68  ?  505 HIS A CA  1 
ATOM   11952 C C   . HIS D 1 489 ? -6.908  76.361  42.730  1.00 56.49  ?  505 HIS A C   1 
ATOM   11953 O O   . HIS D 1 489 ? -7.689  76.572  41.804  1.00 60.88  ?  505 HIS A O   1 
ATOM   11954 C CB  . HIS D 1 489 ? -8.062  76.488  44.945  1.00 53.86  ?  505 HIS A CB  1 
ATOM   11955 C CG  . HIS D 1 489 ? -8.617  75.771  46.123  1.00 51.93  ?  505 HIS A CG  1 
ATOM   11956 N ND1 . HIS D 1 489 ? -7.817  75.139  47.049  1.00 52.11  ?  505 HIS A ND1 1 
ATOM   11957 C CD2 . HIS D 1 489 ? -9.888  75.627  46.559  1.00 56.30  ?  505 HIS A CD2 1 
ATOM   11958 C CE1 . HIS D 1 489 ? -8.573  74.608  47.992  1.00 56.56  ?  505 HIS A CE1 1 
ATOM   11959 N NE2 . HIS D 1 489 ? -9.833  74.892  47.720  1.00 58.71  ?  505 HIS A NE2 1 
ATOM   11960 N N   . VAL D 1 490 ? -5.677  76.841  42.712  1.00 57.17  ?  506 VAL A N   1 
ATOM   11961 C CA  . VAL D 1 490 ? -5.250  77.687  41.602  1.00 59.17  ?  506 VAL A CA  1 
ATOM   11962 C C   . VAL D 1 490 ? -4.736  76.848  40.449  1.00 61.46  ?  506 VAL A C   1 
ATOM   11963 O O   . VAL D 1 490 ? -4.985  77.174  39.280  1.00 64.93  ?  506 VAL A O   1 
ATOM   11964 C CB  . VAL D 1 490 ? -4.184  78.699  42.070  1.00 55.66  ?  506 VAL A CB  1 
ATOM   11965 C CG1 . VAL D 1 490 ? -3.720  79.506  40.915  1.00 57.49  ?  506 VAL A CG1 1 
ATOM   11966 C CG2 . VAL D 1 490 ? -4.744  79.596  43.138  1.00 54.58  ?  506 VAL A CG2 1 
ATOM   11967 N N   . SER D 1 491 ? -4.020  75.774  40.794  1.00 59.92  ?  507 SER A N   1 
ATOM   11968 C CA  . SER D 1 491 ? -3.438  74.875  39.816  1.00 61.00  ?  507 SER A CA  1 
ATOM   11969 C C   . SER D 1 491 ? -4.451  73.902  39.267  1.00 65.41  ?  507 SER A C   1 
ATOM   11970 O O   . SER D 1 491 ? -4.208  73.328  38.202  1.00 72.91  ?  507 SER A O   1 
ATOM   11971 C CB  . SER D 1 491 ? -2.320  74.063  40.434  1.00 61.12  ?  507 SER A CB  1 
ATOM   11972 O OG  . SER D 1 491 ? -2.751  73.510  41.659  1.00 59.57  ?  507 SER A OG  1 
ATOM   11973 N N   . ASN D 1 492 ? -5.558  73.678  39.980  1.00 62.31  ?  508 ASN A N   1 
ATOM   11974 C CA  . ASN D 1 492 ? -6.639  72.843  39.473  1.00 63.79  ?  508 ASN A CA  1 
ATOM   11975 C C   . ASN D 1 492 ? -7.861  73.667  39.039  1.00 67.46  ?  508 ASN A C   1 
ATOM   11976 O O   . ASN D 1 492 ? -8.968  73.111  38.866  1.00 69.02  ?  508 ASN A O   1 
ATOM   11977 C CB  . ASN D 1 492 ? -7.022  71.804  40.519  1.00 63.15  ?  508 ASN A CB  1 
ATOM   11978 C CG  . ASN D 1 492 ? -5.944  70.775  40.710  1.00 65.27  ?  508 ASN A CG  1 
ATOM   11979 O OD1 . ASN D 1 492 ? -6.016  69.670  40.190  1.00 73.21  ?  508 ASN A OD1 1 
ATOM   11980 N ND2 . ASN D 1 492 ? -4.951  71.120  41.505  1.00 61.94  ?  508 ASN A ND2 1 
ATOM   11981 N N   . ASP D 1 493 ? -7.693  74.988  38.888  1.00 66.74  ?  509 ASP A N   1 
ATOM   11982 C CA  . ASP D 1 493 ? -8.649  75.832  38.190  1.00 64.60  ?  509 ASP A CA  1 
ATOM   11983 C C   . ASP D 1 493 ? -10.011 75.875  38.876  1.00 61.48  ?  509 ASP A C   1 
ATOM   11984 O O   . ASP D 1 493 ? -10.984 75.357  38.329  1.00 64.76  ?  509 ASP A O   1 
ATOM   11985 C CB  . ASP D 1 493 ? -8.727  75.334  36.754  1.00 63.65  ?  509 ASP A CB  1 
ATOM   11986 C CG  . ASP D 1 493 ? -9.529  76.210  35.893  1.00 65.84  ?  509 ASP A CG  1 
ATOM   11987 O OD1 . ASP D 1 493 ? -9.455  77.443  36.051  1.00 66.86  ?  509 ASP A OD1 1 
ATOM   11988 O OD2 . ASP D 1 493 ? -10.176 75.670  34.992  1.00 69.77  -1 509 ASP A OD2 1 
ATOM   11989 N N   . TYR D 1 494 ? -10.072 76.508  40.054  1.00 58.60  ?  510 TYR A N   1 
ATOM   11990 C CA  . TYR D 1 494 ? -11.256 76.636  40.906  1.00 61.47  ?  510 TYR A CA  1 
ATOM   11991 C C   . TYR D 1 494 ? -11.400 78.066  41.414  1.00 66.57  ?  510 TYR A C   1 
ATOM   11992 O O   . TYR D 1 494 ? -10.496 78.578  42.076  1.00 68.11  ?  510 TYR A O   1 
ATOM   11993 C CB  . TYR D 1 494 ? -11.166 75.689  42.103  1.00 62.16  ?  510 TYR A CB  1 
ATOM   11994 C CG  . TYR D 1 494 ? -11.403 74.231  41.824  1.00 62.42  ?  510 TYR A CG  1 
ATOM   11995 C CD1 . TYR D 1 494 ? -12.690 73.743  41.570  1.00 68.40  ?  510 TYR A CD1 1 
ATOM   11996 C CD2 . TYR D 1 494 ? -10.353 73.337  41.788  1.00 62.10  ?  510 TYR A CD2 1 
ATOM   11997 C CE1 . TYR D 1 494 ? -12.904 72.386  41.303  1.00 68.67  ?  510 TYR A CE1 1 
ATOM   11998 C CE2 . TYR D 1 494 ? -10.559 71.988  41.519  1.00 65.86  ?  510 TYR A CE2 1 
ATOM   11999 C CZ  . TYR D 1 494 ? -11.827 71.525  41.279  1.00 68.61  ?  510 TYR A CZ  1 
ATOM   12000 O OH  . TYR D 1 494 ? -12.003 70.197  41.019  1.00 69.40  ?  510 TYR A OH  1 
ATOM   12001 N N   . SER D 1 495 ? -12.549 78.690  41.155  1.00 81.05  ?  511 SER A N   1 
ATOM   12002 C CA  . SER D 1 495 ? -12.801 80.010  41.721  1.00 81.95  ?  511 SER A CA  1 
ATOM   12003 C C   . SER D 1 495 ? -12.711 79.941  43.237  1.00 78.44  ?  511 SER A C   1 
ATOM   12004 O O   . SER D 1 495 ? -13.105 78.950  43.851  1.00 81.05  ?  511 SER A O   1 
ATOM   12005 C CB  . SER D 1 495 ? -14.166 80.553  41.272  1.00 81.77  ?  511 SER A CB  1 
ATOM   12006 O OG  . SER D 1 495 ? -15.270 79.844  41.821  1.00 79.60  ?  511 SER A OG  1 
ATOM   12007 N N   . PHE D 1 496 ? -12.160 80.994  43.838  1.00 65.81  ?  512 PHE A N   1 
ATOM   12008 C CA  . PHE D 1 496 ? -11.762 80.990  45.236  1.00 61.26  ?  512 PHE A CA  1 
ATOM   12009 C C   . PHE D 1 496 ? -12.511 81.957  46.141  1.00 62.39  ?  512 PHE A C   1 
ATOM   12010 O O   . PHE D 1 496 ? -12.547 81.717  47.351  1.00 60.42  ?  512 PHE A O   1 
ATOM   12011 C CB  . PHE D 1 496 ? -10.267 81.288  45.347  1.00 63.80  ?  512 PHE A CB  1 
ATOM   12012 C CG  . PHE D 1 496 ? -9.606  80.645  46.525  1.00 58.68  ?  512 PHE A CG  1 
ATOM   12013 C CD1 . PHE D 1 496 ? -9.548  79.274  46.649  1.00 57.23  ?  512 PHE A CD1 1 
ATOM   12014 C CD2 . PHE D 1 496 ? -9.005  81.435  47.495  1.00 56.38  ?  512 PHE A CD2 1 
ATOM   12015 C CE1 . PHE D 1 496 ? -8.936  78.708  47.739  1.00 54.19  ?  512 PHE A CE1 1 
ATOM   12016 C CE2 . PHE D 1 496 ? -8.386  80.885  48.573  1.00 56.97  ?  512 PHE A CE2 1 
ATOM   12017 C CZ  . PHE D 1 496 ? -8.355  79.519  48.706  1.00 56.03  ?  512 PHE A CZ  1 
ATOM   12018 N N   . ILE D 1 497 ? -13.103 83.036  45.611  1.00 65.55  ?  513 ILE A N   1 
ATOM   12019 C CA  . ILE D 1 497 ? -13.858 83.982  46.446  1.00 63.12  ?  513 ILE A CA  1 
ATOM   12020 C C   . ILE D 1 497 ? -15.040 83.336  47.153  1.00 63.74  ?  513 ILE A C   1 
ATOM   12021 O O   . ILE D 1 497 ? -15.581 83.895  48.129  1.00 62.08  ?  513 ILE A O   1 
ATOM   12022 C CB  . ILE D 1 497 ? -14.330 85.177  45.602  1.00 63.90  ?  513 ILE A CB  1 
ATOM   12023 C CG1 . ILE D 1 497 ? -14.516 86.405  46.490  1.00 60.46  ?  513 ILE A CG1 1 
ATOM   12024 C CG2 . ILE D 1 497 ? -15.602 84.801  44.870  1.00 64.41  ?  513 ILE A CG2 1 
ATOM   12025 C CD1 . ILE D 1 497 ? -13.309 86.843  47.194  1.00 57.93  ?  513 ILE A CD1 1 
ATOM   12026 N N   . ARG D 1 498 ? -15.461 82.158  46.684  1.00 60.22  ?  514 ARG A N   1 
ATOM   12027 C CA  . ARG D 1 498 ? -16.520 81.447  47.371  1.00 57.37  ?  514 ARG A CA  1 
ATOM   12028 C C   . ARG D 1 498 ? -16.242 81.266  48.868  1.00 57.06  ?  514 ARG A C   1 
ATOM   12029 O O   . ARG D 1 498 ? -17.187 81.269  49.667  1.00 56.09  ?  514 ARG A O   1 
ATOM   12030 C CB  . ARG D 1 498 ? -16.732 80.105  46.707  1.00 54.20  ?  514 ARG A CB  1 
ATOM   12031 C CG  . ARG D 1 498 ? -15.681 79.162  47.112  1.00 55.13  ?  514 ARG A CG  1 
ATOM   12032 C CD  . ARG D 1 498 ? -15.242 78.393  45.962  1.00 60.63  ?  514 ARG A CD  1 
ATOM   12033 N NE  . ARG D 1 498 ? -16.357 77.552  45.570  1.00 60.74  ?  514 ARG A NE  1 
ATOM   12034 C CZ  . ARG D 1 498 ? -16.496 77.011  44.376  1.00 66.09  ?  514 ARG A CZ  1 
ATOM   12035 N NH1 . ARG D 1 498 ? -15.535 77.100  43.464  1.00 66.72  ?  514 ARG A NH1 1 
ATOM   12036 N NH2 . ARG D 1 498 ? -17.621 76.349  44.097  1.00 69.40  ?  514 ARG A NH2 1 
ATOM   12037 N N   . TYR D 1 499 ? -14.980 81.115  49.286  1.00 55.82  ?  515 TYR A N   1 
ATOM   12038 C CA  . TYR D 1 499 ? -14.750 80.849  50.707  1.00 53.93  ?  515 TYR A CA  1 
ATOM   12039 C C   . TYR D 1 499 ? -14.958 82.107  51.522  1.00 52.07  ?  515 TYR A C   1 
ATOM   12040 O O   . TYR D 1 499 ? -15.515 82.049  52.630  1.00 53.71  ?  515 TYR A O   1 
ATOM   12041 C CB  . TYR D 1 499 ? -13.361 80.249  50.914  1.00 57.03  ?  515 TYR A CB  1 
ATOM   12042 C CG  . TYR D 1 499 ? -13.210 78.933  50.144  1.00 55.99  ?  515 TYR A CG  1 
ATOM   12043 C CD1 . TYR D 1 499 ? -13.851 77.780  50.564  1.00 53.25  ?  515 TYR A CD1 1 
ATOM   12044 C CD2 . TYR D 1 499 ? -12.515 78.874  48.934  1.00 54.41  ?  515 TYR A CD2 1 
ATOM   12045 C CE1 . TYR D 1 499 ? -13.742 76.594  49.853  1.00 52.34  ?  515 TYR A CE1 1 
ATOM   12046 C CE2 . TYR D 1 499 ? -12.412 77.694  48.213  1.00 52.14  ?  515 TYR A CE2 1 
ATOM   12047 C CZ  . TYR D 1 499 ? -13.020 76.558  48.681  1.00 52.11  ?  515 TYR A CZ  1 
ATOM   12048 O OH  . TYR D 1 499 ? -12.916 75.378  47.973  1.00 50.28  ?  515 TYR A OH  1 
ATOM   12049 N N   . TYR D 1 500 ? -14.662 83.262  50.917  1.00 55.69  ?  516 TYR A N   1 
ATOM   12050 C CA  . TYR D 1 500 ? -15.005 84.551  51.522  1.00 57.62  ?  516 TYR A CA  1 
ATOM   12051 C C   . TYR D 1 500 ? -16.508 84.679  51.702  1.00 57.26  ?  516 TYR A C   1 
ATOM   12052 O O   . TYR D 1 500 ? -17.015 84.865  52.825  1.00 58.27  ?  516 TYR A O   1 
ATOM   12053 C CB  . TYR D 1 500 ? -14.467 85.694  50.647  1.00 56.08  ?  516 TYR A CB  1 
ATOM   12054 C CG  . TYR D 1 500 ? -14.606 87.065  51.254  1.00 56.17  ?  516 TYR A CG  1 
ATOM   12055 C CD1 . TYR D 1 500 ? -15.756 87.795  51.088  1.00 61.12  ?  516 TYR A CD1 1 
ATOM   12056 C CD2 . TYR D 1 500 ? -13.598 87.613  52.048  1.00 60.02  ?  516 TYR A CD2 1 
ATOM   12057 C CE1 . TYR D 1 500 ? -15.909 89.062  51.656  1.00 64.30  ?  516 TYR A CE1 1 
ATOM   12058 C CE2 . TYR D 1 500 ? -13.752 88.874  52.632  1.00 63.00  ?  516 TYR A CE2 1 
ATOM   12059 C CZ  . TYR D 1 500 ? -14.918 89.584  52.419  1.00 62.21  ?  516 TYR A CZ  1 
ATOM   12060 O OH  . TYR D 1 500 ? -15.098 90.817  52.968  1.00 64.35  ?  516 TYR A OH  1 
ATOM   12061 N N   . THR D 1 501 ? -17.236 84.533  50.598  1.00 59.60  ?  517 THR A N   1 
ATOM   12062 C CA  . THR D 1 501 ? -18.673 84.755  50.614  1.00 60.02  ?  517 THR A CA  1 
ATOM   12063 C C   . THR D 1 501 ? -19.393 83.778  51.537  1.00 56.22  ?  517 THR A C   1 
ATOM   12064 O O   . THR D 1 501 ? -20.290 84.177  52.287  1.00 55.46  ?  517 THR A O   1 
ATOM   12065 C CB  . THR D 1 501 ? -19.197 84.666  49.184  1.00 60.87  ?  517 THR A CB  1 
ATOM   12066 O OG1 . THR D 1 501 ? -18.940 83.349  48.679  1.00 59.89  ?  517 THR A OG1 1 
ATOM   12067 C CG2 . THR D 1 501 ? -18.537 85.715  48.284  1.00 61.00  ?  517 THR A CG2 1 
ATOM   12068 N N   . ARG D 1 502 ? -19.087 82.482  51.416  1.00 50.57  ?  518 ARG A N   1 
ATOM   12069 C CA  . ARG D 1 502 ? -19.704 81.469  52.266  1.00 49.18  ?  518 ARG A CA  1 
ATOM   12070 C C   . ARG D 1 502 ? -19.517 81.820  53.728  1.00 56.00  ?  518 ARG A C   1 
ATOM   12071 O O   . ARG D 1 502 ? -20.466 81.745  54.530  1.00 55.76  ?  518 ARG A O   1 
ATOM   12072 C CB  . ARG D 1 502 ? -19.078 80.096  52.006  1.00 47.37  ?  518 ARG A CB  1 
ATOM   12073 C CG  . ARG D 1 502 ? -19.318 79.108  53.155  1.00 52.40  ?  518 ARG A CG  1 
ATOM   12074 C CD  . ARG D 1 502 ? -18.306 77.936  53.251  1.00 57.59  ?  518 ARG A CD  1 
ATOM   12075 N NE  . ARG D 1 502 ? -16.970 78.310  53.701  1.00 63.94  ?  518 ARG A NE  1 
ATOM   12076 C CZ  . ARG D 1 502 ? -16.575 78.247  54.971  1.00 67.39  ?  518 ARG A CZ  1 
ATOM   12077 N NH1 . ARG D 1 502 ? -17.371 77.781  55.921  1.00 66.96  ?  518 ARG A NH1 1 
ATOM   12078 N NH2 . ARG D 1 502 ? -15.349 78.664  55.299  1.00 66.68  ?  518 ARG A NH2 1 
ATOM   12079 N N   . THR D 1 503 ? -18.265 82.163  54.100  1.00 64.90  ?  519 THR A N   1 
ATOM   12080 C CA  . THR D 1 503 ? -17.986 82.553  55.477  1.00 59.80  ?  519 THR A CA  1 
ATOM   12081 C C   . THR D 1 503 ? -18.938 83.643  55.907  1.00 61.65  ?  519 THR A C   1 
ATOM   12082 O O   . THR D 1 503 ? -19.599 83.517  56.937  1.00 66.48  ?  519 THR A O   1 
ATOM   12083 C CB  . THR D 1 503 ? -16.540 83.015  55.646  1.00 59.98  ?  519 THR A CB  1 
ATOM   12084 O OG1 . THR D 1 503 ? -15.653 81.919  55.378  1.00 61.78  ?  519 THR A OG1 1 
ATOM   12085 C CG2 . THR D 1 503 ? -16.306 83.517  57.075  1.00 65.34  ?  519 THR A CG2 1 
ATOM   12086 N N   . LEU D 1 504 ? -19.069 84.694  55.098  1.00 59.86  ?  520 LEU A N   1 
ATOM   12087 C CA  . LEU D 1 504 ? -19.959 85.794  55.491  1.00 61.50  ?  520 LEU A CA  1 
ATOM   12088 C C   . LEU D 1 504 ? -21.421 85.341  55.568  1.00 59.06  ?  520 LEU A C   1 
ATOM   12089 O O   . LEU D 1 504 ? -22.129 85.625  56.560  1.00 59.87  ?  520 LEU A O   1 
ATOM   12090 C CB  . LEU D 1 504 ? -19.790 86.985  54.536  1.00 62.76  ?  520 LEU A CB  1 
ATOM   12091 C CG  . LEU D 1 504 ? -18.654 87.952  54.909  1.00 62.19  ?  520 LEU A CG  1 
ATOM   12092 C CD1 . LEU D 1 504 ? -17.280 87.286  54.949  1.00 58.19  ?  520 LEU A CD1 1 
ATOM   12093 C CD2 . LEU D 1 504 ? -18.627 89.108  53.946  1.00 62.92  ?  520 LEU A CD2 1 
ATOM   12094 N N   . TYR D 1 505 ? -21.893 84.649  54.524  1.00 58.24  ?  521 TYR A N   1 
ATOM   12095 C CA  . TYR D 1 505 ? -23.288 84.219  54.508  1.00 57.81  ?  521 TYR A CA  1 
ATOM   12096 C C   . TYR D 1 505 ? -23.639 83.481  55.772  1.00 54.02  ?  521 TYR A C   1 
ATOM   12097 O O   . TYR D 1 505 ? -24.727 83.672  56.321  1.00 54.14  ?  521 TYR A O   1 
ATOM   12098 C CB  . TYR D 1 505 ? -23.630 83.337  53.296  1.00 54.12  ?  521 TYR A CB  1 
ATOM   12099 C CG  . TYR D 1 505 ? -23.546 83.972  51.934  1.00 49.59  ?  521 TYR A CG  1 
ATOM   12100 C CD1 . TYR D 1 505 ? -23.744 85.319  51.768  1.00 52.91  ?  521 TYR A CD1 1 
ATOM   12101 C CD2 . TYR D 1 505 ? -23.319 83.198  50.803  1.00 50.14  ?  521 TYR A CD2 1 
ATOM   12102 C CE1 . TYR D 1 505 ? -23.687 85.897  50.510  1.00 58.49  ?  521 TYR A CE1 1 
ATOM   12103 C CE2 . TYR D 1 505 ? -23.261 83.753  49.547  1.00 52.20  ?  521 TYR A CE2 1 
ATOM   12104 C CZ  . TYR D 1 505 ? -23.442 85.105  49.396  1.00 57.05  ?  521 TYR A CZ  1 
ATOM   12105 O OH  . TYR D 1 505 ? -23.376 85.664  48.124  1.00 59.43  ?  521 TYR A OH  1 
ATOM   12106 N N   . GLN D 1 506 ? -22.731 82.632  56.252  1.00 52.29  ?  522 GLN A N   1 
ATOM   12107 C CA  . GLN D 1 506 ? -23.158 81.702  57.280  1.00 52.34  ?  522 GLN A CA  1 
ATOM   12108 C C   . GLN D 1 506 ? -23.468 82.448  58.571  1.00 53.87  ?  522 GLN A C   1 
ATOM   12109 O O   . GLN D 1 506 ? -24.378 82.068  59.323  1.00 52.50  ?  522 GLN A O   1 
ATOM   12110 C CB  . GLN D 1 506 ? -22.091 80.652  57.518  1.00 53.89  ?  522 GLN A CB  1 
ATOM   12111 C CG  . GLN D 1 506 ? -20.933 81.125  58.358  1.00 53.19  ?  522 GLN A CG  1 
ATOM   12112 C CD  . GLN D 1 506 ? -19.820 80.115  58.405  1.00 58.45  ?  522 GLN A CD  1 
ATOM   12113 O OE1 . GLN D 1 506 ? -19.391 79.587  57.368  1.00 61.71  ?  522 GLN A OE1 1 
ATOM   12114 N NE2 . GLN D 1 506 ? -19.459 79.717  59.612  1.00 57.53  ?  522 GLN A NE2 1 
ATOM   12115 N N   . PHE D 1 507 ? -22.751 83.540  58.831  1.00 55.42  ?  523 PHE A N   1 
ATOM   12116 C CA  . PHE D 1 507 ? -23.024 84.282  60.047  1.00 54.82  ?  523 PHE A CA  1 
ATOM   12117 C C   . PHE D 1 507 ? -24.224 85.175  59.848  1.00 57.19  ?  523 PHE A C   1 
ATOM   12118 O O   . PHE D 1 507 ? -24.958 85.420  60.806  1.00 57.62  ?  523 PHE A O   1 
ATOM   12119 C CB  . PHE D 1 507 ? -21.771 85.037  60.510  1.00 58.25  ?  523 PHE A CB  1 
ATOM   12120 C CG  . PHE D 1 507 ? -20.674 84.104  60.958  1.00 56.10  ?  523 PHE A CG  1 
ATOM   12121 C CD1 . PHE D 1 507 ? -20.785 83.396  62.147  1.00 54.03  ?  523 PHE A CD1 1 
ATOM   12122 C CD2 . PHE D 1 507 ? -19.584 83.857  60.141  1.00 56.90  ?  523 PHE A CD2 1 
ATOM   12123 C CE1 . PHE D 1 507 ? -19.808 82.489  62.538  1.00 52.24  ?  523 PHE A CE1 1 
ATOM   12124 C CE2 . PHE D 1 507 ? -18.608 82.958  60.514  1.00 54.67  ?  523 PHE A CE2 1 
ATOM   12125 C CZ  . PHE D 1 507 ? -18.718 82.276  61.724  1.00 51.49  ?  523 PHE A CZ  1 
ATOM   12126 N N   . GLN D 1 508 ? -24.512 85.572  58.606  1.00 58.71  ?  524 GLN A N   1 
ATOM   12127 C CA  . GLN D 1 508 ? -25.821 86.186  58.374  1.00 56.47  ?  524 GLN A CA  1 
ATOM   12128 C C   . GLN D 1 508 ? -26.948 85.218  58.704  1.00 55.31  ?  524 GLN A C   1 
ATOM   12129 O O   . GLN D 1 508 ? -27.871 85.546  59.468  1.00 55.93  ?  524 GLN A O   1 
ATOM   12130 C CB  . GLN D 1 508 ? -25.930 86.693  56.951  1.00 52.05  ?  524 GLN A CB  1 
ATOM   12131 C CG  . GLN D 1 508 ? -24.906 87.726  56.698  1.00 63.15  ?  524 GLN A CG  1 
ATOM   12132 C CD  . GLN D 1 508 ? -25.070 88.384  55.371  1.00 65.82  ?  524 GLN A CD  1 
ATOM   12133 O OE1 . GLN D 1 508 ? -24.264 88.192  54.467  1.00 66.75  ?  524 GLN A OE1 1 
ATOM   12134 N NE2 . GLN D 1 508 ? -26.150 89.155  55.228  1.00 69.24  ?  524 GLN A NE2 1 
ATOM   12135 N N   . PHE D 1 509 ? -26.870 84.008  58.159  1.00 53.50  ?  525 PHE A N   1 
ATOM   12136 C CA  . PHE D 1 509 ? -27.883 82.992  58.430  1.00 52.01  ?  525 PHE A CA  1 
ATOM   12137 C C   . PHE D 1 509 ? -28.016 82.767  59.925  1.00 52.94  ?  525 PHE A C   1 
ATOM   12138 O O   . PHE D 1 509 ? -29.121 82.814  60.477  1.00 55.31  ?  525 PHE A O   1 
ATOM   12139 C CB  . PHE D 1 509 ? -27.538 81.674  57.719  1.00 48.53  ?  525 PHE A CB  1 
ATOM   12140 C CG  . PHE D 1 509 ? -27.552 81.761  56.209  1.00 48.63  ?  525 PHE A CG  1 
ATOM   12141 C CD1 . PHE D 1 509 ? -28.157 82.826  55.572  1.00 51.64  ?  525 PHE A CD1 1 
ATOM   12142 C CD2 . PHE D 1 509 ? -26.926 80.793  55.427  1.00 47.09  ?  525 PHE A CD2 1 
ATOM   12143 C CE1 . PHE D 1 509 ? -28.164 82.903  54.208  1.00 53.97  ?  525 PHE A CE1 1 
ATOM   12144 C CE2 . PHE D 1 509 ? -26.912 80.877  54.054  1.00 44.62  ?  525 PHE A CE2 1 
ATOM   12145 C CZ  . PHE D 1 509 ? -27.530 81.927  53.449  1.00 51.36  ?  525 PHE A CZ  1 
ATOM   12146 N N   . GLN D 1 510 ? -26.888 82.505  60.593  1.00 53.46  ?  526 GLN A N   1 
ATOM   12147 C CA  . GLN D 1 510 ? -26.932 82.136  62.001  1.00 54.08  ?  526 GLN A CA  1 
ATOM   12148 C C   . GLN D 1 510 ? -27.492 83.276  62.840  1.00 56.15  ?  526 GLN A C   1 
ATOM   12149 O O   . GLN D 1 510 ? -28.336 83.062  63.721  1.00 58.34  ?  526 GLN A O   1 
ATOM   12150 C CB  . GLN D 1 510 ? -25.550 81.702  62.501  1.00 47.09  ?  526 GLN A CB  1 
ATOM   12151 C CG  . GLN D 1 510 ? -25.619 81.169  63.916  1.00 47.19  ?  526 GLN A CG  1 
ATOM   12152 C CD  . GLN D 1 510 ? -26.291 79.808  64.093  1.00 51.45  ?  526 GLN A CD  1 
ATOM   12153 O OE1 . GLN D 1 510 ? -26.820 79.202  63.163  1.00 50.00  ?  526 GLN A OE1 1 
ATOM   12154 N NE2 . GLN D 1 510 ? -26.386 79.395  65.352  1.00 53.35  ?  526 GLN A NE2 1 
ATOM   12155 N N   . GLU D 1 511 ? -27.036 84.499  62.593  1.00 51.87  ?  527 GLU A N   1 
ATOM   12156 C CA  . GLU D 1 511 ? -27.581 85.610  63.344  1.00 55.20  ?  527 GLU A CA  1 
ATOM   12157 C C   . GLU D 1 511 ? -29.087 85.665  63.173  1.00 59.00  ?  527 GLU A C   1 
ATOM   12158 O O   . GLU D 1 511 ? -29.824 85.812  64.151  1.00 65.25  ?  527 GLU A O   1 
ATOM   12159 C CB  . GLU D 1 511 ? -26.950 86.916  62.890  1.00 60.90  ?  527 GLU A CB  1 
ATOM   12160 C CG  . GLU D 1 511 ? -27.348 88.098  63.753  1.00 68.62  ?  527 GLU A CG  1 
ATOM   12161 C CD  . GLU D 1 511 ? -26.695 89.391  63.289  1.00 79.10  ?  527 GLU A CD  1 
ATOM   12162 O OE1 . GLU D 1 511 ? -27.220 90.023  62.341  1.00 82.84  ?  527 GLU A OE1 1 
ATOM   12163 O OE2 . GLU D 1 511 ? -25.631 89.750  63.852  1.00 84.14  -1 527 GLU A OE2 1 
ATOM   12164 N N   . ALA D 1 512 ? -29.565 85.523  61.933  1.00 58.59  ?  528 ALA A N   1 
ATOM   12165 C CA  . ALA D 1 512 ? -30.988 85.714  61.671  1.00 58.52  ?  528 ALA A CA  1 
ATOM   12166 C C   . ALA D 1 512 ? -31.825 84.632  62.338  1.00 56.69  ?  528 ALA A C   1 
ATOM   12167 O O   . ALA D 1 512 ? -32.785 84.931  63.053  1.00 57.96  ?  528 ALA A O   1 
ATOM   12168 C CB  . ALA D 1 512 ? -31.234 85.737  60.167  1.00 62.00  ?  528 ALA A CB  1 
ATOM   12169 N N   . LEU D 1 513 ? -31.478 83.366  62.098  1.00 56.44  ?  529 LEU A N   1 
ATOM   12170 C CA  . LEU D 1 513 ? -32.184 82.251  62.728  1.00 56.97  ?  529 LEU A CA  1 
ATOM   12171 C C   . LEU D 1 513 ? -32.139 82.333  64.257  1.00 59.78  ?  529 LEU A C   1 
ATOM   12172 O O   . LEU D 1 513 ? -33.142 82.042  64.923  1.00 61.04  ?  529 LEU A O   1 
ATOM   12173 C CB  . LEU D 1 513 ? -31.596 80.923  62.242  1.00 53.15  ?  529 LEU A CB  1 
ATOM   12174 C CG  . LEU D 1 513 ? -31.585 80.684  60.748  1.00 47.07  ?  529 LEU A CG  1 
ATOM   12175 C CD1 . LEU D 1 513 ? -31.253 79.277  60.469  1.00 47.70  ?  529 LEU A CD1 1 
ATOM   12176 C CD2 . LEU D 1 513 ? -32.947 80.881  60.268  1.00 53.25  ?  529 LEU A CD2 1 
ATOM   12177 N N   . CYS D 1 514 ? -30.989 82.717  64.840  1.00 59.61  ?  530 CYS A N   1 
ATOM   12178 C CA  . CYS D 1 514 ? -30.899 82.824  66.297  1.00 59.56  ?  530 CYS A CA  1 
ATOM   12179 C C   . CYS D 1 514 ? -31.772 83.946  66.823  1.00 64.42  ?  530 CYS A C   1 
ATOM   12180 O O   . CYS D 1 514 ? -32.417 83.798  67.871  1.00 64.93  ?  530 CYS A O   1 
ATOM   12181 C CB  . CYS D 1 514 ? -29.462 83.046  66.734  1.00 57.41  ?  530 CYS A CB  1 
ATOM   12182 S SG  . CYS D 1 514 ? -28.470 81.552  66.495  1.00 65.04  ?  530 CYS A SG  1 
ATOM   12183 N N   . GLN D 1 515 ? -31.782 85.082  66.118  1.00 65.98  ?  531 GLN A N   1 
ATOM   12184 C CA  . GLN D 1 515 ? -32.771 86.124  66.359  1.00 61.08  ?  531 GLN A CA  1 
ATOM   12185 C C   . GLN D 1 515 ? -34.161 85.517  66.372  1.00 57.93  ?  531 GLN A C   1 
ATOM   12186 O O   . GLN D 1 515 ? -34.924 85.711  67.323  1.00 59.18  ?  531 GLN A O   1 
ATOM   12187 C CB  . GLN D 1 515 ? -32.666 87.179  65.269  1.00 62.31  ?  531 GLN A CB  1 
ATOM   12188 C CG  . GLN D 1 515 ? -33.596 88.323  65.459  1.00 78.43  ?  531 GLN A CG  1 
ATOM   12189 C CD  . GLN D 1 515 ? -33.320 89.457  64.489  1.00 90.35  ?  531 GLN A CD  1 
ATOM   12190 O OE1 . GLN D 1 515 ? -32.193 89.962  64.400  1.00 97.40  ?  531 GLN A OE1 1 
ATOM   12191 N NE2 . GLN D 1 515 ? -34.369 89.907  63.794  1.00 95.13  ?  531 GLN A NE2 1 
ATOM   12192 N N   . ALA D 1 516 ? -34.475 84.734  65.329  1.00 65.16  ?  532 ALA A N   1 
ATOM   12193 C CA  . ALA D 1 516 ? -35.789 84.130  65.156  1.00 63.05  ?  532 ALA A CA  1 
ATOM   12194 C C   . ALA D 1 516 ? -36.051 83.060  66.199  1.00 68.16  ?  532 ALA A C   1 
ATOM   12195 O O   . ALA D 1 516 ? -37.199 82.808  66.559  1.00 71.43  ?  532 ALA A O   1 
ATOM   12196 C CB  . ALA D 1 516 ? -35.896 83.541  63.759  1.00 63.12  ?  532 ALA A CB  1 
ATOM   12197 N N   . ALA D 1 517 ? -35.004 82.424  66.689  1.00 65.49  ?  533 ALA A N   1 
ATOM   12198 C CA  . ALA D 1 517 ? -35.106 81.510  67.808  1.00 65.44  ?  533 ALA A CA  1 
ATOM   12199 C C   . ALA D 1 517 ? -35.086 82.253  69.160  1.00 69.43  ?  533 ALA A C   1 
ATOM   12200 O O   . ALA D 1 517 ? -34.856 81.639  70.217  1.00 71.90  ?  533 ALA A O   1 
ATOM   12201 C CB  . ALA D 1 517 ? -33.987 80.470  67.716  1.00 62.86  ?  533 ALA A CB  1 
ATOM   12202 N N   . LYS D 1 518 ? -35.325 83.567  69.115  1.00 70.31  ?  534 LYS A N   1 
ATOM   12203 C CA  . LYS D 1 518 ? -35.443 84.426  70.291  1.00 71.27  ?  534 LYS A CA  1 
ATOM   12204 C C   . LYS D 1 518 ? -34.281 84.181  71.252  1.00 74.47  ?  534 LYS A C   1 
ATOM   12205 O O   . LYS D 1 518 ? -34.473 83.975  72.452  1.00 79.65  ?  534 LYS A O   1 
ATOM   12206 C CB  . LYS D 1 518 ? -36.777 84.189  70.996  1.00 74.75  ?  534 LYS A CB  1 
ATOM   12207 C CG  . LYS D 1 518 ? -38.000 84.585  70.209  1.00 77.71  ?  534 LYS A CG  1 
ATOM   12208 C CD  . LYS D 1 518 ? -39.274 83.967  70.809  1.00 86.85  ?  534 LYS A CD  1 
ATOM   12209 C CE  . LYS D 1 518 ? -40.430 83.991  69.790  1.00 102.16 ?  534 LYS A CE  1 
ATOM   12210 N NZ  . LYS D 1 518 ? -40.624 85.291  69.078  1.00 104.00 ?  534 LYS A NZ  1 
ATOM   12211 N N   . HIS D 1 519 ? -33.061 84.159  70.705  1.00 73.44  ?  535 HIS A N   1 
ATOM   12212 C CA  . HIS D 1 519 ? -31.892 83.715  71.453  1.00 78.95  ?  535 HIS A CA  1 
ATOM   12213 C C   . HIS D 1 519 ? -31.300 84.866  72.243  1.00 82.95  ?  535 HIS A C   1 
ATOM   12214 O O   . HIS D 1 519 ? -30.762 85.812  71.656  1.00 82.62  ?  535 HIS A O   1 
ATOM   12215 C CB  . HIS D 1 519 ? -30.804 83.158  70.552  1.00 75.43  ?  535 HIS A CB  1 
ATOM   12216 C CG  . HIS D 1 519 ? -29.550 82.835  71.300  1.00 76.86  ?  535 HIS A CG  1 
ATOM   12217 N ND1 . HIS D 1 519 ? -28.460 83.680  71.327  1.00 75.83  ?  535 HIS A ND1 1 
ATOM   12218 C CD2 . HIS D 1 519 ? -29.212 81.759  72.048  1.00 77.91  ?  535 HIS A CD2 1 
ATOM   12219 C CE1 . HIS D 1 519 ? -27.504 83.143  72.061  1.00 73.04  ?  535 HIS A CE1 1 
ATOM   12220 N NE2 . HIS D 1 519 ? -27.934 81.977  72.510  1.00 77.00  ?  535 HIS A NE2 1 
ATOM   12221 N N   . GLU D 1 520 ? -31.350 84.759  73.566  1.00 88.64  ?  536 GLU A N   1 
ATOM   12222 C CA  . GLU D 1 520 ? -30.743 85.760  74.422  1.00 91.56  ?  536 GLU A CA  1 
ATOM   12223 C C   . GLU D 1 520 ? -29.251 85.495  74.578  1.00 90.17  ?  536 GLU A C   1 
ATOM   12224 O O   . GLU D 1 520 ? -28.790 84.353  74.551  1.00 92.48  ?  536 GLU A O   1 
ATOM   12225 C CB  . GLU D 1 520 ? -31.413 85.798  75.807  1.00 103.03 ?  536 GLU A CB  1 
ATOM   12226 C CG  . GLU D 1 520 ? -32.958 85.746  75.857  1.00 110.77 ?  536 GLU A CG  1 
ATOM   12227 C CD  . GLU D 1 520 ? -33.639 87.040  75.342  1.00 120.42 ?  536 GLU A CD  1 
ATOM   12228 O OE1 . GLU D 1 520 ? -32.953 88.095  75.202  1.00 111.07 ?  536 GLU A OE1 1 
ATOM   12229 O OE2 . GLU D 1 520 ? -34.867 86.996  75.082  1.00 126.19 -1 536 GLU A OE2 1 
ATOM   12230 N N   . GLY D 1 521 ? -28.503 86.573  74.757  1.00 81.21  ?  537 GLY A N   1 
ATOM   12231 C CA  . GLY D 1 521 ? -27.095 86.488  75.023  1.00 73.54  ?  537 GLY A CA  1 
ATOM   12232 C C   . GLY D 1 521 ? -26.272 86.745  73.788  1.00 68.41  ?  537 GLY A C   1 
ATOM   12233 O O   . GLY D 1 521 ? -26.753 87.308  72.801  1.00 69.54  ?  537 GLY A O   1 
ATOM   12234 N N   . PRO D 1 522 ? -25.001 86.359  73.837  1.00 66.27  ?  538 PRO A N   1 
ATOM   12235 C CA  . PRO D 1 522 ? -24.140 86.472  72.663  1.00 63.72  ?  538 PRO A CA  1 
ATOM   12236 C C   . PRO D 1 522 ? -24.435 85.380  71.659  1.00 64.20  ?  538 PRO A C   1 
ATOM   12237 O O   . PRO D 1 522 ? -24.833 84.266  72.005  1.00 67.60  ?  538 PRO A O   1 
ATOM   12238 C CB  . PRO D 1 522 ? -22.731 86.309  73.237  1.00 60.09  ?  538 PRO A CB  1 
ATOM   12239 C CG  . PRO D 1 522 ? -22.887 86.433  74.699  1.00 61.21  ?  538 PRO A CG  1 
ATOM   12240 C CD  . PRO D 1 522 ? -24.248 85.973  75.033  1.00 63.28  ?  538 PRO A CD  1 
ATOM   12241 N N   . LEU D 1 523 ? -24.195 85.722  70.398  1.00 58.45  ?  539 LEU A N   1 
ATOM   12242 C CA  . LEU D 1 523 ? -24.562 84.857  69.283  1.00 58.31  ?  539 LEU A CA  1 
ATOM   12243 C C   . LEU D 1 523 ? -23.813 83.535  69.279  1.00 61.60  ?  539 LEU A C   1 
ATOM   12244 O O   . LEU D 1 523 ? -24.353 82.530  68.802  1.00 60.99  ?  539 LEU A O   1 
ATOM   12245 C CB  . LEU D 1 523 ? -24.313 85.598  67.981  1.00 57.11  ?  539 LEU A CB  1 
ATOM   12246 C CG  . LEU D 1 523 ? -24.485 84.947  66.624  1.00 57.67  ?  539 LEU A CG  1 
ATOM   12247 C CD1 . LEU D 1 523 ? -25.882 84.395  66.459  1.00 60.89  ?  539 LEU A CD1 1 
ATOM   12248 C CD2 . LEU D 1 523 ? -24.196 86.022  65.573  1.00 63.58  ?  539 LEU A CD2 1 
ATOM   12249 N N   . HIS D 1 524 ? -22.576 83.499  69.798  1.00 61.42  ?  540 HIS A N   1 
ATOM   12250 C CA  . HIS D 1 524 ? -21.753 82.326  69.524  1.00 56.27  ?  540 HIS A CA  1 
ATOM   12251 C C   . HIS D 1 524 ? -22.153 81.173  70.424  1.00 55.33  ?  540 HIS A C   1 
ATOM   12252 O O   . HIS D 1 524 ? -21.570 80.091  70.287  1.00 57.31  ?  540 HIS A O   1 
ATOM   12253 C CB  . HIS D 1 524 ? -20.262 82.599  69.748  1.00 59.14  ?  540 HIS A CB  1 
ATOM   12254 C CG  . HIS D 1 524 ? -19.838 82.536  71.191  1.00 61.76  ?  540 HIS A CG  1 
ATOM   12255 N ND1 . HIS D 1 524 ? -19.846 83.623  72.040  1.00 62.22  ?  540 HIS A ND1 1 
ATOM   12256 C CD2 . HIS D 1 524 ? -19.304 81.510  71.903  1.00 58.84  ?  540 HIS A CD2 1 
ATOM   12257 C CE1 . HIS D 1 524 ? -19.398 83.251  73.228  1.00 63.02  ?  540 HIS A CE1 1 
ATOM   12258 N NE2 . HIS D 1 524 ? -19.054 81.976  73.169  1.00 56.84  ?  540 HIS A NE2 1 
ATOM   12259 N N   . LYS D 1 525 ? -23.067 81.413  71.365  1.00 59.47  ?  541 LYS A N   1 
ATOM   12260 C CA  . LYS D 1 525 ? -23.574 80.400  72.274  1.00 64.12  ?  541 LYS A CA  1 
ATOM   12261 C C   . LYS D 1 525 ? -24.905 79.829  71.806  1.00 69.18  ?  541 LYS A C   1 
ATOM   12262 O O   . LYS D 1 525 ? -25.418 78.888  72.424  1.00 67.39  ?  541 LYS A O   1 
ATOM   12263 C CB  . LYS D 1 525 ? -23.696 81.006  73.672  1.00 63.93  ?  541 LYS A CB  1 
ATOM   12264 C CG  . LYS D 1 525 ? -22.366 81.460  74.277  1.00 68.89  ?  541 LYS A CG  1 
ATOM   12265 C CD  . LYS D 1 525 ? -22.518 82.461  75.462  1.00 74.07  ?  541 LYS A CD  1 
ATOM   12266 C CE  . LYS D 1 525 ? -23.268 81.971  76.721  1.00 75.28  ?  541 LYS A CE  1 
ATOM   12267 N NZ  . LYS D 1 525 ? -22.551 80.960  77.521  1.00 86.65  ?  541 LYS A NZ  1 
ATOM   12268 N N   . CYS D 1 526 ? -25.437 80.341  70.698  1.00 74.79  ?  542 CYS A N   1 
ATOM   12269 C CA  . CYS D 1 526 ? -26.810 80.076  70.290  1.00 76.61  ?  542 CYS A CA  1 
ATOM   12270 C C   . CYS D 1 526 ? -27.012 78.666  69.777  1.00 74.63  ?  542 CYS A C   1 
ATOM   12271 O O   . CYS D 1 526 ? -26.200 78.152  69.003  1.00 74.92  ?  542 CYS A O   1 
ATOM   12272 C CB  . CYS D 1 526 ? -27.227 81.041  69.193  1.00 75.03  ?  542 CYS A CB  1 
ATOM   12273 S SG  . CYS D 1 526 ? -28.657 80.470  68.218  1.00 80.32  ?  542 CYS A SG  1 
ATOM   12274 N N   . ASP D 1 527 ? -28.150 78.078  70.163  1.00 60.44  ?  543 ASP A N   1 
ATOM   12275 C CA  . ASP D 1 527 ? -28.576 76.761  69.700  1.00 54.36  ?  543 ASP A CA  1 
ATOM   12276 C C   . ASP D 1 527 ? -30.025 76.885  69.237  1.00 60.68  ?  543 ASP A C   1 
ATOM   12277 O O   . ASP D 1 527 ? -30.936 77.111  70.050  1.00 59.56  ?  543 ASP A O   1 
ATOM   12278 C CB  . ASP D 1 527 ? -28.478 75.713  70.805  1.00 55.35  ?  543 ASP A CB  1 
ATOM   12279 C CG  . ASP D 1 527 ? -29.024 74.371  70.361  1.00 55.76  ?  543 ASP A CG  1 
ATOM   12280 O OD1 . ASP D 1 527 ? -29.284 74.282  69.145  1.00 56.44  ?  543 ASP A OD1 1 
ATOM   12281 O OD2 . ASP D 1 527 ? -29.297 73.471  71.205  1.00 54.73  -1 543 ASP A OD2 1 
ATOM   12282 N N   . ILE D 1 528 ? -30.253 76.684  67.944  1.00 63.41  ?  544 ILE A N   1 
ATOM   12283 C CA  . ILE D 1 528 ? -31.565 76.972  67.378  1.00 57.33  ?  544 ILE A CA  1 
ATOM   12284 C C   . ILE D 1 528 ? -32.494 75.782  67.501  1.00 56.68  ?  544 ILE A C   1 
ATOM   12285 O O   . ILE D 1 528 ? -33.532 75.753  66.843  1.00 62.19  ?  544 ILE A O   1 
ATOM   12286 C CB  . ILE D 1 528 ? -31.471 77.374  65.898  1.00 53.09  ?  544 ILE A CB  1 
ATOM   12287 C CG1 . ILE D 1 528 ? -31.116 76.152  65.048  1.00 47.73  ?  544 ILE A CG1 1 
ATOM   12288 C CG2 . ILE D 1 528 ? -30.536 78.555  65.722  1.00 57.42  ?  544 ILE A CG2 1 
ATOM   12289 C CD1 . ILE D 1 528 ? -31.115 76.401  63.616  1.00 43.54  ?  544 ILE A CD1 1 
ATOM   12290 N N   . SER D 1 529 ? -32.123 74.768  68.269  1.00 55.04  ?  545 SER A N   1 
ATOM   12291 C CA  . SER D 1 529 ? -32.977 73.596  68.292  1.00 53.86  ?  545 SER A CA  1 
ATOM   12292 C C   . SER D 1 529 ? -34.351 74.006  68.756  1.00 57.45  ?  545 SER A C   1 
ATOM   12293 O O   . SER D 1 529 ? -34.503 74.992  69.480  1.00 61.66  ?  545 SER A O   1 
ATOM   12294 C CB  . SER D 1 529 ? -32.445 72.507  69.211  1.00 58.29  ?  545 SER A CB  1 
ATOM   12295 O OG  . SER D 1 529 ? -31.169 72.074  68.809  1.00 56.50  ?  545 SER A OG  1 
ATOM   12296 N N   . ASN D 1 530 ? -35.348 73.272  68.272  1.00 56.17  ?  546 ASN A N   1 
ATOM   12297 C CA  . ASN D 1 530 ? -36.732 73.425  68.704  1.00 59.81  ?  546 ASN A CA  1 
ATOM   12298 C C   . ASN D 1 530 ? -37.441 74.667  68.154  1.00 63.15  ?  546 ASN A C   1 
ATOM   12299 O O   . ASN D 1 530 ? -38.680 74.727  68.164  1.00 65.67  ?  546 ASN A O   1 
ATOM   12300 C CB  . ASN D 1 530 ? -36.802 73.450  70.234  1.00 64.33  ?  546 ASN A CB  1 
ATOM   12301 C CG  . ASN D 1 530 ? -36.640 72.089  70.844  1.00 65.72  ?  546 ASN A CG  1 
ATOM   12302 O OD1 . ASN D 1 530 ? -36.936 71.072  70.235  1.00 61.93  ?  546 ASN A OD1 1 
ATOM   12303 N ND2 . ASN D 1 530 ? -36.133 72.064  72.049  1.00 74.04  ?  546 ASN A ND2 1 
ATOM   12304 N N   . SER D 1 531 ? -36.693 75.683  67.718  1.00 63.51  ?  547 SER A N   1 
ATOM   12305 C CA  . SER D 1 531 ? -37.337 76.888  67.195  1.00 65.42  ?  547 SER A CA  1 
ATOM   12306 C C   . SER D 1 531 ? -37.853 76.626  65.782  1.00 65.12  ?  547 SER A C   1 
ATOM   12307 O O   . SER D 1 531 ? -37.131 76.810  64.792  1.00 65.05  ?  547 SER A O   1 
ATOM   12308 C CB  . SER D 1 531 ? -36.386 78.080  67.186  1.00 67.40  ?  547 SER A CB  1 
ATOM   12309 O OG  . SER D 1 531 ? -36.961 79.191  66.532  1.00 66.06  ?  547 SER A OG  1 
ATOM   12310 N N   . THR D 1 532 ? -39.107 76.184  65.685  1.00 68.00  ?  548 THR A N   1 
ATOM   12311 C CA  . THR D 1 532 ? -39.676 75.916  64.375  1.00 64.00  ?  548 THR A CA  1 
ATOM   12312 C C   . THR D 1 532 ? -39.820 77.192  63.572  1.00 66.85  ?  548 THR A C   1 
ATOM   12313 O O   . THR D 1 532 ? -39.843 77.130  62.348  1.00 69.41  ?  548 THR A O   1 
ATOM   12314 C CB  . THR D 1 532 ? -41.035 75.215  64.477  1.00 61.29  ?  548 THR A CB  1 
ATOM   12315 O OG1 . THR D 1 532 ? -41.921 75.997  65.269  1.00 65.36  ?  548 THR A OG1 1 
ATOM   12316 C CG2 . THR D 1 532 ? -40.902 73.842  65.096  1.00 64.22  ?  548 THR A CG2 1 
ATOM   12317 N N   . GLU D 1 533 ? -39.918 78.342  64.228  1.00 71.80  ?  549 GLU A N   1 
ATOM   12318 C CA  . GLU D 1 533 ? -39.929 79.603  63.499  1.00 71.10  ?  549 GLU A CA  1 
ATOM   12319 C C   . GLU D 1 533 ? -38.609 79.800  62.755  1.00 69.27  ?  549 GLU A C   1 
ATOM   12320 O O   . GLU D 1 533 ? -38.595 80.231  61.593  1.00 67.40  ?  549 GLU A O   1 
ATOM   12321 C CB  . GLU D 1 533 ? -40.222 80.745  64.479  1.00 73.72  ?  549 GLU A CB  1 
ATOM   12322 C CG  . GLU D 1 533 ? -41.270 80.389  65.558  1.00 77.96  ?  549 GLU A CG  1 
ATOM   12323 C CD  . GLU D 1 533 ? -40.664 79.564  66.738  1.00 92.34  ?  549 GLU A CD  1 
ATOM   12324 O OE1 . GLU D 1 533 ? -39.764 80.060  67.474  1.00 98.06  ?  549 GLU A OE1 1 
ATOM   12325 O OE2 . GLU D 1 533 ? -41.080 78.383  66.910  1.00 94.97  -1 549 GLU A OE2 1 
ATOM   12326 N N   . ALA D 1 534 ? -37.490 79.438  63.397  1.00 66.06  ?  550 ALA A N   1 
ATOM   12327 C CA  . ALA D 1 534 ? -36.190 79.473  62.727  1.00 61.05  ?  550 ALA A CA  1 
ATOM   12328 C C   . ALA D 1 534 ? -36.146 78.462  61.587  1.00 59.59  ?  550 ALA A C   1 
ATOM   12329 O O   . ALA D 1 534 ? -35.576 78.731  60.516  1.00 55.16  ?  550 ALA A O   1 
ATOM   12330 C CB  . ALA D 1 534 ? -35.073 79.207  63.747  1.00 56.92  ?  550 ALA A CB  1 
ATOM   12331 N N   . GLY D 1 535 ? -36.763 77.294  61.800  1.00 63.35  ?  551 GLY A N   1 
ATOM   12332 C CA  . GLY D 1 535 ? -36.816 76.295  60.756  1.00 58.48  ?  551 GLY A CA  1 
ATOM   12333 C C   . GLY D 1 535 ? -37.569 76.796  59.551  1.00 62.04  ?  551 GLY A C   1 
ATOM   12334 O O   . GLY D 1 535 ? -37.097 76.673  58.426  1.00 64.68  ?  551 GLY A O   1 
ATOM   12335 N N   . GLN D 1 536 ? -38.755 77.362  59.772  1.00 60.10  ?  552 GLN A N   1 
ATOM   12336 C CA  . GLN D 1 536 ? -39.549 77.933  58.688  1.00 60.08  ?  552 GLN A CA  1 
ATOM   12337 C C   . GLN D 1 536 ? -38.756 78.972  57.921  1.00 54.25  ?  552 GLN A C   1 
ATOM   12338 O O   . GLN D 1 536 ? -38.722 78.969  56.688  1.00 52.33  ?  552 GLN A O   1 
ATOM   12339 C CB  . GLN D 1 536 ? -40.805 78.590  59.260  1.00 65.94  ?  552 GLN A CB  1 
ATOM   12340 C CG  . GLN D 1 536 ? -41.684 79.151  58.187  1.00 65.69  ?  552 GLN A CG  1 
ATOM   12341 C CD  . GLN D 1 536 ? -42.218 78.030  57.366  1.00 63.48  ?  552 GLN A CD  1 
ATOM   12342 O OE1 . GLN D 1 536 ? -42.901 77.129  57.882  1.00 57.03  ?  552 GLN A OE1 1 
ATOM   12343 N NE2 . GLN D 1 536 ? -41.743 77.957  56.118  1.00 64.77  ?  552 GLN A NE2 1 
ATOM   12344 N N   . LYS D 1 537 ? -38.126 79.885  58.657  1.00 59.91  ?  553 LYS A N   1 
ATOM   12345 C CA  . LYS D 1 537 ? -37.395 80.996  58.059  1.00 59.36  ?  553 LYS A CA  1 
ATOM   12346 C C   . LYS D 1 537 ? -36.279 80.476  57.168  1.00 56.89  ?  553 LYS A C   1 
ATOM   12347 O O   . LYS D 1 537 ? -36.114 80.959  56.048  1.00 58.84  ?  553 LYS A O   1 
ATOM   12348 C CB  . LYS D 1 537 ? -36.844 81.903  59.170  1.00 56.40  ?  553 LYS A CB  1 
ATOM   12349 C CG  . LYS D 1 537 ? -36.743 83.343  58.799  1.00 58.21  ?  553 LYS A CG  1 
ATOM   12350 C CD  . LYS D 1 537 ? -36.805 84.197  60.054  1.00 60.86  ?  553 LYS A CD  1 
ATOM   12351 C CE  . LYS D 1 537 ? -36.799 85.670  59.722  1.00 69.14  ?  553 LYS A CE  1 
ATOM   12352 N NZ  . LYS D 1 537 ? -37.902 85.862  58.698  1.00 75.40  ?  553 LYS A NZ  1 
ATOM   12353 N N   . LEU D 1 538 ? -35.536 79.452  57.638  1.00 57.94  ?  554 LEU A N   1 
ATOM   12354 C CA  . LEU D 1 538 ? -34.489 78.800  56.844  1.00 56.00  ?  554 LEU A CA  1 
ATOM   12355 C C   . LEU D 1 538 ? -35.062 78.084  55.623  1.00 55.88  ?  554 LEU A C   1 
ATOM   12356 O O   . LEU D 1 538 ? -34.534 78.197  54.504  1.00 53.45  ?  554 LEU A O   1 
ATOM   12357 C CB  . LEU D 1 538 ? -33.725 77.807  57.725  1.00 55.84  ?  554 LEU A CB  1 
ATOM   12358 C CG  . LEU D 1 538 ? -32.590 76.999  57.073  1.00 49.63  ?  554 LEU A CG  1 
ATOM   12359 C CD1 . LEU D 1 538 ? -31.494 77.956  56.654  1.00 46.04  ?  554 LEU A CD1 1 
ATOM   12360 C CD2 . LEU D 1 538 ? -32.022 75.901  58.012  1.00 44.57  ?  554 LEU A CD2 1 
ATOM   12361 N N   . PHE D 1 539 ? -36.122 77.302  55.835  1.00 58.20  ?  555 PHE A N   1 
ATOM   12362 C CA  . PHE D 1 539 ? -36.721 76.523  54.761  1.00 54.82  ?  555 PHE A CA  1 
ATOM   12363 C C   . PHE D 1 539 ? -37.212 77.418  53.637  1.00 54.56  ?  555 PHE A C   1 
ATOM   12364 O O   . PHE D 1 539 ? -37.200 77.008  52.470  1.00 52.98  ?  555 PHE A O   1 
ATOM   12365 C CB  . PHE D 1 539 ? -37.854 75.675  55.326  1.00 49.21  ?  555 PHE A CB  1 
ATOM   12366 C CG  . PHE D 1 539 ? -38.482 74.785  54.320  1.00 53.55  ?  555 PHE A CG  1 
ATOM   12367 C CD1 . PHE D 1 539 ? -37.921 73.567  54.012  1.00 53.46  ?  555 PHE A CD1 1 
ATOM   12368 C CD2 . PHE D 1 539 ? -39.657 75.153  53.682  1.00 56.56  ?  555 PHE A CD2 1 
ATOM   12369 C CE1 . PHE D 1 539 ? -38.511 72.720  53.079  1.00 51.66  ?  555 PHE A CE1 1 
ATOM   12370 C CE2 . PHE D 1 539 ? -40.246 74.313  52.760  1.00 51.67  ?  555 PHE A CE2 1 
ATOM   12371 C CZ  . PHE D 1 539 ? -39.668 73.096  52.462  1.00 51.96  ?  555 PHE A CZ  1 
ATOM   12372 N N   . ASN D 1 540 ? -37.622 78.652  53.968  1.00 56.16  ?  556 ASN A N   1 
ATOM   12373 C CA  . ASN D 1 540 ? -38.055 79.596  52.940  1.00 54.26  ?  556 ASN A CA  1 
ATOM   12374 C C   . ASN D 1 540 ? -36.955 79.851  51.926  1.00 55.73  ?  556 ASN A C   1 
ATOM   12375 O O   . ASN D 1 540 ? -37.238 80.151  50.755  1.00 52.55  ?  556 ASN A O   1 
ATOM   12376 C CB  . ASN D 1 540 ? -38.481 80.928  53.553  1.00 55.99  ?  556 ASN A CB  1 
ATOM   12377 C CG  . ASN D 1 540 ? -39.759 80.801  54.360  1.00 65.95  ?  556 ASN A CG  1 
ATOM   12378 O OD1 . ASN D 1 540 ? -40.520 79.812  54.220  1.00 61.10  ?  556 ASN A OD1 1 
ATOM   12379 N ND2 . ASN D 1 540 ? -40.061 81.844  55.142  1.00 69.75  ?  556 ASN A ND2 1 
ATOM   12380 N N   . MET D 1 541 ? -35.689 79.784  52.358  1.00 58.05  ?  557 MET A N   1 
ATOM   12381 C CA  . MET D 1 541 ? -34.608 79.914  51.387  1.00 54.61  ?  557 MET A CA  1 
ATOM   12382 C C   . MET D 1 541 ? -34.270 78.574  50.788  1.00 52.08  ?  557 MET A C   1 
ATOM   12383 O O   . MET D 1 541 ? -34.022 78.470  49.577  1.00 50.81  ?  557 MET A O   1 
ATOM   12384 C CB  . MET D 1 541 ? -33.368 80.535  52.019  1.00 53.52  ?  557 MET A CB  1 
ATOM   12385 C CG  . MET D 1 541 ? -32.127 80.535  51.124  1.00 54.60  ?  557 MET A CG  1 
ATOM   12386 S SD  . MET D 1 541 ? -31.088 79.020  51.187  1.00 54.71  ?  557 MET A SD  1 
ATOM   12387 C CE  . MET D 1 541 ? -30.554 79.185  52.874  1.00 49.36  ?  557 MET A CE  1 
ATOM   12388 N N   . LEU D 1 542 ? -34.260 77.540  51.624  1.00 53.02  ?  558 LEU A N   1 
ATOM   12389 C CA  . LEU D 1 542 ? -33.817 76.241  51.131  1.00 56.10  ?  558 LEU A CA  1 
ATOM   12390 C C   . LEU D 1 542 ? -34.676 75.800  49.954  1.00 53.16  ?  558 LEU A C   1 
ATOM   12391 O O   . LEU D 1 542 ? -34.163 75.535  48.860  1.00 53.67  ?  558 LEU A O   1 
ATOM   12392 C CB  . LEU D 1 542 ? -33.825 75.195  52.249  1.00 53.66  ?  558 LEU A CB  1 
ATOM   12393 C CG  . LEU D 1 542 ? -32.923 75.504  53.423  1.00 45.68  ?  558 LEU A CG  1 
ATOM   12394 C CD1 . LEU D 1 542 ? -33.074 74.360  54.378  1.00 42.72  ?  558 LEU A CD1 1 
ATOM   12395 C CD2 . LEU D 1 542 ? -31.536 75.627  52.881  1.00 45.59  ?  558 LEU A CD2 1 
ATOM   12396 N N   . ARG D 1 543 ? -35.998 75.802  50.136  1.00 56.48  ?  559 ARG A N   1 
ATOM   12397 C CA  . ARG D 1 543 ? -36.896 75.314  49.099  1.00 52.04  ?  559 ARG A CA  1 
ATOM   12398 C C   . ARG D 1 543 ? -36.700 76.025  47.762  1.00 49.62  ?  559 ARG A C   1 
ATOM   12399 O O   . ARG D 1 543 ? -37.172 75.526  46.742  1.00 53.64  ?  559 ARG A O   1 
ATOM   12400 C CB  . ARG D 1 543 ? -38.363 75.431  49.560  1.00 50.98  ?  559 ARG A CB  1 
ATOM   12401 C CG  . ARG D 1 543 ? -38.887 76.868  49.781  1.00 54.50  ?  559 ARG A CG  1 
ATOM   12402 C CD  . ARG D 1 543 ? -40.414 76.963  49.539  1.00 55.08  ?  559 ARG A CD  1 
ATOM   12403 N NE  . ARG D 1 543 ? -40.589 76.420  48.205  1.00 57.34  ?  559 ARG A NE  1 
ATOM   12404 C CZ  . ARG D 1 543 ? -40.618 77.134  47.087  1.00 60.95  ?  559 ARG A CZ  1 
ATOM   12405 N NH1 . ARG D 1 543 ? -40.650 78.463  47.106  1.00 63.08  ?  559 ARG A NH1 1 
ATOM   12406 N NH2 . ARG D 1 543 ? -40.551 76.501  45.921  1.00 62.15  ?  559 ARG A NH2 1 
ATOM   12407 N N   . LEU D 1 544 ? -36.001 77.157  47.723  1.00 52.79  ?  560 LEU A N   1 
ATOM   12408 C CA  . LEU D 1 544 ? -35.931 77.888  46.465  1.00 53.75  ?  560 LEU A CA  1 
ATOM   12409 C C   . LEU D 1 544 ? -35.104 77.148  45.435  1.00 55.01  ?  560 LEU A C   1 
ATOM   12410 O O   . LEU D 1 544 ? -35.487 77.101  44.269  1.00 59.12  ?  560 LEU A O   1 
ATOM   12411 C CB  . LEU D 1 544 ? -35.371 79.288  46.680  1.00 57.37  ?  560 LEU A CB  1 
ATOM   12412 C CG  . LEU D 1 544 ? -36.354 80.184  47.421  1.00 55.73  ?  560 LEU A CG  1 
ATOM   12413 C CD1 . LEU D 1 544 ? -35.782 81.575  47.584  1.00 59.26  ?  560 LEU A CD1 1 
ATOM   12414 C CD2 . LEU D 1 544 ? -37.691 80.180  46.724  1.00 56.71  ?  560 LEU A CD2 1 
ATOM   12415 N N   . GLY D 1 545 ? -33.979 76.563  45.830  1.00 57.02  ?  561 GLY A N   1 
ATOM   12416 C CA  . GLY D 1 545 ? -33.040 76.093  44.823  1.00 55.52  ?  561 GLY A CA  1 
ATOM   12417 C C   . GLY D 1 545 ? -32.310 77.305  44.285  1.00 58.37  ?  561 GLY A C   1 
ATOM   12418 O O   . GLY D 1 545 ? -31.973 78.200  45.070  1.00 57.10  ?  561 GLY A O   1 
ATOM   12419 N N   . LYS D 1 546 ? -32.093 77.383  42.970  1.00 62.53  ?  562 LYS A N   1 
ATOM   12420 C CA  . LYS D 1 546 ? -31.587 78.615  42.370  1.00 64.46  ?  562 LYS A CA  1 
ATOM   12421 C C   . LYS D 1 546 ? -32.561 79.198  41.349  1.00 66.71  ?  562 LYS A C   1 
ATOM   12422 O O   . LYS D 1 546 ? -32.142 79.809  40.362  1.00 68.03  ?  562 LYS A O   1 
ATOM   12423 C CB  . LYS D 1 546 ? -30.222 78.408  41.720  1.00 65.19  ?  562 LYS A CB  1 
ATOM   12424 C CG  . LYS D 1 546 ? -30.114 77.267  40.727  1.00 67.68  ?  562 LYS A CG  1 
ATOM   12425 C CD  . LYS D 1 546 ? -28.665 77.134  40.190  1.00 73.66  ?  562 LYS A CD  1 
ATOM   12426 C CE  . LYS D 1 546 ? -28.333 78.193  39.120  1.00 75.18  ?  562 LYS A CE  1 
ATOM   12427 N NZ  . LYS D 1 546 ? -26.875 78.226  38.752  1.00 77.71  ?  562 LYS A NZ  1 
ATOM   12428 N N   . SER D 1 547 ? -33.861 79.028  41.600  1.00 61.38  ?  563 SER A N   1 
ATOM   12429 C CA  . SER D 1 547 ? -34.925 79.494  40.717  1.00 58.02  ?  563 SER A CA  1 
ATOM   12430 C C   . SER D 1 547 ? -35.203 80.973  40.901  1.00 62.74  ?  563 SER A C   1 
ATOM   12431 O O   . SER D 1 547 ? -35.658 81.649  39.970  1.00 61.94  ?  563 SER A O   1 
ATOM   12432 C CB  . SER D 1 547 ? -36.201 78.728  41.014  1.00 60.51  ?  563 SER A CB  1 
ATOM   12433 O OG  . SER D 1 547 ? -36.651 79.032  42.328  1.00 60.85  ?  563 SER A OG  1 
ATOM   12434 N N   . GLU D 1 548 ? -34.988 81.459  42.067  1.00 60.51  ?  564 GLU A N   1 
ATOM   12435 C CA  . GLU D 1 548 ? -34.960 82.877  42.302  1.00 58.40  ?  564 GLU A CA  1 
ATOM   12436 C C   . GLU D 1 548 ? -33.524 83.351  42.340  1.00 60.34  ?  564 GLU A C   1 
ATOM   12437 O O   . GLU D 1 548 ? -32.599 82.542  42.459  1.00 59.30  ?  564 GLU A O   1 
ATOM   12438 C CB  . GLU D 1 548 ? -35.666 83.189  43.618  1.00 61.23  ?  564 GLU A CB  1 
ATOM   12439 C CG  . GLU D 1 548 ? -37.132 82.802  43.640  1.00 65.77  ?  564 GLU A CG  1 
ATOM   12440 C CD  . GLU D 1 548 ? -37.973 83.680  42.711  1.00 78.19  ?  564 GLU A CD  1 
ATOM   12441 O OE1 . GLU D 1 548 ? -37.391 84.612  42.107  1.00 77.54  ?  564 GLU A OE1 1 
ATOM   12442 O OE2 . GLU D 1 548 ? -39.209 83.458  42.602  1.00 87.76  -1 564 GLU A OE2 1 
ATOM   12443 N N   . PRO D 1 549 ? -33.306 84.657  42.199  1.00 64.20  ?  565 PRO A N   1 
ATOM   12444 C CA  . PRO D 1 549 ? -31.960 85.218  42.363  1.00 62.49  ?  565 PRO A CA  1 
ATOM   12445 C C   . PRO D 1 549 ? -31.403 84.914  43.740  1.00 62.42  ?  565 PRO A C   1 
ATOM   12446 O O   . PRO D 1 549 ? -32.152 84.788  44.707  1.00 64.50  ?  565 PRO A O   1 
ATOM   12447 C CB  . PRO D 1 549 ? -32.190 86.724  42.210  1.00 61.72  ?  565 PRO A CB  1 
ATOM   12448 C CG  . PRO D 1 549 ? -33.394 86.836  41.416  1.00 65.69  ?  565 PRO A CG  1 
ATOM   12449 C CD  . PRO D 1 549 ? -34.274 85.685  41.801  1.00 64.71  ?  565 PRO A CD  1 
ATOM   12450 N N   . TRP D 1 550 ? -30.070 84.851  43.853  1.00 61.30  ?  566 TRP A N   1 
ATOM   12451 C CA  . TRP D 1 550 ? -29.506 84.594  45.180  1.00 61.88  ?  566 TRP A CA  1 
ATOM   12452 C C   . TRP D 1 550 ? -29.831 85.715  46.160  1.00 61.03  ?  566 TRP A C   1 
ATOM   12453 O O   . TRP D 1 550 ? -30.078 85.448  47.342  1.00 60.36  ?  566 TRP A O   1 
ATOM   12454 C CB  . TRP D 1 550 ? -27.989 84.362  45.141  1.00 60.25  ?  566 TRP A CB  1 
ATOM   12455 C CG  . TRP D 1 550 ? -27.090 85.543  44.836  1.00 61.13  ?  566 TRP A CG  1 
ATOM   12456 C CD1 . TRP D 1 550 ? -26.549 85.851  43.626  1.00 63.75  ?  566 TRP A CD1 1 
ATOM   12457 C CD2 . TRP D 1 550 ? -26.610 86.540  45.744  1.00 58.36  ?  566 TRP A CD2 1 
ATOM   12458 N NE1 . TRP D 1 550 ? -25.758 86.962  43.725  1.00 61.97  ?  566 TRP A NE1 1 
ATOM   12459 C CE2 . TRP D 1 550 ? -25.789 87.408  45.014  1.00 57.84  ?  566 TRP A CE2 1 
ATOM   12460 C CE3 . TRP D 1 550 ? -26.799 86.786  47.100  1.00 61.33  ?  566 TRP A CE3 1 
ATOM   12461 C CZ2 . TRP D 1 550 ? -25.173 88.496  45.586  1.00 60.75  ?  566 TRP A CZ2 1 
ATOM   12462 C CZ3 . TRP D 1 550 ? -26.178 87.870  47.670  1.00 61.48  ?  566 TRP A CZ3 1 
ATOM   12463 C CH2 . TRP D 1 550 ? -25.376 88.708  46.918  1.00 63.91  ?  566 TRP A CH2 1 
ATOM   12464 N N   . THR D 1 551 ? -29.830 86.972  45.701  1.00 57.62  ?  567 THR A N   1 
ATOM   12465 C CA  . THR D 1 551 ? -30.166 88.087  46.591  1.00 63.20  ?  567 THR A CA  1 
ATOM   12466 C C   . THR D 1 551 ? -31.537 87.896  47.260  1.00 66.71  ?  567 THR A C   1 
ATOM   12467 O O   . THR D 1 551 ? -31.704 88.149  48.468  1.00 67.34  ?  567 THR A O   1 
ATOM   12468 C CB  . THR D 1 551 ? -30.140 89.391  45.804  1.00 68.89  ?  567 THR A CB  1 
ATOM   12469 O OG1 . THR D 1 551 ? -31.006 89.254  44.678  1.00 72.58  ?  567 THR A OG1 1 
ATOM   12470 C CG2 . THR D 1 551 ? -28.752 89.649  45.279  1.00 66.85  ?  567 THR A CG2 1 
ATOM   12471 N N   . LEU D 1 552 ? -32.527 87.416  46.489  1.00 68.53  ?  568 LEU A N   1 
ATOM   12472 C CA  . LEU D 1 552 ? -33.847 87.123  47.041  1.00 66.23  ?  568 LEU A CA  1 
ATOM   12473 C C   . LEU D 1 552 ? -33.796 85.944  48.015  1.00 63.41  ?  568 LEU A C   1 
ATOM   12474 O O   . LEU D 1 552 ? -34.445 85.968  49.074  1.00 63.72  ?  568 LEU A O   1 
ATOM   12475 C CB  . LEU D 1 552 ? -34.814 86.827  45.903  1.00 66.44  ?  568 LEU A CB  1 
ATOM   12476 C CG  . LEU D 1 552 ? -36.209 86.359  46.306  1.00 67.13  ?  568 LEU A CG  1 
ATOM   12477 C CD1 . LEU D 1 552 ? -36.855 87.336  47.292  1.00 67.06  ?  568 LEU A CD1 1 
ATOM   12478 C CD2 . LEU D 1 552 ? -37.059 86.118  45.064  1.00 66.07  ?  568 LEU A CD2 1 
ATOM   12479 N N   . ALA D 1 553 ? -33.039 84.902  47.662  1.00 58.72  ?  569 ALA A N   1 
ATOM   12480 C CA  . ALA D 1 553 ? -32.793 83.791  48.572  1.00 58.91  ?  569 ALA A CA  1 
ATOM   12481 C C   . ALA D 1 553 ? -32.282 84.278  49.925  1.00 62.45  ?  569 ALA A C   1 
ATOM   12482 O O   . ALA D 1 553 ? -32.782 83.863  50.978  1.00 66.19  ?  569 ALA A O   1 
ATOM   12483 C CB  . ALA D 1 553 ? -31.795 82.826  47.943  1.00 55.75  ?  569 ALA A CB  1 
ATOM   12484 N N   . LEU D 1 554 ? -31.287 85.162  49.919  1.00 61.69  ?  570 LEU A N   1 
ATOM   12485 C CA  . LEU D 1 554 ? -30.715 85.635  51.178  1.00 65.98  ?  570 LEU A CA  1 
ATOM   12486 C C   . LEU D 1 554 ? -31.733 86.436  51.981  1.00 65.12  ?  570 LEU A C   1 
ATOM   12487 O O   . LEU D 1 554 ? -31.812 86.312  53.218  1.00 63.73  ?  570 LEU A O   1 
ATOM   12488 C CB  . LEU D 1 554 ? -29.472 86.478  50.885  1.00 67.46  ?  570 LEU A CB  1 
ATOM   12489 C CG  . LEU D 1 554 ? -28.669 87.140  51.993  1.00 63.12  ?  570 LEU A CG  1 
ATOM   12490 C CD1 . LEU D 1 554 ? -28.346 86.103  53.015  1.00 59.67  ?  570 LEU A CD1 1 
ATOM   12491 C CD2 . LEU D 1 554 ? -27.417 87.670  51.378  1.00 65.09  ?  570 LEU A CD2 1 
ATOM   12492 N N   . GLU D 1 555 ? -32.514 87.273  51.286  1.00 63.45  ?  571 GLU A N   1 
ATOM   12493 C CA  . GLU D 1 555 ? -33.518 88.089  51.967  1.00 65.05  ?  571 GLU A CA  1 
ATOM   12494 C C   . GLU D 1 555 ? -34.575 87.230  52.654  1.00 64.47  ?  571 GLU A C   1 
ATOM   12495 O O   . GLU D 1 555 ? -35.093 87.603  53.719  1.00 62.94  ?  571 GLU A O   1 
ATOM   12496 C CB  . GLU D 1 555 ? -34.189 89.046  50.977  1.00 68.72  ?  571 GLU A CB  1 
ATOM   12497 C CG  . GLU D 1 555 ? -35.179 89.981  51.630  1.00 70.96  ?  571 GLU A CG  1 
ATOM   12498 C CD  . GLU D 1 555 ? -36.048 90.722  50.632  1.00 79.02  ?  571 GLU A CD  1 
ATOM   12499 O OE1 . GLU D 1 555 ? -36.912 90.036  50.047  1.00 82.53  ?  571 GLU A OE1 1 
ATOM   12500 O OE2 . GLU D 1 555 ? -35.921 91.962  50.460  1.00 79.64  -1 571 GLU A OE2 1 
ATOM   12501 N N   . ASN D 1 556 ? -34.902 86.077  52.068  1.00 63.52  ?  572 ASN A N   1 
ATOM   12502 C CA  . ASN D 1 556 ? -35.887 85.192  52.697  1.00 68.40  ?  572 ASN A CA  1 
ATOM   12503 C C   . ASN D 1 556 ? -35.490 84.792  54.113  1.00 63.17  ?  572 ASN A C   1 
ATOM   12504 O O   . ASN D 1 556 ? -36.363 84.490  54.944  1.00 63.41  ?  572 ASN A O   1 
ATOM   12505 C CB  . ASN D 1 556 ? -36.110 83.954  51.828  1.00 65.73  ?  572 ASN A CB  1 
ATOM   12506 C CG  . ASN D 1 556 ? -37.189 84.158  50.772  1.00 63.89  ?  572 ASN A CG  1 
ATOM   12507 O OD1 . ASN D 1 556 ? -37.541 85.282  50.413  1.00 66.63  ?  572 ASN A OD1 1 
ATOM   12508 N ND2 . ASN D 1 556 ? -37.658 83.055  50.213  1.00 59.71  ?  572 ASN A ND2 1 
ATOM   12509 N N   . VAL D 1 557 ? -34.195 84.791  54.410  1.00 60.49  ?  573 VAL A N   1 
ATOM   12510 C CA  . VAL D 1 557 ? -33.730 84.376  55.725  1.00 61.87  ?  573 VAL A CA  1 
ATOM   12511 C C   . VAL D 1 557 ? -33.432 85.589  56.589  1.00 64.64  ?  573 VAL A C   1 
ATOM   12512 O O   . VAL D 1 557 ? -33.974 85.741  57.694  1.00 65.89  ?  573 VAL A O   1 
ATOM   12513 C CB  . VAL D 1 557 ? -32.468 83.507  55.635  1.00 63.88  ?  573 VAL A CB  1 
ATOM   12514 C CG1 . VAL D 1 557 ? -32.214 82.886  56.956  1.00 65.69  ?  573 VAL A CG1 1 
ATOM   12515 C CG2 . VAL D 1 557 ? -32.603 82.439  54.608  1.00 62.53  ?  573 VAL A CG2 1 
ATOM   12516 N N   . VAL D 1 558 ? -32.551 86.468  56.096  1.00 65.94  ?  574 VAL A N   1 
ATOM   12517 C CA  . VAL D 1 558 ? -31.947 87.491  56.949  1.00 61.59  ?  574 VAL A CA  1 
ATOM   12518 C C   . VAL D 1 558 ? -32.668 88.836  56.886  1.00 65.63  ?  574 VAL A C   1 
ATOM   12519 O O   . VAL D 1 558 ? -32.449 89.690  57.761  1.00 70.53  ?  574 VAL A O   1 
ATOM   12520 C CB  . VAL D 1 558 ? -30.461 87.694  56.594  1.00 62.07  ?  574 VAL A CB  1 
ATOM   12521 C CG1 . VAL D 1 558 ? -29.750 86.331  56.463  1.00 60.67  ?  574 VAL A CG1 1 
ATOM   12522 C CG2 . VAL D 1 558 ? -30.330 88.509  55.333  1.00 64.03  ?  574 VAL A CG2 1 
ATOM   12523 N N   . GLY D 1 559 ? -33.517 89.059  55.892  1.00 69.85  ?  575 GLY A N   1 
ATOM   12524 C CA  . GLY D 1 559 ? -34.160 90.346  55.754  1.00 70.49  ?  575 GLY A CA  1 
ATOM   12525 C C   . GLY D 1 559 ? -33.296 91.397  55.108  1.00 68.31  ?  575 GLY A C   1 
ATOM   12526 O O   . GLY D 1 559 ? -33.460 92.584  55.398  1.00 71.45  ?  575 GLY A O   1 
ATOM   12527 N N   . ALA D 1 560 ? -32.364 91.000  54.248  1.00 70.76  ?  576 ALA A N   1 
ATOM   12528 C CA  . ALA D 1 560 ? -31.582 91.981  53.519  1.00 72.29  ?  576 ALA A CA  1 
ATOM   12529 C C   . ALA D 1 560 ? -31.075 91.341  52.248  1.00 75.18  ?  576 ALA A C   1 
ATOM   12530 O O   . ALA D 1 560 ? -30.826 90.139  52.205  1.00 74.75  ?  576 ALA A O   1 
ATOM   12531 C CB  . ALA D 1 560 ? -30.411 92.508  54.341  1.00 75.17  ?  576 ALA A CB  1 
ATOM   12532 N N   . LYS D 1 561 ? -30.911 92.160  51.221  1.00 82.41  ?  577 LYS A N   1 
ATOM   12533 C CA  . LYS D 1 561 ? -30.610 91.677  49.879  1.00 80.34  ?  577 LYS A CA  1 
ATOM   12534 C C   . LYS D 1 561 ? -29.124 91.565  49.576  1.00 84.24  ?  577 LYS A C   1 
ATOM   12535 O O   . LYS D 1 561 ? -28.792 91.168  48.454  1.00 80.67  ?  577 LYS A O   1 
ATOM   12536 C CB  . LYS D 1 561 ? -31.224 92.598  48.814  1.00 81.36  ?  577 LYS A CB  1 
ATOM   12537 C CG  . LYS D 1 561 ? -32.720 92.736  48.833  1.00 85.10  ?  577 LYS A CG  1 
ATOM   12538 C CD  . LYS D 1 561 ? -33.150 93.762  47.795  1.00 87.55  ?  577 LYS A CD  1 
ATOM   12539 C CE  . LYS D 1 561 ? -34.656 93.869  47.722  1.00 92.06  ?  577 LYS A CE  1 
ATOM   12540 N NZ  . LYS D 1 561 ? -35.026 95.077  46.949  1.00 102.62 ?  577 LYS A NZ  1 
ATOM   12541 N N   . ASN D 1 562 ? -28.218 91.926  50.499  1.00 87.61  ?  578 ASN A N   1 
ATOM   12542 C CA  . ASN D 1 562 ? -26.802 91.886  50.148  1.00 85.12  ?  578 ASN A CA  1 
ATOM   12543 C C   . ASN D 1 562 ? -25.942 91.389  51.306  1.00 81.81  ?  578 ASN A C   1 
ATOM   12544 O O   . ASN D 1 562 ? -26.325 91.460  52.473  1.00 78.06  ?  578 ASN A O   1 
ATOM   12545 C CB  . ASN D 1 562 ? -26.306 93.251  49.677  1.00 86.21  ?  578 ASN A CB  1 
ATOM   12546 C CG  . ASN D 1 562 ? -25.194 93.139  48.624  1.00 91.16  ?  578 ASN A CG  1 
ATOM   12547 O OD1 . ASN D 1 562 ? -24.568 92.082  48.444  1.00 88.81  ?  578 ASN A OD1 1 
ATOM   12548 N ND2 . ASN D 1 562 ? -24.962 94.234  47.907  1.00 100.71 ?  578 ASN A ND2 1 
ATOM   12549 N N   . MET D 1 563 ? -24.756 90.886  50.935  1.00 79.50  ?  579 MET A N   1 
ATOM   12550 C CA  . MET D 1 563 ? -23.728 90.377  51.844  1.00 77.23  ?  579 MET A CA  1 
ATOM   12551 C C   . MET D 1 563 ? -23.375 91.387  52.929  1.00 77.26  ?  579 MET A C   1 
ATOM   12552 O O   . MET D 1 563 ? -23.432 92.601  52.715  1.00 81.09  ?  579 MET A O   1 
ATOM   12553 C CB  . MET D 1 563 ? -22.482 90.037  51.019  1.00 78.08  ?  579 MET A CB  1 
ATOM   12554 C CG  . MET D 1 563 ? -21.386 89.257  51.719  1.00 73.52  ?  579 MET A CG  1 
ATOM   12555 S SD  . MET D 1 563 ? -20.156 88.608  50.539  1.00 70.43  ?  579 MET A SD  1 
ATOM   12556 C CE  . MET D 1 563 ? -19.639 90.084  49.672  1.00 71.46  ?  579 MET A CE  1 
ATOM   12557 N N   . ASN D 1 564 ? -22.985 90.882  54.100  1.00 78.61  ?  580 ASN A N   1 
ATOM   12558 C CA  . ASN D 1 564 ? -22.763 91.752  55.252  1.00 81.03  ?  580 ASN A CA  1 
ATOM   12559 C C   . ASN D 1 564 ? -21.779 91.095  56.208  1.00 80.93  ?  580 ASN A C   1 
ATOM   12560 O O   . ASN D 1 564 ? -21.840 89.875  56.410  1.00 79.06  ?  580 ASN A O   1 
ATOM   12561 C CB  . ASN D 1 564 ? -24.079 92.045  55.991  1.00 82.84  ?  580 ASN A CB  1 
ATOM   12562 C CG  . ASN D 1 564 ? -24.012 93.300  56.857  1.00 92.36  ?  580 ASN A CG  1 
ATOM   12563 O OD1 . ASN D 1 564 ? -23.327 93.325  57.890  1.00 93.57  ?  580 ASN A OD1 1 
ATOM   12564 N ND2 . ASN D 1 564 ? -24.737 94.348  56.443  1.00 98.95  ?  580 ASN A ND2 1 
ATOM   12565 N N   . VAL D 1 565 ? -20.885 91.889  56.797  1.00 81.42  ?  581 VAL A N   1 
ATOM   12566 C CA  . VAL D 1 565 ? -19.833 91.322  57.689  1.00 77.17  ?  581 VAL A CA  1 
ATOM   12567 C C   . VAL D 1 565 ? -20.323 91.415  59.125  1.00 74.02  ?  581 VAL A C   1 
ATOM   12568 O O   . VAL D 1 565 ? -19.968 90.540  59.917  1.00 75.15  ?  581 VAL A O   1 
ATOM   12569 C CB  . VAL D 1 565 ? -18.505 92.078  57.537  1.00 71.74  ?  581 VAL A CB  1 
ATOM   12570 C CG1 . VAL D 1 565 ? -17.628 91.467  56.457  1.00 68.57  ?  581 VAL A CG1 1 
ATOM   12571 C CG2 . VAL D 1 565 ? -18.746 93.552  57.259  1.00 77.46  ?  581 VAL A CG2 1 
ATOM   12572 N N   . ARG D 1 566 ? -21.105 92.444  59.434  1.00 83.45  ?  582 ARG A N   1 
ATOM   12573 C CA  . ARG D 1 566 ? -21.508 92.648  60.845  1.00 89.45  ?  582 ARG A CA  1 
ATOM   12574 C C   . ARG D 1 566 ? -21.755 91.290  61.501  1.00 88.17  ?  582 ARG A C   1 
ATOM   12575 O O   . ARG D 1 566 ? -21.059 90.995  62.474  1.00 86.09  ?  582 ARG A O   1 
ATOM   12576 C CB  . ARG D 1 566 ? -22.712 93.585  60.956  1.00 99.69  ?  582 ARG A CB  1 
ATOM   12577 C CG  . ARG D 1 566 ? -22.797 94.278  62.305  1.00 105.78 ?  582 ARG A CG  1 
ATOM   12578 C CD  . ARG D 1 566 ? -24.169 94.826  62.643  1.00 127.84 ?  582 ARG A CD  1 
ATOM   12579 N NE  . ARG D 1 566 ? -25.242 94.312  61.802  1.00 137.58 ?  582 ARG A NE  1 
ATOM   12580 C CZ  . ARG D 1 566 ? -25.999 93.269  62.113  1.00 122.14 ?  582 ARG A CZ  1 
ATOM   12581 N NH1 . ARG D 1 566 ? -25.791 92.619  63.246  1.00 116.69 ?  582 ARG A NH1 1 
ATOM   12582 N NH2 . ARG D 1 566 ? -26.956 92.875  61.292  1.00 121.63 ?  582 ARG A NH2 1 
ATOM   12583 N N   . PRO D 1 567 ? -22.700 90.452  61.040  1.00 80.26  ?  583 PRO A N   1 
ATOM   12584 C CA  . PRO D 1 567 ? -22.934 89.189  61.705  1.00 79.99  ?  583 PRO A CA  1 
ATOM   12585 C C   . PRO D 1 567 ? -21.608 88.569  62.162  1.00 77.22  ?  583 PRO A C   1 
ATOM   12586 O O   . PRO D 1 567 ? -21.484 88.223  63.313  1.00 71.68  ?  583 PRO A O   1 
ATOM   12587 C CB  . PRO D 1 567 ? -23.524 88.392  60.549  1.00 77.16  ?  583 PRO A CB  1 
ATOM   12588 C CG  . PRO D 1 567 ? -24.396 89.396  59.842  1.00 80.84  ?  583 PRO A CG  1 
ATOM   12589 C CD  . PRO D 1 567 ? -23.580 90.668  59.891  1.00 84.30  ?  583 PRO A CD  1 
ATOM   12590 N N   . LEU D 1 568 ? -20.650 88.458  61.244  1.00 70.38  ?  584 LEU A N   1 
ATOM   12591 C CA  . LEU D 1 568 ? -19.331 87.874  61.591  1.00 64.09  ?  584 LEU A CA  1 
ATOM   12592 C C   . LEU D 1 568 ? -18.746 88.659  62.766  1.00 61.67  ?  584 LEU A C   1 
ATOM   12593 O O   . LEU D 1 568 ? -18.591 88.069  63.843  1.00 59.04  ?  584 LEU A O   1 
ATOM   12594 C CB  . LEU D 1 568 ? -18.433 87.946  60.354  1.00 62.04  ?  584 LEU A CB  1 
ATOM   12595 C CG  . LEU D 1 568 ? -16.992 87.488  60.546  1.00 57.49  ?  584 LEU A CG  1 
ATOM   12596 C CD1 . LEU D 1 568 ? -16.928 85.987  60.767  1.00 53.43  ?  584 LEU A CD1 1 
ATOM   12597 C CD2 . LEU D 1 568 ? -16.158 87.879  59.338  1.00 59.13  ?  584 LEU A CD2 1 
ATOM   12598 N N   . LEU D 1 569 ? -18.445 89.944  62.557  1.00 63.23  ?  585 LEU A N   1 
ATOM   12599 C CA  . LEU D 1 569 ? -17.868 90.744  63.633  1.00 62.10  ?  585 LEU A CA  1 
ATOM   12600 C C   . LEU D 1 569 ? -18.650 90.583  64.921  1.00 66.17  ?  585 LEU A C   1 
ATOM   12601 O O   . LEU D 1 569 ? -18.091 90.669  66.020  1.00 71.13  ?  585 LEU A O   1 
ATOM   12602 C CB  . LEU D 1 569 ? -17.848 92.210  63.218  1.00 56.54  ?  585 LEU A CB  1 
ATOM   12603 C CG  . LEU D 1 569 ? -17.106 92.355  61.897  1.00 61.68  ?  585 LEU A CG  1 
ATOM   12604 C CD1 . LEU D 1 569 ? -16.966 93.803  61.458  1.00 65.07  ?  585 LEU A CD1 1 
ATOM   12605 C CD2 . LEU D 1 569 ? -15.761 91.685  62.010  1.00 61.64  ?  585 LEU A CD2 1 
ATOM   12606 N N   . ASN D 1 570 ? -19.938 90.342  64.802  1.00 68.07  ?  586 ASN A N   1 
ATOM   12607 C CA  . ASN D 1 570 ? -20.783 90.278  65.965  1.00 68.91  ?  586 ASN A CA  1 
ATOM   12608 C C   . ASN D 1 570 ? -20.600 88.939  66.650  1.00 60.70  ?  586 ASN A C   1 
ATOM   12609 O O   . ASN D 1 570 ? -20.676 88.854  67.873  1.00 55.33  ?  586 ASN A O   1 
ATOM   12610 C CB  . ASN D 1 570 ? -22.218 90.527  65.496  1.00 78.49  ?  586 ASN A CB  1 
ATOM   12611 C CG  . ASN D 1 570 ? -23.219 90.453  66.594  1.00 83.29  ?  586 ASN A CG  1 
ATOM   12612 O OD1 . ASN D 1 570 ? -22.874 90.539  67.774  1.00 82.43  ?  586 ASN A OD1 1 
ATOM   12613 N ND2 . ASN D 1 570 ? -24.481 90.249  66.223  1.00 81.34  ?  586 ASN A ND2 1 
ATOM   12614 N N   . TYR D 1 571 ? -20.327 87.900  65.863  1.00 62.55  ?  587 TYR A N   1 
ATOM   12615 C CA  . TYR D 1 571 ? -20.020 86.583  66.418  1.00 63.20  ?  587 TYR A CA  1 
ATOM   12616 C C   . TYR D 1 571 ? -18.778 86.658  67.282  1.00 59.58  ?  587 TYR A C   1 
ATOM   12617 O O   . TYR D 1 571 ? -18.755 86.142  68.406  1.00 55.90  ?  587 TYR A O   1 
ATOM   12618 C CB  . TYR D 1 571 ? -19.868 85.550  65.268  1.00 60.19  ?  587 TYR A CB  1 
ATOM   12619 C CG  . TYR D 1 571 ? -19.595 84.079  65.660  1.00 55.04  ?  587 TYR A CG  1 
ATOM   12620 C CD1 . TYR D 1 571 ? -18.302 83.582  65.873  1.00 49.83  ?  587 TYR A CD1 1 
ATOM   12621 C CD2 . TYR D 1 571 ? -20.653 83.220  65.912  1.00 55.62  ?  587 TYR A CD2 1 
ATOM   12622 C CE1 . TYR D 1 571 ? -18.097 82.237  66.262  1.00 49.83  ?  587 TYR A CE1 1 
ATOM   12623 C CE2 . TYR D 1 571 ? -20.447 81.900  66.317  1.00 51.54  ?  587 TYR A CE2 1 
ATOM   12624 C CZ  . TYR D 1 571 ? -19.187 81.413  66.495  1.00 49.78  ?  587 TYR A CZ  1 
ATOM   12625 O OH  . TYR D 1 571 ? -19.081 80.092  66.899  1.00 46.84  ?  587 TYR A OH  1 
ATOM   12626 N N   . PHE D 1 572 ? -17.782 87.387  66.801  1.00 57.54  ?  588 PHE A N   1 
ATOM   12627 C CA  . PHE D 1 572 ? -16.449 87.441  67.352  1.00 53.00  ?  588 PHE A CA  1 
ATOM   12628 C C   . PHE D 1 572 ? -16.245 88.631  68.252  1.00 58.84  ?  588 PHE A C   1 
ATOM   12629 O O   . PHE D 1 572 ? -15.105 88.927  68.607  1.00 63.98  ?  588 PHE A O   1 
ATOM   12630 C CB  . PHE D 1 572 ? -15.452 87.512  66.209  1.00 51.69  ?  588 PHE A CB  1 
ATOM   12631 C CG  . PHE D 1 572 ? -15.214 86.204  65.550  1.00 54.61  ?  588 PHE A CG  1 
ATOM   12632 C CD1 . PHE D 1 572 ? -14.518 85.204  66.210  1.00 52.58  ?  588 PHE A CD1 1 
ATOM   12633 C CD2 . PHE D 1 572 ? -15.788 85.934  64.303  1.00 54.14  ?  588 PHE A CD2 1 
ATOM   12634 C CE1 . PHE D 1 572 ? -14.320 83.989  65.606  1.00 51.13  ?  588 PHE A CE1 1 
ATOM   12635 C CE2 . PHE D 1 572 ? -15.608 84.722  63.699  1.00 48.37  ?  588 PHE A CE2 1 
ATOM   12636 C CZ  . PHE D 1 572 ? -14.870 83.744  64.346  1.00 48.97  ?  588 PHE A CZ  1 
ATOM   12637 N N   . GLU D 1 573 ? -17.293 89.363  68.595  1.00 61.63  ?  589 GLU A N   1 
ATOM   12638 C CA  . GLU D 1 573 ? -17.028 90.577  69.349  1.00 65.08  ?  589 GLU A CA  1 
ATOM   12639 C C   . GLU D 1 573 ? -16.415 90.313  70.716  1.00 66.20  ?  589 GLU A C   1 
ATOM   12640 O O   . GLU D 1 573 ? -15.466 91.033  71.070  1.00 71.43  ?  589 GLU A O   1 
ATOM   12641 C CB  . GLU D 1 573 ? -18.275 91.436  69.463  1.00 67.99  ?  589 GLU A CB  1 
ATOM   12642 C CG  . GLU D 1 573 ? -18.060 92.404  70.555  1.00 75.99  ?  589 GLU A CG  1 
ATOM   12643 C CD  . GLU D 1 573 ? -18.679 93.690  70.230  1.00 97.55  ?  589 GLU A CD  1 
ATOM   12644 O OE1 . GLU D 1 573 ? -19.494 93.687  69.280  1.00 108.53 ?  589 GLU A OE1 1 
ATOM   12645 O OE2 . GLU D 1 573 ? -18.283 94.702  70.849  1.00 110.79 -1 589 GLU A OE2 1 
ATOM   12646 N N   . PRO D 1 574 ? -16.862 89.336  71.515  1.00 64.06  ?  590 PRO A N   1 
ATOM   12647 C CA  . PRO D 1 574 ? -16.093 88.996  72.732  1.00 65.49  ?  590 PRO A CA  1 
ATOM   12648 C C   . PRO D 1 574 ? -14.602 88.869  72.490  1.00 63.88  ?  590 PRO A C   1 
ATOM   12649 O O   . PRO D 1 574 ? -13.772 89.477  73.188  1.00 64.83  ?  590 PRO A O   1 
ATOM   12650 C CB  . PRO D 1 574 ? -16.698 87.654  73.158  1.00 61.60  ?  590 PRO A CB  1 
ATOM   12651 C CG  . PRO D 1 574 ? -17.992 87.631  72.570  1.00 61.38  ?  590 PRO A CG  1 
ATOM   12652 C CD  . PRO D 1 574 ? -17.927 88.358  71.276  1.00 60.13  ?  590 PRO A CD  1 
ATOM   12653 N N   . LEU D 1 575 ? -14.246 88.092  71.474  1.00 60.12  ?  591 LEU A N   1 
ATOM   12654 C CA  . LEU D 1 575 ? -12.848 87.970  71.100  1.00 58.70  ?  591 LEU A CA  1 
ATOM   12655 C C   . LEU D 1 575 ? -12.271 89.317  70.688  1.00 61.18  ?  591 LEU A C   1 
ATOM   12656 O O   . LEU D 1 575 ? -11.127 89.629  71.018  1.00 62.89  ?  591 LEU A O   1 
ATOM   12657 C CB  . LEU D 1 575 ? -12.688 86.971  69.966  1.00 52.46  ?  591 LEU A CB  1 
ATOM   12658 C CG  . LEU D 1 575 ? -11.222 86.831  69.623  1.00 53.99  ?  591 LEU A CG  1 
ATOM   12659 C CD1 . LEU D 1 575 ? -10.468 86.171  70.751  1.00 57.84  ?  591 LEU A CD1 1 
ATOM   12660 C CD2 . LEU D 1 575 ? -11.101 86.073  68.391  1.00 56.27  ?  591 LEU A CD2 1 
ATOM   12661 N N   . PHE D 1 576 ? -13.046 90.137  69.974  1.00 62.39  ?  592 PHE A N   1 
ATOM   12662 C CA  . PHE D 1 576 ? -12.520 91.427  69.533  1.00 63.98  ?  592 PHE A CA  1 
ATOM   12663 C C   . PHE D 1 576 ? -12.092 92.270  70.718  1.00 65.09  ?  592 PHE A C   1 
ATOM   12664 O O   . PHE D 1 576 ? -10.973 92.789  70.751  1.00 66.00  ?  592 PHE A O   1 
ATOM   12665 C CB  . PHE D 1 576 ? -13.545 92.249  68.761  1.00 65.93  ?  592 PHE A CB  1 
ATOM   12666 C CG  . PHE D 1 576 ? -12.936 93.427  68.045  1.00 57.15  ?  592 PHE A CG  1 
ATOM   12667 C CD1 . PHE D 1 576 ? -11.642 93.373  67.599  1.00 56.92  ?  592 PHE A CD1 1 
ATOM   12668 C CD2 . PHE D 1 576 ? -13.571 94.646  68.022  1.00 58.16  ?  592 PHE A CD2 1 
ATOM   12669 C CE1 . PHE D 1 576 ? -11.058 94.455  66.956  1.00 57.32  ?  592 PHE A CE1 1 
ATOM   12670 C CE2 . PHE D 1 576 ? -12.973 95.748  67.413  1.00 56.59  ?  592 PHE A CE2 1 
ATOM   12671 C CZ  . PHE D 1 576 ? -11.717 95.648  66.872  1.00 51.56  ?  592 PHE A CZ  1 
ATOM   12672 N N   . THR D 1 577 ? -13.005 92.488  71.667  1.00 66.84  ?  593 THR A N   1 
ATOM   12673 C CA  . THR D 1 577 ? -12.685 93.391  72.763  1.00 67.55  ?  593 THR A CA  1 
ATOM   12674 C C   . THR D 1 577 ? -11.553 92.821  73.610  1.00 67.64  ?  593 THR A C   1 
ATOM   12675 O O   . THR D 1 577 ? -10.648 93.563  74.026  1.00 68.99  ?  593 THR A O   1 
ATOM   12676 C CB  . THR D 1 577 ? -13.936 93.693  73.603  1.00 65.88  ?  593 THR A CB  1 
ATOM   12677 O OG1 . THR D 1 577 ? -14.347 92.516  74.299  1.00 64.01  ?  593 THR A OG1 1 
ATOM   12678 C CG2 . THR D 1 577 ? -15.109 94.228  72.723  1.00 64.30  ?  593 THR A CG2 1 
ATOM   12679 N N   . TRP D 1 578 ? -11.543 91.493  73.815  1.00 68.96  ?  594 TRP A N   1 
ATOM   12680 C CA  . TRP D 1 578 ? -10.469 90.881  74.599  1.00 67.27  ?  594 TRP A CA  1 
ATOM   12681 C C   . TRP D 1 578 ? -9.126  91.068  73.910  1.00 66.67  ?  594 TRP A C   1 
ATOM   12682 O O   . TRP D 1 578 ? -8.159  91.475  74.543  1.00 69.08  ?  594 TRP A O   1 
ATOM   12683 C CB  . TRP D 1 578 ? -10.756 89.401  74.824  1.00 66.28  ?  594 TRP A CB  1 
ATOM   12684 C CG  . TRP D 1 578 ? -9.763  88.632  75.649  1.00 64.96  ?  594 TRP A CG  1 
ATOM   12685 C CD1 . TRP D 1 578 ? -9.776  88.476  77.005  1.00 66.67  ?  594 TRP A CD1 1 
ATOM   12686 C CD2 . TRP D 1 578 ? -8.642  87.886  75.177  1.00 64.77  ?  594 TRP A CD2 1 
ATOM   12687 N NE1 . TRP D 1 578 ? -8.731  87.679  77.402  1.00 66.22  ?  594 TRP A NE1 1 
ATOM   12688 C CE2 . TRP D 1 578 ? -8.022  87.304  76.298  1.00 62.18  ?  594 TRP A CE2 1 
ATOM   12689 C CE3 . TRP D 1 578 ? -8.100  87.654  73.915  1.00 66.34  ?  594 TRP A CE3 1 
ATOM   12690 C CZ2 . TRP D 1 578 ? -6.895  86.522  76.197  1.00 62.18  ?  594 TRP A CZ2 1 
ATOM   12691 C CZ3 . TRP D 1 578 ? -6.970  86.863  73.819  1.00 64.51  ?  594 TRP A CZ3 1 
ATOM   12692 C CH2 . TRP D 1 578 ? -6.380  86.313  74.952  1.00 62.88  ?  594 TRP A CH2 1 
ATOM   12693 N N   . LEU D 1 579 ? -9.049  90.780  72.612  1.00 63.96  ?  595 LEU A N   1 
ATOM   12694 C CA  . LEU D 1 579 ? -7.830  91.043  71.849  1.00 65.27  ?  595 LEU A CA  1 
ATOM   12695 C C   . LEU D 1 579 ? -7.388  92.481  71.986  1.00 68.89  ?  595 LEU A C   1 
ATOM   12696 O O   . LEU D 1 579 ? -6.203  92.761  72.199  1.00 79.72  ?  595 LEU A O   1 
ATOM   12697 C CB  . LEU D 1 579 ? -8.024  90.775  70.360  1.00 61.53  ?  595 LEU A CB  1 
ATOM   12698 C CG  . LEU D 1 579 ? -8.080  89.338  69.950  1.00 62.59  ?  595 LEU A CG  1 
ATOM   12699 C CD1 . LEU D 1 579 ? -8.386  89.302  68.487  1.00 62.00  ?  595 LEU A CD1 1 
ATOM   12700 C CD2 . LEU D 1 579 ? -6.762  88.727  70.280  1.00 63.21  ?  595 LEU A CD2 1 
ATOM   12701 N N   . LYS D 1 580 ? -8.298  93.411  71.722  1.00 68.21  ?  596 LYS A N   1 
ATOM   12702 C CA  . LYS D 1 580 ? -7.933  94.810  71.808  1.00 68.97  ?  596 LYS A CA  1 
ATOM   12703 C C   . LYS D 1 580 ? -7.260  95.066  73.139  1.00 80.45  ?  596 LYS A C   1 
ATOM   12704 O O   . LYS D 1 580 ? -6.199  95.697  73.210  1.00 84.08  ?  596 LYS A O   1 
ATOM   12705 C CB  . LYS D 1 580 ? -9.171  95.672  71.671  1.00 69.10  ?  596 LYS A CB  1 
ATOM   12706 C CG  . LYS D 1 580 ? -9.313  96.311  70.352  1.00 65.46  ?  596 LYS A CG  1 
ATOM   12707 C CD  . LYS D 1 580 ? -10.770 96.232  69.962  1.00 63.42  ?  596 LYS A CD  1 
ATOM   12708 C CE  . LYS D 1 580 ? -11.689 96.946  70.936  1.00 63.27  ?  596 LYS A CE  1 
ATOM   12709 N NZ  . LYS D 1 580 ? -13.101 96.712  70.570  1.00 65.87  ?  596 LYS A NZ  1 
ATOM   12710 N N   . ASP D 1 581 ? -7.844  94.521  74.206  1.00 87.38  ?  597 ASP A N   1 
ATOM   12711 C CA  . ASP D 1 581 ? -7.251  94.664  75.525  1.00 92.35  ?  597 ASP A CA  1 
ATOM   12712 C C   . ASP D 1 581 ? -5.851  94.061  75.580  1.00 98.35  ?  597 ASP A C   1 
ATOM   12713 O O   . ASP D 1 581 ? -4.912  94.696  76.055  1.00 105.83 ?  597 ASP A O   1 
ATOM   12714 C CB  . ASP D 1 581 ? -8.146  94.005  76.553  1.00 95.16  ?  597 ASP A CB  1 
ATOM   12715 C CG  . ASP D 1 581 ? -7.566  94.087  77.910  1.00 110.64 ?  597 ASP A CG  1 
ATOM   12716 O OD1 . ASP D 1 581 ? -6.774  93.170  78.267  1.00 107.19 ?  597 ASP A OD1 1 
ATOM   12717 O OD2 . ASP D 1 581 ? -7.891  95.076  78.601  1.00 123.36 -1 597 ASP A OD2 1 
ATOM   12718 N N   . GLN D 1 582 ? -5.701  92.824  75.117  1.00 81.86  ?  598 GLN A N   1 
ATOM   12719 C CA  . GLN D 1 582 ? -4.425  92.124  75.226  1.00 74.73  ?  598 GLN A CA  1 
ATOM   12720 C C   . GLN D 1 582 ? -3.331  92.883  74.506  1.00 80.92  ?  598 GLN A C   1 
ATOM   12721 O O   . GLN D 1 582 ? -2.181  92.920  74.971  1.00 87.46  ?  598 GLN A O   1 
ATOM   12722 C CB  . GLN D 1 582 ? -4.517  90.717  74.631  1.00 68.44  ?  598 GLN A CB  1 
ATOM   12723 C CG  . GLN D 1 582 ? -5.244  89.670  75.496  1.00 72.70  ?  598 GLN A CG  1 
ATOM   12724 C CD  . GLN D 1 582 ? -4.567  89.312  76.809  1.00 73.94  ?  598 GLN A CD  1 
ATOM   12725 O OE1 . GLN D 1 582 ? -3.395  88.914  76.846  1.00 74.30  ?  598 GLN A OE1 1 
ATOM   12726 N NE2 . GLN D 1 582 ? -5.298  89.507  77.910  1.00 75.14  ?  598 GLN A NE2 1 
ATOM   12727 N N   . ASN D 1 583 ? -3.663  93.493  73.368  1.00 79.08  ?  599 ASN A N   1 
ATOM   12728 C CA  . ASN D 1 583 ? -2.651  94.149  72.541  1.00 81.38  ?  599 ASN A CA  1 
ATOM   12729 C C   . ASN D 1 583 ? -2.260  95.550  73.051  1.00 81.61  ?  599 ASN A C   1 
ATOM   12730 O O   . ASN D 1 583 ? -1.552  96.268  72.339  1.00 81.56  ?  599 ASN A O   1 
ATOM   12731 C CB  . ASN D 1 583 ? -3.114  94.283  71.081  1.00 76.38  ?  599 ASN A CB  1 
ATOM   12732 C CG  . ASN D 1 583 ? -3.219  92.947  70.345  1.00 71.45  ?  599 ASN A CG  1 
ATOM   12733 O OD1 . ASN D 1 583 ? -2.661  91.926  70.751  1.00 71.76  ?  599 ASN A OD1 1 
ATOM   12734 N ND2 . ASN D 1 583 ? -3.845  92.993  69.190  1.00 69.48  ?  599 ASN A ND2 1 
ATOM   12735 N N   . LYS D 1 584 ? -2.696  95.936  74.255  1.00 85.52  ?  600 LYS A N   1 
ATOM   12736 C CA  . LYS D 1 584 ? -2.377  97.246  74.797  1.00 79.94  ?  600 LYS A CA  1 
ATOM   12737 C C   . LYS D 1 584 ? -0.876  97.525  74.826  1.00 88.74  ?  600 LYS A C   1 
ATOM   12738 O O   . LYS D 1 584 ? -0.459  98.683  74.713  1.00 85.15  ?  600 LYS A O   1 
ATOM   12739 C CB  . LYS D 1 584 ? -3.002  97.375  76.185  1.00 84.85  ?  600 LYS A CB  1 
ATOM   12740 C CG  . LYS D 1 584 ? -2.540  96.360  77.247  1.00 87.38  ?  600 LYS A CG  1 
ATOM   12741 C CD  . LYS D 1 584 ? -3.529  96.400  78.438  1.00 97.00  ?  600 LYS A CD  1 
ATOM   12742 C CE  . LYS D 1 584 ? -3.316  95.312  79.503  1.00 100.13 ?  600 LYS A CE  1 
ATOM   12743 N NZ  . LYS D 1 584 ? -3.271  93.935  78.916  1.00 98.84  ?  600 LYS A NZ  1 
ATOM   12744 N N   . ASN D 1 585 ? -0.046  96.487  74.955  1.00 88.60  ?  601 ASN A N   1 
ATOM   12745 C CA  . ASN D 1 585 ? 1.404   96.660  74.976  1.00 87.61  ?  601 ASN A CA  1 
ATOM   12746 C C   . ASN D 1 585 ? 2.054   96.093  73.724  1.00 85.45  ?  601 ASN A C   1 
ATOM   12747 O O   . ASN D 1 585 ? 3.209   95.667  73.756  1.00 89.71  ?  601 ASN A O   1 
ATOM   12748 C CB  . ASN D 1 585 ? 2.030   96.012  76.210  1.00 95.90  ?  601 ASN A CB  1 
ATOM   12749 C CG  . ASN D 1 585 ? 1.565   96.643  77.503  1.00 95.62  ?  601 ASN A CG  1 
ATOM   12750 O OD1 . ASN D 1 585 ? 1.264   97.845  77.563  1.00 93.86  ?  601 ASN A OD1 1 
ATOM   12751 N ND2 . ASN D 1 585 ? 1.539   95.842  78.563  1.00 99.16  ?  601 ASN A ND2 1 
ATOM   12752 N N   . SER D 1 586 ? 1.315   96.059  72.624  1.00 82.78  ?  602 SER A N   1 
ATOM   12753 C CA  . SER D 1 586 ? 1.805   95.497  71.381  1.00 76.10  ?  602 SER A CA  1 
ATOM   12754 C C   . SER D 1 586 ? 1.606   96.519  70.272  1.00 70.27  ?  602 SER A C   1 
ATOM   12755 O O   . SER D 1 586 ? 0.681   97.340  70.315  1.00 70.67  ?  602 SER A O   1 
ATOM   12756 C CB  . SER D 1 586 ? 1.061   94.200  71.014  1.00 75.71  ?  602 SER A CB  1 
ATOM   12757 O OG  . SER D 1 586 ? 1.166   93.208  72.014  1.00 75.73  ?  602 SER A OG  1 
ATOM   12758 N N   . PHE D 1 587 ? 2.462   96.469  69.269  1.00 66.08  ?  603 PHE A N   1 
ATOM   12759 C CA  . PHE D 1 587 ? 2.154   97.174  68.043  1.00 63.92  ?  603 PHE A CA  1 
ATOM   12760 C C   . PHE D 1 587 ? 1.147   96.376  67.239  1.00 68.91  ?  603 PHE A C   1 
ATOM   12761 O O   . PHE D 1 587 ? 1.283   95.157  67.082  1.00 74.01  ?  603 PHE A O   1 
ATOM   12762 C CB  . PHE D 1 587 ? 3.418   97.477  67.243  1.00 63.32  ?  603 PHE A CB  1 
ATOM   12763 C CG  . PHE D 1 587 ? 3.150   98.255  65.984  1.00 66.93  ?  603 PHE A CG  1 
ATOM   12764 C CD1 . PHE D 1 587 ? 2.808   99.595  66.033  1.00 64.05  ?  603 PHE A CD1 1 
ATOM   12765 C CD2 . PHE D 1 587 ? 3.357   97.671  64.738  1.00 69.28  ?  603 PHE A CD2 1 
ATOM   12766 C CE1 . PHE D 1 587 ? 2.571   100.314 64.863  1.00 59.60  ?  603 PHE A CE1 1 
ATOM   12767 C CE2 . PHE D 1 587 ? 3.142   98.385  63.578  1.00 63.94  ?  603 PHE A CE2 1 
ATOM   12768 C CZ  . PHE D 1 587 ? 2.754   99.706  63.637  1.00 60.13  ?  603 PHE A CZ  1 
ATOM   12769 N N   . VAL D 1 588 ? 0.125   97.062  66.752  1.00 68.52  ?  604 VAL A N   1 
ATOM   12770 C CA  . VAL D 1 588 ? -0.929  96.453  65.956  1.00 65.91  ?  604 VAL A CA  1 
ATOM   12771 C C   . VAL D 1 588 ? -0.807  96.989  64.545  1.00 66.61  ?  604 VAL A C   1 
ATOM   12772 O O   . VAL D 1 588 ? -1.056  98.176  64.296  1.00 63.15  ?  604 VAL A O   1 
ATOM   12773 C CB  . VAL D 1 588 ? -2.308  96.769  66.525  1.00 67.32  ?  604 VAL A CB  1 
ATOM   12774 C CG1 . VAL D 1 588 ? -3.373  96.295  65.556  1.00 72.04  ?  604 VAL A CG1 1 
ATOM   12775 C CG2 . VAL D 1 588 ? -2.453  96.119  67.867  1.00 69.30  ?  604 VAL A CG2 1 
ATOM   12776 N N   . GLY D 1 589 ? -0.457  96.117  63.613  1.00 67.92  ?  605 GLY A N   1 
ATOM   12777 C CA  . GLY D 1 589 ? -0.187  96.536  62.258  1.00 67.69  ?  605 GLY A CA  1 
ATOM   12778 C C   . GLY D 1 589 ? 1.061   95.868  61.767  1.00 65.84  ?  605 GLY A C   1 
ATOM   12779 O O   . GLY D 1 589 ? 1.603   94.975  62.420  1.00 67.39  ?  605 GLY A O   1 
ATOM   12780 N N   . TRP D 1 590 ? 1.527   96.298  60.592  1.00 67.60  ?  606 TRP A N   1 
ATOM   12781 C CA  . TRP D 1 590 ? 2.780   95.775  60.059  1.00 69.81  ?  606 TRP A CA  1 
ATOM   12782 C C   . TRP D 1 590 ? 3.377   96.725  59.034  1.00 72.15  ?  606 TRP A C   1 
ATOM   12783 O O   . TRP D 1 590 ? 2.671   97.219  58.157  1.00 73.97  ?  606 TRP A O   1 
ATOM   12784 C CB  . TRP D 1 590 ? 2.573   94.412  59.408  1.00 70.68  ?  606 TRP A CB  1 
ATOM   12785 C CG  . TRP D 1 590 ? 1.466   94.345  58.414  1.00 70.60  ?  606 TRP A CG  1 
ATOM   12786 C CD1 . TRP D 1 590 ? 1.541   94.618  57.075  1.00 70.34  ?  606 TRP A CD1 1 
ATOM   12787 C CD2 . TRP D 1 590 ? 0.121   93.957  58.667  1.00 67.89  ?  606 TRP A CD2 1 
ATOM   12788 N NE1 . TRP D 1 590 ? 0.324   94.411  56.483  1.00 71.11  ?  606 TRP A NE1 1 
ATOM   12789 C CE2 . TRP D 1 590 ? -0.566  94.010  57.444  1.00 67.32  ?  606 TRP A CE2 1 
ATOM   12790 C CE3 . TRP D 1 590 ? -0.571  93.562  59.812  1.00 67.63  ?  606 TRP A CE3 1 
ATOM   12791 C CZ2 . TRP D 1 590 ? -1.899  93.685  57.340  1.00 66.27  ?  606 TRP A CZ2 1 
ATOM   12792 C CZ3 . TRP D 1 590 ? -1.888  93.252  59.707  1.00 64.36  ?  606 TRP A CZ3 1 
ATOM   12793 C CH2 . TRP D 1 590 ? -2.543  93.314  58.487  1.00 66.33  ?  606 TRP A CH2 1 
ATOM   12794 N N   . SER D 1 591 ? 4.682   96.945  59.116  1.00 73.04  ?  607 SER A N   1 
ATOM   12795 C CA  . SER D 1 591 ? 5.340   97.594  57.998  1.00 80.11  ?  607 SER A CA  1 
ATOM   12796 C C   . SER D 1 591 ? 5.668   96.551  56.935  1.00 82.34  ?  607 SER A C   1 
ATOM   12797 O O   . SER D 1 591 ? 5.933   95.384  57.233  1.00 82.68  ?  607 SER A O   1 
ATOM   12798 C CB  . SER D 1 591 ? 6.599   98.338  58.447  1.00 83.84  ?  607 SER A CB  1 
ATOM   12799 O OG  . SER D 1 591 ? 7.737   97.496  58.478  1.00 87.56  ?  607 SER A OG  1 
ATOM   12800 N N   . THR D 1 592 ? 5.640   96.980  55.685  1.00 81.63  ?  608 THR A N   1 
ATOM   12801 C CA  . THR D 1 592 ? 5.629   96.048  54.575  1.00 88.48  ?  608 THR A CA  1 
ATOM   12802 C C   . THR D 1 592 ? 7.010   95.636  54.114  1.00 93.70  ?  608 THR A C   1 
ATOM   12803 O O   . THR D 1 592 ? 7.108   94.948  53.091  1.00 94.69  ?  608 THR A O   1 
ATOM   12804 C CB  . THR D 1 592 ? 4.893   96.660  53.400  1.00 85.92  ?  608 THR A CB  1 
ATOM   12805 O OG1 . THR D 1 592 ? 5.591   97.839  52.998  1.00 88.59  ?  608 THR A OG1 1 
ATOM   12806 C CG2 . THR D 1 592 ? 3.498   97.046  53.809  1.00 83.35  ?  608 THR A CG2 1 
ATOM   12807 N N   . ASP D 1 593 ? 8.078   96.031  54.830  1.00 108.67 ?  609 ASP A N   1 
ATOM   12808 C CA  . ASP D 1 593 ? 9.442   95.833  54.347  1.00 111.58 ?  609 ASP A CA  1 
ATOM   12809 C C   . ASP D 1 593 ? 10.359  95.011  55.255  1.00 106.88 ?  609 ASP A C   1 
ATOM   12810 O O   . ASP D 1 593 ? 11.358  94.487  54.754  1.00 110.41 ?  609 ASP A O   1 
ATOM   12811 C CB  . ASP D 1 593 ? 10.103  97.189  54.069  1.00 115.83 ?  609 ASP A CB  1 
ATOM   12812 C CG  . ASP D 1 593 ? 10.112  98.069  55.283  1.00 127.90 ?  609 ASP A CG  1 
ATOM   12813 O OD1 . ASP D 1 593 ? 9.055   98.162  55.941  1.00 128.37 ?  609 ASP A OD1 1 
ATOM   12814 O OD2 . ASP D 1 593 ? 11.183  98.630  55.609  1.00 142.20 -1 609 ASP A OD2 1 
ATOM   12815 N N   . TRP D 1 594 ? 10.070  94.877  56.552  1.00 91.15  ?  610 TRP A N   1 
ATOM   12816 C CA  . TRP D 1 594 ? 10.813  93.905  57.342  1.00 85.94  ?  610 TRP A CA  1 
ATOM   12817 C C   . TRP D 1 594 ? 10.702  92.542  56.708  1.00 91.48  ?  610 TRP A C   1 
ATOM   12818 O O   . TRP D 1 594 ? 9.600   92.092  56.401  1.00 97.09  ?  610 TRP A O   1 
ATOM   12819 C CB  . TRP D 1 594 ? 10.301  93.805  58.770  1.00 84.39  ?  610 TRP A CB  1 
ATOM   12820 C CG  . TRP D 1 594 ? 11.047  92.737  59.553  1.00 84.80  ?  610 TRP A CG  1 
ATOM   12821 C CD1 . TRP D 1 594 ? 12.214  92.887  60.255  1.00 85.92  ?  610 TRP A CD1 1 
ATOM   12822 C CD2 . TRP D 1 594 ? 10.684  91.362  59.684  1.00 83.39  ?  610 TRP A CD2 1 
ATOM   12823 N NE1 . TRP D 1 594 ? 12.593  91.692  60.815  1.00 87.43  ?  610 TRP A NE1 1 
ATOM   12824 C CE2 . TRP D 1 594 ? 11.663  90.741  60.480  1.00 86.58  ?  610 TRP A CE2 1 
ATOM   12825 C CE3 . TRP D 1 594 ? 9.624   90.600  59.218  1.00 84.18  ?  610 TRP A CE3 1 
ATOM   12826 C CZ2 . TRP D 1 594 ? 11.600  89.392  60.819  1.00 87.91  ?  610 TRP A CZ2 1 
ATOM   12827 C CZ3 . TRP D 1 594 ? 9.574   89.275  59.547  1.00 85.16  ?  610 TRP A CZ3 1 
ATOM   12828 C CH2 . TRP D 1 594 ? 10.555  88.679  60.342  1.00 81.36  ?  610 TRP A CH2 1 
ATOM   12829 N N   . SER D 1 595 ? 11.833  91.871  56.523  1.00 87.44  ?  611 SER A N   1 
ATOM   12830 C CA  . SER D 1 595 ? 11.721  90.548  55.948  1.00 91.73  ?  611 SER A CA  1 
ATOM   12831 C C   . SER D 1 595 ? 12.811  89.686  56.551  1.00 93.59  ?  611 SER A C   1 
ATOM   12832 O O   . SER D 1 595 ? 13.889  90.206  56.862  1.00 95.81  ?  611 SER A O   1 
ATOM   12833 C CB  . SER D 1 595 ? 11.808  90.591  54.410  1.00 92.69  ?  611 SER A CB  1 
ATOM   12834 O OG  . SER D 1 595 ? 13.125  90.477  53.924  1.00 96.24  ?  611 SER A OG  1 
ATOM   12835 N N   . PRO D 1 596 ? 12.566  88.395  56.759  1.00 101.59 ?  612 PRO A N   1 
ATOM   12836 C CA  . PRO D 1 596 ? 13.563  87.576  57.470  1.00 107.81 ?  612 PRO A CA  1 
ATOM   12837 C C   . PRO D 1 596 ? 14.935  87.528  56.798  1.00 113.72 ?  612 PRO A C   1 
ATOM   12838 O O   . PRO D 1 596 ? 15.942  87.333  57.497  1.00 117.53 ?  612 PRO A O   1 
ATOM   12839 C CB  . PRO D 1 596 ? 12.906  86.184  57.514  1.00 96.96  ?  612 PRO A CB  1 
ATOM   12840 C CG  . PRO D 1 596 ? 11.454  86.466  57.390  1.00 92.79  ?  612 PRO A CG  1 
ATOM   12841 C CD  . PRO D 1 596 ? 11.352  87.624  56.440  1.00 90.42  ?  612 PRO A CD  1 
ATOM   12842 N N   . TYR D 1 597 ? 15.013  87.714  55.478  1.00 99.27  ?  613 TYR A N   1 
ATOM   12843 C CA  . TYR D 1 597 ? 16.274  87.584  54.762  1.00 100.12 ?  613 TYR A CA  1 
ATOM   12844 C C   . TYR D 1 597 ? 16.977  88.919  54.540  1.00 114.39 ?  613 TYR A C   1 
ATOM   12845 O O   . TYR D 1 597 ? 18.133  88.926  54.109  1.00 128.34 ?  613 TYR A O   1 
ATOM   12846 C CB  . TYR D 1 597 ? 16.055  86.917  53.400  1.00 93.26  ?  613 TYR A CB  1 
ATOM   12847 C CG  . TYR D 1 597 ? 15.038  87.621  52.533  1.00 93.36  ?  613 TYR A CG  1 
ATOM   12848 C CD1 . TYR D 1 597 ? 15.427  88.655  51.708  1.00 97.87  ?  613 TYR A CD1 1 
ATOM   12849 C CD2 . TYR D 1 597 ? 13.698  87.239  52.506  1.00 89.85  ?  613 TYR A CD2 1 
ATOM   12850 C CE1 . TYR D 1 597 ? 14.515  89.314  50.899  1.00 94.38  ?  613 TYR A CE1 1 
ATOM   12851 C CE2 . TYR D 1 597 ? 12.772  87.903  51.680  1.00 84.29  ?  613 TYR A CE2 1 
ATOM   12852 C CZ  . TYR D 1 597 ? 13.199  88.937  50.887  1.00 83.88  ?  613 TYR A CZ  1 
ATOM   12853 O OH  . TYR D 1 597 ? 12.331  89.612  50.077  1.00 86.69  ?  613 TYR A OH  1 
ATOM   12854 N N   . ALA D 1 598 ? 16.313  90.037  54.795  1.00 104.43 ?  614 ALA A N   1 
ATOM   12855 C CA  . ALA D 1 598 ? 16.931  91.341  54.628  1.00 100.57 ?  614 ALA A CA  1 
ATOM   12856 C C   . ALA D 1 598 ? 17.589  91.777  55.916  1.00 97.19  ?  614 ALA A C   1 
ATOM   12857 O O   . ALA D 1 598 ? 16.900  92.259  56.814  1.00 99.18  ?  614 ALA A O   1 
ATOM   12858 C CB  . ALA D 1 598 ? 15.912  92.352  54.213  1.00 96.75  ?  614 ALA A CB  1 
HETATM 12859 C C1  . NAG E 3 .   ? -10.404 53.895  109.594 1.00 81.26  ?  1   NAG E C1  1 
HETATM 12860 C C2  . NAG E 3 .   ? -11.400 53.212  110.511 1.00 80.42  ?  1   NAG E C2  1 
HETATM 12861 C C3  . NAG E 3 .   ? -12.165 52.122  109.760 1.00 82.53  ?  1   NAG E C3  1 
HETATM 12862 C C4  . NAG E 3 .   ? -12.746 52.654  108.452 1.00 85.71  ?  1   NAG E C4  1 
HETATM 12863 C C5  . NAG E 3 .   ? -11.707 53.399  107.617 1.00 81.95  ?  1   NAG E C5  1 
HETATM 12864 C C6  . NAG E 3 .   ? -12.279 54.073  106.387 1.00 83.41  ?  1   NAG E C6  1 
HETATM 12865 C C7  . NAG E 3 .   ? -10.877 53.191  112.886 1.00 79.22  ?  1   NAG E C7  1 
HETATM 12866 C C8  . NAG E 3 .   ? -10.090 52.545  113.991 1.00 82.23  ?  1   NAG E C8  1 
HETATM 12867 N N2  . NAG E 3 .   ? -10.722 52.666  111.671 1.00 79.99  ?  1   NAG E N2  1 
HETATM 12868 O O3  . NAG E 3 .   ? -13.239 51.690  110.591 1.00 85.00  ?  1   NAG E O3  1 
HETATM 12869 O O4  . NAG E 3 .   ? -13.244 51.579  107.672 1.00 90.78  ?  1   NAG E O4  1 
HETATM 12870 O O5  . NAG E 3 .   ? -11.106 54.427  108.413 1.00 84.13  ?  1   NAG E O5  1 
HETATM 12871 O O6  . NAG E 3 .   ? -13.453 54.828  106.675 1.00 94.32  ?  1   NAG E O6  1 
HETATM 12872 O O7  . NAG E 3 .   ? -11.628 54.137  113.085 1.00 73.24  ?  1   NAG E O7  1 
HETATM 12873 C C1  . NAG E 3 .   ? -14.655 51.660  107.852 1.00 98.19  ?  2   NAG E C1  1 
HETATM 12874 C C2  . NAG E 3 .   ? -15.327 51.142  106.594 1.00 98.13  ?  2   NAG E C2  1 
HETATM 12875 C C3  . NAG E 3 .   ? -16.836 51.274  106.726 1.00 100.96 ?  2   NAG E C3  1 
HETATM 12876 C C4  . NAG E 3 .   ? -17.312 50.538  107.980 1.00 107.86 ?  2   NAG E C4  1 
HETATM 12877 C C5  . NAG E 3 .   ? -16.514 50.998  109.224 1.00 107.36 ?  2   NAG E C5  1 
HETATM 12878 C C6  . NAG E 3 .   ? -16.840 50.267  110.524 1.00 103.45 ?  2   NAG E C6  1 
HETATM 12879 C C7  . NAG E 3 .   ? -14.089 51.247  104.476 1.00 94.27  ?  2   NAG E C7  1 
HETATM 12880 C C8  . NAG E 3 .   ? -13.770 52.080  103.265 1.00 98.12  ?  2   NAG E C8  1 
HETATM 12881 N N2  . NAG E 3 .   ? -14.868 51.826  105.395 1.00 97.28  ?  2   NAG E N2  1 
HETATM 12882 O O3  . NAG E 3 .   ? -17.418 50.740  105.536 1.00 101.62 ?  2   NAG E O3  1 
HETATM 12883 O O4  . NAG E 3 .   ? -18.703 50.784  108.182 1.00 108.03 ?  2   NAG E O4  1 
HETATM 12884 O O5  . NAG E 3 .   ? -15.097 50.881  109.000 1.00 102.16 ?  2   NAG E O5  1 
HETATM 12885 O O6  . NAG E 3 .   ? -16.394 48.912  110.586 1.00 94.21  ?  2   NAG E O6  1 
HETATM 12886 O O7  . NAG E 3 .   ? -13.651 50.108  104.620 1.00 86.97  ?  2   NAG E O7  1 
HETATM 12887 C C1  . BMA E 3 .   ? -19.549 49.785  107.503 1.00 103.93 ?  3   BMA E C1  1 
HETATM 12888 C C2  . BMA E 3 .   ? -20.892 50.456  106.899 1.00 96.09  ?  3   BMA E C2  1 
HETATM 12889 C C3  . BMA E 3 .   ? -21.750 49.378  106.238 1.00 94.51  ?  3   BMA E C3  1 
HETATM 12890 C C4  . BMA E 3 .   ? -20.859 48.559  105.120 1.00 96.46  ?  3   BMA E C4  1 
HETATM 12891 C C5  . BMA E 3 .   ? -19.512 47.943  105.743 1.00 103.66 ?  3   BMA E C5  1 
HETATM 12892 C C6  . BMA E 3 .   ? -18.542 47.194  104.715 1.00 100.63 ?  3   BMA E C6  1 
HETATM 12893 O O2  . BMA E 3 .   ? -20.599 51.498  105.921 1.00 89.10  ?  3   BMA E O2  1 
HETATM 12894 O O3  . BMA E 3 .   ? -23.077 49.943  105.794 1.00 92.89  ?  3   BMA E O3  1 
HETATM 12895 O O4  . BMA E 3 .   ? -21.592 47.489  104.372 1.00 91.23  ?  3   BMA E O4  1 
HETATM 12896 O O5  . BMA E 3 .   ? -18.759 48.947  106.539 1.00 105.79 ?  3   BMA E O5  1 
HETATM 12897 O O6  . BMA E 3 .   ? -19.232 46.081  104.014 1.00 94.82  ?  3   BMA E O6  1 
HETATM 12898 C C1  . NAG F 3 .   ? 12.023  60.592  102.621 1.00 105.30 ?  1   NAG F C1  1 
HETATM 12899 C C2  . NAG F 3 .   ? 12.153  61.938  101.817 1.00 105.53 ?  1   NAG F C2  1 
HETATM 12900 C C3  . NAG F 3 .   ? 11.992  63.181  102.711 1.00 101.87 ?  1   NAG F C3  1 
HETATM 12901 C C4  . NAG F 3 .   ? 10.842  63.055  103.706 1.00 98.54  ?  1   NAG F C4  1 
HETATM 12902 C C5  . NAG F 3 .   ? 11.013  61.753  104.484 1.00 99.81  ?  1   NAG F C5  1 
HETATM 12903 C C6  . NAG F 3 .   ? 9.985   61.525  105.565 1.00 103.51 ?  1   NAG F C6  1 
HETATM 12904 C C7  . NAG F 3 .   ? 13.644  62.020  99.815  1.00 124.85 ?  1   NAG F C7  1 
HETATM 12905 C C8  . NAG F 3 .   ? 15.082  62.035  99.372  1.00 128.19 ?  1   NAG F C8  1 
HETATM 12906 N N2  . NAG F 3 .   ? 13.447  61.985  101.143 1.00 121.45 ?  1   NAG F N2  1 
HETATM 12907 O O3  . NAG F 3 .   ? 11.762  64.249  101.803 1.00 95.89  ?  1   NAG F O3  1 
HETATM 12908 O O4  . NAG F 3 .   ? 10.725  64.179  104.588 1.00 102.69 ?  1   NAG F O4  1 
HETATM 12909 O O5  . NAG F 3 .   ? 10.914  60.667  103.554 1.00 92.75  ?  1   NAG F O5  1 
HETATM 12910 O O6  . NAG F 3 .   ? 8.679   61.308  105.038 1.00 110.18 ?  1   NAG F O6  1 
HETATM 12911 O O7  . NAG F 3 .   ? 12.711  62.024  99.003  1.00 121.52 ?  1   NAG F O7  1 
HETATM 12912 C C1  . NAG F 3 .   ? 11.402  65.471  104.284 1.00 107.76 ?  2   NAG F C1  1 
HETATM 12913 C C2  . NAG F 3 .   ? 10.339  66.469  103.755 1.00 111.96 ?  2   NAG F C2  1 
HETATM 12914 C C3  . NAG F 3 .   ? 10.919  67.845  103.455 1.00 108.62 ?  2   NAG F C3  1 
HETATM 12915 C C4  . NAG F 3 .   ? 11.741  68.363  104.614 1.00 103.55 ?  2   NAG F C4  1 
HETATM 12916 C C5  . NAG F 3 .   ? 12.802  67.317  104.984 1.00 107.47 ?  2   NAG F C5  1 
HETATM 12917 C C6  . NAG F 3 .   ? 13.761  67.723  106.094 1.00 106.72 ?  2   NAG F C6  1 
HETATM 12918 C C7  . NAG F 3 .   ? 8.600   65.165  102.710 1.00 116.03 ?  2   NAG F C7  1 
HETATM 12919 C C8  . NAG F 3 .   ? 7.958   64.715  101.430 1.00 117.08 ?  2   NAG F C8  1 
HETATM 12920 N N2  . NAG F 3 .   ? 9.651   65.968  102.582 1.00 112.28 ?  2   NAG F N2  1 
HETATM 12921 O O3  . NAG F 3 .   ? 9.853   68.771  103.238 1.00 107.89 ?  2   NAG F O3  1 
HETATM 12922 O O4  . NAG F 3 .   ? 12.281  69.581  104.104 1.00 104.16 ?  2   NAG F O4  1 
HETATM 12923 O O5  . NAG F 3 .   ? 12.167  66.083  105.367 1.00 111.08 ?  2   NAG F O5  1 
HETATM 12924 O O6  . NAG F 3 .   ? 13.169  67.815  107.385 1.00 106.80 ?  2   NAG F O6  1 
HETATM 12925 O O7  . NAG F 3 .   ? 8.208   64.786  103.823 1.00 116.32 ?  2   NAG F O7  1 
HETATM 12926 C C1  . BMA F 3 .   ? 12.093  70.822  104.824 1.00 101.01 ?  3   BMA F C1  1 
HETATM 12927 C C2  . BMA F 3 .   ? 10.671  70.891  105.608 1.00 95.17  ?  3   BMA F C2  1 
HETATM 12928 C C3  . BMA F 3 .   ? 10.547  72.260  106.271 1.00 95.23  ?  3   BMA F C3  1 
HETATM 12929 C C4  . BMA F 3 .   ? 11.818  72.433  107.241 1.00 100.23 ?  3   BMA F C4  1 
HETATM 12930 C C5  . BMA F 3 .   ? 13.223  72.474  106.431 1.00 104.46 ?  3   BMA F C5  1 
HETATM 12931 C C6  . BMA F 3 .   ? 14.513  72.867  107.307 1.00 107.01 ?  3   BMA F C6  1 
HETATM 12932 O O2  . BMA F 3 .   ? 10.470  69.855  106.658 1.00 88.42  ?  3   BMA F O2  1 
HETATM 12933 O O3  . BMA F 3 .   ? 9.228   72.497  106.920 1.00 91.84  ?  3   BMA F O3  1 
HETATM 12934 O O4  . BMA F 3 .   ? 11.689  73.487  108.291 1.00 92.84  ?  3   BMA F O4  1 
HETATM 12935 O O5  . BMA F 3 .   ? 13.340  71.155  105.674 1.00 106.87 ?  3   BMA F O5  1 
HETATM 12936 O O6  . BMA F 3 .   ? 14.921  71.706  108.014 1.00 106.41 ?  3   BMA F O6  1 
HETATM 12937 C C1  . NAG G 3 .   ? -43.293 79.856  33.635  1.00 88.02  ?  1   NAG G C1  1 
HETATM 12938 C C2  . NAG G 3 .   ? -44.107 80.602  34.685  1.00 93.98  ?  1   NAG G C2  1 
HETATM 12939 C C3  . NAG G 3 .   ? -44.673 79.637  35.736  1.00 99.73  ?  1   NAG G C3  1 
HETATM 12940 C C4  . NAG G 3 .   ? -45.282 78.392  35.091  1.00 95.43  ?  1   NAG G C4  1 
HETATM 12941 C C5  . NAG G 3 .   ? -44.379 77.847  33.983  1.00 88.23  ?  1   NAG G C5  1 
HETATM 12942 C C6  . NAG G 3 .   ? -44.977 76.734  33.168  1.00 88.52  ?  1   NAG G C6  1 
HETATM 12943 C C7  . NAG G 3 .   ? -43.222 82.869  34.834  1.00 107.77 ?  1   NAG G C7  1 
HETATM 12944 C C8  . NAG G 3 .   ? -42.315 83.821  35.578  1.00 106.71 ?  1   NAG G C8  1 
HETATM 12945 N N2  . NAG G 3 .   ? -43.288 81.622  35.313  1.00 101.79 ?  1   NAG G N2  1 
HETATM 12946 O O3  . NAG G 3 .   ? -45.659 80.336  36.503  1.00 99.40  ?  1   NAG G O3  1 
HETATM 12947 O O4  . NAG G 3 .   ? -45.473 77.380  36.068  1.00 97.80  ?  1   NAG G O4  1 
HETATM 12948 O O5  . NAG G 3 .   ? -44.073 78.886  33.053  1.00 89.48  ?  1   NAG G O5  1 
HETATM 12949 O O6  . NAG G 3 .   ? -44.900 75.485  33.848  1.00 98.61  ?  1   NAG G O6  1 
HETATM 12950 O O7  . NAG G 3 .   ? -43.858 83.212  33.836  1.00 101.04 ?  1   NAG G O7  1 
HETATM 12951 C C1  . NAG G 3 .   ? -46.915 77.248  36.065  1.00 102.30 ?  2   NAG G C1  1 
HETATM 12952 C C2  . NAG G 3 .   ? -47.433 75.937  36.665  1.00 107.07 ?  2   NAG G C2  1 
HETATM 12953 C C3  . NAG G 3 .   ? -48.951 75.882  36.508  1.00 110.28 ?  2   NAG G C3  1 
HETATM 12954 C C4  . NAG G 3 .   ? -49.576 77.112  37.185  1.00 111.53 ?  2   NAG G C4  1 
HETATM 12955 C C5  . NAG G 3 .   ? -48.899 78.438  36.718  1.00 114.77 ?  2   NAG G C5  1 
HETATM 12956 C C6  . NAG G 3 .   ? -49.322 79.675  37.507  1.00 114.07 ?  2   NAG G C6  1 
HETATM 12957 C C7  . NAG G 3 .   ? -45.846 74.043  36.733  1.00 105.95 ?  2   NAG G C7  1 
HETATM 12958 C C8  . NAG G 3 .   ? -45.376 74.594  38.049  1.00 108.16 ?  2   NAG G C8  1 
HETATM 12959 N N2  . NAG G 3 .   ? -46.804 74.744  36.108  1.00 110.10 ?  2   NAG G N2  1 
HETATM 12960 O O3  . NAG G 3 .   ? -49.408 74.659  37.088  1.00 114.21 ?  2   NAG G O3  1 
HETATM 12961 O O4  . NAG G 3 .   ? -51.007 77.137  37.074  1.00 110.18 ?  2   NAG G O4  1 
HETATM 12962 O O5  . NAG G 3 .   ? -47.459 78.357  36.807  1.00 108.77 ?  2   NAG G O5  1 
HETATM 12963 O O6  . NAG G 3 .   ? -48.524 80.841  37.297  1.00 107.48 ?  2   NAG G O6  1 
HETATM 12964 O O7  . NAG G 3 .   ? -45.364 73.019  36.246  1.00 103.17 ?  2   NAG G O7  1 
HETATM 12965 C C1  . BMA G 3 .   ? -51.694 76.450  38.198  1.00 110.96 ?  3   BMA G C1  1 
HETATM 12966 C C2  . BMA G 3 .   ? -53.020 75.700  37.680  1.00 106.41 ?  3   BMA G C2  1 
HETATM 12967 C C3  . BMA G 3 .   ? -53.696 74.801  38.775  1.00 103.88 ?  3   BMA G C3  1 
HETATM 12968 C C4  . BMA G 3 .   ? -52.570 74.017  39.636  1.00 108.76 ?  3   BMA G C4  1 
HETATM 12969 C C5  . BMA G 3 .   ? -51.366 74.951  40.121  1.00 108.21 ?  3   BMA G C5  1 
HETATM 12970 C C6  . BMA G 3 .   ? -50.242 74.196  40.886  1.00 106.63 ?  3   BMA G C6  1 
HETATM 12971 O O2  . BMA G 3 .   ? -52.715 74.857  36.508  1.00 97.43  ?  3   BMA G O2  1 
HETATM 12972 O O3  . BMA G 3 .   ? -54.765 73.906  38.192  1.00 97.72  ?  3   BMA G O3  1 
HETATM 12973 O O4  . BMA G 3 .   ? -53.112 73.231  40.772  1.00 108.37 ?  3   BMA G O4  1 
HETATM 12974 O O5  . BMA G 3 .   ? -50.783 75.613  38.987  1.00 111.93 ?  3   BMA G O5  1 
HETATM 12975 O O6  . BMA G 3 .   ? -50.875 73.308  41.836  1.00 108.85 ?  3   BMA G O6  1 
HETATM 12976 C C1  . NAG H 4 .   ? -35.916 70.823  72.713  1.00 84.58  ?  1   NAG H C1  1 
HETATM 12977 C C2  . NAG H 4 .   ? -34.954 71.153  73.863  1.00 83.79  ?  1   NAG H C2  1 
HETATM 12978 C C3  . NAG H 4 .   ? -34.719 69.930  74.751  1.00 85.63  ?  1   NAG H C3  1 
HETATM 12979 C C4  . NAG H 4 .   ? -36.029 69.269  75.188  1.00 89.85  ?  1   NAG H C4  1 
HETATM 12980 C C5  . NAG H 4 .   ? -36.961 69.004  73.991  1.00 88.32  ?  1   NAG H C5  1 
HETATM 12981 C C6  . NAG H 4 .   ? -38.322 68.406  74.349  1.00 85.95  ?  1   NAG H C6  1 
HETATM 12982 C C7  . NAG H 4 .   ? -33.253 72.927  73.525  1.00 82.25  ?  1   NAG H C7  1 
HETATM 12983 C C8  . NAG H 4 .   ? -34.166 73.846  74.297  1.00 82.47  ?  1   NAG H C8  1 
HETATM 12984 N N2  . NAG H 4 .   ? -33.687 71.665  73.351  1.00 77.35  ?  1   NAG H N2  1 
HETATM 12985 O O3  . NAG H 4 .   ? -34.038 70.441  75.893  1.00 83.81  ?  1   NAG H O3  1 
HETATM 12986 O O4  . NAG H 4 .   ? -35.728 68.051  75.866  1.00 89.46  ?  1   NAG H O4  1 
HETATM 12987 O O5  . NAG H 4 .   ? -37.176 70.222  73.254  1.00 81.07  ?  1   NAG H O5  1 
HETATM 12988 O O6  . NAG H 4 .   ? -39.264 69.286  74.961  1.00 85.26  ?  1   NAG H O6  1 
HETATM 12989 O O7  . NAG H 4 .   ? -32.165 73.316  73.075  1.00 79.25  ?  1   NAG H O7  1 
HETATM 12990 C C1  . NAG H 4 .   ? -35.940 68.214  77.305  1.00 93.69  ?  2   NAG H C1  1 
HETATM 12991 C C2  . NAG H 4 .   ? -36.584 66.929  77.837  1.00 94.11  ?  2   NAG H C2  1 
HETATM 12992 C C3  . NAG H 4 .   ? -36.930 67.079  79.324  1.00 96.93  ?  2   NAG H C3  1 
HETATM 12993 C C4  . NAG H 4 .   ? -35.709 67.529  80.122  1.00 99.10  ?  2   NAG H C4  1 
HETATM 12994 C C5  . NAG H 4 .   ? -35.035 68.769  79.482  1.00 105.85 ?  2   NAG H C5  1 
HETATM 12995 C C6  . NAG H 4 .   ? -33.734 69.180  80.143  1.00 104.70 ?  2   NAG H C6  1 
HETATM 12996 C C7  . NAG H 4 .   ? -37.849 65.574  76.219  1.00 90.08  ?  2   NAG H C7  1 
HETATM 12997 C C8  . NAG H 4 .   ? -36.649 64.674  76.157  1.00 88.36  ?  2   NAG H C8  1 
HETATM 12998 N N2  . NAG H 4 .   ? -37.766 66.619  77.051  1.00 93.11  ?  2   NAG H N2  1 
HETATM 12999 O O3  . NAG H 4 .   ? -37.349 65.810  79.819  1.00 98.53  ?  2   NAG H O3  1 
HETATM 13000 O O4  . NAG H 4 .   ? -36.091 67.709  81.484  1.00 88.90  ?  2   NAG H O4  1 
HETATM 13001 O O5  . NAG H 4 .   ? -34.726 68.521  78.095  1.00 106.18 ?  2   NAG H O5  1 
HETATM 13002 O O6  . NAG H 4 .   ? -32.588 68.542  79.578  1.00 98.77  ?  2   NAG H O6  1 
HETATM 13003 O O7  . NAG H 4 .   ? -38.850 65.365  75.549  1.00 88.82  ?  2   NAG H O7  1 
HETATM 13004 C C1  . NAG I 5 .   ? 5.841   32.302  74.891  1.00 144.28 ?  701 NAG B C1  1 
HETATM 13005 C C2  . NAG I 5 .   ? 4.541   31.725  74.301  1.00 144.25 ?  701 NAG B C2  1 
HETATM 13006 C C3  . NAG I 5 .   ? 4.303   32.278  72.908  1.00 144.04 ?  701 NAG B C3  1 
HETATM 13007 C C4  . NAG I 5 .   ? 4.084   33.785  73.012  1.00 148.80 ?  701 NAG B C4  1 
HETATM 13008 C C5  . NAG I 5 .   ? 5.312   34.488  73.616  1.00 156.20 ?  701 NAG B C5  1 
HETATM 13009 C C6  . NAG I 5 .   ? 5.009   35.933  74.008  1.00 158.34 ?  701 NAG B C6  1 
HETATM 13010 C C7  . NAG I 5 .   ? 5.605   29.491  74.060  1.00 146.05 ?  701 NAG B C7  1 
HETATM 13011 C C8  . NAG I 5 .   ? 5.399   28.019  74.200  1.00 147.26 ?  701 NAG B C8  1 
HETATM 13012 N N2  . NAG I 5 .   ? 4.532   30.263  74.315  1.00 142.90 ?  701 NAG B N2  1 
HETATM 13013 O O3  . NAG I 5 .   ? 3.178   31.612  72.338  1.00 137.53 ?  701 NAG B O3  1 
HETATM 13014 O O4  . NAG I 5 .   ? 3.778   34.371  71.749  1.00 146.35 ?  701 NAG B O4  1 
HETATM 13015 O O5  . NAG I 5 .   ? 5.828   33.822  74.797  1.00 146.93 ?  701 NAG B O5  1 
HETATM 13016 O O6  . NAG I 5 .   ? 4.164   36.123  75.146  1.00 151.43 ?  701 NAG B O6  1 
HETATM 13017 O O7  . NAG I 5 .   ? 6.699   29.957  73.737  1.00 146.01 ?  701 NAG B O7  1 
HETATM 13018 C C1  . NAG J 5 .   ? -16.268 23.913  95.729  1.00 111.56 ?  702 NAG B C1  1 
HETATM 13019 C C2  . NAG J 5 .   ? -16.696 23.359  94.368  1.00 119.74 ?  702 NAG B C2  1 
HETATM 13020 C C3  . NAG J 5 .   ? -18.163 23.758  94.083  1.00 123.79 ?  702 NAG B C3  1 
HETATM 13021 C C4  . NAG J 5 .   ? -19.077 23.195  95.183  1.00 126.01 ?  702 NAG B C4  1 
HETATM 13022 C C5  . NAG J 5 .   ? -18.639 23.657  96.591  1.00 120.12 ?  702 NAG B C5  1 
HETATM 13023 C C6  . NAG J 5 .   ? -19.374 22.959  97.741  1.00 110.77 ?  702 NAG B C6  1 
HETATM 13024 C C7  . NAG J 5 .   ? -15.393 24.949  92.916  1.00 116.27 ?  702 NAG B C7  1 
HETATM 13025 C C8  . NAG J 5 .   ? -14.409 25.041  91.773  1.00 103.04 ?  702 NAG B C8  1 
HETATM 13026 N N2  . NAG J 5 .   ? -15.775 23.704  93.272  1.00 121.68 ?  702 NAG B N2  1 
HETATM 13027 O O3  . NAG J 5 .   ? -18.603 23.346  92.784  1.00 119.15 ?  702 NAG B O3  1 
HETATM 13028 O O4  . NAG J 5 .   ? -20.440 23.562  94.975  1.00 127.01 ?  702 NAG B O4  1 
HETATM 13029 O O5  . NAG J 5 .   ? -17.225 23.413  96.805  1.00 110.09 ?  702 NAG B O5  1 
HETATM 13030 O O6  . NAG J 5 .   ? -20.787 23.138  97.846  1.00 91.51  ?  702 NAG B O6  1 
HETATM 13031 O O7  . NAG J 5 .   ? -15.786 25.949  93.507  1.00 113.45 ?  702 NAG B O7  1 
HETATM 13032 C C1  . NAG K 5 .   ? 8.667   0.831   123.173 1.00 146.70 ?  703 NAG B C1  1 
HETATM 13033 C C2  . NAG K 5 .   ? 10.005  0.885   123.920 1.00 144.39 ?  703 NAG B C2  1 
HETATM 13034 C C3  . NAG K 5 .   ? 10.007  -0.094  125.107 1.00 136.18 ?  703 NAG B C3  1 
HETATM 13035 C C4  . NAG K 5 .   ? 8.831   0.223   126.042 1.00 133.28 ?  703 NAG B C4  1 
HETATM 13036 C C5  . NAG K 5 .   ? 7.501   0.166   125.273 1.00 132.56 ?  703 NAG B C5  1 
HETATM 13037 C C6  . NAG K 5 .   ? 6.279   0.525   126.108 1.00 123.47 ?  703 NAG B C6  1 
HETATM 13038 C C7  . NAG K 5 .   ? 12.075  1.569   122.773 1.00 134.51 ?  703 NAG B C7  1 
HETATM 13039 C C8  . NAG K 5 .   ? 13.146  1.179   121.790 1.00 130.46 ?  703 NAG B C8  1 
HETATM 13040 N N2  . NAG K 5 .   ? 11.126  0.650   123.013 1.00 142.22 ?  703 NAG B N2  1 
HETATM 13041 O O3  . NAG K 5 .   ? 11.271  -0.000  125.771 1.00 131.68 ?  703 NAG B O3  1 
HETATM 13042 O O4  . NAG K 5 .   ? 8.742   -0.678  127.143 1.00 123.38 ?  703 NAG B O4  1 
HETATM 13043 O O5  . NAG K 5 .   ? 7.529   1.067   124.142 1.00 134.67 ?  703 NAG B O5  1 
HETATM 13044 O O6  . NAG K 5 .   ? 6.193   -0.128  127.371 1.00 116.97 ?  703 NAG B O6  1 
HETATM 13045 O O7  . NAG K 5 .   ? 12.071  2.669   123.325 1.00 128.44 ?  703 NAG B O7  1 
HETATM 13046 C C1  . NAG L 5 .   ? -12.882 12.761  106.765 1.00 106.24 ?  704 NAG B C1  1 
HETATM 13047 C C2  . NAG L 5 .   ? -11.895 11.578  106.653 1.00 106.92 ?  704 NAG B C2  1 
HETATM 13048 C C3  . NAG L 5 .   ? -12.204 10.738  105.407 1.00 109.67 ?  704 NAG B C3  1 
HETATM 13049 C C4  . NAG L 5 .   ? -13.659 10.263  105.432 1.00 110.92 ?  704 NAG B C4  1 
HETATM 13050 C C5  . NAG L 5 .   ? -14.632 11.449  105.592 1.00 109.48 ?  704 NAG B C5  1 
HETATM 13051 C C6  . NAG L 5 .   ? -16.095 11.040  105.721 1.00 106.54 ?  704 NAG B C6  1 
HETATM 13052 C C7  . NAG L 5 .   ? -9.717  11.911  107.747 1.00 101.61 ?  704 NAG B C7  1 
HETATM 13053 C C8  . NAG L 5 .   ? -10.365 11.392  108.998 1.00 100.23 ?  704 NAG B C8  1 
HETATM 13054 N N2  . NAG L 5 .   ? -10.501 11.998  106.662 1.00 105.23 ?  704 NAG B N2  1 
HETATM 13055 O O3  . NAG L 5 .   ? -11.339 9.607   105.441 1.00 107.23 ?  704 NAG B O3  1 
HETATM 13056 O O4  . NAG L 5 .   ? -13.968 9.446   104.299 1.00 110.04 ?  704 NAG B O4  1 
HETATM 13057 O O5  . NAG L 5 .   ? -14.288 12.238  106.753 1.00 107.15 ?  704 NAG B O5  1 
HETATM 13058 O O6  . NAG L 5 .   ? -16.467 10.507  106.991 1.00 99.33  ?  704 NAG B O6  1 
HETATM 13059 O O7  . NAG L 5 .   ? -8.540  12.246  107.724 1.00 96.83  ?  704 NAG B O7  1 
HETATM 13060 C C1  . NAG M 5 .   ? -17.704 45.380  44.759  1.00 103.03 ?  701 NAG A C1  1 
HETATM 13061 C C2  . NAG M 5 .   ? -19.026 44.847  45.361  1.00 105.65 ?  701 NAG A C2  1 
HETATM 13062 C C3  . NAG M 5 .   ? -19.163 43.341  45.121  1.00 109.77 ?  701 NAG A C3  1 
HETATM 13063 C C4  . NAG M 5 .   ? -19.184 43.091  43.618  1.00 111.34 ?  701 NAG A C4  1 
HETATM 13064 C C5  . NAG M 5 .   ? -17.862 43.537  42.981  1.00 117.16 ?  701 NAG A C5  1 
HETATM 13065 C C6  . NAG M 5 .   ? -17.889 43.389  41.476  1.00 115.51 ?  701 NAG A C6  1 
HETATM 13066 C C7  . NAG M 5 .   ? -20.085 46.054  47.235  1.00 105.06 ?  701 NAG A C7  1 
HETATM 13067 C C8  . NAG M 5 .   ? -20.951 46.722  46.205  1.00 104.50 ?  701 NAG A C8  1 
HETATM 13068 N N2  . NAG M 5 .   ? -19.177 45.179  46.772  1.00 102.30 ?  701 NAG A N2  1 
HETATM 13069 O O3  . NAG M 5 .   ? -20.388 42.875  45.685  1.00 103.06 ?  701 NAG A O3  1 
HETATM 13070 O O4  . NAG M 5 .   ? -19.512 41.744  43.274  1.00 107.13 ?  701 NAG A O4  1 
HETATM 13071 O O5  . NAG M 5 .   ? -17.574 44.923  43.275  1.00 108.13 ?  701 NAG A O5  1 
HETATM 13072 O O6  . NAG M 5 .   ? -19.057 43.947  40.882  1.00 115.39 ?  701 NAG A O6  1 
HETATM 13073 O O7  . NAG M 5 .   ? -20.187 46.315  48.434  1.00 109.75 ?  701 NAG A O7  1 
HETATM 13074 C C1  . NAG N 5 .   ? -21.716 79.220  22.081  1.00 109.07 ?  702 NAG A C1  1 
HETATM 13075 C C2  . NAG N 5 .   ? -21.979 78.900  20.576  1.00 119.64 ?  702 NAG A C2  1 
HETATM 13076 C C3  . NAG N 5 .   ? -22.719 80.060  19.868  1.00 120.84 ?  702 NAG A C3  1 
HETATM 13077 C C4  . NAG N 5 .   ? -23.958 80.493  20.644  1.00 115.78 ?  702 NAG A C4  1 
HETATM 13078 C C5  . NAG N 5 .   ? -23.567 80.913  22.056  1.00 115.56 ?  702 NAG A C5  1 
HETATM 13079 C C6  . NAG N 5 .   ? -24.750 81.335  22.908  1.00 118.48 ?  702 NAG A C6  1 
HETATM 13080 C C7  . NAG N 5 .   ? -20.605 78.041  18.678  1.00 120.40 ?  702 NAG A C7  1 
HETATM 13081 C C8  . NAG N 5 .   ? -19.205 77.833  18.182  1.00 117.89 ?  702 NAG A C8  1 
HETATM 13082 N N2  . NAG N 5 .   ? -20.718 78.593  19.900  1.00 122.62 ?  702 NAG A N2  1 
HETATM 13083 O O3  . NAG N 5 .   ? -23.142 79.641  18.572  1.00 111.88 ?  702 NAG A O3  1 
HETATM 13084 O O4  . NAG N 5 .   ? -24.626 81.541  19.949  1.00 110.13 ?  702 NAG A O4  1 
HETATM 13085 O O5  . NAG N 5 .   ? -22.948 79.792  22.715  1.00 111.01 ?  702 NAG A O5  1 
HETATM 13086 O O6  . NAG N 5 .   ? -25.824 81.905  22.160  1.00 117.74 ?  702 NAG A O6  1 
HETATM 13087 O O7  . NAG N 5 .   ? -21.580 77.729  18.004  1.00 115.28 ?  702 NAG A O7  1 
HETATM 13088 C C1  . NAG O 5 .   ? -40.925 61.254  61.427  1.00 112.32 ?  703 NAG A C1  1 
HETATM 13089 C C2  . NAG O 5 .   ? -40.846 60.247  62.624  1.00 109.51 ?  703 NAG A C2  1 
HETATM 13090 C C3  . NAG O 5 .   ? -42.251 59.902  63.155  1.00 115.71 ?  703 NAG A C3  1 
HETATM 13091 C C4  . NAG O 5 .   ? -43.071 61.163  63.463  1.00 115.91 ?  703 NAG A C4  1 
HETATM 13092 C C5  . NAG O 5 .   ? -43.146 62.101  62.244  1.00 116.69 ?  703 NAG A C5  1 
HETATM 13093 C C6  . NAG O 5 .   ? -43.896 63.404  62.502  1.00 107.14 ?  703 NAG A C6  1 
HETATM 13094 C C7  . NAG O 5 .   ? -38.780 59.004  62.095  1.00 106.45 ?  703 NAG A C7  1 
HETATM 13095 C C8  . NAG O 5 .   ? -38.184 57.673  61.730  1.00 101.96 ?  703 NAG A C8  1 
HETATM 13096 N N2  . NAG O 5 .   ? -40.110 59.034  62.272  1.00 109.63 ?  703 NAG A N2  1 
HETATM 13097 O O3  . NAG O 5 .   ? -42.074 59.105  64.327  1.00 110.06 ?  703 NAG A O3  1 
HETATM 13098 O O4  . NAG O 5 .   ? -44.387 60.853  63.923  1.00 97.39  ?  703 NAG A O4  1 
HETATM 13099 O O5  . NAG O 5 .   ? -41.810 62.448  61.810  1.00 113.96 ?  703 NAG A O5  1 
HETATM 13100 O O6  . NAG O 5 .   ? -45.306 63.383  62.269  1.00 89.06  ?  703 NAG A O6  1 
HETATM 13101 O O7  . NAG O 5 .   ? -38.091 60.013  62.214  1.00 106.50 ?  703 NAG A O7  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   . ASP A 1   ? 1.3110 0.7614 1.1108 0.4434  -0.2536 -0.1440 17  ASP B N   
2     C CA  . ASP A 1   ? 1.2714 0.7731 1.0980 0.4329  -0.2463 -0.1381 17  ASP B CA  
3     C C   . ASP A 1   ? 1.3586 0.8337 1.1684 0.4057  -0.2540 -0.1253 17  ASP B C   
4     O O   . ASP A 1   ? 1.4179 0.8974 1.2319 0.4009  -0.2624 -0.1120 17  ASP B O   
5     C CB  . ASP A 1   ? 1.3358 0.8769 1.1900 0.4486  -0.2493 -0.1311 17  ASP B CB  
6     C CG  . ASP A 1   ? 1.4049 0.9038 1.2417 0.4526  -0.2684 -0.1186 17  ASP B CG  
7     O OD1 . ASP A 1   ? 1.4125 0.8642 1.2259 0.4616  -0.2759 -0.1223 17  ASP B OD1 
8     O OD2 . ASP A 1   ? 1.3330 0.8446 1.1776 0.4451  -0.2762 -0.1049 17  ASP B OD2 
9     N N   . PRO A 2   ? 1.4928 0.9397 1.2828 0.3872  -0.2517 -0.1279 18  PRO B N   
10    C CA  . PRO A 2   ? 1.4558 0.8823 1.2329 0.3611  -0.2572 -0.1145 18  PRO B CA  
11    C C   . PRO A 2   ? 1.6504 1.1056 1.4402 0.3437  -0.2447 -0.1162 18  PRO B C   
12    O O   . PRO A 2   ? 1.7167 1.1830 1.5102 0.3425  -0.2340 -0.1282 18  PRO B O   
13    C CB  . PRO A 2   ? 1.4932 0.8522 1.2325 0.3506  -0.2693 -0.1112 18  PRO B CB  
14    C CG  . PRO A 2   ? 1.4262 0.7784 1.1599 0.3631  -0.2629 -0.1284 18  PRO B CG  
15    C CD  . PRO A 2   ? 1.4822 0.8946 1.2501 0.3876  -0.2500 -0.1395 18  PRO B CD  
16    N N   . SER A 3   ? 1.4319 0.9029 1.2302 0.3320  -0.2457 -0.1043 19  SER B N   
17    C CA  . SER A 3   ? 1.4113 0.8623 1.1968 0.3057  -0.2450 -0.0954 19  SER B CA  
18    C C   . SER A 3   ? 1.4377 0.8810 1.2183 0.2926  -0.2361 -0.1043 19  SER B C   
19    O O   . SER A 3   ? 1.5089 0.9047 1.2628 0.2760  -0.2428 -0.0994 19  SER B O   
20    C CB  . SER A 3   ? 1.4561 0.8515 1.2100 0.2932  -0.2608 -0.0798 19  SER B CB  
21    O OG  . SER A 3   ? 1.5187 0.8684 1.2478 0.2896  -0.2668 -0.0838 19  SER B OG  
22    N N   . THR A 4   ? 1.3231 0.8134 1.1286 0.2964  -0.2215 -0.1156 20  THR B N   
23    C CA  . THR A 4   ? 1.3322 0.8252 1.1355 0.2744  -0.2114 -0.1189 20  THR B CA  
24    C C   . THR A 4   ? 1.3398 0.8466 1.1467 0.2419  -0.2054 -0.1022 20  THR B C   
25    O O   . THR A 4   ? 1.2996 0.8268 1.1156 0.2388  -0.2049 -0.0918 20  THR B O   
26    C CB  . THR A 4   ? 1.2217 0.7646 1.0504 0.2846  -0.1967 -0.1342 20  THR B CB  
27    O OG1 . THR A 4   ? 1.2002 0.8017 1.0584 0.2743  -0.1845 -0.1287 20  THR B OG1 
28    C CG2 . THR A 4   ? 1.2735 0.8282 1.1095 0.3155  -0.1981 -0.1453 20  THR B CG2 
29    N N   . ILE A 5   ? 1.3275 0.8199 1.1249 0.2177  -0.2019 -0.0988 21  ILE B N   
30    C CA  . ILE A 5   ? 1.2471 0.7520 1.0481 0.1880  -0.1953 -0.0826 21  ILE B CA  
31    C C   . ILE A 5   ? 1.1989 0.7658 1.0312 0.1866  -0.1802 -0.0824 21  ILE B C   
32    O O   . ILE A 5   ? 1.3156 0.8961 1.1516 0.1745  -0.1767 -0.0699 21  ILE B O   
33    C CB  . ILE A 5   ? 1.3546 0.8437 1.1470 0.1639  -0.1929 -0.0801 21  ILE B CB  
34    C CG1 . ILE A 5   ? 1.4884 0.9106 1.2460 0.1624  -0.2100 -0.0789 21  ILE B CG1 
35    C CG2 . ILE A 5   ? 1.3575 0.8653 1.1578 0.1353  -0.1842 -0.0631 21  ILE B CG2 
36    C CD1 . ILE A 5   ? 1.5178 0.9021 1.2541 0.1553  -0.2224 -0.0628 21  ILE B CD1 
37    N N   . GLU A 6   ? 1.1584 0.7620 1.0118 0.2003  -0.1719 -0.0965 22  GLU B N   
38    C CA  . GLU A 6   ? 1.1124 0.7732 0.9949 0.1985  -0.1588 -0.0967 22  GLU B CA  
39    C C   . GLU A 6   ? 1.0839 0.7592 0.9725 0.2115  -0.1633 -0.0925 22  GLU B C   
40    O O   . GLU A 6   ? 1.0103 0.7161 0.9117 0.2013  -0.1561 -0.0855 22  GLU B O   
41    C CB  . GLU A 6   ? 1.1151 0.8095 1.0165 0.2095  -0.1503 -0.1119 22  GLU B CB  
42    C CG  . GLU A 6   ? 1.0875 0.8390 1.0183 0.2086  -0.1388 -0.1125 22  GLU B CG  
43    C CD  . GLU A 6   ? 1.1665 0.9521 1.1151 0.2141  -0.1294 -0.1252 22  GLU B CD  
44    O OE1 . GLU A 6   ? 1.2371 1.0124 1.1796 0.2019  -0.1258 -0.1279 22  GLU B OE1 
45    O OE2 . GLU A 6   ? 1.1452 0.9690 1.1137 0.2291  -0.1259 -0.1314 22  GLU B OE2 
46    N N   . GLU A 7   ? 1.0924 0.7456 0.9717 0.2343  -0.1757 -0.0966 23  GLU B N   
47    C CA  . GLU A 7   ? 1.0731 0.7382 0.9576 0.2463  -0.1824 -0.0912 23  GLU B CA  
48    C C   . GLU A 7   ? 1.0731 0.7172 0.9401 0.2276  -0.1866 -0.0745 23  GLU B C   
49    O O   . GLU A 7   ? 1.0663 0.7369 0.9418 0.2220  -0.1835 -0.0678 23  GLU B O   
50    C CB  . GLU A 7   ? 1.1570 0.7964 1.0331 0.2745  -0.1961 -0.0977 23  GLU B CB  
51    C CG  . GLU A 7   ? 1.1500 0.8100 1.0412 0.2947  -0.1905 -0.1147 23  GLU B CG  
52    C CD  . GLU A 7   ? 1.2814 0.9095 1.1613 0.3239  -0.2033 -0.1217 23  GLU B CD  
53    O OE1 . GLU A 7   ? 1.4184 0.9901 1.2692 0.3216  -0.2150 -0.1173 23  GLU B OE1 
54    O OE2 . GLU A 7   ? 1.3620 1.0264 1.2622 0.3433  -0.1993 -0.1294 23  GLU B OE2 
55    N N   . GLN A 8   ? 1.0835 0.6779 0.9237 0.2177  -0.1945 -0.0673 24  GLN B N   
56    C CA  . GLN A 8   ? 1.0899 0.6641 0.9118 0.1975  -0.1969 -0.0506 24  GLN B CA  
57    C C   . GLN A 8   ? 1.0986 0.7102 0.9346 0.1761  -0.1800 -0.0454 24  GLN B C   
58    O O   . GLN A 8   ? 1.0547 0.6749 0.8864 0.1673  -0.1779 -0.0354 24  GLN B O   
59    C CB  . GLN A 8   ? 1.1553 0.6751 0.9494 0.1862  -0.2059 -0.0440 24  GLN B CB  
60    C CG  . GLN A 8   ? 1.2174 0.6940 0.9944 0.2084  -0.2235 -0.0493 24  GLN B CG  
61    C CD  . GLN A 8   ? 1.3141 0.7378 1.0658 0.1990  -0.2321 -0.0478 24  GLN B CD  
62    O OE1 . GLN A 8   ? 1.3564 0.7628 1.0945 0.1730  -0.2311 -0.0347 24  GLN B OE1 
63    N NE2 . GLN A 8   ? 1.4054 0.8014 1.1490 0.2202  -0.2413 -0.0605 24  GLN B NE2 
64    N N   . ALA A 9   ? 1.0579 0.6918 0.9102 0.1686  -0.1680 -0.0527 25  ALA B N   
65    C CA  . ALA A 9   ? 1.0093 0.6747 0.8748 0.1485  -0.1521 -0.0473 25  ALA B CA  
66    C C   . ALA A 9   ? 1.0004 0.7101 0.8860 0.1550  -0.1449 -0.0511 25  ALA B C   
67    O O   . ALA A 9   ? 0.9846 0.7108 0.8721 0.1416  -0.1358 -0.0438 25  ALA B O   
68    C CB  . ALA A 9   ? 1.0194 0.6935 0.8960 0.1387  -0.1437 -0.0529 25  ALA B CB  
69    N N   . LYS A 10  ? 0.9898 0.7181 0.8891 0.1758  -0.1493 -0.0622 26  LYS B N   
70    C CA  . LYS A 10  ? 0.9241 0.6924 0.8410 0.1808  -0.1454 -0.0641 26  LYS B CA  
71    C C   . LYS A 10  ? 0.9740 0.7293 0.8744 0.1795  -0.1535 -0.0535 26  LYS B C   
72    O O   . LYS A 10  ? 0.9426 0.7161 0.8443 0.1683  -0.1465 -0.0486 26  LYS B O   
73    C CB  . LYS A 10  ? 0.9422 0.7355 0.8785 0.2031  -0.1492 -0.0763 26  LYS B CB  
74    C CG  . LYS A 10  ? 0.8994 0.7185 0.8549 0.2029  -0.1387 -0.0869 26  LYS B CG  
75    C CD  . LYS A 10  ? 0.9226 0.7691 0.8966 0.2255  -0.1414 -0.0980 26  LYS B CD  
76    C CE  . LYS A 10  ? 0.9163 0.7866 0.9061 0.2255  -0.1310 -0.1087 26  LYS B CE  
77    N NZ  . LYS A 10  ? 0.8935 0.7866 0.8980 0.2493  -0.1334 -0.1193 26  LYS B NZ  
78    N N   . THR A 11  ? 1.0001 0.7218 0.8829 0.1911  -0.1687 -0.0500 27  THR B N   
79    C CA  . THR A 11  ? 0.9803 0.6866 0.8443 0.1887  -0.1778 -0.0387 27  THR B CA  
80    C C   . THR A 11  ? 1.0059 0.6989 0.8517 0.1644  -0.1689 -0.0271 27  THR B C   
81    O O   . THR A 11  ? 1.0278 0.7296 0.8657 0.1564  -0.1666 -0.0206 27  THR B O   
82    C CB  . THR A 11  ? 1.0308 0.6976 0.8772 0.2039  -0.1963 -0.0355 27  THR B CB  
83    O OG1 . THR A 11  ? 0.9886 0.6689 0.8538 0.2279  -0.2015 -0.0477 27  THR B OG1 
84    C CG2 . THR A 11  ? 0.9826 0.6405 0.8139 0.2051  -0.2078 -0.0251 27  THR B CG2 
85    N N   . PHE A 12  ? 1.0077 0.6798 0.8462 0.1522  -0.1638 -0.0242 28  PHE B N   
86    C CA  . PHE A 12  ? 1.0232 0.6867 0.8478 0.1293  -0.1537 -0.0124 28  PHE B CA  
87    C C   . PHE A 12  ? 0.9368 0.6394 0.7762 0.1207  -0.1374 -0.0141 28  PHE B C   
88    O O   . PHE A 12  ? 0.9174 0.6199 0.7426 0.1114  -0.1332 -0.0061 28  PHE B O   
89    C CB  . PHE A 12  ? 1.0074 0.6529 0.8305 0.1175  -0.1499 -0.0103 28  PHE B CB  
90    C CG  . PHE A 12  ? 0.9696 0.6182 0.7874 0.0942  -0.1364 0.0015  28  PHE B CG  
91    C CD1 . PHE A 12  ? 1.0041 0.6278 0.7960 0.0824  -0.1389 0.0163  28  PHE B CD1 
92    C CD2 . PHE A 12  ? 0.8856 0.5656 0.7255 0.0849  -0.1203 -0.0018 28  PHE B CD2 
93    C CE1 . PHE A 12  ? 1.0181 0.6492 0.8068 0.0622  -0.1246 0.0275  28  PHE B CE1 
94    C CE2 . PHE A 12  ? 0.9412 0.6277 0.7790 0.0658  -0.1069 0.0093  28  PHE B CE2 
95    C CZ  . PHE A 12  ? 1.0439 0.7073 0.8567 0.0548  -0.1082 0.0238  28  PHE B CZ  
96    N N   . LEU A 13  ? 0.9447 0.6793 0.8109 0.1242  -0.1288 -0.0250 29  LEU B N   
97    C CA  . LEU A 13  ? 0.9594 0.7291 0.8411 0.1167  -0.1141 -0.0275 29  LEU B CA  
98    C C   . LEU A 13  ? 0.9524 0.7371 0.8323 0.1236  -0.1184 -0.0292 29  LEU B C   
99    O O   . LEU A 13  ? 0.9133 0.7151 0.7940 0.1150  -0.1081 -0.0282 29  LEU B O   
100   C CB  . LEU A 13  ? 0.9443 0.7422 0.8539 0.1203  -0.1073 -0.0385 29  LEU B CB  
101   C CG  . LEU A 13  ? 0.8936 0.6819 0.8068 0.1100  -0.1016 -0.0367 29  LEU B CG  
102   C CD1 . LEU A 13  ? 0.8553 0.6699 0.7926 0.1182  -0.0993 -0.0491 29  LEU B CD1 
103   C CD2 . LEU A 13  ? 0.8368 0.6324 0.7502 0.0911  -0.0867 -0.0275 29  LEU B CD2 
104   N N   . ASP A 14  ? 0.9841 0.7619 0.8614 0.1393  -0.1340 -0.0315 30  ASP B N   
105   C CA  . ASP A 14  ? 0.9625 0.7546 0.8386 0.1457  -0.1414 -0.0318 30  ASP B CA  
106   C C   . ASP A 14  ? 0.9417 0.7117 0.7875 0.1343  -0.1425 -0.0205 30  ASP B C   
107   O O   . ASP A 14  ? 0.9297 0.7134 0.7711 0.1256  -0.1349 -0.0199 30  ASP B O   
108   C CB  . ASP A 14  ? 0.9385 0.7271 0.8200 0.1660  -0.1586 -0.0351 30  ASP B CB  
109   C CG  . ASP A 14  ? 1.0391 0.8642 0.9412 0.1756  -0.1624 -0.0411 30  ASP B CG  
110   O OD1 . ASP A 14  ? 1.0813 0.9255 0.9848 0.1643  -0.1549 -0.0407 30  ASP B OD1 
111   O OD2 . ASP A 14  ? 1.0830 0.9159 0.9980 0.1942  -0.1736 -0.0453 30  ASP B OD2 
112   N N   . LYS A 15  ? 0.9343 0.6676 0.7567 0.1334  -0.1516 -0.0114 31  LYS B N   
113   C CA  . LYS A 15  ? 0.9617 0.6711 0.7520 0.1201  -0.1508 0.0008  31  LYS B CA  
114   C C   . LYS A 15  ? 1.0084 0.7276 0.7961 0.1027  -0.1298 0.0032  31  LYS B C   
115   O O   . LYS A 15  ? 1.0567 0.7747 0.8250 0.0938  -0.1240 0.0079  31  LYS B O   
116   C CB  . LYS A 15  ? 1.0197 0.6875 0.7876 0.1198  -0.1627 0.0110  31  LYS B CB  
117   C CG  . LYS A 15  ? 1.1627 0.8062 0.8985 0.1013  -0.1570 0.0252  31  LYS B CG  
118   C CD  . LYS A 15  ? 1.2093 0.8458 0.9187 0.0984  -0.1632 0.0320  31  LYS B CD  
119   C CE  . LYS A 15  ? 1.3294 0.9425 1.0063 0.0797  -0.1551 0.0462  31  LYS B CE  
120   N NZ  . LYS A 15  ? 1.3989 1.0067 1.0464 0.0742  -0.1573 0.0519  31  LYS B NZ  
121   N N   . PHE A 16  ? 1.0027 0.7321 0.8096 0.0982  -0.1182 -0.0002 32  PHE B N   
122   C CA  . PHE A 16  ? 0.9677 0.7084 0.7760 0.0833  -0.0983 0.0029  32  PHE B CA  
123   C C   . PHE A 16  ? 0.9570 0.7269 0.7758 0.0834  -0.0882 -0.0047 32  PHE B C   
124   O O   . PHE A 16  ? 0.9942 0.7652 0.8002 0.0735  -0.0751 -0.0007 32  PHE B O   
125   C CB  . PHE A 16  ? 0.9483 0.6947 0.7767 0.0781  -0.0901 0.0021  32  PHE B CB  
126   C CG  . PHE A 16  ? 0.9142 0.6813 0.7532 0.0658  -0.0694 0.0040  32  PHE B CG  
127   C CD1 . PHE A 16  ? 0.8675 0.6234 0.6909 0.0517  -0.0591 0.0164  32  PHE B CD1 
128   C CD2 . PHE A 16  ? 0.8876 0.6860 0.7529 0.0686  -0.0604 -0.0058 32  PHE B CD2 
129   C CE1 . PHE A 16  ? 0.8302 0.6068 0.6654 0.0427  -0.0397 0.0186  32  PHE B CE1 
130   C CE2 . PHE A 16  ? 0.8398 0.6557 0.7156 0.0589  -0.0422 -0.0034 32  PHE B CE2 
131   C CZ  . PHE A 16  ? 0.8484 0.6541 0.7099 0.0469  -0.0316 0.0085  32  PHE B CZ  
132   N N   . ASN A 17  ? 0.9608 0.7541 0.8022 0.0943  -0.0936 -0.0155 33  ASN B N   
133   C CA  . ASN A 17  ? 0.9678 0.7866 0.8184 0.0926  -0.0853 -0.0221 33  ASN B CA  
134   C C   . ASN A 17  ? 1.0311 0.8390 0.8536 0.0896  -0.0892 -0.0187 33  ASN B C   
135   O O   . ASN A 17  ? 1.0286 0.8441 0.8450 0.0828  -0.0779 -0.0207 33  ASN B O   
136   C CB  . ASN A 17  ? 0.8928 0.7396 0.7719 0.1034  -0.0920 -0.0327 33  ASN B CB  
137   C CG  . ASN A 17  ? 0.8224 0.6841 0.7280 0.1042  -0.0849 -0.0376 33  ASN B CG  
138   O OD1 . ASN A 17  ? 0.8821 0.7415 0.7903 0.0947  -0.0722 -0.0343 33  ASN B OD1 
139   N ND2 . ASN A 17  ? 0.8300 0.7079 0.7553 0.1158  -0.0934 -0.0451 33  ASN B ND2 
140   N N   . HIS A 18  ? 1.1038 0.8913 0.9065 0.0941  -0.1052 -0.0133 34  HIS B N   
141   C CA  . HIS A 18  ? 1.1464 0.9243 0.9209 0.0896  -0.1090 -0.0101 34  HIS B CA  
142   C C   . HIS A 18  ? 1.2019 0.9555 0.9440 0.0773  -0.0979 -0.0007 34  HIS B C   
143   O O   . HIS A 18  ? 1.3026 1.0565 1.0273 0.0701  -0.0874 -0.0018 34  HIS B O   
144   C CB  . HIS A 18  ? 1.2071 0.9779 0.9752 0.0994  -0.1317 -0.0079 34  HIS B CB  
145   C CG  . HIS A 18  ? 1.2726 1.0735 1.0740 0.1114  -0.1401 -0.0170 34  HIS B CG  
146   N ND1 . HIS A 18  ? 1.2278 1.0391 1.0566 0.1216  -0.1414 -0.0215 34  HIS B ND1 
147   C CD2 . HIS A 18  ? 1.3266 1.1510 1.1383 0.1135  -0.1462 -0.0223 34  HIS B CD2 
148   C CE1 . HIS A 18  ? 1.2394 1.0811 1.0943 0.1307  -0.1473 -0.0289 34  HIS B CE1 
149   N NE2 . HIS A 18  ? 1.2658 1.1169 1.1122 0.1253  -0.1509 -0.0289 34  HIS B NE2 
150   N N   . GLU A 19  ? 1.1368 0.8691 0.8696 0.0745  -0.0995 0.0086  35  GLU B N   
151   C CA  . GLU A 19  ? 1.1498 0.8655 0.8569 0.0613  -0.0855 0.0185  35  GLU B CA  
152   C C   . GLU A 19  ? 1.0654 0.8016 0.7843 0.0550  -0.0620 0.0140  35  GLU B C   
153   O O   . GLU A 19  ? 1.0742 0.8051 0.7695 0.0474  -0.0488 0.0169  35  GLU B O   
154   C CB  . GLU A 19  ? 1.1231 0.8186 0.8272 0.0575  -0.0892 0.0288  35  GLU B CB  
155   C CG  . GLU A 19  ? 1.2200 0.8828 0.8923 0.0567  -0.1065 0.0397  35  GLU B CG  
156   C CD  . GLU A 19  ? 1.5544 1.2037 1.1874 0.0472  -0.1021 0.0469  35  GLU B CD  
157   O OE1 . GLU A 19  ? 1.4774 1.1394 1.1044 0.0406  -0.0831 0.0440  35  GLU B OE1 
158   O OE2 . GLU A 19  ? 1.7382 1.3621 1.3441 0.0470  -0.1184 0.0554  35  GLU B OE2 
159   N N   . ALA A 20  ? 1.0561 0.8159 0.8107 0.0591  -0.0568 0.0063  36  ALA B N   
160   C CA  . ALA A 20  ? 1.0044 0.7840 0.7749 0.0543  -0.0360 0.0031  36  ALA B CA  
161   C C   . ALA A 20  ? 0.9902 0.7796 0.7541 0.0557  -0.0302 -0.0054 36  ALA B C   
162   O O   . ALA A 20  ? 1.0263 0.8158 0.7784 0.0503  -0.0127 -0.0043 36  ALA B O   
163   C CB  . ALA A 20  ? 1.0031 0.8034 0.8119 0.0579  -0.0352 -0.0022 36  ALA B CB  
164   N N   . GLU A 21  ? 0.9526 0.7512 0.7250 0.0630  -0.0440 -0.0140 37  GLU B N   
165   C CA  . GLU A 21  ? 0.9462 0.7512 0.7104 0.0622  -0.0397 -0.0216 37  GLU B CA  
166   C C   . GLU A 21  ? 0.9630 0.7436 0.6839 0.0563  -0.0361 -0.0172 37  GLU B C   
167   O O   . GLU A 21  ? 0.9516 0.7307 0.6591 0.0529  -0.0219 -0.0211 37  GLU B O   
168   C CB  . GLU A 21  ? 0.9778 0.7961 0.7548 0.0687  -0.0573 -0.0290 37  GLU B CB  
169   C CG  . GLU A 21  ? 0.9403 0.7853 0.7581 0.0753  -0.0612 -0.0347 37  GLU B CG  
170   C CD  . GLU A 21  ? 1.0140 0.8792 0.8449 0.0772  -0.0683 -0.0431 37  GLU B CD  
171   O OE1 . GLU A 21  ? 1.0183 0.8812 0.8363 0.0716  -0.0615 -0.0467 37  GLU B OE1 
172   O OE2 . GLU A 21  ? 1.0967 0.9788 0.9483 0.0843  -0.0820 -0.0456 37  GLU B OE2 
173   N N   . ASP A 22  ? 1.0067 0.7659 0.7029 0.0549  -0.0480 -0.0087 38  ASP B N   
174   C CA  . ASP A 22  ? 0.9952 0.7309 0.6469 0.0481  -0.0438 -0.0041 38  ASP B CA  
175   C C   . ASP A 22  ? 1.0472 0.7796 0.6886 0.0414  -0.0189 0.0009  38  ASP B C   
176   O O   . ASP A 22  ? 1.0796 0.8062 0.6979 0.0385  -0.0050 -0.0026 38  ASP B O   
177   C CB  . ASP A 22  ? 1.0458 0.7584 0.6713 0.0470  -0.0622 0.0053  38  ASP B CB  
178   C CG  . ASP A 22  ? 1.1081 0.7979 0.6855 0.0400  -0.0619 0.0078  38  ASP B CG  
179   O OD1 . ASP A 22  ? 1.0735 0.7653 0.6422 0.0407  -0.0678 -0.0006 38  ASP B OD1 
180   O OD2 . ASP A 22  ? 1.1510 0.8209 0.6983 0.0328  -0.0556 0.0180  38  ASP B OD2 
181   N N   . LEU A 23  ? 1.0722 0.8079 0.7295 0.0388  -0.0130 0.0096  39  LEU B N   
182   C CA  . LEU A 23  ? 1.0483 0.7842 0.6972 0.0316  0.0103  0.0170  39  LEU B CA  
183   C C   . LEU A 23  ? 1.0742 0.8317 0.7439 0.0342  0.0308  0.0089  39  LEU B C   
184   O O   . LEU A 23  ? 1.1255 0.8819 0.7786 0.0314  0.0514  0.0107  39  LEU B O   
185   C CB  . LEU A 23  ? 0.9707 0.7067 0.6345 0.0265  0.0099  0.0289  39  LEU B CB  
186   C CG  . LEU A 23  ? 0.9638 0.6720 0.5919 0.0205  -0.0015 0.0403  39  LEU B CG  
187   C CD1 . LEU A 23  ? 1.0177 0.7199 0.6575 0.0151  -0.0073 0.0520  39  LEU B CD1 
188   C CD2 . LEU A 23  ? 0.9996 0.7022 0.5959 0.0135  0.0187  0.0449  39  LEU B CD2 
189   N N   . PHE A 24  ? 1.0335 0.8106 0.7389 0.0402  0.0257  0.0003  40  PHE B N   
190   C CA  . PHE A 24  ? 1.0071 0.8037 0.7342 0.0432  0.0420  -0.0073 40  PHE B CA  
191   C C   . PHE A 24  ? 1.0569 0.8430 0.7573 0.0456  0.0455  -0.0169 40  PHE B C   
192   O O   . PHE A 24  ? 1.0737 0.8634 0.7714 0.0469  0.0650  -0.0201 40  PHE B O   
193   C CB  . PHE A 24  ? 0.9549 0.7731 0.7237 0.0478  0.0322  -0.0132 40  PHE B CB  
194   C CG  . PHE A 24  ? 0.9912 0.8303 0.7866 0.0505  0.0461  -0.0197 40  PHE B CG  
195   C CD1 . PHE A 24  ? 0.9655 0.8206 0.7850 0.0481  0.0620  -0.0134 40  PHE B CD1 
196   C CD2 . PHE A 24  ? 0.9926 0.8355 0.7899 0.0546  0.0416  -0.0309 40  PHE B CD2 
197   C CE1 . PHE A 24  ? 0.9234 0.7977 0.7688 0.0511  0.0732  -0.0184 40  PHE B CE1 
198   C CE2 . PHE A 24  ? 1.0167 0.8767 0.8383 0.0569  0.0529  -0.0361 40  PHE B CE2 
199   C CZ  . PHE A 24  ? 1.0143 0.8897 0.8600 0.0558  0.0688  -0.0299 40  PHE B CZ  
200   N N   . TYR A 25  ? 1.0642 0.8358 0.7431 0.0462  0.0262  -0.0212 41  TYR B N   
201   C CA  . TYR A 25  ? 1.0705 0.8273 0.7182 0.0462  0.0273  -0.0296 41  TYR B CA  
202   C C   . TYR A 25  ? 1.1254 0.8611 0.7308 0.0421  0.0435  -0.0250 41  TYR B C   
203   O O   . TYR A 25  ? 1.1933 0.9203 0.7782 0.0436  0.0574  -0.0321 41  TYR B O   
204   C CB  . TYR A 25  ? 1.0545 0.8012 0.6874 0.0457  0.0016  -0.0328 41  TYR B CB  
205   C CG  . TYR A 25  ? 1.0346 0.7702 0.6442 0.0446  -0.0005 -0.0432 41  TYR B CG  
206   C CD1 . TYR A 25  ? 1.0730 0.8251 0.7095 0.0472  -0.0048 -0.0522 41  TYR B CD1 
207   C CD2 . TYR A 25  ? 1.0283 0.7359 0.5883 0.0404  0.0043  -0.0442 41  TYR B CD2 
208   C CE1 . TYR A 25  ? 1.0800 0.8192 0.6946 0.0448  -0.0074 -0.0613 41  TYR B CE1 
209   C CE2 . TYR A 25  ? 1.0229 0.7167 0.5594 0.0389  0.0024  -0.0545 41  TYR B CE2 
210   C CZ  . TYR A 25  ? 1.0536 0.7625 0.6178 0.0408  -0.0039 -0.0628 41  TYR B CZ  
211   O OH  . TYR A 25  ? 1.1279 0.8206 0.6685 0.0379  -0.0074 -0.0726 41  TYR B OH  
212   N N   . GLN A 26  ? 1.1214 0.8479 0.7123 0.0372  0.0423  -0.0128 42  GLN B N   
213   C CA  . GLN A 26  ? 1.2159 0.9273 0.7700 0.0324  0.0602  -0.0061 42  GLN B CA  
214   C C   . GLN A 26  ? 1.2711 0.9988 0.8409 0.0357  0.0888  -0.0075 42  GLN B C   
215   O O   . GLN A 26  ? 1.3485 1.0660 0.8909 0.0381  0.1054  -0.0135 42  GLN B O   
216   C CB  . GLN A 26  ? 1.2907 0.9964 0.8393 0.0255  0.0551  0.0095  42  GLN B CB  
217   C CG  . GLN A 26  ? 1.2284 0.9145 0.7574 0.0227  0.0278  0.0144  42  GLN B CG  
218   C CD  . GLN A 26  ? 1.2962 0.9567 0.7758 0.0197  0.0204  0.0116  42  GLN B CD  
219   O OE1 . GLN A 26  ? 1.4346 1.0871 0.8869 0.0193  0.0363  0.0053  42  GLN B OE1 
220   N NE2 . GLN A 26  ? 1.3819 1.0278 0.8481 0.0180  -0.0048 0.0162  42  GLN B NE2 
221   N N   . SER A 27  ? 1.2072 0.9598 0.8206 0.0361  0.0945  -0.0016 43  SER B N   
222   C CA  . SER A 27  ? 1.2391 1.0118 0.8738 0.0390  0.1206  0.0000  43  SER B CA  
223   C C   . SER A 27  ? 1.2262 1.0025 0.8670 0.0479  0.1293  -0.0142 43  SER B C   
224   O O   . SER A 27  ? 1.3000 1.0785 0.9328 0.0525  0.1527  -0.0160 43  SER B O   
225   C CB  . SER A 27  ? 1.2145 1.0127 0.8966 0.0368  0.1197  0.0083  43  SER B CB  
226   O OG  . SER A 27  ? 1.2963 1.1146 0.9961 0.0373  0.1446  0.0146  43  SER B OG  
227   N N   . SER A 28  ? 1.1663 0.9436 0.8219 0.0507  0.1112  -0.0240 44  SER B N   
228   C CA  . SER A 28  ? 1.0961 0.8776 0.7622 0.0577  0.1182  -0.0360 44  SER B CA  
229   C C   . SER A 28  ? 1.2420 0.9945 0.8604 0.0596  0.1209  -0.0459 44  SER B C   
230   O O   . SER A 28  ? 1.3042 1.0536 0.9188 0.0662  0.1371  -0.0536 44  SER B O   
231   C CB  . SER A 28  ? 1.1291 0.9246 0.8293 0.0586  0.0987  -0.0417 44  SER B CB  
232   O OG  . SER A 28  ? 1.1737 0.9911 0.9109 0.0563  0.0950  -0.0328 44  SER B OG  
233   N N   . LEU A 29  ? 1.2578 0.9872 0.8381 0.0540  0.1054  -0.0457 45  LEU B N   
234   C CA  . LEU A 29  ? 1.2983 0.9974 0.8276 0.0544  0.1094  -0.0544 45  LEU B CA  
235   C C   . LEU A 29  ? 1.3806 1.0734 0.8847 0.0570  0.1376  -0.0506 45  LEU B C   
236   O O   . LEU A 29  ? 1.4717 1.1498 0.9520 0.0632  0.1535  -0.0602 45  LEU B O   
237   C CB  . LEU A 29  ? 1.3176 0.9942 0.8112 0.0467  0.0851  -0.0536 45  LEU B CB  
238   C CG  . LEU A 29  ? 1.3616 1.0066 0.8077 0.0448  0.0776  -0.0652 45  LEU B CG  
239   C CD1 . LEU A 29  ? 1.3725 1.0193 0.8347 0.0497  0.0783  -0.0781 45  LEU B CD1 
240   C CD2 . LEU A 29  ? 1.3340 0.9655 0.7592 0.0366  0.0478  -0.0626 45  LEU B CD2 
241   N N   . ALA A 30  ? 1.3358 1.0401 0.8459 0.0526  0.1450  -0.0365 46  ALA B N   
242   C CA  . ALA A 30  ? 1.4120 1.1176 0.9042 0.0548  0.1738  -0.0308 46  ALA B CA  
243   C C   . ALA A 30  ? 1.4724 1.1968 0.9939 0.0661  0.1973  -0.0362 46  ALA B C   
244   O O   . ALA A 30  ? 1.5684 1.2820 1.0630 0.0736  0.2196  -0.0422 46  ALA B O   
245   C CB  . ALA A 30  ? 1.4446 1.1649 0.9488 0.0464  0.1757  -0.0127 46  ALA B CB  
246   N N   . SER A 31  ? 1.4269 1.1784 1.0025 0.0681  0.1921  -0.0346 47  SER B N   
247   C CA  . SER A 31  ? 1.4063 1.1783 1.0147 0.0785  0.2126  -0.0374 47  SER B CA  
248   C C   . SER A 31  ? 1.4251 1.1759 1.0146 0.0878  0.2148  -0.0546 47  SER B C   
249   O O   . SER A 31  ? 1.4405 1.1903 1.0242 0.0986  0.2387  -0.0589 47  SER B O   
250   C CB  . SER A 31  ? 1.3358 1.1393 1.0031 0.0765  0.2031  -0.0313 47  SER B CB  
251   O OG  . SER A 31  ? 1.3707 1.1941 1.0711 0.0861  0.2201  -0.0333 47  SER B OG  
252   N N   . TRP A 32  ? 1.3836 1.1172 0.9636 0.0840  0.1901  -0.0640 48  TRP B N   
253   C CA  . TRP A 32  ? 1.3945 1.1032 0.9516 0.0903  0.1893  -0.0797 48  TRP B CA  
254   C C   . TRP A 32  ? 1.5737 1.2501 1.0718 0.0942  0.2053  -0.0862 48  TRP B C   
255   O O   . TRP A 32  ? 1.6446 1.3057 1.1281 0.1047  0.2206  -0.0969 48  TRP B O   
256   C CB  . TRP A 32  ? 1.3886 1.0851 0.9413 0.0824  0.1583  -0.0861 48  TRP B CB  
257   C CG  . TRP A 32  ? 1.4122 1.0782 0.9348 0.0848  0.1527  -0.1013 48  TRP B CG  
258   C CD1 . TRP A 32  ? 1.5284 1.1564 0.9925 0.0816  0.1480  -0.1094 48  TRP B CD1 
259   C CD2 . TRP A 32  ? 1.4136 1.0824 0.9613 0.0883  0.1469  -0.1095 48  TRP B CD2 
260   N NE1 . TRP A 32  ? 1.5342 1.1395 0.9844 0.0831  0.1406  -0.1225 48  TRP B NE1 
261   C CE2 . TRP A 32  ? 1.4513 1.0812 0.9528 0.0871  0.1396  -0.1224 48  TRP B CE2 
262   C CE3 . TRP A 32  ? 1.3822 1.0811 0.9849 0.0915  0.1468  -0.1067 48  TRP B CE3 
263   C CZ2 . TRP A 32  ? 1.4451 1.0646 0.9541 0.0887  0.1320  -0.1321 48  TRP B CZ2 
264   C CZ3 . TRP A 32  ? 1.4075 1.0978 1.0181 0.0934  0.1399  -0.1160 48  TRP B CZ3 
265   C CH2 . TRP A 32  ? 1.4325 1.0831 0.9969 0.0919  0.1324  -0.1283 48  TRP B CH2 
266   N N   . ASN A 33  ? 1.6193 1.2830 1.0807 0.0860  0.2021  -0.0798 49  ASN B N   
267   C CA  . ASN A 33  ? 1.7025 1.3344 1.1027 0.0886  0.2174  -0.0858 49  ASN B CA  
268   C C   . ASN A 33  ? 1.7675 1.4143 1.1725 0.1000  0.2532  -0.0821 49  ASN B C   
269   O O   . ASN A 33  ? 1.8056 1.4277 1.1669 0.1083  0.2719  -0.0915 49  ASN B O   
270   C CB  . ASN A 33  ? 1.7400 1.3555 1.0991 0.0760  0.2044  -0.0783 49  ASN B CB  
271   C CG  . ASN A 33  ? 1.7224 1.3207 1.0699 0.0657  0.1689  -0.0821 49  ASN B CG  
272   O OD1 . ASN A 33  ? 1.7762 1.3565 1.1139 0.0667  0.1566  -0.0948 49  ASN B OD1 
273   N ND2 . ASN A 33  ? 1.5865 1.1898 0.9338 0.0555  0.1520  -0.0702 49  ASN B ND2 
274   N N   . TYR A 34  ? 1.6522 1.3391 1.1091 0.1008  0.2632  -0.0684 50  TYR B N   
275   C CA  . TYR A 34  ? 1.7141 1.4211 1.1836 0.1126  0.2973  -0.0641 50  TYR B CA  
276   C C   . TYR A 34  ? 1.6559 1.3671 1.1515 0.1283  0.3084  -0.0749 50  TYR B C   
277   O O   . TYR A 34  ? 1.7088 1.4133 1.1870 0.1425  0.3350  -0.0810 50  TYR B O   
278   C CB  . TYR A 34  ? 1.6860 1.4347 1.2004 0.1063  0.3038  -0.0441 50  TYR B CB  
279   C CG  . TYR A 34  ? 1.6800 1.4582 1.2217 0.1187  0.3364  -0.0382 50  TYR B CG  
280   C CD1 . TYR A 34  ? 1.7483 1.5200 1.2532 0.1264  0.3648  -0.0384 50  TYR B CD1 
281   C CD2 . TYR A 34  ? 1.6469 1.4604 1.2507 0.1231  0.3390  -0.0321 50  TYR B CD2 
282   C CE1 . TYR A 34  ? 1.8117 1.6135 1.3436 0.1393  0.3954  -0.0327 50  TYR B CE1 
283   C CE2 . TYR A 34  ? 1.6734 1.5165 1.3048 0.1347  0.3679  -0.0254 50  TYR B CE2 
284   C CZ  . TYR A 34  ? 1.7669 1.6054 1.3636 0.1434  0.3965  -0.0255 50  TYR B CZ  
285   O OH  . TYR A 34  ? 1.8109 1.6830 1.4388 0.1557  0.4242  -0.0183 50  TYR B OH  
286   N N   . ASN A 35  ? 1.5752 1.2968 1.1115 0.1265  0.2889  -0.0773 51  ASN B N   
287   C CA  . ASN A 35  ? 1.5291 1.2569 1.0957 0.1396  0.2963  -0.0851 51  ASN B CA  
288   C C   . ASN A 35  ? 1.5679 1.2519 1.0922 0.1465  0.2919  -0.1045 51  ASN B C   
289   O O   . ASN A 35  ? 1.5821 1.2641 1.1239 0.1586  0.2991  -0.1120 51  ASN B O   
290   C CB  . ASN A 35  ? 1.5029 1.2584 1.1267 0.1330  0.2759  -0.0793 51  ASN B CB  
291   C CG  . ASN A 35  ? 1.4503 1.2512 1.1280 0.1338  0.2892  -0.0630 51  ASN B CG  
292   O OD1 . ASN A 35  ? 1.4845 1.3035 1.1939 0.1456  0.3052  -0.0621 51  ASN B OD1 
293   N ND2 . ASN A 35  ? 1.4021 1.2205 1.0901 0.1211  0.2815  -0.0494 51  ASN B ND2 
294   N N   . THR A 36  ? 1.6470 1.2946 1.1156 0.1385  0.2790  -0.1121 52  THR B N   
295   C CA  . THR A 36  ? 1.6711 1.2726 1.0922 0.1426  0.2736  -0.1301 52  THR B CA  
296   C C   . THR A 36  ? 1.7876 1.3567 1.1439 0.1480  0.2926  -0.1371 52  THR B C   
297   O O   . THR A 36  ? 1.9226 1.4563 1.2432 0.1482  0.2837  -0.1500 52  THR B O   
298   C CB  . THR A 36  ? 1.6358 1.2197 1.0450 0.1267  0.2374  -0.1341 52  THR B CB  
299   O OG1 . THR A 36  ? 1.6802 1.2656 1.0693 0.1136  0.2262  -0.1250 52  THR B OG1 
300   C CG2 . THR A 36  ? 1.5711 1.1848 1.0411 0.1226  0.2194  -0.1294 52  THR B CG2 
301   N N   . ASN A 37  ? 1.7909 1.3808 1.1455 0.1484  0.3122  -0.1254 53  ASN B N   
302   C CA  . ASN A 37  ? 1.8642 1.4360 1.1702 0.1475  0.3226  -0.1269 53  ASN B CA  
303   C C   . ASN A 37  ? 1.8689 1.4802 1.1984 0.1502  0.3479  -0.1104 53  ASN B C   
304   O O   . ASN A 37  ? 1.9007 1.5149 1.2089 0.1390  0.3478  -0.0998 53  ASN B O   
305   C CB  . ASN A 37  ? 2.0074 1.5439 1.2580 0.1313  0.2988  -0.1299 53  ASN B CB  
306   C CG  . ASN A 37  ? 2.1427 1.6590 1.3387 0.1277  0.3073  -0.1303 53  ASN B CG  
307   O OD1 . ASN A 37  ? 2.0670 1.5884 1.2590 0.1386  0.3302  -0.1324 53  ASN B OD1 
308   N ND2 . ASN A 37  ? 2.2345 1.7287 1.3889 0.1120  0.2873  -0.1276 53  ASN B ND2 
309   N N   . ILE A 38  ? 1.8286 1.4723 1.2050 0.1637  0.3677  -0.1067 54  ILE B N   
310   C CA  . ILE A 38  ? 1.8324 1.5196 1.2395 0.1656  0.3910  -0.0896 54  ILE B CA  
311   C C   . ILE A 38  ? 1.8775 1.5559 1.2389 0.1636  0.4052  -0.0879 54  ILE B C   
312   O O   . ILE A 38  ? 1.8775 1.5627 1.2384 0.1761  0.4245  -0.0919 54  ILE B O   
313   C CB  . ILE A 38  ? 1.8173 1.5383 1.2804 0.1815  0.4074  -0.0877 54  ILE B CB  
314   C CG1 . ILE A 38  ? 1.8002 1.5210 1.3005 0.1848  0.3916  -0.0933 54  ILE B CG1 
315   C CG2 . ILE A 38  ? 1.7191 1.4912 1.2248 0.1799  0.4257  -0.0672 54  ILE B CG2 
316   C CD1 . ILE A 38  ? 1.7993 1.5484 1.3503 0.2004  0.4049  -0.0919 54  ILE B CD1 
317   N N   . THR A 39  ? 1.9121 1.5747 1.2335 0.1482  0.3955  -0.0822 55  THR B N   
318   C CA  . THR A 39  ? 1.9825 1.6469 1.2688 0.1438  0.4105  -0.0753 55  THR B CA  
319   C C   . THR A 39  ? 1.9969 1.7009 1.3116 0.1339  0.4200  -0.0524 55  THR B C   
320   O O   . THR A 39  ? 1.9194 1.6421 1.2725 0.1292  0.4122  -0.0431 55  THR B O   
321   C CB  . THR A 39  ? 2.0061 1.6233 1.2229 0.1322  0.3927  -0.0834 55  THR B CB  
322   O OG1 . THR A 39  ? 1.9761 1.5840 1.1832 0.1160  0.3703  -0.0751 55  THR B OG1 
323   C CG2 . THR A 39  ? 2.0196 1.5964 1.2097 0.1390  0.3797  -0.1048 55  THR B CG2 
324   N N   . GLU A 40  ? 2.0826 1.8000 1.3783 0.1304  0.4375  -0.0428 56  GLU B N   
325   C CA  . GLU A 40  ? 2.0743 1.8262 1.3908 0.1177  0.4450  -0.0194 56  GLU B CA  
326   C C   . GLU A 40  ? 2.0161 1.7422 1.2987 0.0987  0.4224  -0.0115 56  GLU B C   
327   O O   . GLU A 40  ? 1.9481 1.6933 1.2589 0.0885  0.4171  0.0049  56  GLU B O   
328   C CB  . GLU A 40  ? 2.1765 1.9511 1.4814 0.1186  0.4696  -0.0115 56  GLU B CB  
329   C CG  . GLU A 40  ? 2.1850 1.9942 1.5065 0.1029  0.4769  0.0141  56  GLU B CG  
330   C CD  . GLU A 40  ? 2.0989 1.9492 1.4888 0.1018  0.4782  0.0286  56  GLU B CD  
331   O OE1 . GLU A 40  ? 2.0806 1.9530 1.5162 0.1170  0.4863  0.0223  56  GLU B OE1 
332   O OE2 . GLU A 40  ? 2.0255 1.8851 1.4227 0.0847  0.4702  0.0473  56  GLU B OE2 
333   N N   . GLU A 41  ? 2.0621 1.7441 1.2842 0.0933  0.4075  -0.0225 57  GLU B N   
334   C CA  . GLU A 41  ? 2.0384 1.6903 1.2269 0.0769  0.3805  -0.0181 57  GLU B CA  
335   C C   . GLU A 41  ? 1.9935 1.6563 1.2353 0.0744  0.3542  -0.0179 57  GLU B C   
336   O O   . GLU A 41  ? 1.9764 1.6505 1.2411 0.0603  0.3331  -0.0037 57  GLU B O   
337   C CB  . GLU A 41  ? 2.0977 1.7024 1.2255 0.0747  0.3638  -0.0343 57  GLU B CB  
338   C CG  . GLU A 41  ? 2.1388 1.7115 1.2365 0.0597  0.3297  -0.0329 57  GLU B CG  
339   C CD  . GLU A 41  ? 2.2694 1.7977 1.3103 0.0568  0.3121  -0.0484 57  GLU B CD  
340   O OE1 . GLU A 41  ? 2.2774 1.7953 1.3148 0.0688  0.3192  -0.0654 57  GLU B OE1 
341   O OE2 . GLU A 41  ? 2.3422 1.8460 1.3452 0.0422  0.2887  -0.0429 57  GLU B OE2 
342   N N   . ASN A 42  ? 2.0141 1.6750 1.2798 0.0879  0.3530  -0.0334 58  ASN B N   
343   C CA  . ASN A 42  ? 1.9535 1.6241 1.2679 0.0842  0.3246  -0.0343 58  ASN B CA  
344   C C   . ASN A 42  ? 1.8997 1.6179 1.2839 0.0843  0.3314  -0.0195 58  ASN B C   
345   O O   . ASN A 42  ? 1.8088 1.5384 1.2309 0.0765  0.3071  -0.0143 58  ASN B O   
346   C CB  . ASN A 42  ? 1.9168 1.5657 1.2286 0.0956  0.3174  -0.0551 58  ASN B CB  
347   C CG  . ASN A 42  ? 1.9672 1.5691 1.2197 0.0892  0.2956  -0.0677 58  ASN B CG  
348   O OD1 . ASN A 42  ? 2.0074 1.5981 1.2399 0.0749  0.2736  -0.0604 58  ASN B OD1 
349   N ND2 . ASN A 42  ? 2.0097 1.5829 1.2332 0.0996  0.3011  -0.0861 58  ASN B ND2 
350   N N   . VAL A 43  ? 1.9130 1.6595 1.3139 0.0927  0.3639  -0.0121 59  VAL B N   
351   C CA  . VAL A 43  ? 1.8394 1.6318 1.2988 0.0878  0.3706  0.0070  59  VAL B CA  
352   C C   . VAL A 43  ? 1.7882 1.5817 1.2414 0.0677  0.3532  0.0243  59  VAL B C   
353   O O   . VAL A 43  ? 1.7153 1.5276 1.2116 0.0585  0.3357  0.0347  59  VAL B O   
354   C CB  . VAL A 43  ? 1.8528 1.6761 1.3234 0.0985  0.4095  0.0147  59  VAL B CB  
355   C CG1 . VAL A 43  ? 1.7047 1.5767 1.2402 0.0923  0.4132  0.0345  59  VAL B CG1 
356   C CG2 . VAL A 43  ? 1.9092 1.7258 1.3765 0.1209  0.4298  -0.0028 59  VAL B CG2 
357   N N   . GLN A 44  ? 1.8308 1.6029 1.2284 0.0606  0.3585  0.0279  60  GLN B N   
358   C CA  . GLN A 44  ? 1.8388 1.6090 1.2262 0.0414  0.3429  0.0457  60  GLN B CA  
359   C C   . GLN A 44  ? 1.7954 1.5456 1.1901 0.0335  0.3040  0.0419  60  GLN B C   
360   O O   . GLN A 44  ? 1.7552 1.5179 1.1798 0.0223  0.2874  0.0555  60  GLN B O   
361   C CB  . GLN A 44  ? 1.9513 1.6972 1.2710 0.0359  0.3545  0.0483  60  GLN B CB  
362   C CG  . GLN A 44  ? 2.0163 1.7913 1.3330 0.0336  0.3886  0.0648  60  GLN B CG  
363   C CD  . GLN A 44  ? 2.0349 1.8455 1.3977 0.0190  0.3858  0.0892  60  GLN B CD  
364   O OE1 . GLN A 44  ? 1.9671 1.8186 1.3777 0.0238  0.4054  0.0976  60  GLN B OE1 
365   N NE2 . GLN A 44  ? 2.0231 1.8170 1.3700 0.0007  0.3612  0.1016  60  GLN B NE2 
366   N N   . ASN A 45  ? 1.8515 1.5711 1.2206 0.0398  0.2889  0.0233  61  ASN B N   
367   C CA  . ASN A 45  ? 1.8064 1.5100 1.1827 0.0334  0.2527  0.0199  61  ASN B CA  
368   C C   . ASN A 45  ? 1.7391 1.4700 1.1808 0.0364  0.2421  0.0204  61  ASN B C   
369   O O   . ASN A 45  ? 1.7118 1.4451 1.1741 0.0279  0.2187  0.0280  61  ASN B O   
370   C CB  . ASN A 45  ? 1.8529 1.5208 1.1885 0.0380  0.2389  0.0013  61  ASN B CB  
371   C CG  . ASN A 45  ? 1.9242 1.5610 1.1900 0.0338  0.2463  0.0002  61  ASN B CG  
372   O OD1 . ASN A 45  ? 1.8642 1.4784 1.0979 0.0227  0.2246  0.0052  61  ASN B OD1 
373   N ND2 . ASN A 45  ? 1.9863 1.6201 1.2268 0.0434  0.2763  -0.0070 61  ASN B ND2 
374   N N   . MET A 46  ? 1.7615 1.5112 1.2346 0.0488  0.2584  0.0119  62  MET B N   
375   C CA  . MET A 46  ? 1.7295 1.5067 1.2640 0.0509  0.2500  0.0134  62  MET B CA  
376   C C   . MET A 46  ? 1.6888 1.4921 1.2558 0.0400  0.2501  0.0333  62  MET B C   
377   O O   . MET A 46  ? 1.6566 1.4667 1.2547 0.0343  0.2289  0.0371  62  MET B O   
378   C CB  . MET A 46  ? 1.6788 1.4735 1.2398 0.0656  0.2712  0.0045  62  MET B CB  
379   C CG  . MET A 46  ? 1.5711 1.3941 1.1931 0.0672  0.2630  0.0064  62  MET B CG  
380   S SD  . MET A 46  ? 1.6126 1.4556 1.2638 0.0846  0.2889  -0.0014 62  MET B SD  
381   C CE  . MET A 46  ? 1.6501 1.5236 1.3696 0.0822  0.2726  0.0025  62  MET B CE  
382   N N   . ASN A 47  ? 1.6849 1.5029 1.2446 0.0368  0.2741  0.0464  63  ASN B N   
383   C CA  . ASN A 47  ? 1.6291 1.4715 1.2188 0.0241  0.2738  0.0670  63  ASN B CA  
384   C C   . ASN A 47  ? 1.5856 1.4053 1.1550 0.0096  0.2468  0.0754  63  ASN B C   
385   O O   . ASN A 47  ? 1.5519 1.3811 1.1537 0.0016  0.2307  0.0841  63  ASN B O   
386   C CB  . ASN A 47  ? 1.7046 1.5699 1.2895 0.0226  0.3056  0.0807  63  ASN B CB  
387   C CG  . ASN A 47  ? 1.6939 1.5932 1.3184 0.0366  0.3314  0.0780  63  ASN B CG  
388   O OD1 . ASN A 47  ? 1.5667 1.4844 1.2388 0.0404  0.3238  0.0755  63  ASN B OD1 
389   N ND2 . ASN A 47  ? 1.6978 1.6058 1.3018 0.0445  0.3621  0.0790  63  ASN B ND2 
390   N N   . ASN A 48  ? 1.6449 1.4327 1.1600 0.0062  0.2406  0.0729  64  ASN B N   
391   C CA  . ASN A 48  ? 1.6132 1.3780 1.1087 -0.0066 0.2139  0.0818  64  ASN B CA  
392   C C   . ASN A 48  ? 1.5528 1.3082 1.0711 -0.0036 0.1835  0.0725  64  ASN B C   
393   O O   . ASN A 48  ? 1.4948 1.2464 1.0266 -0.0119 0.1636  0.0821  64  ASN B O   
394   C CB  . ASN A 48  ? 1.6962 1.4286 1.1280 -0.0103 0.2127  0.0807  64  ASN B CB  
395   C CG  . ASN A 48  ? 1.7764 1.5176 1.1812 -0.0134 0.2436  0.0901  64  ASN B CG  
396   O OD1 . ASN A 48  ? 1.7449 1.5158 1.1777 -0.0186 0.2605  0.1047  64  ASN B OD1 
397   N ND2 . ASN A 48  ? 1.8440 1.5609 1.1941 -0.0105 0.2515  0.0820  64  ASN B ND2 
398   N N   . ALA A 49  ? 1.6300 1.3817 1.1527 0.0084  0.1799  0.0541  65  ALA B N   
399   C CA  . ALA A 49  ? 1.5859 1.3334 1.1320 0.0118  0.1530  0.0452  65  ALA B CA  
400   C C   . ALA A 49  ? 1.4746 1.2506 1.0776 0.0124  0.1517  0.0489  65  ALA B C   
401   O O   . ALA A 49  ? 1.4138 1.1876 1.0354 0.0089  0.1299  0.0518  65  ALA B O   
402   C CB  . ALA A 49  ? 1.5352 1.2722 1.0694 0.0224  0.1502  0.0261  65  ALA B CB  
403   N N   . GLY A 50  ? 1.5535 1.3557 1.1838 0.0173  0.1747  0.0486  66  GLY B N   
404   C CA  . GLY A 50  ? 1.4967 1.3267 1.1784 0.0155  0.1747  0.0547  66  GLY B CA  
405   C C   . GLY A 50  ? 1.4111 1.2432 1.0992 0.0016  0.1676  0.0729  66  GLY B C   
406   O O   . GLY A 50  ? 1.3497 1.1874 1.0673 -0.0020 0.1517  0.0756  66  GLY B O   
407   N N   . ASP A 51  ? 1.4093 1.2353 1.0680 -0.0070 0.1790  0.0859  67  ASP B N   
408   C CA  . ASP A 51  ? 1.4219 1.2461 1.0822 -0.0224 0.1711  0.1048  67  ASP B CA  
409   C C   . ASP A 51  ? 1.3344 1.1306 0.9853 -0.0256 0.1393  0.1031  67  ASP B C   
410   O O   . ASP A 51  ? 1.2603 1.0592 0.9368 -0.0319 0.1256  0.1099  67  ASP B O   
411   C CB  . ASP A 51  ? 1.4672 1.2870 1.0908 -0.0313 0.1881  0.1185  67  ASP B CB  
412   C CG  . ASP A 51  ? 1.5617 1.4169 1.2052 -0.0308 0.2200  0.1266  67  ASP B CG  
413   O OD1 . ASP A 51  ? 1.6176 1.5008 1.3072 -0.0261 0.2258  0.1249  67  ASP B OD1 
414   O OD2 . ASP A 51  ? 1.6277 1.4839 1.2408 -0.0343 0.2395  0.1346  67  ASP B OD2 
415   N N   . LYS A 52  ? 1.3885 1.1568 1.0017 -0.0212 0.1269  0.0946  68  LYS B N   
416   C CA  . LYS A 52  ? 1.3190 1.0619 0.9238 -0.0225 0.0967  0.0941  68  LYS B CA  
417   C C   . LYS A 52  ? 1.2069 0.9605 0.8531 -0.0148 0.0823  0.0840  68  LYS B C   
418   O O   . LYS A 52  ? 1.0916 0.8351 0.7485 -0.0182 0.0631  0.0887  68  LYS B O   
419   C CB  . LYS A 52  ? 1.3516 1.0677 0.9140 -0.0176 0.0855  0.0857  68  LYS B CB  
420   C CG  . LYS A 52  ? 1.3822 1.0821 0.8960 -0.0259 0.0963  0.0953  68  LYS B CG  
421   C CD  . LYS A 52  ? 1.4697 1.1391 0.9416 -0.0234 0.0779  0.0891  68  LYS B CD  
422   C CE  . LYS A 52  ? 1.5439 1.1968 0.9628 -0.0318 0.0905  0.0974  68  LYS B CE  
423   N NZ  . LYS A 52  ? 1.4807 1.1009 0.8542 -0.0332 0.0697  0.0960  68  LYS B NZ  
424   N N   . TRP A 53  ? 1.2571 1.0298 0.9251 -0.0043 0.0915  0.0700  69  TRP B N   
425   C CA  . TRP A 53  ? 1.1580 0.9438 0.8648 0.0025  0.0798  0.0603  69  TRP B CA  
426   C C   . TRP A 53  ? 1.1216 0.9255 0.8640 -0.0047 0.0828  0.0701  69  TRP B C   
427   O O   . TRP A 53  ? 1.0316 0.8324 0.7926 -0.0042 0.0653  0.0683  69  TRP B O   
428   C CB  . TRP A 53  ? 1.1434 0.9447 0.8629 0.0134  0.0899  0.0450  69  TRP B CB  
429   C CG  . TRP A 53  ? 1.0482 0.8704 0.8109 0.0190  0.0848  0.0368  69  TRP B CG  
430   C CD1 . TRP A 53  ? 1.0643 0.9124 0.8580 0.0214  0.1007  0.0349  69  TRP B CD1 
431   C CD2 . TRP A 53  ? 1.0743 0.8937 0.8527 0.0233  0.0624  0.0297  69  TRP B CD2 
432   N NE1 . TRP A 53  ? 1.0660 0.9265 0.8919 0.0255  0.0892  0.0274  69  TRP B NE1 
433   C CE2 . TRP A 53  ? 1.0293 0.8734 0.8464 0.0269  0.0666  0.0237  69  TRP B CE2 
434   C CE3 . TRP A 53  ? 1.0840 0.8833 0.8479 0.0253  0.0396  0.0281  69  TRP B CE3 
435   C CZ2 . TRP A 53  ? 0.9772 0.8268 0.8167 0.0317  0.0500  0.0159  69  TRP B CZ2 
436   C CZ3 . TRP A 53  ? 0.9901 0.7962 0.7788 0.0318  0.0235  0.0201  69  TRP B CZ3 
437   C CH2 . TRP A 53  ? 0.9579 0.7891 0.7829 0.0345  0.0295  0.0138  69  TRP B CH2 
438   N N   . SER A 54  ? 1.1947 1.0185 0.9473 -0.0111 0.1048  0.0803  70  SER B N   
439   C CA  . SER A 54  ? 1.0972 0.9379 0.8813 -0.0211 0.1063  0.0927  70  SER B CA  
440   C C   . SER A 54  ? 1.0441 0.8603 0.8144 -0.0322 0.0869  0.1040  70  SER B C   
441   O O   . SER A 54  ? 1.0140 0.8294 0.8063 -0.0356 0.0730  0.1051  70  SER B O   
442   C CB  . SER A 54  ? 1.1402 1.0065 0.9336 -0.0275 0.1330  0.1053  70  SER B CB  
443   O OG  . SER A 54  ? 1.1992 1.0914 1.0174 -0.0168 0.1496  0.0960  70  SER B OG  
444   N N   . ALA A 55  ? 1.1593 0.9528 0.8905 -0.0380 0.0851  0.1123  71  ALA B N   
445   C CA  . ALA A 55  ? 1.1326 0.8993 0.8467 -0.0497 0.0670  0.1253  71  ALA B CA  
446   C C   . ALA A 55  ? 1.1155 0.8581 0.8290 -0.0412 0.0396  0.1148  71  ALA B C   
447   O O   . ALA A 55  ? 1.0444 0.7705 0.7621 -0.0477 0.0231  0.1214  71  ALA B O   
448   C CB  . ALA A 55  ? 1.1784 0.9266 0.8487 -0.0571 0.0718  0.1362  71  ALA B CB  
449   N N   . PHE A 56  ? 1.1390 0.8792 0.8469 -0.0266 0.0345  0.0984  72  PHE B N   
450   C CA  . PHE A 56  ? 1.0699 0.7957 0.7837 -0.0158 0.0111  0.0871  72  PHE B CA  
451   C C   . PHE A 56  ? 1.0410 0.7845 0.7948 -0.0123 0.0082  0.0801  72  PHE B C   
452   O O   . PHE A 56  ? 1.0456 0.7738 0.8050 -0.0094 -0.0105 0.0778  72  PHE B O   
453   C CB  . PHE A 56  ? 1.0297 0.7549 0.7310 -0.0029 0.0081  0.0729  72  PHE B CB  
454   C CG  . PHE A 56  ? 0.9910 0.7131 0.7071 0.0096  -0.0118 0.0604  72  PHE B CG  
455   C CD1 . PHE A 56  ? 1.0011 0.6964 0.7033 0.0125  -0.0343 0.0633  72  PHE B CD1 
456   C CD2 . PHE A 56  ? 0.9791 0.7259 0.7238 0.0190  -0.0078 0.0462  72  PHE B CD2 
457   C CE1 . PHE A 56  ? 0.9471 0.6426 0.6645 0.0259  -0.0512 0.0519  72  PHE B CE1 
458   C CE2 . PHE A 56  ? 0.9500 0.6976 0.7090 0.0303  -0.0248 0.0355  72  PHE B CE2 
459   C CZ  . PHE A 56  ? 0.9730 0.6962 0.7191 0.0345  -0.0459 0.0381  72  PHE B CZ  
460   N N   . LEU A 57  ? 1.0672 0.8419 0.8479 -0.0112 0.0259  0.0757  73  LEU B N   
461   C CA  . LEU A 57  ? 1.0493 0.8408 0.8665 -0.0102 0.0231  0.0710  73  LEU B CA  
462   C C   . LEU A 57  ? 1.0585 0.8398 0.8803 -0.0239 0.0165  0.0848  73  LEU B C   
463   O O   . LEU A 57  ? 0.9934 0.7642 0.8253 -0.0222 0.0006  0.0806  73  LEU B O   
464   C CB  . LEU A 57  ? 1.0248 0.8509 0.8698 -0.0084 0.0433  0.0670  73  LEU B CB  
465   C CG  . LEU A 57  ? 0.9431 0.7796 0.7948 0.0057  0.0436  0.0498  73  LEU B CG  
466   C CD1 . LEU A 57  ? 0.9250 0.7915 0.8010 0.0073  0.0638  0.0474  73  LEU B CD1 
467   C CD2 . LEU A 57  ? 0.8750 0.7080 0.7414 0.0129  0.0245  0.0396  73  LEU B CD2 
468   N N   . LYS A 58  ? 1.0215 0.8064 0.8357 -0.0381 0.0290  0.1014  74  LYS B N   
469   C CA  . LYS A 58  ? 1.0666 0.8413 0.8839 -0.0542 0.0216  0.1167  74  LYS B CA  
470   C C   . LYS A 58  ? 1.0741 0.8075 0.8669 -0.0537 -0.0034 0.1170  74  LYS B C   
471   O O   . LYS A 58  ? 1.0893 0.8082 0.8899 -0.0585 -0.0179 0.1185  74  LYS B O   
472   C CB  . LYS A 58  ? 1.1513 0.9373 0.9610 -0.0700 0.0391  0.1363  74  LYS B CB  
473   C CG  . LYS A 58  ? 1.3411 1.1272 1.1625 -0.0904 0.0352  0.1548  74  LYS B CG  
474   C CD  . LYS A 58  ? 1.4494 1.2578 1.2709 -0.1065 0.0558  0.1756  74  LYS B CD  
475   C CE  . LYS A 58  ? 1.5216 1.3762 1.3733 -0.1012 0.0824  0.1741  74  LYS B CE  
476   N NZ  . LYS A 58  ? 1.4279 1.3058 1.3212 -0.1004 0.0806  0.1694  74  LYS B NZ  
477   N N   . GLU A 59  ? 1.1597 0.8722 0.9223 -0.0464 -0.0097 0.1142  75  GLU B N   
478   C CA  . GLU A 59  ? 1.1928 0.8650 0.9315 -0.0452 -0.0336 0.1164  75  GLU B CA  
479   C C   . GLU A 59  ? 1.1161 0.7801 0.8681 -0.0289 -0.0507 0.0994  75  GLU B C   
480   O O   . GLU A 59  ? 1.1339 0.7708 0.8816 -0.0297 -0.0686 0.1008  75  GLU B O   
481   C CB  . GLU A 59  ? 1.2912 0.9446 0.9931 -0.0436 -0.0359 0.1208  75  GLU B CB  
482   C CG  . GLU A 59  ? 1.4085 1.0224 1.0871 -0.0370 -0.0614 0.1202  75  GLU B CG  
483   C CD  . GLU A 59  ? 1.5738 1.1571 1.2430 -0.0506 -0.0755 0.1345  75  GLU B CD  
484   O OE1 . GLU A 59  ? 1.5988 1.1928 1.2778 -0.0679 -0.0653 0.1469  75  GLU B OE1 
485   O OE2 . GLU A 59  ? 1.6640 1.2113 1.3154 -0.0444 -0.0977 0.1342  75  GLU B OE2 
486   N N   . GLN A 60  ? 1.0783 0.7661 0.8472 -0.0143 -0.0451 0.0834  76  GLN B N   
487   C CA  . GLN A 60  ? 1.0302 0.7154 0.8139 0.0008  -0.0592 0.0682  76  GLN B CA  
488   C C   . GLN A 60  ? 1.0968 0.7932 0.9074 -0.0041 -0.0581 0.0661  76  GLN B C   
489   O O   . GLN A 60  ? 1.1480 0.8290 0.9623 0.0033  -0.0731 0.0585  76  GLN B O   
490   C CB  . GLN A 60  ? 0.9649 0.6739 0.7599 0.0159  -0.0546 0.0529  76  GLN B CB  
491   C CG  . GLN A 60  ? 1.0020 0.6982 0.7705 0.0226  -0.0605 0.0523  76  GLN B CG  
492   C CD  . GLN A 60  ? 0.9988 0.6642 0.7508 0.0322  -0.0838 0.0515  76  GLN B CD  
493   O OE1 . GLN A 60  ? 0.9643 0.6305 0.7313 0.0456  -0.0954 0.0405  76  GLN B OE1 
494   N NE2 . GLN A 60  ? 1.0794 0.7176 0.7995 0.0260  -0.0906 0.0635  76  GLN B NE2 
495   N N   . SER A 61  ? 1.1264 0.8502 0.9559 -0.0156 -0.0405 0.0723  77  SER B N   
496   C CA  . SER A 61  ? 1.0740 0.8069 0.9268 -0.0240 -0.0406 0.0739  77  SER B CA  
497   C C   . SER A 61  ? 1.1851 0.8813 1.0211 -0.0341 -0.0576 0.0833  77  SER B C   
498   O O   . SER A 61  ? 1.2158 0.8960 1.0548 -0.0287 -0.0718 0.0748  77  SER B O   
499   C CB  . SER A 61  ? 1.0900 0.8561 0.9631 -0.0368 -0.0197 0.0841  77  SER B CB  
500   O OG  . SER A 61  ? 1.1355 0.9141 1.0334 -0.0453 -0.0205 0.0859  77  SER B OG  
501   N N   . THR A 62  ? 1.2434 0.9229 1.0581 -0.0485 -0.0570 0.1006  78  THR B N   
502   C CA  . THR A 62  ? 1.2751 0.9157 1.0711 -0.0602 -0.0747 0.1112  78  THR B CA  
503   C C   . THR A 62  ? 1.2068 0.8099 0.9839 -0.0438 -0.0963 0.0998  78  THR B C   
504   O O   . THR A 62  ? 1.2711 0.8421 1.0396 -0.0472 -0.1129 0.1005  78  THR B O   
505   C CB  . THR A 62  ? 1.2928 0.9223 1.0668 -0.0781 -0.0706 0.1325  78  THR B CB  
506   O OG1 . THR A 62  ? 1.3993 1.0675 1.1937 -0.0917 -0.0488 0.1434  78  THR B OG1 
507   C CG2 . THR A 62  ? 1.3491 0.9373 1.1044 -0.0930 -0.0898 0.1450  78  THR B CG2 
508   N N   . LEU A 63  ? 1.2358 0.8423 1.0066 -0.0257 -0.0969 0.0890  79  LEU B N   
509   C CA  . LEU A 63  ? 1.2854 0.8617 1.0430 -0.0077 -0.1168 0.0782  79  LEU B CA  
510   C C   . LEU A 63  ? 1.2498 0.8363 1.0296 0.0060  -0.1207 0.0606  79  LEU B C   
511   O O   . LEU A 63  ? 1.2344 0.7931 1.0053 0.0193  -0.1374 0.0523  79  LEU B O   
512   C CB  . LEU A 63  ? 1.1528 0.7326 0.8987 0.0065  -0.1176 0.0734  79  LEU B CB  
513   C CG  . LEU A 63  ? 1.1624 0.7089 0.8744 -0.0012 -0.1268 0.0886  79  LEU B CG  
514   C CD1 . LEU A 63  ? 1.2845 0.8431 0.9868 0.0078  -0.1227 0.0857  79  LEU B CD1 
515   C CD2 . LEU A 63  ? 1.1663 0.6697 0.8631 0.0081  -0.1506 0.0866  79  LEU B CD2 
516   N N   . ALA A 64  ? 1.2829 0.9086 1.0905 0.0043  -0.1053 0.0547  80  ALA B N   
517   C CA  . ALA A 64  ? 1.3007 0.9420 1.1287 0.0192  -0.1071 0.0370  80  ALA B CA  
518   C C   . ALA A 64  ? 1.3737 1.0034 1.2080 0.0111  -0.1130 0.0360  80  ALA B C   
519   O O   . ALA A 64  ? 1.3521 0.9755 1.1907 0.0246  -0.1214 0.0219  80  ALA B O   
520   C CB  . ALA A 64  ? 1.2959 0.9839 1.1493 0.0223  -0.0892 0.0305  80  ALA B CB  
521   N N   . GLN A 65  ? 1.4819 1.1071 1.3148 -0.0113 -0.1095 0.0516  81  GLN B N   
522   C CA  . GLN A 65  ? 1.3789 0.9931 1.2162 -0.0251 -0.1154 0.0547  81  GLN B CA  
523   C C   . GLN A 65  ? 1.3911 0.9544 1.2019 -0.0229 -0.1361 0.0536  81  GLN B C   
524   O O   . GLN A 65  ? 1.5085 1.0502 1.3134 -0.0367 -0.1450 0.0584  81  GLN B O   
525   C CB  . GLN A 65  ? 1.3018 0.9333 1.1485 -0.0504 -0.1042 0.0743  81  GLN B CB  
526   C CG  . GLN A 65  ? 1.3052 0.9894 1.1851 -0.0525 -0.0836 0.0733  81  GLN B CG  
527   C CD  . GLN A 65  ? 1.5442 1.2487 1.4328 -0.0728 -0.0701 0.0934  81  GLN B CD  
528   O OE1 . GLN A 65  ? 1.6008 1.2846 1.4769 -0.0906 -0.0771 0.1089  81  GLN B OE1 
529   N NE2 . GLN A 65  ? 1.7484 1.4946 1.6593 -0.0701 -0.0503 0.0934  81  GLN B NE2 
530   N N   . MET A 66  ? 1.5964 1.1407 1.3911 -0.0041 -0.1445 0.0466  82  MET B N   
531   C CA  . MET A 66  ? 1.7465 1.2398 1.5145 0.0058  -0.1653 0.0427  82  MET B CA  
532   C C   . MET A 66  ? 1.6240 1.1180 1.3983 0.0327  -0.1708 0.0208  82  MET B C   
533   O O   . MET A 66  ? 1.6136 1.0687 1.3678 0.0473  -0.1868 0.0152  82  MET B O   
534   C CB  . MET A 66  ? 1.8811 1.3498 1.6248 0.0073  -0.1725 0.0537  82  MET B CB  
535   C CG  . MET A 66  ? 1.9118 1.3744 1.6438 -0.0200 -0.1685 0.0770  82  MET B CG  
536   S SD  . MET A 66  ? 2.1055 1.5472 1.8094 -0.0167 -0.1742 0.0885  82  MET B SD  
537   C CE  . MET A 66  ? 1.9363 1.3930 1.6358 -0.0478 -0.1599 0.1136  82  MET B CE  
538   N N   . TYR A 67  ? 1.3185 0.8562 1.1204 0.0398  -0.1577 0.0091  83  TYR B N   
539   C CA  . TYR A 67  ? 1.2756 0.8214 1.0867 0.0631  -0.1604 -0.0109 83  TYR B CA  
540   C C   . TYR A 67  ? 1.2874 0.8600 1.1191 0.0544  -0.1511 -0.0169 83  TYR B C   
541   O O   . TYR A 67  ? 1.2428 0.8603 1.0993 0.0492  -0.1357 -0.0161 83  TYR B O   
542   C CB  . TYR A 67  ? 1.2954 0.8752 1.1217 0.0826  -0.1537 -0.0195 83  TYR B CB  
543   C CG  . TYR A 67  ? 1.2717 0.8378 1.0828 0.0901  -0.1602 -0.0125 83  TYR B CG  
544   C CD1 . TYR A 67  ? 1.2608 0.8363 1.0681 0.0750  -0.1524 0.0019  83  TYR B CD1 
545   C CD2 . TYR A 67  ? 1.1966 0.7397 0.9960 0.1122  -0.1743 -0.0197 83  TYR B CD2 
546   C CE1 . TYR A 67  ? 1.2335 0.7948 1.0236 0.0802  -0.1590 0.0088  83  TYR B CE1 
547   C CE2 . TYR A 67  ? 1.2131 0.7428 0.9980 0.1176  -0.1818 -0.0118 83  TYR B CE2 
548   C CZ  . TYR A 67  ? 1.1795 0.7179 0.9587 0.1007  -0.1745 0.0025  83  TYR B CZ  
549   O OH  . TYR A 67  ? 1.2433 0.7681 1.0052 0.1046  -0.1822 0.0109  83  TYR B OH  
550   N N   . PRO A 68  ? 1.3576 0.9035 1.1789 0.0531  -0.1605 -0.0235 84  PRO B N   
551   C CA  . PRO A 68  ? 1.2606 0.8249 1.0963 0.0367  -0.1541 -0.0235 84  PRO B CA  
552   C C   . PRO A 68  ? 1.2528 0.8564 1.1115 0.0503  -0.1445 -0.0397 84  PRO B C   
553   O O   . PRO A 68  ? 1.2782 0.8725 1.1307 0.0711  -0.1499 -0.0556 84  PRO B O   
554   C CB  . PRO A 68  ? 1.2720 0.7838 1.0803 0.0299  -0.1709 -0.0243 84  PRO B CB  
555   C CG  . PRO A 68  ? 1.3425 0.8192 1.1296 0.0545  -0.1829 -0.0353 84  PRO B CG  
556   C CD  . PRO A 68  ? 1.4040 0.8952 1.1958 0.0636  -0.1788 -0.0290 84  PRO B CD  
557   N N   . LEU A 69  ? 1.2283 0.8760 1.1136 0.0381  -0.1302 -0.0350 85  LEU B N   
558   C CA  . LEU A 69  ? 1.1841 0.8716 1.0923 0.0480  -0.1207 -0.0480 85  LEU B CA  
559   C C   . LEU A 69  ? 1.2513 0.9214 1.1492 0.0547  -0.1285 -0.0621 85  LEU B C   
560   O O   . LEU A 69  ? 1.2527 0.9457 1.1610 0.0704  -0.1241 -0.0764 85  LEU B O   
561   C CB  . LEU A 69  ? 1.0118 0.7402 0.9469 0.0305  -0.1071 -0.0391 85  LEU B CB  
562   C CG  . LEU A 69  ? 1.0318 0.7813 0.9790 0.0207  -0.0960 -0.0247 85  LEU B CG  
563   C CD1 . LEU A 69  ? 1.0388 0.8242 1.0121 0.0049  -0.0839 -0.0166 85  LEU B CD1 
564   C CD2 . LEU A 69  ? 1.1014 0.8705 1.0548 0.0386  -0.0904 -0.0321 85  LEU B CD2 
565   N N   . GLN A 70  ? 1.3549 0.9849 1.2312 0.0419  -0.1400 -0.0579 86  GLN B N   
566   C CA  . GLN A 70  ? 1.4265 1.0344 1.2878 0.0463  -0.1479 -0.0714 86  GLN B CA  
567   C C   . GLN A 70  ? 1.3972 0.9910 1.2461 0.0766  -0.1521 -0.0895 86  GLN B C   
568   O O   . GLN A 70  ? 1.3882 0.9956 1.2403 0.0889  -0.1488 -0.1048 86  GLN B O   
569   C CB  . GLN A 70  ? 1.4582 1.0201 1.2952 0.0245  -0.1615 -0.0611 86  GLN B CB  
570   C CG  . GLN A 70  ? 1.5700 1.1024 1.3867 0.0200  -0.1716 -0.0711 86  GLN B CG  
571   C CD  . GLN A 70  ? 1.7080 1.1776 1.4859 0.0337  -0.1879 -0.0809 86  GLN B CD  
572   O OE1 . GLN A 70  ? 1.7481 1.1902 1.5131 0.0383  -0.1949 -0.0741 86  GLN B OE1 
573   N NE2 . GLN A 70  ? 1.7736 1.2185 1.5311 0.0404  -0.1944 -0.0967 86  GLN B NE2 
574   N N   . GLU A 71  ? 1.5045 1.0787 1.3432 0.0897  -0.1576 -0.0872 87  GLU B N   
575   C CA  . GLU A 71  ? 1.4958 1.0567 1.3248 0.1197  -0.1626 -0.1019 87  GLU B CA  
576   C C   . GLU A 71  ? 1.4186 1.0281 1.2741 0.1365  -0.1518 -0.1060 87  GLU B C   
577   O O   . GLU A 71  ? 1.4143 1.0159 1.2653 0.1588  -0.1568 -0.1113 87  GLU B O   
578   C CB  . GLU A 71  ? 1.5463 1.0537 1.3473 0.1246  -0.1778 -0.0961 87  GLU B CB  
579   C CG  . GLU A 71  ? 1.6943 1.1454 1.4641 0.1116  -0.1918 -0.0941 87  GLU B CG  
580   C CD  . GLU A 71  ? 1.8786 1.2794 1.6226 0.1130  -0.2067 -0.0847 87  GLU B CD  
581   O OE1 . GLU A 71  ? 2.0210 1.3909 1.7483 0.1380  -0.2161 -0.0950 87  GLU B OE1 
582   O OE2 . GLU A 71  ? 1.9095 1.3026 1.6506 0.0883  -0.2087 -0.0659 87  GLU B OE2 
583   N N   . ILE A 72  ? 1.3441 1.0028 1.2270 0.1260  -0.1383 -0.1028 88  ILE B N   
584   C CA  . ILE A 72  ? 1.2478 0.9519 1.1551 0.1377  -0.1288 -0.1049 88  ILE B CA  
585   C C   . ILE A 72  ? 1.2713 1.0182 1.2002 0.1392  -0.1181 -0.1145 88  ILE B C   
586   O O   . ILE A 72  ? 1.2918 1.0521 1.2293 0.1203  -0.1123 -0.1102 88  ILE B O   
587   C CB  . ILE A 72  ? 1.1806 0.9008 1.0983 0.1225  -0.1229 -0.0891 88  ILE B CB  
588   C CG1 . ILE A 72  ? 1.2740 0.9495 1.1670 0.1184  -0.1339 -0.0783 88  ILE B CG1 
589   C CG2 . ILE A 72  ? 1.1288 0.8921 1.0685 0.1330  -0.1147 -0.0919 88  ILE B CG2 
590   C CD1 . ILE A 72  ? 1.2879 0.9745 1.1849 0.1098  -0.1293 -0.0648 88  ILE B CD1 
591   N N   . GLN A 73  ? 1.2169 0.9866 1.1555 0.1611  -0.1158 -0.1263 89  GLN B N   
592   C CA  . GLN A 73  ? 1.1627 0.9724 1.1195 0.1651  -0.1065 -0.1364 89  GLN B CA  
593   C C   . GLN A 73  ? 1.1584 1.0133 1.1401 0.1744  -0.0998 -0.1362 89  GLN B C   
594   O O   . GLN A 73  ? 1.2499 1.1189 1.2365 0.1958  -0.1004 -0.1460 89  GLN B O   
595   C CB  . GLN A 73  ? 1.2309 1.0235 1.1728 0.1833  -0.1103 -0.1520 89  GLN B CB  
596   C CG  . GLN A 73  ? 1.3992 1.1362 1.3097 0.1771  -0.1206 -0.1531 89  GLN B CG  
597   C CD  . GLN A 73  ? 1.4707 1.1624 1.3591 0.1924  -0.1331 -0.1531 89  GLN B CD  
598   O OE1 . GLN A 73  ? 1.5557 1.2067 1.4252 0.1788  -0.1423 -0.1431 89  GLN B OE1 
599   N NE2 . GLN A 73  ? 1.5268 1.2267 1.4187 0.2203  -0.1339 -0.1631 89  GLN B NE2 
600   N N   . ASN A 74  ? 1.0470 0.9241 1.0438 0.1590  -0.0937 -0.1251 90  ASN B N   
601   C CA  . ASN A 74  ? 1.0401 0.9569 1.0578 0.1663  -0.0890 -0.1249 90  ASN B CA  
602   C C   . ASN A 74  ? 1.0036 0.9517 1.0402 0.1478  -0.0790 -0.1178 90  ASN B C   
603   O O   . ASN A 74  ? 1.0585 1.0442 1.1143 0.1507  -0.0740 -0.1196 90  ASN B O   
604   C CB  . ASN A 74  ? 1.0583 0.9599 1.0680 0.1746  -0.0964 -0.1189 90  ASN B CB  
605   C CG  . ASN A 74  ? 0.9637 0.9044 0.9931 0.1783  -0.0931 -0.1168 90  ASN B CG  
606   O OD1 . ASN A 74  ? 0.9120 0.8684 0.9499 0.1633  -0.0867 -0.1094 90  ASN B OD1 
607   N ND2 . ASN A 74  ? 0.9580 0.9130 0.9938 0.1985  -0.0982 -0.1230 90  ASN B ND2 
608   N N   . LEU A 75  ? 1.0478 0.9807 1.0796 0.1289  -0.0766 -0.1091 91  LEU B N   
609   C CA  . LEU A 75  ? 1.0114 0.9695 1.0606 0.1115  -0.0669 -0.1014 91  LEU B CA  
610   C C   . LEU A 75  ? 0.9436 0.9070 0.9957 0.1084  -0.0640 -0.0928 91  LEU B C   
611   O O   . LEU A 75  ? 0.9841 0.9347 1.0319 0.0950  -0.0607 -0.0824 91  LEU B O   
612   C CB  . LEU A 75  ? 1.0054 1.0035 1.0753 0.1117  -0.0604 -0.1079 91  LEU B CB  
613   C CG  . LEU A 75  ? 1.0592 1.0609 1.1276 0.1138  -0.0609 -0.1173 91  LEU B CG  
614   C CD1 . LEU A 75  ? 1.0682 1.1133 1.1586 0.1103  -0.0534 -0.1202 91  LEU B CD1 
615   C CD2 . LEU A 75  ? 0.9389 0.9109 0.9934 0.1007  -0.0640 -0.1137 91  LEU B CD2 
616   N N   . THR A 76  ? 0.8887 0.8717 0.9478 0.1195  -0.0648 -0.0963 92  THR B N   
617   C CA  . THR A 76  ? 0.8556 0.8386 0.9122 0.1157  -0.0631 -0.0886 92  THR B CA  
618   C C   . THR A 76  ? 0.8934 0.8385 0.9268 0.1161  -0.0694 -0.0819 92  THR B C   
619   O O   . THR A 76  ? 0.9500 0.8862 0.9768 0.1051  -0.0648 -0.0724 92  THR B O   
620   C CB  . THR A 76  ? 0.8219 0.8321 0.8892 0.1258  -0.0651 -0.0931 92  THR B CB  
621   O OG1 . THR A 76  ? 0.9275 0.9389 0.9940 0.1433  -0.0731 -0.1014 92  THR B OG1 
622   C CG2 . THR A 76  ? 0.6790 0.7252 0.7677 0.1186  -0.0573 -0.0948 92  THR B CG2 
623   N N   . VAL A 77  ? 0.9195 0.8406 0.9393 0.1279  -0.0795 -0.0862 93  VAL B N   
624   C CA  . VAL A 77  ? 0.9386 0.8190 0.9347 0.1255  -0.0865 -0.0786 93  VAL B CA  
625   C C   . VAL A 77  ? 0.9731 0.8378 0.9645 0.1073  -0.0820 -0.0708 93  VAL B C   
626   O O   . VAL A 77  ? 0.9453 0.7923 0.9251 0.0960  -0.0807 -0.0594 93  VAL B O   
627   C CB  . VAL A 77  ? 0.9022 0.7578 0.8848 0.1433  -0.0991 -0.0856 93  VAL B CB  
628   C CG1 . VAL A 77  ? 0.9519 0.7620 0.9086 0.1389  -0.1077 -0.0768 93  VAL B CG1 
629   C CG2 . VAL A 77  ? 0.8151 0.6889 0.8047 0.1609  -0.1040 -0.0906 93  VAL B CG2 
630   N N   . LYS A 78  ? 0.9685 0.8407 0.9687 0.1035  -0.0799 -0.0762 94  LYS B N   
631   C CA  . LYS A 78  ? 0.9665 0.8274 0.9652 0.0851  -0.0770 -0.0681 94  LYS B CA  
632   C C   . LYS A 78  ? 0.9487 0.8327 0.9624 0.0703  -0.0647 -0.0578 94  LYS B C   
633   O O   . LYS A 78  ? 1.0373 0.9086 1.0460 0.0560  -0.0621 -0.0458 94  LYS B O   
634   C CB  . LYS A 78  ? 1.0014 0.8683 1.0059 0.0852  -0.0782 -0.0772 94  LYS B CB  
635   C CG  . LYS A 78  ? 1.0580 0.8895 1.0448 0.0761  -0.0863 -0.0749 94  LYS B CG  
636   C CD  . LYS A 78  ? 1.0893 0.9334 1.0830 0.0751  -0.0854 -0.0842 94  LYS B CD  
637   C CE  . LYS A 78  ? 1.2575 1.0683 1.2337 0.0628  -0.0938 -0.0819 94  LYS B CE  
638   N NZ  . LYS A 78  ? 1.3310 1.1631 1.3187 0.0547  -0.0902 -0.0863 94  LYS B NZ  
639   N N   . LEU A 79  ? 0.8894 0.8069 0.9210 0.0741  -0.0570 -0.0617 95  LEU B N   
640   C CA  . LEU A 79  ? 0.8901 0.8263 0.9341 0.0628  -0.0451 -0.0530 95  LEU B CA  
641   C C   . LEU A 79  ? 0.8505 0.7694 0.8785 0.0606  -0.0435 -0.0440 95  LEU B C   
642   O O   . LEU A 79  ? 0.8879 0.8054 0.9167 0.0482  -0.0354 -0.0330 95  LEU B O   
643   C CB  . LEU A 79  ? 0.8225 0.7920 0.8844 0.0681  -0.0395 -0.0596 95  LEU B CB  
644   C CG  . LEU A 79  ? 0.7658 0.7582 0.8467 0.0647  -0.0371 -0.0645 95  LEU B CG  
645   C CD1 . LEU A 79  ? 0.7119 0.7345 0.8083 0.0682  -0.0321 -0.0688 95  LEU B CD1 
646   C CD2 . LEU A 79  ? 0.7659 0.7585 0.8550 0.0488  -0.0314 -0.0548 95  LEU B CD2 
647   N N   . GLN A 80  ? 0.8208 0.7273 0.8340 0.0725  -0.0511 -0.0479 96  GLN B N   
648   C CA  . GLN A 80  ? 0.8247 0.7150 0.8204 0.0693  -0.0495 -0.0390 96  GLN B CA  
649   C C   . GLN A 80  ? 0.8751 0.7345 0.8539 0.0600  -0.0534 -0.0287 96  GLN B C   
650   O O   . GLN A 80  ? 0.9023 0.7555 0.8728 0.0497  -0.0464 -0.0174 96  GLN B O   
651   C CB  . GLN A 80  ? 0.8278 0.7113 0.8109 0.0830  -0.0586 -0.0439 96  GLN B CB  
652   C CG  . GLN A 80  ? 0.8031 0.7166 0.8010 0.0898  -0.0557 -0.0518 96  GLN B CG  
653   C CD  . GLN A 80  ? 0.8484 0.7575 0.8380 0.1042  -0.0679 -0.0569 96  GLN B CD  
654   O OE1 . GLN A 80  ? 0.9036 0.8008 0.8765 0.1051  -0.0714 -0.0523 96  GLN B OE1 
655   N NE2 . GLN A 80  ? 0.8016 0.7173 0.8004 0.1158  -0.0753 -0.0654 96  GLN B NE2 
656   N N   . LEU A 81  ? 0.8886 0.7276 0.8605 0.0633  -0.0646 -0.0323 97  LEU B N   
657   C CA  . LEU A 81  ? 0.9348 0.7397 0.8876 0.0536  -0.0712 -0.0222 97  LEU B CA  
658   C C   . LEU A 81  ? 0.9371 0.7508 0.9010 0.0343  -0.0621 -0.0114 97  LEU B C   
659   O O   . LEU A 81  ? 0.9396 0.7398 0.8932 0.0216  -0.0599 0.0024  97  LEU B O   
660   C CB  . LEU A 81  ? 0.9507 0.7280 0.8913 0.0634  -0.0862 -0.0302 97  LEU B CB  
661   C CG  . LEU A 81  ? 0.9461 0.6969 0.8648 0.0752  -0.0971 -0.0296 97  LEU B CG  
662   C CD1 . LEU A 81  ? 1.0589 0.7778 0.9630 0.0873  -0.1123 -0.0369 97  LEU B CD1 
663   C CD2 . LEU A 81  ? 1.0077 0.7387 0.9090 0.0604  -0.0958 -0.0133 97  LEU B CD2 
664   N N   . GLN A 82  ? 0.9505 0.7899 0.9369 0.0317  -0.0566 -0.0164 98  GLN B N   
665   C CA  . GLN A 82  ? 0.9630 0.8173 0.9652 0.0143  -0.0479 -0.0058 98  GLN B CA  
666   C C   . GLN A 82  ? 0.9377 0.8131 0.9490 0.0089  -0.0325 0.0036  98  GLN B C   
667   O O   . GLN A 82  ? 0.9824 0.8601 0.9976 -0.0055 -0.0260 0.0176  98  GLN B O   
668   C CB  . GLN A 82  ? 0.9712 0.8487 0.9944 0.0144  -0.0466 -0.0139 98  GLN B CB  
669   C CG  . GLN A 82  ? 1.1415 1.0317 1.1808 -0.0034 -0.0414 -0.0026 98  GLN B CG  
670   C CD  . GLN A 82  ? 1.2109 1.1153 1.2640 -0.0038 -0.0444 -0.0109 98  GLN B CD  
671   O OE1 . GLN A 82  ? 1.1953 1.1169 1.2562 0.0085  -0.0426 -0.0230 98  GLN B OE1 
672   N NE2 . GLN A 82  ? 1.2225 1.1210 1.2784 -0.0190 -0.0494 -0.0037 98  GLN B NE2 
673   N N   . ALA A 83  ? 0.9325 0.8241 0.9474 0.0203  -0.0264 -0.0039 99  ALA B N   
674   C CA  . ALA A 83  ? 0.9175 0.8228 0.9348 0.0172  -0.0121 0.0032  99  ALA B CA  
675   C C   . ALA A 83  ? 0.9062 0.7873 0.8990 0.0122  -0.0126 0.0139  99  ALA B C   
676   O O   . ALA A 83  ? 0.9492 0.8380 0.9431 0.0034  0.0000  0.0252  99  ALA B O   
677   C CB  . ALA A 83  ? 0.8558 0.7767 0.8765 0.0299  -0.0088 -0.0079 99  ALA B CB  
678   N N   . LEU A 84  ? 0.8980 0.7503 0.8685 0.0180  -0.0266 0.0112  100 LEU B N   
679   C CA  . LEU A 84  ? 0.9117 0.7405 0.8563 0.0141  -0.0280 0.0211  100 LEU B CA  
680   C C   . LEU A 84  ? 0.9662 0.7784 0.9050 -0.0022 -0.0305 0.0357  100 LEU B C   
681   O O   . LEU A 84  ? 1.0296 0.8295 0.9512 -0.0106 -0.0270 0.0481  100 LEU B O   
682   C CB  . LEU A 84  ? 0.8967 0.7008 0.8200 0.0276  -0.0434 0.0134  100 LEU B CB  
683   C CG  . LEU A 84  ? 0.9222 0.7072 0.8179 0.0285  -0.0452 0.0200  100 LEU B CG  
684   C CD1 . LEU A 84  ? 0.8460 0.6527 0.7436 0.0269  -0.0286 0.0214  100 LEU B CD1 
685   C CD2 . LEU A 84  ? 0.9463 0.7139 0.8281 0.0438  -0.0611 0.0114  100 LEU B CD2 
686   N N   . GLN A 85  ? 1.0471 0.8590 0.9988 -0.0082 -0.0366 0.0349  101 GLN B N   
687   C CA  . GLN A 85  ? 1.0648 0.8552 1.0082 -0.0246 -0.0439 0.0480  101 GLN B CA  
688   C C   . GLN A 85  ? 1.0827 0.8983 1.0461 -0.0425 -0.0305 0.0631  101 GLN B C   
689   O O   . GLN A 85  ? 1.2106 1.0121 1.1645 -0.0584 -0.0329 0.0788  101 GLN B O   
690   C CB  . GLN A 85  ? 1.0642 0.8360 1.0064 -0.0220 -0.0596 0.0387  101 GLN B CB  
691   C CG  . GLN A 85  ? 1.0817 0.8180 0.9985 -0.0079 -0.0754 0.0297  101 GLN B CG  
692   C CD  . GLN A 85  ? 1.0560 0.7751 0.9705 -0.0009 -0.0888 0.0174  101 GLN B CD  
693   O OE1 . GLN A 85  ? 1.0618 0.7976 0.9936 -0.0062 -0.0862 0.0139  101 GLN B OE1 
694   N NE2 . GLN A 85  ? 1.1104 0.7953 1.0025 0.0120  -0.1032 0.0106  101 GLN B NE2 
695   N N   . GLN A 86  ? 1.1188 0.9713 1.1102 -0.0404 -0.0171 0.0599  102 GLN B N   
696   C CA  . GLN A 86  ? 1.1381 1.0185 1.1520 -0.0548 -0.0034 0.0746  102 GLN B CA  
697   C C   . GLN A 86  ? 1.2287 1.1043 1.2283 -0.0636 0.0052  0.0904  102 GLN B C   
698   O O   . GLN A 86  ? 1.3368 1.2190 1.3282 -0.0549 0.0170  0.0884  102 GLN B O   
699   C CB  . GLN A 86  ? 1.1853 1.1034 1.2261 -0.0466 0.0122  0.0687  102 GLN B CB  
700   C CG  . GLN A 86  ? 1.1771 1.0975 1.2075 -0.0300 0.0196  0.0574  102 GLN B CG  
701   C CD  . GLN A 86  ? 1.2389 1.1901 1.2935 -0.0215 0.0309  0.0492  102 GLN B CD  
702   O OE1 . GLN A 86  ? 1.3367 1.3094 1.4176 -0.0268 0.0333  0.0517  102 GLN B OE1 
703   N NE2 . GLN A 86  ? 1.2919 1.2440 1.3363 -0.0091 0.0370  0.0402  102 GLN B NE2 
704   N N   . ASN A 87  ? 1.2347 1.0971 1.2283 -0.0815 -0.0009 0.1062  103 ASN B N   
705   C CA  . ASN A 87  ? 1.2469 1.1075 1.2262 -0.0898 0.0087  0.1216  103 ASN B CA  
706   C C   . ASN A 87  ? 1.2130 1.1149 1.2191 -0.0979 0.0301  0.1353  103 ASN B C   
707   O O   . ASN A 87  ? 1.1874 1.0927 1.1840 -0.1065 0.0403  0.1501  103 ASN B O   
708   C CB  . ASN A 87  ? 1.2628 1.0873 1.2178 -0.1055 -0.0074 0.1343  103 ASN B CB  
709   C CG  . ASN A 87  ? 1.3407 1.1512 1.3023 -0.1165 -0.0243 0.1352  103 ASN B CG  
710   O OD1 . ASN A 87  ? 1.4570 1.2903 1.4448 -0.1163 -0.0225 0.1302  103 ASN B OD1 
711   N ND2 . ASN A 87  ? 1.3215 1.0908 1.2564 -0.1261 -0.0422 0.1413  103 ASN B ND2 
712   N N   . GLY A 88  ? 1.0716 1.0050 1.1099 -0.0940 0.0376  0.1306  104 GLY B N   
713   C CA  . GLY A 88  ? 1.0487 1.0234 1.1148 -0.0956 0.0594  0.1406  104 GLY B CA  
714   C C   . GLY A 88  ? 1.1264 1.1122 1.1927 -0.1119 0.0698  0.1634  104 GLY B C   
715   O O   . GLY A 88  ? 1.1782 1.1540 1.2433 -0.1309 0.0581  0.1776  104 GLY B O   
716   N N   . SER A 89  ? 1.0602 1.0649 1.1252 -0.1050 0.0915  0.1671  105 SER B N   
717   C CA  . SER A 89  ? 1.0436 1.0707 1.1168 -0.1193 0.1062  0.1897  105 SER B CA  
718   C C   . SER A 89  ? 1.0941 1.0920 1.1386 -0.1369 0.0939  0.2035  105 SER B C   
719   O O   . SER A 89  ? 1.0772 1.0935 1.1309 -0.1541 0.1016  0.2254  105 SER B O   
720   C CB  . SER A 89  ? 0.9983 1.0457 1.0682 -0.1061 0.1323  0.1886  105 SER B CB  
721   O OG  . SER A 89  ? 1.1034 1.1560 1.1609 -0.1190 0.1428  0.2080  105 SER B OG  
722   N N   . SER A 90  ? 1.2120 1.1658 1.2232 -0.1331 0.0748  0.1923  106 SER B N   
723   C CA  . SER A 90  ? 1.1700 1.0899 1.1502 -0.1483 0.0613  0.2046  106 SER B CA  
724   C C   . SER A 90  ? 1.2489 1.1562 1.2370 -0.1689 0.0418  0.2160  106 SER B C   
725   O O   . SER A 90  ? 1.2956 1.1791 1.2628 -0.1863 0.0314  0.2312  106 SER B O   
726   C CB  . SER A 90  ? 1.2085 1.0846 1.1512 -0.1350 0.0466  0.1883  106 SER B CB  
727   O OG  . SER A 90  ? 1.2525 1.1032 1.1947 -0.1314 0.0243  0.1757  106 SER B OG  
728   N N   . VAL A 91  ? 1.2983 1.2178 1.3133 -0.1681 0.0350  0.2090  107 VAL B N   
729   C CA  . VAL A 91  ? 1.2615 1.1640 1.2791 -0.1881 0.0146  0.2185  107 VAL B CA  
730   C C   . VAL A 91  ? 1.2451 1.1771 1.2835 -0.2127 0.0222  0.2460  107 VAL B C   
731   O O   . VAL A 91  ? 1.2918 1.2050 1.3251 -0.2346 0.0045  0.2591  107 VAL B O   
732   C CB  . VAL A 91  ? 1.2292 1.1351 1.2656 -0.1791 0.0055  0.2017  107 VAL B CB  
733   C CG1 . VAL A 91  ? 1.1540 1.1128 1.2343 -0.1812 0.0218  0.2088  107 VAL B CG1 
734   C CG2 . VAL A 91  ? 1.2670 1.1345 1.2884 -0.1931 -0.0209 0.2022  107 VAL B CG2 
735   N N   . LEU A 92  ? 1.1238 1.1009 1.1845 -0.2093 0.0479  0.2552  108 LEU B N   
736   C CA  . LEU A 92  ? 1.1539 1.1657 1.2348 -0.2300 0.0598  0.2827  108 LEU B CA  
737   C C   . LEU A 92  ? 1.2330 1.2212 1.2798 -0.2431 0.0585  0.2972  108 LEU B C   
738   O O   . LEU A 92  ? 1.2622 1.2137 1.2720 -0.2319 0.0537  0.2853  108 LEU B O   
739   C CB  . LEU A 92  ? 1.1051 1.1711 1.2179 -0.2171 0.0900  0.2852  108 LEU B CB  
740   C CG  . LEU A 92  ? 1.0526 1.1514 1.2043 -0.2042 0.0964  0.2751  108 LEU B CG  
741   C CD1 . LEU A 92  ? 1.0159 1.1562 1.1870 -0.1868 0.1269  0.2747  108 LEU B CD1 
742   C CD2 . LEU A 92  ? 1.0529 1.1748 1.2387 -0.2258 0.0858  0.2924  108 LEU B CD2 
743   N N   . SER A 93  ? 1.2940 1.3052 1.3542 -0.2677 0.0625  0.3247  109 SER B N   
744   C CA  . SER A 93  ? 1.2690 1.2646 1.2993 -0.2821 0.0641  0.3417  109 SER B CA  
745   C C   . SER A 93  ? 1.2689 1.2960 1.2983 -0.2675 0.0951  0.3424  109 SER B C   
746   O O   . SER A 93  ? 1.2786 1.3473 1.3380 -0.2515 0.1164  0.3361  109 SER B O   
747   C CB  . SER A 93  ? 1.2840 1.2949 1.3290 -0.3139 0.0573  0.3703  109 SER B CB  
748   O OG  . SER A 93  ? 1.3264 1.3981 1.4072 -0.3098 0.0833  0.3781  109 SER B OG  
749   N N   . GLU A 94  ? 1.4966 1.4271 1.1143 0.0419  0.0547  0.1943  110 GLU B N   
750   C CA  . GLU A 94  ? 1.5690 1.4889 1.1562 0.0428  0.0455  0.1955  110 GLU B CA  
751   C C   . GLU A 94  ? 1.6081 1.5598 1.1694 0.0496  0.0559  0.1785  110 GLU B C   
752   O O   . GLU A 94  ? 1.6549 1.6049 1.2014 0.0626  0.0522  0.1713  110 GLU B O   
753   C CB  . GLU A 94  ? 1.5906 1.4917 1.1643 0.0218  0.0357  0.2115  110 GLU B CB  
754   C CG  . GLU A 94  ? 1.6881 1.5551 1.2871 0.0146  0.0235  0.2292  110 GLU B CG  
755   C CD  . GLU A 94  ? 1.7661 1.6196 1.3557 -0.0081 0.0160  0.2453  110 GLU B CD  
756   O OE1 . GLU A 94  ? 1.7525 1.6131 1.3099 -0.0167 0.0148  0.2451  110 GLU B OE1 
757   O OE2 . GLU A 94  ? 1.7839 1.6187 1.3989 -0.0176 0.0106  0.2583  110 GLU B OE2 
758   N N   . ASP A 95  ? 1.6063 1.5874 1.1627 0.0408  0.0689  0.1716  111 ASP B N   
759   C CA  . ASP A 95  ? 1.6487 1.6622 1.1829 0.0473  0.0798  0.1542  111 ASP B CA  
760   C C   . ASP A 95  ? 1.6540 1.6779 1.1974 0.0712  0.0836  0.1403  111 ASP B C   
761   O O   . ASP A 95  ? 1.6596 1.6889 1.1842 0.0819  0.0822  0.1308  111 ASP B O   
762   C CB  . ASP A 95  ? 1.7321 1.7751 1.2665 0.0349  0.0940  0.1490  111 ASP B CB  
763   C CG  . ASP A 95  ? 1.9313 2.0082 1.4434 0.0396  0.1054  0.1312  111 ASP B CG  
764   O OD1 . ASP A 95  ? 2.0203 2.0969 1.5037 0.0331  0.1018  0.1303  111 ASP B OD1 
765   O OD2 . ASP A 95  ? 1.9948 2.0990 1.5184 0.0491  0.1179  0.1180  111 ASP B OD2 
766   N N   . LYS A 96  ? 1.6300 1.6552 1.2034 0.0797  0.0875  0.1396  112 LYS B N   
767   C CA  . LYS A 96  ? 1.5656 1.6015 1.1492 0.1017  0.0914  0.1273  112 LYS B CA  
768   C C   . LYS A 96  ? 1.5624 1.5708 1.1433 0.1148  0.0782  0.1308  112 LYS B C   
769   O O   . LYS A 96  ? 1.5199 1.5383 1.0942 0.1316  0.0798  0.1192  112 LYS B O   
770   C CB  . LYS A 96  ? 1.4126 1.4553 1.0288 0.1057  0.0982  0.1269  112 LYS B CB  
771   C CG  . LYS A 96  ? 1.3630 1.4356 0.9863 0.0946  0.1127  0.1219  112 LYS B CG  
772   C CD  . LYS A 96  ? 1.2295 1.3220 0.8785 0.1066  0.1226  0.1128  112 LYS B CD  
773   C CE  . LYS A 96  ? 1.1364 1.2506 0.7998 0.0937  0.1349  0.1115  112 LYS B CE  
774   N NZ  . LYS A 96  ? 1.1490 1.2995 0.8184 0.1049  0.1487  0.0954  112 LYS B NZ  
775   N N   . SER A 97  ? 1.7780 1.7515 1.3643 0.1075  0.0649  0.1466  113 SER B N   
776   C CA  . SER A 97  ? 1.7333 1.6792 1.3189 0.1198  0.0523  0.1502  113 SER B CA  
777   C C   . SER A 97  ? 1.6336 1.5792 1.1875 0.1207  0.0476  0.1459  113 SER B C   
778   O O   . SER A 97  ? 1.5744 1.5148 1.1232 0.1365  0.0435  0.1395  113 SER B O   
779   C CB  . SER A 97  ? 1.7880 1.6973 1.3898 0.1110  0.0396  0.1681  113 SER B CB  
780   O OG  . SER A 97  ? 1.8652 1.7746 1.4979 0.1095  0.0440  0.1715  113 SER B OG  
781   N N   . LYS A 98  ? 1.5608 1.5118 1.0937 0.1030  0.0480  0.1497  114 LYS B N   
782   C CA  . LYS A 98  ? 1.5205 1.4812 1.0218 0.1019  0.0476  0.1420  114 LYS B CA  
783   C C   . LYS A 98  ? 1.5018 1.4942 0.9974 0.1178  0.0589  0.1219  114 LYS B C   
784   O O   . LYS A 98  ? 1.4072 1.3986 0.8902 0.1296  0.0555  0.1139  114 LYS B O   
785   C CB  . LYS A 98  ? 1.7197 1.6883 1.2026 0.0790  0.0498  0.1478  114 LYS B CB  
786   C CG  . LYS A 98  ? 1.7922 1.7277 1.2788 0.0626  0.0367  0.1688  114 LYS B CG  
787   C CD  . LYS A 98  ? 1.8918 1.8347 1.3573 0.0393  0.0380  0.1752  114 LYS B CD  
788   C CE  . LYS A 98  ? 1.9479 1.9174 1.4243 0.0318  0.0524  0.1707  114 LYS B CE  
789   N NZ  . LYS A 98  ? 1.9702 1.9628 1.4235 0.0141  0.0606  0.1678  114 LYS B NZ  
790   N N   . ARG A 99  ? 1.5712 1.5927 1.0764 0.1182  0.0726  0.1132  115 ARG B N   
791   C CA  . ARG A 99  ? 1.4411 1.4937 0.9432 0.1336  0.0833  0.0941  115 ARG B CA  
792   C C   . ARG A 99  ? 1.3429 1.3846 0.8581 0.1560  0.0782  0.0899  115 ARG B C   
793   O O   . ARG A 99  ? 1.2851 1.3330 0.7871 0.1676  0.0773  0.0793  115 ARG B O   
794   C CB  . ARG A 99  ? 1.5296 1.6121 1.0453 0.1316  0.0977  0.0870  115 ARG B CB  
795   C CG  . ARG A 99  ? 1.7556 1.8599 1.2555 0.1125  0.1068  0.0849  115 ARG B CG  
796   C CD  . ARG A 99  ? 1.8935 2.0175 1.4143 0.1084  0.1185  0.0835  115 ARG B CD  
797   N NE  . ARG A 99  ? 2.1018 2.2652 1.6166 0.1115  0.1333  0.0664  115 ARG B NE  
798   C CZ  . ARG A 99  ? 2.1463 2.3311 1.6581 0.0971  0.1439  0.0641  115 ARG B CZ  
799   N NH1 . ARG A 99  ? 2.1252 2.2963 1.6394 0.0781  0.1414  0.0781  115 ARG B NH1 
800   N NH2 . ARG A 99  ? 2.1098 2.3307 1.6177 0.1021  0.1572  0.0473  115 ARG B NH2 
801   N N   . LEU A 100 ? 1.3609 1.3868 0.9028 0.1618  0.0750  0.0979  116 LEU B N   
802   C CA  . LEU A 100 ? 1.2502 1.2635 0.8069 0.1820  0.0698  0.0958  116 LEU B CA  
803   C C   . LEU A 100 ? 1.2563 1.2492 0.7975 0.1891  0.0588  0.0962  116 LEU B C   
804   O O   . LEU A 100 ? 1.2052 1.2036 0.7462 0.2068  0.0589  0.0861  116 LEU B O   
805   C CB  . LEU A 100 ? 1.2219 1.2118 0.8060 0.1816  0.0645  0.1084  116 LEU B CB  
806   C CG  . LEU A 100 ? 1.1104 1.0865 0.7117 0.2012  0.0594  0.1072  116 LEU B CG  
807   C CD1 . LEU A 100 ? 1.0346 1.0391 0.6406 0.2182  0.0689  0.0922  116 LEU B CD1 
808   C CD2 . LEU A 100 ? 1.1333 1.0878 0.7615 0.1978  0.0551  0.1192  116 LEU B CD2 
809   N N   . ASN A 101 ? 1.3109 1.2785 0.8409 0.1755  0.0485  0.1087  117 ASN B N   
810   C CA  . ASN A 101 ? 1.2992 1.2463 0.8148 0.1813  0.0376  0.1097  117 ASN B CA  
811   C C   . ASN A 101 ? 1.2340 1.2044 0.7244 0.1841  0.0428  0.0948  117 ASN B C   
812   O O   . ASN A 101 ? 1.1676 1.1349 0.6533 0.1988  0.0393  0.0869  117 ASN B O   
813   C CB  . ASN A 101 ? 1.3189 1.2350 0.8282 0.1650  0.0254  0.1268  117 ASN B CB  
814   C CG  . ASN A 101 ? 1.3779 1.2664 0.9140 0.1649  0.0181  0.1407  117 ASN B CG  
815   O OD1 . ASN A 101 ? 1.3083 1.1962 0.8660 0.1794  0.0202  0.1375  117 ASN B OD1 
816   N ND2 . ASN A 101 ? 1.5449 1.4115 1.0803 0.1480  0.0098  0.1561  117 ASN B ND2 
817   N N   . THR A 102 ? 1.2624 1.2570 0.7374 0.1700  0.0516  0.0901  118 THR B N   
818   C CA  . THR A 102 ? 1.2345 1.2534 0.6865 0.1718  0.0575  0.0746  118 THR B CA  
819   C C   . THR A 102 ? 1.1910 1.2301 0.6536 0.1938  0.0645  0.0586  118 THR B C   
820   O O   . THR A 102 ? 1.1442 1.1890 0.5957 0.2040  0.0636  0.0473  118 THR B O   
821   C CB  . THR A 102 ? 1.2140 1.2592 0.6516 0.1544  0.0679  0.0707  118 THR B CB  
822   O OG1 . THR A 102 ? 1.2572 1.2836 0.6833 0.1335  0.0608  0.0860  118 THR B OG1 
823   C CG2 . THR A 102 ? 1.0904 1.1605 0.5049 0.1562  0.0740  0.0536  118 THR B CG2 
824   N N   . ILE A 103 ? 1.1786 1.2283 0.6636 0.2010  0.0711  0.0576  119 ILE B N   
825   C CA  . ILE A 103 ? 1.1351 1.2052 0.6321 0.2214  0.0777  0.0436  119 ILE B CA  
826   C C   . ILE A 103 ? 1.1815 1.2282 0.6880 0.2393  0.0678  0.0451  119 ILE B C   
827   O O   . ILE A 103 ? 1.1887 1.2458 0.6910 0.2539  0.0687  0.0326  119 ILE B O   
828   C CB  . ILE A 103 ? 1.1027 1.1898 0.6210 0.2229  0.0870  0.0433  119 ILE B CB  
829   C CG1 . ILE A 103 ? 1.1379 1.2549 0.6459 0.2084  0.0990  0.0371  119 ILE B CG1 
830   C CG2 . ILE A 103 ? 1.0873 1.1874 0.6221 0.2450  0.0904  0.0331  119 ILE B CG2 
831   C CD1 . ILE A 103 ? 1.1912 1.3187 0.7195 0.2041  0.1065  0.0410  119 ILE B CD1 
832   N N   . LEU A 104 ? 1.1978 1.2135 0.7190 0.2390  0.0585  0.0600  120 LEU B N   
833   C CA  . LEU A 104 ? 1.1650 1.1562 0.6955 0.2551  0.0487  0.0624  120 LEU B CA  
834   C C   . LEU A 104 ? 1.1400 1.1251 0.6500 0.2583  0.0429  0.0564  120 LEU B C   
835   O O   . LEU A 104 ? 1.0862 1.0734 0.5991 0.2760  0.0418  0.0471  120 LEU B O   
836   C CB  . LEU A 104 ? 1.1323 1.0884 0.6770 0.2495  0.0385  0.0800  120 LEU B CB  
837   C CG  . LEU A 104 ? 1.0991 1.0528 0.6694 0.2486  0.0414  0.0874  120 LEU B CG  
838   C CD1 . LEU A 104 ? 1.1432 1.0612 0.7232 0.2393  0.0305  0.1045  120 LEU B CD1 
839   C CD2 . LEU A 104 ? 1.0185 0.9775 0.6069 0.2697  0.0434  0.0805  120 LEU B CD2 
840   N N   . ASN A 105 ? 1.1839 1.1633 0.6732 0.2409  0.0398  0.0612  121 ASN B N   
841   C CA  . ASN A 105 ? 1.1911 1.1636 0.6602 0.2415  0.0339  0.0563  121 ASN B CA  
842   C C   . ASN A 105 ? 1.1617 1.1670 0.6197 0.2492  0.0434  0.0366  121 ASN B C   
843   O O   . ASN A 105 ? 1.1484 1.1519 0.6023 0.2617  0.0404  0.0277  121 ASN B O   
844   C CB  . ASN A 105 ? 1.2049 1.1647 0.6546 0.2193  0.0284  0.0671  121 ASN B CB  
845   C CG  . ASN A 105 ? 1.3117 1.2327 0.7669 0.2170  0.0144  0.0832  121 ASN B CG  
846   O OD1 . ASN A 105 ? 1.4371 1.3419 0.8819 0.2203  0.0059  0.0831  121 ASN B OD1 
847   N ND2 . ASN A 105 ? 1.3279 1.2338 0.8010 0.2115  0.0119  0.0967  121 ASN B ND2 
848   N N   . THR A 106 ? 1.1181 1.1539 0.5724 0.2418  0.0552  0.0292  122 THR B N   
849   C CA  . THR A 106 ? 1.1487 1.2173 0.5938 0.2484  0.0649  0.0097  122 THR B CA  
850   C C   . THR A 106 ? 1.1501 1.2247 0.6131 0.2728  0.0658  -0.0002 122 THR B C   
851   O O   . THR A 106 ? 1.1413 1.2235 0.5977 0.2829  0.0657  -0.0128 122 THR B O   
852   C CB  . THR A 106 ? 1.1438 1.2432 0.5858 0.2374  0.0775  0.0043  122 THR B CB  
853   O OG1 . THR A 106 ? 1.1535 1.2476 0.5772 0.2142  0.0764  0.0133  122 THR B OG1 
854   C CG2 . THR A 106 ? 1.0910 1.2255 0.5262 0.2454  0.0879  -0.0168 122 THR B CG2 
855   N N   . MET A 107 ? 1.1463 1.2175 0.6326 0.2822  0.0667  0.0055  123 MET B N   
856   C CA  . MET A 107 ? 1.0998 1.1728 0.6046 0.3051  0.0661  -0.0010 123 MET B CA  
857   C C   . MET A 107 ? 1.1372 1.1836 0.6411 0.3157  0.0549  0.0009  123 MET B C   
858   O O   . MET A 107 ? 1.0956 1.1503 0.6038 0.3325  0.0554  -0.0107 123 MET B O   
859   C CB  . MET A 107 ? 1.0356 1.1029 0.5640 0.3098  0.0668  0.0084  123 MET B CB  
860   C CG  . MET A 107 ? 0.9986 1.0955 0.5320 0.3037  0.0787  0.0041  123 MET B CG  
861   S SD  . MET A 107 ? 0.9739 1.0686 0.5371 0.3144  0.0800  0.0109  123 MET B SD  
862   C CE  . MET A 107 ? 0.9596 1.0144 0.5294 0.3021  0.0696  0.0317  123 MET B CE  
863   N N   . SER A 108 ? 1.1862 1.2002 0.6861 0.3067  0.0447  0.0155  124 SER B N   
864   C CA  . SER A 108 ? 1.1680 1.1559 0.6700 0.3183  0.0342  0.0175  124 SER B CA  
865   C C   . SER A 108 ? 1.1503 1.1463 0.6327 0.3186  0.0338  0.0052  124 SER B C   
866   O O   . SER A 108 ? 1.1601 1.1520 0.6473 0.3347  0.0305  -0.0026 124 SER B O   
867   C CB  . SER A 108 ? 1.1627 1.1140 0.6663 0.3091  0.0230  0.0356  124 SER B CB  
868   O OG  . SER A 108 ? 1.1235 1.0524 0.6295 0.3218  0.0138  0.0356  124 SER B OG  
869   N N   . THR A 109 ? 1.1912 1.1996 0.6520 0.3007  0.0374  0.0027  125 THR B N   
870   C CA  . THR A 109 ? 1.2270 1.2473 0.6693 0.3002  0.0385  -0.0110 125 THR B CA  
871   C C   . THR A 109 ? 1.2157 1.2706 0.6631 0.3132  0.0491  -0.0308 125 THR B C   
872   O O   . THR A 109 ? 1.2601 1.3212 0.7037 0.3228  0.0488  -0.0436 125 THR B O   
873   C CB  . THR A 109 ? 1.1955 1.2197 0.6120 0.2765  0.0392  -0.0084 125 THR B CB  
874   O OG1 . THR A 109 ? 1.2740 1.3303 0.6849 0.2677  0.0513  -0.0162 125 THR B OG1 
875   C CG2 . THR A 109 ? 1.1951 1.1885 0.6095 0.2621  0.0297  0.0126  125 THR B CG2 
876   N N   . ILE A 110 ? 1.2206 1.2988 0.6776 0.3139  0.0586  -0.0339 126 ILE B N   
877   C CA  . ILE A 110 ? 1.2114 1.3217 0.6757 0.3276  0.0679  -0.0521 126 ILE B CA  
878   C C   . ILE A 110 ? 1.2139 1.3142 0.6971 0.3510  0.0629  -0.0555 126 ILE B C   
879   O O   . ILE A 110 ? 1.2185 1.3350 0.7035 0.3631  0.0657  -0.0711 126 ILE B O   
880   C CB  . ILE A 110 ? 1.1905 1.3256 0.6635 0.3246  0.0783  -0.0534 126 ILE B CB  
881   C CG1 . ILE A 110 ? 1.2004 1.3511 0.6528 0.3021  0.0850  -0.0544 126 ILE B CG1 
882   C CG2 . ILE A 110 ? 1.1369 1.3027 0.6216 0.3414  0.0865  -0.0708 126 ILE B CG2 
883   C CD1 . ILE A 110 ? 1.2397 1.4165 0.6993 0.2979  0.0960  -0.0568 126 ILE B CD1 
884   N N   . TYR A 111 ? 1.1918 1.2650 0.6900 0.3573  0.0551  -0.0409 127 TYR B N   
885   C CA  . TYR A 111 ? 1.1596 1.2211 0.6757 0.3791  0.0497  -0.0427 127 TYR B CA  
886   C C   . TYR A 111 ? 1.2218 1.2664 0.7295 0.3836  0.0421  -0.0467 127 TYR B C   
887   O O   . TYR A 111 ? 1.2207 1.2717 0.7368 0.4004  0.0419  -0.0580 127 TYR B O   
888   C CB  . TYR A 111 ? 1.1127 1.1486 0.6457 0.3827  0.0434  -0.0260 127 TYR B CB  
889   C CG  . TYR A 111 ? 1.1191 1.1416 0.6710 0.4043  0.0378  -0.0261 127 TYR B CG  
890   C CD1 . TYR A 111 ? 1.1640 1.2043 0.7342 0.4196  0.0426  -0.0316 127 TYR B CD1 
891   C CD2 . TYR A 111 ? 1.1283 1.1198 0.6799 0.4090  0.0272  -0.0202 127 TYR B CD2 
892   C CE1 . TYR A 111 ? 1.1611 1.1874 0.7489 0.4389  0.0367  -0.0303 127 TYR B CE1 
893   C CE2 . TYR A 111 ? 1.1317 1.1092 0.7007 0.4281  0.0218  -0.0195 127 TYR B CE2 
894   C CZ  . TYR A 111 ? 1.1434 1.1379 0.7302 0.4429  0.0264  -0.0242 127 TYR B CZ  
895   O OH  . TYR A 111 ? 1.0673 1.0466 0.6707 0.4614  0.0205  -0.0227 127 TYR B OH  
896   N N   . SER A 112 ? 1.3101 1.3312 0.8031 0.3694  0.0350  -0.0365 128 SER B N   
897   C CA  . SER A 112 ? 1.3207 1.3238 0.8059 0.3733  0.0271  -0.0393 128 SER B CA  
898   C C   . SER A 112 ? 1.3898 1.4185 0.8605 0.3718  0.0332  -0.0583 128 SER B C   
899   O O   . SER A 112 ? 1.3875 1.4118 0.8595 0.3827  0.0298  -0.0673 128 SER B O   
900   C CB  . SER A 112 ? 1.2711 1.2433 0.7443 0.3575  0.0177  -0.0230 128 SER B CB  
901   O OG  . SER A 112 ? 1.2720 1.2555 0.7254 0.3358  0.0217  -0.0209 128 SER B OG  
902   N N   . THR A 113 ? 1.4500 1.5065 0.9084 0.3589  0.0426  -0.0655 129 THR B N   
903   C CA  . THR A 113 ? 1.4992 1.5812 0.9424 0.3545  0.0491  -0.0838 129 THR B CA  
904   C C   . THR A 113 ? 1.5509 1.6684 1.0046 0.3650  0.0601  -0.1004 129 THR B C   
905   O O   . THR A 113 ? 1.6768 1.8203 1.1182 0.3588  0.0676  -0.1161 129 THR B O   
906   C CB  . THR A 113 ? 1.5656 1.6531 0.9831 0.3293  0.0515  -0.0805 129 THR B CB  
907   O OG1 . THR A 113 ? 1.5767 1.6846 0.9954 0.3215  0.0603  -0.0792 129 THR B OG1 
908   C CG2 . THR A 113 ? 1.5533 1.6055 0.9617 0.3174  0.0402  -0.0612 129 THR B CG2 
909   N N   . GLY A 114 ? 1.4893 1.6094 0.9649 0.3794  0.0615  -0.0973 130 GLY B N   
910   C CA  . GLY A 114 ? 1.5539 1.7074 1.0407 0.3905  0.0710  -0.1130 130 GLY B CA  
911   C C   . GLY A 114 ? 1.5479 1.7077 1.0410 0.4060  0.0700  -0.1290 130 GLY B C   
912   O O   . GLY A 114 ? 1.4447 1.5809 0.9481 0.4188  0.0614  -0.1244 130 GLY B O   
913   N N   . LYS A 115 ? 1.5696 1.7611 1.0571 0.4046  0.0788  -0.1481 131 LYS B N   
914   C CA  . LYS A 115 ? 1.6010 1.8032 1.0958 0.4185  0.0793  -0.1659 131 LYS B CA  
915   C C   . LYS A 115 ? 1.6358 1.8741 1.1454 0.4252  0.0885  -0.1815 131 LYS B C   
916   O O   . LYS A 115 ? 1.7087 1.9667 1.2167 0.4096  0.0952  -0.1818 131 LYS B O   
917   C CB  . LYS A 115 ? 1.6528 1.8558 1.1258 0.4052  0.0792  -0.1754 131 LYS B CB  
918   C CG  . LYS A 115 ? 1.7353 1.9605 1.1852 0.3829  0.0878  -0.1810 131 LYS B CG  
919   C CD  . LYS A 115 ? 1.8205 2.0527 1.2510 0.3720  0.0890  -0.1948 131 LYS B CD  
920   C CE  . LYS A 115 ? 1.8026 2.0013 1.2198 0.3638  0.0782  -0.1818 131 LYS B CE  
921   N NZ  . LYS A 115 ? 1.7599 1.9436 1.1592 0.3433  0.0755  -0.1629 131 LYS B NZ  
922   N N   . VAL A 116 ? 1.6122 1.8545 1.1470 0.4416  0.0855  -0.1897 132 VAL B N   
923   C CA  . VAL A 116 ? 1.6360 1.9070 1.1966 0.4423  0.0894  -0.2006 132 VAL B CA  
924   C C   . VAL A 116 ? 1.6344 1.9143 1.2014 0.4456  0.0889  -0.2177 132 VAL B C   
925   O O   . VAL A 116 ? 1.6018 1.8632 1.1707 0.4584  0.0826  -0.2186 132 VAL B O   
926   C CB  . VAL A 116 ? 1.5626 1.8318 1.1513 0.4583  0.0853  -0.1923 132 VAL B CB  
927   C CG1 . VAL A 116 ? 1.5616 1.8263 1.1461 0.4533  0.0871  -0.1770 132 VAL B CG1 
928   C CG2 . VAL A 116 ? 1.4554 1.6994 1.0546 0.4778  0.0761  -0.1877 132 VAL B CG2 
929   N N   . CYS A 117 ? 1.6877 1.9954 1.2587 0.4335  0.0958  -0.2316 133 CYS B N   
930   C CA  . CYS A 117 ? 1.7627 2.0828 1.3391 0.4330  0.0973  -0.2497 133 CYS B CA  
931   C C   . CYS A 117 ? 1.9142 2.2529 1.5228 0.4432  0.0974  -0.2577 133 CYS B C   
932   O O   . CYS A 117 ? 1.9431 2.2956 1.5627 0.4406  0.1002  -0.2539 133 CYS B O   
933   C CB  . CYS A 117 ? 1.8137 2.1504 1.3692 0.4096  0.1054  -0.2595 133 CYS B CB  
934   S SG  . CYS A 117 ? 1.8657 2.1837 1.3825 0.3926  0.1055  -0.2451 133 CYS B SG  
935   N N   . ASN A 118 ? 1.9983 2.3369 1.6220 0.4544  0.0939  -0.2686 134 ASN B N   
936   C CA  . ASN A 118 ? 2.0923 2.4435 1.7474 0.4666  0.0917  -0.2739 134 ASN B CA  
937   C C   . ASN A 118 ? 2.2529 2.6351 1.9152 0.4548  0.0999  -0.2880 134 ASN B C   
938   O O   . ASN A 118 ? 2.2972 2.6906 1.9423 0.4381  0.1069  -0.2977 134 ASN B O   
939   C CB  . ASN A 118 ? 2.0994 2.4399 1.7687 0.4808  0.0855  -0.2809 134 ASN B CB  
940   C CG  . ASN A 118 ? 2.2041 2.5559 1.8659 0.4719  0.0903  -0.2996 134 ASN B CG  
941   O OD1 . ASN A 118 ? 2.1648 2.5060 1.8026 0.4640  0.0913  -0.3006 134 ASN B OD1 
942   N ND2 . ASN A 118 ? 2.2518 2.6247 1.9336 0.4728  0.0932  -0.3146 134 ASN B ND2 
943   N N   . PRO A 119 ? 2.1423 2.5382 1.8296 0.4625  0.0988  -0.2890 135 PRO B N   
944   C CA  . PRO A 119 ? 2.1996 2.6235 1.8930 0.4511  0.1065  -0.3004 135 PRO B CA  
945   C C   . PRO A 119 ? 2.2378 2.6774 1.9369 0.4471  0.1106  -0.3211 135 PRO B C   
946   O O   . PRO A 119 ? 2.2820 2.7442 1.9923 0.4416  0.1157  -0.3316 135 PRO B O   
947   C CB  . PRO A 119 ? 2.1760 2.6062 1.8940 0.4628  0.1025  -0.2939 135 PRO B CB  
948   C CG  . PRO A 119 ? 2.1047 2.5141 1.8356 0.4814  0.0926  -0.2865 135 PRO B CG  
949   C CD  . PRO A 119 ? 2.0351 2.4202 1.7442 0.4804  0.0904  -0.2783 135 PRO B CD  
950   N N   . ASP A 120 ? 2.2705 2.6987 1.9622 0.4494  0.1087  -0.3273 136 ASP B N   
951   C CA  . ASP A 120 ? 2.2190 2.6611 1.9171 0.4459  0.1124  -0.3474 136 ASP B CA  
952   C C   . ASP A 120 ? 2.2395 2.6770 1.9111 0.4318  0.1165  -0.3542 136 ASP B C   
953   O O   . ASP A 120 ? 2.1585 2.6092 1.8323 0.4255  0.1209  -0.3715 136 ASP B O   
954   C CB  . ASP A 120 ? 2.1402 2.5748 1.8635 0.4651  0.1051  -0.3515 136 ASP B CB  
955   C CG  . ASP A 120 ? 2.1349 2.5684 1.8819 0.4796  0.0990  -0.3412 136 ASP B CG  
956   O OD1 . ASP A 120 ? 2.1303 2.5836 1.8882 0.4763  0.1026  -0.3449 136 ASP B OD1 
957   O OD2 . ASP A 120 ? 2.1254 2.5372 1.8790 0.4934  0.0906  -0.3286 136 ASP B OD2 
958   N N   . ASN A 121 ? 2.3707 2.7899 2.0175 0.4265  0.1149  -0.3411 137 ASN B N   
959   C CA  . ASN A 121 ? 2.3614 2.7734 1.9803 0.4129  0.1174  -0.3452 137 ASN B CA  
960   C C   . ASN A 121 ? 2.3612 2.7617 1.9532 0.4012  0.1181  -0.3289 137 ASN B C   
961   O O   . ASN A 121 ? 2.2899 2.6677 1.8760 0.4110  0.1115  -0.3137 137 ASN B O   
962   C CB  . ASN A 121 ? 2.2853 2.6779 1.9060 0.4262  0.1103  -0.3467 137 ASN B CB  
963   C CG  . ASN A 121 ? 2.2934 2.6825 1.8878 0.4117  0.1130  -0.3547 137 ASN B CG  
964   O OD1 . ASN A 121 ? 2.2966 2.6992 1.8723 0.3910  0.1204  -0.3603 137 ASN B OD1 
965   N ND2 . ASN A 121 ? 2.2799 2.6502 1.8725 0.4219  0.1068  -0.3548 137 ASN B ND2 
966   N N   . PRO A 122 ? 2.3354 2.7501 1.9116 0.3802  0.1260  -0.3312 138 PRO B N   
967   C CA  . PRO A 122 ? 2.2956 2.7000 1.8481 0.3679  0.1268  -0.3150 138 PRO B CA  
968   C C   . PRO A 122 ? 2.2450 2.6288 1.7666 0.3601  0.1236  -0.3081 138 PRO B C   
969   O O   . PRO A 122 ? 2.1114 2.4845 1.6133 0.3506  0.1233  -0.2935 138 PRO B O   
970   C CB  . PRO A 122 ? 2.3041 2.7305 1.8510 0.3470  0.1365  -0.3218 138 PRO B CB  
971   C CG  . PRO A 122 ? 2.2385 2.6860 1.8147 0.3553  0.1391  -0.3368 138 PRO B CG  
972   C CD  . PRO A 122 ? 2.2811 2.7225 1.8679 0.3699  0.1340  -0.3463 138 PRO B CD  
973   N N   . GLN A 123 ? 2.2880 2.6652 1.8045 0.3634  0.1208  -0.3175 139 GLN B N   
974   C CA  . GLN A 123 ? 2.3271 2.6837 1.8140 0.3568  0.1166  -0.3105 139 GLN B CA  
975   C C   . GLN A 123 ? 2.2354 2.5655 1.7269 0.3785  0.1068  -0.3018 139 GLN B C   
976   O O   . GLN A 123 ? 2.2022 2.5106 1.6688 0.3753  0.1018  -0.2910 139 GLN B O   
977   C CB  . GLN A 123 ? 2.4045 2.7703 1.8770 0.3418  0.1203  -0.3265 139 GLN B CB  
978   C CG  . GLN A 123 ? 2.4196 2.7943 1.9162 0.3548  0.1201  -0.3444 139 GLN B CG  
979   C CD  . GLN A 123 ? 2.4995 2.8626 1.9798 0.3524  0.1166  -0.3508 139 GLN B CD  
980   O OE1 . GLN A 123 ? 2.4733 2.8163 1.9274 0.3477  0.1116  -0.3389 139 GLN B OE1 
981   N NE2 . GLN A 123 ? 2.5810 2.9568 2.0767 0.3552  0.1190  -0.3696 139 GLN B NE2 
982   N N   . GLU A 124 ? 2.1809 2.5111 1.7031 0.3997  0.1035  -0.3057 140 GLU B N   
983   C CA  . GLU A 124 ? 2.0800 2.3844 1.6108 0.4212  0.0942  -0.2977 140 GLU B CA  
984   C C   . GLU A 124 ? 2.0028 2.2954 1.5432 0.4326  0.0905  -0.2796 140 GLU B C   
985   O O   . GLU A 124 ? 2.0153 2.3205 1.5819 0.4411  0.0914  -0.2801 140 GLU B O   
986   C CB  . GLU A 124 ? 2.0366 2.3475 1.5968 0.4361  0.0924  -0.3118 140 GLU B CB  
987   C CG  . GLU A 124 ? 1.9963 2.2837 1.5753 0.4594  0.0831  -0.3020 140 GLU B CG  
988   C CD  . GLU A 124 ? 2.0428 2.3393 1.6545 0.4724  0.0815  -0.3142 140 GLU B CD  
989   O OE1 . GLU A 124 ? 2.0852 2.4081 1.7115 0.4672  0.0873  -0.3261 140 GLU B OE1 
990   O OE2 . GLU A 124 ? 2.0328 2.3094 1.6561 0.4872  0.0741  -0.3115 140 GLU B OE2 
991   N N   . CYS A 125 ? 1.8657 2.1336 1.3846 0.4326  0.0861  -0.2636 141 CYS B N   
992   C CA  . CYS A 125 ? 1.7714 2.0287 1.2954 0.4395  0.0839  -0.2461 141 CYS B CA  
993   C C   . CYS A 125 ? 1.6526 1.8761 1.1783 0.4582  0.0747  -0.2338 141 CYS B C   
994   O O   . CYS A 125 ? 1.5506 1.7587 1.0719 0.4648  0.0700  -0.2386 141 CYS B O   
995   C CB  . CYS A 125 ? 1.8077 2.0675 1.3051 0.4193  0.0884  -0.2366 141 CYS B CB  
996   S SG  . CYS A 125 ? 2.0252 2.3211 1.5167 0.3932  0.0996  -0.2506 141 CYS B SG  
997   N N   . LEU A 126 ? 1.7059 1.9180 1.2401 0.4666  0.0722  -0.2181 142 LEU B N   
998   C CA  . LEU A 126 ? 1.6377 1.8141 1.1766 0.4769  0.0623  -0.2003 142 LEU B CA  
999   C C   . LEU A 126 ? 1.6757 1.8386 1.2066 0.4655  0.0607  -0.1797 142 LEU B C   
1000  O O   . LEU A 126 ? 1.6184 1.8002 1.1533 0.4641  0.0671  -0.1789 142 LEU B O   
1001  C CB  . LEU A 126 ? 1.5290 1.7008 1.0986 0.5009  0.0581  -0.2000 142 LEU B CB  
1002  C CG  . LEU A 126 ? 1.4711 1.6502 1.0611 0.5088  0.0555  -0.2140 142 LEU B CG  
1003  C CD1 . LEU A 126 ? 1.2795 1.4547 0.9043 0.5233  0.0490  -0.2076 142 LEU B CD1 
1004  C CD2 . LEU A 126 ? 1.5829 1.7396 1.1569 0.5112  0.0512  -0.2174 142 LEU B CD2 
1005  N N   . LEU A 127 ? 1.7297 1.8600 1.2503 0.4573  0.0521  -0.1635 143 LEU B N   
1006  C CA  . LEU A 127 ? 1.6905 1.8004 1.2100 0.4507  0.0481  -0.1421 143 LEU B CA  
1007  C C   . LEU A 127 ? 1.7018 1.7940 1.2458 0.4705  0.0420  -0.1329 143 LEU B C   
1008  O O   . LEU A 127 ? 1.6683 1.7539 1.2262 0.4873  0.0381  -0.1392 143 LEU B O   
1009  C CB  . LEU A 127 ? 1.7859 1.8671 1.2864 0.4344  0.0405  -0.1285 143 LEU B CB  
1010  C CG  . LEU A 127 ? 1.8426 1.9289 1.3151 0.4101  0.0428  -0.1288 143 LEU B CG  
1011  C CD1 . LEU A 127 ? 1.8418 1.8918 1.3039 0.3999  0.0322  -0.1103 143 LEU B CD1 
1012  C CD2 . LEU A 127 ? 1.7672 1.8766 1.2316 0.3966  0.0518  -0.1280 143 LEU B CD2 
1013  N N   . LEU A 128 ? 1.7117 1.7959 1.2609 0.4677  0.0413  -0.1175 144 LEU B N   
1014  C CA  . LEU A 128 ? 1.6277 1.6957 1.1992 0.4847  0.0359  -0.1077 144 LEU B CA  
1015  C C   . LEU A 128 ? 1.7067 1.7431 1.2826 0.4938  0.0257  -0.1031 144 LEU B C   
1016  O O   . LEU A 128 ? 1.6118 1.6452 1.2059 0.5129  0.0228  -0.1076 144 LEU B O   
1017  C CB  . LEU A 128 ? 1.5327 1.5903 1.1053 0.4758  0.0353  -0.0900 144 LEU B CB  
1018  C CG  . LEU A 128 ? 1.3955 1.4362 0.9900 0.4908  0.0301  -0.0787 144 LEU B CG  
1019  C CD1 . LEU A 128 ? 1.4319 1.4990 1.0439 0.5071  0.0356  -0.0890 144 LEU B CD1 
1020  C CD2 . LEU A 128 ? 1.3739 1.4027 0.9681 0.4792  0.0295  -0.0619 144 LEU B CD2 
1021  N N   . GLU A 129 ? 1.9876 2.0015 1.5470 0.4799  0.0202  -0.0948 145 GLU B N   
1022  C CA  . GLU A 129 ? 2.0288 2.0136 1.5901 0.4867  0.0108  -0.0915 145 GLU B CA  
1023  C C   . GLU A 129 ? 2.0842 2.0753 1.6278 0.4780  0.0116  -0.1040 145 GLU B C   
1024  O O   . GLU A 129 ? 2.1232 2.1194 1.6454 0.4583  0.0139  -0.1025 145 GLU B O   
1025  C CB  . GLU A 129 ? 2.0038 1.9540 1.5621 0.4786  0.0023  -0.0709 145 GLU B CB  
1026  C CG  . GLU A 129 ? 2.0697 1.9892 1.6297 0.4851  -0.0075 -0.0674 145 GLU B CG  
1027  C CD  . GLU A 129 ? 2.0890 2.0053 1.6715 0.5089  -0.0097 -0.0734 145 GLU B CD  
1028  O OE1 . GLU A 129 ? 2.0488 1.9759 1.6482 0.5202  -0.0066 -0.0725 145 GLU B OE1 
1029  O OE2 . GLU A 129 ? 2.1324 2.0378 1.7157 0.5162  -0.0140 -0.0800 145 GLU B OE2 
1030  N N   . PRO A 130 ? 1.9232 1.9139 1.4749 0.4917  0.0097  -0.1163 146 PRO B N   
1031  C CA  . PRO A 130 ? 1.8498 1.8319 1.4263 0.5149  0.0060  -0.1179 146 PRO B CA  
1032  C C   . PRO A 130 ? 1.7799 1.7920 1.3724 0.5302  0.0128  -0.1355 146 PRO B C   
1033  O O   . PRO A 130 ? 1.6892 1.6937 1.2996 0.5483  0.0091  -0.1399 146 PRO B O   
1034  C CB  . PRO A 130 ? 1.7974 1.7557 1.3705 0.5175  -0.0016 -0.1194 146 PRO B CB  
1035  C CG  . PRO A 130 ? 1.8275 1.8022 1.3783 0.5012  0.0029  -0.1312 146 PRO B CG  
1036  C CD  . PRO A 130 ? 1.8821 1.8686 1.4164 0.4819  0.0077  -0.1240 146 PRO B CD  
1037  N N   . GLY A 131 ? 1.7938 1.8385 1.3810 0.5235  0.0223  -0.1454 147 GLY B N   
1038  C CA  . GLY A 131 ? 1.7730 1.8467 1.3756 0.5375  0.0284  -0.1635 147 GLY B CA  
1039  C C   . GLY A 131 ? 1.7267 1.8090 1.3553 0.5423  0.0270  -0.1547 147 GLY B C   
1040  O O   . GLY A 131 ? 1.7481 1.8224 1.4014 0.5476  0.0196  -0.1499 147 GLY B O   
1041  N N   . LEU A 132 ? 1.5271 1.6261 1.1490 0.5360  0.0338  -0.1518 148 LEU B N   
1042  C CA  . LEU A 132 ? 1.4186 1.5281 1.0630 0.5369  0.0327  -0.1435 148 LEU B CA  
1043  C C   . LEU A 132 ? 1.4198 1.4999 1.0801 0.5413  0.0224  -0.1258 148 LEU B C   
1044  O O   . LEU A 132 ? 1.4234 1.5061 1.1064 0.5428  0.0179  -0.1228 148 LEU B O   
1045  C CB  . LEU A 132 ? 1.3867 1.5115 1.0184 0.5285  0.0409  -0.1400 148 LEU B CB  
1046  C CG  . LEU A 132 ? 1.3930 1.5473 1.0073 0.5170  0.0513  -0.1550 148 LEU B CG  
1047  C CD1 . LEU A 132 ? 1.4187 1.5851 1.0230 0.5063  0.0583  -0.1483 148 LEU B CD1 
1048  C CD2 . LEU A 132 ? 1.3792 1.5604 1.0132 0.5180  0.0527  -0.1692 148 LEU B CD2 
1049  N N   . ASN A 133 ? 1.5295 1.5808 1.1771 0.5407  0.0187  -0.1139 149 ASN B N   
1050  C CA  . ASN A 133 ? 1.4711 1.4929 1.1326 0.5391  0.0089  -0.0966 149 ASN B CA  
1051  C C   . ASN A 133 ? 1.4750 1.4889 1.1543 0.5408  0.0020  -0.0995 149 ASN B C   
1052  O O   . ASN A 133 ? 1.3879 1.3936 1.0863 0.5364  -0.0028 -0.0904 149 ASN B O   
1053  C CB  . ASN A 133 ? 1.4389 1.4302 1.0832 0.5377  0.0053  -0.0864 149 ASN B CB  
1054  C CG  . ASN A 133 ? 1.4505 1.4435 1.0841 0.5344  0.0105  -0.0782 149 ASN B CG  
1055  O OD1 . ASN A 133 ? 1.3524 1.3643 0.9958 0.5314  0.0147  -0.0760 149 ASN B OD1 
1056  N ND2 . ASN A 133 ? 1.5280 1.5036 1.1433 0.5211  0.0084  -0.0710 149 ASN B ND2 
1057  N N   . GLU A 134 ? 1.5415 1.5597 1.2147 0.5458  0.0028  -0.1134 150 GLU B N   
1058  C CA  . GLU A 134 ? 1.5601 1.5701 1.2503 0.5474  -0.0031 -0.1167 150 GLU B CA  
1059  C C   . GLU A 134 ? 1.5568 1.5898 1.2692 0.5485  -0.0015 -0.1224 150 GLU B C   
1060  O O   . GLU A 134 ? 1.5831 1.6059 1.3152 0.5462  -0.0068 -0.1159 150 GLU B O   
1061  C CB  . GLU A 134 ? 1.6303 1.6396 1.3072 0.5521  -0.0020 -0.1310 150 GLU B CB  
1062  C CG  . GLU A 134 ? 1.6772 1.6739 1.3688 0.5538  -0.0082 -0.1345 150 GLU B CG  
1063  C CD  . GLU A 134 ? 1.7216 1.7413 1.4356 0.5566  -0.0063 -0.1457 150 GLU B CD  
1064  O OE1 . GLU A 134 ? 1.7033 1.7525 1.4160 0.5584  0.0008  -0.1577 150 GLU B OE1 
1065  O OE2 . GLU A 134 ? 1.6927 1.7009 1.4259 0.5559  -0.0117 -0.1429 150 GLU B OE2 
1066  N N   . ILE A 135 ? 1.5178 1.5820 1.2274 0.5506  0.0062  -0.1342 151 ILE B N   
1067  C CA  . ILE A 135 ? 1.4110 1.4970 1.1416 0.5515  0.0074  -0.1384 151 ILE B CA  
1068  C C   . ILE A 135 ? 1.3661 1.4424 1.1089 0.5472  0.0037  -0.1219 151 ILE B C   
1069  O O   . ILE A 135 ? 1.3076 1.3807 1.0704 0.5469  -0.0003 -0.1191 151 ILE B O   
1070  C CB  . ILE A 135 ? 1.3918 1.5128 1.1170 0.5513  0.0166  -0.1519 151 ILE B CB  
1071  C CG1 . ILE A 135 ? 1.4254 1.5609 1.1414 0.5523  0.0216  -0.1711 151 ILE B CG1 
1072  C CG2 . ILE A 135 ? 1.2721 1.4122 1.0183 0.5520  0.0170  -0.1528 151 ILE B CG2 
1073  C CD1 . ILE A 135 ? 1.3574 1.5273 1.0670 0.5470  0.0315  -0.1839 151 ILE B CD1 
1074  N N   . MET A 136 ? 1.2985 1.3710 1.0297 0.5430  0.0057  -0.1116 152 MET B N   
1075  C CA  . MET A 136 ? 1.2715 1.3380 1.0135 0.5373  0.0036  -0.0974 152 MET B CA  
1076  C C   . MET A 136 ? 1.2482 1.2854 1.0015 0.5317  -0.0040 -0.0858 152 MET B C   
1077  O O   . MET A 136 ? 1.2206 1.2558 0.9891 0.5269  -0.0059 -0.0781 152 MET B O   
1078  C CB  . MET A 136 ? 1.1812 1.2479 0.9090 0.5331  0.0075  -0.0890 152 MET B CB  
1079  C CG  . MET A 136 ? 1.1923 1.2892 0.9099 0.5352  0.0163  -0.0992 152 MET B CG  
1080  S SD  . MET A 136 ? 1.2453 1.3743 0.9825 0.5369  0.0189  -0.1073 152 MET B SD  
1081  C CE  . MET A 136 ? 1.1579 1.2778 0.9065 0.5310  0.0160  -0.0899 152 MET B CE  
1082  N N   . ALA A 137 ? 1.2889 1.3040 1.0353 0.5311  -0.0078 -0.0849 153 ALA B N   
1083  C CA  . ALA A 137 ? 1.2910 1.2798 1.0496 0.5232  -0.0141 -0.0746 153 ALA B CA  
1084  C C   . ALA A 137 ? 1.2699 1.2600 1.0476 0.5256  -0.0170 -0.0807 153 ALA B C   
1085  O O   . ALA A 137 ? 1.2103 1.1883 1.0049 0.5186  -0.0204 -0.0727 153 ALA B O   
1086  C CB  . ALA A 137 ? 1.4161 1.3796 1.1604 0.5199  -0.0173 -0.0699 153 ALA B CB  
1087  N N   . ASN A 138 ? 1.3294 1.3344 1.1061 0.5347  -0.0152 -0.0954 154 ASN B N   
1088  C CA  . ASN A 138 ? 1.3376 1.3416 1.1333 0.5370  -0.0179 -0.1013 154 ASN B CA  
1089  C C   . ASN A 138 ? 1.2454 1.2736 1.0580 0.5418  -0.0155 -0.1085 154 ASN B C   
1090  O O   . ASN A 138 ? 1.1154 1.1389 0.9486 0.5403  -0.0184 -0.1061 154 ASN B O   
1091  C CB  . ASN A 138 ? 1.4828 1.4848 1.2702 0.5431  -0.0181 -0.1137 154 ASN B CB  
1092  C CG  . ASN A 138 ? 1.4963 1.4717 1.2687 0.5387  -0.0216 -0.1067 154 ASN B CG  
1093  O OD1 . ASN A 138 ? 1.4243 1.3791 1.2069 0.5332  -0.0263 -0.1005 154 ASN B OD1 
1094  N ND2 . ASN A 138 ? 1.5471 1.5237 1.2960 0.5410  -0.0191 -0.1084 154 ASN B ND2 
1095  N N   . SER A 139 ? 1.3441 1.3982 1.1496 0.5468  -0.0102 -0.1170 155 SER B N   
1096  C CA  . SER A 139 ? 1.2644 1.3434 1.0850 0.5526  -0.0076 -0.1283 155 SER B CA  
1097  C C   . SER A 139 ? 1.1094 1.1894 0.9488 0.5499  -0.0098 -0.1194 155 SER B C   
1098  O O   . SER A 139 ? 1.1404 1.2124 0.9772 0.5437  -0.0106 -0.1064 155 SER B O   
1099  C CB  . SER A 139 ? 1.3161 1.4240 1.1250 0.5559  -0.0007 -0.1391 155 SER B CB  
1100  O OG  . SER A 139 ? 1.2935 1.4258 1.1185 0.5605  0.0017  -0.1506 155 SER B OG  
1101  N N   . LEU A 140 ? 1.1850 1.2757 1.0439 0.5546  -0.0103 -0.1272 156 LEU B N   
1102  C CA  . LEU A 140 ? 1.2854 1.3840 1.1622 0.5543  -0.0113 -0.1222 156 LEU B CA  
1103  C C   . LEU A 140 ? 1.3422 1.4717 1.2252 0.5608  -0.0072 -0.1344 156 LEU B C   
1104  O O   . LEU A 140 ? 1.2588 1.3962 1.1576 0.5618  -0.0082 -0.1316 156 LEU B O   
1105  C CB  . LEU A 140 ? 1.1690 1.2512 1.0676 0.5531  -0.0161 -0.1179 156 LEU B CB  
1106  C CG  . LEU A 140 ? 1.1689 1.2217 1.0648 0.5441  -0.0200 -0.1043 156 LEU B CG  
1107  C CD1 . LEU A 140 ? 0.9735 1.0124 0.8925 0.5417  -0.0239 -0.0997 156 LEU B CD1 
1108  C CD2 . LEU A 140 ? 1.2042 1.2526 1.0909 0.5367  -0.0197 -0.0913 156 LEU B CD2 
1109  N N   . ASP A 141 ? 1.4182 1.5659 1.2895 0.5644  -0.0023 -0.1480 157 ASP B N   
1110  C CA  . ASP A 141 ? 1.3990 1.5777 1.2751 0.5682  0.0025  -0.1596 157 ASP B CA  
1111  C C   . ASP A 141 ? 1.3890 1.5790 1.2508 0.5643  0.0060  -0.1534 157 ASP B C   
1112  O O   . ASP A 141 ? 1.4141 1.6009 1.2561 0.5610  0.0087  -0.1517 157 ASP B O   
1113  C CB  . ASP A 141 ? 1.4269 1.6223 1.2986 0.5716  0.0072  -0.1786 157 ASP B CB  
1114  C CG  . ASP A 141 ? 1.5220 1.7506 1.3979 0.5731  0.0130  -0.1911 157 ASP B CG  
1115  O OD1 . ASP A 141 ? 1.5293 1.7694 1.4255 0.5775  0.0124  -0.1985 157 ASP B OD1 
1116  O OD2 . ASP A 141 ? 1.5752 1.8178 1.4351 0.5693  0.0181  -0.1925 157 ASP B OD2 
1117  N N   . TYR A 142 ? 1.4351 1.3576 1.1240 0.5156  0.0331  0.0406  158 TYR B N   
1118  C CA  . TYR A 142 ? 1.3815 1.3434 1.0862 0.4941  0.0466  0.0502  158 TYR B CA  
1119  C C   . TYR A 142 ? 1.3796 1.3678 1.0719 0.4980  0.0596  0.0496  158 TYR B C   
1120  O O   . TYR A 142 ? 1.3677 1.3726 1.0669 0.4790  0.0663  0.0526  158 TYR B O   
1121  C CB  . TYR A 142 ? 1.3531 1.3453 1.0754 0.4913  0.0524  0.0621  158 TYR B CB  
1122  C CG  . TYR A 142 ? 1.2945 1.3272 1.0339 0.4697  0.0649  0.0731  158 TYR B CG  
1123  C CD1 . TYR A 142 ? 1.2634 1.3344 0.9996 0.4728  0.0788  0.0786  158 TYR B CD1 
1124  C CD2 . TYR A 142 ? 1.2981 1.3319 1.0573 0.4471  0.0622  0.0790  158 TYR B CD2 
1125  C CE1 . TYR A 142 ? 1.2257 1.3326 0.9776 0.4529  0.0886  0.0891  158 TYR B CE1 
1126  C CE2 . TYR A 142 ? 1.2265 1.2961 1.0000 0.4282  0.0728  0.0885  158 TYR B CE2 
1127  C CZ  . TYR A 142 ? 1.1881 1.2931 0.9577 0.4308  0.0853  0.0934  158 TYR B CZ  
1128  O OH  . TYR A 142 ? 1.0715 1.2096 0.8550 0.4116  0.0940  0.1029  158 TYR B OH  
1129  N N   . ASN A 143 ? 1.4390 1.4338 1.1139 0.5225  0.0636  0.0466  159 ASN B N   
1130  C CA  . ASN A 143 ? 1.4176 1.4449 1.0838 0.5258  0.0772  0.0492  159 ASN B CA  
1131  C C   . ASN A 143 ? 1.4193 1.4266 1.0698 0.5234  0.0745  0.0396  159 ASN B C   
1132  O O   . ASN A 143 ? 1.3978 1.4303 1.0499 0.5123  0.0840  0.0435  159 ASN B O   
1133  C CB  . ASN A 143 ? 1.4942 1.5376 1.1469 0.5536  0.0833  0.0500  159 ASN B CB  
1134  C CG  . ASN A 143 ? 1.4144 1.4895 1.0845 0.5532  0.0898  0.0624  159 ASN B CG  
1135  O OD1 . ASN A 143 ? 1.3244 1.4202 1.0154 0.5307  0.0936  0.0720  159 ASN B OD1 
1136  N ND2 . ASN A 143 ? 1.4345 1.5124 1.0951 0.5698  0.0896  0.0624  159 ASN B ND2 
1137  N N   . GLU A 144 ? 1.5003 1.4621 1.1366 0.5329  0.0608  0.0277  160 GLU B N   
1138  C CA  . GLU A 144 ? 1.5521 1.4901 1.1743 0.5293  0.0562  0.0183  160 GLU B CA  
1139  C C   . GLU A 144 ? 1.4738 1.4145 1.1141 0.4991  0.0565  0.0221  160 GLU B C   
1140  O O   . GLU A 144 ? 1.5021 1.4544 1.1391 0.4897  0.0625  0.0217  160 GLU B O   
1141  C CB  . GLU A 144 ? 1.5994 1.4866 1.2054 0.5390  0.0387  0.0061  160 GLU B CB  
1142  C CG  . GLU A 144 ? 1.6895 1.5493 1.2755 0.5388  0.0322  -0.0046 160 GLU B CG  
1143  C CD  . GLU A 144 ? 1.6305 1.4403 1.2055 0.5392  0.0126  -0.0152 160 GLU B CD  
1144  O OE1 . GLU A 144 ? 1.5575 1.3544 1.1404 0.5402  0.0041  -0.0144 160 GLU B OE1 
1145  O OE2 . GLU A 144 ? 1.6224 1.4065 1.1821 0.5376  0.0053  -0.0238 160 GLU B OE2 
1146  N N   . ARG A 145 ? 1.3832 1.3139 1.0430 0.4840  0.0501  0.0260  161 ARG B N   
1147  C CA  . ARG A 145 ? 1.3144 1.2492 0.9926 0.4562  0.0509  0.0300  161 ARG B CA  
1148  C C   . ARG A 145 ? 1.2949 1.2759 0.9830 0.4436  0.0661  0.0392  161 ARG B C   
1149  O O   . ARG A 145 ? 1.3199 1.3072 1.0108 0.4279  0.0695  0.0390  161 ARG B O   
1150  C CB  . ARG A 145 ? 1.2830 1.2056 0.9802 0.4457  0.0430  0.0345  161 ARG B CB  
1151  C CG  . ARG A 145 ? 1.3101 1.1862 1.0002 0.4563  0.0260  0.0271  161 ARG B CG  
1152  C CD  . ARG A 145 ? 1.3264 1.1942 1.0382 0.4435  0.0185  0.0337  161 ARG B CD  
1153  N NE  . ARG A 145 ? 1.2519 1.1242 0.9817 0.4178  0.0198  0.0383  161 ARG B NE  
1154  C CZ  . ARG A 145 ? 1.2969 1.1376 1.0294 0.4081  0.0091  0.0345  161 ARG B CZ  
1155  N NH1 . ARG A 145 ? 1.3088 1.1095 1.0288 0.4206  -0.0052 0.0268  161 ARG B NH1 
1156  N NH2 . ARG A 145 ? 1.2854 1.1342 1.0340 0.3856  0.0123  0.0389  161 ARG B NH2 
1157  N N   . LEU A 146 ? 1.2470 1.2602 0.9407 0.4503  0.0745  0.0478  162 LEU B N   
1158  C CA  . LEU A 146 ? 1.2436 1.3010 0.9473 0.4385  0.0878  0.0577  162 LEU B CA  
1159  C C   . LEU A 146 ? 1.2601 1.3301 0.9497 0.4430  0.0943  0.0555  162 LEU B C   
1160  O O   . LEU A 146 ? 1.2700 1.3617 0.9676 0.4257  0.1005  0.0603  162 LEU B O   
1161  C CB  . LEU A 146 ? 1.2255 1.3140 0.9358 0.4480  0.0949  0.0676  162 LEU B CB  
1162  C CG  . LEU A 146 ? 1.1258 1.2616 0.8473 0.4372  0.1076  0.0799  162 LEU B CG  
1163  C CD1 . LEU A 146 ? 1.1040 1.2464 0.8425 0.4093  0.1079  0.0837  162 LEU B CD1 
1164  C CD2 . LEU A 146 ? 1.1810 1.3392 0.9101 0.4467  0.1116  0.0889  162 LEU B CD2 
1165  N N   . TRP A 147 ? 1.2781 1.3347 0.9462 0.4663  0.0925  0.0483  163 TRP B N   
1166  C CA  . TRP A 147 ? 1.2957 1.3661 0.9493 0.4722  0.0990  0.0469  163 TRP B CA  
1167  C C   . TRP A 147 ? 1.3344 1.3832 0.9866 0.4562  0.0937  0.0403  163 TRP B C   
1168  O O   . TRP A 147 ? 1.3412 1.4126 0.9964 0.4443  0.1004  0.0445  163 TRP B O   
1169  C CB  . TRP A 147 ? 1.2842 1.3444 0.9135 0.5025  0.0983  0.0402  163 TRP B CB  
1170  C CG  . TRP A 147 ? 1.3252 1.3905 0.9362 0.5101  0.1024  0.0363  163 TRP B CG  
1171  C CD1 . TRP A 147 ? 1.3399 1.4467 0.9497 0.5120  0.1149  0.0451  163 TRP B CD1 
1172  C CD2 . TRP A 147 ? 1.3313 1.3590 0.9218 0.5181  0.0935  0.0234  163 TRP B CD2 
1173  N NE1 . TRP A 147 ? 1.4004 1.4988 0.9906 0.5201  0.1147  0.0385  163 TRP B NE1 
1174  C CE2 . TRP A 147 ? 1.3814 1.4309 0.9588 0.5241  0.1017  0.0247  163 TRP B CE2 
1175  C CE3 . TRP A 147 ? 1.3230 1.3007 0.9053 0.5199  0.0786  0.0115  163 TRP B CE3 
1176  C CZ2 . TRP A 147 ? 1.5037 1.5266 1.0597 0.5319  0.0959  0.0141  163 TRP B CZ2 
1177  C CZ3 . TRP A 147 ? 1.2924 1.2428 0.8536 0.5274  0.0724  0.0010  163 TRP B CZ3 
1178  C CH2 . TRP A 147 ? 1.4327 1.4054 0.9804 0.5334  0.0812  0.0019  163 TRP B CH2 
1179  N N   . ALA A 148 ? 1.3962 1.4013 1.0444 0.4552  0.0809  0.0306  164 ALA B N   
1180  C CA  . ALA A 148 ? 1.3855 1.3687 1.0347 0.4386  0.0752  0.0250  164 ALA B CA  
1181  C C   . ALA A 148 ? 1.3145 1.3221 0.9857 0.4118  0.0811  0.0332  164 ALA B C   
1182  O O   . ALA A 148 ? 1.3235 1.3413 0.9950 0.4004  0.0847  0.0336  164 ALA B O   
1183  C CB  . ALA A 148 ? 1.3332 1.2686 0.9808 0.4386  0.0601  0.0165  164 ALA B CB  
1184  N N   . TRP A 149 ? 1.2433 1.2622 0.9324 0.4026  0.0824  0.0400  165 TRP B N   
1185  C CA  . TRP A 149 ? 1.1969 1.2347 0.9062 0.3778  0.0865  0.0468  165 TRP B CA  
1186  C C   . TRP A 149 ? 1.2235 1.3026 0.9353 0.3720  0.0979  0.0548  165 TRP B C   
1187  O O   . TRP A 149 ? 1.2169 1.3014 0.9328 0.3565  0.0993  0.0548  165 TRP B O   
1188  C CB  . TRP A 149 ? 1.1943 1.2369 0.9189 0.3734  0.0856  0.0526  165 TRP B CB  
1189  C CG  . TRP A 149 ? 1.1655 1.2187 0.9099 0.3492  0.0873  0.0578  165 TRP B CG  
1190  C CD1 . TRP A 149 ? 1.1138 1.1428 0.8683 0.3358  0.0800  0.0550  165 TRP B CD1 
1191  C CD2 . TRP A 149 ? 1.1141 1.2048 0.8698 0.3362  0.0964  0.0670  165 TRP B CD2 
1192  N NE1 . TRP A 149 ? 1.0610 1.1106 0.8313 0.3161  0.0849  0.0611  165 TRP B NE1 
1193  C CE2 . TRP A 149 ? 1.0480 1.1343 0.8189 0.3157  0.0944  0.0681  165 TRP B CE2 
1194  C CE3 . TRP A 149 ? 1.1118 1.2396 0.8664 0.3398  0.1058  0.0749  165 TRP B CE3 
1195  C CZ2 . TRP A 149 ? 1.0226 1.1382 0.8058 0.2994  0.1008  0.0756  165 TRP B CZ2 
1196  C CZ3 . TRP A 149 ? 1.0896 1.2465 0.8579 0.3225  0.1114  0.0833  165 TRP B CZ3 
1197  C CH2 . TRP A 149 ? 1.0358 1.1854 0.8174 0.3027  0.1087  0.0830  165 TRP B CH2 
1198  N N   . GLU A 150 ? 1.2335 1.3427 0.9438 0.3844  0.1055  0.0624  166 GLU B N   
1199  C CA  . GLU A 150 ? 1.2292 1.3805 0.9444 0.3786  0.1157  0.0725  166 GLU B CA  
1200  C C   . GLU A 150 ? 1.2727 1.4274 0.9749 0.3825  0.1178  0.0698  166 GLU B C   
1201  O O   . GLU A 150 ? 1.3118 1.4896 1.0213 0.3679  0.1221  0.0757  166 GLU B O   
1202  C CB  . GLU A 150 ? 1.1305 1.3120 0.8461 0.3935  0.1229  0.0817  166 GLU B CB  
1203  C CG  . GLU A 150 ? 1.1383 1.3627 0.8551 0.3931  0.1329  0.0927  166 GLU B CG  
1204  C CD  . GLU A 150 ? 1.1338 1.3807 0.8684 0.3675  0.1353  0.1009  166 GLU B CD  
1205  O OE1 . GLU A 150 ? 1.0941 1.3272 0.8404 0.3508  0.1307  0.0988  166 GLU B OE1 
1206  O OE2 . GLU A 150 ? 1.1588 1.4370 0.8951 0.3640  0.1413  0.1095  166 GLU B OE2 
1207  N N   . SER A 151 ? 1.3050 1.4368 0.9874 0.4021  0.1142  0.0610  167 SER B N   
1208  C CA  . SER A 151 ? 1.3706 1.5094 1.0393 0.4074  0.1170  0.0594  167 SER B CA  
1209  C C   . SER A 151 ? 1.4064 1.5232 1.0776 0.3892  0.1109  0.0531  167 SER B C   
1210  O O   . SER A 151 ? 1.4362 1.5724 1.1091 0.3798  0.1148  0.0572  167 SER B O   
1211  C CB  . SER A 151 ? 1.2900 1.4127 0.9346 0.4354  0.1155  0.0519  167 SER B CB  
1212  O OG  . SER A 151 ? 1.3163 1.3939 0.9548 0.4398  0.1041  0.0406  167 SER B OG  
1213  N N   . TRP A 152 ? 1.3699 1.4468 1.0419 0.3840  0.1009  0.0438  168 TRP B N   
1214  C CA  . TRP A 152 ? 1.3510 1.4094 1.0297 0.3641  0.0955  0.0394  168 TRP B CA  
1215  C C   . TRP A 152 ? 1.3434 1.4305 1.0420 0.3411  0.1009  0.0482  168 TRP B C   
1216  O O   . TRP A 152 ? 1.3732 1.4659 1.0741 0.3289  0.1014  0.0485  168 TRP B O   
1217  C CB  . TRP A 152 ? 1.2874 1.3038 0.9691 0.3603  0.0845  0.0313  168 TRP B CB  
1218  C CG  . TRP A 152 ? 1.2577 1.2562 0.9477 0.3403  0.0794  0.0275  168 TRP B CG  
1219  C CD1 . TRP A 152 ? 1.2498 1.2435 0.9586 0.3207  0.0773  0.0292  168 TRP B CD1 
1220  C CD2 . TRP A 152 ? 1.3092 1.2949 0.9897 0.3376  0.0764  0.0222  168 TRP B CD2 
1221  N NE1 . TRP A 152 ? 1.2780 1.2558 0.9900 0.3065  0.0731  0.0251  168 TRP B NE1 
1222  C CE2 . TRP A 152 ? 1.3578 1.3301 1.0530 0.3160  0.0722  0.0209  168 TRP B CE2 
1223  C CE3 . TRP A 152 ? 1.3457 1.3297 1.0062 0.3517  0.0768  0.0185  168 TRP B CE3 
1224  C CZ2 . TRP A 152 ? 1.3111 1.2684 1.0028 0.3077  0.0681  0.0162  168 TRP B CZ2 
1225  C CZ3 . TRP A 152 ? 1.3889 1.3578 1.0453 0.3430  0.0725  0.0139  168 TRP B CZ3 
1226  C CH2 . TRP A 152 ? 1.3172 1.2730 0.9897 0.3209  0.0681  0.0130  168 TRP B CH2 
1227  N N   . ARG A 153 ? 1.3032 1.4089 1.0162 0.3351  0.1045  0.0554  169 ARG B N   
1228  C CA  . ARG A 153 ? 1.2663 1.3971 0.9966 0.3135  0.1084  0.0630  169 ARG B CA  
1229  C C   . ARG A 153 ? 1.3472 1.5184 1.0779 0.3133  0.1165  0.0731  169 ARG B C   
1230  O O   . ARG A 153 ? 1.3116 1.4993 1.0543 0.2946  0.1177  0.0781  169 ARG B O   
1231  C CB  . ARG A 153 ? 1.1653 1.3025 0.9102 0.3058  0.1091  0.0676  169 ARG B CB  
1232  C CG  . ARG A 153 ? 1.1226 1.2283 0.8750 0.2955  0.1018  0.0609  169 ARG B CG  
1233  C CD  . ARG A 153 ? 1.1616 1.2710 0.9233 0.2960  0.1021  0.0650  169 ARG B CD  
1234  N NE  . ARG A 153 ? 1.1784 1.2622 0.9497 0.2839  0.0958  0.0606  169 ARG B NE  
1235  C CZ  . ARG A 153 ? 1.1402 1.1891 0.9071 0.2902  0.0877  0.0535  169 ARG B CZ  
1236  N NH1 . ARG A 153 ? 1.1244 1.1556 0.8755 0.3080  0.0839  0.0480  169 ARG B NH1 
1237  N NH2 . ARG A 153 ? 1.1098 1.1408 0.8882 0.2781  0.0828  0.0520  169 ARG B NH2 
1238  N N   . SER A 154 ? 1.5234 1.7111 1.2418 0.3334  0.1215  0.0766  170 SER B N   
1239  C CA  . SER A 154 ? 1.4964 1.7260 1.2170 0.3336  0.1294  0.0885  170 SER B CA  
1240  C C   . SER A 154 ? 1.5238 1.7562 1.2321 0.3387  0.1301  0.0871  170 SER B C   
1241  O O   . SER A 154 ? 1.5669 1.8314 1.2812 0.3311  0.1345  0.0972  170 SER B O   
1242  C CB  . SER A 154 ? 1.4765 1.7311 1.1940 0.3520  0.1362  0.0966  170 SER B CB  
1243  O OG  . SER A 154 ? 1.5918 1.8353 1.2891 0.3766  0.1369  0.0907  170 SER B OG  
1244  N N   . GLU A 155 ? 1.5969 1.7971 1.2884 0.3509  0.1253  0.0756  171 GLU B N   
1245  C CA  . GLU A 155 ? 1.6895 1.8887 1.3689 0.3539  0.1249  0.0732  171 GLU B CA  
1246  C C   . GLU A 155 ? 1.6430 1.8265 1.3322 0.3306  0.1189  0.0694  171 GLU B C   
1247  O O   . GLU A 155 ? 1.6560 1.8593 1.3490 0.3207  0.1206  0.0752  171 GLU B O   
1248  C CB  . GLU A 155 ? 1.7720 1.9416 1.4276 0.3774  0.1215  0.0620  171 GLU B CB  
1249  C CG  . GLU A 155 ? 1.9196 2.1089 1.5563 0.3978  0.1275  0.0649  171 GLU B CG  
1250  C CD  . GLU A 155 ? 2.0262 2.2238 1.6607 0.3878  0.1273  0.0667  171 GLU B CD  
1251  O OE1 . GLU A 155 ? 1.9505 2.1169 1.5847 0.3759  0.1192  0.0578  171 GLU B OE1 
1252  O OE2 . GLU A 155 ? 2.1547 2.3904 1.7882 0.3922  0.1350  0.0776  171 GLU B OE2 
1253  N N   . VAL A 156 ? 1.4847 1.6344 1.1797 0.3211  0.1116  0.0607  172 VAL B N   
1254  C CA  . VAL A 156 ? 1.3522 1.4821 1.0552 0.3013  0.1054  0.0556  172 VAL B CA  
1255  C C   . VAL A 156 ? 1.2578 1.4052 0.9824 0.2786  0.1066  0.0622  172 VAL B C   
1256  O O   . VAL A 156 ? 1.2285 1.3856 0.9612 0.2630  0.1058  0.0651  172 VAL B O   
1257  C CB  . VAL A 156 ? 1.2906 1.3744 0.9880 0.3041  0.0966  0.0434  172 VAL B CB  
1258  C CG1 . VAL A 156 ? 1.2486 1.3108 0.9514 0.2874  0.0903  0.0380  172 VAL B CG1 
1259  C CG2 . VAL A 156 ? 1.3850 1.4532 1.0600 0.3280  0.0951  0.0374  172 VAL B CG2 
1260  N N   . GLY A 157 ? 1.1559 1.3066 0.8900 0.2766  0.1079  0.0645  173 GLY B N   
1261  C CA  . GLY A 157 ? 1.0992 1.2680 0.8516 0.2572  0.1093  0.0709  173 GLY B CA  
1262  C C   . GLY A 157 ? 1.1025 1.3104 0.8608 0.2503  0.1141  0.0825  173 GLY B C   
1263  O O   . GLY A 157 ? 1.0810 1.2941 0.8497 0.2319  0.1117  0.0842  173 GLY B O   
1264  N N   . LYS A 158 ? 1.1458 1.3817 0.8979 0.2651  0.1204  0.0909  174 LYS B N   
1265  C CA  . LYS A 158 ? 1.1306 1.4065 0.8900 0.2586  0.1246  0.1042  174 LYS B CA  
1266  C C   . LYS A 158 ? 1.1042 1.3816 0.8621 0.2506  0.1220  0.1042  174 LYS B C   
1267  O O   . LYS A 158 ? 1.1564 1.4626 0.9245 0.2387  0.1228  0.1149  174 LYS B O   
1268  C CB  . LYS A 158 ? 1.1707 1.4761 0.9229 0.2783  0.1322  0.1137  174 LYS B CB  
1269  C CG  . LYS A 158 ? 1.0976 1.4234 0.8589 0.2797  0.1362  0.1221  174 LYS B CG  
1270  C CD  . LYS A 158 ? 1.1073 1.4509 0.8575 0.3046  0.1432  0.1274  174 LYS B CD  
1271  C CE  . LYS A 158 ? 1.0782 1.4399 0.8365 0.3083  0.1470  0.1353  174 LYS B CE  
1272  N NZ  . LYS A 158 ? 1.0586 1.4642 0.8298 0.2990  0.1511  0.1525  174 LYS B NZ  
1273  N N   . GLN A 159 ? 1.0789 1.3256 0.8251 0.2559  0.1180  0.0932  175 GLN B N   
1274  C CA  . GLN A 159 ? 1.0416 1.2866 0.7885 0.2452  0.1144  0.0926  175 GLN B CA  
1275  C C   . GLN A 159 ? 1.0733 1.3003 0.8346 0.2222  0.1079  0.0878  175 GLN B C   
1276  O O   . GLN A 159 ? 1.0941 1.3327 0.8644 0.2071  0.1054  0.0922  175 GLN B O   
1277  C CB  . GLN A 159 ? 1.1273 1.3453 0.8560 0.2588  0.1118  0.0826  175 GLN B CB  
1278  C CG  . GLN A 159 ? 1.2894 1.5190 1.0006 0.2832  0.1174  0.0847  175 GLN B CG  
1279  C CD  . GLN A 159 ? 1.3749 1.5751 1.0671 0.2949  0.1135  0.0741  175 GLN B CD  
1280  O OE1 . GLN A 159 ? 1.3807 1.5737 1.0729 0.2851  0.1094  0.0721  175 GLN B OE1 
1281  N NE2 . GLN A 159 ? 1.4911 1.6719 1.1671 0.3156  0.1135  0.0666  175 GLN B NE2 
1282  N N   . LEU A 160 ? 1.1061 1.3039 0.8696 0.2201  0.1049  0.0785  176 LEU B N   
1283  C CA  . LEU A 160 ? 1.0077 1.1855 0.7835 0.2005  0.0991  0.0728  176 LEU B CA  
1284  C C   . LEU A 160 ? 0.9918 1.1926 0.7841 0.1833  0.0997  0.0803  176 LEU B C   
1285  O O   . LEU A 160 ? 0.9878 1.1813 0.7901 0.1660  0.0950  0.0781  176 LEU B O   
1286  C CB  . LEU A 160 ? 1.0063 1.1485 0.7798 0.2043  0.0959  0.0622  176 LEU B CB  
1287  C CG  . LEU A 160 ? 1.0203 1.1348 0.7775 0.2189  0.0928  0.0539  176 LEU B CG  
1288  C CD1 . LEU A 160 ? 0.9697 1.0523 0.7237 0.2263  0.0893  0.0459  176 LEU B CD1 
1289  C CD2 . LEU A 160 ? 1.0512 1.1518 0.8086 0.2088  0.0877  0.0499  176 LEU B CD2 
1290  N N   . ARG A 161 ? 0.9525 1.1805 0.7474 0.1878  0.1046  0.0894  177 ARG B N   
1291  C CA  . ARG A 161 ? 0.9481 1.1954 0.7575 0.1718  0.1042  0.0962  177 ARG B CA  
1292  C C   . ARG A 161 ? 0.9530 1.2120 0.7721 0.1539  0.0997  0.1006  177 ARG B C   
1293  O O   . ARG A 161 ? 0.9949 1.2428 0.8238 0.1378  0.0952  0.0965  177 ARG B O   
1294  C CB  . ARG A 161 ? 0.9908 1.2698 0.8000 0.1813  0.1101  0.1076  177 ARG B CB  
1295  C CG  . ARG A 161 ? 0.9951 1.2972 0.8174 0.1670  0.1096  0.1164  177 ARG B CG  
1296  C CD  . ARG A 161 ? 0.9950 1.2752 0.8228 0.1578  0.1070  0.1083  177 ARG B CD  
1297  N NE  . ARG A 161 ? 1.0217 1.3205 0.8607 0.1426  0.1051  0.1152  177 ARG B NE  
1298  C CZ  . ARG A 161 ? 0.9410 1.2482 0.7828 0.1433  0.1074  0.1186  177 ARG B CZ  
1299  N NH1 . ARG A 161 ? 0.9196 1.2184 0.7553 0.1579  0.1115  0.1159  177 ARG B NH1 
1300  N NH2 . ARG A 161 ? 1.0046 1.3280 0.8554 0.1289  0.1047  0.1249  177 ARG B NH2 
1301  N N   . PRO A 162 ? 0.9310 1.2119 0.7483 0.1558  0.1002  0.1088  178 PRO B N   
1302  C CA  . PRO A 162 ? 0.9431 1.2349 0.7718 0.1372  0.0945  0.1137  178 PRO B CA  
1303  C C   . PRO A 162 ? 0.9618 1.2214 0.7925 0.1267  0.0883  0.1021  178 PRO B C   
1304  O O   . PRO A 162 ? 0.9805 1.2373 0.8230 0.1087  0.0826  0.1014  178 PRO B O   
1305  C CB  . PRO A 162 ? 0.8887 1.2095 0.7132 0.1449  0.0971  0.1252  178 PRO B CB  
1306  C CG  . PRO A 162 ? 0.8764 1.1853 0.6839 0.1669  0.1025  0.1194  178 PRO B CG  
1307  C CD  . PRO A 162 ? 0.8976 1.1945 0.7028 0.1745  0.1056  0.1143  178 PRO B CD  
1308  N N   . LEU A 163 ? 0.9219 1.1562 0.7410 0.1380  0.0890  0.0929  179 LEU B N   
1309  C CA  . LEU A 163 ? 0.9067 1.1088 0.7279 0.1292  0.0832  0.0820  179 LEU B CA  
1310  C C   . LEU A 163 ? 0.9314 1.1131 0.7610 0.1193  0.0810  0.0744  179 LEU B C   
1311  O O   . LEU A 163 ? 0.9448 1.1138 0.7839 0.1041  0.0757  0.0701  179 LEU B O   
1312  C CB  . LEU A 163 ? 0.8895 1.0677 0.6957 0.1443  0.0837  0.0742  179 LEU B CB  
1313  C CG  . LEU A 163 ? 0.8892 1.0861 0.6853 0.1545  0.0858  0.0807  179 LEU B CG  
1314  C CD1 . LEU A 163 ? 0.9323 1.1067 0.7099 0.1737  0.0871  0.0728  179 LEU B CD1 
1315  C CD2 . LEU A 163 ? 0.8393 1.0396 0.6433 0.1394  0.0802  0.0831  179 LEU B CD2 
1316  N N   . TYR A 164 ? 0.9025 1.0817 0.7291 0.1280  0.0851  0.0731  180 TYR B N   
1317  C CA  . TYR A 164 ? 0.8715 1.0326 0.7055 0.1197  0.0836  0.0665  180 TYR B CA  
1318  C C   . TYR A 164 ? 0.9112 1.0894 0.7575 0.1029  0.0814  0.0711  180 TYR B C   
1319  O O   . TYR A 164 ? 0.9007 1.0626 0.7546 0.0909  0.0778  0.0648  180 TYR B O   
1320  C CB  . TYR A 164 ? 0.8394 0.9967 0.6681 0.1325  0.0881  0.0655  180 TYR B CB  
1321  C CG  . TYR A 164 ? 0.8362 0.9643 0.6689 0.1287  0.0861  0.0564  180 TYR B CG  
1322  C CD1 . TYR A 164 ? 0.8681 0.9656 0.6967 0.1328  0.0829  0.0482  180 TYR B CD1 
1323  C CD2 . TYR A 164 ? 0.7983 0.9298 0.6396 0.1196  0.0867  0.0565  180 TYR B CD2 
1324  C CE1 . TYR A 164 ? 0.8584 0.9307 0.6922 0.1289  0.0808  0.0414  180 TYR B CE1 
1325  C CE2 . TYR A 164 ? 0.7973 0.9039 0.6428 0.1163  0.0853  0.0491  180 TYR B CE2 
1326  C CZ  . TYR A 164 ? 0.8273 0.9050 0.6698 0.1209  0.0824  0.0421  180 TYR B CZ  
1327  O OH  . TYR A 164 ? 0.8331 0.8872 0.6813 0.1175  0.0806  0.0363  180 TYR B OH  
1328  N N   . GLU A 165 ? 0.9433 1.1542 0.7914 0.1021  0.0830  0.0825  181 GLU B N   
1329  C CA  . GLU A 165 ? 0.9434 1.1704 0.8025 0.0858  0.0790  0.0877  181 GLU B CA  
1330  C C   . GLU A 165 ? 0.9190 1.1351 0.7855 0.0710  0.0718  0.0840  181 GLU B C   
1331  O O   . GLU A 165 ? 0.8884 1.0931 0.7625 0.0580  0.0674  0.0787  181 GLU B O   
1332  C CB  . GLU A 165 ? 0.9729 1.2377 0.8332 0.0880  0.0810  0.1024  181 GLU B CB  
1333  C CG  . GLU A 165 ? 0.9797 1.2588 0.8339 0.1029  0.0882  0.1076  181 GLU B CG  
1334  C CD  . GLU A 165 ? 1.0788 1.3972 0.9370 0.1026  0.0896  0.1236  181 GLU B CD  
1335  O OE1 . GLU A 165 ? 1.1914 1.5272 1.0560 0.0930  0.0852  0.1317  181 GLU B OE1 
1336  O OE2 . GLU A 165 ? 1.0168 1.3493 0.8725 0.1120  0.0948  0.1291  181 GLU B OE2 
1337  N N   . GLU A 166 ? 0.9538 1.1727 0.8177 0.0735  0.0704  0.0864  182 GLU B N   
1338  C CA  . GLU A 166 ? 0.9997 1.2097 0.8717 0.0591  0.0630  0.0839  182 GLU B CA  
1339  C C   . GLU A 166 ? 0.9583 1.1317 0.8311 0.0559  0.0609  0.0702  182 GLU B C   
1340  O O   . GLU A 166 ? 0.9372 1.0994 0.8192 0.0418  0.0549  0.0659  182 GLU B O   
1341  C CB  . GLU A 166 ? 0.9875 1.2111 0.8565 0.0625  0.0621  0.0909  182 GLU B CB  
1342  C CG  . GLU A 166 ? 1.0728 1.2935 0.9524 0.0460  0.0535  0.0913  182 GLU B CG  
1343  C CD  . GLU A 166 ? 1.1639 1.4029 1.0418 0.0481  0.0523  0.1002  182 GLU B CD  
1344  O OE1 . GLU A 166 ? 1.2495 1.5127 1.1202 0.0603  0.0580  0.1094  182 GLU B OE1 
1345  O OE2 . GLU A 166 ? 1.2427 1.4722 1.1265 0.0380  0.0459  0.0984  182 GLU B OE2 
1346  N N   . TYR A 167 ? 0.8985 1.0529 0.7622 0.0692  0.0653  0.0638  183 TYR B N   
1347  C CA  . TYR A 167 ? 0.8944 1.0149 0.7595 0.0674  0.0636  0.0523  183 TYR B CA  
1348  C C   . TYR A 167 ? 0.8721 0.9859 0.7454 0.0579  0.0630  0.0480  183 TYR B C   
1349  O O   . TYR A 167 ? 0.8245 0.9183 0.7049 0.0485  0.0592  0.0409  183 TYR B O   
1350  C CB  . TYR A 167 ? 0.8763 0.9812 0.7298 0.0843  0.0678  0.0484  183 TYR B CB  
1351  C CG  . TYR A 167 ? 0.8560 0.9317 0.7109 0.0856  0.0677  0.0395  183 TYR B CG  
1352  C CD1 . TYR A 167 ? 0.8315 0.8781 0.6878 0.0832  0.0637  0.0321  183 TYR B CD1 
1353  C CD2 . TYR A 167 ? 0.9178 0.9960 0.7728 0.0899  0.0717  0.0396  183 TYR B CD2 
1354  C CE1 . TYR A 167 ? 0.8333 0.8547 0.6922 0.0848  0.0635  0.0256  183 TYR B CE1 
1355  C CE2 . TYR A 167 ? 0.9346 0.9886 0.7918 0.0915  0.0717  0.0331  183 TYR B CE2 
1356  C CZ  . TYR A 167 ? 0.8751 0.9012 0.7345 0.0891  0.0677  0.0265  183 TYR B CZ  
1357  O OH  . TYR A 167 ? 0.7997 0.8052 0.6624 0.0910  0.0678  0.0222  183 TYR B OH  
1358  N N   . VAL A 168 ? 0.8801 1.0114 0.7525 0.0603  0.0666  0.0526  184 VAL B N   
1359  C CA  . VAL A 168 ? 0.8213 0.9481 0.7002 0.0514  0.0659  0.0488  184 VAL B CA  
1360  C C   . VAL A 168 ? 0.8267 0.9603 0.7145 0.0352  0.0592  0.0498  184 VAL B C   
1361  O O   . VAL A 168 ? 0.8492 0.9666 0.7429 0.0262  0.0562  0.0425  184 VAL B O   
1362  C CB  . VAL A 168 ? 0.7699 0.9139 0.6455 0.0572  0.0708  0.0538  184 VAL B CB  
1363  C CG1 . VAL A 168 ? 0.7592 0.8998 0.6403 0.0471  0.0694  0.0501  184 VAL B CG1 
1364  C CG2 . VAL A 168 ? 0.7575 0.8921 0.6254 0.0728  0.0762  0.0523  184 VAL B CG2 
1365  N N   . VAL A 169 ? 0.8107 0.9680 0.6999 0.0317  0.0563  0.0591  185 VAL B N   
1366  C CA  . VAL A 169 ? 0.8309 0.9951 0.7293 0.0157  0.0483  0.0612  185 VAL B CA  
1367  C C   . VAL A 169 ? 0.9022 1.0418 0.8065 0.0077  0.0431  0.0525  185 VAL B C   
1368  O O   . VAL A 169 ? 0.9247 1.0541 0.8360 -0.0038 0.0378  0.0471  185 VAL B O   
1369  C CB  . VAL A 169 ? 0.8276 1.0212 0.7277 0.0136  0.0454  0.0742  185 VAL B CB  
1370  C CG1 . VAL A 169 ? 0.8192 1.0149 0.7299 -0.0034 0.0353  0.0757  185 VAL B CG1 
1371  C CG2 . VAL A 169 ? 0.8549 1.0745 0.7515 0.0194  0.0496  0.0838  185 VAL B CG2 
1372  N N   . LEU A 170 ? 0.8873 1.0163 0.7883 0.0141  0.0443  0.0511  186 LEU B N   
1373  C CA  . LEU A 170 ? 0.8520 0.9597 0.7593 0.0063  0.0389  0.0446  186 LEU B CA  
1374  C C   . LEU A 170 ? 0.8519 0.9306 0.7609 0.0068  0.0406  0.0333  186 LEU B C   
1375  O O   . LEU A 170 ? 0.8982 0.9624 0.8158 -0.0037 0.0357  0.0274  186 LEU B O   
1376  C CB  . LEU A 170 ? 0.8174 0.9236 0.7196 0.0131  0.0393  0.0472  186 LEU B CB  
1377  C CG  . LEU A 170 ? 0.8662 1.0005 0.7693 0.0103  0.0363  0.0588  186 LEU B CG  
1378  C CD1 . LEU A 170 ? 0.9158 1.0532 0.8085 0.0234  0.0403  0.0619  186 LEU B CD1 
1379  C CD2 . LEU A 170 ? 0.9503 1.0806 0.8653 -0.0056 0.0271  0.0586  186 LEU B CD2 
1380  N N   . LYS A 171 ? 0.8548 0.9246 0.7563 0.0192  0.0472  0.0307  187 LYS B N   
1381  C CA  . LYS A 171 ? 0.8367 0.8815 0.7409 0.0198  0.0489  0.0219  187 LYS B CA  
1382  C C   . LYS A 171 ? 0.8861 0.9326 0.7967 0.0103  0.0476  0.0187  187 LYS B C   
1383  O O   . LYS A 171 ? 0.9202 0.9477 0.8375 0.0045  0.0458  0.0114  187 LYS B O   
1384  C CB  . LYS A 171 ? 0.8258 0.8654 0.7219 0.0339  0.0554  0.0217  187 LYS B CB  
1385  C CG  . LYS A 171 ? 0.8507 0.8784 0.7398 0.0439  0.0556  0.0216  187 LYS B CG  
1386  C CD  . LYS A 171 ? 0.8264 0.8248 0.7208 0.0409  0.0526  0.0145  187 LYS B CD  
1387  C CE  . LYS A 171 ? 0.8081 0.7925 0.6946 0.0502  0.0514  0.0141  187 LYS B CE  
1388  N NZ  . LYS A 171 ? 0.8390 0.7935 0.7318 0.0473  0.0484  0.0080  187 LYS B NZ  
1389  N N   . ASN A 172 ? 0.8388 0.9079 0.7470 0.0090  0.0484  0.0241  188 ASN B N   
1390  C CA  . ASN A 172 ? 0.8367 0.9073 0.7486 0.0007  0.0465  0.0207  188 ASN B CA  
1391  C C   . ASN A 172 ? 0.8808 0.9457 0.8012 -0.0129 0.0381  0.0176  188 ASN B C   
1392  O O   . ASN A 172 ? 0.8947 0.9451 0.8194 -0.0185 0.0364  0.0098  188 ASN B O   
1393  C CB  . ASN A 172 ? 0.8524 0.9487 0.7595 0.0019  0.0480  0.0283  188 ASN B CB  
1394  C CG  . ASN A 172 ? 0.8447 0.9407 0.7461 0.0110  0.0554  0.0273  188 ASN B CG  
1395  O OD1 . ASN A 172 ? 0.8451 0.9220 0.7475 0.0142  0.0585  0.0204  188 ASN B OD1 
1396  N ND2 . ASN A 172 ? 0.7913 0.9094 0.6876 0.0157  0.0581  0.0352  188 ASN B ND2 
1397  N N   . GLU A 173 ? 0.9613 1.0377 0.8844 -0.0179 0.0325  0.0239  189 GLU B N   
1398  C CA  . GLU A 173 ? 0.9841 1.0538 0.9166 -0.0311 0.0234  0.0214  189 GLU B CA  
1399  C C   . GLU A 173 ? 0.8890 0.9305 0.8267 -0.0321 0.0233  0.0119  189 GLU B C   
1400  O O   . GLU A 173 ? 0.9417 0.9707 0.8862 -0.0405 0.0186  0.0052  189 GLU B O   
1401  C CB  . GLU A 173 ? 0.9853 1.0720 0.9205 -0.0353 0.0179  0.0310  189 GLU B CB  
1402  C CG  . GLU A 173 ? 1.1291 1.2450 1.0623 -0.0373 0.0161  0.0414  189 GLU B CG  
1403  C CD  . GLU A 173 ? 1.1777 1.3130 1.1153 -0.0425 0.0102  0.0524  189 GLU B CD  
1404  O OE1 . GLU A 173 ? 1.1497 1.2743 1.0936 -0.0482 0.0052  0.0505  189 GLU B OE1 
1405  O OE2 . GLU A 173 ? 1.2518 1.4139 1.1877 -0.0417 0.0100  0.0635  189 GLU B OE2 
1406  N N   . MET A 174 ? 0.8731 0.9040 0.8076 -0.0231 0.0281  0.0113  190 MET B N   
1407  C CA  . MET A 174 ? 0.8866 0.8909 0.8267 -0.0238 0.0277  0.0039  190 MET B CA  
1408  C C   . MET A 174 ? 0.8947 0.8843 0.8368 -0.0222 0.0317  -0.0038 190 MET B C   
1409  O O   . MET A 174 ? 0.9106 0.8825 0.8609 -0.0280 0.0290  -0.0103 190 MET B O   
1410  C CB  . MET A 174 ? 0.8428 0.8403 0.7770 -0.0136 0.0312  0.0061  190 MET B CB  
1411  C CG  . MET A 174 ? 0.8848 0.8553 0.8234 -0.0126 0.0307  0.0004  190 MET B CG  
1412  S SD  . MET A 174 ? 0.8909 0.8461 0.8273 -0.0029 0.0382  -0.0042 190 MET B SD  
1413  C CE  . MET A 174 ? 0.9513 0.8837 0.8851 0.0051  0.0380  -0.0047 190 MET B CE  
1414  N N   . ALA A 175 ? 0.9478 0.9451 0.8828 -0.0143 0.0382  -0.0027 191 ALA B N   
1415  C CA  . ALA A 175 ? 0.8981 0.8828 0.8351 -0.0123 0.0424  -0.0091 191 ALA B CA  
1416  C C   . ALA A 175 ? 0.8679 0.8559 0.8078 -0.0211 0.0388  -0.0134 191 ALA B C   
1417  O O   . ALA A 175 ? 0.8669 0.8404 0.8115 -0.0225 0.0399  -0.0203 191 ALA B O   
1418  C CB  . ALA A 175 ? 0.9109 0.9022 0.8401 -0.0012 0.0501  -0.0062 191 ALA B CB  
1419  N N   . ARG A 176 ? 0.7725 0.7790 0.7098 -0.0268 0.0341  -0.0092 192 ARG B N   
1420  C CA  . ARG A 176 ? 0.8325 0.8397 0.7717 -0.0358 0.0285  -0.0138 192 ARG B CA  
1421  C C   . ARG A 176 ? 0.8641 0.8560 0.8134 -0.0451 0.0208  -0.0188 192 ARG B C   
1422  O O   . ARG A 176 ? 0.8324 0.8125 0.7849 -0.0492 0.0185  -0.0268 192 ARG B O   
1423  C CB  . ARG A 176 ? 0.8746 0.9054 0.8088 -0.0400 0.0241  -0.0067 192 ARG B CB  
1424  C CG  . ARG A 176 ? 0.8462 0.8934 0.7712 -0.0315 0.0313  -0.0014 192 ARG B CG  
1425  C CD  . ARG A 176 ? 0.8915 0.9625 0.8133 -0.0366 0.0260  0.0071  192 ARG B CD  
1426  N NE  . ARG A 176 ? 0.9121 1.0012 0.8271 -0.0274 0.0327  0.0153  192 ARG B NE  
1427  C CZ  . ARG A 176 ? 1.0182 1.1120 0.9267 -0.0220 0.0384  0.0147  192 ARG B CZ  
1428  N NH1 . ARG A 176 ? 1.0789 1.1628 0.9857 -0.0248 0.0382  0.0068  192 ARG B NH1 
1429  N NH2 . ARG A 176 ? 0.9646 1.0740 0.8679 -0.0133 0.0444  0.0223  192 ARG B NH2 
1430  N N   . ALA A 177 ? 0.9188 0.9106 0.8729 -0.0479 0.0169  -0.0144 193 ALA B N   
1431  C CA  . ALA A 177 ? 0.9395 0.9167 0.9041 -0.0569 0.0093  -0.0184 193 ALA B CA  
1432  C C   . ALA A 177 ? 0.9330 0.8863 0.9032 -0.0535 0.0135  -0.0258 193 ALA B C   
1433  O O   . ALA A 177 ? 0.9570 0.8960 0.9368 -0.0606 0.0078  -0.0304 193 ALA B O   
1434  C CB  . ALA A 177 ? 1.0063 0.9913 0.9741 -0.0607 0.0042  -0.0108 193 ALA B CB  
1435  N N   . ASN A 178 ? 0.8907 0.8398 0.8560 -0.0430 0.0227  -0.0261 194 ASN B N   
1436  C CA  . ASN A 178 ? 0.8782 0.8069 0.8492 -0.0393 0.0271  -0.0319 194 ASN B CA  
1437  C C   . ASN A 178 ? 0.8602 0.7892 0.8280 -0.0355 0.0326  -0.0369 194 ASN B C   
1438  O O   . ASN A 178 ? 0.8563 0.7731 0.8274 -0.0300 0.0384  -0.0396 194 ASN B O   
1439  C CB  . ASN A 178 ? 0.8782 0.8000 0.8474 -0.0306 0.0323  -0.0281 194 ASN B CB  
1440  C CG  . ASN A 178 ? 1.0811 0.9950 1.0549 -0.0342 0.0270  -0.0256 194 ASN B CG  
1441  O OD1 . ASN A 178 ? 1.1036 1.0267 1.0707 -0.0307 0.0267  -0.0198 194 ASN B OD1 
1442  N ND2 . ASN A 178 ? 1.0877 0.9856 1.0726 -0.0413 0.0223  -0.0298 194 ASN B ND2 
1443  N N   . HIS A 179 ? 0.8318 0.7754 0.7928 -0.0380 0.0308  -0.0372 195 HIS B N   
1444  C CA  . HIS A 179 ? 0.8441 0.7880 0.8009 -0.0362 0.0339  -0.0429 195 HIS B CA  
1445  C C   . HIS A 179 ? 0.8358 0.7862 0.7857 -0.0257 0.0439  -0.0403 195 HIS B C   
1446  O O   . HIS A 179 ? 0.8167 0.7607 0.7667 -0.0215 0.0493  -0.0449 195 HIS B O   
1447  C CB  . HIS A 179 ? 0.8436 0.7683 0.8091 -0.0386 0.0328  -0.0514 195 HIS B CB  
1448  C CG  . HIS A 179 ? 0.7799 0.6963 0.7542 -0.0488 0.0227  -0.0536 195 HIS B CG  
1449  N ND1 . HIS A 179 ? 0.8144 0.7158 0.7996 -0.0507 0.0213  -0.0537 195 HIS B ND1 
1450  C CD2 . HIS A 179 ? 0.8518 0.7742 0.8260 -0.0580 0.0127  -0.0540 195 HIS B CD2 
1451  C CE1 . HIS A 179 ? 0.7239 0.6219 0.7157 -0.0606 0.0113  -0.0550 195 HIS B CE1 
1452  N NE2 . HIS A 179 ? 0.7168 0.6273 0.7024 -0.0653 0.0057  -0.0551 195 HIS B NE2 
1453  N N   . TYR A 180 ? 0.7666 0.7303 0.7106 -0.0213 0.0462  -0.0326 196 TYR B N   
1454  C CA  . TYR A 180 ? 0.8007 0.7740 0.7375 -0.0122 0.0541  -0.0288 196 TYR B CA  
1455  C C   . TYR A 180 ? 0.8518 0.8468 0.7794 -0.0132 0.0527  -0.0241 196 TYR B C   
1456  O O   . TYR A 180 ? 0.8989 0.9032 0.8261 -0.0189 0.0464  -0.0204 196 TYR B O   
1457  C CB  . TYR A 180 ? 0.8392 0.8078 0.7772 -0.0045 0.0579  -0.0235 196 TYR B CB  
1458  C CG  . TYR A 180 ? 0.8166 0.7641 0.7638 -0.0028 0.0595  -0.0266 196 TYR B CG  
1459  C CD1 . TYR A 180 ? 0.7993 0.7326 0.7544 -0.0082 0.0541  -0.0285 196 TYR B CD1 
1460  C CD2 . TYR A 180 ? 0.7772 0.7197 0.7258 0.0040  0.0661  -0.0266 196 TYR B CD2 
1461  C CE1 . TYR A 180 ? 0.7296 0.6438 0.6939 -0.0068 0.0554  -0.0305 196 TYR B CE1 
1462  C CE2 . TYR A 180 ? 0.8015 0.7262 0.7596 0.0055  0.0673  -0.0278 196 TYR B CE2 
1463  C CZ  . TYR A 180 ? 0.7375 0.6477 0.7035 0.0002  0.0620  -0.0299 196 TYR B CZ  
1464  O OH  . TYR A 180 ? 0.6972 0.5901 0.6732 0.0020  0.0636  -0.0301 196 TYR B OH  
1465  N N   . GLU A 181 ? 0.8637 0.8680 0.7843 -0.0080 0.0583  -0.0232 197 GLU B N   
1466  C CA  . GLU A 181 ? 0.9680 0.9920 0.8808 -0.0111 0.0553  -0.0190 197 GLU B CA  
1467  C C   . GLU A 181 ? 0.8912 0.9290 0.8023 -0.0079 0.0554  -0.0096 197 GLU B C   
1468  O O   . GLU A 181 ? 0.8974 0.9494 0.8067 -0.0134 0.0497  -0.0049 197 GLU B O   
1469  C CB  . GLU A 181 ? 0.9919 1.0243 0.8968 -0.0077 0.0600  -0.0201 197 GLU B CB  
1470  C CG  . GLU A 181 ? 1.0275 1.0624 0.9301 0.0026  0.0695  -0.0170 197 GLU B CG  
1471  C CD  . GLU A 181 ? 0.9757 1.0135 0.8724 0.0040  0.0732  -0.0211 197 GLU B CD  
1472  O OE1 . GLU A 181 ? 0.8526 0.8816 0.7490 -0.0009 0.0701  -0.0291 197 GLU B OE1 
1473  O OE2 . GLU A 181 ? 0.9265 0.9753 0.8186 0.0103  0.0791  -0.0161 197 GLU B OE2 
1474  N N   . ASP A 182 ? 0.7814 0.8144 0.6934 0.0009  0.0608  -0.0067 198 ASP B N   
1475  C CA  . ASP A 182 ? 0.7802 0.8245 0.6893 0.0058  0.0613  0.0012  198 ASP B CA  
1476  C C   . ASP A 182 ? 0.8135 0.8409 0.7259 0.0129  0.0640  0.0004  198 ASP B C   
1477  O O   . ASP A 182 ? 0.8201 0.8292 0.7378 0.0129  0.0654  -0.0051 198 ASP B O   
1478  C CB  . ASP A 182 ? 0.8118 0.8762 0.7134 0.0117  0.0655  0.0079  198 ASP B CB  
1479  C CG  . ASP A 182 ? 0.8376 0.8974 0.7372 0.0197  0.0727  0.0068  198 ASP B CG  
1480  O OD1 . ASP A 182 ? 0.7976 0.8464 0.6991 0.0276  0.0761  0.0074  198 ASP B OD1 
1481  O OD2 . ASP A 182 ? 0.8605 0.9270 0.7570 0.0181  0.0745  0.0055  198 ASP B OD2 
1482  N N   . TYR A 183 ? 0.7882 0.8212 0.6970 0.0190  0.0645  0.0061  199 TYR B N   
1483  C CA  . TYR A 183 ? 0.7645 0.7798 0.6747 0.0257  0.0654  0.0052  199 TYR B CA  
1484  C C   . TYR A 183 ? 0.7666 0.7723 0.6766 0.0343  0.0707  0.0047  199 TYR B C   
1485  O O   . TYR A 183 ? 0.7594 0.7448 0.6743 0.0364  0.0704  0.0020  199 TYR B O   
1486  C CB  . TYR A 183 ? 0.7479 0.7725 0.6522 0.0314  0.0644  0.0110  199 TYR B CB  
1487  C CG  . TYR A 183 ? 0.7428 0.7481 0.6465 0.0377  0.0635  0.0097  199 TYR B CG  
1488  C CD1 . TYR A 183 ? 0.7424 0.7264 0.6535 0.0322  0.0600  0.0044  199 TYR B CD1 
1489  C CD2 . TYR A 183 ? 0.7229 0.7309 0.6183 0.0496  0.0656  0.0137  199 TYR B CD2 
1490  C CE1 . TYR A 183 ? 0.7999 0.7650 0.7099 0.0378  0.0582  0.0036  199 TYR B CE1 
1491  C CE2 . TYR A 183 ? 0.7347 0.7233 0.6277 0.0559  0.0637  0.0121  199 TYR B CE2 
1492  C CZ  . TYR A 183 ? 0.7415 0.7083 0.6416 0.0497  0.0597  0.0072  199 TYR B CZ  
1493  O OH  . TYR A 183 ? 0.6892 0.6356 0.5864 0.0557  0.0569  0.0059  199 TYR B OH  
1494  N N   . GLY A 184 ? 0.7643 0.7844 0.6698 0.0386  0.0750  0.0081  200 GLY B N   
1495  C CA  . GLY A 184 ? 0.7438 0.7562 0.6505 0.0454  0.0794  0.0084  200 GLY B CA  
1496  C C   . GLY A 184 ? 0.7049 0.7040 0.6193 0.0404  0.0803  0.0030  200 GLY B C   
1497  O O   . GLY A 184 ? 0.7052 0.6897 0.6247 0.0447  0.0819  0.0029  200 GLY B O   
1498  N N   . ASP A 185 ? 0.7283 0.7323 0.6439 0.0315  0.0787  -0.0013 201 ASP B N   
1499  C CA  . ASP A 185 ? 0.7120 0.7043 0.6341 0.0275  0.0797  -0.0071 201 ASP B CA  
1500  C C   . ASP A 185 ? 0.7475 0.7182 0.6781 0.0263  0.0770  -0.0098 201 ASP B C   
1501  O O   . ASP A 185 ? 0.7769 0.7348 0.7147 0.0278  0.0794  -0.0114 201 ASP B O   
1502  C CB  . ASP A 185 ? 0.7645 0.7644 0.6845 0.0186  0.0766  -0.0118 201 ASP B CB  
1503  C CG  . ASP A 185 ? 0.7882 0.7791 0.7123 0.0161  0.0786  -0.0182 201 ASP B CG  
1504  O OD1 . ASP A 185 ? 0.7583 0.7482 0.6835 0.0219  0.0845  -0.0170 201 ASP B OD1 
1505  O OD2 . ASP A 185 ? 0.8246 0.8099 0.7512 0.0086  0.0740  -0.0240 201 ASP B OD2 
1506  N N   . TYR A 186 ? 0.7403 0.7079 0.6706 0.0237  0.0720  -0.0094 202 TYR B N   
1507  C CA  . TYR A 186 ? 0.7192 0.6665 0.6567 0.0223  0.0686  -0.0113 202 TYR B CA  
1508  C C   . TYR A 186 ? 0.6944 0.6290 0.6333 0.0311  0.0705  -0.0077 202 TYR B C   
1509  O O   . TYR A 186 ? 0.6761 0.5936 0.6238 0.0307  0.0703  -0.0090 202 TYR B O   
1510  C CB  . TYR A 186 ? 0.7261 0.6772 0.6609 0.0179  0.0630  -0.0106 202 TYR B CB  
1511  C CG  . TYR A 186 ? 0.7409 0.6751 0.6806 0.0154  0.0580  -0.0117 202 TYR B CG  
1512  C CD1 . TYR A 186 ? 0.7246 0.6498 0.6606 0.0230  0.0574  -0.0085 202 TYR B CD1 
1513  C CD2 . TYR A 186 ? 0.7345 0.6624 0.6815 0.0054  0.0530  -0.0157 202 TYR B CD2 
1514  C CE1 . TYR A 186 ? 0.8183 0.7285 0.7570 0.0205  0.0522  -0.0094 202 TYR B CE1 
1515  C CE2 . TYR A 186 ? 0.7988 0.7128 0.7501 0.0024  0.0481  -0.0161 202 TYR B CE2 
1516  C CZ  . TYR A 186 ? 0.8547 0.7599 0.8016 0.0099  0.0478  -0.0129 202 TYR B CZ  
1517  O OH  . TYR A 186 ? 0.9486 0.8392 0.8989 0.0067  0.0424  -0.0134 202 TYR B OH  
1518  N N   . TRP A 187 ? 0.6901 0.6327 0.6210 0.0394  0.0719  -0.0028 203 TRP B N   
1519  C CA  . TRP A 187 ? 0.6843 0.6130 0.6164 0.0479  0.0722  0.0006  203 TRP B CA  
1520  C C   . TRP A 187 ? 0.6655 0.5911 0.6048 0.0492  0.0762  0.0017  203 TRP B C   
1521  O O   . TRP A 187 ? 0.6121 0.5212 0.5580 0.0526  0.0751  0.0040  203 TRP B O   
1522  C CB  . TRP A 187 ? 0.7575 0.6958 0.6795 0.0575  0.0730  0.0054  203 TRP B CB  
1523  C CG  . TRP A 187 ? 0.7298 0.6648 0.6446 0.0609  0.0691  0.0058  203 TRP B CG  
1524  C CD1 . TRP A 187 ? 0.7771 0.6987 0.6939 0.0567  0.0644  0.0030  203 TRP B CD1 
1525  C CD2 . TRP A 187 ? 0.7182 0.6624 0.6223 0.0707  0.0697  0.0096  203 TRP B CD2 
1526  N NE1 . TRP A 187 ? 0.7864 0.7101 0.6933 0.0629  0.0621  0.0047  203 TRP B NE1 
1527  C CE2 . TRP A 187 ? 0.7680 0.7053 0.6669 0.0722  0.0655  0.0086  203 TRP B CE2 
1528  C CE3 . TRP A 187 ? 0.7323 0.6909 0.6308 0.0786  0.0734  0.0139  203 TRP B CE3 
1529  C CZ2 . TRP A 187 ? 0.8089 0.7533 0.6964 0.0821  0.0654  0.0115  203 TRP B CZ2 
1530  C CZ3 . TRP A 187 ? 0.7436 0.7089 0.6318 0.0882  0.0731  0.0168  203 TRP B CZ3 
1531  C CH2 . TRP A 187 ? 0.7911 0.7494 0.6736 0.0903  0.0693  0.0154  203 TRP B CH2 
1532  N N   . ARG A 188 ? 0.7022 0.6445 0.6400 0.0471  0.0808  0.0011  204 ARG B N   
1533  C CA  . ARG A 188 ? 0.6926 0.6345 0.6366 0.0488  0.0853  0.0027  204 ARG B CA  
1534  C C   . ARG A 188 ? 0.6406 0.5682 0.5954 0.0433  0.0848  -0.0012 204 ARG B C   
1535  O O   . ARG A 188 ? 0.6717 0.5926 0.6349 0.0458  0.0873  0.0017  204 ARG B O   
1536  C CB  . ARG A 188 ? 0.6511 0.6144 0.5892 0.0483  0.0902  0.0028  204 ARG B CB  
1537  C CG  . ARG A 188 ? 0.6521 0.6314 0.5811 0.0543  0.0916  0.0081  204 ARG B CG  
1538  C CD  . ARG A 188 ? 0.7708 0.7700 0.6950 0.0536  0.0964  0.0090  204 ARG B CD  
1539  N NE  . ARG A 188 ? 0.7447 0.7540 0.6636 0.0459  0.0951  0.0039  204 ARG B NE  
1540  C CZ  . ARG A 188 ? 0.7404 0.7615 0.6523 0.0439  0.0923  0.0049  204 ARG B CZ  
1541  N NH1 . ARG A 188 ? 0.7419 0.7670 0.6504 0.0498  0.0915  0.0102  204 ARG B NH1 
1542  N NH2 . ARG A 188 ? 0.7887 0.8173 0.6971 0.0360  0.0898  0.0009  204 ARG B NH2 
1543  N N   . GLY A 189 ? 0.6114 0.5345 0.5672 0.0360  0.0814  -0.0070 205 GLY B N   
1544  C CA  . GLY A 189 ? 0.6699 0.5784 0.6366 0.0310  0.0805  -0.0107 205 GLY B CA  
1545  C C   . GLY A 189 ? 0.6609 0.5519 0.6385 0.0344  0.0800  -0.0063 205 GLY B C   
1546  O O   . GLY A 189 ? 0.6276 0.5114 0.6157 0.0325  0.0820  -0.0071 205 GLY B O   
1547  N N   . ASP A 190 ? 0.6648 0.5489 0.6399 0.0399  0.0771  -0.0012 206 ASP B N   
1548  C CA  . ASP A 190 ? 0.6323 0.4980 0.6172 0.0429  0.0745  0.0040  206 ASP B CA  
1549  C C   . ASP A 190 ? 0.5981 0.4670 0.5931 0.0447  0.0799  0.0081  206 ASP B C   
1550  O O   . ASP A 190 ? 0.6615 0.5175 0.6692 0.0428  0.0790  0.0102  206 ASP B O   
1551  C CB  . ASP A 190 ? 0.6798 0.5415 0.6576 0.0504  0.0710  0.0090  206 ASP B CB  
1552  C CG  . ASP A 190 ? 0.6775 0.5165 0.6633 0.0525  0.0653  0.0135  206 ASP B CG  
1553  O OD1 . ASP A 190 ? 0.7046 0.5286 0.6912 0.0489  0.0598  0.0107  206 ASP B OD1 
1554  O OD2 . ASP A 190 ? 0.6840 0.5198 0.6758 0.0571  0.0656  0.0204  206 ASP B OD2 
1555  N N   . TYR A 191 ? 0.6544 0.5417 0.6441 0.0481  0.0856  0.0098  207 TYR B N   
1556  C CA  . TYR A 191 ? 0.6249 0.5179 0.6232 0.0511  0.0909  0.0153  207 TYR B CA  
1557  C C   . TYR A 191 ? 0.6368 0.5367 0.6390 0.0472  0.0964  0.0102  207 TYR B C   
1558  O O   . TYR A 191 ? 0.6635 0.5719 0.6709 0.0503  0.1022  0.0143  207 TYR B O   
1559  C CB  . TYR A 191 ? 0.5754 0.4853 0.5663 0.0570  0.0943  0.0203  207 TYR B CB  
1560  C CG  . TYR A 191 ? 0.6251 0.5278 0.6120 0.0623  0.0888  0.0253  207 TYR B CG  
1561  C CD1 . TYR A 191 ? 0.6194 0.5244 0.5939 0.0630  0.0858  0.0213  207 TYR B CD1 
1562  C CD2 . TYR A 191 ? 0.6325 0.5255 0.6281 0.0670  0.0860  0.0342  207 TYR B CD2 
1563  C CE1 . TYR A 191 ? 0.6493 0.5471 0.6190 0.0693  0.0809  0.0251  207 TYR B CE1 
1564  C CE2 . TYR A 191 ? 0.6441 0.5283 0.6351 0.0726  0.0799  0.0379  207 TYR B CE2 
1565  C CZ  . TYR A 191 ? 0.6527 0.5389 0.6300 0.0743  0.0776  0.0328  207 TYR B CZ  
1566  O OH  . TYR A 191 ? 0.6471 0.5238 0.6185 0.0813  0.0717  0.0358  207 TYR B OH  
1567  N N   . GLU A 192 ? 0.6078 0.5037 0.6076 0.0411  0.0944  0.0016  208 GLU B N   
1568  C CA  . GLU A 192 ? 0.6174 0.5193 0.6182 0.0380  0.0987  -0.0050 208 GLU B CA  
1569  C C   . GLU A 192 ? 0.6666 0.5585 0.6828 0.0384  0.1011  -0.0024 208 GLU B C   
1570  O O   . GLU A 192 ? 0.6966 0.5721 0.7233 0.0373  0.0966  0.0018  208 GLU B O   
1571  C CB  . GLU A 192 ? 0.6324 0.5309 0.6279 0.0308  0.0939  -0.0141 208 GLU B CB  
1572  C CG  . GLU A 192 ? 0.6923 0.5978 0.6840 0.0275  0.0963  -0.0227 208 GLU B CG  
1573  C CD  . GLU A 192 ? 0.7989 0.7026 0.7846 0.0199  0.0896  -0.0300 208 GLU B CD  
1574  O OE1 . GLU A 192 ? 0.8012 0.6983 0.7869 0.0171  0.0839  -0.0284 208 GLU B OE1 
1575  O OE2 . GLU A 192 ? 0.8575 0.7663 0.8383 0.0168  0.0896  -0.0373 208 GLU B OE2 
1576  N N   . VAL A 193 ? 0.7320 0.6340 0.7493 0.0403  0.1079  -0.0046 209 VAL B N   
1577  C CA  . VAL A 193 ? 0.7311 0.6267 0.7628 0.0411  0.1114  -0.0030 209 VAL B CA  
1578  C C   . VAL A 193 ? 0.8302 0.7350 0.8567 0.0417  0.1170  -0.0118 209 VAL B C   
1579  O O   . VAL A 193 ? 0.8524 0.7737 0.8717 0.0465  0.1235  -0.0111 209 VAL B O   
1580  C CB  . VAL A 193 ? 0.6791 0.5785 0.7218 0.0471  0.1155  0.0096  209 VAL B CB  
1581  C CG1 . VAL A 193 ? 0.7090 0.6064 0.7659 0.0487  0.1204  0.0119  209 VAL B CG1 
1582  C CG2 . VAL A 193 ? 0.6909 0.5770 0.7405 0.0469  0.1087  0.0183  209 VAL B CG2 
1583  N N   . ASN A 194 ? 0.9614 0.8556 0.9916 0.0372  0.1144  -0.0200 210 ASN B N   
1584  C CA  . ASN A 194 ? 0.9959 0.8952 1.0240 0.0394  0.1197  -0.0276 210 ASN B CA  
1585  C C   . ASN A 194 ? 1.0197 0.9114 1.0646 0.0419  0.1235  -0.0247 210 ASN B C   
1586  O O   . ASN A 194 ? 0.9883 0.8651 1.0473 0.0385  0.1192  -0.0206 210 ASN B O   
1587  C CB  . ASN A 194 ? 1.0952 0.9895 1.1145 0.0334  0.1143  -0.0405 210 ASN B CB  
1588  C CG  . ASN A 194 ? 1.1300 1.0366 1.1310 0.0322  0.1126  -0.0452 210 ASN B CG  
1589  O OD1 . ASN A 194 ? 0.9983 0.9187 0.9894 0.0372  0.1184  -0.0467 210 ASN B OD1 
1590  N ND2 . ASN A 194 ? 1.2773 1.1797 1.2736 0.0253  0.1046  -0.0476 210 ASN B ND2 
1591  N N   . GLY A 195 ? 1.0995 1.0016 1.1418 0.0480  0.1313  -0.0278 211 GLY B N   
1592  C CA  . GLY A 195 ? 1.1096 1.0055 1.1650 0.0506  0.1350  -0.0288 211 GLY B CA  
1593  C C   . GLY A 195 ? 1.0738 0.9736 1.1462 0.0559  0.1408  -0.0148 211 GLY B C   
1594  O O   . GLY A 195 ? 1.1626 1.0585 1.2480 0.0587  0.1446  -0.0136 211 GLY B O   
1595  N N   . VAL A 196 ? 0.9862 0.8937 1.0592 0.0576  0.1414  -0.0037 212 VAL B N   
1596  C CA  . VAL A 196 ? 1.0199 0.9319 1.1100 0.0621  0.1457  0.0114  212 VAL B CA  
1597  C C   . VAL A 196 ? 1.0298 0.9651 1.1134 0.0702  0.1551  0.0165  212 VAL B C   
1598  O O   . VAL A 196 ? 1.0051 0.9490 1.0849 0.0711  0.1545  0.0242  212 VAL B O   
1599  C CB  . VAL A 196 ? 0.9437 0.8442 1.0420 0.0576  0.1376  0.0217  212 VAL B CB  
1600  C CG1 . VAL A 196 ? 0.9550 0.8570 1.0732 0.0609  0.1399  0.0375  212 VAL B CG1 
1601  C CG2 . VAL A 196 ? 0.9588 0.8375 1.0600 0.0496  0.1283  0.0153  212 VAL B CG2 
1602  N N   . ASP A 197 ? 0.9992 0.9446 1.0816 0.0766  0.1637  0.0124  213 ASP B N   
1603  C CA  . ASP A 197 ? 1.0227 0.9911 1.0938 0.0845  0.1729  0.0137  213 ASP B CA  
1604  C C   . ASP A 197 ? 0.9945 0.9754 1.0734 0.0867  0.1745  0.0306  213 ASP B C   
1605  O O   . ASP A 197 ? 1.0092 0.9913 1.1078 0.0887  0.1763  0.0446  213 ASP B O   
1606  C CB  . ASP A 197 ? 1.0100 0.9877 1.0844 0.0930  0.1828  0.0116  213 ASP B CB  
1607  C CG  . ASP A 197 ? 1.0506 1.0221 1.1088 0.0934  0.1825  -0.0076 213 ASP B CG  
1608  O OD1 . ASP A 197 ? 1.0561 1.0328 1.0932 0.0926  0.1810  -0.0170 213 ASP B OD1 
1609  O OD2 . ASP A 197 ? 1.1047 1.0667 1.1713 0.0950  0.1836  -0.0126 213 ASP B OD2 
1610  N N   . GLY A 198 ? 1.0797 1.0694 1.1443 0.0858  0.1728  0.0303  214 GLY B N   
1611  C CA  . GLY A 198 ? 1.1233 1.1259 1.1937 0.0882  0.1739  0.0456  214 GLY B CA  
1612  C C   . GLY A 198 ? 1.0287 1.0173 1.1053 0.0823  0.1638  0.0521  214 GLY B C   
1613  O O   . GLY A 198 ? 1.0027 0.9993 1.0845 0.0838  0.1628  0.0647  214 GLY B O   
1614  N N   . TYR A 199 ? 0.8728 0.8407 0.9490 0.0760  0.1559  0.0440  215 TYR B N   
1615  C CA  . TYR A 199 ? 0.8006 0.7534 0.8794 0.0710  0.1459  0.0478  215 TYR B CA  
1616  C C   . TYR A 199 ? 0.8065 0.7513 0.8683 0.0660  0.1404  0.0340  215 TYR B C   
1617  O O   . TYR A 199 ? 0.7588 0.6904 0.8203 0.0622  0.1322  0.0350  215 TYR B O   
1618  C CB  . TYR A 199 ? 0.8117 0.7455 0.9102 0.0680  0.1406  0.0544  215 TYR B CB  
1619  C CG  . TYR A 199 ? 0.8538 0.7943 0.9719 0.0719  0.1436  0.0716  215 TYR B CG  
1620  C CD1 . TYR A 199 ? 0.8514 0.7927 0.9761 0.0726  0.1387  0.0851  215 TYR B CD1 
1621  C CD2 . TYR A 199 ? 0.8801 0.8263 1.0109 0.0750  0.1506  0.0750  215 TYR B CD2 
1622  C CE1 . TYR A 199 ? 0.8121 0.7598 0.9560 0.0754  0.1401  0.1023  215 TYR B CE1 
1623  C CE2 . TYR A 199 ? 0.9001 0.8543 1.0501 0.0784  0.1531  0.0924  215 TYR B CE2 
1624  C CZ  . TYR A 199 ? 0.8439 0.7990 1.0008 0.0781  0.1475  0.1063  215 TYR B CZ  
1625  O OH  . TYR A 199 ? 0.8853 0.8493 1.0627 0.0808  0.1490  0.1251  215 TYR B OH  
1626  N N   . ASP A 200 ? 0.8260 0.7781 0.8738 0.0660  0.1443  0.0215  216 ASP B N   
1627  C CA  . ASP A 200 ? 0.7416 0.6900 0.7731 0.0612  0.1393  0.0094  216 ASP B CA  
1628  C C   . ASP A 200 ? 0.7013 0.6586 0.7218 0.0614  0.1369  0.0128  216 ASP B C   
1629  O O   . ASP A 200 ? 0.6705 0.6416 0.6911 0.0660  0.1409  0.0216  216 ASP B O   
1630  C CB  . ASP A 200 ? 0.8258 0.7824 0.8446 0.0622  0.1439  -0.0027 216 ASP B CB  
1631  C CG  . ASP A 200 ? 0.9252 0.8711 0.9526 0.0618  0.1452  -0.0090 216 ASP B CG  
1632  O OD1 . ASP A 200 ? 0.9607 0.8893 0.9994 0.0570  0.1394  -0.0086 216 ASP B OD1 
1633  O OD2 . ASP A 200 ? 0.8741 0.8286 0.8966 0.0667  0.1519  -0.0144 216 ASP B OD2 
1634  N N   . TYR A 201 ? 0.6965 0.6466 0.7077 0.0564  0.1302  0.0061  217 TYR B N   
1635  C CA  . TYR A 201 ? 0.7168 0.6741 0.7174 0.0565  0.1271  0.0083  217 TYR B CA  
1636  C C   . TYR A 201 ? 0.7189 0.6720 0.7079 0.0506  0.1215  -0.0017 217 TYR B C   
1637  O O   . TYR A 201 ? 0.7121 0.6496 0.7060 0.0461  0.1159  -0.0052 217 TYR B O   
1638  C CB  . TYR A 201 ? 0.7263 0.6745 0.7363 0.0581  0.1227  0.0188  217 TYR B CB  
1639  C CG  . TYR A 201 ? 0.7038 0.6613 0.7061 0.0612  0.1211  0.0245  217 TYR B CG  
1640  C CD1 . TYR A 201 ? 0.6742 0.6284 0.6665 0.0591  0.1156  0.0207  217 TYR B CD1 
1641  C CD2 . TYR A 201 ? 0.7353 0.7043 0.7418 0.0663  0.1247  0.0348  217 TYR B CD2 
1642  C CE1 . TYR A 201 ? 0.6613 0.6233 0.6474 0.0628  0.1142  0.0260  217 TYR B CE1 
1643  C CE2 . TYR A 201 ? 0.7404 0.7166 0.7411 0.0692  0.1226  0.0402  217 TYR B CE2 
1644  C CZ  . TYR A 201 ? 0.6981 0.6703 0.6885 0.0677  0.1175  0.0355  217 TYR B CZ  
1645  O OH  . TYR A 201 ? 0.7577 0.7370 0.7427 0.0715  0.1156  0.0408  217 TYR B OH  
1646  N N   . SER A 202 ? 0.6948 0.6623 0.6692 0.0503  0.1225  -0.0055 218 SER B N   
1647  C CA  . SER A 202 ? 0.7192 0.6859 0.6831 0.0445  0.1168  -0.0134 218 SER B CA  
1648  C C   . SER A 202 ? 0.7071 0.6784 0.6656 0.0451  0.1132  -0.0082 218 SER B C   
1649  O O   . SER A 202 ? 0.7384 0.7145 0.6991 0.0502  0.1152  0.0003  218 SER B O   
1650  C CB  . SER A 202 ? 0.7536 0.7327 0.7046 0.0432  0.1190  -0.0210 218 SER B CB  
1651  O OG  . SER A 202 ? 0.8004 0.7964 0.7426 0.0466  0.1220  -0.0158 218 SER B OG  
1652  N N   . ARG A 203 ? 0.7279 0.6986 0.6793 0.0400  0.1077  -0.0130 219 ARG B N   
1653  C CA  . ARG A 203 ? 0.7456 0.7173 0.6939 0.0411  0.1039  -0.0082 219 ARG B CA  
1654  C C   . ARG A 203 ? 0.8047 0.7950 0.7437 0.0451  0.1068  -0.0033 219 ARG B C   
1655  O O   . ARG A 203 ? 0.7940 0.7859 0.7334 0.0499  0.1063  0.0036  219 ARG B O   
1656  C CB  . ARG A 203 ? 0.7530 0.7206 0.6976 0.0345  0.0974  -0.0136 219 ARG B CB  
1657  C CG  . ARG A 203 ? 0.7033 0.6524 0.6579 0.0302  0.0943  -0.0182 219 ARG B CG  
1658  C CD  . ARG A 203 ? 0.7388 0.6816 0.6926 0.0239  0.0871  -0.0215 219 ARG B CD  
1659  N NE  . ARG A 203 ? 0.7585 0.7119 0.7042 0.0178  0.0838  -0.0264 219 ARG B NE  
1660  C CZ  . ARG A 203 ? 0.7308 0.6792 0.6781 0.0114  0.0807  -0.0337 219 ARG B CZ  
1661  N NH1 . ARG A 203 ? 0.8108 0.7458 0.7672 0.0111  0.0821  -0.0376 219 ARG B NH1 
1662  N NH2 . ARG A 203 ? 0.7298 0.6871 0.6700 0.0054  0.0757  -0.0368 219 ARG B NH2 
1663  N N   . GLY A 204 ? 0.9030 0.9069 0.8335 0.0432  0.1092  -0.0069 220 GLY B N   
1664  C CA  . GLY A 204 ? 0.9045 0.9268 0.8263 0.0461  0.1119  -0.0022 220 GLY B CA  
1665  C C   . GLY A 204 ? 0.9259 0.9530 0.8527 0.0527  0.1176  0.0052  220 GLY B C   
1666  O O   . GLY A 204 ? 1.0334 1.0735 0.9561 0.0563  0.1191  0.0116  220 GLY B O   
1667  N N   . GLN A 205 ? 0.7878 0.8055 0.7244 0.0543  0.1205  0.0052  221 GLN B N   
1668  C CA  . GLN A 205 ? 0.7726 0.7939 0.7170 0.0603  0.1251  0.0141  221 GLN B CA  
1669  C C   . GLN A 205 ? 0.7644 0.7791 0.7146 0.0639  0.1213  0.0222  221 GLN B C   
1670  O O   . GLN A 205 ? 0.7809 0.8025 0.7349 0.0688  0.1233  0.0310  221 GLN B O   
1671  C CB  . GLN A 205 ? 0.7692 0.7819 0.7242 0.0609  0.1286  0.0131  221 GLN B CB  
1672  C CG  . GLN A 205 ? 0.7797 0.7995 0.7441 0.0667  0.1340  0.0233  221 GLN B CG  
1673  C CD  . GLN A 205 ? 1.0337 1.0757 0.9891 0.0696  0.1399  0.0262  221 GLN B CD  
1674  O OE1 . GLN A 205 ? 1.1224 1.1732 1.0660 0.0679  0.1425  0.0185  221 GLN B OE1 
1675  N NE2 . GLN A 205 ? 1.0270 1.0774 0.9874 0.0737  0.1408  0.0375  221 GLN B NE2 
1676  N N   . LEU A 206 ? 0.7249 0.7273 0.6745 0.0619  0.1154  0.0193  222 LEU B N   
1677  C CA  . LEU A 206 ? 0.7525 0.7484 0.7045 0.0666  0.1114  0.0258  222 LEU B CA  
1678  C C   . LEU A 206 ? 0.7905 0.8030 0.7331 0.0699  0.1119  0.0296  222 LEU B C   
1679  O O   . LEU A 206 ? 0.7956 0.8090 0.7414 0.0757  0.1113  0.0375  222 LEU B O   
1680  C CB  . LEU A 206 ? 0.7452 0.7241 0.6978 0.0644  0.1052  0.0217  222 LEU B CB  
1681  C CG  . LEU A 206 ? 0.7137 0.6837 0.6661 0.0703  0.1003  0.0271  222 LEU B CG  
1682  C CD1 . LEU A 206 ? 0.7258 0.6811 0.6903 0.0736  0.0984  0.0334  222 LEU B CD1 
1683  C CD2 . LEU A 206 ? 0.6946 0.6535 0.6429 0.0680  0.0951  0.0218  222 LEU B CD2 
1684  N N   . ILE A 207 ? 0.8038 0.8293 0.7356 0.0662  0.1125  0.0249  223 ILE B N   
1685  C CA  . ILE A 207 ? 0.7857 0.8281 0.7097 0.0693  0.1131  0.0297  223 ILE B CA  
1686  C C   . ILE A 207 ? 0.8212 0.8766 0.7467 0.0722  0.1181  0.0357  223 ILE B C   
1687  O O   . ILE A 207 ? 0.7994 0.8612 0.7259 0.0776  0.1181  0.0435  223 ILE B O   
1688  C CB  . ILE A 207 ? 0.7159 0.7704 0.6290 0.0641  0.1119  0.0249  223 ILE B CB  
1689  C CG1 . ILE A 207 ? 0.7701 0.8153 0.6821 0.0624  0.1067  0.0217  223 ILE B CG1 
1690  C CG2 . ILE A 207 ? 0.6589 0.7314 0.5656 0.0675  0.1129  0.0311  223 ILE B CG2 
1691  C CD1 . ILE A 207 ? 0.7714 0.8293 0.6746 0.0564  0.1044  0.0187  223 ILE B CD1 
1692  N N   . GLU A 208 ? 0.7941 0.8536 0.7198 0.0691  0.1223  0.0325  224 GLU B N   
1693  C CA  . GLU A 208 ? 0.8353 0.9081 0.7626 0.0723  0.1273  0.0391  224 GLU B CA  
1694  C C   . GLU A 208 ? 0.8575 0.9236 0.7970 0.0781  0.1264  0.0488  224 GLU B C   
1695  O O   . GLU A 208 ? 0.9069 0.9828 0.8464 0.0820  0.1262  0.0566  224 GLU B O   
1696  C CB  . GLU A 208 ? 0.9389 1.0162 0.8649 0.0700  0.1324  0.0345  224 GLU B CB  
1697  C CG  . GLU A 208 ? 1.0643 1.1526 0.9759 0.0653  0.1327  0.0270  224 GLU B CG  
1698  C CD  . GLU A 208 ? 1.1109 1.1949 1.0194 0.0623  0.1349  0.0179  224 GLU B CD  
1699  O OE1 . GLU A 208 ? 1.0954 1.1746 1.0124 0.0651  0.1389  0.0192  224 GLU B OE1 
1700  O OE2 . GLU A 208 ? 1.1489 1.2345 1.0468 0.0573  0.1321  0.0099  224 GLU B OE2 
1701  N N   . ASP A 209 ? 0.8406 0.8892 0.7910 0.0784  0.1247  0.0490  225 ASP B N   
1702  C CA  . ASP A 209 ? 0.8308 0.8728 0.7939 0.0831  0.1229  0.0593  225 ASP B CA  
1703  C C   . ASP A 209 ? 0.8221 0.8580 0.7843 0.0876  0.1168  0.0637  225 ASP B C   
1704  O O   . ASP A 209 ? 0.8082 0.8468 0.7768 0.0921  0.1152  0.0734  225 ASP B O   
1705  C CB  . ASP A 209 ? 0.8161 0.8400 0.7916 0.0820  0.1214  0.0594  225 ASP B CB  
1706  C CG  . ASP A 209 ? 0.9110 0.9417 0.8899 0.0798  0.1281  0.0573  225 ASP B CG  
1707  O OD1 . ASP A 209 ? 0.9557 1.0056 0.9296 0.0807  0.1341  0.0589  225 ASP B OD1 
1708  O OD2 . ASP A 209 ? 0.8838 0.9006 0.8702 0.0777  0.1274  0.0541  225 ASP B OD2 
1709  N N   . VAL A 210 ? 0.7927 0.8206 0.7473 0.0869  0.1129  0.0572  226 VAL B N   
1710  C CA  . VAL A 210 ? 0.7706 0.7932 0.7227 0.0928  0.1076  0.0608  226 VAL B CA  
1711  C C   . VAL A 210 ? 0.8326 0.8754 0.7800 0.0960  0.1100  0.0667  226 VAL B C   
1712  O O   . VAL A 210 ? 0.8712 0.9126 0.8236 0.1017  0.1071  0.0748  226 VAL B O   
1713  C CB  . VAL A 210 ? 0.7254 0.7403 0.6687 0.0919  0.1043  0.0531  226 VAL B CB  
1714  C CG1 . VAL A 210 ? 0.7328 0.7501 0.6699 0.0988  0.1010  0.0563  226 VAL B CG1 
1715  C CG2 . VAL A 210 ? 0.7022 0.6935 0.6513 0.0902  0.0998  0.0494  226 VAL B CG2 
1716  N N   . GLU A 211 ? 0.8544 0.9159 0.7930 0.0919  0.1149  0.0632  227 GLU B N   
1717  C CA  . GLU A 211 ? 0.8380 0.9198 0.7715 0.0941  0.1171  0.0688  227 GLU B CA  
1718  C C   . GLU A 211 ? 0.8590 0.9492 0.8009 0.0958  0.1197  0.0777  227 GLU B C   
1719  O O   . GLU A 211 ? 0.8340 0.9321 0.7780 0.1003  0.1184  0.0859  227 GLU B O   
1720  C CB  . GLU A 211 ? 0.8220 0.9196 0.7441 0.0882  0.1205  0.0628  227 GLU B CB  
1721  C CG  . GLU A 211 ? 0.8042 0.9003 0.7182 0.0874  0.1172  0.0577  227 GLU B CG  
1722  C CD  . GLU A 211 ? 0.8887 0.9983 0.7926 0.0801  0.1186  0.0520  227 GLU B CD  
1723  O OE1 . GLU A 211 ? 0.7947 0.9114 0.6959 0.0753  0.1217  0.0493  227 GLU B OE1 
1724  O OE2 . GLU A 211 ? 0.9086 1.0214 0.8069 0.0796  0.1159  0.0506  227 GLU B OE2 
1725  N N   . HIS A 212 ? 0.9718 1.0600 0.9195 0.0928  0.1231  0.0770  228 HIS B N   
1726  C CA  A HIS A 212 ? 1.3060 1.4046 1.2621 0.0941  0.1263  0.0863  228 HIS B CA  
1727  C CA  B HIS A 212 ? 1.2789 1.3777 1.2350 0.0942  0.1263  0.0863  228 HIS B CA  
1728  C C   . HIS A 212 ? 0.9963 1.0841 0.9654 0.0994  0.1206  0.0965  228 HIS B C   
1729  O O   . HIS A 212 ? 0.9611 1.0600 0.9349 0.1023  0.1202  0.1064  228 HIS B O   
1730  C CB  A HIS A 212 ? 1.0464 1.1429 1.0066 0.0908  0.1310  0.0828  228 HIS B CB  
1731  C CB  B HIS A 212 ? 1.2504 1.3489 1.2099 0.0908  0.1314  0.0830  228 HIS B CB  
1732  C CG  A HIS A 212 ? 1.1220 1.2270 1.0695 0.0862  0.1354  0.0727  228 HIS B CG  
1733  C CG  B HIS A 212 ? 1.0243 1.1360 0.9923 0.0924  0.1357  0.0930  228 HIS B CG  
1734  N ND1 A HIS A 212 ? 1.1345 1.2350 1.0826 0.0834  0.1389  0.0662  228 HIS B ND1 
1735  N ND1 B HIS A 212 ? 1.0999 1.2323 1.0601 0.0911  0.1424  0.0929  228 HIS B ND1 
1736  C CD2 A HIS A 212 ? 1.1365 1.2514 1.0705 0.0837  0.1353  0.0673  228 HIS B CD2 
1737  C CD2 B HIS A 212 ? 0.9780 1.0857 0.9614 0.0953  0.1339  0.1041  228 HIS B CD2 
1738  C CE1 A HIS A 212 ? 1.1770 1.2842 1.1115 0.0795  0.1406  0.0569  228 HIS B CE1 
1739  C CE1 B HIS A 212 ? 1.0569 1.1989 1.0275 0.0934  0.1453  0.1035  228 HIS B CE1 
1740  N NE2 A HIS A 212 ? 1.1808 1.2967 1.1071 0.0792  0.1381  0.0578  228 HIS B NE2 
1741  N NE2 B HIS A 212 ? 1.0449 1.1726 1.0305 0.0956  0.1401  0.1111  228 HIS B NE2 
1742  N N   . THR A 213 ? 1.0271 1.0921 1.0022 0.1004  0.1152  0.0944  229 THR B N   
1743  C CA  . THR A 213 ? 0.9393 0.9903 0.9257 0.1052  0.1077  0.1035  229 THR B CA  
1744  C C   . THR A 213 ? 0.8765 0.9277 0.8569 0.1109  0.1028  0.1054  229 THR B C   
1745  O O   . THR A 213 ? 0.8334 0.8833 0.8217 0.1154  0.0979  0.1152  229 THR B O   
1746  C CB  . THR A 213 ? 0.8010 0.8264 0.7942 0.1044  0.1026  0.1004  229 THR B CB  
1747  O OG1 . THR A 213 ? 0.6629 0.6780 0.6451 0.1034  0.1012  0.0891  229 THR B OG1 
1748  C CG2 . THR A 213 ? 0.8373 0.8640 0.8396 0.1001  0.1073  0.1015  229 THR B CG2 
1749  N N   . PHE A 214 ? 0.7734 0.8278 0.7405 0.1110  0.1039  0.0970  230 PHE B N   
1750  C CA  . PHE A 214 ? 0.7384 0.7948 0.7002 0.1175  0.1000  0.0995  230 PHE B CA  
1751  C C   . PHE A 214 ? 0.7638 0.8429 0.7265 0.1183  0.1031  0.1077  230 PHE B C   
1752  O O   . PHE A 214 ? 0.7594 0.8385 0.7243 0.1245  0.0986  0.1141  230 PHE B O   
1753  C CB  . PHE A 214 ? 0.7343 0.7915 0.6826 0.1175  0.1009  0.0901  230 PHE B CB  
1754  C CG  . PHE A 214 ? 0.7692 0.8282 0.7118 0.1253  0.0974  0.0922  230 PHE B CG  
1755  C CD1 . PHE A 214 ? 0.7699 0.8089 0.7151 0.1332  0.0897  0.0942  230 PHE B CD1 
1756  C CD2 . PHE A 214 ? 0.7564 0.8370 0.6910 0.1252  0.1015  0.0928  230 PHE B CD2 
1757  C CE1 . PHE A 214 ? 0.7641 0.8049 0.7031 0.1419  0.0867  0.0958  230 PHE B CE1 
1758  C CE2 . PHE A 214 ? 0.7626 0.8463 0.6926 0.1332  0.0988  0.0954  230 PHE B CE2 
1759  C CZ  . PHE A 214 ? 0.7444 0.8084 0.6764 0.1421  0.0917  0.0966  230 PHE B CZ  
1760  N N   . GLU A 215 ? 0.7900 0.8878 0.7508 0.1124  0.1104  0.1075  231 GLU B N   
1761  C CA  . GLU A 215 ? 0.7503 0.8703 0.7117 0.1127  0.1133  0.1157  231 GLU B CA  
1762  C C   . GLU A 215 ? 0.7371 0.8543 0.7130 0.1163  0.1090  0.1281  231 GLU B C   
1763  O O   . GLU A 215 ? 0.7835 0.9107 0.7614 0.1198  0.1068  0.1359  231 GLU B O   
1764  C CB  . GLU A 215 ? 0.8243 0.9629 0.7801 0.1061  0.1214  0.1131  231 GLU B CB  
1765  C CG  . GLU A 215 ? 0.8563 1.0054 0.7972 0.1027  0.1243  0.1047  231 GLU B CG  
1766  C CD  . GLU A 215 ? 0.9094 1.0740 0.8460 0.1054  0.1234  0.1103  231 GLU B CD  
1767  O OE1 . GLU A 215 ? 0.8808 1.0578 0.8229 0.1068  0.1239  0.1199  231 GLU B OE1 
1768  O OE2 . GLU A 215 ? 1.0693 1.2340 0.9979 0.1064  0.1218  0.1060  231 GLU B OE2 
1769  N N   . GLU A 216 ? 0.7262 0.8303 0.7134 0.1152  0.1072  0.1309  232 GLU B N   
1770  C CA  . GLU A 216 ? 0.7203 0.8218 0.7232 0.1176  0.1021  0.1442  232 GLU B CA  
1771  C C   . GLU A 216 ? 0.6910 0.7701 0.6985 0.1241  0.0910  0.1468  232 GLU B C   
1772  O O   . GLU A 216 ? 0.6731 0.7502 0.6925 0.1271  0.0845  0.1585  232 GLU B O   
1773  C CB  . GLU A 216 ? 0.7472 0.8451 0.7614 0.1139  0.1043  0.1476  232 GLU B CB  
1774  C CG  . GLU A 216 ? 0.8014 0.9153 0.8083 0.1087  0.1149  0.1412  232 GLU B CG  
1775  C CD  . GLU A 216 ? 0.9121 1.0240 0.9310 0.1063  0.1177  0.1455  232 GLU B CD  
1776  O OE1 . GLU A 216 ? 0.9490 1.0673 0.9824 0.1073  0.1161  0.1592  232 GLU B OE1 
1777  O OE2 . GLU A 216 ? 0.9378 1.0417 0.9524 0.1035  0.1213  0.1356  232 GLU B OE2 
1778  N N   . ILE A 217 ? 0.7219 0.7836 0.7198 0.1265  0.0882  0.1362  233 ILE B N   
1779  C CA  . ILE A 217 ? 0.7004 0.7414 0.6985 0.1341  0.0779  0.1369  233 ILE B CA  
1780  C C   . ILE A 217 ? 0.7286 0.7820 0.7204 0.1399  0.0771  0.1394  233 ILE B C   
1781  O O   . ILE A 217 ? 0.7233 0.7663 0.7201 0.1467  0.0684  0.1455  233 ILE B O   
1782  C CB  . ILE A 217 ? 0.7307 0.7516 0.7193 0.1352  0.0760  0.1250  233 ILE B CB  
1783  C CG1 . ILE A 217 ? 0.7685 0.7677 0.7669 0.1325  0.0712  0.1258  233 ILE B CG1 
1784  C CG2 . ILE A 217 ? 0.6662 0.6712 0.6486 0.1447  0.0676  0.1233  233 ILE B CG2 
1785  C CD1 . ILE A 217 ? 0.7853 0.7725 0.7747 0.1300  0.0731  0.1135  233 ILE B CD1 
1786  N N   . LYS A 218 ? 0.7727 0.8476 0.7536 0.1374  0.0855  0.1347  234 LYS B N   
1787  C CA  . LYS A 218 ? 0.7225 0.8112 0.6965 0.1425  0.0858  0.1363  234 LYS B CA  
1788  C C   . LYS A 218 ? 0.7107 0.8020 0.6948 0.1475  0.0797  0.1483  234 LYS B C   
1789  O O   . LYS A 218 ? 0.7394 0.8243 0.7201 0.1558  0.0743  0.1485  234 LYS B O   
1790  C CB  . LYS A 218 ? 0.6467 0.7624 0.6121 0.1366  0.0953  0.1341  234 LYS B CB  
1791  C CG  . LYS A 218 ? 0.7201 0.8353 0.6723 0.1350  0.0989  0.1227  234 LYS B CG  
1792  C CD  . LYS A 218 ? 0.7993 0.9399 0.7434 0.1288  0.1064  0.1214  234 LYS B CD  
1793  C CE  . LYS A 218 ? 0.8559 0.9966 0.7888 0.1246  0.1097  0.1108  234 LYS B CE  
1794  N NZ  . LYS A 218 ? 0.8556 1.0194 0.7805 0.1179  0.1153  0.1099  234 LYS B NZ  
1795  N N   . PRO A 219 ? 0.6913 0.7924 0.6880 0.1432  0.0799  0.1588  235 PRO B N   
1796  C CA  . PRO A 219 ? 0.6996 0.8016 0.7076 0.1478  0.0724  0.1711  235 PRO B CA  
1797  C C   . PRO A 219 ? 0.7565 0.8298 0.7687 0.1562  0.0599  0.1718  235 PRO B C   
1798  O O   . PRO A 219 ? 0.7816 0.8518 0.7914 0.1642  0.0543  0.1735  235 PRO B O   
1799  C CB  . PRO A 219 ? 0.6153 0.7288 0.6371 0.1410  0.0745  0.1816  235 PRO B CB  
1800  C CG  . PRO A 219 ? 0.5999 0.7281 0.6130 0.1338  0.0859  0.1742  235 PRO B CG  
1801  C CD  . PRO A 219 ? 0.6659 0.7777 0.6677 0.1347  0.0867  0.1606  235 PRO B CD  
1802  N N   . LEU A 220 ? 0.7705 0.8218 0.7885 0.1547  0.0549  0.1705  236 LEU B N   
1803  C CA  . LEU A 220 ? 0.7818 0.8028 0.8018 0.1626  0.0418  0.1703  236 LEU B CA  
1804  C C   . LEU A 220 ? 0.7795 0.7921 0.7828 0.1715  0.0411  0.1593  236 LEU B C   
1805  O O   . LEU A 220 ? 0.7942 0.7954 0.7964 0.1810  0.0323  0.1613  236 LEU B O   
1806  C CB  . LEU A 220 ? 0.7695 0.7680 0.7952 0.1589  0.0376  0.1683  236 LEU B CB  
1807  C CG  . LEU A 220 ? 0.7472 0.7115 0.7737 0.1667  0.0227  0.1677  236 LEU B CG  
1808  C CD1 . LEU A 220 ? 0.8131 0.7740 0.8504 0.1721  0.0116  0.1797  236 LEU B CD1 
1809  C CD2 . LEU A 220 ? 0.6911 0.6330 0.7247 0.1624  0.0174  0.1675  236 LEU B CD2 
1810  N N   . TYR A 221 ? 0.7274 0.7462 0.7176 0.1690  0.0501  0.1482  237 TYR B N   
1811  C CA  . TYR A 221 ? 0.7413 0.7535 0.7161 0.1776  0.0498  0.1387  237 TYR B CA  
1812  C C   . TYR A 221 ? 0.7783 0.8071 0.7500 0.1843  0.0506  0.1428  237 TYR B C   
1813  O O   . TYR A 221 ? 0.7993 0.8159 0.7644 0.1955  0.0445  0.1403  237 TYR B O   
1814  C CB  . TYR A 221 ? 0.7168 0.7375 0.6801 0.1723  0.0594  0.1282  237 TYR B CB  
1815  C CG  . TYR A 221 ? 0.7082 0.7248 0.6565 0.1811  0.0594  0.1200  237 TYR B CG  
1816  C CD1 . TYR A 221 ? 0.7456 0.7346 0.6886 0.1899  0.0508  0.1151  237 TYR B CD1 
1817  C CD2 . TYR A 221 ? 0.7088 0.7497 0.6484 0.1810  0.0677  0.1180  237 TYR B CD2 
1818  C CE1 . TYR A 221 ? 0.7841 0.7708 0.7127 0.1991  0.0513  0.1080  237 TYR B CE1 
1819  C CE2 . TYR A 221 ? 0.7228 0.7626 0.6498 0.1895  0.0682  0.1120  237 TYR B CE2 
1820  C CZ  . TYR A 221 ? 0.7734 0.7867 0.6948 0.1989  0.0605  0.1069  237 TYR B CZ  
1821  O OH  . TYR A 221 ? 0.8130 0.8261 0.7210 0.2085  0.0614  0.1011  237 TYR B OH  
1822  N N   . GLU A 222 ? 0.7529 0.8099 0.7284 0.1779  0.0582  0.1487  238 GLU B N   
1823  C CA  . GLU A 222 ? 0.7372 0.8131 0.7102 0.1828  0.0600  0.1531  238 GLU B CA  
1824  C C   . GLU A 222 ? 0.7814 0.8451 0.7634 0.1913  0.0488  0.1613  238 GLU B C   
1825  O O   . GLU A 222 ? 0.8564 0.9224 0.8336 0.2009  0.0465  0.1617  238 GLU B O   
1826  C CB  . GLU A 222 ? 0.7223 0.8284 0.6991 0.1730  0.0688  0.1590  238 GLU B CB  
1827  C CG  . GLU A 222 ? 0.7812 0.9018 0.7466 0.1663  0.0790  0.1506  238 GLU B CG  
1828  C CD  . GLU A 222 ? 0.8577 1.0073 0.8239 0.1578  0.0868  0.1558  238 GLU B CD  
1829  O OE1 . GLU A 222 ? 0.8906 1.0542 0.8621 0.1597  0.0855  0.1649  238 GLU B OE1 
1830  O OE2 . GLU A 222 ? 0.8522 1.0098 0.8133 0.1492  0.0936  0.1505  238 GLU B OE2 
1831  N N   . HIS A 223 ? 0.7609 0.8106 0.7561 0.1884  0.0412  0.1681  239 HIS B N   
1832  C CA  . HIS A 223 ? 0.8277 0.8636 0.8323 0.1962  0.0286  0.1764  239 HIS B CA  
1833  C C   . HIS A 223 ? 0.9086 0.9123 0.9048 0.2080  0.0184  0.1686  239 HIS B C   
1834  O O   . HIS A 223 ? 0.9676 0.9633 0.9622 0.2190  0.0107  0.1701  239 HIS B O   
1835  C CB  . HIS A 223 ? 0.8211 0.8556 0.8441 0.1887  0.0232  0.1884  239 HIS B CB  
1836  C CG  . HIS A 223 ? 0.8243 0.8897 0.8565 0.1818  0.0293  0.1994  239 HIS B CG  
1837  N ND1 . HIS A 223 ? 0.8557 0.9295 0.8951 0.1863  0.0238  0.2089  239 HIS B ND1 
1838  C CD2 . HIS A 223 ? 0.8001 0.8904 0.8337 0.1714  0.0406  0.2016  239 HIS B CD2 
1839  C CE1 . HIS A 223 ? 0.8579 0.9609 0.9037 0.1782  0.0313  0.2174  239 HIS B CE1 
1840  N NE2 . HIS A 223 ? 0.7522 0.8655 0.7938 0.1695  0.0416  0.2128  239 HIS B NE2 
1841  N N   . LEU A 224 ? 0.8830 0.8676 0.8735 0.2062  0.0178  0.1602  240 LEU B N   
1842  C CA  . LEU A 224 ? 0.8895 0.8441 0.8687 0.2175  0.0090  0.1514  240 LEU B CA  
1843  C C   . LEU A 224 ? 0.9281 0.8924 0.8917 0.2281  0.0142  0.1442  240 LEU B C   
1844  O O   . LEU A 224 ? 0.9410 0.8884 0.8982 0.2414  0.0056  0.1419  240 LEU B O   
1845  C CB  . LEU A 224 ? 0.8235 0.7619 0.7973 0.2125  0.0104  0.1428  240 LEU B CB  
1846  C CG  . LEU A 224 ? 0.7920 0.6985 0.7531 0.2230  0.0015  0.1331  240 LEU B CG  
1847  C CD1 . LEU A 224 ? 0.7995 0.6752 0.7693 0.2279  -0.0159 0.1390  240 LEU B CD1 
1848  C CD2 . LEU A 224 ? 0.7776 0.6785 0.7317 0.2164  0.0073  0.1241  240 LEU B CD2 
1849  N N   . HIS A 225 ? 0.8597 0.8520 0.8175 0.2223  0.0279  0.1414  241 HIS B N   
1850  C CA  . HIS A 225 ? 0.9232 0.9299 0.8675 0.2304  0.0344  0.1362  241 HIS B CA  
1851  C C   . HIS A 225 ? 0.9390 0.9556 0.8876 0.2388  0.0310  0.1439  241 HIS B C   
1852  O O   . HIS A 225 ? 0.9207 0.9299 0.8599 0.2527  0.0277  0.1402  241 HIS B O   
1853  C CB  . HIS A 225 ? 0.8921 0.9272 0.8327 0.2195  0.0483  0.1341  241 HIS B CB  
1854  C CG  . HIS A 225 ? 0.8503 0.9031 0.7784 0.2256  0.0556  0.1299  241 HIS B CG  
1855  N ND1 . HIS A 225 ? 0.7743 0.8469 0.7033 0.2310  0.0578  0.1360  241 HIS B ND1 
1856  C CD2 . HIS A 225 ? 0.8144 0.8697 0.7299 0.2267  0.0614  0.1214  241 HIS B CD2 
1857  C CE1 . HIS A 225 ? 0.8132 0.8997 0.7308 0.2356  0.0645  0.1317  241 HIS B CE1 
1858  N NE2 . HIS A 225 ? 0.7431 0.8198 0.6523 0.2330  0.0667  0.1230  241 HIS B NE2 
1859  N N   . ALA A 226 ? 1.1296 1.1632 1.0923 0.2308  0.0317  0.1548  242 ALA B N   
1860  C CA  . ALA A 226 ? 1.1443 1.1885 1.1130 0.2374  0.0282  0.1633  242 ALA B CA  
1861  C C   . ALA A 226 ? 1.1856 1.1997 1.1554 0.2508  0.0133  0.1635  242 ALA B C   
1862  O O   . ALA A 226 ? 1.1787 1.1930 1.1437 0.2635  0.0105  0.1632  242 ALA B O   
1863  C CB  . ALA A 226 ? 1.0585 1.1229 1.0431 0.2256  0.0300  0.1755  242 ALA B CB  
1864  N N   . TYR A 227 ? 0.9558 0.9430 0.9316 0.2485  0.0033  0.1636  243 TYR B N   
1865  C CA  . TYR A 227 ? 0.9634 0.9192 0.9409 0.2600  -0.0130 0.1644  243 TYR B CA  
1866  C C   . TYR A 227 ? 0.9537 0.8887 0.9118 0.2748  -0.0155 0.1514  243 TYR B C   
1867  O O   . TYR A 227 ? 0.9543 0.8743 0.9074 0.2896  -0.0246 0.1501  243 TYR B O   
1868  C CB  . TYR A 227 ? 0.9675 0.9017 0.9577 0.2522  -0.0234 0.1696  243 TYR B CB  
1869  C CG  . TYR A 227 ? 1.0218 0.9183 1.0121 0.2631  -0.0420 0.1690  243 TYR B CG  
1870  C CD1 . TYR A 227 ? 1.0205 0.9106 1.0204 0.2699  -0.0541 0.1778  243 TYR B CD1 
1871  C CD2 . TYR A 227 ? 1.0702 0.9363 1.0508 0.2664  -0.0485 0.1599  243 TYR B CD2 
1872  C CE1 . TYR A 227 ? 1.0361 0.8890 1.0353 0.2802  -0.0728 0.1767  243 TYR B CE1 
1873  C CE2 . TYR A 227 ? 1.0765 0.9059 1.0554 0.2764  -0.0665 0.1588  243 TYR B CE2 
1874  C CZ  . TYR A 227 ? 1.1122 0.9343 1.1001 0.2833  -0.0790 0.1669  243 TYR B CZ  
1875  O OH  . TYR A 227 ? 1.2374 1.0198 1.2221 0.2933  -0.0983 0.1646  243 TYR B OH  
1876  N N   . VAL A 228 ? 0.9764 0.9108 0.9227 0.2716  -0.0075 0.1417  244 VAL B N   
1877  C CA  . VAL A 228 ? 1.0258 0.9412 0.9530 0.2855  -0.0096 0.1298  244 VAL B CA  
1878  C C   . VAL A 228 ? 0.9858 0.9227 0.9031 0.2968  -0.0016 0.1279  244 VAL B C   
1879  O O   . VAL A 228 ? 1.0145 0.9358 0.9202 0.3137  -0.0076 0.1225  244 VAL B O   
1880  C CB  . VAL A 228 ? 0.9809 0.8905 0.8993 0.2784  -0.0036 0.1208  244 VAL B CB  
1881  C CG1 . VAL A 228 ? 0.9824 0.8832 0.8795 0.2920  -0.0014 0.1089  244 VAL B CG1 
1882  C CG2 . VAL A 228 ? 0.9586 0.8398 0.8851 0.2718  -0.0144 0.1219  244 VAL B CG2 
1883  N N   . ARG A 229 ? 0.9612 0.9339 0.8829 0.2881  0.0114  0.1328  245 ARG B N   
1884  C CA  . ARG A 229 ? 1.0130 1.0085 0.9279 0.2978  0.0186  0.1334  245 ARG B CA  
1885  C C   . ARG A 229 ? 1.0551 1.0444 0.9762 0.3094  0.0091  0.1397  245 ARG B C   
1886  O O   . ARG A 229 ? 1.0986 1.0888 1.0099 0.3252  0.0092  0.1366  245 ARG B O   
1887  C CB  . ARG A 229 ? 1.0131 1.0467 0.9336 0.2845  0.0322  0.1392  245 ARG B CB  
1888  C CG  . ARG A 229 ? 1.0019 1.0623 0.9178 0.2928  0.0398  0.1420  245 ARG B CG  
1889  C CD  . ARG A 229 ? 0.9529 1.0475 0.8739 0.2774  0.0517  0.1474  245 ARG B CD  
1890  N NE  . ARG A 229 ? 0.9351 1.0324 0.8713 0.2643  0.0488  0.1553  245 ARG B NE  
1891  C CZ  . ARG A 229 ? 0.9135 1.0323 0.8546 0.2487  0.0568  0.1589  245 ARG B CZ  
1892  N NH1 . ARG A 229 ? 0.8800 1.0184 0.8128 0.2433  0.0670  0.1553  245 ARG B NH1 
1893  N NH2 . ARG A 229 ? 0.8601 0.9800 0.8143 0.2385  0.0538  0.1661  245 ARG B NH2 
1894  N N   . ALA A 230 ? 1.0151 0.9993 0.9531 0.3019  0.0008  0.1491  246 ALA B N   
1895  C CA  . ALA A 230 ? 1.0248 0.9976 0.9699 0.3126  -0.0113 0.1552  246 ALA B CA  
1896  C C   . ALA A 230 ? 1.0928 1.0295 1.0244 0.3311  -0.0233 0.1457  246 ALA B C   
1897  O O   . ALA A 230 ? 1.1374 1.0731 1.0616 0.3473  -0.0254 0.1436  246 ALA B O   
1898  C CB  . ALA A 230 ? 0.9742 0.9432 0.9400 0.3004  -0.0200 0.1669  246 ALA B CB  
1899  N N   . LYS A 231 ? 1.0932 1.0001 1.0204 0.3293  -0.0311 0.1395  247 LYS B N   
1900  C CA  . LYS A 231 ? 1.1285 0.9972 1.0423 0.3463  -0.0448 0.1306  247 LYS B CA  
1901  C C   . LYS A 231 ? 1.1253 0.9959 1.0161 0.3617  -0.0368 0.1184  247 LYS B C   
1902  O O   . LYS A 231 ? 1.1241 0.9748 1.0028 0.3808  -0.0451 0.1126  247 LYS B O   
1903  C CB  . LYS A 231 ? 1.1358 0.9737 1.0519 0.3386  -0.0552 0.1282  247 LYS B CB  
1904  C CG  . LYS A 231 ? 1.1162 0.9471 1.0551 0.3260  -0.0662 0.1411  247 LYS B CG  
1905  C CD  . LYS A 231 ? 1.1581 0.9709 1.1041 0.3368  -0.0828 0.1470  247 LYS B CD  
1906  C CE  . LYS A 231 ? 1.1969 0.9648 1.1280 0.3512  -0.0990 0.1369  247 LYS B CE  
1907  N NZ  . LYS A 231 ? 1.4169 1.1589 1.3551 0.3607  -0.1191 0.1420  247 LYS B NZ  
1908  N N   . LEU A 232 ? 1.1450 1.0391 1.0292 0.3541  -0.0213 0.1147  248 LEU B N   
1909  C CA  . LEU A 232 ? 1.2013 1.1033 1.0656 0.3675  -0.0124 0.1055  248 LEU B CA  
1910  C C   . LEU A 232 ? 1.2815 1.2080 1.1453 0.3790  -0.0065 0.1099  248 LEU B C   
1911  O O   . LEU A 232 ? 1.4235 1.3469 1.2714 0.3976  -0.0053 0.1034  248 LEU B O   
1912  C CB  . LEU A 232 ? 1.1520 1.0760 1.0122 0.3549  0.0021  0.1026  248 LEU B CB  
1913  C CG  . LEU A 232 ? 1.0913 0.9940 0.9489 0.3451  -0.0011 0.0966  248 LEU B CG  
1914  C CD1 . LEU A 232 ? 1.0089 0.9383 0.8633 0.3336  0.0139  0.0947  248 LEU B CD1 
1915  C CD2 . LEU A 232 ? 1.1308 0.9999 0.9698 0.3625  -0.0108 0.0860  248 LEU B CD2 
1916  N N   . MET A 233 ? 1.3024 1.2552 1.1833 0.3682  -0.0020 0.1212  249 MET B N   
1917  C CA  . MET A 233 ? 1.4056 1.3811 1.2887 0.3781  0.0023  0.1270  249 MET B CA  
1918  C C   . MET A 233 ? 1.5055 1.4533 1.3861 0.3970  -0.0125 0.1255  249 MET B C   
1919  O O   . MET A 233 ? 1.5572 1.5087 1.4269 0.4155  -0.0105 0.1222  249 MET B O   
1920  C CB  . MET A 233 ? 1.3898 1.3958 1.2922 0.3604  0.0084  0.1396  249 MET B CB  
1921  C CG  . MET A 233 ? 1.4136 1.4525 1.3204 0.3644  0.0166  0.1474  249 MET B CG  
1922  S SD  . MET A 233 ? 1.3177 1.3863 1.2454 0.3404  0.0221  0.1608  249 MET B SD  
1923  C CE  . MET A 233 ? 1.2548 1.2938 1.1978 0.3382  0.0041  0.1665  249 MET B CE  
1924  N N   . ASN A 234 ? 1.3401 1.2585 1.2302 0.3933  -0.0282 0.1277  250 ASN B N   
1925  C CA  . ASN A 234 ? 1.3037 1.1884 1.1893 0.4114  -0.0452 0.1245  250 ASN B CA  
1926  C C   . ASN A 234 ? 1.3330 1.1913 1.1939 0.4302  -0.0484 0.1099  250 ASN B C   
1927  O O   . ASN A 234 ? 1.2477 1.0810 1.1005 0.4481  -0.0605 0.1052  250 ASN B O   
1928  C CB  . ASN A 234 ? 1.2822 1.1375 1.1823 0.4028  -0.0629 0.1298  250 ASN B CB  
1929  C CG  . ASN A 234 ? 1.3538 1.2297 1.2790 0.3887  -0.0643 0.1454  250 ASN B CG  
1930  O OD1 . ASN A 234 ? 1.3119 1.2187 1.2436 0.3890  -0.0554 0.1523  250 ASN B OD1 
1931  N ND2 . ASN A 234 ? 1.3770 1.2366 1.3168 0.3757  -0.0753 0.1520  250 ASN B ND2 
1932  N N   . ALA A 235 ? 1.4184 1.2795 1.2668 0.4255  -0.0392 0.1022  251 ALA B N   
1933  C CA  . ALA A 235 ? 1.4472 1.2854 1.2709 0.4432  -0.0415 0.0885  251 ALA B CA  
1934  C C   . ALA A 235 ? 1.5120 1.3798 1.3213 0.4540  -0.0248 0.0847  251 ALA B C   
1935  O O   . ALA A 235 ? 1.5336 1.3862 1.3213 0.4717  -0.0256 0.0740  251 ALA B O   
1936  C CB  . ALA A 235 ? 1.3561 1.1719 1.1741 0.4327  -0.0450 0.0820  251 ALA B CB  
1937  N N   . TYR A 236 ? 1.5128 1.3881 1.5518 0.3292  0.1558  0.1302  252 TYR B N   
1938  C CA  . TYR A 236 ? 1.4951 1.3933 1.5373 0.3343  0.1609  0.1308  252 TYR B CA  
1939  C C   . TYR A 236 ? 1.4638 1.3870 1.5256 0.3431  0.1612  0.1461  252 TYR B C   
1940  O O   . TYR A 236 ? 1.4668 1.4159 1.5319 0.3381  0.1554  0.1533  252 TYR B O   
1941  C CB  . TYR A 236 ? 1.4648 1.3775 1.4943 0.3224  0.1548  0.1257  252 TYR B CB  
1942  C CG  . TYR A 236 ? 1.5328 1.4242 1.5423 0.3122  0.1530  0.1114  252 TYR B CG  
1943  C CD1 . TYR A 236 ? 1.6086 1.4897 1.6082 0.3143  0.1612  0.1006  252 TYR B CD1 
1944  C CD2 . TYR A 236 ? 1.5588 1.4428 1.5596 0.2995  0.1430  0.1089  252 TYR B CD2 
1945  C CE1 . TYR A 236 ? 1.6306 1.4929 1.6109 0.3036  0.1590  0.0880  252 TYR B CE1 
1946  C CE2 . TYR A 236 ? 1.5843 1.4503 1.5673 0.2897  0.1405  0.0967  252 TYR B CE2 
1947  C CZ  . TYR A 236 ? 1.6484 1.5035 1.6207 0.2915  0.1482  0.0865  252 TYR B CZ  
1948  O OH  . TYR A 236 ? 1.5778 1.4147 1.5315 0.2806  0.1453  0.0748  252 TYR B OH  
1949  N N   . PRO A 237 ? 1.4069 1.3233 1.4821 0.3561  0.1682  0.1515  253 PRO B N   
1950  C CA  . PRO A 237 ? 1.3408 1.2764 1.4353 0.3629  0.1660  0.1678  253 PRO B CA  
1951  C C   . PRO A 237 ? 1.2846 1.2555 1.3864 0.3643  0.1658  0.1751  253 PRO B C   
1952  O O   . PRO A 237 ? 1.3042 1.2960 1.4124 0.3594  0.1587  0.1861  253 PRO B O   
1953  C CB  . PRO A 237 ? 1.3363 1.2557 1.4425 0.3777  0.1750  0.1698  253 PRO B CB  
1954  C CG  . PRO A 237 ? 1.3616 1.2620 1.4558 0.3797  0.1840  0.1543  253 PRO B CG  
1955  C CD  . PRO A 237 ? 1.3415 1.2316 1.4150 0.3647  0.1780  0.1432  253 PRO B CD  
1956  N N   . SER A 238 ? 1.2119 1.1898 1.3118 0.3696  0.1735  0.1685  254 SER B N   
1957  C CA  . SER A 238 ? 1.1769 1.1879 1.2861 0.3735  0.1751  0.1761  254 SER B CA  
1958  C C   . SER A 238 ? 1.2013 1.2303 1.2970 0.3611  0.1696  0.1721  254 SER B C   
1959  O O   . SER A 238 ? 1.1872 1.2412 1.2859 0.3634  0.1725  0.1745  254 SER B O   
1960  C CB  . SER A 238 ? 1.1609 1.1721 1.2770 0.3864  0.1869  0.1716  254 SER B CB  
1961  O OG  . SER A 238 ? 1.1936 1.1952 1.2915 0.3802  0.1904  0.1559  254 SER B OG  
1962  N N   . TYR A 239 ? 1.2135 1.2307 1.2946 0.3479  0.1619  0.1663  255 TYR B N   
1963  C CA  . TYR A 239 ? 1.1904 1.2213 1.2575 0.3358  0.1566  0.1613  255 TYR B CA  
1964  C C   . TYR A 239 ? 1.1825 1.2232 1.2483 0.3242  0.1460  0.1680  255 TYR B C   
1965  O O   . TYR A 239 ? 1.0923 1.1529 1.1518 0.3162  0.1422  0.1685  255 TYR B O   
1966  C CB  . TYR A 239 ? 1.1796 1.1873 1.2274 0.3292  0.1576  0.1449  255 TYR B CB  
1967  C CG  . TYR A 239 ? 1.1587 1.1604 1.2032 0.3369  0.1682  0.1358  255 TYR B CG  
1968  C CD1 . TYR A 239 ? 1.1100 1.1355 1.1546 0.3391  0.1724  0.1356  255 TYR B CD1 
1969  C CD2 . TYR A 239 ? 1.1978 1.1697 1.2381 0.3410  0.1744  0.1266  255 TYR B CD2 
1970  C CE1 . TYR A 239 ? 1.1321 1.1522 1.1735 0.3452  0.1826  0.1263  255 TYR B CE1 
1971  C CE2 . TYR A 239 ? 1.1424 1.1081 1.1793 0.3471  0.1849  0.1173  255 TYR B CE2 
1972  C CZ  . TYR A 239 ? 1.1501 1.1401 1.1878 0.3492  0.1891  0.1170  255 TYR B CZ  
1973  O OH  . TYR A 239 ? 1.1137 1.0975 1.1482 0.3547  0.2002  0.1070  255 TYR B OH  
1974  N N   . ILE A 240 ? 1.2999 1.3275 1.3712 0.3226  0.1416  0.1730  256 ILE B N   
1975  C CA  . ILE A 240 ? 1.1717 1.2050 1.2411 0.3105  0.1321  0.1773  256 ILE B CA  
1976  C C   . ILE A 240 ? 1.1986 1.2481 1.2844 0.3133  0.1301  0.1931  256 ILE B C   
1977  O O   . ILE A 240 ? 1.2220 1.2624 1.3191 0.3228  0.1333  0.1989  256 ILE B O   
1978  C CB  . ILE A 240 ? 1.1439 1.1481 1.2040 0.3033  0.1277  0.1685  256 ILE B CB  
1979  C CG1 . ILE A 240 ? 1.1363 1.1317 1.1788 0.2953  0.1261  0.1548  256 ILE B CG1 
1980  C CG2 . ILE A 240 ? 1.1326 1.1402 1.1975 0.2945  0.1197  0.1758  256 ILE B CG2 
1981  C CD1 . ILE A 240 ? 1.2899 1.2530 1.3229 0.2927  0.1255  0.1443  256 ILE B CD1 
1982  N N   . SER A 241 ? 1.1144 1.1877 1.2011 0.3044  0.1247  0.2003  257 SER B N   
1983  C CA  . SER A 241 ? 1.0359 1.1251 1.1369 0.3053  0.1225  0.2156  257 SER B CA  
1984  C C   . SER A 241 ? 1.0118 1.0881 1.1124 0.2957  0.1157  0.2169  257 SER B C   
1985  O O   . SER A 241 ? 1.0061 1.0778 1.0964 0.2842  0.1107  0.2096  257 SER B O   
1986  C CB  . SER A 241 ? 0.9720 1.0945 1.0750 0.3003  0.1209  0.2240  257 SER B CB  
1987  O OG  . SER A 241 ? 0.9257 1.0588 1.0370 0.2940  0.1159  0.2361  257 SER B OG  
1988  N N   . PRO A 242 ? 0.9509 1.0225 1.0631 0.2997  0.1151  0.2267  258 PRO B N   
1989  C CA  . PRO A 242 ? 0.9373 0.9963 1.0492 0.2902  0.1090  0.2278  258 PRO B CA  
1990  C C   . PRO A 242 ? 0.9307 1.0104 1.0427 0.2769  0.1032  0.2340  258 PRO B C   
1991  O O   . PRO A 242 ? 0.9274 0.9996 1.0408 0.2684  0.0985  0.2361  258 PRO B O   
1992  C CB  . PRO A 242 ? 0.9771 1.0286 1.1019 0.2991  0.1105  0.2381  258 PRO B CB  
1993  C CG  . PRO A 242 ? 1.0226 1.0952 1.1576 0.3096  0.1152  0.2473  258 PRO B CG  
1994  C CD  . PRO A 242 ? 1.0052 1.0829 1.1319 0.3130  0.1199  0.2372  258 PRO B CD  
1995  N N   . ILE A 243 ? 0.9211 1.0264 1.0315 0.2741  0.1038  0.2368  259 ILE B N   
1996  C CA  . ILE A 243 ? 0.8920 1.0143 0.9998 0.2598  0.0989  0.2400  259 ILE B CA  
1997  C C   . ILE A 243 ? 0.9025 1.0340 0.9986 0.2541  0.0986  0.2312  259 ILE B C   
1998  O O   . ILE A 243 ? 0.8877 1.0349 0.9809 0.2427  0.0954  0.2332  259 ILE B O   
1999  C CB  . ILE A 243 ? 0.8382 0.9871 0.9567 0.2587  0.0988  0.2562  259 ILE B CB  
2000  C CG1 . ILE A 243 ? 0.8199 0.9903 0.9397 0.2671  0.1036  0.2596  259 ILE B CG1 
2001  C CG2 . ILE A 243 ? 0.8697 1.0091 0.9994 0.2631  0.0980  0.2656  259 ILE B CG2 
2002  C CD1 . ILE A 243 ? 0.7397 0.9410 0.8658 0.2624  0.1029  0.2736  259 ILE B CD1 
2003  N N   . GLY A 244 ? 0.9778 1.0990 1.0664 0.2614  0.1021  0.2211  260 GLY B N   
2004  C CA  . GLY A 244 ? 0.9655 1.0961 1.0425 0.2570  0.1021  0.2135  260 GLY B CA  
2005  C C   . GLY A 244 ? 0.9244 1.0364 0.9898 0.2478  0.0973  0.2008  260 GLY B C   
2006  O O   . GLY A 244 ? 0.9105 1.0028 0.9772 0.2445  0.0941  0.1975  260 GLY B O   
2007  N N   . CYS A 245 ? 0.8883 1.0073 0.9425 0.2433  0.0966  0.1938  261 CYS B N   
2008  C CA  . CYS A 245 ? 0.8419 0.9409 0.8849 0.2368  0.0924  0.1810  261 CYS B CA  
2009  C C   . CYS A 245 ? 0.7913 0.8679 0.8284 0.2452  0.0959  0.1717  261 CYS B C   
2010  O O   . CYS A 245 ? 0.8426 0.9226 0.8820 0.2557  0.1024  0.1734  261 CYS B O   
2011  C CB  . CYS A 245 ? 0.8490 0.9607 0.8811 0.2284  0.0897  0.1764  261 CYS B CB  
2012  S SG  . CYS A 245 ? 0.9217 1.0559 0.9567 0.2156  0.0854  0.1837  261 CYS B SG  
2013  N N   . LEU A 246 ? 0.8462 0.9000 0.8756 0.2399  0.0918  0.1615  262 LEU B N   
2014  C CA  . LEU A 246 ? 0.8486 0.8794 0.8701 0.2456  0.0949  0.1516  262 LEU B CA  
2015  C C   . LEU A 246 ? 0.8346 0.8703 0.8433 0.2454  0.0969  0.1443  262 LEU B C   
2016  O O   . LEU A 246 ? 0.8238 0.8680 0.8246 0.2363  0.0919  0.1413  262 LEU B O   
2017  C CB  . LEU A 246 ? 0.8357 0.8414 0.8526 0.2388  0.0894  0.1438  262 LEU B CB  
2018  C CG  . LEU A 246 ? 0.7999 0.7958 0.8274 0.2389  0.0878  0.1489  262 LEU B CG  
2019  C CD1 . LEU A 246 ? 0.8284 0.8049 0.8512 0.2298  0.0813  0.1410  262 LEU B CD1 
2020  C CD2 . LEU A 246 ? 0.8292 0.8111 0.8600 0.2507  0.0947  0.1496  262 LEU B CD2 
2021  N N   . PRO A 247 ? 0.8301 0.8606 0.8364 0.2549  0.1042  0.1410  263 PRO B N   
2022  C CA  . PRO A 247 ? 0.9196 0.9545 0.9129 0.2540  0.1066  0.1335  263 PRO B CA  
2023  C C   . PRO A 247 ? 0.9423 0.9600 0.9201 0.2436  0.1004  0.1220  263 PRO B C   
2024  O O   . PRO A 247 ? 1.0178 1.0105 0.9915 0.2428  0.0994  0.1151  263 PRO B O   
2025  C CB  . PRO A 247 ? 0.9243 0.9505 0.9200 0.2662  0.1162  0.1311  263 PRO B CB  
2026  C CG  . PRO A 247 ? 0.8575 0.8880 0.8707 0.2749  0.1191  0.1422  263 PRO B CG  
2027  C CD  . PRO A 247 ? 0.8517 0.8755 0.8687 0.2671  0.1112  0.1455  263 PRO B CD  
2028  N N   . ALA A 248 ? 0.9321 0.9632 0.9006 0.2355  0.0962  0.1200  264 ALA B N   
2029  C CA  . ALA A 248 ? 0.9561 0.9736 0.9115 0.2244  0.0884  0.1110  264 ALA B CA  
2030  C C   . ALA A 248 ? 1.0450 1.0365 0.9885 0.2245  0.0900  0.0997  264 ALA B C   
2031  O O   . ALA A 248 ? 1.0111 0.9860 0.9463 0.2158  0.0829  0.0931  264 ALA B O   
2032  C CB  . ALA A 248 ? 0.9421 0.9780 0.8879 0.2174  0.0852  0.1103  264 ALA B CB  
2033  N N   . HIS A 249 ? 1.0459 1.0332 0.9888 0.2338  0.0992  0.0975  265 HIS B N   
2034  C CA  . HIS A 249 ? 1.0535 1.0171 0.9837 0.2332  0.1022  0.0864  265 HIS B CA  
2035  C C   . HIS A 249 ? 1.0220 0.9630 0.9582 0.2390  0.1059  0.0853  265 HIS B C   
2036  O O   . HIS A 249 ? 1.0371 0.9598 0.9652 0.2414  0.1116  0.0773  265 HIS B O   
2037  C CB  . HIS A 249 ? 1.0637 1.0354 0.9875 0.2386  0.1110  0.0826  265 HIS B CB  
2038  C CG  . HIS A 249 ? 1.1241 1.1043 1.0624 0.2526  0.1213  0.0888  265 HIS B CG  
2039  N ND1 . HIS A 249 ? 1.1340 1.1375 1.0880 0.2586  0.1221  0.1010  265 HIS B ND1 
2040  C CD2 . HIS A 249 ? 1.1532 1.1216 1.0929 0.2617  0.1313  0.0846  265 HIS B CD2 
2041  C CE1 . HIS A 249 ? 1.1006 1.1065 1.0658 0.2710  0.1314  0.1045  265 HIS B CE1 
2042  N NE2 . HIS A 249 ? 1.1187 1.1034 1.0759 0.2735  0.1375  0.0945  265 HIS B NE2 
2043  N N   . LEU A 250 ? 0.9922 0.9340 0.9419 0.2411  0.1033  0.0930  266 LEU B N   
2044  C CA  . LEU A 250 ? 1.0302 0.9511 0.9857 0.2469  0.1068  0.0927  266 LEU B CA  
2045  C C   . LEU A 250 ? 1.0800 0.9883 1.0368 0.2387  0.0980  0.0926  266 LEU B C   
2046  O O   . LEU A 250 ? 1.0612 0.9579 1.0261 0.2423  0.0989  0.0956  266 LEU B O   
2047  C CB  . LEU A 250 ? 1.0433 0.9758 1.0154 0.2595  0.1140  0.1028  266 LEU B CB  
2048  C CG  . LEU A 250 ? 1.1602 1.1036 1.1330 0.2690  0.1239  0.1025  266 LEU B CG  
2049  C CD1 . LEU A 250 ? 1.1943 1.1513 1.1853 0.2823  0.1308  0.1135  266 LEU B CD1 
2050  C CD2 . LEU A 250 ? 1.2803 1.1989 1.2408 0.2699  0.1298  0.0906  266 LEU B CD2 
2051  N N   . LEU A 251 ? 1.0814 0.9912 1.0301 0.2274  0.0892  0.0887  267 LEU B N   
2052  C CA  . LEU A 251 ? 1.0158 0.9189 0.9688 0.2197  0.0806  0.0897  267 LEU B CA  
2053  C C   . LEU A 251 ? 1.0587 0.9348 1.0008 0.2127  0.0764  0.0801  267 LEU B C   
2054  O O   . LEU A 251 ? 1.0539 0.9211 1.0009 0.2077  0.0706  0.0805  267 LEU B O   
2055  C CB  . LEU A 251 ? 1.0284 0.9520 0.9833 0.2117  0.0731  0.0931  267 LEU B CB  
2056  C CG  . LEU A 251 ? 0.9437 0.8926 0.9107 0.2184  0.0776  0.1038  267 LEU B CG  
2057  C CD1 . LEU A 251 ? 1.0239 0.9949 0.9916 0.2111  0.0721  0.1075  267 LEU B CD1 
2058  C CD2 . LEU A 251 ? 0.9475 0.8930 0.9285 0.2228  0.0791  0.1107  267 LEU B CD2 
2059  N N   . GLY A 252 ? 1.1146 0.9775 1.0419 0.2115  0.0793  0.0714  268 GLY B N   
2060  C CA  . GLY A 252 ? 1.1518 0.9884 1.0676 0.2042  0.0757  0.0626  268 GLY B CA  
2061  C C   . GLY A 252 ? 1.1269 0.9601 1.0277 0.1927  0.0682  0.0554  268 GLY B C   
2062  O O   . GLY A 252 ? 1.0921 0.9036 0.9818 0.1861  0.0653  0.0480  268 GLY B O   
2063  N N   . ASP A 253 ? 1.1120 0.9652 1.0116 0.1895  0.0644  0.0575  269 ASP B N   
2064  C CA  . ASP A 253 ? 1.0625 0.9128 0.9464 0.1795  0.0583  0.0509  269 ASP B CA  
2065  C C   . ASP A 253 ? 1.0430 0.9168 0.9249 0.1811  0.0602  0.0537  269 ASP B C   
2066  O O   . ASP A 253 ? 1.0309 0.9229 0.9238 0.1897  0.0662  0.0608  269 ASP B O   
2067  C CB  . ASP A 253 ? 1.0361 0.8797 0.9202 0.1684  0.0456  0.0497  269 ASP B CB  
2068  C CG  . ASP A 253 ? 1.0391 0.9034 0.9372 0.1671  0.0397  0.0572  269 ASP B CG  
2069  O OD1 . ASP A 253 ? 1.0471 0.9329 0.9500 0.1717  0.0434  0.0627  269 ASP B OD1 
2070  O OD2 . ASP A 253 ? 0.9833 0.8420 0.8875 0.1607  0.0313  0.0574  269 ASP B OD2 
2071  N N   . MET A 254 ? 1.0280 0.9011 0.8949 0.1722  0.0551  0.0482  270 MET B N   
2072  C CA  . MET A 254 ? 1.0355 0.9276 0.8961 0.1725  0.0573  0.0489  270 MET B CA  
2073  C C   . MET A 254 ? 1.0128 0.9306 0.8859 0.1742  0.0547  0.0580  270 MET B C   
2074  O O   . MET A 254 ? 1.0237 0.9601 0.8941 0.1766  0.0586  0.0602  270 MET B O   
2075  C CB  . MET A 254 ? 1.1282 1.0113 0.9694 0.1603  0.0500  0.0411  270 MET B CB  
2076  C CG  . MET A 254 ? 1.1435 1.0442 0.9751 0.1583  0.0511  0.0407  270 MET B CG  
2077  S SD  . MET A 254 ? 1.1565 1.0653 0.9873 0.1699  0.0668  0.0396  270 MET B SD  
2078  C CE  . MET A 254 ? 1.2652 1.1507 1.0728 0.1622  0.0692  0.0267  270 MET B CE  
2079  N N   . TRP A 255 ? 0.9930 0.9126 0.8792 0.1725  0.0487  0.0631  271 TRP B N   
2080  C CA  . TRP A 255 ? 1.0064 0.9496 0.9041 0.1729  0.0467  0.0715  271 TRP B CA  
2081  C C   . TRP A 255 ? 0.9937 0.9424 0.9102 0.1790  0.0493  0.0793  271 TRP B C   
2082  O O   . TRP A 255 ? 0.9575 0.9275 0.8831 0.1808  0.0505  0.0870  271 TRP B O   
2083  C CB  . TRP A 255 ? 1.0004 0.9454 0.8949 0.1616  0.0352  0.0704  271 TRP B CB  
2084  C CG  . TRP A 255 ? 1.0401 0.9783 0.9159 0.1539  0.0306  0.0632  271 TRP B CG  
2085  C CD1 . TRP A 255 ? 1.0684 1.0211 0.9337 0.1512  0.0307  0.0630  271 TRP B CD1 
2086  C CD2 . TRP A 255 ? 1.0316 0.9465 0.8950 0.1479  0.0263  0.0551  271 TRP B CD2 
2087  N NE1 . TRP A 255 ? 1.0449 0.9840 0.8923 0.1432  0.0258  0.0552  271 TRP B NE1 
2088  C CE2 . TRP A 255 ? 1.0426 0.9586 0.8886 0.1409  0.0231  0.0504  271 TRP B CE2 
2089  C CE3 . TRP A 255 ? 0.9875 0.8806 0.8522 0.1468  0.0247  0.0514  271 TRP B CE3 
2090  C CZ2 . TRP A 255 ? 1.0581 0.9541 0.8883 0.1327  0.0181  0.0425  271 TRP B CZ2 
2091  C CZ3 . TRP A 255 ? 1.0411 0.9150 0.8903 0.1389  0.0201  0.0436  271 TRP B CZ3 
2092  C CH2 . TRP A 255 ? 1.0708 0.9461 0.9030 0.1317  0.0167  0.0393  271 TRP B CH2 
2093  N N   . GLY A 256 ? 1.0697 1.0002 0.9912 0.1816  0.0503  0.0778  272 GLY B N   
2094  C CA  . GLY A 256 ? 1.0200 0.9539 0.9582 0.1847  0.0507  0.0846  272 GLY B CA  
2095  C C   . GLY A 256 ? 1.0096 0.9425 0.9543 0.1755  0.0411  0.0850  272 GLY B C   
2096  O O   . GLY A 256 ? 0.9580 0.9004 0.9167 0.1763  0.0411  0.0915  272 GLY B O   
2097  N N   . ARG A 257 ? 0.9508 0.8731 0.8859 0.1666  0.0329  0.0782  273 ARG B N   
2098  C CA  . ARG A 257 ? 0.8535 0.7725 0.7952 0.1577  0.0231  0.0773  273 ARG B CA  
2099  C C   . ARG A 257 ? 0.8649 0.7675 0.8149 0.1579  0.0222  0.0763  273 ARG B C   
2100  O O   . ARG A 257 ? 0.8618 0.7679 0.8242 0.1539  0.0178  0.0787  273 ARG B O   
2101  C CB  . ARG A 257 ? 0.8423 0.7517 0.7710 0.1488  0.0146  0.0705  273 ARG B CB  
2102  C CG  . ARG A 257 ? 0.8625 0.7686 0.7993 0.1399  0.0040  0.0695  273 ARG B CG  
2103  C CD  . ARG A 257 ? 0.8626 0.7599 0.7869 0.1309  -0.0054 0.0637  273 ARG B CD  
2104  N NE  . ARG A 257 ? 0.8313 0.7250 0.7649 0.1229  -0.0158 0.0629  273 ARG B NE  
2105  C CZ  . ARG A 257 ? 0.8741 0.7531 0.8001 0.1151  -0.0250 0.0577  273 ARG B CZ  
2106  N NH1 . ARG A 257 ? 0.9073 0.7723 0.8157 0.1136  -0.0247 0.0526  273 ARG B NH1 
2107  N NH2 . ARG A 257 ? 0.8385 0.7165 0.7755 0.1085  -0.0344 0.0576  273 ARG B NH2 
2108  N N   . PHE A 258 ? 0.8899 0.7738 0.8324 0.1616  0.0262  0.0720  274 PHE B N   
2109  C CA  . PHE A 258 ? 0.9019 0.7694 0.8507 0.1622  0.0264  0.0710  274 PHE B CA  
2110  C C   . PHE A 258 ? 0.9340 0.7960 0.8822 0.1728  0.0370  0.0729  274 PHE B C   
2111  O O   . PHE A 258 ? 0.9581 0.8148 0.8949 0.1769  0.0425  0.0696  274 PHE B O   
2112  C CB  . PHE A 258 ? 0.9155 0.7607 0.8552 0.1542  0.0192  0.0630  274 PHE B CB  
2113  C CG  . PHE A 258 ? 0.8724 0.7217 0.8120 0.1440  0.0081  0.0609  274 PHE B CG  
2114  C CD1 . PHE A 258 ? 0.8330 0.6876 0.7870 0.1390  0.0017  0.0631  274 PHE B CD1 
2115  C CD2 . PHE A 258 ? 0.8656 0.7123 0.7907 0.1390  0.0040  0.0565  274 PHE B CD2 
2116  C CE1 . PHE A 258 ? 0.8020 0.6601 0.7575 0.1303  -0.0084 0.0613  274 PHE B CE1 
2117  C CE2 . PHE A 258 ? 0.8427 0.6925 0.7682 0.1297  -0.0068 0.0551  274 PHE B CE2 
2118  C CZ  . PHE A 258 ? 0.7664 0.6220 0.7078 0.1259  -0.0129 0.0576  274 PHE B CZ  
2119  N N   . TRP A 259 ? 0.9731 0.8360 0.9338 0.1770  0.0400  0.0782  275 TRP B N   
2120  C CA  . TRP A 259 ? 0.9566 0.8125 0.9186 0.1871  0.0494  0.0806  275 TRP B CA  
2121  C C   . TRP A 259 ? 0.9657 0.7943 0.9213 0.1864  0.0500  0.0745  275 TRP B C   
2122  O O   . TRP A 259 ? 0.9722 0.7926 0.9333 0.1924  0.0552  0.0773  275 TRP B O   
2123  C CB  . TRP A 259 ? 0.9325 0.8027 0.9102 0.1917  0.0522  0.0902  275 TRP B CB  
2124  C CG  . TRP A 259 ? 0.8764 0.7737 0.8603 0.1937  0.0537  0.0975  275 TRP B CG  
2125  C CD1 . TRP A 259 ? 0.9071 0.8178 0.8840 0.1921  0.0529  0.0964  275 TRP B CD1 
2126  C CD2 . TRP A 259 ? 0.8135 0.7277 0.8110 0.1962  0.0558  0.1071  275 TRP B CD2 
2127  N NE1 . TRP A 259 ? 0.8689 0.8041 0.8541 0.1938  0.0548  0.1047  275 TRP B NE1 
2128  C CE2 . TRP A 259 ? 0.8368 0.7748 0.8349 0.1962  0.0565  0.1116  275 TRP B CE2 
2129  C CE3 . TRP A 259 ? 0.8139 0.7253 0.8224 0.1977  0.0570  0.1125  275 TRP B CE3 
2130  C CZ2 . TRP A 259 ? 0.8256 0.7847 0.8349 0.1974  0.0586  0.1214  275 TRP B CZ2 
2131  C CZ3 . TRP A 259 ? 0.8411 0.7733 0.8607 0.1988  0.0588  0.1222  275 TRP B CZ3 
2132  C CH2 . TRP A 259 ? 0.8040 0.7599 0.8239 0.1985  0.0597  0.1267  275 TRP B CH2 
2133  N N   . THR A 260 ? 1.0184 0.8324 0.9623 0.1785  0.0445  0.0664  276 THR B N   
2134  C CA  . THR A 260 ? 1.0280 0.8167 0.9664 0.1755  0.0438  0.0609  276 THR B CA  
2135  C C   . THR A 260 ? 1.0165 0.7890 0.9452 0.1831  0.0538  0.0577  276 THR B C   
2136  O O   . THR A 260 ? 0.9926 0.7467 0.9204 0.1847  0.0568  0.0561  276 THR B O   
2137  C CB  . THR A 260 ? 1.0134 0.7914 0.9425 0.1638  0.0341  0.0538  276 THR B CB  
2138  O OG1 . THR A 260 ? 0.9454 0.7397 0.8836 0.1572  0.0251  0.0563  276 THR B OG1 
2139  C CG2 . THR A 260 ? 1.0767 0.8320 1.0037 0.1597  0.0322  0.0497  276 THR B CG2 
2140  N N   . ASN A 261 ? 1.0399 0.8186 0.9612 0.1876  0.0595  0.0565  277 ASN B N   
2141  C CA  . ASN A 261 ? 1.0689 0.8303 0.9813 0.1941  0.0694  0.0523  277 ASN B CA  
2142  C C   . ASN A 261 ? 1.0537 0.8184 0.9779 0.2065  0.0783  0.0591  277 ASN B C   
2143  O O   . ASN A 261 ? 1.0477 0.7939 0.9674 0.2120  0.0862  0.0562  277 ASN B O   
2144  C CB  . ASN A 261 ? 1.1353 0.9000 1.0353 0.1940  0.0730  0.0475  277 ASN B CB  
2145  C CG  . ASN A 261 ? 1.1331 0.8900 1.0195 0.1812  0.0642  0.0404  277 ASN B CG  
2146  O OD1 . ASN A 261 ? 1.0160 0.7535 0.8961 0.1740  0.0598  0.0357  277 ASN B OD1 
2147  N ND2 . ASN A 261 ? 1.1726 0.9441 1.0536 0.1780  0.0615  0.0397  277 ASN B ND2 
2148  N N   . LEU A 262 ? 1.0567 0.8434 0.9957 0.2103  0.0771  0.0682  278 LEU B N   
2149  C CA  . LEU A 262 ? 1.0645 0.8550 1.0156 0.2213  0.0842  0.0760  278 LEU B CA  
2150  C C   . LEU A 262 ? 1.0700 0.8417 1.0247 0.2209  0.0836  0.0765  278 LEU B C   
2151  O O   . LEU A 262 ? 1.1187 0.8905 1.0826 0.2296  0.0891  0.0830  278 LEU B O   
2152  C CB  . LEU A 262 ? 1.0266 0.8460 0.9916 0.2237  0.0824  0.0860  278 LEU B CB  
2153  C CG  . LEU A 262 ? 1.0303 0.8703 0.9921 0.2243  0.0832  0.0864  278 LEU B CG  
2154  C CD1 . LEU A 262 ? 0.9870 0.8548 0.9622 0.2272  0.0827  0.0970  278 LEU B CD1 
2155  C CD2 . LEU A 262 ? 1.0199 0.8536 0.9747 0.2331  0.0932  0.0828  278 LEU B CD2 
2156  N N   . TYR A 263 ? 1.0990 0.8540 1.0461 0.2111  0.0774  0.0699  279 TYR B N   
2157  C CA  . TYR A 263 ? 1.1477 0.8840 1.0966 0.2102  0.0772  0.0698  279 TYR B CA  
2158  C C   . TYR A 263 ? 1.1878 0.9042 1.1316 0.2194  0.0877  0.0681  279 TYR B C   
2159  O O   . TYR A 263 ? 1.1714 0.8836 1.1236 0.2257  0.0913  0.0738  279 TYR B O   
2160  C CB  . TYR A 263 ? 1.1427 0.8647 1.0833 0.1978  0.0689  0.0623  279 TYR B CB  
2161  C CG  . TYR A 263 ? 1.1294 0.8322 1.0707 0.1959  0.0685  0.0616  279 TYR B CG  
2162  C CD1 . TYR A 263 ? 1.1319 0.8433 1.0863 0.1942  0.0645  0.0675  279 TYR B CD1 
2163  C CD2 . TYR A 263 ? 1.1502 0.8263 1.0780 0.1942  0.0719  0.0543  279 TYR B CD2 
2164  C CE1 . TYR A 263 ? 1.1694 0.8636 1.1239 0.1917  0.0640  0.0666  279 TYR B CE1 
2165  C CE2 . TYR A 263 ? 1.2421 0.9007 1.1696 0.1917  0.0714  0.0535  279 TYR B CE2 
2166  C CZ  . TYR A 263 ? 1.2032 0.8711 1.1442 0.1906  0.0673  0.0597  279 TYR B CZ  
2167  O OH  . TYR A 263 ? 1.2400 0.8907 1.1801 0.1876  0.0667  0.0587  279 TYR B OH  
2168  N N   . SER A 264 ? 1.2535 0.9570 1.1835 0.2199  0.0928  0.0603  280 SER B N   
2169  C CA  . SER A 264 ? 1.2161 0.9011 1.1417 0.2290  0.1041  0.0582  280 SER B CA  
2170  C C   . SER A 264 ? 1.1598 0.8584 1.1005 0.2425  0.1109  0.0678  280 SER B C   
2171  O O   . SER A 264 ? 1.0791 0.7630 1.0226 0.2500  0.1175  0.0697  280 SER B O   
2172  C CB  . SER A 264 ? 1.2329 0.9082 1.1430 0.2278  0.1097  0.0489  280 SER B CB  
2173  O OG  . SER A 264 ? 1.1837 0.8792 1.0972 0.2337  0.1136  0.0510  280 SER B OG  
2174  N N   . LEU A 265 ? 1.2197 0.9464 1.1705 0.2453  0.1089  0.0747  281 LEU B N   
2175  C CA  . LEU A 265 ? 1.2268 0.9695 1.1920 0.2577  0.1150  0.0844  281 LEU B CA  
2176  C C   . LEU A 265 ? 1.2022 0.9568 1.1819 0.2579  0.1099  0.0949  281 LEU B C   
2177  O O   . LEU A 265 ? 1.2518 1.0182 1.2439 0.2675  0.1141  0.1042  281 LEU B O   
2178  C CB  . LEU A 265 ? 1.1986 0.9661 1.1656 0.2604  0.1165  0.0860  281 LEU B CB  
2179  C CG  . LEU A 265 ? 1.3506 1.1126 1.3066 0.2634  0.1242  0.0777  281 LEU B CG  
2180  C CD1 . LEU A 265 ? 1.4249 1.2146 1.3845 0.2655  0.1246  0.0810  281 LEU B CD1 
2181  C CD2 . LEU A 265 ? 1.2848 1.0295 1.2420 0.2748  0.1361  0.0763  281 LEU B CD2 
2182  N N   . THR A 266 ? 1.1701 0.9224 1.1488 0.2469  0.1008  0.0937  282 THR B N   
2183  C CA  . THR A 266 ? 1.1759 0.9407 1.1674 0.2444  0.0954  0.1026  282 THR B CA  
2184  C C   . THR A 266 ? 1.1796 0.9250 1.1679 0.2364  0.0905  0.0992  282 THR B C   
2185  O O   . THR A 266 ? 1.0294 0.7836 1.0268 0.2314  0.0850  0.1046  282 THR B O   
2186  C CB  . THR A 266 ? 1.0928 0.8847 1.0895 0.2378  0.0886  0.1058  282 THR B CB  
2187  O OG1 . THR A 266 ? 1.1786 0.9646 1.1658 0.2266  0.0817  0.0970  282 THR B OG1 
2188  C CG2 . THR A 266 ? 1.0855 0.8977 1.0841 0.2447  0.0932  0.1090  282 THR B CG2 
2189  N N   . VAL A 267 ? 1.2941 1.0137 1.2697 0.2343  0.0924  0.0901  283 VAL B N   
2190  C CA  . VAL A 267 ? 1.3134 1.0129 1.2848 0.2271  0.0886  0.0865  283 VAL B CA  
2191  C C   . VAL A 267 ? 1.3314 1.0285 1.3128 0.2319  0.0905  0.0949  283 VAL B C   
2192  O O   . VAL A 267 ? 1.4010 1.0916 1.3848 0.2429  0.0983  0.0990  283 VAL B O   
2193  C CB  . VAL A 267 ? 1.3780 1.0492 1.3331 0.2257  0.0927  0.0763  283 VAL B CB  
2194  C CG1 . VAL A 267 ? 1.4008 1.0630 1.3531 0.2381  0.1041  0.0764  283 VAL B CG1 
2195  C CG2 . VAL A 267 ? 1.4730 1.1231 1.4244 0.2200  0.0903  0.0739  283 VAL B CG2 
2196  N N   . PRO A 268 ? 1.2822 0.9851 1.2703 0.2238  0.0834  0.0978  284 PRO B N   
2197  C CA  . PRO A 268 ? 1.3530 1.0517 1.3489 0.2267  0.0845  0.1055  284 PRO B CA  
2198  C C   . PRO A 268 ? 1.4181 1.0874 1.4058 0.2314  0.0903  0.1026  284 PRO B C   
2199  O O   . PRO A 268 ? 1.4051 1.0711 1.3978 0.2418  0.0963  0.1095  284 PRO B O   
2200  C CB  . PRO A 268 ? 1.2736 0.9801 1.2747 0.2141  0.0757  0.1055  284 PRO B CB  
2201  C CG  . PRO A 268 ? 1.2249 0.9491 1.2264 0.2082  0.0707  0.1020  284 PRO B CG  
2202  C CD  . PRO A 268 ? 1.2290 0.9442 1.2189 0.2118  0.0743  0.0949  284 PRO B CD  
2203  N N   . PHE A 269 ? 1.4095 1.0571 1.3844 0.2243  0.0888  0.0930  285 PHE B N   
2204  C CA  . PHE A 269 ? 1.5255 1.1439 1.4915 0.2265  0.0936  0.0900  285 PHE B CA  
2205  C C   . PHE A 269 ? 1.6234 1.2219 1.5742 0.2282  0.0995  0.0803  285 PHE B C   
2206  O O   . PHE A 269 ? 1.6497 1.2285 1.5879 0.2200  0.0977  0.0719  285 PHE B O   
2207  C CB  . PHE A 269 ? 1.5149 1.1249 1.4794 0.2151  0.0867  0.0878  285 PHE B CB  
2208  C CG  . PHE A 269 ? 1.4927 1.1214 1.4715 0.2127  0.0820  0.0970  285 PHE B CG  
2209  C CD1 . PHE A 269 ? 1.4990 1.1243 1.4839 0.2197  0.0855  0.1058  285 PHE B CD1 
2210  C CD2 . PHE A 269 ? 1.4597 1.1102 1.4463 0.2039  0.0744  0.0974  285 PHE B CD2 
2211  C CE1 . PHE A 269 ? 1.4891 1.1316 1.4863 0.2163  0.0811  0.1145  285 PHE B CE1 
2212  C CE2 . PHE A 269 ? 1.4026 1.0705 1.4020 0.2009  0.0708  0.1057  285 PHE B CE2 
2213  C CZ  . PHE A 269 ? 1.4085 1.0723 1.4126 0.2067  0.0741  0.1142  285 PHE B CZ  
2214  N N   . GLY A 270 ? 1.9420 1.5452 1.8940 0.2388  0.1070  0.0817  286 GLY B N   
2215  C CA  . GLY A 270 ? 1.9902 1.5811 1.9290 0.2396  0.1126  0.0726  286 GLY B CA  
2216  C C   . GLY A 270 ? 2.1130 1.6708 2.0364 0.2381  0.1182  0.0646  286 GLY B C   
2217  O O   . GLY A 270 ? 2.1931 1.7385 2.1063 0.2414  0.1259  0.0581  286 GLY B O   
2218  N N   . GLN A 271 ? 1.7951 1.3377 1.7157 0.2328  0.1151  0.0646  287 GLN B N   
2219  C CA  . GLN A 271 ? 1.7980 1.3088 1.7022 0.2295  0.1199  0.0567  287 GLN B CA  
2220  C C   . GLN A 271 ? 1.8329 1.3345 1.7293 0.2151  0.1112  0.0517  287 GLN B C   
2221  O O   . GLN A 271 ? 1.8528 1.3279 1.7346 0.2106  0.1143  0.0451  287 GLN B O   
2222  C CB  . GLN A 271 ? 1.8117 1.3055 1.7184 0.2402  0.1283  0.0615  287 GLN B CB  
2223  C CG  . GLN A 271 ? 1.8412 1.3471 1.7596 0.2551  0.1360  0.0680  287 GLN B CG  
2224  C CD  . GLN A 271 ? 1.9040 1.3875 1.8214 0.2661  0.1464  0.0698  287 GLN B CD  
2225  O OE1 . GLN A 271 ? 1.9064 1.3972 1.8378 0.2759  0.1480  0.0799  287 GLN B OE1 
2226  N NE2 . GLN A 271 ? 1.9604 1.4160 1.8613 0.2643  0.1537  0.0601  287 GLN B NE2 
2227  N N   . LYS A 272 ? 1.8399 1.3623 1.7456 0.2076  0.1009  0.0545  288 LYS B N   
2228  C CA  . LYS A 272 ? 1.8835 1.3977 1.7826 0.1938  0.0929  0.0490  288 LYS B CA  
2229  C C   . LYS A 272 ? 2.0310 1.5418 1.9181 0.1850  0.0896  0.0400  288 LYS B C   
2230  O O   . LYS A 272 ? 2.0103 1.5367 1.8998 0.1869  0.0891  0.0398  288 LYS B O   
2231  C CB  . LYS A 272 ? 1.7725 1.3091 1.6865 0.1882  0.0834  0.0545  288 LYS B CB  
2232  C CG  . LYS A 272 ? 1.7225 1.2557 1.6438 0.1914  0.0845  0.0614  288 LYS B CG  
2233  C CD  . LYS A 272 ? 1.7436 1.2514 1.6532 0.1836  0.0838  0.0559  288 LYS B CD  
2234  C CE  . LYS A 272 ? 1.7270 1.2320 1.6434 0.1852  0.0838  0.0628  288 LYS B CE  
2235  N NZ  . LYS A 272 ? 1.6503 1.1357 1.5570 0.1749  0.0808  0.0575  288 LYS B NZ  
2236  N N   . PRO A 273 ? 2.3707 1.8619 2.2446 0.1746  0.0870  0.0328  289 PRO B N   
2237  C CA  . PRO A 273 ? 2.3941 1.8807 2.2556 0.1653  0.0835  0.0246  289 PRO B CA  
2238  C C   . PRO A 273 ? 2.2490 1.7615 2.1213 0.1587  0.0725  0.0260  289 PRO B C   
2239  O O   . PRO A 273 ? 2.2119 1.7311 2.0915 0.1509  0.0639  0.0267  289 PRO B O   
2240  C CB  . PRO A 273 ? 2.4403 1.9021 2.2878 0.1550  0.0820  0.0183  289 PRO B CB  
2241  C CG  . PRO A 273 ? 2.4690 1.9324 2.3266 0.1555  0.0796  0.0235  289 PRO B CG  
2242  C CD  . PRO A 273 ? 2.3893 1.8627 2.2590 0.1697  0.0861  0.0320  289 PRO B CD  
2243  N N   . ASN A 274 ? 2.1711 1.6981 2.0449 0.1618  0.0727  0.0262  290 ASN B N   
2244  C CA  . ASN A 274 ? 2.0212 1.5692 1.9024 0.1543  0.0621  0.0263  290 ASN B CA  
2245  C C   . ASN A 274 ? 1.9855 1.5209 1.8554 0.1404  0.0545  0.0189  290 ASN B C   
2246  O O   . ASN A 274 ? 2.0271 1.5382 1.8808 0.1365  0.0585  0.0131  290 ASN B O   
2247  C CB  . ASN A 274 ? 2.0039 1.5676 1.8860 0.1593  0.0639  0.0273  290 ASN B CB  
2248  C CG  . ASN A 274 ? 1.9554 1.5469 1.8519 0.1563  0.0546  0.0314  290 ASN B CG  
2249  O OD1 . ASN A 274 ? 1.9364 1.5315 1.8330 0.1457  0.0449  0.0283  290 ASN B OD1 
2250  N ND2 . ASN A 274 ? 1.8554 1.4667 1.7645 0.1655  0.0576  0.0387  290 ASN B ND2 
2251  N N   . ILE A 275 ? 1.8674 1.4198 1.7464 0.1326  0.0436  0.0193  291 ILE B N   
2252  C CA  . ILE A 275 ? 1.7820 1.3259 1.6540 0.1192  0.0347  0.0135  291 ILE B CA  
2253  C C   . ILE A 275 ? 1.6924 1.2376 1.5542 0.1145  0.0316  0.0097  291 ILE B C   
2254  O O   . ILE A 275 ? 1.6835 1.2479 1.5524 0.1182  0.0298  0.0127  291 ILE B O   
2255  C CB  . ILE A 275 ? 1.6934 1.2542 1.5826 0.1130  0.0243  0.0160  291 ILE B CB  
2256  C CG1 . ILE A 275 ? 1.7653 1.3222 1.6621 0.1159  0.0277  0.0190  291 ILE B CG1 
2257  C CG2 . ILE A 275 ? 1.5392 1.0932 1.4232 0.0995  0.0145  0.0104  291 ILE B CG2 
2258  C CD1 . ILE A 275 ? 1.6492 1.2192 1.5615 0.1084  0.0186  0.0200  291 ILE B CD1 
2259  N N   . ASP A 276 ? 1.6324 1.1567 1.4763 0.1061  0.0313  0.0031  292 ASP B N   
2260  C CA  . ASP A 276 ? 1.6464 1.1700 1.4786 0.0992  0.0273  -0.0009 292 ASP B CA  
2261  C C   . ASP A 276 ? 1.6678 1.1696 1.4838 0.0862  0.0235  -0.0072 292 ASP B C   
2262  O O   . ASP A 276 ? 1.6891 1.1681 1.4882 0.0859  0.0324  -0.0115 292 ASP B O   
2263  C CB  . ASP A 276 ? 1.6251 1.1453 1.4475 0.1072  0.0379  -0.0019 292 ASP B CB  
2264  C CG  . ASP A 276 ? 1.6459 1.1642 1.4543 0.0986  0.0339  -0.0066 292 ASP B CG  
2265  O OD1 . ASP A 276 ? 1.6725 1.1937 1.4805 0.0871  0.0220  -0.0078 292 ASP B OD1 
2266  O OD2 . ASP A 276 ? 1.5918 1.1047 1.3892 0.1027  0.0425  -0.0091 292 ASP B OD2 
2267  N N   . VAL A 277 ? 1.7236 1.2326 1.5451 0.0754  0.0107  -0.0076 293 VAL B N   
2268  C CA  . VAL A 277 ? 1.8817 1.3721 1.6903 0.0626  0.0059  -0.0126 293 VAL B CA  
2269  C C   . VAL A 277 ? 1.8681 1.3474 1.6570 0.0534  0.0041  -0.0173 293 VAL B C   
2270  O O   . VAL A 277 ? 1.8953 1.3611 1.6727 0.0408  -0.0016 -0.0210 293 VAL B O   
2271  C CB  . VAL A 277 ? 1.9553 1.4576 1.7796 0.0548  -0.0070 -0.0109 293 VAL B CB  
2272  C CG1 . VAL A 277 ? 1.8637 1.3732 1.7043 0.0621  -0.0040 -0.0074 293 VAL B CG1 
2273  C CG2 . VAL A 277 ? 1.8974 1.4224 1.7347 0.0528  -0.0176 -0.0080 293 VAL B CG2 
2274  N N   . THR A 278 ? 1.7766 1.2614 1.5608 0.0589  0.0090  -0.0171 294 THR B N   
2275  C CA  . THR A 278 ? 1.7656 1.2398 1.5298 0.0504  0.0088  -0.0219 294 THR B CA  
2276  C C   . THR A 278 ? 1.7964 1.2420 1.5389 0.0414  0.0139  -0.0280 294 THR B C   
2277  O O   . THR A 278 ? 1.7814 1.2166 1.5089 0.0273  0.0074  -0.0317 294 THR B O   
2278  C CB  . THR A 278 ? 1.6899 1.1676 1.4493 0.0603  0.0196  -0.0222 294 THR B CB  
2279  O OG1 . THR A 278 ? 1.5714 1.0757 1.3497 0.0689  0.0161  -0.0164 294 THR B OG1 
2280  C CG2 . THR A 278 ? 1.6373 1.1045 1.3757 0.0499  0.0189  -0.0276 294 THR B CG2 
2281  N N   . ASP A 279 ? 1.7636 1.1963 1.5042 0.0496  0.0256  -0.0287 295 ASP B N   
2282  C CA  . ASP A 279 ? 1.7754 1.1795 1.4944 0.0437  0.0340  -0.0348 295 ASP B CA  
2283  C C   . ASP A 279 ? 1.8675 1.2623 1.5828 0.0308  0.0250  -0.0361 295 ASP B C   
2284  O O   . ASP A 279 ? 1.8780 1.2552 1.5736 0.0174  0.0234  -0.0411 295 ASP B O   
2285  C CB  . ASP A 279 ? 1.7465 1.1417 1.4675 0.0577  0.0487  -0.0342 295 ASP B CB  
2286  C CG  . ASP A 279 ? 1.7333 1.1309 1.4512 0.0675  0.0594  -0.0350 295 ASP B CG  
2287  O OD1 . ASP A 279 ? 1.6758 1.0728 1.3817 0.0602  0.0577  -0.0385 295 ASP B OD1 
2288  O OD2 . ASP A 279 ? 1.7369 1.1387 1.4654 0.0821  0.0684  -0.0316 295 ASP B OD2 
2289  N N   . ALA A 280 ? 1.9626 1.3702 1.6971 0.0338  0.0185  -0.0318 296 ALA B N   
2290  C CA  . ALA A 280 ? 1.9466 1.3511 1.6819 0.0213  0.0077  -0.0326 296 ALA B CA  
2291  C C   . ALA A 280 ? 1.9286 1.3374 1.6583 0.0072  -0.0051 -0.0337 296 ALA B C   
2292  O O   . ALA A 280 ? 1.8900 1.2847 1.6065 -0.0064 -0.0099 -0.0369 296 ALA B O   
2293  C CB  . ALA A 280 ? 1.9380 1.3618 1.6985 0.0268  0.0015  -0.0276 296 ALA B CB  
2294  N N   . MET A 281 ? 1.7978 1.2258 1.5368 0.0099  -0.0108 -0.0308 297 MET B N   
2295  C CA  . MET A 281 ? 1.8038 1.2385 1.5406 -0.0029 -0.0248 -0.0306 297 MET B CA  
2296  C C   . MET A 281 ? 1.8150 1.2288 1.5240 -0.0147 -0.0222 -0.0359 297 MET B C   
2297  O O   . MET A 281 ? 1.7899 1.1971 1.4901 -0.0298 -0.0322 -0.0371 297 MET B O   
2298  C CB  . MET A 281 ? 1.7535 1.2132 1.5066 0.0031  -0.0310 -0.0261 297 MET B CB  
2299  C CG  . MET A 281 ? 1.7481 1.2295 1.5284 0.0135  -0.0336 -0.0209 297 MET B CG  
2300  S SD  . MET A 281 ? 1.5367 1.0445 1.3324 0.0236  -0.0354 -0.0160 297 MET B SD  
2301  C CE  . MET A 281 ? 1.6340 1.1479 1.4276 0.0088  -0.0526 -0.0157 297 MET B CE  
2302  N N   . VAL A 282 ? 1.8637 1.2675 1.5588 -0.0087 -0.0089 -0.0390 298 VAL B N   
2303  C CA  . VAL A 282 ? 1.8251 1.2054 1.4921 -0.0206 -0.0040 -0.0451 298 VAL B CA  
2304  C C   . VAL A 282 ? 1.7955 1.1544 1.4500 -0.0298 -0.0023 -0.0484 298 VAL B C   
2305  O O   . VAL A 282 ? 1.7915 1.1381 1.4292 -0.0462 -0.0084 -0.0511 298 VAL B O   
2306  C CB  . VAL A 282 ? 1.7236 1.0949 1.3792 -0.0113 0.0125  -0.0488 298 VAL B CB  
2307  C CG1 . VAL A 282 ? 1.6273 0.9725 1.2534 -0.0243 0.0191  -0.0559 298 VAL B CG1 
2308  C CG2 . VAL A 282 ? 1.6011 0.9937 1.2665 -0.0049 0.0096  -0.0459 298 VAL B CG2 
2309  N N   . ASP A 283 ? 1.8122 1.1676 1.4753 -0.0203 0.0047  -0.0476 299 ASP B N   
2310  C CA  . ASP A 283 ? 1.8089 1.1409 1.4571 -0.0275 0.0097  -0.0515 299 ASP B CA  
2311  C C   . ASP A 283 ? 1.7576 1.0925 1.4095 -0.0412 -0.0050 -0.0502 299 ASP B C   
2312  O O   . ASP A 283 ? 1.7562 1.0708 1.3910 -0.0520 -0.0032 -0.0539 299 ASP B O   
2313  C CB  . ASP A 283 ? 1.9002 1.2282 1.5570 -0.0126 0.0215  -0.0507 299 ASP B CB  
2314  C CG  . ASP A 283 ? 1.9447 1.2622 1.5927 -0.0012 0.0382  -0.0533 299 ASP B CG  
2315  O OD1 . ASP A 283 ? 1.8823 1.1932 1.5149 -0.0064 0.0416  -0.0569 299 ASP B OD1 
2316  O OD2 . ASP A 283 ? 2.0592 1.3759 1.7163 0.0128  0.0476  -0.0514 299 ASP B OD2 
2317  N N   . GLN A 284 ? 1.7602 1.1196 1.4339 -0.0411 -0.0192 -0.0451 300 GLN B N   
2318  C CA  . GLN A 284 ? 1.7505 1.1150 1.4296 -0.0545 -0.0344 -0.0436 300 GLN B CA  
2319  C C   . GLN A 284 ? 1.7431 1.1120 1.4151 -0.0674 -0.0464 -0.0429 300 GLN B C   
2320  O O   . GLN A 284 ? 1.7192 1.0941 1.3967 -0.0790 -0.0606 -0.0409 300 GLN B O   
2321  C CB  . GLN A 284 ? 1.7087 1.0967 1.4182 -0.0468 -0.0425 -0.0387 300 GLN B CB  
2322  C CG  . GLN A 284 ? 1.6652 1.0498 1.3819 -0.0348 -0.0316 -0.0389 300 GLN B CG  
2323  C CD  . GLN A 284 ? 1.7353 1.1443 1.4819 -0.0269 -0.0383 -0.0342 300 GLN B CD  
2324  O OE1 . GLN A 284 ? 1.7743 1.1994 1.5360 -0.0333 -0.0521 -0.0318 300 GLN B OE1 
2325  N NE2 . GLN A 284 ? 1.7878 1.1998 1.5434 -0.0132 -0.0284 -0.0327 300 GLN B NE2 
2326  N N   . ALA A 285 ? 1.7308 1.0968 1.3908 -0.0657 -0.0408 -0.0444 301 ALA B N   
2327  C CA  . ALA A 285 ? 1.7205 1.0879 1.3697 -0.0785 -0.0507 -0.0442 301 ALA B CA  
2328  C C   . ALA A 285 ? 1.7587 1.1529 1.4324 -0.0777 -0.0672 -0.0379 301 ALA B C   
2329  O O   . ALA A 285 ? 1.7171 1.1153 1.3930 -0.0907 -0.0822 -0.0356 301 ALA B O   
2330  C CB  . ALA A 285 ? 1.6635 1.0107 1.2900 -0.0981 -0.0550 -0.0473 301 ALA B CB  
2331  N N   . TRP A 286 ? 1.7259 1.1383 1.4187 -0.0620 -0.0640 -0.0349 302 TRP B N   
2332  C CA  . TRP A 286 ? 1.6933 1.1313 1.4095 -0.0594 -0.0774 -0.0293 302 TRP B CA  
2333  C C   . TRP A 286 ? 1.7336 1.1753 1.4399 -0.0630 -0.0809 -0.0289 302 TRP B C   
2334  O O   . TRP A 286 ? 1.7134 1.1496 1.4078 -0.0566 -0.0688 -0.0317 302 TRP B O   
2335  C CB  . TRP A 286 ? 1.6357 1.0921 1.3770 -0.0420 -0.0727 -0.0261 302 TRP B CB  
2336  C CG  . TRP A 286 ? 1.6820 1.1401 1.4380 -0.0404 -0.0739 -0.0254 302 TRP B CG  
2337  C CD1 . TRP A 286 ? 1.7297 1.1693 1.4736 -0.0479 -0.0711 -0.0288 302 TRP B CD1 
2338  C CD2 . TRP A 286 ? 1.6734 1.1527 1.4581 -0.0323 -0.0788 -0.0214 302 TRP B CD2 
2339  N NE1 . TRP A 286 ? 1.7211 1.1690 1.4842 -0.0445 -0.0736 -0.0273 302 TRP B NE1 
2340  C CE2 . TRP A 286 ? 1.6633 1.1356 1.4518 -0.0351 -0.0782 -0.0229 302 TRP B CE2 
2341  C CE3 . TRP A 286 ? 1.6524 1.1553 1.4590 -0.0235 -0.0829 -0.0170 302 TRP B CE3 
2342  C CZ2 . TRP A 286 ? 1.6323 1.1206 1.4460 -0.0297 -0.0816 -0.0205 302 TRP B CZ2 
2343  C CZ3 . TRP A 286 ? 1.6571 1.1757 1.4889 -0.0181 -0.0861 -0.0144 302 TRP B CZ3 
2344  C CH2 . TRP A 286 ? 1.6401 1.1514 1.4754 -0.0214 -0.0854 -0.0163 302 TRP B CH2 
2345  N N   . ASP A 287 ? 1.7810 1.2314 1.4919 -0.0740 -0.0974 -0.0256 303 ASP B N   
2346  C CA  . ASP A 287 ? 1.7405 1.1980 1.4459 -0.0783 -0.1042 -0.0240 303 ASP B CA  
2347  C C   . ASP A 287 ? 1.7194 1.2033 1.4527 -0.0702 -0.1144 -0.0180 303 ASP B C   
2348  O O   . ASP A 287 ? 1.6914 1.1879 1.4483 -0.0631 -0.1170 -0.0152 303 ASP B O   
2349  C CB  . ASP A 287 ? 1.7310 1.1761 1.4175 -0.0986 -0.1158 -0.0244 303 ASP B CB  
2350  C CG  . ASP A 287 ? 1.7416 1.1910 1.4418 -0.1079 -0.1310 -0.0208 303 ASP B CG  
2351  O OD1 . ASP A 287 ? 1.7512 1.2140 1.4762 -0.0990 -0.1330 -0.0183 303 ASP B OD1 
2352  O OD2 . ASP A 287 ? 1.7949 1.2346 1.4809 -0.1249 -0.1411 -0.0204 303 ASP B OD2 
2353  N N   . ALA A 288 ? 1.7113 1.2032 1.4410 -0.0719 -0.1196 -0.0163 304 ALA B N   
2354  C CA  . ALA A 288 ? 1.6073 1.1233 1.3611 -0.0646 -0.1284 -0.0108 304 ALA B CA  
2355  C C   . ALA A 288 ? 1.5691 1.0958 1.3462 -0.0684 -0.1427 -0.0066 304 ALA B C   
2356  O O   . ALA A 288 ? 1.4875 1.0290 1.2889 -0.0578 -0.1416 -0.0044 304 ALA B O   
2357  C CB  . ALA A 288 ? 1.5293 1.0485 1.2720 -0.0711 -0.1355 -0.0096 304 ALA B CB  
2358  N N   . GLN A 289 ? 1.4713 0.9909 1.2412 -0.0841 -0.1562 -0.0054 305 GLN B N   
2359  C CA  . GLN A 289 ? 1.4862 1.0112 1.2742 -0.0904 -0.1691 -0.0024 305 GLN B CA  
2360  C C   . GLN A 289 ? 1.5006 1.0307 1.3072 -0.0804 -0.1618 -0.0034 305 GLN B C   
2361  O O   . GLN A 289 ? 1.4395 0.9869 1.2736 -0.0762 -0.1694 -0.0001 305 GLN B O   
2362  C CB  . GLN A 289 ? 1.6070 1.1134 1.3741 -0.1085 -0.1761 -0.0037 305 GLN B CB  
2363  C CG  . GLN A 289 ? 1.6397 1.1487 1.4225 -0.1156 -0.1869 -0.0016 305 GLN B CG  
2364  C CD  . GLN A 289 ? 1.6145 1.1376 1.4150 -0.1229 -0.2070 0.0046  305 GLN B CD  
2365  O OE1 . GLN A 289 ? 1.4802 1.0117 1.2823 -0.1219 -0.2129 0.0077  305 GLN B OE1 
2366  N NE2 . GLN A 289 ? 1.5456 1.0709 1.3594 -0.1305 -0.2177 0.0066  305 GLN B NE2 
2367  N N   . ARG A 290 ? 1.5468 1.0620 1.3391 -0.0767 -0.1469 -0.0082 306 ARG B N   
2368  C CA  . ARG A 290 ? 1.5028 1.0206 1.3101 -0.0688 -0.1403 -0.0093 306 ARG B CA  
2369  C C   . ARG A 290 ? 1.4279 0.9641 1.2562 -0.0523 -0.1337 -0.0074 306 ARG B C   
2370  O O   . ARG A 290 ? 1.3806 0.9292 1.2323 -0.0474 -0.1357 -0.0059 306 ARG B O   
2371  C CB  . ARG A 290 ? 1.5610 1.0556 1.3451 -0.0704 -0.1267 -0.0147 306 ARG B CB  
2372  C CG  . ARG A 290 ? 1.5499 1.0439 1.3452 -0.0626 -0.1185 -0.0163 306 ARG B CG  
2373  C CD  . ARG A 290 ? 1.5059 1.0074 1.3193 -0.0700 -0.1307 -0.0147 306 ARG B CD  
2374  N NE  . ARG A 290 ? 1.5484 1.0472 1.3693 -0.0645 -0.1227 -0.0168 306 ARG B NE  
2375  C CZ  . ARG A 290 ? 1.7004 1.1784 1.5019 -0.0687 -0.1142 -0.0210 306 ARG B CZ  
2376  N NH1 . ARG A 290 ? 1.7183 1.1762 1.4922 -0.0791 -0.1125 -0.0237 306 ARG B NH1 
2377  N NH2 . ARG A 290 ? 1.7701 1.2467 1.5795 -0.0631 -0.1073 -0.0227 306 ARG B NH2 
2378  N N   . ILE A 291 ? 1.4106 0.9494 1.2311 -0.0445 -0.1259 -0.0073 307 ILE B N   
2379  C CA  . ILE A 291 ? 1.4168 0.9747 1.2570 -0.0300 -0.1209 -0.0047 307 ILE B CA  
2380  C C   . ILE A 291 ? 1.3800 0.9587 1.2468 -0.0309 -0.1346 -0.0002 307 ILE B C   
2381  O O   . ILE A 291 ? 1.3422 0.9338 1.2319 -0.0243 -0.1341 0.0012  307 ILE B O   
2382  C CB  . ILE A 291 ? 1.3929 0.9520 1.2202 -0.0236 -0.1129 -0.0049 307 ILE B CB  
2383  C CG1 . ILE A 291 ? 1.4269 0.9677 1.2331 -0.0196 -0.0969 -0.0094 307 ILE B CG1 
2384  C CG2 . ILE A 291 ? 1.3621 0.9430 1.2099 -0.0111 -0.1106 -0.0012 307 ILE B CG2 
2385  C CD1 . ILE A 291 ? 1.4810 1.0212 1.2730 -0.0152 -0.0894 -0.0105 307 ILE B CD1 
2386  N N   . PHE A 292 ? 1.3330 0.9146 1.1972 -0.0394 -0.1472 0.0021  308 PHE B N   
2387  C CA  . PHE A 292 ? 1.2824 0.8835 1.1722 -0.0394 -0.1599 0.0065  308 PHE B CA  
2388  C C   . PHE A 292 ? 1.2464 0.8499 1.1540 -0.0455 -0.1690 0.0070  308 PHE B C   
2389  O O   . PHE A 292 ? 1.2433 0.8642 1.1779 -0.0416 -0.1746 0.0095  308 PHE B O   
2390  C CB  . PHE A 292 ? 1.3291 0.9315 1.2106 -0.0473 -0.1714 0.0092  308 PHE B CB  
2391  C CG  . PHE A 292 ? 1.3305 0.9390 1.2040 -0.0396 -0.1646 0.0098  308 PHE B CG  
2392  C CD1 . PHE A 292 ? 1.3220 0.9164 1.1684 -0.0398 -0.1542 0.0063  308 PHE B CD1 
2393  C CD2 . PHE A 292 ? 1.2821 0.9103 1.1749 -0.0325 -0.1680 0.0135  308 PHE B CD2 
2394  C CE1 . PHE A 292 ? 1.2991 0.8995 1.1384 -0.0330 -0.1479 0.0065  308 PHE B CE1 
2395  C CE2 . PHE A 292 ? 1.2557 0.8896 1.1401 -0.0260 -0.1617 0.0140  308 PHE B CE2 
2396  C CZ  . PHE A 292 ? 1.2532 0.8736 1.1111 -0.0262 -0.1517 0.0105  308 PHE B CZ  
2397  N N   . LYS A 293 ? 1.2793 0.8659 1.1726 -0.0552 -0.1700 0.0043  309 LYS B N   
2398  C CA  . LYS A 293 ? 1.3000 0.8892 1.2101 -0.0603 -0.1770 0.0042  309 LYS B CA  
2399  C C   . LYS A 293 ? 1.2608 0.8578 1.1878 -0.0495 -0.1667 0.0025  309 LYS B C   
2400  O O   . LYS A 293 ? 1.2537 0.8645 1.2066 -0.0489 -0.1727 0.0036  309 LYS B O   
2401  C CB  . LYS A 293 ? 1.3369 0.9056 1.2254 -0.0732 -0.1788 0.0015  309 LYS B CB  
2402  C CG  . LYS A 293 ? 1.3600 0.9226 1.2370 -0.0878 -0.1932 0.0040  309 LYS B CG  
2403  C CD  . LYS A 293 ? 1.3239 0.9013 1.2270 -0.0935 -0.2105 0.0084  309 LYS B CD  
2404  C CE  . LYS A 293 ? 1.3018 0.8737 1.1928 -0.1074 -0.2253 0.0119  309 LYS B CE  
2405  N NZ  . LYS A 293 ? 1.2434 0.8300 1.1610 -0.1125 -0.2429 0.0169  309 LYS B NZ  
2406  N N   . GLU A 294 ? 1.2203 0.8084 1.1333 -0.0413 -0.1511 -0.0003 310 GLU B N   
2407  C CA  . GLU A 294 ? 1.2145 0.8096 1.1426 -0.0317 -0.1416 -0.0014 310 GLU B CA  
2408  C C   . GLU A 294 ? 1.1967 0.8147 1.1496 -0.0225 -0.1427 0.0020  310 GLU B C   
2409  O O   . GLU A 294 ? 1.1644 0.7938 1.1388 -0.0188 -0.1415 0.0019  310 GLU B O   
2410  C CB  . GLU A 294 ? 1.2688 0.8493 1.1770 -0.0245 -0.1252 -0.0042 310 GLU B CB  
2411  C CG  . GLU A 294 ? 1.3906 0.9477 1.2768 -0.0323 -0.1212 -0.0084 310 GLU B CG  
2412  C CD  . GLU A 294 ? 1.4134 0.9700 1.3117 -0.0369 -0.1240 -0.0101 310 GLU B CD  
2413  O OE1 . GLU A 294 ? 1.3206 0.8928 1.2425 -0.0309 -0.1238 -0.0090 310 GLU B OE1 
2414  O OE2 . GLU A 294 ? 1.4591 0.9993 1.3423 -0.0473 -0.1260 -0.0128 310 GLU B OE2 
2415  N N   . ALA A 295 ? 1.2021 0.8268 1.1516 -0.0198 -0.1448 0.0046  311 ALA B N   
2416  C CA  . ALA A 295 ? 1.1564 0.8027 1.1285 -0.0128 -0.1472 0.0080  311 ALA B CA  
2417  C C   . ALA A 295 ? 1.1311 0.7897 1.1286 -0.0189 -0.1610 0.0096  311 ALA B C   
2418  O O   . ALA A 295 ? 1.1107 0.7840 1.1325 -0.0143 -0.1599 0.0099  311 ALA B O   
2419  C CB  . ALA A 295 ? 1.1445 0.7936 1.1048 -0.0104 -0.1476 0.0103  311 ALA B CB  
2420  N N   . GLU A 296 ? 1.1018 0.7548 1.0946 -0.0297 -0.1741 0.0106  312 GLU B N   
2421  C CA  . GLU A 296 ? 1.1120 0.7751 1.1288 -0.0362 -0.1881 0.0123  312 GLU B CA  
2422  C C   . GLU A 296 ? 1.0800 0.7459 1.1134 -0.0360 -0.1850 0.0093  312 GLU B C   
2423  O O   . GLU A 296 ? 1.0421 0.7240 1.1038 -0.0345 -0.1894 0.0099  312 GLU B O   
2424  C CB  . GLU A 296 ? 1.1540 0.8059 1.1581 -0.0493 -0.2013 0.0135  312 GLU B CB  
2425  C CG  . GLU A 296 ? 1.1939 0.8547 1.2224 -0.0570 -0.2166 0.0155  312 GLU B CG  
2426  C CD  . GLU A 296 ? 1.2311 0.8821 1.2464 -0.0702 -0.2308 0.0182  312 GLU B CD  
2427  O OE1 . GLU A 296 ? 1.2236 0.8567 1.2138 -0.0775 -0.2282 0.0160  312 GLU B OE1 
2428  O OE2 . GLU A 296 ? 1.2076 0.8682 1.2376 -0.0738 -0.2447 0.0226  312 GLU B OE2 
2429  N N   . LYS A 297 ? 1.1112 0.7609 1.1267 -0.0387 -0.1778 0.0058  313 LYS B N   
2430  C CA  . LYS A 297 ? 1.0892 0.7393 1.1165 -0.0391 -0.1739 0.0025  313 LYS B CA  
2431  C C   . LYS A 297 ? 1.0865 0.7516 1.1331 -0.0285 -0.1648 0.0022  313 LYS B C   
2432  O O   . LYS A 297 ? 1.0420 0.7196 1.1138 -0.0292 -0.1678 0.0012  313 LYS B O   
2433  C CB  . LYS A 297 ? 1.1051 0.7333 1.1054 -0.0425 -0.1656 -0.0010 313 LYS B CB  
2434  C CG  . LYS A 297 ? 1.0916 0.7155 1.0982 -0.0479 -0.1655 -0.0045 313 LYS B CG  
2435  C CD  . LYS A 297 ? 1.1738 0.7742 1.1513 -0.0512 -0.1565 -0.0080 313 LYS B CD  
2436  C CE  . LYS A 297 ? 1.2238 0.8087 1.1761 -0.0605 -0.1622 -0.0073 313 LYS B CE  
2437  N NZ  . LYS A 297 ? 1.2944 0.8548 1.2165 -0.0648 -0.1532 -0.0110 313 LYS B NZ  
2438  N N   . PHE A 298 ? 1.0809 0.7454 1.1163 -0.0191 -0.1536 0.0031  314 PHE B N   
2439  C CA  . PHE A 298 ? 1.0142 0.6925 1.0655 -0.0096 -0.1445 0.0034  314 PHE B CA  
2440  C C   . PHE A 298 ? 0.9818 0.6812 1.0623 -0.0091 -0.1523 0.0055  314 PHE B C   
2441  O O   . PHE A 298 ? 0.9744 0.6851 1.0767 -0.0081 -0.1505 0.0040  314 PHE B O   
2442  C CB  . PHE A 298 ? 1.0476 0.7232 1.0820 -0.0002 -0.1334 0.0052  314 PHE B CB  
2443  C CG  . PHE A 298 ? 1.0415 0.7344 1.0924 0.0090  -0.1263 0.0072  314 PHE B CG  
2444  C CD1 . PHE A 298 ? 1.0142 0.7095 1.0732 0.0126  -0.1175 0.0057  314 PHE B CD1 
2445  C CD2 . PHE A 298 ? 1.0001 0.7067 1.0576 0.0131  -0.1286 0.0107  314 PHE B CD2 
2446  C CE1 . PHE A 298 ? 0.9408 0.6523 1.0145 0.0198  -0.1111 0.0079  314 PHE B CE1 
2447  C CE2 . PHE A 298 ? 0.9451 0.6677 1.0170 0.0206  -0.1218 0.0126  314 PHE B CE2 
2448  C CZ  . PHE A 298 ? 0.8945 0.6197 0.9745 0.0237  -0.1130 0.0113  314 PHE B CZ  
2449  N N   . PHE A 299 ? 0.9648 0.6691 1.0456 -0.0104 -0.1611 0.0087  315 PHE B N   
2450  C CA  . PHE A 299 ? 0.9325 0.6556 1.0408 -0.0100 -0.1689 0.0108  315 PHE B CA  
2451  C C   . PHE A 299 ? 0.9440 0.6719 1.0748 -0.0173 -0.1781 0.0089  315 PHE B C   
2452  O O   . PHE A 299 ? 0.9523 0.6954 1.1095 -0.0154 -0.1776 0.0080  315 PHE B O   
2453  C CB  . PHE A 299 ? 0.9275 0.6526 1.0297 -0.0111 -0.1775 0.0147  315 PHE B CB  
2454  C CG  . PHE A 299 ? 0.9564 0.6824 1.0431 -0.0032 -0.1685 0.0166  315 PHE B CG  
2455  C CD1 . PHE A 299 ? 0.9889 0.7305 1.0899 0.0049  -0.1613 0.0178  315 PHE B CD1 
2456  C CD2 . PHE A 299 ? 0.9509 0.6621 1.0086 -0.0041 -0.1662 0.0168  315 PHE B CD2 
2457  C CE1 . PHE A 299 ? 0.9214 0.6650 1.0081 0.0123  -0.1525 0.0199  315 PHE B CE1 
2458  C CE2 . PHE A 299 ? 1.0063 0.7193 1.0505 0.0036  -0.1571 0.0182  315 PHE B CE2 
2459  C CZ  . PHE A 299 ? 0.9481 0.6777 1.0070 0.0119  -0.1506 0.0200  315 PHE B CZ  
2460  N N   . VAL A 300 ? 0.9686 0.6844 1.0898 -0.0263 -0.1866 0.0081  316 VAL B N   
2461  C CA  . VAL A 300 ? 0.9723 0.6931 1.1152 -0.0335 -0.1952 0.0062  316 VAL B CA  
2462  C C   . VAL A 300 ? 0.9585 0.6843 1.1140 -0.0304 -0.1850 0.0019  316 VAL B C   
2463  O O   . VAL A 300 ? 0.9587 0.7002 1.1427 -0.0297 -0.1864 0.0007  316 VAL B O   
2464  C CB  . VAL A 300 ? 0.9432 0.6484 1.0699 -0.0441 -0.2036 0.0058  316 VAL B CB  
2465  C CG1 . VAL A 300 ? 0.7895 0.5006 0.9385 -0.0506 -0.2102 0.0033  316 VAL B CG1 
2466  C CG2 . VAL A 300 ? 1.0046 0.7072 1.1234 -0.0490 -0.2162 0.0105  316 VAL B CG2 
2467  N N   . SER A 301 ? 0.9811 0.6938 1.1150 -0.0280 -0.1734 -0.0004 317 SER B N   
2468  C CA  . SER A 301 ? 1.0103 0.7239 1.1513 -0.0269 -0.1643 -0.0045 317 SER B CA  
2469  C C   . SER A 301 ? 0.9886 0.7217 1.1565 -0.0216 -0.1600 -0.0049 317 SER B C   
2470  O O   . SER A 301 ? 1.0376 0.7745 1.2172 -0.0227 -0.1546 -0.0087 317 SER B O   
2471  C CB  . SER A 301 ? 1.0173 0.7149 1.1308 -0.0226 -0.1517 -0.0055 317 SER B CB  
2472  O OG  . SER A 301 ? 1.0211 0.7258 1.1332 -0.0129 -0.1435 -0.0028 317 SER B OG  
2473  N N   . VAL A 302 ? 0.9234 0.6687 1.1011 -0.0168 -0.1622 -0.0014 318 VAL B N   
2474  C CA  . VAL A 302 ? 0.9391 0.7026 1.1410 -0.0124 -0.1572 -0.0018 318 VAL B CA  
2475  C C   . VAL A 302 ? 0.9234 0.7018 1.1540 -0.0155 -0.1683 -0.0012 318 VAL B C   
2476  O O   . VAL A 302 ? 0.9481 0.7420 1.1996 -0.0121 -0.1651 -0.0013 318 VAL B O   
2477  C CB  . VAL A 302 ? 0.9125 0.6794 1.1034 -0.0034 -0.1479 0.0016  318 VAL B CB  
2478  C CG1 . VAL A 302 ? 0.9053 0.6572 1.0693 0.0003  -0.1372 0.0013  318 VAL B CG1 
2479  C CG2 . VAL A 302 ? 0.8481 0.6164 1.0330 -0.0018 -0.1552 0.0059  318 VAL B CG2 
2480  N N   . GLY A 303 ? 0.8866 0.6605 1.1190 -0.0220 -0.1812 -0.0004 319 GLY B N   
2481  C CA  . GLY A 303 ? 0.8793 0.6670 1.1405 -0.0248 -0.1923 0.0006  319 GLY B CA  
2482  C C   . GLY A 303 ? 0.8983 0.6886 1.1568 -0.0225 -0.2002 0.0060  319 GLY B C   
2483  O O   . GLY A 303 ? 0.8998 0.7032 1.1834 -0.0226 -0.2074 0.0074  319 GLY B O   
2484  N N   . LEU A 304 ? 0.8616 0.6400 1.0912 -0.0208 -0.1988 0.0089  320 LEU B N   
2485  C CA  . LEU A 304 ? 0.8841 0.6635 1.1077 -0.0197 -0.2065 0.0138  320 LEU B CA  
2486  C C   . LEU A 304 ? 0.8983 0.6644 1.1062 -0.0279 -0.2188 0.0160  320 LEU B C   
2487  O O   . LEU A 304 ? 0.9463 0.6987 1.1364 -0.0322 -0.2168 0.0138  320 LEU B O   
2488  C CB  . LEU A 304 ? 0.9048 0.6812 1.1058 -0.0123 -0.1957 0.0155  320 LEU B CB  
2489  C CG  . LEU A 304 ? 0.8347 0.6258 1.0500 -0.0047 -0.1849 0.0151  320 LEU B CG  
2490  C CD1 . LEU A 304 ? 0.8019 0.5876 0.9918 0.0019  -0.1739 0.0166  320 LEU B CD1 
2491  C CD2 . LEU A 304 ? 0.8062 0.6110 1.0427 -0.0040 -0.1925 0.0178  320 LEU B CD2 
2492  N N   . PRO A 305 ? 0.9019 0.6711 1.1155 -0.0307 -0.2316 0.0204  321 PRO B N   
2493  C CA  . PRO A 305 ? 0.9781 0.7354 1.1780 -0.0400 -0.2447 0.0230  321 PRO B CA  
2494  C C   . PRO A 305 ? 1.0403 0.7802 1.2022 -0.0417 -0.2411 0.0238  321 PRO B C   
2495  O O   . PRO A 305 ? 0.9734 0.7114 1.1188 -0.0350 -0.2307 0.0237  321 PRO B O   
2496  C CB  . PRO A 305 ? 0.9110 0.6779 1.1295 -0.0416 -0.2588 0.0279  321 PRO B CB  
2497  C CG  . PRO A 305 ? 0.8071 0.5843 1.0308 -0.0326 -0.2509 0.0286  321 PRO B CG  
2498  C CD  . PRO A 305 ? 0.8676 0.6511 1.1007 -0.0265 -0.2356 0.0234  321 PRO B CD  
2499  N N   . ASN A 306 ? 1.0503 0.7776 1.1990 -0.0516 -0.2500 0.0245  322 ASN B N   
2500  C CA  . ASN A 306 ? 1.1287 0.8381 1.2417 -0.0560 -0.2483 0.0249  322 ASN B CA  
2501  C C   . ASN A 306 ? 1.0964 0.8049 1.2004 -0.0591 -0.2588 0.0299  322 ASN B C   
2502  O O   . ASN A 306 ? 1.0749 0.7934 1.1997 -0.0615 -0.2718 0.0339  322 ASN B O   
2503  C CB  . ASN A 306 ? 1.1982 0.8941 1.2999 -0.0665 -0.2528 0.0232  322 ASN B CB  
2504  C CG  . ASN A 306 ? 1.3271 1.0315 1.4554 -0.0739 -0.2678 0.0252  322 ASN B CG  
2505  O OD1 . ASN A 306 ? 1.2852 1.0043 1.4397 -0.0716 -0.2763 0.0282  322 ASN B OD1 
2506  N ND2 . ASN A 306 ? 1.4197 1.1147 1.5415 -0.0829 -0.2709 0.0233  322 ASN B ND2 
2507  N N   . MET A 307 ? 1.1341 0.8307 1.2074 -0.0589 -0.2524 0.0296  323 MET B N   
2508  C CA  . MET A 307 ? 1.1072 0.8021 1.1676 -0.0612 -0.2595 0.0336  323 MET B CA  
2509  C C   . MET A 307 ? 1.1768 0.8702 1.2434 -0.0730 -0.2791 0.0383  323 MET B C   
2510  O O   . MET A 307 ? 1.2211 0.9078 1.2880 -0.0817 -0.2856 0.0380  323 MET B O   
2511  C CB  . MET A 307 ? 1.1673 0.8456 1.1908 -0.0630 -0.2507 0.0314  323 MET B CB  
2512  C CG  . MET A 307 ? 1.1743 0.8520 1.1882 -0.0519 -0.2318 0.0275  323 MET B CG  
2513  S SD  . MET A 307 ? 1.1619 0.8570 1.1875 -0.0394 -0.2255 0.0294  323 MET B SD  
2514  C CE  . MET A 307 ? 1.1026 0.8140 1.1633 -0.0316 -0.2204 0.0279  323 MET B CE  
2515  N N   . THR A 308 ? 1.1914 0.8906 1.2616 -0.0736 -0.2887 0.0429  324 THR B N   
2516  C CA  . THR A 308 ? 1.1851 0.8826 1.2607 -0.0849 -0.3083 0.0484  324 THR B CA  
2517  C C   . THR A 308 ? 1.2337 0.9119 1.2765 -0.0976 -0.3123 0.0485  324 THR B C   
2518  O O   . THR A 308 ? 1.2327 0.8992 1.2462 -0.0971 -0.3010 0.0451  324 THR B O   
2519  C CB  . THR A 308 ? 1.1782 0.8831 1.2594 -0.0838 -0.3175 0.0535  324 THR B CB  
2520  O OG1 . THR A 308 ? 1.1815 0.8759 1.2297 -0.0854 -0.3128 0.0531  324 THR B OG1 
2521  C CG2 . THR A 308 ? 1.1044 0.8262 1.2106 -0.0708 -0.3096 0.0525  324 THR B CG2 
2522  N N   . GLN A 309 ? 1.2272 0.9022 1.2752 -0.1096 -0.3286 0.0525  325 GLN B N   
2523  C CA  . GLN A 309 ? 1.2418 0.8989 1.2582 -0.1238 -0.3349 0.0538  325 GLN B CA  
2524  C C   . GLN A 309 ? 1.2402 0.8916 1.2328 -0.1251 -0.3351 0.0554  325 GLN B C   
2525  O O   . GLN A 309 ? 1.2473 0.8836 1.2068 -0.1300 -0.3275 0.0523  325 GLN B O   
2526  C CB  . GLN A 309 ? 1.2076 0.8651 1.2366 -0.1366 -0.3551 0.0597  325 GLN B CB  
2527  C CG  . GLN A 309 ? 1.2924 0.9320 1.2901 -0.1535 -0.3635 0.0618  325 GLN B CG  
2528  C CD  . GLN A 309 ? 1.4413 1.0842 1.4556 -0.1656 -0.3851 0.0690  325 GLN B CD  
2529  O OE1 . GLN A 309 ? 1.4373 1.0961 1.4878 -0.1602 -0.3928 0.0719  325 GLN B OE1 
2530  N NE2 . GLN A 309 ? 1.4391 1.0674 1.4277 -0.1823 -0.3951 0.0722  325 GLN B NE2 
2531  N N   . GLY A 310 ? 1.2260 0.8894 1.2356 -0.1206 -0.3430 0.0598  326 GLY B N   
2532  C CA  . GLY A 310 ? 1.1933 0.8549 1.1846 -0.1190 -0.3411 0.0607  326 GLY B CA  
2533  C C   . GLY A 310 ? 1.2141 0.8707 1.1840 -0.1107 -0.3205 0.0541  326 GLY B C   
2534  O O   . GLY A 310 ? 1.2585 0.9027 1.1973 -0.1163 -0.3171 0.0526  326 GLY B O   
2535  N N   . PHE A 311 ? 1.2226 0.8881 1.2085 -0.0978 -0.3064 0.0500  327 PHE B N   
2536  C CA  . PHE A 311 ? 1.2446 0.9065 1.2127 -0.0888 -0.2868 0.0444  327 PHE B CA  
2537  C C   . PHE A 311 ? 1.2415 0.8836 1.1761 -0.0969 -0.2804 0.0405  327 PHE B C   
2538  O O   . PHE A 311 ? 1.2003 0.8355 1.1107 -0.0948 -0.2700 0.0376  327 PHE B O   
2539  C CB  . PHE A 311 ? 1.1443 0.8165 1.1336 -0.0763 -0.2739 0.0410  327 PHE B CB  
2540  C CG  . PHE A 311 ? 1.0997 0.7659 1.0698 -0.0683 -0.2546 0.0357  327 PHE B CG  
2541  C CD1 . PHE A 311 ? 1.1372 0.7888 1.0902 -0.0716 -0.2465 0.0314  327 PHE B CD1 
2542  C CD2 . PHE A 311 ? 1.1569 0.8319 1.1261 -0.0577 -0.2445 0.0352  327 PHE B CD2 
2543  C CE1 . PHE A 311 ? 1.1719 0.8175 1.1088 -0.0640 -0.2292 0.0270  327 PHE B CE1 
2544  C CE2 . PHE A 311 ? 1.1866 0.8567 1.1397 -0.0501 -0.2271 0.0309  327 PHE B CE2 
2545  C CZ  . PHE A 311 ? 1.1855 0.8407 1.1230 -0.0530 -0.2196 0.0268  327 PHE B CZ  
2546  N N   . TRP A 312 ? 1.2520 0.8851 1.1855 -0.1055 -0.2847 0.0398  328 TRP B N   
2547  C CA  . TRP A 312 ? 1.2412 0.8545 1.1430 -0.1134 -0.2772 0.0356  328 TRP B CA  
2548  C C   . TRP A 312 ? 1.2918 0.8931 1.1673 -0.1275 -0.2870 0.0378  328 TRP B C   
2549  O O   . TRP A 312 ? 1.3028 0.8920 1.1496 -0.1293 -0.2770 0.0339  328 TRP B O   
2550  C CB  . TRP A 312 ? 1.2040 0.8110 1.1109 -0.1194 -0.2789 0.0342  328 TRP B CB  
2551  C CG  . TRP A 312 ? 1.2350 0.8504 1.1621 -0.1074 -0.2676 0.0308  328 TRP B CG  
2552  C CD1 . TRP A 312 ? 1.2592 0.8884 1.2186 -0.1042 -0.2738 0.0325  328 TRP B CD1 
2553  C CD2 . TRP A 312 ? 1.2556 0.8661 1.1723 -0.0974 -0.2482 0.0252  328 TRP B CD2 
2554  N NE1 . TRP A 312 ? 1.3085 0.9413 1.2769 -0.0935 -0.2592 0.0280  328 TRP B NE1 
2555  C CE2 . TRP A 312 ? 1.2883 0.9097 1.2309 -0.0890 -0.2438 0.0239  328 TRP B CE2 
2556  C CE3 . TRP A 312 ? 1.2390 0.8371 1.1278 -0.0947 -0.2341 0.0211  328 TRP B CE3 
2557  C CZ2 . TRP A 312 ? 1.2582 0.8780 1.1987 -0.0785 -0.2266 0.0193  328 TRP B CZ2 
2558  C CZ3 . TRP A 312 ? 1.2689 0.8658 1.1571 -0.0835 -0.2170 0.0167  328 TRP B CZ3 
2559  C CH2 . TRP A 312 ? 1.2907 0.8981 1.2041 -0.0757 -0.2137 0.0161  328 TRP B CH2 
2560  N N   . GLU A 313 ? 1.2614 0.8660 1.1470 -0.1376 -0.3065 0.0441  329 GLU B N   
2561  C CA  . GLU A 313 ? 1.2676 0.8608 1.1287 -0.1529 -0.3179 0.0471  329 GLU B CA  
2562  C C   . GLU A 313 ? 1.2737 0.8668 1.1174 -0.1492 -0.3121 0.0459  329 GLU B C   
2563  O O   . GLU A 313 ? 1.2573 0.8359 1.0699 -0.1602 -0.3117 0.0442  329 GLU B O   
2564  C CB  . GLU A 313 ? 1.2831 0.8832 1.1632 -0.1619 -0.3407 0.0552  329 GLU B CB  
2565  C CG  . GLU A 313 ? 1.3800 0.9692 1.2532 -0.1781 -0.3518 0.0575  329 GLU B CG  
2566  C CD  . GLU A 313 ? 1.4049 1.0064 1.3107 -0.1809 -0.3703 0.0646  329 GLU B CD  
2567  O OE1 . GLU A 313 ? 1.3664 0.9824 1.2959 -0.1737 -0.3781 0.0690  329 GLU B OE1 
2568  O OE2 . GLU A 313 ? 1.4874 1.0840 1.3952 -0.1906 -0.3771 0.0659  329 GLU B OE2 
2569  N N   . ASN A 314 ? 1.2919 0.9010 1.1546 -0.1345 -0.3071 0.0464  330 ASN B N   
2570  C CA  . ASN A 314 ? 1.2404 0.8524 1.0907 -0.1319 -0.3053 0.0468  330 ASN B CA  
2571  C C   . ASN A 314 ? 1.2243 0.8379 1.0643 -0.1191 -0.2845 0.0407  330 ASN B C   
2572  O O   . ASN A 314 ? 1.2634 0.8755 1.0851 -0.1195 -0.2813 0.0397  330 ASN B O   
2573  C CB  . ASN A 314 ? 1.2061 0.8352 1.0836 -0.1267 -0.3173 0.0529  330 ASN B CB  
2574  C CG  . ASN A 314 ? 1.2276 0.8558 1.1161 -0.1393 -0.3395 0.0600  330 ASN B CG  
2575  O OD1 . ASN A 314 ? 1.2332 0.8477 1.0990 -0.1548 -0.3490 0.0617  330 ASN B OD1 
2576  N ND2 . ASN A 314 ? 1.2131 0.8560 1.1367 -0.1331 -0.3478 0.0642  330 ASN B ND2 
2577  N N   . SER A 315 ? 1.3095 0.8766 1.0199 0.0798  -0.0187 -0.0489 331 SER B N   
2578  C CA  . SER A 315 ? 1.3009 0.8668 1.0257 0.0836  -0.0100 -0.0393 331 SER B CA  
2579  C C   . SER A 315 ? 1.3272 0.8645 1.0377 0.0933  -0.0013 -0.0412 331 SER B C   
2580  O O   . SER A 315 ? 1.3729 0.8896 1.0632 0.0947  -0.0034 -0.0506 331 SER B O   
2581  C CB  . SER A 315 ? 1.2783 0.8526 1.0212 0.0730  -0.0151 -0.0342 331 SER B CB  
2582  O OG  . SER A 315 ? 1.2278 0.8293 0.9854 0.0641  -0.0224 -0.0315 331 SER B OG  
2583  N N   . MET A 316 ? 1.3280 0.8643 1.0491 0.0999  0.0087  -0.0322 332 MET B N   
2584  C CA  . MET A 316 ? 1.4002 0.9108 1.1117 0.1092  0.0180  -0.0320 332 MET B CA  
2585  C C   . MET A 316 ? 1.4035 0.9117 1.1311 0.1056  0.0201  -0.0242 332 MET B C   
2586  O O   . MET A 316 ? 1.3748 0.8960 1.1201 0.1080  0.0263  -0.0132 332 MET B O   
2587  C CB  . MET A 316 ? 1.4196 0.9299 1.1282 0.1219  0.0291  -0.0274 332 MET B CB  
2588  C CG  . MET A 316 ? 1.4868 0.9751 1.1916 0.1310  0.0395  -0.0241 332 MET B CG  
2589  S SD  . MET A 316 ? 1.5887 1.0715 1.2837 0.1467  0.0521  -0.0213 332 MET B SD  
2590  C CE  . MET A 316 ? 1.6953 1.1632 1.3615 0.1491  0.0473  -0.0361 332 MET B CE  
2591  N N   . LEU A 317 ? 1.4697 0.9609 1.1910 0.0999  0.0151  -0.0295 333 LEU B N   
2592  C CA  . LEU A 317 ? 1.5183 1.0091 1.2559 0.0942  0.0149  -0.0225 333 LEU B CA  
2593  C C   . LEU A 317 ? 1.6602 1.1228 1.3909 0.1021  0.0239  -0.0215 333 LEU B C   
2594  O O   . LEU A 317 ? 1.7001 1.1613 1.4449 0.0986  0.0250  -0.0146 333 LEU B O   
2595  C CB  . LEU A 317 ? 1.3737 0.8682 1.1133 0.0803  0.0020  -0.0276 333 LEU B CB  
2596  C CG  . LEU A 317 ? 1.2929 0.8131 1.0378 0.0712  -0.0084 -0.0300 333 LEU B CG  
2597  C CD1 . LEU A 317 ? 1.2660 0.7871 1.0129 0.0579  -0.0202 -0.0340 333 LEU B CD1 
2598  C CD2 . LEU A 317 ? 1.3427 0.8918 1.1090 0.0706  -0.0060 -0.0198 333 LEU B CD2 
2599  N N   . THR A 318 ? 1.7003 1.1404 1.4099 0.1125  0.0304  -0.0278 334 THR B N   
2600  C CA  . THR A 318 ? 1.7766 1.1906 1.4799 0.1217  0.0406  -0.0261 334 THR B CA  
2601  C C   . THR A 318 ? 1.9249 1.3361 1.6211 0.1358  0.0519  -0.0235 334 THR B C   
2602  O O   . THR A 318 ? 1.9302 1.3508 1.6181 0.1382  0.0504  -0.0275 334 THR B O   
2603  C CB  . THR A 318 ? 1.7533 1.1361 1.4340 0.1205  0.0377  -0.0379 334 THR B CB  
2604  O OG1 . THR A 318 ? 1.8663 1.2437 1.5253 0.1227  0.0346  -0.0488 334 THR B OG1 
2605  C CG2 . THR A 318 ? 1.7302 1.1143 1.4170 0.1062  0.0263  -0.0405 334 THR B CG2 
2606  N N   . ASP A 319 ? 2.0487 1.4469 1.7480 0.1454  0.0633  -0.0166 335 ASP B N   
2607  C CA  . ASP A 319 ? 2.1640 1.5551 1.8531 0.1596  0.0743  -0.0153 335 ASP B CA  
2608  C C   . ASP A 319 ? 2.2771 1.6474 1.9377 0.1628  0.0722  -0.0295 335 ASP B C   
2609  O O   . ASP A 319 ? 2.3098 1.6575 1.9564 0.1590  0.0683  -0.0385 335 ASP B O   
2610  C CB  . ASP A 319 ? 2.2646 1.6401 1.9580 0.1699  0.0870  -0.0071 335 ASP B CB  
2611  C CG  . ASP A 319 ? 2.3245 1.7008 2.0137 0.1843  0.0989  -0.0020 335 ASP B CG  
2612  O OD1 . ASP A 319 ? 2.3029 1.6715 1.9726 0.1898  0.0996  -0.0104 335 ASP B OD1 
2613  O OD2 . ASP A 319 ? 2.3328 1.7176 2.0384 0.1900  0.1076  0.0108  335 ASP B OD2 
2614  N N   . PRO A 320 ? 2.4324 1.8101 2.0835 0.1689  0.0741  -0.0320 336 PRO B N   
2615  C CA  . PRO A 320 ? 2.5615 1.9239 2.1864 0.1705  0.0706  -0.0454 336 PRO B CA  
2616  C C   . PRO A 320 ? 2.6322 1.9647 2.2362 0.1832  0.0810  -0.0499 336 PRO B C   
2617  O O   . PRO A 320 ? 2.6421 1.9709 2.2311 0.1915  0.0851  -0.0539 336 PRO B O   
2618  C CB  . PRO A 320 ? 2.4930 1.8794 2.1203 0.1716  0.0687  -0.0441 336 PRO B CB  
2619  C CG  . PRO A 320 ? 2.4112 1.8135 2.0581 0.1780  0.0778  -0.0303 336 PRO B CG  
2620  C CD  . PRO A 320 ? 2.3495 1.7544 2.0157 0.1719  0.0774  -0.0226 336 PRO B CD  
2621  N N   . GLY A 321 ? 2.4788 1.7896 2.0819 0.1849  0.0855  -0.0492 337 GLY B N   
2622  C CA  . GLY A 321 ? 2.3510 1.6325 1.9357 0.1972  0.0963  -0.0528 337 GLY B CA  
2623  C C   . GLY A 321 ? 2.3765 1.6647 1.9645 0.2114  0.1087  -0.0442 337 GLY B C   
2624  O O   . GLY A 321 ? 2.3645 1.6795 1.9706 0.2116  0.1097  -0.0344 337 GLY B O   
2625  N N   . ASN A 322 ? 2.3720 1.6347 1.9409 0.2232  0.1184  -0.0484 338 ASN B N   
2626  C CA  . ASN A 322 ? 2.4336 1.6988 2.0051 0.2378  0.1317  -0.0396 338 ASN B CA  
2627  C C   . ASN A 322 ? 2.4288 1.7036 1.9882 0.2433  0.1322  -0.0432 338 ASN B C   
2628  O O   . ASN A 322 ? 2.3019 1.5904 1.8696 0.2522  0.1403  -0.0337 338 ASN B O   
2629  C CB  . ASN A 322 ? 2.4303 1.6631 1.9881 0.2486  0.1428  -0.0415 338 ASN B CB  
2630  C CG  . ASN A 322 ? 2.3929 1.6294 1.9603 0.2629  0.1572  -0.0288 338 ASN B CG  
2631  O OD1 . ASN A 322 ? 2.3460 1.6098 1.9342 0.2632  0.1588  -0.0167 338 ASN B OD1 
2632  N ND2 . ASN A 322 ? 2.3941 1.6028 1.9463 0.2745  0.1679  -0.0313 338 ASN B ND2 
2633  N N   . VAL A 323 ? 2.5261 1.7950 2.0666 0.2377  0.1233  -0.0562 339 VAL B N   
2634  C CA  . VAL A 323 ? 2.5832 1.8591 2.1097 0.2421  0.1227  -0.0611 339 VAL B CA  
2635  C C   . VAL A 323 ? 2.5700 1.8792 2.1168 0.2410  0.1216  -0.0507 339 VAL B C   
2636  O O   . VAL A 323 ? 2.4553 1.7718 2.0061 0.2515  0.1312  -0.0426 339 VAL B O   
2637  C CB  . VAL A 323 ? 2.5876 1.8559 2.0949 0.2329  0.1109  -0.0756 339 VAL B CB  
2638  C CG1 . VAL A 323 ? 2.5262 1.8028 2.0199 0.2374  0.1101  -0.0801 339 VAL B CG1 
2639  C CG2 . VAL A 323 ? 2.5646 1.7986 2.0504 0.2333  0.1119  -0.0863 339 VAL B CG2 
2640  N N   . GLN A 324 ? 2.8158 2.1453 2.3754 0.2282  0.1102  -0.0507 340 GLN B N   
2641  C CA  . GLN A 324 ? 2.7011 2.0619 2.2799 0.2256  0.1083  -0.0416 340 GLN B CA  
2642  C C   . GLN A 324 ? 2.6938 2.0682 2.2990 0.2231  0.1115  -0.0285 340 GLN B C   
2643  O O   . GLN A 324 ? 2.7257 2.0945 2.3386 0.2157  0.1076  -0.0285 340 GLN B O   
2644  C CB  . GLN A 324 ? 2.5753 1.9514 2.1541 0.2134  0.0948  -0.0482 340 GLN B CB  
2645  C CG  . GLN A 324 ? 2.6895 2.0584 2.2689 0.2011  0.0848  -0.0545 340 GLN B CG  
2646  C CD  . GLN A 324 ? 2.5512 1.9376 2.1324 0.1893  0.0717  -0.0598 340 GLN B CD  
2647  O OE1 . GLN A 324 ? 2.3396 1.7513 1.9352 0.1866  0.0692  -0.0539 340 GLN B OE1 
2648  N NE2 . GLN A 324 ? 2.5693 1.9421 2.1359 0.1820  0.0632  -0.0708 340 GLN B NE2 
2649  N N   . LYS A 325 ? 2.2658 1.6585 1.8851 0.2289  0.1184  -0.0171 341 LYS B N   
2650  C CA  . LYS A 325 ? 2.0972 1.5054 1.7419 0.2269  0.1220  -0.0035 341 LYS B CA  
2651  C C   . LYS A 325 ? 2.0163 1.4545 1.6798 0.2157  0.1134  0.0011  341 LYS B C   
2652  O O   . LYS A 325 ? 1.9623 1.4134 1.6218 0.2147  0.1097  -0.0017 341 LYS B O   
2653  C CB  . LYS A 325 ? 2.0053 1.4148 1.6544 0.2401  0.1356  0.0075  341 LYS B CB  
2654  C CG  . LYS A 325 ? 2.0044 1.3847 1.6367 0.2526  0.1458  0.0047  341 LYS B CG  
2655  C CD  . LYS A 325 ? 2.0689 1.4281 1.6981 0.2480  0.1433  -0.0005 341 LYS B CD  
2656  C CE  . LYS A 325 ? 1.9148 1.2503 1.5374 0.2602  0.1556  0.0025  341 LYS B CE  
2657  N NZ  . LYS A 325 ? 1.7580 1.1088 1.4044 0.2638  0.1635  0.0189  341 LYS B NZ  
2658  N N   . ALA A 326 ? 1.9913 1.4404 1.6752 0.2076  0.1107  0.0083  342 ALA B N   
2659  C CA  . ALA A 326 ? 1.8657 1.3415 1.5676 0.1954  0.1017  0.0118  342 ALA B CA  
2660  C C   . ALA A 326 ? 1.8460 1.3405 1.5731 0.1945  0.1070  0.0269  342 ALA B C   
2661  O O   . ALA A 326 ? 1.9233 1.4108 1.6539 0.2036  0.1174  0.0351  342 ALA B O   
2662  C CB  . ALA A 326 ? 1.8896 1.3610 1.5906 0.1833  0.0903  0.0036  342 ALA B CB  
2663  N N   . VAL A 327 ? 1.7856 1.3047 1.5300 0.1835  0.0996  0.0309  343 VAL B N   
2664  C CA  . VAL A 327 ? 1.7662 1.3069 1.5352 0.1801  0.1027  0.0449  343 VAL B CA  
2665  C C   . VAL A 327 ? 1.8161 1.3608 1.5984 0.1687  0.0954  0.0458  343 VAL B C   
2666  O O   . VAL A 327 ? 1.7268 1.2880 1.5165 0.1575  0.0857  0.0432  343 VAL B O   
2667  C CB  . VAL A 327 ? 1.5952 1.1626 1.3738 0.1765  0.1007  0.0495  343 VAL B CB  
2668  C CG1 . VAL A 327 ? 1.5137 1.1036 1.3177 0.1714  0.1031  0.0636  343 VAL B CG1 
2669  C CG2 . VAL A 327 ? 1.5435 1.1075 1.3100 0.1874  0.1079  0.0495  343 VAL B CG2 
2670  N N   . CYS A 328 ? 1.8324 1.3631 1.6186 0.1717  0.1004  0.0501  344 CYS B N   
2671  C CA  . CYS A 328 ? 1.7930 1.3210 1.5872 0.1616  0.0932  0.0486  344 CYS B CA  
2672  C C   . CYS A 328 ? 1.7300 1.2855 1.5489 0.1511  0.0889  0.0583  344 CYS B C   
2673  O O   . CYS A 328 ? 1.7226 1.2757 1.5505 0.1441  0.0849  0.0596  344 CYS B O   
2674  C CB  . CYS A 328 ? 1.8802 1.3837 1.6711 0.1683  0.1004  0.0506  344 CYS B CB  
2675  S SG  . CYS A 328 ? 2.5608 2.0279 2.3199 0.1755  0.1008  0.0347  344 CYS B SG  
2676  N N   . HIS A 329 ? 1.5283 1.1090 1.3583 0.1490  0.0891  0.0646  345 HIS B N   
2677  C CA  . HIS A 329 ? 1.4421 1.0489 1.2951 0.1380  0.0845  0.0732  345 HIS B CA  
2678  C C   . HIS A 329 ? 1.3982 1.0132 1.2511 0.1256  0.0716  0.0644  345 HIS B C   
2679  O O   . HIS A 329 ? 1.4057 1.0248 1.2481 0.1243  0.0667  0.0563  345 HIS B O   
2680  C CB  . HIS A 329 ? 1.4454 1.0761 1.3095 0.1390  0.0887  0.0824  345 HIS B CB  
2681  C CG  . HIS A 329 ? 1.4623 1.1198 1.3499 0.1278  0.0847  0.0917  345 HIS B CG  
2682  N ND1 . HIS A 329 ? 1.4503 1.1273 1.3432 0.1171  0.0755  0.0881  345 HIS B ND1 
2683  C CD2 . HIS A 329 ? 1.4231 1.0913 1.3301 0.1255  0.0886  0.1045  345 HIS B CD2 
2684  C CE1 . HIS A 329 ? 1.3851 1.0834 1.2991 0.1086  0.0740  0.0979  345 HIS B CE1 
2685  N NE2 . HIS A 329 ? 1.3795 1.0735 1.3027 0.1133  0.0817  0.1081  345 HIS B NE2 
2686  N N   . PRO A 330 ? 1.4105 1.0296 1.2756 0.1162  0.0658  0.0664  346 PRO B N   
2687  C CA  . PRO A 330 ? 1.3829 1.0104 1.2483 0.1041  0.0533  0.0585  346 PRO B CA  
2688  C C   . PRO A 330 ? 1.3574 1.0132 1.2324 0.0972  0.0486  0.0603  346 PRO B C   
2689  O O   . PRO A 330 ? 1.3325 1.0094 1.2262 0.0936  0.0509  0.0711  346 PRO B O   
2690  C CB  . PRO A 330 ? 1.3351 0.9629 1.2149 0.0966  0.0503  0.0636  346 PRO B CB  
2691  C CG  . PRO A 330 ? 1.3517 0.9600 1.2301 0.1068  0.0608  0.0695  346 PRO B CG  
2692  C CD  . PRO A 330 ? 1.3976 1.0112 1.2752 0.1169  0.0706  0.0757  346 PRO B CD  
2693  N N   . THR A 331 ? 1.2508 0.9065 1.1126 0.0951  0.0418  0.0494  347 THR B N   
2694  C CA  . THR A 331 ? 1.2133 0.8907 1.0784 0.0911  0.0382  0.0487  347 THR B CA  
2695  C C   . THR A 331 ? 1.1909 0.8716 1.0494 0.0827  0.0266  0.0382  347 THR B C   
2696  O O   . THR A 331 ? 1.2352 0.8969 1.0783 0.0837  0.0228  0.0289  347 THR B O   
2697  C CB  . THR A 331 ? 1.2296 0.9016 1.0818 0.1018  0.0452  0.0471  347 THR B CB  
2698  O OG1 . THR A 331 ? 1.2638 0.9098 1.0945 0.1093  0.0461  0.0376  347 THR B OG1 
2699  C CG2 . THR A 331 ? 1.2826 0.9583 1.1444 0.1088  0.0562  0.0592  347 THR B CG2 
2700  N N   . ALA A 332 ? 1.1852 0.8903 1.0550 0.0743  0.0211  0.0397  348 ALA B N   
2701  C CA  . ALA A 332 ? 1.1387 0.8508 1.0051 0.0657  0.0101  0.0312  348 ALA B CA  
2702  C C   . ALA A 332 ? 1.1239 0.8469 0.9836 0.0671  0.0086  0.0268  348 ALA B C   
2703  O O   . ALA A 332 ? 1.0557 0.8006 0.9278 0.0627  0.0083  0.0316  348 ALA B O   
2704  C CB  . ALA A 332 ? 1.0821 0.8133 0.9678 0.0536  0.0037  0.0363  348 ALA B CB  
2705  N N   . TRP A 333 ? 1.0775 0.7849 0.9174 0.0727  0.0073  0.0172  349 TRP B N   
2706  C CA  . TRP A 333 ? 1.0400 0.7525 0.8704 0.0769  0.0077  0.0129  349 TRP B CA  
2707  C C   . TRP A 333 ? 1.0440 0.7709 0.8751 0.0684  -0.0024 0.0070  349 TRP B C   
2708  O O   . TRP A 333 ? 1.0877 0.8072 0.9113 0.0644  -0.0098 -0.0001 349 TRP B O   
2709  C CB  . TRP A 333 ? 1.0710 0.7603 0.8796 0.0870  0.0110  0.0056  349 TRP B CB  
2710  C CG  . TRP A 333 ? 1.0880 0.7651 0.8949 0.0965  0.0215  0.0114  349 TRP B CG  
2711  C CD1 . TRP A 333 ? 1.1489 0.8174 0.9629 0.0977  0.0262  0.0174  349 TRP B CD1 
2712  C CD2 . TRP A 333 ? 1.0685 0.7422 0.8673 0.1065  0.0294  0.0128  349 TRP B CD2 
2713  N NE1 . TRP A 333 ? 1.1574 0.8170 0.9677 0.1083  0.0367  0.0224  349 TRP B NE1 
2714  C CE2 . TRP A 333 ? 1.1079 0.7708 0.9089 0.1136  0.0387  0.0197  349 TRP B CE2 
2715  C CE3 . TRP A 333 ? 1.1105 0.7892 0.9005 0.1103  0.0295  0.0091  349 TRP B CE3 
2716  C CZ2 . TRP A 333 ? 1.1942 0.8519 0.9889 0.1242  0.0478  0.0230  349 TRP B CZ2 
2717  C CZ3 . TRP A 333 ? 1.1635 0.8364 0.9470 0.1205  0.0384  0.0123  349 TRP B CZ3 
2718  C CH2 . TRP A 333 ? 1.2272 0.8901 1.0131 0.1273  0.0474  0.0192  349 TRP B CH2 
2719  N N   . ASP A 334 ? 0.9159 0.6626 0.7552 0.0661  -0.0024 0.0098  350 ASP B N   
2720  C CA  . ASP A 334 ? 0.9032 0.6638 0.7417 0.0602  -0.0105 0.0043  350 ASP B CA  
2721  C C   . ASP A 334 ? 0.9833 0.7417 0.8089 0.0679  -0.0076 0.0001  350 ASP B C   
2722  O O   . ASP A 334 ? 1.0137 0.7852 0.8457 0.0686  -0.0039 0.0042  350 ASP B O   
2723  C CB  . ASP A 334 ? 0.9225 0.7070 0.7805 0.0512  -0.0127 0.0105  350 ASP B CB  
2724  C CG  . ASP A 334 ? 1.0375 0.8377 0.8960 0.0454  -0.0202 0.0057  350 ASP B CG  
2725  O OD1 . ASP A 334 ? 1.0660 0.8597 0.9101 0.0485  -0.0237 -0.0023 350 ASP B OD1 
2726  O OD2 . ASP A 334 ? 1.0563 0.8763 0.9304 0.0375  -0.0224 0.0103  350 ASP B OD2 
2727  N N   . LEU A 335 ? 0.9934 0.7355 0.8004 0.0731  -0.0096 -0.0082 351 LEU B N   
2728  C CA  . LEU A 335 ? 1.0162 0.7543 0.8099 0.0814  -0.0062 -0.0118 351 LEU B CA  
2729  C C   . LEU A 335 ? 1.0358 0.7899 0.8299 0.0776  -0.0121 -0.0154 351 LEU B C   
2730  O O   . LEU A 335 ? 1.0094 0.7646 0.7963 0.0836  -0.0089 -0.0166 351 LEU B O   
2731  C CB  . LEU A 335 ? 0.9977 0.7134 0.7710 0.0882  -0.0062 -0.0192 351 LEU B CB  
2732  C CG  . LEU A 335 ? 1.0151 0.7101 0.7821 0.0948  0.0005  -0.0176 351 LEU B CG  
2733  C CD1 . LEU A 335 ? 1.0654 0.7532 0.8363 0.0881  -0.0042 -0.0185 351 LEU B CD1 
2734  C CD2 . LEU A 335 ? 1.0786 0.7552 0.8243 0.1042  0.0033  -0.0241 351 LEU B CD2 
2735  N N   . GLY A 336 ? 0.9783 0.7447 0.7804 0.0680  -0.0205 -0.0170 352 GLY B N   
2736  C CA  . GLY A 336 ? 0.9795 0.7614 0.7823 0.0645  -0.0261 -0.0203 352 GLY B CA  
2737  C C   . GLY A 336 ? 0.9746 0.7498 0.7626 0.0648  -0.0333 -0.0290 352 GLY B C   
2738  O O   . GLY A 336 ? 0.9662 0.7234 0.7413 0.0680  -0.0339 -0.0333 352 GLY B O   
2739  N N   . LYS A 337 ? 1.0284 0.8190 0.8185 0.0613  -0.0386 -0.0314 353 LYS B N   
2740  C CA  . LYS A 337 ? 1.0171 0.8072 0.7960 0.0600  -0.0465 -0.0386 353 LYS B CA  
2741  C C   . LYS A 337 ? 0.9351 0.7140 0.7094 0.0551  -0.0524 -0.0419 353 LYS B C   
2742  O O   . LYS A 337 ? 0.9610 0.7253 0.7192 0.0585  -0.0544 -0.0477 353 LYS B O   
2743  C CB  . LYS A 337 ? 0.9519 0.7324 0.7141 0.0696  -0.0434 -0.0427 353 LYS B CB  
2744  C CG  . LYS A 337 ? 0.9921 0.7786 0.7593 0.0751  -0.0353 -0.0380 353 LYS B CG  
2745  C CD  . LYS A 337 ? 0.9291 0.7126 0.6842 0.0837  -0.0321 -0.0405 353 LYS B CD  
2746  C CE  . LYS A 337 ? 0.8751 0.6772 0.6361 0.0808  -0.0357 -0.0409 353 LYS B CE  
2747  N NZ  . LYS A 337 ? 0.9154 0.7170 0.6691 0.0890  -0.0306 -0.0411 353 LYS B NZ  
2748  N N   . GLY A 338 ? 0.9462 0.7313 0.7345 0.0472  -0.0548 -0.0380 354 GLY B N   
2749  C CA  . GLY A 338 ? 0.9090 0.6852 0.6955 0.0411  -0.0608 -0.0403 354 GLY B CA  
2750  C C   . GLY A 338 ? 0.9065 0.6598 0.6861 0.0454  -0.0556 -0.0401 354 GLY B C   
2751  O O   . GLY A 338 ? 0.9139 0.6580 0.6921 0.0403  -0.0601 -0.0419 354 GLY B O   
2752  N N   . ASP A 339 ? 0.9040 0.6477 0.6793 0.0546  -0.0462 -0.0378 355 ASP B N   
2753  C CA  . ASP A 339 ? 0.9763 0.6970 0.7423 0.0602  -0.0409 -0.0384 355 ASP B CA  
2754  C C   . ASP A 339 ? 1.0467 0.7683 0.8284 0.0587  -0.0354 -0.0300 355 ASP B C   
2755  O O   . ASP A 339 ? 1.0009 0.7303 0.7914 0.0625  -0.0282 -0.0236 355 ASP B O   
2756  C CB  . ASP A 339 ? 1.0023 0.7118 0.7538 0.0715  -0.0339 -0.0407 355 ASP B CB  
2757  C CG  . ASP A 339 ? 1.0399 0.7251 0.7797 0.0780  -0.0284 -0.0421 355 ASP B CG  
2758  O OD1 . ASP A 339 ? 1.0990 0.7757 0.8435 0.0743  -0.0288 -0.0405 355 ASP B OD1 
2759  O OD2 . ASP A 339 ? 1.0282 0.7027 0.7540 0.0872  -0.0234 -0.0448 355 ASP B OD2 
2760  N N   . PHE A 340 ? 1.0666 0.7804 0.8517 0.0531  -0.0387 -0.0298 356 PHE B N   
2761  C CA  . PHE A 340 ? 0.9739 0.6871 0.7734 0.0516  -0.0338 -0.0218 356 PHE B CA  
2762  C C   . PHE A 340 ? 1.0498 0.7369 0.8388 0.0563  -0.0299 -0.0235 356 PHE B C   
2763  O O   . PHE A 340 ? 1.1304 0.8042 0.9083 0.0533  -0.0358 -0.0302 356 PHE B O   
2764  C CB  . PHE A 340 ? 0.9541 0.6835 0.7705 0.0398  -0.0410 -0.0183 356 PHE B CB  
2765  C CG  . PHE A 340 ? 0.9252 0.6801 0.7515 0.0342  -0.0457 -0.0173 356 PHE B CG  
2766  C CD1 . PHE A 340 ? 0.9546 0.7269 0.7963 0.0335  -0.0411 -0.0097 356 PHE B CD1 
2767  C CD2 . PHE A 340 ? 0.9569 0.7183 0.7771 0.0295  -0.0546 -0.0238 356 PHE B CD2 
2768  C CE1 . PHE A 340 ? 0.9451 0.7396 0.7951 0.0283  -0.0451 -0.0093 356 PHE B CE1 
2769  C CE2 . PHE A 340 ? 0.9650 0.7492 0.7942 0.0249  -0.0584 -0.0228 356 PHE B CE2 
2770  C CZ  . PHE A 340 ? 0.9341 0.7343 0.7778 0.0244  -0.0536 -0.0159 356 PHE B CZ  
2771  N N   . ARG A 341 ? 1.0782 0.7584 0.8713 0.0634  -0.0201 -0.0171 357 ARG B N   
2772  C CA  . ARG A 341 ? 1.1082 0.7631 0.8913 0.0696  -0.0146 -0.0181 357 ARG B CA  
2773  C C   . ARG A 341 ? 1.1402 0.7968 0.9399 0.0695  -0.0083 -0.0079 357 ARG B C   
2774  O O   . ARG A 341 ? 1.1305 0.8072 0.9473 0.0669  -0.0062 0.0003  357 ARG B O   
2775  C CB  . ARG A 341 ? 1.1365 0.7769 0.9026 0.0817  -0.0071 -0.0213 357 ARG B CB  
2776  C CG  . ARG A 341 ? 1.1984 0.8371 0.9477 0.0825  -0.0127 -0.0308 357 ARG B CG  
2777  C CD  . ARG A 341 ? 1.2014 0.8275 0.9349 0.0944  -0.0052 -0.0333 357 ARG B CD  
2778  N NE  . ARG A 341 ? 1.2234 0.8559 0.9460 0.0948  -0.0101 -0.0399 357 ARG B NE  
2779  C CZ  . ARG A 341 ? 1.2589 0.8800 0.9639 0.1035  -0.0065 -0.0446 357 ARG B CZ  
2780  N NH1 . ARG A 341 ? 1.3429 0.9438 1.0373 0.1123  0.0013  -0.0450 357 ARG B NH1 
2781  N NH2 . ARG A 341 ? 1.2223 0.8527 0.9205 0.1037  -0.0108 -0.0490 357 ARG B NH2 
2782  N N   . ILE A 342 ? 1.2117 0.8469 1.0061 0.0721  -0.0054 -0.0083 358 ILE B N   
2783  C CA  . ILE A 342 ? 1.1958 0.8283 1.0034 0.0743  0.0021  0.0015  358 ILE B CA  
2784  C C   . ILE A 342 ? 1.2093 0.8162 1.0015 0.0864  0.0113  -0.0003 358 ILE B C   
2785  O O   . ILE A 342 ? 1.2744 0.8616 1.0468 0.0892  0.0093  -0.0100 358 ILE B O   
2786  C CB  . ILE A 342 ? 1.1589 0.7903 0.9773 0.0649  -0.0034 0.0036  358 ILE B CB  
2787  C CG1 . ILE A 342 ? 1.1197 0.7795 0.9576 0.0536  -0.0105 0.0084  358 ILE B CG1 
2788  C CG2 . ILE A 342 ? 1.1473 0.7699 0.9752 0.0695  0.0054  0.0127  358 ILE B CG2 
2789  C CD1 . ILE A 342 ? 1.1221 0.7823 0.9711 0.0439  -0.0164 0.0109  358 ILE B CD1 
2790  N N   . LEU A 343 ? 1.2298 0.8375 1.0304 0.0936  0.0215  0.0089  359 LEU B N   
2791  C CA  . LEU A 343 ? 1.3023 0.8870 1.0896 0.1059  0.0313  0.0085  359 LEU B CA  
2792  C C   . LEU A 343 ? 1.3729 0.9523 1.1733 0.1079  0.0383  0.0184  359 LEU B C   
2793  O O   . LEU A 343 ? 1.3812 0.9788 1.1999 0.1073  0.0425  0.0294  359 LEU B O   
2794  C CB  . LEU A 343 ? 1.2932 0.8842 1.0757 0.1148  0.0381  0.0104  359 LEU B CB  
2795  C CG  . LEU A 343 ? 1.3173 0.8869 1.0820 0.1282  0.0472  0.0078  359 LEU B CG  
2796  C CD1 . LEU A 343 ? 1.3332 0.9165 1.0987 0.1339  0.0521  0.0115  359 LEU B CD1 
2797  C CD2 . LEU A 343 ? 1.3571 0.9137 1.1267 0.1346  0.0565  0.0152  359 LEU B CD2 
2798  N N   . MET A 344 ? 1.3738 0.9280 1.1644 0.1104  0.0398  0.0145  360 MET B N   
2799  C CA  . MET A 344 ? 1.4454 0.9920 1.2475 0.1121  0.0459  0.0232  360 MET B CA  
2800  C C   . MET A 344 ? 1.5969 1.1099 1.3805 0.1189  0.0498  0.0165  360 MET B C   
2801  O O   . MET A 344 ? 1.6387 1.1376 1.4073 0.1145  0.0424  0.0054  360 MET B O   
2802  C CB  . MET A 344 ? 1.3875 0.9474 1.2076 0.0994  0.0380  0.0273  360 MET B CB  
2803  C CG  . MET A 344 ? 1.4857 1.0420 1.3209 0.1013  0.0449  0.0384  360 MET B CG  
2804  S SD  . MET A 344 ? 1.4916 1.0628 1.3481 0.0865  0.0359  0.0437  360 MET B SD  
2805  C CE  . MET A 344 ? 1.3504 0.9508 1.2120 0.0757  0.0248  0.0398  360 MET B CE  
2806  N N   . CYS A 345 ? 1.6728 1.1731 1.4575 0.1292  0.0612  0.0233  361 CYS B N   
2807  C CA  . CYS A 345 ? 1.7748 1.2420 1.5419 0.1364  0.0662  0.0173  361 CYS B CA  
2808  C C   . CYS A 345 ? 1.7909 1.2502 1.5688 0.1302  0.0643  0.0210  361 CYS B C   
2809  O O   . CYS A 345 ? 1.8300 1.2867 1.6198 0.1353  0.0726  0.0313  361 CYS B O   
2810  C CB  . CYS A 345 ? 1.9395 1.3960 1.7012 0.1515  0.0798  0.0225  361 CYS B CB  
2811  S SG  . CYS A 345 ? 2.0453 1.5128 1.7964 0.1589  0.0827  0.0198  361 CYS B SG  
2812  N N   . THR A 346 ? 1.8514 1.3072 1.6250 0.1192  0.0531  0.0129  362 THR B N   
2813  C CA  . THR A 346 ? 1.9025 1.3587 1.6904 0.1101  0.0486  0.0172  362 THR B CA  
2814  C C   . THR A 346 ? 1.9014 1.3258 1.6806 0.1163  0.0555  0.0165  362 THR B C   
2815  O O   . THR A 346 ? 1.9519 1.3497 1.7079 0.1223  0.0577  0.0062  362 THR B O   
2816  C CB  . THR A 346 ? 1.8933 1.3549 1.6777 0.0964  0.0343  0.0083  362 THR B CB  
2817  O OG1 . THR A 346 ? 1.8770 1.3654 1.6661 0.0920  0.0286  0.0077  362 THR B OG1 
2818  C CG2 . THR A 346 ? 1.8504 1.3192 1.6536 0.0858  0.0290  0.0147  362 THR B CG2 
2819  N N   . LYS A 347 ? 1.8514 1.2784 1.6493 0.1150  0.0591  0.0273  363 LYS B N   
2820  C CA  . LYS A 347 ? 1.8547 1.2529 1.6477 0.1188  0.0643  0.0275  363 LYS B CA  
2821  C C   . LYS A 347 ? 1.8382 1.2397 1.6431 0.1051  0.0546  0.0285  363 LYS B C   
2822  O O   . LYS A 347 ? 1.8672 1.2975 1.6916 0.0955  0.0480  0.0348  363 LYS B O   
2823  C CB  . LYS A 347 ? 1.8136 1.2110 1.6189 0.1303  0.0781  0.0408  363 LYS B CB  
2824  C CG  . LYS A 347 ? 1.8258 1.2260 1.6235 0.1431  0.0875  0.0423  363 LYS B CG  
2825  C CD  . LYS A 347 ? 1.8256 1.2008 1.5939 0.1492  0.0880  0.0278  363 LYS B CD  
2826  C CE  . LYS A 347 ? 1.8974 1.2802 1.6601 0.1605  0.0961  0.0298  363 LYS B CE  
2827  N NZ  . LYS A 347 ? 1.9914 1.3529 1.7257 0.1662  0.0961  0.0158  363 LYS B NZ  
2828  N N   . VAL A 348 ? 1.8257 1.1977 1.6187 0.1039  0.0537  0.0221  364 VAL B N   
2829  C CA  . VAL A 348 ? 1.8253 1.1990 1.6273 0.0901  0.0435  0.0218  364 VAL B CA  
2830  C C   . VAL A 348 ? 1.7860 1.1693 1.6136 0.0900  0.0488  0.0373  364 VAL B C   
2831  O O   . VAL A 348 ? 1.7901 1.1503 1.6172 0.0922  0.0532  0.0393  364 VAL B O   
2832  C CB  . VAL A 348 ? 1.8520 1.1908 1.6313 0.0875  0.0397  0.0090  364 VAL B CB  
2833  C CG1 . VAL A 348 ? 1.8766 1.2196 1.6649 0.0719  0.0277  0.0083  364 VAL B CG1 
2834  C CG2 . VAL A 348 ? 1.8057 1.1339 1.5586 0.0897  0.0365  -0.0055 364 VAL B CG2 
2835  N N   . THR A 349 ? 1.7738 1.1913 1.6238 0.0875  0.0486  0.0484  365 THR B N   
2836  C CA  . THR A 349 ? 1.6737 1.1060 1.5492 0.0888  0.0549  0.0648  365 THR B CA  
2837  C C   . THR A 349 ? 1.5920 1.0576 1.4901 0.0746  0.0448  0.0713  365 THR B C   
2838  O O   . THR A 349 ? 1.6276 1.1033 1.5215 0.0643  0.0332  0.0632  365 THR B O   
2839  C CB  . THR A 349 ? 1.6195 1.0620 1.5003 0.1014  0.0670  0.0738  365 THR B CB  
2840  O OG1 . THR A 349 ? 1.5819 1.0559 1.4701 0.0971  0.0623  0.0750  365 THR B OG1 
2841  C CG2 . THR A 349 ? 1.6196 1.0331 1.4756 0.1149  0.0756  0.0653  365 THR B CG2 
2842  N N   . MET A 350 ? 1.5213 1.0046 1.4437 0.0740  0.0492  0.0864  366 MET B N   
2843  C CA  . MET A 350 ? 1.4657 0.9821 1.4093 0.0608  0.0399  0.0927  366 MET B CA  
2844  C C   . MET A 350 ? 1.4704 1.0173 1.4225 0.0617  0.0410  0.0972  366 MET B C   
2845  O O   . MET A 350 ? 1.4412 1.0113 1.3983 0.0517  0.0315  0.0944  366 MET B O   
2846  C CB  . MET A 350 ? 1.4992 1.0222 1.4659 0.0574  0.0423  0.1067  366 MET B CB  
2847  C CG  . MET A 350 ? 1.4603 1.0191 1.4496 0.0438  0.0332  0.1138  366 MET B CG  
2848  S SD  . MET A 350 ? 1.4700 1.0408 1.4880 0.0385  0.0350  0.1310  366 MET B SD  
2849  C CE  . MET A 350 ? 1.2699 0.8829 1.3074 0.0219  0.0223  0.1345  366 MET B CE  
2850  N N   . ASP A 351 ? 1.5701 1.1161 1.5229 0.0738  0.0528  0.1040  367 ASP B N   
2851  C CA  . ASP A 351 ? 1.6042 1.1766 1.5635 0.0757  0.0551  0.1085  367 ASP B CA  
2852  C C   . ASP A 351 ? 1.5344 1.1082 1.4759 0.0737  0.0481  0.0949  367 ASP B C   
2853  O O   . ASP A 351 ? 1.4753 1.0761 1.4248 0.0669  0.0425  0.0956  367 ASP B O   
2854  C CB  . ASP A 351 ? 1.6876 1.2529 1.6466 0.0903  0.0693  0.1167  367 ASP B CB  
2855  C CG  . ASP A 351 ? 1.7541 1.3347 1.7380 0.0907  0.0757  0.1343  367 ASP B CG  
2856  O OD1 . ASP A 351 ? 1.6812 1.2821 1.6838 0.0792  0.0689  0.1406  367 ASP B OD1 
2857  O OD2 . ASP A 351 ? 1.8550 1.4270 1.8396 0.1027  0.0876  0.1420  367 ASP B OD2 
2858  N N   . ASP A 352 ? 1.5746 1.1195 1.4918 0.0790  0.0482  0.0822  368 ASP B N   
2859  C CA  . ASP A 352 ? 1.6185 1.1645 1.5185 0.0774  0.0417  0.0695  368 ASP B CA  
2860  C C   . ASP A 352 ? 1.5728 1.1304 1.4751 0.0628  0.0275  0.0630  368 ASP B C   
2861  O O   . ASP A 352 ? 1.5641 1.1373 1.4625 0.0588  0.0214  0.0573  368 ASP B O   
2862  C CB  . ASP A 352 ? 1.7197 1.2323 1.5927 0.0874  0.0460  0.0581  368 ASP B CB  
2863  C CG  . ASP A 352 ? 1.7432 1.2494 1.6110 0.1024  0.0593  0.0627  368 ASP B CG  
2864  O OD1 . ASP A 352 ? 1.7245 1.2482 1.6108 0.1053  0.0660  0.0761  368 ASP B OD1 
2865  O OD2 . ASP A 352 ? 1.7580 1.2426 1.6033 0.1109  0.0628  0.0532  368 ASP B OD2 
2866  N N   . PHE A 353 ? 1.4487 0.9996 1.3576 0.0549  0.0224  0.0640  369 PHE B N   
2867  C CA  . PHE A 353 ? 1.3981 0.9631 1.3116 0.0406  0.0090  0.0595  369 PHE B CA  
2868  C C   . PHE A 353 ? 1.3663 0.9692 1.3009 0.0336  0.0056  0.0679  369 PHE B C   
2869  O O   . PHE A 353 ? 1.3194 0.9391 1.2516 0.0273  -0.0024 0.0621  369 PHE B O   
2870  C CB  . PHE A 353 ? 1.3722 0.9231 1.2911 0.0343  0.0056  0.0614  369 PHE B CB  
2871  C CG  . PHE A 353 ? 1.2985 0.8671 1.2280 0.0190  -0.0074 0.0606  369 PHE B CG  
2872  C CD1 . PHE A 353 ? 1.2943 0.8530 1.2080 0.0119  -0.0177 0.0481  369 PHE B CD1 
2873  C CD2 . PHE A 353 ? 1.2614 0.8560 1.2164 0.0115  -0.0093 0.0726  369 PHE B CD2 
2874  C CE1 . PHE A 353 ? 1.2601 0.8345 1.1834 -0.0020 -0.0295 0.0477  369 PHE B CE1 
2875  C CE2 . PHE A 353 ? 1.2470 0.8575 1.2114 -0.0023 -0.0210 0.0720  369 PHE B CE2 
2876  C CZ  . PHE A 353 ? 1.2335 0.8338 1.1821 -0.0089 -0.0311 0.0596  369 PHE B CZ  
2877  N N   . LEU A 354 ? 1.4096 1.0262 1.3646 0.0351  0.0122  0.0819  370 LEU B N   
2878  C CA  . LEU A 354 ? 1.3137 0.9658 1.2888 0.0285  0.0099  0.0906  370 LEU B CA  
2879  C C   . LEU A 354 ? 1.2844 0.9485 1.2524 0.0334  0.0123  0.0873  370 LEU B C   
2880  O O   . LEU A 354 ? 1.2942 0.9829 1.2685 0.0259  0.0058  0.0864  370 LEU B O   
2881  C CB  . LEU A 354 ? 1.2784 0.9408 1.2752 0.0301  0.0174  0.1064  370 LEU B CB  
2882  C CG  . LEU A 354 ? 1.2667 0.9196 1.2727 0.0241  0.0144  0.1104  370 LEU B CG  
2883  C CD1 . LEU A 354 ? 1.2387 0.9055 1.2682 0.0243  0.0208  0.1270  370 LEU B CD1 
2884  C CD2 . LEU A 354 ? 1.2626 0.9272 1.2719 0.0099  0.0008  0.1049  370 LEU B CD2 
2885  N N   . THR A 355 ? 1.3358 0.9817 1.2893 0.0461  0.0213  0.0849  371 THR B N   
2886  C CA  . THR A 355 ? 1.3259 0.9812 1.2715 0.0512  0.0238  0.0817  371 THR B CA  
2887  C C   . THR A 355 ? 1.2982 0.9528 1.2283 0.0466  0.0142  0.0680  371 THR B C   
2888  O O   . THR A 355 ? 1.2126 0.8860 1.1433 0.0447  0.0118  0.0664  371 THR B O   
2889  C CB  . THR A 355 ? 1.3034 0.9382 1.2366 0.0659  0.0355  0.0821  371 THR B CB  
2890  O OG1 . THR A 355 ? 1.3087 0.9487 1.2582 0.0702  0.0446  0.0963  371 THR B OG1 
2891  C CG2 . THR A 355 ? 1.2597 0.9033 1.1841 0.0710  0.0378  0.0787  371 THR B CG2 
2892  N N   . ALA A 356 ? 1.3244 0.9572 1.2400 0.0446  0.0088  0.0582  372 ALA B N   
2893  C CA  . ALA A 356 ? 1.3575 0.9899 1.2581 0.0404  -0.0002 0.0458  372 ALA B CA  
2894  C C   . ALA A 356 ? 1.3082 0.9683 1.2230 0.0274  -0.0105 0.0470  372 ALA B C   
2895  O O   . ALA A 356 ? 1.3110 0.9843 1.2207 0.0251  -0.0154 0.0414  372 ALA B O   
2896  C CB  . ALA A 356 ? 1.4279 1.0306 1.3092 0.0407  -0.0037 0.0352  372 ALA B CB  
2897  N N   . HIS A 357 ? 1.1433 0.8127 1.0757 0.0191  -0.0137 0.0544  373 HIS B N   
2898  C CA  . HIS A 357 ? 1.0971 0.7962 1.0449 0.0073  -0.0223 0.0572  373 HIS B CA  
2899  C C   . HIS A 357 ? 1.0354 0.7596 0.9928 0.0089  -0.0185 0.0627  373 HIS B C   
2900  O O   . HIS A 357 ? 1.0314 0.7736 0.9888 0.0035  -0.0249 0.0585  373 HIS B O   
2901  C CB  . HIS A 357 ? 1.0858 0.7925 1.0525 -0.0013 -0.0253 0.0658  373 HIS B CB  
2902  C CG  . HIS A 357 ? 1.1077 0.7944 1.0660 -0.0062 -0.0320 0.0594  373 HIS B CG  
2903  N ND1 . HIS A 357 ? 1.1399 0.7945 1.0844 0.0010  -0.0270 0.0558  373 HIS B ND1 
2904  C CD2 . HIS A 357 ? 1.0861 0.7806 1.0484 -0.0181 -0.0432 0.0564  373 HIS B CD2 
2905  C CE1 . HIS A 357 ? 1.1656 0.8083 1.1051 -0.0066 -0.0351 0.0504  373 HIS B CE1 
2906  N NE2 . HIS A 357 ? 1.1170 0.7838 1.0674 -0.0182 -0.0451 0.0510  373 HIS B NE2 
2907  N N   . HIS A 358 ? 1.0678 0.7931 1.0326 0.0165  -0.0081 0.0720  374 HIS B N   
2908  C CA  . HIS A 358 ? 1.0641 0.8116 1.0369 0.0182  -0.0037 0.0775  374 HIS B CA  
2909  C C   . HIS A 358 ? 1.0312 0.7768 0.9868 0.0227  -0.0048 0.0675  374 HIS B C   
2910  O O   . HIS A 358 ? 0.9901 0.7570 0.9499 0.0174  -0.0091 0.0662  374 HIS B O   
2911  C CB  . HIS A 358 ? 1.0628 0.8067 1.0430 0.0269  0.0082  0.0886  374 HIS B CB  
2912  C CG  . HIS A 358 ? 0.9857 0.7515 0.9751 0.0286  0.0135  0.0959  374 HIS B CG  
2913  N ND1 . HIS A 358 ? 0.9896 0.7770 1.0004 0.0241  0.0164  0.1090  374 HIS B ND1 
2914  C CD2 . HIS A 358 ? 1.0340 0.8013 1.0133 0.0350  0.0174  0.0926  374 HIS B CD2 
2915  C CE1 . HIS A 358 ? 1.0413 0.8434 1.0546 0.0267  0.0211  0.1128  374 HIS B CE1 
2916  N NE2 . HIS A 358 ? 1.0080 0.7980 1.0026 0.0334  0.0219  0.1031  374 HIS B NE2 
2917  N N   . GLU A 359 ? 1.0116 0.7322 0.9479 0.0326  -0.0004 0.0608  375 GLU B N   
2918  C CA  . GLU A 359 ? 1.0090 0.7280 0.9297 0.0380  -0.0001 0.0527  375 GLU B CA  
2919  C C   . GLU A 359 ? 1.0190 0.7425 0.9315 0.0305  -0.0113 0.0422  375 GLU B C   
2920  O O   . GLU A 359 ? 0.9569 0.6935 0.8660 0.0299  -0.0137 0.0385  375 GLU B O   
2921  C CB  . GLU A 359 ? 1.0286 0.7202 0.9314 0.0508  0.0082  0.0491  375 GLU B CB  
2922  C CG  . GLU A 359 ? 1.0122 0.7032 0.9230 0.0598  0.0205  0.0603  375 GLU B CG  
2923  C CD  . GLU A 359 ? 1.1165 0.8331 1.0392 0.0595  0.0241  0.0680  375 GLU B CD  
2924  O OE1 . GLU A 359 ? 1.1712 0.8950 1.0857 0.0595  0.0212  0.0617  375 GLU B OE1 
2925  O OE2 . GLU A 359 ? 1.1103 0.8404 1.0503 0.0589  0.0296  0.0802  375 GLU B OE2 
2926  N N   . MET A 360 ? 1.0177 0.7321 0.9282 0.0241  -0.0185 0.0381  376 MET B N   
2927  C CA  . MET A 360 ? 0.9974 0.7197 0.9026 0.0161  -0.0295 0.0297  376 MET B CA  
2928  C C   . MET A 360 ? 0.9560 0.7098 0.8795 0.0067  -0.0344 0.0349  376 MET B C   
2929  O O   . MET A 360 ? 0.9578 0.7238 0.8777 0.0025  -0.0411 0.0291  376 MET B O   
2930  C CB  . MET A 360 ? 1.0537 0.7590 0.9526 0.0108  -0.0361 0.0246  376 MET B CB  
2931  C CG  . MET A 360 ? 1.1356 0.8447 1.0244 0.0041  -0.0471 0.0147  376 MET B CG  
2932  S SD  . MET A 360 ? 1.0412 0.7264 0.9168 -0.0012 -0.0550 0.0065  376 MET B SD  
2933  C CE  . MET A 360 ? 1.1715 0.8223 1.0226 0.0121  -0.0465 -0.0004 376 MET B CE  
2934  N N   . GLY A 361 ? 1.0347 0.8026 0.9777 0.0034  -0.0311 0.0459  377 GLY B N   
2935  C CA  . GLY A 361 ? 1.0327 0.8309 0.9922 -0.0051 -0.0350 0.0507  377 GLY B CA  
2936  C C   . GLY A 361 ? 0.9412 0.7513 0.8979 -0.0006 -0.0309 0.0502  377 GLY B C   
2937  O O   . GLY A 361 ? 0.8927 0.7221 0.8531 -0.0063 -0.0361 0.0480  377 GLY B O   
2938  N N   . HIS A 362 ? 0.8940 0.6927 0.8444 0.0098  -0.0213 0.0525  378 HIS B N   
2939  C CA  . HIS A 362 ? 0.9411 0.7439 0.8829 0.0157  -0.0177 0.0493  378 HIS B CA  
2940  C C   . HIS A 362 ? 0.9625 0.7622 0.8889 0.0152  -0.0249 0.0376  378 HIS B C   
2941  O O   . HIS A 362 ? 0.9137 0.7304 0.8418 0.0123  -0.0276 0.0356  378 HIS B O   
2942  C CB  . HIS A 362 ? 0.9660 0.7507 0.8985 0.0279  -0.0072 0.0514  378 HIS B CB  
2943  C CG  . HIS A 362 ? 0.8927 0.6866 0.8401 0.0298  0.0012  0.0637  378 HIS B CG  
2944  N ND1 . HIS A 362 ? 0.8165 0.6363 0.7800 0.0234  0.0012  0.0709  378 HIS B ND1 
2945  C CD2 . HIS A 362 ? 0.9472 0.7285 0.8962 0.0370  0.0097  0.0705  378 HIS B CD2 
2946  C CE1 . HIS A 362 ? 0.9361 0.7594 0.9102 0.0264  0.0093  0.0817  378 HIS B CE1 
2947  N NE2 . HIS A 362 ? 0.9845 0.7850 0.9506 0.0349  0.0146  0.0820  378 HIS B NE2 
2948  N N   . ILE A 363 ? 1.0016 0.7789 0.9121 0.0184  -0.0274 0.0297  379 ILE B N   
2949  C CA  . ILE A 363 ? 0.9939 0.7677 0.8888 0.0185  -0.0339 0.0189  379 ILE B CA  
2950  C C   . ILE A 363 ? 0.9665 0.7617 0.8705 0.0074  -0.0438 0.0174  379 ILE B C   
2951  O O   . ILE A 363 ? 0.9790 0.7849 0.8783 0.0069  -0.0471 0.0127  379 ILE B O   
2952  C CB  . ILE A 363 ? 0.9726 0.7195 0.8496 0.0222  -0.0356 0.0111  379 ILE B CB  
2953  C CG1 . ILE A 363 ? 0.9723 0.6986 0.8389 0.0342  -0.0253 0.0120  379 ILE B CG1 
2954  C CG2 . ILE A 363 ? 0.9637 0.7094 0.8259 0.0210  -0.0432 0.0008  379 ILE B CG2 
2955  C CD1 . ILE A 363 ? 0.9777 0.7042 0.8328 0.0420  -0.0216 0.0082  379 ILE B CD1 
2956  N N   . GLN A 364 ? 0.9509 0.7518 0.8672 -0.0013 -0.0487 0.0212  380 GLN B N   
2957  C CA  . GLN A 364 ? 0.9150 0.7382 0.8424 -0.0122 -0.0576 0.0213  380 GLN B CA  
2958  C C   . GLN A 364 ? 0.8779 0.7254 0.8152 -0.0137 -0.0558 0.0249  380 GLN B C   
2959  O O   . GLN A 364 ? 0.8688 0.7294 0.8041 -0.0171 -0.0614 0.0202  380 GLN B O   
2960  C CB  . GLN A 364 ? 0.8849 0.7118 0.8274 -0.0203 -0.0605 0.0279  380 GLN B CB  
2961  C CG  . GLN A 364 ? 0.8448 0.6823 0.7921 -0.0312 -0.0717 0.0253  380 GLN B CG  
2962  C CD  . GLN A 364 ? 0.9270 0.7449 0.8571 -0.0312 -0.0778 0.0161  380 GLN B CD  
2963  O OE1 . GLN A 364 ? 0.9203 0.7465 0.8458 -0.0361 -0.0860 0.0103  380 GLN B OE1 
2964  N NE2 . GLN A 364 ? 0.9940 0.7859 0.9145 -0.0259 -0.0738 0.0147  380 GLN B NE2 
2965  N N   . TYR A 365 ? 0.8997 0.7536 0.8478 -0.0113 -0.0478 0.0334  381 TYR B N   
2966  C CA  . TYR A 365 ? 0.8787 0.7537 0.8349 -0.0125 -0.0451 0.0368  381 TYR B CA  
2967  C C   . TYR A 365 ? 0.9139 0.7844 0.8546 -0.0055 -0.0438 0.0293  381 TYR B C   
2968  O O   . TYR A 365 ? 0.9131 0.8004 0.8562 -0.0086 -0.0462 0.0276  381 TYR B O   
2969  C CB  . TYR A 365 ? 0.8212 0.7000 0.7886 -0.0099 -0.0360 0.0471  381 TYR B CB  
2970  C CG  . TYR A 365 ? 0.7947 0.6998 0.7774 -0.0157 -0.0344 0.0537  381 TYR B CG  
2971  C CD1 . TYR A 365 ? 0.8388 0.7619 0.8233 -0.0215 -0.0400 0.0497  381 TYR B CD1 
2972  C CD2 . TYR A 365 ? 0.7692 0.6807 0.7634 -0.0149 -0.0268 0.0639  381 TYR B CD2 
2973  C CE1 . TYR A 365 ? 0.8543 0.8008 0.8520 -0.0271 -0.0381 0.0554  381 TYR B CE1 
2974  C CE2 . TYR A 365 ? 0.7262 0.6617 0.7335 -0.0209 -0.0253 0.0699  381 TYR B CE2 
2975  C CZ  . TYR A 365 ? 0.7346 0.6871 0.7434 -0.0271 -0.0309 0.0654  381 TYR B CZ  
2976  O OH  . TYR A 365 ? 0.6079 0.5829 0.6285 -0.0331 -0.0292 0.0707  381 TYR B OH  
2977  N N   . ASP A 366 ? 0.9275 0.7755 0.8523 0.0042  -0.0394 0.0252  382 ASP B N   
2978  C CA  . ASP A 366 ? 0.9463 0.7888 0.8559 0.0116  -0.0374 0.0187  382 ASP B CA  
2979  C C   . ASP A 366 ? 0.9828 0.8296 0.8843 0.0081  -0.0465 0.0101  382 ASP B C   
2980  O O   . ASP A 366 ? 0.9424 0.7979 0.8396 0.0098  -0.0469 0.0068  382 ASP B O   
2981  C CB  . ASP A 366 ? 0.9952 0.8124 0.8901 0.0225  -0.0308 0.0168  382 ASP B CB  
2982  C CG  . ASP A 366 ? 1.0365 0.8518 0.9395 0.0272  -0.0208 0.0261  382 ASP B CG  
2983  O OD1 . ASP A 366 ? 1.0386 0.8730 0.9553 0.0232  -0.0187 0.0326  382 ASP B OD1 
2984  O OD2 . ASP A 366 ? 1.0289 0.8249 0.9250 0.0346  -0.0149 0.0273  382 ASP B OD2 
2985  N N   . MET A 367 ? 0.9661 0.8072 0.8658 0.0028  -0.0538 0.0068  383 MET B N   
2986  C CA  . MET A 367 ? 0.9048 0.7506 0.7973 -0.0012 -0.0629 -0.0006 383 MET B CA  
2987  C C   . MET A 367 ? 0.9049 0.7772 0.8118 -0.0099 -0.0680 0.0019  383 MET B C   
2988  O O   . MET A 367 ? 0.9586 0.8406 0.8609 -0.0105 -0.0721 -0.0028 383 MET B O   
2989  C CB  . MET A 367 ? 0.8969 0.7285 0.7836 -0.0049 -0.0691 -0.0042 383 MET B CB  
2990  C CG  . MET A 367 ? 0.9144 0.7188 0.7844 0.0038  -0.0646 -0.0082 383 MET B CG  
2991  S SD  . MET A 367 ? 0.9976 0.7836 0.8630 -0.0013 -0.0703 -0.0108 383 MET B SD  
2992  C CE  . MET A 367 ? 1.0058 0.8008 0.8638 -0.0086 -0.0828 -0.0188 383 MET B CE  
2993  N N   . ALA A 368 ? 1.0080 0.8927 0.9323 -0.0166 -0.0675 0.0095  384 ALA B N   
2994  C CA  . ALA A 368 ? 0.9906 0.9012 0.9292 -0.0254 -0.0723 0.0121  384 ALA B CA  
2995  C C   . ALA A 368 ? 0.9844 0.9076 0.9221 -0.0224 -0.0689 0.0111  384 ALA B C   
2996  O O   . ALA A 368 ? 1.0087 0.9453 0.9460 -0.0255 -0.0742 0.0073  384 ALA B O   
2997  C CB  . ALA A 368 ? 0.9735 0.8949 0.9308 -0.0321 -0.0708 0.0214  384 ALA B CB  
2998  N N   . TYR A 369 ? 0.8976 0.8163 0.8347 -0.0160 -0.0600 0.0145  385 TYR B N   
2999  C CA  . TYR A 369 ? 0.8520 0.7818 0.7885 -0.0135 -0.0564 0.0139  385 TYR B CA  
3000  C C   . TYR A 369 ? 0.9041 0.8201 0.8226 -0.0039 -0.0542 0.0071  385 TYR B C   
3001  O O   . TYR A 369 ? 0.8362 0.7556 0.7525 0.0005  -0.0487 0.0075  385 TYR B O   
3002  C CB  . TYR A 369 ? 0.8430 0.7791 0.7899 -0.0133 -0.0483 0.0221  385 TYR B CB  
3003  C CG  . TYR A 369 ? 0.8647 0.7825 0.8071 -0.0055 -0.0404 0.0257  385 TYR B CG  
3004  C CD1 . TYR A 369 ? 0.8795 0.7793 0.8055 0.0046  -0.0364 0.0209  385 TYR B CD1 
3005  C CD2 . TYR A 369 ? 0.8319 0.7518 0.7868 -0.0081 -0.0364 0.0345  385 TYR B CD2 
3006  C CE1 . TYR A 369 ? 0.8798 0.7637 0.8014 0.0120  -0.0289 0.0244  385 TYR B CE1 
3007  C CE2 . TYR A 369 ? 0.7821 0.6860 0.7330 -0.0004 -0.0286 0.0383  385 TYR B CE2 
3008  C CZ  . TYR A 369 ? 0.8253 0.7112 0.7592 0.0097  -0.0249 0.0330  385 TYR B CZ  
3009  O OH  . TYR A 369 ? 0.8508 0.7206 0.7795 0.0181  -0.0171 0.0363  385 TYR B OH  
3010  N N   . ALA A 370 ? 0.9877 0.8879 0.8930 -0.0007 -0.0581 0.0010  386 ALA B N   
3011  C CA  . ALA A 370 ? 0.8936 0.7817 0.7815 0.0081  -0.0567 -0.0055 386 ALA B CA  
3012  C C   . ALA A 370 ? 0.8581 0.7614 0.7450 0.0071  -0.0598 -0.0090 386 ALA B C   
3013  O O   . ALA A 370 ? 0.7286 0.6291 0.6074 0.0141  -0.0553 -0.0110 386 ALA B O   
3014  C CB  . ALA A 370 ? 0.8736 0.7438 0.7483 0.0099  -0.0613 -0.0112 386 ALA B CB  
3015  N N   . ALA A 371 ? 0.8331 0.7530 0.7288 -0.0015 -0.0673 -0.0094 387 ALA B N   
3016  C CA  . ALA A 371 ? 0.8113 0.7501 0.7108 -0.0042 -0.0701 -0.0110 387 ALA B CA  
3017  C C   . ALA A 371 ? 0.7866 0.7311 0.6881 -0.0002 -0.0625 -0.0088 387 ALA B C   
3018  O O   . ALA A 371 ? 0.7274 0.6756 0.6223 0.0038  -0.0620 -0.0125 387 ALA B O   
3019  C CB  . ALA A 371 ? 0.8338 0.7926 0.7492 -0.0153 -0.0761 -0.0077 387 ALA B CB  
3020  N N   . GLN A 372 ? 0.8483 0.7936 0.7589 -0.0014 -0.0565 -0.0024 388 GLN B N   
3021  C CA  . GLN A 372 ? 0.7338 0.6886 0.6504 -0.0010 -0.0500 0.0012  388 GLN B CA  
3022  C C   . GLN A 372 ? 0.7295 0.6719 0.6329 0.0091  -0.0436 -0.0014 388 GLN B C   
3023  O O   . GLN A 372 ? 0.7750 0.6991 0.6669 0.0162  -0.0418 -0.0034 388 GLN B O   
3024  C CB  . GLN A 372 ? 0.7117 0.6686 0.6403 -0.0048 -0.0455 0.0092  388 GLN B CB  
3025  C CG  . GLN A 372 ? 0.7056 0.6778 0.6496 -0.0154 -0.0508 0.0132  388 GLN B CG  
3026  C CD  . GLN A 372 ? 0.6732 0.6675 0.6264 -0.0221 -0.0529 0.0135  388 GLN B CD  
3027  O OE1 . GLN A 372 ? 0.5954 0.5936 0.5457 -0.0194 -0.0485 0.0125  388 GLN B OE1 
3028  N NE2 . GLN A 372 ? 0.6665 0.6753 0.6311 -0.0312 -0.0590 0.0154  388 GLN B NE2 
3029  N N   . PRO A 373 ? 0.6761 0.6275 0.5806 0.0099  -0.0401 -0.0013 389 PRO B N   
3030  C CA  . PRO A 373 ? 0.7266 0.6669 0.6200 0.0192  -0.0334 -0.0026 389 PRO B CA  
3031  C C   . PRO A 373 ? 0.7455 0.6729 0.6378 0.0234  -0.0264 0.0023  389 PRO B C   
3032  O O   . PRO A 373 ? 0.8075 0.7378 0.7102 0.0187  -0.0253 0.0080  389 PRO B O   
3033  C CB  . PRO A 373 ? 0.6562 0.6107 0.5549 0.0165  -0.0307 -0.0017 389 PRO B CB  
3034  C CG  . PRO A 373 ? 0.6476 0.6196 0.5612 0.0062  -0.0342 0.0015  389 PRO B CG  
3035  C CD  . PRO A 373 ? 0.6647 0.6366 0.5803 0.0024  -0.0418 0.0000  389 PRO B CD  
3036  N N   . PHE A 374 ? 0.7500 0.6636 0.6298 0.0328  -0.0215 0.0005  390 PHE B N   
3037  C CA  . PHE A 374 ? 0.7406 0.6384 0.6157 0.0388  -0.0160 0.0036  390 PHE B CA  
3038  C C   . PHE A 374 ? 0.7637 0.6675 0.6507 0.0355  -0.0099 0.0121  390 PHE B C   
3039  O O   . PHE A 374 ? 0.7391 0.6375 0.6307 0.0350  -0.0082 0.0167  390 PHE B O   
3040  C CB  . PHE A 374 ? 0.7834 0.6670 0.6427 0.0494  -0.0120 0.0000  390 PHE B CB  
3041  C CG  . PHE A 374 ? 0.7259 0.5937 0.5794 0.0565  -0.0055 0.0032  390 PHE B CG  
3042  C CD1 . PHE A 374 ? 0.7618 0.6145 0.6068 0.0604  -0.0072 0.0004  390 PHE B CD1 
3043  C CD2 . PHE A 374 ? 0.7671 0.6354 0.6239 0.0589  0.0024  0.0093  390 PHE B CD2 
3044  C CE1 . PHE A 374 ? 0.7850 0.6229 0.6243 0.0674  -0.0008 0.0034  390 PHE B CE1 
3045  C CE2 . PHE A 374 ? 0.8156 0.6701 0.6672 0.0658  0.0086  0.0127  390 PHE B CE2 
3046  C CZ  . PHE A 374 ? 0.8202 0.6593 0.6631 0.0704  0.0072  0.0097  390 PHE B CZ  
3047  N N   . LEU A 375 ? 0.7814 0.6966 0.6736 0.0330  -0.0065 0.0146  391 LEU B N   
3048  C CA  . LEU A 375 ? 0.7081 0.6289 0.6109 0.0297  -0.0007 0.0231  391 LEU B CA  
3049  C C   . LEU A 375 ? 0.6739 0.6082 0.5923 0.0196  -0.0043 0.0277  391 LEU B C   
3050  O O   . LEU A 375 ? 0.7280 0.6689 0.6566 0.0160  0.0000  0.0355  391 LEU B O   
3051  C CB  . LEU A 375 ? 0.6943 0.6228 0.5982 0.0290  0.0042  0.0250  391 LEU B CB  
3052  C CG  . LEU A 375 ? 0.7133 0.6288 0.6032 0.0389  0.0091  0.0224  391 LEU B CG  
3053  C CD1 . LEU A 375 ? 0.7386 0.6619 0.6288 0.0374  0.0127  0.0228  391 LEU B CD1 
3054  C CD2 . LEU A 375 ? 0.6661 0.5677 0.5516 0.0459  0.0148  0.0268  391 LEU B CD2 
3055  N N   . LEU A 376 ? 0.6539 0.5931 0.5746 0.0150  -0.0120 0.0236  392 LEU B N   
3056  C CA  . LEU A 376 ? 0.6800 0.6322 0.6155 0.0054  -0.0160 0.0279  392 LEU B CA  
3057  C C   . LEU A 376 ? 0.6880 0.6297 0.6232 0.0060  -0.0194 0.0280  392 LEU B C   
3058  O O   . LEU A 376 ? 0.7277 0.6791 0.6745 -0.0018 -0.0235 0.0311  392 LEU B O   
3059  C CB  . LEU A 376 ? 0.6599 0.6294 0.6009 -0.0021 -0.0222 0.0243  392 LEU B CB  
3060  C CG  . LEU A 376 ? 0.6781 0.6567 0.6187 -0.0027 -0.0184 0.0239  392 LEU B CG  
3061  C CD1 . LEU A 376 ? 0.6351 0.6310 0.5810 -0.0097 -0.0237 0.0205  392 LEU B CD1 
3062  C CD2 . LEU A 376 ? 0.7508 0.7355 0.7011 -0.0062 -0.0122 0.0325  392 LEU B CD2 
3063  N N   . ARG A 377 ? 0.6777 0.5997 0.6001 0.0148  -0.0173 0.0251  393 ARG B N   
3064  C CA  . ARG A 377 ? 0.7578 0.6679 0.6782 0.0154  -0.0206 0.0242  393 ARG B CA  
3065  C C   . ARG A 377 ? 0.7639 0.6692 0.6919 0.0163  -0.0147 0.0326  393 ARG B C   
3066  O O   . ARG A 377 ? 0.8167 0.7061 0.7366 0.0247  -0.0087 0.0337  393 ARG B O   
3067  C CB  . ARG A 377 ? 0.7545 0.6459 0.6568 0.0239  -0.0217 0.0164  393 ARG B CB  
3068  C CG  . ARG A 377 ? 0.7543 0.6521 0.6508 0.0222  -0.0285 0.0090  393 ARG B CG  
3069  C CD  . ARG A 377 ? 0.7721 0.6528 0.6511 0.0304  -0.0291 0.0022  393 ARG B CD  
3070  N NE  . ARG A 377 ? 0.8135 0.7008 0.6864 0.0298  -0.0348 -0.0043 393 ARG B NE  
3071  C CZ  . ARG A 377 ? 0.8928 0.7692 0.7503 0.0372  -0.0350 -0.0102 393 ARG B CZ  
3072  N NH1 . ARG A 377 ? 0.8505 0.7085 0.6966 0.0456  -0.0300 -0.0108 393 ARG B NH1 
3073  N NH2 . ARG A 377 ? 0.9484 0.8329 0.8020 0.0361  -0.0405 -0.0153 393 ARG B NH2 
3074  N N   . ASN A 378 ? 0.7480 0.6677 0.6922 0.0076  -0.0162 0.0390  394 ASN B N   
3075  C CA  . ASN A 378 ? 0.7613 0.6800 0.7146 0.0081  -0.0097 0.0485  394 ASN B CA  
3076  C C   . ASN A 378 ? 0.7205 0.6565 0.6918 -0.0025 -0.0131 0.0549  394 ASN B C   
3077  O O   . ASN A 378 ? 0.7172 0.6692 0.6947 -0.0104 -0.0190 0.0527  394 ASN B O   
3078  C CB  . ASN A 378 ? 0.7225 0.6450 0.6760 0.0117  -0.0017 0.0532  394 ASN B CB  
3079  C CG  . ASN A 378 ? 0.8583 0.7658 0.8081 0.0201  0.0060  0.0584  394 ASN B CG  
3080  O OD1 . ASN A 378 ? 0.8078 0.7116 0.7649 0.0194  0.0073  0.0641  394 ASN B OD1 
3081  N ND2 . ASN A 378 ? 1.0038 0.9028 0.9427 0.0282  0.0116  0.0570  394 ASN B ND2 
3082  N N   . GLY A 379 ? 0.6459 0.5794 0.6259 -0.0023 -0.0088 0.0633  395 GLY B N   
3083  C CA  . GLY A 379 ? 0.7006 0.6509 0.6986 -0.0121 -0.0113 0.0707  395 GLY B CA  
3084  C C   . GLY A 379 ? 0.7158 0.6892 0.7246 -0.0194 -0.0102 0.0752  395 GLY B C   
3085  O O   . GLY A 379 ? 0.7299 0.7043 0.7341 -0.0159 -0.0050 0.0756  395 GLY B O   
3086  N N   . ALA A 380 ? 0.7073 0.6992 0.7306 -0.0299 -0.0152 0.0788  396 ALA B N   
3087  C CA  . ALA A 380 ? 0.6530 0.6678 0.6857 -0.0382 -0.0156 0.0814  396 ALA B CA  
3088  C C   . ALA A 380 ? 0.6728 0.6924 0.7094 -0.0368 -0.0072 0.0894  396 ALA B C   
3089  O O   . ALA A 380 ? 0.6915 0.7205 0.7265 -0.0388 -0.0053 0.0882  396 ALA B O   
3090  C CB  . ALA A 380 ? 0.6037 0.6370 0.6525 -0.0493 -0.0213 0.0859  396 ALA B CB  
3091  N N   . ASN A 381 ? 0.6334 0.6471 0.6756 -0.0337 -0.0020 0.0980  397 ASN B N   
3092  C CA  . ASN A 381 ? 0.6169 0.6316 0.6612 -0.0304 0.0066  0.1061  397 ASN B CA  
3093  C C   . ASN A 381 ? 0.6312 0.6267 0.6721 -0.0212 0.0114  0.1099  397 ASN B C   
3094  O O   . ASN A 381 ? 0.6183 0.6022 0.6572 -0.0192 0.0078  0.1069  397 ASN B O   
3095  C CB  . ASN A 381 ? 0.5528 0.5916 0.6148 -0.0407 0.0080  0.1167  397 ASN B CB  
3096  C CG  . ASN A 381 ? 0.5859 0.6316 0.6633 -0.0457 0.0060  0.1250  397 ASN B CG  
3097  O OD1 . ASN A 381 ? 0.6039 0.6342 0.6800 -0.0394 0.0079  0.1272  397 ASN B OD1 
3098  N ND2 . ASN A 381 ? 0.5740 0.6430 0.6660 -0.0572 0.0028  0.1301  397 ASN B ND2 
3099  N N   . GLU A 382 ? 0.6207 0.6136 0.6614 -0.0159 0.0197  0.1171  398 GLU B N   
3100  C CA  . GLU A 382 ? 0.6191 0.5936 0.6556 -0.0058 0.0256  0.1210  398 GLU B CA  
3101  C C   . GLU A 382 ? 0.5958 0.5677 0.6422 -0.0076 0.0238  0.1260  398 GLU B C   
3102  O O   . GLU A 382 ? 0.6304 0.5830 0.6707 0.0011  0.0273  0.1263  398 GLU B O   
3103  C CB  . GLU A 382 ? 0.6295 0.6079 0.6694 -0.0023 0.0346  0.1311  398 GLU B CB  
3104  C CG  . GLU A 382 ? 0.6902 0.6918 0.7498 -0.0116 0.0364  0.1440  398 GLU B CG  
3105  C CD  . GLU A 382 ? 0.7016 0.7103 0.7643 -0.0097 0.0446  0.1537  398 GLU B CD  
3106  O OE1 . GLU A 382 ? 0.7439 0.7440 0.7943 -0.0033 0.0484  0.1501  398 GLU B OE1 
3107  O OE2 . GLU A 382 ? 0.6775 0.6998 0.7551 -0.0140 0.0476  0.1658  398 GLU B OE2 
3108  N N   . GLY A 383 ? 0.5660 0.5562 0.6272 -0.0185 0.0186  0.1297  399 GLY B N   
3109  C CA  . GLY A 383 ? 0.6018 0.5904 0.6736 -0.0204 0.0175  0.1358  399 GLY B CA  
3110  C C   . GLY A 383 ? 0.7470 0.7254 0.8144 -0.0219 0.0096  0.1273  399 GLY B C   
3111  O O   . GLY A 383 ? 0.7388 0.7127 0.8138 -0.0229 0.0086  0.1318  399 GLY B O   
3112  N N   . PHE A 384 ? 0.7099 0.6845 0.7653 -0.0222 0.0039  0.1155  400 PHE B N   
3113  C CA  . PHE A 384 ? 0.6307 0.6035 0.6853 -0.0272 -0.0051 0.1086  400 PHE B CA  
3114  C C   . PHE A 384 ? 0.7053 0.6516 0.7471 -0.0193 -0.0057 0.1026  400 PHE B C   
3115  O O   . PHE A 384 ? 0.7668 0.7090 0.8136 -0.0228 -0.0100 0.1032  400 PHE B O   
3116  C CB  . PHE A 384 ? 0.6474 0.6295 0.6957 -0.0315 -0.0112 0.0993  400 PHE B CB  
3117  C CG  . PHE A 384 ? 0.6344 0.6433 0.6977 -0.0435 -0.0157 0.1030  400 PHE B CG  
3118  C CD1 . PHE A 384 ? 0.6340 0.6611 0.7093 -0.0482 -0.0112 0.1121  400 PHE B CD1 
3119  C CD2 . PHE A 384 ? 0.6588 0.6751 0.7236 -0.0505 -0.0247 0.0971  400 PHE B CD2 
3120  C CE1 . PHE A 384 ? 0.6255 0.6775 0.7137 -0.0596 -0.0155 0.1149  400 PHE B CE1 
3121  C CE2 . PHE A 384 ? 0.6623 0.7037 0.7405 -0.0615 -0.0289 0.1002  400 PHE B CE2 
3122  C CZ  . PHE A 384 ? 0.5983 0.6572 0.6879 -0.0661 -0.0243 0.1088  400 PHE B CZ  
3123  N N   . HIS A 385 ? 0.7440 0.6719 0.7690 -0.0091 -0.0017 0.0965  401 HIS B N   
3124  C CA  . HIS A 385 ? 0.7932 0.6951 0.8046 -0.0018 -0.0023 0.0902  401 HIS B CA  
3125  C C   . HIS A 385 ? 0.8468 0.7391 0.8659 -0.0001 0.0012  0.0979  401 HIS B C   
3126  O O   . HIS A 385 ? 0.8458 0.7284 0.8640 -0.0024 -0.0039 0.0948  401 HIS B O   
3127  C CB  . HIS A 385 ? 0.8740 0.7582 0.8672 0.0096  0.0031  0.0844  401 HIS B CB  
3128  C CG  . HIS A 385 ? 0.8726 0.7500 0.8503 0.0107  -0.0029 0.0720  401 HIS B CG  
3129  N ND1 . HIS A 385 ? 0.8422 0.7013 0.8079 0.0130  -0.0075 0.0639  401 HIS B ND1 
3130  C CD2 . HIS A 385 ? 0.8648 0.7518 0.8373 0.0095  -0.0052 0.0665  401 HIS B CD2 
3131  C CE1 . HIS A 385 ? 0.8619 0.7207 0.8161 0.0131  -0.0125 0.0543  401 HIS B CE1 
3132  N NE2 . HIS A 385 ? 0.8464 0.7216 0.8045 0.0115  -0.0109 0.0558  401 HIS B NE2 
3133  N N   . GLU A 386 ? 0.9508 0.8448 0.9768 0.0044  0.0100  0.1080  402 GLU B N   
3134  C CA  . GLU A 386 ? 0.9570 0.8393 0.9889 0.0080  0.0145  0.1154  402 GLU B CA  
3135  C C   . GLU A 386 ? 0.9653 0.8610 1.0147 -0.0024 0.0091  0.1213  402 GLU B C   
3136  O O   . GLU A 386 ? 1.0117 0.8932 1.0619 -0.0012 0.0085  0.1223  402 GLU B O   
3137  C CB  . GLU A 386 ? 0.9664 0.8491 1.0022 0.0155  0.0254  0.1256  402 GLU B CB  
3138  C CG  . GLU A 386 ? 1.0733 0.9317 1.0899 0.0293  0.0322  0.1204  402 GLU B CG  
3139  C CD  . GLU A 386 ? 1.0875 0.9174 1.0925 0.0362  0.0326  0.1150  402 GLU B CD  
3140  O OE1 . GLU A 386 ? 1.1960 1.0226 1.2112 0.0368  0.0360  0.1234  402 GLU B OE1 
3141  O OE2 . GLU A 386 ? 0.9311 0.7420 0.9174 0.0412  0.0302  0.1034  402 GLU B OE2 
3142  N N   . ALA A 387 ? 0.7996 0.7215 0.8619 -0.0129 0.0045  0.1245  403 ALA B N   
3143  C CA  . ALA A 387 ? 0.7796 0.7156 0.8577 -0.0235 -0.0018 0.1291  403 ALA B CA  
3144  C C   . ALA A 387 ? 0.8254 0.7494 0.8952 -0.0264 -0.0107 0.1189  403 ALA B C   
3145  O O   . ALA A 387 ? 0.8964 0.8149 0.9728 -0.0296 -0.0134 0.1218  403 ALA B O   
3146  C CB  . ALA A 387 ? 0.7221 0.6887 0.8135 -0.0340 -0.0048 0.1332  403 ALA B CB  
3147  N N   . VAL A 388 ? 0.8453 0.7657 0.9008 -0.0258 -0.0154 0.1073  404 VAL B N   
3148  C CA  . VAL A 388 ? 0.8108 0.7199 0.8569 -0.0283 -0.0239 0.0974  404 VAL B CA  
3149  C C   . VAL A 388 ? 0.8575 0.7378 0.8937 -0.0209 -0.0213 0.0954  404 VAL B C   
3150  O O   . VAL A 388 ? 0.9032 0.7761 0.9410 -0.0253 -0.0268 0.0940  404 VAL B O   
3151  C CB  . VAL A 388 ? 0.7792 0.6879 0.8103 -0.0269 -0.0280 0.0859  404 VAL B CB  
3152  C CG1 . VAL A 388 ? 0.8400 0.7309 0.8574 -0.0267 -0.0350 0.0756  404 VAL B CG1 
3153  C CG2 . VAL A 388 ? 0.7504 0.6871 0.7913 -0.0361 -0.0326 0.0865  404 VAL B CG2 
3154  N N   . GLY A 389 ? 0.8748 0.7382 0.9005 -0.0097 -0.0127 0.0955  405 GLY B N   
3155  C CA  . GLY A 389 ? 0.9173 0.7524 0.9328 -0.0019 -0.0091 0.0936  405 GLY B CA  
3156  C C   . GLY A 389 ? 0.9218 0.7561 0.9525 -0.0041 -0.0065 0.1041  405 GLY B C   
3157  O O   . GLY A 389 ? 0.9480 0.7629 0.9739 -0.0032 -0.0082 0.1015  405 GLY B O   
3158  N N   . GLU A 390 ? 0.9586 0.8140 1.0077 -0.0073 -0.0025 0.1162  406 GLU B N   
3159  C CA  . GLU A 390 ? 1.0328 0.8885 1.0973 -0.0087 0.0008  0.1275  406 GLU B CA  
3160  C C   . GLU A 390 ? 1.0659 0.9271 1.1397 -0.0194 -0.0085 0.1272  406 GLU B C   
3161  O O   . GLU A 390 ? 1.1262 0.9733 1.2034 -0.0186 -0.0076 0.1307  406 GLU B O   
3162  C CB  . GLU A 390 ? 1.0001 0.8797 1.0830 -0.0106 0.0067  0.1411  406 GLU B CB  
3163  C CG  . GLU A 390 ? 0.9739 0.8474 1.0504 0.0000  0.0168  0.1443  406 GLU B CG  
3164  C CD  . GLU A 390 ? 1.0798 0.9304 1.1532 0.0100  0.0247  0.1488  406 GLU B CD  
3165  O OE1 . GLU A 390 ? 1.1981 1.0445 1.2812 0.0072  0.0237  0.1541  406 GLU B OE1 
3166  O OE2 . GLU A 390 ? 1.1081 0.9446 1.1690 0.0208  0.0320  0.1468  406 GLU B OE2 
3167  N N   . ILE A 391 ? 0.9289 0.8110 1.0076 -0.0295 -0.0171 0.1237  407 ILE B N   
3168  C CA  . ILE A 391 ? 0.8636 0.7542 0.9532 -0.0404 -0.0258 0.1250  407 ILE B CA  
3169  C C   . ILE A 391 ? 0.9172 0.7823 0.9922 -0.0394 -0.0312 0.1151  407 ILE B C   
3170  O O   . ILE A 391 ? 0.9331 0.7964 1.0159 -0.0458 -0.0362 0.1175  407 ILE B O   
3171  C CB  . ILE A 391 ? 0.7883 0.7083 0.8868 -0.0513 -0.0335 0.1240  407 ILE B CB  
3172  C CG1 . ILE A 391 ? 0.7843 0.7008 0.8658 -0.0506 -0.0389 0.1107  407 ILE B CG1 
3173  C CG2 . ILE A 391 ? 0.8064 0.7503 0.9179 -0.0529 -0.0283 0.1332  407 ILE B CG2 
3174  C CD1 . ILE A 391 ? 0.7091 0.6538 0.7990 -0.0604 -0.0455 0.1098  407 ILE B CD1 
3175  N N   . MET A 392 ? 0.8610 0.7061 0.9149 -0.0316 -0.0302 0.1043  408 MET B N   
3176  C CA  . MET A 392 ? 0.8762 0.6953 0.9147 -0.0302 -0.0345 0.0949  408 MET B CA  
3177  C C   . MET A 392 ? 0.9262 0.7228 0.9655 -0.0247 -0.0283 0.1002  408 MET B C   
3178  O O   . MET A 392 ? 0.9433 0.7305 0.9849 -0.0299 -0.0332 0.0998  408 MET B O   
3179  C CB  . MET A 392 ? 0.9163 0.7200 0.9318 -0.0228 -0.0343 0.0827  408 MET B CB  
3180  C CG  . MET A 392 ? 0.8702 0.6959 0.8852 -0.0267 -0.0388 0.0783  408 MET B CG  
3181  S SD  . MET A 392 ? 0.8242 0.6732 0.8527 -0.0421 -0.0514 0.0785  408 MET B SD  
3182  C CE  . MET A 392 ? 0.7758 0.6538 0.8081 -0.0455 -0.0534 0.0771  408 MET B CE  
3183  N N   . SER A 393 ? 0.9676 0.7551 1.0050 -0.0140 -0.0173 0.1052  409 SER B N   
3184  C CA  . SER A 393 ? 1.0236 0.7912 1.0635 -0.0080 -0.0102 0.1117  409 SER B CA  
3185  C C   . SER A 393 ? 1.0072 0.7906 1.0705 -0.0162 -0.0117 0.1240  409 SER B C   
3186  O O   . SER A 393 ? 1.0583 0.8246 1.1239 -0.0151 -0.0101 0.1272  409 SER B O   
3187  C CB  . SER A 393 ? 1.0377 0.7965 1.0723 0.0051  0.0021  0.1157  409 SER B CB  
3188  O OG  . SER A 393 ? 0.9667 0.7442 1.0203 0.0061  0.0092  0.1301  409 SER B OG  
3189  N N   . LEU A 394 ? 1.0014 0.8170 1.0820 -0.0249 -0.0152 0.1306  410 LEU B N   
3190  C CA  . LEU A 394 ? 0.9767 0.8082 1.0793 -0.0336 -0.0176 0.1420  410 LEU B CA  
3191  C C   . LEU A 394 ? 1.0134 0.8374 1.1148 -0.0423 -0.0277 0.1365  410 LEU B C   
3192  O O   . LEU A 394 ? 1.0285 0.8403 1.1360 -0.0430 -0.0270 0.1415  410 LEU B O   
3193  C CB  . LEU A 394 ? 0.9035 0.7716 1.0242 -0.0420 -0.0197 0.1497  410 LEU B CB  
3194  C CG  . LEU A 394 ? 0.8767 0.7596 1.0058 -0.0370 -0.0105 0.1593  410 LEU B CG  
3195  C CD1 . LEU A 394 ? 0.8443 0.7621 0.9933 -0.0487 -0.0150 0.1672  410 LEU B CD1 
3196  C CD2 . LEU A 394 ? 0.8921 0.7611 1.0263 -0.0280 0.0000  0.1696  410 LEU B CD2 
3197  N N   . SER A 395 ? 0.9982 0.8306 1.0923 -0.0491 -0.0372 0.1266  411 SER B N   
3198  C CA  . SER A 395 ? 1.0162 0.8410 1.1067 -0.0573 -0.0474 0.1203  411 SER B CA  
3199  C C   . SER A 395 ? 1.0540 0.8420 1.1287 -0.0508 -0.0451 0.1145  411 SER B C   
3200  O O   . SER A 395 ? 1.1026 0.8807 1.1810 -0.0562 -0.0494 0.1158  411 SER B O   
3201  C CB  . SER A 395 ? 0.9663 0.8016 1.0467 -0.0625 -0.0563 0.1092  411 SER B CB  
3202  O OG  . SER A 395 ? 0.9640 0.8325 1.0610 -0.0724 -0.0617 0.1143  411 SER B OG  
3203  N N   . ALA A 396 ? 1.1093 0.8763 1.1660 -0.0391 -0.0380 0.1083  412 ALA B N   
3204  C CA  . ALA A 396 ? 1.1390 0.8702 1.1764 -0.0325 -0.0361 0.1002  412 ALA B CA  
3205  C C   . ALA A 396 ? 1.1796 0.8921 1.2228 -0.0268 -0.0279 0.1086  412 ALA B C   
3206  O O   . ALA A 396 ? 1.2162 0.8996 1.2465 -0.0246 -0.0282 0.1026  412 ALA B O   
3207  C CB  . ALA A 396 ? 1.1305 0.8475 1.1471 -0.0217 -0.0309 0.0911  412 ALA B CB  
3208  N N   . ALA A 397 ? 1.3094 1.0370 1.3706 -0.0239 -0.0201 0.1220  413 ALA B N   
3209  C CA  . ALA A 397 ? 1.3055 1.0174 1.3736 -0.0173 -0.0111 0.1314  413 ALA B CA  
3210  C C   . ALA A 397 ? 1.3450 1.0662 1.4332 -0.0267 -0.0153 0.1411  413 ALA B C   
3211  O O   . ALA A 397 ? 1.3596 1.0678 1.4549 -0.0219 -0.0082 0.1497  413 ALA B O   
3212  C CB  . ALA A 397 ? 1.2859 1.0087 1.3623 -0.0081 0.0003  0.1416  413 ALA B CB  
3213  N N   . THR A 398 ? 1.2143 0.9577 1.3120 -0.0397 -0.0262 0.1405  414 THR B N   
3214  C CA  . THR A 398 ? 1.2228 0.9767 1.3402 -0.0491 -0.0303 0.1503  414 THR B CA  
3215  C C   . THR A 398 ? 1.2753 0.9980 1.3830 -0.0500 -0.0332 0.1451  414 THR B C   
3216  O O   . THR A 398 ? 1.3103 1.0095 1.3959 -0.0475 -0.0360 0.1318  414 THR B O   
3217  C CB  . THR A 398 ? 1.1779 0.9638 1.3070 -0.0627 -0.0415 0.1504  414 THR B CB  
3218  O OG1 . THR A 398 ? 1.1847 0.9607 1.2967 -0.0675 -0.0511 0.1363  414 THR B OG1 
3219  C CG2 . THR A 398 ? 1.1601 0.9748 1.2960 -0.0620 -0.0388 0.1538  414 THR B CG2 
3220  N N   . PRO A 399 ? 1.2763 0.9980 1.3999 -0.0537 -0.0326 0.1555  415 PRO B N   
3221  C CA  . PRO A 399 ? 1.3260 1.0186 1.4407 -0.0563 -0.0364 0.1503  415 PRO B CA  
3222  C C   . PRO A 399 ? 1.3671 1.0639 1.4750 -0.0687 -0.0504 0.1402  415 PRO B C   
3223  O O   . PRO A 399 ? 1.4168 1.0853 1.5054 -0.0684 -0.0537 0.1291  415 PRO B O   
3224  C CB  . PRO A 399 ? 1.2807 0.9782 1.4178 -0.0586 -0.0330 0.1656  415 PRO B CB  
3225  C CG  . PRO A 399 ? 1.1991 0.9160 1.3505 -0.0520 -0.0234 0.1775  415 PRO B CG  
3226  C CD  . PRO A 399 ? 1.1809 0.9223 1.3290 -0.0534 -0.0263 0.1725  415 PRO B CD  
3227  N N   . LYS A 400 ? 1.2313 0.9627 1.3543 -0.0796 -0.0587 0.1439  416 LYS B N   
3228  C CA  . LYS A 400 ? 1.2406 0.9782 1.3576 -0.0912 -0.0720 0.1348  416 LYS B CA  
3229  C C   . LYS A 400 ? 1.2719 0.9891 1.3616 -0.0866 -0.0740 0.1188  416 LYS B C   
3230  O O   . LYS A 400 ? 1.3112 1.0074 1.3867 -0.0907 -0.0806 0.1096  416 LYS B O   
3231  C CB  . LYS A 400 ? 1.2601 1.0394 1.3946 -0.1008 -0.0785 0.1400  416 LYS B CB  
3232  C CG  . LYS A 400 ? 1.3360 1.1270 1.4692 -0.1141 -0.0928 0.1334  416 LYS B CG  
3233  C CD  . LYS A 400 ? 1.3290 1.1564 1.4694 -0.1201 -0.0984 0.1327  416 LYS B CD  
3234  C CE  . LYS A 400 ? 1.2990 1.1596 1.4662 -0.1251 -0.0965 0.1474  416 LYS B CE  
3235  N NZ  . LYS A 400 ? 1.1868 1.0817 1.3606 -0.1299 -0.1003 0.1470  416 LYS B NZ  
3236  N N   . HIS A 401 ? 1.2488 0.9706 1.3308 -0.0777 -0.0678 0.1157  417 HIS B N   
3237  C CA  . HIS A 401 ? 1.2562 0.9602 1.3127 -0.0719 -0.0684 0.1014  417 HIS B CA  
3238  C C   . HIS A 401 ? 1.2996 0.9626 1.3369 -0.0638 -0.0631 0.0949  417 HIS B C   
3239  O O   . HIS A 401 ? 1.3460 0.9901 1.3636 -0.0657 -0.0690 0.0827  417 HIS B O   
3240  C CB  . HIS A 401 ? 1.1839 0.9016 1.2386 -0.0634 -0.0614 0.1015  417 HIS B CB  
3241  C CG  . HIS A 401 ? 1.1323 0.8374 1.1630 -0.0584 -0.0628 0.0877  417 HIS B CG  
3242  N ND1 . HIS A 401 ? 1.0658 0.7877 1.0916 -0.0651 -0.0721 0.0801  417 HIS B ND1 
3243  C CD2 . HIS A 401 ? 1.1467 0.8245 1.1571 -0.0470 -0.0558 0.0803  417 HIS B CD2 
3244  C CE1 . HIS A 401 ? 1.0803 0.7859 1.0841 -0.0582 -0.0709 0.0690  417 HIS B CE1 
3245  N NE2 . HIS A 401 ? 1.1184 0.7972 1.1123 -0.0473 -0.0612 0.0687  417 HIS B NE2 
3246  N N   . LEU A 402 ? 1.3565 1.0058 1.3984 -0.0542 -0.0517 0.1027  418 LEU B N   
3247  C CA  . LEU A 402 ? 1.3983 1.0080 1.4215 -0.0450 -0.0452 0.0967  418 LEU B CA  
3248  C C   . LEU A 402 ? 1.4512 1.0395 1.4680 -0.0532 -0.0528 0.0919  418 LEU B C   
3249  O O   . LEU A 402 ? 1.5091 1.0668 1.5032 -0.0502 -0.0532 0.0805  418 LEU B O   
3250  C CB  . LEU A 402 ? 1.4539 1.0568 1.4873 -0.0342 -0.0317 0.1084  418 LEU B CB  
3251  C CG  . LEU A 402 ? 1.3436 0.9648 1.3807 -0.0256 -0.0238 0.1125  418 LEU B CG  
3252  C CD1 . LEU A 402 ? 1.3031 0.9233 1.3543 -0.0167 -0.0115 0.1263  418 LEU B CD1 
3253  C CD2 . LEU A 402 ? 1.2993 0.9006 1.3098 -0.0168 -0.0213 0.0990  418 LEU B CD2 
3254  N N   . LYS A 403 ? 1.5087 1.1129 1.5454 -0.0640 -0.0588 0.1005  419 LYS B N   
3255  C CA  . LYS A 403 ? 1.5436 1.1319 1.5759 -0.0739 -0.0677 0.0963  419 LYS B CA  
3256  C C   . LYS A 403 ? 1.4907 1.0806 1.5064 -0.0817 -0.0794 0.0828  419 LYS B C   
3257  O O   . LYS A 403 ? 1.5097 1.0703 1.5041 -0.0816 -0.0820 0.0719  419 LYS B O   
3258  C CB  . LYS A 403 ? 1.5333 1.1442 1.5922 -0.0844 -0.0724 0.1092  419 LYS B CB  
3259  C CG  . LYS A 403 ? 1.6163 1.2200 1.6904 -0.0776 -0.0616 0.1226  419 LYS B CG  
3260  C CD  . LYS A 403 ? 1.6315 1.2569 1.7314 -0.0886 -0.0668 0.1353  419 LYS B CD  
3261  C CE  . LYS A 403 ? 1.7159 1.3301 1.8293 -0.0816 -0.0562 0.1482  419 LYS B CE  
3262  N NZ  . LYS A 403 ? 1.7796 1.4085 1.9154 -0.0927 -0.0618 0.1594  419 LYS B NZ  
3263  N N   . SER A 404 ? 1.4807 1.1047 1.5052 -0.0879 -0.0861 0.0834  420 SER B N   
3264  C CA  . SER A 404 ? 1.4737 1.1020 1.4842 -0.0956 -0.0974 0.0717  420 SER B CA  
3265  C C   . SER A 404 ? 1.4490 1.0488 1.4309 -0.0875 -0.0948 0.0580  420 SER B C   
3266  O O   . SER A 404 ? 1.5381 1.1246 1.5038 -0.0937 -0.1033 0.0479  420 SER B O   
3267  C CB  . SER A 404 ? 1.4470 1.1152 1.4699 -0.1006 -0.1026 0.0742  420 SER B CB  
3268  O OG  . SER A 404 ? 1.4102 1.0865 1.4252 -0.1108 -0.1151 0.0659  420 SER B OG  
3269  N N   . ILE A 405 ? 1.4355 1.0260 1.4105 -0.0740 -0.0834 0.0578  421 ILE B N   
3270  C CA  . ILE A 405 ? 1.4748 1.0385 1.4225 -0.0657 -0.0803 0.0452  421 ILE B CA  
3271  C C   . ILE A 405 ? 1.5860 1.1100 1.5206 -0.0606 -0.0746 0.0423  421 ILE B C   
3272  O O   . ILE A 405 ? 1.6431 1.1422 1.5563 -0.0513 -0.0690 0.0336  421 ILE B O   
3273  C CB  . ILE A 405 ? 1.4066 0.9782 1.3505 -0.0536 -0.0713 0.0450  421 ILE B CB  
3274  C CG1 . ILE A 405 ? 1.4544 1.0273 1.4126 -0.0444 -0.0590 0.0568  421 ILE B CG1 
3275  C CG2 . ILE A 405 ? 1.3568 0.9660 1.3134 -0.0589 -0.0767 0.0478  421 ILE B CG2 
3276  C CD1 . ILE A 405 ? 1.4499 1.0194 1.3980 -0.0310 -0.0491 0.0546  421 ILE B CD1 
3277  N N   . GLY A 406 ? 1.6120 1.1293 1.5590 -0.0659 -0.0754 0.0496  422 GLY B N   
3278  C CA  . GLY A 406 ? 1.7020 1.1801 1.6359 -0.0621 -0.0707 0.0462  422 GLY B CA  
3279  C C   . GLY A 406 ? 1.7307 1.1866 1.6582 -0.0461 -0.0556 0.0484  422 GLY B C   
3280  O O   . GLY A 406 ? 1.7572 1.1773 1.6692 -0.0416 -0.0511 0.0433  422 GLY B O   
3281  N N   . LEU A 407 ? 1.7878 1.2631 1.7262 -0.0373 -0.0473 0.0558  423 LEU B N   
3282  C CA  . LEU A 407 ? 1.7871 1.2440 1.7233 -0.0224 -0.0325 0.0605  423 LEU B CA  
3283  C C   . LEU A 407 ? 1.8582 1.3171 1.8167 -0.0216 -0.0265 0.0752  423 LEU B C   
3284  O O   . LEU A 407 ? 1.8737 1.3121 1.8301 -0.0100 -0.0146 0.0794  423 LEU B O   
3285  C CB  . LEU A 407 ? 1.7313 1.2070 1.6685 -0.0128 -0.0258 0.0623  423 LEU B CB  
3286  C CG  . LEU A 407 ? 1.7707 1.2349 1.6818 -0.0094 -0.0281 0.0475  423 LEU B CG  
3287  C CD1 . LEU A 407 ? 1.7269 1.2112 1.6394 -0.0011 -0.0225 0.0493  423 LEU B CD1 
3288  C CD2 . LEU A 407 ? 1.8102 1.2321 1.6978 -0.0015 -0.0222 0.0388  423 LEU B CD2 
3289  N N   . LEU A 408 ? 1.8090 1.2931 1.7890 -0.0335 -0.0344 0.0835  424 LEU B N   
3290  C CA  . LEU A 408 ? 1.8350 1.3218 1.8368 -0.0349 -0.0305 0.0975  424 LEU B CA  
3291  C C   . LEU A 408 ? 1.9070 1.3830 1.9098 -0.0477 -0.0407 0.0954  424 LEU B C   
3292  O O   . LEU A 408 ? 1.8158 1.2974 1.8106 -0.0586 -0.0528 0.0865  424 LEU B O   
3293  C CB  . LEU A 408 ? 1.6847 1.2132 1.7139 -0.0377 -0.0301 0.1114  424 LEU B CB  
3294  C CG  . LEU A 408 ? 1.6847 1.2148 1.7355 -0.0350 -0.0224 0.1272  424 LEU B CG  
3295  C CD1 . LEU A 408 ? 1.7520 1.2501 1.7907 -0.0195 -0.0087 0.1270  424 LEU B CD1 
3296  C CD2 . LEU A 408 ? 1.6463 1.2166 1.7217 -0.0363 -0.0206 0.1404  424 LEU B CD2 
3297  N N   . SER A 409 ? 1.9608 1.4205 1.9732 -0.0462 -0.0354 0.1040  425 SER B N   
3298  C CA  . SER A 409 ? 2.0095 1.4539 2.0226 -0.0571 -0.0433 0.1030  425 SER B CA  
3299  C C   . SER A 409 ? 2.0308 1.5090 2.0724 -0.0691 -0.0505 0.1157  425 SER B C   
3300  O O   . SER A 409 ? 1.9670 1.4627 2.0303 -0.0648 -0.0433 0.1301  425 SER B O   
3301  C CB  . SER A 409 ? 2.0453 1.4518 2.0527 -0.0483 -0.0329 0.1055  425 SER B CB  
3302  O OG  . SER A 409 ? 2.1956 1.5855 2.2033 -0.0589 -0.0402 0.1045  425 SER B OG  
3303  N N   . PRO A 410 ? 2.1121 1.6006 2.1548 -0.0844 -0.0649 0.1114  426 PRO B N   
3304  C CA  . PRO A 410 ? 2.0886 1.6110 2.1586 -0.0961 -0.0721 0.1236  426 PRO B CA  
3305  C C   . PRO A 410 ? 2.1013 1.6196 2.1915 -0.0940 -0.0650 0.1385  426 PRO B C   
3306  O O   . PRO A 410 ? 2.0768 1.6265 2.1926 -0.1000 -0.0671 0.1515  426 PRO B O   
3307  C CB  . PRO A 410 ? 2.0449 1.5652 2.1071 -0.1111 -0.0870 0.1150  426 PRO B CB  
3308  C CG  . PRO A 410 ? 2.0702 1.5706 2.1033 -0.1078 -0.0890 0.0983  426 PRO B CG  
3309  C CD  . PRO A 410 ? 2.1088 1.5776 2.1279 -0.0917 -0.0747 0.0959  426 PRO B CD  
3310  N N   . ASP A 411 ? 2.0785 1.5584 2.1574 -0.0851 -0.0561 0.1371  427 ASP B N   
3311  C CA  . ASP A 411 ? 2.0542 1.5267 2.1506 -0.0801 -0.0470 0.1514  427 ASP B CA  
3312  C C   . ASP A 411 ? 2.0571 1.5390 2.1625 -0.0655 -0.0329 0.1609  427 ASP B C   
3313  O O   . ASP A 411 ? 2.0670 1.5273 2.1747 -0.0554 -0.0216 0.1678  427 ASP B O   
3314  C CB  . ASP A 411 ? 2.0356 1.4613 2.1159 -0.0774 -0.0437 0.1459  427 ASP B CB  
3315  C CG  . ASP A 411 ? 2.0627 1.4733 2.1268 -0.0905 -0.0571 0.1330  427 ASP B CG  
3316  O OD1 . ASP A 411 ? 2.0647 1.5038 2.1387 -0.1039 -0.0696 0.1337  427 ASP B OD1 
3317  O OD2 . ASP A 411 ? 2.0397 1.4099 2.0806 -0.0874 -0.0552 0.1223  427 ASP B OD2 
3318  N N   . PHE A 412 ? 2.0026 1.5156 2.1128 -0.0640 -0.0331 0.1617  428 PHE B N   
3319  C CA  . PHE A 412 ? 1.8931 1.4234 2.0170 -0.0530 -0.0214 0.1733  428 PHE B CA  
3320  C C   . PHE A 412 ? 1.8445 1.4166 1.9990 -0.0615 -0.0248 0.1888  428 PHE B C   
3321  O O   . PHE A 412 ? 1.8363 1.4370 1.9971 -0.0729 -0.0357 0.1868  428 PHE B O   
3322  C CB  . PHE A 412 ? 1.8435 1.3806 1.9529 -0.0452 -0.0182 0.1648  428 PHE B CB  
3323  C CG  . PHE A 412 ? 1.8058 1.3554 1.9261 -0.0329 -0.0052 0.1760  428 PHE B CG  
3324  C CD1 . PHE A 412 ? 1.8046 1.3955 1.9466 -0.0367 -0.0061 0.1870  428 PHE B CD1 
3325  C CD2 . PHE A 412 ? 1.7580 1.2785 1.8670 -0.0178 0.0078  0.1759  428 PHE B CD2 
3326  C CE1 . PHE A 412 ? 1.7419 1.3450 1.8938 -0.0260 0.0056  0.1976  428 PHE B CE1 
3327  C CE2 . PHE A 412 ? 1.7479 1.2809 1.8671 -0.0065 0.0197  0.1868  428 PHE B CE2 
3328  C CZ  . PHE A 412 ? 1.7111 1.2856 1.8519 -0.0110 0.0183  0.1978  428 PHE B CZ  
3329  N N   . GLN A 413 ? 1.8560 1.4322 2.0293 -0.0554 -0.0152 0.2044  429 GLN B N   
3330  C CA  . GLN A 413 ? 1.8304 1.4442 2.0336 -0.0630 -0.0174 0.2207  429 GLN B CA  
3331  C C   . GLN A 413 ? 1.7985 1.4419 2.0111 -0.0569 -0.0109 0.2276  429 GLN B C   
3332  O O   . GLN A 413 ? 1.7862 1.4215 2.0000 -0.0439 0.0018  0.2344  429 GLN B O   
3333  C CB  . GLN A 413 ? 1.8714 1.4733 2.0907 -0.0606 -0.0110 0.2347  429 GLN B CB  
3334  C CG  . GLN A 413 ? 1.9130 1.5531 2.1645 -0.0684 -0.0127 0.2531  429 GLN B CG  
3335  C CD  . GLN A 413 ? 1.8890 1.5517 2.1510 -0.0860 -0.0277 0.2526  429 GLN B CD  
3336  O OE1 . GLN A 413 ? 1.8457 1.5082 2.0930 -0.0934 -0.0379 0.2388  429 GLN B OE1 
3337  N NE2 . GLN A 413 ? 1.8121 1.4960 2.1001 -0.0927 -0.0289 0.2684  429 GLN B NE2 
3338  N N   . GLU A 414 ? 1.9322 1.6096 2.1509 -0.0661 -0.0194 0.2259  430 GLU B N   
3339  C CA  . GLU A 414 ? 1.8093 1.5207 2.0430 -0.0637 -0.0146 0.2357  430 GLU B CA  
3340  C C   . GLU A 414 ? 1.8439 1.5813 2.1074 -0.0697 -0.0140 0.2544  430 GLU B C   
3341  O O   . GLU A 414 ? 1.9476 1.6894 2.2212 -0.0806 -0.0222 0.2573  430 GLU B O   
3342  C CB  . GLU A 414 ? 1.7100 1.4474 1.9388 -0.0710 -0.0234 0.2269  430 GLU B CB  
3343  C CG  . GLU A 414 ? 1.6732 1.3877 1.8738 -0.0690 -0.0277 0.2078  430 GLU B CG  
3344  C CD  . GLU A 414 ? 1.6123 1.3502 1.8110 -0.0812 -0.0406 0.1996  430 GLU B CD  
3345  O OE1 . GLU A 414 ? 1.5180 1.2924 1.7333 -0.0869 -0.0429 0.2069  430 GLU B OE1 
3346  O OE2 . GLU A 414 ? 1.5590 1.2789 1.7394 -0.0849 -0.0482 0.1858  430 GLU B OE2 
3347  N N   . ASP A 415 ? 1.7873 1.5420 2.0648 -0.0626 -0.0042 0.2674  431 ASP B N   
3348  C CA  . ASP A 415 ? 1.6918 1.4727 1.9980 -0.0672 -0.0022 0.2864  431 ASP B CA  
3349  C C   . ASP A 415 ? 1.6181 1.4323 1.9357 -0.0647 0.0030  0.2951  431 ASP B C   
3350  O O   . ASP A 415 ? 1.5496 1.3641 1.8526 -0.0596 0.0049  0.2861  431 ASP B O   
3351  C CB  . ASP A 415 ? 1.7079 1.4617 2.0195 -0.0591 0.0067  0.2959  431 ASP B CB  
3352  C CG  . ASP A 415 ? 1.6536 1.3907 1.9588 -0.0420 0.0217  0.2997  431 ASP B CG  
3353  O OD1 . ASP A 415 ? 1.6973 1.4278 1.9843 -0.0353 0.0243  0.2891  431 ASP B OD1 
3354  O OD2 . ASP A 415 ? 1.6768 1.4058 1.9943 -0.0350 0.0310  0.3132  431 ASP B OD2 
3355  N N   . ASN A 416 ? 1.7883 1.4085 1.9120 0.0048  -0.1799 0.1883  432 ASN B N   
3356  C CA  . ASN A 416 ? 1.6907 1.3326 1.7920 0.0056  -0.1647 0.1916  432 ASN B CA  
3357  C C   . ASN A 416 ? 1.7220 1.3719 1.8077 0.0284  -0.1715 0.1801  432 ASN B C   
3358  O O   . ASN A 416 ? 1.6502 1.3223 1.7276 0.0322  -0.1590 0.1755  432 ASN B O   
3359  C CB  . ASN A 416 ? 1.6450 1.2801 1.7303 -0.0018 -0.1633 0.2057  432 ASN B CB  
3360  C CG  . ASN A 416 ? 1.6938 1.3128 1.7926 -0.0208 -0.1634 0.2183  432 ASN B CG  
3361  O OD1 . ASN A 416 ? 1.6892 1.3044 1.8108 -0.0309 -0.1623 0.2174  432 ASN B OD1 
3362  N ND2 . ASN A 416 ? 1.7343 1.3428 1.8184 -0.0251 -0.1658 0.2301  432 ASN B ND2 
3363  N N   . GLU A 417 ? 1.9995 1.6314 2.0810 0.0439  -0.1918 0.1758  433 GLU B N   
3364  C CA  . GLU A 417 ? 1.9284 1.5676 1.9917 0.0659  -0.1990 0.1670  433 GLU B CA  
3365  C C   . GLU A 417 ? 1.8512 1.5042 1.9195 0.0784  -0.1971 0.1531  433 GLU B C   
3366  O O   . GLU A 417 ? 1.7622 1.4367 1.8169 0.0855  -0.1868 0.1498  433 GLU B O   
3367  C CB  . GLU A 417 ? 1.9755 1.5911 2.0343 0.0800  -0.2226 0.1650  433 GLU B CB  
3368  C CG  . GLU A 417 ? 2.0032 1.6053 2.0526 0.0699  -0.2250 0.1786  433 GLU B CG  
3369  C CD  . GLU A 417 ? 2.0821 1.6665 2.1194 0.0876  -0.2471 0.1754  433 GLU B CD  
3370  O OE1 . GLU A 417 ? 2.1233 1.7084 2.1584 0.1087  -0.2595 0.1624  433 GLU B OE1 
3371  O OE2 . GLU A 417 ? 2.0798 1.6501 2.1084 0.0812  -0.2518 0.1858  433 GLU B OE2 
3372  N N   . THR A 418 ? 1.7363 1.3765 1.8235 0.0824  -0.2081 0.1446  434 THR B N   
3373  C CA  . THR A 418 ? 1.6040 1.2557 1.6948 0.0954  -0.2072 0.1310  434 THR B CA  
3374  C C   . THR A 418 ? 1.5771 1.2525 1.6687 0.0832  -0.1846 0.1326  434 THR B C   
3375  O O   . THR A 418 ? 1.5680 1.2604 1.6514 0.0940  -0.1787 0.1248  434 THR B O   
3376  C CB  . THR A 418 ? 1.5702 1.2039 1.6833 0.0995  -0.2217 0.1218  434 THR B CB  
3377  O OG1 . THR A 418 ? 1.5705 1.1942 1.7033 0.0776  -0.2176 0.1301  434 THR B OG1 
3378  C CG2 . THR A 418 ? 1.6168 1.2294 1.7270 0.1190  -0.2468 0.1154  434 THR B CG2 
3379  N N   . GLU A 419 ? 1.6268 1.3040 1.7269 0.0609  -0.1719 0.1431  435 GLU B N   
3380  C CA  . GLU A 419 ? 1.5078 1.2073 1.6083 0.0494  -0.1513 0.1443  435 GLU B CA  
3381  C C   . GLU A 419 ? 1.4063 1.1256 1.4844 0.0508  -0.1389 0.1493  435 GLU B C   
3382  O O   . GLU A 419 ? 1.3250 1.0639 1.3988 0.0522  -0.1269 0.1450  435 GLU B O   
3383  C CB  . GLU A 419 ? 1.5417 1.2383 1.6594 0.0264  -0.1418 0.1528  435 GLU B CB  
3384  C CG  . GLU A 419 ? 1.6226 1.3064 1.7650 0.0257  -0.1510 0.1447  435 GLU B CG  
3385  C CD  . GLU A 419 ? 1.6110 1.2934 1.7725 0.0034  -0.1419 0.1524  435 GLU B CD  
3386  O OE1 . GLU A 419 ? 1.6006 1.2989 1.7567 -0.0108 -0.1243 0.1609  435 GLU B OE1 
3387  O OE2 . GLU A 419 ? 1.6645 1.3311 1.8472 0.0007  -0.1524 0.1494  435 GLU B OE2 
3388  N N   . ILE A 420 ? 1.3876 1.1018 1.4514 0.0511  -0.1423 0.1580  436 ILE B N   
3389  C CA  . ILE A 420 ? 1.3335 1.0656 1.3760 0.0561  -0.1336 0.1609  436 ILE B CA  
3390  C C   . ILE A 420 ? 1.2812 1.0217 1.3145 0.0781  -0.1403 0.1496  436 ILE B C   
3391  O O   . ILE A 420 ? 1.2132 0.9746 1.2353 0.0817  -0.1294 0.1482  436 ILE B O   
3392  C CB  . ILE A 420 ? 1.3330 1.0559 1.3622 0.0536  -0.1381 0.1715  436 ILE B CB  
3393  C CG1 . ILE A 420 ? 1.2710 0.9905 1.3051 0.0312  -0.1274 0.1845  436 ILE B CG1 
3394  C CG2 . ILE A 420 ? 1.2320 0.9715 1.2393 0.0640  -0.1340 0.1717  436 ILE B CG2 
3395  C CD1 . ILE A 420 ? 1.1678 0.9103 1.1960 0.0197  -0.1069 0.1891  436 ILE B CD1 
3396  N N   . ASN A 421 ? 1.2439 0.9683 1.2815 0.0933  -0.1586 0.1415  437 ASN B N   
3397  C CA  . ASN A 421 ? 1.2091 0.9411 1.2380 0.1156  -0.1658 0.1304  437 ASN B CA  
3398  C C   . ASN A 421 ? 1.1981 0.9469 1.2321 0.1155  -0.1540 0.1235  437 ASN B C   
3399  O O   . ASN A 421 ? 1.1600 0.9284 1.1815 0.1235  -0.1459 0.1210  437 ASN B O   
3400  C CB  . ASN A 421 ? 1.2926 1.0029 1.3285 0.1311  -0.1880 0.1218  437 ASN B CB  
3401  C CG  . ASN A 421 ? 1.3080 1.0038 1.3329 0.1398  -0.2034 0.1254  437 ASN B CG  
3402  O OD1 . ASN A 421 ? 1.2860 0.9875 1.2978 0.1341  -0.1975 0.1343  437 ASN B OD1 
3403  N ND2 . ASN A 421 ? 1.4223 1.0998 1.4519 0.1553  -0.2240 0.1172  437 ASN B ND2 
3404  N N   . PHE A 422 ? 1.2171 0.9581 1.2701 0.1055  -0.1527 0.1207  438 PHE B N   
3405  C CA  . PHE A 422 ? 1.1562 0.9101 1.2161 0.1035  -0.1422 0.1140  438 PHE B CA  
3406  C C   . PHE A 422 ? 1.0977 0.8743 1.1487 0.0917  -0.1221 0.1205  438 PHE B C   
3407  O O   . PHE A 422 ? 1.0685 0.8617 1.1103 0.1001  -0.1156 0.1159  438 PHE B O   
3408  C CB  . PHE A 422 ? 1.1898 0.9301 1.2729 0.0925  -0.1448 0.1113  438 PHE B CB  
3409  C CG  . PHE A 422 ? 1.2109 0.9641 1.3023 0.0856  -0.1322 0.1062  438 PHE B CG  
3410  C CD1 . PHE A 422 ? 1.1367 0.8948 1.2270 0.1008  -0.1352 0.0941  438 PHE B CD1 
3411  C CD2 . PHE A 422 ? 1.1817 0.9408 1.2831 0.0643  -0.1185 0.1130  438 PHE B CD2 
3412  C CE1 . PHE A 422 ? 1.1120 0.8807 1.2092 0.0948  -0.1244 0.0892  438 PHE B CE1 
3413  C CE2 . PHE A 422 ? 1.1362 0.9067 1.2454 0.0584  -0.1079 0.1075  438 PHE B CE2 
3414  C CZ  . PHE A 422 ? 1.1515 0.9262 1.2586 0.0735  -0.1111 0.0955  438 PHE B CZ  
3415  N N   . LEU A 423 ? 1.0842 0.8616 1.1378 0.0726  -0.1125 0.1313  439 LEU B N   
3416  C CA  . LEU A 423 ? 1.0713 0.8693 1.1166 0.0612  -0.0945 0.1377  439 LEU B CA  
3417  C C   . LEU A 423 ? 1.0817 0.8945 1.1066 0.0719  -0.0917 0.1394  439 LEU B C   
3418  O O   . LEU A 423 ? 1.0703 0.9023 1.0889 0.0691  -0.0790 0.1398  439 LEU B O   
3419  C CB  . LEU A 423 ? 1.0805 0.8742 1.1298 0.0415  -0.0875 0.1495  439 LEU B CB  
3420  C CG  . LEU A 423 ? 1.0531 0.8435 1.1220 0.0261  -0.0816 0.1493  439 LEU B CG  
3421  C CD1 . LEU A 423 ? 1.0380 0.8266 1.1084 0.0075  -0.0736 0.1621  439 LEU B CD1 
3422  C CD2 . LEU A 423 ? 1.0543 0.8638 1.1233 0.0244  -0.0690 0.1437  439 LEU B CD2 
3423  N N   . LEU A 424 ? 1.0883 0.8930 1.1033 0.0841  -0.1037 0.1402  440 LEU B N   
3424  C CA  . LEU A 424 ? 1.0156 0.8355 1.0125 0.0949  -0.1016 0.1413  440 LEU B CA  
3425  C C   . LEU A 424 ? 0.9924 0.8239 0.9860 0.1113  -0.1027 0.1312  440 LEU B C   
3426  O O   . LEU A 424 ? 0.9715 0.8230 0.9555 0.1135  -0.0927 0.1319  440 LEU B O   
3427  C CB  . LEU A 424 ? 1.0376 0.8453 1.0251 0.1040  -0.1151 0.1442  440 LEU B CB  
3428  C CG  . LEU A 424 ? 0.9899 0.8107 0.9588 0.1137  -0.1147 0.1470  440 LEU B CG  
3429  C CD1 . LEU A 424 ? 0.9932 0.8217 0.9545 0.1361  -0.1230 0.1377  440 LEU B CD1 
3430  C CD2 . LEU A 424 ? 0.9211 0.7627 0.8838 0.1017  -0.0969 0.1536  440 LEU B CD2 
3431  N N   . LYS A 425 ? 0.9875 0.8062 0.9887 0.1232  -0.1151 0.1220  441 LYS B N   
3432  C CA  . LYS A 425 ? 0.9753 0.8042 0.9736 0.1382  -0.1153 0.1124  441 LYS B CA  
3433  C C   . LYS A 425 ? 0.9634 0.8072 0.9656 0.1267  -0.0991 0.1125  441 LYS B C   
3434  O O   . LYS A 425 ? 0.9041 0.7663 0.8968 0.1323  -0.0910 0.1115  441 LYS B O   
3435  C CB  . LYS A 425 ? 0.9882 0.7989 0.9964 0.1508  -0.1310 0.1021  441 LYS B CB  
3436  C CG  . LYS A 425 ? 1.0622 0.8821 1.0641 0.1699  -0.1335 0.0921  441 LYS B CG  
3437  C CD  . LYS A 425 ? 1.1919 0.9933 1.2008 0.1864  -0.1518 0.0813  441 LYS B CD  
3438  C CE  . LYS A 425 ? 1.2281 1.0395 1.2246 0.2101  -0.1567 0.0728  441 LYS B CE  
3439  N NZ  . LYS A 425 ? 1.3186 1.1123 1.3166 0.2292  -0.1774 0.0641  441 LYS B NZ  
3440  N N   . GLN A 426 ? 0.9568 0.7931 0.9735 0.1099  -0.0942 0.1142  442 GLN B N   
3441  C CA  . GLN A 426 ? 0.9274 0.7761 0.9492 0.0979  -0.0798 0.1139  442 GLN B CA  
3442  C C   . GLN A 426 ? 0.9271 0.7958 0.9369 0.0907  -0.0661 0.1217  442 GLN B C   
3443  O O   . GLN A 426 ? 0.9276 0.8107 0.9349 0.0897  -0.0566 0.1194  442 GLN B O   
3444  C CB  . GLN A 426 ? 0.9487 0.7876 0.9875 0.0799  -0.0765 0.1159  442 GLN B CB  
3445  C CG  . GLN A 426 ? 1.0072 0.8289 1.0618 0.0845  -0.0877 0.1070  442 GLN B CG  
3446  C CD  . GLN A 426 ? 0.9844 0.8126 1.0418 0.0917  -0.0852 0.0965  442 GLN B CD  
3447  O OE1 . GLN A 426 ? 0.9695 0.7993 1.0181 0.1098  -0.0918 0.0899  442 GLN B OE1 
3448  N NE2 . GLN A 426 ? 1.0001 0.8333 1.0681 0.0782  -0.0754 0.0951  442 GLN B NE2 
3449  N N   . ALA A 427 ? 0.9852 0.8541 0.9877 0.0853  -0.0654 0.1308  443 ALA B N   
3450  C CA  . ALA A 427 ? 0.9293 0.8166 0.9213 0.0781  -0.0530 0.1382  443 ALA B CA  
3451  C C   . ALA A 427 ? 0.8989 0.8007 0.8772 0.0933  -0.0535 0.1363  443 ALA B C   
3452  O O   . ALA A 427 ? 0.8172 0.7370 0.7906 0.0904  -0.0427 0.1379  443 ALA B O   
3453  C CB  . ALA A 427 ? 0.8886 0.7705 0.8770 0.0677  -0.0523 0.1481  443 ALA B CB  
3454  N N   . LEU A 428 ? 0.8971 0.7917 0.8700 0.1098  -0.0663 0.1328  444 LEU B N   
3455  C CA  . LEU A 428 ? 0.9094 0.8183 0.8705 0.1263  -0.0677 0.1299  444 LEU B CA  
3456  C C   . LEU A 428 ? 0.9492 0.8690 0.9121 0.1306  -0.0615 0.1238  444 LEU B C   
3457  O O   . LEU A 428 ? 0.9446 0.8826 0.8985 0.1370  -0.0557 0.1246  444 LEU B O   
3458  C CB  . LEU A 428 ? 0.9300 0.8272 0.8871 0.1447  -0.0843 0.1249  444 LEU B CB  
3459  C CG  . LEU A 428 ? 0.9182 0.8077 0.8686 0.1450  -0.0918 0.1307  444 LEU B CG  
3460  C CD1 . LEU A 428 ? 0.9521 0.8302 0.8980 0.1647  -0.1092 0.1247  444 LEU B CD1 
3461  C CD2 . LEU A 428 ? 0.9321 0.8409 0.8712 0.1419  -0.0823 0.1378  444 LEU B CD2 
3462  N N   . THR A 429 ? 1.0873 0.9963 1.0619 0.1266  -0.0625 0.1181  445 THR B N   
3463  C CA  . THR A 429 ? 1.0849 1.0015 1.0613 0.1301  -0.0573 0.1118  445 THR B CA  
3464  C C   . THR A 429 ? 1.0397 0.9675 1.0195 0.1127  -0.0425 0.1157  445 THR B C   
3465  O O   . THR A 429 ? 1.0641 1.0079 1.0377 0.1142  -0.0344 0.1163  445 THR B O   
3466  C CB  . THR A 429 ? 1.1050 1.0038 1.0923 0.1363  -0.0672 0.1021  445 THR B CB  
3467  O OG1 . THR A 429 ? 1.0878 0.9773 1.0707 0.1552  -0.0819 0.0971  445 THR B OG1 
3468  C CG2 . THR A 429 ? 1.0176 0.9223 1.0073 0.1381  -0.0615 0.0954  445 THR B CG2 
3469  N N   . ILE A 430 ? 0.9191 0.8387 0.9092 0.0964  -0.0394 0.1185  446 ILE B N   
3470  C CA  . ILE A 430 ? 0.8592 0.7876 0.8541 0.0807  -0.0269 0.1206  446 ILE B CA  
3471  C C   . ILE A 430 ? 0.8576 0.8008 0.8441 0.0715  -0.0174 0.1301  446 ILE B C   
3472  O O   . ILE A 430 ? 0.8281 0.7864 0.8105 0.0684  -0.0084 0.1312  446 ILE B O   
3473  C CB  . ILE A 430 ? 0.8545 0.7693 0.8642 0.0678  -0.0274 0.1193  446 ILE B CB  
3474  C CG1 . ILE A 430 ? 0.8873 0.7894 0.9065 0.0770  -0.0362 0.1085  446 ILE B CG1 
3475  C CG2 . ILE A 430 ? 0.8415 0.7665 0.8554 0.0511  -0.0146 0.1221  446 ILE B CG2 
3476  C CD1 . ILE A 430 ? 0.9143 0.7998 0.9493 0.0687  -0.0415 0.1068  446 ILE B CD1 
3477  N N   . VAL A 431 ? 0.8765 0.8147 0.8605 0.0671  -0.0197 0.1370  447 VAL B N   
3478  C CA  . VAL A 431 ? 0.7931 0.7434 0.7705 0.0568  -0.0109 0.1458  447 VAL B CA  
3479  C C   . VAL A 431 ? 0.7428 0.7087 0.7082 0.0671  -0.0096 0.1475  447 VAL B C   
3480  O O   . VAL A 431 ? 0.6823 0.6638 0.6439 0.0609  -0.0003 0.1513  447 VAL B O   
3481  C CB  . VAL A 431 ? 0.7418 0.6808 0.7190 0.0501  -0.0144 0.1525  447 VAL B CB  
3482  C CG1 . VAL A 431 ? 0.7015 0.6522 0.6710 0.0408  -0.0059 0.1609  447 VAL B CG1 
3483  C CG2 . VAL A 431 ? 0.8004 0.7249 0.7907 0.0394  -0.0153 0.1516  447 VAL B CG2 
3484  N N   . GLY A 432 ? 0.7538 0.7164 0.7140 0.0836  -0.0193 0.1442  448 GLY B N   
3485  C CA  . GLY A 432 ? 0.7062 0.6851 0.6559 0.0949  -0.0184 0.1453  448 GLY B CA  
3486  C C   . GLY A 432 ? 0.6826 0.6775 0.6316 0.0939  -0.0092 0.1441  448 GLY B C   
3487  O O   . GLY A 432 ? 0.7597 0.7712 0.7036 0.0905  -0.0019 0.1493  448 GLY B O   
3488  N N   . THR A 433 ? 0.7689 0.7586 0.7235 0.0967  -0.0099 0.1372  449 THR B N   
3489  C CA  . THR A 433 ? 0.7419 0.7449 0.6950 0.0969  -0.0023 0.1357  449 THR B CA  
3490  C C   . THR A 433 ? 0.7401 0.7520 0.6964 0.0798  0.0087  0.1404  449 THR B C   
3491  O O   . THR A 433 ? 0.7564 0.7822 0.7097 0.0790  0.0153  0.1416  449 THR B O   
3492  C CB  . THR A 433 ? 0.7954 0.7882 0.7532 0.1044  -0.0067 0.1266  449 THR B CB  
3493  O OG1 . THR A 433 ? 0.8318 0.8377 0.7842 0.1107  -0.0019 0.1254  449 THR B OG1 
3494  C CG2 . THR A 433 ? 0.8232 0.8038 0.7929 0.0912  -0.0051 0.1232  449 THR B CG2 
3495  N N   . LEU A 434 ? 0.6929 0.6972 0.6547 0.0663  0.0105  0.1432  450 LEU B N   
3496  C CA  . LEU A 434 ? 0.6583 0.6701 0.6234 0.0506  0.0202  0.1465  450 LEU B CA  
3497  C C   . LEU A 434 ? 0.7052 0.7351 0.6632 0.0483  0.0265  0.1531  450 LEU B C   
3498  O O   . LEU A 434 ? 0.7186 0.7593 0.6764 0.0457  0.0323  0.1528  450 LEU B O   
3499  C CB  . LEU A 434 ? 0.6481 0.6490 0.6193 0.0384  0.0205  0.1489  450 LEU B CB  
3500  C CG  . LEU A 434 ? 0.6789 0.6643 0.6607 0.0359  0.0167  0.1428  450 LEU B CG  
3501  C CD1 . LEU A 434 ? 0.6648 0.6439 0.6514 0.0225  0.0191  0.1475  450 LEU B CD1 
3502  C CD2 . LEU A 434 ? 0.6896 0.6806 0.6758 0.0320  0.0222  0.1374  450 LEU B CD2 
3503  N N   . PRO A 435 ? 0.6899 0.7235 0.6421 0.0492  0.0252  0.1591  451 PRO B N   
3504  C CA  . PRO A 435 ? 0.6668 0.7182 0.6139 0.0467  0.0310  0.1649  451 PRO B CA  
3505  C C   . PRO A 435 ? 0.6926 0.7569 0.6362 0.0573  0.0317  0.1637  451 PRO B C   
3506  O O   . PRO A 435 ? 0.7252 0.8040 0.6684 0.0527  0.0381  0.1667  451 PRO B O   
3507  C CB  . PRO A 435 ? 0.6906 0.7407 0.6318 0.0492  0.0270  0.1698  451 PRO B CB  
3508  C CG  . PRO A 435 ? 0.6778 0.7087 0.6220 0.0475  0.0212  0.1681  451 PRO B CG  
3509  C CD  . PRO A 435 ? 0.7071 0.7295 0.6568 0.0539  0.0175  0.1607  451 PRO B CD  
3510  N N   . PHE A 436 ? 0.6920 0.7513 0.6328 0.0718  0.0249  0.1594  452 PHE B N   
3511  C CA  . PHE A 436 ? 0.7331 0.8042 0.6701 0.0833  0.0255  0.1580  452 PHE B CA  
3512  C C   . PHE A 436 ? 0.7110 0.7868 0.6516 0.0766  0.0322  0.1566  452 PHE B C   
3513  O O   . PHE A 436 ? 0.7219 0.8134 0.6600 0.0773  0.0374  0.1600  452 PHE B O   
3514  C CB  . PHE A 436 ? 0.7149 0.7755 0.6496 0.0994  0.0164  0.1516  452 PHE B CB  
3515  C CG  . PHE A 436 ? 0.6966 0.7683 0.6259 0.1131  0.0166  0.1497  452 PHE B CG  
3516  C CD1 . PHE A 436 ? 0.7169 0.7865 0.6479 0.1140  0.0190  0.1455  452 PHE B CD1 
3517  C CD2 . PHE A 436 ? 0.7574 0.8420 0.6796 0.1255  0.0145  0.1522  452 PHE B CD2 
3518  C CE1 . PHE A 436 ? 0.7256 0.8053 0.6507 0.1267  0.0196  0.1445  452 PHE B CE1 
3519  C CE2 . PHE A 436 ? 0.7749 0.8710 0.6919 0.1381  0.0155  0.1511  452 PHE B CE2 
3520  C CZ  . PHE A 436 ? 0.7666 0.8600 0.6848 0.1387  0.0182  0.1476  452 PHE B CZ  
3521  N N   . THR A 437 ? 0.6764 0.7387 0.6232 0.0692  0.0321  0.1519  453 THR B N   
3522  C CA  . THR A 437 ? 0.7463 0.8091 0.6961 0.0656  0.0361  0.1482  453 THR B CA  
3523  C C   . THR A 437 ? 0.6975 0.7699 0.6498 0.0508  0.0438  0.1527  453 THR B C   
3524  O O   . THR A 437 ? 0.6757 0.7582 0.6269 0.0494  0.0483  0.1541  453 THR B O   
3525  C CB  . THR A 437 ? 0.7816 0.8263 0.7379 0.0643  0.0319  0.1404  453 THR B CB  
3526  O OG1 . THR A 437 ? 0.7552 0.7910 0.7093 0.0796  0.0236  0.1354  453 THR B OG1 
3527  C CG2 . THR A 437 ? 0.7580 0.8025 0.7176 0.0591  0.0358  0.1361  453 THR B CG2 
3528  N N   . TYR A 438 ? 0.6593 0.7282 0.6148 0.0401  0.0450  0.1552  454 TYR B N   
3529  C CA  . TYR A 438 ? 0.7020 0.7805 0.6591 0.0273  0.0514  0.1596  454 TYR B CA  
3530  C C   . TYR A 438 ? 0.7046 0.8006 0.6572 0.0298  0.0543  0.1660  454 TYR B C   
3531  O O   . TYR A 438 ? 0.7006 0.8064 0.6548 0.0231  0.0590  0.1681  454 TYR B O   
3532  C CB  . TYR A 438 ? 0.7118 0.7846 0.6711 0.0175  0.0519  0.1620  454 TYR B CB  
3533  C CG  . TYR A 438 ? 0.6824 0.7672 0.6409 0.0077  0.0572  0.1677  454 TYR B CG  
3534  C CD1 . TYR A 438 ? 0.6727 0.7643 0.6341 0.0001  0.0616  0.1668  454 TYR B CD1 
3535  C CD2 . TYR A 438 ? 0.7297 0.8174 0.6846 0.0057  0.0570  0.1733  454 TYR B CD2 
3536  C CE1 . TYR A 438 ? 0.7359 0.8379 0.6971 -0.0083 0.0653  0.1713  454 TYR B CE1 
3537  C CE2 . TYR A 438 ? 0.7647 0.8630 0.7190 -0.0027 0.0612  0.1778  454 TYR B CE2 
3538  C CZ  . TYR A 438 ? 0.7733 0.8788 0.7312 -0.0097 0.0652  0.1766  454 TYR B CZ  
3539  O OH  . TYR A 438 ? 0.8097 0.9254 0.7677 -0.0176 0.0684  0.1804  454 TYR B OH  
3540  N N   . MET A 439 ? 0.7227 0.8232 0.6703 0.0401  0.0511  0.1687  455 MET B N   
3541  C CA  . MET A 439 ? 0.6780 0.7967 0.6226 0.0424  0.0539  0.1749  455 MET B CA  
3542  C C   . MET A 439 ? 0.6895 0.8179 0.6332 0.0479  0.0565  0.1749  455 MET B C   
3543  O O   . MET A 439 ? 0.7041 0.8450 0.6498 0.0415  0.0614  0.1791  455 MET B O   
3544  C CB  . MET A 439 ? 0.6696 0.7902 0.6090 0.0530  0.0490  0.1768  455 MET B CB  
3545  C CG  . MET A 439 ? 0.6824 0.8221 0.6193 0.0560  0.0511  0.1828  455 MET B CG  
3546  S SD  . MET A 439 ? 0.7760 0.9325 0.7112 0.0664  0.0539  0.1841  455 MET B SD  
3547  C CE  . MET A 439 ? 0.8014 0.9511 0.7300 0.0850  0.0459  0.1794  455 MET B CE  
3548  N N   . LEU A 440 ? 0.6908 0.8139 0.6314 0.0605  0.0528  0.1705  456 LEU B N   
3549  C CA  . LEU A 440 ? 0.7045 0.8360 0.6427 0.0668  0.0553  0.1707  456 LEU B CA  
3550  C C   . LEU A 440 ? 0.6962 0.8274 0.6386 0.0553  0.0600  0.1706  456 LEU B C   
3551  O O   . LEU A 440 ? 0.6890 0.8334 0.6313 0.0530  0.0645  0.1754  456 LEU B O   
3552  C CB  . LEU A 440 ? 0.7604 0.8810 0.6947 0.0809  0.0499  0.1641  456 LEU B CB  
3553  C CG  . LEU A 440 ? 0.7205 0.8475 0.6500 0.0912  0.0512  0.1634  456 LEU B CG  
3554  C CD1 . LEU A 440 ? 0.7007 0.8214 0.6246 0.1091  0.0442  0.1582  456 LEU B CD1 
3555  C CD2 . LEU A 440 ? 0.7045 0.8223 0.6366 0.0845  0.0532  0.1594  456 LEU B CD2 
3556  N N   . GLU A 441 ? 0.6989 0.8150 0.6452 0.0481  0.0586  0.1648  457 GLU B N   
3557  C CA  . GLU A 441 ? 0.6805 0.7959 0.6301 0.0383  0.0620  0.1635  457 GLU B CA  
3558  C C   . GLU A 441 ? 0.7496 0.8756 0.7029 0.0253  0.0662  0.1694  457 GLU B C   
3559  O O   . GLU A 441 ? 0.7562 0.8879 0.7111 0.0192  0.0692  0.1711  457 GLU B O   
3560  C CB  . GLU A 441 ? 0.6397 0.7377 0.5931 0.0346  0.0595  0.1551  457 GLU B CB  
3561  C CG  . GLU A 441 ? 0.6704 0.7661 0.6252 0.0296  0.0613  0.1517  457 GLU B CG  
3562  C CD  . GLU A 441 ? 0.6854 0.7785 0.6350 0.0415  0.0596  0.1487  457 GLU B CD  
3563  O OE1 . GLU A 441 ? 0.6658 0.7692 0.6099 0.0507  0.0606  0.1536  457 GLU B OE1 
3564  O OE2 . GLU A 441 ? 0.6628 0.7440 0.6137 0.0417  0.0575  0.1411  457 GLU B OE2 
3565  N N   . LYS A 442 ? 0.7437 0.8719 0.6981 0.0210  0.0661  0.1725  458 LYS B N   
3566  C CA  . LYS A 442 ? 0.7369 0.8762 0.6941 0.0105  0.0694  0.1779  458 LYS B CA  
3567  C C   . LYS A 442 ? 0.7456 0.9021 0.7022 0.0138  0.0719  0.1845  458 LYS B C   
3568  O O   . LYS A 442 ? 0.7686 0.9334 0.7288 0.0056  0.0746  0.1879  458 LYS B O   
3569  C CB  . LYS A 442 ? 0.7362 0.8746 0.6933 0.0070  0.0685  0.1801  458 LYS B CB  
3570  C CG  . LYS A 442 ? 0.7776 0.9220 0.7382 -0.0054 0.0710  0.1830  458 LYS B CG  
3571  C CD  . LYS A 442 ? 0.7503 0.8966 0.7090 -0.0070 0.0703  0.1865  458 LYS B CD  
3572  C CE  . LYS A 442 ? 0.7462 0.8967 0.7078 -0.0184 0.0723  0.1881  458 LYS B CE  
3573  N NZ  . LYS A 442 ? 0.7869 0.9450 0.7527 -0.0229 0.0740  0.1884  458 LYS B NZ  
3574  N N   . TRP A 443 ? 0.7575 0.9197 0.7098 0.0260  0.0708  0.1863  459 TRP B N   
3575  C CA  . TRP A 443 ? 0.7612 0.9418 0.7133 0.0297  0.0738  0.1930  459 TRP B CA  
3576  C C   . TRP A 443 ? 0.7472 0.9300 0.7000 0.0282  0.0765  0.1936  459 TRP B C   
3577  O O   . TRP A 443 ? 0.7829 0.9784 0.7394 0.0221  0.0798  0.1996  459 TRP B O   
3578  C CB  . TRP A 443 ? 0.7500 0.9367 0.6968 0.0445  0.0718  0.1938  459 TRP B CB  
3579  C CG  . TRP A 443 ? 0.7469 0.9546 0.6940 0.0488  0.0755  0.2008  459 TRP B CG  
3580  C CD1 . TRP A 443 ? 0.7744 0.9986 0.7246 0.0470  0.0771  0.2068  459 TRP B CD1 
3581  C CD2 . TRP A 443 ? 0.7597 0.9748 0.7041 0.0559  0.0782  0.2028  459 TRP B CD2 
3582  N NE1 . TRP A 443 ? 0.7754 1.0178 0.7264 0.0518  0.0810  0.2126  459 TRP B NE1 
3583  C CE2 . TRP A 443 ? 0.7745 1.0116 0.7214 0.0573  0.0819  0.2106  459 TRP B CE2 
3584  C CE3 . TRP A 443 ? 0.7609 0.9661 0.7010 0.0612  0.0778  0.1987  459 TRP B CE3 
3585  C CZ2 . TRP A 443 ? 0.8015 1.0516 0.7465 0.0636  0.0859  0.2153  459 TRP B CZ2 
3586  C CZ3 . TRP A 443 ? 0.7123 0.9294 0.6493 0.0681  0.0814  0.2031  459 TRP B CZ3 
3587  C CH2 . TRP A 443 ? 0.7056 0.9451 0.6450 0.0690  0.0857  0.2117  459 TRP B CH2 
3588  N N   . ARG A 444 ? 0.7196 0.8892 0.6688 0.0337  0.0746  0.1874  460 ARG B N   
3589  C CA  . ARG A 444 ? 0.7057 0.8748 0.6543 0.0323  0.0766  0.1875  460 ARG B CA  
3590  C C   . ARG A 444 ? 0.7086 0.8743 0.6628 0.0176  0.0775  0.1872  460 ARG B C   
3591  O O   . ARG A 444 ? 0.6925 0.8647 0.6481 0.0129  0.0798  0.1913  460 ARG B O   
3592  C CB  . ARG A 444 ? 0.7405 0.8945 0.6840 0.0412  0.0736  0.1797  460 ARG B CB  
3593  C CG  . ARG A 444 ? 0.7511 0.9094 0.6879 0.0569  0.0728  0.1802  460 ARG B CG  
3594  C CD  . ARG A 444 ? 0.7808 0.9203 0.7151 0.0634  0.0678  0.1705  460 ARG B CD  
3595  N NE  . ARG A 444 ? 0.7163 0.8528 0.6436 0.0761  0.0667  0.1678  460 ARG B NE  
3596  C CZ  . ARG A 444 ? 0.7311 0.8506 0.6563 0.0825  0.0620  0.1586  460 ARG B CZ  
3597  N NH1 . ARG A 444 ? 0.6439 0.7487 0.5748 0.0761  0.0585  0.1517  460 ARG B NH1 
3598  N NH2 . ARG A 444 ? 0.8219 0.9396 0.7394 0.0958  0.0607  0.1564  460 ARG B NH2 
3599  N N   . TRP A 445 ? 0.7294 0.8842 0.6865 0.0105  0.0755  0.1819  461 TRP B N   
3600  C CA  . TRP A 445 ? 0.7238 0.8763 0.6859 -0.0025 0.0758  0.1808  461 TRP B CA  
3601  C C   . TRP A 445 ? 0.7029 0.8709 0.6693 -0.0097 0.0780  0.1889  461 TRP B C   
3602  O O   . TRP A 445 ? 0.7181 0.8887 0.6874 -0.0168 0.0784  0.1908  461 TRP B O   
3603  C CB  . TRP A 445 ? 0.7269 0.8684 0.6913 -0.0083 0.0740  0.1749  461 TRP B CB  
3604  C CG  . TRP A 445 ? 0.7021 0.8277 0.6653 -0.0048 0.0716  0.1661  461 TRP B CG  
3605  C CD1 . TRP A 445 ? 0.6953 0.8143 0.6558 0.0008  0.0704  0.1620  461 TRP B CD1 
3606  C CD2 . TRP A 445 ? 0.6717 0.7863 0.6370 -0.0069 0.0698  0.1604  461 TRP B CD2 
3607  N NE1 . TRP A 445 ? 0.6681 0.7724 0.6295 0.0026  0.0677  0.1532  461 TRP B NE1 
3608  C CE2 . TRP A 445 ? 0.6649 0.7668 0.6299 -0.0025 0.0675  0.1524  461 TRP B CE2 
3609  C CE3 . TRP A 445 ? 0.7340 0.8481 0.7012 -0.0120 0.0701  0.1615  461 TRP B CE3 
3610  C CZ2 . TRP A 445 ? 0.6772 0.7671 0.6454 -0.0035 0.0655  0.1457  461 TRP B CZ2 
3611  C CZ3 . TRP A 445 ? 0.6894 0.7913 0.6589 -0.0132 0.0685  0.1555  461 TRP B CZ3 
3612  C CH2 . TRP A 445 ? 0.6294 0.7197 0.6001 -0.0093 0.0663  0.1477  461 TRP B CH2 
3613  N N   . MET A 446 ? 0.7119 0.8899 0.6789 -0.0077 0.0787  0.1936  462 MET B N   
3614  C CA  . MET A 446 ? 0.7998 0.9938 0.7719 -0.0134 0.0805  0.2012  462 MET B CA  
3615  C C   . MET A 446 ? 0.7184 0.9241 0.6911 -0.0103 0.0831  0.2074  462 MET B C   
3616  O O   . MET A 446 ? 0.7309 0.9439 0.7092 -0.0186 0.0838  0.2120  462 MET B O   
3617  C CB  . MET A 446 ? 0.8443 1.0464 0.8165 -0.0105 0.0803  0.2042  462 MET B CB  
3618  C CG  . MET A 446 ? 0.9191 1.1114 0.8913 -0.0162 0.0783  0.2000  462 MET B CG  
3619  S SD  . MET A 446 ? 0.8820 1.0825 0.8529 -0.0128 0.0774  0.2038  462 MET B SD  
3620  C CE  . MET A 446 ? 0.8252 1.0099 0.7890 -0.0034 0.0751  0.1981  462 MET B CE  
3621  N N   . VAL A 447 ? 0.7702 0.9782 0.7372 0.0018  0.0842  0.2081  463 VAL B N   
3622  C CA  . VAL A 447 ? 0.7384 0.9593 0.7055 0.0051  0.0876  0.2150  463 VAL B CA  
3623  C C   . VAL A 447 ? 0.7333 0.9479 0.7023 -0.0034 0.0875  0.2151  463 VAL B C   
3624  O O   . VAL A 447 ? 0.7982 1.0213 0.7738 -0.0109 0.0880  0.2197  463 VAL B O   
3625  C CB  . VAL A 447 ? 0.7027 0.9236 0.6615 0.0203  0.0883  0.2138  463 VAL B CB  
3626  C CG1 . VAL A 447 ? 0.6927 0.9242 0.6505 0.0224  0.0921  0.2206  463 VAL B CG1 
3627  C CG2 . VAL A 447 ? 0.7367 0.9668 0.6936 0.0295  0.0880  0.2149  463 VAL B CG2 
3628  N N   . PHE A 448 ? 0.6994 0.8960 0.6640 -0.0028 0.0849  0.2068  464 PHE B N   
3629  C CA  . PHE A 448 ? 0.6970 0.8853 0.6619 -0.0094 0.0838  0.2053  464 PHE B CA  
3630  C C   . PHE A 448 ? 0.7269 0.9175 0.7001 -0.0236 0.0822  0.2070  464 PHE B C   
3631  O O   . PHE A 448 ? 0.7611 0.9562 0.7376 -0.0299 0.0823  0.2122  464 PHE B O   
3632  C CB  . PHE A 448 ? 0.7488 0.9173 0.7084 -0.0057 0.0807  0.1945  464 PHE B CB  
3633  C CG  . PHE A 448 ? 0.7205 0.8847 0.6718 0.0091  0.0810  0.1919  464 PHE B CG  
3634  C CD1 . PHE A 448 ? 0.7274 0.9017 0.6741 0.0171  0.0841  0.1985  464 PHE B CD1 
3635  C CD2 . PHE A 448 ? 0.7004 0.8511 0.6489 0.0153  0.0779  0.1828  464 PHE B CD2 
3636  C CE1 . PHE A 448 ? 0.6649 0.8355 0.6032 0.0319  0.0838  0.1955  464 PHE B CE1 
3637  C CE2 . PHE A 448 ? 0.7246 0.8709 0.6660 0.0295  0.0770  0.1798  464 PHE B CE2 
3638  C CZ  . PHE A 448 ? 0.6606 0.8170 0.5964 0.0382  0.0798  0.1859  464 PHE B CZ  
3639  N N   . LYS A 449 ? 0.7696 0.9569 0.7460 -0.0286 0.0802  0.2027  465 LYS B N   
3640  C CA  . LYS A 449 ? 0.7551 0.9456 0.7388 -0.0406 0.0781  0.2040  465 LYS B CA  
3641  C C   . LYS A 449 ? 0.7609 0.9671 0.7517 -0.0439 0.0788  0.2120  465 LYS B C   
3642  O O   . LYS A 449 ? 0.7886 0.9956 0.7859 -0.0530 0.0757  0.2126  465 LYS B O   
3643  C CB  . LYS A 449 ? 0.6979 0.8832 0.6823 -0.0433 0.0765  0.1985  465 LYS B CB  
3644  C CG  . LYS A 449 ? 0.7174 0.9013 0.7073 -0.0547 0.0732  0.1964  465 LYS B CG  
3645  C CD  . LYS A 449 ? 0.8714 1.0464 0.8602 -0.0576 0.0716  0.1889  465 LYS B CD  
3646  C CE  . LYS A 449 ? 1.0968 1.2560 1.0807 -0.0541 0.0712  0.1799  465 LYS B CE  
3647  N NZ  . LYS A 449 ? 0.9171 1.0668 0.9010 -0.0583 0.0697  0.1718  465 LYS B NZ  
3648  N N   . GLY A 450 ? 0.7336 0.9506 0.7241 -0.0359 0.0814  0.2160  466 GLY B N   
3649  C CA  . GLY A 450 ? 0.7713 1.0027 0.7703 -0.0383 0.0811  0.2208  466 GLY B CA  
3650  C C   . GLY A 450 ? 0.7990 1.0385 0.8023 -0.0391 0.0802  0.2211  466 GLY B C   
3651  O O   . GLY A 450 ? 0.8007 1.0529 0.8123 -0.0419 0.0795  0.2252  466 GLY B O   
3652  N N   . GLU A 451 ? 0.7901 1.0227 0.7880 -0.0368 0.0801  0.2173  467 GLU B N   
3653  C CA  . GLU A 451 ? 0.7552 0.9939 0.7559 -0.0380 0.0789  0.2178  467 GLU B CA  
3654  C C   . GLU A 451 ? 0.8198 1.0724 0.8204 -0.0291 0.0810  0.2221  467 GLU B C   
3655  O O   . GLU A 451 ? 0.8591 1.1198 0.8631 -0.0299 0.0799  0.2238  467 GLU B O   
3656  C CB  . GLU A 451 ? 0.7936 1.0205 0.7882 -0.0385 0.0782  0.2132  467 GLU B CB  
3657  C CG  . GLU A 451 ? 0.8967 1.1126 0.8922 -0.0476 0.0760  0.2088  467 GLU B CG  
3658  C CD  . GLU A 451 ? 1.0321 1.2357 1.0214 -0.0471 0.0761  0.2037  467 GLU B CD  
3659  O OE1 . GLU A 451 ? 1.0177 1.2196 1.0022 -0.0399 0.0769  0.2032  467 GLU B OE1 
3660  O OE2 . GLU A 451 ? 1.1559 1.3498 1.1454 -0.0532 0.0743  0.1982  467 GLU B OE2 
3661  N N   . ILE A 452 ? 0.8589 1.1149 0.8551 -0.0200 0.0838  0.2239  468 ILE B N   
3662  C CA  . ILE A 452 ? 0.8523 1.1230 0.8478 -0.0104 0.0858  0.2279  468 ILE B CA  
3663  C C   . ILE A 452 ? 0.9237 1.2068 0.9241 -0.0085 0.0880  0.2323  468 ILE B C   
3664  O O   . ILE A 452 ? 0.9230 1.2030 0.9179 -0.0028 0.0901  0.2324  468 ILE B O   
3665  C CB  . ILE A 452 ? 0.8108 1.0761 0.7950 0.0013  0.0870  0.2265  468 ILE B CB  
3666  C CG1 . ILE A 452 ? 0.8607 1.1124 0.8405 -0.0016 0.0847  0.2226  468 ILE B CG1 
3667  C CG2 . ILE A 452 ? 0.8655 1.1474 0.8487 0.0118  0.0885  0.2306  468 ILE B CG2 
3668  C CD1 . ILE A 452 ? 0.8184 1.0581 0.7892 0.0094  0.0825  0.2169  468 ILE B CD1 
3669  N N   . PRO A 453 ? 0.9508 1.2489 0.9615 -0.0129 0.0878  0.2365  469 PRO B N   
3670  C CA  . PRO A 453 ? 0.9270 1.2379 0.9438 -0.0123 0.0901  0.2417  469 PRO B CA  
3671  C C   . PRO A 453 ? 0.9516 1.2729 0.9621 0.0015  0.0937  0.2438  469 PRO B C   
3672  O O   . PRO A 453 ? 0.9752 1.2982 0.9792 0.0101  0.0939  0.2423  469 PRO B O   
3673  C CB  . PRO A 453 ? 0.9723 1.2982 1.0019 -0.0192 0.0887  0.2458  469 PRO B CB  
3674  C CG  . PRO A 453 ? 0.9972 1.3144 1.0271 -0.0254 0.0850  0.2421  469 PRO B CG  
3675  C CD  . PRO A 453 ? 1.0002 1.3041 1.0177 -0.0189 0.0852  0.2372  469 PRO B CD  
3676  N N   . LYS A 454 ? 0.9470 1.2749 0.9587 0.0039  0.0965  0.2474  470 LYS B N   
3677  C CA  . LYS A 454 ? 0.9616 1.3002 0.9668 0.0178  0.1001  0.2494  470 LYS B CA  
3678  C C   . LYS A 454 ? 1.0093 1.3671 1.0171 0.0254  0.1010  0.2518  470 LYS B C   
3679  O O   . LYS A 454 ? 1.0024 1.3627 1.0007 0.0382  0.1017  0.2503  470 LYS B O   
3680  C CB  . LYS A 454 ? 0.9386 1.2840 0.9471 0.0168  0.1030  0.2542  470 LYS B CB  
3681  C CG  . LYS A 454 ? 0.9929 1.3224 0.9916 0.0192  0.1037  0.2520  470 LYS B CG  
3682  C CD  . LYS A 454 ? 0.9857 1.3179 0.9892 0.0130  0.1055  0.2573  470 LYS B CD  
3683  C CE  . LYS A 454 ? 0.9516 1.3068 0.9611 0.0178  0.1095  0.2644  470 LYS B CE  
3684  N NZ  . LYS A 454 ? 0.9801 1.3358 0.9915 0.0133  0.1117  0.2698  470 LYS B NZ  
3685  N N   . ASP A 455 ? 1.0670 1.4387 1.0873 0.0179  0.1004  0.2556  471 ASP B N   
3686  C CA  . ASP A 455 ? 1.0651 1.4575 1.0890 0.0246  0.1014  0.2584  471 ASP B CA  
3687  C C   . ASP A 455 ? 1.0777 1.4646 1.0937 0.0301  0.0990  0.2545  471 ASP B C   
3688  O O   . ASP A 455 ? 1.0670 1.4700 1.0837 0.0371  0.0993  0.2563  471 ASP B O   
3689  C CB  . ASP A 455 ? 1.1036 1.5109 1.1433 0.0144  0.1007  0.2632  471 ASP B CB  
3690  C CG  . ASP A 455 ? 1.2045 1.6002 1.2491 0.0023  0.0963  0.2607  471 ASP B CG  
3691  O OD1 . ASP A 455 ? 1.2132 1.5890 1.2494 0.0006  0.0940  0.2553  471 ASP B OD1 
3692  O OD2 . ASP A 455 ? 1.2676 1.6751 1.3246 -0.0052 0.0950  0.2642  471 ASP B OD2 
3693  N N   . GLN A 456 ? 1.0339 1.3987 1.0422 0.0270  0.0964  0.2495  472 GLN B N   
3694  C CA  . GLN A 456 ? 1.0004 1.3577 0.9999 0.0319  0.0941  0.2464  472 GLN B CA  
3695  C C   . GLN A 456 ? 0.9333 1.2726 0.9192 0.0392  0.0934  0.2422  472 GLN B C   
3696  O O   . GLN A 456 ? 0.8820 1.2105 0.8604 0.0420  0.0905  0.2391  472 GLN B O   
3697  C CB  . GLN A 456 ? 1.0392 1.3883 1.0439 0.0198  0.0908  0.2449  472 GLN B CB  
3698  C CG  . GLN A 456 ? 1.0809 1.4473 1.0986 0.0132  0.0905  0.2490  472 GLN B CG  
3699  C CD  . GLN A 456 ? 1.1645 1.5231 1.1840 0.0047  0.0870  0.2473  472 GLN B CD  
3700  O OE1 . GLN A 456 ? 1.1778 1.5241 1.2009 -0.0059 0.0851  0.2452  472 GLN B OE1 
3701  N NE2 . GLN A 456 ? 1.0955 1.4613 1.1115 0.0099  0.0859  0.2483  472 GLN B NE2 
3702  N N   . TRP A 457 ? 0.9450 1.2801 0.9273 0.0431  0.0955  0.2417  473 TRP B N   
3703  C CA  . TRP A 457 ? 0.9168 1.2347 0.8864 0.0503  0.0947  0.2379  473 TRP B CA  
3704  C C   . TRP A 457 ? 0.9277 1.2413 0.8889 0.0631  0.0904  0.2329  473 TRP B C   
3705  O O   . TRP A 457 ? 0.9399 1.2358 0.8984 0.0606  0.0857  0.2269  473 TRP B O   
3706  C CB  . TRP A 457 ? 0.8828 1.2015 0.8485 0.0569  0.0974  0.2384  473 TRP B CB  
3707  C CG  . TRP A 457 ? 0.9174 1.2226 0.8863 0.0459  0.0977  0.2370  473 TRP B CG  
3708  C CD1 . TRP A 457 ? 0.9301 1.2259 0.9064 0.0308  0.0957  0.2355  473 TRP B CD1 
3709  C CD2 . TRP A 457 ? 0.8553 1.1553 0.8191 0.0498  0.0996  0.2369  473 TRP B CD2 
3710  N NE1 . TRP A 457 ? 0.8747 1.1597 0.8507 0.0253  0.0961  0.2344  473 TRP B NE1 
3711  C CE2 . TRP A 457 ? 0.8130 1.1001 0.7812 0.0365  0.0986  0.2355  473 TRP B CE2 
3712  C CE3 . TRP A 457 ? 0.7806 1.0854 0.7354 0.0641  0.1017  0.2378  473 TRP B CE3 
3713  C CZ2 . TRP A 457 ? 0.8611 1.1400 0.8250 0.0368  0.0997  0.2353  473 TRP B CZ2 
3714  C CZ3 . TRP A 457 ? 0.7865 1.0831 0.7372 0.0644  0.1031  0.2375  473 TRP B CZ3 
3715  C CH2 . TRP A 457 ? 0.8038 1.0874 0.7588 0.0507  0.1021  0.2365  473 TRP B CH2 
3716  N N   . MET A 458 ? 0.9255 1.2551 0.8832 0.0766  0.0913  0.2346  474 MET B N   
3717  C CA  . MET A 458 ? 0.8698 1.1947 0.8198 0.0900  0.0856  0.2287  474 MET B CA  
3718  C C   . MET A 458 ? 0.8537 1.1745 0.8064 0.0844  0.0815  0.2269  474 MET B C   
3719  O O   . MET A 458 ? 0.8287 1.1311 0.7755 0.0873  0.0756  0.2206  474 MET B O   
3720  C CB  . MET A 458 ? 0.8823 1.2293 0.8294 0.1048  0.0875  0.2314  474 MET B CB  
3721  C CG  . MET A 458 ? 0.9531 1.3008 0.8954 0.1110  0.0912  0.2327  474 MET B CG  
3722  S SD  . MET A 458 ? 0.8524 1.1680 0.7860 0.1134  0.0860  0.2235  474 MET B SD  
3723  C CE  . MET A 458 ? 0.9421 1.2477 0.8682 0.1275  0.0766  0.2152  474 MET B CE  
3724  N N   . LYS A 459 ? 0.8956 1.2320 0.8576 0.0753  0.0843  0.2324  475 LYS B N   
3725  C CA  . LYS A 459 ? 0.8769 1.2097 0.8408 0.0704  0.0803  0.2307  475 LYS B CA  
3726  C C   . LYS A 459 ? 0.8477 1.1544 0.8085 0.0619  0.0770  0.2259  475 LYS B C   
3727  O O   . LYS A 459 ? 0.8158 1.1080 0.7697 0.0667  0.0716  0.2208  475 LYS B O   
3728  C CB  . LYS A 459 ? 0.8883 1.2401 0.8639 0.0605  0.0836  0.2371  475 LYS B CB  
3729  C CG  . LYS A 459 ? 0.8778 1.2288 0.8553 0.0570  0.0794  0.2356  475 LYS B CG  
3730  C CD  . LYS A 459 ? 0.9785 1.3461 0.9691 0.0459  0.0820  0.2412  475 LYS B CD  
3731  C CE  . LYS A 459 ? 1.1623 1.5250 1.1530 0.0424  0.0770  0.2386  475 LYS B CE  
3732  N NZ  . LYS A 459 ? 1.1996 1.5706 1.2021 0.0299  0.0776  0.2421  475 LYS B NZ  
3733  N N   . LYS A 460 ? 0.8455 1.1455 0.8107 0.0504  0.0801  0.2271  476 LYS B N   
3734  C CA  . LYS A 460 ? 0.8195 1.0972 0.7827 0.0417  0.0777  0.2226  476 LYS B CA  
3735  C C   . LYS A 460 ? 0.8238 1.0833 0.7781 0.0506  0.0739  0.2162  476 LYS B C   
3736  O O   . LYS A 460 ? 0.8297 1.0735 0.7802 0.0494  0.0698  0.2122  476 LYS B O   
3737  C CB  . LYS A 460 ? 0.8219 1.0966 0.7910 0.0295  0.0811  0.2243  476 LYS B CB  
3738  C CG  . LYS A 460 ? 0.8888 1.1654 0.8654 0.0160  0.0810  0.2264  476 LYS B CG  
3739  C CD  . LYS A 460 ? 0.9996 1.2598 0.9718 0.0126  0.0771  0.2216  476 LYS B CD  
3740  C CE  . LYS A 460 ? 0.9598 1.2093 0.9353 -0.0006 0.0772  0.2198  476 LYS B CE  
3741  N NZ  . LYS A 460 ? 0.9343 1.1678 0.9045 -0.0030 0.0743  0.2155  476 LYS B NZ  
3742  N N   . TRP A 461 ? 0.7979 1.0601 0.7485 0.0608  0.0749  0.2154  477 TRP B N   
3743  C CA  . TRP A 461 ? 0.7970 1.0429 0.7398 0.0710  0.0703  0.2090  477 TRP B CA  
3744  C C   . TRP A 461 ? 0.8255 1.0657 0.7635 0.0778  0.0641  0.2061  477 TRP B C   
3745  O O   . TRP A 461 ? 0.8057 1.0267 0.7414 0.0749  0.0600  0.2019  477 TRP B O   
3746  C CB  . TRP A 461 ? 0.8055 1.0601 0.7443 0.0838  0.0718  0.2092  477 TRP B CB  
3747  C CG  . TRP A 461 ? 0.8149 1.0541 0.7456 0.0968  0.0661  0.2021  477 TRP B CG  
3748  C CD1 . TRP A 461 ? 0.8511 1.0926 0.7755 0.1122  0.0609  0.1993  477 TRP B CD1 
3749  C CD2 . TRP A 461 ? 0.8299 1.0491 0.7587 0.0959  0.0642  0.1964  477 TRP B CD2 
3750  N NE1 . TRP A 461 ? 0.8279 1.0518 0.7469 0.1210  0.0556  0.1923  477 TRP B NE1 
3751  C CE2 . TRP A 461 ? 0.8126 1.0227 0.7345 0.1111  0.0577  0.1904  477 TRP B CE2 
3752  C CE3 . TRP A 461 ? 0.8219 1.0301 0.7544 0.0842  0.0668  0.1951  477 TRP B CE3 
3753  C CZ2 . TRP A 461 ? 0.7778 0.9685 0.6975 0.1145  0.0539  0.1835  477 TRP B CZ2 
3754  C CZ3 . TRP A 461 ? 0.8034 0.9930 0.7332 0.0876  0.0634  0.1882  477 TRP B CZ3 
3755  C CH2 . TRP A 461 ? 0.7923 0.9733 0.7161 0.1025  0.0571  0.1825  477 TRP B CH2 
3756  N N   . TRP A 462 ? 0.8166 1.0740 0.7537 0.0865  0.0634  0.2086  478 TRP B N   
3757  C CA  . TRP A 462 ? 0.8075 1.0582 0.7385 0.0953  0.0563  0.2051  478 TRP B CA  
3758  C C   . TRP A 462 ? 0.8277 1.0706 0.7600 0.0850  0.0544  0.2058  478 TRP B C   
3759  O O   . TRP A 462 ? 0.8449 1.0755 0.7715 0.0898  0.0480  0.2027  478 TRP B O   
3760  C CB  . TRP A 462 ? 0.8013 1.0723 0.7300 0.1090  0.0553  0.2065  478 TRP B CB  
3761  C CG  . TRP A 462 ? 0.7802 1.0526 0.7036 0.1230  0.0541  0.2037  478 TRP B CG  
3762  C CD1 . TRP A 462 ? 0.8378 1.1286 0.7623 0.1286  0.0596  0.2071  478 TRP B CD1 
3763  C CD2 . TRP A 462 ? 0.8295 1.0843 0.7451 0.1346  0.0465  0.1968  478 TRP B CD2 
3764  N NE1 . TRP A 462 ? 0.8131 1.0989 0.7300 0.1438  0.0560  0.2024  478 TRP B NE1 
3765  C CE2 . TRP A 462 ? 0.8479 1.1114 0.7597 0.1477  0.0474  0.1957  478 TRP B CE2 
3766  C CE3 . TRP A 462 ? 0.8823 1.1144 0.7941 0.1350  0.0386  0.1918  478 TRP B CE3 
3767  C CZ2 . TRP A 462 ? 0.8850 1.1351 0.7894 0.1619  0.0401  0.1888  478 TRP B CZ2 
3768  C CZ3 . TRP A 462 ? 0.8751 1.0935 0.7806 0.1481  0.0312  0.1854  478 TRP B CZ3 
3769  C CH2 . TRP A 462 ? 0.8738 1.1012 0.7758 0.1617  0.0317  0.1835  478 TRP B CH2 
3770  N N   . GLU A 463 ? 0.8122 1.0612 0.7516 0.0714  0.0594  0.2098  479 GLU B N   
3771  C CA  . GLU A 463 ? 0.7685 1.0079 0.7081 0.0617  0.0576  0.2100  479 GLU B CA  
3772  C C   . GLU A 463 ? 0.7873 1.0023 0.7233 0.0574  0.0552  0.2058  479 GLU B C   
3773  O O   . GLU A 463 ? 0.7606 0.9620 0.6915 0.0580  0.0505  0.2040  479 GLU B O   
3774  C CB  . GLU A 463 ? 0.8006 1.0515 0.7487 0.0490  0.0628  0.2144  479 GLU B CB  
3775  C CG  . GLU A 463 ? 0.9050 1.1800 0.8580 0.0524  0.0642  0.2187  479 GLU B CG  
3776  C CD  . GLU A 463 ? 0.9619 1.2493 0.9251 0.0401  0.0683  0.2233  479 GLU B CD  
3777  O OE1 . GLU A 463 ? 0.9472 1.2254 0.9135 0.0293  0.0704  0.2232  479 GLU B OE1 
3778  O OE2 . GLU A 463 ? 0.9422 1.2490 0.9110 0.0418  0.0690  0.2267  479 GLU B OE2 
3779  N N   . MET A 464 ? 0.8074 1.0167 0.7458 0.0547  0.0581  0.2040  480 MET B N   
3780  C CA  . MET A 464 ? 0.7972 0.9855 0.7345 0.0495  0.0567  0.1999  480 MET B CA  
3781  C C   . MET A 464 ? 0.8002 0.9741 0.7314 0.0604  0.0501  0.1954  480 MET B C   
3782  O O   . MET A 464 ? 0.8184 0.9764 0.7475 0.0570  0.0467  0.1938  480 MET B O   
3783  C CB  . MET A 464 ? 0.7536 0.9422 0.6953 0.0447  0.0612  0.1990  480 MET B CB  
3784  C CG  . MET A 464 ? 0.7818 0.9806 0.7298 0.0323  0.0660  0.2030  480 MET B CG  
3785  S SD  . MET A 464 ? 0.7356 0.9392 0.6889 0.0269  0.0708  0.2036  480 MET B SD  
3786  C CE  . MET A 464 ? 0.7325 0.9123 0.6837 0.0253  0.0686  0.1960  480 MET B CE  
3787  N N   . LYS A 465 ? 0.8045 0.9843 0.7327 0.0741  0.0478  0.1937  481 LYS B N   
3788  C CA  . LYS A 465 ? 0.7911 0.9590 0.7132 0.0862  0.0399  0.1895  481 LYS B CA  
3789  C C   . LYS A 465 ? 0.7988 0.9611 0.7172 0.0853  0.0351  0.1908  481 LYS B C   
3790  O O   . LYS A 465 ? 0.7913 0.9345 0.7069 0.0856  0.0294  0.1881  481 LYS B O   
3791  C CB  . LYS A 465 ? 0.8141 0.9950 0.7325 0.1025  0.0379  0.1884  481 LYS B CB  
3792  C CG  . LYS A 465 ? 0.7752 0.9539 0.6938 0.1079  0.0393  0.1852  481 LYS B CG  
3793  C CD  . LYS A 465 ? 0.7381 0.8952 0.6538 0.1152  0.0317  0.1783  481 LYS B CD  
3794  C CE  . LYS A 465 ? 0.7766 0.9345 0.6908 0.1246  0.0323  0.1747  481 LYS B CE  
3795  N NZ  . LYS A 465 ? 0.7931 0.9304 0.7055 0.1328  0.0241  0.1672  481 LYS B NZ  
3796  N N   . ARG A 466 ? 0.7980 0.9759 0.7164 0.0838  0.0370  0.1950  482 ARG B N   
3797  C CA  . ARG A 466 ? 0.8128 0.9840 0.7264 0.0838  0.0319  0.1959  482 ARG B CA  
3798  C C   . ARG A 466 ? 0.8075 0.9637 0.7222 0.0695  0.0336  0.1972  482 ARG B C   
3799  O O   . ARG A 466 ? 0.7564 0.8951 0.6666 0.0692  0.0284  0.1962  482 ARG B O   
3800  C CB  . ARG A 466 ? 0.8059 0.9975 0.7195 0.0864  0.0329  0.1993  482 ARG B CB  
3801  C CG  . ARG A 466 ? 0.8060 1.0140 0.7178 0.1017  0.0308  0.1980  482 ARG B CG  
3802  C CD  . ARG A 466 ? 0.9393 1.1719 0.8547 0.1017  0.0341  0.2020  482 ARG B CD  
3803  N NE  . ARG A 466 ? 0.9734 1.2249 0.8882 0.1160  0.0335  0.2012  482 ARG B NE  
3804  C CZ  . ARG A 466 ? 0.9831 1.2462 0.8944 0.1269  0.0289  0.2003  482 ARG B CZ  
3805  N NH1 . ARG A 466 ? 0.9762 1.2344 0.8842 0.1253  0.0241  0.2001  482 ARG B NH1 
3806  N NH2 . ARG A 466 ? 0.9849 1.2656 0.8955 0.1404  0.0289  0.1993  482 ARG B NH2 
3807  N N   . GLU A 467 ? 0.8502 1.0131 0.7709 0.0575  0.0408  0.1996  483 GLU B N   
3808  C CA  . GLU A 467 ? 0.9078 1.0605 0.8289 0.0447  0.0428  0.2012  483 GLU B CA  
3809  C C   . GLU A 467 ? 0.9546 1.0873 0.8762 0.0405  0.0418  0.1981  483 GLU B C   
3810  O O   . GLU A 467 ? 0.9941 1.1125 0.9121 0.0364  0.0394  0.1989  483 GLU B O   
3811  C CB  . GLU A 467 ? 0.9341 1.0994 0.8617 0.0339  0.0496  0.2038  483 GLU B CB  
3812  C CG  . GLU A 467 ? 1.0149 1.1703 0.9423 0.0216  0.0516  0.2048  483 GLU B CG  
3813  C CD  . GLU A 467 ? 1.2029 1.3709 1.1361 0.0121  0.0566  0.2069  483 GLU B CD  
3814  O OE1 . GLU A 467 ? 1.3085 1.4887 1.2420 0.0123  0.0564  0.2097  483 GLU B OE1 
3815  O OE2 . GLU A 467 ? 1.2704 1.4356 1.2084 0.0047  0.0602  0.2053  483 GLU B OE2 
3816  N N   . ILE A 468 ? 0.8944 1.0259 0.8205 0.0415  0.0438  0.1949  484 ILE B N   
3817  C CA  . ILE A 468 ? 0.8191 0.9340 0.7481 0.0365  0.0438  0.1913  484 ILE B CA  
3818  C C   . ILE A 468 ? 0.7773 0.8780 0.7034 0.0467  0.0363  0.1877  484 ILE B C   
3819  O O   . ILE A 468 ? 0.7656 0.8498 0.6912 0.0432  0.0331  0.1872  484 ILE B O   
3820  C CB  . ILE A 468 ? 0.7912 0.9107 0.7262 0.0332  0.0485  0.1887  484 ILE B CB  
3821  C CG1 . ILE A 468 ? 0.7704 0.9015 0.7092 0.0220  0.0549  0.1917  484 ILE B CG1 
3822  C CG2 . ILE A 468 ? 0.8377 0.9402 0.7758 0.0298  0.0474  0.1841  484 ILE B CG2 
3823  C CD1 . ILE A 468 ? 0.7628 0.8998 0.7066 0.0196  0.0588  0.1898  484 ILE B CD1 
3824  N N   . VAL A 469 ? 0.7684 0.8755 0.6927 0.0596  0.0333  0.1853  485 VAL B N   
3825  C CA  . VAL A 469 ? 0.7600 0.8545 0.6820 0.0713  0.0252  0.1808  485 VAL B CA  
3826  C C   . VAL A 469 ? 0.7513 0.8405 0.6667 0.0783  0.0177  0.1821  485 VAL B C   
3827  O O   . VAL A 469 ? 0.7437 0.8158 0.6577 0.0830  0.0101  0.1793  485 VAL B O   
3828  C CB  . VAL A 469 ? 0.7644 0.8689 0.6858 0.0837  0.0249  0.1776  485 VAL B CB  
3829  C CG1 . VAL A 469 ? 0.7791 0.8696 0.6985 0.0962  0.0161  0.1718  485 VAL B CG1 
3830  C CG2 . VAL A 469 ? 0.7511 0.8598 0.6782 0.0761  0.0321  0.1767  485 VAL B CG2 
3831  N N   . GLY A 470 ? 0.7614 0.8640 0.6728 0.0793  0.0189  0.1861  486 GLY B N   
3832  C CA  . GLY A 470 ? 0.8027 0.9002 0.7069 0.0877  0.0107  0.1864  486 GLY B CA  
3833  C C   . GLY A 470 ? 0.7973 0.8996 0.6980 0.1054  0.0040  0.1822  486 GLY B C   
3834  O O   . GLY A 470 ? 0.7735 0.8627 0.6694 0.1146  -0.0059 0.1794  486 GLY B O   
3835  N N   . VAL A 471 ? 0.8378 0.9588 0.7406 0.1106  0.0089  0.1817  487 VAL B N   
3836  C CA  . VAL A 471 ? 0.8358 0.9649 0.7350 0.1280  0.0041  0.1778  487 VAL B CA  
3837  C C   . VAL A 471 ? 0.8287 0.9849 0.7279 0.1313  0.0098  0.1814  487 VAL B C   
3838  O O   . VAL A 471 ? 0.8013 0.9688 0.7059 0.1199  0.0188  0.1856  487 VAL B O   
3839  C CB  . VAL A 471 ? 0.7926 0.9150 0.6949 0.1316  0.0045  0.1733  487 VAL B CB  
3840  C CG1 . VAL A 471 ? 0.8222 0.9579 0.7205 0.1490  0.0021  0.1703  487 VAL B CG1 
3841  C CG2 . VAL A 471 ? 0.7848 0.8817 0.6879 0.1310  -0.0031 0.1692  487 VAL B CG2 
3842  N N   . VAL A 472 ? 0.8531 1.0202 0.7469 0.1470  0.0044  0.1795  488 VAL B N   
3843  C CA  . VAL A 472 ? 0.8688 1.0629 0.7632 0.1508  0.0091  0.1829  488 VAL B CA  
3844  C C   . VAL A 472 ? 0.8975 1.1072 0.7892 0.1678  0.0081  0.1802  488 VAL B C   
3845  O O   . VAL A 472 ? 0.9111 1.1117 0.7968 0.1822  -0.0008 0.1746  488 VAL B O   
3846  C CB  . VAL A 472 ? 0.9096 1.1061 0.7999 0.1526  0.0040  0.1839  488 VAL B CB  
3847  C CG1 . VAL A 472 ? 0.9243 1.1065 0.8063 0.1673  -0.0088 0.1782  488 VAL B CG1 
3848  C CG2 . VAL A 472 ? 0.8988 1.1245 0.7916 0.1562  0.0090  0.1871  488 VAL B CG2 
3849  N N   . GLU A 473 ? 0.8728 1.1064 0.7689 0.1664  0.0171  0.1845  489 GLU B N   
3850  C CA  . GLU A 473 ? 0.8822 1.1336 0.7758 0.1816  0.0182  0.1833  489 GLU B CA  
3851  C C   . GLU A 473 ? 0.9976 1.2629 0.8858 0.1969  0.0117  0.1812  489 GLU B C   
3852  O O   . GLU A 473 ? 1.0621 1.3371 0.9523 0.1923  0.0123  0.1840  489 GLU B O   
3853  C CB  . GLU A 473 ? 0.8725 1.1461 0.7731 0.1739  0.0302  0.1899  489 GLU B CB  
3854  C CG  . GLU A 473 ? 0.9026 1.2000 0.8090 0.1685  0.0352  0.1957  489 GLU B CG  
3855  C CD  . GLU A 473 ? 0.9207 1.2098 0.8326 0.1505  0.0372  0.1988  489 GLU B CD  
3856  O OE1 . GLU A 473 ? 0.9189 1.1836 0.8284 0.1443  0.0328  0.1960  489 GLU B OE1 
3857  O OE2 . GLU A 473 ? 0.9225 1.2300 0.8413 0.1432  0.0426  0.2040  489 GLU B OE2 
3858  N N   . PRO A 474 ? 1.1099 1.3759 0.9909 0.2158  0.0047  0.1756  490 PRO B N   
3859  C CA  . PRO A 474 ? 1.1123 1.3932 0.9878 0.2318  -0.0019 0.1728  490 PRO B CA  
3860  C C   . PRO A 474 ? 1.1340 1.4498 1.0123 0.2382  0.0062  0.1768  490 PRO B C   
3861  O O   . PRO A 474 ? 1.2324 1.5633 1.1064 0.2527  0.0011  0.1741  490 PRO B O   
3862  C CB  . PRO A 474 ? 1.1044 1.3697 0.9711 0.2497  -0.0136 0.1645  490 PRO B CB  
3863  C CG  . PRO A 474 ? 1.1029 1.3591 0.9713 0.2470  -0.0092 0.1642  490 PRO B CG  
3864  C CD  . PRO A 474 ? 1.0566 1.3062 0.9337 0.2241  0.0003  0.1702  490 PRO B CD  
3865  N N   . VAL A 475 ? 1.0370 1.3664 0.9224 0.2282  0.0182  0.1833  491 VAL B N   
3866  C CA  . VAL A 475 ? 1.0364 1.3998 0.9264 0.2317  0.0270  0.1888  491 VAL B CA  
3867  C C   . VAL A 475 ? 1.0417 1.4119 0.9429 0.2109  0.0383  0.1972  491 VAL B C   
3868  O O   . VAL A 475 ? 1.1136 1.4668 1.0167 0.1996  0.0415  0.1984  491 VAL B O   
3869  C CB  . VAL A 475 ? 1.0379 1.4132 0.9225 0.2475  0.0291  0.1876  491 VAL B CB  
3870  C CG1 . VAL A 475 ? 1.0871 1.4990 0.9778 0.2486  0.0402  0.1952  491 VAL B CG1 
3871  C CG2 . VAL A 475 ? 0.9652 1.3320 0.8382 0.2694  0.0165  0.1783  491 VAL B CG2 
3872  N N   . PRO A 476 ? 1.0291 1.4232 0.9384 0.2052  0.0441  0.2027  492 PRO B N   
3873  C CA  . PRO A 476 ? 1.0782 1.4787 0.9988 0.1861  0.0540  0.2106  492 PRO B CA  
3874  C C   . PRO A 476 ? 1.1024 1.5146 1.0251 0.1863  0.0629  0.2156  492 PRO B C   
3875  O O   . PRO A 476 ? 1.1082 1.5416 1.0284 0.1999  0.0654  0.2167  492 PRO B O   
3876  C CB  . PRO A 476 ? 1.1102 1.5352 1.0392 0.1832  0.0563  0.2144  492 PRO B CB  
3877  C CG  . PRO A 476 ? 1.2027 1.6438 1.1254 0.2030  0.0515  0.2102  492 PRO B CG  
3878  C CD  . PRO A 476 ? 1.1500 1.5660 1.0596 0.2154  0.0411  0.2017  492 PRO B CD  
3879  N N   . HIS A 477 ? 1.0203 1.4187 0.9472 0.1711  0.0675  0.2187  493 HIS B N   
3880  C CA  . HIS A 477 ? 0.9708 1.3740 0.8984 0.1696  0.0750  0.2231  493 HIS B CA  
3881  C C   . HIS A 477 ? 0.9346 1.3489 0.8747 0.1514  0.0836  0.2319  493 HIS B C   
3882  O O   . HIS A 477 ? 0.9437 1.3405 0.8878 0.1363  0.0835  0.2319  493 HIS B O   
3883  C CB  . HIS A 477 ? 0.9860 1.3600 0.9066 0.1691  0.0713  0.2176  493 HIS B CB  
3884  C CG  . HIS A 477 ? 0.9681 1.3336 0.8770 0.1886  0.0638  0.2100  493 HIS B CG  
3885  N ND1 . HIS A 477 ? 0.9917 1.3307 0.8945 0.1910  0.0586  0.2036  493 HIS B ND1 
3886  C CD2 . HIS A 477 ? 0.9846 1.3654 0.8873 0.2074  0.0603  0.2073  493 HIS B CD2 
3887  C CE1 . HIS A 477 ? 0.9822 1.3193 0.8756 0.2103  0.0516  0.1973  493 HIS B CE1 
3888  N NE2 . HIS A 477 ? 0.9499 1.3121 0.8425 0.2209  0.0524  0.1993  493 HIS B NE2 
3889  N N   . ASP A 478 ? 0.9396 1.3827 0.8859 0.1530  0.0910  0.2392  494 ASP B N   
3890  C CA  . ASP A 478 ? 0.9492 1.4021 0.9079 0.1359  0.0988  0.2481  494 ASP B CA  
3891  C C   . ASP A 478 ? 0.9419 1.3808 0.8978 0.1301  0.1026  0.2501  494 ASP B C   
3892  O O   . ASP A 478 ? 0.9204 1.3452 0.8652 0.1405  0.1001  0.2451  494 ASP B O   
3893  C CB  . ASP A 478 ? 0.9132 1.4004 0.8814 0.1383  0.1053  0.2555  494 ASP B CB  
3894  C CG  . ASP A 478 ? 0.9573 1.4580 0.9185 0.1556  0.1074  0.2550  494 ASP B CG  
3895  O OD1 . ASP A 478 ? 1.0142 1.4988 0.9610 0.1660  0.1048  0.2506  494 ASP B OD1 
3896  O OD2 . ASP A 478 ? 1.0422 1.5684 1.0127 0.1582  0.1114  0.2591  494 ASP B OD2 
3897  N N   . GLU A 479 ? 1.0457 1.4845 1.0158 0.1132  0.1056  0.2536  495 GLU B N   
3898  C CA  . GLU A 479 ? 0.9965 1.4182 0.9677 0.1042  0.1070  0.2532  495 GLU B CA  
3899  C C   . GLU A 479 ? 0.9610 1.3895 0.9277 0.1145  0.1104  0.2544  495 GLU B C   
3900  O O   . GLU A 479 ? 0.9138 1.3330 0.8827 0.1070  0.1123  0.2556  495 GLU B O   
3901  C CB  . GLU A 479 ? 1.0138 1.4360 1.0008 0.0850  0.1080  0.2566  495 GLU B CB  
3902  C CG  . GLU A 479 ? 1.0502 1.4671 1.0423 0.0749  0.1047  0.2555  495 GLU B CG  
3903  C CD  . GLU A 479 ? 1.0083 1.3993 0.9909 0.0724  0.1010  0.2502  495 GLU B CD  
3904  O OE1 . GLU A 479 ? 1.0280 1.4027 1.0047 0.0720  0.1012  0.2478  495 GLU B OE1 
3905  O OE2 . GLU A 479 ? 1.0915 1.4788 1.0714 0.0719  0.0980  0.2488  495 GLU B OE2 
3906  N N   . THR A 480 ? 0.9247 1.3696 0.8843 0.1321  0.1110  0.2542  496 THR B N   
3907  C CA  . THR A 480 ? 0.9454 1.3948 0.8977 0.1446  0.1136  0.2543  496 THR B CA  
3908  C C   . THR A 480 ? 0.9830 1.4122 0.9178 0.1571  0.1098  0.2480  496 THR B C   
3909  O O   . THR A 480 ? 0.9395 1.3671 0.8667 0.1671  0.1113  0.2471  496 THR B O   
3910  C CB  . THR A 480 ? 0.9347 1.4128 0.8874 0.1593  0.1157  0.2566  496 THR B CB  
3911  O OG1 . THR A 480 ? 0.9278 1.4078 0.8698 0.1736  0.1111  0.2517  496 THR B OG1 
3912  C CG2 . THR A 480 ? 0.9689 1.4683 0.9391 0.1476  0.1188  0.2631  496 THR B CG2 
3913  N N   . TYR A 481 ? 0.9872 1.4017 0.9153 0.1578  0.1044  0.2438  497 TYR B N   
3914  C CA  . TYR A 481 ? 0.9646 1.3531 0.8806 0.1663  0.0974  0.2348  497 TYR B CA  
3915  C C   . TYR A 481 ? 0.9614 1.3253 0.8788 0.1525  0.0973  0.2332  497 TYR B C   
3916  O O   . TYR A 481 ? 0.9653 1.3304 0.8919 0.1354  0.1017  0.2390  497 TYR B O   
3917  C CB  . TYR A 481 ? 0.9713 1.3490 0.8860 0.1704  0.0884  0.2269  497 TYR B CB  
3918  C CG  . TYR A 481 ? 0.9427 1.3383 0.8525 0.1882  0.0854  0.2249  497 TYR B CG  
3919  C CD1 . TYR A 481 ? 0.9373 1.3603 0.8543 0.1874  0.0895  0.2309  497 TYR B CD1 
3920  C CD2 . TYR A 481 ? 0.9858 1.3708 0.8841 0.2065  0.0777  0.2164  497 TYR B CD2 
3921  C CE1 . TYR A 481 ? 0.9585 1.3986 0.8706 0.2048  0.0864  0.2283  497 TYR B CE1 
3922  C CE2 . TYR A 481 ? 0.9625 1.3633 0.8557 0.2239  0.0739  0.2137  497 TYR B CE2 
3923  C CZ  . TYR A 481 ? 0.9380 1.3665 0.8376 0.2233  0.0784  0.2195  497 TYR B CZ  
3924  O OH  . TYR A 481 ? 0.9700 1.4148 0.8639 0.2419  0.0741  0.2160  497 TYR B OH  
3925  N N   . CYS A 482 ? 0.9482 1.2893 0.8568 0.1606  0.0912  0.2245  498 CYS B N   
3926  C CA  . CYS A 482 ? 0.9597 1.2755 0.8694 0.1490  0.0893  0.2205  498 CYS B CA  
3927  C C   . CYS A 482 ? 0.9934 1.2859 0.8966 0.1583  0.0798  0.2093  498 CYS B C   
3928  O O   . CYS A 482 ? 0.9729 1.2515 0.8687 0.1674  0.0768  0.2036  498 CYS B O   
3929  C CB  . CYS A 482 ? 0.9052 1.2198 0.8120 0.1470  0.0947  0.2242  498 CYS B CB  
3930  S SG  . CYS A 482 ? 0.8546 1.1430 0.7658 0.1291  0.0934  0.2208  498 CYS B SG  
3931  N N   . ASP A 483 ? 1.1346 1.4220 1.0408 0.1563  0.0745  0.2060  499 ASP B N   
3932  C CA  . ASP A 483 ? 1.1301 1.3951 1.0313 0.1641  0.0650  0.1962  499 ASP B CA  
3933  C C   . ASP A 483 ? 1.0977 1.3372 1.0003 0.1551  0.0628  0.1908  499 ASP B C   
3934  O O   . ASP A 483 ? 1.1176 1.3411 1.0145 0.1659  0.0565  0.1830  499 ASP B O   
3935  C CB  . ASP A 483 ? 1.1184 1.3834 1.0222 0.1626  0.0600  0.1950  499 ASP B CB  
3936  C CG  . ASP A 483 ? 1.1430 1.4331 1.0451 0.1734  0.0610  0.1987  499 ASP B CG  
3937  O OD1 . ASP A 483 ? 1.1068 1.4120 1.0038 0.1862  0.0639  0.2004  499 ASP B OD1 
3938  O OD2 . ASP A 483 ? 1.1493 1.4443 1.0548 0.1695  0.0590  0.1999  499 ASP B OD2 
3939  N N   . PRO A 484 ? 1.0336 1.2682 0.9438 0.1366  0.0670  0.1938  500 PRO B N   
3940  C CA  . PRO A 484 ? 0.9789 1.1915 0.8899 0.1297  0.0654  0.1882  500 PRO B CA  
3941  C C   . PRO A 484 ? 0.9962 1.2026 0.8995 0.1426  0.0641  0.1839  500 PRO B C   
3942  O O   . PRO A 484 ? 0.9792 1.1676 0.8792 0.1506  0.0572  0.1753  500 PRO B O   
3943  C CB  . PRO A 484 ? 0.9200 1.1377 0.8384 0.1116  0.0721  0.1943  500 PRO B CB  
3944  C CG  . PRO A 484 ? 0.9063 1.1407 0.8298 0.1059  0.0746  0.2008  500 PRO B CG  
3945  C CD  . PRO A 484 ? 0.9827 1.2315 0.9011 0.1219  0.0728  0.2016  500 PRO B CD  
3946  N N   . ALA A 485 ? 0.9239 1.1462 0.8242 0.1455  0.0705  0.1902  501 ALA B N   
3947  C CA  . ALA A 485 ? 0.8907 1.1094 0.7827 0.1567  0.0709  0.1880  501 ALA B CA  
3948  C C   . ALA A 485 ? 0.8749 1.0916 0.7576 0.1785  0.0644  0.1816  501 ALA B C   
3949  O O   . ALA A 485 ? 0.7888 1.0020 0.6632 0.1906  0.0637  0.1787  501 ALA B O   
3950  C CB  . ALA A 485 ? 0.8497 1.0893 0.7410 0.1541  0.0800  0.1985  501 ALA B CB  
3951  N N   . SER A 486 ? 0.9819 1.2002 0.8653 0.1845  0.0590  0.1790  502 SER B N   
3952  C CA  . SER A 486 ? 1.0050 1.2205 0.8797 0.2059  0.0514  0.1722  502 SER B CA  
3953  C C   . SER A 486 ? 0.9892 1.1768 0.8639 0.2091  0.0417  0.1612  502 SER B C   
3954  O O   . SER A 486 ? 1.0042 1.1855 0.8723 0.2270  0.0335  0.1541  502 SER B O   
3955  C CB  . SER A 486 ? 1.0202 1.2500 0.8946 0.2134  0.0484  0.1738  502 SER B CB  
3956  O OG  . SER A 486 ? 1.0822 1.2956 0.9614 0.2077  0.0411  0.1688  502 SER B OG  
3957  N N   . LEU A 487 ? 0.9620 1.1335 0.8445 0.1925  0.0420  0.1594  503 LEU B N   
3958  C CA  . LEU A 487 ? 0.9361 1.0819 0.8206 0.1936  0.0338  0.1493  503 LEU B CA  
3959  C C   . LEU A 487 ? 0.8704 1.0067 0.7530 0.1922  0.0361  0.1462  503 LEU B C   
3960  O O   . LEU A 487 ? 0.8380 0.9828 0.7216 0.1816  0.0444  0.1525  503 LEU B O   
3961  C CB  . LEU A 487 ? 0.8898 1.0243 0.7843 0.1767  0.0323  0.1489  503 LEU B CB  
3962  C CG  . LEU A 487 ? 0.8317 0.9407 0.7314 0.1735  0.0253  0.1397  503 LEU B CG  
3963  C CD1 . LEU A 487 ? 0.8096 0.9087 0.7061 0.1899  0.0143  0.1328  503 LEU B CD1 
3964  C CD2 . LEU A 487 ? 0.7786 0.8808 0.6878 0.1544  0.0270  0.1417  503 LEU B CD2 
3965  N N   . PHE A 488 ? 0.9024 1.0210 0.7821 0.2039  0.0280  0.1362  504 PHE B N   
3966  C CA  . PHE A 488 ? 0.8965 1.0063 0.7717 0.2075  0.0288  0.1321  504 PHE B CA  
3967  C C   . PHE A 488 ? 0.8781 0.9829 0.7603 0.1874  0.0349  0.1343  504 PHE B C   
3968  O O   . PHE A 488 ? 0.8893 1.0010 0.7674 0.1844  0.0414  0.1389  504 PHE B O   
3969  C CB  . PHE A 488 ? 0.8810 0.9693 0.7552 0.2206  0.0176  0.1196  504 PHE B CB  
3970  C CG  . PHE A 488 ? 0.8998 0.9745 0.7718 0.2215  0.0172  0.1134  504 PHE B CG  
3971  C CD1 . PHE A 488 ? 0.9507 1.0309 0.8106 0.2357  0.0189  0.1136  504 PHE B CD1 
3972  C CD2 . PHE A 488 ? 0.9120 0.9685 0.7937 0.2089  0.0148  0.1071  504 PHE B CD2 
3973  C CE1 . PHE A 488 ? 0.9682 1.0347 0.8251 0.2371  0.0180  0.1076  504 PHE B CE1 
3974  C CE2 . PHE A 488 ? 0.9581 1.0021 0.8378 0.2101  0.0138  0.1006  504 PHE B CE2 
3975  C CZ  . PHE A 488 ? 0.9792 1.0275 0.8462 0.2243  0.0151  0.1007  504 PHE B CZ  
3976  N N   . HIS A 489 ? 0.8163 0.9092 0.7089 0.1736  0.0327  0.1313  505 HIS B N   
3977  C CA  . HIS A 489 ? 0.7783 0.8643 0.6776 0.1561  0.0369  0.1312  505 HIS B CA  
3978  C C   . HIS A 489 ? 0.7878 0.8918 0.6871 0.1445  0.0464  0.1421  505 HIS B C   
3979  O O   . HIS A 489 ? 0.8165 0.9180 0.7166 0.1353  0.0502  0.1429  505 HIS B O   
3980  C CB  . HIS A 489 ? 0.7043 0.7781 0.6145 0.1439  0.0335  0.1274  505 HIS B CB  
3981  C CG  . HIS A 489 ? 0.7967 0.8522 0.7092 0.1535  0.0238  0.1172  505 HIS B CG  
3982  N ND1 . HIS A 489 ? 0.8236 0.8790 0.7322 0.1687  0.0170  0.1154  505 HIS B ND1 
3983  C CD2 . HIS A 489 ? 0.8472 0.8841 0.7665 0.1501  0.0190  0.1081  505 HIS B CD2 
3984  C CE1 . HIS A 489 ? 0.8696 0.9061 0.7826 0.1740  0.0081  0.1058  505 HIS B CE1 
3985  N NE2 . HIS A 489 ? 0.8511 0.8766 0.7712 0.1627  0.0094  0.1013  505 HIS B NE2 
3986  N N   . VAL A 490 ? 0.7934 0.9154 0.6921 0.1451  0.0498  0.1503  506 VAL B N   
3987  C CA  . VAL A 490 ? 0.8341 0.9735 0.7350 0.1333  0.0582  0.1607  506 VAL B CA  
3988  C C   . VAL A 490 ? 0.8144 0.9634 0.7074 0.1397  0.0630  0.1654  506 VAL B C   
3989  O O   . VAL A 490 ? 0.7939 0.9440 0.6887 0.1286  0.0677  0.1693  506 VAL B O   
3990  C CB  . VAL A 490 ? 0.8692 1.0251 0.7725 0.1326  0.0598  0.1674  506 VAL B CB  
3991  C CG1 . VAL A 490 ? 0.8271 1.0018 0.7339 0.1211  0.0680  0.1781  506 VAL B CG1 
3992  C CG2 . VAL A 490 ? 0.8222 0.9667 0.7327 0.1240  0.0556  0.1636  506 VAL B CG2 
3993  N N   . SER A 491 ? 0.7379 0.8940 0.6219 0.1579  0.0616  0.1652  507 SER B N   
3994  C CA  . SER A 491 ? 0.7839 0.9506 0.6585 0.1670  0.0663  0.1703  507 SER B CA  
3995  C C   . SER A 491 ? 0.8291 0.9780 0.6973 0.1725  0.0634  0.1630  507 SER B C   
3996  O O   . SER A 491 ? 0.8768 1.0320 0.7352 0.1823  0.0664  0.1663  507 SER B O   
3997  C CB  . SER A 491 ? 0.8191 0.9998 0.6855 0.1865  0.0652  0.1715  507 SER B CB  
3998  O OG  . SER A 491 ? 0.8101 0.9753 0.6747 0.1985  0.0555  0.1607  507 SER B OG  
3999  N N   . ASN A 492 ? 0.8360 0.9634 0.7091 0.1676  0.0574  0.1531  508 ASN B N   
4000  C CA  . ASN A 492 ? 0.8262 0.9360 0.6944 0.1718  0.0541  0.1453  508 ASN B CA  
4001  C C   . ASN A 492 ? 0.7917 0.8896 0.6684 0.1532  0.0548  0.1427  508 ASN B C   
4002  O O   . ASN A 492 ? 0.8366 0.9170 0.7118 0.1547  0.0506  0.1339  508 ASN B O   
4003  C CB  . ASN A 492 ? 0.8820 0.9760 0.7472 0.1882  0.0444  0.1332  508 ASN B CB  
4004  C CG  . ASN A 492 ? 0.9134 1.0182 0.7672 0.2100  0.0429  0.1344  508 ASN B CG  
4005  O OD1 . ASN A 492 ? 0.9153 1.0163 0.7581 0.2246  0.0412  0.1312  508 ASN B OD1 
4006  N ND2 . ASN A 492 ? 0.9060 1.0256 0.7619 0.2122  0.0437  0.1395  508 ASN B ND2 
4007  N N   . ASP A 493 ? 0.7857 0.8928 0.6710 0.1365  0.0594  0.1497  509 ASP B N   
4008  C CA  . ASP A 493 ? 0.8150 0.9151 0.7071 0.1191  0.0610  0.1491  509 ASP B CA  
4009  C C   . ASP A 493 ? 0.7758 0.8550 0.6738 0.1162  0.0545  0.1367  509 ASP B C   
4010  O O   . ASP A 493 ? 0.8840 0.9506 0.7817 0.1124  0.0528  0.1307  509 ASP B O   
4011  C CB  . ASP A 493 ? 0.8217 0.9239 0.7067 0.1182  0.0648  0.1538  509 ASP B CB  
4012  C CG  . ASP A 493 ? 0.7801 0.8768 0.6712 0.1007  0.0661  0.1541  509 ASP B CG  
4013  O OD1 . ASP A 493 ? 0.7757 0.8776 0.6765 0.0871  0.0676  0.1568  509 ASP B OD1 
4014  O OD2 . ASP A 493 ? 0.8322 0.9211 0.7176 0.1008  0.0658  0.1528  509 ASP B OD2 
4015  N N   . TYR A 494 ? 0.6697 0.7455 0.5734 0.1178  0.0507  0.1329  510 TYR B N   
4016  C CA  . TYR A 494 ? 0.7529 0.8116 0.6648 0.1128  0.0453  0.1227  510 TYR B CA  
4017  C C   . TYR A 494 ? 0.7085 0.7713 0.6306 0.0966  0.0477  0.1261  510 TYR B C   
4018  O O   . TYR A 494 ? 0.7364 0.8105 0.6594 0.0961  0.0495  0.1328  510 TYR B O   
4019  C CB  . TYR A 494 ? 0.8056 0.8546 0.7161 0.1282  0.0378  0.1152  510 TYR B CB  
4020  C CG  . TYR A 494 ? 0.8550 0.8947 0.7568 0.1438  0.0336  0.1083  510 TYR B CG  
4021  C CD1 . TYR A 494 ? 0.8785 0.9019 0.7825 0.1421  0.0301  0.0987  510 TYR B CD1 
4022  C CD2 . TYR A 494 ? 0.8838 0.9317 0.7746 0.1607  0.0333  0.1114  510 TYR B CD2 
4023  C CE1 . TYR A 494 ? 0.9123 0.9263 0.8073 0.1570  0.0259  0.0920  510 TYR B CE1 
4024  C CE2 . TYR A 494 ? 0.9005 0.9397 0.7818 0.1760  0.0295  0.1051  510 TYR B CE2 
4025  C CZ  . TYR A 494 ? 0.9172 0.9389 0.8005 0.1740  0.0256  0.0953  510 TYR B CZ  
4026  O OH  . TYR A 494 ? 0.8712 0.8836 0.7444 0.1899  0.0214  0.0887  510 TYR B OH  
4027  N N   . SER A 495 ? 0.6378 0.6916 0.5671 0.0840  0.0474  0.1212  511 SER B N   
4028  C CA  . SER A 495 ? 0.6617 0.7195 0.5995 0.0701  0.0496  0.1244  511 SER B CA  
4029  C C   . SER A 495 ? 0.6848 0.7371 0.6262 0.0752  0.0453  0.1217  511 SER B C   
4030  O O   . SER A 495 ? 0.7301 0.7698 0.6718 0.0850  0.0394  0.1137  511 SER B O   
4031  C CB  . SER A 495 ? 0.6609 0.7108 0.6060 0.0565  0.0499  0.1189  511 SER B CB  
4032  O OG  . SER A 495 ? 0.7341 0.7684 0.6842 0.0590  0.0447  0.1081  511 SER B OG  
4033  N N   . PHE A 496 ? 0.7000 0.7614 0.6441 0.0691  0.0476  0.1285  512 PHE B N   
4034  C CA  . PHE A 496 ? 0.6471 0.7034 0.5935 0.0738  0.0433  0.1273  512 PHE B CA  
4035  C C   . PHE A 496 ? 0.6498 0.6979 0.6054 0.0616  0.0427  0.1249  512 PHE B C   
4036  O O   . PHE A 496 ? 0.6712 0.7089 0.6302 0.0659  0.0374  0.1211  512 PHE B O   
4037  C CB  . PHE A 496 ? 0.6594 0.7302 0.6013 0.0777  0.0451  0.1362  512 PHE B CB  
4038  C CG  . PHE A 496 ? 0.6557 0.7218 0.5951 0.0908  0.0387  0.1342  512 PHE B CG  
4039  C CD1 . PHE A 496 ? 0.6533 0.7144 0.5871 0.1072  0.0337  0.1290  512 PHE B CD1 
4040  C CD2 . PHE A 496 ? 0.6679 0.7332 0.6103 0.0870  0.0369  0.1370  512 PHE B CD2 
4041  C CE1 . PHE A 496 ? 0.7170 0.7733 0.6486 0.1199  0.0265  0.1266  512 PHE B CE1 
4042  C CE2 . PHE A 496 ? 0.6801 0.7398 0.6202 0.0988  0.0299  0.1350  512 PHE B CE2 
4043  C CZ  . PHE A 496 ? 0.7439 0.7991 0.6790 0.1155  0.0243  0.1296  512 PHE B CZ  
4044  N N   . ILE A 497 ? 0.6547 0.7070 0.6146 0.0469  0.0476  0.1271  513 ILE B N   
4045  C CA  . ILE A 497 ? 0.6842 0.7313 0.6518 0.0357  0.0479  0.1262  513 ILE B CA  
4046  C C   . ILE A 497 ? 0.7302 0.7611 0.7048 0.0368  0.0432  0.1165  513 ILE B C   
4047  O O   . ILE A 497 ? 0.7203 0.7454 0.7014 0.0308  0.0423  0.1160  513 ILE B O   
4048  C CB  . ILE A 497 ? 0.6513 0.7067 0.6215 0.0210  0.0536  0.1295  513 ILE B CB  
4049  C CG1 . ILE A 497 ? 0.6723 0.7290 0.6465 0.0115  0.0553  0.1333  513 ILE B CG1 
4050  C CG2 . ILE A 497 ? 0.6517 0.7001 0.6267 0.0149  0.0536  0.1217  513 ILE B CG2 
4051  C CD1 . ILE A 497 ? 0.6733 0.7369 0.6429 0.0158  0.0551  0.1410  513 ILE B CD1 
4052  N N   . ARG A 498 ? 0.7370 0.7605 0.7106 0.0448  0.0400  0.1090  514 ARG B N   
4053  C CA  . ARG A 498 ? 0.6579 0.6663 0.6393 0.0464  0.0350  0.0990  514 ARG B CA  
4054  C C   . ARG A 498 ? 0.6776 0.6776 0.6628 0.0516  0.0295  0.0986  514 ARG B C   
4055  O O   . ARG A 498 ? 0.6428 0.6320 0.6379 0.0478  0.0265  0.0928  514 ARG B O   
4056  C CB  . ARG A 498 ? 0.6606 0.6617 0.6382 0.0578  0.0311  0.0911  514 ARG B CB  
4057  C CG  . ARG A 498 ? 0.6694 0.6667 0.6404 0.0753  0.0253  0.0901  514 ARG B CG  
4058  C CD  . ARG A 498 ? 0.7211 0.7228 0.6812 0.0857  0.0260  0.0902  514 ARG B CD  
4059  N NE  . ARG A 498 ? 0.8359 0.8277 0.7969 0.0873  0.0238  0.0809  514 ARG B NE  
4060  C CZ  . ARG A 498 ? 0.9134 0.9086 0.8657 0.0913  0.0260  0.0814  514 ARG B CZ  
4061  N NH1 . ARG A 498 ? 0.8219 0.8305 0.7647 0.0944  0.0304  0.0908  514 ARG B NH1 
4062  N NH2 . ARG A 498 ? 1.0000 0.9848 0.9532 0.0918  0.0235  0.0723  514 ARG B NH2 
4063  N N   . TYR A 499 ? 0.6921 0.6971 0.6705 0.0600  0.0279  0.1048  515 TYR B N   
4064  C CA  . TYR A 499 ? 0.6790 0.6751 0.6604 0.0654  0.0216  0.1046  515 TYR B CA  
4065  C C   . TYR A 499 ? 0.6690 0.6658 0.6559 0.0522  0.0244  0.1102  515 TYR B C   
4066  O O   . TYR A 499 ? 0.7325 0.7177 0.7269 0.0506  0.0197  0.1080  515 TYR B O   
4067  C CB  . TYR A 499 ? 0.6570 0.6584 0.6286 0.0799  0.0181  0.1083  515 TYR B CB  
4068  C CG  . TYR A 499 ? 0.6789 0.6793 0.6440 0.0949  0.0149  0.1029  515 TYR B CG  
4069  C CD1 . TYR A 499 ? 0.7071 0.6924 0.6755 0.1054  0.0065  0.0933  515 TYR B CD1 
4070  C CD2 . TYR A 499 ? 0.7464 0.7604 0.7024 0.0982  0.0202  0.1072  515 TYR B CD2 
4071  C CE1 . TYR A 499 ? 0.7675 0.7514 0.7286 0.1205  0.0033  0.0880  515 TYR B CE1 
4072  C CE2 . TYR A 499 ? 0.7781 0.7912 0.7269 0.1123  0.0178  0.1029  515 TYR B CE2 
4073  C CZ  . TYR A 499 ? 0.7781 0.7761 0.7287 0.1238  0.0093  0.0931  515 TYR B CZ  
4074  O OH  . TYR A 499 ? 0.7859 0.7829 0.7280 0.1386  0.0069  0.0887  515 TYR B OH  
4075  N N   . TYR A 500 ? 0.6467 0.6564 0.6304 0.0424  0.0317  0.1175  516 TYR B N   
4076  C CA  . TYR A 500 ? 0.6654 0.6760 0.6532 0.0295  0.0350  0.1228  516 TYR B CA  
4077  C C   . TYR A 500 ? 0.7280 0.7309 0.7268 0.0188  0.0364  0.1173  516 TYR B C   
4078  O O   . TYR A 500 ? 0.7398 0.7338 0.7456 0.0146  0.0341  0.1173  516 TYR B O   
4079  C CB  . TYR A 500 ? 0.6429 0.6695 0.6246 0.0227  0.0419  0.1308  516 TYR B CB  
4080  C CG  . TYR A 500 ? 0.6008 0.6294 0.5844 0.0111  0.0453  0.1367  516 TYR B CG  
4081  C CD1 . TYR A 500 ? 0.6391 0.6689 0.6283 -0.0014 0.0501  0.1354  516 TYR B CD1 
4082  C CD2 . TYR A 500 ? 0.6304 0.6580 0.6102 0.0135  0.0430  0.1427  516 TYR B CD2 
4083  C CE1 . TYR A 500 ? 0.6773 0.7090 0.6675 -0.0113 0.0534  0.1407  516 TYR B CE1 
4084  C CE2 . TYR A 500 ? 0.6566 0.6846 0.6373 0.0031  0.0460  0.1480  516 TYR B CE2 
4085  C CZ  . TYR A 500 ? 0.6511 0.6814 0.6369 -0.0092 0.0515  0.1471  516 TYR B CZ  
4086  O OH  . TYR A 500 ? 0.7156 0.7469 0.7015 -0.0192 0.0551  0.1524  516 TYR B OH  
4087  N N   . THR A 501 ? 0.7559 0.7619 0.7566 0.0148  0.0396  0.1122  517 THR B N   
4088  C CA  . THR A 501 ? 0.6907 0.6916 0.7018 0.0054  0.0410  0.1059  517 THR B CA  
4089  C C   . THR A 501 ? 0.7087 0.6947 0.7288 0.0112  0.0342  0.0976  517 THR B C   
4090  O O   . THR A 501 ? 0.7008 0.6815 0.7316 0.0030  0.0345  0.0952  517 THR B O   
4091  C CB  . THR A 501 ? 0.6827 0.6905 0.6922 0.0016  0.0448  0.1022  517 THR B CB  
4092  O OG1 . THR A 501 ? 0.7265 0.7313 0.7306 0.0136  0.0411  0.0977  517 THR B OG1 
4093  C CG2 . THR A 501 ? 0.7497 0.7714 0.7528 -0.0058 0.0509  0.1102  517 THR B CG2 
4094  N N   . ARG A 502 ? 0.7966 0.7762 0.8130 0.0254  0.0279  0.0928  518 ARG B N   
4095  C CA  . ARG A 502 ? 0.7940 0.7586 0.8193 0.0322  0.0199  0.0848  518 ARG B CA  
4096  C C   . ARG A 502 ? 0.7957 0.7538 0.8266 0.0291  0.0169  0.0896  518 ARG B C   
4097  O O   . ARG A 502 ? 0.8210 0.7699 0.8646 0.0238  0.0144  0.0857  518 ARG B O   
4098  C CB  . ARG A 502 ? 0.8496 0.8090 0.8677 0.0499  0.0130  0.0802  518 ARG B CB  
4099  C CG  . ARG A 502 ? 0.8556 0.7991 0.8810 0.0597  0.0027  0.0738  518 ARG B CG  
4100  C CD  . ARG A 502 ? 0.9021 0.8431 0.9170 0.0786  -0.0043 0.0727  518 ARG B CD  
4101  N NE  . ARG A 502 ? 0.9201 0.8684 0.9266 0.0809  -0.0035 0.0824  518 ARG B NE  
4102  C CZ  . ARG A 502 ? 1.0054 0.9456 1.0145 0.0847  -0.0104 0.0843  518 ARG B CZ  
4103  N NH1 . ARG A 502 ? 1.0319 0.9563 1.0516 0.0881  -0.0191 0.0772  518 ARG B NH1 
4104  N NH2 . ARG A 502 ? 0.9756 0.9234 0.9766 0.0856  -0.0091 0.0931  518 ARG B NH2 
4105  N N   . THR A 503 ? 0.7805 0.7433 0.8022 0.0324  0.0169  0.0983  519 THR B N   
4106  C CA  . THR A 503 ? 0.7509 0.7063 0.7761 0.0305  0.0131  0.1034  519 THR B CA  
4107  C C   . THR A 503 ? 0.7292 0.6854 0.7632 0.0136  0.0190  0.1071  519 THR B C   
4108  O O   . THR A 503 ? 0.7471 0.6925 0.7911 0.0100  0.0151  0.1067  519 THR B O   
4109  C CB  . THR A 503 ? 0.7219 0.6841 0.7345 0.0371  0.0125  0.1115  519 THR B CB  
4110  O OG1 . THR A 503 ? 0.7339 0.6946 0.7396 0.0540  0.0062  0.1073  519 THR B OG1 
4111  C CG2 . THR A 503 ? 0.7534 0.7073 0.7679 0.0347  0.0083  0.1174  519 THR B CG2 
4112  N N   . LEU A 504 ? 0.7152 0.6842 0.7462 0.0033  0.0281  0.1106  520 LEU B N   
4113  C CA  . LEU A 504 ? 0.7075 0.6783 0.7464 -0.0118 0.0339  0.1138  520 LEU B CA  
4114  C C   . LEU A 504 ? 0.7387 0.7043 0.7918 -0.0173 0.0339  0.1051  520 LEU B C   
4115  O O   . LEU A 504 ? 0.7811 0.7424 0.8444 -0.0264 0.0350  0.1068  520 LEU B O   
4116  C CB  . LEU A 504 ? 0.7521 0.7380 0.7836 -0.0206 0.0428  0.1196  520 LEU B CB  
4117  C CG  . LEU A 504 ? 0.7559 0.7468 0.7780 -0.0224 0.0449  0.1303  520 LEU B CG  
4118  C CD1 . LEU A 504 ? 0.7367 0.7269 0.7493 -0.0096 0.0395  0.1324  520 LEU B CD1 
4119  C CD2 . LEU A 504 ? 0.7706 0.7764 0.7872 -0.0305 0.0529  0.1335  520 LEU B CD2 
4120  N N   . TYR A 505 ? 0.7109 0.6771 0.7652 -0.0122 0.0328  0.0959  521 TYR B N   
4121  C CA  . TYR A 505 ? 0.7177 0.6784 0.7860 -0.0162 0.0317  0.0864  521 TYR B CA  
4122  C C   . TYR A 505 ? 0.6731 0.6188 0.7529 -0.0123 0.0236  0.0834  521 TYR B C   
4123  O O   . TYR A 505 ? 0.6370 0.5795 0.7303 -0.0218 0.0247  0.0830  521 TYR B O   
4124  C CB  . TYR A 505 ? 0.6736 0.6348 0.7399 -0.0091 0.0300  0.0764  521 TYR B CB  
4125  C CG  . TYR A 505 ? 0.6557 0.6300 0.7126 -0.0130 0.0367  0.0776  521 TYR B CG  
4126  C CD1 . TYR A 505 ? 0.6845 0.6703 0.7401 -0.0253 0.0445  0.0840  521 TYR B CD1 
4127  C CD2 . TYR A 505 ? 0.6162 0.5909 0.6652 -0.0039 0.0346  0.0727  521 TYR B CD2 
4128  C CE1 . TYR A 505 ? 0.6567 0.6537 0.7042 -0.0283 0.0492  0.0848  521 TYR B CE1 
4129  C CE2 . TYR A 505 ? 0.6499 0.6354 0.6910 -0.0077 0.0397  0.0742  521 TYR B CE2 
4130  C CZ  . TYR A 505 ? 0.6620 0.6584 0.7027 -0.0199 0.0466  0.0800  521 TYR B CZ  
4131  O OH  . TYR A 505 ? 0.6225 0.6287 0.6559 -0.0231 0.0503  0.0811  521 TYR B OH  
4132  N N   . GLN A 506 ? 0.6925 0.6292 0.7673 0.0018  0.0151  0.0817  522 GLN B N   
4133  C CA  . GLN A 506 ? 0.7323 0.6533 0.8187 0.0073  0.0055  0.0766  522 GLN B CA  
4134  C C   . GLN A 506 ? 0.7303 0.6471 0.8268 -0.0042 0.0064  0.0838  522 GLN B C   
4135  O O   . GLN A 506 ? 0.7299 0.6373 0.8424 -0.0077 0.0022  0.0793  522 GLN B O   
4136  C CB  . GLN A 506 ? 0.7608 0.6739 0.8382 0.0246  -0.0040 0.0755  522 GLN B CB  
4137  C CG  . GLN A 506 ? 0.7797 0.6932 0.8476 0.0268  -0.0053 0.0859  522 GLN B CG  
4138  C CD  . GLN A 506 ? 0.8321 0.7407 0.8901 0.0453  -0.0142 0.0833  522 GLN B CD  
4139  O OE1 . GLN A 506 ? 0.8620 0.7758 0.9115 0.0548  -0.0138 0.0788  522 GLN B OE1 
4140  N NE2 . GLN A 506 ? 0.8654 0.7633 0.9243 0.0510  -0.0229 0.0860  522 GLN B NE2 
4141  N N   . PHE A 507 ? 0.7468 0.6707 0.8346 -0.0110 0.0121  0.0951  523 PHE B N   
4142  C CA  . PHE A 507 ? 0.7409 0.6605 0.8379 -0.0227 0.0136  0.1022  523 PHE B CA  
4143  C C   . PHE A 507 ? 0.7072 0.6360 0.8142 -0.0374 0.0229  0.1014  523 PHE B C   
4144  O O   . PHE A 507 ? 0.7557 0.6791 0.8774 -0.0459 0.0226  0.1020  523 PHE B O   
4145  C CB  . PHE A 507 ? 0.7538 0.6751 0.8380 -0.0236 0.0148  0.1144  523 PHE B CB  
4146  C CG  . PHE A 507 ? 0.7711 0.6815 0.8488 -0.0092 0.0040  0.1144  523 PHE B CG  
4147  C CD1 . PHE A 507 ? 0.7749 0.6688 0.8627 -0.0061 -0.0060 0.1131  523 PHE B CD1 
4148  C CD2 . PHE A 507 ? 0.8341 0.7510 0.8968 0.0025  0.0030  0.1140  523 PHE B CD2 
4149  C CE1 . PHE A 507 ? 0.8315 0.7153 0.9132 0.0089  -0.0173 0.1115  523 PHE B CE1 
4150  C CE2 . PHE A 507 ? 0.8418 0.7500 0.8984 0.0175  -0.0074 0.1128  523 PHE B CE2 
4151  C CZ  . PHE A 507 ? 0.8591 0.7506 0.9249 0.0211  -0.0178 0.1112  523 PHE B CZ  
4152  N N   . GLN A 508 ? 0.6775 0.6202 0.7780 -0.0405 0.0306  0.0993  524 GLN B N   
4153  C CA  . GLN A 508 ? 0.6950 0.6465 0.8059 -0.0536 0.0385  0.0972  524 GLN B CA  
4154  C C   . GLN A 508 ? 0.7839 0.7274 0.9134 -0.0536 0.0338  0.0867  524 GLN B C   
4155  O O   . GLN A 508 ? 0.8057 0.7488 0.9496 -0.0641 0.0363  0.0880  524 GLN B O   
4156  C CB  . GLN A 508 ? 0.7119 0.6779 0.8134 -0.0552 0.0455  0.0947  524 GLN B CB  
4157  C CG  . GLN A 508 ? 0.7971 0.7720 0.8822 -0.0561 0.0502  0.1047  524 GLN B CG  
4158  C CD  . GLN A 508 ? 0.7732 0.7622 0.8513 -0.0594 0.0567  0.1026  524 GLN B CD  
4159  O OE1 . GLN A 508 ? 0.7277 0.7200 0.7951 -0.0519 0.0554  0.1015  524 GLN B OE1 
4160  N NE2 . GLN A 508 ? 0.7938 0.7917 0.8781 -0.0707 0.0636  0.1023  524 GLN B NE2 
4161  N N   . PHE A 509 ? 0.7834 0.7204 0.9127 -0.0416 0.0267  0.0763  525 PHE B N   
4162  C CA  . PHE A 509 ? 0.7068 0.6325 0.8524 -0.0374 0.0189  0.0654  525 PHE B CA  
4163  C C   . PHE A 509 ? 0.7571 0.6705 0.9157 -0.0403 0.0132  0.0697  525 PHE B C   
4164  O O   . PHE A 509 ? 0.7701 0.6843 0.9455 -0.0513 0.0158  0.0693  525 PHE B O   
4165  C CB  . PHE A 509 ? 0.6572 0.5752 0.7953 -0.0207 0.0105  0.0565  525 PHE B CB  
4166  C CG  . PHE A 509 ? 0.6161 0.5438 0.7443 -0.0181 0.0150  0.0510  525 PHE B CG  
4167  C CD1 . PHE A 509 ? 0.6138 0.5545 0.7442 -0.0299 0.0241  0.0506  525 PHE B CD1 
4168  C CD2 . PHE A 509 ? 0.6164 0.5407 0.7320 -0.0037 0.0101  0.0469  525 PHE B CD2 
4169  C CE1 . PHE A 509 ? 0.5927 0.5413 0.7139 -0.0277 0.0272  0.0456  525 PHE B CE1 
4170  C CE2 . PHE A 509 ? 0.5963 0.5287 0.7025 -0.0021 0.0140  0.0427  525 PHE B CE2 
4171  C CZ  . PHE A 509 ? 0.5525 0.4965 0.6617 -0.0143 0.0222  0.0420  525 PHE B CZ  
4172  N N   . GLN A 510 ? 0.8022 0.7050 0.9531 -0.0310 0.0055  0.0745  526 GLN B N   
4173  C CA  . GLN A 510 ? 0.8071 0.6948 0.9709 -0.0310 -0.0032 0.0765  526 GLN B CA  
4174  C C   . GLN A 510 ? 0.8138 0.7050 0.9877 -0.0482 0.0038  0.0862  526 GLN B C   
4175  O O   . GLN A 510 ? 0.9013 0.7842 1.0944 -0.0539 -0.0001 0.0847  526 GLN B O   
4176  C CB  . GLN A 510 ? 0.8000 0.6776 0.9510 -0.0184 -0.0121 0.0811  526 GLN B CB  
4177  C CG  . GLN A 510 ? 0.8540 0.7132 1.0179 -0.0157 -0.0241 0.0815  526 GLN B CG  
4178  C CD  . GLN A 510 ? 0.9125 0.7593 1.0915 -0.0061 -0.0353 0.0676  526 GLN B CD  
4179  O OE1 . GLN A 510 ? 0.8486 0.7004 1.0300 -0.0028 -0.0335 0.0571  526 GLN B OE1 
4180  N NE2 . GLN A 510 ? 0.9436 0.7733 1.1335 -0.0021 -0.0475 0.0674  526 GLN B NE2 
4181  N N   . GLU A 511 ? 0.7817 0.6860 0.9440 -0.0570 0.0146  0.0959  527 GLU B N   
4182  C CA  . GLU A 511 ? 0.8073 0.7162 0.9781 -0.0730 0.0222  0.1053  527 GLU B CA  
4183  C C   . GLU A 511 ? 0.8658 0.7832 1.0543 -0.0830 0.0281  0.0984  527 GLU B C   
4184  O O   . GLU A 511 ? 0.9023 0.8166 1.1082 -0.0930 0.0287  0.1013  527 GLU B O   
4185  C CB  . GLU A 511 ? 0.8468 0.7679 1.0000 -0.0788 0.0320  0.1165  527 GLU B CB  
4186  C CG  . GLU A 511 ? 0.9324 0.8567 1.0922 -0.0940 0.0392  0.1274  527 GLU B CG  
4187  C CD  . GLU A 511 ? 1.0092 0.9448 1.1513 -0.0992 0.0484  0.1382  527 GLU B CD  
4188  O OE1 . GLU A 511 ? 0.9459 0.8977 1.0839 -0.1044 0.0579  0.1367  527 GLU B OE1 
4189  O OE2 . GLU A 511 ? 1.0854 1.0129 1.2176 -0.0975 0.0452  0.1478  527 GLU B OE2 
4190  N N   . ALA A 512 ? 0.8185 0.7467 1.0035 -0.0802 0.0321  0.0891  528 ALA B N   
4191  C CA  . ALA A 512 ? 0.8578 0.7950 1.0589 -0.0885 0.0371  0.0811  528 ALA B CA  
4192  C C   . ALA A 512 ? 0.8467 0.7714 1.0697 -0.0860 0.0278  0.0716  528 ALA B C   
4193  O O   . ALA A 512 ? 0.8766 0.8046 1.1189 -0.0969 0.0310  0.0711  528 ALA B O   
4194  C CB  . ALA A 512 ? 0.8054 0.7542 0.9967 -0.0841 0.0410  0.0721  528 ALA B CB  
4195  N N   . LEU A 513 ? 0.8364 0.7471 1.0571 -0.0713 0.0163  0.0640  529 LEU B N   
4196  C CA  . LEU A 513 ? 0.8219 0.7196 1.0629 -0.0672 0.0060  0.0540  529 LEU B CA  
4197  C C   . LEU A 513 ? 0.9059 0.7930 1.1617 -0.0746 0.0019  0.0626  529 LEU B C   
4198  O O   . LEU A 513 ? 0.9465 0.8309 1.2255 -0.0814 -0.0001 0.0582  529 LEU B O   
4199  C CB  . LEU A 513 ? 0.7844 0.6694 1.0177 -0.0483 -0.0059 0.0439  529 LEU B CB  
4200  C CG  . LEU A 513 ? 0.7675 0.6595 0.9869 -0.0390 -0.0040 0.0345  529 LEU B CG  
4201  C CD1 . LEU A 513 ? 0.6898 0.5673 0.9066 -0.0208 -0.0168 0.0239  529 LEU B CD1 
4202  C CD2 . LEU A 513 ? 0.7475 0.6515 0.9785 -0.0477 0.0029  0.0258  529 LEU B CD2 
4203  N N   . CYS A 514 ? 0.9051 0.7864 1.1485 -0.0741 0.0007  0.0750  530 CYS B N   
4204  C CA  . CYS A 514 ? 0.9193 0.7889 1.1764 -0.0814 -0.0040 0.0835  530 CYS B CA  
4205  C C   . CYS A 514 ? 0.9841 0.8659 1.2545 -0.1005 0.0078  0.0912  530 CYS B C   
4206  O O   . CYS A 514 ? 0.9874 0.8625 1.2795 -0.1086 0.0046  0.0926  530 CYS B O   
4207  C CB  . CYS A 514 ? 0.9568 0.8174 1.1960 -0.0760 -0.0083 0.0947  530 CYS B CB  
4208  S SG  . CYS A 514 ? 1.0394 0.8845 1.2680 -0.0527 -0.0242 0.0849  530 CYS B SG  
4209  N N   . GLN A 515 ? 0.9869 0.8873 1.2453 -0.1079 0.0213  0.0957  531 GLN B N   
4210  C CA  . GLN A 515 ? 0.9992 0.9136 1.2707 -0.1247 0.0329  0.1008  531 GLN B CA  
4211  C C   . GLN A 515 ? 0.9787 0.8966 1.2742 -0.1273 0.0316  0.0878  531 GLN B C   
4212  O O   . GLN A 515 ? 1.0598 0.9805 1.3761 -0.1397 0.0348  0.0911  531 GLN B O   
4213  C CB  . GLN A 515 ? 1.0561 0.9902 1.3103 -0.1297 0.0464  0.1054  531 GLN B CB  
4214  C CG  . GLN A 515 ? 1.0973 1.0476 1.3632 -0.1461 0.0588  0.1109  531 GLN B CG  
4215  C CD  . GLN A 515 ? 1.2807 1.2482 1.5268 -0.1503 0.0709  0.1179  531 GLN B CD  
4216  O OE1 . GLN A 515 ? 1.3731 1.3373 1.6009 -0.1486 0.0717  0.1286  531 GLN B OE1 
4217  N NE2 . GLN A 515 ? 1.3116 1.2976 1.5615 -0.1551 0.0795  0.1113  531 GLN B NE2 
4218  N N   . ALA A 516 ? 1.0240 0.9421 1.3170 -0.1159 0.0270  0.0729  532 ALA B N   
4219  C CA  . ALA A 516 ? 1.0186 0.9379 1.3340 -0.1163 0.0238  0.0588  532 ALA B CA  
4220  C C   . ALA A 516 ? 1.0186 0.9193 1.3553 -0.1144 0.0112  0.0563  532 ALA B C   
4221  O O   . ALA A 516 ? 0.9980 0.9004 1.3597 -0.1210 0.0103  0.0500  532 ALA B O   
4222  C CB  . ALA A 516 ? 0.9352 0.8558 1.2404 -0.1029 0.0203  0.0440  532 ALA B CB  
4223  N N   . ALA A 517 ? 0.9104 0.7937 1.2385 -0.1057 0.0012  0.0615  533 ALA B N   
4224  C CA  . ALA A 517 ? 0.9677 0.8316 1.3148 -0.1028 -0.0124 0.0596  533 ALA B CA  
4225  C C   . ALA A 517 ? 1.0390 0.9000 1.3996 -0.1182 -0.0098 0.0743  533 ALA B C   
4226  O O   . ALA A 517 ? 1.0816 0.9260 1.4599 -0.1177 -0.0214 0.0740  533 ALA B O   
4227  C CB  . ALA A 517 ? 0.9464 0.7922 1.2776 -0.0848 -0.0259 0.0574  533 ALA B CB  
4228  N N   . LYS A 518 ? 1.0305 0.9063 1.3828 -0.1315 0.0045  0.0873  534 LYS B N   
4229  C CA  . LYS A 518 ? 1.0799 0.9527 1.4400 -0.1457 0.0079  0.1036  534 LYS B CA  
4230  C C   . LYS A 518 ? 1.1303 0.9804 1.4829 -0.1383 -0.0051 0.1110  534 LYS B C   
4231  O O   . LYS A 518 ? 1.1686 1.0040 1.5398 -0.1429 -0.0138 0.1148  534 LYS B O   
4232  C CB  . LYS A 518 ? 1.0809 0.9565 1.4735 -0.1586 0.0090  0.1020  534 LYS B CB  
4233  C CG  . LYS A 518 ? 1.1322 1.0323 1.5312 -0.1678 0.0232  0.0976  534 LYS B CG  
4234  C CD  . LYS A 518 ? 1.2828 1.1850 1.7157 -0.1763 0.0213  0.0908  534 LYS B CD  
4235  C CE  . LYS A 518 ? 1.3664 1.2919 1.8049 -0.1801 0.0322  0.0805  534 LYS B CE  
4236  N NZ  . LYS A 518 ? 1.4301 1.3756 1.8491 -0.1882 0.0486  0.0914  534 LYS B NZ  
4237  N N   . HIS A 519 ? 1.1379 0.9852 1.4637 -0.1268 -0.0068 0.1126  535 HIS B N   
4238  C CA  . HIS A 519 ? 1.1976 1.0250 1.5134 -0.1181 -0.0191 0.1188  535 HIS B CA  
4239  C C   . HIS A 519 ? 1.2767 1.1042 1.5845 -0.1306 -0.0122 0.1375  535 HIS B C   
4240  O O   . HIS A 519 ? 1.2970 1.1416 1.5929 -0.1391 0.0024  0.1449  535 HIS B O   
4241  C CB  . HIS A 519 ? 1.1678 0.9939 1.4583 -0.1001 -0.0236 0.1126  535 HIS B CB  
4242  C CG  . HIS A 519 ? 1.1753 0.9843 1.4520 -0.0904 -0.0348 0.1190  535 HIS B CG  
4243  N ND1 . HIS A 519 ? 1.1880 0.9762 1.4740 -0.0795 -0.0523 0.1131  535 HIS B ND1 
4244  C CD2 . HIS A 519 ? 1.1627 0.9725 1.4168 -0.0891 -0.0318 0.1300  535 HIS B CD2 
4245  C CE1 . HIS A 519 ? 1.2256 1.0029 1.4952 -0.0720 -0.0596 0.1204  535 HIS B CE1 
4246  N NE2 . HIS A 519 ? 1.1833 0.9734 1.4334 -0.0777 -0.0473 0.1306  535 HIS B NE2 
4247  N N   . GLU A 520 ? 1.3626 1.1704 1.6770 -0.1314 -0.0233 0.1449  536 GLU B N   
4248  C CA  . GLU A 520 ? 1.3678 1.1717 1.6719 -0.1409 -0.0193 0.1627  536 GLU B CA  
4249  C C   . GLU A 520 ? 1.3535 1.1432 1.6348 -0.1262 -0.0301 0.1646  536 GLU B C   
4250  O O   . GLU A 520 ? 1.4039 1.1799 1.6867 -0.1111 -0.0449 0.1544  536 GLU B O   
4251  C CB  . GLU A 520 ? 1.4977 1.2890 1.8255 -0.1544 -0.0238 0.1718  536 GLU B CB  
4252  C CG  . GLU A 520 ? 1.5894 1.3895 1.9477 -0.1664 -0.0190 0.1667  536 GLU B CG  
4253  C CD  . GLU A 520 ? 1.6831 1.5097 2.0408 -0.1802 0.0015  0.1713  536 GLU B CD  
4254  O OE1 . GLU A 520 ? 1.6410 1.4776 1.9761 -0.1834 0.0124  0.1814  536 GLU B OE1 
4255  O OE2 . GLU A 520 ? 1.6878 1.5251 2.0691 -0.1881 0.0061  0.1647  536 GLU B OE2 
4256  N N   . GLY A 521 ? 1.2779 1.0716 1.5380 -0.1297 -0.0229 0.1772  537 GLY B N   
4257  C CA  . GLY A 521 ? 1.2777 1.0582 1.5172 -0.1173 -0.0330 0.1804  537 GLY B CA  
4258  C C   . GLY A 521 ? 1.2247 1.0187 1.4386 -0.1067 -0.0270 0.1771  537 GLY B C   
4259  O O   . GLY A 521 ? 1.2146 1.0288 1.4234 -0.1116 -0.0131 0.1756  537 GLY B O   
4260  N N   . PRO A 522 ? 1.1745 0.9578 1.3720 -0.0921 -0.0378 0.1761  538 PRO B N   
4261  C CA  . PRO A 522 ? 1.1479 0.9440 1.3230 -0.0809 -0.0334 0.1719  538 PRO B CA  
4262  C C   . PRO A 522 ? 1.1638 0.9674 1.3445 -0.0708 -0.0346 0.1563  538 PRO B C   
4263  O O   . PRO A 522 ? 1.1466 0.9394 1.3439 -0.0655 -0.0448 0.1470  538 PRO B O   
4264  C CB  . PRO A 522 ? 1.2001 0.9812 1.3599 -0.0677 -0.0466 0.1746  538 PRO B CB  
4265  C CG  . PRO A 522 ? 1.2385 0.9994 1.4099 -0.0754 -0.0556 0.1835  538 PRO B CG  
4266  C CD  . PRO A 522 ? 1.2282 0.9880 1.4265 -0.0859 -0.0543 0.1797  538 PRO B CD  
4267  N N   . LEU A 523 ? 1.0777 0.8994 1.2443 -0.0683 -0.0242 0.1535  539 LEU B N   
4268  C CA  . LEU A 523 ? 1.0200 0.8506 1.1905 -0.0608 -0.0230 0.1398  539 LEU B CA  
4269  C C   . LEU A 523 ? 1.0763 0.8958 1.2432 -0.0412 -0.0374 0.1294  539 LEU B C   
4270  O O   . LEU A 523 ? 1.0950 0.9152 1.2704 -0.0344 -0.0404 0.1171  539 LEU B O   
4271  C CB  . LEU A 523 ? 0.9854 0.8370 1.1404 -0.0633 -0.0092 0.1409  539 LEU B CB  
4272  C CG  . LEU A 523 ? 1.0061 0.8692 1.1590 -0.0557 -0.0061 0.1287  539 LEU B CG  
4273  C CD1 . LEU A 523 ? 0.9729 0.8362 1.1474 -0.0608 -0.0057 0.1190  539 LEU B CD1 
4274  C CD2 . LEU A 523 ? 0.9639 0.8464 1.1011 -0.0609 0.0074  0.1334  539 LEU B CD2 
4275  N N   . HIS A 524 ? 1.0681 0.8772 1.2221 -0.0313 -0.0467 0.1337  540 HIS B N   
4276  C CA  . HIS A 524 ? 1.0473 0.8490 1.1942 -0.0111 -0.0592 0.1242  540 HIS B CA  
4277  C C   . HIS A 524 ? 1.0930 0.8758 1.2578 -0.0042 -0.0747 0.1159  540 HIS B C   
4278  O O   . HIS A 524 ? 1.0916 0.8694 1.2531 0.0132  -0.0847 0.1054  540 HIS B O   
4279  C CB  . HIS A 524 ? 1.0580 0.8573 1.1845 -0.0023 -0.0637 0.1312  540 HIS B CB  
4280  C CG  . HIS A 524 ? 1.1040 0.8847 1.2340 -0.0045 -0.0743 0.1389  540 HIS B CG  
4281  N ND1 . HIS A 524 ? 1.0668 0.8471 1.1950 -0.0196 -0.0675 0.1522  540 HIS B ND1 
4282  C CD2 . HIS A 524 ? 1.1286 0.8899 1.2627 0.0070  -0.0917 0.1352  540 HIS B CD2 
4283  C CE1 . HIS A 524 ? 1.0998 0.8606 1.2314 -0.0182 -0.0802 0.1569  540 HIS B CE1 
4284  N NE2 . HIS A 524 ? 1.1658 0.9148 1.3013 -0.0021 -0.0953 0.1465  540 HIS B NE2 
4285  N N   . LYS A 525 ? 1.1107 0.8833 1.2943 -0.0171 -0.0767 0.1205  541 LYS B N   
4286  C CA  . LYS A 525 ? 1.1145 0.8689 1.3188 -0.0133 -0.0912 0.1133  541 LYS B CA  
4287  C C   . LYS A 525 ? 1.1533 0.9129 1.3769 -0.0174 -0.0877 0.1025  541 LYS B C   
4288  O O   . LYS A 525 ? 1.2201 0.9655 1.4630 -0.0142 -0.0997 0.0951  541 LYS B O   
4289  C CB  . LYS A 525 ? 1.0661 0.8059 1.2824 -0.0261 -0.0959 0.1247  541 LYS B CB  
4290  C CG  . LYS A 525 ? 1.1660 0.8958 1.3652 -0.0217 -0.1026 0.1348  541 LYS B CG  
4291  C CD  . LYS A 525 ? 1.2196 0.9389 1.4282 -0.0386 -0.1023 0.1488  541 LYS B CD  
4292  C CE  . LYS A 525 ? 1.2359 0.9363 1.4707 -0.0416 -0.1154 0.1455  541 LYS B CE  
4293  N NZ  . LYS A 525 ? 1.3685 1.0489 1.6000 -0.0229 -0.1365 0.1389  541 LYS B NZ  
4294  N N   . CYS A 526 ? 1.1075 0.8867 1.3270 -0.0239 -0.0726 0.1010  542 CYS B N   
4295  C CA  . CYS A 526 ? 1.1045 0.8897 1.3440 -0.0317 -0.0678 0.0926  542 CYS B CA  
4296  C C   . CYS A 526 ? 1.0780 0.8590 1.3206 -0.0152 -0.0769 0.0760  542 CYS B C   
4297  O O   . CYS A 526 ? 1.0800 0.8672 1.3041 -0.0020 -0.0762 0.0711  542 CYS B O   
4298  C CB  . CYS A 526 ? 1.1045 0.9117 1.3384 -0.0447 -0.0491 0.0967  542 CYS B CB  
4299  S SG  . CYS A 526 ? 1.0766 0.8944 1.3279 -0.0479 -0.0438 0.0822  542 CYS B SG  
4300  N N   . ASP A 527 ? 1.0279 0.7986 1.2943 -0.0162 -0.0851 0.0675  543 ASP B N   
4301  C CA  . ASP A 527 ? 0.9928 0.7597 1.2650 -0.0020 -0.0932 0.0508  543 ASP B CA  
4302  C C   . ASP A 527 ? 0.9879 0.7644 1.2797 -0.0142 -0.0850 0.0444  543 ASP B C   
4303  O O   . ASP A 527 ? 0.9909 0.7624 1.3066 -0.0264 -0.0867 0.0462  543 ASP B O   
4304  C CB  . ASP A 527 ? 1.0319 0.7762 1.3153 0.0110  -0.1133 0.0438  543 ASP B CB  
4305  C CG  . ASP A 527 ? 1.0182 0.7575 1.3082 0.0262  -0.1222 0.0259  543 ASP B CG  
4306  O OD1 . ASP A 527 ? 0.9997 0.7526 1.2816 0.0281  -0.1129 0.0195  543 ASP B OD1 
4307  O OD2 . ASP A 527 ? 1.0614 0.7825 1.3648 0.0362  -0.1390 0.0181  543 ASP B OD2 
4308  N N   . ILE A 528 ? 0.9742 0.7647 1.2563 -0.0106 -0.0766 0.0367  544 ILE B N   
4309  C CA  . ILE A 528 ? 0.9090 0.7112 1.2056 -0.0203 -0.0680 0.0292  544 ILE B CA  
4310  C C   . ILE A 528 ? 0.9888 0.7798 1.3067 -0.0130 -0.0798 0.0136  544 ILE B C   
4311  O O   . ILE A 528 ? 1.0074 0.8073 1.3388 -0.0199 -0.0741 0.0057  544 ILE B O   
4312  C CB  . ILE A 528 ? 0.8258 0.6441 1.1031 -0.0165 -0.0575 0.0253  544 ILE B CB  
4313  C CG1 . ILE A 528 ? 0.7658 0.5759 1.0324 0.0046  -0.0677 0.0127  544 ILE B CG1 
4314  C CG2 . ILE A 528 ? 0.9334 0.7619 1.1884 -0.0203 -0.0478 0.0386  544 ILE B CG2 
4315  C CD1 . ILE A 528 ? 0.7123 0.5361 0.9627 0.0076  -0.0586 0.0084  544 ILE B CD1 
4316  N N   . SER A 529 ? 1.0047 0.7765 1.3256 0.0016  -0.0965 0.0081  545 SER B N   
4317  C CA  . SER A 529 ? 0.9369 0.6966 1.2779 0.0101  -0.1093 -0.0074 545 SER B CA  
4318  C C   . SER A 529 ? 0.9474 0.7101 1.3190 -0.0075 -0.1061 -0.0081 545 SER B C   
4319  O O   . SER A 529 ? 0.9863 0.7520 1.3672 -0.0241 -0.1001 0.0050  545 SER B O   
4320  C CB  . SER A 529 ? 0.9616 0.6995 1.3043 0.0252  -0.1281 -0.0099 545 SER B CB  
4321  O OG  . SER A 529 ? 0.9326 0.6696 1.2477 0.0425  -0.1309 -0.0103 545 SER B OG  
4322  N N   . ASN A 530 ? 1.0014 0.7632 1.3886 -0.0033 -0.1103 -0.0236 546 ASN B N   
4323  C CA  . ASN A 530 ? 1.0425 0.8067 1.4613 -0.0182 -0.1091 -0.0263 546 ASN B CA  
4324  C C   . ASN A 530 ? 1.0099 0.7970 1.4295 -0.0387 -0.0893 -0.0167 546 ASN B C   
4325  O O   . ASN A 530 ? 1.1055 0.8966 1.5453 -0.0558 -0.0846 -0.0084 546 ASN B O   
4326  C CB  . ASN A 530 ? 1.1193 0.8665 1.5588 -0.0228 -0.1211 -0.0199 546 ASN B CB  
4327  C CG  . ASN A 530 ? 1.1961 0.9202 1.6416 -0.0028 -0.1428 -0.0324 546 ASN B CG  
4328  O OD1 . ASN A 530 ? 1.1709 0.8909 1.5982 0.0166  -0.1487 -0.0428 546 ASN B OD1 
4329  N ND2 . ASN A 530 ? 1.2737 0.9822 1.7447 -0.0074 -0.1553 -0.0306 546 ASN B ND2 
4330  N N   . SER A 531 ? 0.9499 0.7521 1.3473 -0.0372 -0.0776 -0.0170 547 SER B N   
4331  C CA  . SER A 531 ? 0.9888 0.8128 1.3876 -0.0556 -0.0598 -0.0090 547 SER B CA  
4332  C C   . SER A 531 ? 0.9784 0.8159 1.3686 -0.0518 -0.0529 -0.0208 547 SER B C   
4333  O O   . SER A 531 ? 0.9499 0.7941 1.3142 -0.0460 -0.0470 -0.0185 547 SER B O   
4334  C CB  . SER A 531 ? 1.0383 0.8694 1.4168 -0.0632 -0.0497 0.0092  547 SER B CB  
4335  O OG  . SER A 531 ? 1.0283 0.8808 1.4075 -0.0791 -0.0332 0.0149  547 SER B OG  
4336  N N   . THR A 532 ? 0.9589 0.8008 1.3718 -0.0559 -0.0536 -0.0329 548 THR B N   
4337  C CA  . THR A 532 ? 0.9235 0.7761 1.3294 -0.0511 -0.0491 -0.0458 548 THR B CA  
4338  C C   . THR A 532 ? 0.9618 0.8363 1.3533 -0.0627 -0.0320 -0.0375 548 THR B C   
4339  O O   . THR A 532 ? 0.9343 0.8153 1.3077 -0.0559 -0.0285 -0.0437 548 THR B O   
4340  C CB  . THR A 532 ? 0.8966 0.7500 1.3313 -0.0537 -0.0535 -0.0608 548 THR B CB  
4341  O OG1 . THR A 532 ? 0.9181 0.7833 1.3760 -0.0733 -0.0453 -0.0526 548 THR B OG1 
4342  C CG2 . THR A 532 ? 0.8708 0.7016 1.3182 -0.0399 -0.0719 -0.0708 548 THR B CG2 
4343  N N   . GLU A 533 ? 1.0243 0.9101 1.4233 -0.0800 -0.0216 -0.0236 549 GLU B N   
4344  C CA  . GLU A 533 ? 1.0127 0.9184 1.3953 -0.0893 -0.0062 -0.0148 549 GLU B CA  
4345  C C   . GLU A 533 ? 0.9256 0.8282 1.2765 -0.0793 -0.0056 -0.0087 549 GLU B C   
4346  O O   . GLU A 533 ? 0.9240 0.8394 1.2581 -0.0791 0.0025  -0.0096 549 GLU B O   
4347  C CB  . GLU A 533 ? 1.0856 1.0023 1.4789 -0.1081 0.0044  0.0007  549 GLU B CB  
4348  C CG  . GLU A 533 ? 1.1013 1.0186 1.5286 -0.1193 0.0028  -0.0012 549 GLU B CG  
4349  C CD  . GLU A 533 ? 1.1971 1.0925 1.6384 -0.1164 -0.0104 0.0024  549 GLU B CD  
4350  O OE1 . GLU A 533 ? 1.2611 1.1498 1.6934 -0.1200 -0.0099 0.0178  549 GLU B OE1 
4351  O OE2 . GLU A 533 ? 1.2138 1.0988 1.6761 -0.1108 -0.0217 -0.0106 549 GLU B OE2 
4352  N N   . ALA A 534 ? 0.9199 0.8053 1.2629 -0.0698 -0.0152 -0.0036 550 ALA B N   
4353  C CA  . ALA A 534 ? 0.8724 0.7551 1.1865 -0.0594 -0.0153 0.0021  550 ALA B CA  
4354  C C   . ALA A 534 ? 0.8570 0.7361 1.1585 -0.0435 -0.0208 -0.0117 550 ALA B C   
4355  O O   . ALA A 534 ? 0.8563 0.7444 1.1367 -0.0406 -0.0144 -0.0101 550 ALA B O   
4356  C CB  . ALA A 534 ? 0.8371 0.7032 1.1475 -0.0535 -0.0244 0.0109  550 ALA B CB  
4357  N N   . GLY A 535 ? 0.8843 0.7497 1.1984 -0.0327 -0.0331 -0.0251 551 GLY B N   
4358  C CA  . GLY A 535 ? 0.8387 0.7003 1.1411 -0.0176 -0.0382 -0.0386 551 GLY B CA  
4359  C C   . GLY A 535 ? 0.8383 0.7159 1.1382 -0.0239 -0.0286 -0.0451 551 GLY B C   
4360  O O   . GLY A 535 ? 0.7651 0.6455 1.0455 -0.0157 -0.0271 -0.0487 551 GLY B O   
4361  N N   . GLN A 536 ? 0.8321 0.7209 1.1520 -0.0385 -0.0222 -0.0462 552 GLN B N   
4362  C CA  . GLN A 536 ? 0.7963 0.7011 1.1158 -0.0446 -0.0138 -0.0532 552 GLN B CA  
4363  C C   . GLN A 536 ? 0.8233 0.7424 1.1203 -0.0504 -0.0021 -0.0419 552 GLN B C   
4364  O O   . GLN A 536 ? 0.8196 0.7444 1.1019 -0.0458 0.0003  -0.0478 552 GLN B O   
4365  C CB  . GLN A 536 ? 0.8535 0.7681 1.2011 -0.0589 -0.0097 -0.0561 552 GLN B CB  
4366  C CG  . GLN A 536 ? 0.9291 0.8617 1.2787 -0.0657 -0.0013 -0.0639 552 GLN B CG  
4367  C CD  . GLN A 536 ? 0.9334 0.8598 1.2795 -0.0528 -0.0090 -0.0820 552 GLN B CD  
4368  O OE1 . GLN A 536 ? 0.9108 0.8436 1.2382 -0.0493 -0.0054 -0.0850 552 GLN B OE1 
4369  N NE2 . GLN A 536 ? 0.9368 0.8501 1.3008 -0.0454 -0.0203 -0.0943 552 GLN B NE2 
4370  N N   . LYS A 537 ? 0.8217 0.7461 1.1159 -0.0603 0.0048  -0.0257 553 LYS B N   
4371  C CA  . LYS A 537 ? 0.7646 0.7016 1.0376 -0.0652 0.0151  -0.0144 553 LYS B CA  
4372  C C   . LYS A 537 ? 0.7086 0.6389 0.9574 -0.0511 0.0110  -0.0152 553 LYS B C   
4373  O O   . LYS A 537 ? 0.7042 0.6439 0.9385 -0.0505 0.0160  -0.0169 553 LYS B O   
4374  C CB  . LYS A 537 ? 0.7492 0.6883 1.0215 -0.0750 0.0205  0.0029  553 LYS B CB  
4375  C CG  . LYS A 537 ? 0.7303 0.6876 0.9910 -0.0862 0.0337  0.0135  553 LYS B CG  
4376  C CD  . LYS A 537 ? 0.8025 0.7626 1.0712 -0.0988 0.0392  0.0281  553 LYS B CD  
4377  C CE  . LYS A 537 ? 0.8857 0.8639 1.1433 -0.1098 0.0523  0.0389  553 LYS B CE  
4378  N NZ  . LYS A 537 ? 0.8600 0.8554 1.1220 -0.1149 0.0591  0.0297  553 LYS B NZ  
4379  N N   . LEU A 538 ? 0.7283 0.6426 0.9729 -0.0397 0.0015  -0.0139 554 LEU B N   
4380  C CA  . LEU A 538 ? 0.7380 0.6458 0.9611 -0.0249 -0.0031 -0.0154 554 LEU B CA  
4381  C C   . LEU A 538 ? 0.7847 0.6922 1.0040 -0.0169 -0.0058 -0.0300 554 LEU B C   
4382  O O   . LEU A 538 ? 0.7093 0.6233 0.9102 -0.0141 -0.0017 -0.0290 554 LEU B O   
4383  C CB  . LEU A 538 ? 0.6888 0.5793 0.9120 -0.0129 -0.0142 -0.0144 554 LEU B CB  
4384  C CG  . LEU A 538 ? 0.6161 0.4990 0.8186 0.0043  -0.0202 -0.0162 554 LEU B CG  
4385  C CD1 . LEU A 538 ? 0.6753 0.5685 0.8563 0.0026  -0.0122 -0.0041 554 LEU B CD1 
4386  C CD2 . LEU A 538 ? 0.4964 0.3628 0.7032 0.0153  -0.0320 -0.0165 554 LEU B CD2 
4387  N N   . PHE A 539 ? 0.8089 0.7083 1.0456 -0.0130 -0.0133 -0.0438 555 PHE B N   
4388  C CA  . PHE A 539 ? 0.7134 0.6090 0.9467 -0.0033 -0.0182 -0.0590 555 PHE B CA  
4389  C C   . PHE A 539 ? 0.6958 0.6066 0.9218 -0.0110 -0.0092 -0.0609 555 PHE B C   
4390  O O   . PHE A 539 ? 0.7001 0.6092 0.9118 -0.0027 -0.0111 -0.0676 555 PHE B O   
4391  C CB  . PHE A 539 ? 0.6820 0.5690 0.9390 -0.0010 -0.0265 -0.0732 555 PHE B CB  
4392  C CG  . PHE A 539 ? 0.6989 0.5805 0.9521 0.0099  -0.0324 -0.0896 555 PHE B CG  
4393  C CD1 . PHE A 539 ? 0.7192 0.5850 0.9610 0.0280  -0.0427 -0.0962 555 PHE B CD1 
4394  C CD2 . PHE A 539 ? 0.7190 0.6120 0.9777 0.0024  -0.0274 -0.0981 555 PHE B CD2 
4395  C CE1 . PHE A 539 ? 0.7035 0.5637 0.9399 0.0383  -0.0479 -0.1109 555 PHE B CE1 
4396  C CE2 . PHE A 539 ? 0.6362 0.5235 0.8898 0.0124  -0.0331 -0.1131 555 PHE B CE2 
4397  C CZ  . PHE A 539 ? 0.6723 0.5428 0.9146 0.0301  -0.0433 -0.1193 555 PHE B CZ  
4398  N N   . ASN A 540 ? 0.6837 0.6092 0.9201 -0.0267 -0.0002 -0.0559 556 ASN B N   
4399  C CA  . ASN A 540 ? 0.6540 0.5944 0.8847 -0.0337 0.0074  -0.0587 556 ASN B CA  
4400  C C   . ASN A 540 ? 0.7015 0.6459 0.9064 -0.0306 0.0114  -0.0504 556 ASN B C   
4401  O O   . ASN A 540 ? 0.7148 0.6663 0.9107 -0.0311 0.0139  -0.0554 556 ASN B O   
4402  C CB  . ASN A 540 ? 0.6984 0.6543 0.9442 -0.0503 0.0166  -0.0530 556 ASN B CB  
4403  C CG  . ASN A 540 ? 0.7698 0.7238 1.0426 -0.0537 0.0128  -0.0629 556 ASN B CG  
4404  O OD1 . ASN A 540 ? 0.8205 0.7834 1.1097 -0.0661 0.0186  -0.0574 556 ASN B OD1 
4405  N ND2 . ASN A 540 ? 0.7433 0.6844 1.0209 -0.0421 0.0026  -0.0775 556 ASN B ND2 
4406  N N   . MET A 541 ? 0.6491 0.5887 0.8422 -0.0268 0.0113  -0.0383 557 MET B N   
4407  C CA  . MET A 541 ? 0.6649 0.6068 0.8347 -0.0219 0.0137  -0.0309 557 MET B CA  
4408  C C   . MET A 541 ? 0.6863 0.6143 0.8443 -0.0054 0.0051  -0.0366 557 MET B C   
4409  O O   . MET A 541 ? 0.7005 0.6304 0.8417 -0.0006 0.0059  -0.0363 557 MET B O   
4410  C CB  . MET A 541 ? 0.7534 0.7002 0.9162 -0.0274 0.0192  -0.0141 557 MET B CB  
4411  C CG  . MET A 541 ? 0.6157 0.5649 0.7557 -0.0221 0.0213  -0.0043 557 MET B CG  
4412  S SD  . MET A 541 ? 0.6128 0.5466 0.7424 -0.0047 0.0123  -0.0027 557 MET B SD  
4413  C CE  . MET A 541 ? 0.5908 0.5196 0.7327 -0.0089 0.0108  0.0057  557 MET B CE  
4414  N N   . LEU A 542 ? 0.7003 0.6147 0.8668 0.0035  -0.0034 -0.0411 558 LEU B N   
4415  C CA  . LEU A 542 ? 0.7169 0.6180 0.8727 0.0206  -0.0121 -0.0480 558 LEU B CA  
4416  C C   . LEU A 542 ? 0.7513 0.6513 0.9032 0.0248  -0.0142 -0.0610 558 LEU B C   
4417  O O   . LEU A 542 ? 0.7745 0.6736 0.9078 0.0321  -0.0143 -0.0604 558 LEU B O   
4418  C CB  . LEU A 542 ? 0.7097 0.5962 0.8788 0.0292  -0.0221 -0.0538 558 LEU B CB  
4419  C CG  . LEU A 542 ? 0.7145 0.6009 0.8850 0.0258  -0.0209 -0.0405 558 LEU B CG  
4420  C CD1 . LEU A 542 ? 0.6975 0.5684 0.8819 0.0346  -0.0322 -0.0466 558 LEU B CD1 
4421  C CD2 . LEU A 542 ? 0.7060 0.5962 0.8535 0.0314  -0.0177 -0.0288 558 LEU B CD2 
4422  N N   . ARG A 543 ? 0.7345 0.6349 0.9041 0.0197  -0.0158 -0.0727 559 ARG B N   
4423  C CA  . ARG A 543 ? 0.7275 0.6252 0.8956 0.0242  -0.0194 -0.0872 559 ARG B CA  
4424  C C   . ARG A 543 ? 0.7357 0.6428 0.8860 0.0207  -0.0134 -0.0835 559 ARG B C   
4425  O O   . ARG A 543 ? 0.8259 0.7278 0.9687 0.0273  -0.0175 -0.0938 559 ARG B O   
4426  C CB  . ARG A 543 ? 0.6944 0.5964 0.8861 0.0156  -0.0197 -0.0982 559 ARG B CB  
4427  C CG  . ARG A 543 ? 0.7191 0.6399 0.9188 -0.0022 -0.0089 -0.0912 559 ARG B CG  
4428  C CD  . ARG A 543 ? 0.7002 0.6282 0.9172 -0.0088 -0.0087 -0.1046 559 ARG B CD  
4429  N NE  . ARG A 543 ? 0.8790 0.8024 1.0866 -0.0007 -0.0137 -0.1179 559 ARG B NE  
4430  C CZ  . ARG A 543 ? 0.9491 0.8824 1.1455 -0.0052 -0.0093 -0.1185 559 ARG B CZ  
4431  N NH1 . ARG A 543 ? 1.0300 0.9791 1.2235 -0.0173 0.0003  -0.1074 559 ARG B NH1 
4432  N NH2 . ARG A 543 ? 1.0120 0.9382 1.1996 0.0032  -0.0153 -0.1309 559 ARG B NH2 
4433  N N   . LEU A 544 ? 0.7389 0.6583 0.8818 0.0109  -0.0046 -0.0693 560 LEU B N   
4434  C CA  . LEU A 544 ? 0.7442 0.6739 0.8737 0.0055  0.0009  -0.0662 560 LEU B CA  
4435  C C   . LEU A 544 ? 0.7673 0.6906 0.8752 0.0161  -0.0017 -0.0635 560 LEU B C   
4436  O O   . LEU A 544 ? 0.7554 0.6826 0.8532 0.0142  -0.0004 -0.0655 560 LEU B O   
4437  C CB  . LEU A 544 ? 0.7235 0.6683 0.8526 -0.0077 0.0105  -0.0521 560 LEU B CB  
4438  C CG  . LEU A 544 ? 0.6514 0.6065 0.7991 -0.0202 0.0150  -0.0545 560 LEU B CG  
4439  C CD1 . LEU A 544 ? 0.6691 0.6383 0.8134 -0.0318 0.0243  -0.0403 560 LEU B CD1 
4440  C CD2 . LEU A 544 ? 0.6814 0.6404 0.8306 -0.0217 0.0138  -0.0674 560 LEU B CD2 
4441  N N   . GLY A 545 ? 0.8003 0.7142 0.9009 0.0273  -0.0055 -0.0590 561 GLY B N   
4442  C CA  . GLY A 545 ? 0.7887 0.7003 0.8683 0.0355  -0.0058 -0.0534 561 GLY B CA  
4443  C C   . GLY A 545 ? 0.6896 0.6154 0.7606 0.0253  0.0029  -0.0393 561 GLY B C   
4444  O O   . GLY A 545 ? 0.6754 0.6095 0.7534 0.0166  0.0080  -0.0306 561 GLY B O   
4445  N N   . LYS A 546 ? 0.6266 0.5548 0.6827 0.0263  0.0041  -0.0368 562 LYS B N   
4446  C CA  . LYS A 546 ? 0.7222 0.6642 0.7720 0.0155  0.0115  -0.0255 562 LYS B CA  
4447  C C   . LYS A 546 ? 0.7397 0.6869 0.7910 0.0071  0.0122  -0.0326 562 LYS B C   
4448  O O   . LYS A 546 ? 0.7539 0.7086 0.7956 0.0020  0.0153  -0.0262 562 LYS B O   
4449  C CB  . LYS A 546 ? 0.6909 0.6342 0.7231 0.0211  0.0129  -0.0147 562 LYS B CB  
4450  C CG  . LYS A 546 ? 0.6970 0.6303 0.7170 0.0316  0.0078  -0.0206 562 LYS B CG  
4451  C CD  . LYS A 546 ? 0.8043 0.7414 0.8085 0.0360  0.0105  -0.0079 562 LYS B CD  
4452  C CE  . LYS A 546 ? 0.8709 0.8196 0.8696 0.0248  0.0156  0.0004  562 LYS B CE  
4453  N NZ  . LYS A 546 ? 0.9098 0.8643 0.8960 0.0282  0.0190  0.0141  562 LYS B NZ  
4454  N N   . SER A 547 ? 0.6886 0.6320 0.7524 0.0062  0.0087  -0.0462 563 SER B N   
4455  C CA  . SER A 547 ? 0.6870 0.6347 0.7535 0.0000  0.0079  -0.0557 563 SER B CA  
4456  C C   . SER A 547 ? 0.6865 0.6505 0.7605 -0.0141 0.0149  -0.0511 563 SER B C   
4457  O O   . SER A 547 ? 0.6041 0.5739 0.6769 -0.0192 0.0146  -0.0567 563 SER B O   
4458  C CB  . SER A 547 ? 0.7619 0.7009 0.8406 0.0047  0.0016  -0.0724 563 SER B CB  
4459  O OG  . SER A 547 ? 0.7331 0.6761 0.8295 -0.0002 0.0041  -0.0725 563 SER B OG  
4460  N N   . GLU A 548 ? 0.6991 0.6702 0.7809 -0.0198 0.0204  -0.0420 564 GLU B N   
4461  C CA  . GLU A 548 ? 0.6605 0.6471 0.7464 -0.0322 0.0278  -0.0348 564 GLU B CA  
4462  C C   . GLU A 548 ? 0.6775 0.6693 0.7530 -0.0342 0.0327  -0.0184 564 GLU B C   
4463  O O   . GLU A 548 ? 0.6456 0.6297 0.7143 -0.0263 0.0309  -0.0126 564 GLU B O   
4464  C CB  . GLU A 548 ? 0.6426 0.6342 0.7469 -0.0388 0.0308  -0.0374 564 GLU B CB  
4465  C CG  . GLU A 548 ? 0.6735 0.6640 0.7919 -0.0391 0.0272  -0.0535 564 GLU B CG  
4466  C CD  . GLU A 548 ? 0.7373 0.7387 0.8548 -0.0451 0.0283  -0.0607 564 GLU B CD  
4467  O OE1 . GLU A 548 ? 0.7036 0.7133 0.8098 -0.0495 0.0316  -0.0533 564 GLU B OE1 
4468  O OE2 . GLU A 548 ? 0.7754 0.7784 0.9052 -0.0461 0.0260  -0.0740 564 GLU B OE2 
4469  N N   . PRO A 549 ? 0.6904 0.6957 0.7638 -0.0438 0.0384  -0.0113 565 PRO B N   
4470  C CA  . PRO A 549 ? 0.6786 0.6894 0.7427 -0.0457 0.0427  0.0036  565 PRO B CA  
4471  C C   . PRO A 549 ? 0.6962 0.7045 0.7657 -0.0449 0.0451  0.0113  565 PRO B C   
4472  O O   . PRO A 549 ? 0.6624 0.6715 0.7449 -0.0491 0.0466  0.0083  565 PRO B O   
4473  C CB  . PRO A 549 ? 0.6796 0.7049 0.7437 -0.0563 0.0477  0.0066  565 PRO B CB  
4474  C CG  . PRO A 549 ? 0.6381 0.6644 0.7055 -0.0574 0.0443  -0.0064 565 PRO B CG  
4475  C CD  . PRO A 549 ? 0.6724 0.6884 0.7499 -0.0519 0.0402  -0.0176 565 PRO B CD  
4476  N N   . TRP A 550 ? 0.6954 0.7012 0.7549 -0.0397 0.0452  0.0216  566 TRP B N   
4477  C CA  . TRP A 550 ? 0.6522 0.6537 0.7158 -0.0371 0.0456  0.0279  566 TRP B CA  
4478  C C   . TRP A 550 ? 0.6518 0.6619 0.7232 -0.0476 0.0515  0.0341  566 TRP B C   
4479  O O   . TRP A 550 ? 0.6653 0.6706 0.7445 -0.0476 0.0512  0.0366  566 TRP B O   
4480  C CB  . TRP A 550 ? 0.6324 0.6322 0.6836 -0.0298 0.0451  0.0380  566 TRP B CB  
4481  C CG  . TRP A 550 ? 0.7022 0.7134 0.7448 -0.0355 0.0502  0.0497  566 TRP B CG  
4482  C CD1 . TRP A 550 ? 0.7079 0.7250 0.7402 -0.0357 0.0510  0.0532  566 TRP B CD1 
4483  C CD2 . TRP A 550 ? 0.7663 0.7843 0.8104 -0.0421 0.0550  0.0594  566 TRP B CD2 
4484  N NE1 . TRP A 550 ? 0.6524 0.6799 0.6803 -0.0416 0.0557  0.0642  566 TRP B NE1 
4485  C CE2 . TRP A 550 ? 0.6586 0.6866 0.6930 -0.0454 0.0582  0.0678  566 TRP B CE2 
4486  C CE3 . TRP A 550 ? 0.7221 0.7382 0.7750 -0.0457 0.0565  0.0620  566 TRP B CE3 
4487  C CZ2 . TRP A 550 ? 0.6584 0.6941 0.6910 -0.0512 0.0628  0.0778  566 TRP B CZ2 
4488  C CZ3 . TRP A 550 ? 0.6586 0.6821 0.7088 -0.0519 0.0613  0.0727  566 TRP B CZ3 
4489  C CH2 . TRP A 550 ? 0.6528 0.6858 0.6927 -0.0542 0.0643  0.0801  566 TRP B CH2 
4490  N N   . THR A 551 ? 0.6971 0.7193 0.7664 -0.0564 0.0563  0.0364  567 THR B N   
4491  C CA  . THR A 551 ? 0.7147 0.7459 0.7905 -0.0663 0.0624  0.0417  567 THR B CA  
4492  C C   . THR A 551 ? 0.7141 0.7442 0.8060 -0.0702 0.0624  0.0327  567 THR B C   
4493  O O   . THR A 551 ? 0.7484 0.7770 0.8493 -0.0736 0.0645  0.0369  567 THR B O   
4494  C CB  . THR A 551 ? 0.7196 0.7642 0.7883 -0.0732 0.0666  0.0453  567 THR B CB  
4495  O OG1 . THR A 551 ? 0.6796 0.7261 0.7480 -0.0730 0.0639  0.0346  567 THR B OG1 
4496  C CG2 . THR A 551 ? 0.6965 0.7427 0.7516 -0.0701 0.0668  0.0555  567 THR B CG2 
4497  N N   . LEU A 552 ? 0.7049 0.7353 0.8013 -0.0694 0.0597  0.0202  568 LEU B N   
4498  C CA  . LEU A 552 ? 0.7384 0.7679 0.8514 -0.0722 0.0591  0.0105  568 LEU B CA  
4499  C C   . LEU A 552 ? 0.7152 0.7305 0.8366 -0.0656 0.0540  0.0082  568 LEU B C   
4500  O O   . LEU A 552 ? 0.6998 0.7148 0.8360 -0.0701 0.0553  0.0074  568 LEU B O   
4501  C CB  . LEU A 552 ? 0.7597 0.7914 0.8745 -0.0711 0.0559  -0.0035 568 LEU B CB  
4502  C CG  . LEU A 552 ? 0.7571 0.7871 0.8893 -0.0719 0.0537  -0.0163 568 LEU B CG  
4503  C CD1 . LEU A 552 ? 0.7951 0.8352 0.9426 -0.0821 0.0603  -0.0132 568 LEU B CD1 
4504  C CD2 . LEU A 552 ? 0.7295 0.7634 0.8592 -0.0709 0.0508  -0.0288 568 LEU B CD2 
4505  N N   . ALA A 553 ? 0.6997 0.7035 0.8123 -0.0547 0.0479  0.0068  569 ALA B N   
4506  C CA  . ALA A 553 ? 0.6857 0.6755 0.8045 -0.0465 0.0420  0.0047  569 ALA B CA  
4507  C C   . ALA A 553 ? 0.7207 0.7102 0.8448 -0.0509 0.0448  0.0157  569 ALA B C   
4508  O O   . ALA A 553 ? 0.6672 0.6500 0.8057 -0.0514 0.0420  0.0129  569 ALA B O   
4509  C CB  . ALA A 553 ? 0.6902 0.6707 0.7945 -0.0341 0.0367  0.0054  569 ALA B CB  
4510  N N   . LEU A 554 ? 0.7410 0.7373 0.8536 -0.0541 0.0496  0.0282  570 LEU B N   
4511  C CA  . LEU A 554 ? 0.7086 0.7039 0.8233 -0.0578 0.0519  0.0396  570 LEU B CA  
4512  C C   . LEU A 554 ? 0.7318 0.7339 0.8611 -0.0699 0.0572  0.0404  570 LEU B C   
4513  O O   . LEU A 554 ? 0.7549 0.7501 0.8961 -0.0716 0.0554  0.0422  570 LEU B O   
4514  C CB  . LEU A 554 ? 0.6508 0.6530 0.7494 -0.0586 0.0559  0.0517  570 LEU B CB  
4515  C CG  . LEU A 554 ? 0.6769 0.6776 0.7755 -0.0617 0.0578  0.0635  570 LEU B CG  
4516  C CD1 . LEU A 554 ? 0.6709 0.6565 0.7753 -0.0530 0.0500  0.0612  570 LEU B CD1 
4517  C CD2 . LEU A 554 ? 0.7028 0.7090 0.7854 -0.0602 0.0603  0.0739  570 LEU B CD2 
4518  N N   . GLU A 555 ? 0.7066 0.7225 0.8358 -0.0780 0.0634  0.0388  571 GLU B N   
4519  C CA  . GLU A 555 ? 0.7077 0.7327 0.8505 -0.0892 0.0693  0.0391  571 GLU B CA  
4520  C C   . GLU A 555 ? 0.7440 0.7625 0.9064 -0.0890 0.0652  0.0286  571 GLU B C   
4521  O O   . GLU A 555 ? 0.7439 0.7660 0.9205 -0.0974 0.0689  0.0313  571 GLU B O   
4522  C CB  . GLU A 555 ? 0.6755 0.7166 0.8131 -0.0952 0.0752  0.0368  571 GLU B CB  
4523  C CG  . GLU A 555 ? 0.7512 0.8058 0.9001 -0.1063 0.0825  0.0371  571 GLU B CG  
4524  C CD  . GLU A 555 ? 0.8176 0.8870 0.9610 -0.1092 0.0859  0.0313  571 GLU B CD  
4525  O OE1 . GLU A 555 ? 0.8428 0.9118 0.9894 -0.1055 0.0817  0.0183  571 GLU B OE1 
4526  O OE2 . GLU A 555 ? 0.8985 0.9796 1.0344 -0.1150 0.0923  0.0392  571 GLU B OE2 
4527  N N   . ASN A 556 ? 0.7454 0.7539 0.9091 -0.0793 0.0574  0.0170  572 ASN B N   
4528  C CA  . ASN A 556 ? 0.7413 0.7429 0.9243 -0.0783 0.0526  0.0064  572 ASN B CA  
4529  C C   . ASN A 556 ? 0.7606 0.7508 0.9533 -0.0779 0.0492  0.0127  572 ASN B C   
4530  O O   . ASN A 556 ? 0.8118 0.8005 1.0240 -0.0826 0.0482  0.0085  572 ASN B O   
4531  C CB  . ASN A 556 ? 0.6809 0.6726 0.8618 -0.0667 0.0442  -0.0075 572 ASN B CB  
4532  C CG  . ASN A 556 ? 0.7215 0.7230 0.9035 -0.0691 0.0458  -0.0187 572 ASN B CG  
4533  O OD1 . ASN A 556 ? 0.7260 0.7425 0.9048 -0.0778 0.0532  -0.0150 572 ASN B OD1 
4534  N ND2 . ASN A 556 ? 0.7003 0.6930 0.8853 -0.0605 0.0384  -0.0326 572 ASN B ND2 
4535  N N   . VAL A 557 ? 0.7478 0.7302 0.9277 -0.0722 0.0469  0.0224  573 VAL B N   
4536  C CA  . VAL A 557 ? 0.7317 0.7018 0.9187 -0.0704 0.0421  0.0285  573 VAL B CA  
4537  C C   . VAL A 557 ? 0.7514 0.7280 0.9388 -0.0818 0.0494  0.0430  573 VAL B C   
4538  O O   . VAL A 557 ? 0.7304 0.7027 0.9331 -0.0879 0.0488  0.0461  573 VAL B O   
4539  C CB  . VAL A 557 ? 0.6670 0.6244 0.8397 -0.0561 0.0343  0.0298  573 VAL B CB  
4540  C CG1 . VAL A 557 ? 0.6163 0.5582 0.7979 -0.0511 0.0260  0.0319  573 VAL B CG1 
4541  C CG2 . VAL A 557 ? 0.6427 0.5964 0.8093 -0.0452 0.0292  0.0177  573 VAL B CG2 
4542  N N   . VAL A 558 ? 0.8046 0.7915 0.9756 -0.0850 0.0562  0.0519  574 VAL B N   
4543  C CA  . VAL A 558 ? 0.7854 0.7756 0.9508 -0.0922 0.0617  0.0668  574 VAL B CA  
4544  C C   . VAL A 558 ? 0.7626 0.7703 0.9267 -0.1042 0.0725  0.0715  574 VAL B C   
4545  O O   . VAL A 558 ? 0.7473 0.7585 0.9066 -0.1108 0.0778  0.0838  574 VAL B O   
4546  C CB  . VAL A 558 ? 0.7461 0.7317 0.8920 -0.0839 0.0591  0.0744  574 VAL B CB  
4547  C CG1 . VAL A 558 ? 0.7681 0.7382 0.9138 -0.0704 0.0484  0.0685  574 VAL B CG1 
4548  C CG2 . VAL A 558 ? 0.7215 0.7191 0.8529 -0.0830 0.0636  0.0731  574 VAL B CG2 
4549  N N   . GLY A 559 ? 0.8439 0.8626 1.0116 -0.1065 0.0757  0.0619  575 GLY B N   
4550  C CA  . GLY A 559 ? 0.7580 0.7941 0.9262 -0.1171 0.0854  0.0649  575 GLY B CA  
4551  C C   . GLY A 559 ? 0.7436 0.7885 0.8924 -0.1177 0.0902  0.0733  575 GLY B C   
4552  O O   . GLY A 559 ? 0.8348 0.8917 0.9818 -0.1262 0.0982  0.0803  575 GLY B O   
4553  N N   . ALA A 560 ? 0.6985 0.7380 0.8330 -0.1087 0.0856  0.0730  576 ALA B N   
4554  C CA  . ALA A 560 ? 0.7071 0.7541 0.8239 -0.1084 0.0889  0.0805  576 ALA B CA  
4555  C C   . ALA A 560 ? 0.7200 0.7640 0.8270 -0.0990 0.0835  0.0739  576 ALA B C   
4556  O O   . ALA A 560 ? 0.7592 0.7912 0.8684 -0.0906 0.0766  0.0686  576 ALA B O   
4557  C CB  . ALA A 560 ? 0.7135 0.7547 0.8220 -0.1082 0.0894  0.0941  576 ALA B CB  
4558  N N   . LYS A 561 ? 0.7230 0.7774 0.8191 -0.1000 0.0863  0.0743  577 LYS B N   
4559  C CA  . LYS A 561 ? 0.7081 0.7608 0.7968 -0.0928 0.0815  0.0673  577 LYS B CA  
4560  C C   . LYS A 561 ? 0.7986 0.8465 0.8741 -0.0859 0.0787  0.0748  577 LYS B C   
4561  O O   . LYS A 561 ? 0.8345 0.8805 0.9031 -0.0798 0.0749  0.0707  577 LYS B O   
4562  C CB  . LYS A 561 ? 0.7304 0.7963 0.8152 -0.0972 0.0845  0.0632  577 LYS B CB  
4563  C CG  . LYS A 561 ? 0.8070 0.8801 0.9043 -0.1031 0.0872  0.0545  577 LYS B CG  
4564  C CD  . LYS A 561 ? 0.8317 0.9184 0.9228 -0.1065 0.0897  0.0516  577 LYS B CD  
4565  C CE  . LYS A 561 ? 0.9005 0.9971 1.0026 -0.1116 0.0922  0.0418  577 LYS B CE  
4566  N NZ  . LYS A 561 ? 1.0084 1.1196 1.1025 -0.1149 0.0951  0.0417  577 LYS B NZ  
4567  N N   . ASN A 562 ? 0.8692 0.9153 0.9404 -0.0868 0.0805  0.0859  578 ASN B N   
4568  C CA  . ASN A 562 ? 0.8886 0.9332 0.9470 -0.0808 0.0786  0.0934  578 ASN B CA  
4569  C C   . ASN A 562 ? 0.8772 0.9110 0.9360 -0.0761 0.0755  0.0995  578 ASN B C   
4570  O O   . ASN A 562 ? 0.8263 0.8552 0.8937 -0.0799 0.0761  0.1014  578 ASN B O   
4571  C CB  . ASN A 562 ? 0.9759 1.0320 1.0244 -0.0860 0.0836  0.1019  578 ASN B CB  
4572  C CG  . ASN A 562 ? 1.0747 1.1330 1.1111 -0.0800 0.0813  0.1058  578 ASN B CG  
4573  O OD1 . ASN A 562 ? 1.0059 1.0568 1.0398 -0.0715 0.0766  0.1048  578 ASN B OD1 
4574  N ND2 . ASN A 562 ? 1.1762 1.2451 1.2054 -0.0842 0.0844  0.1103  578 ASN B ND2 
4575  N N   . MET A 563 ? 0.7954 0.8262 0.8445 -0.0677 0.0719  0.1028  579 MET B N   
4576  C CA  . MET A 563 ? 0.7941 0.8167 0.8397 -0.0615 0.0684  0.1093  579 MET B CA  
4577  C C   . MET A 563 ? 0.8635 0.8876 0.9081 -0.0685 0.0721  0.1191  579 MET B C   
4578  O O   . MET A 563 ? 0.8696 0.9031 0.9138 -0.0775 0.0782  0.1218  579 MET B O   
4579  C CB  . MET A 563 ? 0.7880 0.8134 0.8218 -0.0530 0.0661  0.1120  579 MET B CB  
4580  C CG  . MET A 563 ? 0.7960 0.8137 0.8252 -0.0434 0.0611  0.1162  579 MET B CG  
4581  S SD  . MET A 563 ? 0.7078 0.7305 0.7257 -0.0327 0.0589  0.1165  579 MET B SD  
4582  C CE  . MET A 563 ? 0.7364 0.7747 0.7472 -0.0412 0.0653  0.1228  579 MET B CE  
4583  N N   . ASN A 564 ? 0.9152 0.9297 0.9593 -0.0642 0.0682  0.1241  580 ASN B N   
4584  C CA  . ASN A 564 ? 0.9312 0.9436 0.9752 -0.0706 0.0705  0.1332  580 ASN B CA  
4585  C C   . ASN A 564 ? 0.8963 0.8963 0.9379 -0.0627 0.0636  0.1374  580 ASN B C   
4586  O O   . ASN A 564 ? 0.8730 0.8625 0.9214 -0.0558 0.0570  0.1315  580 ASN B O   
4587  C CB  . ASN A 564 ? 0.9259 0.9372 0.9832 -0.0803 0.0740  0.1312  580 ASN B CB  
4588  C CG  . ASN A 564 ? 1.0060 1.0199 1.0609 -0.0891 0.0792  0.1414  580 ASN B CG  
4589  O OD1 . ASN A 564 ? 1.0228 1.0273 1.0755 -0.0878 0.0761  0.1486  580 ASN B OD1 
4590  N ND2 . ASN A 564 ? 1.1046 1.1308 1.1591 -0.0978 0.0868  0.1421  580 ASN B ND2 
4591  N N   . VAL A 565 ? 0.8665 0.8676 0.8982 -0.0630 0.0644  0.1469  581 VAL B N   
4592  C CA  . VAL A 565 ? 0.8909 0.8802 0.9199 -0.0559 0.0574  0.1511  581 VAL B CA  
4593  C C   . VAL A 565 ? 0.9575 0.9360 0.9938 -0.0624 0.0562  0.1560  581 VAL B C   
4594  O O   . VAL A 565 ? 0.9825 0.9482 1.0189 -0.0562 0.0485  0.1578  581 VAL B O   
4595  C CB  . VAL A 565 ? 0.8260 0.8209 0.8403 -0.0516 0.0575  0.1584  581 VAL B CB  
4596  C CG1 . VAL A 565 ? 0.8202 0.8210 0.8292 -0.0419 0.0553  0.1540  581 VAL B CG1 
4597  C CG2 . VAL A 565 ? 0.8369 0.8439 0.8464 -0.0615 0.0660  0.1634  581 VAL B CG2 
4598  N N   . ARG A 566 ? 0.5701 0.7797 1.4735 -0.0949 -0.0529 0.0708  582 ARG B N   
4599  C CA  . ARG A 566 ? 0.5798 0.7961 1.4921 -0.1064 -0.0590 0.0864  582 ARG B CA  
4600  C C   . ARG A 566 ? 0.6560 0.8038 1.5582 -0.0932 -0.0909 0.0962  582 ARG B C   
4601  O O   . ARG A 566 ? 0.6624 0.7973 1.5418 -0.0894 -0.1001 0.1155  582 ARG B O   
4602  C CB  . ARG A 566 ? 0.6544 0.9081 1.5792 -0.1275 -0.0414 0.0733  582 ARG B CB  
4603  C CG  . ARG A 566 ? 0.7959 1.0731 1.7164 -0.1413 -0.0373 0.0864  582 ARG B CG  
4604  C CD  . ARG A 566 ? 1.0139 1.3006 1.9312 -0.1546 -0.0286 0.0698  582 ARG B CD  
4605  N NE  . ARG A 566 ? 1.0568 1.3053 1.9900 -0.1478 -0.0411 0.0551  582 ARG B NE  
4606  C CZ  . ARG A 566 ? 0.9823 1.1818 1.9389 -0.1404 -0.0673 0.0598  582 ARG B CZ  
4607  N NH1 . ARG A 566 ? 0.9512 1.1321 1.9189 -0.1415 -0.0853 0.0788  582 ARG B NH1 
4608  N NH2 . ARG A 566 ? 0.8392 1.0065 1.8051 -0.1315 -0.0764 0.0451  582 ARG B NH2 
4609  N N   . PRO A 567 ? 0.7081 0.8097 1.6247 -0.0857 -0.1089 0.0845  583 PRO B N   
4610  C CA  . PRO A 567 ? 0.6585 0.6926 1.5621 -0.0723 -0.1400 0.0948  583 PRO B CA  
4611  C C   . PRO A 567 ? 0.7345 0.7213 1.5783 -0.0453 -0.1534 0.1095  583 PRO B C   
4612  O O   . PRO A 567 ? 0.7626 0.7114 1.5876 -0.0374 -0.1729 0.1258  583 PRO B O   
4613  C CB  . PRO A 567 ? 0.4741 0.4781 1.4093 -0.0722 -0.1520 0.0762  583 PRO B CB  
4614  C CG  . PRO A 567 ? 0.5732 0.6373 1.5533 -0.0943 -0.1284 0.0593  583 PRO B CG  
4615  C CD  . PRO A 567 ? 0.6521 0.7671 1.6102 -0.0957 -0.1021 0.0615  583 PRO B CD  
4616  N N   . LEU A 568 ? 0.6996 0.6863 1.5131 -0.0308 -0.1437 0.1040  584 LEU B N   
4617  C CA  . LEU A 568 ? 0.6912 0.6489 1.4465 -0.0077 -0.1494 0.1192  584 LEU B CA  
4618  C C   . LEU A 568 ? 0.6755 0.6582 1.4140 -0.0124 -0.1440 0.1395  584 LEU B C   
4619  O O   . LEU A 568 ? 0.7365 0.6779 1.4489 -0.0010 -0.1633 0.1563  584 LEU B O   
4620  C CB  . LEU A 568 ? 0.6377 0.6154 1.3707 0.0018  -0.1310 0.1097  584 LEU B CB  
4621  C CG  . LEU A 568 ? 0.6018 0.5497 1.2755 0.0269  -0.1349 0.1218  584 LEU B CG  
4622  C CD1 . LEU A 568 ? 0.6413 0.5101 1.2859 0.0498  -0.1636 0.1260  584 LEU B CD1 
4623  C CD2 . LEU A 568 ? 0.6056 0.5846 1.2755 0.0286  -0.1138 0.1072  584 LEU B CD2 
4624  N N   . LEU A 569 ? 0.7442 0.7949 1.4965 -0.0294 -0.1174 0.1381  585 LEU B N   
4625  C CA  . LEU A 569 ? 0.7361 0.8181 1.4748 -0.0363 -0.1093 0.1563  585 LEU B CA  
4626  C C   . LEU A 569 ? 0.7411 0.8005 1.4945 -0.0438 -0.1282 0.1684  585 LEU B C   
4627  O O   . LEU A 569 ? 0.8579 0.9002 1.5816 -0.0358 -0.1378 0.1878  585 LEU B O   
4628  C CB  . LEU A 569 ? 0.6345 0.7949 1.4000 -0.0591 -0.0787 0.1491  585 LEU B CB  
4629  C CG  . LEU A 569 ? 0.4698 0.6576 1.2241 -0.0539 -0.0583 0.1363  585 LEU B CG  
4630  C CD1 . LEU A 569 ? 0.4170 0.6808 1.1958 -0.0769 -0.0294 0.1317  585 LEU B CD1 
4631  C CD2 . LEU A 569 ? 0.4573 0.6188 1.1555 -0.0292 -0.0620 0.1482  585 LEU B CD2 
4632  N N   . ASN A 570 ? 0.6492 0.7070 1.4483 -0.0587 -0.1343 0.1573  586 ASN B N   
4633  C CA  . ASN A 570 ? 0.7153 0.7563 1.5319 -0.0678 -0.1508 0.1681  586 ASN B CA  
4634  C C   . ASN A 570 ? 0.7823 0.7473 1.5655 -0.0448 -0.1812 0.1798  586 ASN B C   
4635  O O   . ASN A 570 ? 0.8484 0.7967 1.6148 -0.0425 -0.1932 0.1982  586 ASN B O   
4636  C CB  . ASN A 570 ? 0.7146 0.7725 1.5899 -0.0892 -0.1494 0.1520  586 ASN B CB  
4637  C CG  . ASN A 570 ? 0.8545 0.8950 1.7506 -0.0993 -0.1663 0.1620  586 ASN B CG  
4638  O OD1 . ASN A 570 ? 0.9170 0.9484 1.7880 -0.0957 -0.1737 0.1815  586 ASN B OD1 
4639  N ND2 . ASN A 570 ? 0.9891 1.0210 1.9303 -0.1109 -0.1742 0.1491  586 ASN B ND2 
4640  N N   . TYR A 571 ? 0.7479 0.6662 1.5195 -0.0275 -0.1939 0.1697  587 TYR B N   
4641  C CA  . TYR A 571 ? 0.7738 0.6182 1.5101 -0.0043 -0.2221 0.1800  587 TYR B CA  
4642  C C   . TYR A 571 ? 0.8235 0.6595 1.5081 0.0109  -0.2228 0.2003  587 TYR B C   
4643  O O   . TYR A 571 ? 0.8492 0.6436 1.5134 0.0201  -0.2433 0.2162  587 TYR B O   
4644  C CB  . TYR A 571 ? 0.7728 0.5753 1.4986 0.0125  -0.2308 0.1653  587 TYR B CB  
4645  C CG  . TYR A 571 ? 0.7988 0.5481 1.4620 0.0298  -0.2495 0.1631  587 TYR B CG  
4646  C CD1 . TYR A 571 ? 0.8051 0.5368 1.4010 0.0484  -0.2469 0.1694  587 TYR B CD1 
4647  C CD2 . TYR A 571 ? 0.7704 0.5006 1.4313 0.0246  -0.2630 0.1499  587 TYR B CD2 
4648  C CE1 . TYR A 571 ? 0.8495 0.5438 1.3804 0.0601  -0.2552 0.1627  587 TYR B CE1 
4649  C CE2 . TYR A 571 ? 0.8437 0.5386 1.4398 0.0369  -0.2722 0.1448  587 TYR B CE2 
4650  C CZ  . TYR A 571 ? 0.8974 0.5741 1.4300 0.0541  -0.2672 0.1510  587 TYR B CZ  
4651  O OH  . TYR A 571 ? 0.9399 0.5837 1.4136 0.0653  -0.2723 0.1462  587 TYR B OH  
4652  N N   . PHE A 572 ? 0.8164 0.6928 1.4804 0.0133  -0.2003 0.2002  588 PHE B N   
4653  C CA  . PHE A 572 ? 0.7909 0.6577 1.4041 0.0300  -0.2006 0.2182  588 PHE B CA  
4654  C C   . PHE A 572 ? 0.8616 0.7757 1.4759 0.0158  -0.1882 0.2334  588 PHE B C   
4655  O O   . PHE A 572 ? 0.8970 0.8049 1.4706 0.0287  -0.1886 0.2494  588 PHE B O   
4656  C CB  . PHE A 572 ? 0.6936 0.5699 1.2775 0.0442  -0.1856 0.2110  588 PHE B CB  
4657  C CG  . PHE A 572 ? 0.7814 0.5955 1.3417 0.0666  -0.2029 0.2043  588 PHE B CG  
4658  C CD1 . PHE A 572 ? 0.8233 0.5848 1.3314 0.0842  -0.2199 0.2121  588 PHE B CD1 
4659  C CD2 . PHE A 572 ? 0.8045 0.6195 1.3839 0.0656  -0.1974 0.1836  588 PHE B CD2 
4660  C CE1 . PHE A 572 ? 0.9003 0.6259 1.3584 0.0954  -0.2218 0.1922  588 PHE B CE1 
4661  C CE2 . PHE A 572 ? 0.8067 0.5705 1.3527 0.0823  -0.2094 0.1726  588 PHE B CE2 
4662  C CZ  . PHE A 572 ? 0.8659 0.5931 1.3422 0.0940  -0.2170 0.1735  588 PHE B CZ  
4663  N N   . GLU A 573 ? 1.0223 0.9815 1.6813 -0.0101 -0.1778 0.2291  589 GLU B N   
4664  C CA  . GLU A 573 ? 0.9833 0.9954 1.6447 -0.0257 -0.1620 0.2414  589 GLU B CA  
4665  C C   . GLU A 573 ? 1.0061 0.9912 1.6364 -0.0172 -0.1778 0.2651  589 GLU B C   
4666  O O   . GLU A 573 ? 1.0223 1.0404 1.6310 -0.0183 -0.1648 0.2774  589 GLU B O   
4667  C CB  . GLU A 573 ? 1.0482 1.1061 1.7653 -0.0551 -0.1510 0.2316  589 GLU B CB  
4668  C CG  . GLU A 573 ? 1.2081 1.3081 1.9320 -0.0726 -0.1416 0.2456  589 GLU B CG  
4669  C CD  . GLU A 573 ? 1.4495 1.6176 2.2181 -0.1003 -0.1165 0.2326  589 GLU B CD  
4670  O OE1 . GLU A 573 ? 1.3999 1.5744 2.1992 -0.1062 -0.1111 0.2129  589 GLU B OE1 
4671  O OE2 . GLU A 573 ? 1.5396 1.7553 2.3103 -0.1154 -0.1013 0.2419  589 GLU B OE2 
4672  N N   . PRO A 574 ? 0.9959 0.9240 1.6224 -0.0090 -0.2049 0.2727  590 PRO B N   
4673  C CA  . PRO A 574 ? 0.9751 0.8720 1.5631 0.0041  -0.2201 0.2953  590 PRO B CA  
4674  C C   . PRO A 574 ? 0.9392 0.8251 1.4749 0.0270  -0.2159 0.3035  590 PRO B C   
4675  O O   . PRO A 574 ? 0.9100 0.8147 1.4210 0.0286  -0.2101 0.3196  590 PRO B O   
4676  C CB  . PRO A 574 ? 0.8693 0.6970 1.4587 0.0142  -0.2507 0.2970  590 PRO B CB  
4677  C CG  . PRO A 574 ? 0.8682 0.7062 1.5075 -0.0024 -0.2495 0.2789  590 PRO B CG  
4678  C CD  . PRO A 574 ? 0.9598 0.8453 1.6129 -0.0090 -0.2240 0.2616  590 PRO B CD  
4679  N N   . LEU A 575 ? 0.8902 0.7441 1.4084 0.0451  -0.2194 0.2926  591 LEU B N   
4680  C CA  . LEU A 575 ? 0.8580 0.6995 1.3276 0.0673  -0.2153 0.2988  591 LEU B CA  
4681  C C   . LEU A 575 ? 0.8946 0.8041 1.3641 0.0575  -0.1858 0.2971  591 LEU B C   
4682  O O   . LEU A 575 ? 0.9751 0.8913 1.4079 0.0690  -0.1800 0.3097  591 LEU B O   
4683  C CB  . LEU A 575 ? 0.8582 0.6544 1.3128 0.0862  -0.2236 0.2853  591 LEU B CB  
4684  C CG  . LEU A 575 ? 0.8553 0.6392 1.2470 0.1071  -0.2143 0.2816  591 LEU B CG  
4685  C CD1 . LEU A 575 ? 0.9300 0.6826 1.2634 0.1167  -0.2204 0.2841  591 LEU B CD1 
4686  C CD2 . LEU A 575 ? 0.8826 0.6386 1.2528 0.1171  -0.2122 0.2569  591 LEU B CD2 
4687  N N   . PHE A 576 ? 0.8843 0.8453 1.3954 0.0358  -0.1670 0.2820  592 PHE B N   
4688  C CA  . PHE A 576 ? 0.8305 0.8598 1.3454 0.0237  -0.1382 0.2798  592 PHE B CA  
4689  C C   . PHE A 576 ? 0.8148 0.8725 1.3182 0.0159  -0.1337 0.2997  592 PHE B C   
4690  O O   . PHE A 576 ? 0.8142 0.8911 1.2859 0.0243  -0.1226 0.3090  592 PHE B O   
4691  C CB  . PHE A 576 ? 0.8209 0.8989 1.3871 -0.0014 -0.1212 0.2617  592 PHE B CB  
4692  C CG  . PHE A 576 ? 0.6999 0.8429 1.2701 -0.0116 -0.0915 0.2550  592 PHE B CG  
4693  C CD1 . PHE A 576 ? 0.6563 0.8018 1.1878 0.0056  -0.0822 0.2576  592 PHE B CD1 
4694  C CD2 . PHE A 576 ? 0.6812 0.8836 1.2926 -0.0389 -0.0728 0.2475  592 PHE B CD2 
4695  C CE1 . PHE A 576 ? 0.5782 0.7831 1.1137 -0.0040 -0.0554 0.2515  592 PHE B CE1 
4696  C CE2 . PHE A 576 ? 0.5789 0.8403 1.1932 -0.0486 -0.0459 0.2417  592 PHE B CE2 
4697  C CZ  . PHE A 576 ? 0.5222 0.7849 1.0986 -0.0311 -0.0374 0.2439  592 PHE B CZ  
4698  N N   . THR A 577 ? 0.8462 0.9077 1.3759 -0.0008 -0.1422 0.3064  593 THR B N   
4699  C CA  . THR A 577 ? 0.8131 0.9082 1.3364 -0.0118 -0.1358 0.3241  593 THR B CA  
4700  C C   . THR A 577 ? 0.8685 0.9209 1.3439 0.0102  -0.1526 0.3447  593 THR B C   
4701  O O   . THR A 577 ? 0.9410 1.0215 1.3955 0.0095  -0.1432 0.3587  593 THR B O   
4702  C CB  . THR A 577 ? 0.7378 0.8484 1.3016 -0.0360 -0.1402 0.3259  593 THR B CB  
4703  O OG1 . THR A 577 ? 0.7447 0.7937 1.3050 -0.0264 -0.1686 0.3326  593 THR B OG1 
4704  C CG2 . THR A 577 ? 0.7328 0.8800 1.3470 -0.0573 -0.1257 0.3043  593 THR B CG2 
4705  N N   . TRP A 578 ? 0.8577 0.8418 1.3140 0.0304  -0.1773 0.3468  594 TRP B N   
4706  C CA  . TRP A 578 ? 0.9223 0.8653 1.3299 0.0536  -0.1917 0.3649  594 TRP B CA  
4707  C C   . TRP A 578 ? 0.9700 0.9253 1.3417 0.0701  -0.1771 0.3648  594 TRP B C   
4708  O O   . TRP A 578 ? 1.0159 0.9752 1.3551 0.0791  -0.1757 0.3812  594 TRP B O   
4709  C CB  . TRP A 578 ? 0.9441 0.8109 1.3384 0.0716  -0.2206 0.3662  594 TRP B CB  
4710  C CG  . TRP A 578 ? 1.0092 0.8405 1.3411 0.0914  -0.2256 0.3686  594 TRP B CG  
4711  C CD1 . TRP A 578 ? 1.0591 0.8789 1.3675 0.0905  -0.2324 0.3767  594 TRP B CD1 
4712  C CD2 . TRP A 578 ? 1.0288 0.8343 1.3066 0.1133  -0.2185 0.3532  594 TRP B CD2 
4713  N NE1 . TRP A 578 ? 1.1466 0.9361 1.3913 0.1112  -0.2290 0.3674  594 TRP B NE1 
4714  C CE2 . TRP A 578 ? 1.0865 0.8663 1.3111 0.1255  -0.2205 0.3532  594 TRP B CE2 
4715  C CE3 . TRP A 578 ? 1.0189 0.8210 1.2890 0.1240  -0.2100 0.3396  594 TRP B CE3 
4716  C CZ2 . TRP A 578 ? 1.1220 0.8736 1.2877 0.1481  -0.2134 0.3407  594 TRP B CZ2 
4717  C CZ3 . TRP A 578 ? 1.0200 0.7932 1.2293 0.1457  -0.2041 0.3273  594 TRP B CZ3 
4718  C CH2 . TRP A 578 ? 1.0912 0.8401 1.2498 0.1576  -0.2053 0.3284  594 TRP B CH2 
4719  N N   . LEU A 579 ? 0.9435 0.9042 1.3202 0.0745  -0.1664 0.3468  595 LEU B N   
4720  C CA  . LEU A 579 ? 0.8848 0.8637 1.2312 0.0878  -0.1501 0.3454  595 LEU B CA  
4721  C C   . LEU A 579 ? 0.9031 0.9514 1.2550 0.0716  -0.1261 0.3515  595 LEU B C   
4722  O O   . LEU A 579 ? 1.0412 1.0998 1.3595 0.0830  -0.1190 0.3625  595 LEU B O   
4723  C CB  . LEU A 579 ? 0.8677 0.8475 1.2253 0.0909  -0.1410 0.3236  595 LEU B CB  
4724  C CG  . LEU A 579 ? 0.9547 0.8635 1.2942 0.1125  -0.1628 0.3183  595 LEU B CG  
4725  C CD1 . LEU A 579 ? 0.9226 0.8382 1.2786 0.1120  -0.1526 0.2958  595 LEU B CD1 
4726  C CD2 . LEU A 579 ? 0.9152 0.7841 1.2011 0.1394  -0.1724 0.3326  595 LEU B CD2 
4727  N N   . LYS A 580 ? 0.9185 1.0156 1.3129 0.0450  -0.1130 0.3439  596 LYS B N   
4728  C CA  . LYS A 580 ? 0.9095 1.0744 1.3107 0.0281  -0.0892 0.3482  596 LYS B CA  
4729  C C   . LYS A 580 ? 1.0481 1.2136 1.4262 0.0295  -0.0958 0.3716  596 LYS B C   
4730  O O   . LYS A 580 ? 1.0368 1.2358 1.3939 0.0311  -0.0816 0.3805  596 LYS B O   
4731  C CB  . LYS A 580 ? 0.8017 1.0130 1.2540 -0.0010 -0.0760 0.3353  596 LYS B CB  
4732  C CG  . LYS A 580 ? 0.7197 0.9744 1.1895 -0.0089 -0.0524 0.3164  596 LYS B CG  
4733  C CD  . LYS A 580 ? 0.6762 0.9314 1.1918 -0.0244 -0.0540 0.2986  596 LYS B CD  
4734  C CE  . LYS A 580 ? 0.6489 0.9322 1.2005 -0.0503 -0.0534 0.3029  596 LYS B CE  
4735  N NZ  . LYS A 580 ? 0.7728 1.0483 1.3682 -0.0627 -0.0579 0.2854  596 LYS B NZ  
4736  N N   . ASP A 581 ? 1.1593 1.2866 1.5399 0.0295  -0.1179 0.3822  597 ASP B N   
4737  C CA  . ASP A 581 ? 1.2778 1.3953 1.6303 0.0355  -0.1274 0.4050  597 ASP B CA  
4738  C C   . ASP A 581 ? 1.3802 1.4666 1.6830 0.0641  -0.1319 0.4136  597 ASP B C   
4739  O O   . ASP A 581 ? 1.4661 1.5794 1.7459 0.0669  -0.1217 0.4258  597 ASP B O   
4740  C CB  . ASP A 581 ? 1.3453 1.4195 1.7066 0.0335  -0.1525 0.4142  597 ASP B CB  
4741  C CG  . ASP A 581 ? 1.5093 1.5700 1.8406 0.0404  -0.1638 0.4383  597 ASP B CG  
4742  O OD1 . ASP A 581 ? 1.5737 1.5836 1.8670 0.0654  -0.1798 0.4474  597 ASP B OD1 
4743  O OD2 . ASP A 581 ? 1.4643 1.5651 1.8087 0.0212  -0.1564 0.4482  597 ASP B OD2 
4744  N N   . GLN A 582 ? 1.1448 1.1757 1.4310 0.0851  -0.1462 0.4066  598 GLN B N   
4745  C CA  . GLN A 582 ? 1.1161 1.1091 1.3544 0.1132  -0.1537 0.4156  598 GLN B CA  
4746  C C   . GLN A 582 ? 1.0986 1.1328 1.3205 0.1179  -0.1303 0.4118  598 GLN B C   
4747  O O   . GLN A 582 ? 1.2527 1.2671 1.4346 0.1389  -0.1327 0.4216  598 GLN B O   
4748  C CB  . GLN A 582 ? 1.1119 1.0408 1.3344 0.1307  -0.1691 0.3992  598 GLN B CB  
4749  C CG  . GLN A 582 ? 1.1474 1.0238 1.3576 0.1304  -0.1879 0.3883  598 GLN B CG  
4750  C CD  . GLN A 582 ? 1.1792 1.0301 1.3418 0.1394  -0.1925 0.3889  598 GLN B CD  
4751  O OE1 . GLN A 582 ? 1.2356 1.0662 1.3480 0.1576  -0.1875 0.3801  598 GLN B OE1 
4752  N NE2 . GLN A 582 ? 1.1498 0.9982 1.3276 0.1272  -0.2029 0.3979  598 GLN B NE2 
4753  N N   . ASN A 583 ? 1.1008 1.1910 1.3525 0.0991  -0.1075 0.3975  599 ASN B N   
4754  C CA  . ASN A 583 ? 1.1259 1.2577 1.3647 0.1022  -0.0842 0.3924  599 ASN B CA  
4755  C C   . ASN A 583 ? 1.1510 1.3514 1.4003 0.0823  -0.0637 0.4003  599 ASN B C   
4756  O O   . ASN A 583 ? 1.1146 1.3608 1.3658 0.0773  -0.0413 0.3926  599 ASN B O   
4757  C CB  . ASN A 583 ? 0.9598 1.1006 1.2184 0.0998  -0.0729 0.3692  599 ASN B CB  
4758  C CG  . ASN A 583 ? 0.9929 1.0688 1.2295 0.1243  -0.0895 0.3622  599 ASN B CG  
4759  O OD1 . ASN A 583 ? 1.0100 1.0399 1.2092 0.1462  -0.1047 0.3745  599 ASN B OD1 
4760  N ND2 . ASN A 583 ? 0.9602 1.0323 1.2194 0.1207  -0.0863 0.3421  599 ASN B ND2 
4761  N N   . LYS A 584 ? 1.2710 1.4782 1.5253 0.0712  -0.0711 0.4159  600 LYS B N   
4762  C CA  . LYS A 584 ? 1.2001 1.4644 1.4549 0.0563  -0.0545 0.4270  600 LYS B CA  
4763  C C   . LYS A 584 ? 1.3674 1.6373 1.5814 0.0751  -0.0469 0.4366  600 LYS B C   
4764  O O   . LYS A 584 ? 1.2729 1.5962 1.4885 0.0666  -0.0245 0.4343  600 LYS B O   
4765  C CB  . LYS A 584 ? 1.1866 1.4444 1.4503 0.0443  -0.0686 0.4429  600 LYS B CB  
4766  C CG  . LYS A 584 ? 1.3493 1.5415 1.5794 0.0671  -0.0955 0.4590  600 LYS B CG  
4767  C CD  . LYS A 584 ? 1.4313 1.6082 1.6777 0.0541  -0.1126 0.4704  600 LYS B CD  
4768  C CE  . LYS A 584 ? 1.4734 1.5804 1.6897 0.0761  -0.1412 0.4848  600 LYS B CE  
4769  N NZ  . LYS A 584 ? 1.3200 1.3675 1.5216 0.0976  -0.1544 0.4713  600 LYS B NZ  
4770  N N   . ASN A 585 ? 1.7148 1.9292 1.8928 0.1010  -0.0648 0.4460  601 ASN B N   
4771  C CA  . ASN A 585 ? 1.7792 1.9917 1.9168 0.1201  -0.0615 0.4585  601 ASN B CA  
4772  C C   . ASN A 585 ? 1.7051 1.9098 1.8251 0.1376  -0.0522 0.4457  601 ASN B C   
4773  O O   . ASN A 585 ? 1.7258 1.9120 1.8087 0.1566  -0.0522 0.4482  601 ASN B O   
4774  C CB  . ASN A 585 ? 1.8970 2.0487 2.0040 0.1352  -0.0846 0.4652  601 ASN B CB  
4775  C CG  . ASN A 585 ? 1.8976 2.0604 2.0194 0.1190  -0.0930 0.4808  601 ASN B CG  
4776  O OD1 . ASN A 585 ? 1.8379 2.0599 1.9777 0.1007  -0.0792 0.4937  601 ASN B OD1 
4777  N ND2 . ASN A 585 ? 1.9453 2.0543 2.0647 0.1209  -0.1138 0.4740  601 ASN B ND2 
4778  N N   . SER A 586 ? 1.3128 1.5280 1.4582 0.1294  -0.0435 0.4256  602 SER B N   
4779  C CA  . SER A 586 ? 1.1938 1.3866 1.3246 0.1472  -0.0402 0.4116  602 SER B CA  
4780  C C   . SER A 586 ? 1.0177 1.2686 1.1724 0.1315  -0.0143 0.3953  602 SER B C   
4781  O O   . SER A 586 ? 1.0166 1.3165 1.2044 0.1061  -0.0020 0.3920  602 SER B O   
4782  C CB  . SER A 586 ? 1.2176 1.3499 1.3545 0.1563  -0.0604 0.4011  602 SER B CB  
4783  O OG  . SER A 586 ? 1.2907 1.3655 1.4061 0.1704  -0.0856 0.4148  602 SER B OG  
4784  N N   . PHE A 587 ? 0.8548 1.1003 0.9920 0.1465  -0.0057 0.3851  603 PHE B N   
4785  C CA  . PHE A 587 ? 0.7842 1.0799 0.9415 0.1341  0.0182  0.3685  603 PHE B CA  
4786  C C   . PHE A 587 ? 0.7713 1.0444 0.9516 0.1322  0.0141  0.3480  603 PHE B C   
4787  O O   . PHE A 587 ? 0.8457 1.0668 1.0061 0.1528  0.0017  0.3426  603 PHE B O   
4788  C CB  . PHE A 587 ? 0.7760 1.0879 0.9023 0.1494  0.0329  0.3696  603 PHE B CB  
4789  C CG  . PHE A 587 ? 0.7250 1.0911 0.8715 0.1359  0.0580  0.3535  603 PHE B CG  
4790  C CD1 . PHE A 587 ? 0.6847 1.1158 0.8534 0.1125  0.0768  0.3552  603 PHE B CD1 
4791  C CD2 . PHE A 587 ? 0.7433 1.0946 0.8850 0.1471  0.0627  0.3368  603 PHE B CD2 
4792  C CE1 . PHE A 587 ? 0.6908 1.1712 0.8778 0.1000  0.0999  0.3400  603 PHE B CE1 
4793  C CE2 . PHE A 587 ? 0.6884 1.0882 0.8482 0.1350  0.0853  0.3220  603 PHE B CE2 
4794  C CZ  . PHE A 587 ? 0.7365 1.2009 0.9191 0.1116  0.1040  0.3234  603 PHE B CZ  
4795  N N   . VAL A 588 ? 0.7195 1.0336 0.9412 0.1073  0.0257  0.3363  604 VAL B N   
4796  C CA  . VAL A 588 ? 0.7482 1.0445 0.9993 0.1010  0.0207  0.3175  604 VAL B CA  
4797  C C   . VAL A 588 ? 0.6787 1.0117 0.9410 0.0964  0.0426  0.2990  604 VAL B C   
4798  O O   . VAL A 588 ? 0.6420 1.0367 0.9238 0.0773  0.0641  0.2957  604 VAL B O   
4799  C CB  . VAL A 588 ? 0.6967 1.0109 0.9890 0.0759  0.0172  0.3169  604 VAL B CB  
4800  C CG1 . VAL A 588 ? 0.5807 0.8865 0.9077 0.0670  0.0159  0.2961  604 VAL B CG1 
4801  C CG2 . VAL A 588 ? 0.7608 1.0328 1.0408 0.0822  -0.0062 0.3345  604 VAL B CG2 
4802  N N   . GLY A 589 ? 0.7071 1.0021 0.9583 0.1129  0.0369  0.2865  605 GLY B N   
4803  C CA  . GLY A 589 ? 0.6532 0.9747 0.9073 0.1133  0.0558  0.2699  605 GLY B CA  
4804  C C   . GLY A 589 ? 0.6618 0.9638 0.8704 0.1385  0.0574  0.2756  605 GLY B C   
4805  O O   . GLY A 589 ? 0.7317 0.9980 0.9083 0.1554  0.0433  0.2917  605 GLY B O   
4806  N N   . TRP A 590 ? 0.6075 0.9337 0.8132 0.1410  0.0751  0.2624  606 TRP B N   
4807  C CA  . TRP A 590 ? 0.6904 0.9941 0.8529 0.1660  0.0762  0.2662  606 TRP B CA  
4808  C C   . TRP A 590 ? 0.6757 1.0308 0.8349 0.1630  0.1021  0.2583  606 TRP B C   
4809  O O   . TRP A 590 ? 0.6860 1.0734 0.8734 0.1485  0.1161  0.2414  606 TRP B O   
4810  C CB  . TRP A 590 ? 0.7250 0.9630 0.8720 0.1859  0.0590  0.2567  606 TRP B CB  
4811  C CG  . TRP A 590 ? 0.6960 0.9372 0.8764 0.1745  0.0622  0.2349  606 TRP B CG  
4812  C CD1 . TRP A 590 ? 0.6870 0.9511 0.8731 0.1733  0.0787  0.2180  606 TRP B CD1 
4813  C CD2 . TRP A 590 ? 0.6633 0.8857 0.8772 0.1620  0.0486  0.2280  606 TRP B CD2 
4814  N NE1 . TRP A 590 ? 0.6338 0.8934 0.8545 0.1612  0.0758  0.2009  606 TRP B NE1 
4815  C CE2 . TRP A 590 ? 0.6112 0.8459 0.8501 0.1540  0.0576  0.2067  606 TRP B CE2 
4816  C CE3 . TRP A 590 ? 0.6712 0.8672 0.8967 0.1568  0.0294  0.2378  606 TRP B CE3 
4817  C CZ2 . TRP A 590 ? 0.5915 0.8130 0.8666 0.1414  0.0480  0.1952  606 TRP B CZ2 
4818  C CZ3 . TRP A 590 ? 0.6450 0.8285 0.9061 0.1443  0.0203  0.2264  606 TRP B CZ3 
4819  C CH2 . TRP A 590 ? 0.6280 0.8242 0.9139 0.1367  0.0295  0.2053  606 TRP B CH2 
4820  N N   . SER A 591 ? 0.6510 1.0103 0.7748 0.1781  0.1078  0.2699  607 SER B N   
4821  C CA  . SER A 591 ? 0.7547 1.1553 0.8706 0.1790  0.1308  0.2624  607 SER B CA  
4822  C C   . SER A 591 ? 0.7709 1.1329 0.8693 0.1977  0.1279  0.2484  607 SER B C   
4823  O O   . SER A 591 ? 0.8270 1.1288 0.8975 0.2193  0.1095  0.2528  607 SER B O   
4824  C CB  . SER A 591 ? 0.8841 1.3051 0.9693 0.1882  0.1385  0.2799  607 SER B CB  
4825  O OG  . SER A 591 ? 0.9306 1.3018 0.9743 0.2164  0.1278  0.2856  607 SER B OG  
4826  N N   . THR A 592 ? 0.7706 1.1676 0.8840 0.1895  0.1464  0.2317  608 THR B N   
4827  C CA  . THR A 592 ? 0.8492 1.2115 0.9510 0.2042  0.1439  0.2164  608 THR B CA  
4828  C C   . THR A 592 ? 0.9135 1.2611 0.9719 0.2278  0.1483  0.2212  608 THR B C   
4829  O O   . THR A 592 ? 0.9373 1.2520 0.9815 0.2419  0.1454  0.2096  608 THR B O   
4830  C CB  . THR A 592 ? 0.7652 1.1686 0.8973 0.1880  0.1622  0.1960  608 THR B CB  
4831  O OG1 . THR A 592 ? 0.8625 1.3133 0.9869 0.1770  0.1799  0.1950  608 THR B OG1 
4832  C CG2 . THR A 592 ? 0.6510 1.0733 0.8282 0.1639  0.1605  0.1890  608 THR B CG2 
4833  N N   . ASP A 593 ? 1.0296 1.4022 1.0674 0.2320  0.1563  0.2371  609 ASP B N   
4834  C CA  . ASP A 593 ? 1.0318 1.4036 1.0342 0.2510  0.1660  0.2387  609 ASP B CA  
4835  C C   . ASP A 593 ? 1.0260 1.3469 0.9867 0.2762  0.1500  0.2546  609 ASP B C   
4836  O O   . ASP A 593 ? 1.0782 1.3873 1.0079 0.2948  0.1553  0.2544  609 ASP B O   
4837  C CB  . ASP A 593 ? 1.0576 1.4699 1.0648 0.2283  0.1711  0.2316  609 ASP B CB  
4838  C CG  . ASP A 593 ? 1.2072 1.6460 1.2219 0.2178  0.1695  0.2474  609 ASP B CG  
4839  O OD1 . ASP A 593 ? 1.1344 1.5887 1.1712 0.2108  0.1724  0.2586  609 ASP B OD1 
4840  O OD2 . ASP A 593 ? 1.4032 1.8485 1.4060 0.2151  0.1648  0.2476  609 ASP B OD2 
4841  N N   . TRP A 594 ? 0.9613 1.2506 0.9203 0.2779  0.1307  0.2678  610 TRP B N   
4842  C CA  . TRP A 594 ? 0.9587 1.1917 0.8791 0.3017  0.1136  0.2798  610 TRP B CA  
4843  C C   . TRP A 594 ? 0.9996 1.1681 0.9060 0.3102  0.1004  0.2595  610 TRP B C   
4844  O O   . TRP A 594 ? 1.0435 1.2025 0.9700 0.3107  0.0957  0.2532  610 TRP B O   
4845  C CB  . TRP A 594 ? 0.9676 1.1820 0.8944 0.2930  0.0966  0.2907  610 TRP B CB  
4846  C CG  . TRP A 594 ? 1.0108 1.1626 0.9101 0.2965  0.0791  0.2810  610 TRP B CG  
4847  C CD1 . TRP A 594 ? 1.0787 1.2291 0.9583 0.2980  0.0812  0.2813  610 TRP B CD1 
4848  C CD2 . TRP A 594 ? 1.0640 1.1484 0.9563 0.2964  0.0550  0.2697  610 TRP B CD2 
4849  N NE1 . TRP A 594 ? 1.1544 1.2427 1.0143 0.2993  0.0608  0.2719  610 TRP B NE1 
4850  C CE2 . TRP A 594 ? 1.1186 1.1667 0.9857 0.2972  0.0441  0.2648  610 TRP B CE2 
4851  C CE3 . TRP A 594 ? 1.1027 1.1561 1.0105 0.2946  0.0414  0.2626  610 TRP B CE3 
4852  C CZ2 . TRP A 594 ? 1.1633 1.1499 1.0201 0.2948  0.0201  0.2545  610 TRP B CZ2 
4853  C CZ3 . TRP A 594 ? 1.1174 1.1065 1.0133 0.2922  0.0170  0.2511  610 TRP B CZ3 
4854  C CH2 . TRP A 594 ? 1.1432 1.1021 1.0144 0.2916  0.0067  0.2480  610 TRP B CH2 
4855  N N   . SER A 595 ? 1.0326 1.1580 0.9076 0.3149  0.0938  0.2483  611 SER B N   
4856  C CA  . SER A 595 ? 1.1478 1.2126 1.0062 0.3182  0.0797  0.2294  611 SER B CA  
4857  C C   . SER A 595 ? 1.2074 1.2333 1.0385 0.3187  0.0690  0.2238  611 SER B C   
4858  O O   . SER A 595 ? 1.2417 1.2920 1.0638 0.3210  0.0792  0.2304  611 SER B O   
4859  C CB  . SER A 595 ? 1.1826 1.2588 1.0347 0.3257  0.0949  0.2174  611 SER B CB  
4860  O OG  . SER A 595 ? 1.2480 1.3246 1.0727 0.3326  0.1056  0.2113  611 SER B OG  
4861  N N   . PRO A 596 ? 1.1597 1.1289 0.9812 0.3157  0.0485  0.2117  612 PRO B N   
4862  C CA  . PRO A 596 ? 1.1858 1.1239 0.9857 0.3153  0.0388  0.2074  612 PRO B CA  
4863  C C   . PRO A 596 ? 1.2675 1.2146 1.0447 0.3243  0.0551  0.1993  612 PRO B C   
4864  O O   . PRO A 596 ? 1.3524 1.2858 1.1146 0.3253  0.0516  0.1987  612 PRO B O   
4865  C CB  . PRO A 596 ? 1.2208 1.1057 1.0233 0.3080  0.0144  0.1972  612 PRO B CB  
4866  C CG  . PRO A 596 ? 1.1981 1.0851 1.0268 0.3028  0.0070  0.2009  612 PRO B CG  
4867  C CD  . PRO A 596 ? 1.1890 1.1236 1.0256 0.3097  0.0306  0.2041  612 PRO B CD  
4868  N N   . TYR A 597 ? 1.3051 1.2764 1.0803 0.3309  0.0732  0.1936  613 TYR B N   
4869  C CA  . TYR A 597 ? 1.3864 1.3610 1.1391 0.3394  0.0871  0.1846  613 TYR B CA  
4870  C C   . TYR A 597 ? 1.4142 1.4449 1.1700 0.3474  0.1120  0.1919  613 TYR B C   
4871  O O   . TYR A 597 ? 1.4105 1.4442 1.1513 0.3547  0.1213  0.1867  613 TYR B O   
4872  C CB  . TYR A 597 ? 1.2956 1.2512 1.0392 0.3412  0.0885  0.1698  613 TYR B CB  
4873  C CG  . TYR A 597 ? 1.2781 1.2614 1.0385 0.3418  0.0985  0.1708  613 TYR B CG  
4874  C CD1 . TYR A 597 ? 1.3091 1.3385 1.0676 0.3496  0.1230  0.1724  613 TYR B CD1 
4875  C CD2 . TYR A 597 ? 1.2636 1.2286 1.0439 0.3346  0.0840  0.1689  613 TYR B CD2 
4876  C CE1 . TYR A 597 ? 1.2695 1.3284 1.0439 0.3492  0.1327  0.1740  613 TYR B CE1 
4877  C CE2 . TYR A 597 ? 1.2521 1.2448 1.0512 0.3354  0.0941  0.1688  613 TYR B CE2 
4878  C CZ  . TYR A 597 ? 1.2296 1.2703 1.0254 0.3423  0.1184  0.1717  613 TYR B CZ  
4879  O OH  . TYR A 597 ? 1.1735 1.2472 0.9913 0.3409  0.1285  0.1713  613 TYR B OH  
4880  N N   . ALA A 598 ? 1.3590 1.4370 1.1380 0.3459  0.1225  0.2037  614 ALA B N   
4881  C CA  . ALA A 598 ? 1.4197 1.5562 1.2123 0.3511  0.1424  0.2108  614 ALA B CA  
4882  C C   . ALA A 598 ? 1.6466 1.7873 1.4410 0.3470  0.1363  0.2210  614 ALA B C   
4883  O O   . ALA A 598 ? 1.5596 1.7010 1.3644 0.3378  0.1260  0.2325  614 ALA B O   
4884  C CB  . ALA A 598 ? 1.3641 1.5561 1.1881 0.3484  0.1533  0.2197  614 ALA B CB  
4885  N N   . THR B 1   ? 2.1583 1.7294 1.7618 -0.2885 -0.0095 -0.0895 333 THR C N   
4886  C CA  . THR B 1   ? 2.0717 1.6432 1.6889 -0.2786 -0.0049 -0.0884 333 THR C CA  
4887  C C   . THR B 1   ? 2.0644 1.5935 1.6611 -0.2635 0.0117  -0.0923 333 THR C C   
4888  O O   . THR B 1   ? 2.0096 1.5395 1.6178 -0.2465 0.0197  -0.0830 333 THR C O   
4889  C CB  . THR B 1   ? 2.0959 1.6477 1.7008 -0.2876 -0.0013 -0.0842 333 THR C CB  
4890  O OG1 . THR B 1   ? 2.1309 1.6181 1.6926 -0.2841 0.0177  -0.0869 333 THR C OG1 
4891  C CG2 . THR B 1   ? 2.1862 1.7589 1.7955 -0.3057 -0.0134 -0.0794 333 THR C CG2 
4892  N N   . ASN B 2   ? 2.1183 1.6305 1.6989 -0.2583 0.0185  -0.0977 334 ASN C N   
4893  C CA  . ASN B 2   ? 2.1394 1.6290 1.7163 -0.2319 0.0385  -0.0938 334 ASN C CA  
4894  C C   . ASN B 2   ? 2.0712 1.6233 1.6976 -0.2107 0.0284  -0.0832 334 ASN C C   
4895  O O   . ASN B 2   ? 2.0225 1.6197 1.6717 -0.2191 0.0096  -0.0868 334 ASN C O   
4896  C CB  . ASN B 2   ? 2.1829 1.6329 1.7243 -0.2369 0.0497  -0.1045 334 ASN C CB  
4897  C CG  . ASN B 2   ? 2.3480 1.7504 1.8725 -0.2113 0.0819  -0.0992 334 ASN C CG  
4898  O OD1 . ASN B 2   ? 2.3889 1.8071 1.9445 -0.1843 0.0913  -0.0828 334 ASN C OD1 
4899  N ND2 . ASN B 2   ? 2.3435 1.6854 1.8182 -0.2209 0.1003  -0.1108 334 ASN C ND2 
4900  N N   . LEU B 3   ? 1.9541 1.5082 1.5970 -0.1849 0.0408  -0.0676 335 LEU C N   
4901  C CA  . LEU B 3   ? 1.8265 1.4363 1.5098 -0.1692 0.0297  -0.0547 335 LEU C CA  
4902  C C   . LEU B 3   ? 1.8222 1.4483 1.5132 -0.1604 0.0288  -0.0582 335 LEU C C   
4903  O O   . LEU B 3   ? 1.8520 1.4419 1.5244 -0.1514 0.0472  -0.0604 335 LEU C O   
4904  C CB  . LEU B 3   ? 1.7932 1.4033 1.4938 -0.1478 0.0403  -0.0313 335 LEU C CB  
4905  C CG  . LEU B 3   ? 1.7846 1.4483 1.5192 -0.1417 0.0244  -0.0129 335 LEU C CG  
4906  C CD1 . LEU B 3   ? 1.7134 1.3702 1.4607 -0.1274 0.0335  0.0134  335 LEU C CD1 
4907  C CD2 . LEU B 3   ? 1.8480 1.5527 1.6051 -0.1324 0.0150  -0.0078 335 LEU C CD2 
4908  N N   . CYS B 4   ? 1.7317 1.4089 1.4479 -0.1632 0.0096  -0.0585 336 CYS C N   
4909  C CA  . CYS B 4   ? 1.7195 1.4143 1.4418 -0.1593 0.0052  -0.0640 336 CYS C CA  
4910  C C   . CYS B 4   ? 1.6978 1.3915 1.4319 -0.1335 0.0197  -0.0480 336 CYS C C   
4911  O O   . CYS B 4   ? 1.6729 1.3871 1.4299 -0.1197 0.0197  -0.0272 336 CYS C O   
4912  C CB  . CYS B 4   ? 1.6191 1.3659 1.3660 -0.1665 -0.0161 -0.0658 336 CYS C CB  
4913  S SG  . CYS B 4   ? 1.7092 1.4620 1.4520 -0.1946 -0.0300 -0.0827 336 CYS C SG  
4914  N N   . PRO B 5   ? 1.8973 1.5684 1.6170 -0.1280 0.0322  -0.0548 337 PRO C N   
4915  C CA  . PRO B 5   ? 1.9239 1.5929 1.6589 -0.1014 0.0507  -0.0372 337 PRO C CA  
4916  C C   . PRO B 5   ? 1.8069 1.5377 1.5819 -0.0912 0.0331  -0.0199 337 PRO C C   
4917  O O   . PRO B 5   ? 1.8085 1.5589 1.5925 -0.0853 0.0304  -0.0203 337 PRO C O   
4918  C CB  . PRO B 5   ? 2.0125 1.6451 1.7173 -0.1047 0.0649  -0.0537 337 PRO C CB  
4919  C CG  . PRO B 5   ? 1.9719 1.6211 1.6643 -0.1324 0.0400  -0.0744 337 PRO C CG  
4920  C CD  . PRO B 5   ? 1.9401 1.5961 1.6339 -0.1477 0.0266  -0.0763 337 PRO C CD  
4921  N N   . PHE B 6   ? 1.6270 1.3871 1.4217 -0.0922 0.0200  -0.0046 338 PHE C N   
4922  C CA  . PHE B 6   ? 1.4836 1.2970 1.3074 -0.0882 0.0022  0.0127  338 PHE C CA  
4923  C C   . PHE B 6   ? 1.4065 1.2319 1.2597 -0.0643 0.0139  0.0460  338 PHE C C   
4924  O O   . PHE B 6   ? 1.3170 1.1747 1.1906 -0.0559 0.0082  0.0582  338 PHE C O   
4925  C CB  . PHE B 6   ? 1.4646 1.3022 1.2895 -0.1054 -0.0180 0.0142  338 PHE C CB  
4926  C CG  . PHE B 6   ? 1.3400 1.1899 1.1537 -0.1248 -0.0330 -0.0100 338 PHE C CG  
4927  C CD1 . PHE B 6   ? 1.3639 1.2218 1.1771 -0.1255 -0.0365 -0.0237 338 PHE C CD1 
4928  C CD2 . PHE B 6   ? 1.4350 1.2898 1.2419 -0.1416 -0.0423 -0.0162 338 PHE C CD2 
4929  C CE1 . PHE B 6   ? 1.3095 1.1816 1.1195 -0.1417 -0.0494 -0.0415 338 PHE C CE1 
4930  C CE2 . PHE B 6   ? 1.5024 1.3696 1.3064 -0.1564 -0.0519 -0.0343 338 PHE C CE2 
4931  C CZ  . PHE B 6   ? 1.3171 1.1942 1.1249 -0.1558 -0.0559 -0.0458 338 PHE C CZ  
4932  N N   . ASP B 7   ? 1.3449 1.1459 1.2036 -0.0528 0.0309  0.0633  339 ASP C N   
4933  C CA  . ASP B 7   ? 1.4280 1.2440 1.3238 -0.0285 0.0436  0.1011  339 ASP C CA  
4934  C C   . ASP B 7   ? 1.4424 1.2438 1.3435 -0.0091 0.0666  0.1002  339 ASP C C   
4935  O O   . ASP B 7   ? 1.4369 1.2737 1.3751 0.0069  0.0674  0.1288  339 ASP C O   
4936  C CB  . ASP B 7   ? 1.5012 1.2883 1.4032 -0.0184 0.0612  0.1200  339 ASP C CB  
4937  C CG  . ASP B 7   ? 1.5662 1.3915 1.5191 -0.0009 0.0605  0.1706  339 ASP C CG  
4938  O OD1 . ASP B 7   ? 1.5737 1.4035 1.5573 0.0238  0.0808  0.1933  339 ASP C OD1 
4939  O OD2 . ASP B 7   ? 1.5407 1.3924 1.5040 -0.0133 0.0398  0.1903  339 ASP C OD2 
4940  N N   . GLU B 8   ? 1.4303 1.1818 1.2930 -0.0136 0.0838  0.0684  340 GLU C N   
4941  C CA  . GLU B 8   ? 1.4389 1.1726 1.3011 0.0027  0.1075  0.0671  340 GLU C CA  
4942  C C   . GLU B 8   ? 1.2751 1.0597 1.1529 -0.0017 0.0851  0.0658  340 GLU C C   
4943  O O   . GLU B 8   ? 1.3190 1.1006 1.2056 0.0139  0.1027  0.0716  340 GLU C O   
4944  C CB  . GLU B 8   ? 1.6260 1.2878 1.4332 -0.0072 0.1303  0.0333  340 GLU C CB  
4945  C CG  . GLU B 8   ? 1.6513 1.3140 1.4254 -0.0328 0.1107  -0.0001 340 GLU C CG  
4946  C CD  . GLU B 8   ? 1.8190 1.4089 1.5376 -0.0430 0.1362  -0.0260 340 GLU C CD  
4947  O OE1 . GLU B 8   ? 1.8132 1.3570 1.5222 -0.0236 0.1742  -0.0184 340 GLU C OE1 
4948  O OE2 . GLU B 8   ? 1.9579 1.5364 1.6419 -0.0718 0.1187  -0.0523 340 GLU C OE2 
4949  N N   . VAL B 9   ? 1.3003 1.1280 1.1806 -0.0218 0.0498  0.0592  341 VAL C N   
4950  C CA  . VAL B 9   ? 1.2282 1.1007 1.1199 -0.0275 0.0285  0.0575  341 VAL C CA  
4951  C C   . VAL B 9   ? 1.1849 1.1127 1.1183 -0.0195 0.0134  0.0953  341 VAL C C   
4952  O O   . VAL B 9   ? 1.1035 1.0602 1.0586 -0.0097 0.0121  0.1097  341 VAL C O   
4953  C CB  . VAL B 9   ? 1.1733 1.0551 1.0410 -0.0546 0.0026  0.0282  341 VAL C CB  
4954  C CG1 . VAL B 9   ? 1.0266 0.9577 0.9094 -0.0606 -0.0212 0.0326  341 VAL C CG1 
4955  C CG2 . VAL B 9   ? 1.2502 1.0910 1.0834 -0.0647 0.0119  -0.0033 341 VAL C CG2 
4956  N N   . PHE B 10  ? 1.0946 1.0362 1.0368 -0.0266 0.0011  0.1129  342 PHE C N   
4957  C CA  . PHE B 10  ? 1.0427 1.0362 1.0125 -0.0319 -0.0224 0.1471  342 PHE C CA  
4958  C C   . PHE B 10  ? 1.0323 1.0420 1.0477 -0.0081 -0.0077 0.1937  342 PHE C C   
4959  O O   . PHE B 10  ? 0.9414 0.9976 0.9894 -0.0045 -0.0200 0.2261  342 PHE C O   
4960  C CB  . PHE B 10  ? 1.1139 1.1085 1.0648 -0.0551 -0.0416 0.1431  342 PHE C CB  
4961  C CG  . PHE B 10  ? 1.0721 1.0702 0.9914 -0.0797 -0.0612 0.1109  342 PHE C CG  
4962  C CD1 . PHE B 10  ? 1.0830 1.0764 0.9907 -0.0804 -0.0601 0.0835  342 PHE C CD1 
4963  C CD2 . PHE B 10  ? 1.1414 1.1449 1.0428 -0.1023 -0.0782 0.1093  342 PHE C CD2 
4964  C CE1 . PHE B 10  ? 1.0867 1.0841 0.9724 -0.1006 -0.0753 0.0581  342 PHE C CE1 
4965  C CE2 . PHE B 10  ? 1.1251 1.1281 1.0009 -0.1218 -0.0899 0.0816  342 PHE C CE2 
4966  C CZ  . PHE B 10  ? 1.0309 1.0323 0.9022 -0.1197 -0.0882 0.0575  342 PHE C CZ  
4967  N N   . ASN B 11  ? 1.0511 1.0235 1.0710 0.0074  0.0185  0.2005  343 ASN C N   
4968  C CA  . ASN B 11  ? 1.0116 0.9910 1.0793 0.0355  0.0415  0.2450  343 ASN C CA  
4969  C C   . ASN B 11  ? 0.9822 0.9195 1.0487 0.0614  0.0822  0.2336  343 ASN C C   
4970  O O   . ASN B 11  ? 0.9622 0.8609 1.0402 0.0839  0.1176  0.2468  343 ASN C O   
4971  C CB  . ASN B 11  ? 1.0589 1.0231 1.1356 0.0373  0.0470  0.2656  343 ASN C CB  
4972  C CG  . ASN B 11  ? 1.1431 1.1430 1.2124 0.0073  0.0075  0.2756  343 ASN C CG  
4973  O OD1 . ASN B 11  ? 1.1091 1.1502 1.1752 -0.0121 -0.0224 0.2784  343 ASN C OD1 
4974  N ND2 . ASN B 11  ? 1.2239 1.2021 1.2848 0.0016  0.0092  0.2797  343 ASN C ND2 
4975  N N   . ALA B 12  ? 0.9576 0.8975 1.0062 0.0570  0.0792  0.2084  344 ALA C N   
4976  C CA  . ALA B 12  ? 1.0100 0.9145 1.0547 0.0781  0.1156  0.1995  344 ALA C CA  
4977  C C   . ALA B 12  ? 0.9761 0.9255 1.0798 0.1023  0.1252  0.2449  344 ALA C C   
4978  O O   . ALA B 12  ? 0.9171 0.9311 1.0506 0.0933  0.0926  0.2696  344 ALA C O   
4979  C CB  . ALA B 12  ? 0.9878 0.8758 0.9858 0.0592  0.1058  0.1532  344 ALA C CB  
4980  N N   . THR B 13  ? 0.9744 0.8864 1.0926 0.1320  0.1720  0.2565  345 THR C N   
4981  C CA  . THR B 13  ? 0.8904 0.8452 1.0751 0.1594  0.1872  0.3074  345 THR C CA  
4982  C C   . THR B 13  ? 0.8874 0.8803 1.0766 0.1546  0.1723  0.3024  345 THR C C   
4983  O O   . THR B 13  ? 0.9144 0.9762 1.1566 0.1582  0.1522  0.3446  345 THR C O   
4984  C CB  . THR B 13  ? 1.0668 0.9640 1.2651 0.1945  0.2482  0.3209  345 THR C CB  
4985  O OG1 . THR B 13  ? 1.0935 0.9404 1.2694 0.1940  0.2624  0.3125  345 THR C OG1 
4986  C CG2 . THR B 13  ? 1.0472 0.9969 1.3321 0.2257  0.2641  0.3874  345 THR C CG2 
4987  N N   . ARG B 14  ? 0.9382 0.8889 1.0727 0.1442  0.1800  0.2540  346 ARG C N   
4988  C CA  . ARG B 14  ? 0.9378 0.9231 1.0697 0.1351  0.1611  0.2440  346 ARG C CA  
4989  C C   . ARG B 14  ? 0.8231 0.8173 0.9080 0.0994  0.1182  0.2028  346 ARG C C   
4990  O O   . ARG B 14  ? 0.8463 0.8043 0.8898 0.0823  0.1117  0.1719  346 ARG C O   
4991  C CB  . ARG B 14  ? 1.2333 1.1687 1.3432 0.1503  0.2031  0.2253  346 ARG C CB  
4992  C CG  . ARG B 14  ? 1.4107 1.3386 1.5710 0.1872  0.2485  0.2680  346 ARG C CG  
4993  C CD  . ARG B 14  ? 1.5036 1.3462 1.6245 0.2036  0.3072  0.2442  346 ARG C CD  
4994  N NE  . ARG B 14  ? 1.7044 1.4857 1.8014 0.2076  0.3316  0.2366  346 ARG C NE  
4995  C CZ  . ARG B 14  ? 1.8132 1.5772 1.9525 0.2391  0.3716  0.2745  346 ARG C CZ  
4996  N NH1 . ARG B 14  ? 1.6869 1.4848 1.8956 0.2722  0.3991  0.3231  346 ARG C NH1 
4997  N NH2 . ARG B 14  ? 1.8883 1.5955 1.9989 0.2379  0.3881  0.2633  346 ARG C NH2 
4998  N N   . PHE B 15  ? 0.7245 0.7711 0.8211 0.0884  0.0885  0.2070  347 PHE C N   
4999  C CA  . PHE B 15  ? 0.6983 0.7550 0.7563 0.0580  0.0523  0.1712  347 PHE C CA  
5000  C C   . PHE B 15  ? 0.6666 0.7238 0.7134 0.0588  0.0570  0.1549  347 PHE C C   
5001  O O   . PHE B 15  ? 0.6320 0.7096 0.7136 0.0788  0.0738  0.1824  347 PHE C O   
5002  C CB  . PHE B 15  ? 0.7008 0.8179 0.7770 0.0393  0.0090  0.1919  347 PHE C CB  
5003  C CG  . PHE B 15  ? 0.6338 0.7395 0.6911 0.0224  -0.0066 0.1838  347 PHE C CG  
5004  C CD1 . PHE B 15  ? 0.6926 0.7780 0.7646 0.0354  0.0123  0.2025  347 PHE C CD1 
5005  C CD2 . PHE B 15  ? 0.6563 0.7677 0.6808 -0.0057 -0.0368 0.1565  347 PHE C CD2 
5006  C CE1 . PHE B 15  ? 0.7527 0.8275 0.8063 0.0193  -0.0015 0.1949  347 PHE C CE1 
5007  C CE2 . PHE B 15  ? 0.6567 0.7554 0.6636 -0.0205 -0.0472 0.1491  347 PHE C CE2 
5008  C CZ  . PHE B 15  ? 0.7351 0.8159 0.7552 -0.0088 -0.0306 0.1673  347 PHE C CZ  
5009  N N   . ALA B 16  ? 0.6342 0.6678 0.6348 0.0373  0.0445  0.1123  348 ALA C N   
5010  C CA  . ALA B 16  ? 0.6740 0.7103 0.6624 0.0345  0.0449  0.0971  348 ALA C CA  
5011  C C   . ALA B 16  ? 0.6156 0.7203 0.6365 0.0303  0.0139  0.1202  348 ALA C C   
5012  O O   . ALA B 16  ? 0.6488 0.7911 0.6852 0.0200  -0.0139 0.1370  348 ALA C O   
5013  C CB  . ALA B 16  ? 0.7816 0.7850 0.7183 0.0090  0.0326  0.0516  348 ALA C CB  
5014  N N   . SER B 17  ? 0.6428 0.7613 0.6704 0.0362  0.0192  0.1223  349 SER C N   
5015  C CA  . SER B 17  ? 0.6659 0.8461 0.7148 0.0259  -0.0150 0.1391  349 SER C CA  
5016  C C   . SER B 17  ? 0.6449 0.8202 0.6541 -0.0007 -0.0423 0.1003  349 SER C C   
5017  O O   . SER B 17  ? 0.6001 0.7307 0.5730 -0.0084 -0.0324 0.0657  349 SER C O   
5018  C CB  . SER B 17  ? 0.6471 0.8596 0.7332 0.0445  -0.0022 0.1695  349 SER C CB  
5019  O OG  . SER B 17  ? 0.6451 0.8233 0.7143 0.0546  0.0271  0.1513  349 SER C OG  
5020  N N   . VAL B 18  ? 0.6032 0.8229 0.6188 -0.0171 -0.0772 0.1086  350 VAL C N   
5021  C CA  . VAL B 18  ? 0.5631 0.7761 0.5463 -0.0420 -0.1023 0.0774  350 VAL C CA  
5022  C C   . VAL B 18  ? 0.6054 0.7981 0.5635 -0.0493 -0.1008 0.0451  350 VAL C C   
5023  O O   . VAL B 18  ? 0.6979 0.8628 0.6294 -0.0632 -0.1048 0.0159  350 VAL C O   
5024  C CB  . VAL B 18  ? 0.5304 0.7871 0.5195 -0.0586 -0.1351 0.0939  350 VAL C CB  
5025  C CG1 . VAL B 18  ? 0.6095 0.9009 0.6184 -0.0540 -0.1408 0.1133  350 VAL C CG1 
5026  C CG2 . VAL B 18  ? 0.5256 0.7513 0.4876 -0.0735 -0.1413 0.0578  350 VAL C CG2 
5027  N N   . TYR B 19  ? 0.5993 0.8064 0.5670 -0.0412 -0.0950 0.0523  351 TYR C N   
5028  C CA  . TYR B 19  ? 0.6061 0.7955 0.5482 -0.0516 -0.0964 0.0235  351 TYR C CA  
5029  C C   . TYR B 19  ? 0.6726 0.8051 0.5828 -0.0548 -0.0752 -0.0033 351 TYR C C   
5030  O O   . TYR B 19  ? 0.7504 0.8669 0.6345 -0.0734 -0.0860 -0.0296 351 TYR C O   
5031  C CB  . TYR B 19  ? 0.6180 0.8258 0.5739 -0.0405 -0.0875 0.0368  351 TYR C CB  
5032  C CG  . TYR B 19  ? 0.6358 0.8055 0.5892 -0.0211 -0.0466 0.0395  351 TYR C CG  
5033  C CD1 . TYR B 19  ? 0.6506 0.8235 0.6353 0.0024  -0.0227 0.0703  351 TYR C CD1 
5034  C CD2 . TYR B 19  ? 0.6624 0.7903 0.5809 -0.0272 -0.0301 0.0136  351 TYR C CD2 
5035  C CE1 . TYR B 19  ? 0.6334 0.7668 0.6165 0.0226  0.0204  0.0746  351 TYR C CE1 
5036  C CE2 . TYR B 19  ? 0.6359 0.7193 0.5444 -0.0104 0.0129  0.0158  351 TYR C CE2 
5037  C CZ  . TYR B 19  ? 0.5931 0.6789 0.5354 0.0161  0.0396  0.0462  351 TYR C CZ  
5038  O OH  . TYR B 19  ? 0.6563 0.6945 0.5915 0.0359  0.0878  0.0509  351 TYR C OH  
5039  N N   . ALA B 20  ? 0.6452 0.7461 0.5565 -0.0390 -0.0455 0.0050  352 ALA C N   
5040  C CA  . ALA B 20  ? 0.6583 0.6978 0.5328 -0.0444 -0.0235 -0.0183 352 ALA C CA  
5041  C C   . ALA B 20  ? 0.6757 0.7000 0.5503 -0.0448 -0.0224 -0.0171 352 ALA C C   
5042  O O   . ALA B 20  ? 0.6892 0.6674 0.5490 -0.0364 0.0065  -0.0188 352 ALA C O   
5043  C CB  . ALA B 20  ? 0.6669 0.6662 0.5314 -0.0268 0.0180  -0.0137 352 ALA C CB  
5044  N N   . TRP B 21  ? 0.6662 0.7248 0.5538 -0.0557 -0.0519 -0.0150 353 TRP C N   
5045  C CA  . TRP B 21  ? 0.7287 0.7790 0.6184 -0.0573 -0.0535 -0.0116 353 TRP C CA  
5046  C C   . TRP B 21  ? 0.7838 0.7785 0.6405 -0.0651 -0.0369 -0.0336 353 TRP C C   
5047  O O   . TRP B 21  ? 0.8566 0.8266 0.6845 -0.0808 -0.0381 -0.0565 353 TRP C O   
5048  C CB  . TRP B 21  ? 0.7639 0.8443 0.6567 -0.0751 -0.0851 -0.0171 353 TRP C CB  
5049  C CG  . TRP B 21  ? 0.6827 0.7656 0.5600 -0.0944 -0.1030 -0.0411 353 TRP C CG  
5050  C CD1 . TRP B 21  ? 0.6827 0.7902 0.5638 -0.0985 -0.1162 -0.0429 353 TRP C CD1 
5051  C CD2 . TRP B 21  ? 0.7499 0.8094 0.6087 -0.1118 -0.1081 -0.0634 353 TRP C CD2 
5052  N NE1 . TRP B 21  ? 0.7406 0.8262 0.6293 -0.0957 -0.1147 -0.0578 353 TRP C NE1 
5053  C CE2 . TRP B 21  ? 0.7357 0.7980 0.6153 -0.1025 -0.1103 -0.0676 353 TRP C CE2 
5054  C CE3 . TRP B 21  ? 0.7817 0.8110 0.6281 -0.1179 -0.1005 -0.0716 353 TRP C CE3 
5055  C CZ2 . TRP B 21  ? 0.7590 0.8053 0.6496 -0.1000 -0.1082 -0.0758 353 TRP C CZ2 
5056  C CZ3 . TRP B 21  ? 0.7988 0.8159 0.6540 -0.1199 -0.1009 -0.0817 353 TRP C CZ3 
5057  C CH2 . TRP B 21  ? 0.8343 0.8631 0.7149 -0.1090 -0.1043 -0.0813 353 TRP C CH2 
5058  N N   . ASN B 22  ? 0.6982 0.6721 0.5562 -0.0580 -0.0236 -0.0262 354 ASN C N   
5059  C CA  . ASN B 22  ? 0.8818 0.8006 0.7011 -0.0708 -0.0105 -0.0496 354 ASN C CA  
5060  C C   . ASN B 22  ? 0.9084 0.8299 0.7250 -0.0862 -0.0280 -0.0577 354 ASN C C   
5061  O O   . ASN B 22  ? 0.8083 0.7616 0.6487 -0.0826 -0.0409 -0.0437 354 ASN C O   
5062  C CB  . ASN B 22  ? 0.9895 0.8530 0.7913 -0.0554 0.0293  -0.0457 354 ASN C CB  
5063  C CG  . ASN B 22  ? 0.9605 0.8213 0.7834 -0.0384 0.0421  -0.0248 354 ASN C CG  
5064  O OD1 . ASN B 22  ? 0.9786 0.8588 0.8113 -0.0465 0.0227  -0.0227 354 ASN C OD1 
5065  N ND2 . ASN B 22  ? 0.9952 0.8300 0.8264 -0.0141 0.0776  -0.0073 354 ASN C ND2 
5066  N N   . ARG B 23  ? 0.9452 0.8321 0.7297 -0.1065 -0.0289 -0.0796 355 ARG C N   
5067  C CA  . ARG B 23  ? 0.9741 0.8663 0.7575 -0.1244 -0.0467 -0.0886 355 ARG C CA  
5068  C C   . ARG B 23  ? 1.0072 0.8453 0.7591 -0.1317 -0.0287 -0.0971 355 ARG C C   
5069  O O   . ARG B 23  ? 1.0189 0.8120 0.7367 -0.1365 -0.0107 -0.1063 355 ARG C O   
5070  C CB  . ARG B 23  ? 0.9936 0.9042 0.7749 -0.1460 -0.0699 -0.1024 355 ARG C CB  
5071  C CG  . ARG B 23  ? 1.0469 0.9470 0.8311 -0.1564 -0.0728 -0.1067 355 ARG C CG  
5072  C CD  . ARG B 23  ? 1.0449 0.9844 0.8703 -0.1477 -0.0850 -0.1001 355 ARG C CD  
5073  N NE  . ARG B 23  ? 0.9449 0.9179 0.8028 -0.1367 -0.0931 -0.0927 355 ARG C NE  
5074  C CZ  . ARG B 23  ? 0.9670 0.9643 0.8575 -0.1275 -0.0992 -0.0882 355 ARG C CZ  
5075  N NH1 . ARG B 23  ? 1.0372 1.0377 0.9379 -0.1272 -0.1017 -0.0883 355 ARG C NH1 
5076  N NH2 . ARG B 23  ? 0.9657 0.9799 0.8740 -0.1202 -0.1016 -0.0835 355 ARG C NH2 
5077  N N   . LYS B 24  ? 1.0171 0.8555 0.7764 -0.1329 -0.0314 -0.0932 356 LYS C N   
5078  C CA  . LYS B 24  ? 1.0788 0.8668 0.8096 -0.1391 -0.0147 -0.0988 356 LYS C CA  
5079  C C   . LYS B 24  ? 1.1205 0.9186 0.8516 -0.1622 -0.0353 -0.1077 356 LYS C C   
5080  O O   . LYS B 24  ? 1.1144 0.9540 0.8754 -0.1606 -0.0513 -0.1016 356 LYS C O   
5081  C CB  . LYS B 24  ? 1.1041 0.8838 0.8485 -0.1163 0.0038  -0.0811 356 LYS C CB  
5082  C CG  . LYS B 24  ? 1.3363 1.0760 1.0687 -0.0952 0.0384  -0.0729 356 LYS C CG  
5083  C CD  . LYS B 24  ? 1.2745 1.0363 1.0190 -0.0841 0.0408  -0.0684 356 LYS C CD  
5084  C CE  . LYS B 24  ? 1.1826 0.8902 0.8997 -0.0723 0.0784  -0.0700 356 LYS C CE  
5085  N NZ  . LYS B 24  ? 1.2461 0.9253 0.9743 -0.0452 0.1131  -0.0499 356 LYS C NZ  
5086  N N   . ARG B 25  ? 1.2232 0.9833 0.9200 -0.1857 -0.0344 -0.1206 357 ARG C N   
5087  C CA  . ARG B 25  ? 1.2733 1.0618 0.9974 -0.1926 -0.0480 -0.1140 357 ARG C CA  
5088  C C   . ARG B 25  ? 1.2981 1.0609 1.0091 -0.1970 -0.0412 -0.1146 357 ARG C C   
5089  O O   . ARG B 25  ? 1.3905 1.1019 1.0646 -0.2044 -0.0255 -0.1193 357 ARG C O   
5090  C CB  . ARG B 25  ? 1.3748 1.1522 1.0871 -0.2047 -0.0485 -0.1130 357 ARG C CB  
5091  C CG  . ARG B 25  ? 1.4548 1.2728 1.2032 -0.2101 -0.0656 -0.1033 357 ARG C CG  
5092  C CD  . ARG B 25  ? 1.5228 1.3115 1.2401 -0.2297 -0.0634 -0.1014 357 ARG C CD  
5093  N NE  . ARG B 25  ? 1.6931 1.4868 1.4178 -0.2414 -0.0701 -0.0945 357 ARG C NE  
5094  C CZ  . ARG B 25  ? 1.8718 1.6334 1.5615 -0.2616 -0.0674 -0.0919 357 ARG C CZ  
5095  N NH1 . ARG B 25  ? 1.8009 1.5183 1.4418 -0.2730 -0.0560 -0.0963 357 ARG C NH1 
5096  N NH2 . ARG B 25  ? 1.8764 1.6469 1.5761 -0.2720 -0.0750 -0.0843 357 ARG C NH2 
5097  N N   . ILE B 26  ? 1.3776 1.1728 1.1164 -0.1923 -0.0509 -0.1094 358 ILE C N   
5098  C CA  . ILE B 26  ? 1.4129 1.1922 1.1464 -0.1956 -0.0465 -0.1074 358 ILE C CA  
5099  C C   . ILE B 26  ? 1.5149 1.3139 1.2681 -0.2048 -0.0550 -0.1035 358 ILE C C   
5100  O O   . ILE B 26  ? 1.5374 1.3807 1.3278 -0.2009 -0.0664 -0.0979 358 ILE C O   
5101  C CB  . ILE B 26  ? 1.4063 1.2224 1.1708 -0.1785 -0.0498 -0.0951 358 ILE C CB  
5102  C CG1 . ILE B 26  ? 1.4727 1.2976 1.2458 -0.1550 -0.0413 -0.0834 358 ILE C CG1 
5103  C CG2 . ILE B 26  ? 1.4711 1.2742 1.2338 -0.1790 -0.0440 -0.0897 358 ILE C CG2 
5104  C CD1 . ILE B 26  ? 1.5772 1.3592 1.3270 -0.1443 -0.0188 -0.0833 358 ILE C CD1 
5105  N N   . SER B 27  ? 1.4113 1.3345 1.7297 -0.2759 0.1680  0.2569  359 SER C N   
5106  C CA  . SER B 27  ? 1.4288 1.3705 1.7810 -0.2810 0.1739  0.2412  359 SER C CA  
5107  C C   . SER B 27  ? 1.5218 1.4616 1.8747 -0.2950 0.1916  0.2577  359 SER C C   
5108  O O   . SER B 27  ? 1.5072 1.4213 1.8269 -0.2934 0.1864  0.2695  359 SER C O   
5109  C CB  . SER B 27  ? 1.4909 1.4174 1.8702 -0.2749 0.1549  0.2279  359 SER C CB  
5110  O OG  . SER B 27  ? 1.5251 1.4673 1.9167 -0.2638 0.1434  0.2041  359 SER C OG  
5111  N N   . ASN B 28  ? 1.8100 1.7775 2.1822 -0.3019 0.2063  0.2469  360 ASN C N   
5112  C CA  . ASN B 28  ? 1.8628 1.8332 2.2373 -0.3150 0.2238  0.2584  360 ASN C CA  
5113  C C   . ASN B 28  ? 1.7822 1.7490 2.1108 -0.3174 0.2336  0.2749  360 ASN C C   
5114  O O   . ASN B 28  ? 1.7816 1.7246 2.0743 -0.3158 0.2272  0.2813  360 ASN C O   
5115  C CB  . ASN B 28  ? 1.9059 1.8510 2.2754 -0.3114 0.2081  0.2532  360 ASN C CB  
5116  C CG  . ASN B 28  ? 1.9659 1.9073 2.3726 -0.3055 0.1926  0.2370  360 ASN C CG  
5117  O OD1 . ASN B 28  ? 1.9708 1.8904 2.3693 -0.2952 0.1735  0.2357  360 ASN C OD1 
5118  N ND2 . ASN B 28  ? 1.9420 1.9039 2.3872 -0.3114 0.1999  0.2235  360 ASN C ND2 
5119  N N   . CYS B 29  ? 1.4818 1.4744 1.8104 -0.3202 0.2489  0.2776  361 CYS C N   
5120  C CA  . CYS B 29  ? 1.4343 1.4248 1.7231 -0.3211 0.2572  0.2938  361 CYS C CA  
5121  C C   . CYS B 29  ? 1.4034 1.4283 1.6902 -0.3196 0.2685  0.2838  361 CYS C C   
5122  O O   . CYS B 29  ? 1.4352 1.4784 1.7400 -0.3121 0.2608  0.2608  361 CYS C O   
5123  C CB  . CYS B 29  ? 1.4579 1.4168 1.7140 -0.3103 0.2379  0.3007  361 CYS C CB  
5124  S SG  . CYS B 29  ? 1.4908 1.4539 1.7528 -0.2981 0.2237  0.2932  361 CYS C SG  
5125  N N   . VAL B 30  ? 1.4492 1.4830 1.7110 -0.3256 0.2854  0.2987  362 VAL C N   
5126  C CA  . VAL B 30  ? 1.3521 1.4175 1.6037 -0.3237 0.2959  0.2896  362 VAL C CA  
5127  C C   . VAL B 30  ? 1.4738 1.5295 1.6902 -0.3168 0.2912  0.3015  362 VAL C C   
5128  O O   . VAL B 30  ? 1.5337 1.5651 1.7269 -0.3198 0.2922  0.3244  362 VAL C O   
5129  C CB  . VAL B 30  ? 1.2739 1.3601 1.5242 -0.3362 0.3202  0.2962  362 VAL C CB  
5130  C CG1 . VAL B 30  ? 1.3839 1.4446 1.6035 -0.3425 0.3235  0.3175  362 VAL C CG1 
5131  C CG2 . VAL B 30  ? 1.2206 1.3362 1.4561 -0.3339 0.3304  0.2897  362 VAL C CG2 
5132  N N   . ALA B 31  ? 1.5088 1.5846 1.7207 -0.3078 0.2869  0.2862  363 ALA C N   
5133  C CA  . ALA B 31  ? 1.5641 1.6281 1.7499 -0.2978 0.2751  0.2911  363 ALA C CA  
5134  C C   . ALA B 31  ? 1.7163 1.7971 1.8721 -0.2985 0.2886  0.2998  363 ALA C C   
5135  O O   . ALA B 31  ? 1.6214 1.7321 1.7809 -0.3032 0.3043  0.2927  363 ALA C O   
5136  C CB  . ALA B 31  ? 1.5183 1.5888 1.7204 -0.2855 0.2570  0.2673  363 ALA C CB  
5137  N N   . ASP B 32  ? 2.1000 2.1616 2.2264 -0.2929 0.2810  0.3140  364 ASP C N   
5138  C CA  . ASP B 32  ? 2.2570 2.3285 2.3509 -0.2931 0.2921  0.3258  364 ASP C CA  
5139  C C   . ASP B 32  ? 2.3503 2.4321 2.4323 -0.2808 0.2815  0.3135  364 ASP C C   
5140  O O   . ASP B 32  ? 2.5422 2.6232 2.5935 -0.2785 0.2850  0.3255  364 ASP C O   
5141  C CB  . ASP B 32  ? 2.3903 2.4320 2.4570 -0.2976 0.2942  0.3542  364 ASP C CB  
5142  C CG  . ASP B 32  ? 2.6923 2.7416 2.7234 -0.2986 0.3074  0.3650  364 ASP C CG  
5143  O OD1 . ASP B 32  ? 2.7619 2.8447 2.7975 -0.3038 0.3241  0.3614  364 ASP C OD1 
5144  O OD2 . ASP B 32  ? 2.7651 2.7831 2.7606 -0.2908 0.2980  0.3685  364 ASP C OD2 
5145  N N   . TYR B 33  ? 2.0510 2.1426 2.1564 -0.2727 0.2685  0.2897  365 TYR C N   
5146  C CA  . TYR B 33  ? 2.0065 2.1134 2.1018 -0.2617 0.2611  0.2762  365 TYR C CA  
5147  C C   . TYR B 33  ? 2.1115 2.2538 2.1991 -0.2645 0.2786  0.2706  365 TYR C C   
5148  O O   . TYR B 33  ? 2.0841 2.2430 2.1648 -0.2561 0.2744  0.2582  365 TYR C O   
5149  C CB  . TYR B 33  ? 1.7795 1.8900 1.9016 -0.2521 0.2435  0.2512  365 TYR C CB  
5150  C CG  . TYR B 33  ? 1.7279 1.8508 1.8857 -0.2574 0.2471  0.2366  365 TYR C CG  
5151  C CD1 . TYR B 33  ? 1.7647 1.9210 1.9339 -0.2631 0.2634  0.2261  365 TYR C CD1 
5152  C CD2 . TYR B 33  ? 1.5454 1.6484 1.7268 -0.2554 0.2325  0.2305  365 TYR C CD2 
5153  C CE1 . TYR B 33  ? 1.7144 1.8827 1.9158 -0.2680 0.2669  0.2125  365 TYR C CE1 
5154  C CE2 . TYR B 33  ? 1.5069 1.6221 1.7214 -0.2599 0.2354  0.2162  365 TYR C CE2 
5155  C CZ  . TYR B 33  ? 1.6501 1.7983 1.8746 -0.2662 0.2528  0.2071  365 TYR C CZ  
5156  O OH  . TYR B 33  ? 1.6599 1.8223 1.9172 -0.2709 0.2568  0.1925  365 TYR C OH  
5157  N N   . SER B 34  ? 2.1651 2.3199 2.2543 -0.2761 0.2981  0.2789  366 SER C N   
5158  C CA  . SER B 34  ? 2.2493 2.4336 2.3239 -0.2792 0.3156  0.2789  366 SER C CA  
5159  C C   . SER B 34  ? 2.4534 2.6282 2.4892 -0.2761 0.3170  0.2971  366 SER C C   
5160  O O   . SER B 34  ? 2.4032 2.5945 2.4259 -0.2689 0.3156  0.2892  366 SER C O   
5161  C CB  . SER B 34  ? 2.2390 2.4351 2.3221 -0.2928 0.3361  0.2861  366 SER C CB  
5162  O OG  . SER B 34  ? 2.4127 2.5925 2.4688 -0.2999 0.3466  0.3126  366 SER C OG  
5163  N N   . VAL B 35  ? 3.0253 3.1724 3.0426 -0.2811 0.3188  0.3214  367 VAL C N   
5164  C CA  . VAL B 35  ? 3.0311 3.1694 3.0106 -0.2800 0.3230  0.3412  367 VAL C CA  
5165  C C   . VAL B 35  ? 2.9476 3.0545 2.9116 -0.2712 0.3038  0.3494  367 VAL C C   
5166  O O   . VAL B 35  ? 2.9205 3.0195 2.8527 -0.2687 0.3051  0.3644  367 VAL C O   
5167  C CB  . VAL B 35  ? 2.9984 3.1306 2.9631 -0.2923 0.3416  0.3647  367 VAL C CB  
5168  C CG1 . VAL B 35  ? 2.8997 2.9882 2.8594 -0.2920 0.3309  0.3741  367 VAL C CG1 
5169  C CG2 . VAL B 35  ? 2.9967 3.1349 2.9255 -0.2906 0.3519  0.3748  367 VAL C CG2 
5170  N N   . LEU B 36  ? 2.4046 2.4932 2.3892 -0.2665 0.2863  0.3404  368 LEU C N   
5171  C CA  . LEU B 36  ? 2.2710 2.3335 2.2407 -0.2568 0.2675  0.3450  368 LEU C CA  
5172  C C   . LEU B 36  ? 2.2644 2.3426 2.2308 -0.2448 0.2573  0.3268  368 LEU C C   
5173  O O   . LEU B 36  ? 2.1974 2.2585 2.1449 -0.2366 0.2444  0.3317  368 LEU C O   
5174  C CB  . LEU B 36  ? 2.0772 2.1114 2.0673 -0.2559 0.2519  0.3440  368 LEU C CB  
5175  C CG  . LEU B 36  ? 1.8754 1.8774 1.8468 -0.2478 0.2339  0.3541  368 LEU C CG  
5176  C CD1 . LEU B 36  ? 1.6842 1.6519 1.6588 -0.2526 0.2277  0.3702  368 LEU C CD1 
5177  C CD2 . LEU B 36  ? 1.5729 1.5787 1.5590 -0.2360 0.2158  0.3316  368 LEU C CD2 
5178  N N   . TYR B 37  ? 2.2423 2.3532 2.2261 -0.2438 0.2632  0.3061  369 TYR C N   
5179  C CA  . TYR B 37  ? 2.1885 2.3170 2.1673 -0.2331 0.2556  0.2895  369 TYR C CA  
5180  C C   . TYR B 37  ? 2.2617 2.3979 2.2048 -0.2314 0.2639  0.3018  369 TYR C C   
5181  O O   . TYR B 37  ? 2.2303 2.3757 2.1639 -0.2218 0.2560  0.2915  369 TYR C O   
5182  C CB  . TYR B 37  ? 2.1241 2.2863 2.1311 -0.2332 0.2608  0.2646  369 TYR C CB  
5183  C CG  . TYR B 37  ? 2.1117 2.3018 2.1109 -0.2255 0.2615  0.2494  369 TYR C CG  
5184  C CD1 . TYR B 37  ? 2.0307 2.2184 2.0338 -0.2133 0.2435  0.2336  369 TYR C CD1 
5185  C CD2 . TYR B 37  ? 2.1746 2.3941 2.1638 -0.2305 0.2803  0.2501  369 TYR C CD2 
5186  C CE1 . TYR B 37  ? 2.0596 2.2730 2.0559 -0.2062 0.2441  0.2194  369 TYR C CE1 
5187  C CE2 . TYR B 37  ? 2.1306 2.3762 2.1133 -0.2235 0.2810  0.2358  369 TYR C CE2 
5188  C CZ  . TYR B 37  ? 2.1291 2.3715 2.1154 -0.2114 0.2629  0.2206  369 TYR C CZ  
5189  O OH  . TYR B 37  ? 2.1052 2.3734 2.0852 -0.2045 0.2636  0.2064  369 TYR C OH  
5190  N N   . ASN B 38  ? 2.3483 2.4796 2.2709 -0.2403 0.2791  0.3241  370 ASN C N   
5191  C CA  . ASN B 38  ? 2.3554 2.4961 2.2444 -0.2398 0.2893  0.3365  370 ASN C CA  
5192  C C   . ASN B 38  ? 2.3908 2.4999 2.2495 -0.2390 0.2844  0.3610  370 ASN C C   
5193  O O   . ASN B 38  ? 2.3344 2.4476 2.1646 -0.2414 0.2959  0.3764  370 ASN C O   
5194  C CB  . ASN B 38  ? 2.3557 2.5209 2.2428 -0.2505 0.3128  0.3419  370 ASN C CB  
5195  C CG  . ASN B 38  ? 2.3406 2.5395 2.2556 -0.2514 0.3189  0.3178  370 ASN C CG  
5196  O OD1 . ASN B 38  ? 2.3443 2.5438 2.2893 -0.2553 0.3175  0.3077  370 ASN C OD1 
5197  N ND2 . ASN B 38  ? 2.3050 2.5325 2.2104 -0.2478 0.3257  0.3085  370 ASN C ND2 
5198  N N   . PHE B 39  ? 2.5416 2.6192 2.4058 -0.2358 0.2679  0.3650  371 PHE C N   
5199  C CA  . PHE B 39  ? 2.4918 2.5389 2.3275 -0.2337 0.2611  0.3865  371 PHE C CA  
5200  C C   . PHE B 39  ? 2.4773 2.5297 2.2879 -0.2234 0.2544  0.3843  371 PHE C C   
5201  O O   . PHE B 39  ? 2.5196 2.5612 2.3003 -0.2189 0.2589  0.3879  371 PHE C O   
5202  C CB  . PHE B 39  ? 2.4032 2.4157 2.2521 -0.2306 0.2427  0.3866  371 PHE C CB  
5203  C CG  . PHE B 39  ? 2.3625 2.3497 2.2205 -0.2350 0.2453  0.3849  371 PHE C CG  
5204  C CD1 . PHE B 39  ? 2.3890 2.3968 2.2631 -0.2458 0.2626  0.3845  371 PHE C CD1 
5205  C CD2 . PHE B 39  ? 2.3459 2.2896 2.1954 -0.2280 0.2303  0.3819  371 PHE C CD2 
5206  C CE1 . PHE B 39  ? 2.3811 2.3660 2.2617 -0.2500 0.2645  0.3823  371 PHE C CE1 
5207  C CE2 . PHE B 39  ? 2.2714 2.1938 2.1268 -0.2321 0.2325  0.3788  371 PHE C CE2 
5208  C CZ  . PHE B 39  ? 2.3575 2.2999 2.2280 -0.2433 0.2493  0.3795  371 PHE C CZ  
5209  N N   . ALA B 40  ? 2.6140 2.6708 2.4371 -0.2130 0.2386  0.3636  372 ALA C N   
5210  C CA  . ALA B 40  ? 2.5626 2.6299 2.3700 -0.2022 0.2308  0.3541  372 ALA C CA  
5211  C C   . ALA B 40  ? 2.4877 2.5266 2.2718 -0.1940 0.2150  0.3643  372 ALA C C   
5212  O O   . ALA B 40  ? 2.4955 2.5441 2.2604 -0.1864 0.2122  0.3606  372 ALA C O   
5213  C CB  . ALA B 40  ? 2.5433 2.6390 2.3303 -0.2046 0.2487  0.3578  372 ALA C CB  
5214  N N   . PRO B 41  ? 2.0857 2.0905 1.8701 -0.1948 0.2040  0.3762  373 PRO C N   
5215  C CA  . PRO B 41  ? 1.9406 1.9209 1.7095 -0.1851 0.1856  0.3792  373 PRO C CA  
5216  C C   . PRO B 41  ? 1.8021 1.7804 1.5938 -0.1756 0.1668  0.3562  373 PRO C C   
5217  O O   . PRO B 41  ? 1.6858 1.6426 1.4673 -0.1676 0.1504  0.3575  373 PRO C O   
5218  C CB  . PRO B 41  ? 1.8708 1.8068 1.6343 -0.1824 0.1791  0.3813  373 PRO C CB  
5219  C CG  . PRO B 41  ? 1.9473 1.8878 1.7367 -0.1931 0.1877  0.3826  373 PRO C CG  
5220  C CD  . PRO B 41  ? 2.0280 2.0116 1.8233 -0.2030 0.2079  0.3861  373 PRO C CD  
5221  N N   . PHE B 42  ? 1.7627 1.7640 1.5844 -0.1762 0.1690  0.3352  374 PHE C N   
5222  C CA  . PHE B 42  ? 1.6183 1.6161 1.4671 -0.1689 0.1519  0.3138  374 PHE C CA  
5223  C C   . PHE B 42  ? 1.6077 1.6206 1.4501 -0.1574 0.1431  0.2967  374 PHE C C   
5224  O O   . PHE B 42  ? 1.5731 1.6179 1.4179 -0.1567 0.1528  0.2843  374 PHE C O   
5225  C CB  . PHE B 42  ? 1.4945 1.5097 1.3783 -0.1747 0.1583  0.2992  374 PHE C CB  
5226  C CG  . PHE B 42  ? 1.6159 1.6242 1.5041 -0.1872 0.1719  0.3156  374 PHE C CG  
5227  C CD1 . PHE B 42  ? 1.4975 1.4723 1.3867 -0.1905 0.1644  0.3303  374 PHE C CD1 
5228  C CD2 . PHE B 42  ? 1.6937 1.7286 1.5863 -0.1958 0.1919  0.3157  374 PHE C CD2 
5229  C CE1 . PHE B 42  ? 1.5778 1.5458 1.4713 -0.2022 0.1769  0.3456  374 PHE C CE1 
5230  C CE2 . PHE B 42  ? 1.8630 1.8910 1.7601 -0.2075 0.2045  0.3307  374 PHE C CE2 
5231  C CZ  . PHE B 42  ? 1.7826 1.7770 1.6803 -0.2107 0.1969  0.3456  374 PHE C CZ  
5232  N N   . PHE B 43  ? 1.8542 1.8436 1.6887 -0.1485 0.1245  0.2961  375 PHE C N   
5233  C CA  . PHE B 43  ? 1.8784 1.8762 1.7070 -0.1368 0.1130  0.2803  375 PHE C CA  
5234  C C   . PHE B 43  ? 1.8608 1.8707 1.7226 -0.1313 0.1030  0.2534  375 PHE C C   
5235  O O   . PHE B 43  ? 1.7553 1.7659 1.6162 -0.1208 0.0896  0.2393  375 PHE C O   
5236  C CB  . PHE B 43  ? 1.6832 1.6490 1.4907 -0.1297 0.0967  0.2908  375 PHE C CB  
5237  C CG  . PHE B 43  ? 1.7195 1.6818 1.4890 -0.1301 0.1039  0.3105  375 PHE C CG  
5238  C CD1 . PHE B 43  ? 1.7448 1.7199 1.5008 -0.1394 0.1239  0.3257  375 PHE C CD1 
5239  C CD2 . PHE B 43  ? 1.6753 1.6224 1.4226 -0.1209 0.0909  0.3131  375 PHE C CD2 
5240  C CE1 . PHE B 43  ? 1.8057 1.7775 1.5267 -0.1395 0.1305  0.3438  375 PHE C CE1 
5241  C CE2 . PHE B 43  ? 1.6731 1.6173 1.3854 -0.1210 0.0973  0.3309  375 PHE C CE2 
5242  C CZ  . PHE B 43  ? 1.8120 1.7687 1.5111 -0.1303 0.1172  0.3463  375 PHE C CZ  
5243  N N   . THR B 44  ? 1.5854 1.6020 1.4761 -0.1380 0.1084  0.2469  376 THR C N   
5244  C CA  . THR B 44  ? 1.5402 1.5780 1.4631 -0.1351 0.1053  0.2211  376 THR C CA  
5245  C C   . THR B 44  ? 1.5371 1.5811 1.4851 -0.1456 0.1161  0.2214  376 THR C C   
5246  O O   . THR B 44  ? 1.5201 1.5399 1.4798 -0.1491 0.1099  0.2285  376 THR C O   
5247  C CB  . THR B 44  ? 1.5036 1.5239 1.4413 -0.1249 0.0829  0.2061  376 THR C CB  
5248  O OG1 . THR B 44  ? 1.6676 1.6848 1.5831 -0.1150 0.0733  0.2039  376 THR C OG1 
5249  C CG2 . THR B 44  ? 1.3660 1.4077 1.3380 -0.1220 0.0797  0.1796  376 THR C CG2 
5250  N N   . PHE B 45  ? 1.3017 1.3779 1.2582 -0.1509 0.1324  0.2139  377 PHE C N   
5251  C CA  . PHE B 45  ? 1.1655 1.2509 1.1481 -0.1602 0.1425  0.2109  377 PHE C CA  
5252  C C   . PHE B 45  ? 1.1411 1.2549 1.1516 -0.1561 0.1411  0.1832  377 PHE C C   
5253  O O   . PHE B 45  ? 1.1198 1.2649 1.1329 -0.1593 0.1555  0.1758  377 PHE C O   
5254  C CB  . PHE B 45  ? 1.2297 1.3276 1.1975 -0.1710 0.1642  0.2276  377 PHE C CB  
5255  C CG  . PHE B 45  ? 1.2425 1.3449 1.2332 -0.1820 0.1755  0.2294  377 PHE C CG  
5256  C CD1 . PHE B 45  ? 1.1460 1.2549 1.1715 -0.1816 0.1699  0.2105  377 PHE C CD1 
5257  C CD2 . PHE B 45  ? 1.3910 1.4917 1.3680 -0.1928 0.1923  0.2501  377 PHE C CD2 
5258  C CE1 . PHE B 45  ? 1.1659 1.2792 1.2120 -0.1919 0.1806  0.2124  377 PHE C CE1 
5259  C CE2 . PHE B 45  ? 1.4898 1.5947 1.4877 -0.2032 0.2030  0.2518  377 PHE C CE2 
5260  C CZ  . PHE B 45  ? 1.2745 1.3859 1.3072 -0.2027 0.1971  0.2327  377 PHE C CZ  
5261  N N   . LYS B 46  ? 1.0184 1.1212 1.0501 -0.1489 0.1237  0.1677  378 LYS C N   
5262  C CA  . LYS B 46  ? 1.0256 1.1538 1.0824 -0.1433 0.1201  0.1406  378 LYS C CA  
5263  C C   . LYS B 46  ? 0.9889 1.1188 1.0806 -0.1484 0.1203  0.1307  378 LYS C C   
5264  O O   . LYS B 46  ? 0.9976 1.1016 1.1021 -0.1472 0.1074  0.1320  378 LYS C O   
5265  C CB  . LYS B 46  ? 1.0860 1.2057 1.1426 -0.1302 0.1004  0.1263  378 LYS C CB  
5266  C CG  . LYS B 46  ? 1.2752 1.3998 1.3004 -0.1237 0.1000  0.1306  378 LYS C CG  
5267  C CD  . LYS B 46  ? 1.3453 1.5078 1.3653 -0.1261 0.1170  0.1236  378 LYS C CD  
5268  C CE  . LYS B 46  ? 1.3142 1.5037 1.3601 -0.1204 0.1137  0.0954  378 LYS C CE  
5269  N NZ  . LYS B 46  ? 1.2189 1.4338 1.2501 -0.1144 0.1176  0.0858  378 LYS C NZ  
5270  N N   . CYS B 47  ? 1.1317 1.2925 1.2390 -0.1539 0.1348  0.1203  379 CYS C N   
5271  C CA  . CYS B 47  ? 1.1219 1.2879 1.2605 -0.1609 0.1392  0.1132  379 CYS C CA  
5272  C C   . CYS B 47  ? 1.1931 1.3780 1.3624 -0.1545 0.1314  0.0848  379 CYS C C   
5273  O O   . CYS B 47  ? 1.3839 1.6015 1.5626 -0.1560 0.1423  0.0713  379 CYS C O   
5274  C CB  . CYS B 47  ? 0.9809 1.1666 1.1159 -0.1729 0.1620  0.1232  379 CYS C CB  
5275  S SG  . CYS B 47  ? 1.1767 1.3411 1.3249 -0.1847 0.1674  0.1391  379 CYS C SG  
5276  N N   . TYR B 48  ? 1.0991 1.2354 1.1520 -0.3254 0.2154  -0.2090 380 TYR C N   
5277  C CA  . TYR B 48  ? 1.2728 1.3781 1.3408 -0.3286 0.2335  -0.2214 380 TYR C CA  
5278  C C   . TYR B 48  ? 1.4595 1.5319 1.5326 -0.3145 0.2285  -0.2047 380 TYR C C   
5279  O O   . TYR B 48  ? 1.3603 1.4230 1.4308 -0.2976 0.2113  -0.1845 380 TYR C O   
5280  C CB  . TYR B 48  ? 1.1388 1.2248 1.2189 -0.3198 0.2372  -0.2275 380 TYR C CB  
5281  C CG  . TYR B 48  ? 1.0173 1.1332 1.0946 -0.3280 0.2362  -0.2371 380 TYR C CG  
5282  C CD1 . TYR B 48  ? 1.0548 1.1878 1.1230 -0.3392 0.2451  -0.2559 380 TYR C CD1 
5283  C CD2 . TYR B 48  ? 1.0287 1.1531 1.1032 -0.3148 0.2197  -0.2227 380 TYR C CD2 
5284  C CE1 . TYR B 48  ? 0.9472 1.1091 1.0127 -0.3467 0.2426  -0.2630 380 TYR C CE1 
5285  C CE2 . TYR B 48  ? 1.0401 1.1935 1.1111 -0.3200 0.2167  -0.2289 380 TYR C CE2 
5286  C CZ  . TYR B 48  ? 0.9296 1.1051 1.0002 -0.3409 0.2304  -0.2503 380 TYR C CZ  
5287  O OH  . TYR B 48  ? 0.8866 1.0912 0.9543 -0.3453 0.2261  -0.2547 380 TYR C OH  
5288  N N   . GLY B 49  ? 1.6717 1.7235 1.7487 -0.3150 0.2403  -0.2109 381 GLY C N   
5289  C CA  . GLY B 49  ? 1.6847 1.7047 1.7687 -0.3026 0.2371  -0.1961 381 GLY C CA  
5290  C C   . GLY B 49  ? 1.8539 1.8830 1.9304 -0.3062 0.2288  -0.1802 381 GLY C C   
5291  O O   . GLY B 49  ? 1.8345 1.8465 1.9145 -0.3043 0.2342  -0.1775 381 GLY C O   
5292  N N   . VAL B 50  ? 1.6405 1.6965 1.7018 -0.3050 0.2124  -0.1688 382 VAL C N   
5293  C CA  . VAL B 50  ? 1.6366 1.6996 1.6869 -0.3027 0.2004  -0.1513 382 VAL C CA  
5294  C C   . VAL B 50  ? 1.6582 1.7654 1.6908 -0.3168 0.1972  -0.1558 382 VAL C C   
5295  O O   . VAL B 50  ? 1.7289 1.8596 1.7573 -0.3237 0.1988  -0.1675 382 VAL C O   
5296  C CB  . VAL B 50  ? 1.5043 1.5476 1.5525 -0.2820 0.1792  -0.1266 382 VAL C CB  
5297  C CG1 . VAL B 50  ? 1.4872 1.5543 1.5227 -0.2770 0.1637  -0.1204 382 VAL C CG1 
5298  C CG2 . VAL B 50  ? 1.5843 1.6219 1.6267 -0.2794 0.1709  -0.1094 382 VAL C CG2 
5299  N N   . SER B 51  ? 1.8375 1.9568 1.8608 -0.3227 0.1949  -0.1485 383 SER C N   
5300  C CA  . SER B 51  ? 1.8705 2.0311 1.8759 -0.3343 0.1897  -0.1503 383 SER C CA  
5301  C C   . SER B 51  ? 1.8434 2.0120 1.8354 -0.3220 0.1660  -0.1273 383 SER C C   
5302  O O   . SER B 51  ? 1.8806 2.0241 1.8749 -0.3085 0.1554  -0.1087 383 SER C O   
5303  C CB  . SER B 51  ? 1.8665 2.0389 1.8677 -0.3486 0.2012  -0.1564 383 SER C CB  
5304  O OG  . SER B 51  ? 1.8311 2.0393 1.8142 -0.3569 0.1932  -0.1528 383 SER C OG  
5305  N N   . PRO B 52  ? 1.6173 1.8199 1.5945 -0.3259 0.1565  -0.1274 384 PRO C N   
5306  C CA  . PRO B 52  ? 1.6509 1.8588 1.6148 -0.3126 0.1334  -0.1051 384 PRO C CA  
5307  C C   . PRO B 52  ? 1.6861 1.8836 1.6438 -0.3083 0.1244  -0.0865 384 PRO C C   
5308  O O   . PRO B 52  ? 1.7228 1.8913 1.6834 -0.2921 0.1122  -0.0683 384 PRO C O   
5309  C CB  . PRO B 52  ? 1.6772 1.9295 1.6253 -0.3229 0.1292  -0.1120 384 PRO C CB  
5310  C CG  . PRO B 52  ? 1.6469 1.9178 1.5979 -0.3437 0.1496  -0.1358 384 PRO C CG  
5311  C CD  . PRO B 52  ? 1.6421 1.8802 1.6131 -0.3428 0.1658  -0.1472 384 PRO C CD  
5312  N N   . THR B 53  ? 1.7737 1.9942 1.7229 -0.3228 0.1304  -0.0906 385 THR C N   
5313  C CA  . THR B 53  ? 1.7436 1.9569 1.6876 -0.3212 0.1239  -0.0741 385 THR C CA  
5314  C C   . THR B 53  ? 1.8524 2.0259 1.8137 -0.3142 0.1308  -0.0697 385 THR C C   
5315  O O   . THR B 53  ? 1.8877 2.0351 1.8504 -0.2991 0.1167  -0.0501 385 THR C O   
5316  C CB  . THR B 53  ? 1.6015 1.8458 1.5362 -0.3394 0.1335  -0.0832 385 THR C CB  
5317  O OG1 . THR B 53  ? 1.6374 1.8896 1.5805 -0.3535 0.1550  -0.1083 385 THR C OG1 
5318  C CG2 . THR B 53  ? 1.5348 1.8152 1.4491 -0.3428 0.1204  -0.0787 385 THR C CG2 
5319  N N   . LYS B 54  ? 2.1326 2.3009 2.1064 -0.3251 0.1521  -0.0877 386 LYS C N   
5320  C CA  . LYS B 54  ? 2.0936 2.2260 2.0849 -0.3202 0.1618  -0.0867 386 LYS C CA  
5321  C C   . LYS B 54  ? 2.1622 2.2587 2.1621 -0.3004 0.1492  -0.0715 386 LYS C C   
5322  O O   . LYS B 54  ? 2.1596 2.2279 2.1672 -0.2922 0.1461  -0.0583 386 LYS C O   
5323  C CB  . LYS B 54  ? 2.0025 2.1319 2.0066 -0.3308 0.1852  -0.1120 386 LYS C CB  
5324  C CG  . LYS B 54  ? 2.0085 2.1618 2.0081 -0.3493 0.2015  -0.1270 386 LYS C CG  
5325  C CD  . LYS B 54  ? 2.1415 2.2819 2.1453 -0.3493 0.2051  -0.1167 386 LYS C CD  
5326  C CE  . LYS B 54  ? 2.1452 2.3184 2.1349 -0.3632 0.2080  -0.1180 386 LYS C CE  
5327  N NZ  . LYS B 54  ? 2.1389 2.3313 2.1119 -0.3597 0.1873  -0.0992 386 LYS C NZ  
5328  N N   . LEU B 55  ? 2.0585 2.1560 2.0570 -0.2927 0.1421  -0.0737 387 LEU C N   
5329  C CA  . LEU B 55  ? 1.9733 2.0384 1.9780 -0.2731 0.1294  -0.0598 387 LEU C CA  
5330  C C   . LEU B 55  ? 1.9927 2.0447 1.9884 -0.2613 0.1093  -0.0335 387 LEU C C   
5331  O O   . LEU B 55  ? 2.0233 2.0409 2.0289 -0.2509 0.1063  -0.0222 387 LEU C O   
5332  C CB  . LEU B 55  ? 1.9628 2.0405 1.9630 -0.2679 0.1231  -0.0648 387 LEU C CB  
5333  C CG  . LEU B 55  ? 1.9322 1.9888 1.9306 -0.2470 0.1046  -0.0480 387 LEU C CG  
5334  C CD1 . LEU B 55  ? 1.8896 1.9052 1.9070 -0.2364 0.1114  -0.0494 387 LEU C CD1 
5335  C CD2 . LEU B 55  ? 1.8098 1.8925 1.7999 -0.2464 0.0995  -0.0544 387 LEU C CD2 
5336  N N   . ASN B 56  ? 1.8584 1.9377 1.8350 -0.2634 0.0953  -0.0237 388 ASN C N   
5337  C CA  . ASN B 56  ? 1.8268 1.8961 1.7921 -0.2533 0.0751  0.0015  388 ASN C CA  
5338  C C   . ASN B 56  ? 1.7839 1.8288 1.7591 -0.2539 0.0795  0.0099  388 ASN C C   
5339  O O   . ASN B 56  ? 1.7416 1.7546 1.7197 -0.2399 0.0672  0.0277  388 ASN C O   
5340  C CB  . ASN B 56  ? 1.8209 1.9279 1.7650 -0.2614 0.0656  0.0065  388 ASN C CB  
5341  C CG  . ASN B 56  ? 1.9007 2.0260 1.8318 -0.2545 0.0528  0.0078  388 ASN C CG  
5342  O OD1 . ASN B 56  ? 1.9383 2.0506 1.8598 -0.2389 0.0330  0.0263  388 ASN C OD1 
5343  N ND2 . ASN B 56  ? 1.9251 2.0809 1.8548 -0.2662 0.0637  -0.0117 388 ASN C ND2 
5344  N N   . ASP B 57  ? 1.7720 1.8313 1.7526 -0.2700 0.0973  -0.0031 389 ASP C N   
5345  C CA  . ASP B 57  ? 1.6900 1.7285 1.6825 -0.2720 0.1052  0.0016  389 ASP C CA  
5346  C C   . ASP B 57  ? 1.6618 1.6667 1.6753 -0.2657 0.1175  -0.0071 389 ASP C C   
5347  O O   . ASP B 57  ? 1.6412 1.6419 1.6670 -0.2744 0.1356  -0.0184 389 ASP C O   
5348  C CB  . ASP B 57  ? 1.7056 1.7735 1.6953 -0.2909 0.1207  -0.0104 389 ASP C CB  
5349  C CG  . ASP B 57  ? 1.7496 1.8544 1.7180 -0.2982 0.1104  -0.0054 389 ASP C CG  
5350  O OD1 . ASP B 57  ? 1.7756 1.8803 1.7341 -0.2948 0.0956  0.0148  389 ASP C OD1 
5351  O OD2 . ASP B 57  ? 1.7061 1.8391 1.6675 -0.3068 0.1161  -0.0212 389 ASP C OD2 
5352  N N   . LEU B 58  ? 1.7248 1.7060 1.7426 -0.2504 0.1086  -0.0026 390 LEU C N   
5353  C CA  . LEU B 58  ? 1.7653 1.7111 1.8028 -0.2424 0.1181  -0.0083 390 LEU C CA  
5354  C C   . LEU B 58  ? 1.7955 1.7138 1.8323 -0.2222 0.1003  0.0061  390 LEU C C   
5355  O O   . LEU B 58  ? 1.7939 1.7259 1.8190 -0.2169 0.0891  0.0079  390 LEU C O   
5356  C CB  . LEU B 58  ? 1.7198 1.6746 1.7676 -0.2524 0.1401  -0.0352 390 LEU C CB  
5357  C CG  . LEU B 58  ? 1.7074 1.6267 1.7758 -0.2455 0.1523  -0.0433 390 LEU C CG  
5358  C CD1 . LEU B 58  ? 1.6373 1.5316 1.7173 -0.2441 0.1574  -0.0354 390 LEU C CD1 
5359  C CD2 . LEU B 58  ? 1.5766 1.5099 1.6518 -0.2585 0.1742  -0.0705 390 LEU C CD2 
5360  N N   . CYS B 59  ? 1.9365 1.8170 1.9847 -0.2108 0.0968  0.0173  391 CYS C N   
5361  C CA  . CYS B 59  ? 1.9721 1.8217 2.0218 -0.1910 0.0824  0.0290  391 CYS C CA  
5362  C C   . CYS B 59  ? 1.9170 1.7459 1.9845 -0.1868 0.0972  0.0131  391 CYS C C   
5363  O O   . CYS B 59  ? 1.9161 1.7440 1.9974 -0.1972 0.1176  -0.0031 391 CYS C O   
5364  C CB  . CYS B 59  ? 2.0206 1.8389 2.0706 -0.1797 0.0674  0.0523  391 CYS C CB  
5365  S SG  . CYS B 59  ? 2.3037 2.1429 2.3350 -0.1863 0.0521  0.0713  391 CYS C SG  
5366  N N   . PHE B 60  ? 1.7171 1.5287 1.7839 -0.1709 0.0865  0.0181  392 PHE C N   
5367  C CA  . PHE B 60  ? 1.7124 1.5036 1.7949 -0.1651 0.0984  0.0047  392 PHE C CA  
5368  C C   . PHE B 60  ? 1.7396 1.4903 1.8257 -0.1434 0.0838  0.0211  392 PHE C C   
5369  O O   . PHE B 60  ? 1.7399 1.4809 1.8139 -0.1326 0.0632  0.0422  392 PHE C O   
5370  C CB  . PHE B 60  ? 1.6834 1.5014 1.7617 -0.1695 0.1035  -0.0109 392 PHE C CB  
5371  C CG  . PHE B 60  ? 1.6161 1.4691 1.6936 -0.1909 0.1208  -0.0304 392 PHE C CG  
5372  C CD1 . PHE B 60  ? 1.6075 1.4546 1.7006 -0.2013 0.1433  -0.0496 392 PHE C CD1 
5373  C CD2 . PHE B 60  ? 1.5538 1.4447 1.6141 -0.2005 0.1143  -0.0293 392 PHE C CD2 
5374  C CE1 . PHE B 60  ? 1.5509 1.4286 1.6422 -0.2207 0.1592  -0.0679 392 PHE C CE1 
5375  C CE2 . PHE B 60  ? 1.5478 1.4702 1.6068 -0.2201 0.1301  -0.0475 392 PHE C CE2 
5376  C CZ  . PHE B 60  ? 1.5144 1.4299 1.5887 -0.2303 0.1526  -0.0670 392 PHE C CZ  
5377  N N   . THR B 61  ? 1.7617 1.4882 1.8637 -0.1369 0.0945  0.0109  393 THR C N   
5378  C CA  . THR B 61  ? 1.8117 1.5132 1.9106 -0.1109 0.0757  0.0240  393 THR C CA  
5379  C C   . THR B 61  ? 1.7682 1.4589 1.8614 -0.0974 0.0647  0.0301  393 THR C C   
5380  O O   . THR B 61  ? 1.7571 1.4327 1.8346 -0.0789 0.0425  0.0471  393 THR C O   
5381  C CB  . THR B 61  ? 1.9166 1.6231 2.0211 -0.1011 0.0807  0.0118  393 THR C CB  
5382  O OG1 . THR B 61  ? 1.9619 1.6563 2.0532 -0.0787 0.0606  0.0214  393 THR C OG1 
5383  C CG2 . THR B 61  ? 1.9047 1.6236 2.0189 -0.1062 0.0979  -0.0078 393 THR C CG2 
5384  N N   . ASN B 62  ? 1.7600 1.4637 1.8589 -0.1051 0.0774  0.0152  394 ASN C N   
5385  C CA  . ASN B 62  ? 1.6995 1.4055 1.7883 -0.0904 0.0633  0.0218  394 ASN C CA  
5386  C C   . ASN B 62  ? 1.5821 1.3316 1.6650 -0.1040 0.0714  0.0060  394 ASN C C   
5387  O O   . ASN B 62  ? 1.5499 1.3077 1.6453 -0.1145 0.0905  -0.0143 394 ASN C O   
5388  C CB  . ASN B 62  ? 1.6883 1.3733 1.7817 -0.0709 0.0598  0.0201  394 ASN C CB  
5389  C CG  . ASN B 62  ? 1.6644 1.3339 1.7340 -0.0465 0.0323  0.0395  394 ASN C CG  
5390  O OD1 . ASN B 62  ? 1.6925 1.3536 1.7489 -0.0440 0.0198  0.0557  394 ASN C OD1 
5391  N ND2 . ASN B 62  ? 1.5366 1.2053 1.5944 -0.0301 0.0249  0.0359  394 ASN C ND2 
5392  N N   . VAL B 63  ? 1.4314 1.2087 1.4952 -0.1043 0.0570  0.0148  395 VAL C N   
5393  C CA  . VAL B 63  ? 1.3319 1.1499 1.3897 -0.1151 0.0625  0.0012  395 VAL C CA  
5394  C C   . VAL B 63  ? 1.2948 1.1096 1.3513 -0.0996 0.0554  0.0028  395 VAL C C   
5395  O O   . VAL B 63  ? 1.3072 1.0987 1.3569 -0.0794 0.0380  0.0206  395 VAL C O   
5396  C CB  . VAL B 63  ? 1.2757 1.1270 1.3138 -0.1229 0.0512  0.0093  395 VAL C CB  
5397  C CG1 . VAL B 63  ? 1.2439 1.1375 1.2773 -0.1362 0.0590  -0.0065 395 VAL C CG1 
5398  C CG2 . VAL B 63  ? 1.2817 1.1325 1.3219 -0.1361 0.0579  0.0093  395 VAL C CG2 
5399  N N   . TYR B 64  ? 1.1943 1.0330 1.2565 -0.1091 0.0684  -0.0153 396 TYR C N   
5400  C CA  . TYR B 64  ? 1.0571 0.8971 1.1199 -0.0965 0.0642  -0.0159 396 TYR C CA  
5401  C C   . TYR B 64  ? 1.0100 0.8973 1.0609 -0.1065 0.0625  -0.0226 396 TYR C C   
5402  O O   . TYR B 64  ? 0.9853 0.8991 1.0416 -0.1262 0.0786  -0.0416 396 TYR C O   
5403  C CB  . TYR B 64  ? 1.0768 0.8967 1.1607 -0.0978 0.0825  -0.0318 396 TYR C CB  
5404  C CG  . TYR B 64  ? 1.1299 0.9008 1.2241 -0.0808 0.0798  -0.0221 396 TYR C CG  
5405  C CD1 . TYR B 64  ? 1.1304 0.8786 1.2150 -0.0583 0.0591  -0.0008 396 TYR C CD1 
5406  C CD2 . TYR B 64  ? 1.1291 0.8760 1.2416 -0.0872 0.0974  -0.0339 396 TYR C CD2 
5407  C CE1 . TYR B 64  ? 1.2000 0.9024 1.2935 -0.0425 0.0559  0.0084  396 TYR C CE1 
5408  C CE2 . TYR B 64  ? 1.2306 0.9396 1.3492 -0.0697 0.0919  -0.0241 396 TYR C CE2 
5409  C CZ  . TYR B 64  ? 1.2391 0.9324 1.3446 -0.0472 0.0689  -0.0032 396 TYR C CZ  
5410  O OH  . TYR B 64  ? 1.2890 0.9796 1.3786 -0.0285 0.0516  0.0053  396 TYR C OH  
5411  N N   . ALA B 65  ? 1.0628 0.9613 1.0970 -0.0930 0.0431  -0.0073 397 ALA C N   
5412  C CA  . ALA B 65  ? 0.9173 0.8610 0.9402 -0.1008 0.0405  -0.0126 397 ALA C CA  
5413  C C   . ALA B 65  ? 0.9013 0.8462 0.9296 -0.0891 0.0403  -0.0155 397 ALA C C   
5414  O O   . ALA B 65  ? 0.9383 0.8682 0.9590 -0.0675 0.0243  0.0005  397 ALA C O   
5415  C CB  . ALA B 65  ? 0.9374 0.8967 0.9375 -0.0952 0.0202  0.0052  397 ALA C CB  
5416  N N   . ASP B 66  ? 0.7843 0.7446 0.8263 -0.1032 0.0586  -0.0361 398 ASP C N   
5417  C CA  . ASP B 66  ? 0.7741 0.7434 0.8219 -0.0966 0.0609  -0.0415 398 ASP C CA  
5418  C C   . ASP B 66  ? 0.7743 0.7931 0.8098 -0.1052 0.0563  -0.0448 398 ASP C C   
5419  O O   . ASP B 66  ? 0.7328 0.7812 0.7660 -0.1265 0.0651  -0.0574 398 ASP C O   
5420  C CB  . ASP B 66  ? 0.7790 0.7404 0.8478 -0.1090 0.0834  -0.0626 398 ASP C CB  
5421  C CG  . ASP B 66  ? 0.7981 0.7163 0.8804 -0.1067 0.0923  -0.0640 398 ASP C CG  
5422  O OD1 . ASP B 66  ? 0.8810 0.7658 0.9614 -0.0879 0.0806  -0.0476 398 ASP C OD1 
5423  O OD2 . ASP B 66  ? 0.7336 0.6516 0.8278 -0.1243 0.1110  -0.0817 398 ASP C OD2 
5424  N N   . SER B 67  ? 0.8601 0.8885 0.8879 -0.0889 0.0433  -0.0344 399 SER C N   
5425  C CA  . SER B 67  ? 0.7664 0.8427 0.7834 -0.0959 0.0390  -0.0374 399 SER C CA  
5426  C C   . SER B 67  ? 0.7438 0.8293 0.7690 -0.0882 0.0416  -0.0415 399 SER C C   
5427  O O   . SER B 67  ? 0.8002 0.8546 0.8318 -0.0689 0.0380  -0.0334 399 SER C O   
5428  C CB  . SER B 67  ? 0.8284 0.9172 0.8224 -0.0835 0.0169  -0.0177 399 SER C CB  
5429  O OG  . SER B 67  ? 0.8101 0.8659 0.7983 -0.0568 0.0012  0.0018  399 SER C OG  
5430  N N   . PHE B 68  ? 0.6558 0.7849 0.6806 -0.1036 0.0476  -0.0538 400 PHE C N   
5431  C CA  . PHE B 68  ? 0.6301 0.7764 0.6620 -0.0990 0.0500  -0.0580 400 PHE C CA  
5432  C C   . PHE B 68  ? 0.5948 0.7948 0.6198 -0.1170 0.0518  -0.0677 400 PHE C C   
5433  O O   . PHE B 68  ? 0.6186 0.8400 0.6310 -0.1285 0.0480  -0.0678 400 PHE C O   
5434  C CB  . PHE B 68  ? 0.6012 0.7216 0.6554 -0.1032 0.0680  -0.0720 400 PHE C CB  
5435  C CG  . PHE B 68  ? 0.6258 0.7483 0.6905 -0.1292 0.0875  -0.0928 400 PHE C CG  
5436  C CD1 . PHE B 68  ? 0.6407 0.7333 0.7072 -0.1328 0.0918  -0.0930 400 PHE C CD1 
5437  C CD2 . PHE B 68  ? 0.6176 0.7748 0.6877 -0.1508 0.1001  -0.1112 400 PHE C CD2 
5438  C CE1 . PHE B 68  ? 0.6208 0.7161 0.6954 -0.1560 0.1096  -0.1118 400 PHE C CE1 
5439  C CE2 . PHE B 68  ? 0.6137 0.7711 0.6918 -0.1746 0.1180  -0.1307 400 PHE C CE2 
5440  C CZ  . PHE B 68  ? 0.5820 0.7094 0.6617 -0.1768 0.1226  -0.1308 400 PHE C CZ  
5441  N N   . VAL B 69  ? 0.5827 0.8050 0.6161 -0.1202 0.0577  -0.0759 401 VAL C N   
5442  C CA  . VAL B 69  ? 0.5755 0.8505 0.6023 -0.1363 0.0580  -0.0840 401 VAL C CA  
5443  C C   . VAL B 69  ? 0.5760 0.8661 0.6201 -0.1518 0.0748  -0.1029 401 VAL C C   
5444  O O   . VAL B 69  ? 0.5800 0.8505 0.6373 -0.1412 0.0792  -0.1028 401 VAL C O   
5445  C CB  . VAL B 69  ? 0.5097 0.8088 0.5204 -0.1181 0.0385  -0.0663 401 VAL C CB  
5446  C CG1 . VAL B 69  ? 0.5484 0.8373 0.5697 -0.1033 0.0391  -0.0631 401 VAL C CG1 
5447  C CG2 . VAL B 69  ? 0.5082 0.8599 0.5111 -0.1344 0.0379  -0.0736 401 VAL C CG2 
5448  N N   . ILE B 70  ? 0.5311 0.8552 0.5749 -0.1773 0.0842  -0.1192 402 ILE C N   
5449  C CA  . ILE B 70  ? 0.5262 0.8622 0.5859 -0.1957 0.1014  -0.1390 402 ILE C CA  
5450  C C   . ILE B 70  ? 0.5763 0.9667 0.6265 -0.2130 0.0992  -0.1458 402 ILE C C   
5451  O O   . ILE B 70  ? 0.6279 1.0409 0.6617 -0.2040 0.0833  -0.1322 402 ILE C O   
5452  C CB  . ILE B 70  ? 0.5120 0.8182 0.5840 -0.2114 0.1199  -0.1558 402 ILE C CB  
5453  C CG1 . ILE B 70  ? 0.5230 0.8372 0.5842 -0.2273 0.1217  -0.1612 402 ILE C CG1 
5454  C CG2 . ILE B 70  ? 0.5254 0.7798 0.6052 -0.1922 0.1196  -0.1466 402 ILE C CG2 
5455  C CD1 . ILE B 70  ? 0.5167 0.7951 0.5880 -0.2372 0.1374  -0.1733 402 ILE C CD1 
5456  N N   . ARG B 71  ? 0.7023 0.7302 0.6100 -0.0144 -0.0061 0.0160  403 ARG C N   
5457  C CA  . ARG B 71  ? 0.6809 0.6993 0.5860 -0.0244 -0.0013 0.0221  403 ARG C CA  
5458  C C   . ARG B 71  ? 0.7202 0.7238 0.6280 -0.0295 -0.0006 0.0190  403 ARG C C   
5459  O O   . ARG B 71  ? 0.7882 0.7894 0.7020 -0.0249 -0.0031 0.0109  403 ARG C O   
5460  C CB  . ARG B 71  ? 0.6368 0.6558 0.5304 -0.0269 -0.0023 0.0370  403 ARG C CB  
5461  C CG  . ARG B 71  ? 0.6972 0.7111 0.5837 -0.0233 -0.0079 0.0431  403 ARG C CG  
5462  C CD  . ARG B 71  ? 0.7783 0.7926 0.6523 -0.0240 -0.0105 0.0570  403 ARG C CD  
5463  N NE  . ARG B 71  ? 0.9040 0.9038 0.7731 -0.0277 -0.0119 0.0630  403 ARG C NE  
5464  C CZ  . ARG B 71  ? 0.9749 0.9706 0.8331 -0.0274 -0.0154 0.0741  403 ARG C CZ  
5465  N NH1 . ARG B 71  ? 0.9146 0.9200 0.7650 -0.0232 -0.0186 0.0800  403 ARG C NH1 
5466  N NH2 . ARG B 71  ? 0.9386 0.9200 0.7939 -0.0315 -0.0156 0.0784  403 ARG C NH2 
5467  N N   . GLY B 72  ? 0.7435 0.7378 0.6476 -0.0394 0.0031  0.0249  404 GLY C N   
5468  C CA  . GLY B 72  ? 0.8458 0.8265 0.7528 -0.0454 0.0047  0.0208  404 GLY C CA  
5469  C C   . GLY B 72  ? 0.8561 0.8296 0.7632 -0.0408 0.0004  0.0208  404 GLY C C   
5470  O O   . GLY B 72  ? 0.8088 0.7789 0.7255 -0.0383 0.0002  0.0095  404 GLY C O   
5471  N N   . ASN B 73  ? 0.9268 0.8978 0.8241 -0.0397 -0.0029 0.0332  405 ASN C N   
5472  C CA  . ASN B 73  ? 0.9614 0.9240 0.8587 -0.0359 -0.0069 0.0350  405 ASN C CA  
5473  C C   . ASN B 73  ? 0.9750 0.9443 0.8815 -0.0246 -0.0120 0.0257  405 ASN C C   
5474  O O   . ASN B 73  ? 1.0166 0.9784 0.9296 -0.0217 -0.0144 0.0219  405 ASN C O   
5475  C CB  . ASN B 73  ? 1.0440 1.0054 0.9282 -0.0349 -0.0104 0.0501  405 ASN C CB  
5476  C CG  . ASN B 73  ? 1.0636 1.0234 0.9378 -0.0444 -0.0063 0.0604  405 ASN C CG  
5477  O OD1 . ASN B 73  ? 0.9987 0.9684 0.8718 -0.0452 -0.0045 0.0613  405 ASN C OD1 
5478  N ND2 . ASN B 73  ? 1.2151 1.1627 1.0826 -0.0517 -0.0046 0.0682  405 ASN C ND2 
5479  N N   . GLU B 74  ? 0.8375 0.8214 0.7447 -0.0182 -0.0140 0.0228  406 GLU C N   
5480  C CA  . GLU B 74  ? 0.8046 0.7975 0.7203 -0.0081 -0.0186 0.0134  406 GLU C CA  
5481  C C   . GLU B 74  ? 0.7891 0.7796 0.7189 -0.0083 -0.0158 -0.0023 406 GLU C C   
5482  O O   . GLU B 74  ? 0.8101 0.8009 0.7485 -0.0015 -0.0201 -0.0087 406 GLU C O   
5483  C CB  . GLU B 74  ? 0.8269 0.8362 0.7391 -0.0037 -0.0195 0.0135  406 GLU C CB  
5484  C CG  . GLU B 74  ? 0.7653 0.7831 0.6669 0.0018  -0.0254 0.0242  406 GLU C CG  
5485  C CD  . GLU B 74  ? 0.8305 0.8413 0.7195 -0.0026 -0.0260 0.0390  406 GLU C CD  
5486  O OE1 . GLU B 74  ? 1.2056 1.2109 1.0918 -0.0106 -0.0205 0.0426  406 GLU C OE1 
5487  O OE2 . GLU B 74  ? 0.9103 0.9244 0.7914 0.0019  -0.0318 0.0469  406 GLU C OE2 
5488  N N   . VAL B 75  ? 0.7733 0.7619 0.7065 -0.0159 -0.0090 -0.0090 407 VAL C N   
5489  C CA  . VAL B 75  ? 0.7451 0.7339 0.6912 -0.0156 -0.0064 -0.0253 407 VAL C CA  
5490  C C   . VAL B 75  ? 0.7767 0.7544 0.7309 -0.0152 -0.0078 -0.0301 407 VAL C C   
5491  O O   . VAL B 75  ? 0.7673 0.7482 0.7332 -0.0094 -0.0096 -0.0419 407 VAL C O   
5492  C CB  . VAL B 75  ? 0.7356 0.7214 0.6827 -0.0257 0.0012  -0.0303 407 VAL C CB  
5493  C CG1 . VAL B 75  ? 0.7914 0.7713 0.7501 -0.0288 0.0047  -0.0457 407 VAL C CG1 
5494  C CG2 . VAL B 75  ? 0.6891 0.6874 0.6343 -0.0240 0.0029  -0.0308 407 VAL C CG2 
5495  N N   . SER B 76  ? 0.7835 0.7484 0.7320 -0.0212 -0.0069 -0.0209 408 SER C N   
5496  C CA  . SER B 76  ? 0.7501 0.7030 0.7052 -0.0211 -0.0081 -0.0224 408 SER C CA  
5497  C C   . SER B 76  ? 0.7366 0.6947 0.7002 -0.0086 -0.0158 -0.0252 408 SER C C   
5498  O O   . SER B 76  ? 0.7193 0.6690 0.6933 -0.0072 -0.0165 -0.0303 408 SER C O   
5499  C CB  . SER B 76  ? 0.8566 0.7984 0.8004 -0.0271 -0.0075 -0.0077 408 SER C CB  
5500  O OG  . SER B 76  ? 0.8899 0.8279 0.8245 -0.0389 -0.0014 -0.0025 408 SER C OG  
5501  N N   . GLN B 77  ? 0.7594 0.7312 0.7190 0.0001  -0.0215 -0.0217 409 GLN C N   
5502  C CA  . GLN B 77  ? 0.7280 0.7065 0.6941 0.0116  -0.0297 -0.0229 409 GLN C CA  
5503  C C   . GLN B 77  ? 0.7327 0.7248 0.7090 0.0178  -0.0309 -0.0367 409 GLN C C   
5504  O O   . GLN B 77  ? 0.7516 0.7514 0.7337 0.0272  -0.0381 -0.0381 409 GLN C O   
5505  C CB  . GLN B 77  ? 0.7504 0.7359 0.7037 0.0168  -0.0363 -0.0087 409 GLN C CB  
5506  C CG  . GLN B 77  ? 0.8386 0.8131 0.7818 0.0141  -0.0380 0.0060  409 GLN C CG  
5507  C CD  . GLN B 77  ? 0.8608 0.8434 0.7878 0.0142  -0.0402 0.0184  409 GLN C CD  
5508  O OE1 . GLN B 77  ? 0.8762 0.8709 0.8009 0.0218  -0.0465 0.0201  409 GLN C OE1 
5509  N NE2 . GLN B 77  ? 0.9290 0.9059 0.8450 0.0058  -0.0352 0.0267  409 GLN C NE2 
5510  N N   . ILE B 78  ? 0.7050 0.7015 0.6824 0.0128  -0.0244 -0.0458 410 ILE C N   
5511  C CA  . ILE B 78  ? 0.6448 0.6545 0.6315 0.0185  -0.0251 -0.0592 410 ILE C CA  
5512  C C   . ILE B 78  ? 0.6876 0.6893 0.6896 0.0170  -0.0225 -0.0730 410 ILE C C   
5513  O O   . ILE B 78  ? 0.7566 0.7555 0.7629 0.0102  -0.0153 -0.0837 410 ILE C O   
5514  C CB  . ILE B 78  ? 0.6502 0.6683 0.6315 0.0143  -0.0193 -0.0627 410 ILE C CB  
5515  C CG1 . ILE B 78  ? 0.6831 0.7083 0.6503 0.0152  -0.0213 -0.0490 410 ILE C CG1 
5516  C CG2 . ILE B 78  ? 0.6606 0.6925 0.6506 0.0203  -0.0198 -0.0763 410 ILE C CG2 
5517  C CD1 . ILE B 78  ? 0.6588 0.6942 0.6227 0.0245  -0.0298 -0.0429 410 ILE C CD1 
5518  N N   . ALA B 79  ? 0.6895 0.6868 0.7000 0.0228  -0.0281 -0.0722 411 ALA C N   
5519  C CA  . ALA B 79  ? 0.7250 0.7115 0.7501 0.0204  -0.0253 -0.0827 411 ALA C CA  
5520  C C   . ALA B 79  ? 0.7741 0.7611 0.8102 0.0306  -0.0338 -0.0812 411 ALA C C   
5521  O O   . ALA B 79  ? 0.8080 0.7970 0.8365 0.0362  -0.0410 -0.0675 411 ALA C O   
5522  C CB  . ALA B 79  ? 0.7884 0.7578 0.8084 0.0091  -0.0188 -0.0774 411 ALA C CB  
5523  N N   . PRO B 80  ? 0.8452 0.8302 0.8995 0.0329  -0.0334 -0.0948 412 PRO C N   
5524  C CA  . PRO B 80  ? 0.8511 0.8385 0.9180 0.0437  -0.0423 -0.0937 412 PRO C CA  
5525  C C   . PRO B 80  ? 0.9013 0.8739 0.9670 0.0432  -0.0447 -0.0809 412 PRO C C   
5526  O O   . PRO B 80  ? 0.8552 0.8130 0.9217 0.0342  -0.0375 -0.0818 412 PRO C O   
5527  C CB  . PRO B 80  ? 0.8509 0.8389 0.9385 0.0444  -0.0392 -0.1130 412 PRO C CB  
5528  C CG  . PRO B 80  ? 0.8726 0.8497 0.9579 0.0315  -0.0280 -0.1207 412 PRO C CG  
5529  C CD  . PRO B 80  ? 0.8750 0.8536 0.9396 0.0249  -0.0245 -0.1109 412 PRO C CD  
5530  N N   . GLY B 81  ? 1.0904 1.0674 1.1532 0.0522  -0.0547 -0.0686 413 GLY C N   
5531  C CA  . GLY B 81  ? 1.0972 1.0608 1.1606 0.0536  -0.0582 -0.0565 413 GLY C CA  
5532  C C   . GLY B 81  ? 1.1095 1.0645 1.1525 0.0466  -0.0557 -0.0410 413 GLY C C   
5533  O O   . GLY B 81  ? 1.1465 1.0899 1.1883 0.0472  -0.0583 -0.0301 413 GLY C O   
5534  N N   . GLN B 82  ? 0.9934 0.9538 1.0211 0.0400  -0.0506 -0.0398 414 GLN C N   
5535  C CA  . GLN B 82  ? 0.9335 0.8888 0.9414 0.0341  -0.0490 -0.0246 414 GLN C CA  
5536  C C   . GLN B 82  ? 0.9464 0.9116 0.9429 0.0419  -0.0585 -0.0113 414 GLN C C   
5537  O O   . GLN B 82  ? 0.9599 0.9409 0.9562 0.0478  -0.0629 -0.0148 414 GLN C O   
5538  C CB  . GLN B 82  ? 0.8784 0.8370 0.8764 0.0247  -0.0405 -0.0284 414 GLN C CB  
5539  C CG  . GLN B 82  ? 0.8797 0.8258 0.8843 0.0147  -0.0313 -0.0373 414 GLN C CG  
5540  C CD  . GLN B 82  ? 1.0165 0.9463 1.0161 0.0089  -0.0294 -0.0268 414 GLN C CD  
5541  O OE1 . GLN B 82  ? 1.0570 0.9854 1.0417 0.0086  -0.0320 -0.0117 414 GLN C OE1 
5542  N NE2 . GLN B 82  ? 1.0719 0.9892 1.0846 0.0047  -0.0248 -0.0348 414 GLN C NE2 
5543  N N   . THR B 83  ? 1.0169 0.9728 1.0036 0.0413  -0.0616 0.0036  415 THR C N   
5544  C CA  . THR B 83  ? 0.9994 0.9640 0.9701 0.0452  -0.0686 0.0174  415 THR C CA  
5545  C C   . THR B 83  ? 0.9724 0.9296 0.9252 0.0359  -0.0629 0.0281  415 THR C C   
5546  O O   . THR B 83  ? 0.9240 0.8670 0.8729 0.0327  -0.0624 0.0373  415 THR C O   
5547  C CB  . THR B 83  ? 1.0127 0.9750 0.9852 0.0537  -0.0793 0.0277  415 THR C CB  
5548  O OG1 . THR B 83  ? 0.9566 0.9018 0.9226 0.0493  -0.0778 0.0394  415 THR C OG1 
5549  C CG2 . THR B 83  ? 1.0672 1.0330 1.0621 0.0631  -0.0853 0.0176  415 THR C CG2 
5550  N N   . GLY B 84  ? 0.9347 0.9015 0.8779 0.0315  -0.0585 0.0266  416 GLY C N   
5551  C CA  . GLY B 84  ? 0.9747 0.9406 0.8995 0.0256  -0.0564 0.0391  416 GLY C CA  
5552  C C   . GLY B 84  ? 0.9684 0.9473 0.8817 0.0313  -0.0638 0.0479  416 GLY C C   
5553  O O   . GLY B 84  ? 0.9281 0.9071 0.8414 0.0380  -0.0724 0.0542  416 GLY C O   
5554  N N   . ASN B 85  ? 0.9056 0.8954 0.8093 0.0280  -0.0604 0.0483  417 ASN C N   
5555  C CA  . ASN B 85  ? 0.8431 0.8461 0.7343 0.0308  -0.0651 0.0557  417 ASN C CA  
5556  C C   . ASN B 85  ? 0.8392 0.8596 0.7360 0.0344  -0.0648 0.0444  417 ASN C C   
5557  O O   . ASN B 85  ? 0.7559 0.7895 0.6475 0.0390  -0.0704 0.0465  417 ASN C O   
5558  C CB  . ASN B 85  ? 0.8941 0.8954 0.7701 0.0227  -0.0597 0.0651  417 ASN C CB  
5559  C CG  . ASN B 85  ? 0.8940 0.9029 0.7546 0.0242  -0.0651 0.0768  417 ASN C CG  
5560  O OD1 . ASN B 85  ? 0.8227 0.8375 0.6824 0.0308  -0.0734 0.0791  417 ASN C OD1 
5561  N ND2 . ASN B 85  ? 0.9857 0.9950 0.8340 0.0176  -0.0605 0.0842  417 ASN C ND2 
5562  N N   . ILE B 86  ? 0.8956 0.9160 0.8023 0.0315  -0.0578 0.0324  418 ILE C N   
5563  C CA  . ILE B 86  ? 0.8194 0.8551 0.7323 0.0342  -0.0562 0.0207  418 ILE C CA  
5564  C C   . ILE B 86  ? 0.9107 0.9496 0.8384 0.0415  -0.0609 0.0100  418 ILE C C   
5565  O O   . ILE B 86  ? 0.9108 0.9645 0.8410 0.0470  -0.0648 0.0045  418 ILE C O   
5566  C CB  . ILE B 86  ? 0.7628 0.7964 0.6776 0.0267  -0.0461 0.0144  418 ILE C CB  
5567  C CG1 . ILE B 86  ? 0.7984 0.8487 0.7129 0.0280  -0.0438 0.0078  418 ILE C CG1 
5568  C CG2 . ILE B 86  ? 0.7985 0.8239 0.7275 0.0249  -0.0420 0.0021  418 ILE C CG2 
5569  C CD1 . ILE B 86  ? 0.7665 0.8163 0.6800 0.0214  -0.0356 0.0059  418 ILE C CD1 
5570  N N   . ALA B 87  ? 1.0587 1.0842 0.9965 0.0417  -0.0611 0.0074  419 ALA C N   
5571  C CA  . ALA B 87  ? 0.9932 1.0209 0.9468 0.0490  -0.0662 -0.0019 419 ALA C CA  
5572  C C   . ALA B 87  ? 1.0748 1.1002 1.0271 0.0557  -0.0766 0.0088  419 ALA C C   
5573  O O   . ALA B 87  ? 1.1738 1.1889 1.1375 0.0586  -0.0794 0.0079  419 ALA C O   
5574  C CB  . ALA B 87  ? 1.0543 1.0692 1.0216 0.0453  -0.0602 -0.0122 419 ALA C CB  
5575  N N   . ASP B 88  ? 0.9271 0.9614 0.8650 0.0573  -0.0820 0.0197  420 ASP C N   
5576  C CA  . ASP B 88  ? 0.9379 0.9767 0.8742 0.0646  -0.0934 0.0280  420 ASP C CA  
5577  C C   . ASP B 88  ? 0.8400 0.8892 0.7572 0.0630  -0.0964 0.0388  420 ASP C C   
5578  O O   . ASP B 88  ? 0.8073 0.8522 0.7140 0.0638  -0.1029 0.0526  420 ASP C O   
5579  C CB  . ASP B 88  ? 0.9868 1.0082 0.9270 0.0663  -0.0977 0.0371  420 ASP C CB  
5580  C CG  . ASP B 88  ? 0.9090 0.9146 0.8379 0.0581  -0.0914 0.0467  420 ASP C CG  
5581  O OD1 . ASP B 88  ? 0.9625 0.9710 0.8811 0.0514  -0.0842 0.0466  420 ASP C OD1 
5582  O OD2 . ASP B 88  ? 0.7839 0.7743 0.7152 0.0584  -0.0935 0.0539  420 ASP C OD2 
5583  N N   . TYR B 89  ? 0.7686 0.8304 0.6811 0.0598  -0.0906 0.0324  421 TYR C N   
5584  C CA  . TYR B 89  ? 0.7797 0.8560 0.6776 0.0590  -0.0930 0.0381  421 TYR C CA  
5585  C C   . TYR B 89  ? 0.7785 0.8683 0.6803 0.0569  -0.0854 0.0248  421 TYR C C   
5586  O O   . TYR B 89  ? 0.7722 0.8773 0.6660 0.0563  -0.0856 0.0244  421 TYR C O   
5587  C CB  . TYR B 89  ? 0.8200 0.8898 0.7002 0.0527  -0.0909 0.0521  421 TYR C CB  
5588  C CG  . TYR B 89  ? 0.8265 0.8844 0.6985 0.0537  -0.0984 0.0672  421 TYR C CG  
5589  C CD1 . TYR B 89  ? 0.8426 0.9058 0.7126 0.0594  -0.1094 0.0731  421 TYR C CD1 
5590  C CD2 . TYR B 89  ? 0.8649 0.9076 0.7286 0.0481  -0.0944 0.0766  421 TYR C CD2 
5591  C CE1 . TYR B 89  ? 0.9063 0.9579 0.7683 0.0601  -0.1162 0.0876  421 TYR C CE1 
5592  C CE2 . TYR B 89  ? 0.8103 0.8418 0.6656 0.0485  -0.1005 0.0904  421 TYR C CE2 
5593  C CZ  . TYR B 89  ? 0.7792 0.8147 0.6337 0.0546  -0.1113 0.0959  421 TYR C CZ  
5594  O OH  . TYR B 89  ? 0.8399 0.8636 0.6858 0.0548  -0.1175 0.1103  421 TYR C OH  
5595  N N   . ASN B 90  ? 0.7869 0.8707 0.7007 0.0552  -0.0780 0.0137  422 ASN C N   
5596  C CA  . ASN B 90  ? 0.7468 0.8399 0.6630 0.0519  -0.0693 0.0028  422 ASN C CA  
5597  C C   . ASN B 90  ? 0.7173 0.8146 0.6501 0.0550  -0.0672 -0.0139 422 ASN C C   
5598  O O   . ASN B 90  ? 0.7372 0.8504 0.6726 0.0578  -0.0675 -0.0224 422 ASN C O   
5599  C CB  . ASN B 90  ? 0.7205 0.8030 0.6311 0.0440  -0.0607 0.0072  422 ASN C CB  
5600  C CG  . ASN B 90  ? 0.7052 0.7928 0.6001 0.0402  -0.0598 0.0182  422 ASN C CG  
5601  O OD1 . ASN B 90  ? 0.7387 0.8393 0.6270 0.0426  -0.0640 0.0203  422 ASN C OD1 
5602  N ND2 . ASN B 90  ? 0.8103 0.8884 0.6994 0.0338  -0.0542 0.0247  422 ASN C ND2 
5603  N N   . TYR B 91  ? 0.7156 0.7994 0.6596 0.0543  -0.0646 -0.0194 423 TYR C N   
5604  C CA  . TYR B 91  ? 0.7279 0.8154 0.6876 0.0564  -0.0616 -0.0363 423 TYR C CA  
5605  C C   . TYR B 91  ? 0.7574 0.8302 0.7292 0.0577  -0.0634 -0.0387 423 TYR C C   
5606  O O   . TYR B 91  ? 0.8047 0.8636 0.7788 0.0516  -0.0568 -0.0401 423 TYR C O   
5607  C CB  . TYR B 91  ? 0.6595 0.7471 0.6199 0.0499  -0.0509 -0.0447 423 TYR C CB  
5608  C CG  . TYR B 91  ? 0.6282 0.7189 0.6030 0.0505  -0.0465 -0.0624 423 TYR C CG  
5609  C CD1 . TYR B 91  ? 0.6655 0.7727 0.6452 0.0550  -0.0475 -0.0731 423 TYR C CD1 
5610  C CD2 . TYR B 91  ? 0.6282 0.7049 0.6121 0.0467  -0.0420 -0.0688 423 TYR C CD2 
5611  C CE1 . TYR B 91  ? 0.6572 0.7667 0.6499 0.0553  -0.0432 -0.0897 423 TYR C CE1 
5612  C CE2 . TYR B 91  ? 0.5989 0.6777 0.5956 0.0467  -0.0380 -0.0853 423 TYR C CE2 
5613  C CZ  . TYR B 91  ? 0.6149 0.7098 0.6160 0.0512  -0.0387 -0.0956 423 TYR C CZ  
5614  O OH  . TYR B 91  ? 0.6605 0.7568 0.6740 0.0507  -0.0343 -0.1121 423 TYR C OH  
5615  N N   . LYS B 92  ? 0.7528 0.8288 0.7331 0.0653  -0.0720 -0.0396 424 LYS C N   
5616  C CA  . LYS B 92  ? 0.7840 0.8462 0.7772 0.0671  -0.0739 -0.0414 424 LYS C CA  
5617  C C   . LYS B 92  ? 0.7413 0.8082 0.7525 0.0696  -0.0716 -0.0596 424 LYS C C   
5618  O O   . LYS B 92  ? 0.7320 0.8147 0.7477 0.0750  -0.0756 -0.0667 424 LYS C O   
5619  C CB  . LYS B 92  ? 0.8010 0.8616 0.7942 0.0739  -0.0853 -0.0296 424 LYS C CB  
5620  C CG  . LYS B 92  ? 0.7107 0.7628 0.7227 0.0791  -0.0894 -0.0344 424 LYS C CG  
5621  C CD  . LYS B 92  ? 0.7540 0.7850 0.7688 0.0736  -0.0840 -0.0312 424 LYS C CD  
5622  C CE  . LYS B 92  ? 0.8050 0.8261 0.8163 0.0770  -0.0919 -0.0154 424 LYS C CE  
5623  N NZ  . LYS B 92  ? 0.8359 0.8366 0.8553 0.0731  -0.0872 -0.0148 424 LYS C NZ  
5624  N N   . LEU B 93  ? 0.8055 0.8592 0.8258 0.0647  -0.0647 -0.0674 425 LEU C N   
5625  C CA  . LEU B 93  ? 0.7497 0.8041 0.7881 0.0661  -0.0621 -0.0846 425 LEU C CA  
5626  C C   . LEU B 93  ? 0.8253 0.8753 0.8788 0.0733  -0.0699 -0.0844 425 LEU C C   
5627  O O   . LEU B 93  ? 0.8842 0.9249 0.9341 0.0750  -0.0750 -0.0709 425 LEU C O   
5628  C CB  . LEU B 93  ? 0.7317 0.7727 0.7723 0.0564  -0.0514 -0.0920 425 LEU C CB  
5629  C CG  . LEU B 93  ? 0.7308 0.7760 0.7619 0.0493  -0.0431 -0.0960 425 LEU C CG  
5630  C CD1 . LEU B 93  ? 0.7873 0.8216 0.8263 0.0412  -0.0340 -0.1080 425 LEU C CD1 
5631  C CD2 . LEU B 93  ? 0.6903 0.7548 0.7224 0.0548  -0.0452 -0.1037 425 LEU C CD2 
5632  N N   . PRO B 94  ? 0.8072 0.8632 0.8783 0.0776  -0.0708 -0.0991 426 PRO C N   
5633  C CA  . PRO B 94  ? 0.8490 0.9024 0.9368 0.0855  -0.0788 -0.0992 426 PRO C CA  
5634  C C   . PRO B 94  ? 0.8786 0.9134 0.9784 0.0805  -0.0725 -0.1045 426 PRO C C   
5635  O O   . PRO B 94  ? 0.8686 0.8961 0.9673 0.0715  -0.0620 -0.1134 426 PRO C O   
5636  C CB  . PRO B 94  ? 0.8856 0.9557 0.9873 0.0914  -0.0813 -0.1145 426 PRO C CB  
5637  C CG  . PRO B 94  ? 0.8900 0.9633 0.9868 0.0839  -0.0706 -0.1268 426 PRO C CG  
5638  C CD  . PRO B 94  ? 0.8173 0.8874 0.8924 0.0776  -0.0668 -0.1145 426 PRO C CD  
5639  N N   . ASP B 95  ? 0.9137 0.9408 1.0258 0.0861  -0.0788 -0.0994 427 ASP C N   
5640  C CA  . ASP B 95  ? 0.9020 0.9114 1.0271 0.0811  -0.0723 -0.1055 427 ASP C CA  
5641  C C   . ASP B 95  ? 0.9430 0.9556 1.0851 0.0789  -0.0656 -0.1271 427 ASP C C   
5642  O O   . ASP B 95  ? 0.9218 0.9222 1.0667 0.0695  -0.0555 -0.1356 427 ASP C O   
5643  C CB  . ASP B 95  ? 0.8251 0.8264 0.9627 0.0884  -0.0804 -0.0967 427 ASP C CB  
5644  C CG  . ASP B 95  ? 0.9119 0.9110 1.0320 0.0907  -0.0875 -0.0756 427 ASP C CG  
5645  O OD1 . ASP B 95  ? 0.9729 0.9638 1.0748 0.0824  -0.0817 -0.0674 427 ASP C OD1 
5646  O OD2 . ASP B 95  ? 0.9443 0.9498 1.0685 0.1003  -0.0991 -0.0669 427 ASP C OD2 
5647  N N   . ASP B 96  ? 1.0906 1.1200 1.2425 0.0865  -0.0708 -0.1365 428 ASP C N   
5648  C CA  . ASP B 96  ? 1.0992 1.1333 1.2680 0.0854  -0.0654 -0.1576 428 ASP C CA  
5649  C C   . ASP B 96  ? 1.1110 1.1528 1.2679 0.0783  -0.0572 -0.1672 428 ASP C C   
5650  O O   . ASP B 96  ? 1.1274 1.1799 1.2945 0.0799  -0.0554 -0.1833 428 ASP C O   
5651  C CB  . ASP B 96  ? 1.1075 1.1561 1.2947 0.0972  -0.0752 -0.1635 428 ASP C CB  
5652  C CG  . ASP B 96  ? 1.2854 1.3529 1.4601 0.1042  -0.0845 -0.1545 428 ASP C CG  
5653  O OD1 . ASP B 96  ? 1.2956 1.3631 1.4648 0.1098  -0.0941 -0.1376 428 ASP C OD1 
5654  O OD2 . ASP B 96  ? 1.2566 1.3387 1.4267 0.1033  -0.0819 -0.1644 428 ASP C OD2 
5655  N N   . PHE B 97  ? 0.9248 0.9611 1.0611 0.0706  -0.0521 -0.1579 429 PHE C N   
5656  C CA  . PHE B 97  ? 0.8915 0.9340 1.0159 0.0638  -0.0445 -0.1648 429 PHE C CA  
5657  C C   . PHE B 97  ? 0.9038 0.9425 1.0386 0.0566  -0.0348 -0.1843 429 PHE C C   
5658  O O   . PHE B 97  ? 0.9271 0.9522 1.0724 0.0514  -0.0300 -0.1904 429 PHE C O   
5659  C CB  . PHE B 97  ? 0.8951 0.9290 0.9988 0.0562  -0.0406 -0.1503 429 PHE C CB  
5660  C CG  . PHE B 97  ? 0.8860 0.9288 0.9756 0.0519  -0.0357 -0.1517 429 PHE C CG  
5661  C CD1 . PHE B 97  ? 0.8999 0.9580 0.9801 0.0579  -0.0412 -0.1452 429 PHE C CD1 
5662  C CD2 . PHE B 97  ? 0.9042 0.9407 0.9916 0.0417  -0.0254 -0.1611 429 PHE C CD2 
5663  C CE1 . PHE B 97  ? 0.9107 0.9768 0.9797 0.0538  -0.0358 -0.1473 429 PHE C CE1 
5664  C CE2 . PHE B 97  ? 0.9049 0.9487 0.9808 0.0379  -0.0208 -0.1618 429 PHE C CE2 
5665  C CZ  . PHE B 97  ? 0.8668 0.9251 0.9343 0.0440  -0.0255 -0.1556 429 PHE C CZ  
5666  N N   . THR B 98  ? 0.9292 0.9801 1.0605 0.0556  -0.0314 -0.1943 430 THR C N   
5667  C CA  . THR B 98  ? 0.9854 1.0343 1.1236 0.0482  -0.0220 -0.2129 430 THR C CA  
5668  C C   . THR B 98  ? 1.0220 1.0782 1.1456 0.0433  -0.0165 -0.2145 430 THR C C   
5669  O O   . THR B 98  ? 1.0336 1.1033 1.1605 0.0463  -0.0159 -0.2258 430 THR C O   
5670  C CB  . THR B 98  ? 0.9484 1.0072 1.1070 0.0546  -0.0244 -0.2299 430 THR C CB  
5671  O OG1 . THR B 98  ? 1.1018 1.1799 1.2577 0.0635  -0.0311 -0.2288 430 THR C OG1 
5672  C CG2 . THR B 98  ? 0.9269 0.9792 1.1037 0.0603  -0.0299 -0.2295 430 THR C CG2 
5673  N N   . GLY B 99  ? 1.1117 1.1588 1.2193 0.0355  -0.0122 -0.2034 431 GLY C N   
5674  C CA  . GLY B 99  ? 1.0745 1.1254 1.1704 0.0293  -0.0055 -0.2057 431 GLY C CA  
5675  C C   . GLY B 99  ? 1.0263 1.0629 1.1094 0.0183  0.0004  -0.1957 431 GLY C C   
5676  O O   . GLY B 99  ? 1.0750 1.0987 1.1574 0.0149  -0.0001 -0.1876 431 GLY C O   
5677  N N   . CYS B 100 ? 0.9774 1.0167 1.0503 0.0130  0.0058  -0.1955 432 CYS C N   
5678  C CA  . CYS B 100 ? 0.9867 1.0138 1.0474 0.0025  0.0109  -0.1854 432 CYS C CA  
5679  C C   . CYS B 100 ? 0.9530 0.9832 0.9999 0.0052  0.0070  -0.1666 432 CYS C C   
5680  O O   . CYS B 100 ? 0.9629 1.0068 1.0068 0.0129  0.0031  -0.1637 432 CYS C O   
5681  C CB  . CYS B 100 ? 1.0769 1.1036 1.1352 -0.0060 0.0192  -0.1953 432 CYS C CB  
5682  S SG  . CYS B 100 ? 1.4287 1.4361 1.4855 -0.0221 0.0274  -0.1984 432 CYS C SG  
5683  N N   . VAL B 101 ? 0.9617 0.9793 0.9998 -0.0022 0.0087  -0.1542 433 VAL C N   
5684  C CA  . VAL B 101 ? 0.9453 0.9646 0.9696 -0.0020 0.0066  -0.1368 433 VAL C CA  
5685  C C   . VAL B 101 ? 0.9207 0.9327 0.9367 -0.0135 0.0138  -0.1336 433 VAL C C   
5686  O O   . VAL B 101 ? 1.0057 1.0045 1.0219 -0.0233 0.0180  -0.1346 433 VAL C O   
5687  C CB  . VAL B 101 ? 0.8960 0.9073 0.9164 -0.0001 0.0013  -0.1229 433 VAL C CB  
5688  C CG1 . VAL B 101 ? 0.8486 0.8598 0.8541 -0.0025 0.0008  -0.1060 433 VAL C CG1 
5689  C CG2 . VAL B 101 ? 0.8835 0.9020 0.9113 0.0116  -0.0071 -0.1233 433 VAL C CG2 
5690  N N   . ILE B 102 ? 0.8447 0.8653 0.8539 -0.0128 0.0152  -0.1290 434 ILE C N   
5691  C CA  . ILE B 102 ? 0.8660 0.8819 0.8694 -0.0227 0.0216  -0.1267 434 ILE C CA  
5692  C C   . ILE B 102 ? 0.8810 0.9000 0.8735 -0.0222 0.0199  -0.1097 434 ILE C C   
5693  O O   . ILE B 102 ? 0.8444 0.8754 0.8351 -0.0137 0.0163  -0.1062 434 ILE C O   
5694  C CB  . ILE B 102 ? 0.8264 0.8505 0.8351 -0.0225 0.0263  -0.1403 434 ILE C CB  
5695  C CG1 . ILE B 102 ? 0.8623 0.8843 0.8821 -0.0227 0.0278  -0.1578 434 ILE C CG1 
5696  C CG2 . ILE B 102 ? 0.9404 0.9587 0.9439 -0.0327 0.0324  -0.1370 434 ILE C CG2 
5697  C CD1 . ILE B 102 ? 0.8985 0.9243 0.9226 -0.0257 0.0336  -0.1716 434 ILE C CD1 
5698  N N   . ALA B 103 ? 1.0603 1.0690 1.0455 -0.0317 0.0225  -0.0994 435 ALA C N   
5699  C CA  . ALA B 103 ? 0.9826 0.9932 0.9578 -0.0319 0.0208  -0.0827 435 ALA C CA  
5700  C C   . ALA B 103 ? 1.0727 1.0772 1.0435 -0.0428 0.0260  -0.0773 435 ALA C C   
5701  O O   . ALA B 103 ? 1.2486 1.2417 1.2194 -0.0526 0.0291  -0.0794 435 ALA C O   
5702  C CB  . ALA B 103 ? 1.0273 1.0309 0.9967 -0.0313 0.0163  -0.0712 435 ALA C CB  
5703  N N   . TRP B 104 ? 0.8833 0.8955 0.8507 -0.0416 0.0269  -0.0697 436 TRP C N   
5704  C CA  . TRP B 104 ? 0.8767 0.8837 0.8403 -0.0514 0.0307  -0.0617 436 TRP C CA  
5705  C C   . TRP B 104 ? 0.8385 0.8502 0.7948 -0.0498 0.0286  -0.0455 436 TRP C C   
5706  O O   . TRP B 104 ? 0.8156 0.8367 0.7706 -0.0407 0.0252  -0.0428 436 TRP C O   
5707  C CB  . TRP B 104 ? 0.8198 0.8305 0.7897 -0.0535 0.0356  -0.0712 436 TRP C CB  
5708  C CG  . TRP B 104 ? 0.7548 0.7794 0.7292 -0.0438 0.0357  -0.0761 436 TRP C CG  
5709  C CD1 . TRP B 104 ? 0.7551 0.7872 0.7301 -0.0426 0.0379  -0.0703 436 TRP C CD1 
5710  C CD2 . TRP B 104 ? 0.7846 0.8179 0.7646 -0.0347 0.0343  -0.0885 436 TRP C CD2 
5711  N NE1 . TRP B 104 ? 0.7579 0.8028 0.7378 -0.0336 0.0383  -0.0785 436 TRP C NE1 
5712  C CE2 . TRP B 104 ? 0.7109 0.7571 0.6934 -0.0287 0.0359  -0.0895 436 TRP C CE2 
5713  C CE3 . TRP B 104 ? 0.8184 0.8505 0.8023 -0.0310 0.0319  -0.0990 436 TRP C CE3 
5714  C CZ2 . TRP B 104 ? 0.7142 0.7722 0.7015 -0.0201 0.0352  -0.1003 436 TRP C CZ2 
5715  C CZ3 . TRP B 104 ? 0.7922 0.8364 0.7816 -0.0217 0.0305  -0.1093 436 TRP C CZ3 
5716  C CH2 . TRP B 104 ? 0.7760 0.8331 0.7663 -0.0166 0.0321  -0.1099 436 TRP C CH2 
5717  N N   . ASN B 105 ? 0.8240 0.8293 0.7753 -0.0593 0.0304  -0.0344 437 ASN C N   
5718  C CA  . ASN B 105 ? 0.7508 0.7630 0.6979 -0.0574 0.0294  -0.0210 437 ASN C CA  
5719  C C   . ASN B 105 ? 0.7523 0.7772 0.7052 -0.0509 0.0313  -0.0239 437 ASN C C   
5720  O O   . ASN B 105 ? 0.7622 0.7917 0.7226 -0.0475 0.0336  -0.0365 437 ASN C O   
5721  C CB  . ASN B 105 ? 0.6799 0.6870 0.6229 -0.0675 0.0311  -0.0082 437 ASN C CB  
5722  C CG  . ASN B 105 ? 0.7370 0.7382 0.6703 -0.0712 0.0283  0.0046  437 ASN C CG  
5723  O OD1 . ASN B 105 ? 0.8146 0.8104 0.7443 -0.0697 0.0259  0.0029  437 ASN C OD1 
5724  N ND2 . ASN B 105 ? 0.6731 0.6773 0.6028 -0.0743 0.0283  0.0178  437 ASN C ND2 
5725  N N   . SER B 106 ? 0.6790 0.7094 0.6289 -0.0502 0.0308  -0.0120 438 SER C N   
5726  C CA  . SER B 106 ? 0.7020 0.7459 0.6561 -0.0419 0.0317  -0.0146 438 SER C CA  
5727  C C   . SER B 106 ? 0.7354 0.7834 0.6866 -0.0435 0.0318  -0.0004 438 SER C C   
5728  O O   . SER B 106 ? 0.7554 0.8147 0.7102 -0.0383 0.0333  -0.0003 438 SER C O   
5729  C CB  . SER B 106 ? 0.6509 0.7007 0.6027 -0.0329 0.0277  -0.0205 438 SER C CB  
5730  O OG  . SER B 106 ? 0.6352 0.6974 0.5858 -0.0265 0.0270  -0.0171 438 SER C OG  
5731  N N   . ASN B 107 ? 0.6654 0.7042 0.6103 -0.0515 0.0306  0.0110  439 ASN C N   
5732  C CA  . ASN B 107 ? 0.6669 0.7092 0.6087 -0.0536 0.0303  0.0250  439 ASN C CA  
5733  C C   . ASN B 107 ? 0.6635 0.7141 0.6154 -0.0531 0.0344  0.0255  439 ASN C C   
5734  O O   . ASN B 107 ? 0.5983 0.6576 0.5510 -0.0501 0.0348  0.0323  439 ASN C O   
5735  C CB  . ASN B 107 ? 0.6411 0.6724 0.5758 -0.0636 0.0291  0.0360  439 ASN C CB  
5736  C CG  . ASN B 107 ? 0.6556 0.6898 0.5828 -0.0641 0.0270  0.0499  439 ASN C CG  
5737  O OD1 . ASN B 107 ? 0.6932 0.7317 0.6148 -0.0579 0.0245  0.0511  439 ASN C OD1 
5738  N ND2 . ASN B 107 ? 0.6815 0.7134 0.6084 -0.0720 0.0279  0.0607  439 ASN C ND2 
5739  N N   . LYS B 108 ? 0.6627 0.7105 0.6229 -0.0561 0.0377  0.0181  440 LYS C N   
5740  C CA  . LYS B 108 ? 0.6892 0.7435 0.6603 -0.0559 0.0417  0.0194  440 LYS C CA  
5741  C C   . LYS B 108 ? 0.6424 0.7100 0.6194 -0.0464 0.0441  0.0125  440 LYS C C   
5742  O O   . LYS B 108 ? 0.6337 0.7093 0.6171 -0.0448 0.0465  0.0178  440 LYS C O   
5743  C CB  . LYS B 108 ? 0.7753 0.8232 0.7536 -0.0614 0.0447  0.0129  440 LYS C CB  
5744  C CG  . LYS B 108 ? 0.9455 0.9830 0.9205 -0.0730 0.0435  0.0239  440 LYS C CG  
5745  C CD  . LYS B 108 ? 1.1214 1.1479 1.0960 -0.0808 0.0445  0.0164  440 LYS C CD  
5746  C CE  . LYS B 108 ? 1.1402 1.1594 1.1142 -0.0929 0.0440  0.0281  440 LYS C CE  
5747  N NZ  . LYS B 108 ? 1.1544 1.1705 1.1370 -0.0974 0.0471  0.0229  440 LYS C NZ  
5748  N N   . LEU B 109 ? 0.6526 0.7235 0.6282 -0.0403 0.0435  0.0005  441 LEU C N   
5749  C CA  . LEU B 109 ? 0.6590 0.7429 0.6412 -0.0328 0.0467  -0.0074 441 LEU C CA  
5750  C C   . LEU B 109 ? 0.6802 0.7720 0.6547 -0.0263 0.0433  -0.0085 441 LEU C C   
5751  O O   . LEU B 109 ? 0.7576 0.8616 0.7362 -0.0209 0.0460  -0.0138 441 LEU C O   
5752  C CB  . LEU B 109 ? 0.6778 0.7624 0.6687 -0.0311 0.0507  -0.0226 441 LEU C CB  
5753  C CG  . LEU B 109 ? 0.6940 0.7757 0.6820 -0.0288 0.0489  -0.0353 441 LEU C CG  
5754  C CD1 . LEU B 109 ? 0.7040 0.7889 0.7021 -0.0273 0.0544  -0.0496 441 LEU C CD1 
5755  C CD2 . LEU B 109 ? 0.7311 0.7989 0.7122 -0.0351 0.0453  -0.0319 441 LEU C CD2 
5756  N N   . ASP B 110 ? 0.6589 0.7443 0.6223 -0.0269 0.0378  -0.0033 442 ASP C N   
5757  C CA  . ASP B 110 ? 0.6536 0.7465 0.6093 -0.0211 0.0340  -0.0025 442 ASP C CA  
5758  C C   . ASP B 110 ? 0.6483 0.7406 0.5949 -0.0231 0.0312  0.0120  442 ASP C C   
5759  O O   . ASP B 110 ? 0.6656 0.7641 0.6049 -0.0190 0.0281  0.0139  442 ASP C O   
5760  C CB  . ASP B 110 ? 0.7215 0.8101 0.6723 -0.0179 0.0294  -0.0096 442 ASP C CB  
5761  C CG  . ASP B 110 ? 0.7493 0.8448 0.7077 -0.0130 0.0316  -0.0253 442 ASP C CG  
5762  O OD1 . ASP B 110 ? 0.7439 0.8524 0.7045 -0.0084 0.0334  -0.0294 442 ASP C OD1 
5763  O OD2 . ASP B 110 ? 0.7929 0.8815 0.7547 -0.0142 0.0317  -0.0339 442 ASP C OD2 
5764  N N   . SER B 111 ? 0.6755 0.7611 0.6218 -0.0296 0.0320  0.0223  443 SER C N   
5765  C CA  . SER B 111 ? 0.6736 0.7595 0.6116 -0.0319 0.0298  0.0358  443 SER C CA  
5766  C C   . SER B 111 ? 0.6184 0.7100 0.5647 -0.0347 0.0343  0.0419  443 SER C C   
5767  O O   . SER B 111 ? 0.5834 0.6715 0.5389 -0.0385 0.0373  0.0413  443 SER C O   
5768  C CB  . SER B 111 ? 0.6679 0.7402 0.5963 -0.0375 0.0259  0.0436  443 SER C CB  
5769  O OG  . SER B 111 ? 0.7019 0.7680 0.6336 -0.0452 0.0279  0.0506  443 SER C OG  
5770  N N   . LYS B 112 ? 0.6776 0.7788 0.6219 -0.0325 0.0349  0.0467  444 LYS C N   
5771  C CA  . LYS B 112 ? 0.7901 0.8989 0.7447 -0.0338 0.0396  0.0508  444 LYS C CA  
5772  C C   . LYS B 112 ? 0.8173 0.9258 0.7648 -0.0379 0.0377  0.0650  444 LYS C C   
5773  O O   . LYS B 112 ? 0.8101 0.9172 0.7441 -0.0375 0.0338  0.0696  444 LYS C O   
5774  C CB  . LYS B 112 ? 0.8231 0.9463 0.7853 -0.0279 0.0440  0.0414  444 LYS C CB  
5775  C CG  . LYS B 112 ? 0.9115 1.0433 0.8643 -0.0260 0.0426  0.0454  444 LYS C CG  
5776  C CD  . LYS B 112 ? 0.9621 1.1091 0.9236 -0.0231 0.0484  0.0397  444 LYS C CD  
5777  C CE  . LYS B 112 ? 1.0420 1.1961 0.9903 -0.0222 0.0459  0.0430  444 LYS C CE  
5778  N NZ  . LYS B 112 ? 0.9922 1.1551 0.9441 -0.0246 0.0498  0.0489  444 LYS C NZ  
5779  N N   . VAL B 113 ? 0.7853 0.8946 0.7421 -0.0420 0.0405  0.0722  445 VAL C N   
5780  C CA  . VAL B 113 ? 0.7728 0.8827 0.7244 -0.0463 0.0392  0.0854  445 VAL C CA  
5781  C C   . VAL B 113 ? 0.8223 0.9427 0.7684 -0.0424 0.0398  0.0849  445 VAL C C   
5782  O O   . VAL B 113 ? 0.8524 0.9838 0.8076 -0.0382 0.0441  0.0772  445 VAL C O   
5783  C CB  . VAL B 113 ? 0.7122 0.8248 0.6784 -0.0500 0.0425  0.0917  445 VAL C CB  
5784  C CG1 . VAL B 113 ? 0.5909 0.7026 0.5504 -0.0553 0.0403  0.1054  445 VAL C CG1 
5785  C CG2 . VAL B 113 ? 0.7296 0.8333 0.7030 -0.0537 0.0425  0.0901  445 VAL C CG2 
5786  N N   . GLY B 114 ? 0.8750 0.9919 0.8058 -0.0444 0.0357  0.0926  446 GLY C N   
5787  C CA  . GLY B 114 ? 0.9010 1.0273 0.8248 -0.0419 0.0359  0.0929  446 GLY C CA  
5788  C C   . GLY B 114 ? 0.9912 1.1181 0.9043 -0.0371 0.0327  0.0857  446 GLY C C   
5789  O O   . GLY B 114 ? 0.9996 1.1352 0.9066 -0.0353 0.0328  0.0849  446 GLY C O   
5790  N N   . GLY B 115 ? 1.3528 1.4713 1.2640 -0.0353 0.0297  0.0802  447 GLY C N   
5791  C CA  . GLY B 115 ? 1.3135 1.4303 1.2133 -0.0313 0.0250  0.0759  447 GLY C CA  
5792  C C   . GLY B 115 ? 1.2541 1.3796 1.1598 -0.0253 0.0263  0.0625  447 GLY C C   
5793  O O   . GLY B 115 ? 1.2757 1.4138 1.1842 -0.0232 0.0295  0.0581  447 GLY C O   
5794  N N   . ASN B 116 ? 0.9425 1.0616 0.8501 -0.0229 0.0243  0.0552  448 ASN C N   
5795  C CA  . ASN B 116 ? 0.9192 1.0465 0.8328 -0.0175 0.0255  0.0419  448 ASN C CA  
5796  C C   . ASN B 116 ? 0.8703 0.9982 0.7718 -0.0137 0.0191  0.0409  448 ASN C C   
5797  O O   . ASN B 116 ? 0.9031 1.0204 0.7995 -0.0131 0.0141  0.0420  448 ASN C O   
5798  C CB  . ASN B 116 ? 0.8711 0.9923 0.7953 -0.0172 0.0275  0.0334  448 ASN C CB  
5799  C CG  . ASN B 116 ? 0.8237 0.9517 0.7515 -0.0117 0.0275  0.0199  448 ASN C CG  
5800  O OD1 . ASN B 116 ? 0.8269 0.9675 0.7543 -0.0086 0.0288  0.0153  448 ASN C OD1 
5801  N ND2 . ASN B 116 ? 0.7658 0.8863 0.6978 -0.0110 0.0266  0.0127  448 ASN C ND2 
5802  N N   . TYR B 117 ? 0.8074 0.9475 0.7043 -0.0115 0.0190  0.0390  449 TYR C N   
5803  C CA  . TYR B 117 ? 0.8041 0.9448 0.6887 -0.0084 0.0120  0.0399  449 TYR C CA  
5804  C C   . TYR B 117 ? 0.8569 1.0062 0.7458 -0.0032 0.0110  0.0271  449 TYR C C   
5805  O O   . TYR B 117 ? 0.9188 1.0702 0.7988 -0.0002 0.0047  0.0273  449 TYR C O   
5806  C CB  . TYR B 117 ? 0.8244 0.9722 0.6977 -0.0105 0.0110  0.0477  449 TYR C CB  
5807  C CG  . TYR B 117 ? 0.8872 1.0273 0.7551 -0.0158 0.0115  0.0605  449 TYR C CG  
5808  C CD1 . TYR B 117 ? 0.9206 1.0455 0.7839 -0.0176 0.0078  0.0680  449 TYR C CD1 
5809  C CD2 . TYR B 117 ? 0.8909 1.0393 0.7585 -0.0193 0.0160  0.0647  449 TYR C CD2 
5810  C CE1 . TYR B 117 ? 0.8848 1.0031 0.7425 -0.0230 0.0084  0.0797  449 TYR C CE1 
5811  C CE2 . TYR B 117 ? 0.8606 1.0027 0.7234 -0.0243 0.0164  0.0763  449 TYR C CE2 
5812  C CZ  . TYR B 117 ? 0.8307 0.9578 0.6881 -0.0261 0.0124  0.0839  449 TYR C CZ  
5813  O OH  . TYR B 117 ? 0.7838 0.9048 0.6359 -0.0315 0.0128  0.0952  449 TYR C OH  
5814  N N   . ASN B 118 ? 0.7978 0.9518 0.7002 -0.0021 0.0169  0.0163  450 ASN C N   
5815  C CA  . ASN B 118 ? 0.8024 0.9657 0.7091 0.0024  0.0168  0.0034  450 ASN C CA  
5816  C C   . ASN B 118 ? 0.8070 0.9625 0.7106 0.0061  0.0095  0.0011  450 ASN C C   
5817  O O   . ASN B 118 ? 0.8939 1.0575 0.7960 0.0101  0.0060  -0.0058 450 ASN C O   
5818  C CB  . ASN B 118 ? 0.8911 1.0580 0.8132 0.0023  0.0249  -0.0071 450 ASN C CB  
5819  C CG  . ASN B 118 ? 1.0433 1.2246 0.9702 0.0012  0.0318  -0.0112 450 ASN C CG  
5820  O OD1 . ASN B 118 ? 1.0431 1.2299 0.9623 -0.0009 0.0314  -0.0041 450 ASN C OD1 
5821  N ND2 . ASN B 118 ? 1.2272 1.4150 1.1669 0.0023  0.0386  -0.0231 450 ASN C ND2 
5822  N N   . TYR B 119 ? 0.7574 0.8976 0.6607 0.0045  0.0072  0.0066  451 TYR C N   
5823  C CA  . TYR B 119 ? 0.7386 0.8700 0.6414 0.0075  0.0013  0.0039  451 TYR C CA  
5824  C C   . TYR B 119 ? 0.7413 0.8665 0.6310 0.0079  -0.0064 0.0155  451 TYR C C   
5825  O O   . TYR B 119 ? 0.7276 0.8439 0.6112 0.0037  -0.0064 0.0266  451 TYR C O   
5826  C CB  . TYR B 119 ? 0.6770 0.7952 0.5877 0.0043  0.0044  0.0020  451 TYR C CB  
5827  C CG  . TYR B 119 ? 0.6955 0.8176 0.6191 0.0036  0.0116  -0.0093 451 TYR C CG  
5828  C CD1 . TYR B 119 ? 0.8426 0.9718 0.7713 0.0013  0.0182  -0.0093 451 TYR C CD1 
5829  C CD2 . TYR B 119 ? 0.7587 0.8770 0.6898 0.0052  0.0118  -0.0201 451 TYR C CD2 
5830  C CE1 . TYR B 119 ? 0.8939 1.0255 0.8349 0.0008  0.0247  -0.0197 451 TYR C CE1 
5831  C CE2 . TYR B 119 ? 0.7634 0.8837 0.7053 0.0043  0.0181  -0.0304 451 TYR C CE2 
5832  C CZ  . TYR B 119 ? 0.8382 0.9650 0.7849 0.0023  0.0244  -0.0302 451 TYR C CZ  
5833  O OH  . TYR B 119 ? 0.9409 1.0691 0.8988 0.0015  0.0305  -0.0407 451 TYR C OH  
5834  N N   . ARG B 120 ? 0.7610 0.8906 0.6470 0.0128  -0.0131 0.0131  452 ARG C N   
5835  C CA  . ARG B 120 ? 0.7207 0.8462 0.5940 0.0136  -0.0208 0.0242  452 ARG C CA  
5836  C C   . ARG B 120 ? 0.6790 0.7961 0.5546 0.0180  -0.0277 0.0223  452 ARG C C   
5837  O O   . ARG B 120 ? 0.6812 0.8014 0.5671 0.0216  -0.0274 0.0107  452 ARG C O   
5838  C CB  . ARG B 120 ? 0.7027 0.8433 0.5683 0.0151  -0.0234 0.0246  452 ARG C CB  
5839  C CG  . ARG B 120 ? 0.7100 0.8593 0.5712 0.0107  -0.0177 0.0280  452 ARG C CG  
5840  C CD  . ARG B 120 ? 0.7089 0.8714 0.5608 0.0122  -0.0226 0.0282  452 ARG C CD  
5841  N NE  . ARG B 120 ? 0.6956 0.8747 0.5538 0.0123  -0.0169 0.0167  452 ARG C NE  
5842  C CZ  . ARG B 120 ? 0.7215 0.9149 0.5739 0.0131  -0.0200 0.0135  452 ARG C CZ  
5843  N NH1 . ARG B 120 ? 0.7326 0.9261 0.5717 0.0136  -0.0288 0.0220  452 ARG C NH1 
5844  N NH2 . ARG B 120 ? 0.8300 1.0378 0.6900 0.0132  -0.0141 0.0012  452 ARG C NH2 
5845  N N   . TYR B 121 ? 0.6835 0.7901 0.5505 0.0179  -0.0337 0.0333  453 TYR C N   
5846  C CA  . TYR B 121 ? 0.7151 0.8156 0.5839 0.0230  -0.0415 0.0329  453 TYR C CA  
5847  C C   . TYR B 121 ? 0.7864 0.8929 0.6438 0.0259  -0.0499 0.0410  453 TYR C C   
5848  O O   . TYR B 121 ? 0.8548 0.9674 0.7008 0.0228  -0.0496 0.0485  453 TYR C O   
5849  C CB  . TYR B 121 ? 0.7288 0.8101 0.5983 0.0209  -0.0424 0.0389  453 TYR C CB  
5850  C CG  . TYR B 121 ? 0.8103 0.8822 0.6674 0.0154  -0.0418 0.0534  453 TYR C CG  
5851  C CD1 . TYR B 121 ? 0.9192 0.9919 0.7633 0.0161  -0.0478 0.0644  453 TYR C CD1 
5852  C CD2 . TYR B 121 ? 0.8796 0.9403 0.7381 0.0094  -0.0362 0.0560  453 TYR C CD2 
5853  C CE1 . TYR B 121 ? 0.9533 1.0170 0.7861 0.0107  -0.0469 0.0769  453 TYR C CE1 
5854  C CE2 . TYR B 121 ? 0.9371 0.9896 0.7851 0.0040  -0.0353 0.0683  453 TYR C CE2 
5855  C CZ  . TYR B 121 ? 0.9015 0.9553 0.7366 0.0047  -0.0404 0.0786  453 TYR C CZ  
5856  O OH  . TYR B 121 ? 0.9439 0.9892 0.7682 -0.0010 -0.0392 0.0905  453 TYR C OH  
5857  N N   . ARG B 122 ? 0.7532 0.8573 0.6136 0.0314  -0.0579 0.0404  454 ARG C N   
5858  C CA  . ARG B 122 ? 0.7635 0.8680 0.6128 0.0338  -0.0672 0.0510  454 ARG C CA  
5859  C C   . ARG B 122 ? 0.8167 0.9024 0.6616 0.0320  -0.0693 0.0622  454 ARG C C   
5860  O O   . ARG B 122 ? 0.8164 0.8904 0.6719 0.0336  -0.0689 0.0584  454 ARG C O   
5861  C CB  . ARG B 122 ? 0.8455 0.9558 0.7025 0.0411  -0.0754 0.0453  454 ARG C CB  
5862  C CG  . ARG B 122 ? 0.7927 0.9148 0.6401 0.0436  -0.0843 0.0509  454 ARG C CG  
5863  C CD  . ARG B 122 ? 0.7258 0.8575 0.5839 0.0504  -0.0907 0.0420  454 ARG C CD  
5864  N NE  . ARG B 122 ? 0.7089 0.8599 0.5655 0.0489  -0.0869 0.0332  454 ARG C NE  
5865  C CZ  . ARG B 122 ? 0.7009 0.8641 0.5442 0.0462  -0.0897 0.0386  454 ARG C CZ  
5866  N NH1 . ARG B 122 ? 0.7475 0.9060 0.5773 0.0451  -0.0971 0.0528  454 ARG C NH1 
5867  N NH2 . ARG B 122 ? 0.6303 0.8099 0.4732 0.0435  -0.0837 0.0295  454 ARG C NH2 
5868  N N   . LEU B 123 ? 0.7950 0.8772 0.6246 0.0287  -0.0717 0.0756  455 LEU C N   
5869  C CA  . LEU B 123 ? 0.9032 0.9672 0.7296 0.0281  -0.0750 0.0856  455 LEU C CA  
5870  C C   . LEU B 123 ? 0.9007 0.9625 0.7192 0.0321  -0.0858 0.0955  455 LEU C C   
5871  O O   . LEU B 123 ? 0.9682 1.0143 0.7864 0.0326  -0.0888 0.1028  455 LEU C O   
5872  C CB  . LEU B 123 ? 0.8451 0.8997 0.6618 0.0205  -0.0690 0.0945  455 LEU C CB  
5873  C CG  . LEU B 123 ? 0.8483 0.9037 0.6469 0.0165  -0.0709 0.1074  455 LEU C CG  
5874  C CD1 . LEU B 123 ? 0.8590 0.9031 0.6530 0.0096  -0.0644 0.1137  455 LEU C CD1 
5875  C CD2 . LEU B 123 ? 0.9854 1.0588 0.7789 0.0150  -0.0688 0.1041  455 LEU C CD2 
5876  N N   . PHE B 124 ? 0.8214 0.8978 0.6342 0.0348  -0.0919 0.0959  456 PHE C N   
5877  C CA  . PHE B 124 ? 0.8382 0.9126 0.6432 0.0382  -0.1030 0.1062  456 PHE C CA  
5878  C C   . PHE B 124 ? 0.8425 0.9303 0.6558 0.0449  -0.1105 0.0991  456 PHE C C   
5879  O O   . PHE B 124 ? 0.8815 0.9861 0.6964 0.0446  -0.1078 0.0899  456 PHE C O   
5880  C CB  . PHE B 124 ? 0.8856 0.9648 0.6703 0.0328  -0.1045 0.1173  456 PHE C CB  
5881  C CG  . PHE B 124 ? 0.8572 0.9236 0.6320 0.0263  -0.0988 0.1262  456 PHE C CG  
5882  C CD1 . PHE B 124 ? 0.8977 0.9460 0.6784 0.0261  -0.0966 0.1289  456 PHE C CD1 
5883  C CD2 . PHE B 124 ? 0.8735 0.9469 0.6333 0.0196  -0.0953 0.1313  456 PHE C CD2 
5884  C CE1 . PHE B 124 ? 0.9510 0.9888 0.7223 0.0196  -0.0912 0.1367  456 PHE C CE1 
5885  C CE2 . PHE B 124 ? 0.8945 0.9574 0.6454 0.0135  -0.0900 0.1392  456 PHE C CE2 
5886  C CZ  . PHE B 124 ? 0.9166 0.9619 0.6730 0.0134  -0.0881 0.1421  456 PHE C CZ  
5887  N N   . ARG B 125 ? 0.8721 0.9532 0.6908 0.0508  -0.1199 0.1037  457 ARG C N   
5888  C CA  . ARG B 125 ? 0.8844 0.9790 0.7116 0.0572  -0.1276 0.0973  457 ARG C CA  
5889  C C   . ARG B 125 ? 0.9172 1.0023 0.7476 0.0630  -0.1391 0.1069  457 ARG C C   
5890  O O   . ARG B 125 ? 0.8899 0.9566 0.7253 0.0639  -0.1385 0.1117  457 ARG C O   
5891  C CB  . ARG B 125 ? 0.8037 0.9035 0.6501 0.0605  -0.1220 0.0802  457 ARG C CB  
5892  C CG  . ARG B 125 ? 0.8809 0.9973 0.7361 0.0663  -0.1286 0.0718  457 ARG C CG  
5893  C CD  . ARG B 125 ? 0.8387 0.9604 0.7109 0.0681  -0.1210 0.0541  457 ARG C CD  
5894  N NE  . ARG B 125 ? 0.6779 0.8169 0.5583 0.0730  -0.1261 0.0446  457 ARG C NE  
5895  C CZ  . ARG B 125 ? 0.7878 0.9262 0.6830 0.0801  -0.1333 0.0410  457 ARG C CZ  
5896  N NH1 . ARG B 125 ? 0.8237 0.9445 0.7284 0.0832  -0.1354 0.0447  457 ARG C NH1 
5897  N NH2 . ARG B 125 ? 0.9002 1.0562 0.8010 0.0839  -0.1384 0.0334  457 ARG C NH2 
5898  N N   . LYS B 126 ? 0.9054 1.0031 0.7329 0.0665  -0.1495 0.1100  458 LYS C N   
5899  C CA  . LYS B 126 ? 0.9054 0.9944 0.7338 0.0716  -0.1616 0.1219  458 LYS C CA  
5900  C C   . LYS B 126 ? 0.8525 0.9291 0.7034 0.0787  -0.1627 0.1164  458 LYS C C   
5901  O O   . LYS B 126 ? 0.8852 0.9467 0.7389 0.0817  -0.1686 0.1265  458 LYS C O   
5902  C CB  . LYS B 126 ? 0.9524 1.0588 0.7749 0.0740  -0.1734 0.1258  458 LYS C CB  
5903  C CG  . LYS B 126 ? 1.0052 1.1324 0.8127 0.0677  -0.1709 0.1224  458 LYS C CG  
5904  C CD  . LYS B 126 ? 0.9559 1.0959 0.7543 0.0689  -0.1849 0.1314  458 LYS C CD  
5905  C CE  . LYS B 126 ? 1.1070 1.2691 0.8904 0.0621  -0.1835 0.1280  458 LYS C CE  
5906  N NZ  . LYS B 126 ? 1.3885 1.5485 1.1512 0.0526  -0.1767 0.1344  458 LYS C NZ  
5907  N N   . SER B 127 ? 0.8335 0.9153 0.7008 0.0808  -0.1562 0.1003  459 SER C N   
5908  C CA  . SER B 127 ? 0.8269 0.9011 0.7171 0.0877  -0.1579 0.0927  459 SER C CA  
5909  C C   . SER B 127 ? 0.8344 0.9085 0.7365 0.0857  -0.1458 0.0760  459 SER C C   
5910  O O   . SER B 127 ? 0.8549 0.9412 0.7510 0.0815  -0.1391 0.0684  459 SER C O   
5911  C CB  . SER B 127 ? 0.9418 1.0302 0.8423 0.0953  -0.1693 0.0901  459 SER C CB  
5912  O OG  . SER B 127 ? 0.9834 1.0934 0.8788 0.0934  -0.1676 0.0813  459 SER C OG  
5913  N N   . ASN B 128 ? 0.8285 0.8894 0.7485 0.0886  -0.1433 0.0700  460 ASN C N   
5914  C CA  . ASN B 128 ? 0.8177 0.8764 0.7490 0.0859  -0.1320 0.0545  460 ASN C CA  
5915  C C   . ASN B 128 ? 0.8629 0.9401 0.8051 0.0897  -0.1325 0.0397  460 ASN C C   
5916  O O   . ASN B 128 ? 0.8400 0.9283 0.7881 0.0962  -0.1424 0.0399  460 ASN C O   
5917  C CB  . ASN B 128 ? 0.7966 0.8368 0.7443 0.0875  -0.1297 0.0518  460 ASN C CB  
5918  C CG  . ASN B 128 ? 0.8493 0.8706 0.7867 0.0825  -0.1271 0.0647  460 ASN C CG  
5919  O OD1 . ASN B 128 ? 0.9000 0.9089 0.8401 0.0769  -0.1176 0.0607  460 ASN C OD1 
5920  N ND2 . ASN B 128 ? 0.8773 0.8975 0.8006 0.0834  -0.1351 0.0805  460 ASN C ND2 
5921  N N   . LEU B 129 ? 0.8574 0.9378 0.8025 0.0855  -0.1218 0.0269  461 LEU C N   
5922  C CA  . LEU B 129 ? 0.8170 0.9148 0.7713 0.0882  -0.1209 0.0122  461 LEU C CA  
5923  C C   . LEU B 129 ? 0.8894 0.9842 0.8664 0.0944  -0.1233 0.0014  461 LEU C C   
5924  O O   . LEU B 129 ? 0.9680 1.0461 0.9548 0.0939  -0.1203 0.0004  461 LEU C O   
5925  C CB  . LEU B 129 ? 0.7565 0.8577 0.7076 0.0817  -0.1085 0.0019  461 LEU C CB  
5926  C CG  . LEU B 129 ? 0.6872 0.8016 0.6223 0.0770  -0.1048 0.0038  461 LEU C CG  
5927  C CD1 . LEU B 129 ? 0.7103 0.8283 0.6504 0.0728  -0.0933 -0.0102 461 LEU C CD1 
5928  C CD2 . LEU B 129 ? 0.6622 0.7955 0.5929 0.0808  -0.1132 0.0049  461 LEU C CD2 
5929  N N   . LYS B 130 ? 0.9864 1.0981 0.9720 0.0997  -0.1284 -0.0073 462 LYS C N   
5930  C CA  . LYS B 130 ? 0.9132 1.0260 0.9213 0.1052  -0.1296 -0.0207 462 LYS C CA  
5931  C C   . LYS B 130 ? 0.8753 0.9901 0.8895 0.1007  -0.1174 -0.0381 462 LYS C C   
5932  O O   . LYS B 130 ? 0.8846 1.0083 0.8870 0.0959  -0.1113 -0.0410 462 LYS C O   
5933  C CB  . LYS B 130 ? 0.9859 1.1172 0.9998 0.1124  -0.1408 -0.0220 462 LYS C CB  
5934  C CG  . LYS B 130 ? 1.1445 1.2733 1.1554 0.1175  -0.1543 -0.0050 462 LYS C CG  
5935  C CD  . LYS B 130 ? 1.2851 1.4198 1.3172 0.1267  -0.1646 -0.0091 462 LYS C CD  
5936  C CE  . LYS B 130 ? 1.3281 1.4418 1.3760 0.1303  -0.1661 -0.0053 462 LYS C CE  
5937  N NZ  . LYS B 130 ? 1.3408 1.4581 1.4084 0.1399  -0.1785 -0.0037 462 LYS C NZ  
5938  N N   . PRO B 131 ? 0.7787 0.8850 0.8111 0.1017  -0.1133 -0.0500 463 PRO C N   
5939  C CA  . PRO B 131 ? 0.7335 0.8385 0.7696 0.0958  -0.1011 -0.0651 463 PRO C CA  
5940  C C   . PRO B 131 ? 0.7200 0.8448 0.7513 0.0955  -0.0988 -0.0742 463 PRO C C   
5941  O O   . PRO B 131 ? 0.7942 0.9350 0.8295 0.1013  -0.1063 -0.0768 463 PRO C O   
5942  C CB  . PRO B 131 ? 0.6767 0.7746 0.7353 0.0988  -0.1003 -0.0776 463 PRO C CB  
5943  C CG  . PRO B 131 ? 0.6941 0.7795 0.7572 0.1024  -0.1073 -0.0657 463 PRO C CG  
5944  C CD  . PRO B 131 ? 0.8241 0.9178 0.8734 0.1065  -0.1181 -0.0491 463 PRO C CD  
5945  N N   . PHE B 132 ? 0.6740 0.7979 0.6956 0.0883  -0.0888 -0.0773 464 PHE C N   
5946  C CA  . PHE B 132 ? 0.6805 0.8201 0.6990 0.0865  -0.0835 -0.0878 464 PHE C CA  
5947  C C   . PHE B 132 ? 0.7095 0.8660 0.7150 0.0884  -0.0896 -0.0798 464 PHE C C   
5948  O O   . PHE B 132 ? 0.6632 0.8357 0.6672 0.0878  -0.0865 -0.0890 464 PHE C O   
5949  C CB  . PHE B 132 ? 0.6839 0.8311 0.7201 0.0900  -0.0826 -0.1059 464 PHE C CB  
5950  C CG  . PHE B 132 ? 0.6843 0.8198 0.7282 0.0845  -0.0720 -0.1178 464 PHE C CG  
5951  C CD1 . PHE B 132 ? 0.7340 0.8675 0.7692 0.0772  -0.0619 -0.1206 464 PHE C CD1 
5952  C CD2 . PHE B 132 ? 0.7258 0.8518 0.7862 0.0862  -0.0722 -0.1258 464 PHE C CD2 
5953  C CE1 . PHE B 132 ? 0.7903 0.9125 0.8319 0.0713  -0.0527 -0.1307 464 PHE C CE1 
5954  C CE2 . PHE B 132 ? 0.7772 0.8923 0.8440 0.0800  -0.0623 -0.1369 464 PHE C CE2 
5955  C CZ  . PHE B 132 ? 0.7744 0.8875 0.8314 0.0724  -0.0529 -0.1391 464 PHE C CZ  
5956  N N   . GLU B 133 ? 0.6644 0.8176 0.6598 0.0898  -0.0976 -0.0632 465 GLU C N   
5957  C CA  . GLU B 133 ? 0.6457 0.8124 0.6254 0.0894  -0.1025 -0.0535 465 GLU C CA  
5958  C C   . GLU B 133 ? 0.6986 0.8641 0.6638 0.0817  -0.0929 -0.0505 465 GLU C C   
5959  O O   . GLU B 133 ? 0.7010 0.8524 0.6664 0.0770  -0.0846 -0.0509 465 GLU C O   
5960  C CB  . GLU B 133 ? 0.7090 0.8693 0.6821 0.0924  -0.1135 -0.0362 465 GLU C CB  
5961  C CG  . GLU B 133 ? 0.7945 0.9717 0.7607 0.0961  -0.1249 -0.0291 465 GLU C CG  
5962  C CD  . GLU B 133 ? 0.7854 0.9549 0.7384 0.0963  -0.1340 -0.0091 465 GLU C CD  
5963  O OE1 . GLU B 133 ? 0.7575 0.9143 0.7191 0.1009  -0.1407 -0.0024 465 GLU C OE1 
5964  O OE2 . GLU B 133 ? 0.6977 0.8758 0.6332 0.0922  -0.1352 -0.0009 465 GLU C OE2 
5965  N N   . ARG B 134 ? 0.6706 0.8519 0.6239 0.0800  -0.0939 -0.0477 466 ARG C N   
5966  C CA  . ARG B 134 ? 0.6866 0.8690 0.6264 0.0732  -0.0859 -0.0437 466 ARG C CA  
5967  C C   . ARG B 134 ? 0.7307 0.9221 0.6545 0.0721  -0.0927 -0.0308 466 ARG C C   
5968  O O   . ARG B 134 ? 0.7845 0.9926 0.7066 0.0744  -0.0986 -0.0331 466 ARG C O   
5969  C CB  . ARG B 134 ? 0.6268 0.8211 0.5701 0.0702  -0.0758 -0.0584 466 ARG C CB  
5970  C CG  . ARG B 134 ? 0.6197 0.8071 0.5571 0.0635  -0.0650 -0.0569 466 ARG C CG  
5971  C CD  . ARG B 134 ? 0.6036 0.8058 0.5425 0.0608  -0.0563 -0.0693 466 ARG C CD  
5972  N NE  . ARG B 134 ? 0.5824 0.7865 0.5358 0.0630  -0.0525 -0.0854 466 ARG C NE  
5973  C CZ  . ARG B 134 ? 0.7342 0.9537 0.6935 0.0664  -0.0549 -0.0964 466 ARG C CZ  
5974  N NH1 . ARG B 134 ? 0.8900 1.1255 0.8419 0.0679  -0.0614 -0.0929 466 ARG C NH1 
5975  N NH2 . ARG B 134 ? 0.8345 1.0535 0.8071 0.0681  -0.0512 -0.1109 466 ARG C NH2 
5976  N N   . ASP B 135 ? 0.7340 0.9143 0.6457 0.0681  -0.0917 -0.0175 467 ASP C N   
5977  C CA  . ASP B 135 ? 0.7209 0.9080 0.6155 0.0652  -0.0962 -0.0052 467 ASP C CA  
5978  C C   . ASP B 135 ? 0.7473 0.9386 0.6335 0.0583  -0.0857 -0.0065 467 ASP C C   
5979  O O   . ASP B 135 ? 0.7143 0.8925 0.6001 0.0548  -0.0786 -0.0038 467 ASP C O   
5980  C CB  . ASP B 135 ? 0.7395 0.9114 0.6258 0.0656  -0.1032 0.0114  467 ASP C CB  
5981  C CG  . ASP B 135 ? 0.8198 1.0012 0.6926 0.0657  -0.1134 0.0226  467 ASP C CG  
5982  O OD1 . ASP B 135 ? 1.0087 1.2067 0.8835 0.0684  -0.1190 0.0175  467 ASP C OD1 
5983  O OD2 . ASP B 135 ? 0.7824 0.9554 0.6416 0.0624  -0.1153 0.0364  467 ASP C OD2 
5984  N N   . ILE B 136 ? 0.7242 0.9339 0.6038 0.0560  -0.0849 -0.0101 468 ILE C N   
5985  C CA  . ILE B 136 ? 0.6840 0.8997 0.5574 0.0496  -0.0746 -0.0124 468 ILE C CA  
5986  C C   . ILE B 136 ? 0.6329 0.8575 0.4891 0.0456  -0.0791 -0.0018 468 ILE C C   
5987  O O   . ILE B 136 ? 0.6386 0.8755 0.4891 0.0405  -0.0726 -0.0055 468 ILE C O   
5988  C CB  . ILE B 136 ? 0.6316 0.8615 0.5147 0.0493  -0.0666 -0.0294 468 ILE C CB  
5989  C CG1 . ILE B 136 ? 0.6543 0.9013 0.5389 0.0527  -0.0739 -0.0356 468 ILE C CG1 
5990  C CG2 . ILE B 136 ? 0.6298 0.8489 0.5282 0.0516  -0.0608 -0.0392 468 ILE C CG2 
5991  C CD1 . ILE B 136 ? 0.7311 0.9965 0.6175 0.0494  -0.0658 -0.0488 468 ILE C CD1 
5992  N N   . SER B 137 ? 0.6765 0.8942 0.5245 0.0475  -0.0897 0.0113  469 SER C N   
5993  C CA  . SER B 137 ? 0.6655 0.8919 0.4965 0.0437  -0.0959 0.0217  469 SER C CA  
5994  C C   . SER B 137 ? 0.7245 0.9411 0.5425 0.0377  -0.0919 0.0331  469 SER C C   
5995  O O   . SER B 137 ? 0.7949 0.9936 0.6129 0.0386  -0.0926 0.0415  469 SER C O   
5996  C CB  . SER B 137 ? 0.7529 0.9777 0.5820 0.0488  -0.1102 0.0302  469 SER C CB  
5997  O OG  . SER B 137 ? 0.7124 0.9186 0.5364 0.0499  -0.1154 0.0444  469 SER C OG  
5998  N N   . THR B 138 ? 0.7282 0.5960 0.7494 -0.0884 -0.0744 0.0926  470 THR C N   
5999  C CA  . THR B 138 ? 0.7892 0.6828 0.7800 -0.0995 -0.0750 0.1051  470 THR C CA  
6000  C C   . THR B 138 ? 0.8230 0.7323 0.8031 -0.1020 -0.0854 0.1180  470 THR C C   
6001  O O   . THR B 138 ? 0.9127 0.8564 0.8763 -0.0986 -0.0944 0.1258  470 THR C O   
6002  C CB  . THR B 138 ? 0.7901 0.7155 0.7723 -0.0896 -0.0784 0.1017  470 THR C CB  
6003  O OG1 . THR B 138 ? 0.8411 0.7920 0.8305 -0.0724 -0.0923 0.1011  470 THR C OG1 
6004  C CG2 . THR B 138 ? 0.7446 0.6539 0.7422 -0.0836 -0.0699 0.0874  470 THR C CG2 
6005  N N   . GLU B 139 ? 0.8615 0.7447 0.8511 -0.1086 -0.0839 0.1205  471 GLU C N   
6006  C CA  . GLU B 139 ? 0.8309 0.7247 0.8130 -0.1110 -0.0933 0.1321  471 GLU C CA  
6007  C C   . GLU B 139 ? 0.8594 0.7555 0.8144 -0.1312 -0.0876 0.1452  471 GLU C C   
6008  O O   . GLU B 139 ? 0.9239 0.7927 0.8773 -0.1452 -0.0754 0.1445  471 GLU C O   
6009  C CB  . GLU B 139 ? 0.8977 0.7607 0.9034 -0.1090 -0.0939 0.1284  471 GLU C CB  
6010  C CG  . GLU B 139 ? 0.9119 0.7838 0.9194 -0.1052 -0.1057 0.1364  471 GLU C CG  
6011  C CD  . GLU B 139 ? 1.0157 0.8534 1.0349 -0.1142 -0.1017 0.1382  471 GLU C CD  
6012  O OE1 . GLU B 139 ? 1.0979 0.9086 1.1430 -0.1075 -0.0987 0.1273  471 GLU C OE1 
6013  O OE2 . GLU B 139 ? 1.1154 0.9546 1.1186 -0.1271 -0.1025 0.1506  471 GLU C OE2 
6014  N N   . ILE B 140 ? 0.8514 0.7797 0.7848 -0.1330 -0.0959 0.1568  472 ILE C N   
6015  C CA  . ILE B 140 ? 0.8552 0.7876 0.7614 -0.1522 -0.0910 0.1700  472 ILE C CA  
6016  C C   . ILE B 140 ? 0.8608 0.7585 0.7725 -0.1659 -0.0844 0.1735  472 ILE C C   
6017  O O   . ILE B 140 ? 0.9418 0.8230 0.8740 -0.1592 -0.0884 0.1699  472 ILE C O   
6018  C CB  . ILE B 140 ? 0.8496 0.8190 0.7358 -0.1507 -0.1029 0.1822  472 ILE C CB  
6019  C CG1 . ILE B 140 ? 0.8848 0.8892 0.7600 -0.1413 -0.1074 0.1806  472 ILE C CG1 
6020  C CG2 . ILE B 140 ? 0.9712 0.9402 0.8335 -0.1701 -0.0992 0.1963  472 ILE C CG2 
6021  C CD1 . ILE B 140 ? 0.9337 0.9367 0.7957 -0.1508 -0.0967 0.1793  472 ILE C CD1 
6022  N N   . TYR B 141 ? 0.8422 0.7282 0.7365 -0.1849 -0.0744 0.1806  473 TYR C N   
6023  C CA  . TYR B 141 ? 0.8430 0.6952 0.7428 -0.1982 -0.0676 0.1837  473 TYR C CA  
6024  C C   . TYR B 141 ? 0.9361 0.7984 0.8218 -0.2060 -0.0747 0.1981  473 TYR C C   
6025  O O   . TYR B 141 ? 0.9979 0.8862 0.8587 -0.2126 -0.0778 0.2089  473 TYR C O   
6026  C CB  . TYR B 141 ? 0.8811 0.7113 0.7714 -0.2152 -0.0524 0.1834  473 TYR C CB  
6027  C CG  . TYR B 141 ? 0.8523 0.6438 0.7524 -0.2274 -0.0440 0.1838  473 TYR C CG  
6028  C CD1 . TYR B 141 ? 0.8909 0.6782 0.7765 -0.2421 -0.0437 0.1964  473 TYR C CD1 
6029  C CD2 . TYR B 141 ? 0.8943 0.6533 0.8189 -0.2239 -0.0367 0.1713  473 TYR C CD2 
6030  C CE1 . TYR B 141 ? 0.9108 0.6619 0.8062 -0.2533 -0.0359 0.1967  473 TYR C CE1 
6031  C CE2 . TYR B 141 ? 0.9473 0.6700 0.8819 -0.2350 -0.0288 0.1714  473 TYR C CE2 
6032  C CZ  . TYR B 141 ? 0.9377 0.6567 0.8578 -0.2496 -0.0285 0.1840  473 TYR C CZ  
6033  O OH  . TYR B 141 ? 0.9976 0.6806 0.9279 -0.2603 -0.0207 0.1839  473 TYR C OH  
6034  N N   . GLN B 142 ? 0.9932 0.8338 0.8953 -0.2054 -0.0771 0.1981  474 GLN C N   
6035  C CA  . GLN B 142 ? 0.9875 0.8337 0.8810 -0.2112 -0.0844 0.2104  474 GLN C CA  
6036  C C   . GLN B 142 ? 1.0558 0.8784 0.9372 -0.2327 -0.0738 0.2184  474 GLN C C   
6037  O O   . GLN B 142 ? 1.1039 0.8959 0.9997 -0.2376 -0.0699 0.2170  474 GLN C O   
6038  C CB  . GLN B 142 ? 1.2401 1.0739 1.1598 -0.1984 -0.0923 0.2051  474 GLN C CB  
6039  C CG  . GLN B 142 ? 1.2826 1.1176 1.2003 -0.2014 -0.1008 0.2157  474 GLN C CG  
6040  C CD  . GLN B 142 ? 1.3098 1.1830 1.2165 -0.1917 -0.1153 0.2229  474 GLN C CD  
6041  O OE1 . GLN B 142 ? 1.3608 1.2617 1.2438 -0.1958 -0.1170 0.2303  474 GLN C OE1 
6042  N NE2 . GLN B 142 ? 1.4240 1.2991 1.3486 -0.1779 -0.1258 0.2200  474 GLN C NE2 
6043  N N   . ALA B 143 ? 1.1702 1.0073 1.0245 -0.2458 -0.0692 0.2271  475 ALA C N   
6044  C CA  . ALA B 143 ? 1.1506 0.9657 0.9922 -0.2668 -0.0583 0.2345  475 ALA C CA  
6045  C C   . ALA B 143 ? 1.2082 1.0291 1.0363 -0.2761 -0.0640 0.2486  475 ALA C C   
6046  O O   . ALA B 143 ? 1.2247 1.0184 1.0553 -0.2887 -0.0577 0.2522  475 ALA C O   
6047  C CB  . ALA B 143 ? 1.1232 0.9474 0.9428 -0.2777 -0.0494 0.2368  475 ALA C CB  
6048  N N   . GLY B 144 ? 1.0859 0.9417 0.8996 -0.2706 -0.0756 0.2569  476 GLY C N   
6049  C CA  . GLY B 144 ? 1.3033 1.1653 1.1086 -0.2759 -0.0830 0.2689  476 GLY C CA  
6050  C C   . GLY B 144 ? 1.5568 1.4225 1.3826 -0.2593 -0.0951 0.2652  476 GLY C C   
6051  O O   . GLY B 144 ? 1.5671 1.4413 1.4081 -0.2427 -0.0999 0.2552  476 GLY C O   
6052  N N   . ASN B 145 ? 1.8639 1.7236 1.6904 -0.2636 -0.1003 0.2734  477 ASN C N   
6053  C CA  . ASN B 145 ? 1.9606 1.8181 1.8098 -0.2481 -0.1106 0.2685  477 ASN C CA  
6054  C C   . ASN B 145 ? 1.9134 1.8095 1.7585 -0.2321 -0.1247 0.2696  477 ASN C C   
6055  O O   . ASN B 145 ? 1.9986 1.8955 1.8645 -0.2161 -0.1329 0.2625  477 ASN C O   
6056  C CB  . ASN B 145 ? 2.0025 1.8438 1.8548 -0.2558 -0.1131 0.2765  477 ASN C CB  
6057  C CG  . ASN B 145 ? 2.2306 2.0586 2.1117 -0.2413 -0.1203 0.2688  477 ASN C CG  
6058  O OD1 . ASN B 145 ? 2.2474 2.0958 2.1305 -0.2305 -0.1331 0.2720  477 ASN C OD1 
6059  N ND2 . ASN B 145 ? 2.1965 1.9898 2.1001 -0.2412 -0.1119 0.2585  477 ASN C ND2 
6060  N N   . LYS B 146 ? 1.5904 1.5177 1.4096 -0.2361 -0.1276 0.2782  478 LYS C N   
6061  C CA  . LYS B 146 ? 1.5145 1.4794 1.3285 -0.2214 -0.1405 0.2793  478 LYS C CA  
6062  C C   . LYS B 146 ? 1.5160 1.4840 1.3490 -0.2041 -0.1416 0.2649  478 LYS C C   
6063  O O   . LYS B 146 ? 1.5446 1.4965 1.3832 -0.2065 -0.1311 0.2564  478 LYS C O   
6064  C CB  . LYS B 146 ? 1.4900 1.4849 1.2731 -0.2301 -0.1406 0.2894  478 LYS C CB  
6065  C CG  . LYS B 146 ? 1.4624 1.4601 1.2245 -0.2459 -0.1413 0.3046  478 LYS C CG  
6066  C CD  . LYS B 146 ? 1.2896 1.3265 1.0245 -0.2475 -0.1481 0.3150  478 LYS C CD  
6067  C CE  . LYS B 146 ? 1.1402 1.1830 0.8634 -0.2564 -0.1514 0.3254  478 LYS C CE  
6068  N NZ  . LYS B 146 ? 1.1438 1.2238 0.8645 -0.2437 -0.1619 0.3243  478 LYS C NZ  
6069  N N   . PRO B 147 ? 1.5053 1.4934 1.3485 -0.1866 -0.1540 0.2616  479 PRO C N   
6070  C CA  . PRO B 147 ? 1.4362 1.4252 1.2995 -0.1695 -0.1552 0.2474  479 PRO C CA  
6071  C C   . PRO B 147 ? 1.4654 1.4822 1.3134 -0.1662 -0.1543 0.2458  479 PRO C C   
6072  O O   . PRO B 147 ? 1.4677 1.5166 1.2947 -0.1669 -0.1611 0.2549  479 PRO C O   
6073  C CB  . PRO B 147 ? 1.4145 1.4166 1.2921 -0.1532 -0.1695 0.2463  479 PRO C CB  
6074  C CG  . PRO B 147 ? 1.5269 1.5208 1.3996 -0.1626 -0.1732 0.2573  479 PRO C CG  
6075  C CD  . PRO B 147 ? 1.5958 1.5953 1.4400 -0.1817 -0.1665 0.2691  479 PRO C CD  
6076  N N   . CYS B 148 ? 1.6108 1.6157 1.4696 -0.1625 -0.1460 0.2342  480 CYS C N   
6077  C CA  . CYS B 148 ? 1.5545 1.5837 1.4015 -0.1583 -0.1447 0.2312  480 CYS C CA  
6078  C C   . CYS B 148 ? 1.5125 1.5513 1.3796 -0.1374 -0.1509 0.2188  480 CYS C C   
6079  O O   . CYS B 148 ? 1.5618 1.5843 1.4437 -0.1329 -0.1437 0.2070  480 CYS C O   
6080  C CB  . CYS B 148 ? 1.5507 1.5623 1.3900 -0.1717 -0.1300 0.2287  480 CYS C CB  
6081  S SG  . CYS B 148 ? 1.9861 2.0139 1.7887 -0.1925 -0.1267 0.2458  480 CYS C SG  
6082  N N   . ASN B 149 ? 1.4037 1.4715 1.2694 -0.1250 -0.1643 0.2217  481 ASN C N   
6083  C CA  . ASN B 149 ? 1.3371 1.4175 1.2207 -0.1044 -0.1717 0.2108  481 ASN C CA  
6084  C C   . ASN B 149 ? 1.1721 1.2706 1.0467 -0.1012 -0.1675 0.2057  481 ASN C C   
6085  O O   . ASN B 149 ? 1.1272 1.2602 0.9877 -0.0952 -0.1748 0.2095  481 ASN C O   
6086  C CB  . ASN B 149 ? 1.3379 1.4465 1.2201 -0.0928 -0.1871 0.2161  481 ASN C CB  
6087  C CG  . ASN B 149 ? 1.4399 1.5322 1.3315 -0.0950 -0.1921 0.2211  481 ASN C CG  
6088  O OD1 . ASN B 149 ? 1.4654 1.5353 1.3518 -0.1104 -0.1852 0.2271  481 ASN C OD1 
6089  N ND2 . ASN B 149 ? 1.4378 1.5399 1.3442 -0.0793 -0.2040 0.2181  481 ASN C ND2 
6090  N N   . GLY B 150 ? 1.2100 1.2847 1.0936 -0.1047 -0.1557 0.1966  482 GLY C N   
6091  C CA  . GLY B 150 ? 1.1862 1.2760 1.0637 -0.1008 -0.1516 0.1906  482 GLY C CA  
6092  C C   . GLY B 150 ? 1.2824 1.3894 1.1300 -0.1152 -0.1470 0.2008  482 GLY C C   
6093  O O   . GLY B 150 ? 1.2020 1.3226 1.0422 -0.1134 -0.1432 0.1969  482 GLY C O   
6094  N N   . VAL B 151 ? 1.4632 1.5693 1.2941 -0.1296 -0.1471 0.2136  483 VAL C N   
6095  C CA  . VAL B 151 ? 1.3218 1.4446 1.1231 -0.1443 -0.1435 0.2249  483 VAL C CA  
6096  C C   . VAL B 151 ? 1.3056 1.4020 1.1029 -0.1593 -0.1284 0.2228  483 VAL C C   
6097  O O   . VAL B 151 ? 1.4101 1.4734 1.2175 -0.1679 -0.1215 0.2217  483 VAL C O   
6098  C CB  . VAL B 151 ? 1.3615 1.4900 1.1481 -0.1542 -0.1490 0.2391  483 VAL C CB  
6099  C CG1 . VAL B 151 ? 1.3017 1.4534 1.0578 -0.1665 -0.1474 0.2505  483 VAL C CG1 
6100  C CG2 . VAL B 151 ? 1.5195 1.6648 1.3157 -0.1396 -0.1634 0.2401  483 VAL C CG2 
6101  N N   . ALA B 152 ? 1.1675 1.2784 0.9492 -0.1635 -0.1232 0.2230  484 ALA C N   
6102  C CA  . ALA B 152 ? 1.1529 1.2417 0.9266 -0.1796 -0.1090 0.2228  484 ALA C CA  
6103  C C   . ALA B 152 ? 1.2077 1.3104 0.9519 -0.1963 -0.1080 0.2380  484 ALA C C   
6104  O O   . ALA B 152 ? 1.2051 1.3410 0.9303 -0.1951 -0.1132 0.2442  484 ALA C O   
6105  C CB  . ALA B 152 ? 1.0202 1.1135 0.7965 -0.1740 -0.1030 0.2128  484 ALA C CB  
6106  N N   . GLY B 153 ? 1.2343 1.3123 0.9750 -0.2115 -0.1020 0.2443  485 GLY C N   
6107  C CA  . GLY B 153 ? 1.2409 1.3325 0.9562 -0.2254 -0.1040 0.2596  485 GLY C CA  
6108  C C   . GLY B 153 ? 1.2107 1.2714 0.9223 -0.2438 -0.0947 0.2653  485 GLY C C   
6109  O O   . GLY B 153 ? 1.2337 1.2673 0.9512 -0.2515 -0.0827 0.2592  485 GLY C O   
6110  N N   . VAL B 154 ? 1.0707 1.1348 0.7781 -0.2482 -0.0989 0.2723  486 VAL C N   
6111  C CA  . VAL B 154 ? 1.0737 1.1088 0.7828 -0.2624 -0.0895 0.2730  486 VAL C CA  
6112  C C   . VAL B 154 ? 1.1421 1.1419 0.8682 -0.2642 -0.0883 0.2734  486 VAL C C   
6113  O O   . VAL B 154 ? 1.1743 1.1771 0.9183 -0.2494 -0.0976 0.2688  486 VAL C O   
6114  C CB  . VAL B 154 ? 0.8913 0.9379 0.5959 -0.2652 -0.0928 0.2763  486 VAL C CB  
6115  C CG1 . VAL B 154 ? 0.8311 0.9135 0.5293 -0.2582 -0.0953 0.2720  486 VAL C CG1 
6116  C CG2 . VAL B 154 ? 1.0208 1.0613 0.7300 -0.2635 -0.1029 0.2857  486 VAL C CG2 
6117  N N   . ASN B 155 ? 1.0947 1.0615 0.8247 -0.2769 -0.0756 0.2707  487 ASN C N   
6118  C CA  . ASN B 155 ? 1.1286 1.0589 0.8836 -0.2757 -0.0713 0.2629  487 ASN C CA  
6119  C C   . ASN B 155 ? 1.0175 0.9457 0.7993 -0.2555 -0.0756 0.2485  487 ASN C C   
6120  O O   . ASN B 155 ? 1.0930 0.9999 0.8978 -0.2489 -0.0774 0.2426  487 ASN C O   
6121  C CB  . ASN B 155 ? 1.2002 1.1240 0.9546 -0.2812 -0.0768 0.2726  487 ASN C CB  
6122  C CG  . ASN B 155 ? 1.2192 1.1353 0.9638 -0.2932 -0.0675 0.2724  487 ASN C CG  
6123  O OD1 . ASN B 155 ? 1.2528 1.1530 1.0009 -0.2965 -0.0550 0.2620  487 ASN C OD1 
6124  N ND2 . ASN B 155 ? 1.2454 1.1765 0.9816 -0.2944 -0.0738 0.2789  487 ASN C ND2 
6125  N N   . CYS B 156 ? 0.9792 0.9286 0.7579 -0.2462 -0.0766 0.2427  488 CYS C N   
6126  C CA  . CYS B 156 ? 1.0043 0.9639 0.8028 -0.2255 -0.0837 0.2312  488 CYS C CA  
6127  C C   . CYS B 156 ? 1.0174 0.9839 0.8136 -0.2221 -0.0773 0.2228  488 CYS C C   
6128  O O   . CYS B 156 ? 1.0711 1.0697 0.8500 -0.2195 -0.0814 0.2267  488 CYS C O   
6129  C CB  . CYS B 156 ? 1.0823 1.0772 0.8741 -0.2143 -0.0987 0.2375  488 CYS C CB  
6130  S SG  . CYS B 156 ? 1.3676 1.3539 1.1655 -0.2157 -0.1069 0.2456  488 CYS C SG  
6131  N N   . TYR B 157 ? 0.8761 0.8132 0.6901 -0.2218 -0.0676 0.2113  489 TYR C N   
6132  C CA  . TYR B 157 ? 0.9550 0.8949 0.7631 -0.2232 -0.0593 0.2051  489 TYR C CA  
6133  C C   . TYR B 157 ? 0.8885 0.8202 0.7220 -0.2065 -0.0592 0.1894  489 TYR C C   
6134  O O   . TYR B 157 ? 0.8947 0.7974 0.7513 -0.2029 -0.0565 0.1815  489 TYR C O   
6135  C CB  . TYR B 157 ? 0.9132 0.8264 0.7113 -0.2433 -0.0444 0.2074  489 TYR C CB  
6136  C CG  . TYR B 157 ? 0.9293 0.8390 0.7090 -0.2605 -0.0432 0.2216  489 TYR C CG  
6137  C CD1 . TYR B 157 ? 0.9051 0.8447 0.6573 -0.2676 -0.0473 0.2340  489 TYR C CD1 
6138  C CD2 . TYR B 157 ? 0.9330 0.8084 0.7224 -0.2705 -0.0371 0.2224  489 TYR C CD2 
6139  C CE1 . TYR B 157 ? 0.9765 0.9140 0.7140 -0.2812 -0.0463 0.2448  489 TYR C CE1 
6140  C CE2 . TYR B 157 ? 0.9458 0.8175 0.7183 -0.2866 -0.0358 0.2354  489 TYR C CE2 
6141  C CZ  . TYR B 157 ? 0.9841 0.8891 0.7348 -0.2872 -0.0403 0.2420  489 TYR C CZ  
6142  O OH  . TYR B 157 ? 0.9517 0.8581 0.6967 -0.2913 -0.0391 0.2434  489 TYR C OH  
6143  N N   . PHE B 158 ? 0.4913 0.9978 0.7431 -0.0487 -0.0966 0.1333  490 PHE C N   
6144  C CA  . PHE B 158 ? 0.4997 0.9807 0.7269 -0.0482 -0.0828 0.1128  490 PHE C CA  
6145  C C   . PHE B 158 ? 0.5336 0.9852 0.7578 -0.0556 -0.0852 0.1000  490 PHE C C   
6146  O O   . PHE B 158 ? 0.5408 0.9775 0.7649 -0.0552 -0.0897 0.1044  490 PHE C O   
6147  C CB  . PHE B 158 ? 0.4552 0.9278 0.6624 -0.0385 -0.0718 0.1140  490 PHE C CB  
6148  C CG  . PHE B 158 ? 0.5571 1.0088 0.7387 -0.0371 -0.0568 0.0944  490 PHE C CG  
6149  C CD1 . PHE B 158 ? 0.6207 1.0781 0.7988 -0.0403 -0.0516 0.0829  490 PHE C CD1 
6150  C CD2 . PHE B 158 ? 0.6647 1.0883 0.8257 -0.0335 -0.0484 0.0867  490 PHE C CD2 
6151  C CE1 . PHE B 158 ? 0.6699 1.1063 0.8240 -0.0397 -0.0380 0.0642  490 PHE C CE1 
6152  C CE2 . PHE B 158 ? 0.7398 1.1423 0.8768 -0.0328 -0.0348 0.0685  490 PHE C CE2 
6153  C CZ  . PHE B 158 ? 0.7196 1.1284 0.8532 -0.0361 -0.0296 0.0572  490 PHE C CZ  
6154  N N   . PRO B 159 ? 0.5262 0.9687 0.7476 -0.0623 -0.0823 0.0838  491 PRO C N   
6155  C CA  . PRO B 159 ? 0.5631 0.9844 0.7882 -0.0701 -0.0878 0.0747  491 PRO C CA  
6156  C C   . PRO B 159 ? 0.5894 0.9769 0.7940 -0.0690 -0.0797 0.0634  491 PRO C C   
6157  O O   . PRO B 159 ? 0.6064 0.9750 0.8133 -0.0745 -0.0846 0.0572  491 PRO C O   
6158  C CB  . PRO B 159 ? 0.6254 1.0507 0.8531 -0.0767 -0.0856 0.0611  491 PRO C CB  
6159  C CG  . PRO B 159 ? 0.6044 1.0393 0.8186 -0.0718 -0.0737 0.0566  491 PRO C CG  
6160  C CD  . PRO B 159 ? 0.5279 0.9826 0.7455 -0.0633 -0.0754 0.0748  491 PRO C CD  
6161  N N   . LEU B 160 ? 0.5799 0.9585 0.7642 -0.0620 -0.0677 0.0603  492 LEU C N   
6162  C CA  . LEU B 160 ? 0.6375 0.9835 0.8016 -0.0608 -0.0599 0.0499  492 LEU C CA  
6163  C C   . LEU B 160 ? 0.6825 1.0249 0.8456 -0.0542 -0.0637 0.0639  492 LEU C C   
6164  O O   . LEU B 160 ? 0.7398 1.1022 0.9068 -0.0474 -0.0647 0.0780  492 LEU C O   
6165  C CB  . LEU B 160 ? 0.6478 0.9811 0.7877 -0.0580 -0.0437 0.0350  492 LEU C CB  
6166  C CG  . LEU B 160 ? 0.5567 0.8835 0.6939 -0.0660 -0.0391 0.0174  492 LEU C CG  
6167  C CD1 . LEU B 160 ? 0.6688 1.0245 0.8159 -0.0653 -0.0403 0.0221  492 LEU C CD1 
6168  C CD2 . LEU B 160 ? 0.4934 0.7959 0.6047 -0.0651 -0.0241 0.0007  492 LEU C CD2 
6169  N N   . GLN B 161 ? 0.7033 1.0209 0.8619 -0.0563 -0.0665 0.0602  493 GLN C N   
6170  C CA  . GLN B 161 ? 0.6967 1.0051 0.8507 -0.0504 -0.0688 0.0705  493 GLN C CA  
6171  C C   . GLN B 161 ? 0.7005 0.9771 0.8278 -0.0476 -0.0560 0.0567  493 GLN C C   
6172  O O   . GLN B 161 ? 0.6285 0.8861 0.7443 -0.0525 -0.0487 0.0395  493 GLN C O   
6173  C CB  . GLN B 161 ? 0.7093 1.0134 0.8794 -0.0546 -0.0838 0.0790  493 GLN C CB  
6174  C CG  . GLN B 161 ? 0.8343 1.1411 1.0074 -0.0483 -0.0899 0.0954  493 GLN C CG  
6175  C CD  . GLN B 161 ? 0.9659 1.3076 1.1592 -0.0457 -0.0984 0.1149  493 GLN C CD  
6176  O OE1 . GLN B 161 ? 0.8710 1.2353 1.0739 -0.0476 -0.0982 0.1157  493 GLN C OE1 
6177  N NE2 . GLN B 161 ? 0.9003 1.2474 1.0999 -0.0410 -0.1056 0.1311  493 GLN C NE2 
6178  N N   . SER B 162 ? 0.6929 0.9641 0.8103 -0.0396 -0.0534 0.0647  494 SER C N   
6179  C CA  . SER B 162 ? 0.6453 0.8864 0.7367 -0.0360 -0.0415 0.0532  494 SER C CA  
6180  C C   . SER B 162 ? 0.6489 0.8701 0.7397 -0.0359 -0.0484 0.0572  494 SER C C   
6181  O O   . SER B 162 ? 0.6447 0.8792 0.7506 -0.0337 -0.0598 0.0737  494 SER C O   
6182  C CB  . SER B 162 ? 0.6899 0.9362 0.7658 -0.0261 -0.0308 0.0565  494 SER C CB  
6183  O OG  . SER B 162 ? 0.6750 0.9475 0.7649 -0.0199 -0.0381 0.0761  494 SER C OG  
6184  N N   . TYR B 163 ? 0.7142 0.9040 0.7883 -0.0389 -0.0419 0.0420  495 TYR C N   
6185  C CA  . TYR B 163 ? 0.6861 0.8540 0.7565 -0.0385 -0.0474 0.0442  495 TYR C CA  
6186  C C   . TYR B 163 ? 0.7651 0.9315 0.8242 -0.0284 -0.0435 0.0537  495 TYR C C   
6187  O O   . TYR B 163 ? 0.8098 0.9744 0.8523 -0.0229 -0.0311 0.0489  495 TYR C O   
6188  C CB  . TYR B 163 ? 0.6520 0.7859 0.7046 -0.0428 -0.0398 0.0260  495 TYR C CB  
6189  C CG  . TYR B 163 ? 0.6274 0.7581 0.6863 -0.0523 -0.0403 0.0131  495 TYR C CG  
6190  C CD1 . TYR B 163 ? 0.6330 0.7884 0.7135 -0.0572 -0.0487 0.0175  495 TYR C CD1 
6191  C CD2 . TYR B 163 ? 0.7041 0.8057 0.7513 -0.0565 -0.0367 -0.0003 495 TYR C CD2 
6192  C CE1 . TYR B 163 ? 0.6369 0.7882 0.7229 -0.0654 -0.0495 0.0058  495 TYR C CE1 
6193  C CE2 . TYR B 163 ? 0.6540 0.7525 0.7086 -0.0649 -0.0386 -0.0109 495 TYR C CE2 
6194  C CZ  . TYR B 163 ? 0.6004 0.7247 0.6751 -0.0692 -0.0455 -0.0073 495 TYR C CZ  
6195  O OH  . TYR B 163 ? 0.6507 0.7745 0.7341 -0.0772 -0.0477 -0.0171 495 TYR C OH  
6196  N N   . GLY B 164 ? 0.9160 1.0844 0.9846 -0.0258 -0.0545 0.0677  496 GLY C N   
6197  C CA  . GLY B 164 ? 0.9386 1.1095 0.9985 -0.0159 -0.0512 0.0780  496 GLY C CA  
6198  C C   . GLY B 164 ? 0.9788 1.1158 1.0128 -0.0118 -0.0418 0.0684  496 GLY C C   
6199  O O   . GLY B 164 ? 1.0830 1.2144 1.1150 -0.0064 -0.0463 0.0781  496 GLY C O   
6200  N N   . PHE B 165 ? 0.7894 0.9041 0.8038 -0.0144 -0.0293 0.0499  497 PHE C N   
6201  C CA  . PHE B 165 ? 0.7495 0.8283 0.7437 -0.0145 -0.0239 0.0389  497 PHE C CA  
6202  C C   . PHE B 165 ? 0.8380 0.9059 0.8159 -0.0044 -0.0192 0.0449  497 PHE C C   
6203  O O   . PHE B 165 ? 0.8922 0.9670 0.8594 0.0026  -0.0099 0.0461  497 PHE C O   
6204  C CB  . PHE B 165 ? 0.7715 0.8302 0.7475 -0.0189 -0.0104 0.0188  497 PHE C CB  
6205  C CG  . PHE B 165 ? 0.7469 0.8013 0.7329 -0.0294 -0.0146 0.0089  497 PHE C CG  
6206  C CD1 . PHE B 165 ? 0.7182 0.7625 0.7131 -0.0333 -0.0255 0.0113  497 PHE C CD1 
6207  C CD2 . PHE B 165 ? 0.7040 0.7593 0.6863 -0.0350 -0.0061 -0.0047 497 PHE C CD2 
6208  C CE1 . PHE B 165 ? 0.6367 0.6757 0.6393 -0.0422 -0.0287 0.0017  497 PHE C CE1 
6209  C CE2 . PHE B 165 ? 0.6268 0.6770 0.6170 -0.0441 -0.0090 -0.0143 497 PHE C CE2 
6210  C CZ  . PHE B 165 ? 0.6501 0.6917 0.6500 -0.0474 -0.0201 -0.0111 497 PHE C CZ  
6211  N N   . ARG B 166 ? 0.7747 0.8243 0.7501 -0.0035 -0.0257 0.0483  498 ARG C N   
6212  C CA  . ARG B 166 ? 0.7429 0.7829 0.7075 0.0056  -0.0256 0.0571  498 ARG C CA  
6213  C C   . ARG B 166 ? 0.7169 0.7219 0.6666 0.0042  -0.0256 0.0490  498 ARG C C   
6214  O O   . ARG B 166 ? 0.7197 0.7200 0.6813 -0.0020 -0.0366 0.0498  498 ARG C O   
6215  C CB  . ARG B 166 ? 0.7370 0.8041 0.7248 0.0085  -0.0403 0.0782  498 ARG C CB  
6216  C CG  . ARG B 166 ? 0.7847 0.8844 0.7815 0.0149  -0.0386 0.0906  498 ARG C CG  
6217  C CD  . ARG B 166 ? 0.7363 0.8630 0.7586 0.0162  -0.0544 0.1119  498 ARG C CD  
6218  N NE  . ARG B 166 ? 0.8117 0.9724 0.8554 0.0133  -0.0590 0.1197  498 ARG C NE  
6219  C CZ  . ARG B 166 ? 0.8195 1.0037 0.8641 0.0194  -0.0526 0.1258  498 ARG C CZ  
6220  N NH1 . ARG B 166 ? 0.8313 1.0121 0.8591 0.0297  -0.0430 0.1278  498 ARG C NH1 
6221  N NH2 . ARG B 166 ? 0.7379 0.9499 0.8004 0.0155  -0.0562 0.1303  498 ARG C NH2 
6222  N N   . PRO B 167 ? 0.6821 0.6626 0.6064 0.0104  -0.0145 0.0423  499 PRO C N   
6223  C CA  . PRO B 167 ? 0.6809 0.6256 0.5880 0.0080  -0.0117 0.0310  499 PRO C CA  
6224  C C   . PRO B 167 ? 0.7209 0.6595 0.6388 0.0066  -0.0265 0.0394  499 PRO C C   
6225  O O   . PRO B 167 ? 0.7452 0.6577 0.6541 0.0024  -0.0267 0.0297  499 PRO C O   
6226  C CB  . PRO B 167 ? 0.6710 0.5964 0.5514 0.0170  0.0011  0.0273  499 PRO C CB  
6227  C CG  . PRO B 167 ? 0.7053 0.6570 0.5931 0.0253  -0.0004 0.0419  499 PRO C CG  
6228  C CD  . PRO B 167 ? 0.6893 0.6733 0.5993 0.0205  -0.0048 0.0461  499 PRO C CD  
6229  N N   . THR B 168 ? 0.7446 0.7066 0.6816 0.0098  -0.0391 0.0574  500 THR C N   
6230  C CA  . THR B 168 ? 0.6507 0.6079 0.5968 0.0102  -0.0536 0.0680  500 THR C CA  
6231  C C   . THR B 168 ? 0.6804 0.6500 0.6510 0.0014  -0.0687 0.0721  500 THR C C   
6232  O O   . THR B 168 ? 0.6679 0.6406 0.6514 0.0013  -0.0833 0.0838  500 THR C O   
6233  C CB  . THR B 168 ? 0.5244 0.5005 0.4769 0.0191  -0.0583 0.0859  500 THR C CB  
6234  O OG1 . THR B 168 ? 0.5144 0.5269 0.4938 0.0171  -0.0681 0.0996  500 THR C OG1 
6235  C CG2 . THR B 168 ? 0.5622 0.5362 0.4950 0.0275  -0.0426 0.0823  500 THR C CG2 
6236  N N   . TYR B 169 ? 0.6546 0.6307 0.6315 -0.0059 -0.0656 0.0625  501 TYR C N   
6237  C CA  . TYR B 169 ? 0.6032 0.5931 0.6029 -0.0141 -0.0782 0.0650  501 TYR C CA  
6238  C C   . TYR B 169 ? 0.6126 0.5747 0.6067 -0.0191 -0.0831 0.0557  501 TYR C C   
6239  O O   . TYR B 169 ? 0.6628 0.5954 0.6344 -0.0174 -0.0740 0.0442  501 TYR C O   
6240  C CB  . TYR B 169 ? 0.6083 0.6141 0.6138 -0.0190 -0.0710 0.0570  501 TYR C CB  
6241  C CG  . TYR B 169 ? 0.6041 0.6463 0.6274 -0.0170 -0.0739 0.0701  501 TYR C CG  
6242  C CD1 . TYR B 169 ? 0.6342 0.6913 0.6617 -0.0095 -0.0776 0.0859  501 TYR C CD1 
6243  C CD2 . TYR B 169 ? 0.6021 0.6629 0.6348 -0.0217 -0.0707 0.0655  501 TYR C CD2 
6244  C CE1 . TYR B 169 ? 0.6573 0.7487 0.7007 -0.0071 -0.0794 0.0982  501 TYR C CE1 
6245  C CE2 . TYR B 169 ? 0.6476 0.7412 0.6949 -0.0194 -0.0724 0.0771  501 TYR C CE2 
6246  C CZ  . TYR B 169 ? 0.6119 0.7212 0.6645 -0.0120 -0.0765 0.0934  501 TYR C CZ  
6247  O OH  . TYR B 169 ? 0.5782 0.7213 0.6455 -0.0098 -0.0775 0.1046  501 TYR C OH  
6248  N N   . GLY B 170 ? 0.6022 0.5737 0.6167 -0.0252 -0.0976 0.0607  502 GLY C N   
6249  C CA  . GLY B 170 ? 0.6198 0.5670 0.6298 -0.0303 -0.1016 0.0503  502 GLY C CA  
6250  C C   . GLY B 170 ? 0.6370 0.5694 0.6317 -0.0338 -0.0863 0.0312  502 GLY C C   
6251  O O   . GLY B 170 ? 0.6886 0.6345 0.6819 -0.0340 -0.0758 0.0271  502 GLY C O   
6252  N N   . VAL B 171 ? 0.6831 0.5868 0.6649 -0.0363 -0.0845 0.0192  503 VAL C N   
6253  C CA  . VAL B 171 ? 0.6735 0.5661 0.6446 -0.0411 -0.0714 0.0015  503 VAL C CA  
6254  C C   . VAL B 171 ? 0.6746 0.5906 0.6668 -0.0480 -0.0763 0.0006  503 VAL C C   
6255  O O   . VAL B 171 ? 0.6549 0.5765 0.6442 -0.0514 -0.0652 -0.0097 503 VAL C O   
6256  C CB  . VAL B 171 ? 0.6614 0.5194 0.6148 -0.0422 -0.0683 -0.0106 503 VAL C CB  
6257  C CG1 . VAL B 171 ? 0.7311 0.5829 0.6807 -0.0485 -0.0590 -0.0265 503 VAL C CG1 
6258  C CG2 . VAL B 171 ? 0.7864 0.6208 0.7137 -0.0358 -0.0564 -0.0146 503 VAL C CG2 
6259  N N   . GLY B 172 ? 0.5815 0.5125 0.5955 -0.0503 -0.0933 0.0119  504 GLY C N   
6260  C CA  . GLY B 172 ? 0.6610 0.6161 0.6958 -0.0563 -0.0986 0.0127  504 GLY C CA  
6261  C C   . GLY B 172 ? 0.6267 0.6075 0.6667 -0.0557 -0.0906 0.0150  504 GLY C C   
6262  O O   . GLY B 172 ? 0.7367 0.7317 0.7860 -0.0608 -0.0882 0.0092  504 GLY C O   
6263  N N   . HIS B 173 ? 0.5786 0.5646 0.6111 -0.0492 -0.0853 0.0222  505 HIS C N   
6264  C CA  . HIS B 173 ? 0.5669 0.5822 0.6088 -0.0476 -0.0820 0.0291  505 HIS C CA  
6265  C C   . HIS B 173 ? 0.6067 0.6136 0.6268 -0.0437 -0.0638 0.0195  505 HIS C C   
6266  O O   . HIS B 173 ? 0.6223 0.6498 0.6452 -0.0403 -0.0595 0.0253  505 HIS C O   
6267  C CB  . HIS B 173 ? 0.6536 0.6880 0.7093 -0.0428 -0.0936 0.0491  505 HIS C CB  
6268  C CG  . HIS B 173 ? 0.6714 0.7277 0.7540 -0.0472 -0.1107 0.0613  505 HIS C CG  
6269  N ND1 . HIS B 173 ? 0.5367 0.6263 0.6383 -0.0480 -0.1146 0.0714  505 HIS C ND1 
6270  C CD2 . HIS B 173 ? 0.7410 0.7907 0.8344 -0.0500 -0.1259 0.0671  505 HIS C CD2 
6271  C CE1 . HIS B 173 ? 0.5925 0.6951 0.7158 -0.0518 -0.1312 0.0827  505 HIS C CE1 
6272  N NE2 . HIS B 173 ? 0.6303 0.7088 0.7491 -0.0532 -0.1385 0.0798  505 HIS C NE2 
6273  N N   . GLN B 174 ? 0.5702 0.5470 0.5682 -0.0435 -0.0536 0.0061  506 GLN C N   
6274  C CA  . GLN B 174 ? 0.6045 0.5664 0.5784 -0.0395 -0.0367 -0.0035 506 GLN C CA  
6275  C C   . GLN B 174 ? 0.7367 0.7016 0.7071 -0.0451 -0.0254 -0.0179 506 GLN C C   
6276  O O   . GLN B 174 ? 0.7225 0.6901 0.7035 -0.0525 -0.0290 -0.0245 506 GLN C O   
6277  C CB  . GLN B 174 ? 0.6759 0.6026 0.6286 -0.0376 -0.0322 -0.0112 506 GLN C CB  
6278  C CG  . GLN B 174 ? 0.7724 0.6938 0.7211 -0.0298 -0.0383 0.0015  506 GLN C CG  
6279  C CD  . GLN B 174 ? 0.7509 0.6366 0.6767 -0.0270 -0.0334 -0.0057 506 GLN C CD  
6280  O OE1 . GLN B 174 ? 0.7864 0.6496 0.6960 -0.0302 -0.0229 -0.0209 506 GLN C OE1 
6281  N NE2 . GLN B 174 ? 0.7311 0.6122 0.6565 -0.0213 -0.0418 0.0057  506 GLN C NE2 
6282  N N   . PRO B 175 ? 0.7015 0.6661 0.6571 -0.0420 -0.0119 -0.0234 507 PRO C N   
6283  C CA  . PRO B 175 ? 0.6484 0.6132 0.5995 -0.0479 -0.0014 -0.0379 507 PRO C CA  
6284  C C   . PRO B 175 ? 0.7083 0.6445 0.6467 -0.0536 0.0047  -0.0536 507 PRO C C   
6285  O O   . PRO B 175 ? 0.7753 0.6843 0.6948 -0.0507 0.0101  -0.0580 507 PRO C O   
6286  C CB  . PRO B 175 ? 0.6574 0.6224 0.5914 -0.0420 0.0114  -0.0398 507 PRO C CB  
6287  C CG  . PRO B 175 ? 0.6498 0.6024 0.5717 -0.0332 0.0111  -0.0312 507 PRO C CG  
6288  C CD  . PRO B 175 ? 0.7013 0.6657 0.6435 -0.0329 -0.0056 -0.0168 507 PRO C CD  
6289  N N   . TYR B 176 ? 0.7275 0.6705 0.6770 -0.0616 0.0036  -0.0617 508 TYR C N   
6290  C CA  . TYR B 176 ? 0.7435 0.6632 0.6808 -0.0675 0.0122  -0.0780 508 TYR C CA  
6291  C C   . TYR B 176 ? 0.7521 0.6818 0.6891 -0.0728 0.0218  -0.0888 508 TYR C C   
6292  O O   . TYR B 176 ? 0.6862 0.6422 0.6425 -0.0760 0.0157  -0.0853 508 TYR C O   
6293  C CB  . TYR B 176 ? 0.7688 0.6861 0.7198 -0.0726 0.0019  -0.0791 508 TYR C CB  
6294  C CG  . TYR B 176 ? 0.7817 0.6810 0.7289 -0.0690 -0.0059 -0.0733 508 TYR C CG  
6295  C CD1 . TYR B 176 ? 0.7518 0.6636 0.7109 -0.0641 -0.0189 -0.0571 508 TYR C CD1 
6296  C CD2 . TYR B 176 ? 0.8317 0.7015 0.7636 -0.0707 -0.0006 -0.0841 508 TYR C CD2 
6297  C CE1 . TYR B 176 ? 0.8508 0.7451 0.8063 -0.0611 -0.0269 -0.0520 508 TYR C CE1 
6298  C CE2 . TYR B 176 ? 0.9286 0.7808 0.8561 -0.0673 -0.0081 -0.0793 508 TYR C CE2 
6299  C CZ  . TYR B 176 ? 0.9152 0.7794 0.8545 -0.0626 -0.0216 -0.0634 508 TYR C CZ  
6300  O OH  . TYR B 176 ? 0.8633 0.7087 0.7974 -0.0594 -0.0293 -0.0592 508 TYR C OH  
6301  N N   . ARG B 177 ? 0.7777 0.6860 0.6930 -0.0741 0.0364  -0.1020 509 ARG C N   
6302  C CA  . ARG B 177 ? 0.6908 0.6062 0.6049 -0.0800 0.0456  -0.1135 509 ARG C CA  
6303  C C   . ARG B 177 ? 0.7364 0.6442 0.6565 -0.0885 0.0454  -0.1243 509 ARG C C   
6304  O O   . ARG B 177 ? 0.8194 0.7051 0.7321 -0.0889 0.0451  -0.1277 509 ARG C O   
6305  C CB  . ARG B 177 ? 0.6792 0.5768 0.5679 -0.0780 0.0613  -0.1225 509 ARG C CB  
6306  C CG  . ARG B 177 ? 0.7133 0.6006 0.5874 -0.0682 0.0627  -0.1138 509 ARG C CG  
6307  C CD  . ARG B 177 ? 0.7566 0.6260 0.6045 -0.0638 0.0767  -0.1198 509 ARG C CD  
6308  N NE  . ARG B 177 ? 0.7473 0.6356 0.5949 -0.0600 0.0799  -0.1164 509 ARG C NE  
6309  C CZ  . ARG B 177 ? 0.7972 0.6731 0.6234 -0.0566 0.0918  -0.1224 509 ARG C CZ  
6310  N NH1 . ARG B 177 ? 0.9335 0.7789 0.7373 -0.0584 0.1028  -0.1339 509 ARG C NH1 
6311  N NH2 . ARG B 177 ? 0.7668 0.6606 0.5931 -0.0506 0.0924  -0.1158 509 ARG C NH2 
6312  N N   . VAL B 178 ? 0.6878 0.6161 0.6230 -0.0948 0.0441  -0.1286 510 VAL C N   
6313  C CA  . VAL B 178 ? 0.7214 0.6464 0.6645 -0.1028 0.0436  -0.1386 510 VAL C CA  
6314  C C   . VAL B 178 ? 0.7432 0.6724 0.6826 -0.1092 0.0543  -0.1513 510 VAL C C   
6315  O O   . VAL B 178 ? 0.7724 0.7186 0.7137 -0.1084 0.0566  -0.1496 510 VAL C O   
6316  C CB  . VAL B 178 ? 0.6418 0.5887 0.6114 -0.1051 0.0285  -0.1311 510 VAL C CB  
6317  C CG1 . VAL B 178 ? 0.6764 0.6134 0.6490 -0.1013 0.0182  -0.1226 510 VAL C CG1 
6318  C CG2 . VAL B 178 ? 0.7011 0.6775 0.6855 -0.1031 0.0220  -0.1208 510 VAL C CG2 
6319  N N   . VAL B 179 ? 0.7728 0.6863 0.7071 -0.1156 0.0607  -0.1640 511 VAL C N   
6320  C CA  . VAL B 179 ? 0.8050 0.7213 0.7379 -0.1233 0.0700  -0.1771 511 VAL C CA  
6321  C C   . VAL B 179 ? 0.8354 0.7547 0.7825 -0.1301 0.0660  -0.1834 511 VAL C C   
6322  O O   . VAL B 179 ? 0.8760 0.7767 0.8184 -0.1300 0.0655  -0.1856 511 VAL C O   
6323  C CB  . VAL B 179 ? 0.8017 0.6911 0.7084 -0.1243 0.0855  -0.1879 511 VAL C CB  
6324  C CG1 . VAL B 179 ? 0.8559 0.7513 0.7630 -0.1325 0.0939  -0.2003 511 VAL C CG1 
6325  C CG2 . VAL B 179 ? 0.8123 0.6965 0.7039 -0.1163 0.0888  -0.1811 511 VAL C CG2 
6326  N N   . VAL B 180 ? 0.8123 0.7551 0.7762 -0.1355 0.0632  -0.1861 512 VAL C N   
6327  C CA  . VAL B 180 ? 0.8016 0.7520 0.7811 -0.1419 0.0594  -0.1922 512 VAL C CA  
6328  C C   . VAL B 180 ? 0.8958 0.8442 0.8698 -0.1499 0.0713  -0.2067 512 VAL C C   
6329  O O   . VAL B 180 ? 0.9047 0.8681 0.8805 -0.1519 0.0742  -0.2084 512 VAL C O   
6330  C CB  . VAL B 180 ? 0.7632 0.7438 0.7681 -0.1418 0.0455  -0.1830 512 VAL C CB  
6331  C CG1 . VAL B 180 ? 0.8116 0.7982 0.8316 -0.1475 0.0410  -0.1889 512 VAL C CG1 
6332  C CG2 . VAL B 180 ? 0.8148 0.7986 0.8250 -0.1344 0.0338  -0.1680 512 VAL C CG2 
6333  N N   . LEU B 181 ? 0.9399 0.8696 0.9069 -0.1543 0.0780  -0.2168 513 LEU C N   
6334  C CA  . LEU B 181 ? 0.9349 0.8672 0.9017 -0.1577 0.0867  -0.2226 513 LEU C CA  
6335  C C   . LEU B 181 ? 1.0208 0.9739 1.0102 -0.1615 0.0795  -0.2235 513 LEU C C   
6336  O O   . LEU B 181 ? 1.0566 1.0061 1.0529 -0.1596 0.0738  -0.2210 513 LEU C O   
6337  C CB  . LEU B 181 ? 0.9245 0.8337 0.8761 -0.1536 0.0952  -0.2212 513 LEU C CB  
6338  C CG  . LEU B 181 ? 0.8726 0.7615 0.8030 -0.1486 0.1005  -0.2186 513 LEU C CG  
6339  C CD1 . LEU B 181 ? 0.9240 0.7939 0.8425 -0.1453 0.1074  -0.2167 513 LEU C CD1 
6340  C CD2 . LEU B 181 ? 0.9064 0.8022 0.8306 -0.1508 0.1068  -0.2218 513 LEU C CD2 
6341  N N   . SER B 182 ? 1.0570 1.0316 1.0570 -0.1664 0.0794  -0.2269 514 SER C N   
6342  C CA  . SER B 182 ? 1.0873 1.0831 1.1078 -0.1697 0.0740  -0.2278 514 SER C CA  
6343  C C   . SER B 182 ? 1.1489 1.1401 1.1646 -0.1712 0.0847  -0.2323 514 SER C C   
6344  O O   . SER B 182 ? 1.1111 1.1023 1.1185 -0.1737 0.0932  -0.2359 514 SER C O   
6345  C CB  . SER B 182 ? 1.1056 1.1279 1.1400 -0.1736 0.0676  -0.2280 514 SER C CB  
6346  O OG  . SER B 182 ? 1.2522 1.2940 1.3020 -0.1766 0.0661  -0.2298 514 SER C OG  
6347  N N   . PHE B 183 ? 1.1970 1.1837 1.2174 -0.1699 0.0842  -0.2318 515 PHE C N   
6348  C CA  . PHE B 183 ? 1.2757 1.2602 1.2947 -0.1720 0.0931  -0.2356 515 PHE C CA  
6349  C C   . PHE B 183 ? 1.3890 1.3962 1.4279 -0.1751 0.0883  -0.2378 515 PHE C C   
6350  O O   . PHE B 183 ? 1.3674 1.3762 1.4152 -0.1733 0.0836  -0.2368 515 PHE C O   
6351  C CB  . PHE B 183 ? 1.2456 1.2101 1.2559 -0.1681 0.0957  -0.2337 515 PHE C CB  
6352  C CG  . PHE B 183 ? 1.2479 1.1900 1.2378 -0.1652 0.1028  -0.2318 515 PHE C CG  
6353  C CD1 . PHE B 183 ? 1.2691 1.2087 1.2487 -0.1672 0.1101  -0.2333 515 PHE C CD1 
6354  C CD2 . PHE B 183 ? 1.2596 1.1828 1.2403 -0.1598 0.1011  -0.2279 515 PHE C CD2 
6355  C CE1 . PHE B 183 ? 1.3287 1.2470 1.2890 -0.1638 0.1163  -0.2308 515 PHE C CE1 
6356  C CE2 . PHE B 183 ? 1.3559 1.2586 1.3176 -0.1564 0.1071  -0.2253 515 PHE C CE2 
6357  C CZ  . PHE B 183 ? 1.3466 1.2468 1.2981 -0.1583 0.1147  -0.2266 515 PHE C CZ  
6358  N N   . GLU B 184 ? 1.4773 1.5018 1.5227 -0.1791 0.0894  -0.2408 516 GLU C N   
6359  C CA  . GLU B 184 ? 1.6266 1.6710 1.6889 -0.1816 0.0865  -0.2430 516 GLU C CA  
6360  C C   . GLU B 184 ? 1.7054 1.7447 1.7632 -0.1848 0.0978  -0.2482 516 GLU C C   
6361  O O   . GLU B 184 ? 1.6946 1.7199 1.7375 -0.1862 0.1074  -0.2499 516 GLU C O   
6362  C CB  . GLU B 184 ? 1.6589 1.7255 1.7313 -0.1843 0.0819  -0.2435 516 GLU C CB  
6363  C CG  . GLU B 184 ? 1.6848 1.7520 1.7488 -0.1887 0.0921  -0.2490 516 GLU C CG  
6364  C CD  . GLU B 184 ? 1.7089 1.7959 1.7796 -0.1910 0.0880  -0.2496 516 GLU C CD  
6365  O OE1 . GLU B 184 ? 1.7610 1.8683 1.8483 -0.1910 0.0802  -0.2481 516 GLU C OE1 
6366  O OE2 . GLU B 184 ? 1.6591 1.7411 1.7176 -0.1925 0.0930  -0.2517 516 GLU C OE2 
6367  N N   . LEU B 185 ? 1.8668 1.9179 1.9379 -0.1857 0.0961  -0.2502 517 LEU C N   
6368  C CA  . LEU B 185 ? 1.9449 1.9957 2.0148 -0.1899 0.1063  -0.2556 517 LEU C CA  
6369  C C   . LEU B 185 ? 1.9497 2.0233 2.0374 -0.1918 0.1021  -0.2582 517 LEU C C   
6370  O O   . LEU B 185 ? 1.9734 2.0535 2.0724 -0.1889 0.0946  -0.2564 517 LEU C O   
6371  C CB  . LEU B 185 ? 1.9405 1.9742 2.0034 -0.1882 0.1115  -0.2557 517 LEU C CB  
6372  C CG  . LEU B 185 ? 1.9299 1.9661 1.9962 -0.1922 0.1201  -0.2609 517 LEU C CG  
6373  C CD1 . LEU B 185 ? 1.9343 1.9648 1.9901 -0.1976 0.1315  -0.2642 517 LEU C CD1 
6374  C CD2 . LEU B 185 ? 1.8333 1.8549 1.8953 -0.1891 0.1216  -0.2598 517 LEU C CD2 
6375  N N   . LEU B 186 ? 1.8646 1.9495 1.9541 -0.1964 0.1065  -0.2622 518 LEU C N   
6376  C CA  . LEU B 186 ? 1.9121 2.0174 2.0171 -0.1981 0.1036  -0.2650 518 LEU C CA  
6377  C C   . LEU B 186 ? 1.9851 2.0925 2.0863 -0.2043 0.1142  -0.2713 518 LEU C C   
6378  O O   . LEU B 186 ? 2.0369 2.1287 2.1250 -0.2070 0.1238  -0.2732 518 LEU C O   
6379  C CB  . LEU B 186 ? 1.8486 1.9716 1.9644 -0.1959 0.0920  -0.2610 518 LEU C CB  
6380  C CG  . LEU B 186 ? 1.7602 1.8914 1.8730 -0.1978 0.0912  -0.2610 518 LEU C CG  
6381  C CD1 . LEU B 186 ? 1.6057 1.7567 1.7331 -0.1949 0.0787  -0.2560 518 LEU C CD1 
6382  C CD2 . LEU B 186 ? 1.7038 1.8200 1.8021 -0.1972 0.0935  -0.2591 518 LEU C CD2 
6383  N N   . HIS B 187 ? 2.0024 2.1288 2.1149 -0.2065 0.1119  -0.2741 519 HIS C N   
6384  C CA  . HIS B 187 ? 2.0186 2.1491 2.1307 -0.2126 0.1208  -0.2806 519 HIS C CA  
6385  C C   . HIS B 187 ? 2.1272 2.2517 2.2271 -0.2168 0.1272  -0.2827 519 HIS C C   
6386  O O   . HIS B 187 ? 2.0364 2.1600 2.1332 -0.2223 0.1356  -0.2877 519 HIS C O   
6387  C CB  . HIS B 187 ? 1.9190 2.0712 2.0466 -0.2129 0.1152  -0.2824 519 HIS C CB  
6388  C CG  . HIS B 187 ? 1.9053 2.0627 2.0444 -0.2103 0.1120  -0.2824 519 HIS C CG  
6389  N ND1 . HIS B 187 ? 1.8843 2.0309 2.0204 -0.2115 0.1194  -0.2852 519 HIS C ND1 
6390  C CD2 . HIS B 187 ? 1.8857 2.0575 2.0388 -0.2064 0.1020  -0.2797 519 HIS C CD2 
6391  C CE1 . HIS B 187 ? 1.8157 1.9702 1.9637 -0.2086 0.1144  -0.2851 519 HIS C CE1 
6392  N NE2 . HIS B 187 ? 1.8281 1.9975 1.9864 -0.2054 0.1037  -0.2816 519 HIS C NE2 
6393  N N   . ALA B 188 ? 2.6107 2.7309 2.7034 -0.2145 0.1235  -0.2791 520 ALA C N   
6394  C CA  . ALA B 188 ? 2.5640 2.6757 2.6433 -0.2182 0.1299  -0.2811 520 ALA C CA  
6395  C C   . ALA B 188 ? 2.6438 2.7335 2.7091 -0.2202 0.1402  -0.2818 520 ALA C C   
6396  O O   . ALA B 188 ? 2.6797 2.7591 2.7436 -0.2175 0.1410  -0.2794 520 ALA C O   
6397  C CB  . ALA B 188 ? 2.4456 2.5564 2.5194 -0.2149 0.1240  -0.2772 520 ALA C CB  
6398  N N   . PRO B 189 ? 2.2637 2.3459 2.3184 -0.2251 0.1479  -0.2848 521 PRO C N   
6399  C CA  . PRO B 189 ? 2.1684 2.2305 2.2104 -0.2276 0.1577  -0.2851 521 PRO C CA  
6400  C C   . PRO B 189 ? 2.0661 2.1081 2.0954 -0.2223 0.1574  -0.2793 521 PRO C C   
6401  O O   . PRO B 189 ? 2.0299 2.0654 2.0501 -0.2193 0.1546  -0.2765 521 PRO C O   
6402  C CB  . PRO B 189 ? 2.1246 2.1834 2.1575 -0.2330 0.1630  -0.2884 521 PRO C CB  
6403  C CG  . PRO B 189 ? 2.0999 2.1813 2.1455 -0.2351 0.1580  -0.2921 521 PRO C CG  
6404  C CD  . PRO B 189 ? 2.1646 2.2589 2.2212 -0.2292 0.1477  -0.2887 521 PRO C CD  
6405  N N   . ALA B 190 ? 2.0383 2.0699 2.0662 -0.2210 0.1606  -0.2778 522 ALA C N   
6406  C CA  . ALA B 190 ? 1.9205 1.9333 1.9374 -0.2153 0.1597  -0.2722 522 ALA C CA  
6407  C C   . ALA B 190 ? 1.8903 1.8812 1.8885 -0.2166 0.1678  -0.2707 522 ALA C C   
6408  O O   . ALA B 190 ? 1.9184 1.9027 1.9135 -0.2209 0.1757  -0.2728 522 ALA C O   
6409  C CB  . ALA B 190 ? 1.8646 1.8760 1.8882 -0.2129 0.1589  -0.2713 522 ALA C CB  
6410  N N   . THR B 191 ? 1.7744 1.7541 1.7600 -0.2126 0.1658  -0.2670 523 THR C N   
6411  C CA  . THR B 191 ? 1.7238 1.6835 1.6912 -0.2133 0.1724  -0.2655 523 THR C CA  
6412  C C   . THR B 191 ? 1.6637 1.6035 1.6167 -0.2060 0.1708  -0.2592 523 THR C C   
6413  O O   . THR B 191 ? 1.6250 1.5490 1.5623 -0.2049 0.1745  -0.2573 523 THR C O   
6414  C CB  . THR B 191 ? 1.7550 1.7197 1.7186 -0.2162 0.1727  -0.2683 523 THR C CB  
6415  O OG1 . THR B 191 ? 1.7604 1.7362 1.7287 -0.2123 0.1645  -0.2672 523 THR C OG1 
6416  C CG2 . THR B 191 ? 1.7772 1.7572 1.7514 -0.2241 0.1759  -0.2746 523 THR C CG2 
6417  N N   . VAL B 192 ? 1.7409 1.6806 1.6983 -0.2006 0.1652  -0.2559 524 VAL C N   
6418  C CA  . VAL B 192 ? 1.6536 1.5750 1.5979 -0.1934 0.1632  -0.2500 524 VAL C CA  
6419  C C   . VAL B 192 ? 1.7886 1.7004 1.7325 -0.1917 0.1651  -0.2480 524 VAL C C   
6420  O O   . VAL B 192 ? 1.7755 1.6971 1.7318 -0.1907 0.1604  -0.2485 524 VAL C O   
6421  C CB  . VAL B 192 ? 1.5268 1.4554 1.4756 -0.1882 0.1538  -0.2477 524 VAL C CB  
6422  C CG1 . VAL B 192 ? 1.5001 1.4090 1.4331 -0.1811 0.1527  -0.2420 524 VAL C CG1 
6423  C CG2 . VAL B 192 ? 1.5520 1.4966 1.5062 -0.1909 0.1512  -0.2509 524 VAL C CG2 
6424  N N   . CYS B 193 ? 1.9645 1.8571 1.8939 -0.1911 0.1716  -0.2456 525 CYS C N   
6425  C CA  . CYS B 193 ? 1.9591 1.8432 1.8876 -0.1909 0.1751  -0.2447 525 CYS C CA  
6426  C C   . CYS B 193 ? 1.9515 1.8128 1.8630 -0.1844 0.1758  -0.2387 525 CYS C C   
6427  O O   . CYS B 193 ? 1.9006 1.7515 1.7998 -0.1813 0.1758  -0.2359 525 CYS C O   
6428  C CB  . CYS B 193 ? 2.0821 1.9685 2.0126 -0.1991 0.1843  -0.2493 525 CYS C CB  
6429  S SG  . CYS B 193 ? 2.2634 2.1775 2.2148 -0.2068 0.1838  -0.2567 525 CYS C SG  
6430  N N   . GLY B 194 ? 1.7929 1.6467 1.7036 -0.1821 0.1765  -0.2370 526 GLY C N   
6431  C CA  . GLY B 194 ? 1.7365 1.5690 1.6316 -0.1762 0.1775  -0.2316 526 GLY C CA  
6432  C C   . GLY B 194 ? 1.6235 1.4473 1.5154 -0.1781 0.1838  -0.2319 526 GLY C C   
6433  O O   . GLY B 194 ? 1.3969 1.2056 1.2759 -0.1786 0.1902  -0.2300 526 GLY C O   
6434  N N   . THR C 1   ? 1.5638 1.4455 1.2525 -0.0182 -0.3323 -0.0184 333 THR D N   
6435  C CA  . THR C 1   ? 1.7045 1.5993 1.4469 -0.0311 -0.3499 -0.0108 333 THR D CA  
6436  C C   . THR C 1   ? 1.8512 1.7043 1.5985 -0.0315 -0.3537 -0.0066 333 THR D C   
6437  O O   . THR C 1   ? 1.7606 1.6039 1.5336 -0.0249 -0.3629 -0.0123 333 THR D O   
6438  C CB  . THR C 1   ? 1.7091 1.6193 1.4670 -0.0141 -0.3582 -0.0280 333 THR D CB  
6439  O OG1 . THR C 1   ? 1.7959 1.6610 1.5193 0.0152  -0.3561 -0.0478 333 THR D OG1 
6440  C CG2 . THR C 1   ? 1.5756 1.5260 1.3266 -0.0104 -0.3523 -0.0347 333 THR D CG2 
6441  N N   . ASN C 2   ? 2.0456 1.8772 1.7742 -0.0395 -0.3395 0.0034  334 ASN D N   
6442  C CA  . ASN C 2   ? 2.0460 1.8436 1.7862 -0.0416 -0.3329 0.0092  334 ASN D CA  
6443  C C   . ASN C 2   ? 1.9916 1.8012 1.7531 -0.0701 -0.3292 0.0326  334 ASN D C   
6444  O O   . ASN C 2   ? 1.9514 1.7700 1.6866 -0.0776 -0.3220 0.0379  334 ASN D O   
6445  C CB  . ASN C 2   ? 2.0808 1.8270 1.7663 -0.0151 -0.3160 -0.0078 334 ASN D CB  
6446  C CG  . ASN C 2   ? 2.1316 1.8427 1.8310 -0.0061 -0.3134 -0.0117 334 ASN D CG  
6447  O OD1 . ASN C 2   ? 2.1302 1.8443 1.8551 0.0012  -0.3260 -0.0184 334 ASN D OD1 
6448  N ND2 . ASN C 2   ? 2.1397 1.8172 1.8233 -0.0066 -0.2966 -0.0079 334 ASN D ND2 
6449  N N   . LEU C 3   ? 1.8716 1.6806 1.6800 -0.0852 -0.3352 0.0459  335 LEU D N   
6450  C CA  . LEU C 3   ? 1.8280 1.6533 1.6670 -0.1138 -0.3370 0.0693  335 LEU D CA  
6451  C C   . LEU C 3   ? 1.9277 1.7353 1.7294 -0.1167 -0.3208 0.0728  335 LEU D C   
6452  O O   . LEU C 3   ? 1.9737 1.7447 1.7342 -0.0972 -0.3055 0.0590  335 LEU D O   
6453  C CB  . LEU C 3   ? 1.7321 1.5468 1.6191 -0.1219 -0.3429 0.0783  335 LEU D CB  
6454  C CG  . LEU C 3   ? 1.8996 1.7247 1.8253 -0.1491 -0.3468 0.1016  335 LEU D CG  
6455  C CD1 . LEU C 3   ? 1.8991 1.7284 1.8802 -0.1569 -0.3607 0.1093  335 LEU D CD1 
6456  C CD2 . LEU C 3   ? 1.8236 1.6147 1.7284 -0.1449 -0.3292 0.1008  335 LEU D CD2 
6457  N N   . CYS C 4   ? 1.8738 1.7056 1.6888 -0.1415 -0.3243 0.0915  336 CYS D N   
6458  C CA  . CYS C 4   ? 1.8130 1.6301 1.5973 -0.1478 -0.3112 0.0969  336 CYS D CA  
6459  C C   . CYS C 4   ? 1.6998 1.4920 1.5063 -0.1547 -0.3051 0.1047  336 CYS D C   
6460  O O   . CYS C 4   ? 1.6092 1.4156 1.4659 -0.1724 -0.3166 0.1198  336 CYS D O   
6461  C CB  . CYS C 4   ? 1.7873 1.6378 1.5761 -0.1718 -0.3181 0.1140  336 CYS D CB  
6462  S SG  . CYS C 4   ? 2.0640 1.9360 1.8061 -0.1627 -0.3154 0.1038  336 CYS D SG  
6463  N N   . PRO C 5   ? 1.7382 1.4937 1.5090 -0.1423 -0.2870 0.0954  337 PRO D N   
6464  C CA  . PRO C 5   ? 1.6653 1.3965 1.4592 -0.1470 -0.2792 0.1007  337 PRO D CA  
6465  C C   . PRO C 5   ? 1.5979 1.3505 1.4287 -0.1758 -0.2878 0.1229  337 PRO D C   
6466  O O   . PRO C 5   ? 1.6425 1.3974 1.4508 -0.1865 -0.2833 0.1292  337 PRO D O   
6467  C CB  . PRO C 5   ? 1.7293 1.4214 1.4688 -0.1309 -0.2572 0.0873  337 PRO D CB  
6468  C CG  . PRO C 5   ? 1.7303 1.4325 1.4228 -0.1266 -0.2560 0.0819  337 PRO D CG  
6469  C CD  . PRO C 5   ? 1.8232 1.5581 1.5306 -0.1244 -0.2725 0.0802  337 PRO D CD  
6470  N N   . PHE C 6   ? 1.6229 1.3908 1.5091 -0.1883 -0.3017 0.1348  338 PHE D N   
6471  C CA  . PHE C 6   ? 1.4961 1.2824 1.4192 -0.2148 -0.3118 0.1560  338 PHE D CA  
6472  C C   . PHE C 6   ? 1.4523 1.2196 1.4105 -0.2181 -0.3072 0.1603  338 PHE D C   
6473  O O   . PHE C 6   ? 1.4986 1.2664 1.4682 -0.2340 -0.3065 0.1718  338 PHE D O   
6474  C CB  . PHE C 6   ? 1.4127 1.2350 1.3743 -0.2311 -0.3336 0.1701  338 PHE D CB  
6475  C CG  . PHE C 6   ? 1.4401 1.2889 1.3766 -0.2407 -0.3392 0.1753  338 PHE D CG  
6476  C CD1 . PHE C 6   ? 1.4686 1.3087 1.3538 -0.2361 -0.3265 0.1691  338 PHE D CD1 
6477  C CD2 . PHE C 6   ? 1.5774 1.4565 1.5388 -0.2493 -0.3484 0.1853  338 PHE D CD2 
6478  C CE1 . PHE C 6   ? 1.4937 1.3578 1.3541 -0.2440 -0.3307 0.1734  338 PHE D CE1 
6479  C CE2 . PHE C 6   ? 1.6659 1.5665 1.6040 -0.2532 -0.3421 0.1882  338 PHE D CE2 
6480  C CZ  . PHE C 6   ? 1.6052 1.4999 1.4950 -0.2512 -0.3346 0.1820  338 PHE D CZ  
6481  N N   . ASP C 7   ? 1.4834 1.2340 1.4598 -0.2031 -0.3044 0.1508  339 ASP D N   
6482  C CA  . ASP C 7   ? 1.5565 1.2874 1.5643 -0.2041 -0.2969 0.1531  339 ASP D CA  
6483  C C   . ASP C 7   ? 1.5730 1.2788 1.5462 -0.2011 -0.2761 0.1476  339 ASP D C   
6484  O O   . ASP C 7   ? 1.5770 1.2813 1.5754 -0.2152 -0.2739 0.1577  339 ASP D O   
6485  C CB  . ASP C 7   ? 1.5866 1.2966 1.6051 -0.1836 -0.2925 0.1397  339 ASP D CB  
6486  C CG  . ASP C 7   ? 1.6364 1.3441 1.7130 -0.1908 -0.2974 0.1485  339 ASP D CG  
6487  O OD1 . ASP C 7   ? 1.6331 1.3667 1.7532 -0.2122 -0.3149 0.1668  339 ASP D OD1 
6488  O OD2 . ASP C 7   ? 1.6838 1.3620 1.7605 -0.1746 -0.2828 0.1370  339 ASP D OD2 
6489  N N   . GLU C 8   ? 1.4972 1.1849 1.4116 -0.1840 -0.2622 0.1322  340 GLU D N   
6490  C CA  . GLU C 8   ? 1.4919 1.1512 1.3665 -0.1792 -0.2411 0.1252  340 GLU D CA  
6491  C C   . GLU C 8   ? 1.4101 1.0846 1.2944 -0.2035 -0.2453 0.1409  340 GLU D C   
6492  O O   . GLU C 8   ? 1.3448 0.9983 1.2199 -0.2062 -0.2303 0.1397  340 GLU D O   
6493  C CB  . GLU C 8   ? 1.5380 1.1821 1.3469 -0.1595 -0.2312 0.1087  340 GLU D CB  
6494  C CG  . GLU C 8   ? 1.5745 1.1899 1.3361 -0.1557 -0.2110 0.1021  340 GLU D CG  
6495  C CD  . GLU C 8   ? 1.6086 1.2116 1.3057 -0.1374 -0.2041 0.0874  340 GLU D CD  
6496  O OE1 . GLU C 8   ? 1.5427 1.1146 1.2077 -0.1133 -0.1917 0.0704  340 GLU D OE1 
6497  O OE2 . GLU C 8   ? 1.6456 1.2676 1.3218 -0.1469 -0.2105 0.0928  340 GLU D OE2 
6498  N N   . VAL C 9   ? 1.4123 1.1216 1.3133 -0.2213 -0.2653 0.1553  341 VAL D N   
6499  C CA  . VAL C 9   ? 1.3484 1.0746 1.2632 -0.2458 -0.2739 0.1721  341 VAL D CA  
6500  C C   . VAL C 9   ? 1.2526 0.9953 1.2336 -0.2633 -0.2893 0.1884  341 VAL D C   
6501  O O   . VAL C 9   ? 1.2403 0.9873 1.2401 -0.2669 -0.2827 0.1922  341 VAL D O   
6502  C CB  . VAL C 9   ? 1.3030 1.0546 1.1898 -0.2546 -0.2854 0.1782  341 VAL D CB  
6503  C CG1 . VAL C 9   ? 1.1940 0.9672 1.1066 -0.2812 -0.3006 0.1983  341 VAL D CG1 
6504  C CG2 . VAL C 9   ? 1.3834 1.1157 1.2046 -0.2427 -0.2689 0.1652  341 VAL D CG2 
6505  N N   . PHE C 10  ? 1.1797 0.9435 1.1939 -0.2621 -0.3038 0.1929  342 PHE D N   
6506  C CA  . PHE C 10  ? 1.2102 1.0047 1.2741 -0.2617 -0.3096 0.2039  342 PHE D CA  
6507  C C   . PHE C 10  ? 1.2385 1.0187 1.3366 -0.2522 -0.2983 0.1975  342 PHE D C   
6508  O O   . PHE C 10  ? 1.2590 1.0512 1.3830 -0.2540 -0.2952 0.2025  342 PHE D O   
6509  C CB  . PHE C 10  ? 1.2072 1.0274 1.2945 -0.2600 -0.3250 0.2122  342 PHE D CB  
6510  C CG  . PHE C 10  ? 1.1757 1.0176 1.2410 -0.2692 -0.3336 0.2232  342 PHE D CG  
6511  C CD1 . PHE C 10  ? 1.2122 1.0482 1.2326 -0.2779 -0.3305 0.2212  342 PHE D CD1 
6512  C CD2 . PHE C 10  ? 1.1223 0.9868 1.2098 -0.2701 -0.3424 0.2373  342 PHE D CD2 
6513  C CE1 . PHE C 10  ? 1.2322 1.0874 1.2321 -0.2862 -0.3359 0.2315  342 PHE D CE1 
6514  C CE2 . PHE C 10  ? 1.1920 1.0714 1.2576 -0.2789 -0.3465 0.2487  342 PHE D CE2 
6515  C CZ  . PHE C 10  ? 1.2034 1.0795 1.2264 -0.2869 -0.3426 0.2458  342 PHE D CZ  
6516  N N   . ASN C 11  ? 1.2517 1.0048 1.3497 -0.2416 -0.2922 0.1861  343 ASN D N   
6517  C CA  . ASN C 11  ? 1.2072 0.9464 1.3378 -0.2318 -0.2801 0.1800  343 ASN D CA  
6518  C C   . ASN C 11  ? 1.1466 0.8465 1.2483 -0.2272 -0.2573 0.1691  343 ASN D C   
6519  O O   . ASN C 11  ? 1.1767 0.8537 1.2931 -0.2163 -0.2435 0.1607  343 ASN D O   
6520  C CB  . ASN C 11  ? 1.2723 1.0050 1.4250 -0.2206 -0.2866 0.1750  343 ASN D CB  
6521  C CG  . ASN C 11  ? 1.4298 1.2016 1.6162 -0.2242 -0.3068 0.1874  343 ASN D CG  
6522  O OD1 . ASN C 11  ? 1.3913 1.1910 1.5827 -0.2332 -0.3144 0.1999  343 ASN D OD1 
6523  N ND2 . ASN C 11  ? 1.5399 1.3089 1.7461 -0.2156 -0.3146 0.1839  343 ASN D ND2 
6524  N N   . ALA C 12  ? 1.2770 0.9686 1.3372 -0.2352 -0.2524 0.1697  344 ALA D N   
6525  C CA  . ALA C 12  ? 1.3194 0.9731 1.3474 -0.2315 -0.2297 0.1606  344 ALA D CA  
6526  C C   . ALA C 12  ? 1.3352 0.9980 1.4062 -0.2324 -0.2170 0.1609  344 ALA D C   
6527  O O   . ALA C 12  ? 1.2977 0.9984 1.4103 -0.2399 -0.2276 0.1703  344 ALA D O   
6528  C CB  . ALA C 12  ? 1.3580 1.0105 1.3362 -0.2394 -0.2276 0.1618  344 ALA D CB  
6529  N N   . THR C 13  ? 1.2543 0.8785 1.3109 -0.2236 -0.1937 0.1502  345 THR D N   
6530  C CA  . THR C 13  ? 1.2780 0.9069 1.3794 -0.2230 -0.1796 0.1486  345 THR D CA  
6531  C C   . THR C 13  ? 1.3013 0.9613 1.4234 -0.2374 -0.1831 0.1567  345 THR D C   
6532  O O   . THR C 13  ? 1.3220 1.0115 1.4946 -0.2405 -0.1899 0.1623  345 THR D O   
6533  C CB  . THR C 13  ? 1.3214 0.9006 1.3957 -0.2122 -0.1514 0.1358  345 THR D CB  
6534  O OG1 . THR C 13  ? 1.4513 0.9976 1.4892 -0.1944 -0.1490 0.1259  345 THR D OG1 
6535  C CG2 . THR C 13  ? 1.3063 0.8895 1.4319 -0.2098 -0.1373 0.1334  345 THR D CG2 
6536  N N   . ARG C 14  ? 1.3849 1.0366 1.4654 -0.2453 -0.1800 0.1571  346 ARG D N   
6537  C CA  . ARG C 14  ? 1.3849 1.0629 1.4804 -0.2580 -0.1847 0.1640  346 ARG D CA  
6538  C C   . ARG C 14  ? 1.3143 1.0042 1.3707 -0.2666 -0.2005 0.1709  346 ARG D C   
6539  O O   . ARG C 14  ? 1.3089 0.9812 1.3207 -0.2639 -0.2032 0.1687  346 ARG D O   
6540  C CB  . ARG C 14  ? 1.5823 1.2369 1.6720 -0.2604 -0.1606 0.1566  346 ARG D CB  
6541  C CG  . ARG C 14  ? 1.7033 1.3575 1.8436 -0.2556 -0.1474 0.1525  346 ARG D CG  
6542  C CD  . ARG C 14  ? 1.7759 1.4158 1.9231 -0.2612 -0.1250 0.1468  346 ARG D CD  
6543  N NE  . ARG C 14  ? 1.8625 1.4959 2.0516 -0.2563 -0.1091 0.1414  346 ARG D NE  
6544  C CZ  . ARG C 14  ? 1.7810 1.4019 1.9827 -0.2611 -0.0879 0.1359  346 ARG D CZ  
6545  N NH1 . ARG C 14  ? 1.5881 1.2045 1.7692 -0.2714 -0.0812 0.1352  346 ARG D NH1 
6546  N NH2 . ARG C 14  ? 1.7347 1.3495 1.9724 -0.2561 -0.0745 0.1313  346 ARG D NH2 
6547  N N   . PHE C 15  ? 1.1747 0.8925 1.2463 -0.2768 -0.2111 0.1791  347 PHE D N   
6548  C CA  . PHE C 15  ? 1.1238 0.8559 1.1628 -0.2856 -0.2271 0.1871  347 PHE D CA  
6549  C C   . PHE C 15  ? 1.0724 0.7952 1.0876 -0.2943 -0.2189 0.1855  347 PHE D C   
6550  O O   . PHE C 15  ? 1.0441 0.7604 1.0822 -0.2950 -0.2053 0.1809  347 PHE D O   
6551  C CB  . PHE C 15  ? 1.1009 0.8722 1.1737 -0.2890 -0.2502 0.2003  347 PHE D CB  
6552  C CG  . PHE C 15  ? 1.0508 0.8339 1.1259 -0.2844 -0.2641 0.2050  347 PHE D CG  
6553  C CD1 . PHE C 15  ? 1.0558 0.8327 1.1569 -0.2742 -0.2602 0.1999  347 PHE D CD1 
6554  C CD2 . PHE C 15  ? 1.0013 0.8026 1.0551 -0.2906 -0.2814 0.2153  347 PHE D CD2 
6555  C CE1 . PHE C 15  ? 1.0667 0.8553 1.1727 -0.2705 -0.2739 0.2043  347 PHE D CE1 
6556  C CE2 . PHE C 15  ? 0.9534 0.7665 1.0120 -0.2872 -0.2931 0.2200  347 PHE D CE2 
6557  C CZ  . PHE C 15  ? 1.0116 0.8190 1.0971 -0.2773 -0.2899 0.2144  347 PHE D CZ  
6558  N N   . ALA C 16  ? 0.9352 0.6579 0.9052 -0.3015 -0.2276 0.1894  348 ALA D N   
6559  C CA  . ALA C 16  ? 1.0113 0.7221 0.9514 -0.3099 -0.2210 0.1876  348 ALA D CA  
6560  C C   . ALA C 16  ? 1.0219 0.7628 0.9906 -0.3188 -0.2364 0.1976  348 ALA D C   
6561  O O   . ALA C 16  ? 1.0310 0.7984 1.0089 -0.3214 -0.2570 0.2089  348 ALA D O   
6562  C CB  . ALA C 16  ? 1.1577 0.8505 1.0301 -0.3135 -0.2229 0.1865  348 ALA D CB  
6563  N N   . SER C 17  ? 1.0152 0.7495 0.9945 -0.3233 -0.2267 0.1940  349 SER D N   
6564  C CA  . SER C 17  ? 0.9743 0.7325 0.9737 -0.3317 -0.2430 0.2036  349 SER D CA  
6565  C C   . SER C 17  ? 0.9614 0.7215 0.9105 -0.3402 -0.2574 0.2106  349 SER D C   
6566  O O   . SER C 17  ? 1.0012 0.7378 0.8984 -0.3423 -0.2486 0.2045  349 SER D O   
6567  C CB  . SER C 17  ? 0.9487 0.7001 0.9727 -0.3358 -0.2305 0.1979  349 SER D CB  
6568  O OG  . SER C 17  ? 0.9064 0.6274 0.8935 -0.3387 -0.2112 0.1880  349 SER D OG  
6569  N N   . VAL C 18  ? 0.9494 0.7349 0.9105 -0.3443 -0.2793 0.2240  350 VAL D N   
6570  C CA  . VAL C 18  ? 0.9919 0.7831 0.9092 -0.3511 -0.2946 0.2331  350 VAL D CA  
6571  C C   . VAL C 18  ? 0.9954 0.7668 0.8589 -0.3604 -0.2905 0.2290  350 VAL D C   
6572  O O   . VAL C 18  ? 1.0826 0.8492 0.8982 -0.3651 -0.2956 0.2308  350 VAL D O   
6573  C CB  . VAL C 18  ? 0.9521 0.7686 0.8927 -0.3543 -0.3167 0.2494  350 VAL D CB  
6574  C CG1 . VAL C 18  ? 0.9059 0.7250 0.8753 -0.3581 -0.3194 0.2512  350 VAL D CG1 
6575  C CG2 . VAL C 18  ? 0.9709 0.7908 0.8642 -0.3632 -0.3308 0.2599  350 VAL D CG2 
6576  N N   . TYR C 19  ? 1.0105 0.7696 0.8794 -0.3639 -0.2812 0.2230  351 TYR D N   
6577  C CA  . TYR C 19  ? 1.0510 0.7908 0.8664 -0.3732 -0.2795 0.2201  351 TYR D CA  
6578  C C   . TYR C 19  ? 1.0689 0.7780 0.8331 -0.3700 -0.2621 0.2081  351 TYR D C   
6579  O O   . TYR C 19  ? 1.1563 0.8489 0.8649 -0.3768 -0.2628 0.2060  351 TYR D O   
6580  C CB  . TYR C 19  ? 1.0377 0.7704 0.8717 -0.3780 -0.2734 0.2164  351 TYR D CB  
6581  C CG  . TYR C 19  ? 0.9103 0.6184 0.7485 -0.3724 -0.2472 0.2021  351 TYR D CG  
6582  C CD1 . TYR C 19  ? 0.8833 0.5972 0.7729 -0.3637 -0.2362 0.1980  351 TYR D CD1 
6583  C CD2 . TYR C 19  ? 0.9348 0.6117 0.7253 -0.3761 -0.2330 0.1930  351 TYR D CD2 
6584  C CE1 . TYR C 19  ? 0.8835 0.5736 0.7770 -0.3590 -0.2114 0.1860  351 TYR D CE1 
6585  C CE2 . TYR C 19  ? 0.9707 0.6224 0.7639 -0.3706 -0.2079 0.1810  351 TYR D CE2 
6586  C CZ  . TYR C 19  ? 0.9307 0.5893 0.7762 -0.3623 -0.1968 0.1778  351 TYR D CZ  
6587  O OH  . TYR C 19  ? 1.0888 0.7200 0.9357 -0.3572 -0.1702 0.1664  351 TYR D OH  
6588  N N   . ALA C 20  ? 1.0982 0.7960 0.8779 -0.3591 -0.2458 0.1998  352 ALA D N   
6589  C CA  . ALA C 20  ? 1.0943 0.7592 0.8257 -0.3522 -0.2289 0.1891  352 ALA D CA  
6590  C C   . ALA C 20  ? 1.1547 0.8296 0.8950 -0.3444 -0.2341 0.1914  352 ALA D C   
6591  O O   . ALA C 20  ? 1.1518 0.8076 0.8950 -0.3337 -0.2191 0.1835  352 ALA D O   
6592  C CB  . ALA C 20  ? 0.9746 0.6097 0.7110 -0.3453 -0.2031 0.1770  352 ALA D CB  
6593  N N   . TRP C 21  ? 1.1108 0.8144 0.8557 -0.3499 -0.2551 0.2026  353 TRP D N   
6594  C CA  . TRP C 21  ? 1.2266 0.9431 0.9846 -0.3439 -0.2618 0.2058  353 TRP D CA  
6595  C C   . TRP C 21  ? 1.3968 1.0809 1.0992 -0.3375 -0.2493 0.1966  353 TRP D C   
6596  O O   . TRP C 21  ? 1.4257 1.0913 1.0697 -0.3400 -0.2452 0.1935  353 TRP D O   
6597  C CB  . TRP C 21  ? 1.2012 0.9504 0.9634 -0.3519 -0.2847 0.2198  353 TRP D CB  
6598  C CG  . TRP C 21  ? 1.2108 0.9561 0.9197 -0.3638 -0.2915 0.2220  353 TRP D CG  
6599  C CD1 . TRP C 21  ? 1.2171 0.9602 0.9132 -0.3725 -0.2954 0.2242  353 TRP D CD1 
6600  C CD2 . TRP C 21  ? 1.2874 1.0298 0.9511 -0.3674 -0.2933 0.2187  353 TRP D CD2 
6601  N NE1 . TRP C 21  ? 1.2422 0.9818 0.8887 -0.3827 -0.3008 0.2217  353 TRP D NE1 
6602  C CE2 . TRP C 21  ? 1.2510 0.9912 0.8856 -0.3784 -0.2944 0.2150  353 TRP D CE2 
6603  C CE3 . TRP C 21  ? 1.3280 1.0712 0.9824 -0.3585 -0.2882 0.2147  353 TRP D CE3 
6604  C CZ2 . TRP C 21  ? 1.2964 1.0383 0.9045 -0.3705 -0.2791 0.2058  353 TRP D CZ2 
6605  C CZ3 . TRP C 21  ? 1.3327 1.0835 0.9582 -0.3487 -0.2760 0.2042  353 TRP D CZ3 
6606  C CH2 . TRP C 21  ? 1.3294 1.0806 0.9345 -0.3527 -0.2698 0.1997  353 TRP D CH2 
6607  N N   . ASN C 22  ? 1.4405 1.1155 1.1572 -0.3264 -0.2427 0.1922  354 ASN D N   
6608  C CA  . ASN C 22  ? 1.4801 1.1314 1.1439 -0.3099 -0.2306 0.1810  354 ASN D CA  
6609  C C   . ASN C 22  ? 1.5032 1.1842 1.1722 -0.3054 -0.2450 0.1848  354 ASN D C   
6610  O O   . ASN C 22  ? 1.3813 1.0913 1.0957 -0.3197 -0.2643 0.1994  354 ASN D O   
6611  C CB  . ASN C 22  ? 1.5204 1.1421 1.1846 -0.2905 -0.2091 0.1660  354 ASN D CB  
6612  C CG  . ASN C 22  ? 1.6341 1.2684 1.3604 -0.2897 -0.2147 0.1702  354 ASN D CG  
6613  O OD1 . ASN C 22  ? 1.6869 1.3518 1.4476 -0.2965 -0.2339 0.1807  354 ASN D OD1 
6614  N ND2 . ASN C 22  ? 1.5035 1.1124 1.2434 -0.2812 -0.1970 0.1617  354 ASN D ND2 
6615  N N   . ARG C 23  ? 1.5484 1.2203 1.1701 -0.2846 -0.2348 0.1706  355 ARG D N   
6616  C CA  . ARG C 23  ? 1.5064 1.2046 1.1139 -0.2799 -0.2456 0.1715  355 ARG D CA  
6617  C C   . ARG C 23  ? 1.5367 1.2200 1.1170 -0.2523 -0.2327 0.1530  355 ARG D C   
6618  O O   . ARG C 23  ? 1.6159 1.2679 1.1474 -0.2369 -0.2153 0.1386  355 ARG D O   
6619  C CB  . ARG C 23  ? 1.5069 1.2132 1.0744 -0.2859 -0.2463 0.1719  355 ARG D CB  
6620  C CG  . ARG C 23  ? 1.4778 1.1990 1.0230 -0.2634 -0.2336 0.1544  355 ARG D CG  
6621  C CD  . ARG C 23  ? 1.4446 1.1826 0.9815 -0.2656 -0.2264 0.1513  355 ARG D CD  
6622  N NE  . ARG C 23  ? 1.4268 1.1999 1.0015 -0.2823 -0.2398 0.1654  355 ARG D NE  
6623  C CZ  . ARG C 23  ? 1.4278 1.2202 1.0006 -0.2845 -0.2359 0.1653  355 ARG D CZ  
6624  N NH1 . ARG C 23  ? 1.5127 1.2957 1.0518 -0.2712 -0.2206 0.1523  355 ARG D NH1 
6625  N NH2 . ARG C 23  ? 1.3744 1.1946 0.9797 -0.2999 -0.2473 0.1789  355 ARG D NH2 
6626  N N   . LYS C 24  ? 1.5418 1.2448 1.1533 -0.2461 -0.2414 0.1531  356 LYS D N   
6627  C CA  . LYS C 24  ? 1.6063 1.2985 1.1932 -0.2199 -0.2328 0.1356  356 LYS D CA  
6628  C C   . LYS C 24  ? 1.6621 1.3826 1.2294 -0.2159 -0.2425 0.1344  356 LYS D C   
6629  O O   . LYS C 24  ? 1.6690 1.4241 1.2693 -0.2320 -0.2591 0.1483  356 LYS D O   
6630  C CB  . LYS C 24  ? 1.5355 1.2250 1.1671 -0.2123 -0.2338 0.1331  356 LYS D CB  
6631  C CG  . LYS C 24  ? 1.7073 1.3534 1.3203 -0.1960 -0.2126 0.1192  356 LYS D CG  
6632  C CD  . LYS C 24  ? 1.8308 1.4568 1.4356 -0.2099 -0.2024 0.1245  356 LYS D CD  
6633  C CE  . LYS C 24  ? 1.8671 1.4458 1.4263 -0.1927 -0.1773 0.1084  356 LYS D CE  
6634  N NZ  . LYS C 24  ? 1.8351 1.3871 1.4055 -0.1757 -0.1637 0.0976  356 LYS D NZ  
6635  N N   . ARG C 25  ? 1.7035 1.4102 1.2213 -0.1938 -0.2289 0.1165  357 ARG D N   
6636  C CA  . ARG C 25  ? 1.7752 1.5139 1.2947 -0.1794 -0.2245 0.1064  357 ARG D CA  
6637  C C   . ARG C 25  ? 1.7975 1.5478 1.3380 -0.1718 -0.2372 0.1042  357 ARG D C   
6638  O O   . ARG C 25  ? 1.8051 1.5320 1.3213 -0.1502 -0.2325 0.0892  357 ARG D O   
6639  C CB  . ARG C 25  ? 1.9292 1.6517 1.4050 -0.1533 -0.2028 0.0860  357 ARG D CB  
6640  C CG  . ARG C 25  ? 2.0763 1.8345 1.5531 -0.1423 -0.1959 0.0791  357 ARG D CG  
6641  C CD  . ARG C 25  ? 2.2241 1.9709 1.6684 -0.1108 -0.1790 0.0578  357 ARG D CD  
6642  N NE  . ARG C 25  ? 2.2947 2.0744 1.7482 -0.0955 -0.1816 0.0495  357 ARG D NE  
6643  C CZ  . ARG C 25  ? 2.2955 2.0732 1.7324 -0.0694 -0.1728 0.0321  357 ARG D CZ  
6644  N NH1 . ARG C 25  ? 2.2723 2.0151 1.6830 -0.0544 -0.1593 0.0211  357 ARG D NH1 
6645  N NH2 . ARG C 25  ? 2.2082 2.0195 1.6573 -0.0594 -0.1781 0.0261  357 ARG D NH2 
6646  N N   . ILE C 26  ? 1.8163 1.6013 1.4034 -0.1892 -0.2532 0.1187  358 ILE D N   
6647  C CA  . ILE C 26  ? 1.7938 1.5965 1.4084 -0.1835 -0.2658 0.1168  358 ILE D CA  
6648  C C   . ILE C 26  ? 1.8994 1.7284 1.5025 -0.1674 -0.2575 0.1041  358 ILE D C   
6649  O O   . ILE C 26  ? 1.9350 1.7959 1.5539 -0.1783 -0.2568 0.1117  358 ILE D O   
6650  C CB  . ILE C 26  ? 1.7675 1.5963 1.4408 -0.2081 -0.2839 0.1373  358 ILE D CB  
6651  C CG1 . ILE C 26  ? 1.8065 1.6145 1.5041 -0.2215 -0.2866 0.1483  358 ILE D CG1 
6652  C CG2 . ILE C 26  ? 1.7307 1.5768 1.4360 -0.2020 -0.2958 0.1343  358 ILE D CG2 
6653  C CD1 . ILE C 26  ? 1.8023 1.5673 1.4787 -0.2024 -0.2687 0.1332  358 ILE D CD1 
6654  N N   . SER C 27  ? 1.9856 1.7999 1.5597 -0.1408 -0.2509 0.0843  359 SER D N   
6655  C CA  . SER C 27  ? 1.9487 1.7867 1.5098 -0.1220 -0.2429 0.0701  359 SER D CA  
6656  C C   . SER C 27  ? 1.8787 1.7060 1.4298 -0.0979 -0.2459 0.0526  359 SER D C   
6657  O O   . SER C 27  ? 1.8552 1.6469 1.3963 -0.0912 -0.2492 0.0482  359 SER D O   
6658  C CB  . SER C 27  ? 2.0339 1.8642 1.5581 -0.1097 -0.2228 0.0610  359 SER D CB  
6659  O OG  . SER C 27  ? 2.1989 2.0561 1.7349 -0.1249 -0.2209 0.0718  359 SER D OG  
6660  N N   . ASN C 28  ? 1.9766 1.8343 1.5295 -0.0845 -0.2450 0.0420  360 ASN D N   
6661  C CA  . ASN C 28  ? 1.9032 1.7583 1.4464 -0.0592 -0.2465 0.0228  360 ASN D CA  
6662  C C   . ASN C 28  ? 1.7796 1.6180 1.3436 -0.0596 -0.2633 0.0228  360 ASN D C   
6663  O O   . ASN C 28  ? 1.5970 1.3993 1.1382 -0.0397 -0.2605 0.0090  360 ASN D O   
6664  C CB  . ASN C 28  ? 1.8639 1.6905 1.3639 -0.0338 -0.2267 0.0052  360 ASN D CB  
6665  C CG  . ASN C 28  ? 1.9962 1.8339 1.4794 -0.0348 -0.2100 0.0068  360 ASN D CG  
6666  O OD1 . ASN C 28  ? 2.1381 1.9520 1.6081 -0.0433 -0.2015 0.0137  360 ASN D OD1 
6667  N ND2 . ASN C 28  ? 1.9092 1.7833 1.3936 -0.0262 -0.2057 -0.0003 360 ASN D ND2 
6668  N N   . CYS C 29  ? 1.8229 1.6902 1.4337 -0.0809 -0.2798 0.0376  361 CYS D N   
6669  C CA  . CYS C 29  ? 1.8777 1.7360 1.5238 -0.0899 -0.2972 0.0446  361 CYS D CA  
6670  C C   . CYS C 29  ? 1.9107 1.8138 1.6126 -0.1141 -0.3086 0.0615  361 CYS D C   
6671  O O   . CYS C 29  ? 1.9277 1.8619 1.6340 -0.1242 -0.3029 0.0682  361 CYS D O   
6672  C CB  . CYS C 29  ? 1.9627 1.7807 1.6008 -0.0966 -0.2938 0.0522  361 CYS D CB  
6673  S SG  . CYS C 29  ? 1.8956 1.7199 1.5576 -0.1305 -0.2927 0.0790  361 CYS D SG  
6674  N N   . VAL C 30  ? 1.8702 1.7744 1.6145 -0.1215 -0.3234 0.0674  362 VAL D N   
6675  C CA  . VAL C 30  ? 1.9275 1.8697 1.7275 -0.1418 -0.3319 0.0820  362 VAL D CA  
6676  C C   . VAL C 30  ? 1.9210 1.8535 1.7584 -0.1620 -0.3387 0.1006  362 VAL D C   
6677  O O   . VAL C 30  ? 1.9121 1.8146 1.7523 -0.1557 -0.3454 0.0973  362 VAL D O   
6678  C CB  . VAL C 30  ? 2.0191 1.9775 1.8426 -0.1301 -0.3415 0.0699  362 VAL D CB  
6679  C CG1 . VAL C 30  ? 1.9936 1.9150 1.8087 -0.1111 -0.3493 0.0561  362 VAL D CG1 
6680  C CG2 . VAL C 30  ? 2.0229 2.0114 1.9040 -0.1517 -0.3483 0.0860  362 VAL D CG2 
6681  N N   . ALA C 31  ? 2.0036 1.9602 1.8698 -0.1849 -0.3370 0.1197  363 ALA D N   
6682  C CA  . ALA C 31  ? 2.0529 1.9988 1.9432 -0.2039 -0.3391 0.1383  363 ALA D CA  
6683  C C   . ALA C 31  ? 2.0887 2.0424 2.0335 -0.2138 -0.3477 0.1493  363 ALA D C   
6684  O O   . ALA C 31  ? 1.9952 1.9731 1.9628 -0.2165 -0.3493 0.1509  363 ALA D O   
6685  C CB  . ALA C 31  ? 1.9943 1.9540 1.8747 -0.2210 -0.3306 0.1526  363 ALA D CB  
6686  N N   . ASP C 32  ? 2.2623 2.1943 2.2273 -0.2192 -0.3522 0.1572  364 ASP D N   
6687  C CA  . ASP C 32  ? 2.4139 2.3468 2.4277 -0.2260 -0.3582 0.1680  364 ASP D CA  
6688  C C   . ASP C 32  ? 2.4255 2.3625 2.4588 -0.2444 -0.3553 0.1907  364 ASP D C   
6689  O O   . ASP C 32  ? 2.5163 2.4436 2.5816 -0.2470 -0.3591 0.2003  364 ASP D O   
6690  C CB  . ASP C 32  ? 2.4529 2.3573 2.4784 -0.2152 -0.3657 0.1591  364 ASP D CB  
6691  C CG  . ASP C 32  ? 2.6718 2.5763 2.7449 -0.2171 -0.3712 0.1665  364 ASP D CG  
6692  O OD1 . ASP C 32  ? 2.7315 2.6573 2.8207 -0.2204 -0.3712 0.1710  364 ASP D OD1 
6693  O OD2 . ASP C 32  ? 2.7543 2.6375 2.8475 -0.2154 -0.3749 0.1681  364 ASP D OD2 
6694  N N   . TYR C 33  ? 2.3241 2.2745 2.3365 -0.2553 -0.3488 0.1994  365 TYR D N   
6695  C CA  . TYR C 33  ? 2.2435 2.1989 2.2723 -0.2707 -0.3482 0.2214  365 TYR D CA  
6696  C C   . TYR C 33  ? 2.5005 2.4703 2.5579 -0.2737 -0.3518 0.2298  365 TYR D C   
6697  O O   . TYR C 33  ? 2.4959 2.4681 2.5648 -0.2838 -0.3534 0.2478  365 TYR D O   
6698  C CB  . TYR C 33  ? 1.9857 1.9500 1.9845 -0.2825 -0.3417 0.2295  365 TYR D CB  
6699  C CG  . TYR C 33  ? 1.9597 1.9428 1.9294 -0.2795 -0.3359 0.2180  365 TYR D CG  
6700  C CD1 . TYR C 33  ? 2.0862 2.0929 2.0665 -0.2809 -0.3362 0.2181  365 TYR D CD1 
6701  C CD2 . TYR C 33  ? 1.8203 1.7983 1.7501 -0.2759 -0.3292 0.2086  365 TYR D CD2 
6702  C CE1 . TYR C 33  ? 2.0753 2.1022 2.0306 -0.2765 -0.3308 0.2071  365 TYR D CE1 
6703  C CE2 . TYR C 33  ? 1.9189 1.9146 1.8200 -0.2696 -0.3226 0.1974  365 TYR D CE2 
6704  C CZ  . TYR C 33  ? 2.0686 2.0901 1.9839 -0.2698 -0.3237 0.1966  365 TYR D CZ  
6705  O OH  . TYR C 33  ? 2.0705 2.1118 1.9599 -0.2623 -0.3175 0.1852  365 TYR D OH  
6706  N N   . SER C 34  ? 3.0092 2.9870 3.0758 -0.2643 -0.3543 0.2166  366 SER D N   
6707  C CA  . SER C 34  ? 3.1967 3.1859 3.2909 -0.2672 -0.3582 0.2232  366 SER D CA  
6708  C C   . SER C 34  ? 3.3587 3.3304 3.4838 -0.2654 -0.3643 0.2323  366 SER D C   
6709  O O   . SER C 34  ? 3.3248 3.2991 3.4635 -0.2738 -0.3669 0.2491  366 SER D O   
6710  C CB  . SER C 34  ? 3.0747 3.0765 3.1718 -0.2564 -0.3602 0.2049  366 SER D CB  
6711  O OG  . SER C 34  ? 3.2025 3.1875 3.3200 -0.2445 -0.3667 0.1956  366 SER D OG  
6712  N N   . VAL C 35  ? 2.8201 2.7730 2.9547 -0.2538 -0.3675 0.2215  367 VAL D N   
6713  C CA  . VAL C 35  ? 2.7996 2.7371 2.9655 -0.2497 -0.3734 0.2276  367 VAL D CA  
6714  C C   . VAL C 35  ? 2.7285 2.6503 2.8962 -0.2500 -0.3727 0.2346  367 VAL D C   
6715  O O   . VAL C 35  ? 2.6923 2.6035 2.8864 -0.2457 -0.3773 0.2400  367 VAL D O   
6716  C CB  . VAL C 35  ? 2.8175 2.7445 2.9986 -0.2361 -0.3789 0.2110  367 VAL D CB  
6717  C CG1 . VAL C 35  ? 2.7604 2.6670 2.9302 -0.2267 -0.3792 0.1977  367 VAL D CG1 
6718  C CG2 . VAL C 35  ? 2.8155 2.7351 3.0310 -0.2339 -0.3856 0.2187  367 VAL D CG2 
6719  N N   . LEU C 36  ? 2.5581 2.4791 2.6992 -0.2545 -0.3673 0.2340  368 LEU D N   
6720  C CA  . LEU C 36  ? 2.3583 2.2685 2.5020 -0.2565 -0.3664 0.2419  368 LEU D CA  
6721  C C   . LEU C 36  ? 2.3954 2.3148 2.5414 -0.2662 -0.3680 0.2616  368 LEU D C   
6722  O O   . LEU C 36  ? 2.2123 2.1255 2.3700 -0.2655 -0.3700 0.2686  368 LEU D O   
6723  C CB  . LEU C 36  ? 2.0935 1.9960 2.2063 -0.2577 -0.3609 0.2327  368 LEU D CB  
6724  C CG  . LEU C 36  ? 1.7602 1.6497 1.8771 -0.2582 -0.3589 0.2357  368 LEU D CG  
6725  C CD1 . LEU C 36  ? 1.6193 1.4888 1.7188 -0.2536 -0.3554 0.2192  368 LEU D CD1 
6726  C CD2 . LEU C 36  ? 1.4898 1.3893 1.5859 -0.2697 -0.3565 0.2486  368 LEU D CD2 
6727  N N   . TYR C 37  ? 2.8833 2.8176 3.0186 -0.2749 -0.3678 0.2696  369 TYR D N   
6728  C CA  . TYR C 37  ? 2.8551 2.7955 2.9902 -0.2846 -0.3716 0.2887  369 TYR D CA  
6729  C C   . TYR C 37  ? 2.8487 2.7841 3.0159 -0.2804 -0.3805 0.2976  369 TYR D C   
6730  O O   . TYR C 37  ? 2.6852 2.6220 2.8547 -0.2865 -0.3865 0.3133  369 TYR D O   
6731  C CB  . TYR C 37  ? 2.8557 2.8129 2.9722 -0.2953 -0.3691 0.2937  369 TYR D CB  
6732  C CG  . TYR C 37  ? 2.8091 2.7726 2.9283 -0.3055 -0.3753 0.3132  369 TYR D CG  
6733  C CD1 . TYR C 37  ? 2.7009 2.6640 2.8012 -0.3151 -0.3770 0.3271  369 TYR D CD1 
6734  C CD2 . TYR C 37  ? 2.8471 2.8159 2.9854 -0.3061 -0.3806 0.3177  369 TYR D CD2 
6735  C CE1 . TYR C 37  ? 2.7556 2.7226 2.8554 -0.3248 -0.3846 0.3451  369 TYR D CE1 
6736  C CE2 . TYR C 37  ? 2.8132 2.7861 2.9513 -0.3162 -0.3875 0.3359  369 TYR D CE2 
6737  C CZ  . TYR C 37  ? 2.8477 2.8195 2.9660 -0.3255 -0.3899 0.3497  369 TYR D CZ  
6738  O OH  . TYR C 37  ? 2.8836 2.8581 2.9996 -0.3358 -0.3987 0.3681  369 TYR D OH  
6739  N N   . ASN C 38  ? 2.6217 2.5499 2.8126 -0.2699 -0.3825 0.2877  370 ASN D N   
6740  C CA  . ASN C 38  ? 2.6599 2.5830 2.8816 -0.2654 -0.3910 0.2945  370 ASN D CA  
6741  C C   . ASN C 38  ? 2.5559 2.4659 2.8017 -0.2542 -0.3931 0.2885  370 ASN D C   
6742  O O   . ASN C 38  ? 2.5511 2.4554 2.8244 -0.2481 -0.3999 0.2903  370 ASN D O   
6743  C CB  . ASN C 38  ? 2.7279 2.6545 2.9600 -0.2635 -0.3929 0.2890  370 ASN D CB  
6744  C CG  . ASN C 38  ? 2.7443 2.6871 2.9580 -0.2749 -0.3908 0.2948  370 ASN D CG  
6745  O OD1 . ASN C 38  ? 2.7832 2.7354 2.9752 -0.2779 -0.3836 0.2863  370 ASN D OD1 
6746  N ND2 . ASN C 38  ? 2.6862 2.6328 2.9092 -0.2815 -0.3977 0.3090  370 ASN D ND2 
6747  N N   . PHE C 39  ? 2.4597 2.3651 2.6968 -0.2518 -0.3874 0.2811  371 PHE D N   
6748  C CA  . PHE C 39  ? 2.4216 2.3172 2.6843 -0.2425 -0.3883 0.2758  371 PHE D CA  
6749  C C   . PHE C 39  ? 2.4913 2.3889 2.7760 -0.2432 -0.3963 0.2899  371 PHE D C   
6750  O O   . PHE C 39  ? 2.4990 2.3911 2.8147 -0.2355 -0.4016 0.2894  371 PHE D O   
6751  C CB  . PHE C 39  ? 2.2931 2.1840 2.5409 -0.2422 -0.3797 0.2662  371 PHE D CB  
6752  C CG  . PHE C 39  ? 2.3239 2.2044 2.5604 -0.2369 -0.3742 0.2488  371 PHE D CG  
6753  C CD1 . PHE C 39  ? 2.3697 2.2524 2.5922 -0.2373 -0.3754 0.2434  371 PHE D CD1 
6754  C CD2 . PHE C 39  ? 2.3217 2.1887 2.5621 -0.2316 -0.3677 0.2368  371 PHE D CD2 
6755  C CE1 . PHE C 39  ? 2.2849 2.1559 2.4953 -0.2315 -0.3731 0.2264  371 PHE D CE1 
6756  C CE2 . PHE C 39  ? 2.2382 2.0892 2.4644 -0.2269 -0.3640 0.2205  371 PHE D CE2 
6757  C CZ  . PHE C 39  ? 2.1976 2.0504 2.4082 -0.2264 -0.3685 0.2153  371 PHE D CZ  
6758  N N   . ALA C 40  ? 2.5837 2.4882 2.8522 -0.2525 -0.3982 0.3024  372 ALA D N   
6759  C CA  . ALA C 40  ? 2.4484 2.3552 2.7272 -0.2568 -0.4082 0.3189  372 ALA D CA  
6760  C C   . ALA C 40  ? 2.3285 2.2343 2.6196 -0.2555 -0.4098 0.3209  372 ALA D C   
6761  O O   . ALA C 40  ? 2.2504 2.1579 2.5441 -0.2608 -0.4192 0.3352  372 ALA D O   
6762  C CB  . ALA C 40  ? 2.4188 2.3218 2.7252 -0.2524 -0.4179 0.3248  372 ALA D CB  
6763  N N   . PRO C 41  ? 2.3444 2.2472 2.6440 -0.2496 -0.4014 0.3075  373 PRO D N   
6764  C CA  . PRO C 41  ? 2.2506 2.1543 2.5638 -0.2500 -0.4028 0.3103  373 PRO D CA  
6765  C C   . PRO C 41  ? 2.1489 2.0569 2.4320 -0.2603 -0.4022 0.3168  373 PRO D C   
6766  O O   . PRO C 41  ? 2.1194 2.0276 2.4102 -0.2611 -0.4009 0.3155  373 PRO D O   
6767  C CB  . PRO C 41  ? 2.3345 2.2329 2.6649 -0.2419 -0.3917 0.2931  373 PRO D CB  
6768  C CG  . PRO C 41  ? 2.2534 2.1480 2.5600 -0.2414 -0.3832 0.2820  373 PRO D CG  
6769  C CD  . PRO C 41  ? 2.3035 2.2007 2.6017 -0.2432 -0.3907 0.2898  373 PRO D CD  
6770  N N   . PHE C 42  ? 1.9782 1.8896 2.2285 -0.2686 -0.4030 0.3236  374 PHE D N   
6771  C CA  . PHE C 42  ? 1.8023 1.7165 2.0194 -0.2783 -0.4008 0.3274  374 PHE D CA  
6772  C C   . PHE C 42  ? 1.7772 1.6929 1.9912 -0.2862 -0.4132 0.3454  374 PHE D C   
6773  O O   . PHE C 42  ? 1.6254 1.5423 1.8317 -0.2917 -0.4206 0.3579  374 PHE D O   
6774  C CB  . PHE C 42  ? 1.7306 1.6474 1.9121 -0.2841 -0.3940 0.3246  374 PHE D CB  
6775  C CG  . PHE C 42  ? 1.7597 1.6732 1.9446 -0.2766 -0.3853 0.3089  374 PHE D CG  
6776  C CD1 . PHE C 42  ? 1.6079 1.5151 1.7970 -0.2709 -0.3768 0.2940  374 PHE D CD1 
6777  C CD2 . PHE C 42  ? 1.7727 1.6886 1.9543 -0.2764 -0.3854 0.3087  374 PHE D CD2 
6778  C CE1 . PHE C 42  ? 1.6786 1.5794 1.8686 -0.2644 -0.3704 0.2800  374 PHE D CE1 
6779  C CE2 . PHE C 42  ? 1.9925 1.9040 2.1765 -0.2695 -0.3792 0.2939  374 PHE D CE2 
6780  C CZ  . PHE C 42  ? 1.8818 1.7847 2.0689 -0.2634 -0.3724 0.2798  374 PHE D CZ  
6781  N N   . PHE C 43  ? 2.0184 1.9330 2.2375 -0.2878 -0.4153 0.3464  375 PHE D N   
6782  C CA  . PHE C 43  ? 2.0483 1.9619 2.2665 -0.2950 -0.4283 0.3625  375 PHE D CA  
6783  C C   . PHE C 43  ? 2.1382 2.0528 2.3139 -0.3077 -0.4300 0.3721  375 PHE D C   
6784  O O   . PHE C 43  ? 2.1500 2.0637 2.3211 -0.3151 -0.4390 0.3836  375 PHE D O   
6785  C CB  . PHE C 43  ? 1.8888 1.8011 2.1301 -0.2920 -0.4292 0.3581  375 PHE D CB  
6786  C CG  . PHE C 43  ? 1.8914 1.8020 2.1785 -0.2826 -0.4343 0.3572  375 PHE D CG  
6787  C CD1 . PHE C 43  ? 1.9198 1.8297 2.2260 -0.2743 -0.4323 0.3525  375 PHE D CD1 
6788  C CD2 . PHE C 43  ? 1.8022 1.7114 2.1134 -0.2828 -0.4424 0.3621  375 PHE D CD2 
6789  C CE1 . PHE C 43  ? 1.9057 1.8133 2.2530 -0.2660 -0.4375 0.3521  375 PHE D CE1 
6790  C CE2 . PHE C 43  ? 1.7103 1.6180 2.0643 -0.2747 -0.4477 0.3619  375 PHE D CE2 
6791  C CZ  . PHE C 43  ? 1.8640 1.7708 2.2356 -0.2662 -0.4451 0.3570  375 PHE D CZ  
6792  N N   . THR C 44  ? 1.8529 1.7698 1.9987 -0.3107 -0.4188 0.3638  376 THR D N   
6793  C CA  . THR C 44  ? 1.8281 1.7487 1.9355 -0.3226 -0.4157 0.3684  376 THR D CA  
6794  C C   . THR C 44  ? 1.8133 1.7365 1.8983 -0.3228 -0.4042 0.3595  376 THR D C   
6795  O O   . THR C 44  ? 1.7983 1.7182 1.8700 -0.3211 -0.3971 0.3498  376 THR D O   
6796  C CB  . THR C 44  ? 1.7054 1.6239 1.7938 -0.3298 -0.4161 0.3690  376 THR D CB  
6797  O OG1 . THR C 44  ? 1.8015 1.7170 1.9105 -0.3308 -0.4282 0.3784  376 THR D OG1 
6798  C CG2 . THR C 44  ? 1.7082 1.6319 1.7584 -0.3415 -0.4084 0.3682  376 THR D CG2 
6799  N N   . PHE C 45  ? 1.6231 1.5522 1.7046 -0.3254 -0.4023 0.3619  377 PHE D N   
6800  C CA  . PHE C 45  ? 1.5308 1.4633 1.5944 -0.3265 -0.3930 0.3552  377 PHE D CA  
6801  C C   . PHE C 45  ? 1.4864 1.4290 1.5241 -0.3389 -0.3883 0.3591  377 PHE D C   
6802  O O   . PHE C 45  ? 1.4592 1.4083 1.5029 -0.3424 -0.3911 0.3658  377 PHE D O   
6803  C CB  . PHE C 45  ? 1.6200 1.5519 1.7099 -0.3180 -0.3953 0.3534  377 PHE D CB  
6804  C CG  . PHE C 45  ? 1.6838 1.6196 1.7634 -0.3160 -0.3844 0.3401  377 PHE D CG  
6805  C CD1 . PHE C 45  ? 1.6295 1.5705 1.6751 -0.3253 -0.3766 0.3386  377 PHE D CD1 
6806  C CD2 . PHE C 45  ? 1.8121 1.7461 1.9167 -0.3051 -0.3824 0.3288  377 PHE D CD2 
6807  C CE1 . PHE C 45  ? 1.6901 1.6358 1.7282 -0.3231 -0.3675 0.3251  377 PHE D CE1 
6808  C CE2 . PHE C 45  ? 1.9768 1.9139 2.0727 -0.3029 -0.3743 0.3158  377 PHE D CE2 
6809  C CZ  . PHE C 45  ? 1.9361 1.8799 1.9992 -0.3115 -0.3671 0.3136  377 PHE D CZ  
6810  N N   . LYS C 46  ? 1.4468 1.3907 1.4559 -0.3462 -0.3813 0.3551  378 LYS D N   
6811  C CA  . LYS C 46  ? 1.4722 1.4256 1.4584 -0.3585 -0.3771 0.3588  378 LYS D CA  
6812  C C   . LYS C 46  ? 1.4651 1.4222 1.4223 -0.3635 -0.3641 0.3490  378 LYS D C   
6813  O O   . LYS C 46  ? 1.4429 1.3928 1.3852 -0.3628 -0.3591 0.3411  378 LYS D O   
6814  C CB  . LYS C 46  ? 1.5306 1.4814 1.5111 -0.3647 -0.3826 0.3648  378 LYS D CB  
6815  C CG  . LYS C 46  ? 1.5189 1.4693 1.5219 -0.3651 -0.3954 0.3769  378 LYS D CG  
6816  C CD  . LYS C 46  ? 1.5110 1.4708 1.5025 -0.3763 -0.3960 0.3847  378 LYS D CD  
6817  C CE  . LYS C 46  ? 1.4290 1.3848 1.4275 -0.3816 -0.4081 0.3957  378 LYS D CE  
6818  N NZ  . LYS C 46  ? 1.3267 1.2884 1.3343 -0.3862 -0.4145 0.4053  378 LYS D NZ  
6819  N N   . CYS C 47  ? 1.5256 1.4938 1.4756 -0.3689 -0.3592 0.3496  379 CYS D N   
6820  C CA  . CYS C 47  ? 1.6200 1.5953 1.5425 -0.3770 -0.3473 0.3416  379 CYS D CA  
6821  C C   . CYS C 47  ? 1.7206 1.7038 1.6240 -0.3901 -0.3440 0.3448  379 CYS D C   
6822  O O   . CYS C 47  ? 1.6380 1.6343 1.5407 -0.3985 -0.3451 0.3523  379 CYS D O   
6823  C CB  . CYS C 47  ? 1.5617 1.5479 1.4863 -0.3782 -0.3446 0.3414  379 CYS D CB  
6824  S SG  . CYS C 47  ? 1.6701 1.6509 1.5898 -0.3691 -0.3380 0.3251  379 CYS D SG  
6825  N N   . TYR C 48  ? 1.9560 1.9311 1.8432 -0.3929 -0.3402 0.3388  380 TYR D N   
6826  C CA  . TYR C 48  ? 1.9691 1.9494 1.8377 -0.4065 -0.3370 0.3396  380 TYR D CA  
6827  C C   . TYR C 48  ? 1.9874 1.9825 1.8360 -0.4160 -0.3269 0.3320  380 TYR D C   
6828  O O   . TYR C 48  ? 1.9665 1.9602 1.7934 -0.4220 -0.3207 0.3230  380 TYR D O   
6829  C CB  . TYR C 48  ? 1.7586 1.7243 1.6176 -0.4067 -0.3375 0.3351  380 TYR D CB  
6830  C CG  . TYR C 48  ? 1.6591 1.6126 1.5364 -0.3975 -0.3491 0.3429  380 TYR D CG  
6831  C CD1 . TYR C 48  ? 1.6281 1.5845 1.5256 -0.3954 -0.3602 0.3550  380 TYR D CD1 
6832  C CD2 . TYR C 48  ? 1.6235 1.5640 1.4993 -0.3910 -0.3503 0.3376  380 TYR D CD2 
6833  C CE1 . TYR C 48  ? 1.7363 1.6837 1.6544 -0.3878 -0.3725 0.3610  380 TYR D CE1 
6834  C CE2 . TYR C 48  ? 1.6221 1.5553 1.5183 -0.3833 -0.3628 0.3443  380 TYR D CE2 
6835  C CZ  . TYR C 48  ? 1.6751 1.6120 1.5939 -0.3819 -0.3739 0.3556  380 TYR D CZ  
6836  O OH  . TYR C 48  ? 1.4936 1.4236 1.4363 -0.3757 -0.3863 0.3614  380 TYR D OH  
6837  N N   . GLY C 49  ? 1.7086 1.7185 1.5640 -0.4171 -0.3262 0.3363  381 GLY D N   
6838  C CA  . GLY C 49  ? 1.7769 1.8053 1.6147 -0.4267 -0.3181 0.3318  381 GLY D CA  
6839  C C   . GLY C 49  ? 1.9306 1.9760 1.7783 -0.4274 -0.3184 0.3375  381 GLY D C   
6840  O O   . GLY C 49  ? 1.9409 2.0014 1.7921 -0.4360 -0.3210 0.3471  381 GLY D O   
6841  N N   . VAL C 50  ? 1.9069 1.9522 1.7588 -0.4148 -0.3158 0.3274  382 VAL D N   
6842  C CA  . VAL C 50  ? 1.8769 1.9399 1.7436 -0.4076 -0.3171 0.3257  382 VAL D CA  
6843  C C   . VAL C 50  ? 1.9482 1.9987 1.8420 -0.4058 -0.3287 0.3414  382 VAL D C   
6844  O O   . VAL C 50  ? 2.0238 2.0540 1.9249 -0.4034 -0.3351 0.3488  382 VAL D O   
6845  C CB  . VAL C 50  ? 1.8189 1.8877 1.6804 -0.3864 -0.3104 0.3002  382 VAL D CB  
6846  C CG1 . VAL C 50  ? 1.7507 1.7940 1.6197 -0.3746 -0.3130 0.2937  382 VAL D CG1 
6847  C CG2 . VAL C 50  ? 1.9289 2.0186 1.8062 -0.3783 -0.3118 0.2940  382 VAL D CG2 
6848  N N   . SER C 51  ? 1.9378 2.0045 1.8485 -0.4028 -0.3317 0.3421  383 SER D N   
6849  C CA  . SER C 51  ? 2.0163 2.0769 1.9554 -0.3976 -0.3421 0.3513  383 SER D CA  
6850  C C   . SER C 51  ? 2.0769 2.1158 2.0354 -0.3817 -0.3464 0.3443  383 SER D C   
6851  O O   . SER C 51  ? 2.1146 2.1421 2.0624 -0.3760 -0.3418 0.3343  383 SER D O   
6852  C CB  . SER C 51  ? 2.1073 2.1924 2.0605 -0.3942 -0.3404 0.3423  383 SER D CB  
6853  O OG  . SER C 51  ? 2.1479 2.2276 2.1326 -0.3839 -0.3473 0.3403  383 SER D OG  
6854  N N   . PRO C 52  ? 2.1391 2.1715 2.1266 -0.3744 -0.3553 0.3488  384 PRO D N   
6855  C CA  . PRO C 52  ? 2.2017 2.2184 2.2100 -0.3580 -0.3571 0.3372  384 PRO D CA  
6856  C C   . PRO C 52  ? 2.1900 2.2147 2.2131 -0.3454 -0.3528 0.3165  384 PRO D C   
6857  O O   . PRO C 52  ? 2.1480 2.1699 2.1609 -0.3371 -0.3468 0.3003  384 PRO D O   
6858  C CB  . PRO C 52  ? 2.2879 2.2936 2.3198 -0.3566 -0.3691 0.3517  384 PRO D CB  
6859  C CG  . PRO C 52  ? 2.2613 2.2784 2.2881 -0.3700 -0.3740 0.3678  384 PRO D CG  
6860  C CD  . PRO C 52  ? 2.1517 2.1861 2.1508 -0.3821 -0.3653 0.3671  384 PRO D CD  
6861  N N   . THR C 53  ? 2.2003 2.2333 2.2468 -0.3430 -0.3568 0.3163  385 THR D N   
6862  C CA  . THR C 53  ? 2.1976 2.2374 2.2581 -0.3306 -0.3543 0.2961  385 THR D CA  
6863  C C   . THR C 53  ? 2.1297 2.1956 2.1779 -0.3331 -0.3485 0.2860  385 THR D C   
6864  O O   . THR C 53  ? 2.0705 2.1425 2.1194 -0.3208 -0.3458 0.2660  385 THR D O   
6865  C CB  . THR C 53  ? 2.2083 2.2438 2.3018 -0.3252 -0.3617 0.2974  385 THR D CB  
6866  O OG1 . THR C 53  ? 2.1726 2.2158 2.2705 -0.3377 -0.3667 0.3154  385 THR D OG1 
6867  C CG2 . THR C 53  ? 2.3695 2.3809 2.4794 -0.3155 -0.3665 0.2979  385 THR D CG2 
6868  N N   . LYS C 54  ? 2.0349 2.4931 1.9323 -0.3157 -0.0127 0.1306  386 LYS D N   
6869  C CA  . LYS C 54  ? 1.9908 2.4870 1.9033 -0.3177 -0.0161 0.1390  386 LYS D CA  
6870  C C   . LYS C 54  ? 2.0424 2.5570 1.9798 -0.3050 -0.0184 0.1403  386 LYS D C   
6871  O O   . LYS C 54  ? 2.0871 2.6301 2.0362 -0.3092 -0.0223 0.1491  386 LYS D O   
6872  C CB  . LYS C 54  ? 1.8772 2.3921 1.7950 -0.3131 -0.0135 0.1379  386 LYS D CB  
6873  C CG  . LYS C 54  ? 1.8263 2.3760 1.7503 -0.3224 -0.0169 0.1482  386 LYS D CG  
6874  C CD  . LYS C 54  ? 1.7064 2.2796 1.6415 -0.3144 -0.0141 0.1469  386 LYS D CD  
6875  C CE  . LYS C 54  ? 1.6384 2.2398 1.5707 -0.3288 -0.0171 0.1573  386 LYS D CE  
6876  N NZ  . LYS C 54  ? 1.5500 2.1357 1.4551 -0.3500 -0.0194 0.1618  386 LYS D NZ  
6877  N N   . LEU C 55  ? 2.1533 2.6517 2.0986 -0.2902 -0.0164 0.1325  387 LEU D N   
6878  C CA  . LEU C 55  ? 2.1575 2.6725 2.1268 -0.2769 -0.0185 0.1331  387 LEU D CA  
6879  C C   . LEU C 55  ? 2.1520 2.6699 2.1216 -0.2871 -0.0241 0.1407  387 LEU D C   
6880  O O   . LEU C 55  ? 2.1924 2.7279 2.1828 -0.2782 -0.0268 0.1432  387 LEU D O   
6881  C CB  . LEU C 55  ? 2.0410 2.5362 2.0168 -0.2592 -0.0152 0.1227  387 LEU D CB  
6882  C CG  . LEU C 55  ? 1.9782 2.4358 1.9386 -0.2602 -0.0138 0.1166  387 LEU D CG  
6883  C CD1 . LEU C 55  ? 1.9755 2.4302 1.9454 -0.2564 -0.0175 0.1177  387 LEU D CD1 
6884  C CD2 . LEU C 55  ? 1.8820 2.3249 1.8446 -0.2454 -0.0091 0.1070  387 LEU D CD2 
6885  N N   . ASN C 56  ? 2.0398 2.5408 1.9870 -0.3058 -0.0258 0.1445  388 ASN D N   
6886  C CA  . ASN C 56  ? 1.9661 2.4762 1.9126 -0.3191 -0.0316 0.1540  388 ASN D CA  
6887  C C   . ASN C 56  ? 1.9466 2.4972 1.9131 -0.3191 -0.0353 0.1636  388 ASN D C   
6888  O O   . ASN C 56  ? 1.8305 2.3965 1.8124 -0.3177 -0.0396 0.1693  388 ASN D O   
6889  C CB  . ASN C 56  ? 1.8482 2.3398 1.7659 -0.3414 -0.0326 0.1581  388 ASN D CB  
6890  C CG  . ASN C 56  ? 1.8132 2.2646 1.7112 -0.3434 -0.0294 0.1502  388 ASN D CG  
6891  O OD1 . ASN C 56  ? 1.8748 2.3129 1.7726 -0.3435 -0.0311 0.1494  388 ASN D OD1 
6892  N ND2 . ASN C 56  ? 1.8423 2.2743 1.7246 -0.3442 -0.0247 0.1443  388 ASN D ND2 
6893  N N   . ASP C 57  ? 2.1004 2.6692 2.0675 -0.3205 -0.0335 0.1657  389 ASP D N   
6894  C CA  . ASP C 57  ? 2.1968 2.8035 2.1784 -0.3246 -0.0368 0.1764  389 ASP D CA  
6895  C C   . ASP C 57  ? 2.1899 2.8240 2.2025 -0.3045 -0.0357 0.1754  389 ASP D C   
6896  O O   . ASP C 57  ? 2.2190 2.8860 2.2455 -0.3043 -0.0365 0.1825  389 ASP D O   
6897  C CB  . ASP C 57  ? 2.2196 2.8338 2.1873 -0.3357 -0.0353 0.1793  389 ASP D CB  
6898  C CG  . ASP C 57  ? 2.1591 2.7414 2.0946 -0.3535 -0.0352 0.1782  389 ASP D CG  
6899  O OD1 . ASP C 57  ? 2.1775 2.7427 2.1017 -0.3640 -0.0383 0.1807  389 ASP D OD1 
6900  O OD2 . ASP C 57  ? 2.1301 2.7039 2.0516 -0.3570 -0.0320 0.1748  389 ASP D OD2 
6901  N N   . LEU C 58  ? 1.9328 2.5539 1.9561 -0.2879 -0.0338 0.1669  390 LEU D N   
6902  C CA  . LEU C 58  ? 1.8560 2.4998 1.9078 -0.2686 -0.0329 0.1655  390 LEU D CA  
6903  C C   . LEU C 58  ? 1.8196 2.4513 1.8804 -0.2610 -0.0357 0.1632  390 LEU D C   
6904  O O   . LEU C 58  ? 1.7962 2.3964 1.8442 -0.2594 -0.0344 0.1554  390 LEU D O   
6905  C CB  . LEU C 58  ? 1.7823 2.4234 1.8383 -0.2527 -0.0264 0.1554  390 LEU D CB  
6906  C CG  . LEU C 58  ? 1.7215 2.3852 1.8049 -0.2320 -0.0240 0.1526  390 LEU D CG  
6907  C CD1 . LEU C 58  ? 1.6457 2.3496 1.7481 -0.2334 -0.0260 0.1633  390 LEU D CD1 
6908  C CD2 . LEU C 58  ? 1.5832 2.2393 1.6648 -0.2199 -0.0176 0.1425  390 LEU D CD2 
6909  N N   . CYS C 59  ? 1.7696 2.4266 1.8522 -0.2570 -0.0396 0.1704  391 CYS D N   
6910  C CA  . CYS C 59  ? 1.8095 2.4596 1.9041 -0.2488 -0.0428 0.1691  391 CYS D CA  
6911  C C   . CYS C 59  ? 1.7511 2.4052 1.8659 -0.2253 -0.0394 0.1609  391 CYS D C   
6912  O O   . CYS C 59  ? 1.7352 2.4117 1.8643 -0.2151 -0.0361 0.1606  391 CYS D O   
6913  C CB  . CYS C 59  ? 1.8272 2.5016 1.9354 -0.2571 -0.0495 0.1817  391 CYS D CB  
6914  S SG  . CYS C 59  ? 1.9452 2.6200 2.0311 -0.2857 -0.0541 0.1933  391 CYS D SG  
6915  N N   . PHE C 60  ? 1.7463 2.3783 1.8615 -0.2171 -0.0402 0.1543  392 PHE D N   
6916  C CA  . PHE C 60  ? 1.7950 2.4240 1.9251 -0.1956 -0.0371 0.1454  392 PHE D CA  
6917  C C   . PHE C 60  ? 1.7949 2.4319 1.9445 -0.1880 -0.0421 0.1485  392 PHE D C   
6918  O O   . PHE C 60  ? 1.7767 2.4093 1.9222 -0.1997 -0.0476 0.1545  392 PHE D O   
6919  C CB  . PHE C 60  ? 1.7874 2.3811 1.8999 -0.1917 -0.0333 0.1342  392 PHE D CB  
6920  C CG  . PHE C 60  ? 1.7346 2.3212 1.8305 -0.1966 -0.0281 0.1306  392 PHE D CG  
6921  C CD1 . PHE C 60  ? 1.7533 2.3537 1.8583 -0.1849 -0.0233 0.1266  392 PHE D CD1 
6922  C CD2 . PHE C 60  ? 1.6542 2.2206 1.7253 -0.2135 -0.0281 0.1314  392 PHE D CD2 
6923  C CE1 . PHE C 60  ? 1.7105 2.3052 1.8005 -0.1903 -0.0190 0.1237  392 PHE D CE1 
6924  C CE2 . PHE C 60  ? 1.6730 2.2329 1.7291 -0.2184 -0.0237 0.1285  392 PHE D CE2 
6925  C CZ  . PHE C 60  ? 1.7052 2.2798 1.7710 -0.2069 -0.0194 0.1248  392 PHE D CZ  
6926  N N   . THR C 61  ? 1.8827 2.5311 2.0531 -0.1688 -0.0403 0.1444  393 THR D N   
6927  C CA  . THR C 61  ? 1.9512 2.6104 2.1426 -0.1605 -0.0451 0.1479  393 THR D CA  
6928  C C   . THR C 61  ? 2.0692 2.6990 2.2532 -0.1586 -0.0481 0.1423  393 THR D C   
6929  O O   . THR C 61  ? 1.9779 2.6107 2.1695 -0.1625 -0.0542 0.1479  393 THR D O   
6930  C CB  . THR C 61  ? 2.0159 2.6952 2.2311 -0.1403 -0.0419 0.1451  393 THR D CB  
6931  O OG1 . THR C 61  ? 2.0861 2.7759 2.3221 -0.1324 -0.0469 0.1489  393 THR D OG1 
6932  C CG2 . THR C 61  ? 2.0024 2.6612 2.2120 -0.1260 -0.0363 0.1325  393 THR D CG2 
6933  N N   . ASN C 62  ? 2.5088 3.1107 2.6781 -0.1534 -0.0440 0.1319  394 ASN D N   
6934  C CA  . ASN C 62  ? 2.4226 2.9966 2.5850 -0.1507 -0.0463 0.1264  394 ASN D CA  
6935  C C   . ASN C 62  ? 2.3373 2.8821 2.4777 -0.1518 -0.0411 0.1175  394 ASN D C   
6936  O O   . ASN C 62  ? 2.3362 2.8775 2.4789 -0.1389 -0.0363 0.1102  394 ASN D O   
6937  C CB  . ASN C 62  ? 2.3991 2.9766 2.5821 -0.1313 -0.0476 0.1223  394 ASN D CB  
6938  C CG  . ASN C 62  ? 2.4130 2.9957 2.6079 -0.1334 -0.0552 0.1283  394 ASN D CG  
6939  O OD1 . ASN C 62  ? 2.3739 2.9620 2.5641 -0.1494 -0.0595 0.1367  394 ASN D OD1 
6940  N ND2 . ASN C 62  ? 2.3789 2.9592 2.5886 -0.1175 -0.0569 0.1242  394 ASN D ND2 
6941  N N   . VAL C 63  ? 1.7862 2.3099 1.9052 -0.1671 -0.0418 0.1182  395 VAL D N   
6942  C CA  . VAL C 63  ? 1.5869 2.0807 1.6863 -0.1671 -0.0371 0.1098  395 VAL D CA  
6943  C C   . VAL C 63  ? 1.5572 2.0289 1.6583 -0.1566 -0.0383 0.1034  395 VAL D C   
6944  O O   . VAL C 63  ? 1.5888 2.0585 1.6943 -0.1594 -0.0435 0.1065  395 VAL D O   
6945  C CB  . VAL C 63  ? 1.4510 1.9304 1.5265 -0.1873 -0.0367 0.1130  395 VAL D CB  
6946  C CG1 . VAL C 63  ? 1.3878 1.8382 1.4448 -0.1864 -0.0313 0.1048  395 VAL D CG1 
6947  C CG2 . VAL C 63  ? 1.4552 1.9578 1.5302 -0.1971 -0.0362 0.1199  395 VAL D CG2 
6948  N N   . TYR C 64  ? 1.3106 1.7668 1.4089 -0.1446 -0.0339 0.0948  396 TYR D N   
6949  C CA  . TYR C 64  ? 1.2634 1.6975 1.3619 -0.1345 -0.0347 0.0885  396 TYR D CA  
6950  C C   . TYR C 64  ? 1.1801 1.5837 1.2561 -0.1405 -0.0305 0.0834  396 TYR D C   
6951  O O   . TYR C 64  ? 1.1723 1.5725 1.2399 -0.1408 -0.0255 0.0805  396 TYR D O   
6952  C CB  . TYR C 64  ? 1.2613 1.7025 1.3762 -0.1147 -0.0334 0.0832  396 TYR D CB  
6953  C CG  . TYR C 64  ? 1.3278 1.7929 1.4663 -0.1056 -0.0379 0.0869  396 TYR D CG  
6954  C CD1 . TYR C 64  ? 1.3502 1.8173 1.4949 -0.1099 -0.0443 0.0918  396 TYR D CD1 
6955  C CD2 . TYR C 64  ? 1.3999 1.8857 1.5545 -0.0928 -0.0357 0.0858  396 TYR D CD2 
6956  C CE1 . TYR C 64  ? 1.5328 2.0217 1.6998 -0.1015 -0.0487 0.0957  396 TYR D CE1 
6957  C CE2 . TYR C 64  ? 1.4643 1.9715 1.6409 -0.0838 -0.0395 0.0893  396 TYR D CE2 
6958  C CZ  . TYR C 64  ? 1.5643 2.0729 1.7473 -0.0882 -0.0461 0.0944  396 TYR D CZ  
6959  O OH  . TYR C 64  ? 1.6274 2.1571 1.8329 -0.0796 -0.0501 0.0984  396 TYR D OH  
6960  N N   . ALA C 65  ? 1.1885 1.5702 1.2546 -0.1459 -0.0324 0.0826  397 ALA D N   
6961  C CA  . ALA C 65  ? 1.1489 1.5008 1.1941 -0.1516 -0.0281 0.0782  397 ALA D CA  
6962  C C   . ALA C 65  ? 1.1358 1.4673 1.1831 -0.1384 -0.0277 0.0716  397 ALA D C   
6963  O O   . ALA C 65  ? 1.1590 1.4824 1.2088 -0.1380 -0.0316 0.0720  397 ALA D O   
6964  C CB  . ALA C 65  ? 1.1553 1.4960 1.1839 -0.1701 -0.0293 0.0825  397 ALA D CB  
6965  N N   . ASP C 66  ? 1.1107 1.4344 1.1573 -0.1280 -0.0234 0.0659  398 ASP D N   
6966  C CA  . ASP C 66  ? 0.9939 1.2966 1.0403 -0.1168 -0.0227 0.0601  398 ASP D CA  
6967  C C   . ASP C 66  ? 1.0062 1.2802 1.0326 -0.1246 -0.0186 0.0577  398 ASP D C   
6968  O O   . ASP C 66  ? 0.9790 1.2481 0.9930 -0.1323 -0.0142 0.0577  398 ASP D O   
6969  C CB  . ASP C 66  ? 0.9919 1.3002 1.0476 -0.1019 -0.0203 0.0555  398 ASP D CB  
6970  C CG  . ASP C 66  ? 1.0403 1.3773 1.1139 -0.0951 -0.0227 0.0577  398 ASP D CG  
6971  O OD1 . ASP C 66  ? 1.0759 1.4253 1.1599 -0.0960 -0.0277 0.0617  398 ASP D OD1 
6972  O OD2 . ASP C 66  ? 1.0730 1.4207 1.1506 -0.0893 -0.0195 0.0557  398 ASP D OD2 
6973  N N   . SER C 67  ? 0.9746 1.2295 0.9982 -0.1222 -0.0200 0.0559  399 SER D N   
6974  C CA  . SER C 67  ? 0.9227 1.1494 0.9285 -0.1281 -0.0155 0.0535  399 SER D CA  
6975  C C   . SER C 67  ? 0.9250 1.1342 0.9339 -0.1149 -0.0150 0.0488  399 SER D C   
6976  O O   . SER C 67  ? 0.9468 1.1599 0.9678 -0.1060 -0.0196 0.0483  399 SER D O   
6977  C CB  . SER C 67  ? 0.9672 1.1842 0.9610 -0.1431 -0.0167 0.0569  399 SER D CB  
6978  O OG  . SER C 67  ? 0.9574 1.1825 0.9617 -0.1417 -0.0228 0.0592  399 SER D OG  
6979  N N   . PHE C 68  ? 0.8844 1.0748 0.8828 -0.1137 -0.0096 0.0457  400 PHE D N   
6980  C CA  . PHE C 68  ? 0.8978 1.0685 0.8967 -0.1030 -0.0087 0.0420  400 PHE D CA  
6981  C C   . PHE C 68  ? 0.8849 1.0313 0.8675 -0.1083 -0.0023 0.0405  400 PHE D C   
6982  O O   . PHE C 68  ? 0.9134 1.0547 0.8828 -0.1213 0.0009  0.0423  400 PHE D O   
6983  C CB  . PHE C 68  ? 0.8574 1.0388 0.8707 -0.0875 -0.0103 0.0394  400 PHE D CB  
6984  C CG  . PHE C 68  ? 0.8769 1.0716 0.8911 -0.0869 -0.0074 0.0388  400 PHE D CG  
6985  C CD1 . PHE C 68  ? 0.9003 1.1213 0.9249 -0.0866 -0.0098 0.0407  400 PHE D CD1 
6986  C CD2 . PHE C 68  ? 0.7858 0.9672 0.7906 -0.0872 -0.0023 0.0369  400 PHE D CD2 
6987  C CE1 . PHE C 68  ? 0.8555 1.0893 0.8807 -0.0865 -0.0068 0.0402  400 PHE D CE1 
6988  C CE2 . PHE C 68  ? 0.7397 0.9338 0.7450 -0.0875 0.0002  0.0365  400 PHE D CE2 
6989  C CZ  . PHE C 68  ? 0.7770 0.9970 0.7920 -0.0872 -0.0020 0.0380  400 PHE D CZ  
6990  N N   . VAL C 69  ? 0.9180 1.0489 0.9014 -0.0984 -0.0005 0.0377  401 VAL D N   
6991  C CA  . VAL C 69  ? 0.9208 1.0278 0.8906 -0.1019 0.0055  0.0367  401 VAL D CA  
6992  C C   . VAL C 69  ? 0.8759 0.9772 0.8511 -0.0895 0.0068  0.0344  401 VAL D C   
6993  O O   . VAL C 69  ? 0.8840 0.9907 0.8711 -0.0778 0.0029  0.0331  401 VAL D O   
6994  C CB  . VAL C 69  ? 0.8792 0.9651 0.8410 -0.1059 0.0065  0.0370  401 VAL D CB  
6995  C CG1 . VAL C 69  ? 0.9486 1.0316 0.9210 -0.0935 0.0030  0.0357  401 VAL D CG1 
6996  C CG2 . VAL C 69  ? 0.8651 0.9265 0.8124 -0.1106 0.0134  0.0364  401 VAL D CG2 
6997  N N   . ILE C 70  ? 0.9222 1.0122 0.8881 -0.0927 0.0120  0.0340  402 ILE D N   
6998  C CA  . ILE C 70  ? 0.8568 0.9417 0.8265 -0.0830 0.0135  0.0324  402 ILE D CA  
6999  C C   . ILE C 70  ? 0.8766 0.9379 0.8334 -0.0881 0.0195  0.0330  402 ILE D C   
7000  O O   . ILE C 70  ? 0.9041 0.9500 0.8517 -0.0951 0.0219  0.0338  402 ILE D O   
7001  C CB  . ILE C 70  ? 0.7897 0.8959 0.7657 -0.0805 0.0127  0.0317  402 ILE D CB  
7002  C CG1 . ILE C 70  ? 0.8283 0.9423 0.7953 -0.0933 0.0153  0.0332  402 ILE D CG1 
7003  C CG2 . ILE C 70  ? 0.6838 0.8119 0.6738 -0.0736 0.0072  0.0312  402 ILE D CG2 
7004  C CD1 . ILE C 70  ? 0.7973 0.9373 0.7720 -0.0921 0.0138  0.0330  402 ILE D CD1 
7005  N N   . ARG C 71  ? 0.7805 0.8381 0.7363 -0.0852 0.0222  0.0326  403 ARG D N   
7006  C CA  . ARG C 71  ? 0.8216 0.8600 0.7650 -0.0920 0.0280  0.0336  403 ARG D CA  
7007  C C   . ARG C 71  ? 0.8866 0.9346 0.8276 -0.0957 0.0297  0.0337  403 ARG D C   
7008  O O   . ARG C 71  ? 0.9238 0.9896 0.8737 -0.0899 0.0270  0.0326  403 ARG D O   
7009  C CB  . ARG C 71  ? 0.8999 0.9178 0.8443 -0.0841 0.0299  0.0341  403 ARG D CB  
7010  C CG  . ARG C 71  ? 0.9844 1.0112 0.9402 -0.0722 0.0267  0.0332  403 ARG D CG  
7011  C CD  . ARG C 71  ? 0.9832 0.9958 0.9438 -0.0619 0.0265  0.0341  403 ARG D CD  
7012  N NE  . ARG C 71  ? 1.0841 1.1022 1.0469 -0.0589 0.0269  0.0340  403 ARG D NE  
7013  C CZ  . ARG C 71  ? 1.1295 1.1434 1.0981 -0.0498 0.0253  0.0346  403 ARG D CZ  
7014  N NH1 . ARG C 71  ? 1.1951 1.1999 1.1687 -0.0418 0.0229  0.0354  403 ARG D NH1 
7015  N NH2 . ARG C 71  ? 1.0536 1.0745 1.0232 -0.0486 0.0255  0.0343  403 ARG D NH2 
7016  N N   . GLY C 72  ? 0.9596 0.9951 0.8881 -0.1055 0.0345  0.0349  404 GLY D N   
7017  C CA  . GLY C 72  ? 0.9755 1.0151 0.8995 -0.1101 0.0367  0.0353  404 GLY D CA  
7018  C C   . GLY C 72  ? 0.9763 1.0336 0.9103 -0.1025 0.0341  0.0342  404 GLY D C   
7019  O O   . GLY C 72  ? 0.9760 1.0547 0.9129 -0.1052 0.0321  0.0336  404 GLY D O   
7020  N N   . ASN C 73  ? 1.0419 1.0911 0.9815 -0.0931 0.0341  0.0339  405 ASN D N   
7021  C CA  . ASN C 73  ? 1.1267 1.1907 1.0741 -0.0865 0.0321  0.0326  405 ASN D CA  
7022  C C   . ASN C 73  ? 1.1379 1.2256 1.0952 -0.0818 0.0279  0.0306  405 ASN D C   
7023  O O   . ASN C 73  ? 1.1523 1.2578 1.1132 -0.0813 0.0273  0.0295  405 ASN D O   
7024  C CB  . ASN C 73  ? 1.2161 1.2680 1.1688 -0.0763 0.0316  0.0328  405 ASN D CB  
7025  C CG  . ASN C 73  ? 1.3191 1.3467 1.2644 -0.0791 0.0356  0.0355  405 ASN D CG  
7026  O OD1 . ASN C 73  ? 1.3459 1.3585 1.2870 -0.0812 0.0374  0.0366  405 ASN D OD1 
7027  N ND2 . ASN C 73  ? 1.3682 1.3920 1.3124 -0.0790 0.0371  0.0367  405 ASN D ND2 
7028  N N   . GLU C 74  ? 0.9495 1.0382 0.9122 -0.0777 0.0250  0.0302  406 GLU D N   
7029  C CA  . GLU C 74  ? 0.8502 0.9619 0.8230 -0.0735 0.0210  0.0288  406 GLU D CA  
7030  C C   . GLU C 74  ? 0.8220 0.9528 0.7922 -0.0831 0.0214  0.0295  406 GLU D C   
7031  O O   . GLU C 74  ? 0.7734 0.9258 0.7521 -0.0795 0.0195  0.0285  406 GLU D O   
7032  C CB  . GLU C 74  ? 0.8974 1.0075 0.8759 -0.0694 0.0174  0.0288  406 GLU D CB  
7033  C CG  . GLU C 74  ? 0.8389 0.9456 0.8274 -0.0562 0.0138  0.0275  406 GLU D CG  
7034  C CD  . GLU C 74  ? 0.9142 1.0014 0.9012 -0.0501 0.0148  0.0277  406 GLU D CD  
7035  O OE1 . GLU C 74  ? 1.1322 1.2007 1.1107 -0.0554 0.0179  0.0294  406 GLU D OE1 
7036  O OE2 . GLU C 74  ? 0.9601 1.0513 0.9550 -0.0398 0.0121  0.0263  406 GLU D OE2 
7037  N N   . VAL C 75  ? 0.8235 0.9471 0.7823 -0.0954 0.0238  0.0316  407 VAL D N   
7038  C CA  . VAL C 75  ? 0.8377 0.9801 0.7947 -0.1048 0.0230  0.0331  407 VAL D CA  
7039  C C   . VAL C 75  ? 0.8735 1.0362 0.8346 -0.1041 0.0233  0.0324  407 VAL D C   
7040  O O   . VAL C 75  ? 0.8891 1.0750 0.8575 -0.1043 0.0211  0.0329  407 VAL D O   
7041  C CB  . VAL C 75  ? 0.8052 0.9342 0.7469 -0.1188 0.0260  0.0353  407 VAL D CB  
7042  C CG1 . VAL C 75  ? 0.7970 0.9442 0.7344 -0.1292 0.0260  0.0372  407 VAL D CG1 
7043  C CG2 . VAL C 75  ? 0.8952 1.0151 0.8347 -0.1214 0.0247  0.0362  407 VAL D CG2 
7044  N N   . SER C 76  ? 0.8281 0.9826 0.7851 -0.1031 0.0260  0.0315  408 SER D N   
7045  C CA  . SER C 76  ? 0.7741 0.9455 0.7343 -0.1021 0.0267  0.0305  408 SER D CA  
7046  C C   . SER C 76  ? 0.8009 0.9943 0.7752 -0.0921 0.0239  0.0286  408 SER D C   
7047  O O   . SER C 76  ? 0.8332 1.0469 0.8110 -0.0931 0.0243  0.0282  408 SER D O   
7048  C CB  . SER C 76  ? 0.8339 0.9902 0.7910 -0.0984 0.0289  0.0295  408 SER D CB  
7049  O OG  . SER C 76  ? 0.9490 1.0823 0.8943 -0.1057 0.0317  0.0314  408 SER D OG  
7050  N N   . GLN C 77  ? 0.8304 1.0197 0.8131 -0.0823 0.0213  0.0273  409 GLN D N   
7051  C CA  . GLN C 77  ? 0.8641 1.0716 0.8604 -0.0716 0.0187  0.0253  409 GLN D CA  
7052  C C   . GLN C 77  ? 0.8829 1.1104 0.8859 -0.0743 0.0162  0.0270  409 GLN D C   
7053  O O   . GLN C 77  ? 0.8869 1.1339 0.9016 -0.0668 0.0147  0.0258  409 GLN D O   
7054  C CB  . GLN C 77  ? 0.8431 1.0376 0.8455 -0.0598 0.0164  0.0234  409 GLN D CB  
7055  C CG  . GLN C 77  ? 0.8357 1.0150 0.8353 -0.0540 0.0179  0.0218  409 GLN D CG  
7056  C CD  . GLN C 77  ? 0.8225 0.9809 0.8225 -0.0479 0.0161  0.0220  409 GLN D CD  
7057  O OE1 . GLN C 77  ? 0.8325 0.9946 0.8412 -0.0396 0.0126  0.0210  409 GLN D OE1 
7058  N NE2 . GLN C 77  ? 0.8263 0.9634 0.8173 -0.0520 0.0184  0.0237  409 GLN D NE2 
7059  N N   . ILE C 78  ? 0.8321 1.0550 0.8283 -0.0845 0.0158  0.0300  410 ILE D N   
7060  C CA  . ILE C 78  ? 0.8111 1.0534 0.8141 -0.0876 0.0129  0.0325  410 ILE D CA  
7061  C C   . ILE C 78  ? 0.9303 1.1926 0.9316 -0.0954 0.0146  0.0342  410 ILE D C   
7062  O O   . ILE C 78  ? 0.9736 1.2355 0.9648 -0.1084 0.0154  0.0374  410 ILE D O   
7063  C CB  . ILE C 78  ? 0.8039 1.0341 0.8002 -0.0960 0.0114  0.0351  410 ILE D CB  
7064  C CG1 . ILE C 78  ? 0.8280 1.0383 0.8262 -0.0876 0.0099  0.0332  410 ILE D CG1 
7065  C CG2 . ILE C 78  ? 0.8465 1.0976 0.8503 -0.0996 0.0079  0.0383  410 ILE D CG2 
7066  C CD1 . ILE C 78  ? 0.8235 1.0432 0.8369 -0.0732 0.0067  0.0309  410 ILE D CD1 
7067  N N   . ALA C 79  ? 0.9446 1.2237 0.9551 -0.0875 0.0152  0.0322  411 ALA D N   
7068  C CA  . ALA C 79  ? 0.9956 1.2924 1.0046 -0.0927 0.0176  0.0329  411 ALA D CA  
7069  C C   . ALA C 79  ? 1.0133 1.3297 1.0365 -0.0807 0.0177  0.0303  411 ALA D C   
7070  O O   . ALA C 79  ? 0.9881 1.2967 1.0176 -0.0687 0.0170  0.0269  411 ALA D O   
7071  C CB  . ALA C 79  ? 1.0782 1.3592 1.0740 -0.0984 0.0210  0.0319  411 ALA D CB  
7072  N N   . PRO C 80  ? 1.0893 1.4310 1.1176 -0.0833 0.0186  0.0319  412 PRO D N   
7073  C CA  . PRO C 80  ? 1.0936 1.4541 1.1356 -0.0714 0.0194  0.0292  412 PRO D CA  
7074  C C   . PRO C 80  ? 1.0765 1.4274 1.1147 -0.0653 0.0226  0.0244  412 PRO D C   
7075  O O   . PRO C 80  ? 1.0344 1.3785 1.0614 -0.0731 0.0249  0.0244  412 PRO D O   
7076  C CB  . PRO C 80  ? 1.0662 1.4548 1.1123 -0.0782 0.0203  0.0329  412 PRO D CB  
7077  C CG  . PRO C 80  ? 1.1103 1.4912 1.1407 -0.0934 0.0214  0.0357  412 PRO D CG  
7078  C CD  . PRO C 80  ? 1.1640 1.5165 1.1841 -0.0973 0.0198  0.0358  412 PRO D CD  
7079  N N   . GLY C 81  ? 1.0994 1.4489 1.1465 -0.0519 0.0222  0.0206  413 GLY D N   
7080  C CA  . GLY C 81  ? 1.1385 1.4807 1.1828 -0.0456 0.0250  0.0162  413 GLY D CA  
7081  C C   . GLY C 81  ? 1.1484 1.4618 1.1840 -0.0440 0.0243  0.0145  413 GLY D C   
7082  O O   . GLY C 81  ? 1.0879 1.3934 1.1259 -0.0341 0.0245  0.0110  413 GLY D O   
7083  N N   . GLN C 82  ? 1.1718 1.4693 1.1972 -0.0538 0.0236  0.0174  414 GLN D N   
7084  C CA  . GLN C 82  ? 1.1571 1.4269 1.1750 -0.0528 0.0230  0.0170  414 GLN D CA  
7085  C C   . GLN C 82  ? 1.1338 1.3955 1.1598 -0.0401 0.0202  0.0147  414 GLN D C   
7086  O O   . GLN C 82  ? 1.2071 1.4764 1.2417 -0.0361 0.0174  0.0154  414 GLN D O   
7087  C CB  . GLN C 82  ? 1.0602 1.3170 1.0693 -0.0636 0.0223  0.0206  414 GLN D CB  
7088  C CG  . GLN C 82  ? 1.0571 1.3130 1.0547 -0.0762 0.0250  0.0226  414 GLN D CG  
7089  C CD  . GLN C 82  ? 1.2039 1.4440 1.1945 -0.0756 0.0272  0.0211  414 GLN D CD  
7090  O OE1 . GLN C 82  ? 1.2370 1.4583 1.2274 -0.0692 0.0264  0.0201  414 GLN D OE1 
7091  N NE2 . GLN C 82  ? 1.2712 1.5202 1.2570 -0.0817 0.0296  0.0212  414 GLN D NE2 
7092  N N   . THR C 83  ? 1.0998 1.3468 1.1233 -0.0338 0.0207  0.0124  415 THR D N   
7093  C CA  . THR C 83  ? 1.0594 1.2946 1.0882 -0.0226 0.0177  0.0107  415 THR D CA  
7094  C C   . THR C 83  ? 0.9373 1.1467 0.9571 -0.0244 0.0178  0.0118  415 THR D C   
7095  O O   . THR C 83  ? 0.8594 1.0615 0.8753 -0.0223 0.0192  0.0105  415 THR D O   
7096  C CB  . THR C 83  ? 1.0414 1.2848 1.0774 -0.0112 0.0178  0.0068  415 THR D CB  
7097  O OG1 . THR C 83  ? 0.8773 1.1088 0.9059 -0.0107 0.0198  0.0054  415 THR D OG1 
7098  C CG2 . THR C 83  ? 1.0209 1.2924 1.0654 -0.0100 0.0194  0.0057  415 THR D CG2 
7099  N N   . GLY C 84  ? 0.9788 1.1753 0.9953 -0.0287 0.0164  0.0145  416 GLY D N   
7100  C CA  . GLY C 84  ? 0.9837 1.1560 0.9956 -0.0267 0.0155  0.0156  416 GLY D CA  
7101  C C   . GLY C 84  ? 0.9603 1.1286 0.9803 -0.0159 0.0113  0.0146  416 GLY D C   
7102  O O   . GLY C 84  ? 0.9068 1.0880 0.9351 -0.0076 0.0097  0.0120  416 GLY D O   
7103  N N   . ASN C 85  ? 0.9487 1.0982 0.9657 -0.0161 0.0099  0.0167  417 ASN D N   
7104  C CA  . ASN C 85  ? 0.8920 1.0354 0.9154 -0.0075 0.0056  0.0164  417 ASN D CA  
7105  C C   . ASN C 85  ? 0.8529 1.0086 0.8826 -0.0086 0.0030  0.0167  417 ASN D C   
7106  O O   . ASN C 85  ? 0.8754 1.0342 0.9133 -0.0005 -0.0011 0.0158  417 ASN D O   
7107  C CB  . ASN C 85  ? 0.9334 1.0528 0.9510 -0.0086 0.0054  0.0190  417 ASN D CB  
7108  C CG  . ASN C 85  ? 0.9728 1.0834 0.9959 0.0016  0.0009  0.0189  417 ASN D CG  
7109  O OD1 . ASN C 85  ? 0.8767 0.9980 0.9077 0.0098  -0.0024 0.0166  417 ASN D OD1 
7110  N ND2 . ASN C 85  ? 1.0331 1.1241 1.0520 0.0010  0.0007  0.0215  417 ASN D ND2 
7111  N N   . ILE C 86  ? 0.8876 1.0496 0.9133 -0.0190 0.0050  0.0184  418 ILE D N   
7112  C CA  . ILE C 86  ? 0.9018 1.0718 0.9324 -0.0211 0.0021  0.0196  418 ILE D CA  
7113  C C   . ILE C 86  ? 0.9088 1.1050 0.9482 -0.0202 0.0015  0.0188  418 ILE D C   
7114  O O   . ILE C 86  ? 0.9189 1.1256 0.9678 -0.0158 -0.0023 0.0190  418 ILE D O   
7115  C CB  . ILE C 86  ? 0.8422 1.0019 0.8628 -0.0333 0.0043  0.0224  418 ILE D CB  
7116  C CG1 . ILE C 86  ? 0.8813 1.0373 0.9048 -0.0335 0.0007  0.0237  418 ILE D CG1 
7117  C CG2 . ILE C 86  ? 0.8144 0.9912 0.8329 -0.0432 0.0061  0.0236  418 ILE D CG2 
7118  C CD1 . ILE C 86  ? 0.8984 1.0379 0.9111 -0.0432 0.0030  0.0259  418 ILE D CD1 
7119  N N   . ALA C 87  ? 0.8739 1.0813 0.9111 -0.0234 0.0050  0.0180  419 ALA D N   
7120  C CA  . ALA C 87  ? 0.8696 1.1028 0.9147 -0.0234 0.0051  0.0178  419 ALA D CA  
7121  C C   . ALA C 87  ? 0.9116 1.1543 0.9670 -0.0104 0.0040  0.0145  419 ALA D C   
7122  O O   . ALA C 87  ? 0.9708 1.2333 1.0319 -0.0087 0.0057  0.0134  419 ALA D O   
7123  C CB  . ALA C 87  ? 0.8789 1.1207 0.9169 -0.0331 0.0093  0.0187  419 ALA D CB  
7124  N N   . ASP C 88  ? 0.9413 1.1700 0.9988 -0.0013 0.0013  0.0129  420 ASP D N   
7125  C CA  . ASP C 88  ? 0.9863 1.2243 1.0538 0.0110  -0.0002 0.0099  420 ASP D CA  
7126  C C   . ASP C 88  ? 0.9865 1.2093 1.0567 0.0190  -0.0049 0.0095  420 ASP D C   
7127  O O   . ASP C 88  ? 1.0307 1.2565 1.1083 0.0298  -0.0071 0.0071  420 ASP D O   
7128  C CB  . ASP C 88  ? 1.0688 1.3075 1.1327 0.0145  0.0035  0.0067  420 ASP D CB  
7129  C CG  . ASP C 88  ? 1.0258 1.2427 1.0778 0.0107  0.0052  0.0071  420 ASP D CG  
7130  O OD1 . ASP C 88  ? 1.0099 1.2121 1.0567 0.0055  0.0040  0.0098  420 ASP D OD1 
7131  O OD2 . ASP C 88  ? 1.0592 1.2739 1.1072 0.0129  0.0078  0.0049  420 ASP D OD2 
7132  N N   . TYR C 89  ? 0.8513 1.0578 0.9157 0.0138  -0.0064 0.0120  421 TYR D N   
7133  C CA  . TYR C 89  ? 0.8428 1.0402 0.9120 0.0203  -0.0116 0.0124  421 TYR D CA  
7134  C C   . TYR C 89  ? 0.8668 1.0678 0.9386 0.0139  -0.0143 0.0154  421 TYR D C   
7135  O O   . TYR C 89  ? 0.8764 1.0746 0.9544 0.0192  -0.0192 0.0158  421 TYR D O   
7136  C CB  . TYR C 89  ? 0.9128 1.0858 0.9745 0.0226  -0.0122 0.0127  421 TYR D CB  
7137  C CG  . TYR C 89  ? 0.9356 1.1044 0.9967 0.0312  -0.0116 0.0099  421 TYR D CG  
7138  C CD1 . TYR C 89  ? 0.9367 1.1158 1.0065 0.0413  -0.0139 0.0072  421 TYR D CD1 
7139  C CD2 . TYR C 89  ? 0.9333 1.0850 0.9852 0.0297  -0.0094 0.0105  421 TYR D CD2 
7140  C CE1 . TYR C 89  ? 0.9217 1.0958 0.9897 0.0487  -0.0134 0.0045  421 TYR D CE1 
7141  C CE2 . TYR C 89  ? 0.9284 1.0755 0.9791 0.0369  -0.0094 0.0084  421 TYR D CE2 
7142  C CZ  . TYR C 89  ? 0.9651 1.1232 1.0234 0.0463  -0.0114 0.0052  421 TYR D CZ  
7143  O OH  . TYR C 89  ? 1.0709 1.2236 1.1270 0.0532  -0.0113 0.0029  421 TYR D OH  
7144  N N   . ASN C 90  ? 0.9610 1.1687 1.0282 0.0025  -0.0116 0.0176  422 ASN D N   
7145  C CA  . ASN C 90  ? 0.9286 1.1362 0.9958 -0.0049 -0.0141 0.0207  422 ASN D CA  
7146  C C   . ASN C 90  ? 0.9331 1.1635 1.0054 -0.0116 -0.0140 0.0228  422 ASN D C   
7147  O O   . ASN C 90  ? 0.9971 1.2384 1.0786 -0.0104 -0.0182 0.0245  422 ASN D O   
7148  C CB  . ASN C 90  ? 0.9564 1.1441 1.0101 -0.0144 -0.0114 0.0223  422 ASN D CB  
7149  C CG  . ASN C 90  ? 0.9558 1.1219 1.0069 -0.0090 -0.0133 0.0219  422 ASN D CG  
7150  O OD1 . ASN C 90  ? 0.9956 1.1621 1.0549 0.0005  -0.0177 0.0210  422 ASN D OD1 
7151  N ND2 . ASN C 90  ? 0.9996 1.1466 1.0395 -0.0150 -0.0100 0.0230  422 ASN D ND2 
7152  N N   . TYR C 91  ? 0.9211 1.1590 0.9875 -0.0190 -0.0095 0.0232  423 TYR D N   
7153  C CA  . TYR C 91  ? 0.8650 1.1235 0.9342 -0.0276 -0.0091 0.0262  423 TYR D CA  
7154  C C   . TYR C 91  ? 0.8527 1.1241 0.9202 -0.0294 -0.0046 0.0253  423 TYR D C   
7155  O O   . TYR C 91  ? 0.8475 1.1097 0.9029 -0.0374 -0.0008 0.0254  423 TYR D O   
7156  C CB  . TYR C 91  ? 0.8046 1.0537 0.8632 -0.0413 -0.0089 0.0296  423 TYR D CB  
7157  C CG  . TYR C 91  ? 0.8929 1.1618 0.9522 -0.0517 -0.0086 0.0333  423 TYR D CG  
7158  C CD1 . TYR C 91  ? 0.9499 1.2386 1.0219 -0.0504 -0.0128 0.0361  423 TYR D CD1 
7159  C CD2 . TYR C 91  ? 0.8692 1.1382 0.9172 -0.0625 -0.0044 0.0345  423 TYR D CD2 
7160  C CE1 . TYR C 91  ? 0.9560 1.2640 1.0292 -0.0603 -0.0128 0.0404  423 TYR D CE1 
7161  C CE2 . TYR C 91  ? 0.8953 1.1830 0.9436 -0.0725 -0.0045 0.0385  423 TYR D CE2 
7162  C CZ  . TYR C 91  ? 0.9430 1.2503 1.0039 -0.0714 -0.0087 0.0416  423 TYR D CZ  
7163  O OH  . TYR C 91  ? 1.0103 1.3366 1.0715 -0.0819 -0.0089 0.0463  423 TYR D OH  
7164  N N   . LYS C 92  ? 0.8735 1.1663 0.9529 -0.0224 -0.0048 0.0244  424 LYS D N   
7165  C CA  . LYS C 92  ? 0.8751 1.1803 0.9538 -0.0221 -0.0004 0.0228  424 LYS D CA  
7166  C C   . LYS C 92  ? 0.9050 1.2352 0.9886 -0.0295 0.0002  0.0265  424 LYS D C   
7167  O O   . LYS C 92  ? 0.8940 1.2391 0.9893 -0.0275 -0.0031 0.0290  424 LYS D O   
7168  C CB  . LYS C 92  ? 0.8933 1.2028 0.9808 -0.0078 0.0001  0.0185  424 LYS D CB  
7169  C CG  . LYS C 92  ? 0.8750 1.2051 0.9669 -0.0057 0.0041  0.0170  424 LYS D CG  
7170  C CD  . LYS C 92  ? 0.9059 1.2264 0.9848 -0.0113 0.0086  0.0153  424 LYS D CD  
7171  C CE  . LYS C 92  ? 0.9779 1.2913 1.0565 -0.0008 0.0106  0.0104  424 LYS D CE  
7172  N NZ  . LYS C 92  ? 1.0179 1.3277 1.0857 -0.0067 0.0151  0.0091  424 LYS D NZ  
7173  N N   . LEU C 93  ? 1.0004 1.3354 1.0756 -0.0384 0.0041  0.0273  425 LEU D N   
7174  C CA  . LEU C 93  ? 1.0271 1.3861 1.1054 -0.0464 0.0050  0.0312  425 LEU D CA  
7175  C C   . LEU C 93  ? 1.0650 1.4446 1.1530 -0.0382 0.0080  0.0290  425 LEU D C   
7176  O O   . LEU C 93  ? 1.1204 1.4926 1.2046 -0.0326 0.0111  0.0245  425 LEU D O   
7177  C CB  . LEU C 93  ? 1.0150 1.3676 1.0779 -0.0610 0.0076  0.0334  425 LEU D CB  
7178  C CG  . LEU C 93  ? 0.9639 1.2993 1.0165 -0.0715 0.0054  0.0364  425 LEU D CG  
7179  C CD1 . LEU C 93  ? 0.9828 1.3207 1.0232 -0.0871 0.0072  0.0401  425 LEU D CD1 
7180  C CD2 . LEU C 93  ? 0.9545 1.2974 1.0176 -0.0694 0.0006  0.0392  425 LEU D CD2 
7181  N N   . PRO C 94  ? 1.1609 1.5663 1.2613 -0.0378 0.0071  0.0323  426 PRO D N   
7182  C CA  . PRO C 94  ? 1.1671 1.5939 1.2773 -0.0301 0.0105  0.0304  426 PRO D CA  
7183  C C   . PRO C 94  ? 1.2511 1.6823 1.3508 -0.0386 0.0150  0.0302  426 PRO D C   
7184  O O   . PRO C 94  ? 1.2835 1.7126 1.3728 -0.0522 0.0148  0.0340  426 PRO D O   
7185  C CB  . PRO C 94  ? 1.1550 1.6079 1.2800 -0.0305 0.0082  0.0358  426 PRO D CB  
7186  C CG  . PRO C 94  ? 1.1594 1.6068 1.2771 -0.0441 0.0046  0.0413  426 PRO D CG  
7187  C CD  . PRO C 94  ? 1.1601 1.5767 1.2663 -0.0445 0.0030  0.0382  426 PRO D CD  
7188  N N   . ASP C 95  ? 1.2054 1.6422 1.3073 -0.0309 0.0191  0.0258  427 ASP D N   
7189  C CA  . ASP C 95  ? 1.1946 1.6347 1.2860 -0.0391 0.0232  0.0254  427 ASP D CA  
7190  C C   . ASP C 95  ? 1.2726 1.7385 1.3673 -0.0486 0.0238  0.0310  427 ASP D C   
7191  O O   . ASP C 95  ? 1.2679 1.7355 1.3519 -0.0591 0.0259  0.0323  427 ASP D O   
7192  C CB  . ASP C 95  ? 1.1555 1.5963 1.2481 -0.0293 0.0275  0.0194  427 ASP D CB  
7193  C CG  . ASP C 95  ? 1.1862 1.6007 1.2742 -0.0209 0.0265  0.0145  427 ASP D CG  
7194  O OD1 . ASP C 95  ? 1.2152 1.6076 1.2914 -0.0273 0.0251  0.0150  427 ASP D OD1 
7195  O OD2 . ASP C 95  ? 1.1644 1.5799 1.2601 -0.0081 0.0275  0.0103  427 ASP D OD2 
7196  N N   . ASP C 96  ? 1.3118 1.7978 1.4210 -0.0455 0.0218  0.0348  428 ASP D N   
7197  C CA  . ASP C 96  ? 1.3400 1.8503 1.4529 -0.0555 0.0213  0.0416  428 ASP D CA  
7198  C C   . ASP C 96  ? 1.3921 1.8952 1.4991 -0.0675 0.0164  0.0475  428 ASP D C   
7199  O O   . ASP C 96  ? 1.4812 2.0041 1.5970 -0.0720 0.0140  0.0538  428 ASP D O   
7200  C CB  . ASP C 96  ? 1.2778 1.8164 1.4108 -0.0457 0.0221  0.0433  428 ASP D CB  
7201  C CG  . ASP C 96  ? 1.3297 1.8638 1.4754 -0.0340 0.0187  0.0423  428 ASP D CG  
7202  O OD1 . ASP C 96  ? 1.3555 1.8938 1.5065 -0.0386 0.0140  0.0480  428 ASP D OD1 
7203  O OD2 . ASP C 96  ? 1.3123 1.8375 1.4617 -0.0208 0.0205  0.0360  428 ASP D OD2 
7204  N N   . PHE C 97  ? 1.3407 1.8159 1.4330 -0.0730 0.0151  0.0457  429 PHE D N   
7205  C CA  . PHE C 97  ? 1.3167 1.7817 1.4014 -0.0846 0.0111  0.0504  429 PHE D CA  
7206  C C   . PHE C 97  ? 1.3683 1.8477 1.4463 -0.1003 0.0109  0.0569  429 PHE D C   
7207  O O   . PHE C 97  ? 1.4479 1.9347 1.5195 -0.1054 0.0141  0.0568  429 PHE D O   
7208  C CB  . PHE C 97  ? 1.2772 1.7090 1.3466 -0.0871 0.0111  0.0469  429 PHE D CB  
7209  C CG  . PHE C 97  ? 1.1806 1.5984 1.2453 -0.0938 0.0070  0.0500  429 PHE D CG  
7210  C CD1 . PHE C 97  ? 1.2182 1.6314 1.2697 -0.1099 0.0062  0.0546  429 PHE D CD1 
7211  C CD2 . PHE C 97  ? 1.1488 1.5595 1.2225 -0.0845 0.0038  0.0487  429 PHE D CD2 
7212  C CE1 . PHE C 97  ? 1.1179 1.5178 1.1640 -0.1167 0.0028  0.0573  429 PHE D CE1 
7213  C CE2 . PHE C 97  ? 1.1294 1.5281 1.1985 -0.0915 0.0000  0.0516  429 PHE D CE2 
7214  C CZ  . PHE C 97  ? 1.1010 1.4943 1.1561 -0.1078 -0.0002 0.0559  429 PHE D CZ  
7215  N N   . THR C 98  ? 1.3314 1.8140 1.4099 -0.1086 0.0068  0.0629  430 THR D N   
7216  C CA  . THR C 98  ? 1.3156 1.8112 1.3872 -0.1246 0.0056  0.0700  430 THR D CA  
7217  C C   . THR C 98  ? 1.3134 1.7881 1.3688 -0.1387 0.0028  0.0730  430 THR D C   
7218  O O   . THR C 98  ? 1.3514 1.8221 1.3916 -0.1522 0.0038  0.0754  430 THR D O   
7219  C CB  . THR C 98  ? 1.2477 1.7762 1.3380 -0.1224 0.0035  0.0763  430 THR D CB  
7220  O OG1 . THR C 98  ? 1.2516 1.7784 1.3531 -0.1163 -0.0007 0.0775  430 THR D OG1 
7221  C CG2 . THR C 98  ? 1.2417 1.7906 1.3454 -0.1100 0.0075  0.0732  430 THR D CG2 
7222  N N   . GLY C 99  ? 1.3834 1.8433 1.4405 -0.1359 -0.0004 0.0724  431 GLY D N   
7223  C CA  . GLY C 99  ? 1.3532 1.7932 1.3954 -0.1488 -0.0027 0.0750  431 GLY D CA  
7224  C C   . GLY C 99  ? 1.4311 1.8436 1.4513 -0.1579 0.0001  0.0722  431 GLY D C   
7225  O O   . GLY C 99  ? 1.4730 1.8864 1.4854 -0.1614 0.0034  0.0711  431 GLY D O   
7226  N N   . CYS C 100 ? 1.4056 1.7934 1.4157 -0.1623 -0.0011 0.0715  432 CYS D N   
7227  C CA  . CYS C 100 ? 1.4495 1.8092 1.4388 -0.1716 0.0015  0.0696  432 CYS D CA  
7228  C C   . CYS C 100 ? 1.3930 1.7252 1.3799 -0.1627 0.0026  0.0639  432 CYS D C   
7229  O O   . CYS C 100 ? 1.3610 1.6929 1.3587 -0.1543 -0.0001 0.0630  432 CYS D O   
7230  C CB  . CYS C 100 ? 1.4457 1.8005 1.4213 -0.1892 -0.0006 0.0753  432 CYS D CB  
7231  S SG  . CYS C 100 ? 1.5599 1.9092 1.5139 -0.2066 0.0022  0.0780  432 CYS D SG  
7232  N N   . VAL C 101 ? 1.2454 1.5540 1.2176 -0.1656 0.0064  0.0606  433 VAL D N   
7233  C CA  . VAL C 101 ? 1.1480 1.4300 1.1172 -0.1576 0.0080  0.0557  433 VAL D CA  
7234  C C   . VAL C 101 ? 1.1550 1.4101 1.1040 -0.1696 0.0106  0.0560  433 VAL D C   
7235  O O   . VAL C 101 ? 1.2572 1.5060 1.1944 -0.1766 0.0138  0.0559  433 VAL D O   
7236  C CB  . VAL C 101 ? 1.0963 1.3764 1.0714 -0.1450 0.0107  0.0507  433 VAL D CB  
7237  C CG1 . VAL C 101 ? 1.0339 1.2846 1.0015 -0.1409 0.0129  0.0470  433 VAL D CG1 
7238  C CG2 . VAL C 101 ? 1.0477 1.3470 1.0424 -0.1309 0.0083  0.0492  433 VAL D CG2 
7239  N N   . ILE C 102 ? 1.0145 1.2530 0.9593 -0.1716 0.0095  0.0561  434 ILE D N   
7240  C CA  . ILE C 102 ? 1.0386 1.2535 0.9638 -0.1847 0.0119  0.0571  434 ILE D CA  
7241  C C   . ILE C 102 ? 1.0219 1.2097 0.9442 -0.1778 0.0139  0.0532  434 ILE D C   
7242  O O   . ILE C 102 ? 0.9475 1.1365 0.8808 -0.1690 0.0110  0.0522  434 ILE D O   
7243  C CB  . ILE C 102 ? 1.0805 1.3028 1.0008 -0.1977 0.0086  0.0622  434 ILE D CB  
7244  C CG1 . ILE C 102 ? 1.2344 1.4864 1.1599 -0.2037 0.0061  0.0670  434 ILE D CG1 
7245  C CG2 . ILE C 102 ? 1.1369 1.3330 1.0348 -0.2119 0.0118  0.0629  434 ILE D CG2 
7246  C CD1 . ILE C 102 ? 1.2885 1.5470 1.2057 -0.2197 0.0032  0.0731  434 ILE D CD1 
7247  N N   . ALA C 103 ? 1.2685 1.4318 1.1760 -0.1823 0.0186  0.0515  435 ALA D N   
7248  C CA  . ALA C 103 ? 1.1458 1.2846 1.0523 -0.1740 0.0212  0.0480  435 ALA D CA  
7249  C C   . ALA C 103 ? 1.1941 1.3050 1.0812 -0.1840 0.0261  0.0479  435 ALA D C   
7250  O O   . ALA C 103 ? 1.3558 1.4633 1.2318 -0.1924 0.0289  0.0488  435 ALA D O   
7251  C CB  . ALA C 103 ? 1.2286 1.3682 1.1441 -0.1610 0.0225  0.0448  435 ALA D CB  
7252  N N   . TRP C 104 ? 0.9739 1.0644 0.8573 -0.1823 0.0274  0.0465  436 TRP D N   
7253  C CA  . TRP C 104 ? 1.1000 1.1618 0.9654 -0.1906 0.0330  0.0461  436 TRP D CA  
7254  C C   . TRP C 104 ? 1.0470 1.0870 0.9150 -0.1804 0.0357  0.0432  436 TRP D C   
7255  O O   . TRP C 104 ? 0.9823 1.0281 0.8635 -0.1698 0.0324  0.0422  436 TRP D O   
7256  C CB  . TRP C 104 ? 1.1397 1.1960 0.9906 -0.2062 0.0328  0.0486  436 TRP D CB  
7257  C CG  . TRP C 104 ? 0.9500 1.0130 0.8079 -0.2053 0.0285  0.0494  436 TRP D CG  
7258  C CD1 . TRP C 104 ? 0.8736 0.9170 0.7248 -0.2072 0.0301  0.0484  436 TRP D CD1 
7259  C CD2 . TRP C 104 ? 0.9172 1.0081 0.7903 -0.2022 0.0220  0.0515  436 TRP D CD2 
7260  N NE1 . TRP C 104 ? 0.8293 0.8867 0.6904 -0.2059 0.0246  0.0498  436 TRP D NE1 
7261  C CE2 . TRP C 104 ? 0.8587 0.9452 0.7336 -0.2027 0.0195  0.0518  436 TRP D CE2 
7262  C CE3 . TRP C 104 ? 0.9787 1.0980 0.8643 -0.1988 0.0182  0.0533  436 TRP D CE3 
7263  C CZ2 . TRP C 104 ? 0.9093 1.0184 0.7984 -0.2001 0.0130  0.0541  436 TRP D CZ2 
7264  C CZ3 . TRP C 104 ? 0.9257 1.0679 0.8259 -0.1957 0.0122  0.0555  436 TRP D CZ3 
7265  C CH2 . TRP C 104 ? 0.9124 1.0491 0.8142 -0.1965 0.0095  0.0560  436 TRP D CH2 
7266  N N   . ASN C 105 ? 1.2122 1.2268 1.0673 -0.1836 0.0418  0.0424  437 ASN D N   
7267  C CA  . ASN C 105 ? 1.1057 1.0967 0.9602 -0.1767 0.0452  0.0406  437 ASN D CA  
7268  C C   . ASN C 105 ? 1.0743 1.0620 0.9290 -0.1779 0.0433  0.0405  437 ASN D C   
7269  O O   . ASN C 105 ? 1.1064 1.1047 0.9573 -0.1873 0.0403  0.0421  437 ASN D O   
7270  C CB  . ASN C 105 ? 1.1779 1.1404 1.0162 -0.1830 0.0526  0.0403  437 ASN D CB  
7271  C CG  . ASN C 105 ? 1.2127 1.1669 1.0550 -0.1746 0.0557  0.0397  437 ASN D CG  
7272  O OD1 . ASN C 105 ? 1.2306 1.2017 1.0835 -0.1684 0.0527  0.0398  437 ASN D OD1 
7273  N ND2 . ASN C 105 ? 1.1372 1.0650 0.9724 -0.1734 0.0616  0.0393  437 ASN D ND2 
7274  N N   . SER C 106 ? 1.0364 1.0079 0.8946 -0.1693 0.0453  0.0389  438 SER D N   
7275  C CA  . SER C 106 ? 0.9849 0.9577 0.8482 -0.1670 0.0421  0.0386  438 SER D CA  
7276  C C   . SER C 106 ? 0.9936 0.9429 0.8563 -0.1596 0.0463  0.0372  438 SER D C   
7277  O O   . SER C 106 ? 0.9762 0.9221 0.8426 -0.1565 0.0444  0.0367  438 SER D O   
7278  C CB  . SER C 106 ? 0.9165 0.9163 0.7984 -0.1578 0.0345  0.0389  438 SER D CB  
7279  O OG  . SER C 106 ? 0.9270 0.9249 0.8179 -0.1497 0.0316  0.0381  438 SER D OG  
7280  N N   . ASN C 107 ? 0.9874 0.9207 0.8454 -0.1571 0.0519  0.0369  439 ASN D N   
7281  C CA  . ASN C 107 ? 0.9788 0.8891 0.8361 -0.1503 0.0568  0.0362  439 ASN D CA  
7282  C C   . ASN C 107 ? 1.0424 0.9354 0.8887 -0.1572 0.0600  0.0356  439 ASN D C   
7283  O O   . ASN C 107 ? 1.0423 0.9243 0.8931 -0.1498 0.0611  0.0351  439 ASN D O   
7284  C CB  . ASN C 107 ? 0.9767 0.8708 0.8273 -0.1505 0.0632  0.0367  439 ASN D CB  
7285  C CG  . ASN C 107 ? 0.9682 0.8488 0.8267 -0.1384 0.0657  0.0371  439 ASN D CG  
7286  O OD1 . ASN C 107 ? 0.9897 0.8817 0.8630 -0.1270 0.0609  0.0372  439 ASN D OD1 
7287  N ND2 . ASN C 107 ? 1.0010 0.8563 0.8495 -0.1407 0.0732  0.0374  439 ASN D ND2 
7288  N N   . LYS C 108 ? 1.0516 0.9418 0.8830 -0.1717 0.0617  0.0358  440 LYS D N   
7289  C CA  . LYS C 108 ? 1.0532 0.9248 0.8714 -0.1799 0.0656  0.0350  440 LYS D CA  
7290  C C   . LYS C 108 ? 0.9892 0.8705 0.8165 -0.1764 0.0599  0.0348  440 LYS D C   
7291  O O   . LYS C 108 ? 0.9815 0.8478 0.8087 -0.1723 0.0626  0.0339  440 LYS D O   
7292  C CB  . LYS C 108 ? 1.0268 0.8947 0.8264 -0.1971 0.0678  0.0356  440 LYS D CB  
7293  C CG  . LYS C 108 ? 1.0279 0.8747 0.8132 -0.2021 0.0759  0.0353  440 LYS D CG  
7294  C CD  . LYS C 108 ? 1.1846 1.0394 0.9583 -0.2154 0.0749  0.0367  440 LYS D CD  
7295  C CE  . LYS C 108 ? 1.2281 1.0569 0.9823 -0.2243 0.0833  0.0363  440 LYS D CE  
7296  N NZ  . LYS C 108 ? 1.2216 1.0440 0.9551 -0.2423 0.0845  0.0369  440 LYS D NZ  
7297  N N   . LEU C 109 ? 0.9825 0.8893 0.8188 -0.1775 0.0521  0.0359  441 LEU D N   
7298  C CA  . LEU C 109 ? 0.9825 0.8992 0.8270 -0.1756 0.0461  0.0361  441 LEU D CA  
7299  C C   . LEU C 109 ? 0.9883 0.9200 0.8538 -0.1596 0.0401  0.0360  441 LEU D C   
7300  O O   . LEU C 109 ? 1.0157 0.9461 0.8874 -0.1549 0.0372  0.0356  441 LEU D O   
7301  C CB  . LEU C 109 ? 0.9361 0.8699 0.7765 -0.1885 0.0411  0.0381  441 LEU D CB  
7302  C CG  . LEU C 109 ? 0.9437 0.9058 0.7925 -0.1902 0.0350  0.0403  441 LEU D CG  
7303  C CD1 . LEU C 109 ? 0.9684 0.9433 0.8137 -0.2025 0.0300  0.0430  441 LEU D CD1 
7304  C CD2 . LEU C 109 ? 0.9657 0.9257 0.8053 -0.1957 0.0391  0.0407  441 LEU D CD2 
7305  N N   . ASP C 110 ? 0.9192 0.8637 0.7952 -0.1510 0.0382  0.0361  442 ASP D N   
7306  C CA  . ASP C 110 ? 0.9223 0.8809 0.8171 -0.1366 0.0321  0.0359  442 ASP D CA  
7307  C C   . ASP C 110 ? 0.9427 0.8856 0.8421 -0.1246 0.0351  0.0351  442 ASP D C   
7308  O O   . ASP C 110 ? 0.9111 0.8612 0.8240 -0.1133 0.0302  0.0350  442 ASP D O   
7309  C CB  . ASP C 110 ? 0.9129 0.8951 0.8181 -0.1323 0.0278  0.0363  442 ASP D CB  
7310  C CG  . ASP C 110 ? 0.9714 0.9760 0.8801 -0.1392 0.0220  0.0378  442 ASP D CG  
7311  O OD1 . ASP C 110 ? 0.9728 0.9847 0.8893 -0.1368 0.0168  0.0382  442 ASP D OD1 
7312  O OD2 . ASP C 110 ? 1.0311 1.0470 0.9357 -0.1468 0.0223  0.0389  442 ASP D OD2 
7313  N N   . SER C 111 ? 0.9842 0.9065 0.8734 -0.1267 0.0427  0.0350  443 SER D N   
7314  C CA  . SER C 111 ? 0.9664 0.8733 0.8599 -0.1162 0.0459  0.0352  443 SER D CA  
7315  C C   . SER C 111 ? 1.0260 0.9105 0.9107 -0.1191 0.0511  0.0349  443 SER D C   
7316  O O   . SER C 111 ? 1.0362 0.9129 0.9079 -0.1308 0.0540  0.0343  443 SER D O   
7317  C CB  . SER C 111 ? 0.9260 0.8263 0.8164 -0.1153 0.0508  0.0358  443 SER D CB  
7318  O OG  . SER C 111 ? 0.9751 0.8526 0.8506 -0.1231 0.0589  0.0358  443 SER D OG  
7319  N N   . LYS C 112 ? 1.0513 0.9259 0.9432 -0.1084 0.0520  0.0356  444 LYS D N   
7320  C CA  . LYS C 112 ? 1.0840 0.9384 0.9696 -0.1092 0.0569  0.0356  444 LYS D CA  
7321  C C   . LYS C 112 ? 1.0860 0.9262 0.9769 -0.0986 0.0610  0.0374  444 LYS D C   
7322  O O   . LYS C 112 ? 1.0863 0.9357 0.9884 -0.0893 0.0575  0.0387  444 LYS D O   
7323  C CB  . LYS C 112 ? 1.0653 0.9283 0.9568 -0.1079 0.0505  0.0351  444 LYS D CB  
7324  C CG  . LYS C 112 ? 1.0943 0.9635 1.0016 -0.0939 0.0447  0.0362  444 LYS D CG  
7325  C CD  . LYS C 112 ? 1.1652 1.0345 1.0737 -0.0950 0.0409  0.0358  444 LYS D CD  
7326  C CE  . LYS C 112 ? 1.1134 0.9925 1.0375 -0.0825 0.0332  0.0369  444 LYS D CE  
7327  N NZ  . LYS C 112 ? 1.1392 1.0026 1.0616 -0.0802 0.0357  0.0376  444 LYS D NZ  
7328  N N   . VAL C 113 ? 1.0946 0.9124 0.9773 -0.1003 0.0686  0.0377  445 VAL D N   
7329  C CA  . VAL C 113 ? 1.1168 0.9189 1.0026 -0.0921 0.0743  0.0402  445 VAL D CA  
7330  C C   . VAL C 113 ? 1.0791 0.8845 0.9791 -0.0794 0.0696  0.0423  445 VAL D C   
7331  O O   . VAL C 113 ? 1.0345 0.8244 0.9342 -0.0757 0.0741  0.0438  445 VAL D O   
7332  C CB  . VAL C 113 ? 1.1564 0.9327 1.0281 -0.0985 0.0850  0.0399  445 VAL D CB  
7333  C CG1 . VAL C 113 ? 1.0431 0.8035 0.9174 -0.0915 0.0917  0.0430  445 VAL D CG1 
7334  C CG2 . VAL C 113 ? 1.2419 1.0148 1.0969 -0.1134 0.0886  0.0373  445 VAL D CG2 
7335  N N   . GLY C 114 ? 1.1591 0.9843 1.0714 -0.0725 0.0608  0.0426  446 GLY D N   
7336  C CA  . GLY C 114 ? 1.1137 0.9425 1.0383 -0.0614 0.0554  0.0446  446 GLY D CA  
7337  C C   . GLY C 114 ? 1.1592 1.0113 1.0938 -0.0575 0.0454  0.0435  446 GLY D C   
7338  O O   . GLY C 114 ? 1.1526 1.0127 1.0941 -0.0533 0.0390  0.0433  446 GLY D O   
7339  N N   . GLY C 115 ? 1.3539 1.2173 1.2890 -0.0593 0.0441  0.0427  447 GLY D N   
7340  C CA  . GLY C 115 ? 1.2940 1.1789 1.2397 -0.0539 0.0355  0.0419  447 GLY D CA  
7341  C C   . GLY C 115 ? 1.2333 1.1327 1.1802 -0.0583 0.0296  0.0396  447 GLY D C   
7342  O O   . GLY C 115 ? 1.2470 1.1502 1.2007 -0.0533 0.0242  0.0398  447 GLY D O   
7343  N N   . ASN C 116 ? 0.9981 0.9056 0.9383 -0.0682 0.0305  0.0379  448 ASN D N   
7344  C CA  . ASN C 116 ? 0.9131 0.8397 0.8577 -0.0712 0.0236  0.0366  448 ASN D CA  
7345  C C   . ASN C 116 ? 0.8817 0.8269 0.8405 -0.0608 0.0161  0.0365  448 ASN D C   
7346  O O   . ASN C 116 ? 0.8649 0.8202 0.8254 -0.0603 0.0162  0.0360  448 ASN D O   
7347  C CB  . ASN C 116 ? 0.9695 0.9013 0.9041 -0.0839 0.0263  0.0356  448 ASN D CB  
7348  C CG  . ASN C 116 ? 0.9875 0.9432 0.9286 -0.0865 0.0191  0.0351  448 ASN D CG  
7349  O OD1 . ASN C 116 ? 1.0093 0.9746 0.9593 -0.0822 0.0125  0.0351  448 ASN D OD1 
7350  N ND2 . ASN C 116 ? 0.9235 0.8891 0.8603 -0.0937 0.0203  0.0349  448 ASN D ND2 
7351  N N   . TYR C 117 ? 0.9086 0.8581 0.8770 -0.0525 0.0098  0.0369  449 TYR D N   
7352  C CA  . TYR C 117 ? 0.8815 0.8468 0.8628 -0.0422 0.0029  0.0366  449 TYR D CA  
7353  C C   . TYR C 117 ? 0.8832 0.8685 0.8712 -0.0436 -0.0041 0.0355  449 TYR D C   
7354  O O   . TYR C 117 ? 0.8656 0.8623 0.8647 -0.0346 -0.0108 0.0353  449 TYR D O   
7355  C CB  . TYR C 117 ? 0.8958 0.8529 0.8839 -0.0310 -0.0001 0.0382  449 TYR D CB  
7356  C CG  . TYR C 117 ? 0.9290 0.8673 0.9126 -0.0283 0.0062  0.0403  449 TYR D CG  
7357  C CD1 . TYR C 117 ? 0.9251 0.8614 0.9050 -0.0298 0.0111  0.0405  449 TYR D CD1 
7358  C CD2 . TYR C 117 ? 0.9216 0.8446 0.9051 -0.0243 0.0073  0.0425  449 TYR D CD2 
7359  C CE1 . TYR C 117 ? 0.9184 0.8383 0.8951 -0.0276 0.0166  0.0430  449 TYR D CE1 
7360  C CE2 . TYR C 117 ? 0.9502 0.8569 0.9307 -0.0218 0.0133  0.0452  449 TYR D CE2 
7361  C CZ  . TYR C 117 ? 0.9469 0.8521 0.9241 -0.0236 0.0178  0.0455  449 TYR D CZ  
7362  O OH  . TYR C 117 ? 0.9706 0.8607 0.9457 -0.0214 0.0235  0.0486  449 TYR D OH  
7363  N N   . ASN C 118 ? 0.8153 0.8051 0.7967 -0.0550 -0.0026 0.0351  450 ASN D N   
7364  C CA  . ASN C 118 ? 0.8192 0.8278 0.8072 -0.0576 -0.0091 0.0350  450 ASN D CA  
7365  C C   . ASN C 118 ? 0.7711 0.7997 0.7646 -0.0572 -0.0108 0.0344  450 ASN D C   
7366  O O   . ASN C 118 ? 0.7808 0.8276 0.7846 -0.0545 -0.0172 0.0345  450 ASN D O   
7367  C CB  . ASN C 118 ? 0.8351 0.8389 0.8132 -0.0709 -0.0073 0.0355  450 ASN D CB  
7368  C CG  . ASN C 118 ? 0.9101 0.9086 0.8908 -0.0698 -0.0115 0.0361  450 ASN D CG  
7369  O OD1 . ASN C 118 ? 0.9148 0.9084 0.9024 -0.0594 -0.0145 0.0363  450 ASN D OD1 
7370  N ND2 . ASN C 118 ? 0.9909 0.9897 0.9649 -0.0814 -0.0119 0.0367  450 ASN D ND2 
7371  N N   . TYR C 119 ? 0.8367 0.8628 0.8243 -0.0596 -0.0052 0.0340  451 TYR D N   
7372  C CA  . TYR C 119 ? 0.8369 0.8825 0.8301 -0.0584 -0.0066 0.0334  451 TYR D CA  
7373  C C   . TYR C 119 ? 0.7876 0.8335 0.7883 -0.0457 -0.0076 0.0324  451 TYR D C   
7374  O O   . TYR C 119 ? 0.7528 0.7818 0.7497 -0.0420 -0.0043 0.0327  451 TYR D O   
7375  C CB  . TYR C 119 ? 0.8043 0.8501 0.7869 -0.0693 -0.0008 0.0336  451 TYR D CB  
7376  C CG  . TYR C 119 ? 0.8384 0.8795 0.8094 -0.0837 0.0017  0.0348  451 TYR D CG  
7377  C CD1 . TYR C 119 ? 0.9052 0.9244 0.8652 -0.0889 0.0060  0.0350  451 TYR D CD1 
7378  C CD2 . TYR C 119 ? 0.8554 0.9145 0.8272 -0.0918 -0.0008 0.0360  451 TYR D CD2 
7379  C CE1 . TYR C 119 ? 0.9394 0.9534 0.8875 -0.1027 0.0084  0.0358  451 TYR D CE1 
7380  C CE2 . TYR C 119 ? 0.8759 0.9308 0.8361 -0.1059 0.0011  0.0374  451 TYR D CE2 
7381  C CZ  . TYR C 119 ? 0.9289 0.9607 0.8769 -0.1112 0.0056  0.0371  451 TYR D CZ  
7382  O OH  . TYR C 119 ? 1.0095 1.0362 0.9451 -0.1256 0.0075  0.0384  451 TYR D OH  
7383  N N   . ARG C 120 ? 0.7465 0.8117 0.7580 -0.0393 -0.0121 0.0314  452 ARG D N   
7384  C CA  . ARG C 120 ? 0.7334 0.8001 0.7527 -0.0269 -0.0142 0.0303  452 ARG D CA  
7385  C C   . ARG C 120 ? 0.7731 0.8573 0.7967 -0.0252 -0.0137 0.0289  452 ARG D C   
7386  O O   . ARG C 120 ? 0.8325 0.9316 0.8565 -0.0320 -0.0135 0.0292  452 ARG D O   
7387  C CB  . ARG C 120 ? 0.7239 0.7951 0.7537 -0.0179 -0.0214 0.0301  452 ARG D CB  
7388  C CG  . ARG C 120 ? 0.7108 0.7642 0.7378 -0.0162 -0.0223 0.0313  452 ARG D CG  
7389  C CD  . ARG C 120 ? 0.7472 0.8053 0.7849 -0.0058 -0.0298 0.0311  452 ARG D CD  
7390  N NE  . ARG C 120 ? 0.8392 0.8970 0.8790 -0.0087 -0.0342 0.0322  452 ARG D NE  
7391  C CZ  . ARG C 120 ? 0.8286 0.8908 0.8775 -0.0010 -0.0414 0.0323  452 ARG D CZ  
7392  N NH1 . ARG C 120 ? 0.7381 0.8047 0.7944 0.0101  -0.0449 0.0313  452 ARG D NH1 
7393  N NH2 . ARG C 120 ? 0.9001 0.9607 0.9499 -0.0047 -0.0452 0.0335  452 ARG D NH2 
7394  N N   . TYR C 121 ? 0.7451 0.8273 0.7714 -0.0164 -0.0134 0.0278  453 TYR D N   
7395  C CA  . TYR C 121 ? 0.7466 0.8464 0.7792 -0.0120 -0.0140 0.0260  453 TYR D CA  
7396  C C   . TYR C 121 ? 0.7641 0.8668 0.8062 0.0010  -0.0189 0.0245  453 TYR D C   
7397  O O   . TYR C 121 ? 0.7524 0.8420 0.7953 0.0067  -0.0217 0.0252  453 TYR D O   
7398  C CB  . TYR C 121 ? 0.7890 0.8864 0.8147 -0.0152 -0.0083 0.0255  453 TYR D CB  
7399  C CG  . TYR C 121 ? 0.8316 0.9089 0.8517 -0.0119 -0.0058 0.0263  453 TYR D CG  
7400  C CD1 . TYR C 121 ? 0.8374 0.9083 0.8625 -0.0014 -0.0092 0.0261  453 TYR D CD1 
7401  C CD2 . TYR C 121 ? 0.9067 0.9727 0.9169 -0.0193 -0.0001 0.0275  453 TYR D CD2 
7402  C CE1 . TYR C 121 ? 0.8704 0.9240 0.8910 0.0011  -0.0072 0.0277  453 TYR D CE1 
7403  C CE2 . TYR C 121 ? 0.8960 0.9442 0.9021 -0.0166 0.0022  0.0290  453 TYR D CE2 
7404  C CZ  . TYR C 121 ? 0.8870 0.9296 0.8986 -0.0064 -0.0015 0.0293  453 TYR D CZ  
7405  O OH  . TYR C 121 ? 1.0202 1.0463 1.0287 -0.0036 0.0003  0.0316  453 TYR D OH  
7406  N N   . ARG C 122 ? 0.7666 0.8866 0.8156 0.0056  -0.0198 0.0226  454 ARG D N   
7407  C CA  . ARG C 122 ? 0.7531 0.8748 0.8084 0.0175  -0.0227 0.0206  454 ARG D CA  
7408  C C   . ARG C 122 ? 0.8306 0.9435 0.8789 0.0177  -0.0182 0.0200  454 ARG D C   
7409  O O   . ARG C 122 ? 0.8327 0.9513 0.8762 0.0107  -0.0135 0.0199  454 ARG D O   
7410  C CB  . ARG C 122 ? 0.7786 0.9226 0.8436 0.0219  -0.0243 0.0185  454 ARG D CB  
7411  C CG  . ARG C 122 ? 0.8174 0.9647 0.8918 0.0334  -0.0298 0.0171  454 ARG D CG  
7412  C CD  . ARG C 122 ? 0.8623 1.0322 0.9471 0.0362  -0.0312 0.0158  454 ARG D CD  
7413  N NE  . ARG C 122 ? 0.8831 1.0579 0.9748 0.0354  -0.0364 0.0177  454 ARG D NE  
7414  C CZ  . ARG C 122 ? 0.8941 1.0636 0.9914 0.0430  -0.0422 0.0177  454 ARG D CZ  
7415  N NH1 . ARG C 122 ? 0.8434 0.9994 0.9385 0.0514  -0.0437 0.0162  454 ARG D NH1 
7416  N NH2 . ARG C 122 ? 0.9164 1.0934 1.0210 0.0413  -0.0470 0.0196  454 ARG D NH2 
7417  N N   . LEU C 123 ? 0.8293 0.9289 0.8768 0.0254  -0.0199 0.0201  455 LEU D N   
7418  C CA  . LEU C 123 ? 0.8232 0.9190 0.8661 0.0268  -0.0166 0.0193  455 LEU D CA  
7419  C C   . LEU C 123 ? 0.8266 0.9281 0.8747 0.0372  -0.0193 0.0168  455 LEU D C   
7420  O O   . LEU C 123 ? 0.8911 0.9966 0.9366 0.0373  -0.0163 0.0152  455 LEU D O   
7421  C CB  . LEU C 123 ? 0.7955 0.8699 0.8304 0.0245  -0.0143 0.0223  455 LEU D CB  
7422  C CG  . LEU C 123 ? 0.8258 0.8825 0.8597 0.0307  -0.0171 0.0246  455 LEU D CG  
7423  C CD1 . LEU C 123 ? 0.7486 0.7899 0.7744 0.0252  -0.0125 0.0277  455 LEU D CD1 
7424  C CD2 . LEU C 123 ? 0.8889 0.9403 0.9259 0.0321  -0.0210 0.0260  455 LEU D CD2 
7425  N N   . PHE C 124 ? 0.7622 0.8653 0.8174 0.0453  -0.0249 0.0160  456 PHE D N   
7426  C CA  . PHE C 124 ? 0.7835 0.8900 0.8426 0.0554  -0.0276 0.0134  456 PHE D CA  
7427  C C   . PHE C 124 ? 0.7767 0.9025 0.8461 0.0601  -0.0300 0.0107  456 PHE D C   
7428  O O   . PHE C 124 ? 0.8129 0.9421 0.8883 0.0606  -0.0341 0.0117  456 PHE D O   
7429  C CB  . PHE C 124 ? 0.8118 0.9013 0.8698 0.0619  -0.0325 0.0151  456 PHE D CB  
7430  C CG  . PHE C 124 ? 0.7703 0.8418 0.8195 0.0588  -0.0302 0.0182  456 PHE D CG  
7431  C CD1 . PHE C 124 ? 0.8035 0.8748 0.8467 0.0538  -0.0248 0.0181  456 PHE D CD1 
7432  C CD2 . PHE C 124 ? 0.7628 0.8181 0.8103 0.0604  -0.0334 0.0217  456 PHE D CD2 
7433  C CE1 . PHE C 124 ? 0.8459 0.9011 0.8819 0.0507  -0.0228 0.0215  456 PHE D CE1 
7434  C CE2 . PHE C 124 ? 0.8294 0.8688 0.8699 0.0576  -0.0311 0.0252  456 PHE D CE2 
7435  C CZ  . PHE C 124 ? 0.8773 0.9164 0.9123 0.0527  -0.0258 0.0252  456 PHE D CZ  
7436  N N   . ARG C 125 ? 0.7944 0.9326 0.8660 0.0636  -0.0276 0.0075  457 ARG D N   
7437  C CA  . ARG C 125 ? 0.8949 1.0512 0.9774 0.0697  -0.0296 0.0051  457 ARG D CA  
7438  C C   . ARG C 125 ? 0.9077 1.0689 0.9905 0.0772  -0.0276 0.0013  457 ARG D C   
7439  O O   . ARG C 125 ? 0.9417 1.0999 1.0170 0.0741  -0.0231 0.0004  457 ARG D O   
7440  C CB  . ARG C 125 ? 0.8703 1.0453 0.9576 0.0623  -0.0272 0.0060  457 ARG D CB  
7441  C CG  . ARG C 125 ? 0.8846 1.0792 0.9850 0.0675  -0.0298 0.0050  457 ARG D CG  
7442  C CD  . ARG C 125 ? 0.9299 1.1404 1.0334 0.0577  -0.0278 0.0075  457 ARG D CD  
7443  N NE  . ARG C 125 ? 0.8789 1.1084 0.9956 0.0610  -0.0308 0.0080  457 ARG D NE  
7444  C CZ  . ARG C 125 ? 0.9091 1.1581 1.0337 0.0645  -0.0283 0.0065  457 ARG D CZ  
7445  N NH1 . ARG C 125 ? 0.9245 1.1774 1.0445 0.0645  -0.0226 0.0040  457 ARG D NH1 
7446  N NH2 . ARG C 125 ? 0.9261 1.1916 1.0638 0.0680  -0.0314 0.0078  457 ARG D NH2 
7447  N N   . LYS C 126 ? 0.9067 1.0751 0.9980 0.0869  -0.0310 -0.0010 458 LYS D N   
7448  C CA  . LYS C 126 ? 0.8767 1.0486 0.9679 0.0946  -0.0289 -0.0051 458 LYS D CA  
7449  C C   . LYS C 126 ? 0.8601 1.0498 0.9524 0.0912  -0.0222 -0.0072 458 LYS D C   
7450  O O   . LYS C 126 ? 0.8832 1.0737 0.9721 0.0951  -0.0189 -0.0106 458 LYS D O   
7451  C CB  . LYS C 126 ? 0.8502 1.0263 0.9508 0.1058  -0.0336 -0.0071 458 LYS D CB  
7452  C CG  . LYS C 126 ? 0.9175 1.0848 1.0220 0.1078  -0.0410 -0.0043 458 LYS D CG  
7453  C CD  . LYS C 126 ? 0.9655 1.1338 1.0774 0.1199  -0.0459 -0.0067 458 LYS D CD  
7454  C CE  . LYS C 126 ? 1.0747 1.2349 1.1908 0.1221  -0.0539 -0.0039 458 LYS D CE  
7455  N NZ  . LYS C 126 ? 1.2361 1.3738 1.3415 0.1204  -0.0568 -0.0016 458 LYS D NZ  
7456  N N   . SER C 127 ? 0.8818 1.0856 0.9781 0.0835  -0.0202 -0.0052 459 SER D N   
7457  C CA  . SER C 127 ? 0.9563 1.1797 1.0556 0.0815  -0.0146 -0.0071 459 SER D CA  
7458  C C   . SER C 127 ? 0.9866 1.2210 1.0867 0.0702  -0.0129 -0.0036 459 SER D C   
7459  O O   . SER C 127 ? 0.9742 1.2052 1.0761 0.0660  -0.0165 -0.0003 459 SER D O   
7460  C CB  . SER C 127 ? 1.0008 1.2406 1.1124 0.0916  -0.0151 -0.0098 459 SER D CB  
7461  O OG  . SER C 127 ? 1.0718 1.3162 1.1936 0.0941  -0.0205 -0.0075 459 SER D OG  
7462  N N   . ASN C 128 ? 0.9397 1.1876 1.0382 0.0653  -0.0074 -0.0044 460 ASN D N   
7463  C CA  . ASN C 128 ? 0.9080 1.1641 1.0041 0.0532  -0.0052 -0.0011 460 ASN D CA  
7464  C C   . ASN C 128 ? 0.9648 1.2388 1.0724 0.0520  -0.0076 0.0015  460 ASN D C   
7465  O O   . ASN C 128 ? 0.9965 1.2834 1.1158 0.0607  -0.0090 0.0002  460 ASN D O   
7466  C CB  . ASN C 128 ? 0.9491 1.2155 1.0404 0.0482  0.0009  -0.0025 460 ASN D CB  
7467  C CG  . ASN C 128 ? 1.0310 1.2794 1.1095 0.0456  0.0032  -0.0037 460 ASN D CG  
7468  O OD1 . ASN C 128 ? 1.0498 1.2954 1.1201 0.0355  0.0059  -0.0018 460 ASN D OD1 
7469  N ND2 . ASN C 128 ? 1.1553 1.3908 1.2319 0.0543  0.0018  -0.0063 460 ASN D ND2 
7470  N N   . LEU C 129 ? 0.9976 1.2725 1.1018 0.0408  -0.0079 0.0053  461 LEU D N   
7471  C CA  . LEU C 129 ? 0.9628 1.2537 1.0767 0.0376  -0.0105 0.0088  461 LEU D CA  
7472  C C   . LEU C 129 ? 0.9694 1.2855 1.0897 0.0355  -0.0068 0.0093  461 LEU D C   
7473  O O   . LEU C 129 ? 0.9767 1.2961 1.0894 0.0287  -0.0022 0.0091  461 LEU D O   
7474  C CB  . LEU C 129 ? 0.9354 1.2171 1.0417 0.0255  -0.0120 0.0128  461 LEU D CB  
7475  C CG  . LEU C 129 ? 0.9019 1.1684 1.0092 0.0282  -0.0175 0.0138  461 LEU D CG  
7476  C CD1 . LEU C 129 ? 0.7332 0.9954 0.8349 0.0160  -0.0186 0.0178  461 LEU D CD1 
7477  C CD2 . LEU C 129 ? 0.8880 1.1672 1.0099 0.0381  -0.0216 0.0134  461 LEU D CD2 
7478  N N   . LYS C 130 ? 0.9833 1.3177 1.1181 0.0413  -0.0089 0.0104  462 LYS D N   
7479  C CA  . LYS C 130 ? 0.9183 1.2788 1.0609 0.0388  -0.0057 0.0122  462 LYS D CA  
7480  C C   . LYS C 130 ? 0.8694 1.2361 1.0080 0.0241  -0.0064 0.0177  462 LYS D C   
7481  O O   . LYS C 130 ? 0.8930 1.2460 1.0264 0.0182  -0.0100 0.0200  462 LYS D O   
7482  C CB  . LYS C 130 ? 0.8650 1.2430 1.0252 0.0496  -0.0077 0.0123  462 LYS D CB  
7483  C CG  . LYS C 130 ? 0.9257 1.2973 1.0876 0.0633  -0.0060 0.0064  462 LYS D CG  
7484  C CD  . LYS C 130 ? 0.9536 1.3482 1.1272 0.0708  -0.0017 0.0050  462 LYS D CD  
7485  C CE  . LYS C 130 ? 1.0416 1.4348 1.2043 0.0687  0.0051  0.0012  462 LYS D CE  
7486  N NZ  . LYS C 130 ? 1.0289 1.4373 1.1980 0.0775  0.0109  -0.0027 462 LYS D NZ  
7487  N N   . PRO C 131 ? 0.8969 1.2828 1.0363 0.0175  -0.0027 0.0198  463 PRO D N   
7488  C CA  . PRO C 131 ? 0.8765 1.2655 1.0089 0.0022  -0.0031 0.0249  463 PRO D CA  
7489  C C   . PRO C 131 ? 0.8319 1.2225 0.9704 -0.0013 -0.0089 0.0295  463 PRO D C   
7490  O O   . PRO C 131 ? 0.7845 1.1871 0.9377 0.0066  -0.0120 0.0306  463 PRO D O   
7491  C CB  . PRO C 131 ? 0.8862 1.3013 1.0236 -0.0013 0.0009  0.0269  463 PRO D CB  
7492  C CG  . PRO C 131 ? 0.8965 1.3131 1.0350 0.0088  0.0053  0.0214  463 PRO D CG  
7493  C CD  . PRO C 131 ? 0.9044 1.3072 1.0482 0.0224  0.0026  0.0173  463 PRO D CD  
7494  N N   . PHE C 132 ? 0.8322 1.2085 0.9588 -0.0130 -0.0103 0.0320  464 PHE D N   
7495  C CA  . PHE C 132 ? 0.8422 1.2196 0.9717 -0.0197 -0.0153 0.0369  464 PHE D CA  
7496  C C   . PHE C 132 ? 0.8294 1.1991 0.9680 -0.0094 -0.0205 0.0356  464 PHE D C   
7497  O O   . PHE C 132 ? 0.8358 1.2126 0.9821 -0.0122 -0.0253 0.0397  464 PHE D O   
7498  C CB  . PHE C 132 ? 0.7955 1.2009 0.9352 -0.0252 -0.0161 0.0425  464 PHE D CB  
7499  C CG  . PHE C 132 ? 0.8533 1.2616 0.9812 -0.0410 -0.0140 0.0464  464 PHE D CG  
7500  C CD1 . PHE C 132 ? 0.9170 1.3082 1.0318 -0.0528 -0.0157 0.0485  464 PHE D CD1 
7501  C CD2 . PHE C 132 ? 0.8581 1.2857 0.9873 -0.0441 -0.0101 0.0477  464 PHE D CD2 
7502  C CE1 . PHE C 132 ? 0.9820 1.3747 1.0846 -0.0677 -0.0137 0.0520  464 PHE D CE1 
7503  C CE2 . PHE C 132 ? 0.9198 1.3499 1.0374 -0.0591 -0.0085 0.0515  464 PHE D CE2 
7504  C CZ  . PHE C 132 ? 0.9891 1.4015 1.0931 -0.0710 -0.0104 0.0536  464 PHE D CZ  
7505  N N   . GLU C 133 ? 0.7934 1.1491 0.9313 0.0021  -0.0198 0.0302  465 GLU D N   
7506  C CA  . GLU C 133 ? 0.7755 1.1226 0.9210 0.0123  -0.0248 0.0287  465 GLU D CA  
7507  C C   . GLU C 133 ? 0.8255 1.1492 0.9603 0.0063  -0.0277 0.0294  465 GLU D C   
7508  O O   . GLU C 133 ? 0.8540 1.1641 0.9745 -0.0030 -0.0247 0.0295  465 GLU D O   
7509  C CB  . GLU C 133 ? 0.7828 1.1234 0.9300 0.0261  -0.0228 0.0230  465 GLU D CB  
7510  C CG  . GLU C 133 ? 0.8059 1.1526 0.9677 0.0399  -0.0266 0.0215  465 GLU D CG  
7511  C CD  . GLU C 133 ? 0.9571 1.2885 1.1156 0.0517  -0.0255 0.0157  465 GLU D CD  
7512  O OE1 . GLU C 133 ? 0.9736 1.3106 1.1312 0.0565  -0.0204 0.0123  465 GLU D OE1 
7513  O OE2 . GLU C 133 ? 1.0376 1.3524 1.1948 0.0565  -0.0300 0.0147  465 GLU D OE2 
7514  N N   . ARG C 134 ? 0.8646 1.1842 1.0067 0.0111  -0.0336 0.0302  466 ARG D N   
7515  C CA  . ARG C 134 ? 0.9037 1.2004 1.0371 0.0082  -0.0365 0.0301  466 ARG D CA  
7516  C C   . ARG C 134 ? 0.9743 1.2611 1.1136 0.0218  -0.0403 0.0270  466 ARG D C   
7517  O O   . ARG C 134 ? 0.9773 1.2774 1.1303 0.0313  -0.0431 0.0266  466 ARG D O   
7518  C CB  . ARG C 134 ? 0.8707 1.1699 1.0044 -0.0026 -0.0406 0.0351  466 ARG D CB  
7519  C CG  . ARG C 134 ? 0.8960 1.1719 1.0140 -0.0122 -0.0398 0.0355  466 ARG D CG  
7520  C CD  . ARG C 134 ? 0.8611 1.1359 0.9795 -0.0208 -0.0449 0.0396  466 ARG D CD  
7521  N NE  . ARG C 134 ? 0.9311 1.2248 1.0520 -0.0317 -0.0450 0.0444  466 ARG D NE  
7522  C CZ  . ARG C 134 ? 0.8928 1.2068 1.0281 -0.0308 -0.0498 0.0481  466 ARG D CZ  
7523  N NH1 . ARG C 134 ? 0.8878 1.2047 1.0361 -0.0200 -0.0551 0.0475  466 ARG D NH1 
7524  N NH2 . ARG C 134 ? 0.8254 1.1576 0.9625 -0.0408 -0.0492 0.0529  466 ARG D NH2 
7525  N N   . ASP C 135 ? 1.0501 1.3134 1.1790 0.0224  -0.0403 0.0251  467 ASP D N   
7526  C CA  . ASP C 135 ? 1.0619 1.3120 1.1935 0.0332  -0.0446 0.0229  467 ASP D CA  
7527  C C   . ASP C 135 ? 0.9658 1.1965 1.0891 0.0275  -0.0473 0.0245  467 ASP D C   
7528  O O   . ASP C 135 ? 0.9869 1.2023 1.0974 0.0212  -0.0433 0.0242  467 ASP D O   
7529  C CB  . ASP C 135 ? 1.1162 1.3566 1.2435 0.0422  -0.0414 0.0186  467 ASP D CB  
7530  C CG  . ASP C 135 ? 1.1760 1.4160 1.3124 0.0561  -0.0458 0.0162  467 ASP D CG  
7531  O OD1 . ASP C 135 ? 1.1666 1.4219 1.3160 0.0607  -0.0495 0.0171  467 ASP D OD1 
7532  O OD2 . ASP C 135 ? 1.1944 1.4180 1.3246 0.0622  -0.0457 0.0136  467 ASP D OD2 
7533  N N   . ILE C 136 ? 0.9052 1.1363 1.0360 0.0300  -0.0538 0.0261  468 ILE D N   
7534  C CA  . ILE C 136 ? 0.8677 1.0807 0.9911 0.0252  -0.0564 0.0275  468 ILE D CA  
7535  C C   . ILE C 136 ? 0.8883 1.0911 1.0162 0.0367  -0.0618 0.0259  468 ILE D C   
7536  O O   . ILE C 136 ? 0.8602 1.0571 0.9899 0.0355  -0.0672 0.0277  468 ILE D O   
7537  C CB  . ILE C 136 ? 0.8073 1.0281 0.9332 0.0148  -0.0596 0.0315  468 ILE D CB  
7538  C CG1 . ILE C 136 ? 0.7926 1.0347 0.9351 0.0199  -0.0650 0.0332  468 ILE D CG1 
7539  C CG2 . ILE C 136 ? 0.8046 1.0291 0.9216 0.0018  -0.0541 0.0333  468 ILE D CG2 
7540  C CD1 . ILE C 136 ? 0.7318 0.9772 0.8792 0.0135  -0.0715 0.0372  468 ILE D CD1 
7541  N N   . SER C 137 ? 0.8784 1.0789 1.0076 0.0473  -0.0606 0.0226  469 SER D N   
7542  C CA  . SER C 137 ? 0.8889 1.0794 1.0215 0.0582  -0.0659 0.0212  469 SER D CA  
7543  C C   . SER C 137 ? 0.8204 0.9875 0.9407 0.0574  -0.0646 0.0210  469 SER D C   
7544  O O   . SER C 137 ? 0.8768 1.0367 0.9879 0.0543  -0.0586 0.0201  469 SER D O   
7545  C CB  . SER C 137 ? 0.9573 1.1560 1.0965 0.0699  -0.0654 0.0179  469 SER D CB  
7546  O OG  . SER C 137 ? 0.9668 1.1532 1.0966 0.0730  -0.0609 0.0153  469 SER D OG  
7547  N N   . THR C 138 ? 0.7530 0.9087 0.8737 0.0599  -0.0703 0.0222  470 THR D N   
7548  C CA  . THR C 138 ? 0.8371 0.9713 0.9478 0.0606  -0.0697 0.0226  470 THR D CA  
7549  C C   . THR C 138 ? 0.8995 1.0259 1.0119 0.0726  -0.0735 0.0210  470 THR D C   
7550  O O   . THR C 138 ? 0.9109 1.0214 1.0189 0.0749  -0.0764 0.0223  470 THR D O   
7551  C CB  . THR C 138 ? 0.8488 0.9735 0.9566 0.0540  -0.0726 0.0254  470 THR D CB  
7552  O OG1 . THR C 138 ? 0.9208 1.0488 1.0375 0.0597  -0.0809 0.0261  470 THR D OG1 
7553  C CG2 . THR C 138 ? 0.8701 1.0025 0.9755 0.0416  -0.0691 0.0270  470 THR D CG2 
7554  N N   . GLU C 139 ? 0.8878 1.0253 1.0064 0.0801  -0.0734 0.0183  471 GLU D N   
7555  C CA  . GLU C 139 ? 0.8654 0.9954 0.9842 0.0912  -0.0764 0.0164  471 GLU D CA  
7556  C C   . GLU C 139 ? 0.8829 0.9975 0.9903 0.0911  -0.0719 0.0160  471 GLU D C   
7557  O O   . GLU C 139 ? 0.9067 1.0231 1.0086 0.0857  -0.0651 0.0154  471 GLU D O   
7558  C CB  . GLU C 139 ? 0.9171 1.0635 1.0449 0.0983  -0.0762 0.0134  471 GLU D CB  
7559  C CG  . GLU C 139 ? 0.9923 1.1333 1.1219 0.1102  -0.0801 0.0111  471 GLU D CG  
7560  C CD  . GLU C 139 ? 1.1634 1.3165 1.2962 0.1155  -0.0754 0.0073  471 GLU D CD  
7561  O OE1 . GLU C 139 ? 1.3891 1.5601 1.5330 0.1172  -0.0758 0.0068  471 GLU D OE1 
7562  O OE2 . GLU C 139 ? 1.1597 1.3052 1.2842 0.1174  -0.0711 0.0052  471 GLU D OE2 
7563  N N   . ILE C 140 ? 1.0043 1.1038 1.1082 0.0971  -0.0762 0.0168  472 ILE D N   
7564  C CA  . ILE C 140 ? 0.9401 1.0229 1.0333 0.0963  -0.0732 0.0179  472 ILE D CA  
7565  C C   . ILE C 140 ? 0.8902 0.9759 0.9803 0.0996  -0.0685 0.0149  472 ILE D C   
7566  O O   . ILE C 140 ? 0.9554 1.0489 1.0503 0.1072  -0.0703 0.0119  472 ILE D O   
7567  C CB  . ILE C 140 ? 0.9626 1.0305 1.0540 0.1024  -0.0800 0.0200  472 ILE D CB  
7568  C CG1 . ILE C 140 ? 0.9662 1.0288 1.0584 0.0971  -0.0830 0.0234  472 ILE D CG1 
7569  C CG2 . ILE C 140 ? 0.9725 1.0262 1.0548 0.1043  -0.0777 0.0209  472 ILE D CG2 
7570  C CD1 . ILE C 140 ? 0.9315 0.9891 1.0173 0.0871  -0.0765 0.0254  472 ILE D CD1 
7571  N N   . TYR C 141 ? 0.8182 0.8975 0.9000 0.0941  -0.0625 0.0157  473 TYR D N   
7572  C CA  . TYR C 141 ? 0.8789 0.9622 0.9575 0.0961  -0.0578 0.0128  473 TYR D CA  
7573  C C   . TYR C 141 ? 0.9590 1.0301 1.0332 0.1040  -0.0611 0.0124  473 TYR D C   
7574  O O   . TYR C 141 ? 0.9883 1.0438 1.0580 0.1048  -0.0645 0.0158  473 TYR D O   
7575  C CB  . TYR C 141 ? 0.8701 0.9508 0.9413 0.0871  -0.0507 0.0139  473 TYR D CB  
7576  C CG  . TYR C 141 ? 0.7987 0.8857 0.8666 0.0873  -0.0454 0.0110  473 TYR D CG  
7577  C CD1 . TYR C 141 ? 0.8975 0.9732 0.9584 0.0903  -0.0449 0.0110  473 TYR D CD1 
7578  C CD2 . TYR C 141 ? 0.8455 0.9506 0.9175 0.0843  -0.0412 0.0084  473 TYR D CD2 
7579  C CE1 . TYR C 141 ? 0.9073 0.9887 0.9646 0.0898  -0.0401 0.0083  473 TYR D CE1 
7580  C CE2 . TYR C 141 ? 0.8581 0.9696 0.9270 0.0842  -0.0362 0.0057  473 TYR D CE2 
7581  C CZ  . TYR C 141 ? 0.8825 0.9818 0.9438 0.0869  -0.0356 0.0054  473 TYR D CZ  
7582  O OH  . TYR C 141 ? 0.8920 0.9971 0.9495 0.0863  -0.0308 0.0026  473 TYR D OH  
7583  N N   . GLN C 142 ? 0.9700 1.0484 1.0452 0.1097  -0.0598 0.0084  474 GLN D N   
7584  C CA  . GLN C 142 ? 1.0049 1.0728 1.0757 0.1176  -0.0630 0.0074  474 GLN D CA  
7585  C C   . GLN C 142 ? 1.0194 1.0802 1.0802 0.1144  -0.0578 0.0073  474 GLN D C   
7586  O O   . GLN C 142 ? 1.0765 1.1424 1.1354 0.1177  -0.0549 0.0035  474 GLN D O   
7587  C CB  . GLN C 142 ? 1.2028 1.2822 1.2806 0.1263  -0.0647 0.0027  474 GLN D CB  
7588  C CG  . GLN C 142 ? 1.2144 1.2827 1.2869 0.1350  -0.0683 0.0009  474 GLN D CG  
7589  C CD  . GLN C 142 ? 1.2565 1.3146 1.3310 0.1403  -0.0771 0.0033  474 GLN D CD  
7590  O OE1 . GLN C 142 ? 1.3084 1.3559 1.3802 0.1366  -0.0803 0.0079  474 GLN D OE1 
7591  N NE2 . GLN C 142 ? 1.2221 1.2828 1.3007 0.1493  -0.0809 0.0002  474 GLN D NE2 
7592  N N   . ALA C 143 ? 1.0719 1.1211 1.1263 0.1077  -0.0562 0.0116  475 ALA D N   
7593  C CA  . ALA C 143 ? 1.0299 1.0740 1.0759 0.1034  -0.0510 0.0120  475 ALA D CA  
7594  C C   . ALA C 143 ? 1.0511 1.0835 1.0900 0.1088  -0.0537 0.0119  475 ALA D C   
7595  O O   . ALA C 143 ? 1.1074 1.1391 1.1399 0.1067  -0.0496 0.0106  475 ALA D O   
7596  C CB  . ALA C 143 ? 1.0062 1.0408 1.0478 0.0950  -0.0485 0.0171  475 ALA D CB  
7597  N N   . GLY C 144 ? 1.0235 1.0470 1.0629 0.1154  -0.0607 0.0132  476 GLY D N   
7598  C CA  . GLY C 144 ? 1.0545 1.0651 1.0861 0.1199  -0.0640 0.0138  476 GLY D CA  
7599  C C   . GLY C 144 ? 1.1823 1.1985 1.2152 0.1283  -0.0655 0.0081  476 GLY D C   
7600  O O   . GLY C 144 ? 1.1709 1.2028 1.2104 0.1303  -0.0623 0.0032  476 GLY D O   
7601  N N   . ASN C 145 ? 1.1895 1.1919 1.2155 0.1332  -0.0705 0.0091  477 ASN D N   
7602  C CA  . ASN C 145 ? 1.1583 1.1615 1.1827 0.1413  -0.0721 0.0040  477 ASN D CA  
7603  C C   . ASN C 145 ? 1.1169 1.1161 1.1460 0.1488  -0.0803 0.0045  477 ASN D C   
7604  O O   . ASN C 145 ? 1.1486 1.1464 1.1765 0.1563  -0.0826 0.0006  477 ASN D O   
7605  C CB  . ASN C 145 ? 1.2069 1.1961 1.2180 0.1405  -0.0717 0.0047  477 ASN D CB  
7606  C CG  . ASN C 145 ? 1.3076 1.3003 1.3155 0.1465  -0.0693 -0.0019 477 ASN D CG  
7607  O OD1 . ASN C 145 ? 1.1868 1.1956 1.2016 0.1483  -0.0641 -0.0072 477 ASN D OD1 
7608  N ND2 . ASN C 145 ? 1.5652 1.5427 1.5623 0.1496  -0.0728 -0.0016 477 ASN D ND2 
7609  N N   . LYS C 146 ? 1.0975 1.0945 1.1316 0.1466  -0.0846 0.0091  478 LYS D N   
7610  C CA  . LYS C 146 ? 1.1230 1.1144 1.1607 0.1519  -0.0932 0.0111  478 LYS D CA  
7611  C C   . LYS C 146 ? 1.2558 1.2620 1.3066 0.1519  -0.0938 0.0100  478 LYS D C   
7612  O O   . LYS C 146 ? 1.3098 1.3262 1.3648 0.1457  -0.0882 0.0100  478 LYS D O   
7613  C CB  . LYS C 146 ? 1.1137 1.0892 1.1454 0.1482  -0.0977 0.0184  478 LYS D CB  
7614  C CG  . LYS C 146 ? 1.0983 1.0575 1.1196 0.1520  -0.1031 0.0204  478 LYS D CG  
7615  C CD  . LYS C 146 ? 1.0588 1.0033 1.0753 0.1486  -0.1081 0.0284  478 LYS D CD  
7616  C CE  . LYS C 146 ? 1.0950 1.0240 1.1004 0.1523  -0.1138 0.0303  478 LYS D CE  
7617  N NZ  . LYS C 146 ? 1.0820 1.0106 1.0892 0.1609  -0.1204 0.0267  478 LYS D NZ  
7618  N N   . PRO C 147 ? 1.2836 1.2912 1.3407 0.1583  -0.1007 0.0093  479 PRO D N   
7619  C CA  . PRO C 147 ? 1.2789 1.3011 1.3487 0.1580  -0.1018 0.0086  479 PRO D CA  
7620  C C   . PRO C 147 ? 1.3591 1.3780 1.4308 0.1513  -0.1041 0.0139  479 PRO D C   
7621  O O   . PRO C 147 ? 1.3614 1.3661 1.4279 0.1513  -0.1095 0.0184  479 PRO D O   
7622  C CB  . PRO C 147 ? 1.2495 1.2716 1.3242 0.1672  -0.1092 0.0066  479 PRO D CB  
7623  C CG  . PRO C 147 ? 1.2448 1.2569 1.3100 0.1728  -0.1088 0.0038  479 PRO D CG  
7624  C CD  . PRO C 147 ? 1.3044 1.3032 1.3574 0.1669  -0.1063 0.0073  479 PRO D CD  
7625  N N   . CYS C 148 ? 1.4649 1.4969 1.5436 0.1455  -0.1000 0.0136  480 CYS D N   
7626  C CA  . CYS C 148 ? 1.3740 1.4041 1.4549 0.1390  -0.1015 0.0180  480 CYS D CA  
7627  C C   . CYS C 148 ? 1.3785 1.4212 1.4707 0.1397  -0.1054 0.0172  480 CYS D C   
7628  O O   . CYS C 148 ? 1.4295 1.4871 1.5280 0.1362  -0.1010 0.0152  480 CYS D O   
7629  C CB  . CYS C 148 ? 1.3261 1.3579 1.4036 0.1299  -0.0934 0.0192  480 CYS D CB  
7630  S SG  . CYS C 148 ? 1.7090 1.7207 1.7745 0.1272  -0.0925 0.0240  480 CYS D SG  
7631  N N   . ASN C 149 ? 1.3312 1.3677 1.4256 0.1432  -0.1138 0.0194  481 ASN D N   
7632  C CA  . ASN C 149 ? 1.3182 1.3659 1.4235 0.1442  -0.1188 0.0191  481 ASN D CA  
7633  C C   . ASN C 149 ? 1.2739 1.3226 1.3807 0.1352  -0.1183 0.0226  481 ASN D C   
7634  O O   . ASN C 149 ? 1.2621 1.3033 1.3689 0.1345  -0.1244 0.0259  481 ASN D O   
7635  C CB  . ASN C 149 ? 1.3260 1.3668 1.4330 0.1521  -0.1285 0.0198  481 ASN D CB  
7636  C CG  . ASN C 149 ? 1.3728 1.4103 1.4767 0.1609  -0.1289 0.0162  481 ASN D CG  
7637  O OD1 . ASN C 149 ? 1.3821 1.4146 1.4780 0.1607  -0.1231 0.0148  481 ASN D OD1 
7638  N ND2 . ASN C 149 ? 1.4780 1.5184 1.5883 0.1686  -0.1355 0.0146  481 ASN D ND2 
7639  N N   . GLY C 150 ? 1.2411 1.2987 1.3485 0.1280  -0.1107 0.0218  482 GLY D N   
7640  C CA  . GLY C 150 ? 1.1958 1.2515 1.3018 0.1186  -0.1088 0.0249  482 GLY D CA  
7641  C C   . GLY C 150 ? 1.3164 1.3540 1.4125 0.1164  -0.1078 0.0285  482 GLY D C   
7642  O O   . GLY C 150 ? 1.3248 1.3569 1.4187 0.1099  -0.1069 0.0315  482 GLY D O   
7643  N N   . VAL C 151 ? 1.3450 1.3727 1.4350 0.1218  -0.1080 0.0285  483 VAL D N   
7644  C CA  . VAL C 151 ? 1.3180 1.3304 1.3990 0.1190  -0.1054 0.0323  483 VAL D CA  
7645  C C   . VAL C 151 ? 1.2798 1.2944 1.3578 0.1104  -0.0963 0.0324  483 VAL D C   
7646  O O   . VAL C 151 ? 1.3448 1.3710 1.4247 0.1083  -0.0911 0.0290  483 VAL D O   
7647  C CB  . VAL C 151 ? 1.4561 1.4600 1.5307 0.1250  -0.1060 0.0320  483 VAL D CB  
7648  C CG1 . VAL C 151 ? 1.4450 1.4322 1.5111 0.1226  -0.1050 0.0373  483 VAL D CG1 
7649  C CG2 . VAL C 151 ? 1.4929 1.4968 1.5705 0.1339  -0.1143 0.0304  483 VAL D CG2 
7650  N N   . ALA C 152 ? 1.2346 1.2379 1.3076 0.1055  -0.0941 0.0366  484 ALA D N   
7651  C CA  . ALA C 152 ? 1.0880 1.0893 1.1561 0.0984  -0.0853 0.0371  484 ALA D CA  
7652  C C   . ALA C 152 ? 1.0817 1.0669 1.1428 0.0998  -0.0849 0.0416  484 ALA D C   
7653  O O   . ALA C 152 ? 1.0077 0.9823 1.0673 0.0985  -0.0866 0.0461  484 ALA D O   
7654  C CB  . ALA C 152 ? 1.0698 1.0734 1.1388 0.0901  -0.0818 0.0379  484 ALA D CB  
7655  N N   . GLY C 153 ? 1.0387 1.0221 1.0959 0.1025  -0.0832 0.0406  485 GLY D N   
7656  C CA  . GLY C 153 ? 0.9918 0.9604 1.0428 0.1044  -0.0845 0.0454  485 GLY D CA  
7657  C C   . GLY C 153 ? 0.9082 0.8747 0.9535 0.1034  -0.0797 0.0450  485 GLY D C   
7658  O O   . GLY C 153 ? 0.9759 0.9473 1.0202 0.0977  -0.0725 0.0435  485 GLY D O   
7659  N N   . VAL C 154 ? 0.9803 0.9394 1.0213 0.1083  -0.0835 0.0464  486 VAL D N   
7660  C CA  . VAL C 154 ? 1.0073 0.9643 1.0422 0.1066  -0.0790 0.0461  486 VAL D CA  
7661  C C   . VAL C 154 ? 1.0204 0.9915 1.0571 0.1078  -0.0761 0.0389  486 VAL D C   
7662  O O   . VAL C 154 ? 1.0424 1.0208 1.0830 0.1136  -0.0802 0.0349  486 VAL D O   
7663  C CB  . VAL C 154 ? 0.9528 0.8971 0.9812 0.1105  -0.0839 0.0500  486 VAL D CB  
7664  C CG1 . VAL C 154 ? 0.8731 0.8048 0.9010 0.1100  -0.0877 0.0576  486 VAL D CG1 
7665  C CG2 . VAL C 154 ? 1.0296 0.9771 1.0583 0.1181  -0.0900 0.0458  486 VAL D CG2 
7666  N N   . ASN C 155 ? 0.9785 0.9538 1.0126 0.1023  -0.0688 0.0377  487 ASN D N   
7667  C CA  . ASN C 155 ? 1.0211 1.0099 1.0562 0.1025  -0.0649 0.0315  487 ASN D CA  
7668  C C   . ASN C 155 ? 0.9967 1.0004 1.0404 0.1044  -0.0658 0.0271  487 ASN D C   
7669  O O   . ASN C 155 ? 1.0186 1.0337 1.0651 0.1082  -0.0653 0.0219  487 ASN D O   
7670  C CB  . ASN C 155 ? 1.0319 1.0172 1.0619 0.1080  -0.0673 0.0296  487 ASN D CB  
7671  C CG  . ASN C 155 ? 1.0356 1.0109 1.0573 0.1039  -0.0645 0.0331  487 ASN D CG  
7672  O OD1 . ASN C 155 ? 1.1402 1.1170 1.1606 0.0969  -0.0585 0.0344  487 ASN D OD1 
7673  N ND2 . ASN C 155 ? 1.0908 1.0546 1.1065 0.1075  -0.0690 0.0355  487 ASN D ND2 
7674  N N   . CYS C 156 ? 1.0421 1.0454 1.0899 0.1016  -0.0671 0.0294  488 CYS D N   
7675  C CA  . CYS C 156 ? 0.9850 1.0011 1.0411 0.1021  -0.0688 0.0266  488 CYS D CA  
7676  C C   . CYS C 156 ? 0.9125 0.9280 0.9693 0.0941  -0.0655 0.0290  488 CYS D C   
7677  O O   . CYS C 156 ? 0.8743 0.8786 0.9299 0.0931  -0.0679 0.0332  488 CYS D O   
7678  C CB  . CYS C 156 ? 1.0346 1.0484 1.0949 0.1095  -0.0773 0.0268  488 CYS D CB  
7679  S SG  . CYS C 156 ? 1.2211 1.2363 1.2805 0.1190  -0.0807 0.0229  488 CYS D SG  
7680  N N   . TYR C 157 ? 0.9471 0.9747 1.0056 0.0885  -0.0602 0.0265  489 TYR D N   
7681  C CA  . TYR C 157 ? 0.9560 0.9825 1.0133 0.0799  -0.0560 0.0284  489 TYR D CA  
7682  C C   . TYR C 157 ? 0.8736 0.9150 0.9377 0.0773  -0.0567 0.0260  489 TYR D C   
7683  O O   . TYR C 157 ? 0.8309 0.8869 0.9004 0.0804  -0.0575 0.0225  489 TYR D O   
7684  C CB  . TYR C 157 ? 0.9679 0.9925 1.0188 0.0734  -0.0484 0.0287  489 TYR D CB  
7685  C CG  . TYR C 157 ? 0.9730 0.9869 1.0185 0.0765  -0.0481 0.0306  489 TYR D CG  
7686  C CD1 . TYR C 157 ? 1.0323 1.0293 1.0739 0.0767  -0.0494 0.0358  489 TYR D CD1 
7687  C CD2 . TYR C 157 ? 0.9526 0.9731 0.9966 0.0791  -0.0467 0.0274  489 TYR D CD2 
7688  C CE1 . TYR C 157 ? 0.9665 0.9537 1.0031 0.0790  -0.0497 0.0383  489 TYR D CE1 
7689  C CE2 . TYR C 157 ? 0.9825 0.9927 1.0207 0.0812  -0.0468 0.0293  489 TYR D CE2 
7690  C CZ  . TYR C 157 ? 0.9538 0.9474 0.9883 0.0809  -0.0486 0.0350  489 TYR D CZ  
7691  O OH  . TYR C 157 ? 1.1275 1.1115 1.1562 0.0823  -0.0490 0.0375  489 TYR D OH  
7692  N N   . PHE C 158 ? 0.7796 0.8167 0.8434 0.0717  -0.0568 0.0283  490 PHE D N   
7693  C CA  . PHE C 158 ? 0.8100 0.8594 0.8777 0.0658  -0.0559 0.0270  490 PHE D CA  
7694  C C   . PHE C 158 ? 0.8147 0.8737 0.8798 0.0595  -0.0491 0.0252  490 PHE D C   
7695  O O   . PHE C 158 ? 0.8065 0.8567 0.8642 0.0541  -0.0434 0.0266  490 PHE D O   
7696  C CB  . PHE C 158 ? 0.8413 0.8812 0.9060 0.0594  -0.0554 0.0300  490 PHE D CB  
7697  C CG  . PHE C 158 ? 0.8119 0.8634 0.8811 0.0542  -0.0569 0.0292  490 PHE D CG  
7698  C CD1 . PHE C 158 ? 0.7985 0.8636 0.8770 0.0592  -0.0630 0.0275  490 PHE D CD1 
7699  C CD2 . PHE C 158 ? 0.8022 0.8518 0.8663 0.0438  -0.0519 0.0301  490 PHE D CD2 
7700  C CE1 . PHE C 158 ? 0.8213 0.8982 0.9046 0.0538  -0.0646 0.0274  490 PHE D CE1 
7701  C CE2 . PHE C 158 ? 0.8293 0.8898 0.8967 0.0379  -0.0534 0.0298  490 PHE D CE2 
7702  C CZ  . PHE C 158 ? 0.8235 0.8981 0.9009 0.0427  -0.0599 0.0287  490 PHE D CZ  
7703  N N   . PRO C 159 ? 0.7714 0.8485 0.8427 0.0597  -0.0493 0.0224  491 PRO D N   
7704  C CA  . PRO C 159 ? 0.7760 0.8630 0.8449 0.0546  -0.0431 0.0207  491 PRO D CA  
7705  C C   . PRO C 159 ? 0.7856 0.8709 0.8485 0.0431  -0.0380 0.0224  491 PRO D C   
7706  O O   . PRO C 159 ? 0.8079 0.8975 0.8665 0.0380  -0.0325 0.0216  491 PRO D O   
7707  C CB  . PRO C 159 ? 0.8176 0.9250 0.8962 0.0587  -0.0455 0.0180  491 PRO D CB  
7708  C CG  . PRO C 159 ? 0.8224 0.9313 0.9079 0.0616  -0.0521 0.0190  491 PRO D CG  
7709  C CD  . PRO C 159 ? 0.8127 0.9023 0.8940 0.0655  -0.0554 0.0210  491 PRO D CD  
7710  N N   . LEU C 160 ? 0.7588 0.8367 0.8202 0.0384  -0.0393 0.0245  492 LEU D N   
7711  C CA  . LEU C 160 ? 0.7745 0.8512 0.8299 0.0269  -0.0346 0.0258  492 LEU D CA  
7712  C C   . LEU C 160 ? 0.7175 0.7736 0.7637 0.0230  -0.0309 0.0282  492 LEU D C   
7713  O O   . LEU C 160 ? 0.7339 0.7784 0.7803 0.0259  -0.0339 0.0299  492 LEU D O   
7714  C CB  . LEU C 160 ? 0.8024 0.8881 0.8625 0.0228  -0.0383 0.0263  492 LEU D CB  
7715  C CG  . LEU C 160 ? 0.7426 0.8504 0.8107 0.0215  -0.0403 0.0252  492 LEU D CG  
7716  C CD1 . LEU C 160 ? 0.7633 0.8822 0.8431 0.0318  -0.0468 0.0240  492 LEU D CD1 
7717  C CD2 . LEU C 160 ? 0.7651 0.8715 0.8311 0.0125  -0.0413 0.0273  492 LEU D CD2 
7718  N N   . GLN C 161 ? 0.7434 0.7955 0.7819 0.0159  -0.0243 0.0285  493 GLN D N   
7719  C CA  . GLN C 161 ? 0.7798 0.8129 0.8097 0.0115  -0.0195 0.0309  493 GLN D CA  
7720  C C   . GLN C 161 ? 0.7657 0.7978 0.7891 0.0000  -0.0155 0.0313  493 GLN D C   
7721  O O   . GLN C 161 ? 0.8200 0.8670 0.8446 -0.0052 -0.0155 0.0299  493 GLN D O   
7722  C CB  . GLN C 161 ? 0.8569 0.8856 0.8825 0.0118  -0.0151 0.0312  493 GLN D CB  
7723  C CG  . GLN C 161 ? 0.9078 0.9166 0.9279 0.0120  -0.0120 0.0343  493 GLN D CG  
7724  C CD  . GLN C 161 ? 1.0302 1.0332 1.0552 0.0222  -0.0171 0.0357  493 GLN D CD  
7725  O OE1 . GLN C 161 ? 0.8434 0.8561 0.8753 0.0287  -0.0231 0.0340  493 GLN D OE1 
7726  N NE2 . GLN C 161 ? 1.1782 1.1651 1.1998 0.0237  -0.0150 0.0392  493 GLN D NE2 
7727  N N   . SER C 162 ? 0.7490 0.7637 0.7653 -0.0044 -0.0118 0.0334  494 SER D N   
7728  C CA  . SER C 162 ? 0.8033 0.8155 0.8117 -0.0160 -0.0075 0.0335  494 SER D CA  
7729  C C   . SER C 162 ? 0.7898 0.7888 0.7883 -0.0220 0.0002  0.0346  494 SER D C   
7730  O O   . SER C 162 ? 0.8404 0.8260 0.8376 -0.0176 0.0024  0.0363  494 SER D O   
7731  C CB  . SER C 162 ? 0.8353 0.8393 0.8422 -0.0187 -0.0090 0.0344  494 SER D CB  
7732  O OG  . SER C 162 ? 0.8395 0.8287 0.8475 -0.0121 -0.0099 0.0363  494 SER D OG  
7733  N N   . TYR C 163 ? 0.7787 0.7818 0.7702 -0.0323 0.0040  0.0339  495 TYR D N   
7734  C CA  . TYR C 163 ? 0.7832 0.7745 0.7648 -0.0390 0.0112  0.0348  495 TYR D CA  
7735  C C   . TYR C 163 ? 0.7771 0.7464 0.7515 -0.0419 0.0154  0.0366  495 TYR D C   
7736  O O   . TYR C 163 ? 0.8434 0.8095 0.8144 -0.0470 0.0153  0.0364  495 TYR D O   
7737  C CB  . TYR C 163 ? 0.7784 0.7791 0.7531 -0.0503 0.0138  0.0339  495 TYR D CB  
7738  C CG  . TYR C 163 ? 0.7012 0.7251 0.6822 -0.0495 0.0105  0.0323  495 TYR D CG  
7739  C CD1 . TYR C 163 ? 0.7748 0.8092 0.7660 -0.0391 0.0064  0.0313  495 TYR D CD1 
7740  C CD2 . TYR C 163 ? 0.7471 0.7793 0.7218 -0.0594 0.0132  0.0322  495 TYR D CD2 
7741  C CE1 . TYR C 163 ? 0.7610 0.8155 0.7572 -0.0384 0.0046  0.0299  495 TYR D CE1 
7742  C CE2 . TYR C 163 ? 0.8116 0.8644 0.7914 -0.0590 0.0113  0.0311  495 TYR D CE2 
7743  C CZ  . TYR C 163 ? 0.7555 0.8195 0.7464 -0.0482 0.0072  0.0299  495 TYR D CZ  
7744  O OH  . TYR C 163 ? 0.7388 0.8236 0.7348 -0.0478 0.0060  0.0287  495 TYR D OH  
7745  N N   . GLY C 164 ? 0.7009 0.6550 0.6728 -0.0391 0.0195  0.0386  496 GLY D N   
7746  C CA  . GLY C 164 ? 0.8269 0.7615 0.7937 -0.0406 0.0234  0.0403  496 GLY D CA  
7747  C C   . GLY C 164 ? 0.8418 0.7655 0.7959 -0.0523 0.0304  0.0400  496 GLY D C   
7748  O O   . GLY C 164 ? 0.9518 0.8576 0.9000 -0.0536 0.0366  0.0419  496 GLY D O   
7749  N N   . PHE C 165 ? 0.8329 0.7662 0.7823 -0.0610 0.0296  0.0380  497 PHE D N   
7750  C CA  . PHE C 165 ? 0.8597 0.7858 0.7964 -0.0726 0.0359  0.0377  497 PHE D CA  
7751  C C   . PHE C 165 ? 0.9146 0.8169 0.8415 -0.0767 0.0427  0.0387  497 PHE D C   
7752  O O   . PHE C 165 ? 0.9602 0.8560 0.8875 -0.0756 0.0420  0.0387  497 PHE D O   
7753  C CB  . PHE C 165 ? 0.8942 0.8348 0.8272 -0.0819 0.0335  0.0362  497 PHE D CB  
7754  C CG  . PHE C 165 ? 0.8599 0.8218 0.7984 -0.0815 0.0298  0.0354  497 PHE D CG  
7755  C CD1 . PHE C 165 ? 0.8304 0.7917 0.7673 -0.0811 0.0328  0.0359  497 PHE D CD1 
7756  C CD2 . PHE C 165 ? 0.8394 0.8218 0.7840 -0.0826 0.0239  0.0346  497 PHE D CD2 
7757  C CE1 . PHE C 165 ? 0.8293 0.8102 0.7706 -0.0812 0.0300  0.0351  497 PHE D CE1 
7758  C CE2 . PHE C 165 ? 0.8399 0.8420 0.7895 -0.0823 0.0213  0.0341  497 PHE D CE2 
7759  C CZ  . PHE C 165 ? 0.8521 0.8534 0.7996 -0.0818 0.0246  0.0341  497 PHE D CZ  
7760  N N   . ARG C 166 ? 0.8952 0.7844 0.8133 -0.0815 0.0496  0.0396  498 ARG D N   
7761  C CA  . ARG C 166 ? 0.9631 0.8277 0.8720 -0.0844 0.0576  0.0408  498 ARG D CA  
7762  C C   . ARG C 166 ? 0.9859 0.8433 0.8818 -0.0953 0.0636  0.0404  498 ARG D C   
7763  O O   . ARG C 166 ? 0.9916 0.8598 0.8889 -0.0963 0.0621  0.0405  498 ARG D O   
7764  C CB  . ARG C 166 ? 0.9558 0.8091 0.8721 -0.0739 0.0595  0.0438  498 ARG D CB  
7765  C CG  . ARG C 166 ? 1.0048 0.8560 0.9296 -0.0651 0.0561  0.0448  498 ARG D CG  
7766  C CD  . ARG C 166 ? 0.9250 0.7677 0.8578 -0.0550 0.0570  0.0487  498 ARG D CD  
7767  N NE  . ARG C 166 ? 0.9296 0.7862 0.8749 -0.0451 0.0487  0.0493  498 ARG D NE  
7768  C CZ  . ARG C 166 ? 1.0016 0.8591 0.9524 -0.0398 0.0446  0.0495  498 ARG D CZ  
7769  N NH1 . ARG C 166 ? 1.0559 0.8994 1.0020 -0.0420 0.0487  0.0499  498 ARG D NH1 
7770  N NH2 . ARG C 166 ? 0.9806 0.8529 0.9417 -0.0322 0.0364  0.0493  498 ARG D NH2 
7771  N N   . PRO C 167 ? 0.9847 0.8238 0.8674 -0.1036 0.0703  0.0399  499 PRO D N   
7772  C CA  . PRO C 167 ? 1.0147 0.8475 0.8835 -0.1153 0.0753  0.0393  499 PRO D CA  
7773  C C   . PRO C 167 ? 1.0422 0.8663 0.9106 -0.1132 0.0795  0.0414  499 PRO D C   
7774  O O   . PRO C 167 ? 0.9867 0.8138 0.8476 -0.1211 0.0807  0.0411  499 PRO D O   
7775  C CB  . PRO C 167 ? 1.0290 0.8413 0.8839 -0.1232 0.0817  0.0382  499 PRO D CB  
7776  C CG  . PRO C 167 ? 1.0022 0.8052 0.8652 -0.1131 0.0824  0.0392  499 PRO D CG  
7777  C CD  . PRO C 167 ? 0.9867 0.8116 0.8658 -0.1037 0.0731  0.0395  499 PRO D CD  
7778  N N   . THR C 168 ? 1.0659 0.8795 0.9424 -0.1031 0.0816  0.0439  500 THR D N   
7779  C CA  . THR C 168 ? 1.0428 0.8462 0.9197 -0.1010 0.0859  0.0467  500 THR D CA  
7780  C C   . THR C 168 ? 1.0294 0.8509 0.9170 -0.0956 0.0799  0.0478  500 THR D C   
7781  O O   . THR C 168 ? 1.0389 0.8540 0.9302 -0.0918 0.0820  0.0508  500 THR D O   
7782  C CB  . THR C 168 ? 1.0111 0.7940 0.8913 -0.0936 0.0913  0.0496  500 THR D CB  
7783  O OG1 . THR C 168 ? 1.0726 0.8648 0.9677 -0.0819 0.0856  0.0515  500 THR D OG1 
7784  C CG2 . THR C 168 ? 1.0158 0.7837 0.8868 -0.0979 0.0964  0.0479  500 THR D CG2 
7785  N N   . TYR C 169 ? 1.0152 0.8593 0.9077 -0.0955 0.0728  0.0456  501 TYR D N   
7786  C CA  . TYR C 169 ? 0.9408 0.8030 0.8425 -0.0908 0.0674  0.0460  501 TYR D CA  
7787  C C   . TYR C 169 ? 0.9116 0.7770 0.8050 -0.1001 0.0694  0.0457  501 TYR D C   
7788  O O   . TYR C 169 ? 0.9631 0.8189 0.8437 -0.1102 0.0740  0.0450  501 TYR D O   
7789  C CB  . TYR C 169 ? 0.9063 0.7906 0.8159 -0.0876 0.0597  0.0435  501 TYR D CB  
7790  C CG  . TYR C 169 ? 0.8700 0.7557 0.7915 -0.0757 0.0556  0.0444  501 TYR D CG  
7791  C CD1 . TYR C 169 ? 0.9104 0.7772 0.8332 -0.0704 0.0591  0.0469  501 TYR D CD1 
7792  C CD2 . TYR C 169 ? 0.8536 0.7591 0.7844 -0.0705 0.0482  0.0426  501 TYR D CD2 
7793  C CE1 . TYR C 169 ? 0.9255 0.7939 0.8589 -0.0599 0.0547  0.0481  501 TYR D CE1 
7794  C CE2 . TYR C 169 ? 0.8784 0.7846 0.8192 -0.0601 0.0439  0.0434  501 TYR D CE2 
7795  C CZ  . TYR C 169 ? 0.8934 0.7813 0.8353 -0.0550 0.0469  0.0461  501 TYR D CZ  
7796  O OH  . TYR C 169 ? 0.7631 0.6532 0.7148 -0.0451 0.0419  0.0471  501 TYR D OH  
7797  N N   . GLY C 170 ? 0.9396 0.8175 0.8395 -0.0969 0.0662  0.0465  502 GLY D N   
7798  C CA  . GLY C 170 ? 0.9795 0.8621 0.8723 -0.1054 0.0676  0.0465  502 GLY D CA  
7799  C C   . GLY C 170 ? 1.0469 0.9509 0.9379 -0.1113 0.0634  0.0437  502 GLY D C   
7800  O O   . GLY C 170 ? 1.0149 0.9337 0.9137 -0.1065 0.0583  0.0420  502 GLY D O   
7801  N N   . VAL C 171 ? 1.1606 1.0661 1.0413 -0.1220 0.0654  0.0436  503 VAL D N   
7802  C CA  . VAL C 171 ? 1.1746 1.0986 1.0515 -0.1298 0.0622  0.0417  503 VAL D CA  
7803  C C   . VAL C 171 ? 1.1893 1.1395 1.0790 -0.1230 0.0556  0.0405  503 VAL D C   
7804  O O   . VAL C 171 ? 1.1723 1.1386 1.0639 -0.1253 0.0520  0.0391  503 VAL D O   
7805  C CB  . VAL C 171 ? 1.1838 1.1047 1.0478 -0.1421 0.0653  0.0425  503 VAL D CB  
7806  C CG1 . VAL C 171 ? 1.2253 1.1696 1.0876 -0.1493 0.0612  0.0415  503 VAL D CG1 
7807  C CG2 . VAL C 171 ? 1.2451 1.1412 1.0946 -0.1501 0.0715  0.0429  503 VAL D CG2 
7808  N N   . GLY C 172 ? 1.0874 1.0417 0.9867 -0.1143 0.0540  0.0410  504 GLY D N   
7809  C CA  . GLY C 172 ? 1.0396 1.0160 0.9508 -0.1066 0.0483  0.0395  504 GLY D CA  
7810  C C   . GLY C 172 ? 0.9862 0.9639 0.9069 -0.0970 0.0450  0.0385  504 GLY D C   
7811  O O   . GLY C 172 ? 1.0318 1.0287 0.9615 -0.0918 0.0401  0.0369  504 GLY D O   
7812  N N   . HIS C 173 ? 0.8943 0.8521 0.8134 -0.0941 0.0474  0.0397  505 HIS D N   
7813  C CA  . HIS C 173 ? 0.8851 0.8430 0.8132 -0.0847 0.0440  0.0392  505 HIS D CA  
7814  C C   . HIS C 173 ? 0.9263 0.8793 0.8495 -0.0895 0.0444  0.0384  505 HIS D C   
7815  O O   . HIS C 173 ? 0.8961 0.8448 0.8248 -0.0830 0.0424  0.0383  505 HIS D O   
7816  C CB  . HIS C 173 ? 0.9040 0.8445 0.8360 -0.0764 0.0457  0.0415  505 HIS D CB  
7817  C CG  . HIS C 173 ? 0.9402 0.8887 0.8815 -0.0677 0.0423  0.0422  505 HIS D CG  
7818  N ND1 . HIS C 173 ? 0.9303 0.8775 0.8700 -0.0694 0.0442  0.0437  505 HIS D ND1 
7819  C CD2 . HIS C 173 ? 0.9592 0.9180 0.9110 -0.0579 0.0369  0.0414  505 HIS D CD2 
7820  C CE1 . HIS C 173 ? 0.9870 0.9425 0.9353 -0.0612 0.0404  0.0439  505 HIS D CE1 
7821  N NE2 . HIS C 173 ? 1.0041 0.9663 0.9596 -0.0539 0.0360  0.0424  505 HIS D NE2 
7822  N N   . GLN C 174 ? 0.9508 0.9035 0.8632 -0.1011 0.0469  0.0380  506 GLN D N   
7823  C CA  . GLN C 174 ? 0.8707 0.8192 0.7748 -0.1095 0.0479  0.0374  506 GLN D CA  
7824  C C   . GLN C 174 ? 0.8650 0.8374 0.7751 -0.1107 0.0419  0.0363  506 GLN D C   
7825  O O   . GLN C 174 ? 0.8420 0.8337 0.7579 -0.1095 0.0388  0.0359  506 GLN D O   
7826  C CB  . GLN C 174 ? 0.8935 0.8303 0.7819 -0.1224 0.0536  0.0380  506 GLN D CB  
7827  C CG  . GLN C 174 ? 0.9159 0.8247 0.7962 -0.1229 0.0604  0.0391  506 GLN D CG  
7828  C CD  . GLN C 174 ? 0.9783 0.8736 0.8418 -0.1360 0.0662  0.0394  506 GLN D CD  
7829  O OE1 . GLN C 174 ? 1.1008 1.0075 0.9576 -0.1456 0.0646  0.0390  506 GLN D OE1 
7830  N NE2 . GLN C 174 ? 0.9542 0.8247 0.8105 -0.1364 0.0728  0.0404  506 GLN D NE2 
7831  N N   . PRO C 175 ? 0.9611 0.9325 0.8700 -0.1133 0.0402  0.0359  507 PRO D N   
7832  C CA  . PRO C 175 ? 0.9385 0.9326 0.8549 -0.1138 0.0340  0.0355  507 PRO D CA  
7833  C C   . PRO C 175 ? 0.9153 0.9218 0.8240 -0.1261 0.0341  0.0363  507 PRO D C   
7834  O O   . PRO C 175 ? 0.9730 0.9667 0.8673 -0.1373 0.0386  0.0370  507 PRO D O   
7835  C CB  . PRO C 175 ? 0.9195 0.9048 0.8348 -0.1144 0.0329  0.0354  507 PRO D CB  
7836  C CG  . PRO C 175 ? 0.9369 0.8960 0.8390 -0.1199 0.0399  0.0357  507 PRO D CG  
7837  C CD  . PRO C 175 ? 0.9555 0.9051 0.8578 -0.1147 0.0438  0.0361  507 PRO D CD  
7838  N N   . TYR C 176 ? 0.8074 0.8388 0.7257 -0.1240 0.0292  0.0363  508 TYR D N   
7839  C CA  . TYR C 176 ? 0.8889 0.9364 0.8024 -0.1348 0.0283  0.0377  508 TYR D CA  
7840  C C   . TYR C 176 ? 0.9121 0.9814 0.8355 -0.1345 0.0221  0.0387  508 TYR D C   
7841  O O   . TYR C 176 ? 0.9114 0.9956 0.8496 -0.1234 0.0180  0.0378  508 TYR D O   
7842  C CB  . TYR C 176 ? 0.8900 0.9498 0.8061 -0.1334 0.0289  0.0376  508 TYR D CB  
7843  C CG  . TYR C 176 ? 0.9444 0.9873 0.8470 -0.1404 0.0347  0.0380  508 TYR D CG  
7844  C CD1 . TYR C 176 ? 0.9973 1.0178 0.8973 -0.1351 0.0387  0.0373  508 TYR D CD1 
7845  C CD2 . TYR C 176 ? 0.9836 1.0333 0.8764 -0.1523 0.0359  0.0395  508 TYR D CD2 
7846  C CE1 . TYR C 176 ? 1.0573 1.0620 0.9455 -0.1415 0.0439  0.0380  508 TYR D CE1 
7847  C CE2 . TYR C 176 ? 1.1392 1.1730 1.0194 -0.1591 0.0408  0.0400  508 TYR D CE2 
7848  C CZ  . TYR C 176 ? 1.1625 1.1737 1.0406 -0.1535 0.0450  0.0392  508 TYR D CZ  
7849  O OH  . TYR C 176 ? 1.1955 1.1903 1.0616 -0.1601 0.0499  0.0399  508 TYR D OH  
7850  N N   . ARG C 177 ? 0.9012 0.9725 0.8163 -0.1468 0.0214  0.0407  509 ARG D N   
7851  C CA  . ARG C 177 ? 0.8570 0.9514 0.7824 -0.1474 0.0153  0.0425  509 ARG D CA  
7852  C C   . ARG C 177 ? 0.8606 0.9784 0.7892 -0.1512 0.0140  0.0443  509 ARG D C   
7853  O O   . ARG C 177 ? 0.8942 1.0082 0.8119 -0.1590 0.0177  0.0449  509 ARG D O   
7854  C CB  . ARG C 177 ? 0.8306 0.9189 0.7478 -0.1585 0.0140  0.0445  509 ARG D CB  
7855  C CG  . ARG C 177 ? 0.8732 0.9315 0.7764 -0.1620 0.0193  0.0430  509 ARG D CG  
7856  C CD  . ARG C 177 ? 0.9407 0.9867 0.8328 -0.1730 0.0196  0.0441  509 ARG D CD  
7857  N NE  . ARG C 177 ? 0.9361 0.9837 0.8380 -0.1667 0.0152  0.0438  509 ARG D NE  
7858  C CZ  . ARG C 177 ? 1.0199 1.0642 0.9163 -0.1756 0.0132  0.0453  509 ARG D CZ  
7859  N NH1 . ARG C 177 ? 1.1048 1.1438 0.9852 -0.1917 0.0153  0.0473  509 ARG D NH1 
7860  N NH2 . ARG C 177 ? 1.0286 1.0738 0.9348 -0.1686 0.0091  0.0448  509 ARG D NH2 
7861  N N   . VAL C 178 ? 0.8589 1.0010 0.8032 -0.1447 0.0088  0.0452  510 VAL D N   
7862  C CA  . VAL C 178 ? 0.8657 1.0328 0.8166 -0.1454 0.0074  0.0467  510 VAL D CA  
7863  C C   . VAL C 178 ? 0.8904 1.0820 0.8530 -0.1466 0.0018  0.0500  510 VAL D C   
7864  O O   . VAL C 178 ? 0.8730 1.0666 0.8455 -0.1401 -0.0022 0.0498  510 VAL D O   
7865  C CB  . VAL C 178 ? 0.8348 1.0082 0.7965 -0.1315 0.0082  0.0436  510 VAL D CB  
7866  C CG1 . VAL C 178 ? 0.8477 1.0051 0.7984 -0.1335 0.0134  0.0420  510 VAL D CG1 
7867  C CG2 . VAL C 178 ? 0.8178 0.9828 0.7886 -0.1191 0.0061  0.0411  510 VAL D CG2 
7868  N N   . VAL C 179 ? 0.9121 1.1235 0.8746 -0.1543 0.0012  0.0533  511 VAL D N   
7869  C CA  . VAL C 179 ? 0.8818 1.1196 0.8560 -0.1563 -0.0039 0.0575  511 VAL D CA  
7870  C C   . VAL C 179 ? 0.9097 1.1717 0.8926 -0.1529 -0.0034 0.0583  511 VAL D C   
7871  O O   . VAL C 179 ? 0.9824 1.2437 0.9551 -0.1601 -0.0001 0.0587  511 VAL D O   
7872  C CB  . VAL C 179 ? 0.9071 1.1448 0.8696 -0.1737 -0.0053 0.0626  511 VAL D CB  
7873  C CG1 . VAL C 179 ? 0.9674 1.2323 0.9440 -0.1748 -0.0110 0.0676  511 VAL D CG1 
7874  C CG2 . VAL C 179 ? 0.9292 1.1399 0.8790 -0.1792 -0.0041 0.0614  511 VAL D CG2 
7875  N N   . VAL C 180 ? 0.8286 1.1117 0.8301 -0.1422 -0.0068 0.0586  512 VAL D N   
7876  C CA  . VAL C 180 ? 0.9403 1.2480 0.9522 -0.1374 -0.0062 0.0591  512 VAL D CA  
7877  C C   . VAL C 180 ? 0.9906 1.3247 1.0132 -0.1421 -0.0106 0.0652  512 VAL D C   
7878  O O   . VAL C 180 ? 1.0294 1.3713 1.0656 -0.1351 -0.0148 0.0661  512 VAL D O   
7879  C CB  . VAL C 180 ? 0.9078 1.2181 0.9329 -0.1196 -0.0056 0.0541  512 VAL D CB  
7880  C CG1 . VAL C 180 ? 0.9684 1.3031 1.0023 -0.1158 -0.0041 0.0544  512 VAL D CG1 
7881  C CG2 . VAL C 180 ? 0.8829 1.1668 0.8977 -0.1155 -0.0018 0.0490  512 VAL D CG2 
7882  N N   . LEU C 181 ? 1.0717 1.4194 1.0883 -0.1543 -0.0100 0.0698  513 LEU D N   
7883  C CA  . LEU C 181 ? 1.0952 1.4695 1.1214 -0.1605 -0.0140 0.0769  513 LEU D CA  
7884  C C   . LEU C 181 ? 1.1901 1.5918 1.2329 -0.1506 -0.0133 0.0771  513 LEU D C   
7885  O O   . LEU C 181 ? 1.2558 1.6675 1.2942 -0.1550 -0.0104 0.0780  513 LEU D O   
7886  C CB  . LEU C 181 ? 1.0947 1.4685 1.1046 -0.1799 -0.0140 0.0824  513 LEU D CB  
7887  C CG  . LEU C 181 ? 0.9805 1.3255 0.9713 -0.1909 -0.0136 0.0819  513 LEU D CG  
7888  C CD1 . LEU C 181 ? 0.8618 1.2075 0.8362 -0.2100 -0.0135 0.0874  513 LEU D CD1 
7889  C CD2 . LEU C 181 ? 0.9603 1.3029 0.9591 -0.1885 -0.0182 0.0831  513 LEU D CD2 
7890  N N   . SER C 182 ? 1.1903 1.6038 1.2521 -0.1370 -0.0158 0.0761  514 SER D N   
7891  C CA  . SER C 182 ? 1.2548 1.6960 1.3345 -0.1270 -0.0153 0.0768  514 SER D CA  
7892  C C   . SER C 182 ? 1.3524 1.8205 1.4392 -0.1367 -0.0184 0.0856  514 SER D C   
7893  O O   . SER C 182 ? 1.3993 1.8743 1.4947 -0.1385 -0.0233 0.0902  514 SER D O   
7894  C CB  . SER C 182 ? 1.2024 1.6451 1.2991 -0.1094 -0.0170 0.0729  514 SER D CB  
7895  O OG  . SER C 182 ? 1.2267 1.6988 1.3429 -0.1013 -0.0176 0.0755  514 SER D OG  
7896  N N   . PHE C 183 ? 1.4494 1.9327 1.5324 -0.1436 -0.0157 0.0884  515 PHE D N   
7897  C CA  . PHE C 183 ? 1.4588 1.9709 1.5495 -0.1523 -0.0181 0.0973  515 PHE D CA  
7898  C C   . PHE C 183 ? 1.5563 2.0958 1.6697 -0.1379 -0.0171 0.0974  515 PHE D C   
7899  O O   . PHE C 183 ? 1.5372 2.0840 1.6516 -0.1321 -0.0125 0.0939  515 PHE D O   
7900  C CB  . PHE C 183 ? 1.3664 1.8811 1.4411 -0.1669 -0.0158 0.1003  515 PHE D CB  
7901  C CG  . PHE C 183 ? 1.3251 1.8170 1.3779 -0.1833 -0.0170 0.1020  515 PHE D CG  
7902  C CD1 . PHE C 183 ? 1.3517 1.8319 1.4023 -0.1883 -0.0211 0.1043  515 PHE D CD1 
7903  C CD2 . PHE C 183 ? 1.3250 1.8056 1.3587 -0.1936 -0.0137 0.1010  515 PHE D CD2 
7904  C CE1 . PHE C 183 ? 1.3757 1.8336 1.4049 -0.2036 -0.0216 0.1055  515 PHE D CE1 
7905  C CE2 . PHE C 183 ? 1.4379 1.8960 1.4507 -0.2083 -0.0142 0.1022  515 PHE D CE2 
7906  C CZ  . PHE C 183 ? 1.4731 1.9194 1.4832 -0.2134 -0.0179 0.1043  515 PHE D CZ  
7907  N N   . GLU C 184 ? 1.6673 2.2217 1.7987 -0.1321 -0.0212 0.1014  516 GLU D N   
7908  C CA  . GLU C 184 ? 1.8017 2.3847 1.9552 -0.1199 -0.0202 0.1030  516 GLU D CA  
7909  C C   . GLU C 184 ? 1.9138 2.5259 2.0756 -0.1308 -0.0231 0.1141  516 GLU D C   
7910  O O   . GLU C 184 ? 1.9429 2.5529 2.0992 -0.1440 -0.0281 0.1207  516 GLU D O   
7911  C CB  . GLU C 184 ? 1.8910 2.4724 2.0616 -0.1037 -0.0224 0.0997  516 GLU D CB  
7912  C CG  . GLU C 184 ? 1.9567 2.5464 2.1381 -0.1078 -0.0292 0.1070  516 GLU D CG  
7913  C CD  . GLU C 184 ? 1.9285 2.5126 2.1244 -0.0923 -0.0318 0.1032  516 GLU D CD  
7914  O OE1 . GLU C 184 ? 1.8729 2.4705 2.0849 -0.0770 -0.0293 0.1004  516 GLU D OE1 
7915  O OE2 . GLU C 184 ? 1.9278 2.4948 2.1193 -0.0956 -0.0363 0.1032  516 GLU D OE2 
7916  N N   . LEU C 185 ? 2.0301 2.6691 2.2040 -0.1258 -0.0199 0.1163  517 LEU D N   
7917  C CA  . LEU C 185 ? 2.0435 2.7137 2.2286 -0.1341 -0.0225 0.1275  517 LEU D CA  
7918  C C   . LEU C 185 ? 2.0341 2.7326 2.2429 -0.1188 -0.0193 0.1280  517 LEU D C   
7919  O O   . LEU C 185 ? 2.0112 2.7148 2.2190 -0.1125 -0.0134 0.1231  517 LEU D O   
7920  C CB  . LEU C 185 ? 2.0335 2.7076 2.2012 -0.1519 -0.0216 0.1323  517 LEU D CB  
7921  C CG  . LEU C 185 ? 2.0380 2.7481 2.2173 -0.1589 -0.0226 0.1433  517 LEU D CG  
7922  C CD1 . LEU C 185 ? 2.0088 2.7293 2.1951 -0.1689 -0.0297 0.1540  517 LEU D CD1 
7923  C CD2 . LEU C 185 ? 2.0077 2.7200 2.1690 -0.1732 -0.0203 0.1455  517 LEU D CD2 
7924  N N   . LEU C 186 ? 2.0516 2.7681 2.2814 -0.1131 -0.0232 0.1340  518 LEU D N   
7925  C CA  . LEU C 186 ? 2.0245 2.7701 2.2786 -0.0992 -0.0203 0.1359  518 LEU D CA  
7926  C C   . LEU C 186 ? 2.1466 2.9203 2.4190 -0.1047 -0.0256 0.1488  518 LEU D C   
7927  O O   . LEU C 186 ? 2.1295 2.9071 2.3930 -0.1226 -0.0300 0.1575  518 LEU D O   
7928  C CB  . LEU C 186 ? 1.8944 2.6289 2.1594 -0.0785 -0.0179 0.1263  518 LEU D CB  
7929  C CG  . LEU C 186 ? 1.8721 2.5967 2.1484 -0.0698 -0.0231 0.1255  518 LEU D CG  
7930  C CD1 . LEU C 186 ? 1.6283 2.3472 1.9151 -0.0487 -0.0190 0.1160  518 LEU D CD1 
7931  C CD2 . LEU C 186 ? 1.8689 2.5635 2.1270 -0.0799 -0.0280 0.1236  518 LEU D CD2 
7932  N N   . HIS C 187 ? 2.1754 2.9685 2.4731 -0.0897 -0.0252 0.1505  519 HIS D N   
7933  C CA  . HIS C 187 ? 2.2051 3.0281 2.5233 -0.0932 -0.0297 0.1633  519 HIS D CA  
7934  C C   . HIS C 187 ? 2.3863 3.1998 2.7050 -0.1015 -0.0383 0.1689  519 HIS D C   
7935  O O   . HIS C 187 ? 2.3318 3.1677 2.6631 -0.1094 -0.0432 0.1811  519 HIS D O   
7936  C CB  . HIS C 187 ? 2.0714 2.9166 2.4172 -0.0734 -0.0261 0.1630  519 HIS D CB  
7937  C CG  . HIS C 187 ? 2.0447 2.9094 2.3948 -0.0675 -0.0181 0.1614  519 HIS D CG  
7938  N ND1 . HIS C 187 ? 2.0551 2.9362 2.3973 -0.0816 -0.0169 0.1682  519 HIS D ND1 
7939  C CD2 . HIS C 187 ? 1.9685 2.8388 2.3293 -0.0493 -0.0109 0.1538  519 HIS D CD2 
7940  C CE1 . HIS C 187 ? 1.9168 2.8133 2.2651 -0.0724 -0.0093 0.1648  519 HIS D CE1 
7941  N NE2 . HIS C 187 ? 1.9110 2.8011 2.2704 -0.0528 -0.0053 0.1560  519 HIS D NE2 
7942  N N   . ALA C 188 ? 2.9701 3.7517 3.2758 -0.0999 -0.0402 0.1608  520 ALA D N   
7943  C CA  . ALA C 188 ? 2.9115 3.6833 3.2169 -0.1079 -0.0482 0.1656  520 ALA D CA  
7944  C C   . ALA C 188 ? 2.9844 3.7562 3.2730 -0.1317 -0.0524 0.1745  520 ALA D C   
7945  O O   . ALA C 188 ? 3.0265 3.7936 3.2969 -0.1413 -0.0488 0.1731  520 ALA D O   
7946  C CB  . ALA C 188 ? 2.7967 3.5340 3.0908 -0.1009 -0.0488 0.1545  520 ALA D CB  
7947  N N   . PRO C 189 ? 2.5055 3.2833 2.7999 -0.1420 -0.0601 0.1841  521 PRO D N   
7948  C CA  . PRO C 189 ? 2.2999 3.0800 2.5792 -0.1654 -0.0644 0.1938  521 PRO D CA  
7949  C C   . PRO C 189 ? 2.1950 2.9437 2.4423 -0.1783 -0.0627 0.1875  521 PRO D C   
7950  O O   . PRO C 189 ? 2.1672 2.8881 2.4027 -0.1797 -0.0648 0.1817  521 PRO D O   
7951  C CB  . PRO C 189 ? 2.2862 3.0692 2.5759 -0.1710 -0.0730 0.2018  521 PRO D CB  
7952  C CG  . PRO C 189 ? 2.3026 3.1027 2.6215 -0.1511 -0.0731 0.2016  521 PRO D CG  
7953  C CD  . PRO C 189 ? 2.4374 3.2249 2.7551 -0.1323 -0.0653 0.1878  521 PRO D CD  
7954  N N   . ALA C 190 ? 1.9573 2.7104 2.1906 -0.1883 -0.0592 0.1890  522 ALA D N   
7955  C CA  . ALA C 190 ? 1.8529 2.5763 2.0561 -0.1998 -0.0569 0.1828  522 ALA D CA  
7956  C C   . ALA C 190 ? 1.7544 2.4657 1.9416 -0.2206 -0.0631 0.1897  522 ALA D C   
7957  O O   . ALA C 190 ? 1.6083 2.3405 1.7987 -0.2343 -0.0675 0.2019  522 ALA D O   
7958  C CB  . ALA C 190 ? 1.7179 2.4510 1.9115 -0.2047 -0.0517 0.1830  522 ALA D CB  
7959  N N   . THR C 191 ? 1.7622 2.4394 1.9318 -0.2231 -0.0635 0.1821  523 THR D N   
7960  C CA  . THR C 191 ? 1.7226 2.3854 1.8758 -0.2423 -0.0689 0.1875  523 THR D CA  
7961  C C   . THR C 191 ? 1.6962 2.3208 1.8210 -0.2488 -0.0658 0.1784  523 THR D C   
7962  O O   . THR C 191 ? 1.6162 2.2209 1.7308 -0.2565 -0.0691 0.1781  523 THR D O   
7963  C CB  . THR C 191 ? 1.6649 2.3299 1.8333 -0.2393 -0.0754 0.1911  523 THR D CB  
7964  O OG1 . THR C 191 ? 1.6345 2.2826 1.8094 -0.2206 -0.0732 0.1799  523 THR D OG1 
7965  C CG2 . THR C 191 ? 1.7316 2.4344 1.9276 -0.2359 -0.0795 0.2023  523 THR D CG2 
7966  N N   . VAL C 192 ? 1.7585 2.3724 1.8706 -0.2458 -0.0593 0.1712  524 VAL D N   
7967  C CA  . VAL C 192 ? 1.7773 2.3560 1.8626 -0.2523 -0.0558 0.1632  524 VAL D CA  
7968  C C   . VAL C 192 ? 1.8854 2.4666 1.9541 -0.2641 -0.0524 0.1653  524 VAL D C   
7969  O O   . VAL C 192 ? 1.8697 2.4566 1.9414 -0.2545 -0.0474 0.1604  524 VAL D O   
7970  C CB  . VAL C 192 ? 1.7321 2.2905 1.8191 -0.2339 -0.0510 0.1505  524 VAL D CB  
7971  C CG1 . VAL C 192 ? 1.7243 2.2454 1.7847 -0.2416 -0.0482 0.1437  524 VAL D CG1 
7972  C CG2 . VAL C 192 ? 1.7349 2.2978 1.8431 -0.2192 -0.0543 0.1490  524 VAL D CG2 
7973  N N   . CYS C 193 ? 2.0989 2.6745 2.1489 -0.2852 -0.0552 0.1722  525 CYS D N   
7974  C CA  . CYS C 193 ? 2.0610 2.6439 2.0965 -0.2991 -0.0537 0.1770  525 CYS D CA  
7975  C C   . CYS C 193 ? 1.9700 2.5189 1.9737 -0.3140 -0.0516 0.1732  525 CYS D C   
7976  O O   . CYS C 193 ? 2.0178 2.5383 2.0113 -0.3130 -0.0508 0.1669  525 CYS D O   
7977  C CB  . CYS C 193 ? 2.0650 2.6780 2.1085 -0.3124 -0.0597 0.1912  525 CYS D CB  
7978  S SG  . CYS C 193 ? 2.2652 2.9207 2.3466 -0.2956 -0.0615 0.1969  525 CYS D SG  
7979  N N   . GLY C 194 ? 1.6458 2.1978 1.6336 -0.3279 -0.0507 0.1774  526 GLY D N   
7980  C CA  . GLY C 194 ? 1.5479 2.0682 1.5050 -0.3427 -0.0485 0.1744  526 GLY D CA  
7981  C C   . GLY C 194 ? 1.4516 1.9794 1.3917 -0.3613 -0.0494 0.1819  526 GLY D C   
7982  O O   . GLY C 194 ? 1.3515 1.8597 1.2674 -0.3796 -0.0506 0.1846  526 GLY D O   
7983  N N   . PRO D 2   ? 1.2327 0.9615 1.1118 -0.1306 -0.3873 0.2368  18  PRO A N   
7984  C CA  . PRO D 2   ? 1.3659 1.0993 1.2221 -0.1390 -0.3677 0.2365  18  PRO A CA  
7985  C C   . PRO D 2   ? 1.3636 1.1093 1.2346 -0.1342 -0.3480 0.2305  18  PRO A C   
7986  O O   . PRO D 2   ? 1.4337 1.1908 1.3354 -0.1241 -0.3466 0.2231  18  PRO A O   
7987  C CB  . PRO D 2   ? 1.2900 1.0047 1.1120 -0.1504 -0.3747 0.2495  18  PRO A CB  
7988  C CG  . PRO D 2   ? 1.1209 0.8225 0.9558 -0.1455 -0.3899 0.2562  18  PRO A CG  
7989  C CD  . PRO D 2   ? 1.1832 0.8926 1.0531 -0.1329 -0.4013 0.2481  18  PRO A CD  
7990  N N   . SER D 3   ? 1.5496 1.2950 1.4006 -0.1411 -0.3331 0.2325  19  SER A N   
7991  C CA  . SER D 3   ? 1.5707 1.3298 1.4349 -0.1363 -0.3135 0.2255  19  SER A CA  
7992  C C   . SER D 3   ? 1.6282 1.3805 1.4855 -0.1386 -0.3089 0.2308  19  SER A C   
7993  O O   . SER D 3   ? 1.6779 1.4200 1.5069 -0.1491 -0.3080 0.2378  19  SER A O   
7994  C CB  . SER D 3   ? 1.5948 1.3640 1.4460 -0.1408 -0.2969 0.2194  19  SER A CB  
7995  O OG  . SER D 3   ? 1.7474 1.5073 1.5648 -0.1528 -0.2966 0.2253  19  SER A OG  
7996  N N   . THR D 4   ? 1.3708 1.1304 1.2543 -0.1292 -0.3053 0.2268  20  THR A N   
7997  C CA  . THR D 4   ? 1.3147 1.0681 1.1955 -0.1304 -0.3022 0.2311  20  THR A CA  
7998  C C   . THR D 4   ? 1.3436 1.1057 1.2115 -0.1343 -0.2809 0.2274  20  THR A C   
7999  O O   . THR D 4   ? 1.3420 1.1171 1.2113 -0.1326 -0.2681 0.2199  20  THR A O   
8000  C CB  . THR D 4   ? 1.1890 0.9481 1.1036 -0.1186 -0.3070 0.2270  20  THR A CB  
8001  O OG1 . THR D 4   ? 1.1862 0.9648 1.1189 -0.1112 -0.2897 0.2173  20  THR A OG1 
8002  C CG2 . THR D 4   ? 1.2176 0.9770 1.1519 -0.1120 -0.3234 0.2250  20  THR A CG2 
8003  N N   . ILE D 5   ? 1.2700 1.0241 1.1250 -0.1399 -0.2778 0.2326  21  ILE A N   
8004  C CA  . ILE D 5   ? 1.2079 0.9713 1.0530 -0.1427 -0.2580 0.2279  21  ILE A CA  
8005  C C   . ILE D 5   ? 1.1371 0.9188 1.0097 -0.1307 -0.2455 0.2176  21  ILE A C   
8006  O O   . ILE D 5   ? 1.1679 0.9616 1.0375 -0.1298 -0.2305 0.2107  21  ILE A O   
8007  C CB  . ILE D 5   ? 1.2766 1.0291 1.1060 -0.1507 -0.2570 0.2346  21  ILE A CB  
8008  C CG1 . ILE D 5   ? 1.3802 1.1179 1.1751 -0.1655 -0.2640 0.2442  21  ILE A CG1 
8009  C CG2 . ILE D 5   ? 1.2476 1.0129 1.0759 -0.1501 -0.2369 0.2273  21  ILE A CG2 
8010  C CD1 . ILE D 5   ? 1.3157 1.0620 1.0870 -0.1738 -0.2486 0.2396  21  ILE A CD1 
8011  N N   . GLU D 6   ? 1.1075 0.8922 1.0075 -0.1211 -0.2522 0.2160  22  GLU A N   
8012  C CA  . GLU D 6   ? 1.1239 0.9275 1.0503 -0.1097 -0.2409 0.2065  22  GLU A CA  
8013  C C   . GLU D 6   ? 1.0589 0.8748 0.9940 -0.1056 -0.2362 0.2004  22  GLU A C   
8014  O O   . GLU D 6   ? 1.0493 0.8802 0.9937 -0.1003 -0.2217 0.1935  22  GLU A O   
8015  C CB  . GLU D 6   ? 1.1589 0.9646 1.1140 -0.1005 -0.2508 0.2051  22  GLU A CB  
8016  C CG  . GLU D 6   ? 1.1281 0.9559 1.1121 -0.0887 -0.2403 0.1949  22  GLU A CG  
8017  C CD  . GLU D 6   ? 1.1733 1.0061 1.1862 -0.0796 -0.2482 0.1916  22  GLU A CD  
8018  O OE1 . GLU D 6   ? 1.2181 1.0418 1.2284 -0.0814 -0.2513 0.1948  22  GLU A OE1 
8019  O OE2 . GLU D 6   ? 1.1298 0.9767 1.1689 -0.0708 -0.2511 0.1850  22  GLU A OE2 
8020  N N   . GLU D 7   ? 1.0392 0.8486 0.9707 -0.1082 -0.2481 0.2030  23  GLU A N   
8021  C CA  . GLU D 7   ? 1.0027 0.8234 0.9431 -0.1051 -0.2435 0.1971  23  GLU A CA  
8022  C C   . GLU D 7   ? 0.9989 0.8212 0.9175 -0.1114 -0.2300 0.1952  23  GLU A C   
8023  O O   . GLU D 7   ? 1.0038 0.8388 0.9312 -0.1072 -0.2177 0.1887  23  GLU A O   
8024  C CB  . GLU D 7   ? 1.0770 0.8915 1.0217 -0.1057 -0.2604 0.1992  23  GLU A CB  
8025  C CG  . GLU D 7   ? 1.0874 0.9008 1.0556 -0.0987 -0.2751 0.1995  23  GLU A CG  
8026  C CD  . GLU D 7   ? 1.2188 1.0245 1.1884 -0.0998 -0.2932 0.2017  23  GLU A CD  
8027  O OE1 . GLU D 7   ? 1.3234 1.1149 1.2676 -0.1086 -0.3005 0.2085  23  GLU A OE1 
8028  O OE2 . GLU D 7   ? 1.1794 0.9945 1.1756 -0.0921 -0.3000 0.1962  23  GLU A OE2 
8029  N N   . GLN D 8   ? 1.0309 0.8409 0.9213 -0.1217 -0.2326 0.2005  24  GLN A N   
8030  C CA  . GLN D 8   ? 1.1060 0.9189 0.9763 -0.1278 -0.2197 0.1972  24  GLN A CA  
8031  C C   . GLN D 8   ? 1.0856 0.9096 0.9621 -0.1230 -0.2028 0.1915  24  GLN A C   
8032  O O   . GLN D 8   ? 1.0536 0.8866 0.9305 -0.1211 -0.1911 0.1852  24  GLN A O   
8033  C CB  . GLN D 8   ? 1.1246 0.9249 0.9634 -0.1401 -0.2238 0.2034  24  GLN A CB  
8034  C CG  . GLN D 8   ? 1.2098 0.9984 1.0384 -0.1457 -0.2411 0.2098  24  GLN A CG  
8035  C CD  . GLN D 8   ? 1.2792 1.0545 1.0780 -0.1578 -0.2466 0.2182  24  GLN A CD  
8036  O OE1 . GLN D 8   ? 1.2413 1.0188 1.0206 -0.1650 -0.2353 0.2166  24  GLN A OE1 
8037  N NE2 . GLN D 8   ? 1.3700 1.1318 1.1650 -0.1605 -0.2644 0.2271  24  GLN A NE2 
8038  N N   . ALA D 9   ? 1.1490 0.9723 1.0316 -0.1204 -0.2021 0.1935  25  ALA A N   
8039  C CA  . ALA D 9   ? 1.0316 0.8655 0.9202 -0.1156 -0.1870 0.1881  25  ALA A CA  
8040  C C   . ALA D 9   ? 0.9444 0.7936 0.8577 -0.1047 -0.1798 0.1816  25  ALA A C   
8041  O O   . ALA D 9   ? 0.9667 0.8252 0.8794 -0.1020 -0.1661 0.1760  25  ALA A O   
8042  C CB  . ALA D 9   ? 1.0366 0.8660 0.9293 -0.1151 -0.1904 0.1917  25  ALA A CB  
8043  N N   . LYS D 10  ? 0.8754 0.7276 0.8106 -0.0986 -0.1892 0.1821  26  LYS A N   
8044  C CA  . LYS D 10  ? 0.8602 0.7281 0.8184 -0.0897 -0.1826 0.1763  26  LYS A CA  
8045  C C   . LYS D 10  ? 0.9084 0.7792 0.8601 -0.0916 -0.1756 0.1734  26  LYS A C   
8046  O O   . LYS D 10  ? 0.9007 0.7825 0.8599 -0.0868 -0.1636 0.1688  26  LYS A O   
8047  C CB  . LYS D 10  ? 0.8420 0.7136 0.8241 -0.0842 -0.1947 0.1764  26  LYS A CB  
8048  C CG  . LYS D 10  ? 0.9140 0.7889 0.9128 -0.0784 -0.1994 0.1761  26  LYS A CG  
8049  C CD  . LYS D 10  ? 1.0059 0.8862 1.0296 -0.0728 -0.2117 0.1743  26  LYS A CD  
8050  C CE  . LYS D 10  ? 1.0989 0.9818 1.1403 -0.0669 -0.2181 0.1731  26  LYS A CE  
8051  N NZ  . LYS D 10  ? 1.0741 0.9605 1.1388 -0.0621 -0.2328 0.1708  26  LYS A NZ  
8052  N N   . THR D 11  ? 0.9091 0.7700 0.8475 -0.0986 -0.1837 0.1758  27  THR A N   
8053  C CA  . THR D 11  ? 0.8829 0.7460 0.8156 -0.1008 -0.1776 0.1723  27  THR A CA  
8054  C C   . THR D 11  ? 0.9007 0.7641 0.8159 -0.1036 -0.1646 0.1691  27  THR A C   
8055  O O   . THR D 11  ? 0.8840 0.7540 0.8029 -0.1008 -0.1547 0.1644  27  THR A O   
8056  C CB  . THR D 11  ? 0.9562 0.8099 0.8792 -0.1075 -0.1895 0.1746  27  THR A CB  
8057  O OG1 . THR D 11  ? 0.9872 0.8407 0.9273 -0.1041 -0.2026 0.1770  27  THR A OG1 
8058  C CG2 . THR D 11  ? 0.9078 0.7649 0.8310 -0.1086 -0.1844 0.1700  27  THR A CG2 
8059  N N   . PHE D 12  ? 0.9414 0.7976 0.8372 -0.1096 -0.1647 0.1713  28  PHE A N   
8060  C CA  . PHE D 12  ? 0.9127 0.7714 0.7934 -0.1120 -0.1521 0.1668  28  PHE A CA  
8061  C C   . PHE D 12  ? 0.8999 0.7704 0.7958 -0.1027 -0.1400 0.1621  28  PHE A C   
8062  O O   . PHE D 12  ? 0.8795 0.7547 0.7727 -0.1011 -0.1301 0.1567  28  PHE A O   
8063  C CB  . PHE D 12  ? 0.9409 0.7927 0.8030 -0.1191 -0.1533 0.1700  28  PHE A CB  
8064  C CG  . PHE D 12  ? 0.9348 0.7920 0.7860 -0.1200 -0.1397 0.1641  28  PHE A CG  
8065  C CD1 . PHE D 12  ? 0.9771 0.8357 0.8141 -0.1243 -0.1335 0.1583  28  PHE A CD1 
8066  C CD2 . PHE D 12  ? 0.9397 0.8012 0.7952 -0.1167 -0.1337 0.1635  28  PHE A CD2 
8067  C CE1 . PHE D 12  ? 0.9979 0.8624 0.8257 -0.1249 -0.1217 0.1515  28  PHE A CE1 
8068  C CE2 . PHE D 12  ? 0.9614 0.8287 0.8071 -0.1175 -0.1215 0.1571  28  PHE A CE2 
8069  C CZ  . PHE D 12  ? 1.0196 0.8885 0.8514 -0.1215 -0.1155 0.1510  28  PHE A CZ  
8070  N N   . LEU D 13  ? 0.9081 0.7836 0.8204 -0.0964 -0.1413 0.1640  29  LEU A N   
8071  C CA  . LEU D 13  ? 0.8652 0.7535 0.7923 -0.0873 -0.1304 0.1598  29  LEU A CA  
8072  C C   . LEU D 13  ? 0.8573 0.7530 0.7984 -0.0822 -0.1270 0.1577  29  LEU A C   
8073  O O   . LEU D 13  ? 0.8447 0.7487 0.7903 -0.0769 -0.1163 0.1539  29  LEU A O   
8074  C CB  . LEU D 13  ? 0.8747 0.7683 0.8183 -0.0817 -0.1336 0.1614  29  LEU A CB  
8075  C CG  . LEU D 13  ? 0.8652 0.7513 0.7949 -0.0869 -0.1351 0.1633  29  LEU A CG  
8076  C CD1 . LEU D 13  ? 0.9144 0.8036 0.8622 -0.0818 -0.1412 0.1650  29  LEU A CD1 
8077  C CD2 . LEU D 13  ? 0.8544 0.7445 0.7718 -0.0875 -0.1221 0.1583  29  LEU A CD2 
8078  N N   . ASP D 14  ? 0.8868 0.7793 0.8348 -0.0841 -0.1364 0.1602  30  ASP A N   
8079  C CA  . ASP D 14  ? 0.9019 0.8013 0.8641 -0.0804 -0.1333 0.1585  30  ASP A CA  
8080  C C   . ASP D 14  ? 0.8863 0.7820 0.8362 -0.0833 -0.1263 0.1553  30  ASP A C   
8081  O O   . ASP D 14  ? 0.7925 0.6948 0.7502 -0.0786 -0.1177 0.1531  30  ASP A O   
8082  C CB  . ASP D 14  ? 0.8830 0.7808 0.8565 -0.0820 -0.1453 0.1610  30  ASP A CB  
8083  C CG  . ASP D 14  ? 0.9341 0.8449 0.9313 -0.0758 -0.1428 0.1598  30  ASP A CG  
8084  O OD1 . ASP D 14  ? 0.8800 0.7991 0.8816 -0.0715 -0.1314 0.1579  30  ASP A OD1 
8085  O OD2 . ASP D 14  ? 0.9938 0.9067 1.0045 -0.0757 -0.1524 0.1606  30  ASP A OD2 
8086  N N   . LYS D 15  ? 0.8960 0.7815 0.8271 -0.0911 -0.1305 0.1549  31  LYS A N   
8087  C CA  . LYS D 15  ? 0.8805 0.7630 0.7991 -0.0938 -0.1238 0.1500  31  LYS A CA  
8088  C C   . LYS D 15  ? 0.9094 0.7970 0.8232 -0.0896 -0.1120 0.1459  31  LYS A C   
8089  O O   . LYS D 15  ? 0.9346 0.8246 0.8503 -0.0863 -0.1043 0.1419  31  LYS A O   
8090  C CB  . LYS D 15  ? 0.8553 0.7282 0.7538 -0.1034 -0.1306 0.1495  31  LYS A CB  
8091  C CG  . LYS D 15  ? 0.9011 0.7723 0.7836 -0.1069 -0.1237 0.1427  31  LYS A CG  
8092  C CD  . LYS D 15  ? 0.9889 0.8603 0.8797 -0.1052 -0.1216 0.1389  31  LYS A CD  
8093  C CE  . LYS D 15  ? 1.1745 1.0444 1.0509 -0.1082 -0.1158 0.1309  31  LYS A CE  
8094  N NZ  . LYS D 15  ? 1.2111 1.0804 1.0983 -0.1052 -0.1132 0.1271  31  LYS A NZ  
8095  N N   . PHE D 16  ? 0.9152 0.8042 0.8233 -0.0896 -0.1108 0.1468  32  PHE A N   
8096  C CA  . PHE D 16  ? 0.8767 0.7714 0.7802 -0.0857 -0.0999 0.1420  32  PHE A CA  
8097  C C   . PHE D 16  ? 0.8704 0.7749 0.7912 -0.0759 -0.0926 0.1411  32  PHE A C   
8098  O O   . PHE D 16  ? 0.8817 0.7890 0.8000 -0.0724 -0.0843 0.1363  32  PHE A O   
8099  C CB  . PHE D 16  ? 0.8581 0.7533 0.7557 -0.0874 -0.1003 0.1434  32  PHE A CB  
8100  C CG  . PHE D 16  ? 0.8203 0.7241 0.7186 -0.0816 -0.0891 0.1382  32  PHE A CG  
8101  C CD1 . PHE D 16  ? 0.8721 0.7759 0.7545 -0.0847 -0.0820 0.1316  32  PHE A CD1 
8102  C CD2 . PHE D 16  ? 0.8039 0.7172 0.7190 -0.0730 -0.0858 0.1389  32  PHE A CD2 
8103  C CE1 . PHE D 16  ? 0.8360 0.7486 0.7196 -0.0789 -0.0719 0.1257  32  PHE A CE1 
8104  C CE2 . PHE D 16  ? 0.8001 0.7223 0.7159 -0.0672 -0.0757 0.1335  32  PHE A CE2 
8105  C CZ  . PHE D 16  ? 0.7957 0.7171 0.6958 -0.0701 -0.0690 0.1270  32  PHE A CZ  
8106  N N   . ASN D 17  ? 0.8005 0.7112 0.7389 -0.0712 -0.0957 0.1453  33  ASN A N   
8107  C CA  . ASN D 17  ? 0.8081 0.7301 0.7624 -0.0625 -0.0887 0.1448  33  ASN A CA  
8108  C C   . ASN D 17  ? 0.8399 0.7602 0.7944 -0.0615 -0.0842 0.1434  33  ASN A C   
8109  O O   . ASN D 17  ? 0.8842 0.8094 0.8396 -0.0558 -0.0757 0.1408  33  ASN A O   
8110  C CB  . ASN D 17  ? 0.8007 0.7303 0.7746 -0.0593 -0.0942 0.1488  33  ASN A CB  
8111  C CG  . ASN D 17  ? 0.8020 0.7352 0.7798 -0.0578 -0.0975 0.1493  33  ASN A CG  
8112  O OD1 . ASN D 17  ? 0.7811 0.7155 0.7512 -0.0565 -0.0923 0.1466  33  ASN A OD1 
8113  N ND2 . ASN D 17  ? 0.8560 0.7900 0.8462 -0.0583 -0.1071 0.1522  33  ASN A ND2 
8114  N N   . HIS D 18  ? 0.8804 0.7929 0.8338 -0.0669 -0.0901 0.1448  34  HIS A N   
8115  C CA  . HIS D 18  ? 0.8748 0.7855 0.8320 -0.0658 -0.0865 0.1440  34  HIS A CA  
8116  C C   . HIS D 18  ? 0.9261 0.8305 0.8685 -0.0667 -0.0816 0.1379  34  HIS A C   
8117  O O   . HIS D 18  ? 0.9444 0.8503 0.8893 -0.0616 -0.0748 0.1361  34  HIS A O   
8118  C CB  . HIS D 18  ? 0.8878 0.7935 0.8512 -0.0711 -0.0946 0.1466  34  HIS A CB  
8119  C CG  . HIS D 18  ? 0.9251 0.8389 0.9054 -0.0694 -0.0991 0.1510  34  HIS A CG  
8120  N ND1 . HIS D 18  ? 0.9288 0.8439 0.9099 -0.0705 -0.1061 0.1525  34  HIS A ND1 
8121  C CD2 . HIS D 18  ? 0.8946 0.8165 0.8923 -0.0668 -0.0980 0.1538  34  HIS A CD2 
8122  C CE1 . HIS D 18  ? 0.8946 0.8187 0.8940 -0.0679 -0.1094 0.1549  34  HIS A CE1 
8123  N NE2 . HIS D 18  ? 0.8893 0.8186 0.8989 -0.0661 -0.1042 0.1556  34  HIS A NE2 
8124  N N   . GLU D 19  ? 1.0924 0.9902 1.0191 -0.0733 -0.0852 0.1346  35  GLU A N   
8125  C CA  . GLU D 19  ? 1.0956 0.9904 1.0081 -0.0743 -0.0801 0.1269  35  GLU A CA  
8126  C C   . GLU D 19  ? 1.0188 0.9212 0.9323 -0.0666 -0.0710 0.1238  35  GLU A C   
8127  O O   . GLU D 19  ? 1.0141 0.9162 0.9260 -0.0626 -0.0655 0.1185  35  GLU A O   
8128  C CB  . GLU D 19  ? 1.1044 0.9948 0.9991 -0.0829 -0.0843 0.1241  35  GLU A CB  
8129  C CG  . GLU D 19  ? 1.1861 1.0689 1.0728 -0.0905 -0.0905 0.1216  35  GLU A CG  
8130  C CD  . GLU D 19  ? 1.3754 1.2554 1.2652 -0.0883 -0.0873 0.1156  35  GLU A CD  
8131  O OE1 . GLU D 19  ? 1.2978 1.1808 1.1914 -0.0814 -0.0797 0.1119  35  GLU A OE1 
8132  O OE2 . GLU D 19  ? 1.4649 1.3393 1.3541 -0.0934 -0.0931 0.1145  35  GLU A OE2 
8133  N N   . ALA D 20  ? 0.9109 0.8202 0.8281 -0.0640 -0.0699 0.1267  36  ALA A N   
8134  C CA  . ALA D 20  ? 0.9041 0.8214 0.8206 -0.0574 -0.0617 0.1226  36  ALA A CA  
8135  C C   . ALA D 20  ? 0.9024 0.8261 0.8324 -0.0482 -0.0565 0.1244  36  ALA A C   
8136  O O   . ALA D 20  ? 0.9114 0.8382 0.8388 -0.0426 -0.0499 0.1192  36  ALA A O   
8137  C CB  . ALA D 20  ? 0.9121 0.8347 0.8287 -0.0579 -0.0624 0.1244  36  ALA A CB  
8138  N N   . GLU D 21  ? 0.8187 0.7455 0.7631 -0.0464 -0.0593 0.1314  37  GLU A N   
8139  C CA  . GLU D 21  ? 0.7585 0.6917 0.7141 -0.0389 -0.0542 0.1339  37  GLU A CA  
8140  C C   . GLU D 21  ? 0.7759 0.7006 0.7269 -0.0383 -0.0522 0.1313  37  GLU A C   
8141  O O   . GLU D 21  ? 0.7831 0.7109 0.7355 -0.0312 -0.0465 0.1301  37  GLU A O   
8142  C CB  . GLU D 21  ? 0.7782 0.7166 0.7495 -0.0389 -0.0574 0.1412  37  GLU A CB  
8143  C CG  . GLU D 21  ? 0.8745 0.8226 0.8544 -0.0381 -0.0601 0.1431  37  GLU A CG  
8144  C CD  . GLU D 21  ? 1.0364 0.9976 1.0342 -0.0336 -0.0585 0.1478  37  GLU A CD  
8145  O OE1 . GLU D 21  ? 0.9539 0.9209 0.9550 -0.0282 -0.0520 0.1490  37  GLU A OE1 
8146  O OE2 . GLU D 21  ? 1.0371 1.0032 1.0455 -0.0357 -0.0643 0.1499  37  GLU A OE2 
8147  N N   . ASP D 22  ? 0.8313 0.7450 0.7766 -0.0452 -0.0573 0.1299  38  ASP A N   
8148  C CA  . ASP D 22  ? 0.8307 0.7363 0.7737 -0.0437 -0.0557 0.1266  38  ASP A CA  
8149  C C   . ASP D 22  ? 0.8104 0.7157 0.7415 -0.0408 -0.0513 0.1169  38  ASP A C   
8150  O O   . ASP D 22  ? 0.7954 0.7000 0.7278 -0.0342 -0.0473 0.1142  38  ASP A O   
8151  C CB  . ASP D 22  ? 0.8475 0.7423 0.7901 -0.0512 -0.0621 0.1267  38  ASP A CB  
8152  C CG  . ASP D 22  ? 0.8904 0.7768 0.8364 -0.0490 -0.0612 0.1254  38  ASP A CG  
8153  O OD1 . ASP D 22  ? 0.8465 0.7346 0.8032 -0.0449 -0.0589 0.1323  38  ASP A OD1 
8154  O OD2 . ASP D 22  ? 0.9438 0.8227 0.8818 -0.0513 -0.0626 0.1174  38  ASP A OD2 
8155  N N   . LEU D 23  ? 0.8395 0.7462 0.7593 -0.0456 -0.0520 0.1115  39  LEU A N   
8156  C CA  . LEU D 23  ? 0.8219 0.7309 0.7311 -0.0434 -0.0471 0.1012  39  LEU A CA  
8157  C C   . LEU D 23  ? 0.8654 0.7842 0.7791 -0.0338 -0.0403 0.1004  39  LEU A C   
8158  O O   . LEU D 23  ? 0.8823 0.8026 0.7927 -0.0283 -0.0360 0.0924  39  LEU A O   
8159  C CB  . LEU D 23  ? 0.7853 0.6955 0.6813 -0.0514 -0.0486 0.0970  39  LEU A CB  
8160  C CG  . LEU D 23  ? 0.8562 0.7576 0.7453 -0.0586 -0.0535 0.0929  39  LEU A CG  
8161  C CD1 . LEU D 23  ? 0.9680 0.8697 0.8427 -0.0684 -0.0563 0.0904  39  LEU A CD1 
8162  C CD2 . LEU D 23  ? 0.8912 0.7915 0.7787 -0.0539 -0.0498 0.0829  39  LEU A CD2 
8163  N N   . PHE D 24  ? 0.8096 0.7360 0.7316 -0.0313 -0.0396 0.1075  40  PHE A N   
8164  C CA  . PHE D 24  ? 0.7574 0.6950 0.6831 -0.0228 -0.0333 0.1057  40  PHE A CA  
8165  C C   . PHE D 24  ? 0.7636 0.7022 0.6978 -0.0142 -0.0307 0.1090  40  PHE A C   
8166  O O   . PHE D 24  ? 0.7736 0.7175 0.7067 -0.0064 -0.0257 0.1040  40  PHE A O   
8167  C CB  . PHE D 24  ? 0.7453 0.6917 0.6771 -0.0234 -0.0338 0.1107  40  PHE A CB  
8168  C CG  . PHE D 24  ? 0.7915 0.7508 0.7280 -0.0148 -0.0275 0.1081  40  PHE A CG  
8169  C CD1 . PHE D 24  ? 0.7575 0.7216 0.6859 -0.0143 -0.0233 0.0995  40  PHE A CD1 
8170  C CD2 . PHE D 24  ? 0.7420 0.7101 0.6911 -0.0074 -0.0254 0.1136  40  PHE A CD2 
8171  C CE1 . PHE D 24  ? 0.6434 0.6200 0.5769 -0.0062 -0.0176 0.0961  40  PHE A CE1 
8172  C CE2 . PHE D 24  ? 0.6911 0.6724 0.6444 0.0007  -0.0198 0.1105  40  PHE A CE2 
8173  C CZ  . PHE D 24  ? 0.6650 0.6502 0.6108 0.0017  -0.0160 0.1015  40  PHE A CZ  
8174  N N   . TYR D 25  ? 0.7191 0.6524 0.6611 -0.0161 -0.0343 0.1172  41  TYR A N   
8175  C CA  . TYR D 25  ? 0.6844 0.6157 0.6321 -0.0097 -0.0324 0.1210  41  TYR A CA  
8176  C C   . TYR D 25  ? 0.7404 0.6619 0.6810 -0.0074 -0.0323 0.1132  41  TYR A C   
8177  O O   . TYR D 25  ? 0.7789 0.7017 0.7203 0.0009  -0.0293 0.1118  41  TYR A O   
8178  C CB  . TYR D 25  ? 0.7066 0.6328 0.6632 -0.0143 -0.0364 0.1304  41  TYR A CB  
8179  C CG  . TYR D 25  ? 0.7015 0.6287 0.6650 -0.0085 -0.0339 0.1371  41  TYR A CG  
8180  C CD1 . TYR D 25  ? 0.7294 0.6706 0.7008 -0.0042 -0.0303 0.1431  41  TYR A CD1 
8181  C CD2 . TYR D 25  ? 0.7063 0.6210 0.6683 -0.0072 -0.0352 0.1372  41  TYR A CD2 
8182  C CE1 . TYR D 25  ? 0.7246 0.6680 0.7009 0.0004  -0.0279 0.1501  41  TYR A CE1 
8183  C CE2 . TYR D 25  ? 0.7230 0.6375 0.6901 -0.0024 -0.0333 0.1447  41  TYR A CE2 
8184  C CZ  . TYR D 25  ? 0.6955 0.6247 0.6690 0.0011  -0.0294 0.1516  41  TYR A CZ  
8185  O OH  . TYR D 25  ? 0.6886 0.6188 0.6657 0.0052  -0.0274 0.1599  41  TYR A OH  
8186  N N   . GLN D 26  ? 0.7535 0.6653 0.6876 -0.0144 -0.0364 0.1078  42  GLN A N   
8187  C CA  . GLN D 26  ? 0.7932 0.6985 0.7202 -0.0126 -0.0363 0.0968  42  GLN A CA  
8188  C C   . GLN D 26  ? 0.7832 0.6980 0.7064 -0.0043 -0.0306 0.0888  42  GLN A C   
8189  O O   . GLN D 26  ? 0.7650 0.6781 0.6908 0.0042  -0.0293 0.0869  42  GLN A O   
8190  C CB  . GLN D 26  ? 0.9240 0.8257 0.8413 -0.0217 -0.0393 0.0888  42  GLN A CB  
8191  C CG  . GLN D 26  ? 0.8785 0.7707 0.7971 -0.0307 -0.0458 0.0928  42  GLN A CG  
8192  C CD  . GLN D 26  ? 0.8635 0.7441 0.7888 -0.0293 -0.0491 0.0937  42  GLN A CD  
8193  O OE1 . GLN D 26  ? 0.9699 0.8477 0.8976 -0.0216 -0.0472 0.0907  42  GLN A OE1 
8194  N NE2 . GLN D 26  ? 0.9423 0.8155 0.8713 -0.0364 -0.0544 0.0981  42  GLN A NE2 
8195  N N   . SER D 27  ? 0.8292 0.7535 0.7463 -0.0071 -0.0278 0.0843  43  SER A N   
8196  C CA  . SER D 27  ? 0.8462 0.7808 0.7594 -0.0007 -0.0221 0.0749  43  SER A CA  
8197  C C   . SER D 27  ? 0.7587 0.7000 0.6798 0.0104  -0.0187 0.0791  43  SER A C   
8198  O O   . SER D 27  ? 0.7384 0.6802 0.6589 0.0186  -0.0169 0.0723  43  SER A O   
8199  C CB  . SER D 27  ? 0.8830 0.8267 0.7905 -0.0062 -0.0196 0.0724  43  SER A CB  
8200  O OG  . SER D 27  ? 0.8959 0.8486 0.7983 -0.0021 -0.0141 0.0607  43  SER A OG  
8201  N N   . SER D 28  ? 0.7348 0.6819 0.6636 0.0110  -0.0182 0.0900  44  SER A N   
8202  C CA  . SER D 28  ? 0.7337 0.6910 0.6691 0.0211  -0.0143 0.0935  44  SER A CA  
8203  C C   . SER D 28  ? 0.7181 0.6675 0.6560 0.0277  -0.0157 0.0968  44  SER A C   
8204  O O   . SER D 28  ? 0.7677 0.7230 0.7060 0.0374  -0.0128 0.0939  44  SER A O   
8205  C CB  . SER D 28  ? 0.6859 0.6525 0.6300 0.0197  -0.0139 0.1036  44  SER A CB  
8206  O OG  . SER D 28  ? 0.6696 0.6408 0.6122 0.0134  -0.0142 0.1014  44  SER A OG  
8207  N N   . LEU D 29  ? 0.6931 0.6289 0.6327 0.0228  -0.0205 0.1028  45  LEU A N   
8208  C CA  . LEU D 29  ? 0.7211 0.6470 0.6626 0.0286  -0.0226 0.1057  45  LEU A CA  
8209  C C   . LEU D 29  ? 0.7453 0.6662 0.6811 0.0342  -0.0232 0.0925  45  LEU A C   
8210  O O   . LEU D 29  ? 0.7739 0.6933 0.7106 0.0436  -0.0232 0.0918  45  LEU A O   
8211  C CB  . LEU D 29  ? 0.7206 0.6325 0.6663 0.0213  -0.0277 0.1146  45  LEU A CB  
8212  C CG  . LEU D 29  ? 0.6854 0.5872 0.6356 0.0252  -0.0300 0.1235  45  LEU A CG  
8213  C CD1 . LEU D 29  ? 0.7375 0.6506 0.6899 0.0334  -0.0260 0.1303  45  LEU A CD1 
8214  C CD2 . LEU D 29  ? 0.6815 0.5769 0.6379 0.0159  -0.0330 0.1342  45  LEU A CD2 
8215  N N   . ALA D 30  ? 0.7562 0.6750 0.6859 0.0285  -0.0240 0.0812  46  ALA A N   
8216  C CA  . ALA D 30  ? 0.7717 0.6896 0.6970 0.0340  -0.0239 0.0663  46  ALA A CA  
8217  C C   . ALA D 30  ? 0.8137 0.7458 0.7382 0.0438  -0.0186 0.0604  46  ALA A C   
8218  O O   . ALA D 30  ? 0.7918 0.7227 0.7170 0.0534  -0.0193 0.0536  46  ALA A O   
8219  C CB  . ALA D 30  ? 0.8479 0.7658 0.7660 0.0250  -0.0244 0.0550  46  ALA A CB  
8220  N N   . SER D 31  ? 0.8211 0.7667 0.7451 0.0417  -0.0138 0.0626  47  SER A N   
8221  C CA  . SER D 31  ? 0.7542 0.7151 0.6784 0.0499  -0.0084 0.0566  47  SER A CA  
8222  C C   . SER D 31  ? 0.7508 0.7137 0.6805 0.0606  -0.0083 0.0644  47  SER A C   
8223  O O   . SER D 31  ? 0.8242 0.7927 0.7537 0.0707  -0.0069 0.0569  47  SER A O   
8224  C CB  . SER D 31  ? 0.7215 0.6944 0.6458 0.0442  -0.0044 0.0589  47  SER A CB  
8225  O OG  . SER D 31  ? 0.7605 0.7487 0.6866 0.0522  0.0009  0.0534  47  SER A OG  
8226  N N   . TRP D 32  ? 0.6980 0.6577 0.6327 0.0583  -0.0100 0.0794  48  TRP A N   
8227  C CA  . TRP D 32  ? 0.7127 0.6738 0.6513 0.0668  -0.0102 0.0886  48  TRP A CA  
8228  C C   . TRP D 32  ? 0.7828 0.7300 0.7197 0.0735  -0.0148 0.0861  48  TRP A C   
8229  O O   . TRP D 32  ? 0.8749 0.8254 0.8122 0.0839  -0.0147 0.0873  48  TRP A O   
8230  C CB  . TRP D 32  ? 0.7066 0.6650 0.6505 0.0608  -0.0116 0.1044  48  TRP A CB  
8231  C CG  . TRP D 32  ? 0.6694 0.6281 0.6159 0.0673  -0.0120 0.1151  48  TRP A CG  
8232  C CD1 . TRP D 32  ? 0.6923 0.6349 0.6383 0.0687  -0.0168 0.1216  48  TRP A CD1 
8233  C CD2 . TRP D 32  ? 0.6737 0.6492 0.6239 0.0721  -0.0079 0.1221  48  TRP A CD2 
8234  N NE1 . TRP D 32  ? 0.7006 0.6484 0.6481 0.0739  -0.0158 0.1328  48  TRP A NE1 
8235  C CE2 . TRP D 32  ? 0.6690 0.6381 0.6191 0.0760  -0.0101 0.1331  48  TRP A CE2 
8236  C CE3 . TRP D 32  ? 0.6446 0.6405 0.5987 0.0734  -0.0027 0.1198  48  TRP A CE3 
8237  C CZ2 . TRP D 32  ? 0.6566 0.6402 0.6090 0.0807  -0.0070 0.1417  48  TRP A CZ2 
8238  C CZ3 . TRP D 32  ? 0.6132 0.6237 0.5711 0.0788  0.0002  0.1272  48  TRP A CZ3 
8239  C CH2 . TRP D 32  ? 0.6255 0.6306 0.5820 0.0822  -0.0017 0.1381  48  TRP A CH2 
8240  N N   . ASN D 33  ? 0.7498 0.6811 0.6854 0.0679  -0.0197 0.0831  49  ASN A N   
8241  C CA  . ASN D 33  ? 0.7763 0.6934 0.7121 0.0748  -0.0252 0.0804  49  ASN A CA  
8242  C C   . ASN D 33  ? 0.8472 0.7706 0.7803 0.0842  -0.0243 0.0635  49  ASN A C   
8243  O O   . ASN D 33  ? 0.9600 0.8776 0.8941 0.0943  -0.0279 0.0622  49  ASN A O   
8244  C CB  . ASN D 33  ? 0.8423 0.7412 0.7791 0.0670  -0.0310 0.0798  49  ASN A CB  
8245  C CG  . ASN D 33  ? 0.7668 0.6584 0.7074 0.0578  -0.0325 0.0958  49  ASN A CG  
8246  O OD1 . ASN D 33  ? 0.7191 0.6124 0.6624 0.0596  -0.0316 0.1096  49  ASN A OD1 
8247  N ND2 . ASN D 33  ? 0.7431 0.6266 0.6839 0.0479  -0.0352 0.0934  49  ASN A ND2 
8248  N N   . TYR D 34  ? 0.8643 0.7991 0.7940 0.0809  -0.0200 0.0502  50  TYR A N   
8249  C CA  . TYR D 34  ? 0.8713 0.8159 0.7995 0.0901  -0.0181 0.0339  50  TYR A CA  
8250  C C   . TYR D 34  ? 0.8025 0.7607 0.7322 0.1002  -0.0143 0.0376  50  TYR A C   
8251  O O   . TYR D 34  ? 0.8551 0.8137 0.7858 0.1118  -0.0165 0.0323  50  TYR A O   
8252  C CB  . TYR D 34  ? 0.8989 0.8546 0.8228 0.0835  -0.0133 0.0192  50  TYR A CB  
8253  C CG  . TYR D 34  ? 0.9386 0.9082 0.8620 0.0930  -0.0099 0.0029  50  TYR A CG  
8254  C CD1 . TYR D 34  ? 1.0197 0.9841 0.9448 0.1017  -0.0144 -0.0096 50  TYR A CD1 
8255  C CD2 . TYR D 34  ? 0.9022 0.8901 0.8244 0.0928  -0.0026 -0.0016 50  TYR A CD2 
8256  C CE1 . TYR D 34  ? 1.0125 0.9905 0.9381 0.1107  -0.0116 -0.0260 50  TYR A CE1 
8257  C CE2 . TYR D 34  ? 0.9652 0.9667 0.8877 0.1013  0.0007  -0.0181 50  TYR A CE2 
8258  C CZ  . TYR D 34  ? 1.0104 1.0072 0.9346 0.1103  -0.0038 -0.0304 50  TYR A CZ  
8259  O OH  . TYR D 34  ? 0.9737 0.9842 0.8993 0.1193  -0.0013 -0.0477 50  TYR A OH  
8260  N N   . ASN D 35  ? 0.7757 0.7459 0.7064 0.0962  -0.0092 0.0459  51  ASN A N   
8261  C CA  . ASN D 35  ? 0.7382 0.7246 0.6710 0.1049  -0.0049 0.0481  51  ASN A CA  
8262  C C   . ASN D 35  ? 0.8039 0.7854 0.7385 0.1128  -0.0083 0.0613  51  ASN A C   
8263  O O   . ASN D 35  ? 0.8572 0.8528 0.7930 0.1210  -0.0053 0.0629  51  ASN A O   
8264  C CB  . ASN D 35  ? 0.6888 0.6882 0.6237 0.0976  0.0005  0.0534  51  ASN A CB  
8265  C CG  . ASN D 35  ? 0.7430 0.7551 0.6761 0.0950  0.0056  0.0387  51  ASN A CG  
8266  O OD1 . ASN D 35  ? 0.7281 0.7555 0.6629 0.1026  0.0099  0.0312  51  ASN A OD1 
8267  N ND2 . ASN D 35  ? 0.7241 0.7293 0.6531 0.0844  0.0051  0.0337  51  ASN A ND2 
8268  N N   . THR D 36  ? 0.8773 0.8399 0.8119 0.1102  -0.0144 0.0710  52  THR A N   
8269  C CA  . THR D 36  ? 0.8801 0.8359 0.8149 0.1174  -0.0183 0.0835  52  THR A CA  
8270  C C   . THR D 36  ? 0.9372 0.8738 0.8710 0.1233  -0.0263 0.0797  52  THR A C   
8271  O O   . THR D 36  ? 0.9603 0.8875 0.8935 0.1287  -0.0308 0.0909  52  THR A O   
8272  C CB  . THR D 36  ? 0.8677 0.8186 0.8044 0.1089  -0.0185 0.1023  52  THR A CB  
8273  O OG1 . THR D 36  ? 0.8872 0.8219 0.8250 0.0982  -0.0220 0.1038  52  THR A OG1 
8274  C CG2 . THR D 36  ? 0.8272 0.7983 0.7666 0.1056  -0.0117 0.1063  52  THR A CG2 
8275  N N   . ASN D 37  ? 0.9944 0.9252 0.9282 0.1221  -0.0283 0.0641  53  ASN A N   
8276  C CA  . ASN D 37  ? 1.0615 0.9740 0.9964 0.1277  -0.0367 0.0584  53  ASN A CA  
8277  C C   . ASN D 37  ? 1.1410 1.0597 1.0762 0.1339  -0.0370 0.0355  53  ASN A C   
8278  O O   . ASN D 37  ? 1.2524 1.1603 1.1898 0.1428  -0.0441 0.0285  53  ASN A O   
8279  C CB  . ASN D 37  ? 1.0428 0.9360 0.9798 0.1172  -0.0414 0.0642  53  ASN A CB  
8280  C CG  . ASN D 37  ? 1.1579 1.0296 1.0977 0.1230  -0.0512 0.0654  53  ASN A CG  
8281  O OD1 . ASN D 37  ? 1.2349 1.1043 1.1742 0.1343  -0.0547 0.0673  53  ASN A OD1 
8282  N ND2 . ASN D 37  ? 1.3563 1.2111 1.2994 0.1152  -0.0561 0.0652  53  ASN A ND2 
8283  N N   . ILE D 38  ? 1.0351 0.9713 0.9686 0.1299  -0.0296 0.0238  54  ILE A N   
8284  C CA  . ILE D 38  ? 1.0494 0.9962 0.9829 0.1341  -0.0279 0.0012  54  ILE A CA  
8285  C C   . ILE D 38  ? 1.1378 1.0692 1.0744 0.1388  -0.0364 -0.0095 54  ILE A C   
8286  O O   . ILE D 38  ? 1.2039 1.1345 1.1431 0.1517  -0.0410 -0.0170 54  ILE A O   
8287  C CB  . ILE D 38  ? 0.9847 0.9494 0.9185 0.1463  -0.0243 -0.0066 54  ILE A CB  
8288  C CG1 . ILE D 38  ? 1.0285 1.0089 0.9611 0.1447  -0.0169 0.0044  54  ILE A CG1 
8289  C CG2 . ILE D 38  ? 0.9001 0.8797 0.8337 0.1454  -0.0195 -0.0290 54  ILE A CG2 
8290  C CD1 . ILE D 38  ? 0.9385 0.9389 0.8723 0.1567  -0.0129 -0.0056 54  ILE A CD1 
8291  N N   . THR D 39  ? 1.1649 1.0839 1.1023 0.1290  -0.0395 -0.0102 55  THR A N   
8292  C CA  . THR D 39  ? 1.1837 1.0937 1.1251 0.1320  -0.0461 -0.0267 55  THR A CA  
8293  C C   . THR D 39  ? 1.2802 1.2003 1.2187 0.1208  -0.0411 -0.0414 55  THR A C   
8294  O O   . THR D 39  ? 1.2783 1.2053 1.2116 0.1095  -0.0348 -0.0341 55  THR A O   
8295  C CB  . THR D 39  ? 1.1960 1.0807 1.1419 0.1320  -0.0558 -0.0158 55  THR A CB  
8296  O OG1 . THR D 39  ? 1.2301 1.1074 1.1746 0.1178  -0.0546 -0.0046 55  THR A OG1 
8297  C CG2 . THR D 39  ? 1.1459 1.0223 1.0922 0.1413  -0.0595 0.0013  55  THR A CG2 
8298  N N   . GLU D 40  ? 1.5511 1.4737 1.4926 0.1243  -0.0440 -0.0629 56  GLU A N   
8299  C CA  . GLU D 40  ? 1.6190 1.5539 1.5567 0.1137  -0.0390 -0.0789 56  GLU A CA  
8300  C C   . GLU D 40  ? 1.5297 1.4537 1.4648 0.0995  -0.0402 -0.0699 56  GLU A C   
8301  O O   . GLU D 40  ? 1.5086 1.4428 1.4368 0.0873  -0.0341 -0.0720 56  GLU A O   
8302  C CB  . GLU D 40  ? 1.6397 1.5791 1.5831 0.1211  -0.0430 -0.1041 56  GLU A CB  
8303  C CG  . GLU D 40  ? 1.6784 1.6320 1.6184 0.1111  -0.0385 -0.1240 56  GLU A CG  
8304  C CD  . GLU D 40  ? 1.7238 1.6983 1.6549 0.1033  -0.0272 -0.1260 56  GLU A CD  
8305  O OE1 . GLU D 40  ? 1.6233 1.6074 1.5547 0.1113  -0.0232 -0.1239 56  GLU A OE1 
8306  O OE2 . GLU D 40  ? 1.7675 1.7491 1.6918 0.0895  -0.0227 -0.1309 56  GLU A OE2 
8307  N N   . GLU D 41  ? 1.2953 1.1984 1.2358 0.1007  -0.0484 -0.0587 57  GLU A N   
8308  C CA  . GLU D 41  ? 1.2709 1.1627 1.2101 0.0882  -0.0500 -0.0471 57  GLU A CA  
8309  C C   . GLU D 41  ? 1.2285 1.1271 1.1609 0.0792  -0.0429 -0.0304 57  GLU A C   
8310  O O   . GLU D 41  ? 1.1875 1.0922 1.1141 0.0671  -0.0391 -0.0316 57  GLU A O   
8311  C CB  . GLU D 41  ? 1.1906 1.0591 1.1375 0.0925  -0.0592 -0.0352 57  GLU A CB  
8312  C CG  . GLU D 41  ? 1.1732 1.0298 1.1200 0.0806  -0.0607 -0.0203 57  GLU A CG  
8313  C CD  . GLU D 41  ? 1.3020 1.1360 1.2569 0.0850  -0.0695 -0.0086 57  GLU A CD  
8314  O OE1 . GLU D 41  ? 1.4305 1.2607 1.3872 0.0961  -0.0716 -0.0030 57  GLU A OE1 
8315  O OE2 . GLU D 41  ? 1.2327 1.0527 1.1919 0.0776  -0.0743 -0.0046 57  GLU A OE2 
8316  N N   . ASN D 42  ? 1.1753 1.0726 1.1086 0.0849  -0.0417 -0.0143 58  ASN A N   
8317  C CA  . ASN D 42  ? 1.0807 0.9843 1.0100 0.0773  -0.0359 0.0014  58  ASN A CA  
8318  C C   . ASN D 42  ? 1.1215 1.0443 1.0441 0.0717  -0.0279 -0.0080 58  ASN A C   
8319  O O   . ASN D 42  ? 1.1148 1.0414 1.0336 0.0616  -0.0245 0.0007  58  ASN A O   
8320  C CB  . ASN D 42  ? 1.0438 0.9479 0.9753 0.0858  -0.0351 0.0160  58  ASN A CB  
8321  C CG  . ASN D 42  ? 1.0555 0.9404 0.9919 0.0869  -0.0419 0.0312  58  ASN A CG  
8322  O OD1 . ASN D 42  ? 1.1598 1.0325 1.0979 0.0781  -0.0454 0.0362  58  ASN A OD1 
8323  N ND2 . ASN D 42  ? 1.1037 0.9858 1.0419 0.0973  -0.0439 0.0387  58  ASN A ND2 
8324  N N   . VAL D 43  ? 1.2706 1.2055 1.1921 0.0779  -0.0253 -0.0258 59  VAL A N   
8325  C CA  . VAL D 43  ? 1.2501 1.2022 1.1650 0.0709  -0.0181 -0.0372 59  VAL A CA  
8326  C C   . VAL D 43  ? 1.2468 1.1957 1.1563 0.0571  -0.0189 -0.0411 59  VAL A C   
8327  O O   . VAL D 43  ? 1.2329 1.1894 1.1355 0.0465  -0.0141 -0.0380 59  VAL A O   
8328  C CB  . VAL D 43  ? 1.1945 1.1598 1.1104 0.0796  -0.0158 -0.0581 59  VAL A CB  
8329  C CG1 . VAL D 43  ? 1.1227 1.1070 1.0316 0.0716  -0.0071 -0.0682 59  VAL A CG1 
8330  C CG2 . VAL D 43  ? 1.2428 1.2096 1.1641 0.0942  -0.0167 -0.0549 59  VAL A CG2 
8331  N N   . GLN D 44  ? 1.2247 1.1624 1.1375 0.0570  -0.0253 -0.0482 60  GLN A N   
8332  C CA  . GLN D 44  ? 1.2410 1.1773 1.1484 0.0440  -0.0263 -0.0532 60  GLN A CA  
8333  C C   . GLN D 44  ? 1.2812 1.2085 1.1863 0.0343  -0.0274 -0.0339 60  GLN A C   
8334  O O   . GLN D 44  ? 1.2960 1.2290 1.1930 0.0226  -0.0246 -0.0330 60  GLN A O   
8335  C CB  . GLN D 44  ? 1.2417 1.1691 1.1549 0.0467  -0.0334 -0.0666 60  GLN A CB  
8336  C CG  . GLN D 44  ? 1.4320 1.3750 1.3430 0.0474  -0.0307 -0.0917 60  GLN A CG  
8337  C CD  . GLN D 44  ? 1.4166 1.3752 1.3153 0.0333  -0.0235 -0.0974 60  GLN A CD  
8338  O OE1 . GLN D 44  ? 1.4201 1.3948 1.3138 0.0331  -0.0163 -0.1041 60  GLN A OE1 
8339  N NE2 . GLN D 44  ? 1.3802 1.3342 1.2739 0.0214  -0.0258 -0.0956 60  GLN A NE2 
8340  N N   . ASN D 45  ? 1.1988 1.1122 1.1111 0.0388  -0.0318 -0.0184 61  ASN A N   
8341  C CA  . ASN D 45  ? 1.1138 1.0201 1.0253 0.0297  -0.0329 -0.0011 61  ASN A CA  
8342  C C   . ASN D 45  ? 1.1049 1.0231 1.0116 0.0259  -0.0266 0.0075  61  ASN A C   
8343  O O   . ASN D 45  ? 1.1620 1.0809 1.0638 0.0152  -0.0262 0.0134  61  ASN A O   
8344  C CB  . ASN D 45  ? 1.0926 0.9833 1.0129 0.0343  -0.0382 0.0137  61  ASN A CB  
8345  C CG  . ASN D 45  ? 1.1503 1.0267 1.0768 0.0378  -0.0455 0.0063  61  ASN A CG  
8346  O OD1 . ASN D 45  ? 1.1346 1.0006 1.0634 0.0305  -0.0501 0.0083  61  ASN A OD1 
8347  N ND2 . ASN D 45  ? 1.2193 1.0945 1.1500 0.0496  -0.0473 -0.0018 61  ASN A ND2 
8348  N N   . MET D 46  ? 1.0475 0.9749 0.9559 0.0349  -0.0224 0.0082  62  MET A N   
8349  C CA  . MET D 46  ? 1.0675 1.0079 0.9727 0.0321  -0.0163 0.0133  62  MET A CA  
8350  C C   . MET D 46  ? 1.0746 1.0235 0.9701 0.0215  -0.0130 0.0037  62  MET A C   
8351  O O   . MET D 46  ? 1.1120 1.0624 1.0039 0.0125  -0.0121 0.0122  62  MET A O   
8352  C CB  . MET D 46  ? 1.0243 0.9754 0.9327 0.0442  -0.0121 0.0099  62  MET A CB  
8353  C CG  . MET D 46  ? 0.9794 0.9446 0.8864 0.0425  -0.0059 0.0139  62  MET A CG  
8354  S SD  . MET D 46  ? 0.9483 0.9274 0.8596 0.0572  -0.0013 0.0070  62  MET A SD  
8355  C CE  . MET D 46  ? 0.9569 0.9514 0.8683 0.0531  0.0052  0.0123  62  MET A CE  
8356  N N   . ASN D 47  ? 1.0966 1.0518 0.9881 0.0222  -0.0113 -0.0141 63  ASN A N   
8357  C CA  . ASN D 47  ? 1.1499 1.1147 1.0310 0.0111  -0.0076 -0.0235 63  ASN A CA  
8358  C C   . ASN D 47  ? 1.1602 1.1163 1.0353 -0.0016 -0.0118 -0.0183 63  ASN A C   
8359  O O   . ASN D 47  ? 1.1848 1.1451 1.0516 -0.0121 -0.0098 -0.0145 63  ASN A O   
8360  C CB  . ASN D 47  ? 1.2231 1.1977 1.1020 0.0140  -0.0051 -0.0451 63  ASN A CB  
8361  C CG  . ASN D 47  ? 1.1585 1.1463 1.0404 0.0235  0.0006  -0.0525 63  ASN A CG  
8362  O OD1 . ASN D 47  ? 1.1331 1.1280 1.0141 0.0227  0.0052  -0.0453 63  ASN A OD1 
8363  N ND2 . ASN D 47  ? 1.1605 1.1520 1.0470 0.0329  -0.0001 -0.0680 63  ASN A ND2 
8364  N N   . ASN D 48  ? 1.1603 1.1044 1.0396 -0.0011 -0.0180 -0.0187 64  ASN A N   
8365  C CA  . ASN D 48  ? 1.1982 1.1349 1.0724 -0.0129 -0.0224 -0.0142 64  ASN A CA  
8366  C C   . ASN D 48  ? 1.1954 1.1275 1.0698 -0.0179 -0.0236 0.0046  64  ASN A C   
8367  O O   . ASN D 48  ? 1.2040 1.1377 1.0697 -0.0290 -0.0239 0.0078  64  ASN A O   
8368  C CB  . ASN D 48  ? 1.1639 1.0880 1.0447 -0.0110 -0.0293 -0.0173 64  ASN A CB  
8369  C CG  . ASN D 48  ? 1.1936 1.1221 1.0755 -0.0064 -0.0296 -0.0374 64  ASN A CG  
8370  O OD1 . ASN D 48  ? 1.2290 1.1714 1.1033 -0.0094 -0.0247 -0.0511 64  ASN A OD1 
8371  N ND2 . ASN D 48  ? 1.1850 1.1015 1.0766 -0.0004 -0.0358 -0.0400 64  ASN A ND2 
8372  N N   . ALA D 49  ? 1.1625 1.0888 1.0470 -0.0102 -0.0247 0.0170  65  ALA A N   
8373  C CA  . ALA D 49  ? 1.1203 1.0440 1.0070 -0.0144 -0.0260 0.0334  65  ALA A CA  
8374  C C   . ALA D 49  ? 1.1146 1.0496 0.9952 -0.0185 -0.0213 0.0347  65  ALA A C   
8375  O O   . ALA D 49  ? 1.2058 1.1395 1.0823 -0.0275 -0.0234 0.0421  65  ALA A O   
8376  C CB  . ALA D 49  ? 1.0490 0.9681 0.9474 -0.0053 -0.0268 0.0449  65  ALA A CB  
8377  N N   . GLY D 50  ? 1.1910 1.1368 1.0713 -0.0119 -0.0154 0.0271  66  GLY A N   
8378  C CA  . GLY D 50  ? 1.2163 1.1726 1.0916 -0.0160 -0.0108 0.0272  66  GLY A CA  
8379  C C   . GLY D 50  ? 1.2095 1.1673 1.0713 -0.0289 -0.0108 0.0211  66  GLY A C   
8380  O O   . GLY D 50  ? 1.2365 1.1963 1.0934 -0.0365 -0.0106 0.0274  66  GLY A O   
8381  N N   . ASP D 51  ? 1.1445 1.1013 1.0005 -0.0319 -0.0117 0.0092  67  ASP A N   
8382  C CA  . ASP D 51  ? 1.1431 1.1030 0.9849 -0.0450 -0.0116 0.0027  67  ASP A CA  
8383  C C   . ASP D 51  ? 1.0818 1.0315 0.9195 -0.0546 -0.0182 0.0145  67  ASP A C   
8384  O O   . ASP D 51  ? 1.0937 1.0450 0.9209 -0.0652 -0.0186 0.0182  67  ASP A O   
8385  C CB  . ASP D 51  ? 1.2074 1.1711 1.0456 -0.0449 -0.0108 -0.0149 67  ASP A CB  
8386  C CG  . ASP D 51  ? 1.1962 1.1734 1.0351 -0.0385 -0.0038 -0.0296 67  ASP A CG  
8387  O OD1 . ASP D 51  ? 1.2001 1.1844 1.0400 -0.0361 0.0011  -0.0263 67  ASP A OD1 
8388  O OD2 . ASP D 51  ? 1.2343 1.2151 1.0743 -0.0351 -0.0037 -0.0450 67  ASP A OD2 
8389  N N   . LYS D 52  ? 1.1018 1.0407 0.9478 -0.0513 -0.0239 0.0203  68  LYS A N   
8390  C CA  . LYS D 52  ? 1.0921 1.0215 0.9368 -0.0591 -0.0308 0.0313  68  LYS A CA  
8391  C C   . LYS D 52  ? 1.0390 0.9678 0.8860 -0.0608 -0.0318 0.0455  68  LYS A C   
8392  O O   . LYS D 52  ? 1.0384 0.9637 0.8784 -0.0703 -0.0363 0.0521  68  LYS A O   
8393  C CB  . LYS D 52  ? 1.0857 1.0047 0.9421 -0.0536 -0.0357 0.0348  68  LYS A CB  
8394  C CG  . LYS D 52  ? 1.2090 1.1269 1.0651 -0.0516 -0.0363 0.0204  68  LYS A CG  
8395  C CD  . LYS D 52  ? 1.2342 1.1395 1.1012 -0.0486 -0.0423 0.0245  68  LYS A CD  
8396  C CE  . LYS D 52  ? 1.1755 1.0795 1.0446 -0.0450 -0.0434 0.0090  68  LYS A CE  
8397  N NZ  . LYS D 52  ? 1.1826 1.0734 1.0615 -0.0444 -0.0501 0.0119  68  LYS A NZ  
8398  N N   . TRP D 53  ? 1.0093 0.9423 0.8662 -0.0516 -0.0281 0.0498  69  TRP A N   
8399  C CA  . TRP D 53  ? 0.9598 0.8944 0.8208 -0.0523 -0.0289 0.0611  69  TRP A CA  
8400  C C   . TRP D 53  ? 0.9728 0.9132 0.8221 -0.0603 -0.0264 0.0585  69  TRP A C   
8401  O O   . TRP D 53  ? 0.9729 0.9093 0.8183 -0.0680 -0.0311 0.0669  69  TRP A O   
8402  C CB  . TRP D 53  ? 0.9399 0.8801 0.8140 -0.0402 -0.0249 0.0641  69  TRP A CB  
8403  C CG  . TRP D 53  ? 0.9042 0.8498 0.7837 -0.0395 -0.0242 0.0720  69  TRP A CG  
8404  C CD1 . TRP D 53  ? 0.9069 0.8628 0.7880 -0.0351 -0.0185 0.0683  69  TRP A CD1 
8405  C CD2 . TRP D 53  ? 0.8823 0.8241 0.7696 -0.0416 -0.0298 0.0842  69  TRP A CD2 
8406  N NE1 . TRP D 53  ? 0.8882 0.8467 0.7771 -0.0350 -0.0203 0.0773  69  TRP A NE1 
8407  C CE2 . TRP D 53  ? 0.7908 0.7410 0.6839 -0.0386 -0.0274 0.0869  69  TRP A CE2 
8408  C CE3 . TRP D 53  ? 0.8907 0.8235 0.7814 -0.0457 -0.0368 0.0921  69  TRP A CE3 
8409  C CZ2 . TRP D 53  ? 0.7739 0.7239 0.6763 -0.0395 -0.0321 0.0967  69  TRP A CZ2 
8410  C CZ3 . TRP D 53  ? 0.8750 0.8081 0.7745 -0.0467 -0.0413 0.1019  69  TRP A CZ3 
8411  C CH2 . TRP D 53  ? 0.7989 0.7406 0.7044 -0.0434 -0.0391 0.1039  69  TRP A CH2 
8412  N N   . SER D 54  ? 0.9812 0.9310 0.8253 -0.0586 -0.0194 0.0470  70  SER A N   
8413  C CA  . SER D 54  ? 0.9605 0.9160 0.7929 -0.0676 -0.0165 0.0441  70  SER A CA  
8414  C C   . SER D 54  ? 0.9930 0.9428 0.8101 -0.0815 -0.0212 0.0451  70  SER A C   
8415  O O   . SER D 54  ? 1.0294 0.9780 0.8375 -0.0908 -0.0228 0.0507  70  SER A O   
8416  C CB  . SER D 54  ? 0.9783 0.9457 0.8071 -0.0647 -0.0081 0.0291  70  SER A CB  
8417  O OG  . SER D 54  ? 1.0983 1.0731 0.9388 -0.0534 -0.0033 0.0282  70  SER A OG  
8418  N N   . ALA D 55  ? 1.0392 0.9854 0.8529 -0.0832 -0.0239 0.0396  71  ALA A N   
8419  C CA  . ALA D 55  ? 1.0537 0.9958 0.8526 -0.0961 -0.0287 0.0397  71  ALA A CA  
8420  C C   . ALA D 55  ? 1.0755 1.0070 0.8761 -0.1002 -0.0372 0.0551  71  ALA A C   
8421  O O   . ALA D 55  ? 1.1092 1.0381 0.8974 -0.1111 -0.0408 0.0605  71  ALA A O   
8422  C CB  . ALA D 55  ? 1.0218 0.9634 0.8198 -0.0955 -0.0298 0.0291  71  ALA A CB  
8423  N N   . PHE D 56  ? 0.9985 0.9241 0.8148 -0.0917 -0.0408 0.0623  72  PHE A N   
8424  C CA  . PHE D 56  ? 1.0301 0.9474 0.8518 -0.0937 -0.0488 0.0760  72  PHE A CA  
8425  C C   . PHE D 56  ? 1.0321 0.9506 0.8526 -0.0964 -0.0493 0.0837  72  PHE A C   
8426  O O   . PHE D 56  ? 1.0411 0.9528 0.8581 -0.1030 -0.0569 0.0928  72  PHE A O   
8427  C CB  . PHE D 56  ? 0.9837 0.8982 0.8243 -0.0830 -0.0499 0.0811  72  PHE A CB  
8428  C CG  . PHE D 56  ? 0.9118 0.8208 0.7615 -0.0836 -0.0572 0.0939  72  PHE A CG  
8429  C CD1 . PHE D 56  ? 0.9322 0.8334 0.7788 -0.0903 -0.0653 0.0982  72  PHE A CD1 
8430  C CD2 . PHE D 56  ? 0.9261 0.8390 0.7872 -0.0776 -0.0561 0.1004  72  PHE A CD2 
8431  C CE1 . PHE D 56  ? 0.9759 0.8733 0.8318 -0.0904 -0.0722 0.1084  72  PHE A CE1 
8432  C CE2 . PHE D 56  ? 0.8610 0.7706 0.7316 -0.0779 -0.0630 0.1103  72  PHE A CE2 
8433  C CZ  . PHE D 56  ? 0.9172 0.8189 0.7853 -0.0842 -0.0711 0.1143  72  PHE A CZ  
8434  N N   . LEU D 57  ? 1.0151 0.9417 0.8389 -0.0911 -0.0420 0.0797  73  LEU A N   
8435  C CA  . LEU D 57  ? 1.0544 0.9819 0.8795 -0.0930 -0.0427 0.0865  73  LEU A CA  
8436  C C   . LEU D 57  ? 1.1280 1.0546 0.9341 -0.1061 -0.0429 0.0852  73  LEU A C   
8437  O O   . LEU D 57  ? 1.1333 1.0537 0.9364 -0.1122 -0.0491 0.0946  73  LEU A O   
8438  C CB  . LEU D 57  ? 1.0089 0.9462 0.8464 -0.0823 -0.0351 0.0828  73  LEU A CB  
8439  C CG  . LEU D 57  ? 0.9360 0.8733 0.7929 -0.0716 -0.0374 0.0898  73  LEU A CG  
8440  C CD1 . LEU D 57  ? 0.9282 0.8762 0.7963 -0.0608 -0.0301 0.0857  73  LEU A CD1 
8441  C CD2 . LEU D 57  ? 0.9443 0.8770 0.8062 -0.0749 -0.0447 0.1003  73  LEU A CD2 
8442  N N   . LYS D 58  ? 1.2515 1.1843 1.0447 -0.1108 -0.0368 0.0738  74  LYS A N   
8443  C CA  . LYS D 58  ? 1.3400 1.2725 1.1132 -0.1251 -0.0371 0.0732  74  LYS A CA  
8444  C C   . LYS D 58  ? 1.3395 1.2609 1.1033 -0.1343 -0.0476 0.0827  74  LYS A C   
8445  O O   . LYS D 58  ? 1.3395 1.2546 1.0937 -0.1435 -0.0529 0.0917  74  LYS A O   
8446  C CB  . LYS D 58  ? 1.3656 1.3088 1.1270 -0.1292 -0.0289 0.0578  74  LYS A CB  
8447  C CG  . LYS D 58  ? 1.4797 1.4261 1.2205 -0.1446 -0.0266 0.0565  74  LYS A CG  
8448  C CD  . LYS D 58  ? 1.5423 1.5031 1.2732 -0.1486 -0.0169 0.0393  74  LYS A CD  
8449  C CE  . LYS D 58  ? 1.6159 1.5874 1.3604 -0.1372 -0.0077 0.0297  74  LYS A CE  
8450  N NZ  . LYS D 58  ? 1.5096 1.4801 1.2592 -0.1368 -0.0061 0.0375  74  LYS A NZ  
8451  N N   . GLU D 59  ? 1.3881 1.3063 1.1561 -0.1310 -0.0514 0.0813  75  GLU A N   
8452  C CA  . GLU D 59  ? 1.3737 1.2825 1.1338 -0.1388 -0.0616 0.0887  75  GLU A CA  
8453  C C   . GLU D 59  ? 1.3545 1.2538 1.1229 -0.1378 -0.0707 0.1032  75  GLU A C   
8454  O O   . GLU D 59  ? 1.3274 1.2194 1.0835 -0.1476 -0.0784 0.1112  75  GLU A O   
8455  C CB  . GLU D 59  ? 1.3100 1.2179 1.0769 -0.1341 -0.0635 0.0835  75  GLU A CB  
8456  C CG  . GLU D 59  ? 1.4243 1.3226 1.1887 -0.1394 -0.0746 0.0922  75  GLU A CG  
8457  C CD  . GLU D 59  ? 1.6479 1.5448 1.3883 -0.1543 -0.0790 0.0931  75  GLU A CD  
8458  O OE1 . GLU D 59  ? 1.7253 1.6298 1.4507 -0.1614 -0.0724 0.0857  75  GLU A OE1 
8459  O OE2 . GLU D 59  ? 1.6554 1.5439 1.3919 -0.1593 -0.0893 0.1017  75  GLU A OE2 
8460  N N   . GLN D 60  ? 1.1393 1.0390 0.9286 -0.1260 -0.0702 0.1066  76  GLN A N   
8461  C CA  . GLN D 60  ? 1.0890 0.9817 0.8892 -0.1239 -0.0789 0.1185  76  GLN A CA  
8462  C C   . GLN D 60  ? 1.0808 0.9722 0.8777 -0.1276 -0.0795 0.1237  76  GLN A C   
8463  O O   . GLN D 60  ? 1.0539 0.9370 0.8527 -0.1305 -0.0892 0.1335  76  GLN A O   
8464  C CB  . GLN D 60  ? 1.0160 0.9122 0.8393 -0.1108 -0.0772 0.1193  76  GLN A CB  
8465  C CG  . GLN D 60  ? 1.0143 0.9090 0.8429 -0.1079 -0.0787 0.1168  76  GLN A CG  
8466  C CD  . GLN D 60  ? 1.0207 0.9064 0.8475 -0.1136 -0.0901 0.1239  76  GLN A CD  
8467  O OE1 . GLN D 60  ? 0.9993 0.8816 0.8364 -0.1118 -0.0972 0.1322  76  GLN A OE1 
8468  N NE2 . GLN D 60  ? 1.0591 0.9419 0.8743 -0.1199 -0.0923 0.1196  76  GLN A NE2 
8469  N N   . SER D 61  ? 1.1846 1.0839 0.9774 -0.1276 -0.0699 0.1168  77  SER A N   
8470  C CA  . SER D 61  ? 1.1799 1.0770 0.9663 -0.1340 -0.0704 0.1211  77  SER A CA  
8471  C C   . SER D 61  ? 1.2455 1.1330 1.0100 -0.1489 -0.0779 0.1274  77  SER A C   
8472  O O   . SER D 61  ? 1.2659 1.1432 1.0297 -0.1532 -0.0873 0.1381  77  SER A O   
8473  C CB  . SER D 61  ? 1.2361 1.1445 1.0195 -0.1331 -0.0580 0.1108  77  SER A CB  
8474  O OG  . SER D 61  ? 1.3632 1.2692 1.1429 -0.1390 -0.0585 0.1152  77  SER A OG  
8475  N N   . THR D 62  ? 1.2174 1.1086 0.9638 -0.1570 -0.0739 0.1202  78  THR A N   
8476  C CA  . THR D 62  ? 1.2290 1.1130 0.9525 -0.1718 -0.0808 0.1255  78  THR A CA  
8477  C C   . THR D 62  ? 1.2098 1.0810 0.9369 -0.1720 -0.0951 0.1374  78  THR A C   
8478  O O   . THR D 62  ? 1.2278 1.0886 0.9459 -0.1799 -0.1041 0.1481  78  THR A O   
8479  C CB  . THR D 62  ? 1.1850 1.0772 0.8944 -0.1770 -0.0753 0.1141  78  THR A CB  
8480  O OG1 . THR D 62  ? 1.2689 1.1739 0.9776 -0.1755 -0.0625 0.1019  78  THR A OG1 
8481  C CG2 . THR D 62  ? 1.1129 1.0010 0.7967 -0.1931 -0.0807 0.1182  78  THR A CG2 
8482  N N   . LEU D 63  ? 1.2212 1.0929 0.9624 -0.1631 -0.0977 0.1357  79  LEU A N   
8483  C CA  . LEU D 63  ? 1.2093 1.0708 0.9562 -0.1624 -0.1109 0.1453  79  LEU A CA  
8484  C C   . LEU D 63  ? 1.2524 1.1066 1.0121 -0.1587 -0.1184 0.1554  79  LEU A C   
8485  O O   . LEU D 63  ? 1.3119 1.1553 1.0680 -0.1632 -0.1310 0.1649  79  LEU A O   
8486  C CB  . LEU D 63  ? 1.1585 1.0235 0.9222 -0.1525 -0.1104 0.1407  79  LEU A CB  
8487  C CG  . LEU D 63  ? 1.0876 0.9536 0.8377 -0.1587 -0.1112 0.1348  79  LEU A CG  
8488  C CD1 . LEU D 63  ? 1.1185 0.9891 0.8860 -0.1486 -0.1075 0.1284  79  LEU A CD1 
8489  C CD2 . LEU D 63  ? 1.1024 0.9586 0.8426 -0.1666 -0.1248 0.1435  79  LEU A CD2 
8490  N N   . ALA D 64  ? 1.2466 1.1069 1.0224 -0.1499 -0.1115 0.1529  80  ALA A N   
8491  C CA  . ALA D 64  ? 1.2254 1.0807 1.0176 -0.1446 -0.1187 0.1607  80  ALA A CA  
8492  C C   . ALA D 64  ? 1.2525 1.0981 1.0308 -0.1548 -0.1243 0.1682  80  ALA A C   
8493  O O   . ALA D 64  ? 1.2696 1.1059 1.0561 -0.1540 -0.1355 0.1769  80  ALA A O   
8494  C CB  . ALA D 64  ? 1.2226 1.0890 1.0356 -0.1324 -0.1093 0.1549  80  ALA A CB  
8495  N N   . GLN D 65  ? 1.2078 1.0556 0.9656 -0.1648 -0.1168 0.1648  81  GLN A N   
8496  C CA  . GLN D 65  ? 1.2873 1.1255 1.0297 -0.1765 -0.1215 0.1727  81  GLN A CA  
8497  C C   . GLN D 65  ? 1.2995 1.1235 1.0247 -0.1869 -0.1357 0.1835  81  GLN A C   
8498  O O   . GLN D 65  ? 1.2946 1.1116 0.9977 -0.2004 -0.1379 0.1891  81  GLN A O   
8499  C CB  . GLN D 65  ? 1.3168 1.1632 1.0413 -0.1854 -0.1087 0.1653  81  GLN A CB  
8500  C CG  . GLN D 65  ? 1.3884 1.2454 1.1272 -0.1779 -0.0971 0.1575  81  GLN A CG  
8501  C CD  . GLN D 65  ? 1.5368 1.4059 1.2603 -0.1845 -0.0833 0.1462  81  GLN A CD  
8502  O OE1 . GLN D 65  ? 1.5989 1.4667 1.2985 -0.1979 -0.0831 0.1465  81  GLN A OE1 
8503  N NE2 . GLN D 65  ? 1.5309 1.4128 1.2681 -0.1752 -0.0718 0.1359  81  GLN A NE2 
8504  N N   . MET D 66  ? 1.4578 1.2779 1.1923 -0.1812 -0.1453 0.1863  82  MET A N   
8505  C CA  . MET D 66  ? 1.4971 1.3038 1.2186 -0.1890 -0.1606 0.1965  82  MET A CA  
8506  C C   . MET D 66  ? 1.4259 1.2231 1.1679 -0.1810 -0.1747 0.2044  82  MET A C   
8507  O O   . MET D 66  ? 1.4468 1.2337 1.1829 -0.1844 -0.1886 0.2118  82  MET A O   
8508  C CB  . MET D 66  ? 1.4771 1.2879 1.1895 -0.1910 -0.1613 0.1919  82  MET A CB  
8509  C CG  . MET D 66  ? 1.6022 1.4224 1.2926 -0.2003 -0.1498 0.1835  82  MET A CG  
8510  S SD  . MET D 66  ? 1.9020 1.7297 1.5867 -0.2004 -0.1488 0.1746  82  MET A SD  
8511  C CE  . MET D 66  ? 1.7263 1.5691 1.3946 -0.2071 -0.1315 0.1610  82  MET A CE  
8512  N N   . TYR D 67  ? 1.3044 1.1062 1.0709 -0.1700 -0.1716 0.2019  83  TYR A N   
8513  C CA  . TYR D 67  ? 1.2984 1.0934 1.0869 -0.1620 -0.1843 0.2077  83  TYR A CA  
8514  C C   . TYR D 67  ? 1.3577 1.1484 1.1508 -0.1628 -0.1836 0.2108  83  TYR A C   
8515  O O   . TYR D 67  ? 1.4132 1.2156 1.2214 -0.1551 -0.1724 0.2033  83  TYR A O   
8516  C CB  . TYR D 67  ? 1.1898 0.9972 1.0065 -0.1475 -0.1808 0.2004  83  TYR A CB  
8517  C CG  . TYR D 67  ? 1.2256 1.0390 1.0388 -0.1466 -0.1777 0.1955  83  TYR A CG  
8518  C CD1 . TYR D 67  ? 1.2505 1.0741 1.0547 -0.1477 -0.1633 0.1871  83  TYR A CD1 
8519  C CD2 . TYR D 67  ? 1.1759 0.9847 0.9952 -0.1449 -0.1899 0.1987  83  TYR A CD2 
8520  C CE1 . TYR D 67  ? 1.2464 1.0745 1.0484 -0.1470 -0.1612 0.1823  83  TYR A CE1 
8521  C CE2 . TYR D 67  ? 1.1525 0.9666 0.9694 -0.1446 -0.1872 0.1939  83  TYR A CE2 
8522  C CZ  . TYR D 67  ? 1.2054 1.0286 1.0137 -0.1458 -0.1729 0.1858  83  TYR A CZ  
8523  O OH  . TYR D 67  ? 1.2023 1.0300 1.0095 -0.1454 -0.1706 0.1805  83  TYR A OH  
8524  N N   . PRO D 68  ? 1.3348 1.1091 1.1156 -0.1720 -0.1955 0.2215  84  PRO A N   
8525  C CA  . PRO D 68  ? 1.3437 1.1129 1.1283 -0.1740 -0.1946 0.2243  84  PRO A CA  
8526  C C   . PRO D 68  ? 1.4144 1.1877 1.2330 -0.1597 -0.1984 0.2212  84  PRO A C   
8527  O O   . PRO D 68  ? 1.4143 1.1825 1.2481 -0.1532 -0.2120 0.2244  84  PRO A O   
8528  C CB  . PRO D 68  ? 1.4349 1.1830 1.1989 -0.1869 -0.2097 0.2382  84  PRO A CB  
8529  C CG  . PRO D 68  ? 1.4143 1.1563 1.1791 -0.1845 -0.2235 0.2424  84  PRO A CG  
8530  C CD  . PRO D 68  ? 1.4406 1.1993 1.2074 -0.1792 -0.2123 0.2319  84  PRO A CD  
8531  N N   . LEU D 69  ? 1.3740 1.1577 1.2047 -0.1548 -0.1867 0.2142  85  LEU A N   
8532  C CA  . LEU D 69  ? 1.3589 1.1502 1.2225 -0.1408 -0.1887 0.2094  85  LEU A CA  
8533  C C   . LEU D 69  ? 1.4461 1.2212 1.3200 -0.1411 -0.2065 0.2179  85  LEU A C   
8534  O O   . LEU D 69  ? 1.4541 1.2341 1.3564 -0.1294 -0.2130 0.2146  85  LEU A O   
8535  C CB  . LEU D 69  ? 1.2587 1.0642 1.1316 -0.1363 -0.1732 0.2003  85  LEU A CB  
8536  C CG  . LEU D 69  ? 1.1887 1.0102 1.0525 -0.1356 -0.1550 0.1909  85  LEU A CG  
8537  C CD1 . LEU D 69  ? 1.1489 0.9817 1.0217 -0.1319 -0.1425 0.1830  85  LEU A CD1 
8538  C CD2 . LEU D 69  ? 1.2385 1.0722 1.1169 -0.1245 -0.1527 0.1854  85  LEU A CD2 
8539  N N   . GLN D 70  ? 1.5484 1.3045 1.3998 -0.1546 -0.2146 0.2287  86  GLN A N   
8540  C CA  . GLN D 70  ? 1.6113 1.3486 1.4703 -0.1561 -0.2328 0.2380  86  GLN A CA  
8541  C C   . GLN D 70  ? 1.6052 1.3368 1.4777 -0.1489 -0.2500 0.2411  86  GLN A C   
8542  O O   . GLN D 70  ? 1.6946 1.4195 1.5895 -0.1420 -0.2636 0.2426  86  GLN A O   
8543  C CB  . GLN D 70  ? 1.6965 1.4145 1.5236 -0.1739 -0.2371 0.2501  86  GLN A CB  
8544  C CG  . GLN D 70  ? 1.8015 1.4970 1.6324 -0.1781 -0.2544 0.2611  86  GLN A CG  
8545  C CD  . GLN D 70  ? 1.9023 1.5774 1.7219 -0.1829 -0.2756 0.2739  86  GLN A CD  
8546  O OE1 . GLN D 70  ? 1.9443 1.6200 1.7443 -0.1877 -0.2761 0.2763  86  GLN A OE1 
8547  N NE2 . GLN D 70  ? 1.8815 1.5377 1.7122 -0.1822 -0.2935 0.2820  86  GLN A NE2 
8548  N N   . GLU D 71  ? 1.5395 1.2748 1.4008 -0.1499 -0.2498 0.2409  87  GLU A N   
8549  C CA  . GLU D 71  ? 1.5491 1.2803 1.4214 -0.1440 -0.2654 0.2430  87  GLU A CA  
8550  C C   . GLU D 71  ? 1.4414 1.1936 1.3411 -0.1297 -0.2591 0.2312  87  GLU A C   
8551  O O   . GLU D 71  ? 1.3125 1.0661 1.2157 -0.1267 -0.2663 0.2308  87  GLU A O   
8552  C CB  . GLU D 71  ? 1.6289 1.3506 1.4713 -0.1549 -0.2704 0.2503  87  GLU A CB  
8553  C CG  . GLU D 71  ? 1.6924 1.3924 1.5065 -0.1698 -0.2800 0.2638  87  GLU A CG  
8554  C CD  . GLU D 71  ? 1.8010 1.4965 1.5845 -0.1806 -0.2819 0.2690  87  GLU A CD  
8555  O OE1 . GLU D 71  ? 1.8893 1.5768 1.6729 -0.1792 -0.2975 0.2736  87  GLU A OE1 
8556  O OE2 . GLU D 71  ? 1.7841 1.4857 1.5444 -0.1901 -0.2677 0.2672  87  GLU A OE2 
8557  N N   . ILE D 72  ? 1.4362 1.2050 1.3548 -0.1213 -0.2458 0.2217  88  ILE A N   
8558  C CA  . ILE D 72  ? 1.3550 1.1451 1.2977 -0.1088 -0.2378 0.2110  88  ILE A CA  
8559  C C   . ILE D 72  ? 1.3044 1.1039 1.2791 -0.0976 -0.2395 0.2047  88  ILE A C   
8560  O O   . ILE D 72  ? 1.3558 1.1537 1.3320 -0.0987 -0.2354 0.2042  88  ILE A O   
8561  C CB  . ILE D 72  ? 1.3065 1.1115 1.2384 -0.1094 -0.2173 0.2043  88  ILE A CB  
8562  C CG1 . ILE D 72  ? 1.3563 1.1522 1.2565 -0.1213 -0.2160 0.2095  88  ILE A CG1 
8563  C CG2 . ILE D 72  ? 1.1914 1.0167 1.1461 -0.0976 -0.2100 0.1950  88  ILE A CG2 
8564  C CD1 . ILE D 72  ? 1.2970 1.1066 1.1891 -0.1208 -0.1995 0.2023  88  ILE A CD1 
8565  N N   . GLN D 73  ? 1.2693 1.0804 1.2706 -0.0869 -0.2451 0.1988  89  GLN A N   
8566  C CA  . GLN D 73  ? 1.2186 1.0373 1.2519 -0.0765 -0.2516 0.1929  89  GLN A CA  
8567  C C   . GLN D 73  ? 1.1806 1.0262 1.2386 -0.0649 -0.2402 0.1811  89  GLN A C   
8568  O O   . GLN D 73  ? 1.2087 1.0666 1.2913 -0.0564 -0.2391 0.1738  89  GLN A O   
8569  C CB  . GLN D 73  ? 1.2950 1.1012 1.3408 -0.0745 -0.2740 0.1968  89  GLN A CB  
8570  C CG  . GLN D 73  ? 1.4012 1.1787 1.4266 -0.0849 -0.2893 0.2096  89  GLN A CG  
8571  C CD  . GLN D 73  ? 1.4168 1.1803 1.4061 -0.0976 -0.2892 0.2194  89  GLN A CD  
8572  O OE1 . GLN D 73  ? 1.4190 1.1657 1.3833 -0.1088 -0.2901 0.2285  89  GLN A OE1 
8573  N NE2 . GLN D 73  ? 1.3650 1.1350 1.3522 -0.0962 -0.2894 0.2174  89  GLN A NE2 
8574  N N   . ASN D 74  ? 1.1925 1.0476 1.2446 -0.0648 -0.2324 0.1792  90  ASN A N   
8575  C CA  . ASN D 74  ? 1.1488 1.0286 1.2179 -0.0560 -0.2188 0.1697  90  ASN A CA  
8576  C C   . ASN D 74  ? 1.0812 0.9690 1.1428 -0.0558 -0.2019 0.1664  90  ASN A C   
8577  O O   . ASN D 74  ? 1.0111 0.8921 1.0471 -0.0633 -0.1929 0.1699  90  ASN A O   
8578  C CB  . ASN D 74  ? 1.1448 1.0286 1.2059 -0.0579 -0.2151 0.1701  90  ASN A CB  
8579  C CG  . ASN D 74  ? 1.0730 0.9812 1.1528 -0.0494 -0.2034 0.1617  90  ASN A CG  
8580  O OD1 . ASN D 74  ? 1.0276 0.9487 1.1108 -0.0454 -0.1900 0.1570  90  ASN A OD1 
8581  N ND2 . ASN D 74  ? 1.0888 1.0035 1.1805 -0.0472 -0.2087 0.1598  90  ASN A ND2 
8582  N N   . LEU D 75  ? 1.1118 1.0150 1.1961 -0.0471 -0.1976 0.1588  91  LEU A N   
8583  C CA  . LEU D 75  ? 1.0594 0.9691 1.1375 -0.0468 -0.1834 0.1553  91  LEU A CA  
8584  C C   . LEU D 75  ? 0.9144 0.8362 0.9808 -0.0461 -0.1665 0.1524  91  LEU A C   
8585  O O   . LEU D 75  ? 0.8419 0.7600 0.8893 -0.0509 -0.1565 0.1530  91  LEU A O   
8586  C CB  . LEU D 75  ? 1.1025 1.0279 1.2090 -0.0369 -0.1831 0.1468  91  LEU A CB  
8587  C CG  . LEU D 75  ? 1.0975 1.0116 1.2182 -0.0364 -0.1984 0.1478  91  LEU A CG  
8588  C CD1 . LEU D 75  ? 1.0670 1.0006 1.2141 -0.0265 -0.1934 0.1372  91  LEU A CD1 
8589  C CD2 . LEU D 75  ? 1.0413 0.9299 1.1374 -0.0480 -0.2032 0.1574  91  LEU A CD2 
8590  N N   . THR D 76  ? 0.9336 0.8701 1.0116 -0.0404 -0.1631 0.1490  92  THR A N   
8591  C CA  . THR D 76  ? 0.8605 0.8065 0.9276 -0.0398 -0.1479 0.1469  92  THR A CA  
8592  C C   . THR D 76  ? 0.8845 0.8140 0.9233 -0.0497 -0.1471 0.1531  92  THR A C   
8593  O O   . THR D 76  ? 0.8889 0.8201 0.9120 -0.0517 -0.1351 0.1517  92  THR A O   
8594  C CB  . THR D 76  ? 0.8639 0.8281 0.9494 -0.0327 -0.1451 0.1429  92  THR A CB  
8595  O OG1 . THR D 76  ? 1.0666 1.0244 1.1589 -0.0347 -0.1582 0.1459  92  THR A OG1 
8596  C CG2 . THR D 76  ? 0.7618 0.7468 0.8737 -0.0228 -0.1428 0.1352  92  THR A CG2 
8597  N N   . VAL D 77  ? 0.9656 0.8795 0.9975 -0.0560 -0.1603 0.1593  93  VAL A N   
8598  C CA  . VAL D 77  ? 0.9771 0.8751 0.9808 -0.0664 -0.1605 0.1649  93  VAL A CA  
8599  C C   . VAL D 77  ? 0.9541 0.8428 0.9396 -0.0731 -0.1567 0.1668  93  VAL A C   
8600  O O   . VAL D 77  ? 0.9522 0.8377 0.9161 -0.0791 -0.1480 0.1667  93  VAL A O   
8601  C CB  . VAL D 77  ? 1.0131 0.8973 1.0141 -0.0714 -0.1767 0.1712  93  VAL A CB  
8602  C CG1 . VAL D 77  ? 1.0341 0.9029 1.0051 -0.0827 -0.1773 0.1767  93  VAL A CG1 
8603  C CG2 . VAL D 77  ? 0.9608 0.8559 0.9801 -0.0655 -0.1793 0.1682  93  VAL A CG2 
8604  N N   . LYS D 78  ? 0.9283 0.8134 0.9234 -0.0720 -0.1630 0.1675  94  LYS A N   
8605  C CA  . LYS D 78  ? 0.9407 0.8169 0.9200 -0.0790 -0.1597 0.1694  94  LYS A CA  
8606  C C   . LYS D 78  ? 0.9077 0.7983 0.8845 -0.0756 -0.1421 0.1618  94  LYS A C   
8607  O O   . LYS D 78  ? 0.9433 0.8292 0.8986 -0.0832 -0.1345 0.1619  94  LYS A O   
8608  C CB  . LYS D 78  ? 1.0316 0.9013 1.0262 -0.0775 -0.1710 0.1714  94  LYS A CB  
8609  C CG  . LYS D 78  ? 1.1255 0.9728 1.0992 -0.0899 -0.1798 0.1806  94  LYS A CG  
8610  C CD  . LYS D 78  ? 1.1525 0.9921 1.1421 -0.0884 -0.1905 0.1823  94  LYS A CD  
8611  C CE  . LYS D 78  ? 1.2227 1.0395 1.1879 -0.1025 -0.1972 0.1925  94  LYS A CE  
8612  N NZ  . LYS D 78  ? 1.2855 1.0956 1.2622 -0.1028 -0.2021 0.1932  94  LYS A NZ  
8613  N N   . LEU D 79  ? 0.9534 0.8629 0.9516 -0.0642 -0.1353 0.1546  95  LEU A N   
8614  C CA  . LEU D 79  ? 0.9162 0.8409 0.9147 -0.0590 -0.1196 0.1469  95  LEU A CA  
8615  C C   . LEU D 79  ? 0.9102 0.8345 0.8890 -0.0626 -0.1105 0.1463  95  LEU A C   
8616  O O   . LEU D 79  ? 0.9323 0.8590 0.8981 -0.0648 -0.1001 0.1423  95  LEU A O   
8617  C CB  . LEU D 79  ? 0.8315 0.7766 0.8562 -0.0463 -0.1158 0.1406  95  LEU A CB  
8618  C CG  . LEU D 79  ? 0.8002 0.7513 0.8463 -0.0409 -0.1207 0.1372  95  LEU A CG  
8619  C CD1 . LEU D 79  ? 0.7498 0.7241 0.8192 -0.0290 -0.1152 0.1301  95  LEU A CD1 
8620  C CD2 . LEU D 79  ? 0.7455 0.6925 0.7819 -0.0449 -0.1152 0.1352  95  LEU A CD2 
8621  N N   . GLN D 80  ? 0.8696 0.7916 0.8473 -0.0630 -0.1144 0.1493  96  GLN A N   
8622  C CA  . GLN D 80  ? 0.8523 0.7736 0.8134 -0.0659 -0.1066 0.1480  96  GLN A CA  
8623  C C   . GLN D 80  ? 0.9132 0.8200 0.8479 -0.0780 -0.1079 0.1509  96  GLN A C   
8624  O O   . GLN D 80  ? 0.9518 0.8604 0.8713 -0.0808 -0.0983 0.1467  96  GLN A O   
8625  C CB  . GLN D 80  ? 0.8074 0.7294 0.7753 -0.0640 -0.1112 0.1503  96  GLN A CB  
8626  C CG  . GLN D 80  ? 0.7943 0.7328 0.7859 -0.0532 -0.1079 0.1469  96  GLN A CG  
8627  C CD  . GLN D 80  ? 0.8143 0.7534 0.8160 -0.0524 -0.1148 0.1496  96  GLN A CD  
8628  O OE1 . GLN D 80  ? 0.8823 0.8214 0.8782 -0.0533 -0.1106 0.1497  96  GLN A OE1 
8629  N NE2 . GLN D 80  ? 0.7827 0.7217 0.8000 -0.0509 -0.1259 0.1515  96  GLN A NE2 
8630  N N   . LEU D 81  ? 0.9833 0.8762 0.9122 -0.0854 -0.1199 0.1579  97  LEU A N   
8631  C CA  . LEU D 81  ? 1.0560 0.9360 0.9582 -0.0979 -0.1213 0.1614  97  LEU A CA  
8632  C C   . LEU D 81  ? 1.0607 0.9429 0.9537 -0.1015 -0.1124 0.1577  97  LEU A C   
8633  O O   . LEU D 81  ? 1.0790 0.9612 0.9525 -0.1083 -0.1046 0.1545  97  LEU A O   
8634  C CB  . LEU D 81  ? 1.0595 0.9237 0.9580 -0.1046 -0.1375 0.1708  97  LEU A CB  
8635  C CG  . LEU D 81  ? 0.9983 0.8561 0.8889 -0.1081 -0.1447 0.1743  97  LEU A CG  
8636  C CD1 . LEU D 81  ? 1.1275 0.9699 1.0136 -0.1143 -0.1608 0.1833  97  LEU A CD1 
8637  C CD2 . LEU D 81  ? 1.0236 0.8807 0.8910 -0.1156 -0.1372 0.1716  97  LEU A CD2 
8638  N N   . GLN D 82  ? 1.1294 1.0155 1.0384 -0.0965 -0.1130 0.1567  98  GLN A N   
8639  C CA  . GLN D 82  ? 1.1827 1.0729 1.0873 -0.0988 -0.1042 0.1522  98  GLN A CA  
8640  C C   . GLN D 82  ? 1.1609 1.0664 1.0639 -0.0932 -0.0888 0.1421  98  GLN A C   
8641  O O   . GLN D 82  ? 1.2052 1.1125 1.0934 -0.0991 -0.0802 0.1375  98  GLN A O   
8642  C CB  . GLN D 82  ? 1.1741 1.0675 1.1019 -0.0919 -0.1087 0.1519  98  GLN A CB  
8643  C CG  . GLN D 82  ? 1.2752 1.1700 1.2024 -0.0948 -0.1033 0.1485  98  GLN A CG  
8644  C CD  . GLN D 82  ? 1.3000 1.1936 1.2504 -0.0894 -0.1122 0.1499  98  GLN A CD  
8645  O OE1 . GLN D 82  ? 1.3837 1.2677 1.3312 -0.0962 -0.1160 0.1529  98  GLN A OE1 
8646  N NE2 . GLN D 82  ? 1.1296 1.0331 1.1034 -0.0778 -0.1161 0.1476  98  GLN A NE2 
8647  N N   . ALA D 83  ? 1.0937 1.0107 1.0125 -0.0819 -0.0855 0.1383  99  ALA A N   
8648  C CA  . ALA D 83  ? 1.0638 0.9932 0.9808 -0.0760 -0.0730 0.1302  99  ALA A CA  
8649  C C   . ALA D 83  ? 1.0705 0.9938 0.9638 -0.0848 -0.0694 0.1287  99  ALA A C   
8650  O O   . ALA D 83  ? 1.1021 1.0314 0.9855 -0.0864 -0.0596 0.1212  99  ALA A O   
8651  C CB  . ALA D 83  ? 0.9701 0.9078 0.9039 -0.0656 -0.0735 0.1301  99  ALA A CB  
8652  N N   . LEU D 84  ? 1.0815 0.9945 0.9666 -0.0905 -0.0775 0.1346  100 LEU A N   
8653  C CA  . LEU D 84  ? 1.0938 1.0038 0.9600 -0.0968 -0.0741 0.1318  100 LEU A CA  
8654  C C   . LEU D 84  ? 1.1396 1.0412 0.9824 -0.1108 -0.0751 0.1331  100 LEU A C   
8655  O O   . LEU D 84  ? 1.1050 1.0068 0.9311 -0.1169 -0.0709 0.1285  100 LEU A O   
8656  C CB  . LEU D 84  ? 1.0183 0.9226 0.8878 -0.0960 -0.0820 0.1367  100 LEU A CB  
8657  C CG  . LEU D 84  ? 0.9339 0.8378 0.7953 -0.0968 -0.0795 0.1332  100 LEU A CG  
8658  C CD1 . LEU D 84  ? 0.8484 0.7637 0.7145 -0.0886 -0.0678 0.1241  100 LEU A CD1 
8659  C CD2 . LEU D 84  ? 0.9015 0.8016 0.7748 -0.0936 -0.0881 0.1389  100 LEU A CD2 
8660  N N   . GLN D 85  ? 1.2159 1.1105 1.0575 -0.1164 -0.0806 0.1390  101 GLN A N   
8661  C CA  . GLN D 85  ? 1.2396 1.1255 1.0579 -0.1312 -0.0822 0.1420  101 GLN A CA  
8662  C C   . GLN D 85  ? 1.3415 1.2361 1.1522 -0.1347 -0.0703 0.1337  101 GLN A C   
8663  O O   . GLN D 85  ? 1.4775 1.3697 1.2662 -0.1471 -0.0676 0.1326  101 GLN A O   
8664  C CB  . GLN D 85  ? 1.1795 1.0511 0.9980 -0.1372 -0.0951 0.1535  101 GLN A CB  
8665  C CG  . GLN D 85  ? 1.2247 1.0847 1.0398 -0.1401 -0.1083 0.1622  101 GLN A CG  
8666  C CD  . GLN D 85  ? 1.2841 1.1297 1.1019 -0.1443 -0.1221 0.1732  101 GLN A CD  
8667  O OE1 . GLN D 85  ? 1.3314 1.1761 1.1570 -0.1437 -0.1217 0.1739  101 GLN A OE1 
8668  N NE2 . GLN D 85  ? 1.2890 1.1233 1.1024 -0.1476 -0.1351 0.1812  101 GLN A NE2 
8669  N N   . GLN D 86  ? 1.2980 1.2035 1.1260 -0.1247 -0.0631 0.1274  102 GLN A N   
8670  C CA  . GLN D 86  ? 1.3121 1.2269 1.1347 -0.1275 -0.0519 0.1186  102 GLN A CA  
8671  C C   . GLN D 86  ? 1.3518 1.2732 1.1566 -0.1326 -0.0432 0.1096  102 GLN A C   
8672  O O   . GLN D 86  ? 1.3292 1.2565 1.1381 -0.1247 -0.0402 0.1042  102 GLN A O   
8673  C CB  . GLN D 86  ? 1.3306 1.2593 1.1756 -0.1132 -0.0447 0.1111  102 GLN A CB  
8674  C CG  . GLN D 86  ? 1.3456 1.2832 1.2025 -0.1000 -0.0417 0.1066  102 GLN A CG  
8675  C CD  . GLN D 86  ? 1.3494 1.3006 1.2285 -0.0856 -0.0364 0.1011  102 GLN A CD  
8676  O OE1 . GLN D 86  ? 1.4227 1.3793 1.3086 -0.0847 -0.0330 0.0978  102 GLN A OE1 
8677  N NE2 . GLN D 86  ? 1.3503 1.3076 1.2406 -0.0747 -0.0355 0.1000  102 GLN A NE2 
8678  N N   . ASN D 87  ? 1.4489 1.3695 1.2342 -0.1462 -0.0395 0.1076  103 ASN A N   
8679  C CA  . ASN D 87  ? 1.4820 1.4108 1.2508 -0.1517 -0.0314 0.0973  103 ASN A CA  
8680  C C   . ASN D 87  ? 1.5218 1.4659 1.2915 -0.1503 -0.0183 0.0837  103 ASN A C   
8681  O O   . ASN D 87  ? 1.5453 1.4981 1.3024 -0.1549 -0.0111 0.0731  103 ASN A O   
8682  C CB  . ASN D 87  ? 1.5563 1.4764 1.2992 -0.1694 -0.0359 0.1028  103 ASN A CB  
8683  C CG  . ASN D 87  ? 1.6270 1.5335 1.3632 -0.1803 -0.0440 0.1158  103 ASN A CG  
8684  O OD1 . ASN D 87  ? 1.6532 1.5585 1.4031 -0.1762 -0.0442 0.1183  103 ASN A OD1 
8685  N ND2 . ASN D 87  ? 1.5352 1.4312 1.2500 -0.1943 -0.0513 0.1242  103 ASN A ND2 
8686  N N   . GLY D 88  ? 1.5423 1.4907 1.3274 -0.1440 -0.0154 0.0826  104 GLY A N   
8687  C CA  . GLY D 88  ? 1.4357 1.3998 1.2253 -0.1404 -0.0033 0.0690  104 GLY A CA  
8688  C C   . GLY D 88  ? 1.5172 1.4886 1.2865 -0.1537 0.0049  0.0596  104 GLY A C   
8689  O O   . GLY D 88  ? 1.5203 1.4839 1.2719 -0.1699 0.0023  0.0659  104 GLY A O   
8690  N N   . SER D 89  ? 1.4581 1.4450 1.2295 -0.1470 0.0145  0.0440  105 SER A N   
8691  C CA  . SER D 89  ? 1.5265 1.5242 1.2811 -0.1587 0.0234  0.0321  105 SER A CA  
8692  C C   . SER D 89  ? 1.5458 1.5379 1.2782 -0.1721 0.0197  0.0348  105 SER A C   
8693  O O   . SER D 89  ? 1.5840 1.5828 1.2988 -0.1866 0.0253  0.0286  105 SER A O   
8694  C CB  . SER D 89  ? 1.5229 1.5387 1.2871 -0.1466 0.0333  0.0138  105 SER A CB  
8695  O OG  . SER D 89  ? 1.5432 1.5693 1.2921 -0.1548 0.0395  0.0008  105 SER A OG  
8696  N N   . SER D 90  ? 1.5133 1.4943 1.2460 -0.1685 0.0105  0.0438  106 SER A N   
8697  C CA  . SER D 90  ? 1.5059 1.4817 1.2178 -0.1813 0.0061  0.0468  106 SER A CA  
8698  C C   . SER D 90  ? 1.4878 1.4536 1.1812 -0.1997 0.0017  0.0586  106 SER A C   
8699  O O   . SER D 90  ? 1.5403 1.5035 1.2132 -0.2129 -0.0012 0.0610  106 SER A O   
8700  C CB  . SER D 90  ? 1.5066 1.4722 1.2252 -0.1728 -0.0034 0.0541  106 SER A CB  
8701  O OG  . SER D 90  ? 1.5135 1.4628 1.2355 -0.1738 -0.0145 0.0713  106 SER A OG  
8702  N N   . VAL D 91  ? 1.5294 1.4904 1.2293 -0.2014 0.0014  0.0654  107 VAL A N   
8703  C CA  . VAL D 91  ? 1.4697 1.4200 1.1516 -0.2196 -0.0028 0.0769  107 VAL A CA  
8704  C C   . VAL D 91  ? 1.4779 1.4413 1.1442 -0.2340 0.0086  0.0667  107 VAL A C   
8705  O O   . VAL D 91  ? 1.4091 1.3651 1.0560 -0.2519 0.0062  0.0756  107 VAL A O   
8706  C CB  . VAL D 91  ? 1.4722 1.4089 1.1679 -0.2165 -0.0101 0.0901  107 VAL A CB  
8707  C CG1 . VAL D 91  ? 1.4600 1.4075 1.1683 -0.2132 -0.0002 0.0811  107 VAL A CG1 
8708  C CG2 . VAL D 91  ? 1.5316 1.4501 1.2088 -0.2332 -0.0204 0.1069  107 VAL A CG2 
8709  N N   . LEU D 92  ? 1.4441 1.4266 1.1186 -0.2269 0.0206  0.0486  108 LEU A N   
8710  C CA  . LEU D 92  ? 1.4206 1.4189 1.0798 -0.2407 0.0319  0.0359  108 LEU A CA  
8711  C C   . LEU D 92  ? 1.4059 1.4109 1.0456 -0.2494 0.0326  0.0296  108 LEU A C   
8712  O O   . LEU D 92  ? 1.4386 1.4409 1.0828 -0.2397 0.0272  0.0291  108 LEU A O   
8713  C CB  . LEU D 92  ? 1.4476 1.4654 1.1233 -0.2292 0.0439  0.0168  108 LEU A CB  
8714  C CG  . LEU D 92  ? 1.4504 1.4682 1.1468 -0.2196 0.0462  0.0174  108 LEU A CG  
8715  C CD1 . LEU D 92  ? 1.4408 1.4790 1.1528 -0.2055 0.0567  -0.0028 108 LEU A CD1 
8716  C CD2 . LEU D 92  ? 1.4529 1.4679 1.1391 -0.2370 0.0491  0.0226  108 LEU A CD2 
8717  N N   . SER D 93  ? 1.4468 1.4620 1.0655 -0.2680 0.0395  0.0238  109 SER A N   
8718  C CA  . SER D 93  ? 1.5355 1.5629 1.1371 -0.2762 0.0423  0.0133  109 SER A CA  
8719  C C   . SER D 93  ? 1.6537 1.6952 1.2721 -0.2584 0.0470  -0.0052 109 SER A C   
8720  O O   . SER D 93  ? 1.7020 1.7504 1.3405 -0.2443 0.0524  -0.0142 109 SER A O   
8721  C CB  . SER D 93  ? 1.5005 1.5430 1.0814 -0.2969 0.0524  0.0050  109 SER A CB  
8722  O OG  . SER D 93  ? 1.5434 1.6074 1.1362 -0.2907 0.0651  -0.0162 109 SER A OG  
8723  N N   . GLU D 94  ? 1.8485 1.8934 1.4593 -0.2586 0.0439  -0.0106 110 GLU A N   
8724  C CA  . GLU D 94  ? 1.8025 1.8576 1.4299 -0.2413 0.0464  -0.0268 110 GLU A CA  
8725  C C   . GLU D 94  ? 1.7759 1.8537 1.4100 -0.2387 0.0593  -0.0488 110 GLU A C   
8726  O O   . GLU D 94  ? 1.7883 1.8720 1.4425 -0.2208 0.0618  -0.0599 110 GLU A O   
8727  C CB  . GLU D 94  ? 1.9353 1.9925 1.5519 -0.2449 0.0418  -0.0311 110 GLU A CB  
8728  C CG  . GLU D 94  ? 2.0263 2.0622 1.6372 -0.2465 0.0286  -0.0109 110 GLU A CG  
8729  C CD  . GLU D 94  ? 2.2503 2.2906 1.8454 -0.2551 0.0249  -0.0155 110 GLU A CD  
8730  O OE1 . GLU D 94  ? 2.2733 2.3306 1.8711 -0.2518 0.0307  -0.0353 110 GLU A OE1 
8731  O OE2 . GLU D 94  ? 2.3331 2.3605 1.9136 -0.2649 0.0158  0.0000  110 GLU A OE2 
8732  N N   . ASP D 95  ? 1.8987 1.9889 1.5163 -0.2565 0.0672  -0.0546 111 ASP A N   
8733  C CA  . ASP D 95  ? 1.8421 1.9558 1.4645 -0.2564 0.0799  -0.0766 111 ASP A CA  
8734  C C   . ASP D 95  ? 1.7971 1.9098 1.4397 -0.2444 0.0837  -0.0765 111 ASP A C   
8735  O O   . ASP D 95  ? 1.7348 1.8601 1.3949 -0.2292 0.0890  -0.0929 111 ASP A O   
8736  C CB  . ASP D 95  ? 1.8409 1.9667 1.4386 -0.2811 0.0868  -0.0800 111 ASP A CB  
8737  C CG  . ASP D 95  ? 1.9869 2.1390 1.5878 -0.2837 0.1001  -0.1037 111 ASP A CG  
8738  O OD1 . ASP D 95  ? 2.0321 2.2013 1.6389 -0.2763 0.1035  -0.1243 111 ASP A OD1 
8739  O OD2 . ASP D 95  ? 2.1249 2.2804 1.7243 -0.2923 0.1067  -0.1022 111 ASP A OD2 
8740  N N   . LYS D 96  ? 1.7083 1.8058 1.3490 -0.2505 0.0805  -0.0583 112 LYS A N   
8741  C CA  . LYS D 96  ? 1.5728 1.6681 1.2336 -0.2387 0.0827  -0.0568 112 LYS A CA  
8742  C C   . LYS D 96  ? 1.5331 1.6203 1.2166 -0.2149 0.0764  -0.0542 112 LYS A C   
8743  O O   . LYS D 96  ? 1.4998 1.5947 1.2020 -0.2009 0.0809  -0.0629 112 LYS A O   
8744  C CB  . LYS D 96  ? 1.4411 1.5195 1.0955 -0.2504 0.0783  -0.0367 112 LYS A CB  
8745  C CG  . LYS D 96  ? 1.3646 1.4488 0.9958 -0.2751 0.0840  -0.0364 112 LYS A CG  
8746  C CD  . LYS D 96  ? 1.2876 1.3615 0.9214 -0.2824 0.0840  -0.0244 112 LYS A CD  
8747  C CE  . LYS D 96  ? 1.3089 1.3805 0.9158 -0.3090 0.0856  -0.0164 112 LYS A CE  
8748  N NZ  . LYS D 96  ? 1.2773 1.3553 0.8860 -0.3192 0.0944  -0.0198 112 LYS A NZ  
8749  N N   . SER D 97  ? 1.5120 1.5837 1.1937 -0.2108 0.0660  -0.0419 113 SER A N   
8750  C CA  . SER D 97  ? 1.4962 1.5615 1.1977 -0.1897 0.0604  -0.0402 113 SER A CA  
8751  C C   . SER D 97  ? 1.5923 1.6750 1.3045 -0.1769 0.0670  -0.0617 113 SER A C   
8752  O O   . SER D 97  ? 1.5748 1.6603 1.3064 -0.1597 0.0682  -0.0660 113 SER A O   
8753  C CB  . SER D 97  ? 1.5266 1.5759 1.2218 -0.1903 0.0493  -0.0270 113 SER A CB  
8754  O OG  . SER D 97  ? 1.5609 1.5930 1.2463 -0.2012 0.0415  -0.0071 113 SER A OG  
8755  N N   . LYS D 98  ? 1.8039 1.8987 1.5038 -0.1848 0.0705  -0.0756 114 LYS A N   
8756  C CA  . LYS D 98  ? 1.7494 1.8612 1.4595 -0.1732 0.0761  -0.0978 114 LYS A CA  
8757  C C   . LYS D 98  ? 1.6452 1.7733 1.3650 -0.1694 0.0861  -0.1116 114 LYS A C   
8758  O O   . LYS D 98  ? 1.6151 1.7502 1.3524 -0.1519 0.0878  -0.1226 114 LYS A O   
8759  C CB  . LYS D 98  ? 1.8082 1.9314 1.5033 -0.1841 0.0779  -0.1113 114 LYS A CB  
8760  C CG  . LYS D 98  ? 1.9183 2.0257 1.6077 -0.1844 0.0672  -0.0993 114 LYS A CG  
8761  C CD  . LYS D 98  ? 1.9446 2.0625 1.6224 -0.1920 0.0672  -0.1130 114 LYS A CD  
8762  C CE  . LYS D 98  ? 1.9090 2.0387 1.5631 -0.2150 0.0726  -0.1165 114 LYS A CE  
8763  N NZ  . LYS D 98  ? 1.8062 1.9561 1.4544 -0.2196 0.0766  -0.1391 114 LYS A NZ  
8764  N N   . ARG D 99  ? 1.4852 1.6188 1.1945 -0.1852 0.0922  -0.1103 115 ARG A N   
8765  C CA  . ARG D 99  ? 1.4060 1.5556 1.1253 -0.1822 0.1019  -0.1236 115 ARG A CA  
8766  C C   . ARG D 99  ? 1.3112 1.4531 1.0515 -0.1646 0.0993  -0.1160 115 ARG A C   
8767  O O   . ARG D 99  ? 1.2695 1.4246 1.0252 -0.1508 0.1043  -0.1306 115 ARG A O   
8768  C CB  . ARG D 99  ? 1.4921 1.6465 1.1961 -0.2038 0.1083  -0.1211 115 ARG A CB  
8769  C CG  . ARG D 99  ? 1.6902 1.8612 1.3757 -0.2207 0.1147  -0.1352 115 ARG A CG  
8770  C CD  . ARG D 99  ? 1.8133 1.9819 1.4780 -0.2455 0.1178  -0.1250 115 ARG A CD  
8771  N NE  . ARG D 99  ? 1.8817 2.0732 1.5439 -0.2560 0.1306  -0.1428 115 ARG A NE  
8772  C CZ  . ARG D 99  ? 1.8962 2.1020 1.5381 -0.2771 0.1374  -0.1507 115 ARG A CZ  
8773  N NH1 . ARG D 99  ? 1.9098 2.1111 1.5318 -0.2892 0.1327  -0.1441 115 ARG A NH1 
8774  N NH2 . ARG D 99  ? 1.9080 2.1347 1.5497 -0.2865 0.1494  -0.1665 115 ARG A NH2 
8775  N N   . LEU D 100 ? 1.3453 1.4672 1.0863 -0.1652 0.0915  -0.0940 116 LEU A N   
8776  C CA  . LEU D 100 ? 1.2535 1.3696 1.0144 -0.1496 0.0890  -0.0869 116 LEU A CA  
8777  C C   . LEU D 100 ? 1.1981 1.3156 0.9743 -0.1284 0.0860  -0.0927 116 LEU A C   
8778  O O   . LEU D 100 ? 1.1574 1.2844 0.9499 -0.1140 0.0896  -0.1013 116 LEU A O   
8779  C CB  . LEU D 100 ? 1.2473 1.3419 1.0064 -0.1543 0.0801  -0.0631 116 LEU A CB  
8780  C CG  . LEU D 100 ? 1.1740 1.2627 0.9531 -0.1408 0.0769  -0.0544 116 LEU A CG  
8781  C CD1 . LEU D 100 ? 1.0887 1.1925 0.8773 -0.1398 0.0861  -0.0661 116 LEU A CD1 
8782  C CD2 . LEU D 100 ? 1.1696 1.2376 0.9458 -0.1477 0.0673  -0.0323 116 LEU A CD2 
8783  N N   . ASN D 101 ? 1.2066 1.3148 0.9776 -0.1264 0.0792  -0.0883 117 ASN A N   
8784  C CA  . ASN D 101 ? 1.2120 1.3201 0.9968 -0.1072 0.0759  -0.0932 117 ASN A CA  
8785  C C   . ASN D 101 ? 1.2033 1.3313 0.9942 -0.0993 0.0832  -0.1171 117 ASN A C   
8786  O O   . ASN D 101 ? 1.1640 1.2953 0.9704 -0.0814 0.0827  -0.1224 117 ASN A O   
8787  C CB  . ASN D 101 ? 1.3043 1.3993 1.0823 -0.1083 0.0676  -0.0856 117 ASN A CB  
8788  C CG  . ASN D 101 ? 1.3201 1.3949 1.0973 -0.1108 0.0586  -0.0622 117 ASN A CG  
8789  O OD1 . ASN D 101 ? 1.2910 1.3609 1.0768 -0.1074 0.0575  -0.0518 117 ASN A OD1 
8790  N ND2 . ASN D 101 ? 1.4724 1.5364 1.2402 -0.1164 0.0518  -0.0551 117 ASN A ND2 
8791  N N   . THR D 102 ? 1.2428 1.3850 1.0218 -0.1125 0.0901  -0.1318 118 THR A N   
8792  C CA  . THR D 102 ? 1.1694 1.3328 0.9550 -0.1058 0.0974  -0.1564 118 THR A CA  
8793  C C   . THR D 102 ? 1.0907 1.2642 0.8903 -0.0967 0.1031  -0.1620 118 THR A C   
8794  O O   . THR D 102 ? 1.0707 1.2517 0.8850 -0.0791 0.1034  -0.1728 118 THR A O   
8795  C CB  . THR D 102 ? 1.1871 1.3657 0.9568 -0.1242 0.1044  -0.1708 118 THR A CB  
8796  O OG1 . THR D 102 ? 1.2627 1.4351 1.0206 -0.1309 0.0991  -0.1691 118 THR A OG1 
8797  C CG2 . THR D 102 ? 1.0633 1.2657 0.8418 -0.1171 0.1122  -0.1976 118 THR A CG2 
8798  N N   . ILE D 103 ? 1.0843 1.2590 0.8792 -0.1091 0.1077  -0.1559 119 ILE A N   
8799  C CA  . ILE D 103 ? 1.0322 1.2166 0.8411 -0.1014 0.1131  -0.1610 119 ILE A CA  
8800  C C   . ILE D 103 ? 1.0491 1.2253 0.8752 -0.0805 0.1070  -0.1526 119 ILE A C   
8801  O O   . ILE D 103 ? 1.0504 1.2389 0.8909 -0.0655 0.1100  -0.1646 119 ILE A O   
8802  C CB  . ILE D 103 ? 1.0551 1.2353 0.8577 -0.1174 0.1161  -0.1499 119 ILE A CB  
8803  C CG1 . ILE D 103 ? 1.0624 1.2545 0.8489 -0.1383 0.1241  -0.1600 119 ILE A CG1 
8804  C CG2 . ILE D 103 ? 1.1017 1.2888 0.9216 -0.1074 0.1196  -0.1522 119 ILE A CG2 
8805  C CD1 . ILE D 103 ? 1.1141 1.2940 0.8909 -0.1551 0.1233  -0.1430 119 ILE A CD1 
8806  N N   . LEU D 104 ? 1.0654 1.2216 0.8902 -0.0798 0.0984  -0.1316 120 LEU A N   
8807  C CA  . LEU D 104 ? 1.0929 1.2419 0.9334 -0.0619 0.0928  -0.1220 120 LEU A CA  
8808  C C   . LEU D 104 ? 1.0381 1.1936 0.8871 -0.0446 0.0917  -0.1343 120 LEU A C   
8809  O O   . LEU D 104 ? 0.9675 1.1306 0.8307 -0.0290 0.0927  -0.1391 120 LEU A O   
8810  C CB  . LEU D 104 ? 1.0762 1.2037 0.9127 -0.0652 0.0835  -0.0994 120 LEU A CB  
8811  C CG  . LEU D 104 ? 0.9871 1.1026 0.8177 -0.0789 0.0808  -0.0826 120 LEU A CG  
8812  C CD1 . LEU D 104 ? 1.0796 1.1761 0.9064 -0.0792 0.0708  -0.0651 120 LEU A CD1 
8813  C CD2 . LEU D 104 ? 0.9142 1.0325 0.7588 -0.0736 0.0822  -0.0782 120 LEU A CD2 
8814  N N   . ASN D 105 ? 1.0788 1.2316 0.9192 -0.0474 0.0892  -0.1398 121 ASN A N   
8815  C CA  . ASN D 105 ? 1.0274 1.1845 0.8756 -0.0319 0.0869  -0.1519 121 ASN A CA  
8816  C C   . ASN D 105 ? 0.9668 1.1451 0.8235 -0.0239 0.0941  -0.1738 121 ASN A C   
8817  O O   . ASN D 105 ? 0.9564 1.1383 0.8255 -0.0060 0.0920  -0.1795 121 ASN A O   
8818  C CB  . ASN D 105 ? 1.0877 1.2404 0.9253 -0.0388 0.0836  -0.1570 121 ASN A CB  
8819  C CG  . ASN D 105 ? 1.1816 1.3141 1.0194 -0.0342 0.0740  -0.1403 121 ASN A CG  
8820  O OD1 . ASN D 105 ? 1.2569 1.3857 1.1034 -0.0199 0.0693  -0.1432 121 ASN A OD1 
8821  N ND2 . ASN D 105 ? 1.2947 1.4136 1.1233 -0.0463 0.0705  -0.1226 121 ASN A ND2 
8822  N N   . THR D 106 ? 0.9515 1.1443 0.8015 -0.0373 0.1024  -0.1862 122 THR A N   
8823  C CA  . THR D 106 ? 0.9649 1.1801 0.8230 -0.0312 0.1099  -0.2092 122 THR A CA  
8824  C C   . THR D 106 ? 0.9416 1.1618 0.8144 -0.0183 0.1115  -0.2070 122 THR A C   
8825  O O   . THR D 106 ? 0.8623 1.0926 0.7472 -0.0014 0.1114  -0.2194 122 THR A O   
8826  C CB  . THR D 106 ? 0.8991 1.1287 0.7462 -0.0508 0.1190  -0.2211 122 THR A CB  
8827  O OG1 . THR D 106 ? 0.8995 1.1280 0.7331 -0.0621 0.1179  -0.2259 122 THR A OG1 
8828  C CG2 . THR D 106 ? 0.8338 1.0878 0.6912 -0.0440 0.1269  -0.2456 122 THR A CG2 
8829  N N   . MET D 107 ? 0.9070 1.1213 0.7793 -0.0263 0.1129  -0.1923 123 MET A N   
8830  C CA  . MET D 107 ? 0.8421 1.0599 0.7289 -0.0142 0.1134  -0.1881 123 MET A CA  
8831  C C   . MET D 107 ? 0.8654 1.0761 0.7625 0.0062  0.1058  -0.1812 123 MET A C   
8832  O O   . MET D 107 ? 0.8925 1.1147 0.8022 0.0218  0.1070  -0.1900 123 MET A O   
8833  C CB  . MET D 107 ? 0.8386 1.0462 0.7232 -0.0260 0.1132  -0.1701 123 MET A CB  
8834  C CG  . MET D 107 ? 0.8522 1.0676 0.7285 -0.0456 0.1212  -0.1763 123 MET A CG  
8835  S SD  . MET D 107 ? 0.8288 1.0343 0.7080 -0.0561 0.1208  -0.1584 123 MET A SD  
8836  C CE  . MET D 107 ? 0.9792 1.1579 0.8478 -0.0625 0.1099  -0.1328 123 MET A CE  
8837  N N   . SER D 108 ? 0.8893 1.0813 0.7808 0.0061  0.0979  -0.1658 124 SER A N   
8838  C CA  . SER D 108 ? 0.8600 1.0440 0.7600 0.0236  0.0907  -0.1576 124 SER A CA  
8839  C C   . SER D 108 ? 0.8606 1.0547 0.7663 0.0381  0.0904  -0.1753 124 SER A C   
8840  O O   . SER D 108 ? 0.8667 1.0666 0.7837 0.0547  0.0890  -0.1773 124 SER A O   
8841  C CB  . SER D 108 ? 0.9148 1.0777 0.8071 0.0189  0.0829  -0.1401 124 SER A CB  
8842  O OG  . SER D 108 ? 0.8888 1.0435 0.7889 0.0341  0.0762  -0.1310 124 SER A OG  
8843  N N   . THR D 109 ? 0.8618 1.0590 0.7603 0.0323  0.0913  -0.1892 125 THR A N   
8844  C CA  . THR D 109 ? 0.8859 1.0913 0.7910 0.0469  0.0893  -0.2065 125 THR A CA  
8845  C C   . THR D 109 ? 0.8709 1.0991 0.7852 0.0538  0.0963  -0.2259 125 THR A C   
8846  O O   . THR D 109 ? 0.8777 1.1125 0.8014 0.0709  0.0936  -0.2363 125 THR A O   
8847  C CB  . THR D 109 ? 0.8695 1.0730 0.7666 0.0401  0.0875  -0.2175 125 THR A CB  
8848  O OG1 . THR D 109 ? 0.8421 1.0632 0.7340 0.0273  0.0960  -0.2355 125 THR A OG1 
8849  C CG2 . THR D 109 ? 0.8813 1.0636 0.7680 0.0294  0.0817  -0.1983 125 THR A CG2 
8850  N N   . ILE D 110 ? 0.9078 1.1475 0.8201 0.0414  0.1048  -0.2303 126 ILE A N   
8851  C CA  . ILE D 110 ? 0.9120 1.1645 0.8376 0.0464  0.1076  -0.2390 126 ILE A CA  
8852  C C   . ILE D 110 ? 0.8633 1.1153 0.8005 0.0631  0.1044  -0.2307 126 ILE A C   
8853  O O   . ILE D 110 ? 0.8910 1.1437 0.8390 0.0769  0.0989  -0.2341 126 ILE A O   
8854  C CB  . ILE D 110 ? 0.8711 1.1304 0.7947 0.0288  0.1149  -0.2395 126 ILE A CB  
8855  C CG1 . ILE D 110 ? 0.8539 1.1170 0.7689 0.0127  0.1177  -0.2490 126 ILE A CG1 
8856  C CG2 . ILE D 110 ? 0.9016 1.1683 0.8413 0.0350  0.1148  -0.2416 126 ILE A CG2 
8857  C CD1 . ILE D 110 ? 0.8529 1.1233 0.7660 -0.0044 0.1248  -0.2498 126 ILE A CD1 
8858  N N   . TYR D 111 ? 0.7818 1.0334 0.7168 0.0612  0.1076  -0.2196 127 TYR A N   
8859  C CA  . TYR D 111 ? 0.7597 1.0126 0.7064 0.0763  0.1047  -0.2108 127 TYR A CA  
8860  C C   . TYR D 111 ? 0.8530 1.1007 0.8031 0.0946  0.0970  -0.2096 127 TYR A C   
8861  O O   . TYR D 111 ? 0.8124 1.0623 0.7738 0.1070  0.0931  -0.2082 127 TYR A O   
8862  C CB  . TYR D 111 ? 0.7293 0.9682 0.6745 0.0692  0.1024  -0.1878 127 TYR A CB  
8863  C CG  . TYR D 111 ? 0.6637 0.9067 0.6212 0.0823  0.1005  -0.1788 127 TYR A CG  
8864  C CD1 . TYR D 111 ? 0.6708 0.9277 0.6378 0.0816  0.1061  -0.1835 127 TYR A CD1 
8865  C CD2 . TYR D 111 ? 0.6988 0.9329 0.6588 0.0955  0.0931  -0.1667 127 TYR A CD2 
8866  C CE1 . TYR D 111 ? 0.6811 0.9439 0.6601 0.0938  0.1044  -0.1765 127 TYR A CE1 
8867  C CE2 . TYR D 111 ? 0.6153 0.8554 0.5858 0.1071  0.0917  -0.1590 127 TYR A CE2 
8868  C CZ  . TYR D 111 ? 0.6917 0.9468 0.6719 0.1065  0.0973  -0.1644 127 TYR A CZ  
8869  O OH  . TYR D 111 ? 0.6813 0.9448 0.6728 0.1180  0.0961  -0.1584 127 TYR A OH  
8870  N N   . SER D 112 ? 0.8239 1.0543 0.7659 0.0924  0.0906  -0.2015 128 SER A N   
8871  C CA  . SER D 112 ? 0.8561 1.0788 0.8017 0.1092  0.0824  -0.1976 128 SER A CA  
8872  C C   . SER D 112 ? 0.8901 1.1243 0.8400 0.1208  0.0816  -0.2200 128 SER A C   
8873  O O   . SER D 112 ? 0.9556 1.1893 0.9126 0.1370  0.0758  -0.2191 128 SER A O   
8874  C CB  . SER D 112 ? 0.8668 1.0669 0.8044 0.1041  0.0752  -0.1814 128 SER A CB  
8875  O OG  . SER D 112 ? 0.9273 1.1251 0.8571 0.0940  0.0757  -0.1922 128 SER A OG  
8876  N N   . THR D 113 ? 0.9107 1.1484 0.8584 0.1093  0.0839  -0.2330 129 THR A N   
8877  C CA  . THR D 113 ? 0.9332 1.1724 0.8887 0.1155  0.0785  -0.2447 129 THR A CA  
8878  C C   . THR D 113 ? 0.9697 1.2191 0.9336 0.1074  0.0815  -0.2513 129 THR A C   
8879  O O   . THR D 113 ? 0.9942 1.2476 0.9645 0.1096  0.0779  -0.2624 129 THR A O   
8880  C CB  . THR D 113 ? 0.9193 1.1538 0.8680 0.1114  0.0761  -0.2552 129 THR A CB  
8881  O OG1 . THR D 113 ? 0.8216 1.0622 0.7646 0.0920  0.0827  -0.2611 129 THR A OG1 
8882  C CG2 . THR D 113 ? 0.9530 1.1733 0.8922 0.1156  0.0722  -0.2454 129 THR A CG2 
8883  N N   . GLY D 114 ? 0.9958 1.0665 0.9653 -0.0333 0.2307  -0.2018 130 GLY A N   
8884  C CA  . GLY D 114 ? 1.0317 1.1183 1.0053 -0.0324 0.2257  -0.1917 130 GLY A CA  
8885  C C   . GLY D 114 ? 1.0826 1.1679 1.0771 -0.0129 0.2291  -0.1860 130 GLY A C   
8886  O O   . GLY D 114 ? 1.0687 1.1380 1.0674 -0.0024 0.2232  -0.1811 130 GLY A O   
8887  N N   . LYS D 115 ? 1.1144 1.2182 1.1226 -0.0076 0.2388  -0.1862 131 LYS A N   
8888  C CA  . LYS D 115 ? 1.1324 1.2392 1.1612 0.0117  0.2424  -0.1799 131 LYS A CA  
8889  C C   . LYS D 115 ? 1.1300 1.2618 1.1660 0.0112  0.2397  -0.1737 131 LYS A C   
8890  O O   . LYS D 115 ? 1.1270 1.2747 1.1585 -0.0010 0.2440  -0.1781 131 LYS A O   
8891  C CB  . LYS D 115 ? 1.2493 1.3509 1.2962 0.0250  0.2625  -0.1883 131 LYS A CB  
8892  C CG  . LYS D 115 ? 1.2962 1.4105 1.3477 0.0186  0.2798  -0.2011 131 LYS A CG  
8893  C CD  . LYS D 115 ? 1.3665 1.4752 1.4423 0.0355  0.3003  -0.2073 131 LYS A CD  
8894  C CE  . LYS D 115 ? 1.3592 1.4403 1.4348 0.0393  0.3052  -0.2135 131 LYS A CE  
8895  N NZ  . LYS D 115 ? 1.1711 1.2443 1.2305 0.0221  0.3060  -0.2268 131 LYS A NZ  
8896  N N   . VAL D 116 ? 1.1487 1.2853 1.1955 0.0240  0.2322  -0.1635 132 VAL A N   
8897  C CA  . VAL D 116 ? 1.1408 1.3032 1.1974 0.0253  0.2287  -0.1575 132 VAL A CA  
8898  C C   . VAL D 116 ? 1.2190 1.3917 1.2988 0.0466  0.2379  -0.1537 132 VAL A C   
8899  O O   . VAL D 116 ? 1.2404 1.3987 1.3257 0.0608  0.2385  -0.1498 132 VAL A O   
8900  C CB  . VAL D 116 ? 1.0652 1.2299 1.1132 0.0190  0.2090  -0.1486 132 VAL A CB  
8901  C CG1 . VAL D 116 ? 1.1153 1.2726 1.1433 -0.0013 0.2005  -0.1499 132 VAL A CG1 
8902  C CG2 . VAL D 116 ? 1.0423 1.1903 1.0907 0.0312  0.2005  -0.1428 132 VAL A CG2 
8903  N N   . CYS D 117 ? 1.2751 1.4741 1.3693 0.0489  0.2447  -0.1537 133 CYS A N   
8904  C CA  . CYS D 117 ? 1.4509 1.6632 1.5695 0.0696  0.2548  -0.1495 133 CYS A CA  
8905  C C   . CYS D 117 ? 1.4585 1.6971 1.5860 0.0747  0.2434  -0.1400 133 CYS A C   
8906  O O   . CYS D 117 ? 1.3708 1.6239 1.4912 0.0601  0.2340  -0.1403 133 CYS A O   
8907  C CB  . CYS D 117 ? 1.5802 1.8028 1.7128 0.0711  0.2746  -0.1585 133 CYS A CB  
8908  S SG  . CYS D 117 ? 1.5841 1.7827 1.7028 0.0582  0.2869  -0.1737 133 CYS A SG  
8909  N N   . ASN D 118 ? 1.5392 1.7843 1.6826 0.0952  0.2444  -0.1314 134 ASN A N   
8910  C CA  . ASN D 118 ? 1.6519 1.9239 1.8036 0.1013  0.2328  -0.1226 134 ASN A CA  
8911  C C   . ASN D 118 ? 1.8436 2.1480 2.0092 0.0968  0.2377  -0.1253 134 ASN A C   
8912  O O   . ASN D 118 ? 1.9016 2.2117 2.0812 0.1020  0.2544  -0.1297 134 ASN A O   
8913  C CB  . ASN D 118 ? 1.7492 2.0250 1.9157 0.1256  0.2347  -0.1118 134 ASN A CB  
8914  C CG  . ASN D 118 ? 1.8490 2.1343 2.0401 0.1427  0.2539  -0.1103 134 ASN A CG  
8915  O OD1 . ASN D 118 ? 1.8132 2.1297 2.0232 0.1526  0.2556  -0.1049 134 ASN A OD1 
8916  N ND2 . ASN D 118 ? 1.8870 2.1455 2.0793 0.1464  0.2687  -0.1154 134 ASN A ND2 
8917  N N   . PRO D 119 ? 1.5716 1.8980 1.7356 0.0875  0.2246  -0.1233 135 PRO A N   
8918  C CA  . PRO D 119 ? 1.4671 1.8242 1.6436 0.0803  0.2293  -0.1269 135 PRO A CA  
8919  C C   . PRO D 119 ? 1.5564 1.9405 1.7603 0.1013  0.2384  -0.1215 135 PRO A C   
8920  O O   . PRO D 119 ? 1.4310 1.8486 1.6493 0.1000  0.2372  -0.1211 135 PRO A O   
8921  C CB  . PRO D 119 ? 1.1828 1.5546 1.3520 0.0665  0.2115  -0.1253 135 PRO A CB  
8922  C CG  . PRO D 119 ? 1.3727 1.7342 1.5362 0.0765  0.1993  -0.1186 135 PRO A CG  
8923  C CD  . PRO D 119 ? 1.4465 1.7726 1.5996 0.0834  0.2056  -0.1186 135 PRO A CD  
8924  N N   . ASP D 120 ? 1.6440 2.0143 1.8564 0.1211  0.2471  -0.1165 136 ASP A N   
8925  C CA  . ASP D 120 ? 1.6426 2.0359 1.8821 0.1438  0.2560  -0.1086 136 ASP A CA  
8926  C C   . ASP D 120 ? 1.5975 1.9719 1.8498 0.1574  0.2766  -0.1102 136 ASP A C   
8927  O O   . ASP D 120 ? 1.7063 2.0968 1.9833 0.1780  0.2859  -0.1024 136 ASP A O   
8928  C CB  . ASP D 120 ? 1.5883 1.9910 1.8298 0.1590  0.2430  -0.0957 136 ASP A CB  
8929  C CG  . ASP D 120 ? 1.5669 1.9810 1.7934 0.1444  0.2228  -0.0964 136 ASP A CG  
8930  O OD1 . ASP D 120 ? 1.6013 2.0434 1.8340 0.1337  0.2185  -0.1003 136 ASP A OD1 
8931  O OD2 . ASP D 120 ? 1.5446 1.9383 1.7536 0.1420  0.2120  -0.0944 136 ASP A OD2 
8932  N N   . ASN D 121 ? 1.7350 2.0773 1.9727 0.1468  0.2844  -0.1201 137 ASN A N   
8933  C CA  . ASN D 121 ? 1.8539 2.1747 2.1038 0.1603  0.3033  -0.1220 137 ASN A CA  
8934  C C   . ASN D 121 ? 2.0184 2.3080 2.2466 0.1421  0.3072  -0.1355 137 ASN A C   
8935  O O   . ASN D 121 ? 2.1467 2.4077 2.3616 0.1427  0.3037  -0.1344 137 ASN A O   
8936  C CB  . ASN D 121 ? 1.8647 2.1760 2.1212 0.1819  0.3005  -0.1077 137 ASN A CB  
8937  C CG  . ASN D 121 ? 1.8654 2.1635 2.1443 0.2010  0.3207  -0.1053 137 ASN A CG  
8938  O OD1 . ASN D 121 ? 1.8476 2.1452 2.1344 0.1973  0.3299  -0.1138 137 ASN A OD1 
8939  N ND2 . ASN D 121 ? 1.7614 2.0474 2.0420 0.2164  0.3149  -0.0922 137 ASN A ND2 
8940  N N   . PRO D 122 ? 2.1422 2.4389 2.3655 0.1248  0.3138  -0.1481 138 PRO A N   
8941  C CA  . PRO D 122 ? 2.1713 2.4468 2.3679 0.1025  0.3112  -0.1596 138 PRO A CA  
8942  C C   . PRO D 122 ? 2.2363 2.4788 2.4287 0.1047  0.3231  -0.1675 138 PRO A C   
8943  O O   . PRO D 122 ? 2.2102 2.4438 2.3948 0.0919  0.3337  -0.1816 138 PRO A O   
8944  C CB  . PRO D 122 ? 2.0667 2.3639 2.2651 0.0881  0.3193  -0.1696 138 PRO A CB  
8945  C CG  . PRO D 122 ? 2.0494 2.3806 2.2682 0.0975  0.3165  -0.1613 138 PRO A CG  
8946  C CD  . PRO D 122 ? 2.0554 2.3857 2.2958 0.1238  0.3202  -0.1505 138 PRO A CD  
8947  N N   . GLN D 123 ? 2.9458 3.1712 3.1429 0.1206  0.3208  -0.1584 139 GLN A N   
8948  C CA  . GLN D 123 ? 2.9061 3.1040 3.1075 0.1296  0.3295  -0.1597 139 GLN A CA  
8949  C C   . GLN D 123 ? 2.9280 3.1011 3.1202 0.1355  0.3217  -0.1530 139 GLN A C   
8950  O O   . GLN D 123 ? 2.9503 3.0995 3.1250 0.1236  0.3196  -0.1609 139 GLN A O   
8951  C CB  . GLN D 123 ? 2.8602 3.0662 3.0857 0.1488  0.3362  -0.1514 139 GLN A CB  
8952  C CG  . GLN D 123 ? 2.9432 3.1721 3.1870 0.1681  0.3321  -0.1357 139 GLN A CG  
8953  C CD  . GLN D 123 ? 3.0640 3.2769 3.3198 0.1861  0.3330  -0.1253 139 GLN A CD  
8954  O OE1 . GLN D 123 ? 3.0803 3.2625 3.3266 0.1821  0.3341  -0.1293 139 GLN A OE1 
8955  N NE2 . GLN D 123 ? 3.1856 3.4193 3.4639 0.2040  0.3338  -0.1135 139 GLN A NE2 
8956  N N   . GLU D 124 ? 2.3576 2.5354 2.5624 0.1546  0.3181  -0.1383 140 GLU A N   
8957  C CA  . GLU D 124 ? 2.1030 2.2706 2.2984 0.1591  0.3085  -0.1302 140 GLU A CA  
8958  C C   . GLU D 124 ? 1.9005 2.0713 2.0698 0.1369  0.2903  -0.1352 140 GLU A C   
8959  O O   . GLU D 124 ? 1.7248 1.9184 1.8907 0.1334  0.2767  -0.1293 140 GLU A O   
8960  C CB  . GLU D 124 ? 2.0146 2.2033 2.2248 0.1792  0.3030  -0.1128 140 GLU A CB  
8961  C CG  . GLU D 124 ? 1.8365 2.0246 2.0313 0.1799  0.2837  -0.1029 140 GLU A CG  
8962  C CD  . GLU D 124 ? 1.8840 2.1014 2.0929 0.1973  0.2780  -0.0876 140 GLU A CD  
8963  O OE1 . GLU D 124 ? 1.9348 2.1803 2.1592 0.2004  0.2819  -0.0871 140 GLU A OE1 
8964  O OE2 . GLU D 124 ? 1.9077 2.1220 2.1125 0.2078  0.2698  -0.0764 140 GLU A OE2 
8965  N N   . CYS D 125 ? 1.7956 1.9459 1.9489 0.1209  0.2923  -0.1474 141 CYS A N   
8966  C CA  . CYS D 125 ? 1.5507 1.6973 1.6788 0.1006  0.2760  -0.1509 141 CYS A CA  
8967  C C   . CYS D 125 ? 1.4061 1.5276 1.5225 0.1028  0.2669  -0.1470 141 CYS A C   
8968  O O   . CYS D 125 ? 1.4505 1.5555 1.5767 0.1164  0.2761  -0.1449 141 CYS A O   
8969  C CB  . CYS D 125 ? 1.5312 1.6734 1.6480 0.0819  0.2831  -0.1657 141 CYS A CB  
8970  S SG  . CYS D 125 ? 1.7538 1.9218 1.8871 0.0801  0.3007  -0.1743 141 CYS A SG  
8971  N N   . LEU D 126 ? 1.2687 1.3873 1.3654 0.0891  0.2495  -0.1458 142 LEU A N   
8972  C CA  . LEU D 126 ? 1.2413 1.3372 1.3256 0.0885  0.2396  -0.1433 142 LEU A CA  
8973  C C   . LEU D 126 ? 1.1477 1.2303 1.2128 0.0685  0.2352  -0.1529 142 LEU A C   
8974  O O   . LEU D 126 ? 1.2240 1.3192 1.2795 0.0536  0.2295  -0.1555 142 LEU A O   
8975  C CB  . LEU D 126 ? 1.1425 1.2481 1.2228 0.0918  0.2222  -0.1326 142 LEU A CB  
8976  C CG  . LEU D 126 ? 1.1108 1.2340 1.2109 0.1122  0.2283  -0.1233 142 LEU A CG  
8977  C CD1 . LEU D 126 ? 1.0529 1.1933 1.1511 0.1156  0.2125  -0.1142 142 LEU A CD1 
8978  C CD2 . LEU D 126 ? 1.2791 1.3843 1.3903 0.1292  0.2413  -0.1202 142 LEU A CD2 
8979  N N   . LEU D 127 ? 1.0619 1.1211 1.1230 0.0685  0.2397  -0.1584 143 LEU A N   
8980  C CA  . LEU D 127 ? 1.0295 1.0755 1.0712 0.0518  0.2308  -0.1643 143 LEU A CA  
8981  C C   . LEU D 127 ? 1.0001 1.0404 1.0316 0.0506  0.2116  -0.1550 143 LEU A C   
8982  O O   . LEU D 127 ? 1.0345 1.0782 1.0739 0.0635  0.2075  -0.1462 143 LEU A O   
8983  C CB  . LEU D 127 ? 1.0672 1.0918 1.1102 0.0528  0.2417  -0.1737 143 LEU A CB  
8984  C CG  . LEU D 127 ? 1.0527 1.0777 1.1053 0.0519  0.2620  -0.1867 143 LEU A CG  
8985  C CD1 . LEU D 127 ? 1.1551 1.1573 1.2062 0.0498  0.2683  -0.1965 143 LEU A CD1 
8986  C CD2 . LEU D 127 ? 1.0608 1.1028 1.1029 0.0353  0.2624  -0.1942 143 LEU A CD2 
8987  N N   . LEU D 128 ? 0.9649 0.9976 0.9794 0.0353  0.1998  -0.1569 144 LEU A N   
8988  C CA  . LEU D 128 ? 0.9660 0.9904 0.9731 0.0348  0.1830  -0.1494 144 LEU A CA  
8989  C C   . LEU D 128 ? 1.0444 1.0518 1.0581 0.0490  0.1853  -0.1474 144 LEU A C   
8990  O O   . LEU D 128 ? 1.0205 1.0285 1.0369 0.0576  0.1772  -0.1397 144 LEU A O   
8991  C CB  . LEU D 128 ? 0.9266 0.9433 0.9165 0.0174  0.1714  -0.1511 144 LEU A CB  
8992  C CG  . LEU D 128 ? 0.8957 0.9017 0.8797 0.0165  0.1548  -0.1443 144 LEU A CG  
8993  C CD1 . LEU D 128 ? 0.9223 0.9427 0.9104 0.0182  0.1467  -0.1372 144 LEU A CD1 
8994  C CD2 . LEU D 128 ? 0.8579 0.8566 0.8270 0.0005  0.1445  -0.1447 144 LEU A CD2 
8995  N N   . GLU D 129 ? 1.0571 1.0502 1.0740 0.0512  0.1972  -0.1548 145 GLU A N   
8996  C CA  . GLU D 129 ? 1.0531 1.0300 1.0793 0.0651  0.2040  -0.1536 145 GLU A CA  
8997  C C   . GLU D 129 ? 1.0624 1.0401 1.1050 0.0759  0.2244  -0.1574 145 GLU A C   
8998  O O   . GLU D 129 ? 1.1169 1.0942 1.1598 0.0678  0.2348  -0.1682 145 GLU A O   
8999  C CB  . GLU D 129 ? 1.0525 1.0095 1.0701 0.0573  0.2004  -0.1598 145 GLU A CB  
9000  C CG  . GLU D 129 ? 1.1475 1.0868 1.1752 0.0699  0.2090  -0.1597 145 GLU A CG  
9001  C CD  . GLU D 129 ? 1.1408 1.0798 1.1730 0.0839  0.2031  -0.1478 145 GLU A CD  
9002  O OE1 . GLU D 129 ? 1.1119 1.0591 1.1360 0.0810  0.1878  -0.1417 145 GLU A OE1 
9003  O OE2 . GLU D 129 ? 1.2020 1.1328 1.2463 0.0979  0.2147  -0.1448 145 GLU A OE2 
9004  N N   . PRO D 130 ? 1.0572 1.0361 1.1145 0.0942  0.2315  -0.1489 146 PRO A N   
9005  C CA  . PRO D 130 ? 1.0263 1.0057 1.0843 0.1058  0.2223  -0.1369 146 PRO A CA  
9006  C C   . PRO D 130 ? 1.0114 1.0156 1.0725 0.1117  0.2153  -0.1276 146 PRO A C   
9007  O O   . PRO D 130 ? 1.0164 1.0248 1.0796 0.1229  0.2096  -0.1180 146 PRO A O   
9008  C CB  . PRO D 130 ? 1.0179 0.9848 1.0916 0.1225  0.2382  -0.1335 146 PRO A CB  
9009  C CG  . PRO D 130 ? 1.0359 1.0092 1.1228 0.1247  0.2546  -0.1387 146 PRO A CG  
9010  C CD  . PRO D 130 ? 1.0956 1.0711 1.1710 0.1051  0.2524  -0.1520 146 PRO A CD  
9011  N N   . GLY D 131 ? 1.0227 1.0445 1.0845 0.1041  0.2163  -0.1309 147 GLY A N   
9012  C CA  . GLY D 131 ? 1.0408 1.0886 1.1103 0.1111  0.2134  -0.1233 147 GLY A CA  
9013  C C   . GLY D 131 ? 0.9723 1.0334 1.0314 0.1032  0.1946  -0.1194 147 GLY A C   
9014  O O   . GLY D 131 ? 0.9457 1.0166 1.0076 0.1131  0.1876  -0.1113 147 GLY A O   
9015  N N   . LEU D 132 ? 0.9846 1.0470 1.0322 0.0849  0.1869  -0.1254 148 LEU A N   
9016  C CA  . LEU D 132 ? 0.9495 1.0233 0.9893 0.0756  0.1703  -0.1225 148 LEU A CA  
9017  C C   . LEU D 132 ? 0.9565 1.0146 0.9877 0.0759  0.1582  -0.1201 148 LEU A C   
9018  O O   . LEU D 132 ? 0.9527 1.0218 0.9842 0.0785  0.1477  -0.1157 148 LEU A O   
9019  C CB  . LEU D 132 ? 0.8230 0.8992 0.8526 0.0557  0.1660  -0.1279 148 LEU A CB  
9020  C CG  . LEU D 132 ? 0.8221 0.9142 0.8567 0.0503  0.1769  -0.1322 148 LEU A CG  
9021  C CD1 . LEU D 132 ? 0.7325 0.8249 0.7536 0.0301  0.1699  -0.1352 148 LEU A CD1 
9022  C CD2 . LEU D 132 ? 0.9169 1.0357 0.9663 0.0596  0.1800  -0.1279 148 LEU A CD2 
9023  N N   . ASN D 133 ? 0.9517 0.9856 0.9758 0.0727  0.1594  -0.1238 149 ASN A N   
9024  C CA  . ASN D 133 ? 0.9733 0.9918 0.9912 0.0743  0.1494  -0.1219 149 ASN A CA  
9025  C C   . ASN D 133 ? 0.9524 0.9776 0.9782 0.0916  0.1506  -0.1150 149 ASN A C   
9026  O O   . ASN D 133 ? 0.8949 0.9211 0.9168 0.0927  0.1393  -0.1125 149 ASN A O   
9027  C CB  . ASN D 133 ? 0.9425 0.9365 0.9553 0.0709  0.1538  -0.1272 149 ASN A CB  
9028  C CG  . ASN D 133 ? 0.8822 0.8699 0.8833 0.0526  0.1466  -0.1322 149 ASN A CG  
9029  O OD1 . ASN D 133 ? 0.7947 0.7910 0.7902 0.0422  0.1359  -0.1303 149 ASN A OD1 
9030  N ND2 . ASN D 133 ? 0.9649 0.9389 0.9629 0.0483  0.1533  -0.1384 149 ASN A ND2 
9031  N N   . GLU D 134 ? 1.0307 1.0623 1.0681 0.1055  0.1644  -0.1117 150 GLU A N   
9032  C CA  . GLU D 134 ? 1.0413 1.0810 1.0862 0.1232  0.1666  -0.1029 150 GLU A CA  
9033  C C   . GLU D 134 ? 0.9702 1.0376 1.0160 0.1242  0.1557  -0.0987 150 GLU A C   
9034  O O   . GLU D 134 ? 0.9951 1.0687 1.0387 0.1310  0.1481  -0.0943 150 GLU A O   
9035  C CB  . GLU D 134 ? 1.0688 1.1076 1.1278 0.1375  0.1850  -0.0994 150 GLU A CB  
9036  C CG  . GLU D 134 ? 1.1450 1.1881 1.2125 0.1574  0.1903  -0.0882 150 GLU A CG  
9037  C CD  . GLU D 134 ? 1.2066 1.2813 1.2796 0.1661  0.1850  -0.0799 150 GLU A CD  
9038  O OE1 . GLU D 134 ? 1.2023 1.2953 1.2801 0.1607  0.1847  -0.0824 150 GLU A OE1 
9039  O OE2 . GLU D 134 ? 1.2536 1.3361 1.3254 0.1771  0.1803  -0.0715 150 GLU A OE2 
9040  N N   . ILE D 135 ? 0.9308 1.0155 0.9792 0.1156  0.1545  -0.1014 151 ILE A N   
9041  C CA  . ILE D 135 ? 0.9130 1.0248 0.9630 0.1129  0.1437  -0.0998 151 ILE A CA  
9042  C C   . ILE D 135 ? 0.8637 0.9685 0.9024 0.1010  0.1279  -0.1036 151 ILE A C   
9043  O O   . ILE D 135 ? 0.8795 0.9947 0.9176 0.1066  0.1199  -0.1013 151 ILE A O   
9044  C CB  . ILE D 135 ? 0.9023 1.0326 0.9582 0.1043  0.1467  -0.1027 151 ILE A CB  
9045  C CG1 . ILE D 135 ? 0.8997 1.0422 0.9706 0.1183  0.1622  -0.0986 151 ILE A CG1 
9046  C CG2 . ILE D 135 ? 0.7748 0.9287 0.8306 0.0960  0.1337  -0.1036 151 ILE A CG2 
9047  C CD1 . ILE D 135 ? 0.8572 1.0177 0.9347 0.1099  0.1668  -0.1025 151 ILE A CD1 
9048  N N   . MET D 136 ? 0.8845 0.9731 0.9147 0.0844  0.1235  -0.1096 152 MET A N   
9049  C CA  . MET D 136 ? 0.8445 0.9260 0.8667 0.0726  0.1092  -0.1128 152 MET A CA  
9050  C C   . MET D 136 ? 0.8350 0.9039 0.8535 0.0808  0.1047  -0.1119 152 MET A C   
9051  O O   . MET D 136 ? 0.7526 0.8248 0.7688 0.0765  0.0936  -0.1141 152 MET A O   
9052  C CB  . MET D 136 ? 0.8267 0.8887 0.8404 0.0564  0.1068  -0.1168 152 MET A CB  
9053  C CG  . MET D 136 ? 0.8051 0.8779 0.8199 0.0465  0.1113  -0.1180 152 MET A CG  
9054  S SD  . MET D 136 ? 0.7471 0.8500 0.7692 0.0400  0.1049  -0.1178 152 MET A SD  
9055  C CE  . MET D 136 ? 0.8399 0.9300 0.8553 0.0252  0.0889  -0.1200 152 MET A CE  
9056  N N   . ALA D 137 ? 0.8604 0.9146 0.8793 0.0920  0.1139  -0.1093 153 ALA A N   
9057  C CA  . ALA D 137 ? 0.8343 0.8770 0.8499 0.0998  0.1109  -0.1081 153 ALA A CA  
9058  C C   . ALA D 137 ? 0.8368 0.9019 0.8569 0.1141  0.1107  -0.1025 153 ALA A C   
9059  O O   . ALA D 137 ? 0.8230 0.8900 0.8391 0.1155  0.1025  -0.1036 153 ALA A O   
9060  C CB  . ALA D 137 ? 0.9107 0.9297 0.9260 0.1057  0.1214  -0.1075 153 ALA A CB  
9061  N N   . ASN D 138 ? 0.8389 0.9226 0.8676 0.1250  0.1196  -0.0964 154 ASN A N   
9062  C CA  . ASN D 138 ? 0.8452 0.9512 0.8778 0.1405  0.1197  -0.0888 154 ASN A CA  
9063  C C   . ASN D 138 ? 0.8384 0.9791 0.8753 0.1387  0.1116  -0.0890 154 ASN A C   
9064  O O   . ASN D 138 ? 0.8120 0.9719 0.8474 0.1449  0.1048  -0.0871 154 ASN A O   
9065  C CB  . ASN D 138 ? 0.8797 0.9847 0.9212 0.1577  0.1352  -0.0793 154 ASN A CB  
9066  C CG  . ASN D 138 ? 0.9458 1.0190 0.9847 0.1605  0.1436  -0.0793 154 ASN A CG  
9067  O OD1 . ASN D 138 ? 1.0346 1.1011 1.0699 0.1689  0.1437  -0.0753 154 ASN A OD1 
9068  N ND2 . ASN D 138 ? 1.0090 1.0638 1.0500 0.1532  0.1514  -0.0844 154 ASN A ND2 
9069  N N   . SER D 139 ? 0.8228 0.9741 0.8652 0.1299  0.1123  -0.0919 155 SER A N   
9070  C CA  . SER D 139 ? 0.8405 1.0284 0.8907 0.1316  0.1078  -0.0904 155 SER A CA  
9071  C C   . SER D 139 ? 0.8448 1.0461 0.8905 0.1204  0.0928  -0.0979 155 SER A C   
9072  O O   . SER D 139 ? 0.8181 1.0016 0.8577 0.1043  0.0861  -0.1059 155 SER A O   
9073  C CB  . SER D 139 ? 0.8723 1.0696 0.9308 0.1245  0.1132  -0.0922 155 SER A CB  
9074  O OG  . SER D 139 ? 0.8060 1.0409 0.8734 0.1266  0.1082  -0.0910 155 SER A OG  
9075  N N   . LEU D 140 ? 0.8729 1.1069 0.9226 0.1290  0.0878  -0.0951 156 LEU A N   
9076  C CA  . LEU D 140 ? 0.8217 1.0762 0.8703 0.1188  0.0745  -0.1037 156 LEU A CA  
9077  C C   . LEU D 140 ? 0.8303 1.1147 0.8895 0.1111  0.0716  -0.1067 156 LEU A C   
9078  O O   . LEU D 140 ? 0.8411 1.1426 0.9014 0.1002  0.0612  -0.1154 156 LEU A O   
9079  C CB  . LEU D 140 ? 0.7023 0.9787 0.7476 0.1310  0.0693  -0.1010 156 LEU A CB  
9080  C CG  . LEU D 140 ? 0.6660 0.9201 0.7004 0.1379  0.0699  -0.0995 156 LEU A CG  
9081  C CD1 . LEU D 140 ? 0.6747 0.9575 0.7054 0.1483  0.0643  -0.0976 156 LEU A CD1 
9082  C CD2 . LEU D 140 ? 0.7028 0.9300 0.7310 0.1205  0.0630  -0.1114 156 LEU A CD2 
9083  N N   . ASP D 141 ? 0.9714 1.2635 1.0398 0.1162  0.0811  -0.1007 157 ASP A N   
9084  C CA  . ASP D 141 ? 0.9708 1.2937 1.0508 0.1091  0.0790  -0.1037 157 ASP A CA  
9085  C C   . ASP D 141 ? 0.8891 1.1943 0.9673 0.0878  0.0775  -0.1120 157 ASP A C   
9086  O O   . ASP D 141 ? 0.8811 1.1581 0.9548 0.0842  0.0851  -0.1108 157 ASP A O   
9087  C CB  . ASP D 141 ? 0.9564 1.2979 1.0492 0.1234  0.0903  -0.0942 157 ASP A CB  
9088  C CG  . ASP D 141 ? 0.8674 1.2397 0.9731 0.1148  0.0888  -0.0980 157 ASP A CG  
9089  O OD1 . ASP D 141 ? 1.0264 1.4368 1.1401 0.1187  0.0817  -0.0981 157 ASP A OD1 
9090  O OD2 . ASP D 141 ? 0.7761 1.1360 0.8837 0.1031  0.0943  -0.1017 157 ASP A OD2 
9091  N N   . TYR D 142 ? 0.7829 1.1067 0.8653 0.0736  0.0681  -0.1203 158 TYR A N   
9092  C CA  . TYR D 142 ? 0.8103 1.1159 0.8903 0.0524  0.0653  -0.1274 158 TYR A CA  
9093  C C   . TYR D 142 ? 0.7641 1.0690 0.8492 0.0473  0.0750  -0.1247 158 TYR A C   
9094  O O   . TYR D 142 ? 0.7598 1.0381 0.8380 0.0348  0.0772  -0.1260 158 TYR A O   
9095  C CB  . TYR D 142 ? 0.7884 1.1170 0.8752 0.0389  0.0548  -0.1368 158 TYR A CB  
9096  C CG  . TYR D 142 ? 0.7872 1.0975 0.8735 0.0164  0.0518  -0.1432 158 TYR A CG  
9097  C CD1 . TYR D 142 ? 0.7751 1.0935 0.8684 0.0057  0.0568  -0.1427 158 TYR A CD1 
9098  C CD2 . TYR D 142 ? 0.8110 1.1001 0.8917 0.0056  0.0436  -0.1499 158 TYR A CD2 
9099  C CE1 . TYR D 142 ? 0.7394 1.0427 0.8326 -0.0151 0.0542  -0.1469 158 TYR A CE1 
9100  C CE2 . TYR D 142 ? 0.7760 1.0492 0.8583 -0.0146 0.0409  -0.1543 158 TYR A CE2 
9101  C CZ  . TYR D 142 ? 0.7077 0.9881 0.7958 -0.0250 0.0461  -0.1521 158 TYR A CZ  
9102  O OH  . TYR D 142 ? 0.5626 0.8270 0.6521 -0.0449 0.0439  -0.1546 158 TYR A OH  
9103  N N   . ASN D 143 ? 0.7789 1.1155 0.8767 0.0554  0.0803  -0.1214 159 ASN A N   
9104  C CA  . ASN D 143 ? 0.7715 1.1101 0.8752 0.0490  0.0898  -0.1206 159 ASN A CA  
9105  C C   . ASN D 143 ? 0.7549 1.0664 0.8524 0.0574  0.1018  -0.1154 159 ASN A C   
9106  O O   . ASN D 143 ? 0.7439 1.0409 0.8380 0.0468  0.1082  -0.1170 159 ASN A O   
9107  C CB  . ASN D 143 ? 0.8104 1.1922 0.9318 0.0558  0.0923  -0.1191 159 ASN A CB  
9108  C CG  . ASN D 143 ? 0.7385 1.1476 0.8678 0.0416  0.0819  -0.1268 159 ASN A CG  
9109  O OD1 . ASN D 143 ? 0.6123 1.0061 0.7360 0.0231  0.0761  -0.1334 159 ASN A OD1 
9110  N ND2 . ASN D 143 ? 0.9141 1.3641 1.0570 0.0511  0.0790  -0.1260 159 ASN A ND2 
9111  N N   . GLU D 144 ? 0.7978 1.1025 0.8936 0.0757  0.1051  -0.1094 160 GLU A N   
9112  C CA  . GLU D 144 ? 0.7773 1.0550 0.8685 0.0836  0.1170  -0.1057 160 GLU A CA  
9113  C C   . GLU D 144 ? 0.7746 1.0161 0.8503 0.0691  0.1141  -0.1103 160 GLU A C   
9114  O O   . GLU D 144 ? 0.7710 0.9967 0.8429 0.0619  0.1220  -0.1121 160 GLU A O   
9115  C CB  . GLU D 144 ? 0.7909 1.0685 0.8841 0.1055  0.1203  -0.0977 160 GLU A CB  
9116  C CG  . GLU D 144 ? 0.7486 1.0049 0.8435 0.1179  0.1353  -0.0929 160 GLU A CG  
9117  C CD  . GLU D 144 ? 0.8743 1.1272 0.9697 0.1378  0.1375  -0.0840 160 GLU A CD  
9118  O OE1 . GLU D 144 ? 0.8907 1.1601 0.9840 0.1427  0.1273  -0.0813 160 GLU A OE1 
9119  O OE2 . GLU D 144 ? 1.0339 1.2685 1.1325 0.1484  0.1504  -0.0798 160 GLU A OE2 
9120  N N   . ARG D 145 ? 0.7861 1.0170 0.8533 0.0640  0.1023  -0.1128 161 ARG A N   
9121  C CA  . ARG D 145 ? 0.7831 0.9812 0.8372 0.0513  0.0978  -0.1162 161 ARG A CA  
9122  C C   . ARG D 145 ? 0.7799 0.9755 0.8320 0.0317  0.0965  -0.1196 161 ARG A C   
9123  O O   . ARG D 145 ? 0.8493 1.0213 0.8922 0.0234  0.0994  -0.1199 161 ARG A O   
9124  C CB  . ARG D 145 ? 0.7709 0.9638 0.8203 0.0503  0.0855  -0.1188 161 ARG A CB  
9125  C CG  . ARG D 145 ? 0.7861 0.9803 0.8349 0.0689  0.0866  -0.1148 161 ARG A CG  
9126  C CD  . ARG D 145 ? 0.7874 0.9741 0.8303 0.0649  0.0752  -0.1194 161 ARG A CD  
9127  N NE  . ARG D 145 ? 0.7942 0.9476 0.8284 0.0531  0.0728  -0.1223 161 ARG A NE  
9128  C CZ  . ARG D 145 ? 0.8214 0.9485 0.8484 0.0590  0.0765  -0.1201 161 ARG A CZ  
9129  N NH1 . ARG D 145 ? 0.8196 0.9477 0.8470 0.0759  0.0831  -0.1152 161 ARG A NH1 
9130  N NH2 . ARG D 145 ? 0.8334 0.9337 0.8536 0.0476  0.0738  -0.1223 161 ARG A NH2 
9131  N N   . LEU D 146 ? 0.7558 0.9774 0.8168 0.0238  0.0926  -0.1220 162 LEU A N   
9132  C CA  . LEU D 146 ? 0.7602 0.9817 0.8205 0.0050  0.0926  -0.1242 162 LEU A CA  
9133  C C   . LEU D 146 ? 0.7527 0.9735 0.8123 0.0049  0.1056  -0.1224 162 LEU A C   
9134  O O   . LEU D 146 ? 0.7692 0.9735 0.8196 -0.0081 0.1075  -0.1226 162 LEU A O   
9135  C CB  . LEU D 146 ? 0.7620 1.0147 0.8347 -0.0026 0.0873  -0.1276 162 LEU A CB  
9136  C CG  . LEU D 146 ? 0.6980 0.9515 0.7711 -0.0227 0.0882  -0.1289 162 LEU A CG  
9137  C CD1 . LEU D 146 ? 0.7460 0.9666 0.8065 -0.0357 0.0826  -0.1281 162 LEU A CD1 
9138  C CD2 . LEU D 146 ? 0.6332 0.9161 0.7199 -0.0308 0.0831  -0.1333 162 LEU A CD2 
9139  N N   . TRP D 147 ? 0.7536 0.9943 0.8238 0.0191  0.1150  -0.1208 163 TRP A N   
9140  C CA  . TRP D 147 ? 0.7771 1.0165 0.8481 0.0195  0.1287  -0.1209 163 TRP A CA  
9141  C C   . TRP D 147 ? 0.7880 0.9943 0.8451 0.0192  0.1328  -0.1212 163 TRP A C   
9142  O O   . TRP D 147 ? 0.8038 0.9990 0.8519 0.0061  0.1363  -0.1233 163 TRP A O   
9143  C CB  . TRP D 147 ? 0.7923 1.0559 0.8794 0.0372  0.1388  -0.1186 163 TRP A CB  
9144  C CG  . TRP D 147 ? 0.8545 1.1109 0.9429 0.0405  0.1543  -0.1200 163 TRP A CG  
9145  C CD1 . TRP D 147 ? 0.8862 1.1516 0.9766 0.0299  0.1629  -0.1238 163 TRP A CD1 
9146  C CD2 . TRP D 147 ? 0.8850 1.1262 0.9751 0.0563  0.1646  -0.1183 163 TRP A CD2 
9147  N NE1 . TRP D 147 ? 0.9057 1.1611 0.9977 0.0373  0.1777  -0.1261 163 TRP A NE1 
9148  C CE2 . TRP D 147 ? 0.9073 1.1472 1.0001 0.0536  0.1791  -0.1228 163 TRP A CE2 
9149  C CE3 . TRP D 147 ? 0.8510 1.0790 0.9406 0.0719  0.1635  -0.1138 163 TRP A CE3 
9150  C CZ2 . TRP D 147 ? 0.9975 1.2227 1.0942 0.0656  0.1927  -0.1239 163 TRP A CZ2 
9151  C CZ3 . TRP D 147 ? 0.8960 1.1090 0.9893 0.0839  0.1770  -0.1134 163 TRP A CZ3 
9152  C CH2 . TRP D 147 ? 0.9909 1.2019 1.0883 0.0805  0.1914  -0.1188 163 TRP A CH2 
9153  N N   . ALA D 148 ? 0.8075 0.9989 0.8625 0.0329  0.1324  -0.1191 164 ALA A N   
9154  C CA  . ALA D 148 ? 0.8032 0.9644 0.8468 0.0328  0.1367  -0.1204 164 ALA A CA  
9155  C C   . ALA D 148 ? 0.7930 0.9371 0.8225 0.0136  0.1291  -0.1221 164 ALA A C   
9156  O O   . ALA D 148 ? 0.8704 1.0054 0.8922 0.0050  0.1353  -0.1245 164 ALA A O   
9157  C CB  . ALA D 148 ? 0.8337 0.9804 0.8761 0.0469  0.1337  -0.1176 164 ALA A CB  
9158  N N   . TRP D 149 ? 0.7969 0.9387 0.8238 0.0066  0.1157  -0.1209 165 TRP A N   
9159  C CA  . TRP D 149 ? 0.7524 0.8768 0.7681 -0.0101 0.1072  -0.1205 165 TRP A CA  
9160  C C   . TRP D 149 ? 0.7874 0.9206 0.7999 -0.0254 0.1117  -0.1205 165 TRP A C   
9161  O O   . TRP D 149 ? 0.8918 1.0110 0.8928 -0.0340 0.1142  -0.1201 165 TRP A O   
9162  C CB  . TRP D 149 ? 0.7547 0.8804 0.7735 -0.0141 0.0941  -0.1203 165 TRP A CB  
9163  C CG  . TRP D 149 ? 0.7600 0.8639 0.7703 -0.0277 0.0842  -0.1188 165 TRP A CG  
9164  C CD1 . TRP D 149 ? 0.7463 0.8270 0.7511 -0.0248 0.0773  -0.1185 165 TRP A CD1 
9165  C CD2 . TRP D 149 ? 0.7838 0.8870 0.7915 -0.0457 0.0807  -0.1164 165 TRP A CD2 
9166  N NE1 . TRP D 149 ? 0.7199 0.7857 0.7200 -0.0393 0.0694  -0.1159 165 TRP A NE1 
9167  C CE2 . TRP D 149 ? 0.7445 0.8231 0.7458 -0.0524 0.0714  -0.1139 165 TRP A CE2 
9168  C CE3 . TRP D 149 ? 0.7772 0.8985 0.7881 -0.0569 0.0851  -0.1155 165 TRP A CE3 
9169  C CZ2 . TRP D 149 ? 0.7450 0.8159 0.7434 -0.0692 0.0663  -0.1092 165 TRP A CZ2 
9170  C CZ3 . TRP D 149 ? 0.7716 0.8851 0.7783 -0.0746 0.0803  -0.1112 165 TRP A CZ3 
9171  C CH2 . TRP D 149 ? 0.7355 0.8236 0.7362 -0.0802 0.0710  -0.1075 165 TRP A CH2 
9172  N N   . GLU D 150 ? 0.7598 0.9185 0.7827 -0.0289 0.1131  -0.1210 166 GLU A N   
9173  C CA  . GLU D 150 ? 0.8600 1.0278 0.8802 -0.0454 0.1162  -0.1203 166 GLU A CA  
9174  C C   . GLU D 150 ? 0.8841 1.0546 0.9001 -0.0445 0.1301  -0.1227 166 GLU A C   
9175  O O   . GLU D 150 ? 0.9000 1.0651 0.9047 -0.0583 0.1324  -0.1218 166 GLU A O   
9176  C CB  . GLU D 150 ? 0.8588 1.0557 0.8934 -0.0490 0.1156  -0.1213 166 GLU A CB  
9177  C CG  . GLU D 150 ? 0.8284 1.0394 0.8627 -0.0639 0.1227  -0.1210 166 GLU A CG  
9178  C CD  . GLU D 150 ? 0.8771 1.0713 0.8989 -0.0832 0.1165  -0.1164 166 GLU A CD  
9179  O OE1 . GLU D 150 ? 0.8879 1.0615 0.9048 -0.0853 0.1058  -0.1137 166 GLU A OE1 
9180  O OE2 . GLU D 150 ? 0.9303 1.1309 0.9467 -0.0957 0.1230  -0.1147 166 GLU A OE2 
9181  N N   . SER D 151 ? 0.9703 1.1505 0.9958 -0.0287 0.1402  -0.1257 167 SER A N   
9182  C CA  . SER D 151 ? 0.9689 1.1529 0.9932 -0.0284 0.1549  -0.1300 167 SER A CA  
9183  C C   . SER D 151 ? 1.0021 1.1602 1.0118 -0.0295 0.1571  -0.1322 167 SER A C   
9184  O O   . SER D 151 ? 1.0720 1.2308 1.0747 -0.0370 0.1663  -0.1364 167 SER A O   
9185  C CB  . SER D 151 ? 1.0093 1.2115 1.0512 -0.0112 0.1662  -0.1322 167 SER A CB  
9186  O OG  . SER D 151 ? 1.0865 1.2802 1.1340 0.0062  0.1639  -0.1299 167 SER A OG  
9187  N N   . TRP D 152 ? 0.8779 1.0147 0.8827 -0.0235 0.1487  -0.1301 168 TRP A N   
9188  C CA  . TRP D 152 ? 0.8851 0.9990 0.8752 -0.0287 0.1482  -0.1319 168 TRP A CA  
9189  C C   . TRP D 152 ? 0.8962 1.0080 0.8721 -0.0484 0.1419  -0.1289 168 TRP A C   
9190  O O   . TRP D 152 ? 0.9837 1.0954 0.9493 -0.0569 0.1486  -0.1322 168 TRP A O   
9191  C CB  . TRP D 152 ? 0.8735 0.9661 0.8618 -0.0200 0.1394  -0.1298 168 TRP A CB  
9192  C CG  . TRP D 152 ? 0.8652 0.9352 0.8399 -0.0249 0.1379  -0.1319 168 TRP A CG  
9193  C CD1 . TRP D 152 ? 0.8456 0.8995 0.8098 -0.0335 0.1252  -0.1277 168 TRP A CD1 
9194  C CD2 . TRP D 152 ? 0.8329 0.8961 0.8050 -0.0218 0.1496  -0.1390 168 TRP A CD2 
9195  N NE1 . TRP D 152 ? 0.7741 0.8138 0.7290 -0.0354 0.1274  -0.1313 168 TRP A NE1 
9196  C CE2 . TRP D 152 ? 0.8406 0.8856 0.7998 -0.0290 0.1424  -0.1390 168 TRP A CE2 
9197  C CE3 . TRP D 152 ? 0.7991 0.8698 0.7800 -0.0136 0.1657  -0.1459 168 TRP A CE3 
9198  C CZ2 . TRP D 152 ? 0.8619 0.8980 0.8162 -0.0292 0.1505  -0.1467 168 TRP A CZ2 
9199  C CZ3 . TRP D 152 ? 0.8747 0.9340 0.8513 -0.0138 0.1747  -0.1539 168 TRP A CZ3 
9200  C CH2 . TRP D 152 ? 0.8976 0.9406 0.8606 -0.0221 0.1669  -0.1548 168 TRP A CH2 
9201  N N   . ARG D 153 ? 0.8991 1.0106 0.8748 -0.0560 0.1297  -0.1226 169 ARG A N   
9202  C CA  . ARG D 153 ? 0.9430 1.0500 0.9058 -0.0740 0.1238  -0.1173 169 ARG A CA  
9203  C C   . ARG D 153 ? 0.9839 1.1112 0.9443 -0.0857 0.1328  -0.1180 169 ARG A C   
9204  O O   . ARG D 153 ? 0.9688 1.0936 0.9162 -0.1006 0.1302  -0.1130 169 ARG A O   
9205  C CB  . ARG D 153 ? 0.9186 1.0189 0.8844 -0.0798 0.1100  -0.1106 169 ARG A CB  
9206  C CG  . ARG D 153 ? 0.8350 0.9114 0.7973 -0.0743 0.1000  -0.1088 169 ARG A CG  
9207  C CD  . ARG D 153 ? 0.8066 0.8797 0.7776 -0.0752 0.0892  -0.1059 169 ARG A CD  
9208  N NE  . ARG D 153 ? 0.8439 0.8938 0.8121 -0.0710 0.0797  -0.1043 169 ARG A NE  
9209  C CZ  . ARG D 153 ? 0.8189 0.8614 0.7908 -0.0564 0.0795  -0.1085 169 ARG A CZ  
9210  N NH1 . ARG D 153 ? 0.6901 0.7448 0.6679 -0.0437 0.0889  -0.1136 169 ARG A NH1 
9211  N NH2 . ARG D 153 ? 0.7804 0.8028 0.7511 -0.0543 0.0703  -0.1071 169 ARG A NH2 
9212  N N   . SER D 154 ? 0.9840 1.1322 0.9570 -0.0793 0.1433  -0.1230 170 SER A N   
9213  C CA  . SER D 154 ? 1.0207 1.1893 0.9922 -0.0907 0.1528  -0.1244 170 SER A CA  
9214  C C   . SER D 154 ? 1.1000 1.2744 1.0681 -0.0876 0.1683  -0.1333 170 SER A C   
9215  O O   . SER D 154 ? 1.0847 1.2660 1.0409 -0.1009 0.1738  -0.1342 170 SER A O   
9216  C CB  . SER D 154 ? 1.0404 1.2326 1.0296 -0.0892 0.1544  -0.1242 170 SER A CB  
9217  O OG  . SER D 154 ? 1.1697 1.3742 1.1740 -0.0725 0.1636  -0.1303 170 SER A OG  
9218  N N   . GLU D 155 ? 1.2811 1.4538 1.2598 -0.0709 0.1764  -0.1400 171 GLU A N   
9219  C CA  . GLU D 155 ? 1.3836 1.5564 1.3591 -0.0688 0.1911  -0.1498 171 GLU A CA  
9220  C C   . GLU D 155 ? 1.3297 1.4829 1.2858 -0.0765 0.1869  -0.1510 171 GLU A C   
9221  O O   . GLU D 155 ? 1.3471 1.5058 1.2897 -0.0889 0.1927  -0.1551 171 GLU A O   
9222  C CB  . GLU D 155 ? 1.4291 1.6017 1.4229 -0.0484 0.2008  -0.1551 171 GLU A CB  
9223  C CG  . GLU D 155 ? 1.5015 1.6913 1.5080 -0.0430 0.2203  -0.1646 171 GLU A CG  
9224  C CD  . GLU D 155 ? 1.6042 1.7874 1.5996 -0.0500 0.2321  -0.1758 171 GLU A CD  
9225  O OE1 . GLU D 155 ? 1.5324 1.6943 1.5201 -0.0472 0.2299  -0.1785 171 GLU A OE1 
9226  O OE2 . GLU D 155 ? 1.6508 1.8510 1.6455 -0.0582 0.2439  -0.1827 171 GLU A OE2 
9227  N N   . VAL D 156 ? 1.1396 1.2717 1.0936 -0.0696 0.1767  -0.1477 172 VAL A N   
9228  C CA  . VAL D 156 ? 1.1055 1.2211 1.0440 -0.0749 0.1740  -0.1503 172 VAL A CA  
9229  C C   . VAL D 156 ? 1.0375 1.1486 0.9588 -0.0910 0.1605  -0.1409 172 VAL A C   
9230  O O   . VAL D 156 ? 0.9950 1.1045 0.9004 -0.1012 0.1608  -0.1428 172 VAL A O   
9231  C CB  . VAL D 156 ? 1.0495 1.1453 0.9952 -0.0598 0.1710  -0.1517 172 VAL A CB  
9232  C CG1 . VAL D 156 ? 0.9760 1.0573 0.9097 -0.0635 0.1711  -0.1573 172 VAL A CG1 
9233  C CG2 . VAL D 156 ? 1.0990 1.2012 1.0632 -0.0440 0.1851  -0.1582 172 VAL A CG2 
9234  N N   . GLY D 157 ? 1.0160 1.1266 0.9405 -0.0942 0.1491  -0.1306 173 GLY A N   
9235  C CA  . GLY D 157 ? 0.9953 1.0977 0.9059 -0.1077 0.1365  -0.1202 173 GLY A CA  
9236  C C   . GLY D 157 ? 1.0209 1.1393 0.9202 -0.1247 0.1396  -0.1158 173 GLY A C   
9237  O O   . GLY D 157 ? 1.0131 1.1257 0.8977 -0.1363 0.1315  -0.1071 173 GLY A O   
9238  N N   . LYS D 158 ? 1.0045 1.1435 0.9108 -0.1262 0.1512  -0.1205 174 LYS A N   
9239  C CA  . LYS D 158 ? 1.0199 1.1755 0.9158 -0.1429 0.1550  -0.1159 174 LYS A CA  
9240  C C   . LYS D 158 ? 1.0121 1.1733 0.8904 -0.1500 0.1631  -0.1226 174 LYS A C   
9241  O O   . LYS D 158 ? 1.0099 1.1750 0.8704 -0.1646 0.1596  -0.1150 174 LYS A O   
9242  C CB  . LYS D 158 ? 1.1181 1.2959 1.0289 -0.1421 0.1653  -0.1198 174 LYS A CB  
9243  C CG  . LYS D 158 ? 1.0652 1.2449 0.9893 -0.1434 0.1568  -0.1115 174 LYS A CG  
9244  C CD  . LYS D 158 ? 1.1092 1.3113 1.0531 -0.1365 0.1669  -0.1183 174 LYS A CD  
9245  C CE  . LYS D 158 ? 1.1271 1.3328 1.0861 -0.1366 0.1579  -0.1126 174 LYS A CE  
9246  N NZ  . LYS D 158 ? 1.0820 1.2994 1.0398 -0.1543 0.1571  -0.1051 174 LYS A NZ  
9247  N N   . GLN D 159 ? 0.9528 1.1152 0.8365 -0.1396 0.1744  -0.1368 175 GLN A N   
9248  C CA  . GLN D 159 ? 0.9893 1.1531 0.8579 -0.1445 0.1810  -0.1461 175 GLN A CA  
9249  C C   . GLN D 159 ? 1.0032 1.1540 0.8536 -0.1526 0.1665  -0.1368 175 GLN A C   
9250  O O   . GLN D 159 ? 0.9872 1.1483 0.8183 -0.1667 0.1664  -0.1343 175 GLN A O   
9251  C CB  . GLN D 159 ? 0.9813 1.1376 0.8626 -0.1291 0.1912  -0.1608 175 GLN A CB  
9252  C CG  . GLN D 159 ? 0.9609 1.1303 0.8621 -0.1192 0.2065  -0.1697 175 GLN A CG  
9253  C CD  . GLN D 159 ? 1.0606 1.2206 0.9747 -0.1042 0.2177  -0.1831 175 GLN A CD  
9254  O OE1 . GLN D 159 ? 1.0662 1.2209 0.9713 -0.1073 0.2230  -0.1933 175 GLN A OE1 
9255  N NE2 . GLN D 159 ? 1.2253 1.3844 1.1610 -0.0883 0.2221  -0.1830 175 GLN A NE2 
9256  N N   . LEU D 160 ? 0.9955 1.1251 0.8521 -0.1438 0.1538  -0.1305 176 LEU A N   
9257  C CA  . LEU D 160 ? 0.9464 1.0623 0.7894 -0.1480 0.1409  -0.1238 176 LEU A CA  
9258  C C   . LEU D 160 ? 0.9507 1.0685 0.7810 -0.1619 0.1295  -0.1064 176 LEU A C   
9259  O O   . LEU D 160 ? 0.9715 1.0807 0.7901 -0.1660 0.1188  -0.0991 176 LEU A O   
9260  C CB  . LEU D 160 ? 0.9394 1.0324 0.7945 -0.1342 0.1313  -0.1221 176 LEU A CB  
9261  C CG  . LEU D 160 ? 0.9252 1.0104 0.7928 -0.1190 0.1401  -0.1361 176 LEU A CG  
9262  C CD1 . LEU D 160 ? 0.8365 0.9019 0.7169 -0.1063 0.1301  -0.1313 176 LEU A CD1 
9263  C CD2 . LEU D 160 ? 0.9315 1.0172 0.7887 -0.1219 0.1455  -0.1473 176 LEU A CD2 
9264  N N   . ARG D 161 ? 0.9901 1.1190 0.8235 -0.1692 0.1318  -0.0990 177 ARG A N   
9265  C CA  . ARG D 161 ? 1.0282 1.1544 0.8539 -0.1811 0.1207  -0.0805 177 ARG A CA  
9266  C C   . ARG D 161 ? 1.0773 1.2148 0.8790 -0.1956 0.1196  -0.0735 177 ARG A C   
9267  O O   . ARG D 161 ? 1.0934 1.2198 0.8861 -0.1989 0.1068  -0.0611 177 ARG A O   
9268  C CB  . ARG D 161 ? 1.0687 1.2040 0.9064 -0.1853 0.1244  -0.0755 177 ARG A CB  
9269  C CG  . ARG D 161 ? 1.0931 1.2262 0.9247 -0.1991 0.1158  -0.0565 177 ARG A CG  
9270  C CD  . ARG D 161 ? 1.0951 1.2033 0.9308 -0.1956 0.0997  -0.0448 177 ARG A CD  
9271  N NE  . ARG D 161 ? 1.1032 1.2092 0.9313 -0.2094 0.0930  -0.0254 177 ARG A NE  
9272  C CZ  . ARG D 161 ? 1.0672 1.1619 0.9084 -0.2127 0.0867  -0.0146 177 ARG A CZ  
9273  N NH1 . ARG D 161 ? 1.0357 1.1220 0.8976 -0.2037 0.0851  -0.0218 177 ARG A NH1 
9274  N NH2 . ARG D 161 ? 1.1047 1.1970 0.9383 -0.2256 0.0820  0.0041  177 ARG A NH2 
9275  N N   . PRO D 162 ? 1.1324 1.2929 0.9230 -0.2048 0.1323  -0.0801 178 PRO A N   
9276  C CA  . PRO D 162 ? 1.1572 1.3308 0.9227 -0.2187 0.1306  -0.0735 178 PRO A CA  
9277  C C   . PRO D 162 ? 1.1295 1.2972 0.8847 -0.2149 0.1249  -0.0799 178 PRO A C   
9278  O O   . PRO D 162 ? 1.1600 1.3293 0.8983 -0.2229 0.1147  -0.0675 178 PRO A O   
9279  C CB  . PRO D 162 ? 1.2057 1.4059 0.9647 -0.2267 0.1481  -0.0848 178 PRO A CB  
9280  C CG  . PRO D 162 ? 1.1695 1.3672 0.9497 -0.2128 0.1590  -0.1029 178 PRO A CG  
9281  C CD  . PRO D 162 ? 1.1008 1.2782 0.9008 -0.2026 0.1490  -0.0944 178 PRO A CD  
9282  N N   . LEU D 163 ? 1.0423 1.2042 0.8080 -0.2029 0.1317  -0.0987 179 LEU A N   
9283  C CA  . LEU D 163 ? 1.0229 1.1783 0.7819 -0.1992 0.1268  -0.1062 179 LEU A CA  
9284  C C   . LEU D 163 ? 1.0537 1.1896 0.8136 -0.1961 0.1081  -0.0900 179 LEU A C   
9285  O O   . LEU D 163 ? 1.0937 1.2322 0.8394 -0.2009 0.0995  -0.0858 179 LEU A O   
9286  C CB  . LEU D 163 ? 0.9612 1.1085 0.7369 -0.1853 0.1372  -0.1266 179 LEU A CB  
9287  C CG  . LEU D 163 ? 0.9260 1.0921 0.7028 -0.1875 0.1569  -0.1442 179 LEU A CG  
9288  C CD1 . LEU D 163 ? 0.9220 1.0768 0.7215 -0.1711 0.1675  -0.1597 179 LEU A CD1 
9289  C CD2 . LEU D 163 ? 0.8761 1.0614 0.6318 -0.1998 0.1623  -0.1542 179 LEU A CD2 
9290  N N   . TYR D 164 ? 1.0641 1.1819 0.8410 -0.1884 0.1015  -0.0806 180 TYR A N   
9291  C CA  . TYR D 164 ? 1.0338 1.1321 0.8139 -0.1850 0.0847  -0.0662 180 TYR A CA  
9292  C C   . TYR D 164 ? 1.0342 1.1379 0.8004 -0.1980 0.0754  -0.0449 180 TYR A C   
9293  O O   . TYR D 164 ? 1.0222 1.1163 0.7843 -0.1980 0.0621  -0.0330 180 TYR A O   
9294  C CB  . TYR D 164 ? 0.9988 1.0773 0.8010 -0.1739 0.0809  -0.0639 180 TYR A CB  
9295  C CG  . TYR D 164 ? 0.9911 1.0471 0.8012 -0.1652 0.0672  -0.0583 180 TYR A CG  
9296  C CD1 . TYR D 164 ? 1.0037 1.0519 0.8177 -0.1550 0.0676  -0.0710 180 TYR A CD1 
9297  C CD2 . TYR D 164 ? 0.9513 0.9941 0.7656 -0.1678 0.0546  -0.0404 180 TYR A CD2 
9298  C CE1 . TYR D 164 ? 0.9935 1.0223 0.8156 -0.1471 0.0558  -0.0664 180 TYR A CE1 
9299  C CE2 . TYR D 164 ? 0.9104 0.9333 0.7335 -0.1596 0.0429  -0.0361 180 TYR A CE2 
9300  C CZ  . TYR D 164 ? 0.9575 0.9742 0.7840 -0.1493 0.0434  -0.0493 180 TYR A CZ  
9301  O OH  . TYR D 164 ? 0.9661 0.9642 0.8018 -0.1411 0.0325  -0.0459 180 TYR A OH  
9302  N N   . GLU D 165 ? 1.0454 1.1638 0.8056 -0.2087 0.0824  -0.0387 181 GLU A N   
9303  C CA  . GLU D 165 ? 1.1220 1.2481 0.8667 -0.2222 0.0755  -0.0176 181 GLU A CA  
9304  C C   . GLU D 165 ? 1.1379 1.2796 0.8594 -0.2288 0.0720  -0.0170 181 GLU A C   
9305  O O   . GLU D 165 ? 1.1196 1.2563 0.8339 -0.2308 0.0584  -0.0008 181 GLU A O   
9306  C CB  . GLU D 165 ? 1.1590 1.3019 0.9004 -0.2333 0.0865  -0.0140 181 GLU A CB  
9307  C CG  . GLU D 165 ? 1.1407 1.2739 0.9049 -0.2285 0.0907  -0.0158 181 GLU A CG  
9308  C CD  . GLU D 165 ? 1.2412 1.3919 1.0022 -0.2416 0.1001  -0.0090 181 GLU A CD  
9309  O OE1 . GLU D 165 ? 1.3282 1.4999 1.0684 -0.2533 0.1058  -0.0062 181 GLU A OE1 
9310  O OE2 . GLU D 165 ? 1.2276 1.3729 1.0067 -0.2407 0.1022  -0.0074 181 GLU A OE2 
9311  N N   . GLU D 166 ? 1.1373 1.2996 0.8478 -0.2323 0.0844  -0.0354 182 GLU A N   
9312  C CA  . GLU D 166 ? 1.1559 1.3372 0.8440 -0.2397 0.0825  -0.0387 182 GLU A CA  
9313  C C   . GLU D 166 ? 1.1482 1.3154 0.8409 -0.2303 0.0705  -0.0414 182 GLU A C   
9314  O O   . GLU D 166 ? 1.1548 1.3326 0.8313 -0.2360 0.0609  -0.0336 182 GLU A O   
9315  C CB  . GLU D 166 ? 1.1975 1.4008 0.8777 -0.2439 0.1000  -0.0626 182 GLU A CB  
9316  C CG  . GLU D 166 ? 1.3484 1.5785 1.0022 -0.2554 0.1005  -0.0681 182 GLU A CG  
9317  C CD  . GLU D 166 ? 1.4213 1.6738 1.0685 -0.2609 0.1199  -0.0933 182 GLU A CD  
9318  O OE1 . GLU D 166 ? 1.3221 1.5745 0.9807 -0.2591 0.1329  -0.1000 182 GLU A OE1 
9319  O OE2 . GLU D 166 ? 1.5096 1.7798 1.1418 -0.2665 0.1223  -0.1074 182 GLU A OE2 
9320  N N   . TYR D 167 ? 1.1252 1.2699 0.8399 -0.2161 0.0708  -0.0517 183 TYR A N   
9321  C CA  . TYR D 167 ? 1.0963 1.2263 0.8182 -0.2065 0.0605  -0.0548 183 TYR A CA  
9322  C C   . TYR D 167 ? 1.0978 1.2145 0.8214 -0.2059 0.0428  -0.0307 183 TYR A C   
9323  O O   . TYR D 167 ? 1.1582 1.2761 0.8762 -0.2052 0.0319  -0.0267 183 TYR A O   
9324  C CB  . TYR D 167 ? 1.0399 1.1502 0.7846 -0.1918 0.0670  -0.0706 183 TYR A CB  
9325  C CG  . TYR D 167 ? 1.0145 1.1019 0.7736 -0.1798 0.0557  -0.0688 183 TYR A CG  
9326  C CD1 . TYR D 167 ? 1.0078 1.0747 0.7810 -0.1738 0.0462  -0.0541 183 TYR A CD1 
9327  C CD2 . TYR D 167 ? 1.0554 1.1412 0.8166 -0.1742 0.0563  -0.0836 183 TYR A CD2 
9328  C CE1 . TYR D 167 ? 0.9531 0.9996 0.7402 -0.1628 0.0370  -0.0533 183 TYR A CE1 
9329  C CE2 . TYR D 167 ? 1.0295 1.0946 0.8050 -0.1631 0.0470  -0.0822 183 TYR A CE2 
9330  C CZ  . TYR D 167 ? 0.9366 0.9825 0.7246 -0.1573 0.0374  -0.0669 183 TYR A CZ  
9331  O OH  . TYR D 167 ? 0.9630 0.9892 0.7654 -0.1465 0.0290  -0.0662 183 TYR A OH  
9332  N N   . VAL D 168 ? 1.1482 1.2530 0.8807 -0.2066 0.0399  -0.0146 184 VAL A N   
9333  C CA  . VAL D 168 ? 1.1515 1.2431 0.8870 -0.2065 0.0243  0.0088  184 VAL A CA  
9334  C C   . VAL D 168 ? 1.2130 1.3258 0.9249 -0.2190 0.0182  0.0252  184 VAL A C   
9335  O O   . VAL D 168 ? 1.2618 1.3720 0.9711 -0.2176 0.0045  0.0386  184 VAL A O   
9336  C CB  . VAL D 168 ? 1.1357 1.2100 0.8870 -0.2059 0.0239  0.0211  184 VAL A CB  
9337  C CG1 . VAL D 168 ? 1.1168 1.1779 0.8715 -0.2071 0.0093  0.0461  184 VAL A CG1 
9338  C CG2 . VAL D 168 ? 1.1073 1.1627 0.8810 -0.1929 0.0279  0.0058  184 VAL A CG2 
9339  N N   . VAL D 169 ? 1.1937 1.3300 0.8881 -0.2311 0.0283  0.0243  185 VAL A N   
9340  C CA  . VAL D 169 ? 1.2477 1.4087 0.9166 -0.2439 0.0238  0.0395  185 VAL A CA  
9341  C C   . VAL D 169 ? 1.2810 1.4562 0.9376 -0.2430 0.0168  0.0311  185 VAL A C   
9342  O O   . VAL D 169 ? 1.3057 1.4852 0.9547 -0.2444 0.0026  0.0495  185 VAL A O   
9343  C CB  . VAL D 169 ? 1.2274 1.4133 0.8796 -0.2568 0.0385  0.0344  185 VAL A CB  
9344  C CG1 . VAL D 169 ? 1.3492 1.5654 0.9720 -0.2697 0.0349  0.0450  185 VAL A CG1 
9345  C CG2 . VAL D 169 ? 1.2118 1.3872 0.8740 -0.2605 0.0427  0.0487  185 VAL A CG2 
9346  N N   . LEU D 170 ? 1.2011 1.3850 0.8567 -0.2408 0.0270  0.0034  186 LEU A N   
9347  C CA  . LEU D 170 ? 1.2335 1.4334 0.8781 -0.2417 0.0221  -0.0079 186 LEU A CA  
9348  C C   . LEU D 170 ? 1.2541 1.4342 0.9140 -0.2301 0.0070  -0.0018 186 LEU A C   
9349  O O   . LEU D 170 ? 1.2690 1.4625 0.9183 -0.2328 -0.0054 0.0076  186 LEU A O   
9350  C CB  . LEU D 170 ? 1.1916 1.4008 0.8366 -0.2412 0.0378  -0.0400 186 LEU A CB  
9351  C CG  . LEU D 170 ? 1.1466 1.3839 0.7715 -0.2549 0.0514  -0.0469 186 LEU A CG  
9352  C CD1 . LEU D 170 ? 1.2302 1.4674 0.8642 -0.2519 0.0702  -0.0758 186 LEU A CD1 
9353  C CD2 . LEU D 170 ? 1.1526 1.4203 0.7527 -0.2656 0.0454  -0.0473 186 LEU A CD2 
9354  N N   . LYS D 171 ? 1.2240 1.3746 0.9090 -0.2171 0.0082  -0.0082 187 LYS A N   
9355  C CA  . LYS D 171 ? 1.1696 1.3012 0.8704 -0.2060 -0.0049 -0.0039 187 LYS A CA  
9356  C C   . LYS D 171 ? 1.2149 1.3429 0.9141 -0.2074 -0.0210 0.0262  187 LYS A C   
9357  O O   . LYS D 171 ? 1.2450 1.3730 0.9468 -0.2032 -0.0340 0.0330  187 LYS A O   
9358  C CB  . LYS D 171 ? 1.1180 1.2197 0.8445 -0.1927 -0.0001 -0.0136 187 LYS A CB  
9359  C CG  . LYS D 171 ? 1.0391 1.1396 0.7725 -0.1869 0.0129  -0.0419 187 LYS A CG  
9360  C CD  . LYS D 171 ? 1.0301 1.1293 0.7683 -0.1811 0.0061  -0.0515 187 LYS A CD  
9361  C CE  . LYS D 171 ? 0.9756 1.0722 0.7223 -0.1755 0.0196  -0.0793 187 LYS A CE  
9362  N NZ  . LYS D 171 ? 0.9373 1.0279 0.6935 -0.1687 0.0129  -0.0877 187 LYS A NZ  
9363  N N   . ASN D 172 ? 1.2071 1.3327 0.9031 -0.2135 -0.0200 0.0450  188 ASN A N   
9364  C CA  . ASN D 172 ? 1.2983 1.4200 0.9935 -0.2152 -0.0342 0.0752  188 ASN A CA  
9365  C C   . ASN D 172 ? 1.3593 1.5126 1.0297 -0.2243 -0.0422 0.0860  188 ASN A C   
9366  O O   . ASN D 172 ? 1.4047 1.5575 1.0777 -0.2205 -0.0571 0.1025  188 ASN A O   
9367  C CB  . ASN D 172 ? 1.3123 1.4233 1.0114 -0.2204 -0.0299 0.0925  188 ASN A CB  
9368  C CG  . ASN D 172 ? 1.2426 1.3184 0.9703 -0.2097 -0.0338 0.0981  188 ASN A CG  
9369  O OD1 . ASN D 172 ? 1.1750 1.2348 0.9181 -0.1987 -0.0429 0.0964  188 ASN A OD1 
9370  N ND2 . ASN D 172 ? 1.3086 1.3737 1.0440 -0.2135 -0.0266 0.1039  188 ASN A ND2 
9371  N N   . GLU D 173 ? 1.3645 1.5471 1.0110 -0.2363 -0.0328 0.0768  189 GLU A N   
9372  C CA  . GLU D 173 ? 1.4158 1.6318 1.0379 -0.2449 -0.0411 0.0848  189 GLU A CA  
9373  C C   . GLU D 173 ? 1.3725 1.5922 1.0004 -0.2375 -0.0503 0.0717  189 GLU A C   
9374  O O   . GLU D 173 ? 1.4012 1.6301 1.0257 -0.2363 -0.0659 0.0894  189 GLU A O   
9375  C CB  . GLU D 173 ? 1.4640 1.7126 1.0597 -0.2591 -0.0281 0.0716  189 GLU A CB  
9376  C CG  . GLU D 173 ? 1.5580 1.8102 1.1439 -0.2687 -0.0206 0.0887  189 GLU A CG  
9377  C CD  . GLU D 173 ? 1.6108 1.8987 1.1692 -0.2832 -0.0085 0.0764  189 GLU A CD  
9378  O OE1 . GLU D 173 ? 1.5634 1.8775 1.1062 -0.2873 -0.0103 0.0617  189 GLU A OE1 
9379  O OE2 . GLU D 173 ? 1.6464 1.9365 1.2001 -0.2906 0.0033  0.0799  189 GLU A OE2 
9380  N N   . MET D 174 ? 1.3471 1.5594 0.9854 -0.2322 -0.0406 0.0413  190 MET A N   
9381  C CA  . MET D 174 ? 1.3106 1.5247 0.9570 -0.2256 -0.0469 0.0256  190 MET A CA  
9382  C C   . MET D 174 ? 1.3315 1.5272 0.9957 -0.2147 -0.0641 0.0454  190 MET A C   
9383  O O   . MET D 174 ? 1.3672 1.5796 1.0273 -0.2146 -0.0767 0.0501  190 MET A O   
9384  C CB  . MET D 174 ? 1.2642 1.4612 0.9267 -0.2186 -0.0325 -0.0049 190 MET A CB  
9385  C CG  . MET D 174 ? 1.2744 1.4689 0.9491 -0.2114 -0.0350 -0.0251 190 MET A CG  
9386  S SD  . MET D 174 ? 1.2636 1.4208 0.9698 -0.1937 -0.0460 -0.0161 190 MET A SD  
9387  C CE  . MET D 174 ? 1.2199 1.3658 0.9423 -0.1861 -0.0329 -0.0512 190 MET A CE  
9388  N N   . ALA D 175 ? 1.3616 1.5240 1.0469 -0.2057 -0.0646 0.0563  191 ALA A N   
9389  C CA  . ALA D 175 ? 1.3349 1.4772 1.0402 -0.1947 -0.0793 0.0731  191 ALA A CA  
9390  C C   . ALA D 175 ? 1.4467 1.6025 1.1417 -0.1991 -0.0936 0.1056  191 ALA A C   
9391  O O   . ALA D 175 ? 1.4403 1.6000 1.1419 -0.1935 -0.1079 0.1163  191 ALA A O   
9392  C CB  . ALA D 175 ? 1.2947 1.3994 1.0245 -0.1851 -0.0751 0.0748  191 ALA A CB  
9393  N N   . ARG D 176 ? 1.5517 1.7147 1.2319 -0.2088 -0.0897 0.1229  192 ARG A N   
9394  C CA  . ARG D 176 ? 1.5244 1.7000 1.1946 -0.2131 -0.1022 0.1565  192 ARG A CA  
9395  C C   . ARG D 176 ? 1.5223 1.7359 1.1725 -0.2179 -0.1126 0.1578  192 ARG A C   
9396  O O   . ARG D 176 ? 1.5244 1.7447 1.1764 -0.2145 -0.1282 0.1826  192 ARG A O   
9397  C CB  . ARG D 176 ? 1.5179 1.6987 1.1726 -0.2247 -0.0937 0.1721  192 ARG A CB  
9398  C CG  . ARG D 176 ? 1.5059 1.6517 1.1812 -0.2212 -0.0842 0.1727  192 ARG A CG  
9399  C CD  . ARG D 176 ? 1.5227 1.6750 1.1840 -0.2337 -0.0746 0.1867  192 ARG A CD  
9400  N NE  . ARG D 176 ? 1.5590 1.6892 1.2347 -0.2330 -0.0609 0.1730  192 ARG A NE  
9401  C CZ  . ARG D 176 ? 1.5605 1.6578 1.2614 -0.2268 -0.0613 0.1815  192 ARG A CZ  
9402  N NH1 . ARG D 176 ? 1.5810 1.6590 1.2991 -0.2189 -0.0739 0.2015  192 ARG A NH1 
9403  N NH2 . ARG D 176 ? 1.4795 1.5641 1.1899 -0.2284 -0.0485 0.1689  192 ARG A NH2 
9404  N N   . ALA D 177 ? 1.4845 1.7234 1.1174 -0.2253 -0.1043 0.1306  193 ALA A N   
9405  C CA  . ALA D 177 ? 1.4313 1.7098 1.0447 -0.2315 -0.1133 0.1277  193 ALA A CA  
9406  C C   . ALA D 177 ? 1.4755 1.7497 1.1077 -0.2204 -0.1255 0.1211  193 ALA A C   
9407  O O   . ALA D 177 ? 1.4938 1.7972 1.1160 -0.2225 -0.1392 0.1306  193 ALA A O   
9408  C CB  . ALA D 177 ? 1.3798 1.6849 0.9719 -0.2432 -0.0990 0.0974  193 ALA A CB  
9409  N N   . ASN D 178 ? 1.4269 1.6679 1.0861 -0.2089 -0.1208 0.1046  194 ASN A N   
9410  C CA  . ASN D 178 ? 1.4245 1.6581 1.1046 -0.1977 -0.1316 0.0993  194 ASN A CA  
9411  C C   . ASN D 178 ? 1.4459 1.6561 1.1476 -0.1863 -0.1452 0.1286  194 ASN A C   
9412  O O   . ASN D 178 ? 1.4144 1.6116 1.1387 -0.1751 -0.1527 0.1246  194 ASN A O   
9413  C CB  . ASN D 178 ? 1.3090 1.5199 1.0072 -0.1909 -0.1194 0.0672  194 ASN A CB  
9414  C CG  . ASN D 178 ? 1.3493 1.5863 1.0329 -0.1997 -0.1099 0.0365  194 ASN A CG  
9415  O OD1 . ASN D 178 ? 1.3927 1.6256 1.0706 -0.2043 -0.0933 0.0170  194 ASN A OD1 
9416  N ND2 . ASN D 178 ? 1.3759 1.6409 1.0544 -0.2023 -0.1202 0.0317  194 ASN A ND2 
9417  N N   . HIS D 179 ? 1.5060 1.7106 1.2023 -0.1891 -0.1477 0.1575  195 HIS A N   
9418  C CA  . HIS D 179 ? 1.4880 1.6735 1.2032 -0.1798 -0.1605 0.1887  195 HIS A CA  
9419  C C   . HIS D 179 ? 1.3836 1.5243 1.1305 -0.1677 -0.1559 0.1831  195 HIS A C   
9420  O O   . HIS D 179 ? 1.3894 1.5121 1.1598 -0.1566 -0.1663 0.1976  195 HIS A O   
9421  C CB  . HIS D 179 ? 1.5440 1.7521 1.2621 -0.1748 -0.1785 0.2007  195 HIS A CB  
9422  C CG  . HIS D 179 ? 1.5256 1.7821 1.2120 -0.1870 -0.1839 0.2040  195 HIS A CG  
9423  N ND1 . HIS D 179 ? 1.5673 1.8531 1.2440 -0.1909 -0.1852 0.1787  195 HIS A ND1 
9424  C CD2 . HIS D 179 ? 1.5718 1.8536 1.2338 -0.1965 -0.1881 0.2295  195 HIS A CD2 
9425  C CE1 . HIS D 179 ? 1.6338 1.9623 1.2810 -0.2026 -0.1902 0.1870  195 HIS A CE1 
9426  N NE2 . HIS D 179 ? 1.6423 1.9696 1.2791 -0.2060 -0.1922 0.2185  195 HIS A NE2 
9427  N N   . TYR D 180 ? 1.3385 1.4624 1.0865 -0.1696 -0.1403 0.1618  196 TYR A N   
9428  C CA  . TYR D 180 ? 1.2921 1.3763 1.0652 -0.1613 -0.1346 0.1610  196 TYR A CA  
9429  C C   . TYR D 180 ? 1.2936 1.3709 1.0582 -0.1697 -0.1275 0.1773  196 TYR A C   
9430  O O   . TYR D 180 ? 1.3460 1.4490 1.0846 -0.1819 -0.1232 0.1809  196 TYR A O   
9431  C CB  . TYR D 180 ? 1.1977 1.2677 0.9802 -0.1565 -0.1224 0.1274  196 TYR A CB  
9432  C CG  . TYR D 180 ? 1.1037 1.1760 0.8980 -0.1480 -0.1267 0.1085  196 TYR A CG  
9433  C CD1 . TYR D 180 ? 1.0777 1.1787 0.8559 -0.1537 -0.1247 0.0895  196 TYR A CD1 
9434  C CD2 . TYR D 180 ? 1.0693 1.1155 0.8917 -0.1348 -0.1323 0.1094  196 TYR A CD2 
9435  C CE1 . TYR D 180 ? 0.9824 1.0844 0.7733 -0.1466 -0.1275 0.0714  196 TYR A CE1 
9436  C CE2 . TYR D 180 ? 1.0166 1.0645 0.8508 -0.1273 -0.1354 0.0924  196 TYR A CE2 
9437  C CZ  . TYR D 180 ? 0.9741 1.0497 0.7929 -0.1333 -0.1330 0.0738  196 TYR A CZ  
9438  O OH  . TYR D 180 ? 0.8868 0.9631 0.7193 -0.1264 -0.1351 0.0567  196 TYR A OH  
9439  N N   . GLU D 181 ? 1.2319 1.2758 1.0191 -0.1639 -0.1260 0.1874  197 GLU A N   
9440  C CA  . GLU D 181 ? 1.2150 1.2532 0.9962 -0.1727 -0.1202 0.2055  197 GLU A CA  
9441  C C   . GLU D 181 ? 1.2686 1.3070 1.0404 -0.1801 -0.1036 0.1845  197 GLU A C   
9442  O O   . GLU D 181 ? 1.2894 1.3369 1.0468 -0.1910 -0.0973 0.1956  197 GLU A O   
9443  C CB  . GLU D 181 ? 1.2018 1.2062 1.0106 -0.1660 -0.1243 0.2257  197 GLU A CB  
9444  C CG  . GLU D 181 ? 1.3095 1.2812 1.1468 -0.1552 -0.1204 0.2076  197 GLU A CG  
9445  C CD  . GLU D 181 ? 1.3566 1.3003 1.2226 -0.1462 -0.1291 0.2275  197 GLU A CD  
9446  O OE1 . GLU D 181 ? 1.3073 1.2593 1.1742 -0.1435 -0.1413 0.2502  197 GLU A OE1 
9447  O OE2 . GLU D 181 ? 1.4066 1.3211 1.2949 -0.1420 -0.1235 0.2204  197 GLU A OE2 
9448  N N   . ASP D 182 ? 1.2933 1.3237 1.0732 -0.1741 -0.0961 0.1552  198 ASP A N   
9449  C CA  . ASP D 182 ? 1.2515 1.2832 1.0250 -0.1789 -0.0803 0.1336  198 ASP A CA  
9450  C C   . ASP D 182 ? 1.1905 1.2202 0.9703 -0.1708 -0.0756 0.1039  198 ASP A C   
9451  O O   . ASP D 182 ? 1.1923 1.2191 0.9814 -0.1624 -0.0843 0.1005  198 ASP A O   
9452  C CB  . ASP D 182 ? 1.2386 1.2450 1.0284 -0.1790 -0.0737 0.1389  198 ASP A CB  
9453  C CG  . ASP D 182 ? 1.2335 1.2075 1.0532 -0.1664 -0.0792 0.1388  198 ASP A CG  
9454  O OD1 . ASP D 182 ? 1.2228 1.1878 1.0534 -0.1573 -0.0763 0.1168  198 ASP A OD1 
9455  O OD2 . ASP D 182 ? 1.2375 1.1951 1.0706 -0.1660 -0.0854 0.1608  198 ASP A OD2 
9456  N N   . TYR D 183 ? 1.0617 1.0937 0.8373 -0.1732 -0.0614 0.0830  199 TYR A N   
9457  C CA  . TYR D 183 ? 1.0141 1.0435 0.7962 -0.1654 -0.0554 0.0559  199 TYR A CA  
9458  C C   . TYR D 183 ? 1.0301 1.0295 0.8389 -0.1520 -0.0581 0.0512  199 TYR A C   
9459  O O   . TYR D 183 ? 1.0181 1.0137 0.8354 -0.1437 -0.0593 0.0367  199 TYR A O   
9460  C CB  . TYR D 183 ? 0.9993 1.0382 0.7721 -0.1703 -0.0390 0.0365  199 TYR A CB  
9461  C CG  . TYR D 183 ? 0.9691 1.0091 0.7457 -0.1640 -0.0307 0.0093  199 TYR A CG  
9462  C CD1 . TYR D 183 ? 0.9652 1.0170 0.7375 -0.1628 -0.0355 0.0006  199 TYR A CD1 
9463  C CD2 . TYR D 183 ? 0.9862 1.0173 0.7709 -0.1599 -0.0172 -0.0074 199 TYR A CD2 
9464  C CE1 . TYR D 183 ? 0.9295 0.9812 0.7066 -0.1578 -0.0263 -0.0244 199 TYR A CE1 
9465  C CE2 . TYR D 183 ? 0.9511 0.9823 0.7402 -0.1540 -0.0083 -0.0306 199 TYR A CE2 
9466  C CZ  . TYR D 183 ? 0.9488 0.9892 0.7344 -0.1532 -0.0123 -0.0392 199 TYR A CZ  
9467  O OH  . TYR D 183 ? 0.9581 0.9970 0.7497 -0.1478 -0.0021 -0.0622 199 TYR A OH  
9468  N N   . GLY D 184 ? 0.9940 0.9728 0.8169 -0.1503 -0.0587 0.0629  200 GLY A N   
9469  C CA  . GLY D 184 ? 0.9861 0.9378 0.8341 -0.1383 -0.0625 0.0599  200 GLY A CA  
9470  C C   . GLY D 184 ? 0.9955 0.9429 0.8528 -0.1314 -0.0760 0.0691  200 GLY A C   
9471  O O   . GLY D 184 ? 0.9355 0.8713 0.8075 -0.1210 -0.0776 0.0568  200 GLY A O   
9472  N N   . ASP D 185 ? 1.0560 1.0145 0.9047 -0.1371 -0.0858 0.0913  201 ASP A N   
9473  C CA  . ASP D 185 ? 1.0219 0.9796 0.8798 -0.1305 -0.0995 0.1025  201 ASP A CA  
9474  C C   . ASP D 185 ? 0.9786 0.9548 0.8288 -0.1282 -0.1005 0.0847  201 ASP A C   
9475  O O   . ASP D 185 ? 0.9644 0.9319 0.8306 -0.1183 -0.1061 0.0785  201 ASP A O   
9476  C CB  . ASP D 185 ? 1.0859 1.0543 0.9344 -0.1378 -0.1089 0.1325  201 ASP A CB  
9477  C CG  . ASP D 185 ? 1.1053 1.0714 0.9671 -0.1301 -0.1243 0.1499  201 ASP A CG  
9478  O OD1 . ASP D 185 ? 1.1128 1.0562 0.9995 -0.1188 -0.1275 0.1455  201 ASP A OD1 
9479  O OD2 . ASP D 185 ? 1.0905 1.0775 0.9386 -0.1354 -0.1331 0.1701  201 ASP A OD2 
9480  N N   . TYR D 186 ? 0.9557 0.9571 0.7825 -0.1376 -0.0938 0.0747  202 TYR A N   
9481  C CA  . TYR D 186 ? 0.9044 0.9225 0.7247 -0.1369 -0.0915 0.0535  202 TYR A CA  
9482  C C   . TYR D 186 ? 0.9280 0.9249 0.7681 -0.1255 -0.0853 0.0326  202 TYR A C   
9483  O O   . TYR D 186 ? 0.9457 0.9419 0.7968 -0.1186 -0.0911 0.0262  202 TYR A O   
9484  C CB  . TYR D 186 ? 0.9534 0.9964 0.7488 -0.1487 -0.0807 0.0415  202 TYR A CB  
9485  C CG  . TYR D 186 ? 0.9706 1.0317 0.7587 -0.1501 -0.0754 0.0169  202 TYR A CG  
9486  C CD1 . TYR D 186 ? 1.0049 1.0529 0.8037 -0.1439 -0.0632 -0.0073 202 TYR A CD1 
9487  C CD2 . TYR D 186 ? 1.0507 1.1430 0.8211 -0.1584 -0.0817 0.0177  202 TYR A CD2 
9488  C CE1 . TYR D 186 ? 1.0746 1.1367 0.8692 -0.1455 -0.0569 -0.0299 202 TYR A CE1 
9489  C CE2 . TYR D 186 ? 1.1022 1.2109 0.8677 -0.1609 -0.0758 -0.0070 202 TYR A CE2 
9490  C CZ  . TYR D 186 ? 1.1312 1.2231 0.9098 -0.1545 -0.0629 -0.0308 202 TYR A CZ  
9491  O OH  . TYR D 186 ? 1.1422 1.2475 0.9185 -0.1570 -0.0555 -0.0555 202 TYR A OH  
9492  N N   . TRP D 187 ? 0.9186 0.8991 0.7645 -0.1232 -0.0737 0.0228  203 TRP A N   
9493  C CA  . TRP D 187 ? 0.8673 0.8301 0.7302 -0.1124 -0.0672 0.0039  203 TRP A CA  
9494  C C   . TRP D 187 ? 0.8737 0.8166 0.7588 -0.1018 -0.0772 0.0112  203 TRP A C   
9495  O O   . TRP D 187 ? 0.8903 0.8276 0.7870 -0.0937 -0.0768 -0.0019 203 TRP A O   
9496  C CB  . TRP D 187 ? 0.9090 0.8584 0.7758 -0.1107 -0.0552 -0.0043 203 TRP A CB  
9497  C CG  . TRP D 187 ? 0.9365 0.8997 0.7901 -0.1157 -0.0424 -0.0199 203 TRP A CG  
9498  C CD1 . TRP D 187 ? 0.9290 0.9121 0.7699 -0.1204 -0.0387 -0.0319 203 TRP A CD1 
9499  C CD2 . TRP D 187 ? 0.9598 0.9176 0.8143 -0.1152 -0.0300 -0.0284 203 TRP A CD2 
9500  N NE1 . TRP D 187 ? 0.9392 0.9290 0.7724 -0.1235 -0.0240 -0.0466 203 TRP A NE1 
9501  C CE2 . TRP D 187 ? 0.9424 0.9172 0.7841 -0.1198 -0.0187 -0.0441 203 TRP A CE2 
9502  C CE3 . TRP D 187 ? 0.9452 0.8870 0.8107 -0.1119 -0.0275 -0.0244 203 TRP A CE3 
9503  C CZ2 . TRP D 187 ? 0.9470 0.9230 0.7875 -0.1200 -0.0049 -0.0546 203 TRP A CZ2 
9504  C CZ3 . TRP D 187 ? 0.9498 0.8948 0.8129 -0.1126 -0.0147 -0.0349 203 TRP A CZ3 
9505  C CH2 . TRP D 187 ? 0.9783 0.9401 0.8293 -0.1161 -0.0036 -0.0492 203 TRP A CH2 
9506  N N   . ARG D 188 ? 0.9211 0.8516 0.8144 -0.1016 -0.0846 0.0312  204 ARG A N   
9507  C CA  . ARG D 188 ? 0.8968 0.8073 0.8135 -0.0914 -0.0931 0.0377  204 ARG A CA  
9508  C C   . ARG D 188 ? 0.8850 0.8081 0.8041 -0.0886 -0.1045 0.0422  204 ARG A C   
9509  O O   . ARG D 188 ? 0.8912 0.8011 0.8306 -0.0790 -0.1107 0.0432  204 ARG A O   
9510  C CB  . ARG D 188 ? 0.9276 0.8227 0.8535 -0.0929 -0.0982 0.0588  204 ARG A CB  
9511  C CG  . ARG D 188 ? 0.8665 0.7490 0.7937 -0.0958 -0.0880 0.0543  204 ARG A CG  
9512  C CD  . ARG D 188 ? 0.8613 0.7247 0.8035 -0.0965 -0.0927 0.0730  204 ARG A CD  
9513  N NE  . ARG D 188 ? 0.9329 0.8069 0.8640 -0.1057 -0.0987 0.0970  204 ARG A NE  
9514  C CZ  . ARG D 188 ? 0.9796 0.8660 0.8929 -0.1170 -0.0931 0.1031  204 ARG A CZ  
9515  N NH1 . ARG D 188 ? 0.9877 0.8787 0.8924 -0.1207 -0.0812 0.0865  204 ARG A NH1 
9516  N NH2 . ARG D 188 ? 1.0356 0.9305 0.9402 -0.1245 -0.0992 0.1272  204 ARG A NH2 
9517  N N   . GLY D 189 ? 0.8729 0.8230 0.7722 -0.0971 -0.1072 0.0446  205 GLY A N   
9518  C CA  . GLY D 189 ? 0.9084 0.8753 0.8089 -0.0950 -0.1165 0.0433  205 GLY A CA  
9519  C C   . GLY D 189 ? 0.9078 0.8636 0.8268 -0.0847 -0.1140 0.0245  205 GLY A C   
9520  O O   . GLY D 189 ? 0.9005 0.8529 0.8362 -0.0774 -0.1242 0.0310  205 GLY A O   
9521  N N   . ASP D 190 ? 0.8624 0.8118 0.7801 -0.0835 -0.1002 0.0024  206 ASP A N   
9522  C CA  . ASP D 190 ? 0.8552 0.7973 0.7876 -0.0750 -0.0960 -0.0164 206 ASP A CA  
9523  C C   . ASP D 190 ? 0.8334 0.7553 0.7911 -0.0634 -0.1032 -0.0106 206 ASP A C   
9524  O O   . ASP D 190 ? 0.8514 0.7705 0.8221 -0.0567 -0.1020 -0.0234 206 ASP A O   
9525  C CB  . ASP D 190 ? 0.8772 0.8082 0.8085 -0.0729 -0.0795 -0.0362 206 ASP A CB  
9526  C CG  . ASP D 190 ? 0.9079 0.8366 0.8503 -0.0664 -0.0734 -0.0560 206 ASP A CG  
9527  O OD1 . ASP D 190 ? 0.8590 0.7678 0.8194 -0.0562 -0.0715 -0.0602 206 ASP A OD1 
9528  O OD2 . ASP D 190 ? 0.9588 0.9065 0.8923 -0.0721 -0.0709 -0.0670 206 ASP A OD2 
9529  N N   . TYR D 191 ? 0.8242 0.7313 0.7906 -0.0611 -0.1095 0.0074  207 TYR A N   
9530  C CA  . TYR D 191 ? 0.8435 0.7311 0.8355 -0.0502 -0.1155 0.0119  207 TYR A CA  
9531  C C   . TYR D 191 ? 0.8478 0.7432 0.8483 -0.0488 -0.1312 0.0328  207 TYR A C   
9532  O O   . TYR D 191 ? 0.8766 0.7555 0.9000 -0.0399 -0.1369 0.0396  207 TYR A O   
9533  C CB  . TYR D 191 ? 0.8656 0.7274 0.8679 -0.0468 -0.1105 0.0147  207 TYR A CB  
9534  C CG  . TYR D 191 ? 0.8772 0.7304 0.8747 -0.0460 -0.0959 -0.0042 207 TYR A CG  
9535  C CD1 . TYR D 191 ? 0.8710 0.7320 0.8494 -0.0545 -0.0880 -0.0060 207 TYR A CD1 
9536  C CD2 . TYR D 191 ? 0.8253 0.6651 0.8375 -0.0364 -0.0899 -0.0200 207 TYR A CD2 
9537  C CE1 . TYR D 191 ? 0.8462 0.7013 0.8218 -0.0527 -0.0753 -0.0218 207 TYR A CE1 
9538  C CE2 . TYR D 191 ? 0.8149 0.6491 0.8226 -0.0348 -0.0771 -0.0352 207 TYR A CE2 
9539  C CZ  . TYR D 191 ? 0.8278 0.6698 0.8177 -0.0426 -0.0701 -0.0358 207 TYR A CZ  
9540  O OH  . TYR D 191 ? 0.8249 0.6629 0.8115 -0.0402 -0.0577 -0.0497 207 TYR A OH  
9541  N N   . GLU D 192 ? 0.8395 0.7608 0.8227 -0.0571 -0.1382 0.0430  208 GLU A N   
9542  C CA  . GLU D 192 ? 0.8286 0.7591 0.8176 -0.0561 -0.1535 0.0674  208 GLU A CA  
9543  C C   . GLU D 192 ? 0.8224 0.7627 0.8281 -0.0485 -0.1628 0.0644  208 GLU A C   
9544  O O   . GLU D 192 ? 0.8484 0.8012 0.8510 -0.0492 -0.1586 0.0444  208 GLU A O   
9545  C CB  . GLU D 192 ? 0.9036 0.8611 0.8655 -0.0683 -0.1574 0.0801  208 GLU A CB  
9546  C CG  . GLU D 192 ? 0.9478 0.9142 0.9117 -0.0685 -0.1720 0.1106  208 GLU A CG  
9547  C CD  . GLU D 192 ? 0.9577 0.9484 0.8924 -0.0815 -0.1735 0.1242  208 GLU A CD  
9548  O OE1 . GLU D 192 ? 0.9028 0.9066 0.8152 -0.0908 -0.1635 0.1080  208 GLU A OE1 
9549  O OE2 . GLU D 192 ? 1.0240 1.0221 0.9587 -0.0820 -0.1847 0.1516  208 GLU A OE2 
9550  N N   . VAL D 193 ? 0.9049 0.8390 0.9304 -0.0411 -0.1747 0.0842  209 VAL A N   
9551  C CA  . VAL D 193 ? 0.9189 0.8640 0.9632 -0.0331 -0.1850 0.0848  209 VAL A CA  
9552  C C   . VAL D 193 ? 1.0264 0.9824 1.0768 -0.0312 -0.2009 0.1153  209 VAL A C   
9553  O O   . VAL D 193 ? 1.0370 0.9713 1.1009 -0.0267 -0.2031 0.1336  209 VAL A O   
9554  C CB  . VAL D 193 ? 0.9154 0.8345 0.9889 -0.0209 -0.1807 0.0726  209 VAL A CB  
9555  C CG1 . VAL D 193 ? 0.9245 0.8556 1.0195 -0.0126 -0.1923 0.0768  209 VAL A CG1 
9556  C CG2 . VAL D 193 ? 0.9619 0.8748 1.0296 -0.0220 -0.1660 0.0439  209 VAL A CG2 
9557  N N   . ASN D 194 ? 0.9593 0.9494 1.0019 -0.0340 -0.2120 0.1206  210 ASN A N   
9558  C CA  . ASN D 194 ? 0.9129 0.9212 0.9557 -0.0334 -0.2277 0.1511  210 ASN A CA  
9559  C C   . ASN D 194 ? 0.9933 1.0192 1.0579 -0.0243 -0.2411 0.1551  210 ASN A C   
9560  O O   . ASN D 194 ? 0.9642 1.0076 1.0293 -0.0251 -0.2403 0.1337  210 ASN A O   
9561  C CB  . ASN D 194 ? 0.8719 0.9126 0.8800 -0.0472 -0.2300 0.1572  210 ASN A CB  
9562  C CG  . ASN D 194 ? 0.9362 0.9619 0.9251 -0.0556 -0.2198 0.1620  210 ASN A CG  
9563  O OD1 . ASN D 194 ? 0.9866 0.9941 0.9828 -0.0533 -0.2220 0.1851  210 ASN A OD1 
9564  N ND2 . ASN D 194 ? 0.9694 1.0039 0.9347 -0.0659 -0.2082 0.1405  210 ASN A ND2 
9565  N N   . GLY D 195 ? 1.0477 1.0692 1.1319 -0.0156 -0.2530 0.1832  211 GLY A N   
9566  C CA  . GLY D 195 ? 1.0035 1.0440 1.1098 -0.0061 -0.2673 0.1919  211 GLY A CA  
9567  C C   . GLY D 195 ? 1.0419 1.0761 1.1709 0.0014  -0.2629 0.1655  211 GLY A C   
9568  O O   . GLY D 195 ? 1.0221 1.0867 1.1502 -0.0002 -0.2686 0.1540  211 GLY A O   
9569  N N   . VAL D 196 ? 1.0919 1.0882 1.2406 0.0087  -0.2520 0.1545  212 VAL A N   
9570  C CA  . VAL D 196 ? 1.0928 1.0779 1.2714 0.0194  -0.2495 0.1375  212 VAL A CA  
9571  C C   . VAL D 196 ? 1.1930 1.1430 1.4011 0.0310  -0.2488 0.1513  212 VAL A C   
9572  O O   . VAL D 196 ? 1.1662 1.0851 1.3732 0.0301  -0.2366 0.1437  212 VAL A O   
9573  C CB  . VAL D 196 ? 1.0078 0.9829 1.1786 0.0154  -0.2334 0.1037  212 VAL A CB  
9574  C CG1 . VAL D 196 ? 1.0052 0.9760 1.2052 0.0256  -0.2321 0.0876  212 VAL A CG1 
9575  C CG2 . VAL D 196 ? 1.0044 1.0094 1.1441 0.0022  -0.2313 0.0903  212 VAL A CG2 
9576  N N   . ASP D 197 ? 1.2273 1.1825 1.4624 0.0418  -0.2616 0.1715  213 ASP A N   
9577  C CA  . ASP D 197 ? 1.2790 1.1999 1.5426 0.0521  -0.2604 0.1863  213 ASP A CA  
9578  C C   . ASP D 197 ? 1.2958 1.1835 1.5761 0.0570  -0.2456 0.1611  213 ASP A C   
9579  O O   . ASP D 197 ? 1.2609 1.1518 1.5589 0.0636  -0.2439 0.1432  213 ASP A O   
9580  C CB  . ASP D 197 ? 1.3705 1.3005 1.6667 0.0652  -0.2751 0.2092  213 ASP A CB  
9581  C CG  . ASP D 197 ? 1.5141 1.4607 1.8013 0.0635  -0.2883 0.2451  213 ASP A CG  
9582  O OD1 . ASP D 197 ? 1.5125 1.4357 1.7940 0.0603  -0.2837 0.2602  213 ASP A OD1 
9583  O OD2 . ASP D 197 ? 1.5990 1.5818 1.8861 0.0655  -0.3031 0.2587  213 ASP A OD2 
9584  N N   . GLY D 198 ? 1.3374 1.1952 1.6121 0.0534  -0.2349 0.1595  214 GLY A N   
9585  C CA  . GLY D 198 ? 1.2698 1.0967 1.5595 0.0577  -0.2213 0.1376  214 GLY A CA  
9586  C C   . GLY D 198 ? 1.2673 1.0913 1.5303 0.0484  -0.2077 0.1121  214 GLY A C   
9587  O O   . GLY D 198 ? 1.2683 1.0700 1.5409 0.0516  -0.1962 0.0928  214 GLY A O   
9588  N N   . TYR D 199 ? 1.1319 0.9782 1.3623 0.0372  -0.2084 0.1116  215 TYR A N   
9589  C CA  . TYR D 199 ? 1.0718 0.9183 1.2777 0.0290  -0.1955 0.0877  215 TYR A CA  
9590  C C   . TYR D 199 ? 1.0455 0.9031 1.2181 0.0161  -0.1945 0.0959  215 TYR A C   
9591  O O   . TYR D 199 ? 1.0061 0.8700 1.1564 0.0086  -0.1851 0.0780  215 TYR A O   
9592  C CB  . TYR D 199 ? 1.0241 0.8920 1.2278 0.0294  -0.1946 0.0680  215 TYR A CB  
9593  C CG  . TYR D 199 ? 1.0098 0.8660 1.2434 0.0408  -0.1914 0.0538  215 TYR A CG  
9594  C CD1 . TYR D 199 ? 1.0195 0.8531 1.2573 0.0434  -0.1772 0.0331  215 TYR A CD1 
9595  C CD2 . TYR D 199 ? 0.9985 0.8671 1.2566 0.0492  -0.2025 0.0621  215 TYR A CD2 
9596  C CE1 . TYR D 199 ? 0.9881 0.8124 1.2519 0.0533  -0.1737 0.0204  215 TYR A CE1 
9597  C CE2 . TYR D 199 ? 1.0002 0.8590 1.2860 0.0593  -0.1989 0.0491  215 TYR A CE2 
9598  C CZ  . TYR D 199 ? 0.9635 0.8001 1.2515 0.0611  -0.1843 0.0283  215 TYR A CZ  
9599  O OH  . TYR D 199 ? 1.0395 0.8681 1.3547 0.0709  -0.1806 0.0158  215 TYR A OH  
9600  N N   . ASP D 200 ? 1.1360 0.9971 1.3054 0.0135  -0.2035 0.1227  216 ASP A N   
9601  C CA  . ASP D 200 ? 1.0561 0.9301 1.1943 0.0010  -0.2028 0.1322  216 ASP A CA  
9602  C C   . ASP D 200 ? 1.0382 0.8870 1.1685 -0.0039 -0.1895 0.1237  216 ASP A C   
9603  O O   . ASP D 200 ? 1.0415 0.8627 1.1921 0.0026  -0.1830 0.1156  216 ASP A O   
9604  C CB  . ASP D 200 ? 1.2046 1.0879 1.3435 0.0004  -0.2157 0.1657  216 ASP A CB  
9605  C CG  . ASP D 200 ? 1.3003 1.2146 1.4446 0.0046  -0.2309 0.1772  216 ASP A CG  
9606  O OD1 . ASP D 200 ? 1.3297 1.2684 1.4629 0.0017  -0.2314 0.1596  216 ASP A OD1 
9607  O OD2 . ASP D 200 ? 1.4162 1.3313 1.5765 0.0108  -0.2422 0.2046  216 ASP A OD2 
9608  N N   . TYR D 201 ? 1.0153 0.8755 1.1162 -0.0157 -0.1854 0.1253  217 TYR A N   
9609  C CA  . TYR D 201 ? 1.0207 0.8625 1.1118 -0.0215 -0.1727 0.1162  217 TYR A CA  
9610  C C   . TYR D 201 ? 1.0021 0.8604 1.0629 -0.0346 -0.1713 0.1260  217 TYR A C   
9611  O O   . TYR D 201 ? 0.9841 0.8653 1.0216 -0.0415 -0.1686 0.1146  217 TYR A O   
9612  C CB  . TYR D 201 ? 0.9881 0.8239 1.0776 -0.0194 -0.1607 0.0858  217 TYR A CB  
9613  C CG  . TYR D 201 ? 0.9896 0.8030 1.0781 -0.0215 -0.1482 0.0748  217 TYR A CG  
9614  C CD1 . TYR D 201 ? 0.9770 0.7976 1.0404 -0.0315 -0.1399 0.0692  217 TYR A CD1 
9615  C CD2 . TYR D 201 ? 1.0171 0.8041 1.1301 -0.0135 -0.1446 0.0688  217 TYR A CD2 
9616  C CE1 . TYR D 201 ? 1.0122 0.8157 1.0756 -0.0332 -0.1294 0.0594  217 TYR A CE1 
9617  C CE2 . TYR D 201 ? 1.0090 0.7793 1.1206 -0.0159 -0.1339 0.0579  217 TYR A CE2 
9618  C CZ  . TYR D 201 ? 1.0045 0.7838 1.0915 -0.0256 -0.1267 0.0537  217 TYR A CZ  
9619  O OH  . TYR D 201 ? 0.9823 0.7477 1.0690 -0.0277 -0.1168 0.0430  217 TYR A OH  
9620  N N   . SER D 202 ? 1.0035 0.8497 1.0655 -0.0384 -0.1723 0.1464  218 SER A N   
9621  C CA  . SER D 202 ? 0.9567 0.8163 0.9928 -0.0508 -0.1709 0.1595  218 SER A CA  
9622  C C   . SER D 202 ? 1.0060 0.8625 1.0245 -0.0585 -0.1566 0.1392  218 SER A C   
9623  O O   . SER D 202 ? 1.0379 0.8747 1.0681 -0.0541 -0.1479 0.1209  218 SER A O   
9624  C CB  . SER D 202 ? 1.0116 0.8557 1.0602 -0.0511 -0.1757 0.1885  218 SER A CB  
9625  O OG  . SER D 202 ? 1.0389 0.8519 1.1035 -0.0504 -0.1667 0.1834  218 SER A OG  
9626  N N   . ARG D 203 ? 1.0341 0.9125 1.0241 -0.0700 -0.1542 0.1425  219 ARG A N   
9627  C CA  . ARG D 203 ? 0.9988 0.8778 0.9719 -0.0773 -0.1406 0.1242  219 ARG A CA  
9628  C C   . ARG D 203 ? 0.9773 0.8333 0.9582 -0.0803 -0.1335 0.1290  219 ARG A C   
9629  O O   . ARG D 203 ? 0.9765 0.8297 0.9494 -0.0842 -0.1223 0.1130  219 ARG A O   
9630  C CB  . ARG D 203 ? 0.9859 0.8950 0.9282 -0.0890 -0.1395 0.1266  219 ARG A CB  
9631  C CG  . ARG D 203 ? 0.9769 0.9120 0.9095 -0.0885 -0.1453 0.1188  219 ARG A CG  
9632  C CD  . ARG D 203 ? 1.0440 1.0056 0.9461 -0.1009 -0.1395 0.1133  219 ARG A CD  
9633  N NE  . ARG D 203 ? 1.0938 1.0665 0.9813 -0.1099 -0.1439 0.1387  219 ARG A NE  
9634  C CZ  . ARG D 203 ? 1.0889 1.0876 0.9634 -0.1141 -0.1549 0.1560  219 ARG A CZ  
9635  N NH1 . ARG D 203 ? 1.1143 1.1349 0.9858 -0.1121 -0.1619 0.1477  219 ARG A NH1 
9636  N NH2 . ARG D 203 ? 1.1281 1.1335 0.9915 -0.1214 -0.1583 0.1818  219 ARG A NH2 
9637  N N   . GLY D 204 ? 1.0164 0.8575 1.0130 -0.0789 -0.1397 0.1513  220 GLY A N   
9638  C CA  . GLY D 204 ? 1.0123 0.8289 1.0219 -0.0811 -0.1328 0.1532  220 GLY A CA  
9639  C C   . GLY D 204 ? 1.0644 0.8556 1.1026 -0.0700 -0.1316 0.1402  220 GLY A C   
9640  O O   . GLY D 204 ? 1.2036 0.9762 1.2524 -0.0710 -0.1237 0.1314  220 GLY A O   
9641  N N   . GLN D 205 ? 1.0164 0.8082 1.0676 -0.0598 -0.1390 0.1382  221 GLN A N   
9642  C CA  . GLN D 205 ? 1.0641 0.8327 1.1426 -0.0493 -0.1372 0.1250  221 GLN A CA  
9643  C C   . GLN D 205 ? 1.0903 0.8565 1.1629 -0.0487 -0.1258 0.0966  221 GLN A C   
9644  O O   . GLN D 205 ? 1.1195 0.8655 1.2104 -0.0438 -0.1206 0.0846  221 GLN A O   
9645  C CB  . GLN D 205 ? 1.1097 0.8829 1.2025 -0.0386 -0.1469 0.1274  221 GLN A CB  
9646  C CG  . GLN D 205 ? 1.1770 0.9264 1.3004 -0.0275 -0.1457 0.1170  221 GLN A CG  
9647  C CD  . GLN D 205 ? 1.2413 0.9649 1.3871 -0.0274 -0.1454 0.1311  221 GLN A CD  
9648  O OE1 . GLN D 205 ? 1.3669 1.0910 1.5147 -0.0304 -0.1520 0.1568  221 GLN A OE1 
9649  N NE2 . GLN D 205 ? 1.1667 0.8684 1.3294 -0.0246 -0.1373 0.1144  221 GLN A NE2 
9650  N N   . LEU D 206 ? 1.0629 0.8501 1.1103 -0.0539 -0.1212 0.0859  222 LEU A N   
9651  C CA  . LEU D 206 ? 1.0580 0.8441 1.0989 -0.0536 -0.1097 0.0618  222 LEU A CA  
9652  C C   . LEU D 206 ? 1.0810 0.8550 1.1232 -0.0597 -0.1021 0.0608  222 LEU A C   
9653  O O   . LEU D 206 ? 1.1452 0.9078 1.1968 -0.0557 -0.0953 0.0443  222 LEU A O   
9654  C CB  . LEU D 206 ? 1.0039 0.8144 1.0193 -0.0582 -0.1056 0.0519  222 LEU A CB  
9655  C CG  . LEU D 206 ? 0.9072 0.7186 0.9152 -0.0573 -0.0933 0.0291  222 LEU A CG  
9656  C CD1 . LEU D 206 ? 0.8904 0.6945 0.9119 -0.0463 -0.0918 0.0131  222 LEU A CD1 
9657  C CD2 . LEU D 206 ? 0.9294 0.7645 0.9123 -0.0646 -0.0889 0.0244  222 LEU A CD2 
9658  N N   . ILE D 207 ? 1.1062 0.8840 1.1395 -0.0696 -0.1031 0.0781  223 ILE A N   
9659  C CA  . ILE D 207 ? 1.0787 0.8460 1.1154 -0.0760 -0.0956 0.0759  223 ILE A CA  
9660  C C   . ILE D 207 ? 1.1109 0.8516 1.1768 -0.0708 -0.0965 0.0757  223 ILE A C   
9661  O O   . ILE D 207 ? 1.1167 0.8482 1.1907 -0.0703 -0.0893 0.0596  223 ILE A O   
9662  C CB  . ILE D 207 ? 1.0897 0.8667 1.1116 -0.0885 -0.0955 0.0949  223 ILE A CB  
9663  C CG1 . ILE D 207 ? 1.0453 0.8489 1.0382 -0.0947 -0.0910 0.0888  223 ILE A CG1 
9664  C CG2 . ILE D 207 ? 1.0572 0.8206 1.0887 -0.0949 -0.0888 0.0944  223 ILE A CG2 
9665  C CD1 . ILE D 207 ? 0.9749 0.7913 0.9510 -0.1074 -0.0904 0.1071  223 ILE A CD1 
9666  N N   . GLU D 208 ? 1.2230 0.9522 1.3059 -0.0667 -0.1051 0.0927  224 GLU A N   
9667  C CA  . GLU D 208 ? 1.2893 0.9923 1.4022 -0.0617 -0.1050 0.0908  224 GLU A CA  
9668  C C   . GLU D 208 ? 1.3360 1.0332 1.4586 -0.0523 -0.1008 0.0655  224 GLU A C   
9669  O O   . GLU D 208 ? 1.3945 1.0780 1.5302 -0.0526 -0.0946 0.0524  224 GLU A O   
9670  C CB  . GLU D 208 ? 1.3478 1.0391 1.4805 -0.0565 -0.1147 0.1127  224 GLU A CB  
9671  C CG  . GLU D 208 ? 1.4988 1.1875 1.6305 -0.0652 -0.1177 0.1405  224 GLU A CG  
9672  C CD  . GLU D 208 ? 1.6174 1.3095 1.7555 -0.0598 -0.1294 0.1657  224 GLU A CD  
9673  O OE1 . GLU D 208 ? 1.6235 1.3115 1.7776 -0.0483 -0.1350 0.1615  224 GLU A OE1 
9674  O OE2 . GLU D 208 ? 1.7222 1.4227 1.8491 -0.0669 -0.1331 0.1899  224 GLU A OE2 
9675  N N   . ASP D 209 ? 1.1469 0.8555 1.2634 -0.0444 -0.1038 0.0578  225 ASP A N   
9676  C CA  . ASP D 209 ? 1.1143 0.8170 1.2408 -0.0351 -0.0994 0.0353  225 ASP A CA  
9677  C C   . ASP D 209 ? 1.1038 0.8134 1.2166 -0.0379 -0.0891 0.0155  225 ASP A C   
9678  O O   . ASP D 209 ? 1.1143 0.8138 1.2391 -0.0336 -0.0840 -0.0005 225 ASP A O   
9679  C CB  . ASP D 209 ? 1.0146 0.7280 1.1391 -0.0267 -0.1041 0.0317  225 ASP A CB  
9680  C CG  . ASP D 209 ? 1.1020 0.8088 1.2452 -0.0211 -0.1143 0.0481  225 ASP A CG  
9681  O OD1 . ASP D 209 ? 1.1201 0.8079 1.2848 -0.0203 -0.1165 0.0581  225 ASP A OD1 
9682  O OD2 . ASP D 209 ? 1.2391 0.9596 1.3779 -0.0166 -0.1197 0.0492  225 ASP A OD2 
9683  N N   . VAL D 210 ? 1.0622 0.7902 1.1505 -0.0446 -0.0859 0.0160  226 VAL A N   
9684  C CA  . VAL D 210 ? 1.0402 0.7756 1.1173 -0.0462 -0.0761 -0.0013 226 VAL A CA  
9685  C C   . VAL D 210 ? 1.0332 0.7574 1.1210 -0.0518 -0.0722 -0.0035 226 VAL A C   
9686  O O   . VAL D 210 ? 1.0057 0.7275 1.0986 -0.0487 -0.0662 -0.0205 226 VAL A O   
9687  C CB  . VAL D 210 ? 1.0317 0.7885 1.0827 -0.0527 -0.0728 0.0005  226 VAL A CB  
9688  C CG1 . VAL D 210 ? 0.9510 0.7151 0.9928 -0.0562 -0.0629 -0.0124 226 VAL A CG1 
9689  C CG2 . VAL D 210 ? 0.9809 0.7492 1.0227 -0.0470 -0.0744 -0.0041 226 VAL A CG2 
9690  N N   . GLU D 211 ? 1.0197 0.7375 1.1120 -0.0603 -0.0754 0.0138  227 GLU A N   
9691  C CA  . GLU D 211 ? 1.0515 0.7579 1.1567 -0.0667 -0.0713 0.0113  227 GLU A CA  
9692  C C   . GLU D 211 ? 1.0343 0.7203 1.1662 -0.0599 -0.0718 0.0016  227 GLU A C   
9693  O O   . GLU D 211 ? 1.0382 0.7211 1.1775 -0.0606 -0.0660 -0.0149 227 GLU A O   
9694  C CB  . GLU D 211 ? 1.0600 0.7629 1.1652 -0.0777 -0.0737 0.0332  227 GLU A CB  
9695  C CG  . GLU D 211 ? 1.0260 0.7500 1.1059 -0.0873 -0.0696 0.0377  227 GLU A CG  
9696  C CD  . GLU D 211 ? 1.0691 0.7919 1.1464 -0.0984 -0.0717 0.0615  227 GLU A CD  
9697  O OE1 . GLU D 211 ? 1.0652 0.7715 1.1589 -0.0977 -0.0775 0.0778  227 GLU A OE1 
9698  O OE2 . GLU D 211 ? 1.0467 0.7856 1.1057 -0.1077 -0.0670 0.0644  227 GLU A OE2 
9699  N N   . HIS D 212 ? 1.1045 0.7780 1.2515 -0.0533 -0.0785 0.0108  228 HIS A N   
9700  C CA  A HIS D 212 ? 1.3148 0.9684 1.4890 -0.0472 -0.0781 0.0012  228 HIS A CA  
9701  C CA  B HIS D 212 ? 1.5903 1.2439 1.7645 -0.0468 -0.0783 0.0013  228 HIS A CA  
9702  C C   . HIS D 212 ? 1.0647 0.7237 1.2374 -0.0390 -0.0732 -0.0232 228 HIS A C   
9703  O O   . HIS D 212 ? 1.0986 0.7462 1.2886 -0.0371 -0.0695 -0.0374 228 HIS A O   
9704  C CB  A HIS D 212 ? 1.0260 0.6665 1.2182 -0.0407 -0.0862 0.0172  228 HIS A CB  
9705  C CB  B HIS D 212 ? 1.1173 0.7591 1.3085 -0.0395 -0.0864 0.0160  228 HIS A CB  
9706  C CG  A HIS D 212 ? 1.1366 0.7675 1.3363 -0.0480 -0.0903 0.0420  228 HIS A CG  
9707  C CG  B HIS D 212 ? 1.1103 0.7323 1.3306 -0.0318 -0.0854 0.0049  228 HIS A CG  
9708  N ND1 A HIS D 212 ? 1.0956 0.7203 1.3062 -0.0432 -0.0988 0.0628  228 HIS A ND1 
9709  N ND1 B HIS D 212 ? 1.0528 0.6526 1.2996 -0.0345 -0.0852 0.0116  228 HIS A ND1 
9710  C CD2 A HIS D 212 ? 1.0942 0.7213 1.2927 -0.0597 -0.0868 0.0504  228 HIS A CD2 
9711  C CD2 B HIS D 212 ? 1.0446 0.6657 1.2722 -0.0219 -0.0836 -0.0131 228 HIS A CD2 
9712  C CE1 A HIS D 212 ? 1.0848 0.7018 1.2997 -0.0512 -0.1002 0.0840  228 HIS A CE1 
9713  C CE1 B HIS D 212 ? 0.9942 0.5805 1.2636 -0.0265 -0.0833 -0.0029 228 HIS A CE1 
9714  N NE2 A HIS D 212 ? 1.0406 0.6583 1.2486 -0.0617 -0.0926 0.0767  228 HIS A NE2 
9715  N NE2 B HIS D 212 ? 0.9778 0.5775 1.2354 -0.0188 -0.0824 -0.0178 228 HIS A NE2 
9716  N N   . THR D 213 ? 1.1064 0.7828 1.2588 -0.0345 -0.0722 -0.0288 229 THR A N   
9717  C CA  . THR D 213 ? 1.0816 0.7625 1.2330 -0.0266 -0.0667 -0.0504 229 THR A CA  
9718  C C   . THR D 213 ? 1.0413 0.7334 1.1811 -0.0315 -0.0591 -0.0633 229 THR A C   
9719  O O   . THR D 213 ? 1.0262 0.7179 1.1721 -0.0275 -0.0544 -0.0806 229 THR A O   
9720  C CB  . THR D 213 ? 0.9989 0.6912 1.1382 -0.0183 -0.0676 -0.0527 229 THR A CB  
9721  O OG1 . THR D 213 ? 0.9699 0.6792 1.0858 -0.0233 -0.0674 -0.0452 229 THR A OG1 
9722  C CG2 . THR D 213 ? 0.9685 0.6513 1.1235 -0.0119 -0.0749 -0.0443 229 THR A CG2 
9723  N N   . PHE D 214 ? 1.0429 0.7463 1.1668 -0.0404 -0.0579 -0.0550 230 PHE A N   
9724  C CA  . PHE D 214 ? 0.9492 0.6647 1.0646 -0.0450 -0.0511 -0.0663 230 PHE A CA  
9725  C C   . PHE D 214 ? 0.9518 0.6563 1.0859 -0.0509 -0.0496 -0.0727 230 PHE A C   
9726  O O   . PHE D 214 ? 0.9066 0.6198 1.0402 -0.0512 -0.0445 -0.0885 230 PHE A O   
9727  C CB  . PHE D 214 ? 0.9647 0.6952 1.0607 -0.0533 -0.0497 -0.0559 230 PHE A CB  
9728  C CG  . PHE D 214 ? 0.9654 0.7104 1.0533 -0.0573 -0.0430 -0.0662 230 PHE A CG  
9729  C CD1 . PHE D 214 ? 0.9283 0.6859 1.0076 -0.0493 -0.0379 -0.0806 230 PHE A CD1 
9730  C CD2 . PHE D 214 ? 0.9862 0.7332 1.0761 -0.0688 -0.0416 -0.0612 230 PHE A CD2 
9731  C CE1 . PHE D 214 ? 0.9246 0.6981 0.9975 -0.0519 -0.0321 -0.0895 230 PHE A CE1 
9732  C CE2 . PHE D 214 ? 0.9933 0.7565 1.0773 -0.0723 -0.0356 -0.0714 230 PHE A CE2 
9733  C CZ  . PHE D 214 ? 0.9896 0.7668 1.0649 -0.0634 -0.0313 -0.0853 230 PHE A CZ  
9734  N N   . GLU D 215 ? 0.9557 0.6421 1.1071 -0.0556 -0.0538 -0.0608 231 GLU A N   
9735  C CA  . GLU D 215 ? 0.9495 0.6220 1.1232 -0.0606 -0.0517 -0.0690 231 GLU A CA  
9736  C C   . GLU D 215 ? 0.9181 0.5879 1.1025 -0.0522 -0.0490 -0.0904 231 GLU A C   
9737  O O   . GLU D 215 ? 0.9779 0.6495 1.1705 -0.0565 -0.0447 -0.1057 231 GLU A O   
9738  C CB  . GLU D 215 ? 0.9805 0.6302 1.1749 -0.0641 -0.0561 -0.0524 231 GLU A CB  
9739  C CG  . GLU D 215 ? 1.0783 0.7278 1.2686 -0.0763 -0.0565 -0.0340 231 GLU A CG  
9740  C CD  . GLU D 215 ? 1.1144 0.7659 1.3112 -0.0877 -0.0504 -0.0438 231 GLU A CD  
9741  O OE1 . GLU D 215 ? 1.0807 0.7215 1.2979 -0.0881 -0.0474 -0.0596 231 GLU A OE1 
9742  O OE2 . GLU D 215 ? 1.2668 0.9321 1.4483 -0.0965 -0.0483 -0.0364 231 GLU A OE2 
9743  N N   . GLU D 216 ? 0.9031 0.5698 1.0882 -0.0409 -0.0512 -0.0922 232 GLU A N   
9744  C CA  . GLU D 216 ? 0.9686 0.6348 1.1622 -0.0329 -0.0478 -0.1126 232 GLU A CA  
9745  C C   . GLU D 216 ? 0.8952 0.5839 1.0682 -0.0291 -0.0427 -0.1261 232 GLU A C   
9746  O O   . GLU D 216 ? 0.9054 0.5985 1.0828 -0.0258 -0.0386 -0.1442 232 GLU A O   
9747  C CB  . GLU D 216 ? 1.0415 0.6962 1.2460 -0.0220 -0.0511 -0.1107 232 GLU A CB  
9748  C CG  . GLU D 216 ? 1.0993 0.7341 1.3226 -0.0230 -0.0573 -0.0929 232 GLU A CG  
9749  C CD  . GLU D 216 ? 1.1980 0.8237 1.4350 -0.0115 -0.0605 -0.0928 232 GLU A CD  
9750  O OE1 . GLU D 216 ? 1.2345 0.8553 1.4845 -0.0056 -0.0566 -0.1106 232 GLU A OE1 
9751  O OE2 . GLU D 216 ? 1.1778 0.8024 1.4132 -0.0087 -0.0670 -0.0753 232 GLU A OE2 
9752  N N   . ILE D 217 ? 0.9424 0.6462 1.0934 -0.0293 -0.0423 -0.1178 233 ILE A N   
9753  C CA  . ILE D 217 ? 0.8633 0.5878 0.9979 -0.0261 -0.0366 -0.1296 233 ILE A CA  
9754  C C   . ILE D 217 ? 0.8637 0.5972 1.0007 -0.0346 -0.0337 -0.1385 233 ILE A C   
9755  O O   . ILE D 217 ? 0.8866 0.6341 1.0198 -0.0312 -0.0296 -0.1534 233 ILE A O   
9756  C CB  . ILE D 217 ? 0.8605 0.5987 0.9732 -0.0244 -0.0356 -0.1201 233 ILE A CB  
9757  C CG1 . ILE D 217 ? 0.9401 0.6758 1.0499 -0.0137 -0.0358 -0.1206 233 ILE A CG1 
9758  C CG2 . ILE D 217 ? 0.8116 0.5706 0.9100 -0.0238 -0.0296 -0.1282 233 ILE A CG2 
9759  C CD1 . ILE D 217 ? 0.9726 0.7170 1.0656 -0.0133 -0.0357 -0.1103 233 ILE A CD1 
9760  N N   . LYS D 218 ? 0.8859 0.6125 1.0304 -0.0460 -0.0357 -0.1296 234 LYS A N   
9761  C CA  . LYS D 218 ? 0.8786 0.6182 1.0225 -0.0558 -0.0326 -0.1357 234 LYS A CA  
9762  C C   . LYS D 218 ? 0.8394 0.5887 0.9901 -0.0544 -0.0293 -0.1572 234 LYS A C   
9763  O O   . LYS D 218 ? 0.8381 0.6100 0.9776 -0.0556 -0.0262 -0.1640 234 LYS A O   
9764  C CB  . LYS D 218 ? 0.8692 0.5945 1.0273 -0.0686 -0.0345 -0.1254 234 LYS A CB  
9765  C CG  . LYS D 218 ? 0.8657 0.5944 1.0107 -0.0747 -0.0359 -0.1054 234 LYS A CG  
9766  C CD  . LYS D 218 ? 0.9272 0.6412 1.0879 -0.0871 -0.0368 -0.0954 234 LYS A CD  
9767  C CE  . LYS D 218 ? 1.0204 0.7338 1.1700 -0.0925 -0.0391 -0.0729 234 LYS A CE  
9768  N NZ  . LYS D 218 ? 1.0819 0.7794 1.2496 -0.1044 -0.0390 -0.0633 234 LYS A NZ  
9769  N N   . PRO D 219 ? 0.8148 0.5506 0.9832 -0.0518 -0.0295 -0.1688 235 PRO A N   
9770  C CA  . PRO D 219 ? 0.8132 0.5624 0.9861 -0.0519 -0.0261 -0.1907 235 PRO A CA  
9771  C C   . PRO D 219 ? 0.8384 0.6097 0.9927 -0.0409 -0.0234 -0.1988 235 PRO A C   
9772  O O   . PRO D 219 ? 0.7967 0.5912 0.9442 -0.0428 -0.0210 -0.2092 235 PRO A O   
9773  C CB  . PRO D 219 ? 0.7826 0.5098 0.9789 -0.0509 -0.0265 -0.2001 235 PRO A CB  
9774  C CG  . PRO D 219 ? 0.8058 0.5085 1.0142 -0.0550 -0.0300 -0.1821 235 PRO A CG  
9775  C CD  . PRO D 219 ? 0.8333 0.5420 1.0210 -0.0506 -0.0326 -0.1634 235 PRO A CD  
9776  N N   . LEU D 220 ? 0.8407 0.6065 0.9881 -0.0293 -0.0234 -0.1944 236 LEU A N   
9777  C CA  . LEU D 220 ? 0.8165 0.6026 0.9456 -0.0190 -0.0197 -0.1985 236 LEU A CA  
9778  C C   . LEU D 220 ? 0.8122 0.6187 0.9249 -0.0217 -0.0182 -0.1914 236 LEU A C   
9779  O O   . LEU D 220 ? 0.7736 0.6033 0.8763 -0.0179 -0.0149 -0.1991 236 LEU A O   
9780  C CB  . LEU D 220 ? 0.7996 0.5761 0.9229 -0.0083 -0.0195 -0.1908 236 LEU A CB  
9781  C CG  . LEU D 220 ? 0.6993 0.4958 0.8050 0.0022  -0.0142 -0.1947 236 LEU A CG  
9782  C CD1 . LEU D 220 ? 0.7449 0.5563 0.8526 0.0042  -0.0114 -0.2123 236 LEU A CD1 
9783  C CD2 . LEU D 220 ? 0.5605 0.3505 0.6597 0.0126  -0.0122 -0.1884 236 LEU A CD2 
9784  N N   . TYR D 221 ? 0.7645 0.5637 0.8746 -0.0281 -0.0203 -0.1762 237 TYR A N   
9785  C CA  . TYR D 221 ? 0.7745 0.5928 0.8703 -0.0309 -0.0180 -0.1697 237 TYR A CA  
9786  C C   . TYR D 221 ? 0.8267 0.6632 0.9266 -0.0388 -0.0170 -0.1796 237 TYR A C   
9787  O O   . TYR D 221 ? 0.8746 0.7354 0.9638 -0.0348 -0.0139 -0.1837 237 TYR A O   
9788  C CB  . TYR D 221 ? 0.7418 0.5501 0.8339 -0.0374 -0.0202 -0.1524 237 TYR A CB  
9789  C CG  . TYR D 221 ? 0.7493 0.5782 0.8272 -0.0401 -0.0167 -0.1474 237 TYR A CG  
9790  C CD1 . TYR D 221 ? 0.7015 0.5453 0.7650 -0.0302 -0.0121 -0.1481 237 TYR A CD1 
9791  C CD2 . TYR D 221 ? 0.7570 0.5907 0.8376 -0.0525 -0.0171 -0.1424 237 TYR A CD2 
9792  C CE1 . TYR D 221 ? 0.7343 0.5968 0.7874 -0.0317 -0.0081 -0.1443 237 TYR A CE1 
9793  C CE2 . TYR D 221 ? 0.7355 0.5891 0.8047 -0.0545 -0.0133 -0.1388 237 TYR A CE2 
9794  C CZ  . TYR D 221 ? 0.7342 0.6021 0.7900 -0.0438 -0.0089 -0.1400 237 TYR A CZ  
9795  O OH  . TYR D 221 ? 0.7374 0.6250 0.7839 -0.0452 -0.0043 -0.1368 237 TYR A OH  
9796  N N   . GLU D 222 ? 0.8685 0.6941 0.9852 -0.0500 -0.0195 -0.1835 238 GLU A N   
9797  C CA  . GLU D 222 ? 0.8821 0.7247 1.0061 -0.0591 -0.0186 -0.1956 238 GLU A CA  
9798  C C   . GLU D 222 ? 0.8405 0.7059 0.9598 -0.0516 -0.0167 -0.2121 238 GLU A C   
9799  O O   . GLU D 222 ? 0.8443 0.7362 0.9589 -0.0540 -0.0155 -0.2178 238 GLU A O   
9800  C CB  . GLU D 222 ? 0.9383 0.7616 1.0848 -0.0707 -0.0204 -0.2011 238 GLU A CB  
9801  C CG  . GLU D 222 ? 0.9713 0.7794 1.1245 -0.0822 -0.0216 -0.1856 238 GLU A CG  
9802  C CD  . GLU D 222 ? 1.1263 0.9168 1.3044 -0.0941 -0.0219 -0.1926 238 GLU A CD  
9803  O OE1 . GLU D 222 ? 1.0972 0.8986 1.2852 -0.0978 -0.0203 -0.2119 238 GLU A OE1 
9804  O OE2 . GLU D 222 ? 1.3278 1.0947 1.5164 -0.1001 -0.0233 -0.1787 238 GLU A OE2 
9805  N N   . HIS D 223 ? 0.7879 0.6454 0.9089 -0.0427 -0.0165 -0.2197 239 HIS A N   
9806  C CA  . HIS D 223 ? 0.8029 0.6842 0.9190 -0.0366 -0.0146 -0.2354 239 HIS A CA  
9807  C C   . HIS D 223 ? 0.7806 0.6837 0.8765 -0.0249 -0.0117 -0.2286 239 HIS A C   
9808  O O   . HIS D 223 ? 0.8282 0.7603 0.9179 -0.0232 -0.0106 -0.2356 239 HIS A O   
9809  C CB  . HIS D 223 ? 0.7881 0.6558 0.9128 -0.0315 -0.0143 -0.2470 239 HIS A CB  
9810  C CG  . HIS D 223 ? 0.7796 0.6370 0.9255 -0.0428 -0.0155 -0.2613 239 HIS A CG  
9811  N ND1 . HIS D 223 ? 0.8371 0.7162 0.9877 -0.0486 -0.0149 -0.2803 239 HIS A ND1 
9812  C CD2 . HIS D 223 ? 0.8024 0.6310 0.9673 -0.0506 -0.0170 -0.2585 239 HIS A CD2 
9813  C CE1 . HIS D 223 ? 0.8469 0.7093 1.0193 -0.0594 -0.0152 -0.2909 239 HIS A CE1 
9814  N NE2 . HIS D 223 ? 0.7928 0.6235 0.9748 -0.0605 -0.0163 -0.2771 239 HIS A NE2 
9815  N N   . LEU D 224 ? 0.7748 0.6656 0.8613 -0.0169 -0.0102 -0.2148 240 LEU A N   
9816  C CA  . LEU D 224 ? 0.8100 0.7197 0.8798 -0.0070 -0.0061 -0.2074 240 LEU A CA  
9817  C C   . LEU D 224 ? 0.7900 0.7218 0.8567 -0.0132 -0.0058 -0.2046 240 LEU A C   
9818  O O   . LEU D 224 ? 0.7594 0.7176 0.8176 -0.0066 -0.0032 -0.2061 240 LEU A O   
9819  C CB  . LEU D 224 ? 0.7659 0.6583 0.8284 -0.0010 -0.0043 -0.1933 240 LEU A CB  
9820  C CG  . LEU D 224 ? 0.6909 0.6015 0.7385 0.0088  0.0013  -0.1865 240 LEU A CG  
9821  C CD1 . LEU D 224 ? 0.7022 0.6263 0.7440 0.0213  0.0051  -0.1931 240 LEU A CD1 
9822  C CD2 . LEU D 224 ? 0.7230 0.6176 0.7649 0.0116  0.0034  -0.1742 240 LEU A CD2 
9823  N N   . HIS D 225 ? 0.8023 0.7237 0.8768 -0.0259 -0.0083 -0.1997 241 HIS A N   
9824  C CA  . HIS D 225 ? 0.7984 0.7382 0.8723 -0.0341 -0.0078 -0.1965 241 HIS A CA  
9825  C C   . HIS D 225 ? 0.7997 0.7657 0.8800 -0.0386 -0.0090 -0.2110 241 HIS A C   
9826  O O   . HIS D 225 ? 0.7646 0.7588 0.8388 -0.0358 -0.0072 -0.2108 241 HIS A O   
9827  C CB  . HIS D 225 ? 0.8042 0.7229 0.8860 -0.0469 -0.0100 -0.1877 241 HIS A CB  
9828  C CG  . HIS D 225 ? 0.7844 0.7181 0.8669 -0.0571 -0.0089 -0.1834 241 HIS A CG  
9829  N ND1 . HIS D 225 ? 0.7883 0.7373 0.8821 -0.0673 -0.0100 -0.1942 241 HIS A ND1 
9830  C CD2 . HIS D 225 ? 0.7658 0.7030 0.8400 -0.0594 -0.0063 -0.1707 241 HIS A CD2 
9831  C CE1 . HIS D 225 ? 0.7873 0.7481 0.8803 -0.0754 -0.0082 -0.1873 241 HIS A CE1 
9832  N NE2 . HIS D 225 ? 0.7264 0.6805 0.8070 -0.0705 -0.0057 -0.1731 241 HIS A NE2 
9833  N N   . ALA D 226 ? 0.8926 0.8506 0.9864 -0.0461 -0.0119 -0.2240 242 ALA A N   
9834  C CA  . ALA D 226 ? 0.8823 0.8671 0.9827 -0.0513 -0.0131 -0.2404 242 ALA A CA  
9835  C C   . ALA D 226 ? 0.8482 0.8625 0.9354 -0.0377 -0.0117 -0.2446 242 ALA A C   
9836  O O   . ALA D 226 ? 0.8792 0.9263 0.9647 -0.0386 -0.0121 -0.2495 242 ALA A O   
9837  C CB  . ALA D 226 ? 0.8995 0.8690 1.0164 -0.0596 -0.0152 -0.2559 242 ALA A CB  
9838  N N   . TYR D 227 ? 0.7271 0.7311 0.8052 -0.0246 -0.0098 -0.2414 243 TYR A N   
9839  C CA  . TYR D 227 ? 0.6907 0.7206 0.7565 -0.0111 -0.0077 -0.2441 243 TYR A CA  
9840  C C   . TYR D 227 ? 0.6681 0.7165 0.7224 -0.0028 -0.0044 -0.2302 243 TYR A C   
9841  O O   . TYR D 227 ? 0.6254 0.7069 0.6743 0.0033  -0.0040 -0.2324 243 TYR A O   
9842  C CB  . TYR D 227 ? 0.7541 0.7651 0.8145 -0.0002 -0.0053 -0.2430 243 TYR A CB  
9843  C CG  . TYR D 227 ? 0.7222 0.7545 0.7686 0.0153  -0.0017 -0.2418 243 TYR A CG  
9844  C CD1 . TYR D 227 ? 0.7440 0.8014 0.7886 0.0175  -0.0028 -0.2558 243 TYR A CD1 
9845  C CD2 . TYR D 227 ? 0.7605 0.7894 0.7958 0.0275  0.0033  -0.2265 243 TYR A CD2 
9846  C CE1 . TYR D 227 ? 0.7041 0.7815 0.7351 0.0321  0.0008  -0.2525 243 TYR A CE1 
9847  C CE2 . TYR D 227 ? 0.7303 0.7771 0.7541 0.0419  0.0076  -0.2236 243 TYR A CE2 
9848  C CZ  . TYR D 227 ? 0.7207 0.7919 0.7419 0.0444  0.0062  -0.2355 243 TYR A CZ  
9849  O OH  . TYR D 227 ? 0.7671 0.8562 0.7761 0.0592  0.0108  -0.2302 243 TYR A OH  
9850  N N   . VAL D 228 ? 0.7056 0.7342 0.7568 -0.0021 -0.0019 -0.2158 244 VAL A N   
9851  C CA  . VAL D 228 ? 0.7117 0.7557 0.7538 0.0057  0.0025  -0.2036 244 VAL A CA  
9852  C C   . VAL D 228 ? 0.7303 0.8000 0.7779 -0.0030 0.0009  -0.2055 244 VAL A C   
9853  O O   . VAL D 228 ? 0.7556 0.8527 0.7985 0.0046  0.0035  -0.2012 244 VAL A O   
9854  C CB  . VAL D 228 ? 0.6781 0.6952 0.7159 0.0070  0.0059  -0.1901 244 VAL A CB  
9855  C CG1 . VAL D 228 ? 0.6801 0.7116 0.7123 0.0104  0.0109  -0.1794 244 VAL A CG1 
9856  C CG2 . VAL D 228 ? 0.6852 0.6857 0.7166 0.0187  0.0089  -0.1876 244 VAL A CG2 
9857  N N   . ARG D 229 ? 0.7778 0.8397 0.8372 -0.0190 -0.0030 -0.2119 245 ARG A N   
9858  C CA  . ARG D 229 ? 0.7756 0.8620 0.8423 -0.0291 -0.0043 -0.2150 245 ARG A CA  
9859  C C   . ARG D 229 ? 0.7285 0.8518 0.7968 -0.0263 -0.0068 -0.2275 245 ARG A C   
9860  O O   . ARG D 229 ? 0.7035 0.8579 0.7714 -0.0241 -0.0061 -0.2254 245 ARG A O   
9861  C CB  . ARG D 229 ? 0.7684 0.8359 0.8487 -0.0473 -0.0071 -0.2191 245 ARG A CB  
9862  C CG  . ARG D 229 ? 0.7622 0.8547 0.8517 -0.0589 -0.0078 -0.2236 245 ARG A CG  
9863  C CD  . ARG D 229 ? 0.7617 0.8334 0.8648 -0.0767 -0.0091 -0.2251 245 ARG A CD  
9864  N NE  . ARG D 229 ? 0.7661 0.8158 0.8781 -0.0808 -0.0120 -0.2358 245 ARG A NE  
9865  C CZ  . ARG D 229 ? 0.8179 0.8392 0.9422 -0.0933 -0.0127 -0.2349 245 ARG A CZ  
9866  N NH1 . ARG D 229 ? 0.8156 0.8305 0.9447 -0.1045 -0.0110 -0.2250 245 ARG A NH1 
9867  N NH2 . ARG D 229 ? 0.8950 0.8942 1.0277 -0.0943 -0.0145 -0.2435 245 ARG A NH2 
9868  N N   . ALA D 230 ? 0.7355 0.8574 0.8062 -0.0264 -0.0099 -0.2410 246 ALA A N   
9869  C CA  . ALA D 230 ? 0.7332 0.8926 0.8020 -0.0218 -0.0123 -0.2528 246 ALA A CA  
9870  C C   . ALA D 230 ? 0.7355 0.9190 0.7909 -0.0039 -0.0091 -0.2410 246 ALA A C   
9871  O O   . ALA D 230 ? 0.7718 0.9930 0.8273 -0.0014 -0.0105 -0.2420 246 ALA A O   
9872  C CB  . ALA D 230 ? 0.6753 0.8255 0.7453 -0.0217 -0.0143 -0.2672 246 ALA A CB  
9873  N N   . LYS D 231 ? 0.7259 0.8881 0.7709 0.0088  -0.0044 -0.2290 247 LYS A N   
9874  C CA  . LYS D 231 ? 0.6822 0.8643 0.7159 0.0266  -0.0001 -0.2177 247 LYS A CA  
9875  C C   . LYS D 231 ? 0.7017 0.8990 0.7368 0.0288  0.0031  -0.2058 247 LYS A C   
9876  O O   . LYS D 231 ? 0.6449 0.8761 0.6775 0.0387  0.0039  -0.2016 247 LYS A O   
9877  C CB  . LYS D 231 ? 0.6041 0.7565 0.6290 0.0376  0.0051  -0.2090 247 LYS A CB  
9878  C CG  . LYS D 231 ? 0.6936 0.8317 0.7170 0.0377  0.0032  -0.2201 247 LYS A CG  
9879  C CD  . LYS D 231 ? 0.6367 0.8043 0.6548 0.0440  0.0013  -0.2299 247 LYS A CD  
9880  C CE  . LYS D 231 ? 0.6688 0.8498 0.6744 0.0628  0.0071  -0.2165 247 LYS A CE  
9881  N NZ  . LYS D 231 ? 0.8074 1.0144 0.8058 0.0691  0.0055  -0.2251 247 LYS A NZ  
9882  N N   . LEU D 232 ? 0.6953 0.8691 0.7346 0.0200  0.0051  -0.1997 248 LEU A N   
9883  C CA  . LEU D 232 ? 0.7404 0.9287 0.7819 0.0209  0.0090  -0.1899 248 LEU A CA  
9884  C C   . LEU D 232 ? 0.8592 1.0832 0.9105 0.0123  0.0045  -0.1981 248 LEU A C   
9885  O O   . LEU D 232 ? 0.9615 1.2155 1.0142 0.0194  0.0066  -0.1924 248 LEU A O   
9886  C CB  . LEU D 232 ? 0.7297 0.8879 0.7728 0.0115  0.0120  -0.1830 248 LEU A CB  
9887  C CG  . LEU D 232 ? 0.7211 0.8462 0.7558 0.0182  0.0171  -0.1735 248 LEU A CG  
9888  C CD1 . LEU D 232 ? 0.6663 0.7710 0.7031 0.0061  0.0184  -0.1683 248 LEU A CD1 
9889  C CD2 . LEU D 232 ? 0.6717 0.8055 0.6990 0.0364  0.0248  -0.1632 248 LEU A CD2 
9890  N N   . MET D 233 ? 0.8817 1.1030 0.9415 -0.0032 -0.0014 -0.2119 249 MET A N   
9891  C CA  . MET D 233 ? 0.8299 1.0848 0.9009 -0.0136 -0.0058 -0.2223 249 MET A CA  
9892  C C   . MET D 233 ? 0.8309 1.1285 0.8982 -0.0012 -0.0082 -0.2253 249 MET A C   
9893  O O   . MET D 233 ? 0.8847 1.2185 0.9585 -0.0019 -0.0096 -0.2259 249 MET A O   
9894  C CB  . MET D 233 ? 0.8999 1.1374 0.9808 -0.0313 -0.0105 -0.2374 249 MET A CB  
9895  C CG  . MET D 233 ? 0.9131 1.1717 1.0091 -0.0481 -0.0141 -0.2496 249 MET A CG  
9896  S SD  . MET D 233 ? 0.8137 1.0374 0.9213 -0.0660 -0.0170 -0.2645 249 MET A SD  
9897  C CE  . MET D 233 ? 0.7395 0.9704 0.8387 -0.0548 -0.0200 -0.2768 249 MET A CE  
9898  N N   . ASN D 234 ? 0.7375 1.0330 0.7941 0.0110  -0.0084 -0.2257 250 ASN A N   
9899  C CA  . ASN D 234 ? 0.6770 1.0135 0.7277 0.0257  -0.0096 -0.2232 250 ASN A CA  
9900  C C   . ASN D 234 ? 0.7434 1.0873 0.7901 0.0417  -0.0029 -0.2039 250 ASN A C   
9901  O O   . ASN D 234 ? 0.7545 1.1373 0.8012 0.0523  -0.0037 -0.1994 250 ASN A O   
9902  C CB  . ASN D 234 ? 0.6389 0.9747 0.6783 0.0357  -0.0105 -0.2270 250 ASN A CB  
9903  C CG  . ASN D 234 ? 0.6905 1.0305 0.7342 0.0225  -0.0169 -0.2484 250 ASN A CG  
9904  O OD1 . ASN D 234 ? 0.7079 1.0612 0.7638 0.0068  -0.0215 -0.2615 250 ASN A OD1 
9905  N ND2 . ASN D 234 ? 0.7276 1.0557 0.7623 0.0283  -0.0164 -0.2530 250 ASN A ND2 
9906  N N   . ALA D 235 ? 0.8123 1.1214 0.8558 0.0449  0.0040  -0.1924 251 ALA A N   
9907  C CA  . ALA D 235 ? 0.8553 1.1742 0.8964 0.0611  0.0113  -0.1758 251 ALA A CA  
9908  C C   . ALA D 235 ? 0.8955 1.2255 0.9469 0.0553  0.0140  -0.1714 251 ALA A C   
9909  O O   . ALA D 235 ? 0.8419 1.1867 0.8947 0.0683  0.0200  -0.1593 251 ALA A O   
9910  C CB  . ALA D 235 ? 0.8111 1.0921 0.8430 0.0707  0.0191  -0.1652 251 ALA A CB  
9911  N N   . TYR D 236 ? 0.9577 1.1425 0.9740 0.0003  0.0307  -0.1803 252 TYR A N   
9912  C CA  . TYR D 236 ? 1.0482 1.2450 1.0702 -0.0019 0.0289  -0.1853 252 TYR A CA  
9913  C C   . TYR D 236 ? 1.2168 1.4149 1.2226 -0.0094 0.0280  -0.1864 252 TYR A C   
9914  O O   . TYR D 236 ? 1.2544 1.4494 1.2515 -0.0143 0.0294  -0.1910 252 TYR A O   
9915  C CB  . TYR D 236 ? 0.9320 1.1274 0.9597 -0.0017 0.0312  -0.1911 252 TYR A CB  
9916  C CG  . TYR D 236 ? 0.9384 1.1308 0.9803 0.0050  0.0321  -0.1904 252 TYR A CG  
9917  C CD1 . TYR D 236 ? 0.9600 1.1622 1.0176 0.0098  0.0298  -0.1909 252 TYR A CD1 
9918  C CD2 . TYR D 236 ? 0.9778 1.1575 1.0172 0.0066  0.0351  -0.1891 252 TYR A CD2 
9919  C CE1 . TYR D 236 ? 1.0060 1.2040 1.0750 0.0157  0.0303  -0.1900 252 TYR A CE1 
9920  C CE2 . TYR D 236 ? 0.9901 1.1667 1.0414 0.0121  0.0357  -0.1879 252 TYR A CE2 
9921  C CZ  . TYR D 236 ? 1.0326 1.2177 1.0980 0.0164  0.0332  -0.1883 252 TYR A CZ  
9922  O OH  . TYR D 236 ? 0.9490 1.1294 1.0245 0.0216  0.0334  -0.1868 252 TYR A OH  
9923  N N   . PRO D 237 ? 1.4367 1.6385 1.4372 -0.0112 0.0254  -0.1819 253 PRO A N   
9924  C CA  . PRO D 237 ? 1.4784 1.6764 1.4593 -0.0184 0.0250  -0.1814 253 PRO A CA  
9925  C C   . PRO D 237 ? 1.4163 1.6226 1.3933 -0.0244 0.0238  -0.1868 253 PRO A C   
9926  O O   . PRO D 237 ? 1.4307 1.6298 1.3918 -0.0303 0.0245  -0.1893 253 PRO A O   
9927  C CB  . PRO D 237 ? 1.4754 1.6778 1.4550 -0.0188 0.0217  -0.1752 253 PRO A CB  
9928  C CG  . PRO D 237 ? 1.4018 1.6144 1.4017 -0.0127 0.0194  -0.1744 253 PRO A CG  
9929  C CD  . PRO D 237 ? 1.3213 1.5292 1.3320 -0.0070 0.0222  -0.1769 253 PRO A CD  
9930  N N   . SER D 238 ? 1.2730 1.4946 1.2648 -0.0229 0.0217  -0.1890 254 SER A N   
9931  C CA  . SER D 238 ? 1.2970 1.5306 1.2869 -0.0289 0.0202  -0.1938 254 SER A CA  
9932  C C   . SER D 238 ? 1.3091 1.5415 1.3014 -0.0304 0.0227  -0.2009 254 SER A C   
9933  O O   . SER D 238 ? 1.3734 1.6187 1.3697 -0.0342 0.0217  -0.2057 254 SER A O   
9934  C CB  . SER D 238 ? 1.4395 1.6912 1.4447 -0.0264 0.0170  -0.1931 254 SER A CB  
9935  O OG  . SER D 238 ? 1.4066 1.6643 1.4319 -0.0191 0.0178  -0.1959 254 SER A OG  
9936  N N   . TYR D 239 ? 1.2491 1.4668 1.2386 -0.0284 0.0257  -0.2016 255 TYR A N   
9937  C CA  . TYR D 239 ? 1.1338 1.3498 1.1283 -0.0291 0.0277  -0.2077 255 TYR A CA  
9938  C C   . TYR D 239 ? 1.0815 1.2806 1.0623 -0.0326 0.0296  -0.2096 255 TYR A C   
9939  O O   . TYR D 239 ? 1.0620 1.2600 1.0440 -0.0356 0.0303  -0.2150 255 TYR A O   
9940  C CB  . TYR D 239 ? 1.0228 1.2407 1.0372 -0.0205 0.0293  -0.2076 255 TYR A CB  
9941  C CG  . TYR D 239 ? 0.9552 1.1899 0.9872 -0.0163 0.0275  -0.2084 255 TYR A CG  
9942  C CD1 . TYR D 239 ? 0.8156 1.0640 0.8535 -0.0196 0.0272  -0.2146 255 TYR A CD1 
9943  C CD2 . TYR D 239 ? 0.9498 1.1867 0.9923 -0.0090 0.0259  -0.2032 255 TYR A CD2 
9944  C CE1 . TYR D 239 ? 0.8017 1.0659 0.8566 -0.0148 0.0257  -0.2159 255 TYR A CE1 
9945  C CE2 . TYR D 239 ? 0.8544 1.1059 0.9133 -0.0044 0.0236  -0.2042 255 TYR A CE2 
9946  C CZ  . TYR D 239 ? 0.8187 1.0841 0.8841 -0.0069 0.0236  -0.2107 255 TYR A CZ  
9947  O OH  . TYR D 239 ? 0.8375 1.1179 0.9200 -0.0015 0.0214  -0.2122 255 TYR A OH  
9948  N N   . ILE D 240 ? 1.0756 1.2613 1.0444 -0.0318 0.0303  -0.2057 256 ILE A N   
9949  C CA  . ILE D 240 ? 0.9980 1.1677 0.9575 -0.0330 0.0321  -0.2075 256 ILE A CA  
9950  C C   . ILE D 240 ? 1.0148 1.1754 0.9519 -0.0392 0.0304  -0.2071 256 ILE A C   
9951  O O   . ILE D 240 ? 1.0496 1.2083 0.9790 -0.0383 0.0301  -0.2024 256 ILE A O   
9952  C CB  . ILE D 240 ? 0.9579 1.1185 0.9252 -0.0250 0.0350  -0.2036 256 ILE A CB  
9953  C CG1 . ILE D 240 ? 0.8820 1.0466 0.8683 -0.0199 0.0365  -0.2049 256 ILE A CG1 
9954  C CG2 . ILE D 240 ? 0.9264 1.0706 0.8807 -0.0263 0.0365  -0.2044 256 ILE A CG2 
9955  C CD1 . ILE D 240 ? 0.8557 1.0176 0.8522 -0.0119 0.0381  -0.1994 256 ILE A CD1 
9956  N N   . SER D 241 ? 0.9490 1.1021 0.8744 -0.0456 0.0292  -0.2121 257 SER A N   
9957  C CA  . SER D 241 ? 0.9991 1.1426 0.9016 -0.0519 0.0268  -0.2121 257 SER A CA  
9958  C C   . SER D 241 ? 0.9584 1.0850 0.8528 -0.0477 0.0288  -0.2101 257 SER A C   
9959  O O   . SER D 241 ? 0.9616 1.0816 0.8650 -0.0430 0.0313  -0.2110 257 SER A O   
9960  C CB  . SER D 241 ? 0.9881 1.1286 0.8794 -0.0609 0.0237  -0.2179 257 SER A CB  
9961  O OG  . SER D 241 ? 0.8743 0.9959 0.7481 -0.0632 0.0212  -0.2128 257 SER A OG  
9962  N N   . PRO D 242 ? 0.8798 0.9990 0.7567 -0.0498 0.0277  -0.2075 258 PRO A N   
9963  C CA  . PRO D 242 ? 0.8874 0.9916 0.7567 -0.0453 0.0300  -0.2058 258 PRO A CA  
9964  C C   . PRO D 242 ? 0.9371 1.0264 0.7952 -0.0478 0.0287  -0.2106 258 PRO A C   
9965  O O   . PRO D 242 ? 0.9702 1.0471 0.8231 -0.0436 0.0307  -0.2101 258 PRO A O   
9966  C CB  . PRO D 242 ? 0.9122 1.0139 0.7647 -0.0479 0.0287  -0.2021 258 PRO A CB  
9967  C CG  . PRO D 242 ? 1.0282 1.1379 0.8725 -0.0563 0.0244  -0.2036 258 PRO A CG  
9968  C CD  . PRO D 242 ? 1.0116 1.1365 0.8754 -0.0561 0.0244  -0.2057 258 PRO A CD  
9969  N N   . ILE D 243 ? 0.9559 1.0442 0.8128 -0.0537 0.0246  -0.2103 259 ILE A N   
9970  C CA  . ILE D 243 ? 0.9361 1.0077 0.7879 -0.0551 0.0215  -0.2084 259 ILE A CA  
9971  C C   . ILE D 243 ? 0.9301 1.0053 0.7974 -0.0552 0.0219  -0.2109 259 ILE A C   
9972  O O   . ILE D 243 ? 0.9375 0.9998 0.8018 -0.0570 0.0190  -0.2092 259 ILE A O   
9973  C CB  . ILE D 243 ? 0.8997 0.9626 0.7343 -0.0621 0.0151  -0.2034 259 ILE A CB  
9974  C CG1 . ILE D 243 ? 0.8883 0.9665 0.7282 -0.0684 0.0130  -0.2031 259 ILE A CG1 
9975  C CG2 . ILE D 243 ? 0.9394 0.9947 0.7571 -0.0614 0.0144  -0.2006 259 ILE A CG2 
9976  C CD1 . ILE D 243 ? 0.7763 0.8466 0.6037 -0.0754 0.0068  -0.1983 259 ILE A CD1 
9977  N N   . GLY D 244 ? 0.9657 1.0574 0.8493 -0.0532 0.0253  -0.2147 260 GLY A N   
9978  C CA  . GLY D 244 ? 0.9692 1.0662 0.8666 -0.0547 0.0254  -0.2168 260 GLY A CA  
9979  C C   . GLY D 244 ? 0.9548 1.0488 0.8661 -0.0482 0.0294  -0.2196 260 GLY A C   
9980  O O   . GLY D 244 ? 0.9133 1.0030 0.8253 -0.0420 0.0326  -0.2202 260 GLY A O   
9981  N N   . CYS D 245 ? 0.9641 1.0602 0.8862 -0.0501 0.0291  -0.2209 261 CYS A N   
9982  C CA  . CYS D 245 ? 0.8638 0.9591 0.8009 -0.0446 0.0327  -0.2234 261 CYS A CA  
9983  C C   . CYS D 245 ? 0.8494 0.9592 0.8019 -0.0381 0.0362  -0.2228 261 CYS A C   
9984  O O   . CYS D 245 ? 0.8720 0.9932 0.8241 -0.0382 0.0357  -0.2213 261 CYS A O   
9985  C CB  . CYS D 245 ? 0.8183 0.9103 0.7614 -0.0492 0.0309  -0.2231 261 CYS A CB  
9986  S SG  . CYS D 245 ? 0.8683 0.9404 0.7971 -0.0548 0.0256  -0.2181 261 CYS A SG  
9987  N N   . LEU D 246 ? 0.7892 0.8972 0.7563 -0.0322 0.0389  -0.2209 262 LEU A N   
9988  C CA  . LEU D 246 ? 0.7429 0.8624 0.7245 -0.0257 0.0408  -0.2170 262 LEU A CA  
9989  C C   . LEU D 246 ? 0.7430 0.8723 0.7369 -0.0270 0.0407  -0.2203 262 LEU A C   
9990  O O   . LEU D 246 ? 0.7411 0.8650 0.7366 -0.0305 0.0406  -0.2240 262 LEU A O   
9991  C CB  . LEU D 246 ? 0.7444 0.8573 0.7343 -0.0179 0.0436  -0.2121 262 LEU A CB  
9992  C CG  . LEU D 246 ? 0.7152 0.8197 0.6934 -0.0161 0.0443  -0.2092 262 LEU A CG  
9993  C CD1 . LEU D 246 ? 0.7308 0.8282 0.7163 -0.0097 0.0472  -0.2054 262 LEU A CD1 
9994  C CD2 . LEU D 246 ? 0.7325 0.8450 0.7066 -0.0148 0.0440  -0.2059 262 LEU A CD2 
9995  N N   . PRO D 247 ? 0.7719 0.9156 0.7741 -0.0250 0.0404  -0.2197 263 PRO A N   
9996  C CA  . PRO D 247 ? 0.8197 0.9727 0.8348 -0.0250 0.0407  -0.2232 263 PRO A CA  
9997  C C   . PRO D 247 ? 0.7636 0.9111 0.7923 -0.0186 0.0428  -0.2208 263 PRO A C   
9998  O O   . PRO D 247 ? 0.7793 0.9258 0.8142 -0.0114 0.0436  -0.2153 263 PRO A O   
9999  C CB  . PRO D 247 ? 0.7848 0.9540 0.8057 -0.0227 0.0396  -0.2221 263 PRO A CB  
10000 C CG  . PRO D 247 ? 0.7872 0.9556 0.7930 -0.0263 0.0379  -0.2203 263 PRO A CG  
10001 C CD  . PRO D 247 ? 0.7899 0.9423 0.7867 -0.0249 0.0390  -0.2172 263 PRO A CD  
10002 N N   . ALA D 248 ? 0.7795 0.9233 0.8119 -0.0218 0.0434  -0.2249 264 ALA A N   
10003 C CA  . ALA D 248 ? 0.8418 0.9768 0.8839 -0.0173 0.0452  -0.2226 264 ALA A CA  
10004 C C   . ALA D 248 ? 0.8995 1.0417 0.9562 -0.0087 0.0458  -0.2187 264 ALA A C   
10005 O O   . ALA D 248 ? 0.8995 1.0342 0.9616 -0.0032 0.0467  -0.2137 264 ALA A O   
10006 C CB  . ALA D 248 ? 0.7988 0.9295 0.8416 -0.0236 0.0454  -0.2281 264 ALA A CB  
10007 N N   . HIS D 249 ? 0.7211 0.8776 0.7839 -0.0076 0.0448  -0.2208 265 HIS A N   
10008 C CA  . HIS D 249 ? 0.7477 0.9105 0.8239 0.0006  0.0444  -0.2176 265 HIS A CA  
10009 C C   . HIS D 249 ? 0.7365 0.8991 0.8119 0.0060  0.0433  -0.2109 265 HIS A C   
10010 O O   . HIS D 249 ? 0.7566 0.9246 0.8418 0.0123  0.0419  -0.2079 265 HIS A O   
10011 C CB  . HIS D 249 ? 0.7451 0.9239 0.8282 0.0002  0.0434  -0.2226 265 HIS A CB  
10012 C CG  . HIS D 249 ? 0.8141 1.0034 0.8901 -0.0030 0.0417  -0.2233 265 HIS A CG  
10013 N ND1 . HIS D 249 ? 0.7794 0.9669 0.8412 -0.0114 0.0416  -0.2260 265 HIS A ND1 
10014 C CD2 . HIS D 249 ? 0.8141 1.0158 0.8950 0.0006  0.0397  -0.2216 265 HIS A CD2 
10015 C CE1 . HIS D 249 ? 0.7267 0.9247 0.7841 -0.0129 0.0398  -0.2257 265 HIS A CE1 
10016 N NE2 . HIS D 249 ? 0.8118 1.0189 0.8812 -0.0058 0.0386  -0.2230 265 HIS A NE2 
10017 N N   . LEU D 250 ? 0.7437 0.9000 0.8071 0.0034  0.0437  -0.2085 266 LEU A N   
10018 C CA  . LEU D 250 ? 0.7767 0.9331 0.8377 0.0073  0.0430  -0.2025 266 LEU A CA  
10019 C C   . LEU D 250 ? 0.7377 0.8813 0.7952 0.0093  0.0448  -0.1980 266 LEU A C   
10020 O O   . LEU D 250 ? 0.7574 0.8990 0.8090 0.0108  0.0450  -0.1937 266 LEU A O   
10021 C CB  . LEU D 250 ? 0.8495 1.0112 0.8988 0.0028  0.0418  -0.2035 266 LEU A CB  
10022 C CG  . LEU D 250 ? 0.7931 0.9699 0.8462 0.0009  0.0397  -0.2071 266 LEU A CG  
10023 C CD1 . LEU D 250 ? 0.8757 1.0564 0.9155 -0.0045 0.0383  -0.2073 266 LEU A CD1 
10024 C CD2 . LEU D 250 ? 0.9277 1.1128 0.9949 0.0080  0.0379  -0.2041 266 LEU A CD2 
10025 N N   . LEU D 251 ? 0.7667 0.9017 0.8274 0.0091  0.0463  -0.1989 267 LEU A N   
10026 C CA  . LEU D 251 ? 0.6989 0.8225 0.7562 0.0104  0.0482  -0.1952 267 LEU A CA  
10027 C C   . LEU D 251 ? 0.6703 0.7912 0.7373 0.0164  0.0484  -0.1895 267 LEU A C   
10028 O O   . LEU D 251 ? 0.7381 0.8513 0.8031 0.0178  0.0500  -0.1857 267 LEU A O   
10029 C CB  . LEU D 251 ? 0.6834 0.7977 0.7365 0.0055  0.0492  -0.1992 267 LEU A CB  
10030 C CG  . LEU D 251 ? 0.6812 0.7960 0.7214 -0.0009 0.0483  -0.2040 267 LEU A CG  
10031 C CD1 . LEU D 251 ? 0.6855 0.7911 0.7214 -0.0065 0.0482  -0.2084 267 LEU A CD1 
10032 C CD2 . LEU D 251 ? 0.5870 0.6981 0.6176 0.0005  0.0490  -0.2007 267 LEU A CD2 
10033 N N   . GLY D 252 ? 0.6569 0.7840 0.7339 0.0200  0.0466  -0.1886 268 GLY A N   
10034 C CA  . GLY D 252 ? 0.6903 0.8153 0.7740 0.0255  0.0458  -0.1823 268 GLY A CA  
10035 C C   . GLY D 252 ? 0.6957 0.8144 0.7875 0.0273  0.0458  -0.1814 268 GLY A C   
10036 O O   . GLY D 252 ? 0.7289 0.8447 0.8256 0.0315  0.0447  -0.1758 268 GLY A O   
10037 N N   . ASP D 253 ? 0.6925 0.8081 0.7848 0.0237  0.0469  -0.1865 269 ASP A N   
10038 C CA  . ASP D 253 ? 0.6454 0.7570 0.7458 0.0249  0.0466  -0.1871 269 ASP A CA  
10039 C C   . ASP D 253 ? 0.6239 0.7391 0.7241 0.0200  0.0471  -0.1950 269 ASP A C   
10040 O O   . ASP D 253 ? 0.6911 0.8128 0.7853 0.0163  0.0473  -0.1992 269 ASP A O   
10041 C CB  . ASP D 253 ? 0.6957 0.7950 0.7960 0.0249  0.0479  -0.1825 269 ASP A CB  
10042 C CG  . ASP D 253 ? 0.7036 0.7954 0.7970 0.0190  0.0500  -0.1854 269 ASP A CG  
10043 O OD1 . ASP D 253 ? 0.7039 0.7982 0.7929 0.0140  0.0503  -0.1919 269 ASP A OD1 
10044 O OD2 . ASP D 253 ? 0.6569 0.7404 0.7491 0.0193  0.0511  -0.1812 269 ASP A OD2 
10045 N N   . MET D 254 ? 0.5802 0.6911 0.6860 0.0196  0.0474  -0.1969 270 MET A N   
10046 C CA  . MET D 254 ? 0.5893 0.7048 0.6959 0.0151  0.0480  -0.2046 270 MET A CA  
10047 C C   . MET D 254 ? 0.6015 0.7128 0.6984 0.0067  0.0494  -0.2090 270 MET A C   
10048 O O   . MET D 254 ? 0.6360 0.7538 0.7311 0.0017  0.0495  -0.2157 270 MET A O   
10049 C CB  . MET D 254 ? 0.6393 0.7496 0.7535 0.0166  0.0481  -0.2052 270 MET A CB  
10050 C CG  . MET D 254 ? 0.6725 0.7869 0.7878 0.0114  0.0493  -0.2134 270 MET A CG  
10051 S SD  . MET D 254 ? 0.5509 0.6848 0.6688 0.0120  0.0486  -0.2198 270 MET A SD  
10052 C CE  . MET D 254 ? 0.6398 0.7780 0.7712 0.0212  0.0470  -0.2191 270 MET A CE  
10053 N N   . TRP D 255 ? 0.6025 0.7034 0.6932 0.0047  0.0500  -0.2058 271 TRP A N   
10054 C CA  . TRP D 255 ? 0.6290 0.7241 0.7104 -0.0033 0.0503  -0.2103 271 TRP A CA  
10055 C C   . TRP D 255 ? 0.6694 0.7619 0.7416 -0.0037 0.0502  -0.2082 271 TRP A C   
10056 O O   . TRP D 255 ? 0.6789 0.7654 0.7419 -0.0099 0.0497  -0.2115 271 TRP A O   
10057 C CB  . TRP D 255 ? 0.6523 0.7340 0.7348 -0.0067 0.0508  -0.2099 271 TRP A CB  
10058 C CG  . TRP D 255 ? 0.6692 0.7508 0.7606 -0.0052 0.0512  -0.2105 271 TRP A CG  
10059 C CD1 . TRP D 255 ? 0.6400 0.7245 0.7328 -0.0099 0.0515  -0.2169 271 TRP A CD1 
10060 C CD2 . TRP D 255 ? 0.6286 0.7067 0.7282 0.0015  0.0511  -0.2044 271 TRP A CD2 
10061 N NE1 . TRP D 255 ? 0.6288 0.7114 0.7303 -0.0060 0.0519  -0.2154 271 TRP A NE1 
10062 C CE2 . TRP D 255 ? 0.6533 0.7315 0.7588 0.0010  0.0513  -0.2075 271 TRP A CE2 
10063 C CE3 . TRP D 255 ? 0.5980 0.6729 0.6998 0.0075  0.0508  -0.1967 271 TRP A CE3 
10064 C CZ2 . TRP D 255 ? 0.6657 0.7396 0.7784 0.0066  0.0508  -0.2029 271 TRP A CZ2 
10065 C CZ3 . TRP D 255 ? 0.6468 0.7184 0.7556 0.0123  0.0501  -0.1920 271 TRP A CZ3 
10066 C CH2 . TRP D 255 ? 0.6787 0.7492 0.7928 0.0121  0.0499  -0.1950 271 TRP A CH2 
10067 N N   . GLY D 256 ? 0.7872 0.8830 0.8609 0.0025  0.0504  -0.2028 272 GLY A N   
10068 C CA  . GLY D 256 ? 0.7809 0.8730 0.8461 0.0026  0.0508  -0.2005 272 GLY A CA  
10069 C C   . GLY D 256 ? 0.8062 0.8857 0.8705 0.0021  0.0517  -0.1979 272 GLY A C   
10070 O O   . GLY D 256 ? 0.8289 0.9029 0.8844 -0.0002 0.0518  -0.1990 272 GLY A O   
10071 N N   . ARG D 257 ? 0.7047 0.7793 0.7777 0.0042  0.0521  -0.1947 273 ARG A N   
10072 C CA  . ARG D 257 ? 0.6344 0.6976 0.7080 0.0039  0.0528  -0.1915 273 ARG A CA  
10073 C C   . ARG D 257 ? 0.6727 0.7360 0.7444 0.0085  0.0541  -0.1864 273 ARG A C   
10074 O O   . ARG D 257 ? 0.6808 0.7373 0.7478 0.0073  0.0546  -0.1864 273 ARG A O   
10075 C CB  . ARG D 257 ? 0.6490 0.7078 0.7319 0.0055  0.0527  -0.1881 273 ARG A CB  
10076 C CG  . ARG D 257 ? 0.7324 0.7795 0.8164 0.0045  0.0531  -0.1843 273 ARG A CG  
10077 C CD  . ARG D 257 ? 0.7152 0.7563 0.8069 0.0049  0.0527  -0.1808 273 ARG A CD  
10078 N NE  . ARG D 257 ? 0.6963 0.7267 0.7891 0.0036  0.0529  -0.1767 273 ARG A NE  
10079 C CZ  . ARG D 257 ? 0.6870 0.7123 0.7860 0.0055  0.0527  -0.1706 273 ARG A CZ  
10080 N NH1 . ARG D 257 ? 0.7797 0.8086 0.8835 0.0089  0.0521  -0.1680 273 ARG A NH1 
10081 N NH2 . ARG D 257 ? 0.6612 0.6773 0.7612 0.0037  0.0526  -0.1670 273 ARG A NH2 
10082 N N   . PHE D 258 ? 0.6706 0.7416 0.7460 0.0136  0.0544  -0.1823 274 PHE A N   
10083 C CA  . PHE D 258 ? 0.6825 0.7555 0.7555 0.0174  0.0558  -0.1778 274 PHE A CA  
10084 C C   . PHE D 258 ? 0.7146 0.7974 0.7837 0.0187  0.0552  -0.1786 274 PHE A C   
10085 O O   . PHE D 258 ? 0.7038 0.7930 0.7763 0.0189  0.0535  -0.1802 274 PHE A O   
10086 C CB  . PHE D 258 ? 0.7150 0.7871 0.7958 0.0218  0.0561  -0.1704 274 PHE A CB  
10087 C CG  . PHE D 258 ? 0.6892 0.7522 0.7751 0.0205  0.0561  -0.1685 274 PHE A CG  
10088 C CD1 . PHE D 258 ? 0.6467 0.7028 0.7310 0.0195  0.0575  -0.1675 274 PHE A CD1 
10089 C CD2 . PHE D 258 ? 0.7267 0.7877 0.8191 0.0203  0.0546  -0.1678 274 PHE A CD2 
10090 C CE1 . PHE D 258 ? 0.6963 0.7439 0.7855 0.0178  0.0571  -0.1653 274 PHE A CE1 
10091 C CE2 . PHE D 258 ? 0.6983 0.7500 0.7947 0.0185  0.0544  -0.1656 274 PHE A CE2 
10092 C CZ  . PHE D 258 ? 0.7005 0.7454 0.7953 0.0170  0.0556  -0.1642 274 PHE A CZ  
10093 N N   . TRP D 259 ? 0.7293 0.8132 0.7914 0.0197  0.0566  -0.1774 275 TRP A N   
10094 C CA  . TRP D 259 ? 0.6848 0.7770 0.7425 0.0208  0.0561  -0.1769 275 TRP A CA  
10095 C C   . TRP D 259 ? 0.6898 0.7854 0.7516 0.0251  0.0564  -0.1702 275 TRP A C   
10096 O O   . TRP D 259 ? 0.6949 0.7938 0.7507 0.0258  0.0572  -0.1685 275 TRP A O   
10097 C CB  . TRP D 259 ? 0.6549 0.7454 0.7003 0.0183  0.0571  -0.1800 275 TRP A CB  
10098 C CG  . TRP D 259 ? 0.6107 0.6988 0.6497 0.0131  0.0557  -0.1866 275 TRP A CG  
10099 C CD1 . TRP D 259 ? 0.5846 0.6728 0.6279 0.0100  0.0541  -0.1902 275 TRP A CD1 
10100 C CD2 . TRP D 259 ? 0.5890 0.6727 0.6151 0.0098  0.0557  -0.1904 275 TRP A CD2 
10101 N NE1 . TRP D 259 ? 0.6042 0.6894 0.6379 0.0044  0.0528  -0.1960 275 TRP A NE1 
10102 C CE2 . TRP D 259 ? 0.5781 0.6599 0.6008 0.0042  0.0535  -0.1961 275 TRP A CE2 
10103 C CE3 . TRP D 259 ? 0.6015 0.6825 0.6179 0.0108  0.0571  -0.1897 275 TRP A CE3 
10104 C CZ2 . TRP D 259 ? 0.6160 0.6929 0.6254 -0.0006 0.0520  -0.2007 275 TRP A CZ2 
10105 C CZ3 . TRP D 259 ? 0.6364 0.7120 0.6398 0.0068  0.0559  -0.1944 275 TRP A CZ3 
10106 C CH2 . TRP D 259 ? 0.6458 0.7191 0.6456 0.0010  0.0531  -0.1997 275 TRP A CH2 
10107 N N   . THR D 260 ? 0.8030 0.8970 0.8738 0.0275  0.0557  -0.1662 276 THR A N   
10108 C CA  . THR D 260 ? 0.8104 0.9068 0.8838 0.0307  0.0555  -0.1596 276 THR A CA  
10109 C C   . THR D 260 ? 0.8478 0.9517 0.9215 0.0320  0.0527  -0.1584 276 THR A C   
10110 O O   . THR D 260 ? 0.8881 0.9952 0.9574 0.0326  0.0529  -0.1552 276 THR A O   
10111 C CB  . THR D 260 ? 0.7771 0.8690 0.8587 0.0325  0.0547  -0.1550 276 THR A CB  
10112 O OG1 . THR D 260 ? 0.7698 0.8544 0.8520 0.0308  0.0568  -0.1566 276 THR A OG1 
10113 C CG2 . THR D 260 ? 0.8455 0.9394 0.9276 0.0347  0.0547  -0.1481 276 THR A CG2 
10114 N N   . ASN D 261 ? 0.7219 0.8288 0.8005 0.0323  0.0500  -0.1612 277 ASN A N   
10115 C CA  . ASN D 261 ? 0.7190 0.8329 0.7997 0.0342  0.0466  -0.1593 277 ASN A CA  
10116 C C   . ASN D 261 ? 0.6916 0.8111 0.7641 0.0321  0.0467  -0.1613 277 ASN A C   
10117 O O   . ASN D 261 ? 0.6197 0.7446 0.6928 0.0333  0.0438  -0.1589 277 ASN A O   
10118 C CB  . ASN D 261 ? 0.7241 0.8404 0.8132 0.0358  0.0436  -0.1619 277 ASN A CB  
10119 C CG  . ASN D 261 ? 0.7191 0.8290 0.8149 0.0380  0.0429  -0.1586 277 ASN A CG  
10120 O OD1 . ASN D 261 ? 0.7143 0.8214 0.8102 0.0397  0.0421  -0.1524 277 ASN A OD1 
10121 N ND2 . ASN D 261 ? 0.7628 0.8700 0.8633 0.0376  0.0430  -0.1624 277 ASN A ND2 
10122 N N   . LEU D 262 ? 0.6386 0.7560 0.7029 0.0289  0.0496  -0.1651 278 LEU A N   
10123 C CA  . LEU D 262 ? 0.6157 0.7368 0.6704 0.0267  0.0498  -0.1661 278 LEU A CA  
10124 C C   . LEU D 262 ? 0.6381 0.7582 0.6872 0.0274  0.0512  -0.1610 278 LEU A C   
10125 O O   . LEU D 262 ? 0.6755 0.7977 0.7155 0.0253  0.0514  -0.1614 278 LEU A O   
10126 C CB  . LEU D 262 ? 0.5818 0.7000 0.6275 0.0227  0.0517  -0.1718 278 LEU A CB  
10127 C CG  . LEU D 262 ? 0.6065 0.7254 0.6555 0.0204  0.0507  -0.1775 278 LEU A CG  
10128 C CD1 . LEU D 262 ? 0.6107 0.7266 0.6478 0.0156  0.0516  -0.1824 278 LEU A CD1 
10129 C CD2 . LEU D 262 ? 0.6635 0.7915 0.7198 0.0212  0.0475  -0.1786 278 LEU A CD2 
10130 N N   . TYR D 263 ? 0.6446 0.7618 0.6981 0.0297  0.0520  -0.1562 279 TYR A N   
10131 C CA  . TYR D 263 ? 0.6603 0.7773 0.7076 0.0295  0.0537  -0.1518 279 TYR A CA  
10132 C C   . TYR D 263 ? 0.6513 0.7736 0.6964 0.0289  0.0504  -0.1487 279 TYR A C   
10133 O O   . TYR D 263 ? 0.6415 0.7643 0.6769 0.0267  0.0519  -0.1479 279 TYR A O   
10134 C CB  . TYR D 263 ? 0.6634 0.7775 0.7158 0.0314  0.0550  -0.1470 279 TYR A CB  
10135 C CG  . TYR D 263 ? 0.6170 0.7320 0.6634 0.0308  0.0573  -0.1427 279 TYR A CG  
10136 C CD1 . TYR D 263 ? 0.6304 0.7436 0.6690 0.0299  0.0622  -0.1446 279 TYR A CD1 
10137 C CD2 . TYR D 263 ? 0.5896 0.7068 0.6387 0.0310  0.0544  -0.1366 279 TYR A CD2 
10138 C CE1 . TYR D 263 ? 0.6746 0.7893 0.7080 0.0291  0.0649  -0.1410 279 TYR A CE1 
10139 C CE2 . TYR D 263 ? 0.6980 0.8163 0.7413 0.0295  0.0566  -0.1326 279 TYR A CE2 
10140 C CZ  . TYR D 263 ? 0.7309 0.8485 0.7666 0.0286  0.0623  -0.1350 279 TYR A CZ  
10141 O OH  . TYR D 263 ? 0.7547 0.8744 0.7848 0.0269  0.0649  -0.1315 279 TYR A OH  
10142 N N   . SER D 264 ? 0.6626 0.7881 0.7160 0.0307  0.0456  -0.1471 280 SER A N   
10143 C CA  . SER D 264 ? 0.6240 0.7544 0.6762 0.0301  0.0414  -0.1449 280 SER A CA  
10144 C C   . SER D 264 ? 0.6554 0.7887 0.6984 0.0268  0.0423  -0.1482 280 SER A C   
10145 O O   . SER D 264 ? 0.6766 0.8109 0.7121 0.0245  0.0417  -0.1454 280 SER A O   
10146 C CB  . SER D 264 ? 0.6006 0.7345 0.6638 0.0330  0.0360  -0.1451 280 SER A CB  
10147 O OG  . SER D 264 ? 0.6006 0.7384 0.6664 0.0329  0.0360  -0.1511 280 SER A OG  
10148 N N   . LEU D 265 ? 0.6156 0.7496 0.6579 0.0259  0.0436  -0.1541 281 LEU A N   
10149 C CA  . LEU D 265 ? 0.5463 0.6832 0.5796 0.0223  0.0437  -0.1574 281 LEU A CA  
10150 C C   . LEU D 265 ? 0.6387 0.7698 0.6585 0.0195  0.0481  -0.1586 281 LEU A C   
10151 O O   . LEU D 265 ? 0.6246 0.7567 0.6344 0.0161  0.0479  -0.1607 281 LEU A O   
10152 C CB  . LEU D 265 ? 0.5230 0.6633 0.5606 0.0217  0.0429  -0.1633 281 LEU A CB  
10153 C CG  . LEU D 265 ? 0.5839 0.7320 0.6331 0.0240  0.0385  -0.1641 281 LEU A CG  
10154 C CD1 . LEU D 265 ? 0.6549 0.8064 0.7055 0.0220  0.0390  -0.1707 281 LEU A CD1 
10155 C CD2 . LEU D 265 ? 0.6341 0.7888 0.6827 0.0235  0.0344  -0.1611 281 LEU A CD2 
10156 N N   . THR D 266 ? 0.6716 0.7968 0.6908 0.0210  0.0518  -0.1575 282 THR A N   
10157 C CA  . THR D 266 ? 0.6717 0.7910 0.6795 0.0194  0.0561  -0.1599 282 THR A CA  
10158 C C   . THR D 266 ? 0.6806 0.7971 0.6852 0.0205  0.0596  -0.1560 282 THR A C   
10159 O O   . THR D 266 ? 0.7041 0.8158 0.7005 0.0202  0.0634  -0.1582 282 THR A O   
10160 C CB  . THR D 266 ? 0.5658 0.6803 0.5756 0.0198  0.0577  -0.1649 282 THR A CB  
10161 O OG1 . THR D 266 ? 0.6247 0.7376 0.6452 0.0229  0.0586  -0.1628 282 THR A OG1 
10162 C CG2 . THR D 266 ? 0.6524 0.7697 0.6641 0.0177  0.0549  -0.1695 282 THR A CG2 
10163 N N   . VAL D 267 ? 0.6954 0.8148 0.7058 0.0217  0.0581  -0.1506 283 VAL A N   
10164 C CA  . VAL D 267 ? 0.7564 0.8742 0.7637 0.0220  0.0617  -0.1472 283 VAL A CA  
10165 C C   . VAL D 267 ? 0.8072 0.9232 0.7999 0.0192  0.0645  -0.1480 283 VAL A C   
10166 O O   . VAL D 267 ? 0.9007 1.0183 0.8872 0.0163  0.0618  -0.1473 283 VAL A O   
10167 C CB  . VAL D 267 ? 0.7778 0.8987 0.7918 0.0224  0.0587  -0.1409 283 VAL A CB  
10168 C CG1 . VAL D 267 ? 0.7956 0.9201 0.8090 0.0206  0.0535  -0.1391 283 VAL A CG1 
10169 C CG2 . VAL D 267 ? 0.8048 0.9255 0.8133 0.0213  0.0623  -0.1373 283 VAL A CG2 
10170 N N   . PRO D 268 ? 0.7750 0.8874 0.7618 0.0199  0.0698  -0.1496 284 PRO A N   
10171 C CA  . PRO D 268 ? 0.8066 0.9164 0.7786 0.0174  0.0727  -0.1507 284 PRO A CA  
10172 C C   . PRO D 268 ? 0.8502 0.9629 0.8180 0.0144  0.0718  -0.1455 284 PRO A C   
10173 O O   . PRO D 268 ? 0.9262 1.0392 0.8871 0.0111  0.0689  -0.1445 284 PRO A O   
10174 C CB  . PRO D 268 ? 0.7759 0.8824 0.7461 0.0200  0.0784  -0.1532 284 PRO A CB  
10175 C CG  . PRO D 268 ? 0.7900 0.8959 0.7714 0.0231  0.0778  -0.1548 284 PRO A CG  
10176 C CD  . PRO D 268 ? 0.7788 0.8890 0.7717 0.0231  0.0731  -0.1511 284 PRO A CD  
10177 N N   . PHE D 269 ? 0.7770 0.8919 0.7484 0.0150  0.0741  -0.1419 285 PHE A N   
10178 C CA  . PHE D 269 ? 0.8276 0.9446 0.7938 0.0112  0.0735  -0.1369 285 PHE A CA  
10179 C C   . PHE D 269 ? 0.8771 0.9978 0.8545 0.0112  0.0677  -0.1318 285 PHE A C   
10180 O O   . PHE D 269 ? 0.9185 1.0413 0.9021 0.0118  0.0679  -0.1284 285 PHE A O   
10181 C CB  . PHE D 269 ? 0.8348 0.9522 0.7965 0.0112  0.0799  -0.1367 285 PHE A CB  
10182 C CG  . PHE D 269 ? 0.8301 0.9430 0.7811 0.0122  0.0851  -0.1422 285 PHE A CG  
10183 C CD1 . PHE D 269 ? 0.8678 0.9772 0.8042 0.0086  0.0859  -0.1431 285 PHE A CD1 
10184 C CD2 . PHE D 269 ? 0.8535 0.9645 0.8089 0.0167  0.0882  -0.1468 285 PHE A CD2 
10185 C CE1 . PHE D 269 ? 0.9019 1.0059 0.8273 0.0098  0.0903  -0.1484 285 PHE A CE1 
10186 C CE2 . PHE D 269 ? 0.8396 0.9452 0.7848 0.0180  0.0920  -0.1523 285 PHE A CE2 
10187 C CZ  . PHE D 269 ? 0.8838 0.9856 0.8136 0.0147  0.0931  -0.1532 285 PHE A CZ  
10188 N N   . GLY D 270 ? 0.8837 1.0052 0.8632 0.0104  0.0620  -0.1315 286 GLY A N   
10189 C CA  . GLY D 270 ? 0.9068 1.0310 0.8977 0.0116  0.0556  -0.1282 286 GLY A CA  
10190 C C   . GLY D 270 ? 0.9094 1.0346 0.9006 0.0090  0.0525  -0.1217 286 GLY A C   
10191 O O   . GLY D 270 ? 0.8427 0.9690 0.8437 0.0106  0.0474  -0.1187 286 GLY A O   
10192 N N   . GLN D 271 ? 0.9017 1.0262 0.8820 0.0045  0.0551  -0.1196 287 GLN A N   
10193 C CA  . GLN D 271 ? 0.9750 1.1001 0.9539 0.0006  0.0515  -0.1135 287 GLN A CA  
10194 C C   . GLN D 271 ? 1.0541 1.1806 1.0340 0.0002  0.0556  -0.1113 287 GLN A C   
10195 O O   . GLN D 271 ? 1.1632 1.2903 1.1430 -0.0032 0.0519  -0.1059 287 GLN A O   
10196 C CB  . GLN D 271 ? 1.0858 1.2091 1.0516 -0.0055 0.0511  -0.1117 287 GLN A CB  
10197 C CG  . GLN D 271 ? 1.1877 1.3102 1.1512 -0.0058 0.0477  -0.1137 287 GLN A CG  
10198 C CD  . GLN D 271 ? 1.2738 1.3943 1.2266 -0.0125 0.0445  -0.1100 287 GLN A CD  
10199 O OE1 . GLN D 271 ? 1.3223 1.4404 1.2640 -0.0152 0.0471  -0.1118 287 GLN A OE1 
10200 N NE2 . GLN D 271 ? 1.2621 1.3825 1.2173 -0.0155 0.0384  -0.1043 287 GLN A NE2 
10201 N N   . LYS D 272 ? 1.1223 1.2494 1.1028 0.0034  0.0627  -0.1153 288 LYS A N   
10202 C CA  . LYS D 272 ? 1.1206 1.2504 1.1027 0.0033  0.0670  -0.1135 288 LYS A CA  
10203 C C   . LYS D 272 ? 1.2368 1.3676 1.2311 0.0058  0.0627  -0.1101 288 LYS A C   
10204 O O   . LYS D 272 ? 1.1137 1.2427 1.1165 0.0101  0.0601  -0.1122 288 LYS A O   
10205 C CB  . LYS D 272 ? 1.0691 1.1992 1.0497 0.0067  0.0752  -0.1190 288 LYS A CB  
10206 C CG  . LYS D 272 ? 1.0959 1.2253 1.0630 0.0040  0.0810  -0.1218 288 LYS A CG  
10207 C CD  . LYS D 272 ? 1.1009 1.2342 1.0617 -0.0004 0.0850  -0.1189 288 LYS A CD  
10208 C CE  . LYS D 272 ? 1.0751 1.2065 1.0225 -0.0018 0.0914  -0.1233 288 LYS A CE  
10209 N NZ  . LYS D 272 ? 1.2013 1.3371 1.1425 -0.0047 0.0978  -0.1229 288 LYS A NZ  
10210 N N   . PRO D 273 ? 1.5199 1.6531 1.5146 0.0029  0.0619  -0.1050 289 PRO A N   
10211 C CA  . PRO D 273 ? 1.5329 1.6658 1.5376 0.0048  0.0572  -0.1012 289 PRO A CA  
10212 C C   . PRO D 273 ? 1.4062 1.5393 1.4194 0.0103  0.0615  -0.1047 289 PRO A C   
10213 O O   . PRO D 273 ? 1.3733 1.5082 1.3844 0.0117  0.0687  -0.1085 289 PRO A O   
10214 C CB  . PRO D 273 ? 1.5675 1.7034 1.5679 -0.0006 0.0569  -0.0954 289 PRO A CB  
10215 C CG  . PRO D 273 ? 1.6096 1.7494 1.6008 -0.0033 0.0652  -0.0982 289 PRO A CG  
10216 C CD  . PRO D 273 ? 1.5368 1.6733 1.5222 -0.0025 0.0660  -0.1029 289 PRO A CD  
10217 N N   . ASN D 274 ? 1.3047 1.4351 1.3271 0.0135  0.0567  -0.1035 290 ASN A N   
10218 C CA  . ASN D 274 ? 1.1809 1.3101 1.2117 0.0179  0.0595  -0.1058 290 ASN A CA  
10219 C C   . ASN D 274 ? 1.0924 1.2228 1.1276 0.0170  0.0582  -0.0999 290 ASN A C   
10220 O O   . ASN D 274 ? 1.1442 1.2726 1.1806 0.0153  0.0514  -0.0949 290 ASN A O   
10221 C CB  . ASN D 274 ? 1.1941 1.3193 1.2315 0.0215  0.0552  -0.1087 290 ASN A CB  
10222 C CG  . ASN D 274 ? 1.2785 1.4015 1.3226 0.0253  0.0585  -0.1125 290 ASN A CG  
10223 O OD1 . ASN D 274 ? 1.3650 1.4882 1.4065 0.0263  0.0639  -0.1175 290 ASN A OD1 
10224 N ND2 . ASN D 274 ? 1.2178 1.3376 1.2700 0.0273  0.0546  -0.1104 290 ASN A ND2 
10225 N N   . ILE D 275 ? 0.9387 1.0720 0.9764 0.0180  0.0642  -0.1006 291 ILE A N   
10226 C CA  . ILE D 275 ? 0.8092 0.9457 0.8492 0.0159  0.0643  -0.0947 291 ILE A CA  
10227 C C   . ILE D 275 ? 0.7363 0.8677 0.7837 0.0173  0.0580  -0.0906 291 ILE A C   
10228 O O   . ILE D 275 ? 0.7376 0.8652 0.7920 0.0212  0.0587  -0.0932 291 ILE A O   
10229 C CB  . ILE D 275 ? 0.7673 0.9087 0.8099 0.0174  0.0722  -0.0969 291 ILE A CB  
10230 C CG1 . ILE D 275 ? 0.6900 0.8370 0.7248 0.0159  0.0789  -0.1004 291 ILE A CG1 
10231 C CG2 . ILE D 275 ? 0.6939 0.8388 0.7403 0.0153  0.0715  -0.0903 291 ILE A CG2 
10232 C CD1 . ILE D 275 ? 0.6457 0.7987 0.6836 0.0177  0.0864  -0.1023 291 ILE A CD1 
10233 N N   . ASP D 276 ? 0.6118 0.7425 0.6567 0.0137  0.0519  -0.0840 292 ASP A N   
10234 C CA  . ASP D 276 ? 0.5931 0.7173 0.6432 0.0151  0.0449  -0.0801 292 ASP A CA  
10235 C C   . ASP D 276 ? 0.6265 0.7516 0.6730 0.0101  0.0406  -0.0719 292 ASP A C   
10236 O O   . ASP D 276 ? 0.6052 0.7289 0.6456 0.0064  0.0343  -0.0682 292 ASP A O   
10237 C CB  . ASP D 276 ? 0.6514 0.7703 0.7021 0.0172  0.0387  -0.0823 292 ASP A CB  
10238 C CG  . ASP D 276 ? 0.6294 0.7412 0.6851 0.0192  0.0314  -0.0790 292 ASP A CG  
10239 O OD1 . ASP D 276 ? 0.6044 0.7142 0.6627 0.0189  0.0310  -0.0749 292 ASP A OD1 
10240 O OD2 . ASP D 276 ? 0.7104 0.8184 0.7671 0.0211  0.0256  -0.0804 292 ASP A OD2 
10241 N N   . VAL D 277 ? 0.6573 0.7841 0.7073 0.0099  0.0431  -0.0688 293 VAL A N   
10242 C CA  . VAL D 277 ? 0.6239 0.7533 0.6699 0.0044  0.0401  -0.0611 293 VAL A CA  
10243 C C   . VAL D 277 ? 0.6305 0.7505 0.6767 0.0042  0.0303  -0.0554 293 VAL A C   
10244 O O   . VAL D 277 ? 0.6703 0.7902 0.7142 0.0003  0.0273  -0.0485 293 VAL A O   
10245 C CB  . VAL D 277 ? 0.5693 0.7056 0.6192 0.0041  0.0472  -0.0600 293 VAL A CB  
10246 C CG1 . VAL D 277 ? 0.5942 0.7395 0.6429 0.0045  0.0564  -0.0657 293 VAL A CG1 
10247 C CG2 . VAL D 277 ? 0.5917 0.7225 0.6506 0.0092  0.0483  -0.0620 293 VAL A CG2 
10248 N N   . THR D 278 ? 0.6376 0.7497 0.6862 0.0082  0.0252  -0.0582 294 THR A N   
10249 C CA  . THR D 278 ? 0.6338 0.7363 0.6832 0.0090  0.0161  -0.0534 294 THR A CA  
10250 C C   . THR D 278 ? 0.6799 0.7805 0.7202 0.0031  0.0078  -0.0465 294 THR A C   
10251 O O   . THR D 278 ? 0.6488 0.7445 0.6863 0.0005  0.0021  -0.0397 294 THR A O   
10252 C CB  . THR D 278 ? 0.6083 0.7038 0.6626 0.0148  0.0123  -0.0583 294 THR A CB  
10253 O OG1 . THR D 278 ? 0.6913 0.7878 0.7531 0.0193  0.0192  -0.0648 294 THR A OG1 
10254 C CG2 . THR D 278 ? 0.5642 0.6496 0.6192 0.0159  0.0039  -0.0535 294 THR A CG2 
10255 N N   . ASP D 279 ? 0.6918 0.7950 0.7266 0.0007  0.0063  -0.0480 295 ASP A N   
10256 C CA  . ASP D 279 ? 0.6835 0.7847 0.7087 -0.0060 -0.0018 -0.0416 295 ASP A CA  
10257 C C   . ASP D 279 ? 0.6605 0.7681 0.6801 -0.0129 0.0010  -0.0358 295 ASP A C   
10258 O O   . ASP D 279 ? 0.6432 0.7472 0.6554 -0.0186 -0.0067 -0.0286 295 ASP A O   
10259 C CB  . ASP D 279 ? 0.7833 0.8872 0.8035 -0.0083 -0.0025 -0.0445 295 ASP A CB  
10260 C CG  . ASP D 279 ? 0.7871 0.8838 0.8106 -0.0034 -0.0093 -0.0476 295 ASP A CG  
10261 O OD1 . ASP D 279 ? 0.7844 0.8727 0.8116 0.0005  -0.0163 -0.0461 295 ASP A OD1 
10262 O OD2 . ASP D 279 ? 0.8581 0.9577 0.8799 -0.0038 -0.0079 -0.0514 295 ASP A OD2 
10263 N N   . ALA D 280 ? 0.6646 0.7821 0.6875 -0.0126 0.0118  -0.0390 296 ALA A N   
10264 C CA  . ALA D 280 ? 0.6539 0.7800 0.6728 -0.0188 0.0157  -0.0343 296 ALA A CA  
10265 C C   . ALA D 280 ? 0.7011 0.8228 0.7218 -0.0194 0.0115  -0.0277 296 ALA A C   
10266 O O   . ALA D 280 ? 0.7933 0.9157 0.8063 -0.0266 0.0065  -0.0203 296 ALA A O   
10267 C CB  . ALA D 280 ? 0.5807 0.7178 0.6046 -0.0165 0.0282  -0.0401 296 ALA A CB  
10268 N N   . MET D 281 ? 0.7506 0.8675 0.7805 -0.0127 0.0135  -0.0301 297 MET A N   
10269 C CA  . MET D 281 ? 0.7268 0.8367 0.7584 -0.0126 0.0089  -0.0241 297 MET A CA  
10270 C C   . MET D 281 ? 0.7677 0.8666 0.7913 -0.0156 -0.0037 -0.0178 297 MET A C   
10271 O O   . MET D 281 ? 0.7486 0.8457 0.7661 -0.0211 -0.0086 -0.0098 297 MET A O   
10272 C CB  . MET D 281 ? 0.6811 0.7855 0.7232 -0.0047 0.0122  -0.0292 297 MET A CB  
10273 C CG  . MET D 281 ? 0.6399 0.7534 0.6897 -0.0017 0.0236  -0.0352 297 MET A CG  
10274 S SD  . MET D 281 ? 0.5843 0.6900 0.6440 0.0067  0.0260  -0.0430 297 MET A SD  
10275 C CE  . MET D 281 ? 0.6278 0.7220 0.6895 0.0069  0.0198  -0.0364 297 MET A CE  
10276 N N   . VAL D 282 ? 0.7357 0.8269 0.7589 -0.0120 -0.0095 -0.0212 298 VAL A N   
10277 C CA  . VAL D 282 ? 0.7162 0.7956 0.7322 -0.0139 -0.0223 -0.0157 298 VAL A CA  
10278 C C   . VAL D 282 ? 0.7321 0.8142 0.7356 -0.0236 -0.0277 -0.0091 298 VAL A C   
10279 O O   . VAL D 282 ? 0.7713 0.8466 0.7670 -0.0284 -0.0363 -0.0013 298 VAL A O   
10280 C CB  . VAL D 282 ? 0.6500 0.7222 0.6694 -0.0077 -0.0270 -0.0214 298 VAL A CB  
10281 C CG1 . VAL D 282 ? 0.6575 0.7181 0.6693 -0.0095 -0.0404 -0.0161 298 VAL A CG1 
10282 C CG2 . VAL D 282 ? 0.6532 0.7211 0.6836 0.0008  -0.0231 -0.0267 298 VAL A CG2 
10283 N N   . ASP D 283 ? 0.6868 0.7788 0.6875 -0.0274 -0.0228 -0.0119 299 ASP A N   
10284 C CA  . ASP D 283 ? 0.7486 0.8434 0.7368 -0.0376 -0.0279 -0.0060 299 ASP A CA  
10285 C C   . ASP D 283 ? 0.7426 0.8445 0.7266 -0.0444 -0.0253 0.0006  299 ASP A C   
10286 O O   . ASP D 283 ? 0.7397 0.8404 0.7121 -0.0535 -0.0326 0.0077  299 ASP A O   
10287 C CB  . ASP D 283 ? 0.7940 0.8976 0.7796 -0.0404 -0.0224 -0.0108 299 ASP A CB  
10288 C CG  . ASP D 283 ? 0.8426 0.9381 0.8279 -0.0372 -0.0289 -0.0146 299 ASP A CG  
10289 O OD1 . ASP D 283 ? 0.8579 0.9415 0.8448 -0.0328 -0.0383 -0.0137 299 ASP A OD1 
10290 O OD2 . ASP D 283 ? 0.8309 0.9322 0.8141 -0.0391 -0.0246 -0.0187 299 ASP A OD2 
10291 N N   . GLN D 284 ? 0.7570 0.8663 0.7499 -0.0408 -0.0156 -0.0013 300 GLN A N   
10292 C CA  . GLN D 284 ? 0.7449 0.8619 0.7347 -0.0472 -0.0134 0.0052  300 GLN A CA  
10293 C C   . GLN D 284 ? 0.7428 0.8491 0.7321 -0.0466 -0.0205 0.0121  300 GLN A C   
10294 O O   . GLN D 284 ? 0.7464 0.8586 0.7336 -0.0518 -0.0192 0.0183  300 GLN A O   
10295 C CB  . GLN D 284 ? 0.7202 0.8522 0.7190 -0.0450 0.0006  0.0005  300 GLN A CB  
10296 C CG  . GLN D 284 ? 0.7132 0.8558 0.7114 -0.0459 0.0084  -0.0060 300 GLN A CG  
10297 C CD  . GLN D 284 ? 0.7370 0.8931 0.7447 -0.0421 0.0219  -0.0115 300 GLN A CD  
10298 O OE1 . GLN D 284 ? 0.8075 0.9690 0.8201 -0.0423 0.0252  -0.0083 300 GLN A OE1 
10299 N NE2 . GLN D 284 ? 0.7561 0.9169 0.7662 -0.0387 0.0291  -0.0195 300 GLN A NE2 
10300 N N   . ALA D 285 ? 0.8314 0.9227 0.8222 -0.0407 -0.0281 0.0113  301 ALA A N   
10301 C CA  . ALA D 285 ? 0.8122 0.8906 0.8002 -0.0403 -0.0365 0.0178  301 ALA A CA  
10302 C C   . ALA D 285 ? 0.7733 0.8525 0.7718 -0.0352 -0.0293 0.0169  301 ALA A C   
10303 O O   . ALA D 285 ? 0.8443 0.9183 0.8396 -0.0379 -0.0330 0.0241  301 ALA A O   
10304 C CB  . ALA D 285 ? 0.9375 1.0149 0.9117 -0.0510 -0.0446 0.0282  301 ALA A CB  
10305 N N   . TRP D 286 ? 0.6729 0.7582 0.6830 -0.0284 -0.0192 0.0084  302 TRP A N   
10306 C CA  . TRP D 286 ? 0.5863 0.6701 0.6063 -0.0234 -0.0136 0.0071  302 TRP A CA  
10307 C C   . TRP D 286 ? 0.6418 0.7086 0.6628 -0.0182 -0.0208 0.0074  302 TRP A C   
10308 O O   . TRP D 286 ? 0.6738 0.7316 0.6915 -0.0155 -0.0280 0.0053  302 TRP A O   
10309 C CB  . TRP D 286 ? 0.5840 0.6773 0.6149 -0.0178 -0.0021 -0.0024 302 TRP A CB  
10310 C CG  . TRP D 286 ? 0.5616 0.6717 0.5942 -0.0214 0.0071  -0.0032 302 TRP A CG  
10311 C CD1 . TRP D 286 ? 0.5948 0.7148 0.6192 -0.0293 0.0067  0.0013  302 TRP A CD1 
10312 C CD2 . TRP D 286 ? 0.5542 0.6734 0.5970 -0.0170 0.0181  -0.0098 302 TRP A CD2 
10313 N NE1 . TRP D 286 ? 0.4953 0.6307 0.5249 -0.0297 0.0174  -0.0022 302 TRP A NE1 
10314 C CE2 . TRP D 286 ? 0.5470 0.6816 0.5880 -0.0219 0.0242  -0.0090 302 TRP A CE2 
10315 C CE3 . TRP D 286 ? 0.5637 0.6791 0.6166 -0.0097 0.0230  -0.0163 302 TRP A CE3 
10316 C CZ2 . TRP D 286 ? 0.5934 0.7392 0.6428 -0.0187 0.0349  -0.0147 302 TRP A CZ2 
10317 C CZ3 . TRP D 286 ? 0.5582 0.6839 0.6188 -0.0072 0.0330  -0.0216 302 TRP A CZ3 
10318 C CH2 . TRP D 286 ? 0.5907 0.7312 0.6497 -0.0112 0.0388  -0.0209 302 TRP A CH2 
10319 N N   . ASP D 287 ? 0.7291 0.7914 0.7544 -0.0168 -0.0191 0.0100  303 ASP A N   
10320 C CA  . ASP D 287 ? 0.7303 0.7772 0.7579 -0.0118 -0.0236 0.0097  303 ASP A CA  
10321 C C   . ASP D 287 ? 0.7052 0.7543 0.7444 -0.0075 -0.0144 0.0052  303 ASP A C   
10322 O O   . ASP D 287 ? 0.7030 0.7651 0.7483 -0.0081 -0.0053 0.0025  303 ASP A O   
10323 C CB  . ASP D 287 ? 0.7833 0.8185 0.8002 -0.0168 -0.0338 0.0202  303 ASP A CB  
10324 C CG  . ASP D 287 ? 0.8558 0.8991 0.8700 -0.0241 -0.0311 0.0285  303 ASP A CG  
10325 O OD1 . ASP D 287 ? 0.7936 0.8515 0.8156 -0.0246 -0.0210 0.0257  303 ASP A OD1 
10326 O OD2 . ASP D 287 ? 0.9755 1.0105 0.9795 -0.0295 -0.0394 0.0379  303 ASP A OD2 
10327 N N   . ALA D 288 ? 0.6409 0.6769 0.6831 -0.0033 -0.0168 0.0041  304 ALA A N   
10328 C CA  . ALA D 288 ? 0.6016 0.6382 0.6542 0.0002  -0.0088 -0.0005 304 ALA A CA  
10329 C C   . ALA D 288 ? 0.6526 0.6958 0.7067 -0.0047 -0.0046 0.0059  304 ALA A C   
10330 O O   . ALA D 288 ? 0.6605 0.7143 0.7228 -0.0038 0.0042  0.0018  304 ALA A O   
10331 C CB  . ALA D 288 ? 0.5622 0.5827 0.6161 0.0042  -0.0127 -0.0018 304 ALA A CB  
10332 N N   . GLN D 289 ? 0.6503 0.6867 0.6965 -0.0099 -0.0113 0.0160  305 GLN A N   
10333 C CA  . GLN D 289 ? 0.6112 0.6556 0.6563 -0.0162 -0.0092 0.0240  305 GLN A CA  
10334 C C   . GLN D 289 ? 0.6195 0.6837 0.6699 -0.0176 -0.0006 0.0209  305 GLN A C   
10335 O O   . GLN D 289 ? 0.6577 0.7294 0.7172 -0.0168 0.0069  0.0194  305 GLN A O   
10336 C CB  . GLN D 289 ? 0.7208 0.7588 0.7522 -0.0227 -0.0194 0.0345  305 GLN A CB  
10337 C CG  . GLN D 289 ? 0.7683 0.8178 0.7964 -0.0306 -0.0182 0.0432  305 GLN A CG  
10338 C CD  . GLN D 289 ? 0.6753 0.7191 0.7048 -0.0332 -0.0184 0.0503  305 GLN A CD  
10339 O OE1 . GLN D 289 ? 0.6810 0.7121 0.7149 -0.0290 -0.0184 0.0484  305 GLN A OE1 
10340 N NE2 . GLN D 289 ? 0.6517 0.7042 0.6765 -0.0409 -0.0194 0.0595  305 GLN A NE2 
10341 N N   . ARG D 290 ? 0.6266 0.6989 0.6712 -0.0197 -0.0018 0.0198  306 ARG A N   
10342 C CA  . ARG D 290 ? 0.5885 0.6791 0.6375 -0.0207 0.0068  0.0158  306 ARG A CA  
10343 C C   . ARG D 290 ? 0.5837 0.6785 0.6443 -0.0137 0.0159  0.0053  306 ARG A C   
10344 O O   . ARG D 290 ? 0.6169 0.7245 0.6844 -0.0136 0.0240  0.0031  306 ARG A O   
10345 C CB  . ARG D 290 ? 0.5934 0.6889 0.6332 -0.0242 0.0032  0.0158  306 ARG A CB  
10346 C CG  . ARG D 290 ? 0.5399 0.6524 0.5827 -0.0248 0.0117  0.0104  306 ARG A CG  
10347 C CD  . ARG D 290 ? 0.5447 0.6708 0.5909 -0.0287 0.0176  0.0142  306 ARG A CD  
10348 N NE  . ARG D 290 ? 0.4843 0.6268 0.5316 -0.0298 0.0253  0.0093  306 ARG A NE  
10349 C CZ  . ARG D 290 ? 0.5526 0.7007 0.5896 -0.0364 0.0222  0.0122  306 ARG A CZ  
10350 N NH1 . ARG D 290 ? 0.5203 0.6585 0.5459 -0.0417 0.0113  0.0194  306 ARG A NH1 
10351 N NH2 . ARG D 290 ? 0.6213 0.7851 0.6588 -0.0383 0.0297  0.0081  306 ARG A NH2 
10352 N N   . ILE D 291 ? 0.5869 0.6717 0.6500 -0.0078 0.0147  -0.0015 307 ILE A N   
10353 C CA  . ILE D 291 ? 0.6098 0.6982 0.6829 -0.0020 0.0228  -0.0111 307 ILE A CA  
10354 C C   . ILE D 291 ? 0.6451 0.7337 0.7265 -0.0016 0.0275  -0.0098 307 ILE A C   
10355 O O   . ILE D 291 ? 0.6044 0.7039 0.6927 -0.0003 0.0353  -0.0138 307 ILE A O   
10356 C CB  . ILE D 291 ? 0.6108 0.6886 0.6849 0.0035  0.0203  -0.0181 307 ILE A CB  
10357 C CG1 . ILE D 291 ? 0.5841 0.6651 0.6521 0.0035  0.0175  -0.0208 307 ILE A CG1 
10358 C CG2 . ILE D 291 ? 0.6006 0.6802 0.6838 0.0085  0.0277  -0.0274 307 ILE A CG2 
10359 C CD1 . ILE D 291 ? 0.5443 0.6161 0.6132 0.0084  0.0140  -0.0267 307 ILE A CD1 
10360 N N   . PHE D 292 ? 0.6317 0.7080 0.7122 -0.0029 0.0225  -0.0040 308 PHE A N   
10361 C CA  . PHE D 292 ? 0.5682 0.6429 0.6566 -0.0028 0.0262  -0.0025 308 PHE A CA  
10362 C C   . PHE D 292 ? 0.5495 0.6375 0.6398 -0.0073 0.0296  0.0036  308 PHE A C   
10363 O O   . PHE D 292 ? 0.5318 0.6248 0.6310 -0.0061 0.0352  0.0020  308 PHE A O   
10364 C CB  . PHE D 292 ? 0.5113 0.5687 0.5970 -0.0038 0.0199  0.0026  308 PHE A CB  
10365 C CG  . PHE D 292 ? 0.5319 0.5780 0.6200 0.0013  0.0193  -0.0052 308 PHE A CG  
10366 C CD1 . PHE D 292 ? 0.5434 0.5831 0.6255 0.0034  0.0140  -0.0075 308 PHE A CD1 
10367 C CD2 . PHE D 292 ? 0.5479 0.5917 0.6446 0.0041  0.0246  -0.0114 308 PHE A CD2 
10368 C CE1 . PHE D 292 ? 0.5705 0.6017 0.6554 0.0082  0.0140  -0.0154 308 PHE A CE1 
10369 C CE2 . PHE D 292 ? 0.5727 0.6076 0.6712 0.0081  0.0245  -0.0192 308 PHE A CE2 
10370 C CZ  . PHE D 292 ? 0.5565 0.5859 0.6495 0.0103  0.0194  -0.0213 308 PHE A CZ  
10371 N N   . LYS D 293 ? 0.5386 0.6329 0.6206 -0.0125 0.0260  0.0104  309 LYS A N   
10372 C CA  . LYS D 293 ? 0.5637 0.6737 0.6472 -0.0171 0.0297  0.0155  309 LYS A CA  
10373 C C   . LYS D 293 ? 0.6168 0.7429 0.7075 -0.0138 0.0391  0.0070  309 LYS A C   
10374 O O   . LYS D 293 ? 0.5971 0.7351 0.6952 -0.0143 0.0449  0.0077  309 LYS A O   
10375 C CB  . LYS D 293 ? 0.6119 0.7245 0.6831 -0.0239 0.0232  0.0235  309 LYS A CB  
10376 C CG  . LYS D 293 ? 0.6364 0.7356 0.6991 -0.0288 0.0138  0.0340  309 LYS A CG  
10377 C CD  . LYS D 293 ? 0.6365 0.7390 0.7032 -0.0327 0.0150  0.0419  309 LYS A CD  
10378 C CE  . LYS D 293 ? 0.6649 0.7503 0.7219 -0.0370 0.0051  0.0519  309 LYS A CE  
10379 N NZ  . LYS D 293 ? 0.6455 0.7307 0.7047 -0.0416 0.0047  0.0610  309 LYS A NZ  
10380 N N   . GLU D 294 ? 0.5835 0.7102 0.6717 -0.0105 0.0404  -0.0008 310 GLU A N   
10381 C CA  . GLU D 294 ? 0.5806 0.7206 0.6742 -0.0072 0.0491  -0.0092 310 GLU A CA  
10382 C C   . GLU D 294 ? 0.5760 0.7130 0.6804 -0.0012 0.0544  -0.0162 310 GLU A C   
10383 O O   . GLU D 294 ? 0.5865 0.7350 0.6976 0.0010  0.0617  -0.0205 310 GLU A O   
10384 C CB  . GLU D 294 ? 0.5601 0.7005 0.6472 -0.0059 0.0486  -0.0150 310 GLU A CB  
10385 C CG  . GLU D 294 ? 0.5472 0.6945 0.6239 -0.0124 0.0452  -0.0097 310 GLU A CG  
10386 C CD  . GLU D 294 ? 0.6627 0.8289 0.7410 -0.0159 0.0519  -0.0085 310 GLU A CD  
10387 O OE1 . GLU D 294 ? 0.6354 0.8103 0.7228 -0.0116 0.0604  -0.0146 310 GLU A OE1 
10388 O OE2 . GLU D 294 ? 0.6793 0.8513 0.7492 -0.0232 0.0484  -0.0016 310 GLU A OE2 
10389 N N   . ALA D 295 ? 0.6179 0.7395 0.7237 0.0014  0.0508  -0.0176 311 ALA A N   
10390 C CA  . ALA D 295 ? 0.5970 0.7139 0.7121 0.0056  0.0546  -0.0231 311 ALA A CA  
10391 C C   . ALA D 295 ? 0.6152 0.7366 0.7377 0.0036  0.0565  -0.0174 311 ALA A C   
10392 O O   . ALA D 295 ? 0.6057 0.7333 0.7367 0.0065  0.0623  -0.0220 311 ALA A O   
10393 C CB  . ALA D 295 ? 0.5738 0.6733 0.6878 0.0075  0.0498  -0.0250 311 ALA A CB  
10394 N N   . GLU D 296 ? 0.6344 0.7515 0.7533 -0.0015 0.0511  -0.0071 312 GLU A N   
10395 C CA  . GLU D 296 ? 0.6880 0.8107 0.8129 -0.0045 0.0523  -0.0002 312 GLU A CA  
10396 C C   . GLU D 296 ? 0.7154 0.8588 0.8453 -0.0044 0.0592  -0.0018 312 GLU A C   
10397 O O   . GLU D 296 ? 0.6531 0.8026 0.7933 -0.0021 0.0639  -0.0038 312 GLU A O   
10398 C CB  . GLU D 296 ? 0.6714 0.7881 0.7884 -0.0110 0.0449  0.0117  312 GLU A CB  
10399 C CG  . GLU D 296 ? 0.7243 0.8478 0.8458 -0.0155 0.0452  0.0206  312 GLU A CG  
10400 C CD  . GLU D 296 ? 0.8665 0.9796 0.9785 -0.0221 0.0368  0.0325  312 GLU A CD  
10401 O OE1 . GLU D 296 ? 0.9063 1.0206 1.0074 -0.0257 0.0324  0.0363  312 GLU A OE1 
10402 O OE2 . GLU D 296 ? 0.8647 0.9677 0.9794 -0.0240 0.0341  0.0382  312 GLU A OE2 
10403 N N   . LYS D 297 ? 0.6141 0.7681 0.7366 -0.0070 0.0596  -0.0009 313 LYS A N   
10404 C CA  . LYS D 297 ? 0.5931 0.7676 0.7189 -0.0072 0.0665  -0.0031 313 LYS A CA  
10405 C C   . LYS D 297 ? 0.5375 0.7166 0.6720 0.0000  0.0741  -0.0143 313 LYS A C   
10406 O O   . LYS D 297 ? 0.4565 0.6493 0.5993 0.0016  0.0801  -0.0160 313 LYS A O   
10407 C CB  . LYS D 297 ? 0.6673 0.8489 0.7819 -0.0113 0.0652  -0.0020 313 LYS A CB  
10408 C CG  . LYS D 297 ? 0.6654 0.8693 0.7805 -0.0150 0.0708  -0.0004 313 LYS A CG  
10409 C CD  . LYS D 297 ? 0.6348 0.8451 0.7374 -0.0204 0.0692  0.0006  313 LYS A CD  
10410 C CE  . LYS D 297 ? 0.7692 0.9675 0.8596 -0.0271 0.0585  0.0100  313 LYS A CE  
10411 N NZ  . LYS D 297 ? 0.6554 0.8564 0.7322 -0.0334 0.0544  0.0123  313 LYS A NZ  
10412 N N   . PHE D 298 ? 0.5586 0.7265 0.6909 0.0044  0.0736  -0.0221 314 PHE A N   
10413 C CA  . PHE D 298 ? 0.5535 0.7236 0.6917 0.0108  0.0797  -0.0328 314 PHE A CA  
10414 C C   . PHE D 298 ? 0.5139 0.6816 0.6635 0.0138  0.0815  -0.0338 314 PHE A C   
10415 O O   . PHE D 298 ? 0.5153 0.6937 0.6723 0.0172  0.0875  -0.0383 314 PHE A O   
10416 C CB  . PHE D 298 ? 0.5674 0.7248 0.7002 0.0139  0.0776  -0.0397 314 PHE A CB  
10417 C CG  . PHE D 298 ? 0.5157 0.6703 0.6538 0.0199  0.0820  -0.0499 314 PHE A CG  
10418 C CD1 . PHE D 298 ? 0.4883 0.6536 0.6266 0.0231  0.0883  -0.0570 314 PHE A CD1 
10419 C CD2 . PHE D 298 ? 0.5013 0.6414 0.6429 0.0219  0.0793  -0.0525 314 PHE A CD2 
10420 C CE1 . PHE D 298 ? 0.4703 0.6318 0.6121 0.0285  0.0916  -0.0662 314 PHE A CE1 
10421 C CE2 . PHE D 298 ? 0.4943 0.6310 0.6395 0.0266  0.0825  -0.0617 314 PHE A CE2 
10422 C CZ  . PHE D 298 ? 0.4573 0.6044 0.6023 0.0301  0.0884  -0.0684 314 PHE A CZ  
10423 N N   . PHE D 299 ? 0.5228 0.6756 0.6737 0.0125  0.0763  -0.0300 315 PHE A N   
10424 C CA  . PHE D 299 ? 0.5217 0.6708 0.6831 0.0145  0.0774  -0.0306 315 PHE A CA  
10425 C C   . PHE D 299 ? 0.5145 0.6784 0.6835 0.0125  0.0799  -0.0244 315 PHE A C   
10426 O O   . PHE D 299 ? 0.4811 0.6517 0.6600 0.0163  0.0843  -0.0286 315 PHE A O   
10427 C CB  . PHE D 299 ? 0.5296 0.6599 0.6901 0.0122  0.0712  -0.0268 315 PHE A CB  
10428 C CG  . PHE D 299 ? 0.4818 0.5988 0.6376 0.0148  0.0695  -0.0343 315 PHE A CG  
10429 C CD1 . PHE D 299 ? 0.4720 0.5863 0.6321 0.0194  0.0727  -0.0440 315 PHE A CD1 
10430 C CD2 . PHE D 299 ? 0.4531 0.5607 0.6000 0.0127  0.0645  -0.0318 315 PHE A CD2 
10431 C CE1 . PHE D 299 ? 0.4641 0.5671 0.6196 0.0212  0.0711  -0.0508 315 PHE A CE1 
10432 C CE2 . PHE D 299 ? 0.4403 0.5372 0.5838 0.0151  0.0631  -0.0388 315 PHE A CE2 
10433 C CZ  . PHE D 299 ? 0.4742 0.5692 0.6220 0.0190  0.0666  -0.0483 315 PHE A CZ  
10434 N N   . VAL D 300 ? 0.4954 0.6649 0.6596 0.0065  0.0771  -0.0145 316 VAL A N   
10435 C CA  . VAL D 300 ? 0.4521 0.6383 0.6229 0.0040  0.0798  -0.0084 316 VAL A CA  
10436 C C   . VAL D 300 ? 0.4863 0.6911 0.6623 0.0083  0.0879  -0.0160 316 VAL A C   
10437 O O   . VAL D 300 ? 0.5282 0.7452 0.7148 0.0099  0.0918  -0.0157 316 VAL A O   
10438 C CB  . VAL D 300 ? 0.4491 0.6399 0.6112 -0.0038 0.0755  0.0027  316 VAL A CB  
10439 C CG1 . VAL D 300 ? 0.4135 0.6252 0.5820 -0.0064 0.0795  0.0074  316 VAL A CG1 
10440 C CG2 . VAL D 300 ? 0.5603 0.7332 0.7179 -0.0084 0.0673  0.0117  316 VAL A CG2 
10441 N N   . SER D 301 ? 0.5252 0.7324 0.6939 0.0104  0.0905  -0.0230 317 SER A N   
10442 C CA  . SER D 301 ? 0.5216 0.7465 0.6942 0.0139  0.0984  -0.0298 317 SER A CA  
10443 C C   . SER D 301 ? 0.5453 0.7704 0.7293 0.0214  0.1027  -0.0380 317 SER A C   
10444 O O   . SER D 301 ? 0.5548 0.7963 0.7454 0.0245  0.1091  -0.0418 317 SER A O   
10445 C CB  . SER D 301 ? 0.5312 0.7570 0.6933 0.0146  0.1003  -0.0360 317 SER A CB  
10446 O OG  . SER D 301 ? 0.5697 0.7826 0.7312 0.0202  0.1005  -0.0448 317 SER A OG  
10447 N N   . VAL D 302 ? 0.4938 0.7013 0.6803 0.0243  0.0993  -0.0411 318 VAL A N   
10448 C CA  . VAL D 302 ? 0.5397 0.7458 0.7365 0.0307  0.1022  -0.0484 318 VAL A CA  
10449 C C   . VAL D 302 ? 0.5613 0.7659 0.7695 0.0295  0.0996  -0.0420 318 VAL A C   
10450 O O   . VAL D 302 ? 0.5862 0.7862 0.8031 0.0342  0.1001  -0.0471 318 VAL A O   
10451 C CB  . VAL D 302 ? 0.5342 0.7230 0.7267 0.0345  0.1004  -0.0571 318 VAL A CB  
10452 C CG1 . VAL D 302 ? 0.5199 0.7108 0.7020 0.0357  0.1030  -0.0632 318 VAL A CG1 
10453 C CG2 . VAL D 302 ? 0.5474 0.7175 0.7364 0.0305  0.0932  -0.0520 318 VAL A CG2 
10454 N N   . GLY D 303 ? 0.5047 0.7126 0.7125 0.0232  0.0964  -0.0309 319 GLY A N   
10455 C CA  . GLY D 303 ? 0.5173 0.7257 0.7358 0.0215  0.0942  -0.0241 319 GLY A CA  
10456 C C   . GLY D 303 ? 0.5875 0.7754 0.8035 0.0170  0.0867  -0.0174 319 GLY A C   
10457 O O   . GLY D 303 ? 0.6458 0.8337 0.8686 0.0137  0.0841  -0.0092 319 GLY A O   
10458 N N   . LEU D 304 ? 0.4446 0.6153 0.6512 0.0167  0.0834  -0.0206 320 LEU A N   
10459 C CA  . LEU D 304 ? 0.4664 0.6172 0.6694 0.0124  0.0766  -0.0149 320 LEU A CA  
10460 C C   . LEU D 304 ? 0.4734 0.6256 0.6699 0.0051  0.0725  -0.0025 320 LEU A C   
10461 O O   . LEU D 304 ? 0.4509 0.6186 0.6440 0.0033  0.0746  0.0006  320 LEU A O   
10462 C CB  . LEU D 304 ? 0.5208 0.6564 0.7154 0.0144  0.0750  -0.0227 320 LEU A CB  
10463 C CG  . LEU D 304 ? 0.4939 0.6236 0.6943 0.0199  0.0770  -0.0333 320 LEU A CG  
10464 C CD1 . LEU D 304 ? 0.4980 0.6183 0.6895 0.0221  0.0768  -0.0417 320 LEU A CD1 
10465 C CD2 . LEU D 304 ? 0.4521 0.5669 0.6578 0.0174  0.0726  -0.0301 320 LEU A CD2 
10466 N N   . PRO D 305 ? 0.4533 0.5890 0.6469 0.0004  0.0663  0.0048  321 PRO A N   
10467 C CA  . PRO D 305 ? 0.5123 0.6475 0.6984 -0.0067 0.0616  0.0171  321 PRO A CA  
10468 C C   . PRO D 305 ? 0.5434 0.6721 0.7153 -0.0087 0.0582  0.0180  321 PRO A C   
10469 O O   . PRO D 305 ? 0.6061 0.7263 0.7735 -0.0052 0.0583  0.0099  321 PRO A O   
10470 C CB  . PRO D 305 ? 0.5393 0.6567 0.7274 -0.0103 0.0563  0.0233  321 PRO A CB  
10471 C CG  . PRO D 305 ? 0.4935 0.5958 0.6829 -0.0060 0.0566  0.0130  321 PRO A CG  
10472 C CD  . PRO D 305 ? 0.4681 0.5846 0.6647 0.0009  0.0632  0.0023  321 PRO A CD  
10473 N N   . ASN D 306 ? 0.5505 0.6824 0.7150 -0.0150 0.0543  0.0287  322 ASN A N   
10474 C CA  . ASN D 306 ? 0.7032 0.8259 0.8539 -0.0173 0.0493  0.0306  322 ASN A CA  
10475 C C   . ASN D 306 ? 0.6514 0.7504 0.7971 -0.0189 0.0430  0.0334  322 ASN A C   
10476 O O   . ASN D 306 ? 0.6199 0.7102 0.7710 -0.0205 0.0417  0.0369  322 ASN A O   
10477 C CB  . ASN D 306 ? 0.7590 0.8916 0.9008 -0.0237 0.0463  0.0403  322 ASN A CB  
10478 C CG  . ASN D 306 ? 0.9867 1.1342 1.1351 -0.0282 0.0478  0.0489  322 ASN A CG  
10479 O OD1 . ASN D 306 ? 1.1142 1.2580 1.2712 -0.0286 0.0477  0.0521  322 ASN A OD1 
10480 N ND2 . ASN D 306 ? 1.1918 1.3569 1.3357 -0.0321 0.0490  0.0526  322 ASN A ND2 
10481 N N   . MET D 307 ? 0.6101 0.6985 0.7456 -0.0183 0.0394  0.0312  323 MET A N   
10482 C CA  . MET D 307 ? 0.5886 0.6551 0.7186 -0.0196 0.0336  0.0333  323 MET A CA  
10483 C C   . MET D 307 ? 0.6266 0.6862 0.7512 -0.0267 0.0277  0.0468  323 MET A C   
10484 O O   . MET D 307 ? 0.6098 0.6801 0.7300 -0.0311 0.0261  0.0548  323 MET A O   
10485 C CB  . MET D 307 ? 0.5549 0.6135 0.6749 -0.0174 0.0304  0.0290  323 MET A CB  
10486 C CG  . MET D 307 ? 0.5299 0.5928 0.6532 -0.0110 0.0351  0.0163  323 MET A CG  
10487 S SD  . MET D 307 ? 0.5391 0.5892 0.6702 -0.0071 0.0376  0.0072  323 MET A SD  
10488 C CE  . MET D 307 ? 0.5606 0.6269 0.7047 -0.0047 0.0451  0.0030  323 MET A CE  
10489 N N   . THR D 308 ? 0.6323 0.6734 0.7563 -0.0283 0.0242  0.0493  324 THR A N   
10490 C CA  . THR D 308 ? 0.5851 0.6163 0.7029 -0.0352 0.0182  0.0620  324 THR A CA  
10491 C C   . THR D 308 ? 0.6063 0.6289 0.7087 -0.0382 0.0111  0.0681  324 THR A C   
10492 O O   . THR D 308 ? 0.6149 0.6292 0.7114 -0.0345 0.0093  0.0619  324 THR A O   
10493 C CB  . THR D 308 ? 0.5918 0.6036 0.7120 -0.0362 0.0165  0.0622  324 THR A CB  
10494 O OG1 . THR D 308 ? 0.5759 0.5715 0.6892 -0.0334 0.0140  0.0561  324 THR A OG1 
10495 C CG2 . THR D 308 ? 0.6376 0.6556 0.7721 -0.0329 0.0226  0.0549  324 THR A CG2 
10496 N N   . GLN D 309 ? 0.6170 0.6410 0.7125 -0.0450 0.0064  0.0806  325 GLN A N   
10497 C CA  . GLN D 309 ? 0.6757 0.6881 0.7550 -0.0490 -0.0020 0.0881  325 GLN A CA  
10498 C C   . GLN D 309 ? 0.6828 0.6714 0.7558 -0.0465 -0.0062 0.0848  325 GLN A C   
10499 O O   . GLN D 309 ? 0.7121 0.6915 0.7737 -0.0457 -0.0117 0.0847  325 GLN A O   
10500 C CB  . GLN D 309 ? 0.6952 0.7062 0.7682 -0.0575 -0.0070 0.1027  325 GLN A CB  
10501 C CG  . GLN D 309 ? 0.8028 0.8011 0.8578 -0.0623 -0.0165 0.1115  325 GLN A CG  
10502 C CD  . GLN D 309 ? 1.0950 1.0894 1.1439 -0.0713 -0.0215 0.1263  325 GLN A CD  
10503 O OE1 . GLN D 309 ? 1.0607 1.0634 1.1203 -0.0735 -0.0175 0.1297  325 GLN A OE1 
10504 N NE2 . GLN D 309 ? 1.2789 1.2598 1.3103 -0.0765 -0.0309 0.1355  325 GLN A NE2 
10505 N N   . GLY D 310 ? 0.6481 0.6259 0.7280 -0.0457 -0.0041 0.0825  326 GLY A N   
10506 C CA  . GLY D 310 ? 0.6205 0.5769 0.6953 -0.0435 -0.0070 0.0783  326 GLY A CA  
10507 C C   . GLY D 310 ? 0.6356 0.5949 0.7127 -0.0360 -0.0041 0.0652  326 GLY A C   
10508 O O   . GLY D 310 ? 0.7007 0.6468 0.7699 -0.0338 -0.0082 0.0626  326 GLY A O   
10509 N N   . PHE D 311 ? 0.6540 0.6305 0.7420 -0.0320 0.0030  0.0570  327 PHE A N   
10510 C CA  . PHE D 311 ? 0.6103 0.5909 0.7004 -0.0253 0.0059  0.0449  327 PHE A CA  
10511 C C   . PHE D 311 ? 0.6193 0.6006 0.6986 -0.0247 0.0008  0.0465  327 PHE A C   
10512 O O   . PHE D 311 ? 0.6050 0.5779 0.6804 -0.0206 -0.0014 0.0404  327 PHE A O   
10513 C CB  . PHE D 311 ? 0.6053 0.6047 0.7070 -0.0220 0.0138  0.0376  327 PHE A CB  
10514 C CG  . PHE D 311 ? 0.6429 0.6489 0.7454 -0.0161 0.0167  0.0267  327 PHE A CG  
10515 C CD1 . PHE D 311 ? 0.6528 0.6514 0.7593 -0.0118 0.0191  0.0164  327 PHE A CD1 
10516 C CD2 . PHE D 311 ? 0.5995 0.6198 0.6989 -0.0155 0.0171  0.0268  327 PHE A CD2 
10517 C CE1 . PHE D 311 ? 0.5803 0.5855 0.6874 -0.0067 0.0215  0.0069  327 PHE A CE1 
10518 C CE2 . PHE D 311 ? 0.5573 0.5833 0.6572 -0.0105 0.0196  0.0173  327 PHE A CE2 
10519 C CZ  . PHE D 311 ? 0.6007 0.6194 0.7047 -0.0060 0.0218  0.0075  327 PHE A CZ  
10520 N N   . TRP D 312 ? 0.6289 0.6202 0.7031 -0.0290 -0.0015 0.0551  328 TRP A N   
10521 C CA  . TRP D 312 ? 0.6320 0.6239 0.6950 -0.0296 -0.0073 0.0574  328 TRP A CA  
10522 C C   . TRP D 312 ? 0.6578 0.6283 0.7082 -0.0314 -0.0165 0.0634  328 TRP A C   
10523 O O   . TRP D 312 ? 0.7067 0.6698 0.7507 -0.0278 -0.0208 0.0594  328 TRP A O   
10524 C CB  . TRP D 312 ? 0.6133 0.6217 0.6734 -0.0349 -0.0076 0.0651  328 TRP A CB  
10525 C CG  . TRP D 312 ? 0.6338 0.6641 0.7048 -0.0325 0.0012  0.0583  328 TRP A CG  
10526 C CD1 . TRP D 312 ? 0.6637 0.7082 0.7440 -0.0345 0.0071  0.0604  328 TRP A CD1 
10527 C CD2 . TRP D 312 ? 0.6170 0.6562 0.6909 -0.0272 0.0052  0.0479  328 TRP A CD2 
10528 N NE1 . TRP D 312 ? 0.6645 0.7264 0.7526 -0.0306 0.0144  0.0519  328 TRP A NE1 
10529 C CE2 . TRP D 312 ? 0.6246 0.6830 0.7085 -0.0263 0.0134  0.0442  328 TRP A CE2 
10530 C CE3 . TRP D 312 ? 0.6035 0.6365 0.6725 -0.0231 0.0025  0.0414  328 TRP A CE3 
10531 C CZ2 . TRP D 312 ? 0.6156 0.6857 0.7033 -0.0219 0.0188  0.0347  328 TRP A CZ2 
10532 C CZ3 . TRP D 312 ? 0.6048 0.6501 0.6782 -0.0190 0.0077  0.0323  328 TRP A CZ3 
10533 C CH2 . TRP D 312 ? 0.6201 0.6832 0.7021 -0.0186 0.0158  0.0291  328 TRP A CH2 
10534 N N   . GLU D 313 ? 0.6567 0.6165 0.7031 -0.0367 -0.0198 0.0730  329 GLU A N   
10535 C CA  . GLU D 313 ? 0.7022 0.6403 0.7354 -0.0385 -0.0286 0.0788  329 GLU A CA  
10536 C C   . GLU D 313 ? 0.7190 0.6431 0.7541 -0.0319 -0.0281 0.0688  329 GLU A C   
10537 O O   . GLU D 313 ? 0.7809 0.6936 0.8067 -0.0295 -0.0346 0.0679  329 GLU A O   
10538 C CB  . GLU D 313 ? 0.8006 0.7291 0.8300 -0.0455 -0.0314 0.0904  329 GLU A CB  
10539 C CG  . GLU D 313 ? 0.8905 0.8197 0.9065 -0.0528 -0.0389 0.1035  329 GLU A CG  
10540 C CD  . GLU D 313 ? 0.9507 0.8835 0.9684 -0.0604 -0.0382 0.1146  329 GLU A CD  
10541 O OE1 . GLU D 313 ? 0.9353 0.8625 0.9614 -0.0604 -0.0342 0.1136  329 GLU A OE1 
10542 O OE2 . GLU D 313 ? 0.9951 0.9369 1.0059 -0.0668 -0.0417 0.1242  329 GLU A OE2 
10543 N N   . ASN D 314 ? 0.7040 0.6303 0.7514 -0.0288 -0.0207 0.0604  330 ASN A N   
10544 C CA  . ASN D 314 ? 0.7035 0.6144 0.7519 -0.0250 -0.0204 0.0531  330 ASN A CA  
10545 C C   . ASN D 314 ? 0.6907 0.6089 0.7467 -0.0177 -0.0157 0.0393  330 ASN A C   
10546 O O   . ASN D 314 ? 0.7044 0.6107 0.7592 -0.0141 -0.0167 0.0329  330 ASN A O   
10547 C CB  . ASN D 314 ? 0.7417 0.6457 0.7968 -0.0282 -0.0164 0.0538  330 ASN A CB  
10548 C CG  . ASN D 314 ? 0.7071 0.6021 0.7553 -0.0357 -0.0209 0.0674  330 ASN A CG  
10549 O OD1 . ASN D 314 ? 0.7077 0.6079 0.7629 -0.0396 -0.0174 0.0712  330 ASN A OD1 
10550 N ND2 . ASN D 314 ? 0.7106 0.5922 0.7446 -0.0380 -0.0291 0.0751  330 ASN A ND2 
10551 N N   . SER D 315 ? 0.6811 0.6183 0.7451 -0.0156 -0.0101 0.0342  331 SER A N   
10552 C CA  . SER D 315 ? 0.6051 0.5480 0.6751 -0.0091 -0.0061 0.0216  331 SER A CA  
10553 C C   . SER D 315 ? 0.6514 0.5880 0.7129 -0.0057 -0.0125 0.0201  331 SER A C   
10554 O O   . SER D 315 ? 0.6667 0.5974 0.7178 -0.0083 -0.0198 0.0287  331 SER A O   
10555 C CB  . SER D 315 ? 0.5910 0.5546 0.6690 -0.0076 0.0003  0.0170  331 SER A CB  
10556 O OG  . SER D 315 ? 0.5829 0.5516 0.6695 -0.0098 0.0060  0.0171  331 SER A OG  
10557 N N   . MET D 316 ? 0.6795 0.6162 0.7453 0.0001  -0.0104 0.0093  332 MET A N   
10558 C CA  . MET D 316 ? 0.6494 0.5842 0.7102 0.0047  -0.0154 0.0056  332 MET A CA  
10559 C C   . MET D 316 ? 0.6207 0.5733 0.6875 0.0078  -0.0109 -0.0015 332 MET A C   
10560 O O   . MET D 316 ? 0.6233 0.5810 0.6980 0.0114  -0.0052 -0.0113 332 MET A O   
10561 C CB  . MET D 316 ? 0.6469 0.5690 0.7083 0.0091  -0.0165 -0.0017 332 MET A CB  
10562 C CG  . MET D 316 ? 0.7433 0.6672 0.8032 0.0151  -0.0202 -0.0080 332 MET A CG  
10563 S SD  . MET D 316 ? 0.8366 0.7452 0.8959 0.0202  -0.0229 -0.0150 332 MET A SD  
10564 C CE  . MET D 316 ? 0.7632 0.6517 0.8092 0.0161  -0.0317 -0.0025 332 MET A CE  
10565 N N   . LEU D 317 ? 0.6215 0.5830 0.6834 0.0058  -0.0137 0.0038  333 LEU A N   
10566 C CA  . LEU D 317 ? 0.6961 0.6744 0.7626 0.0077  -0.0092 -0.0019 333 LEU A CA  
10567 C C   . LEU D 317 ? 0.7008 0.6799 0.7635 0.0118  -0.0140 -0.0061 333 LEU A C   
10568 O O   . LEU D 317 ? 0.6482 0.6403 0.7127 0.0125  -0.0114 -0.0096 333 LEU A O   
10569 C CB  . LEU D 317 ? 0.6397 0.6303 0.7049 0.0025  -0.0073 0.0052  333 LEU A CB  
10570 C CG  . LEU D 317 ? 0.5504 0.5425 0.6205 -0.0013 -0.0027 0.0096  333 LEU A CG  
10571 C CD1 . LEU D 317 ? 0.5722 0.5782 0.6409 -0.0058 -0.0012 0.0157  333 LEU A CD1 
10572 C CD2 . LEU D 317 ? 0.5356 0.5329 0.6169 0.0019  0.0057  0.0003  333 LEU A CD2 
10573 N N   . THR D 318 ? 0.7135 0.6787 0.7714 0.0146  -0.0209 -0.0063 334 THR A N   
10574 C CA  . THR D 318 ? 0.7053 0.6703 0.7607 0.0190  -0.0262 -0.0106 334 THR A CA  
10575 C C   . THR D 318 ? 0.8004 0.7506 0.8552 0.0237  -0.0305 -0.0142 334 THR A C   
10576 O O   . THR D 318 ? 0.7709 0.7074 0.8207 0.0219  -0.0339 -0.0087 334 THR A O   
10577 C CB  . THR D 318 ? 0.7139 0.6775 0.7584 0.0157  -0.0349 -0.0023 334 THR A CB  
10578 O OG1 . THR D 318 ? 0.6704 0.6193 0.7061 0.0125  -0.0415 0.0067  334 THR A OG1 
10579 C CG2 . THR D 318 ? 0.6596 0.6377 0.7032 0.0104  -0.0315 0.0018  334 THR A CG2 
10580 N N   . ASP D 319 ? 0.8839 0.8368 0.9429 0.0297  -0.0310 -0.0230 335 ASP A N   
10581 C CA  . ASP D 319 ? 0.8963 0.8376 0.9555 0.0352  -0.0353 -0.0278 335 ASP A CA  
10582 C C   . ASP D 319 ? 0.9584 0.8836 1.0062 0.0344  -0.0459 -0.0193 335 ASP A C   
10583 O O   . ASP D 319 ? 0.9270 0.8524 0.9676 0.0335  -0.0532 -0.0144 335 ASP A O   
10584 C CB  . ASP D 319 ? 0.9204 0.8697 0.9846 0.0410  -0.0360 -0.0365 335 ASP A CB  
10585 C CG  . ASP D 319 ? 1.0071 0.9486 1.0750 0.0474  -0.0377 -0.0439 335 ASP A CG  
10586 O OD1 . ASP D 319 ? 1.0307 0.9571 1.0924 0.0485  -0.0443 -0.0401 335 ASP A OD1 
10587 O OD2 . ASP D 319 ? 1.1465 1.0970 1.2230 0.0511  -0.0327 -0.0536 335 ASP A OD2 
10588 N N   . PRO D 320 ? 1.0461 0.9568 1.0911 0.0344  -0.0472 -0.0175 336 PRO A N   
10589 C CA  . PRO D 320 ? 1.0357 0.9298 1.0682 0.0325  -0.0570 -0.0082 336 PRO A CA  
10590 C C   . PRO D 320 ? 1.1119 0.9962 1.1405 0.0392  -0.0659 -0.0116 336 PRO A C   
10591 O O   . PRO D 320 ? 1.1939 1.0614 1.2162 0.0410  -0.0712 -0.0097 336 PRO A O   
10592 C CB  . PRO D 320 ? 1.0324 0.9149 1.0643 0.0299  -0.0535 -0.0061 336 PRO A CB  
10593 C CG  . PRO D 320 ? 1.0009 0.8894 1.0448 0.0340  -0.0450 -0.0179 336 PRO A CG  
10594 C CD  . PRO D 320 ? 1.0335 0.9419 1.0856 0.0347  -0.0395 -0.0230 336 PRO A CD  
10595 N N   . GLY D 321 ? 1.1276 1.0219 1.1599 0.0429  -0.0676 -0.0165 337 GLY A N   
10596 C CA  . GLY D 321 ? 1.3819 1.2672 1.4107 0.0492  -0.0772 -0.0190 337 GLY A CA  
10597 C C   . GLY D 321 ? 1.4977 1.3810 1.5355 0.0570  -0.0740 -0.0300 337 GLY A C   
10598 O O   . GLY D 321 ? 1.3522 1.2418 1.3991 0.0572  -0.0641 -0.0364 337 GLY A O   
10599 N N   . ASN D 322 ? 1.7828 1.6570 1.8177 0.0635  -0.0830 -0.0323 338 ASN A N   
10600 C CA  . ASN D 322 ? 1.8982 1.7719 1.9420 0.0717  -0.0810 -0.0433 338 ASN A CA  
10601 C C   . ASN D 322 ? 1.8773 1.7328 1.9159 0.0734  -0.0827 -0.0428 338 ASN A C   
10602 O O   . ASN D 322 ? 1.8792 1.7348 1.9256 0.0789  -0.0787 -0.0523 338 ASN A O   
10603 C CB  . ASN D 322 ? 1.9502 1.8260 1.9958 0.0788  -0.0895 -0.0474 338 ASN A CB  
10604 C CG  . ASN D 322 ? 2.0490 1.9325 2.1076 0.0870  -0.0853 -0.0603 338 ASN A CG  
10605 O OD1 . ASN D 322 ? 2.0383 1.9291 2.1052 0.0864  -0.0748 -0.0667 338 ASN A OD1 
10606 N ND2 . ASN D 322 ? 2.0932 1.9754 2.1537 0.0944  -0.0936 -0.0642 338 ASN A ND2 
10607 N N   . VAL D 323 ? 1.6465 1.4868 1.6719 0.0682  -0.0884 -0.0320 339 VAL A N   
10608 C CA  . VAL D 323 ? 1.5651 1.3862 1.5836 0.0691  -0.0905 -0.0305 339 VAL A CA  
10609 C C   . VAL D 323 ? 1.5192 1.3433 1.5454 0.0666  -0.0787 -0.0355 339 VAL A C   
10610 O O   . VAL D 323 ? 1.4289 1.2488 1.4600 0.0716  -0.0758 -0.0440 339 VAL A O   
10611 C CB  . VAL D 323 ? 1.5670 1.3718 1.5686 0.0627  -0.0990 -0.0168 339 VAL A CB  
10612 C CG1 . VAL D 323 ? 1.4809 1.2647 1.4745 0.0633  -0.1011 -0.0150 339 VAL A CG1 
10613 C CG2 . VAL D 323 ? 1.5369 1.3374 1.5299 0.0647  -0.1117 -0.0122 339 VAL A CG2 
10614 N N   . GLN D 324 ? 1.4116 1.2429 1.4388 0.0585  -0.0720 -0.0303 340 GLN A N   
10615 C CA  . GLN D 324 ? 1.2640 1.0981 1.2980 0.0548  -0.0614 -0.0341 340 GLN A CA  
10616 C C   . GLN D 324 ? 1.2557 1.1111 1.3032 0.0555  -0.0523 -0.0426 340 GLN A C   
10617 O O   . GLN D 324 ? 1.2925 1.1607 1.3417 0.0536  -0.0519 -0.0400 340 GLN A O   
10618 C CB  . GLN D 324 ? 1.2049 1.0329 1.2317 0.0456  -0.0601 -0.0229 340 GLN A CB  
10619 C CG  . GLN D 324 ? 1.1585 0.9960 1.1818 0.0407  -0.0625 -0.0140 340 GLN A CG  
10620 C CD  . GLN D 324 ? 1.1576 0.9908 1.1757 0.0315  -0.0602 -0.0035 340 GLN A CD  
10621 O OE1 . GLN D 324 ? 1.0208 0.8548 1.0448 0.0285  -0.0523 -0.0059 340 GLN A OE1 
10622 N NE2 . GLN D 324 ? 1.0967 0.9261 1.1040 0.0268  -0.0672 0.0079  340 GLN A NE2 
10623 N N   . LYS D 325 ? 1.1736 1.0325 1.2297 0.0574  -0.0449 -0.0526 341 LYS A N   
10624 C CA  . LYS D 325 ? 1.1739 1.0519 1.2413 0.0571  -0.0366 -0.0602 341 LYS A CA  
10625 C C   . LYS D 325 ? 1.0585 0.9382 1.1272 0.0491  -0.0292 -0.0568 341 LYS A C   
10626 O O   . LYS D 325 ? 0.9796 0.8455 1.0430 0.0448  -0.0290 -0.0521 341 LYS A O   
10627 C CB  . LYS D 325 ? 1.2255 1.1093 1.3021 0.0629  -0.0327 -0.0733 341 LYS A CB  
10628 C CG  . LYS D 325 ? 1.3288 1.2117 1.4062 0.0720  -0.0400 -0.0779 341 LYS A CG  
10629 C CD  . LYS D 325 ? 1.4282 1.3170 1.5031 0.0741  -0.0473 -0.0730 341 LYS A CD  
10630 C CE  . LYS D 325 ? 1.3890 1.2834 1.4693 0.0832  -0.0524 -0.0805 341 LYS A CE  
10631 N NZ  . LYS D 325 ? 1.2021 1.1150 1.2948 0.0861  -0.0459 -0.0911 341 LYS A NZ  
10632 N N   . ALA D 326 ? 1.0354 0.9313 1.1107 0.0471  -0.0236 -0.0590 342 ALA A N   
10633 C CA  . ALA D 326 ? 0.8882 0.7873 0.9652 0.0401  -0.0172 -0.0557 342 ALA A CA  
10634 C C   . ALA D 326 ? 0.8630 0.7780 0.9496 0.0403  -0.0094 -0.0647 342 ALA A C   
10635 O O   . ALA D 326 ? 0.9147 0.8424 1.0049 0.0440  -0.0095 -0.0688 342 ALA A O   
10636 C CB  . ALA D 326 ? 0.9227 0.8242 0.9944 0.0361  -0.0200 -0.0447 342 ALA A CB  
10637 N N   . VAL D 327 ? 0.8208 0.7348 0.9107 0.0357  -0.0031 -0.0673 343 VAL A N   
10638 C CA  . VAL D 327 ? 0.8253 0.7530 0.9229 0.0354  0.0036  -0.0758 343 VAL A CA  
10639 C C   . VAL D 327 ? 0.8754 0.8155 0.9743 0.0339  0.0055  -0.0720 343 VAL A C   
10640 O O   . VAL D 327 ? 0.8453 0.7844 0.9436 0.0290  0.0077  -0.0662 343 VAL A O   
10641 C CB  . VAL D 327 ? 0.7649 0.6864 0.8647 0.0304  0.0089  -0.0797 343 VAL A CB  
10642 C CG1 . VAL D 327 ? 0.7671 0.7015 0.8733 0.0290  0.0152  -0.0876 343 VAL A CG1 
10643 C CG2 . VAL D 327 ? 0.7498 0.6618 0.8487 0.0325  0.0076  -0.0851 343 VAL A CG2 
10644 N N   . CYS D 328 ? 0.8667 0.8190 0.9677 0.0381  0.0048  -0.0756 344 CYS A N   
10645 C CA  . CYS D 328 ? 0.8685 0.8318 0.9690 0.0373  0.0052  -0.0715 344 CYS A CA  
10646 C C   . CYS D 328 ? 0.8664 0.8413 0.9719 0.0354  0.0123  -0.0765 344 CYS A C   
10647 O O   . CYS D 328 ? 0.8502 0.8351 0.9553 0.0352  0.0132  -0.0742 344 CYS A O   
10648 C CB  . CYS D 328 ? 0.8375 0.8073 0.9367 0.0421  0.0004  -0.0723 344 CYS A CB  
10649 S SG  . CYS D 328 ? 1.1687 1.1263 1.2595 0.0435  -0.0096 -0.0632 344 CYS A SG  
10650 N N   . HIS D 329 ? 0.8454 0.8189 0.9548 0.0336  0.0171  -0.0832 345 HIS A N   
10651 C CA  . HIS D 329 ? 0.7636 0.7457 0.8763 0.0311  0.0229  -0.0865 345 HIS A CA  
10652 C C   . HIS D 329 ? 0.7454 0.7267 0.8566 0.0275  0.0236  -0.0777 345 HIS A C   
10653 O O   . HIS D 329 ? 0.8058 0.7763 0.9147 0.0246  0.0214  -0.0710 345 HIS A O   
10654 C CB  . HIS D 329 ? 0.7430 0.7214 0.8587 0.0286  0.0269  -0.0942 345 HIS A CB  
10655 C CG  . HIS D 329 ? 0.8258 0.8117 0.9438 0.0262  0.0320  -0.0984 345 HIS A CG  
10656 N ND1 . HIS D 329 ? 0.8594 0.8408 0.9782 0.0218  0.0343  -0.0951 345 HIS A ND1 
10657 C CD2 . HIS D 329 ? 0.9385 0.9354 1.0579 0.0277  0.0349  -0.1053 345 HIS A CD2 
10658 C CE1 . HIS D 329 ? 0.8234 0.8123 0.9439 0.0210  0.0381  -0.1003 345 HIS A CE1 
10659 N NE2 . HIS D 329 ? 0.9749 0.9731 1.0953 0.0244  0.0386  -0.1064 345 HIS A NE2 
10660 N N   . PRO D 330 ? 0.7474 0.7400 0.8594 0.0275  0.0262  -0.0769 346 PRO A N   
10661 C CA  . PRO D 330 ? 0.7294 0.7231 0.8408 0.0243  0.0270  -0.0687 346 PRO A CA  
10662 C C   . PRO D 330 ? 0.7412 0.7293 0.8561 0.0206  0.0305  -0.0694 346 PRO A C   
10663 O O   . PRO D 330 ? 0.7442 0.7366 0.8624 0.0204  0.0347  -0.0765 346 PRO A O   
10664 C CB  . PRO D 330 ? 0.7059 0.7140 0.8177 0.0259  0.0297  -0.0701 346 PRO A CB  
10665 C CG  . PRO D 330 ? 0.7085 0.7209 0.8192 0.0296  0.0282  -0.0758 346 PRO A CG  
10666 C CD  . PRO D 330 ? 0.7798 0.7850 0.8927 0.0305  0.0281  -0.0826 346 PRO A CD  
10667 N N   . THR D 331 ? 0.6982 0.6761 0.8117 0.0172  0.0281  -0.0618 347 THR A N   
10668 C CA  . THR D 331 ? 0.6867 0.6570 0.8032 0.0130  0.0304  -0.0617 347 THR A CA  
10669 C C   . THR D 331 ? 0.6623 0.6304 0.7786 0.0093  0.0293  -0.0512 347 THR A C   
10670 O O   . THR D 331 ? 0.6756 0.6416 0.7874 0.0089  0.0253  -0.0429 347 THR A O   
10671 C CB  . THR D 331 ? 0.7050 0.6616 0.8199 0.0115  0.0287  -0.0651 347 THR A CB  
10672 O OG1 . THR D 331 ? 0.7209 0.6700 0.8305 0.0128  0.0235  -0.0598 347 THR A OG1 
10673 C CG2 . THR D 331 ? 0.6620 0.6227 0.7787 0.0139  0.0311  -0.0767 347 THR A CG2 
10674 N N   . ALA D 332 ? 0.6219 0.5903 0.7430 0.0066  0.0325  -0.0514 348 ALA A N   
10675 C CA  . ALA D 332 ? 0.6001 0.5705 0.7230 0.0036  0.0324  -0.0423 348 ALA A CA  
10676 C C   . ALA D 332 ? 0.6290 0.5852 0.7530 -0.0017 0.0310  -0.0380 348 ALA A C   
10677 O O   . ALA D 332 ? 0.6025 0.5569 0.7314 -0.0036 0.0335  -0.0420 348 ALA A O   
10678 C CB  . ALA D 332 ? 0.5833 0.5681 0.7118 0.0054  0.0371  -0.0454 348 ALA A CB  
10679 N N   . TRP D 333 ? 0.6250 0.5709 0.7437 -0.0046 0.0265  -0.0293 349 TRP A N   
10680 C CA  . TRP D 333 ? 0.5768 0.5063 0.6940 -0.0100 0.0243  -0.0247 349 TRP A CA  
10681 C C   . TRP D 333 ? 0.6502 0.5812 0.7717 -0.0142 0.0245  -0.0163 349 TRP A C   
10682 O O   . TRP D 333 ? 0.6399 0.5787 0.7603 -0.0143 0.0233  -0.0081 349 TRP A O   
10683 C CB  . TRP D 333 ? 0.5700 0.4875 0.6785 -0.0110 0.0190  -0.0185 349 TRP A CB  
10684 C CG  . TRP D 333 ? 0.6574 0.5724 0.7627 -0.0068 0.0183  -0.0266 349 TRP A CG  
10685 C CD1 . TRP D 333 ? 0.6507 0.5779 0.7566 -0.0011 0.0193  -0.0325 349 TRP A CD1 
10686 C CD2 . TRP D 333 ? 0.6710 0.5711 0.7722 -0.0078 0.0166  -0.0300 349 TRP A CD2 
10687 N NE1 . TRP D 333 ? 0.6079 0.5292 0.7110 0.0017  0.0180  -0.0390 349 TRP A NE1 
10688 C CE2 . TRP D 333 ? 0.6387 0.5439 0.7391 -0.0022 0.0166  -0.0380 349 TRP A CE2 
10689 C CE3 . TRP D 333 ? 0.6802 0.5631 0.7784 -0.0132 0.0151  -0.0270 349 TRP A CE3 
10690 C CZ2 . TRP D 333 ? 0.6839 0.5787 0.7812 -0.0013 0.0154  -0.0435 349 TRP A CZ2 
10691 C CZ3 . TRP D 333 ? 0.6747 0.5465 0.7689 -0.0127 0.0141  -0.0325 349 TRP A CZ3 
10692 C CH2 . TRP D 333 ? 0.6867 0.5650 0.7809 -0.0066 0.0144  -0.0408 349 TRP A CH2 
10693 N N   . ASP D 334 ? 0.7364 0.6600 0.8624 -0.0179 0.0259  -0.0185 350 ASP A N   
10694 C CA  . ASP D 334 ? 0.7103 0.6304 0.8405 -0.0229 0.0251  -0.0105 350 ASP A CA  
10695 C C   . ASP D 334 ? 0.7933 0.6926 0.9179 -0.0291 0.0214  -0.0057 350 ASP A C   
10696 O O   . ASP D 334 ? 0.8291 0.7178 0.9544 -0.0319 0.0219  -0.0118 350 ASP A O   
10697 C CB  . ASP D 334 ? 0.6908 0.6171 0.8300 -0.0223 0.0288  -0.0173 350 ASP A CB  
10698 C CG  . ASP D 334 ? 0.8613 0.7833 1.0064 -0.0274 0.0277  -0.0101 350 ASP A CG  
10699 O OD1 . ASP D 334 ? 0.8165 0.7298 0.9589 -0.0324 0.0243  0.0006  350 ASP A OD1 
10700 O OD2 . ASP D 334 ? 0.9300 0.8577 1.0828 -0.0263 0.0301  -0.0151 350 ASP A OD2 
10701 N N   . LEU D 335 ? 0.7347 0.6275 0.8529 -0.0318 0.0173  0.0052  351 LEU A N   
10702 C CA  . LEU D 335 ? 0.7417 0.6136 0.8532 -0.0377 0.0137  0.0096  351 LEU A CA  
10703 C C   . LEU D 335 ? 0.7401 0.6044 0.8552 -0.0447 0.0124  0.0176  351 LEU A C   
10704 O O   . LEU D 335 ? 0.7084 0.5541 0.8183 -0.0507 0.0097  0.0213  351 LEU A O   
10705 C CB  . LEU D 335 ? 0.7247 0.5898 0.8256 -0.0376 0.0090  0.0174  351 LEU A CB  
10706 C CG  . LEU D 335 ? 0.7346 0.6023 0.8301 -0.0315 0.0083  0.0114  351 LEU A CG  
10707 C CD1 . LEU D 335 ? 0.7217 0.6088 0.8198 -0.0269 0.0093  0.0124  351 LEU A CD1 
10708 C CD2 . LEU D 335 ? 0.7823 0.6341 0.8661 -0.0334 0.0027  0.0184  351 LEU A CD2 
10709 N N   . GLY D 336 ? 0.7208 0.5989 0.8445 -0.0441 0.0142  0.0206  352 GLY A N   
10710 C CA  . GLY D 336 ? 0.7283 0.6009 0.8562 -0.0504 0.0125  0.0291  352 GLY A CA  
10711 C C   . GLY D 336 ? 0.6958 0.5642 0.8172 -0.0545 0.0081  0.0433  352 GLY A C   
10712 O O   . GLY D 336 ? 0.6816 0.5521 0.7949 -0.0524 0.0062  0.0467  352 GLY A O   
10713 N N   . LYS D 337 ? 0.6711 0.5327 0.7955 -0.0610 0.0060  0.0521  353 LYS A N   
10714 C CA  . LYS D 337 ? 0.6626 0.5262 0.7846 -0.0654 0.0025  0.0665  353 LYS A CA  
10715 C C   . LYS D 337 ? 0.6433 0.5263 0.7644 -0.0607 0.0033  0.0693  353 LYS A C   
10716 O O   . LYS D 337 ? 0.6220 0.5022 0.7337 -0.0636 -0.0008 0.0795  353 LYS A O   
10717 C CB  . LYS D 337 ? 0.6523 0.4931 0.7615 -0.0725 -0.0030 0.0759  353 LYS A CB  
10718 C CG  . LYS D 337 ? 0.7263 0.5486 0.8355 -0.0764 -0.0029 0.0703  353 LYS A CG  
10719 C CD  . LYS D 337 ? 0.7844 0.5836 0.8837 -0.0850 -0.0079 0.0799  353 LYS A CD  
10720 C CE  . LYS D 337 ? 0.8090 0.6103 0.9159 -0.0901 -0.0083 0.0857  353 LYS A CE  
10721 N NZ  . LYS D 337 ? 0.8529 0.6449 0.9392 -0.0923 -0.0084 0.0843  353 LYS A NZ  
10722 N N   . GLY D 338 ? 0.6114 0.5136 0.7416 -0.0541 0.0083  0.0604  354 GLY A N   
10723 C CA  . GLY D 338 ? 0.5875 0.5104 0.7190 -0.0504 0.0100  0.0626  354 GLY A CA  
10724 C C   . GLY D 338 ? 0.6230 0.5494 0.7461 -0.0457 0.0098  0.0579  354 GLY A C   
10725 O O   . GLY D 338 ? 0.6681 0.6107 0.7906 -0.0436 0.0105  0.0603  354 GLY A O   
10726 N N   . ASP D 339 ? 0.6554 0.5676 0.7722 -0.0441 0.0088  0.0512  355 ASP A N   
10727 C CA  . ASP D 339 ? 0.7123 0.6245 0.8202 -0.0401 0.0072  0.0479  355 ASP A CA  
10728 C C   . ASP D 339 ? 0.7441 0.6672 0.8580 -0.0330 0.0123  0.0339  355 ASP A C   
10729 O O   . ASP D 339 ? 0.7154 0.6317 0.8328 -0.0318 0.0146  0.0248  355 ASP A O   
10730 C CB  . ASP D 339 ? 0.7518 0.6412 0.8488 -0.0429 0.0024  0.0500  355 ASP A CB  
10731 C CG  . ASP D 339 ? 0.8232 0.7107 0.9108 -0.0386 -0.0004 0.0472  355 ASP A CG  
10732 O OD1 . ASP D 339 ? 0.8335 0.7369 0.9232 -0.0334 0.0017  0.0424  355 ASP A OD1 
10733 O OD2 . ASP D 339 ? 0.7801 0.6492 0.8581 -0.0403 -0.0046 0.0492  355 ASP A OD2 
10734 N N   . PHE D 340 ? 0.6885 0.6285 0.8028 -0.0289 0.0139  0.0324  356 PHE A N   
10735 C CA  . PHE D 340 ? 0.6284 0.5783 0.7462 -0.0225 0.0181  0.0203  356 PHE A CA  
10736 C C   . PHE D 340 ? 0.6297 0.5819 0.7389 -0.0194 0.0153  0.0199  356 PHE A C   
10737 O O   . PHE D 340 ? 0.6221 0.5767 0.7247 -0.0217 0.0115  0.0289  356 PHE A O   
10738 C CB  . PHE D 340 ? 0.6063 0.5752 0.7336 -0.0200 0.0234  0.0172  356 PHE A CB  
10739 C CG  . PHE D 340 ? 0.5821 0.5507 0.7185 -0.0226 0.0254  0.0186  356 PHE A CG  
10740 C CD1 . PHE D 340 ? 0.6829 0.6476 0.8256 -0.0210 0.0283  0.0092  356 PHE A CD1 
10741 C CD2 . PHE D 340 ? 0.5644 0.5370 0.7032 -0.0268 0.0241  0.0292  356 PHE A CD2 
10742 C CE1 . PHE D 340 ? 0.6498 0.6140 0.8013 -0.0232 0.0296  0.0101  356 PHE A CE1 
10743 C CE2 . PHE D 340 ? 0.6217 0.5945 0.7699 -0.0288 0.0256  0.0302  356 PHE A CE2 
10744 C CZ  . PHE D 340 ? 0.6210 0.5892 0.7758 -0.0269 0.0282  0.0205  356 PHE A CZ  
10745 N N   . ARG D 341 ? 0.5896 0.5412 0.6986 -0.0146 0.0168  0.0093  357 ARG A N   
10746 C CA  . ARG D 341 ? 0.5685 0.5193 0.6697 -0.0113 0.0135  0.0077  357 ARG A CA  
10747 C C   . ARG D 341 ? 0.5925 0.5516 0.6978 -0.0055 0.0175  -0.0047 357 ARG A C   
10748 O O   . ARG D 341 ? 0.5987 0.5571 0.7102 -0.0046 0.0215  -0.0126 357 ARG A O   
10749 C CB  . ARG D 341 ? 0.6324 0.5639 0.7253 -0.0126 0.0080  0.0101  357 ARG A CB  
10750 C CG  . ARG D 341 ? 0.6857 0.6056 0.7719 -0.0188 0.0029  0.0231  357 ARG A CG  
10751 C CD  . ARG D 341 ? 0.6930 0.5922 0.7703 -0.0196 -0.0021 0.0244  357 ARG A CD  
10752 N NE  . ARG D 341 ? 0.6699 0.5552 0.7414 -0.0262 -0.0061 0.0356  357 ARG A NE  
10753 C CZ  . ARG D 341 ? 0.7101 0.5768 0.7712 -0.0278 -0.0116 0.0396  357 ARG A CZ  
10754 N NH1 . ARG D 341 ? 0.7636 0.6234 0.8208 -0.0229 -0.0132 0.0323  357 ARG A NH1 
10755 N NH2 . ARG D 341 ? 0.7519 0.6068 0.8062 -0.0343 -0.0157 0.0513  357 ARG A NH2 
10756 N N   . ILE D 342 ? 0.6092 0.5756 0.7103 -0.0022 0.0158  -0.0062 358 ILE A N   
10757 C CA  . ILE D 342 ? 0.5666 0.5394 0.6700 0.0031  0.0185  -0.0171 358 ILE A CA  
10758 C C   . ILE D 342 ? 0.6308 0.5956 0.7268 0.0055  0.0129  -0.0175 358 ILE A C   
10759 O O   . ILE D 342 ? 0.6513 0.6142 0.7401 0.0042  0.0075  -0.0096 358 ILE A O   
10760 C CB  . ILE D 342 ? 0.5649 0.5559 0.6710 0.0052  0.0222  -0.0194 358 ILE A CB  
10761 C CG1 . ILE D 342 ? 0.5910 0.5905 0.7057 0.0049  0.0286  -0.0231 358 ILE A CG1 
10762 C CG2 . ILE D 342 ? 0.6331 0.6281 0.7384 0.0099  0.0227  -0.0283 358 ILE A CG2 
10763 C CD1 . ILE D 342 ? 0.5029 0.5201 0.6196 0.0071  0.0327  -0.0257 358 ILE A CD1 
10764 N N   . LEU D 343 ? 0.6673 0.6273 0.7649 0.0088  0.0137  -0.0265 359 LEU A N   
10765 C CA  . LEU D 343 ? 0.6048 0.5578 0.6971 0.0123  0.0087  -0.0287 359 LEU A CA  
10766 C C   . LEU D 343 ? 0.6622 0.6281 0.7576 0.0170  0.0110  -0.0372 359 LEU A C   
10767 O O   . LEU D 343 ? 0.6806 0.6514 0.7818 0.0185  0.0161  -0.0461 359 LEU A O   
10768 C CB  . LEU D 343 ? 0.5620 0.5010 0.6545 0.0123  0.0083  -0.0331 359 LEU A CB  
10769 C CG  . LEU D 343 ? 0.6140 0.5417 0.7007 0.0154  0.0027  -0.0339 359 LEU A CG  
10770 C CD1 . LEU D 343 ? 0.6350 0.5515 0.7236 0.0147  0.0047  -0.0400 359 LEU A CD1 
10771 C CD2 . LEU D 343 ? 0.7260 0.6619 0.8124 0.0213  0.0004  -0.0393 359 LEU A CD2 
10772 N N   . MET D 344 ? 0.6188 0.5900 0.7096 0.0187  0.0070  -0.0341 360 MET A N   
10773 C CA  . MET D 344 ? 0.6281 0.6114 0.7211 0.0225  0.0089  -0.0412 360 MET A CA  
10774 C C   . MET D 344 ? 0.6818 0.6639 0.7681 0.0242  0.0017  -0.0374 360 MET A C   
10775 O O   . MET D 344 ? 0.6470 0.6275 0.7272 0.0208  -0.0024 -0.0282 360 MET A O   
10776 C CB  . MET D 344 ? 0.6118 0.6094 0.7081 0.0209  0.0145  -0.0413 360 MET A CB  
10777 C CG  . MET D 344 ? 0.7084 0.7172 0.8069 0.0244  0.0174  -0.0495 360 MET A CG  
10778 S SD  . MET D 344 ? 0.8259 0.8509 0.9273 0.0230  0.0242  -0.0504 360 MET A SD  
10779 C CE  . MET D 344 ? 0.6016 0.6227 0.7074 0.0193  0.0277  -0.0462 360 MET A CE  
10780 N N   . CYS D 345 ? 0.7389 0.7215 0.8261 0.0290  -0.0003 -0.0444 361 CYS A N   
10781 C CA  . CYS D 345 ? 0.6986 0.6790 0.7799 0.0312  -0.0081 -0.0418 361 CYS A CA  
10782 C C   . CYS D 345 ? 0.7071 0.7014 0.7879 0.0308  -0.0070 -0.0423 361 CYS A C   
10783 O O   . CYS D 345 ? 0.7744 0.7748 0.8576 0.0344  -0.0068 -0.0489 361 CYS A O   
10784 C CB  . CYS D 345 ? 0.7312 0.7056 0.8145 0.0368  -0.0111 -0.0490 361 CYS A CB  
10785 S SG  . CYS D 345 ? 0.7571 0.7153 0.8403 0.0367  -0.0117 -0.0489 361 CYS A SG  
10786 N N   . THR D 346 ? 0.6987 0.6980 0.7762 0.0260  -0.0061 -0.0351 362 THR A N   
10787 C CA  . THR D 346 ? 0.6423 0.6560 0.7202 0.0246  -0.0022 -0.0361 362 THR A CA  
10788 C C   . THR D 346 ? 0.6733 0.6889 0.7455 0.0253  -0.0087 -0.0351 362 THR A C   
10789 O O   . THR D 346 ? 0.7011 0.7093 0.7657 0.0234  -0.0167 -0.0279 362 THR A O   
10790 C CB  . THR D 346 ? 0.6288 0.6477 0.7050 0.0191  0.0005  -0.0286 362 THR A CB  
10791 O OG1 . THR D 346 ? 0.6664 0.6813 0.7479 0.0184  0.0051  -0.0288 362 THR A OG1 
10792 C CG2 . THR D 346 ? 0.6603 0.6944 0.7380 0.0180  0.0061  -0.0312 362 THR A CG2 
10793 N N   . LYS D 347 ? 0.6274 0.6519 0.7026 0.0279  -0.0059 -0.0421 363 LYS A N   
10794 C CA  . LYS D 347 ? 0.5905 0.6198 0.6607 0.0274  -0.0106 -0.0413 363 LYS A CA  
10795 C C   . LYS D 347 ? 0.6031 0.6441 0.6704 0.0223  -0.0062 -0.0381 363 LYS A C   
10796 O O   . LYS D 347 ? 0.6566 0.7029 0.7273 0.0206  0.0010  -0.0380 363 LYS A O   
10797 C CB  . LYS D 347 ? 0.6629 0.6958 0.7380 0.0324  -0.0096 -0.0505 363 LYS A CB  
10798 C CG  . LYS D 347 ? 0.6960 0.7199 0.7757 0.0378  -0.0123 -0.0554 363 LYS A CG  
10799 C CD  . LYS D 347 ? 0.6737 0.6848 0.7477 0.0383  -0.0220 -0.0492 363 LYS A CD  
10800 C CE  . LYS D 347 ? 0.7558 0.7577 0.8343 0.0435  -0.0236 -0.0542 363 LYS A CE  
10801 N NZ  . LYS D 347 ? 0.8378 0.8258 0.9098 0.0442  -0.0331 -0.0480 363 LYS A NZ  
10802 N N   . VAL D 348 ? 0.5625 0.6075 0.6234 0.0197  -0.0105 -0.0355 364 VAL A N   
10803 C CA  . VAL D 348 ? 0.5890 0.6459 0.6468 0.0147  -0.0058 -0.0333 364 VAL A CA  
10804 C C   . VAL D 348 ? 0.6250 0.6905 0.6857 0.0170  -0.0008 -0.0414 364 VAL A C   
10805 O O   . VAL D 348 ? 0.7258 0.7940 0.7817 0.0155  -0.0043 -0.0414 364 VAL A O   
10806 C CB  . VAL D 348 ? 0.5825 0.6384 0.6299 0.0087  -0.0133 -0.0248 364 VAL A CB  
10807 C CG1 . VAL D 348 ? 0.6303 0.6994 0.6747 0.0031  -0.0076 -0.0230 364 VAL A CG1 
10808 C CG2 . VAL D 348 ? 0.5692 0.6160 0.6134 0.0064  -0.0179 -0.0170 364 VAL A CG2 
10809 N N   . THR D 349 ? 0.5818 0.6512 0.6498 0.0201  0.0074  -0.0479 365 THR A N   
10810 C CA  . THR D 349 ? 0.5846 0.6620 0.6548 0.0220  0.0130  -0.0556 365 THR A CA  
10811 C C   . THR D 349 ? 0.5914 0.6768 0.6646 0.0209  0.0224  -0.0575 365 THR A C   
10812 O O   . THR D 349 ? 0.6263 0.7108 0.7016 0.0195  0.0244  -0.0536 365 THR A O   
10813 C CB  . THR D 349 ? 0.6126 0.6855 0.6886 0.0276  0.0127  -0.0631 365 THR A CB  
10814 O OG1 . THR D 349 ? 0.6990 0.7698 0.7812 0.0294  0.0181  -0.0662 365 THR A OG1 
10815 C CG2 . THR D 349 ? 0.6697 0.7325 0.7449 0.0296  0.0035  -0.0605 365 THR A CG2 
10816 N N   . MET D 350 ? 0.5618 0.6550 0.6349 0.0215  0.0280  -0.0633 366 MET A N   
10817 C CA  . MET D 350 ? 0.5547 0.6542 0.6311 0.0218  0.0366  -0.0665 366 MET A CA  
10818 C C   . MET D 350 ? 0.6432 0.7372 0.7269 0.0256  0.0392  -0.0716 366 MET A C   
10819 O O   . MET D 350 ? 0.6528 0.7482 0.7404 0.0256  0.0442  -0.0720 366 MET A O   
10820 C CB  . MET D 350 ? 0.5211 0.6288 0.5939 0.0213  0.0412  -0.0713 366 MET A CB  
10821 C CG  . MET D 350 ? 0.4986 0.6125 0.5741 0.0223  0.0498  -0.0757 366 MET A CG  
10822 S SD  . MET D 350 ? 0.5253 0.6466 0.5943 0.0216  0.0543  -0.0811 366 MET A SD  
10823 C CE  . MET D 350 ? 0.6188 0.7462 0.6907 0.0236  0.0641  -0.0864 366 MET A CE  
10824 N N   . ASP D 351 ? 0.7402 0.8281 0.8257 0.0286  0.0359  -0.0757 367 ASP A N   
10825 C CA  . ASP D 351 ? 0.7409 0.8230 0.8325 0.0312  0.0378  -0.0804 367 ASP A CA  
10826 C C   . ASP D 351 ? 0.7241 0.7994 0.8185 0.0300  0.0363  -0.0747 367 ASP A C   
10827 O O   . ASP D 351 ? 0.7389 0.8122 0.8376 0.0300  0.0403  -0.0764 367 ASP A O   
10828 C CB  . ASP D 351 ? 0.8931 0.9709 0.9859 0.0341  0.0339  -0.0851 367 ASP A CB  
10829 C CG  . ASP D 351 ? 0.9271 1.0107 1.0191 0.0354  0.0372  -0.0927 367 ASP A CG  
10830 O OD1 . ASP D 351 ? 1.0133 1.1023 1.1039 0.0344  0.0430  -0.0949 367 ASP A OD1 
10831 O OD2 . ASP D 351 ? 1.0071 1.0902 1.0994 0.0374  0.0338  -0.0962 367 ASP A OD2 
10832 N N   . ASP D 352 ? 0.5637 0.6344 0.6549 0.0285  0.0300  -0.0676 368 ASP A N   
10833 C CA  . ASP D 352 ? 0.6131 0.6766 0.7059 0.0269  0.0284  -0.0617 368 ASP A CA  
10834 C C   . ASP D 352 ? 0.6134 0.6835 0.7060 0.0234  0.0322  -0.0566 368 ASP A C   
10835 O O   . ASP D 352 ? 0.5983 0.6649 0.6946 0.0224  0.0341  -0.0542 368 ASP A O   
10836 C CB  . ASP D 352 ? 0.6116 0.6664 0.7001 0.0266  0.0198  -0.0560 368 ASP A CB  
10837 C CG  . ASP D 352 ? 0.7141 0.7607 0.8054 0.0306  0.0169  -0.0613 368 ASP A CG  
10838 O OD1 . ASP D 352 ? 0.7247 0.7745 0.8203 0.0329  0.0214  -0.0695 368 ASP A OD1 
10839 O OD2 . ASP D 352 ? 0.6828 0.7198 0.7717 0.0313  0.0102  -0.0576 368 ASP A OD2 
10840 N N   . PHE D 353 ? 0.6111 0.6911 0.6997 0.0214  0.0338  -0.0551 369 PHE A N   
10841 C CA  . PHE D 353 ? 0.5432 0.6320 0.6326 0.0186  0.0387  -0.0516 369 PHE A CA  
10842 C C   . PHE D 353 ? 0.5437 0.6350 0.6400 0.0210  0.0459  -0.0576 369 PHE A C   
10843 O O   . PHE D 353 ? 0.5622 0.6557 0.6625 0.0196  0.0486  -0.0544 369 PHE A O   
10844 C CB  . PHE D 353 ? 0.5523 0.6519 0.6359 0.0161  0.0400  -0.0509 369 PHE A CB  
10845 C CG  . PHE D 353 ? 0.5469 0.6583 0.6320 0.0140  0.0467  -0.0498 369 PHE A CG  
10846 C CD1 . PHE D 353 ? 0.5224 0.6380 0.6056 0.0093  0.0454  -0.0414 369 PHE A CD1 
10847 C CD2 . PHE D 353 ? 0.5414 0.6599 0.6292 0.0165  0.0541  -0.0572 369 PHE A CD2 
10848 C CE1 . PHE D 353 ? 0.5181 0.6464 0.6035 0.0076  0.0519  -0.0408 369 PHE A CE1 
10849 C CE2 . PHE D 353 ? 0.5257 0.6556 0.6153 0.0153  0.0605  -0.0568 369 PHE A CE2 
10850 C CZ  . PHE D 353 ? 0.4795 0.6151 0.5686 0.0109  0.0596  -0.0487 369 PHE A CZ  
10851 N N   . LEU D 354 ? 0.5171 0.6077 0.6150 0.0243  0.0484  -0.0662 370 LEU A N   
10852 C CA  . LEU D 354 ? 0.4922 0.5834 0.5955 0.0262  0.0542  -0.0719 370 LEU A CA  
10853 C C   . LEU D 354 ? 0.5350 0.6152 0.6433 0.0266  0.0524  -0.0720 370 LEU A C   
10854 O O   . LEU D 354 ? 0.6011 0.6805 0.7143 0.0263  0.0555  -0.0721 370 LEU A O   
10855 C CB  . LEU D 354 ? 0.5635 0.6576 0.6652 0.0288  0.0574  -0.0809 370 LEU A CB  
10856 C CG  . LEU D 354 ? 0.5436 0.6477 0.6400 0.0285  0.0603  -0.0826 370 LEU A CG  
10857 C CD1 . LEU D 354 ? 0.4850 0.5888 0.5804 0.0311  0.0634  -0.0915 370 LEU A CD1 
10858 C CD2 . LEU D 354 ? 0.5244 0.6381 0.6210 0.0270  0.0650  -0.0796 370 LEU A CD2 
10859 N N   . THR D 355 ? 0.5250 0.5964 0.6320 0.0272  0.0474  -0.0722 371 THR A N   
10860 C CA  . THR D 355 ? 0.5496 0.6101 0.6604 0.0268  0.0457  -0.0717 371 THR A CA  
10861 C C   . THR D 355 ? 0.5805 0.6382 0.6927 0.0237  0.0445  -0.0628 371 THR A C   
10862 O O   . THR D 355 ? 0.5783 0.6294 0.6947 0.0227  0.0454  -0.0625 371 THR A O   
10863 C CB  . THR D 355 ? 0.5572 0.6097 0.6661 0.0282  0.0406  -0.0733 371 THR A CB  
10864 O OG1 . THR D 355 ? 0.5818 0.6379 0.6906 0.0307  0.0426  -0.0820 371 THR A OG1 
10865 C CG2 . THR D 355 ? 0.5685 0.6088 0.6801 0.0273  0.0386  -0.0726 371 THR A CG2 
10866 N N   . ALA D 356 ? 0.5525 0.6153 0.6610 0.0216  0.0424  -0.0554 372 ALA A N   
10867 C CA  . ALA D 356 ? 0.4782 0.5395 0.5878 0.0182  0.0413  -0.0468 372 ALA A CA  
10868 C C   . ALA D 356 ? 0.5174 0.5851 0.6336 0.0181  0.0475  -0.0484 372 ALA A C   
10869 O O   . ALA D 356 ? 0.5987 0.6602 0.7192 0.0166  0.0474  -0.0457 372 ALA A O   
10870 C CB  . ALA D 356 ? 0.4807 0.5473 0.5842 0.0151  0.0378  -0.0386 372 ALA A CB  
10871 N N   . HIS D 357 ? 0.4892 0.5685 0.6061 0.0198  0.0525  -0.0531 373 HIS A N   
10872 C CA  . HIS D 357 ? 0.4856 0.5707 0.6090 0.0206  0.0581  -0.0556 373 HIS A CA  
10873 C C   . HIS D 357 ? 0.4914 0.5665 0.6196 0.0222  0.0589  -0.0615 373 HIS A C   
10874 O O   . HIS D 357 ? 0.5305 0.6039 0.6646 0.0214  0.0603  -0.0600 373 HIS A O   
10875 C CB  . HIS D 357 ? 0.4746 0.5727 0.5969 0.0227  0.0634  -0.0606 373 HIS A CB  
10876 C CG  . HIS D 357 ? 0.4751 0.5845 0.5933 0.0201  0.0637  -0.0547 373 HIS A CG  
10877 N ND1 . HIS D 357 ? 0.4709 0.5797 0.5817 0.0180  0.0591  -0.0511 373 HIS A ND1 
10878 C CD2 . HIS D 357 ? 0.5421 0.6645 0.6626 0.0192  0.0681  -0.0528 373 HIS A CD2 
10879 C CE1 . HIS D 357 ? 0.5388 0.6588 0.6464 0.0150  0.0604  -0.0467 373 HIS A CE1 
10880 N NE2 . HIS D 357 ? 0.5209 0.6500 0.6345 0.0157  0.0662  -0.0476 373 HIS A NE2 
10881 N N   . HIS D 358 ? 0.5262 0.5947 0.6519 0.0239  0.0577  -0.0682 374 HIS A N   
10882 C CA  . HIS D 358 ? 0.5297 0.5881 0.6589 0.0240  0.0578  -0.0735 374 HIS A CA  
10883 C C   . HIS D 358 ? 0.5160 0.5629 0.6475 0.0208  0.0542  -0.0673 374 HIS A C   
10884 O O   . HIS D 358 ? 0.4711 0.5134 0.6076 0.0194  0.0552  -0.0671 374 HIS A O   
10885 C CB  . HIS D 358 ? 0.4919 0.5465 0.6173 0.0258  0.0568  -0.0813 374 HIS A CB  
10886 C CG  . HIS D 358 ? 0.5149 0.5595 0.6424 0.0250  0.0567  -0.0874 374 HIS A CG  
10887 N ND1 . HIS D 358 ? 0.5356 0.5817 0.6624 0.0264  0.0594  -0.0961 374 HIS A ND1 
10888 C CD2 . HIS D 358 ? 0.5021 0.5348 0.6308 0.0225  0.0538  -0.0864 374 HIS A CD2 
10889 C CE1 . HIS D 358 ? 0.5153 0.5512 0.6430 0.0243  0.0581  -0.1000 374 HIS A CE1 
10890 N NE2 . HIS D 358 ? 0.4704 0.4982 0.5995 0.0220  0.0549  -0.0945 374 HIS A NE2 
10891 N N   . GLU D 359 ? 0.5211 0.5621 0.6486 0.0196  0.0496  -0.0626 375 GLU A N   
10892 C CA  . GLU D 359 ? 0.4784 0.5066 0.6064 0.0165  0.0460  -0.0573 375 GLU A CA  
10893 C C   . GLU D 359 ? 0.5410 0.5711 0.6721 0.0134  0.0460  -0.0483 375 GLU A C   
10894 O O   . GLU D 359 ? 0.6051 0.6263 0.7396 0.0107  0.0452  -0.0458 375 GLU A O   
10895 C CB  . GLU D 359 ? 0.4542 0.4760 0.5763 0.0167  0.0409  -0.0549 375 GLU A CB  
10896 C CG  . GLU D 359 ? 0.4457 0.4647 0.5666 0.0194  0.0408  -0.0642 375 GLU A CG  
10897 C CD  . GLU D 359 ? 0.5697 0.5804 0.6940 0.0181  0.0426  -0.0703 375 GLU A CD  
10898 O OE1 . GLU D 359 ? 0.6511 0.6516 0.7767 0.0148  0.0409  -0.0657 375 GLU A OE1 
10899 O OE2 . GLU D 359 ? 0.5803 0.5942 0.7056 0.0197  0.0453  -0.0792 375 GLU A OE2 
10900 N N   . MET D 360 ? 0.5500 0.5923 0.6800 0.0134  0.0470  -0.0435 376 MET A N   
10901 C CA  . MET D 360 ? 0.5069 0.5543 0.6407 0.0106  0.0478  -0.0356 376 MET A CA  
10902 C C   . MET D 360 ? 0.4702 0.5215 0.6124 0.0118  0.0525  -0.0398 376 MET A C   
10903 O O   . MET D 360 ? 0.5161 0.5662 0.6632 0.0093  0.0522  -0.0341 376 MET A O   
10904 C CB  . MET D 360 ? 0.4611 0.5226 0.5920 0.0100  0.0485  -0.0305 376 MET A CB  
10905 C CG  . MET D 360 ? 0.4696 0.5367 0.6038 0.0062  0.0485  -0.0212 376 MET A CG  
10906 S SD  . MET D 360 ? 0.4934 0.5755 0.6221 0.0029  0.0478  -0.0127 376 MET A SD  
10907 C CE  . MET D 360 ? 0.5667 0.6348 0.6843 0.0000  0.0391  -0.0063 376 MET A CE  
10908 N N   . GLY D 361 ? 0.4880 0.5437 0.6316 0.0156  0.0563  -0.0495 377 GLY A N   
10909 C CA  . GLY D 361 ? 0.4671 0.5233 0.6179 0.0168  0.0595  -0.0542 377 GLY A CA  
10910 C C   . GLY D 361 ? 0.4597 0.5001 0.6126 0.0141  0.0566  -0.0546 377 GLY A C   
10911 O O   . GLY D 361 ? 0.4942 0.5321 0.6534 0.0128  0.0570  -0.0530 377 GLY A O   
10912 N N   . HIS D 362 ? 0.5055 0.5350 0.6533 0.0130  0.0536  -0.0568 378 HIS A N   
10913 C CA  . HIS D 362 ? 0.5138 0.5275 0.6624 0.0093  0.0507  -0.0562 378 HIS A CA  
10914 C C   . HIS D 362 ? 0.5262 0.5361 0.6774 0.0053  0.0482  -0.0453 378 HIS A C   
10915 O O   . HIS D 362 ? 0.5693 0.5726 0.7255 0.0026  0.0477  -0.0439 378 HIS A O   
10916 C CB  . HIS D 362 ? 0.5712 0.5751 0.7136 0.0087  0.0478  -0.0593 378 HIS A CB  
10917 C CG  . HIS D 362 ? 0.5607 0.5650 0.7012 0.0111  0.0496  -0.0704 378 HIS A CG  
10918 N ND1 . HIS D 362 ? 0.5393 0.5429 0.6827 0.0113  0.0518  -0.0776 378 HIS A ND1 
10919 C CD2 . HIS D 362 ? 0.5573 0.5629 0.6932 0.0133  0.0491  -0.0754 378 HIS A CD2 
10920 C CE1 . HIS D 362 ? 0.5505 0.5549 0.6902 0.0129  0.0527  -0.0862 378 HIS A CE1 
10921 N NE2 . HIS D 362 ? 0.5823 0.5886 0.7180 0.0143  0.0513  -0.0850 378 HIS A NE2 
10922 N N   . ILE D 363 ? 0.5311 0.5450 0.6783 0.0045  0.0462  -0.0373 379 ILE A N   
10923 C CA  . ILE D 363 ? 0.5912 0.6020 0.7395 0.0001  0.0435  -0.0260 379 ILE A CA  
10924 C C   . ILE D 363 ? 0.5585 0.5800 0.7153 0.0002  0.0466  -0.0236 379 ILE A C   
10925 O O   . ILE D 363 ? 0.5945 0.6113 0.7552 -0.0036 0.0448  -0.0165 379 ILE A O   
10926 C CB  . ILE D 363 ? 0.5642 0.5778 0.7052 -0.0011 0.0403  -0.0180 379 ILE A CB  
10927 C CG1 . ILE D 363 ? 0.6397 0.6408 0.7729 -0.0010 0.0364  -0.0197 379 ILE A CG1 
10928 C CG2 . ILE D 363 ? 0.5052 0.5187 0.6470 -0.0057 0.0380  -0.0063 379 ILE A CG2 
10929 C CD1 . ILE D 363 ? 0.6461 0.6294 0.7773 -0.0052 0.0326  -0.0156 379 ILE A CD1 
10930 N N   . GLN D 364 ? 0.5541 0.5903 0.7139 0.0046  0.0511  -0.0293 380 GLN A N   
10931 C CA  . GLN D 364 ? 0.4862 0.5342 0.6547 0.0056  0.0545  -0.0280 380 GLN A CA  
10932 C C   . GLN D 364 ? 0.5421 0.5811 0.7177 0.0052  0.0544  -0.0318 380 GLN A C   
10933 O O   . GLN D 364 ? 0.6124 0.6524 0.7951 0.0032  0.0538  -0.0262 380 GLN A O   
10934 C CB  . GLN D 364 ? 0.4636 0.5278 0.6323 0.0107  0.0595  -0.0345 380 GLN A CB  
10935 C CG  . GLN D 364 ? 0.4483 0.5296 0.6228 0.0114  0.0629  -0.0303 380 GLN A CG  
10936 C CD  . GLN D 364 ? 0.4517 0.5381 0.6215 0.0072  0.0605  -0.0198 380 GLN A CD  
10937 O OE1 . GLN D 364 ? 0.5256 0.6179 0.7001 0.0044  0.0601  -0.0119 380 GLN A OE1 
10938 N NE2 . GLN D 364 ? 0.4676 0.5501 0.6279 0.0063  0.0579  -0.0192 380 GLN A NE2 
10939 N N   . TYR D 365 ? 0.5711 0.6009 0.7444 0.0067  0.0543  -0.0410 381 TYR A N   
10940 C CA  . TYR D 365 ? 0.6036 0.6214 0.7814 0.0049  0.0528  -0.0447 381 TYR A CA  
10941 C C   . TYR D 365 ? 0.6043 0.6080 0.7820 -0.0015 0.0482  -0.0359 381 TYR A C   
10942 O O   . TYR D 365 ? 0.6532 0.6534 0.8378 -0.0040 0.0470  -0.0322 381 TYR A O   
10943 C CB  . TYR D 365 ? 0.6269 0.6361 0.7994 0.0059  0.0528  -0.0553 381 TYR A CB  
10944 C CG  . TYR D 365 ? 0.5982 0.5997 0.7742 0.0057  0.0524  -0.0629 381 TYR A CG  
10945 C CD1 . TYR D 365 ? 0.5907 0.5897 0.7747 0.0042  0.0512  -0.0599 381 TYR A CD1 
10946 C CD2 . TYR D 365 ? 0.5682 0.5651 0.7389 0.0068  0.0528  -0.0730 381 TYR A CD2 
10947 C CE1 . TYR D 365 ? 0.6290 0.6200 0.8155 0.0040  0.0499  -0.0672 381 TYR A CE1 
10948 C CE2 . TYR D 365 ? 0.5680 0.5573 0.7404 0.0061  0.0517  -0.0802 381 TYR A CE2 
10949 C CZ  . TYR D 365 ? 0.5873 0.5730 0.7673 0.0047  0.0500  -0.0774 381 TYR A CZ  
10950 O OH  . TYR D 365 ? 0.5287 0.5054 0.7097 0.0037  0.0479  -0.0844 381 TYR A OH  
10951 N N   . ASP D 366 ? 0.6806 0.6759 0.8503 -0.0043 0.0455  -0.0322 382 ASP A N   
10952 C CA  . ASP D 366 ? 0.7314 0.7112 0.8992 -0.0106 0.0410  -0.0243 382 ASP A CA  
10953 C C   . ASP D 366 ? 0.7163 0.7006 0.8898 -0.0134 0.0399  -0.0134 382 ASP A C   
10954 O O   . ASP D 366 ? 0.7012 0.6760 0.8792 -0.0176 0.0377  -0.0100 382 ASP A O   
10955 C CB  . ASP D 366 ? 0.7375 0.7098 0.8955 -0.0119 0.0383  -0.0216 382 ASP A CB  
10956 C CG  . ASP D 366 ? 0.7708 0.7371 0.9240 -0.0099 0.0389  -0.0320 382 ASP A CG  
10957 O OD1 . ASP D 366 ? 0.8441 0.8066 1.0002 -0.0100 0.0402  -0.0400 382 ASP A OD1 
10958 O OD2 . ASP D 366 ? 0.7936 0.7587 0.9399 -0.0086 0.0377  -0.0323 382 ASP A OD2 
10959 N N   . MET D 367 ? 0.6575 0.6562 0.8304 -0.0119 0.0411  -0.0075 383 MET A N   
10960 C CA  . MET D 367 ? 0.5807 0.5877 0.7594 -0.0143 0.0407  0.0023  383 MET A CA  
10961 C C   . MET D 367 ? 0.5878 0.6018 0.7785 -0.0121 0.0433  -0.0011 383 MET A C   
10962 O O   . MET D 367 ? 0.5978 0.6134 0.7952 -0.0152 0.0419  0.0066  383 MET A O   
10963 C CB  . MET D 367 ? 0.5680 0.5920 0.7438 -0.0125 0.0425  0.0065  383 MET A CB  
10964 C CG  . MET D 367 ? 0.5083 0.5251 0.6725 -0.0153 0.0385  0.0122  383 MET A CG  
10965 S SD  . MET D 367 ? 0.4534 0.4895 0.6127 -0.0132 0.0403  0.0145  383 MET A SD  
10966 C CE  . MET D 367 ? 0.4846 0.5372 0.6502 -0.0166 0.0412  0.0252  383 MET A CE  
10967 N N   . ALA D 368 ? 0.5965 0.6151 0.7902 -0.0068 0.0468  -0.0125 384 ALA A N   
10968 C CA  . ALA D 368 ? 0.6216 0.6480 0.8265 -0.0038 0.0490  -0.0159 384 ALA A CA  
10969 C C   . ALA D 368 ? 0.6051 0.6153 0.8148 -0.0080 0.0451  -0.0151 384 ALA A C   
10970 O O   . ALA D 368 ? 0.5738 0.5883 0.7934 -0.0082 0.0447  -0.0116 384 ALA A O   
10971 C CB  . ALA D 368 ? 0.6643 0.6990 0.8696 0.0030  0.0534  -0.0282 384 ALA A CB  
10972 N N   . TYR D 369 ? 0.6190 0.7481 0.7506 0.0423  -0.0098 0.0250  385 TYR A N   
10973 C CA  . TYR D 369 ? 0.6077 0.7248 0.7246 0.0379  -0.0196 0.0248  385 TYR A CA  
10974 C C   . TYR D 369 ? 0.6078 0.7451 0.7470 0.0326  -0.0266 0.0227  385 TYR A C   
10975 O O   . TYR D 369 ? 0.6640 0.7938 0.7889 0.0244  -0.0342 0.0202  385 TYR A O   
10976 C CB  . TYR D 369 ? 0.6417 0.7366 0.7208 0.0257  -0.0205 0.0201  385 TYR A CB  
10977 C CG  . TYR D 369 ? 0.6538 0.7565 0.7277 0.0109  -0.0173 0.0127  385 TYR A CG  
10978 C CD1 . TYR D 369 ? 0.6474 0.7695 0.7381 0.0023  -0.0211 0.0089  385 TYR A CD1 
10979 C CD2 . TYR D 369 ? 0.6597 0.7498 0.7116 0.0055  -0.0108 0.0093  385 TYR A CD2 
10980 C CE1 . TYR D 369 ? 0.6657 0.7947 0.7521 -0.0109 -0.0182 0.0024  385 TYR A CE1 
10981 C CE2 . TYR D 369 ? 0.6134 0.7104 0.6612 -0.0079 -0.0081 0.0025  385 TYR A CE2 
10982 C CZ  . TYR D 369 ? 0.6046 0.7211 0.6697 -0.0161 -0.0117 -0.0008 385 TYR A CZ  
10983 O OH  . TYR D 369 ? 0.5944 0.7186 0.6570 -0.0294 -0.0093 -0.0074 385 TYR A OH  
10984 N N   . ALA D 370 ? 0.6454 0.8081 0.8189 0.0368  -0.0240 0.0234  386 ALA A N   
10985 C CA  . ALA D 370 ? 0.6646 0.8461 0.8581 0.0308  -0.0307 0.0208  386 ALA A CA  
10986 C C   . ALA D 370 ? 0.6838 0.8662 0.8908 0.0395  -0.0398 0.0253  386 ALA A C   
10987 O O   . ALA D 370 ? 0.7108 0.9055 0.9309 0.0348  -0.0471 0.0231  386 ALA A O   
10988 C CB  . ALA D 370 ? 0.6717 0.8807 0.8967 0.0304  -0.0248 0.0191  386 ALA A CB  
10989 N N   . ALA D 371 ? 0.5899 0.7589 0.7932 0.0520  -0.0398 0.0314  387 ALA A N   
10990 C CA  . ALA D 371 ? 0.5508 0.7174 0.7627 0.0595  -0.0492 0.0354  387 ALA A CA  
10991 C C   . ALA D 371 ? 0.5526 0.6981 0.7329 0.0522  -0.0577 0.0333  387 ALA A C   
10992 O O   . ALA D 371 ? 0.5764 0.7246 0.7638 0.0529  -0.0674 0.0337  387 ALA A O   
10993 C CB  . ALA D 371 ? 0.6094 0.7687 0.8287 0.0755  -0.0464 0.0428  387 ALA A CB  
10994 N N   . GLN D 372 ? 0.5208 0.6450 0.6669 0.0460  -0.0543 0.0314  388 GLN A N   
10995 C CA  . GLN D 372 ? 0.5704 0.6742 0.6840 0.0370  -0.0607 0.0287  388 GLN A CA  
10996 C C   . GLN D 372 ? 0.6309 0.7472 0.7514 0.0268  -0.0681 0.0239  388 GLN A C   
10997 O O   . GLN D 372 ? 0.6314 0.7710 0.7762 0.0229  -0.0659 0.0210  388 GLN A O   
10998 C CB  . GLN D 372 ? 0.5737 0.6614 0.6567 0.0279  -0.0538 0.0251  388 GLN A CB  
10999 C CG  . GLN D 372 ? 0.5954 0.6670 0.6653 0.0364  -0.0470 0.0290  388 GLN A CG  
11000 C CD  . GLN D 372 ? 0.6549 0.7032 0.7049 0.0436  -0.0520 0.0336  388 GLN A CD  
11001 O OE1 . GLN D 372 ? 0.7000 0.7387 0.7368 0.0396  -0.0604 0.0329  388 GLN A OE1 
11002 N NE2 . GLN D 372 ? 0.6436 0.6803 0.6877 0.0537  -0.0464 0.0380  388 GLN A NE2 
11003 N N   . PRO D 373 ? 0.6005 0.7018 0.6998 0.0220  -0.0766 0.0228  389 PRO A N   
11004 C CA  . PRO D 373 ? 0.6123 0.7229 0.7128 0.0108  -0.0828 0.0176  389 PRO A CA  
11005 C C   . PRO D 373 ? 0.6318 0.7458 0.7215 -0.0033 -0.0763 0.0114  389 PRO A C   
11006 O O   . PRO D 373 ? 0.6642 0.7664 0.7355 -0.0064 -0.0685 0.0106  389 PRO A O   
11007 C CB  . PRO D 373 ? 0.6386 0.7265 0.7113 0.0094  -0.0917 0.0182  389 PRO A CB  
11008 C CG  . PRO D 373 ? 0.6209 0.6858 0.6723 0.0166  -0.0884 0.0226  389 PRO A CG  
11009 C CD  . PRO D 373 ? 0.5532 0.6293 0.6284 0.0279  -0.0815 0.0267  389 PRO A CD  
11010 N N   . PHE D 374 ? 0.6397 0.7696 0.7408 -0.0121 -0.0801 0.0069  390 PHE A N   
11011 C CA  . PHE D 374 ? 0.6002 0.7390 0.6986 -0.0255 -0.0744 0.0008  390 PHE A CA  
11012 C C   . PHE D 374 ? 0.6587 0.7736 0.7191 -0.0352 -0.0708 -0.0020 390 PHE A C   
11013 O O   . PHE D 374 ? 0.6795 0.7958 0.7346 -0.0419 -0.0626 -0.0052 390 PHE A O   
11014 C CB  . PHE D 374 ? 0.6128 0.7679 0.7246 -0.0331 -0.0811 -0.0033 390 PHE A CB  
11015 C CG  . PHE D 374 ? 0.5430 0.7076 0.6524 -0.0472 -0.0762 -0.0097 390 PHE A CG  
11016 C CD1 . PHE D 374 ? 0.6005 0.7481 0.6784 -0.0597 -0.0760 -0.0138 390 PHE A CD1 
11017 C CD2 . PHE D 374 ? 0.5931 0.7845 0.7332 -0.0484 -0.0725 -0.0117 390 PHE A CD2 
11018 C CE1 . PHE D 374 ? 0.5457 0.7025 0.6225 -0.0730 -0.0715 -0.0197 390 PHE A CE1 
11019 C CE2 . PHE D 374 ? 0.6111 0.8115 0.7492 -0.0618 -0.0683 -0.0178 390 PHE A CE2 
11020 C CZ  . PHE D 374 ? 0.5238 0.7070 0.6306 -0.0740 -0.0679 -0.0217 390 PHE A CZ  
11021 N N   . LEU D 375 ? 0.6803 0.7729 0.7140 -0.0362 -0.0769 -0.0010 391 LEU A N   
11022 C CA  . LEU D 375 ? 0.6757 0.7449 0.6732 -0.0460 -0.0736 -0.0037 391 LEU A CA  
11023 C C   . LEU D 375 ? 0.6335 0.6845 0.6148 -0.0396 -0.0675 -0.0004 391 LEU A C   
11024 O O   . LEU D 375 ? 0.6712 0.7021 0.6233 -0.0467 -0.0643 -0.0023 391 LEU A O   
11025 C CB  . LEU D 375 ? 0.6409 0.6925 0.6146 -0.0501 -0.0820 -0.0040 391 LEU A CB  
11026 C CG  . LEU D 375 ? 0.5981 0.6608 0.5780 -0.0579 -0.0888 -0.0078 391 LEU A CG  
11027 C CD1 . LEU D 375 ? 0.7240 0.7663 0.6808 -0.0569 -0.0975 -0.0061 391 LEU A CD1 
11028 C CD2 . LEU D 375 ? 0.5395 0.6060 0.5116 -0.0724 -0.0841 -0.0138 391 LEU A CD2 
11029 N N   . LEU D 376 ? 0.5986 0.6552 0.5976 -0.0263 -0.0657 0.0046  392 LEU A N   
11030 C CA  . LEU D 376 ? 0.6786 0.7195 0.6634 -0.0205 -0.0590 0.0074  392 LEU A CA  
11031 C C   . LEU D 376 ? 0.7573 0.8144 0.7621 -0.0175 -0.0500 0.0069  392 LEU A C   
11032 O O   . LEU D 376 ? 0.7894 0.8364 0.7873 -0.0105 -0.0442 0.0096  392 LEU A O   
11033 C CB  . LEU D 376 ? 0.6811 0.7089 0.6630 -0.0068 -0.0634 0.0140  392 LEU A CB  
11034 C CG  . LEU D 376 ? 0.6902 0.7000 0.6506 -0.0085 -0.0725 0.0149  392 LEU A CG  
11035 C CD1 . LEU D 376 ? 0.7163 0.7139 0.6753 0.0057  -0.0759 0.0216  392 LEU A CD1 
11036 C CD2 . LEU D 376 ? 0.7492 0.7371 0.6737 -0.0206 -0.0710 0.0111  392 LEU A CD2 
11037 N N   . ARG D 377 ? 0.6972 0.7784 0.7251 -0.0231 -0.0485 0.0033  393 ARG A N   
11038 C CA  . ARG D 377 ? 0.6564 0.7544 0.7043 -0.0205 -0.0400 0.0026  393 ARG A CA  
11039 C C   . ARG D 377 ? 0.7048 0.7955 0.7326 -0.0329 -0.0336 -0.0031 393 ARG A C   
11040 O O   . ARG D 377 ? 0.7325 0.8340 0.7633 -0.0447 -0.0333 -0.0086 393 ARG A O   
11041 C CB  . ARG D 377 ? 0.6040 0.7312 0.6875 -0.0197 -0.0419 0.0019  393 ARG A CB  
11042 C CG  . ARG D 377 ? 0.6221 0.7579 0.7289 -0.0069 -0.0478 0.0076  393 ARG A CG  
11043 C CD  . ARG D 377 ? 0.6422 0.8065 0.7820 -0.0088 -0.0499 0.0056  393 ARG A CD  
11044 N NE  . ARG D 377 ? 0.5643 0.7404 0.7302 0.0014  -0.0567 0.0097  393 ARG A NE  
11045 C CZ  . ARG D 377 ? 0.6365 0.8344 0.8278 -0.0012 -0.0613 0.0077  393 ARG A CZ  
11046 N NH1 . ARG D 377 ? 0.6021 0.8106 0.7936 -0.0141 -0.0606 0.0016  393 ARG A NH1 
11047 N NH2 . ARG D 377 ? 0.6955 0.9051 0.9136 0.0094  -0.0666 0.0117  393 ARG A NH2 
11048 N N   . ASN D 378 ? 0.7080 0.7794 0.7146 -0.0302 -0.0287 -0.0020 394 ASN A N   
11049 C CA  . ASN D 378 ? 0.7291 0.7907 0.7153 -0.0405 -0.0226 -0.0072 394 ASN A CA  
11050 C C   . ASN D 378 ? 0.7659 0.8064 0.7324 -0.0334 -0.0179 -0.0046 394 ASN A C   
11051 O O   . ASN D 378 ? 0.8222 0.8562 0.7914 -0.0205 -0.0190 0.0014  394 ASN A O   
11052 C CB  . ASN D 378 ? 0.8080 0.8576 0.7709 -0.0548 -0.0265 -0.0119 394 ASN A CB  
11053 C CG  . ASN D 378 ? 0.8932 0.9518 0.8557 -0.0685 -0.0218 -0.0189 394 ASN A CG  
11054 O OD1 . ASN D 378 ? 0.8146 0.8725 0.7745 -0.0693 -0.0147 -0.0210 394 ASN A OD1 
11055 N ND2 . ASN D 378 ? 0.9037 0.9706 0.8685 -0.0793 -0.0258 -0.0226 394 ASN A ND2 
11056 N N   . GLY D 379 ? 0.7118 0.7410 0.6586 -0.0417 -0.0128 -0.0091 395 GLY A N   
11057 C CA  . GLY D 379 ? 0.6967 0.7050 0.6234 -0.0358 -0.0087 -0.0072 395 GLY A CA  
11058 C C   . GLY D 379 ? 0.7419 0.7232 0.6398 -0.0360 -0.0132 -0.0051 395 GLY A C   
11059 O O   . GLY D 379 ? 0.7503 0.7260 0.6374 -0.0444 -0.0187 -0.0067 395 GLY A O   
11060 N N   . ALA D 380 ? 0.7385 0.7025 0.6233 -0.0265 -0.0106 -0.0014 396 ALA A N   
11061 C CA  . ALA D 380 ? 0.7550 0.6934 0.6141 -0.0244 -0.0147 0.0016  396 ALA A CA  
11062 C C   . ALA D 380 ? 0.7917 0.7143 0.6244 -0.0390 -0.0162 -0.0034 396 ALA A C   
11063 O O   . ALA D 380 ? 0.7846 0.6961 0.6045 -0.0417 -0.0222 -0.0021 396 ALA A O   
11064 C CB  . ALA D 380 ? 0.7685 0.6904 0.6158 -0.0137 -0.0103 0.0052  396 ALA A CB  
11065 N N   . ASN D 381 ? 0.8030 0.7234 0.6269 -0.0483 -0.0108 -0.0091 397 ASN A N   
11066 C CA  . ASN D 381 ? 0.7984 0.7094 0.6033 -0.0639 -0.0112 -0.0148 397 ASN A CA  
11067 C C   . ASN D 381 ? 0.7871 0.7143 0.6036 -0.0726 -0.0060 -0.0210 397 ASN A C   
11068 O O   . ASN D 381 ? 0.7563 0.6995 0.5928 -0.0660 -0.0021 -0.0205 397 ASN A O   
11069 C CB  . ASN D 381 ? 0.8412 0.7219 0.6132 -0.0661 -0.0102 -0.0150 397 ASN A CB  
11070 C CG  . ASN D 381 ? 0.8503 0.7230 0.6157 -0.0623 -0.0038 -0.0162 397 ASN A CG  
11071 O OD1 . ASN D 381 ? 0.8208 0.7075 0.5984 -0.0653 0.0009  -0.0202 397 ASN A OD1 
11072 N ND2 . ASN D 381 ? 0.8559 0.7061 0.6019 -0.0549 -0.0036 -0.0127 397 ASN A ND2 
11073 N N   . GLU D 382 ? 0.8324 0.7540 0.6352 -0.0873 -0.0054 -0.0267 398 GLU A N   
11074 C CA  . GLU D 382 ? 0.8332 0.7716 0.6482 -0.0970 -0.0013 -0.0329 398 GLU A CA  
11075 C C   . GLU D 382 ? 0.7381 0.6808 0.5595 -0.0918 0.0051  -0.0343 398 GLU A C   
11076 O O   . GLU D 382 ? 0.6863 0.6457 0.5217 -0.0974 0.0087  -0.0389 398 GLU A O   
11077 C CB  . GLU D 382 ? 0.8739 0.8010 0.6693 -0.1133 -0.0008 -0.0389 398 GLU A CB  
11078 C CG  . GLU D 382 ? 0.8823 0.7820 0.6486 -0.1169 0.0019  -0.0406 398 GLU A CG  
11079 C CD  . GLU D 382 ? 0.9079 0.7968 0.6567 -0.1326 0.0017  -0.0456 398 GLU A CD  
11080 O OE1 . GLU D 382 ? 0.9168 0.8153 0.6718 -0.1393 -0.0015 -0.0464 398 GLU A OE1 
11081 O OE2 . GLU D 382 ? 0.9537 0.8242 0.6828 -0.1380 0.0049  -0.0487 398 GLU A OE2 
11082 N N   . GLY D 383 ? 0.7280 0.6561 0.5398 -0.0805 0.0065  -0.0302 399 GLY A N   
11083 C CA  . GLY D 383 ? 0.6997 0.6275 0.5126 -0.0760 0.0124  -0.0319 399 GLY A CA  
11084 C C   . GLY D 383 ? 0.7236 0.6680 0.5603 -0.0617 0.0146  -0.0273 399 GLY A C   
11085 O O   . GLY D 383 ? 0.7254 0.6724 0.5656 -0.0574 0.0199  -0.0287 399 GLY A O   
11086 N N   . PHE D 384 ? 0.7090 0.6645 0.5625 -0.0539 0.0108  -0.0219 400 PHE A N   
11087 C CA  . PHE D 384 ? 0.6571 0.6203 0.5271 -0.0380 0.0133  -0.0164 400 PHE A CA  
11088 C C   . PHE D 384 ? 0.6327 0.6228 0.5312 -0.0363 0.0175  -0.0179 400 PHE A C   
11089 O O   . PHE D 384 ? 0.6280 0.6205 0.5326 -0.0269 0.0228  -0.0164 400 PHE A O   
11090 C CB  . PHE D 384 ? 0.7497 0.7124 0.6265 -0.0287 0.0079  -0.0095 400 PHE A CB  
11091 C CG  . PHE D 384 ? 0.7166 0.6537 0.5711 -0.0208 0.0068  -0.0052 400 PHE A CG  
11092 C CD1 . PHE D 384 ? 0.7297 0.6431 0.5542 -0.0292 0.0053  -0.0078 400 PHE A CD1 
11093 C CD2 . PHE D 384 ? 0.6812 0.6180 0.5452 -0.0052 0.0073  0.0016  400 PHE A CD2 
11094 C CE1 . PHE D 384 ? 0.7604 0.6504 0.5646 -0.0221 0.0042  -0.0039 400 PHE A CE1 
11095 C CE2 . PHE D 384 ? 0.7253 0.6391 0.5693 0.0020  0.0062  0.0056  400 PHE A CE2 
11096 C CZ  . PHE D 384 ? 0.7707 0.6609 0.5845 -0.0064 0.0045  0.0029  400 PHE A CZ  
11097 N N   . HIS D 385 ? 0.6192 0.6294 0.5349 -0.0448 0.0153  -0.0207 401 HIS A N   
11098 C CA  . HIS D 385 ? 0.6227 0.6597 0.5677 -0.0424 0.0190  -0.0216 401 HIS A CA  
11099 C C   . HIS D 385 ? 0.6289 0.6671 0.5712 -0.0441 0.0260  -0.0260 401 HIS A C   
11100 O O   . HIS D 385 ? 0.5501 0.5998 0.5090 -0.0341 0.0308  -0.0238 401 HIS A O   
11101 C CB  . HIS D 385 ? 0.6091 0.6661 0.5705 -0.0531 0.0157  -0.0249 401 HIS A CB  
11102 C CG  . HIS D 385 ? 0.6188 0.6929 0.6053 -0.0457 0.0116  -0.0200 401 HIS A CG  
11103 N ND1 . HIS D 385 ? 0.5643 0.6604 0.5802 -0.0368 0.0150  -0.0176 401 HIS A ND1 
11104 C CD2 . HIS D 385 ? 0.6421 0.7172 0.6309 -0.0476 0.0045  -0.0182 401 HIS A CD2 
11105 C CE1 . HIS D 385 ? 0.5733 0.6819 0.6084 -0.0326 0.0101  -0.0139 401 HIS A CE1 
11106 N NE2 . HIS D 385 ? 0.6258 0.7221 0.6449 -0.0390 0.0033  -0.0144 401 HIS A NE2 
11107 N N   . GLU D 386 ? 0.6935 0.7217 0.6171 -0.0572 0.0265  -0.0325 402 GLU A N   
11108 C CA  . GLU D 386 ? 0.6592 0.6905 0.5824 -0.0594 0.0324  -0.0373 402 GLU A CA  
11109 C C   . GLU D 386 ? 0.6797 0.6912 0.5858 -0.0492 0.0360  -0.0352 402 GLU A C   
11110 O O   . GLU D 386 ? 0.7425 0.7589 0.6534 -0.0451 0.0413  -0.0370 402 GLU A O   
11111 C CB  . GLU D 386 ? 0.5528 0.5837 0.4664 -0.0771 0.0320  -0.0453 402 GLU A CB  
11112 C CG  . GLU D 386 ? 0.5103 0.5694 0.4487 -0.0868 0.0320  -0.0493 402 GLU A CG  
11113 C CD  . GLU D 386 ? 0.4804 0.5621 0.4434 -0.0811 0.0376  -0.0502 402 GLU A CD  
11114 O OE1 . GLU D 386 ? 0.6164 0.6910 0.5699 -0.0810 0.0418  -0.0534 402 GLU A OE1 
11115 O OE2 . GLU D 386 ? 0.3465 0.4531 0.3367 -0.0796 0.0383  -0.0493 402 GLU A OE2 
11116 N N   . ALA D 387 ? 0.6542 0.6461 0.5443 -0.0425 0.0333  -0.0305 403 ALA A N   
11117 C CA  . ALA D 387 ? 0.6810 0.6575 0.5600 -0.0299 0.0369  -0.0272 403 ALA A CA  
11118 C C   . ALA D 387 ? 0.5980 0.5900 0.5010 -0.0145 0.0402  -0.0213 403 ALA A C   
11119 O O   . ALA D 387 ? 0.6005 0.5913 0.5041 -0.0058 0.0457  -0.0208 403 ALA A O   
11120 C CB  . ALA D 387 ? 0.7313 0.6820 0.5860 -0.0274 0.0332  -0.0239 403 ALA A CB  
11121 N N   . VAL D 388 ? 0.6319 0.6382 0.5548 -0.0106 0.0369  -0.0166 404 VAL A N   
11122 C CA  . VAL D 388 ? 0.6053 0.6284 0.5543 0.0034  0.0401  -0.0109 404 VAL A CA  
11123 C C   . VAL D 388 ? 0.5866 0.6301 0.5542 0.0024  0.0458  -0.0144 404 VAL A C   
11124 O O   . VAL D 388 ? 0.5883 0.6364 0.5657 0.0143  0.0515  -0.0114 404 VAL A O   
11125 C CB  . VAL D 388 ? 0.5352 0.5713 0.5038 0.0057  0.0348  -0.0063 404 VAL A CB  
11126 C CG1 . VAL D 388 ? 0.4841 0.5438 0.4856 0.0167  0.0383  -0.0021 404 VAL A CG1 
11127 C CG2 . VAL D 388 ? 0.5465 0.5634 0.5007 0.0125  0.0306  -0.0010 404 VAL A CG2 
11128 N N   . GLY D 389 ? 0.5277 0.5837 0.5006 -0.0116 0.0445  -0.0206 405 GLY A N   
11129 C CA  . GLY D 389 ? 0.5513 0.6263 0.5407 -0.0134 0.0497  -0.0243 405 GLY A CA  
11130 C C   . GLY D 389 ? 0.6119 0.6744 0.5849 -0.0113 0.0551  -0.0276 405 GLY A C   
11131 O O   . GLY D 389 ? 0.5694 0.6436 0.5561 -0.0040 0.0609  -0.0273 405 GLY A O   
11132 N N   . GLU D 390 ? 0.6565 0.6948 0.5999 -0.0174 0.0532  -0.0309 406 GLU A N   
11133 C CA  . GLU D 390 ? 0.6453 0.6705 0.5715 -0.0167 0.0574  -0.0350 406 GLU A CA  
11134 C C   . GLU D 390 ? 0.6641 0.6812 0.5886 0.0007  0.0620  -0.0296 406 GLU A C   
11135 O O   . GLU D 390 ? 0.7171 0.7356 0.6417 0.0054  0.0672  -0.0317 406 GLU A O   
11136 C CB  . GLU D 390 ? 0.6701 0.6708 0.5662 -0.0269 0.0539  -0.0393 406 GLU A CB  
11137 C CG  . GLU D 390 ? 0.7164 0.7227 0.6111 -0.0444 0.0509  -0.0458 406 GLU A CG  
11138 C CD  . GLU D 390 ? 0.8861 0.9013 0.7844 -0.0508 0.0547  -0.0528 406 GLU A CD  
11139 O OE1 . GLU D 390 ? 0.9242 0.9317 0.8154 -0.0428 0.0587  -0.0534 406 GLU A OE1 
11140 O OE2 . GLU D 390 ? 0.8771 0.9069 0.7854 -0.0634 0.0535  -0.0574 406 GLU A OE2 
11141 N N   . ILE D 391 ? 0.6023 0.6088 0.5231 0.0104  0.0601  -0.0227 407 ILE A N   
11142 C CA  . ILE D 391 ? 0.6227 0.6191 0.5394 0.0269  0.0647  -0.0175 407 ILE A CA  
11143 C C   . ILE D 391 ? 0.6012 0.6193 0.5451 0.0375  0.0706  -0.0144 407 ILE A C   
11144 O O   . ILE D 391 ? 0.6160 0.6284 0.5572 0.0498  0.0762  -0.0120 407 ILE A O   
11145 C CB  . ILE D 391 ? 0.6696 0.6515 0.5789 0.0353  0.0615  -0.0104 407 ILE A CB  
11146 C CG1 . ILE D 391 ? 0.6193 0.6205 0.5554 0.0389  0.0591  -0.0050 407 ILE A CG1 
11147 C CG2 . ILE D 391 ? 0.6617 0.6213 0.5435 0.0251  0.0557  -0.0132 407 ILE A CG2 
11148 C CD1 . ILE D 391 ? 0.6071 0.5946 0.5361 0.0463  0.0553  0.0013  407 ILE A CD1 
11149 N N   . MET D 392 ? 0.5660 0.6088 0.5361 0.0331  0.0697  -0.0143 408 MET A N   
11150 C CA  . MET D 392 ? 0.5559 0.6209 0.5530 0.0415  0.0755  -0.0120 408 MET A CA  
11151 C C   . MET D 392 ? 0.5795 0.6463 0.5716 0.0393  0.0807  -0.0179 408 MET A C   
11152 O O   . MET D 392 ? 0.6026 0.6686 0.5971 0.0517  0.0869  -0.0154 408 MET A O   
11153 C CB  . MET D 392 ? 0.5415 0.6319 0.5665 0.0353  0.0728  -0.0117 408 MET A CB  
11154 C CG  . MET D 392 ? 0.5777 0.6657 0.6058 0.0356  0.0665  -0.0071 408 MET A CG  
11155 S SD  . MET D 392 ? 0.6086 0.6834 0.6363 0.0555  0.0685  0.0028  408 MET A SD  
11156 C CE  . MET D 392 ? 0.5282 0.5943 0.5497 0.0507  0.0589  0.0055  408 MET A CE  
11157 N N   . SER D 393 ? 0.5885 0.6571 0.5730 0.0238  0.0782  -0.0258 409 SER A N   
11158 C CA  . SER D 393 ? 0.5635 0.6348 0.5446 0.0217  0.0826  -0.0316 409 SER A CA  
11159 C C   . SER D 393 ? 0.6127 0.6590 0.5673 0.0290  0.0849  -0.0322 409 SER A C   
11160 O O   . SER D 393 ? 0.6527 0.7003 0.6071 0.0353  0.0901  -0.0339 409 SER A O   
11161 C CB  . SER D 393 ? 0.6468 0.7261 0.6271 0.0032  0.0791  -0.0397 409 SER A CB  
11162 O OG  . SER D 393 ? 0.9092 0.9667 0.8612 -0.0060 0.0762  -0.0454 409 SER A OG  
11163 N N   . LEU D 394 ? 0.6350 0.6586 0.5678 0.0297  0.0812  -0.0304 410 LEU A N   
11164 C CA  . LEU D 394 ? 0.6274 0.6274 0.5366 0.0387  0.0836  -0.0301 410 LEU A CA  
11165 C C   . LEU D 394 ? 0.6528 0.6572 0.5738 0.0574  0.0901  -0.0233 410 LEU A C   
11166 O O   . LEU D 394 ? 0.6784 0.6774 0.5921 0.0644  0.0949  -0.0250 410 LEU A O   
11167 C CB  . LEU D 394 ? 0.6218 0.5971 0.5074 0.0380  0.0790  -0.0281 410 LEU A CB  
11168 C CG  . LEU D 394 ? 0.6619 0.6222 0.5261 0.0223  0.0730  -0.0340 410 LEU A CG  
11169 C CD1 . LEU D 394 ? 0.6632 0.5971 0.5040 0.0280  0.0709  -0.0304 410 LEU A CD1 
11170 C CD2 . LEU D 394 ? 0.7143 0.6712 0.5671 0.0111  0.0733  -0.0432 410 LEU A CD2 
11171 N N   . SER D 395 ? 0.7024 0.7167 0.6421 0.0657  0.0905  -0.0157 411 SER A N   
11172 C CA  . SER D 395 ? 0.6954 0.7123 0.6462 0.0840  0.0970  -0.0085 411 SER A CA  
11173 C C   . SER D 395 ? 0.6171 0.6554 0.5888 0.0874  0.1033  -0.0098 411 SER A C   
11174 O O   . SER D 395 ? 0.6416 0.6782 0.6151 0.1012  0.1100  -0.0066 411 SER A O   
11175 C CB  . SER D 395 ? 0.6334 0.6561 0.6005 0.0914  0.0955  -0.0002 411 SER A CB  
11176 O OG  . SER D 395 ? 0.6567 0.6558 0.6026 0.0954  0.0924  0.0030  411 SER A OG  
11177 N N   . ALA D 396 ? 0.5905 0.6488 0.5780 0.0751  0.1014  -0.0144 412 ALA A N   
11178 C CA  . ALA D 396 ? 0.6183 0.6996 0.6295 0.0782  0.1071  -0.0149 412 ALA A CA  
11179 C C   . ALA D 396 ? 0.7092 0.7861 0.7075 0.0761  0.1103  -0.0216 412 ALA A C   
11180 O O   . ALA D 396 ? 0.7006 0.7887 0.7118 0.0850  0.1170  -0.0204 412 ALA A O   
11181 C CB  . ALA D 396 ? 0.5670 0.6724 0.6016 0.0661  0.1037  -0.0170 412 ALA A CB  
11182 N N   . ALA D 397 ? 0.6935 0.7539 0.6667 0.0647  0.1058  -0.0287 413 ALA A N   
11183 C CA  . ALA D 397 ? 0.6305 0.6856 0.5902 0.0608  0.1075  -0.0362 413 ALA A CA  
11184 C C   . ALA D 397 ? 0.6537 0.6881 0.5932 0.0747  0.1115  -0.0348 413 ALA A C   
11185 O O   . ALA D 397 ? 0.6665 0.6983 0.5979 0.0749  0.1139  -0.0401 413 ALA A O   
11186 C CB  . ALA D 397 ? 0.7018 0.7477 0.6443 0.0426  0.1007  -0.0442 413 ALA A CB  
11187 N N   . THR D 398 ? 0.6848 0.7043 0.6160 0.0862  0.1122  -0.0280 414 THR A N   
11188 C CA  . THR D 398 ? 0.7260 0.7249 0.6372 0.0996  0.1159  -0.0265 414 THR A CA  
11189 C C   . THR D 398 ? 0.7451 0.7556 0.6686 0.1111  0.1238  -0.0254 414 THR A C   
11190 O O   . THR D 398 ? 0.7052 0.7392 0.6563 0.1136  0.1274  -0.0221 414 THR A O   
11191 C CB  . THR D 398 ? 0.7732 0.7592 0.6803 0.1124  0.1168  -0.0177 414 THR A CB  
11192 O OG1 . THR D 398 ? 0.7563 0.7613 0.6916 0.1233  0.1220  -0.0099 414 THR A OG1 
11193 C CG2 . THR D 398 ? 0.7383 0.7155 0.6371 0.1022  0.1094  -0.0175 414 THR A CG2 
11194 N N   . PRO D 399 ? 0.7995 0.7934 0.7029 0.1187  0.1265  -0.0280 415 PRO A N   
11195 C CA  . PRO D 399 ? 0.7622 0.7641 0.6751 0.1326  0.1347  -0.0256 415 PRO A CA  
11196 C C   . PRO D 399 ? 0.7600 0.7669 0.6889 0.1487  0.1405  -0.0150 415 PRO A C   
11197 O O   . PRO D 399 ? 0.7267 0.7530 0.6790 0.1558  0.1467  -0.0115 415 PRO A O   
11198 C CB  . PRO D 399 ? 0.8369 0.8145 0.7199 0.1379  0.1350  -0.0300 415 PRO A CB  
11199 C CG  . PRO D 399 ? 0.8758 0.8396 0.7388 0.1221  0.1268  -0.0376 415 PRO A CG  
11200 C CD  . PRO D 399 ? 0.8254 0.7935 0.6969 0.1141  0.1222  -0.0339 415 PRO A CD  
11201 N N   . LYS D 400 ? 0.7927 0.7827 0.7101 0.1545  0.1388  -0.0098 416 LYS A N   
11202 C CA  . LYS D 400 ? 0.7733 0.7672 0.7063 0.1701  0.1443  0.0006  416 LYS A CA  
11203 C C   . LYS D 400 ? 0.7325 0.7555 0.7010 0.1681  0.1461  0.0043  416 LYS A C   
11204 O O   . LYS D 400 ? 0.7097 0.7462 0.6979 0.1798  0.1538  0.0093  416 LYS A O   
11205 C CB  . LYS D 400 ? 0.7486 0.7231 0.6670 0.1726  0.1403  0.0049  416 LYS A CB  
11206 C CG  . LYS D 400 ? 0.7768 0.7528 0.7090 0.1903  0.1466  0.0154  416 LYS A CG  
11207 C CD  . LYS D 400 ? 0.7789 0.7469 0.7116 0.1924  0.1428  0.0217  416 LYS A CD  
11208 C CE  . LYS D 400 ? 0.7799 0.7176 0.6788 0.1930  0.1390  0.0204  416 LYS A CE  
11209 N NZ  . LYS D 400 ? 0.8411 0.7701 0.7386 0.1938  0.1346  0.0259  416 LYS A NZ  
11210 N N   . HIS D 401 ? 0.6866 0.7195 0.6633 0.1528  0.1390  0.0015  417 HIS A N   
11211 C CA  . HIS D 401 ? 0.6648 0.7249 0.6743 0.1489  0.1392  0.0042  417 HIS A CA  
11212 C C   . HIS D 401 ? 0.6525 0.7334 0.6798 0.1482  0.1444  0.0011  417 HIS A C   
11213 O O   . HIS D 401 ? 0.6297 0.7301 0.6847 0.1560  0.1499  0.0065  417 HIS A O   
11214 C CB  . HIS D 401 ? 0.6534 0.7169 0.6626 0.1314  0.1300  0.0002  417 HIS A CB  
11215 C CG  . HIS D 401 ? 0.6422 0.7315 0.6835 0.1274  0.1291  0.0031  417 HIS A CG  
11216 N ND1 . HIS D 401 ? 0.5837 0.6773 0.6407 0.1345  0.1285  0.0109  417 HIS A ND1 
11217 C CD2 . HIS D 401 ? 0.6329 0.7450 0.6935 0.1165  0.1281  -0.0012 417 HIS A CD2 
11218 C CE1 . HIS D 401 ? 0.6383 0.7562 0.7232 0.1286  0.1272  0.0113  417 HIS A CE1 
11219 N NE2 . HIS D 401 ? 0.5463 0.6759 0.6338 0.1176  0.1270  0.0041  417 HIS A NE2 
11220 N N   . LEU D 402 ? 0.6917 0.7694 0.7043 0.1384  0.1425  -0.0076 418 LEU A N   
11221 C CA  . LEU D 402 ? 0.6731 0.7703 0.7013 0.1361  0.1467  -0.0114 418 LEU A CA  
11222 C C   . LEU D 402 ? 0.6875 0.7865 0.7223 0.1544  0.1565  -0.0063 418 LEU A C   
11223 O O   . LEU D 402 ? 0.6612 0.7793 0.7206 0.1534  0.1576  -0.0048 418 LEU A O   
11224 C CB  . LEU D 402 ? 0.6375 0.7278 0.6460 0.1227  0.1424  -0.0219 418 LEU A CB  
11225 C CG  . LEU D 402 ? 0.6449 0.7371 0.6515 0.1043  0.1336  -0.0264 418 LEU A CG  
11226 C CD1 . LEU D 402 ? 0.6708 0.7530 0.6562 0.0904  0.1288  -0.0365 418 LEU A CD1 
11227 C CD2 . LEU D 402 ? 0.5908 0.7126 0.6302 0.0990  0.1346  -0.0251 418 LEU A CD2 
11228 N N   . LYS D 403 ? 0.6975 0.7732 0.7092 0.1662  0.1591  -0.0043 419 LYS A N   
11229 C CA  . LYS D 403 ? 0.7086 0.7813 0.7255 0.1782  0.1625  0.0016  419 LYS A CA  
11230 C C   . LYS D 403 ? 0.7515 0.8371 0.7961 0.1798  0.1608  0.0100  419 LYS A C   
11231 O O   . LYS D 403 ? 0.7331 0.8312 0.7969 0.1756  0.1580  0.0114  419 LYS A O   
11232 C CB  . LYS D 403 ? 0.7521 0.7969 0.7400 0.1908  0.1651  0.0035  419 LYS A CB  
11233 C CG  . LYS D 403 ? 0.8241 0.8524 0.7825 0.1896  0.1653  -0.0052 419 LYS A CG  
11234 C CD  . LYS D 403 ? 0.8827 0.8828 0.8137 0.2021  0.1666  -0.0027 419 LYS A CD  
11235 C CE  . LYS D 403 ? 1.0172 1.0007 0.9202 0.2003  0.1652  -0.0115 419 LYS A CE  
11236 N NZ  . LYS D 403 ? 1.1227 1.0809 1.0021 0.2119  0.1655  -0.0086 419 LYS A NZ  
11237 N N   . SER D 404 ? 0.8163 0.8984 0.8622 0.1850  0.1618  0.0149  420 SER A N   
11238 C CA  . SER D 404 ? 0.7370 0.8285 0.8070 0.1872  0.1597  0.0229  420 SER A CA  
11239 C C   . SER D 404 ? 0.7260 0.8421 0.8249 0.1753  0.1551  0.0212  420 SER A C   
11240 O O   . SER D 404 ? 0.7109 0.8324 0.8258 0.1757  0.1527  0.0253  420 SER A O   
11241 C CB  . SER D 404 ? 0.8503 0.9373 0.9191 0.1924  0.1606  0.0269  420 SER A CB  
11242 O OG  . SER D 404 ? 1.0695 1.1594 1.1559 0.1971  0.1586  0.0351  420 SER A OG  
11243 N N   . ILE D 405 ? 0.6747 0.8048 0.7793 0.1641  0.1536  0.0147  421 ILE A N   
11244 C CA  . ILE D 405 ? 0.6174 0.7693 0.7488 0.1526  0.1482  0.0127  421 ILE A CA  
11245 C C   . ILE D 405 ? 0.6162 0.7729 0.7499 0.1459  0.1462  0.0072  421 ILE A C   
11246 O O   . ILE D 405 ? 0.5774 0.7494 0.7303 0.1365  0.1412  0.0045  421 ILE A O   
11247 C CB  . ILE D 405 ? 0.5524 0.7200 0.6934 0.1419  0.1464  0.0088  421 ILE A CB  
11248 C CG1 . ILE D 405 ? 0.5626 0.7275 0.6844 0.1368  0.1497  0.0015  421 ILE A CG1 
11249 C CG2 . ILE D 405 ? 0.6549 0.8190 0.7957 0.1485  0.1480  0.0146  421 ILE A CG2 
11250 C CD1 . ILE D 405 ? 0.5242 0.7069 0.6569 0.1218  0.1461  -0.0035 421 ILE A CD1 
11251 N N   . GLY D 406 ? 0.6350 0.7783 0.7487 0.1505  0.1493  0.0051  422 GLY A N   
11252 C CA  . GLY D 406 ? 0.6519 0.7986 0.7673 0.1455  0.1474  0.0005  422 GLY A CA  
11253 C C   . GLY D 406 ? 0.6672 0.8211 0.7783 0.1347  0.1465  -0.0087 422 GLY A C   
11254 O O   . GLY D 406 ? 0.6775 0.8373 0.7944 0.1286  0.1439  -0.0132 422 GLY A O   
11255 N N   . LEU D 407 ? 0.5927 0.7459 0.6932 0.1319  0.1487  -0.0120 423 LEU A N   
11256 C CA  . LEU D 407 ? 0.6216 0.7809 0.7166 0.1209  0.1481  -0.0211 423 LEU A CA  
11257 C C   . LEU D 407 ? 0.6887 0.8296 0.7549 0.1263  0.1514  -0.0251 423 LEU A C   
11258 O O   . LEU D 407 ? 0.7023 0.8453 0.7599 0.1179  0.1511  -0.0332 423 LEU A O   
11259 C CB  . LEU D 407 ? 0.5956 0.7662 0.6939 0.1115  0.1481  -0.0240 423 LEU A CB  
11260 C CG  . LEU D 407 ? 0.4765 0.6672 0.6028 0.1018  0.1432  -0.0231 423 LEU A CG  
11261 C CD1 . LEU D 407 ? 0.4554 0.6557 0.5804 0.0933  0.1439  -0.0253 423 LEU A CD1 
11262 C CD2 . LEU D 407 ? 0.5614 0.7619 0.7034 0.0925  0.1383  -0.0280 423 LEU A CD2 
11263 N N   . LEU D 408 ? 0.6501 0.7722 0.7007 0.1398  0.1541  -0.0199 424 LEU A N   
11264 C CA  . LEU D 408 ? 0.6809 0.7824 0.7013 0.1454  0.1563  -0.0241 424 LEU A CA  
11265 C C   . LEU D 408 ? 0.7841 0.8723 0.7996 0.1574  0.1569  -0.0178 424 LEU A C   
11266 O O   . LEU D 408 ? 0.8264 0.9121 0.8495 0.1652  0.1579  -0.0094 424 LEU A O   
11267 C CB  . LEU D 408 ? 0.7012 0.7877 0.6982 0.1489  0.1592  -0.0255 424 LEU A CB  
11268 C CG  . LEU D 408 ? 0.7787 0.8426 0.7433 0.1464  0.1562  -0.0332 424 LEU A CG  
11269 C CD1 . LEU D 408 ? 0.8651 0.9431 0.8355 0.1350  0.1549  -0.0416 424 LEU A CD1 
11270 C CD2 . LEU D 408 ? 0.8150 0.8624 0.7616 0.1355  0.1478  -0.0357 424 LEU A CD2 
11271 N N   . SER D 409 ? 0.8663 0.9470 0.8708 0.1583  0.1563  -0.0213 425 SER A N   
11272 C CA  . SER D 409 ? 0.8848 0.9555 0.8875 0.1691  0.1571  -0.0140 425 SER A CA  
11273 C C   . SER D 409 ? 0.9742 1.0214 0.9524 0.1813  0.1599  -0.0102 425 SER A C   
11274 O O   . SER D 409 ? 1.0418 1.0763 0.9980 0.1812  0.1604  -0.0158 425 SER A O   
11275 C CB  . SER D 409 ? 1.0016 1.0704 0.9997 0.1680  0.1557  -0.0175 425 SER A CB  
11276 O OG  . SER D 409 ? 1.0430 1.1021 1.0384 0.1781  0.1569  -0.0101 425 SER A OG  
11277 N N   . PRO D 410 ? 1.0765 1.1165 1.0568 0.1913  0.1613  -0.0012 426 PRO A N   
11278 C CA  . PRO D 410 ? 1.1516 1.1673 1.1070 0.2034  0.1636  0.0024  426 PRO A CA  
11279 C C   . PRO D 410 ? 1.3753 1.3722 1.3021 0.2061  0.1630  -0.0038 426 PRO A C   
11280 O O   . PRO D 410 ? 1.3379 1.3133 1.2399 0.2131  0.1637  -0.0042 426 PRO A O   
11281 C CB  . PRO D 410 ? 1.0671 1.0826 1.0333 0.2109  0.1650  0.0125  426 PRO A CB  
11282 C CG  . PRO D 410 ? 0.9757 1.0148 0.9732 0.2028  0.1633  0.0144  426 PRO A CG  
11283 C CD  . PRO D 410 ? 0.9833 1.0363 0.9879 0.1911  0.1607  0.0056  426 PRO A CD  
11284 N N   . ASP D 411 ? 1.5797 1.5836 1.5094 0.2004  0.1610  -0.0089 427 ASP A N   
11285 C CA  . ASP D 411 ? 1.7103 1.6984 1.6152 0.2017  0.1594  -0.0155 427 ASP A CA  
11286 C C   . ASP D 411 ? 1.7527 1.7374 1.6437 0.1932  0.1574  -0.0262 427 ASP A C   
11287 O O   . ASP D 411 ? 1.7138 1.6967 1.5957 0.1876  0.1547  -0.0342 427 ASP A O   
11288 C CB  . ASP D 411 ? 1.7053 1.7025 1.6194 0.1987  0.1578  -0.0169 427 ASP A CB  
11289 C CG  . ASP D 411 ? 1.7237 1.7293 1.6564 0.2031  0.1595  -0.0074 427 ASP A CG  
11290 O OD1 . ASP D 411 ? 1.7290 1.7262 1.6593 0.2118  0.1619  0.0007  427 ASP A OD1 
11291 O OD2 . ASP D 411 ? 1.7210 1.7413 1.6707 0.1972  0.1582  -0.0084 427 ASP A OD2 
11292 N N   . PHE D 412 ? 1.4459 1.4293 1.3345 0.1914  0.1585  -0.0266 428 PHE A N   
11293 C CA  . PHE D 412 ? 1.4403 1.4166 1.3107 0.1829  0.1566  -0.0369 428 PHE A CA  
11294 C C   . PHE D 412 ? 1.5247 1.4707 1.3619 0.1902  0.1559  -0.0383 428 PHE A C   
11295 O O   . PHE D 412 ? 1.4729 1.4085 1.3064 0.2004  0.1582  -0.0307 428 PHE A O   
11296 C CB  . PHE D 412 ? 1.2720 1.2640 1.1566 0.1745  0.1579  -0.0379 428 PHE A CB  
11297 C CG  . PHE D 412 ? 1.2409 1.2289 1.1122 0.1575  0.1511  -0.0483 428 PHE A CG  
11298 C CD1 . PHE D 412 ? 1.3163 1.2832 1.1657 0.1510  0.1444  -0.0507 428 PHE A CD1 
11299 C CD2 . PHE D 412 ? 1.1022 1.1066 0.9835 0.1462  0.1496  -0.0555 428 PHE A CD2 
11300 C CE1 . PHE D 412 ? 1.2669 1.2296 1.1057 0.1331  0.1365  -0.0599 428 PHE A CE1 
11301 C CE2 . PHE D 412 ? 1.0872 1.0877 0.9582 0.1284  0.1416  -0.0648 428 PHE A CE2 
11302 C CZ  . PHE D 412 ? 1.1441 1.1237 0.9941 0.1219  0.1352  -0.0670 428 PHE A CZ  
11303 N N   . GLN D 413 ? 1.8378 1.7697 1.6518 0.1846  0.1519  -0.0482 429 GLN A N   
11304 C CA  . GLN D 413 ? 1.7992 1.7012 1.5806 0.1891  0.1494  -0.0512 429 GLN A CA  
11305 C C   . GLN D 413 ? 1.7658 1.6625 1.5391 0.1722  0.1419  -0.0568 429 GLN A C   
11306 O O   . GLN D 413 ? 1.7978 1.7003 1.5711 0.1571  0.1366  -0.0655 429 GLN A O   
11307 C CB  . GLN D 413 ? 1.9189 1.8090 1.6848 0.1893  0.1450  -0.0566 429 GLN A CB  
11308 C CG  . GLN D 413 ? 1.9840 1.8432 1.7168 0.1928  0.1411  -0.0602 429 GLN A CG  
11309 C CD  . GLN D 413 ? 2.0525 1.8972 1.7783 0.2079  0.1443  -0.0501 429 GLN A CD  
11310 O OE1 . GLN D 413 ? 1.9985 1.8538 1.7416 0.2143  0.1493  -0.0409 429 GLN A OE1 
11311 N NE2 . GLN D 413 ? 2.1021 1.9228 1.8031 0.2133  0.1409  -0.0517 429 GLN A NE2 
11312 N N   . GLU D 414 ? 1.5365 1.4228 1.3049 0.1731  0.1402  -0.0514 430 GLU A N   
11313 C CA  . GLU D 414 ? 1.5148 1.3917 1.2724 0.1570  0.1317  -0.0562 430 GLU A CA  
11314 C C   . GLU D 414 ? 1.5552 1.4025 1.2804 0.1601  0.1282  -0.0610 430 GLU A C   
11315 O O   . GLU D 414 ? 1.6273 1.4585 1.3394 0.1760  0.1319  -0.0561 430 GLU A O   
11316 C CB  . GLU D 414 ? 1.5586 1.4392 1.3271 0.1560  0.1312  -0.0482 430 GLU A CB  
11317 C CG  . GLU D 414 ? 1.4711 1.3788 1.2714 0.1599  0.1367  -0.0415 430 GLU A CG  
11318 C CD  . GLU D 414 ? 1.3760 1.2835 1.1854 0.1689  0.1393  -0.0312 430 GLU A CD  
11319 O OE1 . GLU D 414 ? 1.3768 1.2702 1.1740 0.1640  0.1342  -0.0302 430 GLU A OE1 
11320 O OE2 . GLU D 414 ? 1.3523 1.2738 1.1815 0.1810  0.1465  -0.0240 430 GLU A OE2 
11321 N N   . ASP D 415 ? 1.5019 1.3422 1.2149 0.1451  0.1211  -0.0707 431 ASP A N   
11322 C CA  . ASP D 415 ? 1.5015 1.3144 1.1846 0.1459  0.1168  -0.0769 431 ASP A CA  
11323 C C   . ASP D 415 ? 1.4185 1.2204 1.0909 0.1294  0.1090  -0.0813 431 ASP A C   
11324 O O   . ASP D 415 ? 1.3476 1.1643 1.0357 0.1163  0.1067  -0.0808 431 ASP A O   
11325 C CB  . ASP D 415 ? 1.5057 1.3185 1.1822 0.1457  0.1162  -0.0858 431 ASP A CB  
11326 C CG  . ASP D 415 ? 1.4212 1.2556 1.1151 0.1285  0.1133  -0.0927 431 ASP A CG  
11327 O OD1 . ASP D 415 ? 1.3874 1.2206 1.0798 0.1116  0.1070  -0.0975 431 ASP A OD1 
11328 O OD2 . ASP D 415 ? 1.4117 1.2638 1.1204 0.1319  0.1173  -0.0935 431 ASP A OD2 
11329 N N   . ASN D 416 ? 1.0753 1.2975 1.2592 0.0493  0.0603  -0.1413 432 ASN A N   
11330 C CA  . ASN D 416 ? 1.0779 1.2764 1.2483 0.0391  0.0573  -0.1445 432 ASN A CA  
11331 C C   . ASN D 416 ? 1.0046 1.1969 1.1687 0.0264  0.0648  -0.1409 432 ASN A C   
11332 O O   . ASN D 416 ? 0.9657 1.1389 1.1197 0.0168  0.0624  -0.1372 432 ASN A O   
11333 C CB  . ASN D 416 ? 1.1450 1.3467 1.3162 0.0430  0.0567  -0.1530 432 ASN A CB  
11334 C CG  . ASN D 416 ? 1.1783 1.3684 1.3468 0.0487  0.0462  -0.1578 432 ASN A CG  
11335 O OD1 . ASN D 416 ? 1.2281 1.4100 1.3950 0.0511  0.0394  -0.1547 432 ASN A OD1 
11336 N ND2 . ASN D 416 ? 1.1421 1.3306 1.3099 0.0503  0.0446  -0.1654 432 ASN A ND2 
11337 N N   . GLU D 417 ? 0.9869 1.1967 1.1575 0.0269  0.0741  -0.1417 433 GLU A N   
11338 C CA  . GLU D 417 ? 0.8433 1.0468 1.0067 0.0154  0.0810  -0.1409 433 GLU A CA  
11339 C C   . GLU D 417 ? 0.8223 1.0214 0.9831 0.0077  0.0844  -0.1337 433 GLU A C   
11340 O O   . GLU D 417 ? 0.7995 0.9812 0.9488 -0.0035 0.0846  -0.1322 433 GLU A O   
11341 C CB  . GLU D 417 ? 0.8477 1.0719 1.0189 0.0189  0.0898  -0.1443 433 GLU A CB  
11342 C CG  . GLU D 417 ? 0.9165 1.1461 1.0908 0.0271  0.0860  -0.1522 433 GLU A CG  
11343 C CD  . GLU D 417 ? 0.8820 1.1282 1.0611 0.0287  0.0940  -0.1567 433 GLU A CD  
11344 O OE1 . GLU D 417 ? 0.8372 1.0941 1.0188 0.0248  0.1034  -0.1535 433 GLU A OE1 
11345 O OE2 . GLU D 417 ? 0.8781 1.1262 1.0583 0.0340  0.0906  -0.1638 433 GLU A OE2 
11346 N N   . THR D 418 ? 0.9112 1.1263 1.0828 0.0136  0.0871  -0.1293 434 THR A N   
11347 C CA  . THR D 418 ? 0.8970 1.1078 1.0669 0.0065  0.0899  -0.1230 434 THR A CA  
11348 C C   . THR D 418 ? 0.8394 1.0268 0.9980 0.0005  0.0815  -0.1209 434 THR A C   
11349 O O   . THR D 418 ? 0.7834 0.9579 0.9331 -0.0098 0.0829  -0.1180 434 THR A O   
11350 C CB  . THR D 418 ? 0.9071 1.1381 1.0917 0.0144  0.0929  -0.1184 434 THR A CB  
11351 O OG1 . THR D 418 ? 1.0233 1.2604 1.2145 0.0254  0.0860  -0.1192 434 THR A OG1 
11352 C CG2 . THR D 418 ? 0.9550 1.2085 1.1502 0.0174  0.1033  -0.1183 434 THR A CG2 
11353 N N   . GLU D 419 ? 0.8865 1.0689 1.0453 0.0071  0.0728  -0.1222 435 GLU A N   
11354 C CA  . GLU D 419 ? 0.8323 0.9927 0.9804 0.0020  0.0646  -0.1202 435 GLU A CA  
11355 C C   . GLU D 419 ? 0.7522 0.8919 0.8860 -0.0086 0.0633  -0.1222 435 GLU A C   
11356 O O   . GLU D 419 ? 0.7164 0.8400 0.8405 -0.0171 0.0610  -0.1188 435 GLU A O   
11357 C CB  . GLU D 419 ? 0.8733 1.0328 1.0245 0.0116  0.0557  -0.1216 435 GLU A CB  
11358 C CG  . GLU D 419 ? 0.8943 1.0703 1.0575 0.0203  0.0556  -0.1177 435 GLU A CG  
11359 C CD  . GLU D 419 ? 0.9898 1.1653 1.1556 0.0301  0.0468  -0.1191 435 GLU A CD  
11360 O OE1 . GLU D 419 ? 0.9817 1.1382 1.1374 0.0276  0.0396  -0.1213 435 GLU A OE1 
11361 O OE2 . GLU D 419 ? 1.1047 1.2986 1.2825 0.0401  0.0471  -0.1173 435 GLU A OE2 
11362 N N   . ILE D 420 ? 0.7881 0.9284 0.9208 -0.0081 0.0646  -0.1276 436 ILE A N   
11363 C CA  . ILE D 420 ? 0.7423 0.8630 0.8621 -0.0183 0.0633  -0.1290 436 ILE A CA  
11364 C C   . ILE D 420 ? 0.7048 0.8241 0.8192 -0.0286 0.0710  -0.1259 436 ILE A C   
11365 O O   . ILE D 420 ? 0.6810 0.7827 0.7838 -0.0382 0.0692  -0.1235 436 ILE A O   
11366 C CB  . ILE D 420 ? 0.7711 0.8924 0.8916 -0.0151 0.0621  -0.1358 436 ILE A CB  
11367 C CG1 . ILE D 420 ? 0.7509 0.8677 0.8738 -0.0064 0.0526  -0.1385 436 ILE A CG1 
11368 C CG2 . ILE D 420 ? 0.7710 0.8750 0.8798 -0.0261 0.0624  -0.1367 436 ILE A CG2 
11369 C CD1 . ILE D 420 ? 0.7424 0.8351 0.8544 -0.0121 0.0443  -0.1362 436 ILE A CD1 
11370 N N   . ASN D 421 ? 0.7022 0.8405 0.8250 -0.0265 0.0798  -0.1256 437 ASN A N   
11371 C CA  . ASN D 421 ? 0.6746 0.8131 0.7935 -0.0354 0.0872  -0.1222 437 ASN A CA  
11372 C C   . ASN D 421 ? 0.6549 0.7813 0.7678 -0.0409 0.0837  -0.1169 437 ASN A C   
11373 O O   . ASN D 421 ? 0.6439 0.7562 0.7454 -0.0509 0.0842  -0.1150 437 ASN A O   
11374 C CB  . ASN D 421 ? 0.6932 0.8553 0.8247 -0.0305 0.0962  -0.1213 437 ASN A CB  
11375 C CG  . ASN D 421 ? 0.7264 0.9003 0.8612 -0.0289 0.1025  -0.1257 437 ASN A CG  
11376 O OD1 . ASN D 421 ? 0.7435 0.9079 0.8712 -0.0318 0.1005  -0.1297 437 ASN A OD1 
11377 N ND2 . ASN D 421 ? 0.7483 0.9442 0.8950 -0.0235 0.1103  -0.1250 437 ASN A ND2 
11378 N N   . PHE D 422 ? 0.6607 0.7937 0.7815 -0.0339 0.0803  -0.1146 438 PHE A N   
11379 C CA  . PHE D 422 ? 0.6293 0.7534 0.7464 -0.0377 0.0768  -0.1098 438 PHE A CA  
11380 C C   . PHE D 422 ? 0.6298 0.7304 0.7327 -0.0443 0.0692  -0.1093 438 PHE A C   
11381 O O   . PHE D 422 ? 0.5680 0.6572 0.6615 -0.0532 0.0696  -0.1064 438 PHE A O   
11382 C CB  . PHE D 422 ? 0.6271 0.7621 0.7557 -0.0279 0.0731  -0.1079 438 PHE A CB  
11383 C CG  . PHE D 422 ? 0.6273 0.7523 0.7520 -0.0309 0.0679  -0.1035 438 PHE A CG  
11384 C CD1 . PHE D 422 ? 0.6229 0.7517 0.7498 -0.0355 0.0723  -0.0999 438 PHE A CD1 
11385 C CD2 . PHE D 422 ? 0.6595 0.7690 0.7767 -0.0305 0.0587  -0.1033 438 PHE A CD2 
11386 C CE1 . PHE D 422 ? 0.6095 0.7290 0.7325 -0.0386 0.0675  -0.0964 438 PHE A CE1 
11387 C CE2 . PHE D 422 ? 0.6514 0.7513 0.7641 -0.0339 0.0541  -0.0993 438 PHE A CE2 
11388 C CZ  . PHE D 422 ? 0.6210 0.7262 0.7366 -0.0379 0.0584  -0.0960 438 PHE A CZ  
11389 N N   . LEU D 423 ? 0.6550 0.7488 0.7566 -0.0395 0.0622  -0.1120 439 LEU A N   
11390 C CA  . LEU D 423 ? 0.6378 0.7098 0.7273 -0.0446 0.0545  -0.1111 439 LEU A CA  
11391 C C   . LEU D 423 ? 0.6267 0.6867 0.7049 -0.0553 0.0575  -0.1112 439 LEU A C   
11392 O O   . LEU D 423 ? 0.6381 0.6821 0.7054 -0.0627 0.0541  -0.1082 439 LEU A O   
11393 C CB  . LEU D 423 ? 0.6748 0.7430 0.7663 -0.0370 0.0472  -0.1147 439 LEU A CB  
11394 C CG  . LEU D 423 ? 0.7331 0.8063 0.8315 -0.0281 0.0415  -0.1131 439 LEU A CG  
11395 C CD1 . LEU D 423 ? 0.7523 0.8211 0.8521 -0.0205 0.0340  -0.1168 439 LEU A CD1 
11396 C CD2 . LEU D 423 ? 0.7341 0.7943 0.8247 -0.0337 0.0373  -0.1079 439 LEU A CD2 
11397 N N   . LEU D 424 ? 0.6864 0.7551 0.7671 -0.0562 0.0641  -0.1144 440 LEU A N   
11398 C CA  . LEU D 424 ? 0.6874 0.7461 0.7579 -0.0662 0.0674  -0.1144 440 LEU A CA  
11399 C C   . LEU D 424 ? 0.6307 0.6880 0.6955 -0.0742 0.0721  -0.1099 440 LEU A C   
11400 O O   . LEU D 424 ? 0.6180 0.6604 0.6710 -0.0827 0.0704  -0.1074 440 LEU A O   
11401 C CB  . LEU D 424 ? 0.6396 0.7100 0.7151 -0.0644 0.0737  -0.1190 440 LEU A CB  
11402 C CG  . LEU D 424 ? 0.5677 0.6278 0.6332 -0.0739 0.0763  -0.1196 440 LEU A CG  
11403 C CD1 . LEU D 424 ? 0.6142 0.6796 0.6763 -0.0810 0.0848  -0.1166 440 LEU A CD1 
11404 C CD2 . LEU D 424 ? 0.5723 0.6099 0.6266 -0.0798 0.0684  -0.1177 440 LEU A CD2 
11405 N N   . LYS D 425 ? 0.6071 0.6804 0.6804 -0.0714 0.0783  -0.1090 441 LYS A N   
11406 C CA  . LYS D 425 ? 0.5734 0.6459 0.6425 -0.0782 0.0823  -0.1052 441 LYS A CA  
11407 C C   . LYS D 425 ? 0.6397 0.6977 0.7012 -0.0813 0.0750  -0.1016 441 LYS A C   
11408 O O   . LYS D 425 ? 0.6723 0.7198 0.7230 -0.0899 0.0754  -0.0990 441 LYS A O   
11409 C CB  . LYS D 425 ? 0.5666 0.6589 0.6489 -0.0729 0.0887  -0.1047 441 LYS A CB  
11410 C CG  . LYS D 425 ? 0.6223 0.7156 0.7018 -0.0795 0.0938  -0.1017 441 LYS A CG  
11411 C CD  . LYS D 425 ? 0.6840 0.7971 0.7769 -0.0751 0.1012  -0.1013 441 LYS A CD  
11412 C CE  . LYS D 425 ? 0.7355 0.8482 0.8234 -0.0833 0.1078  -0.0996 441 LYS A CE  
11413 N NZ  . LYS D 425 ? 0.9653 1.0969 1.0646 -0.0803 0.1172  -0.1001 441 LYS A NZ  
11414 N N   . GLN D 426 ? 0.6186 0.6761 0.6851 -0.0743 0.0682  -0.1014 442 GLN A N   
11415 C CA  . GLN D 426 ? 0.5812 0.6251 0.6406 -0.0765 0.0607  -0.0981 442 GLN A CA  
11416 C C   . GLN D 426 ? 0.5820 0.6070 0.6277 -0.0836 0.0566  -0.0975 442 GLN A C   
11417 O O   . GLN D 426 ? 0.6006 0.6158 0.6364 -0.0910 0.0559  -0.0943 442 GLN A O   
11418 C CB  . GLN D 426 ? 0.5945 0.6416 0.6618 -0.0670 0.0542  -0.0984 442 GLN A CB  
11419 C CG  . GLN D 426 ? 0.5857 0.6499 0.6658 -0.0611 0.0574  -0.0972 442 GLN A CG  
11420 C CD  . GLN D 426 ? 0.6417 0.7025 0.7188 -0.0658 0.0567  -0.0934 442 GLN A CD  
11421 O OE1 . GLN D 426 ? 0.6431 0.7054 0.7174 -0.0724 0.0624  -0.0925 442 GLN A OE1 
11422 N NE2 . GLN D 426 ? 0.6690 0.7266 0.7477 -0.0620 0.0498  -0.0913 442 GLN A NE2 
11423 N N   . ALA D 427 ? 0.6098 0.6302 0.6550 -0.0815 0.0542  -0.1004 443 ALA A N   
11424 C CA  . ALA D 427 ? 0.6496 0.6518 0.6833 -0.0877 0.0496  -0.0993 443 ALA A CA  
11425 C C   . ALA D 427 ? 0.6583 0.6559 0.6825 -0.0978 0.0551  -0.0976 443 ALA A C   
11426 O O   . ALA D 427 ? 0.6589 0.6416 0.6722 -0.1044 0.0516  -0.0946 443 ALA A O   
11427 C CB  . ALA D 427 ? 0.6470 0.6466 0.6839 -0.0833 0.0465  -0.1034 443 ALA A CB  
11428 N N   . LEU D 428 ? 0.6789 0.6894 0.7072 -0.0989 0.0637  -0.0993 444 LEU A N   
11429 C CA  . LEU D 428 ? 0.7029 0.7105 0.7224 -0.1082 0.0694  -0.0976 444 LEU A CA  
11430 C C   . LEU D 428 ? 0.7121 0.7147 0.7244 -0.1133 0.0687  -0.0933 444 LEU A C   
11431 O O   . LEU D 428 ? 0.6554 0.6479 0.6563 -0.1214 0.0688  -0.0905 444 LEU A O   
11432 C CB  . LEU D 428 ? 0.6914 0.7154 0.7179 -0.1072 0.0788  -0.1003 444 LEU A CB  
11433 C CG  . LEU D 428 ? 0.6916 0.7209 0.7228 -0.1044 0.0812  -0.1047 444 LEU A CG  
11434 C CD1 . LEU D 428 ? 0.6494 0.6960 0.6871 -0.1037 0.0911  -0.1065 444 LEU A CD1 
11435 C CD2 . LEU D 428 ? 0.6800 0.6942 0.7005 -0.1117 0.0788  -0.1040 444 LEU A CD2 
11436 N N   . THR D 429 ? 0.7169 0.7273 0.7362 -0.1087 0.0680  -0.0927 445 THR A N   
11437 C CA  . THR D 429 ? 0.7186 0.7252 0.7320 -0.1130 0.0671  -0.0893 445 THR A CA  
11438 C C   . THR D 429 ? 0.6788 0.6707 0.6846 -0.1140 0.0581  -0.0863 445 THR A C   
11439 O O   . THR D 429 ? 0.7107 0.6938 0.7059 -0.1205 0.0568  -0.0832 445 THR A O   
11440 C CB  . THR D 429 ? 0.7406 0.7612 0.7651 -0.1080 0.0697  -0.0897 445 THR A CB  
11441 O OG1 . THR D 429 ? 0.7423 0.7770 0.7741 -0.1073 0.0785  -0.0918 445 THR A OG1 
11442 C CG2 . THR D 429 ? 0.7307 0.7470 0.7490 -0.1130 0.0688  -0.0868 445 THR A CG2 
11443 N N   . ILE D 430 ? 0.6877 0.6774 0.6986 -0.1072 0.0520  -0.0872 446 ILE A N   
11444 C CA  . ILE D 430 ? 0.6833 0.6623 0.6900 -0.1059 0.0436  -0.0845 446 ILE A CA  
11445 C C   . ILE D 430 ? 0.7256 0.6888 0.7236 -0.1089 0.0383  -0.0832 446 ILE A C   
11446 O O   . ILE D 430 ? 0.7348 0.6863 0.7235 -0.1129 0.0336  -0.0795 446 ILE A O   
11447 C CB  . ILE D 430 ? 0.6218 0.6089 0.6402 -0.0961 0.0401  -0.0860 446 ILE A CB  
11448 C CG1 . ILE D 430 ? 0.6048 0.6066 0.6319 -0.0938 0.0446  -0.0861 446 ILE A CG1 
11449 C CG2 . ILE D 430 ? 0.6728 0.6485 0.6871 -0.0940 0.0310  -0.0836 446 ILE A CG2 
11450 C CD1 . ILE D 430 ? 0.5840 0.5987 0.6251 -0.0840 0.0441  -0.0880 446 ILE A CD1 
11451 N N   . VAL D 431 ? 0.7695 0.7325 0.7709 -0.1068 0.0388  -0.0863 447 VAL A N   
11452 C CA  . VAL D 431 ? 0.7410 0.6890 0.7354 -0.1098 0.0341  -0.0853 447 VAL A CA  
11453 C C   . VAL D 431 ? 0.6989 0.6410 0.6835 -0.1194 0.0381  -0.0830 447 VAL A C   
11454 O O   . VAL D 431 ? 0.6933 0.6220 0.6685 -0.1246 0.0341  -0.0790 447 VAL A O   
11455 C CB  . VAL D 431 ? 0.6042 0.5542 0.6065 -0.1037 0.0326  -0.0900 447 VAL A CB  
11456 C CG1 . VAL D 431 ? 0.5775 0.5118 0.5734 -0.1074 0.0279  -0.0889 447 VAL A CG1 
11457 C CG2 . VAL D 431 ? 0.6352 0.5892 0.6458 -0.0941 0.0274  -0.0915 447 VAL A CG2 
11458 N N   . GLY D 432 ? 0.6736 0.6261 0.6603 -0.1217 0.0462  -0.0851 448 GLY A N   
11459 C CA  . GLY D 432 ? 0.6995 0.6479 0.6769 -0.1306 0.0506  -0.0829 448 GLY A CA  
11460 C C   . GLY D 432 ? 0.7538 0.6936 0.7200 -0.1368 0.0485  -0.0776 448 GLY A C   
11461 O O   . GLY D 432 ? 0.7540 0.6822 0.7111 -0.1427 0.0462  -0.0740 448 GLY A O   
11462 N N   . THR D 433 ? 0.7449 0.6909 0.7123 -0.1352 0.0490  -0.0769 449 THR A N   
11463 C CA  . THR D 433 ? 0.7219 0.6620 0.6794 -0.1404 0.0471  -0.0725 449 THR A CA  
11464 C C   . THR D 433 ? 0.7511 0.6765 0.7016 -0.1414 0.0389  -0.0684 449 THR A C   
11465 O O   . THR D 433 ? 0.7555 0.6741 0.6956 -0.1472 0.0377  -0.0641 449 THR A O   
11466 C CB  . THR D 433 ? 0.6947 0.6443 0.6571 -0.1371 0.0479  -0.0733 449 THR A CB  
11467 O OG1 . THR D 433 ? 0.7598 0.7072 0.7128 -0.1429 0.0487  -0.0703 449 THR A OG1 
11468 C CG2 . THR D 433 ? 0.6647 0.6127 0.6330 -0.1300 0.0410  -0.0735 449 THR A CG2 
11469 N N   . LEU D 434 ? 0.7721 0.6930 0.7282 -0.1355 0.0331  -0.0696 450 LEU A N   
11470 C CA  . LEU D 434 ? 0.7750 0.6830 0.7257 -0.1353 0.0250  -0.0656 450 LEU A CA  
11471 C C   . LEU D 434 ? 0.7727 0.6683 0.7136 -0.1424 0.0237  -0.0613 450 LEU A C   
11472 O O   . LEU D 434 ? 0.7908 0.6795 0.7227 -0.1462 0.0207  -0.0563 450 LEU A O   
11473 C CB  . LEU D 434 ? 0.7439 0.6505 0.7033 -0.1271 0.0195  -0.0682 450 LEU A CB  
11474 C CG  . LEU D 434 ? 0.6972 0.6149 0.6653 -0.1199 0.0192  -0.0707 450 LEU A CG  
11475 C CD1 . LEU D 434 ? 0.6880 0.6038 0.6635 -0.1118 0.0134  -0.0727 450 LEU A CD1 
11476 C CD2 . LEU D 434 ? 0.6668 0.5835 0.6293 -0.1218 0.0170  -0.0671 450 LEU A CD2 
11477 N N   . PRO D 435 ? 0.7999 0.6925 0.7424 -0.1443 0.0256  -0.0628 451 PRO A N   
11478 C CA  . PRO D 435 ? 0.8083 0.6896 0.7418 -0.1516 0.0246  -0.0580 451 PRO A CA  
11479 C C   . PRO D 435 ? 0.7967 0.6814 0.7210 -0.1589 0.0299  -0.0547 451 PRO A C   
11480 O O   . PRO D 435 ? 0.8431 0.7193 0.7582 -0.1640 0.0275  -0.0488 451 PRO A O   
11481 C CB  . PRO D 435 ? 0.8171 0.6973 0.7563 -0.1515 0.0263  -0.0616 451 PRO A CB  
11482 C CG  . PRO D 435 ? 0.7806 0.6676 0.7309 -0.1429 0.0252  -0.0675 451 PRO A CG  
11483 C CD  . PRO D 435 ? 0.8072 0.7061 0.7595 -0.1400 0.0282  -0.0686 451 PRO A CD  
11484 N N   . PHE D 436 ? 0.7126 0.6099 0.6393 -0.1591 0.0370  -0.0581 452 PHE A N   
11485 C CA  . PHE D 436 ? 0.7218 0.6227 0.6396 -0.1655 0.0418  -0.0553 452 PHE A CA  
11486 C C   . PHE D 436 ? 0.8387 0.7359 0.7492 -0.1664 0.0376  -0.0511 452 PHE A C   
11487 O O   . PHE D 436 ? 0.8900 0.7819 0.7903 -0.1722 0.0371  -0.0459 452 PHE A O   
11488 C CB  . PHE D 436 ? 0.6861 0.6015 0.6090 -0.1644 0.0496  -0.0599 452 PHE A CB  
11489 C CG  . PHE D 436 ? 0.7023 0.6222 0.6167 -0.1701 0.0545  -0.0579 452 PHE A CG  
11490 C CD1 . PHE D 436 ? 0.7977 0.7211 0.7096 -0.1694 0.0535  -0.0572 452 PHE A CD1 
11491 C CD2 . PHE D 436 ? 0.7565 0.6759 0.6645 -0.1764 0.0592  -0.0560 452 PHE A CD2 
11492 C CE1 . PHE D 436 ? 0.7852 0.7127 0.6891 -0.1743 0.0576  -0.0557 452 PHE A CE1 
11493 C CE2 . PHE D 436 ? 0.7623 0.6859 0.6619 -0.1813 0.0635  -0.0540 452 PHE A CE2 
11494 C CZ  . PHE D 436 ? 0.7673 0.6950 0.6649 -0.1801 0.0626  -0.0540 452 PHE A CZ  
11495 N N   . THR D 437 ? 0.8598 0.7602 0.7758 -0.1604 0.0342  -0.0531 453 THR A N   
11496 C CA  . THR D 437 ? 0.7710 0.6702 0.6815 -0.1604 0.0305  -0.0502 453 THR A CA  
11497 C C   . THR D 437 ? 0.8202 0.7064 0.7237 -0.1621 0.0237  -0.0444 453 THR A C   
11498 O O   . THR D 437 ? 0.8814 0.7646 0.7750 -0.1665 0.0227  -0.0397 453 THR A O   
11499 C CB  . THR D 437 ? 0.7581 0.6636 0.6778 -0.1532 0.0282  -0.0538 453 THR A CB  
11500 O OG1 . THR D 437 ? 0.7422 0.6605 0.6686 -0.1519 0.0347  -0.0584 453 THR A OG1 
11501 C CG2 . THR D 437 ? 0.8176 0.7211 0.7320 -0.1529 0.0234  -0.0509 453 THR A CG2 
11502 N N   . TYR D 438 ? 0.8043 0.6833 0.7132 -0.1580 0.0187  -0.0448 454 TYR A N   
11503 C CA  . TYR D 438 ? 0.8418 0.7080 0.7452 -0.1593 0.0122  -0.0391 454 TYR A CA  
11504 C C   . TYR D 438 ? 0.8527 0.7134 0.7468 -0.1670 0.0142  -0.0338 454 TYR A C   
11505 O O   . TYR D 438 ? 0.8802 0.7351 0.7660 -0.1699 0.0109  -0.0278 454 TYR A O   
11506 C CB  . TYR D 438 ? 0.8519 0.7107 0.7630 -0.1543 0.0074  -0.0408 454 TYR A CB  
11507 C CG  . TYR D 438 ? 0.9128 0.7577 0.8186 -0.1575 0.0023  -0.0347 454 TYR A CG  
11508 C CD1 . TYR D 438 ? 0.9306 0.7698 0.8287 -0.1588 -0.0022 -0.0286 454 TYR A CD1 
11509 C CD2 . TYR D 438 ? 0.9618 0.7993 0.8709 -0.1589 0.0019  -0.0350 454 TYR A CD2 
11510 C CE1 . TYR D 438 ? 0.9764 0.8034 0.8700 -0.1617 -0.0065 -0.0222 454 TYR A CE1 
11511 C CE2 . TYR D 438 ? 1.0046 0.8290 0.9096 -0.1620 -0.0028 -0.0289 454 TYR A CE2 
11512 C CZ  . TYR D 438 ? 1.0110 0.8303 0.9084 -0.1634 -0.0069 -0.0222 454 TYR A CZ  
11513 O OH  . TYR D 438 ? 1.0173 0.8242 0.9114 -0.1663 -0.0114 -0.0155 454 TYR A OH  
11514 N N   . MET D 439 ? 0.8266 0.6903 0.7220 -0.1705 0.0199  -0.0358 455 MET A N   
11515 C CA  . MET D 439 ? 0.8683 0.7271 0.7555 -0.1779 0.0219  -0.0305 455 MET A CA  
11516 C C   . MET D 439 ? 0.8737 0.7380 0.7508 -0.1822 0.0247  -0.0271 455 MET A C   
11517 O O   . MET D 439 ? 0.8611 0.7196 0.7295 -0.1863 0.0224  -0.0203 455 MET A O   
11518 C CB  . MET D 439 ? 0.8174 0.6794 0.7088 -0.1802 0.0276  -0.0340 455 MET A CB  
11519 C CG  . MET D 439 ? 0.8210 0.6786 0.7058 -0.1879 0.0302  -0.0291 455 MET A CG  
11520 S SD  . MET D 439 ? 0.9074 0.7731 0.7805 -0.1943 0.0364  -0.0255 455 MET A SD  
11521 C CE  . MET D 439 ? 0.8990 0.7779 0.7786 -0.1929 0.0448  -0.0335 455 MET A CE  
11522 N N   . LEU D 440 ? 0.8169 0.6929 0.6952 -0.1813 0.0298  -0.0317 456 LEU A N   
11523 C CA  . LEU D 440 ? 0.8387 0.7202 0.7076 -0.1851 0.0326  -0.0293 456 LEU A CA  
11524 C C   . LEU D 440 ? 0.9023 0.7794 0.7653 -0.1841 0.0263  -0.0248 456 LEU A C   
11525 O O   . LEU D 440 ? 0.9484 0.8234 0.8015 -0.1884 0.0257  -0.0190 456 LEU A O   
11526 C CB  . LEU D 440 ? 0.8061 0.7001 0.6790 -0.1833 0.0381  -0.0354 456 LEU A CB  
11527 C CG  . LEU D 440 ? 0.7947 0.6957 0.6589 -0.1869 0.0416  -0.0344 456 LEU A CG  
11528 C CD1 . LEU D 440 ? 0.7891 0.7010 0.6582 -0.1868 0.0490  -0.0400 456 LEU A CD1 
11529 C CD2 . LEU D 440 ? 0.7788 0.6812 0.6415 -0.1838 0.0369  -0.0343 456 LEU A CD2 
11530 N N   . GLU D 441 ? 0.9162 0.7928 0.7853 -0.1781 0.0217  -0.0273 457 GLU A N   
11531 C CA  . GLU D 441 ? 0.9025 0.7756 0.7662 -0.1768 0.0157  -0.0233 457 GLU A CA  
11532 C C   . GLU D 441 ? 0.9021 0.7637 0.7600 -0.1794 0.0112  -0.0158 457 GLU A C   
11533 O O   . GLU D 441 ? 0.9088 0.7690 0.7582 -0.1813 0.0085  -0.0103 457 GLU A O   
11534 C CB  . GLU D 441 ? 0.9107 0.7848 0.7826 -0.1698 0.0114  -0.0270 457 GLU A CB  
11535 C CG  . GLU D 441 ? 0.8908 0.7652 0.7571 -0.1684 0.0066  -0.0243 457 GLU A CG  
11536 C CD  . GLU D 441 ? 0.8821 0.7672 0.7456 -0.1693 0.0099  -0.0272 457 GLU A CD  
11537 O OE1 . GLU D 441 ? 0.8621 0.7514 0.7198 -0.1742 0.0150  -0.0268 457 GLU A OE1 
11538 O OE2 . GLU D 441 ? 0.9601 0.8492 0.8267 -0.1653 0.0069  -0.0295 457 GLU A OE2 
11539 N N   . LYS D 442 ? 0.9325 0.7864 0.7955 -0.1796 0.0103  -0.0153 458 LYS A N   
11540 C CA  . LYS D 442 ? 0.9847 0.8272 0.8438 -0.1822 0.0060  -0.0079 458 LYS A CA  
11541 C C   . LYS D 442 ? 0.9716 0.8148 0.8207 -0.1891 0.0091  -0.0019 458 LYS A C   
11542 O O   . LYS D 442 ? 0.9763 0.8150 0.8183 -0.1911 0.0056  0.0055  458 LYS A O   
11543 C CB  . LYS D 442 ? 1.0077 0.8424 0.8750 -0.1812 0.0049  -0.0096 458 LYS A CB  
11544 C CG  . LYS D 442 ? 1.1304 0.9522 0.9972 -0.1811 -0.0017 -0.0033 458 LYS A CG  
11545 C CD  . LYS D 442 ? 1.1419 0.9549 1.0155 -0.1819 -0.0026 -0.0039 458 LYS A CD  
11546 C CE  . LYS D 442 ? 1.2701 1.0703 1.1440 -0.1806 -0.0100 0.0021  458 LYS A CE  
11547 N NZ  . LYS D 442 ? 1.2375 1.0377 1.1018 -0.1824 -0.0123 0.0097  458 LYS A NZ  
11548 N N   . TRP D 443 ? 0.9900 0.8397 0.8386 -0.1926 0.0158  -0.0046 459 TRP A N   
11549 C CA  . TRP D 443 ? 0.9977 0.8497 0.8369 -0.1990 0.0194  0.0007  459 TRP A CA  
11550 C C   . TRP D 443 ? 0.9859 0.8436 0.8157 -0.1992 0.0183  0.0037  459 TRP A C   
11551 O O   . TRP D 443 ? 0.9970 0.8523 0.8186 -0.2026 0.0168  0.0114  459 TRP A O   
11552 C CB  . TRP D 443 ? 0.9532 0.8128 0.7939 -0.2018 0.0270  -0.0040 459 TRP A CB  
11553 C CG  . TRP D 443 ? 0.9748 0.8375 0.8061 -0.2080 0.0310  0.0011  459 TRP A CG  
11554 C CD1 . TRP D 443 ? 0.9885 0.8461 0.8177 -0.2132 0.0323  0.0064  459 TRP A CD1 
11555 C CD2 . TRP D 443 ? 0.9926 0.8646 0.8151 -0.2097 0.0341  0.0017  459 TRP A CD2 
11556 N NE1 . TRP D 443 ? 0.9670 0.8307 0.7862 -0.2180 0.0362  0.0106  459 TRP A NE1 
11557 C CE2 . TRP D 443 ? 0.9925 0.8651 0.8073 -0.2158 0.0374  0.0076  459 TRP A CE2 
11558 C CE3 . TRP D 443 ? 0.9790 0.8590 0.7996 -0.2066 0.0343  -0.0024 459 TRP A CE3 
11559 C CZ2 . TRP D 443 ? 1.0302 0.9115 0.8351 -0.2184 0.0408  0.0094  459 TRP A CZ2 
11560 C CZ3 . TRP D 443 ? 0.9734 0.8615 0.7847 -0.2094 0.0375  -0.0010 459 TRP A CZ3 
11561 C CH2 . TRP D 443 ? 1.0097 0.8985 0.8129 -0.2151 0.0408  0.0048  459 TRP A CH2 
11562 N N   . ARG D 444 ? 0.9382 0.8037 0.7699 -0.1953 0.0188  -0.0022 460 ARG A N   
11563 C CA  . ARG D 444 ? 0.9053 0.7767 0.7289 -0.1950 0.0174  -0.0005 460 ARG A CA  
11564 C C   . ARG D 444 ? 0.9612 0.8257 0.7816 -0.1930 0.0101  0.0056  460 ARG A C   
11565 O O   . ARG D 444 ? 0.9910 0.8577 0.8021 -0.1950 0.0088  0.0111  460 ARG A O   
11566 C CB  . ARG D 444 ? 0.8494 0.7295 0.6775 -0.1910 0.0188  -0.0083 460 ARG A CB  
11567 C CG  . ARG D 444 ? 0.8669 0.7568 0.6948 -0.1932 0.0259  -0.0132 460 ARG A CG  
11568 C CD  . ARG D 444 ? 0.9043 0.7993 0.7417 -0.1879 0.0259  -0.0207 460 ARG A CD  
11569 N NE  . ARG D 444 ? 0.9327 0.8384 0.7689 -0.1880 0.0296  -0.0253 460 ARG A NE  
11570 C CZ  . ARG D 444 ? 0.8618 0.7730 0.7058 -0.1836 0.0292  -0.0311 460 ARG A CZ  
11571 N NH1 . ARG D 444 ? 0.8662 0.7740 0.7190 -0.1787 0.0252  -0.0328 460 ARG A NH1 
11572 N NH2 . ARG D 444 ? 0.8548 0.7753 0.6979 -0.1841 0.0327  -0.0352 460 ARG A NH2 
11573 N N   . TRP D 445 ? 0.9654 0.8227 0.7934 -0.1887 0.0053  0.0045  461 TRP A N   
11574 C CA  . TRP D 445 ? 0.9670 0.8181 0.7922 -0.1865 -0.0014 0.0103  461 TRP A CA  
11575 C C   . TRP D 445 ? 1.0502 0.8944 0.8692 -0.1910 -0.0026 0.0197  461 TRP A C   
11576 O O   . TRP D 445 ? 1.0976 0.9410 0.9099 -0.1911 -0.0063 0.0261  461 TRP A O   
11577 C CB  . TRP D 445 ? 0.9385 0.7822 0.7731 -0.1811 -0.0061 0.0078  461 TRP A CB  
11578 C CG  . TRP D 445 ? 0.8855 0.7355 0.7259 -0.1759 -0.0066 0.0006  461 TRP A CG  
11579 C CD1 . TRP D 445 ? 0.9061 0.7664 0.7439 -0.1751 -0.0049 -0.0030 461 TRP A CD1 
11580 C CD2 . TRP D 445 ? 0.8730 0.7199 0.7237 -0.1704 -0.0091 -0.0042 461 TRP A CD2 
11581 N NE1 . TRP D 445 ? 0.8912 0.7550 0.7376 -0.1697 -0.0060 -0.0094 461 TRP A NE1 
11582 C CE2 . TRP D 445 ? 0.8680 0.7241 0.7222 -0.1666 -0.0086 -0.0100 461 TRP A CE2 
11583 C CE3 . TRP D 445 ? 0.8648 0.7025 0.7225 -0.1682 -0.0119 -0.0041 461 TRP A CE3 
11584 C CZ2 . TRP D 445 ? 0.8607 0.7175 0.7249 -0.1606 -0.0105 -0.0152 461 TRP A CZ2 
11585 C CZ3 . TRP D 445 ? 0.8794 0.7178 0.7465 -0.1620 -0.0139 -0.0097 461 TRP A CZ3 
11586 C CH2 . TRP D 445 ? 0.8515 0.6997 0.7217 -0.1582 -0.0132 -0.0149 461 TRP A CH2 
11587 N N   . MET D 446 ? 1.0411 0.8805 0.8628 -0.1948 0.0003  0.0210  462 MET A N   
11588 C CA  . MET D 446 ? 1.0977 0.9314 0.9140 -0.1997 -0.0004 0.0304  462 MET A CA  
11589 C C   . MET D 446 ? 1.1431 0.9858 0.9485 -0.2040 0.0033  0.0345  462 MET A C   
11590 O O   . MET D 446 ? 1.1550 0.9969 0.9535 -0.2054 0.0007  0.0429  462 MET A O   
11591 C CB  . MET D 446 ? 1.1093 0.9358 0.9317 -0.2029 0.0016  0.0307  462 MET A CB  
11592 C CG  . MET D 446 ? 1.1896 1.0054 1.0220 -0.1993 -0.0031 0.0288  462 MET A CG  
11593 S SD  . MET D 446 ? 1.2333 1.0414 1.0719 -0.2038 -0.0007 0.0294  462 MET A SD  
11594 C CE  . MET D 446 ? 1.2355 1.0493 1.0834 -0.1997 0.0028  0.0169  462 MET A CE  
11595 N N   . VAL D 447 ? 1.1416 0.9932 0.9455 -0.2059 0.0095  0.0291  463 VAL A N   
11596 C CA  . VAL D 447 ? 1.1466 1.0075 0.9399 -0.2094 0.0130  0.0323  463 VAL A CA  
11597 C C   . VAL D 447 ? 1.1465 1.0117 0.9330 -0.2066 0.0089  0.0350  463 VAL A C   
11598 O O   . VAL D 447 ? 1.2180 1.0856 0.9958 -0.2089 0.0080  0.0427  463 VAL A O   
11599 C CB  . VAL D 447 ? 1.0416 0.9121 0.8350 -0.2104 0.0197  0.0244  463 VAL A CB  
11600 C CG1 . VAL D 447 ? 1.0892 0.9704 0.8715 -0.2125 0.0226  0.0261  463 VAL A CG1 
11601 C CG2 . VAL D 447 ? 1.0293 0.8966 0.8272 -0.2142 0.0243  0.0237  463 VAL A CG2 
11602 N N   . PHE D 448 ? 1.1299 0.9961 0.9208 -0.2014 0.0059  0.0291  464 PHE A N   
11603 C CA  . PHE D 448 ? 1.1723 1.0432 0.9574 -0.1984 0.0018  0.0307  464 PHE A CA  
11604 C C   . PHE D 448 ? 1.2323 1.0954 1.0152 -0.1978 -0.0040 0.0400  464 PHE A C   
11605 O O   . PHE D 448 ? 1.2808 1.1486 1.0552 -0.1978 -0.0060 0.0456  464 PHE A O   
11606 C CB  . PHE D 448 ? 1.1270 1.0010 0.9184 -0.1932 0.0002  0.0220  464 PHE A CB  
11607 C CG  . PHE D 448 ? 1.0081 0.8911 0.8012 -0.1936 0.0057  0.0136  464 PHE A CG  
11608 C CD1 . PHE D 448 ? 1.0199 0.9112 0.8048 -0.1972 0.0102  0.0141  464 PHE A CD1 
11609 C CD2 . PHE D 448 ? 0.9528 0.8366 0.7558 -0.1900 0.0062  0.0054  464 PHE A CD2 
11610 C CE1 . PHE D 448 ? 0.9602 0.8598 0.7468 -0.1975 0.0153  0.0065  464 PHE A CE1 
11611 C CE2 . PHE D 448 ? 0.9571 0.8496 0.7624 -0.1903 0.0114  -0.0019 464 PHE A CE2 
11612 C CZ  . PHE D 448 ? 0.9369 0.8370 0.7340 -0.1941 0.0160  -0.0015 464 PHE A CZ  
11613 N N   . LYS D 449 ? 1.2469 1.0985 1.0376 -0.1967 -0.0070 0.0417  465 LYS A N   
11614 C CA  . LYS D 449 ? 1.2034 1.0468 0.9931 -0.1963 -0.0123 0.0509  465 LYS A CA  
11615 C C   . LYS D 449 ? 1.2326 1.0746 1.0167 -0.2018 -0.0105 0.0605  465 LYS A C   
11616 O O   . LYS D 449 ? 1.2821 1.1195 1.0639 -0.2019 -0.0143 0.0696  465 LYS A O   
11617 C CB  . LYS D 449 ? 1.1785 1.0096 0.9786 -0.1936 -0.0159 0.0494  465 LYS A CB  
11618 C CG  . LYS D 449 ? 1.2203 1.0431 1.0209 -0.1909 -0.0225 0.0568  465 LYS A CG  
11619 C CD  . LYS D 449 ? 1.2953 1.1084 1.1064 -0.1864 -0.0264 0.0524  465 LYS A CD  
11620 C CE  . LYS D 449 ? 1.3003 1.1197 1.1152 -0.1814 -0.0263 0.0422  465 LYS A CE  
11621 N NZ  . LYS D 449 ? 1.1440 0.9550 0.9675 -0.1760 -0.0311 0.0394  465 LYS A NZ  
11622 N N   . GLY D 450 ? 1.2941 1.1403 1.0764 -0.2063 -0.0047 0.0590  466 GLY A N   
11623 C CA  . GLY D 450 ? 1.2930 1.1392 1.0701 -0.2117 -0.0025 0.0681  466 GLY A CA  
11624 C C   . GLY D 450 ? 1.2170 1.0519 1.0012 -0.2151 -0.0025 0.0717  466 GLY A C   
11625 O O   . GLY D 450 ? 1.2197 1.0525 1.0010 -0.2192 -0.0024 0.0813  466 GLY A O   
11626 N N   . GLU D 451 ? 1.1822 1.0103 0.9763 -0.2134 -0.0027 0.0644  467 GLU A N   
11627 C CA  . GLU D 451 ? 1.1904 1.0074 0.9923 -0.2161 -0.0032 0.0669  467 GLU A CA  
11628 C C   . GLU D 451 ? 1.1508 0.9709 0.9535 -0.2209 0.0031  0.0638  467 GLU A C   
11629 O O   . GLU D 451 ? 1.1190 0.9311 0.9293 -0.2228 0.0032  0.0632  467 GLU A O   
11630 C CB  . GLU D 451 ? 1.2060 1.0137 1.0182 -0.2112 -0.0074 0.0610  467 GLU A CB  
11631 C CG  . GLU D 451 ? 1.2386 1.0416 1.0503 -0.2070 -0.0140 0.0658  467 GLU A CG  
11632 C CD  . GLU D 451 ? 1.2520 1.0478 1.0727 -0.2012 -0.0182 0.0593  467 GLU A CD  
11633 O OE1 . GLU D 451 ? 1.2708 1.0655 1.0986 -0.2003 -0.0161 0.0511  467 GLU A OE1 
11634 O OE2 . GLU D 451 ? 1.2193 1.0114 1.0397 -0.1973 -0.0235 0.0625  467 GLU A OE2 
11635 N N   . ILE D 452 ? 1.1611 0.9930 0.9560 -0.2227 0.0082  0.0618  468 ILE A N   
11636 C CA  . ILE D 452 ? 1.1595 0.9956 0.9538 -0.2273 0.0146  0.0597  468 ILE A CA  
11637 C C   . ILE D 452 ? 1.1780 1.0248 0.9605 -0.2305 0.0179  0.0653  468 ILE A C   
11638 O O   . ILE D 452 ? 1.1915 1.0480 0.9679 -0.2281 0.0192  0.0614  468 ILE A O   
11639 C CB  . ILE D 452 ? 1.1984 1.0388 0.9984 -0.2248 0.0183  0.0476  468 ILE A CB  
11640 C CG1 . ILE D 452 ? 1.1739 1.0046 0.9853 -0.2206 0.0143  0.0426  468 ILE A CG1 
11641 C CG2 . ILE D 452 ? 1.2097 1.0543 1.0096 -0.2294 0.0251  0.0455  468 ILE A CG2 
11642 C CD1 . ILE D 452 ? 1.1420 0.9771 0.9599 -0.2173 0.0174  0.0315  468 ILE A CD1 
11643 N N   . PRO D 453 ? 1.2090 1.0545 0.9882 -0.2357 0.0190  0.0745  469 PRO A N   
11644 C CA  . PRO D 453 ? 1.2484 1.1051 1.0161 -0.2386 0.0226  0.0797  469 PRO A CA  
11645 C C   . PRO D 453 ? 1.3154 1.1812 1.0806 -0.2400 0.0295  0.0718  469 PRO A C   
11646 O O   . PRO D 453 ? 1.3076 1.1703 1.0801 -0.2408 0.0323  0.0653  469 PRO A O   
11647 C CB  . PRO D 453 ? 1.2690 1.1209 1.0364 -0.2439 0.0222  0.0914  469 PRO A CB  
11648 C CG  . PRO D 453 ? 1.2832 1.1208 1.0609 -0.2429 0.0168  0.0935  469 PRO A CG  
11649 C CD  . PRO D 453 ? 1.2475 1.0812 1.0333 -0.2386 0.0162  0.0816  469 PRO A CD  
11650 N N   . LYS D 454 ? 1.3565 1.2342 1.1112 -0.2402 0.0322  0.0725  470 LYS A N   
11651 C CA  . LYS D 454 ? 1.3740 1.2615 1.1253 -0.2409 0.0387  0.0649  470 LYS A CA  
11652 C C   . LYS D 454 ? 1.3503 1.2359 1.1054 -0.2457 0.0438  0.0644  470 LYS A C   
11653 O O   . LYS D 454 ? 1.3322 1.2190 1.0926 -0.2450 0.0476  0.0554  470 LYS A O   
11654 C CB  . LYS D 454 ? 1.3876 1.2874 1.1262 -0.2413 0.0403  0.0687  470 LYS A CB  
11655 C CG  . LYS D 454 ? 1.3468 1.2533 1.0819 -0.2360 0.0382  0.0626  470 LYS A CG  
11656 C CD  . LYS D 454 ? 1.3763 1.2936 1.0990 -0.2358 0.0378  0.0683  470 LYS A CD  
11657 C CE  . LYS D 454 ? 1.3635 1.2898 1.0783 -0.2398 0.0440  0.0702  470 LYS A CE  
11658 N NZ  . LYS D 454 ? 1.3459 1.2844 1.0487 -0.2384 0.0438  0.0732  470 LYS A NZ  
11659 N N   . ASP D 455 ? 1.3248 1.2073 1.0780 -0.2504 0.0437  0.0744  471 ASP A N   
11660 C CA  . ASP D 455 ? 1.3922 1.2732 1.1483 -0.2555 0.0484  0.0752  471 ASP A CA  
11661 C C   . ASP D 455 ? 1.3873 1.2583 1.1562 -0.2552 0.0477  0.0690  471 ASP A C   
11662 O O   . ASP D 455 ? 1.3963 1.2669 1.1684 -0.2590 0.0518  0.0679  471 ASP A O   
11663 C CB  . ASP D 455 ? 1.4896 1.3688 1.2418 -0.2605 0.0473  0.0883  471 ASP A CB  
11664 C CG  . ASP D 455 ? 1.4337 1.3006 1.1931 -0.2601 0.0406  0.0949  471 ASP A CG  
11665 O OD1 . ASP D 455 ? 1.4040 1.2641 1.1699 -0.2556 0.0364  0.0894  471 ASP A OD1 
11666 O OD2 . ASP D 455 ? 1.4042 1.2678 1.1631 -0.2642 0.0394  0.1057  471 ASP A OD2 
11667 N N   . GLN D 456 ? 1.3006 1.1641 1.0768 -0.2506 0.0426  0.0650  472 GLN A N   
11668 C CA  . GLN D 456 ? 1.2632 1.1184 1.0513 -0.2494 0.0419  0.0584  472 GLN A CA  
11669 C C   . GLN D 456 ? 1.2292 1.0880 1.0214 -0.2438 0.0427  0.0469  472 GLN A C   
11670 O O   . GLN D 456 ? 1.2023 1.0554 1.0046 -0.2416 0.0418  0.0407  472 GLN A O   
11671 C CB  . GLN D 456 ? 1.2677 1.1096 1.0628 -0.2488 0.0349  0.0637  472 GLN A CB  
11672 C CG  . GLN D 456 ? 1.3411 1.1787 1.1341 -0.2543 0.0338  0.0755  472 GLN A CG  
11673 C CD  . GLN D 456 ? 1.3502 1.1735 1.1524 -0.2540 0.0273  0.0798  472 GLN A CD  
11674 O OE1 . GLN D 456 ? 1.3325 1.1484 1.1433 -0.2563 0.0272  0.0785  472 GLN A OE1 
11675 N NE2 . GLN D 456 ? 1.3022 1.1220 1.1028 -0.2509 0.0218  0.0849  472 GLN A NE2 
11676 N N   . TRP D 457 ? 1.2159 1.0842 1.0011 -0.2414 0.0443  0.0441  473 TRP A N   
11677 C CA  . TRP D 457 ? 1.1828 1.0553 0.9723 -0.2362 0.0451  0.0339  473 TRP A CA  
11678 C C   . TRP D 457 ? 1.1581 1.0308 0.9566 -0.2361 0.0493  0.0260  473 TRP A C   
11679 O O   . TRP D 457 ? 1.1256 0.9915 0.9339 -0.2328 0.0464  0.0218  473 TRP A O   
11680 C CB  . TRP D 457 ? 1.1765 1.0611 0.9570 -0.2355 0.0483  0.0317  473 TRP A CB  
11681 C CG  . TRP D 457 ? 1.1893 1.0744 0.9651 -0.2321 0.0429  0.0343  473 TRP A CG  
11682 C CD1 . TRP D 457 ? 1.1901 1.0667 0.9673 -0.2306 0.0363  0.0400  473 TRP A CD1 
11683 C CD2 . TRP D 457 ? 1.1467 1.0415 0.9163 -0.2296 0.0436  0.0308  473 TRP A CD2 
11684 N NE1 . TRP D 457 ? 1.1875 1.0684 0.9593 -0.2273 0.0329  0.0406  473 TRP A NE1 
11685 C CE2 . TRP D 457 ? 1.1753 1.0673 0.9424 -0.2266 0.0372  0.0348  473 TRP A CE2 
11686 C CE3 . TRP D 457 ? 1.1390 1.0444 0.9050 -0.2294 0.0489  0.0247  473 TRP A CE3 
11687 C CZ2 . TRP D 457 ? 1.1960 1.0959 0.9573 -0.2236 0.0358  0.0325  473 TRP A CZ2 
11688 C CZ3 . TRP D 457 ? 1.1519 1.0645 0.9125 -0.2265 0.0474  0.0223  473 TRP A CZ3 
11689 C CH2 . TRP D 457 ? 1.1910 1.1010 0.9492 -0.2236 0.0408  0.0260  473 TRP A CH2 
11690 N N   . MET D 458 ? 1.1881 1.0686 0.9831 -0.2395 0.0562  0.0244  474 MET A N   
11691 C CA  . MET D 458 ? 1.1354 1.0177 0.9383 -0.2394 0.0609  0.0171  474 MET A CA  
11692 C C   . MET D 458 ? 1.1323 1.0041 0.9436 -0.2408 0.0582  0.0188  474 MET A C   
11693 O O   . MET D 458 ? 1.1211 0.9907 0.9423 -0.2376 0.0580  0.0119  474 MET A O   
11694 C CB  . MET D 458 ? 1.0320 0.9241 0.8285 -0.2435 0.0686  0.0170  474 MET A CB  
11695 C CG  . MET D 458 ? 1.1041 1.0064 0.8938 -0.2415 0.0712  0.0138  474 MET A CG  
11696 S SD  . MET D 458 ? 1.0373 0.9415 0.8357 -0.2341 0.0693  0.0040  474 MET A SD  
11697 C CE  . MET D 458 ? 1.0447 0.9491 0.8554 -0.2329 0.0735  -0.0034 474 MET A CE  
11698 N N   . LYS D 459 ? 1.1915 1.0566 0.9994 -0.2451 0.0554  0.0280  475 LYS A N   
11699 C CA  . LYS D 459 ? 1.1971 1.0516 1.0134 -0.2468 0.0524  0.0298  475 LYS A CA  
11700 C C   . LYS D 459 ? 1.1460 0.9917 0.9714 -0.2413 0.0460  0.0261  475 LYS A C   
11701 O O   . LYS D 459 ? 1.1089 0.9493 0.9440 -0.2400 0.0451  0.0214  475 LYS A O   
11702 C CB  . LYS D 459 ? 1.2298 1.0787 1.0412 -0.2523 0.0500  0.0413  475 LYS A CB  
11703 C CG  . LYS D 459 ? 1.1411 0.9789 0.9616 -0.2548 0.0470  0.0436  475 LYS A CG  
11704 C CD  . LYS D 459 ? 1.2214 1.0535 1.0377 -0.2595 0.0438  0.0560  475 LYS A CD  
11705 C CE  . LYS D 459 ? 1.2185 1.0377 1.0449 -0.2617 0.0395  0.0589  475 LYS A CE  
11706 N NZ  . LYS D 459 ? 1.2346 1.0468 1.0589 -0.2648 0.0348  0.0713  475 LYS A NZ  
11707 N N   . LYS D 460 ? 1.1188 0.9631 0.9412 -0.2377 0.0414  0.0279  476 LYS A N   
11708 C CA  . LYS D 460 ? 1.1354 0.9725 0.9662 -0.2318 0.0356  0.0238  476 LYS A CA  
11709 C C   . LYS D 460 ? 1.1178 0.9616 0.9545 -0.2267 0.0384  0.0130  476 LYS A C   
11710 O O   . LYS D 460 ? 1.0976 0.9365 0.9442 -0.2229 0.0359  0.0076  476 LYS A O   
11711 C CB  . LYS D 460 ? 1.2495 1.0835 1.0754 -0.2294 0.0299  0.0291  476 LYS A CB  
11712 C CG  . LYS D 460 ? 1.3048 1.1259 1.1338 -0.2299 0.0231  0.0365  476 LYS A CG  
11713 C CD  . LYS D 460 ? 1.2233 1.0354 1.0643 -0.2260 0.0193  0.0308  476 LYS A CD  
11714 C CE  . LYS D 460 ? 1.2238 1.0276 1.0662 -0.2217 0.0117  0.0342  476 LYS A CE  
11715 N NZ  . LYS D 460 ? 1.1319 0.9278 0.9851 -0.2164 0.0072  0.0284  476 LYS A NZ  
11716 N N   . TRP D 461 ? 1.2032 1.0584 1.0345 -0.2265 0.0435  0.0097  477 TRP A N   
11717 C CA  . TRP D 461 ? 1.1203 0.9829 0.9578 -0.2215 0.0463  0.0001  477 TRP A CA  
11718 C C   . TRP D 461 ? 1.1066 0.9679 0.9541 -0.2208 0.0484  -0.0054 477 TRP A C   
11719 O O   . TRP D 461 ? 1.1239 0.9814 0.9805 -0.2156 0.0450  -0.0102 477 TRP A O   
11720 C CB  . TRP D 461 ? 1.0701 0.9452 0.9009 -0.2228 0.0527  -0.0022 477 TRP A CB  
11721 C CG  . TRP D 461 ? 1.0551 0.9387 0.8928 -0.2182 0.0565  -0.0114 477 TRP A CG  
11722 C CD1 . TRP D 461 ? 1.0631 0.9539 0.9048 -0.2190 0.0632  -0.0165 477 TRP A CD1 
11723 C CD2 . TRP D 461 ? 1.0535 0.9396 0.8960 -0.2121 0.0538  -0.0163 477 TRP A CD2 
11724 N NE1 . TRP D 461 ? 1.0885 0.9865 0.9371 -0.2137 0.0650  -0.0239 477 TRP A NE1 
11725 C CE2 . TRP D 461 ? 1.0213 0.9165 0.8707 -0.2095 0.0592  -0.0239 477 TRP A CE2 
11726 C CE3 . TRP D 461 ? 1.0351 0.9172 0.8769 -0.2085 0.0473  -0.0147 477 TRP A CE3 
11727 C CZ2 . TRP D 461 ? 0.9493 0.8494 0.8053 -0.2036 0.0584  -0.0296 477 TRP A CZ2 
11728 C CZ3 . TRP D 461 ? 0.9893 0.8762 0.8372 -0.2028 0.0464  -0.0207 477 TRP A CZ3 
11729 C CH2 . TRP D 461 ? 0.9716 0.8674 0.8267 -0.2004 0.0519  -0.0279 477 TRP A CH2 
11730 N N   . TRP D 462 ? 1.0913 0.9550 0.9368 -0.2260 0.0536  -0.0042 478 TRP A N   
11731 C CA  . TRP D 462 ? 1.0328 0.8972 0.8872 -0.2255 0.0565  -0.0099 478 TRP A CA  
11732 C C   . TRP D 462 ? 0.9937 0.8460 0.8560 -0.2244 0.0502  -0.0092 478 TRP A C   
11733 O O   . TRP D 462 ? 0.9704 0.8228 0.8424 -0.2202 0.0499  -0.0162 478 TRP A O   
11734 C CB  . TRP D 462 ? 0.9908 0.8616 0.8405 -0.2315 0.0636  -0.0085 478 TRP A CB  
11735 C CG  . TRP D 462 ? 0.9677 0.8516 0.8138 -0.2303 0.0702  -0.0129 478 TRP A CG  
11736 C CD1 . TRP D 462 ? 0.9768 0.8672 0.8125 -0.2335 0.0737  -0.0093 478 TRP A CD1 
11737 C CD2 . TRP D 462 ? 0.8999 0.7921 0.7537 -0.2253 0.0738  -0.0217 478 TRP A CD2 
11738 N NE1 . TRP D 462 ? 0.9269 0.8285 0.7634 -0.2309 0.0793  -0.0156 478 TRP A NE1 
11739 C CE2 . TRP D 462 ? 0.9123 0.8153 0.7601 -0.2259 0.0796  -0.0229 478 TRP A CE2 
11740 C CE3 . TRP D 462 ? 0.9050 0.7973 0.7705 -0.2200 0.0728  -0.0285 478 TRP A CE3 
11741 C CZ2 . TRP D 462 ? 0.9148 0.8280 0.7685 -0.2218 0.0844  -0.0303 478 TRP A CZ2 
11742 C CZ3 . TRP D 462 ? 0.8791 0.7823 0.7500 -0.2157 0.0776  -0.0355 478 TRP A CZ3 
11743 C CH2 . TRP D 462 ? 0.9043 0.8177 0.7697 -0.2168 0.0834  -0.0362 478 TRP A CH2 
11744 N N   . GLU D 463 ? 1.0217 0.8637 0.8805 -0.2273 0.0449  -0.0011 479 GLU A N   
11745 C CA  . GLU D 463 ? 1.0011 0.8309 0.8683 -0.2259 0.0386  -0.0007 479 GLU A CA  
11746 C C   . GLU D 463 ? 1.0147 0.8433 0.8893 -0.2179 0.0345  -0.0073 479 GLU A C   
11747 O O   . GLU D 463 ? 1.0095 0.8348 0.8938 -0.2146 0.0328  -0.0130 479 GLU A O   
11748 C CB  . GLU D 463 ? 1.0314 0.8508 0.8941 -0.2295 0.0333  0.0095  479 GLU A CB  
11749 C CG  . GLU D 463 ? 1.1246 0.9435 0.9824 -0.2373 0.0363  0.0166  479 GLU A CG  
11750 C CD  . GLU D 463 ? 1.2238 1.0332 1.0780 -0.2407 0.0311  0.0275  479 GLU A CD  
11751 O OE1 . GLU D 463 ? 1.2734 1.0772 1.1276 -0.2370 0.0254  0.0297  479 GLU A OE1 
11752 O OE2 . GLU D 463 ? 1.2305 1.0391 1.0813 -0.2471 0.0331  0.0343  479 GLU A OE2 
11753 N N   . MET D 464 ? 1.0339 0.8665 0.9041 -0.2146 0.0334  -0.0071 480 MET A N   
11754 C CA  . MET D 464 ? 0.9962 0.8293 0.8725 -0.2069 0.0299  -0.0128 480 MET A CA  
11755 C C   . MET D 464 ? 0.9883 0.8329 0.8709 -0.2028 0.0352  -0.0221 480 MET A C   
11756 O O   . MET D 464 ? 0.9693 0.8138 0.8603 -0.1964 0.0325  -0.0278 480 MET A O   
11757 C CB  . MET D 464 ? 1.0046 0.8386 0.8739 -0.2054 0.0270  -0.0088 480 MET A CB  
11758 C CG  . MET D 464 ? 0.9971 0.8199 0.8621 -0.2077 0.0209  0.0000  480 MET A CG  
11759 S SD  . MET D 464 ? 1.1056 0.9320 0.9603 -0.2071 0.0188  0.0053  480 MET A SD  
11760 C CE  . MET D 464 ? 0.9419 0.7719 0.8036 -0.1983 0.0162  -0.0029 480 MET A CE  
11761 N N   . LYS D 465 ? 0.9662 0.8211 0.8450 -0.2061 0.0427  -0.0236 481 LYS A N   
11762 C CA  . LYS D 465 ? 0.9379 0.8028 0.8244 -0.2024 0.0478  -0.0320 481 LYS A CA  
11763 C C   . LYS D 465 ? 0.9870 0.8478 0.8824 -0.2015 0.0469  -0.0358 481 LYS A C   
11764 O O   . LYS D 465 ? 1.0145 0.8812 0.9189 -0.1958 0.0480  -0.0430 481 LYS A O   
11765 C CB  . LYS D 465 ? 0.9488 0.8253 0.8299 -0.2063 0.0562  -0.0328 481 LYS A CB  
11766 C CG  . LYS D 465 ? 0.9063 0.7912 0.7826 -0.2048 0.0585  -0.0333 481 LYS A CG  
11767 C CD  . LYS D 465 ? 0.8561 0.7502 0.7419 -0.1979 0.0605  -0.0411 481 LYS A CD  
11768 C CE  . LYS D 465 ? 0.8056 0.7096 0.6878 -0.1972 0.0642  -0.0425 481 LYS A CE  
11769 N NZ  . LYS D 465 ? 0.7497 0.6628 0.6424 -0.1907 0.0663  -0.0494 481 LYS A NZ  
11770 N N   . ARG D 466 ? 0.9461 0.7975 0.8398 -0.2067 0.0449  -0.0311 482 ARG A N   
11771 C CA  . ARG D 466 ? 0.9471 0.7954 0.8498 -0.2059 0.0443  -0.0354 482 ARG A CA  
11772 C C   . ARG D 466 ? 0.9906 0.8288 0.9011 -0.2005 0.0362  -0.0373 482 ARG A C   
11773 O O   . ARG D 466 ? 0.9376 0.7768 0.8575 -0.1959 0.0353  -0.0441 482 ARG A O   
11774 C CB  . ARG D 466 ? 1.0033 0.8461 0.9024 -0.2139 0.0456  -0.0301 482 ARG A CB  
11775 C CG  . ARG D 466 ? 0.9895 0.8421 0.8816 -0.2197 0.0538  -0.0285 482 ARG A CG  
11776 C CD  . ARG D 466 ? 0.9983 0.8430 0.8854 -0.2277 0.0530  -0.0204 482 ARG A CD  
11777 N NE  . ARG D 466 ? 1.0452 0.8987 0.9243 -0.2334 0.0604  -0.0175 482 ARG A NE  
11778 C CZ  . ARG D 466 ? 1.1172 0.9723 0.9970 -0.2384 0.0643  -0.0172 482 ARG A CZ  
11779 N NH1 . ARG D 466 ? 1.1771 1.0255 1.0655 -0.2386 0.0615  -0.0197 482 ARG A NH1 
11780 N NH2 . ARG D 466 ? 1.1658 1.0297 1.0374 -0.2431 0.0712  -0.0146 482 ARG A NH2 
11781 N N   . GLU D 467 ? 0.9838 0.8124 0.8901 -0.2006 0.0301  -0.0312 483 GLU A N   
11782 C CA  . GLU D 467 ? 0.9875 0.8048 0.9003 -0.1963 0.0221  -0.0316 483 GLU A CA  
11783 C C   . GLU D 467 ? 1.0020 0.8233 0.9193 -0.1876 0.0194  -0.0368 483 GLU A C   
11784 O O   . GLU D 467 ? 0.9987 0.8162 0.9247 -0.1820 0.0151  -0.0417 483 GLU A O   
11785 C CB  . GLU D 467 ? 1.0382 0.8432 0.9451 -0.2004 0.0167  -0.0219 483 GLU A CB  
11786 C CG  . GLU D 467 ? 1.1145 0.9072 1.0275 -0.1957 0.0082  -0.0218 483 GLU A CG  
11787 C CD  . GLU D 467 ? 1.3703 1.1506 1.2787 -0.2001 0.0032  -0.0117 483 GLU A CD  
11788 O OE1 . GLU D 467 ? 1.5263 1.2996 1.4360 -0.2056 0.0027  -0.0078 483 GLU A OE1 
11789 O OE2 . GLU D 467 ? 1.4872 1.2651 1.3911 -0.1979 -0.0004 -0.0075 483 GLU A OE2 
11790 N N   . ILE D 468 ? 0.9670 0.7961 0.8790 -0.1863 0.0216  -0.0360 484 ILE A N   
11791 C CA  . ILE D 468 ? 0.9648 0.7976 0.8811 -0.1784 0.0187  -0.0400 484 ILE A CA  
11792 C C   . ILE D 468 ? 0.9466 0.7937 0.8690 -0.1740 0.0245  -0.0479 484 ILE A C   
11793 O O   . ILE D 468 ? 0.9527 0.8023 0.8836 -0.1668 0.0221  -0.0534 484 ILE A O   
11794 C CB  . ILE D 468 ? 0.9021 0.7347 0.8101 -0.1789 0.0168  -0.0346 484 ILE A CB  
11795 C CG1 . ILE D 468 ? 0.8695 0.6883 0.7729 -0.1819 0.0105  -0.0267 484 ILE A CG1 
11796 C CG2 . ILE D 468 ? 0.8859 0.7231 0.7986 -0.1710 0.0140  -0.0387 484 ILE A CG2 
11797 C CD1 . ILE D 468 ? 0.9529 0.7728 0.8473 -0.1834 0.0095  -0.0210 484 ILE A CD1 
11798 N N   . VAL D 469 ? 0.8743 0.7312 0.7926 -0.1782 0.0320  -0.0482 485 VAL A N   
11799 C CA  . VAL D 469 ? 0.8498 0.7212 0.7739 -0.1742 0.0380  -0.0548 485 VAL A CA  
11800 C C   . VAL D 469 ? 0.8897 0.7647 0.8215 -0.1732 0.0411  -0.0604 485 VAL A C   
11801 O O   . VAL D 469 ? 0.8629 0.7483 0.8031 -0.1673 0.0437  -0.0668 485 VAL A O   
11802 C CB  . VAL D 469 ? 0.8273 0.7078 0.7439 -0.1787 0.0448  -0.0529 485 VAL A CB  
11803 C CG1 . VAL D 469 ? 0.8156 0.7110 0.7388 -0.1741 0.0505  -0.0592 485 VAL A CG1 
11804 C CG2 . VAL D 469 ? 0.8600 0.7366 0.7681 -0.1804 0.0415  -0.0473 485 VAL A CG2 
11805 N N   . GLY D 470 ? 0.8889 0.7561 0.8187 -0.1788 0.0407  -0.0581 486 GLY A N   
11806 C CA  . GLY D 470 ? 0.8399 0.7121 0.7755 -0.1793 0.0449  -0.0630 486 GLY A CA  
11807 C C   . GLY D 470 ? 0.8341 0.7194 0.7665 -0.1826 0.0542  -0.0641 486 GLY A C   
11808 O O   . GLY D 470 ? 0.8704 0.7667 0.8098 -0.1791 0.0589  -0.0703 486 GLY A O   
11809 N N   . VAL D 471 ? 0.8526 0.7376 0.7747 -0.1888 0.0569  -0.0582 487 VAL A N   
11810 C CA  . VAL D 471 ? 0.8742 0.7709 0.7922 -0.1923 0.0656  -0.0586 487 VAL A CA  
11811 C C   . VAL D 471 ? 0.9581 0.8491 0.8658 -0.2013 0.0671  -0.0517 487 VAL A C   
11812 O O   . VAL D 471 ? 0.9207 0.8011 0.8225 -0.2042 0.0618  -0.0453 487 VAL A O   
11813 C CB  . VAL D 471 ? 0.8295 0.7353 0.7459 -0.1892 0.0681  -0.0594 487 VAL A CB  
11814 C CG1 . VAL D 471 ? 0.8279 0.7435 0.7378 -0.1939 0.0764  -0.0583 487 VAL A CG1 
11815 C CG2 . VAL D 471 ? 0.7875 0.7017 0.7153 -0.1807 0.0683  -0.0664 487 VAL A CG2 
11816 N N   . VAL D 472 ? 0.9488 0.8475 0.8548 -0.2054 0.0744  -0.0526 488 VAL A N   
11817 C CA  . VAL D 472 ? 0.9485 0.8432 0.8458 -0.2138 0.0764  -0.0464 488 VAL A CA  
11818 C C   . VAL D 472 ? 0.9150 0.8216 0.8055 -0.2169 0.0849  -0.0459 488 VAL A C   
11819 O O   . VAL D 472 ? 0.8975 0.8159 0.7925 -0.2131 0.0903  -0.0516 488 VAL A O   
11820 C CB  . VAL D 472 ? 0.8963 0.7865 0.7987 -0.2163 0.0760  -0.0476 488 VAL A CB  
11821 C CG1 . VAL D 472 ? 0.9194 0.8218 0.8298 -0.2128 0.0820  -0.0557 488 VAL A CG1 
11822 C CG2 . VAL D 472 ? 0.9626 0.8482 0.8566 -0.2251 0.0775  -0.0403 488 VAL A CG2 
11823 N N   . GLU D 473 ? 0.8327 0.7366 0.7129 -0.2237 0.0861  -0.0390 489 GLU A N   
11824 C CA  . GLU D 473 ? 0.8606 0.7749 0.7330 -0.2264 0.0934  -0.0380 489 GLU A CA  
11825 C C   . GLU D 473 ? 0.9712 0.8921 0.8434 -0.2305 0.1004  -0.0391 489 GLU A C   
11826 O O   . GLU D 473 ? 1.0624 0.9768 0.9346 -0.2348 0.0988  -0.0362 489 GLU A O   
11827 C CB  . GLU D 473 ? 0.9106 0.8202 0.7712 -0.2310 0.0912  -0.0300 489 GLU A CB  
11828 C CG  . GLU D 473 ? 0.9463 0.8482 0.8006 -0.2382 0.0898  -0.0222 489 GLU A CG  
11829 C CD  . GLU D 473 ? 0.9781 0.8662 0.8371 -0.2380 0.0815  -0.0192 489 GLU A CD  
11830 O OE1 . GLU D 473 ? 0.9643 0.8495 0.8329 -0.2324 0.0780  -0.0248 489 GLU A OE1 
11831 O OE2 . GLU D 473 ? 1.0034 0.8835 0.8562 -0.2427 0.0780  -0.0109 489 GLU A OE2 
11832 N N   . PRO D 474 ? 0.9807 0.9144 0.8531 -0.2294 0.1081  -0.0432 490 PRO A N   
11833 C CA  . PRO D 474 ? 1.0402 0.9810 0.9126 -0.2329 0.1151  -0.0444 490 PRO A CA  
11834 C C   . PRO D 474 ? 1.0537 0.9932 0.9145 -0.2409 0.1177  -0.0372 490 PRO A C   
11835 O O   . PRO D 474 ? 1.1408 1.0835 1.0018 -0.2446 0.1220  -0.0372 490 PRO A O   
11836 C CB  . PRO D 474 ? 1.0440 0.9991 0.9200 -0.2287 0.1223  -0.0504 490 PRO A CB  
11837 C CG  . PRO D 474 ? 0.9488 0.9040 0.8209 -0.2264 0.1203  -0.0492 490 PRO A CG  
11838 C CD  . PRO D 474 ? 0.9440 0.8863 0.8164 -0.2252 0.1108  -0.0462 490 PRO A CD  
11839 N N   . VAL D 475 ? 0.9757 0.9114 0.8267 -0.2434 0.1153  -0.0310 491 VAL A N   
11840 C CA  . VAL D 475 ? 0.9724 0.9083 0.8116 -0.2504 0.1178  -0.0236 491 VAL A CA  
11841 C C   . VAL D 475 ? 1.0973 1.0218 0.9312 -0.2521 0.1099  -0.0163 491 VAL A C   
11842 O O   . VAL D 475 ? 1.0415 0.9622 0.8776 -0.2476 0.1049  -0.0176 491 VAL A O   
11843 C CB  . VAL D 475 ? 0.9963 0.9438 0.8279 -0.2506 0.1247  -0.0244 491 VAL A CB  
11844 C CG1 . VAL D 475 ? 1.0590 1.0070 0.8777 -0.2570 0.1264  -0.0164 491 VAL A CG1 
11845 C CG2 . VAL D 475 ? 0.9892 0.9483 0.8261 -0.2490 0.1328  -0.0308 491 VAL A CG2 
11846 N N   . PRO D 476 ? 1.0959 1.0151 0.9233 -0.2583 0.1085  -0.0082 492 PRO A N   
11847 C CA  . PRO D 476 ? 1.0751 0.9841 0.8983 -0.2595 0.1011  -0.0008 492 PRO A CA  
11848 C C   . PRO D 476 ? 1.0990 1.0128 0.9113 -0.2594 0.1017  0.0027  492 PRO A C   
11849 O O   . PRO D 476 ? 1.1224 1.0460 0.9276 -0.2612 0.1081  0.0026  492 PRO A O   
11850 C CB  . PRO D 476 ? 1.0704 0.9739 0.8912 -0.2664 0.1005  0.0068  492 PRO A CB  
11851 C CG  . PRO D 476 ? 1.0886 1.0025 0.9067 -0.2695 0.1089  0.0049  492 PRO A CG  
11852 C CD  . PRO D 476 ? 1.1068 1.0283 0.9323 -0.2642 0.1131  -0.0055 492 PRO A CD  
11853 N N   . HIS D 477 ? 1.1772 1.0843 0.9883 -0.2570 0.0949  0.0056  493 HIS A N   
11854 C CA  . HIS D 477 ? 1.1283 1.0402 0.9302 -0.2558 0.0946  0.0077  493 HIS A CA  
11855 C C   . HIS D 477 ? 1.0974 1.0022 0.8924 -0.2585 0.0889  0.0176  493 HIS A C   
11856 O O   . HIS D 477 ? 1.0883 0.9831 0.8881 -0.2568 0.0821  0.0196  493 HIS A O   
11857 C CB  . HIS D 477 ? 1.0823 0.9958 0.8894 -0.2490 0.0926  0.0005  493 HIS A CB  
11858 C CG  . HIS D 477 ? 1.0837 1.0076 0.8949 -0.2464 0.0995  -0.0079 493 HIS A CG  
11859 N ND1 . HIS D 477 ? 1.0394 0.9667 0.8573 -0.2404 0.0989  -0.0149 493 HIS A ND1 
11860 C CD2 . HIS D 477 ? 1.0872 1.0195 0.8970 -0.2490 0.1072  -0.0098 493 HIS A CD2 
11861 C CE1 . HIS D 477 ? 1.0286 0.9658 0.8495 -0.2394 0.1061  -0.0207 493 HIS A CE1 
11862 N NE2 . HIS D 477 ? 1.0500 0.9904 0.8658 -0.2446 0.1112  -0.0178 493 HIS A NE2 
11863 N N   . ASP D 478 ? 1.2062 1.1164 0.9902 -0.2625 0.0917  0.0238  494 ASP A N   
11864 C CA  . ASP D 478 ? 1.2366 1.1430 1.0129 -0.2645 0.0869  0.0335  494 ASP A CA  
11865 C C   . ASP D 478 ? 1.2584 1.1678 1.0303 -0.2598 0.0840  0.0317  494 ASP A C   
11866 O O   . ASP D 478 ? 1.3008 1.2130 1.0774 -0.2551 0.0846  0.0232  494 ASP A O   
11867 C CB  . ASP D 478 ? 1.2959 1.2086 1.0622 -0.2701 0.0912  0.0408  494 ASP A CB  
11868 C CG  . ASP D 478 ? 1.3279 1.2532 1.0876 -0.2696 0.0983  0.0360  494 ASP A CG  
11869 O OD1 . ASP D 478 ? 1.3338 1.2626 1.0971 -0.2649 0.0994  0.0274  494 ASP A OD1 
11870 O OD2 . ASP D 478 ? 1.4386 1.3705 1.1896 -0.2737 0.1026  0.0409  494 ASP A OD2 
11871 N N   . GLU D 479 ? 1.1985 1.1085 0.9615 -0.2610 0.0810  0.0396  495 GLU A N   
11872 C CA  . GLU D 479 ? 1.1704 1.0826 0.9297 -0.2564 0.0772  0.0381  495 GLU A CA  
11873 C C   . GLU D 479 ? 1.1505 1.0748 0.9019 -0.2551 0.0819  0.0338  495 GLU A C   
11874 O O   . GLU D 479 ? 1.1916 1.1189 0.9392 -0.2516 0.0790  0.0324  495 GLU A O   
11875 C CB  . GLU D 479 ? 1.1624 1.0702 0.9161 -0.2573 0.0713  0.0483  495 GLU A CB  
11876 C CG  . GLU D 479 ? 1.2377 1.1327 0.9996 -0.2584 0.0662  0.0528  495 GLU A CG  
11877 C CD  . GLU D 479 ? 1.2235 1.1115 0.9960 -0.2533 0.0623  0.0453  495 GLU A CD  
11878 O OE1 . GLU D 479 ? 1.1898 1.0819 0.9620 -0.2486 0.0614  0.0393  495 GLU A OE1 
11879 O OE2 . GLU D 479 ? 1.2344 1.1129 1.0160 -0.2540 0.0599  0.0454  495 GLU A OE2 
11880 N N   . THR D 480 ? 1.1225 1.0541 0.8716 -0.2577 0.0891  0.0313  496 THR A N   
11881 C CA  . THR D 480 ? 1.1462 1.0888 0.8900 -0.2557 0.0936  0.0255  496 THR A CA  
11882 C C   . THR D 480 ? 1.1936 1.1362 0.9464 -0.2504 0.0929  0.0155  496 THR A C   
11883 O O   . THR D 480 ? 1.1603 1.1096 0.9102 -0.2473 0.0935  0.0108  496 THR A O   
11884 C CB  . THR D 480 ? 1.1703 1.1204 0.9108 -0.2594 0.1016  0.0246  496 THR A CB  
11885 O OG1 . THR D 480 ? 1.2095 1.1566 0.9608 -0.2594 0.1046  0.0191  496 THR A OG1 
11886 C CG2 . THR D 480 ? 1.1250 1.0744 0.8580 -0.2648 0.1019  0.0349  496 THR A CG2 
11887 N N   . TYR D 481 ? 1.1149 1.0502 0.8792 -0.2490 0.0913  0.0123  497 TYR A N   
11888 C CA  . TYR D 481 ? 1.1047 1.0406 0.8787 -0.2439 0.0912  0.0032  497 TYR A CA  
11889 C C   . TYR D 481 ? 1.1097 1.0406 0.8856 -0.2396 0.0837  0.0031  497 TYR A C   
11890 O O   . TYR D 481 ? 1.1377 1.0627 0.9092 -0.2405 0.0783  0.0100  497 TYR A O   
11891 C CB  . TYR D 481 ? 1.0682 0.9996 0.8535 -0.2437 0.0926  -0.0003 497 TYR A CB  
11892 C CG  . TYR D 481 ? 1.0920 1.0296 0.8774 -0.2469 0.1004  -0.0021 497 TYR A CG  
11893 C CD1 . TYR D 481 ? 1.0989 1.0352 0.8789 -0.2525 0.1024  0.0044  497 TYR A CD1 
11894 C CD2 . TYR D 481 ? 1.1180 1.0635 0.9089 -0.2442 0.1059  -0.0102 497 TYR A CD2 
11895 C CE1 . TYR D 481 ? 1.0811 1.0237 0.8612 -0.2553 0.1097  0.0025  497 TYR A CE1 
11896 C CE2 . TYR D 481 ? 1.1173 1.0692 0.9086 -0.2467 0.1134  -0.0120 497 TYR A CE2 
11897 C CZ  . TYR D 481 ? 1.0787 1.0292 0.8643 -0.2523 0.1153  -0.0059 497 TYR A CZ  
11898 O OH  . TYR D 481 ? 1.0660 1.0236 0.8521 -0.2545 0.1229  -0.0082 497 TYR A OH  
11899 N N   . CYS D 482 ? 1.0466 0.9804 0.8296 -0.2348 0.0837  -0.0048 498 CYS A N   
11900 C CA  . CYS D 482 ? 1.0013 0.9304 0.7880 -0.2303 0.0768  -0.0059 498 CYS A CA  
11901 C C   . CYS D 482 ? 0.9555 0.8852 0.7550 -0.2257 0.0776  -0.0141 498 CYS A C   
11902 O O   . CYS D 482 ? 0.9618 0.8959 0.7645 -0.2218 0.0768  -0.0193 498 CYS A O   
11903 C CB  . CYS D 482 ? 1.0237 0.9584 0.8020 -0.2290 0.0749  -0.0055 498 CYS A CB  
11904 S SG  . CYS D 482 ? 1.0124 0.9407 0.7920 -0.2246 0.0655  -0.0037 498 CYS A SG  
11905 N N   . ASP D 483 ? 0.9625 0.8883 0.7698 -0.2261 0.0790  -0.0153 499 ASP A N   
11906 C CA  . ASP D 483 ? 0.9491 0.8778 0.7683 -0.2218 0.0811  -0.0231 499 ASP A CA  
11907 C C   . ASP D 483 ? 0.8875 0.8144 0.7134 -0.2159 0.0756  -0.0265 499 ASP A C   
11908 O O   . ASP D 483 ? 0.8983 0.8322 0.7309 -0.2124 0.0783  -0.0328 499 ASP A O   
11909 C CB  . ASP D 483 ? 1.0580 0.9822 0.8841 -0.2229 0.0825  -0.0233 499 ASP A CB  
11910 C CG  . ASP D 483 ? 0.9951 0.9224 0.8151 -0.2287 0.0885  -0.0203 499 ASP A CG  
11911 O OD1 . ASP D 483 ? 1.0011 0.9363 0.8136 -0.2308 0.0931  -0.0201 499 ASP A OD1 
11912 O OD2 . ASP D 483 ? 0.9180 0.8398 0.7405 -0.2312 0.0884  -0.0180 499 ASP A OD2 
11913 N N   . PRO D 484 ? 0.9559 0.8743 0.7804 -0.2146 0.0681  -0.0224 500 PRO A N   
11914 C CA  . PRO D 484 ? 0.9690 0.8871 0.7983 -0.2092 0.0632  -0.0255 500 PRO A CA  
11915 C C   . PRO D 484 ? 0.9212 0.8491 0.7490 -0.2077 0.0658  -0.0299 500 PRO A C   
11916 O O   . PRO D 484 ? 0.8801 0.8128 0.7171 -0.2035 0.0667  -0.0360 500 PRO A O   
11917 C CB  . PRO D 484 ? 0.9612 0.8707 0.7841 -0.2099 0.0560  -0.0186 500 PRO A CB  
11918 C CG  . PRO D 484 ? 0.9492 0.8517 0.7699 -0.2140 0.0561  -0.0132 500 PRO A CG  
11919 C CD  . PRO D 484 ? 0.9844 0.8931 0.8041 -0.2178 0.0639  -0.0148 500 PRO A CD  
11920 N N   . ALA D 485 ? 0.8905 0.8221 0.7072 -0.2112 0.0672  -0.0269 501 ALA A N   
11921 C CA  . ALA D 485 ? 0.8580 0.7986 0.6716 -0.2102 0.0694  -0.0307 501 ALA A CA  
11922 C C   . ALA D 485 ? 0.8238 0.7727 0.6452 -0.2091 0.0762  -0.0376 501 ALA A C   
11923 O O   . ALA D 485 ? 0.8159 0.7721 0.6376 -0.2076 0.0778  -0.0417 501 ALA A O   
11924 C CB  . ALA D 485 ? 0.8349 0.7784 0.6347 -0.2146 0.0708  -0.0259 501 ALA A CB  
11925 N N   . SER D 486 ? 0.8038 0.7524 0.6314 -0.2097 0.0803  -0.0387 502 SER A N   
11926 C CA  . SER D 486 ? 0.7986 0.7560 0.6331 -0.2089 0.0875  -0.0444 502 SER A CA  
11927 C C   . SER D 486 ? 0.8264 0.7863 0.6746 -0.2031 0.0865  -0.0499 502 SER A C   
11928 O O   . SER D 486 ? 0.8594 0.8272 0.7152 -0.2016 0.0923  -0.0546 502 SER A O   
11929 C CB  . SER D 486 ? 0.7424 0.6994 0.5772 -0.2120 0.0927  -0.0430 502 SER A CB  
11930 O OG  . SER D 486 ? 0.7904 0.7428 0.6352 -0.2090 0.0903  -0.0443 502 SER A OG  
11931 N N   . LEU D 487 ? 0.7728 0.7264 0.6245 -0.1998 0.0794  -0.0491 503 LEU A N   
11932 C CA  . LEU D 487 ? 0.7757 0.7318 0.6400 -0.1940 0.0776  -0.0537 503 LEU A CA  
11933 C C   . LEU D 487 ? 0.7744 0.7327 0.6373 -0.1921 0.0737  -0.0550 503 LEU A C   
11934 O O   . LEU D 487 ? 0.8009 0.7542 0.6546 -0.1935 0.0687  -0.0512 503 LEU A O   
11935 C CB  . LEU D 487 ? 0.7757 0.7235 0.6454 -0.1911 0.0722  -0.0522 503 LEU A CB  
11936 C CG  . LEU D 487 ? 0.6991 0.6486 0.5811 -0.1846 0.0690  -0.0559 503 LEU A CG  
11937 C CD1 . LEU D 487 ? 0.6857 0.6443 0.5786 -0.1823 0.0756  -0.0608 503 LEU A CD1 
11938 C CD2 . LEU D 487 ? 0.7114 0.6510 0.5952 -0.1825 0.0627  -0.0533 503 LEU A CD2 
11939 N N   . PHE D 488 ? 0.7522 0.7186 0.6244 -0.1889 0.0762  -0.0602 504 PHE A N   
11940 C CA  . PHE D 488 ? 0.7512 0.7207 0.6231 -0.1872 0.0730  -0.0623 504 PHE A CA  
11941 C C   . PHE D 488 ? 0.8113 0.7733 0.6784 -0.1860 0.0644  -0.0591 504 PHE A C   
11942 O O   . PHE D 488 ? 0.8253 0.7868 0.6828 -0.1878 0.0616  -0.0575 504 PHE A O   
11943 C CB  . PHE D 488 ? 0.7559 0.7328 0.6426 -0.1826 0.0748  -0.0676 504 PHE A CB  
11944 C CG  . PHE D 488 ? 0.7795 0.7586 0.6685 -0.1802 0.0703  -0.0698 504 PHE A CG  
11945 C CD1 . PHE D 488 ? 0.7905 0.7754 0.6762 -0.1820 0.0726  -0.0724 504 PHE A CD1 
11946 C CD2 . PHE D 488 ? 0.7849 0.7600 0.6788 -0.1762 0.0634  -0.0692 504 PHE A CD2 
11947 C CE1 . PHE D 488 ? 0.8245 0.8113 0.7126 -0.1799 0.0681  -0.0748 504 PHE A CE1 
11948 C CE2 . PHE D 488 ? 0.8234 0.8007 0.7194 -0.1742 0.0590  -0.0712 504 PHE A CE2 
11949 C CZ  . PHE D 488 ? 0.8453 0.8284 0.7387 -0.1761 0.0612  -0.0742 504 PHE A CZ  
11950 N N   . HIS D 489 ? 0.8111 0.7676 0.6846 -0.1826 0.0601  -0.0580 505 HIS A N   
11951 C CA  . HIS D 489 ? 0.7773 0.7277 0.6487 -0.1802 0.0519  -0.0556 505 HIS A CA  
11952 C C   . HIS D 489 ? 0.7818 0.7256 0.6390 -0.1842 0.0487  -0.0497 505 HIS A C   
11953 O O   . HIS D 489 ? 0.8398 0.7810 0.6924 -0.1831 0.0428  -0.0478 505 HIS A O   
11954 C CB  . HIS D 489 ? 0.7403 0.6856 0.6206 -0.1760 0.0486  -0.0553 505 HIS A CB  
11955 C CG  . HIS D 489 ? 0.7086 0.6612 0.6032 -0.1714 0.0511  -0.0603 505 HIS A CG  
11956 N ND1 . HIS D 489 ? 0.7066 0.6662 0.6072 -0.1719 0.0585  -0.0634 505 HIS A ND1 
11957 C CD2 . HIS D 489 ? 0.7601 0.7146 0.6647 -0.1659 0.0473  -0.0624 505 HIS A CD2 
11958 C CE1 . HIS D 489 ? 0.7564 0.7222 0.6702 -0.1669 0.0593  -0.0670 505 HIS A CE1 
11959 N NE2 . HIS D 489 ? 0.7838 0.7467 0.7003 -0.1632 0.0524  -0.0664 505 HIS A NE2 
11960 N N   . VAL D 490 ? 0.7934 0.7348 0.6439 -0.1886 0.0523  -0.0465 506 VAL A N   
11961 C CA  . VAL D 490 ? 0.8250 0.7602 0.6629 -0.1921 0.0491  -0.0399 506 VAL A CA  
11962 C C   . VAL D 490 ? 0.8554 0.7968 0.6831 -0.1951 0.0510  -0.0396 506 VAL A C   
11963 O O   . VAL D 490 ? 0.9029 0.8424 0.7217 -0.1958 0.0465  -0.0357 506 VAL A O   
11964 C CB  . VAL D 490 ? 0.7833 0.7127 0.6190 -0.1956 0.0515  -0.0357 506 VAL A CB  
11965 C CG1 . VAL D 490 ? 0.8122 0.7363 0.6358 -0.1993 0.0485  -0.0284 506 VAL A CG1 
11966 C CG2 . VAL D 490 ? 0.7685 0.6915 0.6139 -0.1922 0.0487  -0.0363 506 VAL A CG2 
11967 N N   . SER D 491 ? 0.8327 0.7819 0.6620 -0.1965 0.0577  -0.0438 507 SER A N   
11968 C CA  . SER D 491 ? 0.8472 0.8030 0.6674 -0.1990 0.0603  -0.0445 507 SER A CA  
11969 C C   . SER D 491 ? 0.9005 0.8615 0.7232 -0.1958 0.0573  -0.0492 507 SER A C   
11970 O O   . SER D 491 ? 0.9969 0.9624 0.8109 -0.1972 0.0571  -0.0494 507 SER A O   
11971 C CB  . SER D 491 ? 0.8462 0.8084 0.6678 -0.2014 0.0686  -0.0475 507 SER A CB  
11972 O OG  . SER D 491 ? 0.8209 0.7864 0.6561 -0.1982 0.0714  -0.0529 507 SER A OG  
11973 N N   . ASN D 492 ? 0.8572 0.8184 0.6919 -0.1915 0.0550  -0.0531 508 ASN A N   
11974 C CA  . ASN D 492 ? 0.8733 0.8388 0.7116 -0.1884 0.0513  -0.0574 508 ASN A CA  
11975 C C   . ASN D 492 ? 0.9216 0.8814 0.7600 -0.1854 0.0430  -0.0547 508 ASN A C   
11976 O O   . ASN D 492 ? 0.9385 0.9011 0.7827 -0.1820 0.0393  -0.0583 508 ASN A O   
11977 C CB  . ASN D 492 ? 0.8584 0.8301 0.7110 -0.1856 0.0549  -0.0637 508 ASN A CB  
11978 C CG  . ASN D 492 ? 0.8831 0.8618 0.7352 -0.1882 0.0626  -0.0668 508 ASN A CG  
11979 O OD1 . ASN D 492 ? 0.9815 0.9664 0.8335 -0.1882 0.0636  -0.0709 508 ASN A OD1 
11980 N ND2 . ASN D 492 ? 0.8411 0.8191 0.6934 -0.1903 0.0682  -0.0651 508 ASN A ND2 
11981 N N   . ASP D 493 ? 0.9172 0.8688 0.7498 -0.1865 0.0402  -0.0485 509 ASP A N   
11982 C CA  . ASP D 493 ? 0.8930 0.8392 0.7222 -0.1845 0.0326  -0.0447 509 ASP A CA  
11983 C C   . ASP D 493 ? 0.8500 0.7949 0.6910 -0.1793 0.0284  -0.0475 509 ASP A C   
11984 O O   . ASP D 493 ? 0.8900 0.8382 0.7324 -0.1768 0.0244  -0.0500 509 ASP A O   
11985 C CB  . ASP D 493 ? 0.8828 0.8337 0.7018 -0.1854 0.0301  -0.0444 509 ASP A CB  
11986 C CG  . ASP D 493 ? 0.9140 0.8603 0.7275 -0.1838 0.0229  -0.0396 509 ASP A CG  
11987 O OD1 . ASP D 493 ? 0.9301 0.8684 0.7419 -0.1842 0.0208  -0.0338 509 ASP A OD1 
11988 O OD2 . ASP D 493 ? 0.9632 0.9143 0.7737 -0.1822 0.0193  -0.0416 509 ASP A OD2 
11989 N N   . TYR D 494 ? 0.8124 0.7527 0.6615 -0.1777 0.0293  -0.0472 510 TYR A N   
11990 C CA  . TYR D 494 ? 0.8451 0.7845 0.7061 -0.1725 0.0260  -0.0496 510 TYR A CA  
11991 C C   . TYR D 494 ? 0.9126 0.8424 0.7745 -0.1713 0.0228  -0.0452 510 TYR A C   
11992 O O   . TYR D 494 ? 0.9330 0.8596 0.7951 -0.1733 0.0265  -0.0439 510 TYR A O   
11993 C CB  . TYR D 494 ? 0.8474 0.7937 0.7207 -0.1708 0.0316  -0.0553 510 TYR A CB  
11994 C CG  . TYR D 494 ? 0.8463 0.8020 0.7234 -0.1705 0.0337  -0.0605 510 TYR A CG  
11995 C CD1 . TYR D 494 ? 0.9191 0.8776 0.8021 -0.1668 0.0289  -0.0630 510 TYR A CD1 
11996 C CD2 . TYR D 494 ? 0.8410 0.8025 0.7159 -0.1738 0.0402  -0.0629 510 TYR A CD2 
11997 C CE1 . TYR D 494 ? 0.9182 0.8851 0.8056 -0.1666 0.0305  -0.0680 510 TYR A CE1 
11998 C CE2 . TYR D 494 ? 0.8846 0.8543 0.7635 -0.1735 0.0420  -0.0679 510 TYR A CE2 
11999 C CZ  . TYR D 494 ? 0.9164 0.8885 0.8018 -0.1700 0.0371  -0.0705 510 TYR A CZ  
12000 O OH  . TYR D 494 ? 0.9223 0.9021 0.8124 -0.1698 0.0387  -0.0756 510 TYR A OH  
12001 N N   . SER D 495 ? 1.0972 1.0225 0.9601 -0.1678 0.0160  -0.0433 511 SER A N   
12002 C CA  . SER D 495 ? 1.1108 1.0270 0.9760 -0.1658 0.0127  -0.0398 511 SER A CA  
12003 C C   . SER D 495 ? 1.0618 0.9796 0.9389 -0.1632 0.0162  -0.0437 511 SER A C   
12004 O O   . SER D 495 ? 1.0892 1.0150 0.9753 -0.1605 0.0186  -0.0487 511 SER A O   
12005 C CB  . SER D 495 ? 1.1096 1.0220 0.9752 -0.1617 0.0050  -0.0378 511 SER A CB  
12006 O OG  . SER D 495 ? 1.0767 0.9949 0.9527 -0.1568 0.0035  -0.0425 511 SER A OG  
12007 N N   . PHE D 496 ? 0.9042 0.8148 0.7815 -0.1639 0.0165  -0.0412 512 PHE A N   
12008 C CA  . PHE D 496 ? 0.8427 0.7554 0.7296 -0.1622 0.0206  -0.0447 512 PHE A CA  
12009 C C   . PHE D 496 ? 0.8562 0.7633 0.7509 -0.1570 0.0163  -0.0448 512 PHE A C   
12010 O O   . PHE D 496 ? 0.8263 0.7381 0.7312 -0.1537 0.0191  -0.0488 512 PHE A O   
12011 C CB  . PHE D 496 ? 0.8774 0.7879 0.7590 -0.1676 0.0258  -0.0430 512 PHE A CB  
12012 C CG  . PHE D 496 ? 0.8073 0.7251 0.6970 -0.1672 0.0327  -0.0477 512 PHE A CG  
12013 C CD1 . PHE D 496 ? 0.7842 0.7126 0.6776 -0.1671 0.0376  -0.0520 512 PHE A CD1 
12014 C CD2 . PHE D 496 ? 0.7782 0.6922 0.6718 -0.1671 0.0343  -0.0479 512 PHE A CD2 
12015 C CE1 . PHE D 496 ? 0.7408 0.6763 0.6419 -0.1665 0.0441  -0.0559 512 PHE A CE1 
12016 C CE2 . PHE D 496 ? 0.7807 0.7021 0.6816 -0.1665 0.0406  -0.0522 512 PHE A CE2 
12017 C CZ  . PHE D 496 ? 0.7640 0.6963 0.6686 -0.1662 0.0457  -0.0559 512 PHE A CZ  
12018 N N   . ILE D 497 ? 0.9288 0.6570 0.9048 -0.1943 -0.0084 -0.0029 513 ILE A N   
12019 C CA  . ILE D 497 ? 0.9019 0.6190 0.8776 -0.1821 -0.0150 -0.0087 513 ILE A CA  
12020 C C   . ILE D 497 ? 0.8977 0.6342 0.8898 -0.1636 -0.0142 -0.0082 513 ILE A C   
12021 O O   . ILE D 497 ? 0.8751 0.6126 0.8711 -0.1514 -0.0174 -0.0143 513 ILE A O   
12022 C CB  . ILE D 497 ? 0.9303 0.6087 0.8889 -0.1857 -0.0256 -0.0071 513 ILE A CB  
12023 C CG1 . ILE D 497 ? 0.8939 0.5571 0.8463 -0.1786 -0.0320 -0.0155 513 ILE A CG1 
12024 C CG2 . ILE D 497 ? 0.9375 0.6098 0.8998 -0.1771 -0.0298 0.0003  513 ILE A CG2 
12025 C CD1 . ILE D 497 ? 0.8620 0.5294 0.8098 -0.1875 -0.0286 -0.0227 513 ILE A CD1 
12026 N N   . ARG D 498 ? 0.8449 0.5971 0.8460 -0.1615 -0.0100 -0.0010 514 ARG A N   
12027 C CA  . ARG D 498 ? 0.7968 0.5700 0.8131 -0.1457 -0.0084 -0.0004 514 ARG A CA  
12028 C C   . ARG D 498 ? 0.7812 0.5788 0.8081 -0.1373 -0.0034 -0.0081 514 ARG A C   
12029 O O   . ARG D 498 ? 0.7624 0.5701 0.7986 -0.1230 -0.0049 -0.0108 514 ARG A O   
12030 C CB  . ARG D 498 ? 0.7493 0.5376 0.7722 -0.1476 -0.0032 0.0081  514 ARG A CB  
12031 C CG  . ARG D 498 ? 0.7515 0.5636 0.7796 -0.1530 0.0060  0.0071  514 ARG A CG  
12032 C CD  . ARG D 498 ? 0.8230 0.6338 0.8467 -0.1640 0.0091  0.0147  514 ARG A CD  
12033 N NE  . ARG D 498 ? 0.8202 0.6370 0.8507 -0.1567 0.0087  0.0219  514 ARG A NE  
12034 C CZ  . ARG D 498 ? 0.8919 0.7011 0.9180 -0.1635 0.0086  0.0301  514 ARG A CZ  
12035 N NH1 . ARG D 498 ? 0.9049 0.7071 0.9228 -0.1740 0.0098  0.0317  514 ARG A NH1 
12036 N NH2 . ARG D 498 ? 0.9302 0.7443 0.9625 -0.1561 0.0075  0.0362  514 ARG A NH2 
12037 N N   . TYR D 499 ? 0.7622 0.5705 0.7880 -0.1457 0.0025  -0.0122 515 TYR A N   
12038 C CA  . TYR D 499 ? 0.7268 0.5594 0.7631 -0.1373 0.0074  -0.0191 515 TYR A CA  
12039 C C   . TYR D 499 ? 0.7084 0.5287 0.7412 -0.1309 0.0017  -0.0273 515 TYR A C   
12040 O O   . TYR D 499 ? 0.7208 0.5563 0.7635 -0.1178 0.0024  -0.0320 515 TYR A O   
12041 C CB  . TYR D 499 ? 0.7602 0.6098 0.7969 -0.1472 0.0153  -0.0211 515 TYR A CB  
12042 C CG  . TYR D 499 ? 0.7417 0.6040 0.7817 -0.1518 0.0208  -0.0132 515 TYR A CG  
12043 C CD1 . TYR D 499 ? 0.6959 0.5800 0.7475 -0.1420 0.0249  -0.0100 515 TYR A CD1 
12044 C CD2 . TYR D 499 ? 0.7289 0.5794 0.7591 -0.1661 0.0211  -0.0085 515 TYR A CD2 
12045 C CE1 . TYR D 499 ? 0.6808 0.5742 0.7337 -0.1459 0.0293  -0.0028 515 TYR A CE1 
12046 C CE2 . TYR D 499 ? 0.6958 0.5568 0.7283 -0.1696 0.0257  -0.0015 515 TYR A CE2 
12047 C CZ  . TYR D 499 ? 0.6848 0.5666 0.7283 -0.1593 0.0296  0.0014  515 TYR A CZ  
12048 O OH  . TYR D 499 ? 0.6586 0.5491 0.7028 -0.1627 0.0337  0.0083  515 TYR A OH  
12049 N N   . TYR D 500 ? 0.7692 0.5599 0.7870 -0.1392 -0.0048 -0.0286 516 TYR A N   
12050 C CA  . TYR D 500 ? 0.8018 0.5743 0.8131 -0.1327 -0.0122 -0.0357 516 TYR A CA  
12051 C C   . TYR D 500 ? 0.7957 0.5663 0.8135 -0.1161 -0.0177 -0.0350 516 TYR A C   
12052 O O   . TYR D 500 ? 0.8019 0.5844 0.8278 -0.1028 -0.0181 -0.0411 516 TYR A O   
12053 C CB  . TYR D 500 ? 0.8006 0.5383 0.7920 -0.1460 -0.0188 -0.0358 516 TYR A CB  
12054 C CG  . TYR D 500 ? 0.8123 0.5282 0.7937 -0.1414 -0.0265 -0.0435 516 TYR A CG  
12055 C CD1 . TYR D 500 ? 0.8836 0.5786 0.8602 -0.1304 -0.0358 -0.0436 516 TYR A CD1 
12056 C CD2 . TYR D 500 ? 0.8622 0.5795 0.8388 -0.1473 -0.0246 -0.0512 516 TYR A CD2 
12057 C CE1 . TYR D 500 ? 0.9344 0.6081 0.9006 -0.1250 -0.0434 -0.0511 516 TYR A CE1 
12058 C CE2 . TYR D 500 ? 0.9104 0.6066 0.8769 -0.1427 -0.0319 -0.0584 516 TYR A CE2 
12059 C CZ  . TYR D 500 ? 0.9097 0.5834 0.8706 -0.1313 -0.0414 -0.0583 516 TYR A CZ  
12060 O OH  . TYR D 500 ? 0.9480 0.5995 0.8977 -0.1258 -0.0493 -0.0655 516 TYR A OH  
12061 N N   . THR D 501 ? 0.8308 0.5883 0.8454 -0.1166 -0.0218 -0.0275 517 THR A N   
12062 C CA  . THR D 501 ? 0.8360 0.5894 0.8550 -0.1017 -0.0282 -0.0268 517 THR A CA  
12063 C C   . THR D 501 ? 0.7703 0.5577 0.8082 -0.0884 -0.0226 -0.0274 517 THR A C   
12064 O O   . THR D 501 ? 0.7571 0.5492 0.8008 -0.0739 -0.0263 -0.0323 517 THR A O   
12065 C CB  . THR D 501 ? 0.8553 0.5900 0.8674 -0.1066 -0.0329 -0.0181 517 THR A CB  
12066 O OG1 . THR D 501 ? 0.8339 0.5879 0.8536 -0.1133 -0.0250 -0.0107 517 THR A OG1 
12067 C CG2 . THR D 501 ? 0.8757 0.5745 0.8674 -0.1199 -0.0391 -0.0176 517 THR A CG2 
12068 N N   . ARG D 502 ? 0.6882 0.4985 0.7348 -0.0930 -0.0142 -0.0221 518 ARG A N   
12069 C CA  . ARG D 502 ? 0.6546 0.4966 0.7172 -0.0823 -0.0085 -0.0221 518 ARG A CA  
12070 C C   . ARG D 502 ? 0.7343 0.5905 0.8029 -0.0739 -0.0066 -0.0316 518 ARG A C   
12071 O O   . ARG D 502 ? 0.7231 0.5942 0.8015 -0.0601 -0.0073 -0.0347 518 ARG A O   
12072 C CB  . ARG D 502 ? 0.6236 0.4850 0.6911 -0.0906 0.0003  -0.0161 518 ARG A CB  
12073 C CG  . ARG D 502 ? 0.6718 0.5658 0.7532 -0.0817 0.0073  -0.0181 518 ARG A CG  
12074 C CD  . ARG D 502 ? 0.7306 0.6431 0.8144 -0.0898 0.0163  -0.0155 518 ARG A CD  
12075 N NE  . ARG D 502 ? 0.8128 0.7249 0.8919 -0.0970 0.0192  -0.0215 518 ARG A NE  
12076 C CZ  . ARG D 502 ? 0.8486 0.7783 0.9336 -0.0918 0.0232  -0.0286 518 ARG A CZ  
12077 N NH1 . ARG D 502 ? 0.8331 0.7824 0.9286 -0.0798 0.0251  -0.0303 518 ARG A NH1 
12078 N NH2 . ARG D 502 ? 0.8418 0.7699 0.9217 -0.0991 0.0252  -0.0341 518 ARG A NH2 
12079 N N   . THR D 503 ? 0.8499 0.7032 0.9127 -0.0825 -0.0038 -0.0363 519 THR A N   
12080 C CA  . THR D 503 ? 0.7800 0.6450 0.8471 -0.0755 -0.0021 -0.0456 519 THR A CA  
12081 C C   . THR D 503 ? 0.8083 0.6604 0.8738 -0.0629 -0.0103 -0.0512 519 THR A C   
12082 O O   . THR D 503 ? 0.8598 0.7304 0.9356 -0.0499 -0.0092 -0.0558 519 THR A O   
12083 C CB  . THR D 503 ? 0.7876 0.6456 0.8459 -0.0876 0.0002  -0.0501 519 THR A CB  
12084 O OG1 . THR D 503 ? 0.8037 0.6784 0.8651 -0.0973 0.0083  -0.0459 519 THR A OG1 
12085 C CG2 . THR D 503 ? 0.8508 0.7190 0.9129 -0.0799 0.0011  -0.0600 519 THR A CG2 
12086 N N   . LEU D 504 ? 0.8007 0.6210 0.8526 -0.0661 -0.0188 -0.0509 520 LEU A N   
12087 C CA  . LEU D 504 ? 0.8276 0.6332 0.8761 -0.0532 -0.0276 -0.0568 520 LEU A CA  
12088 C C   . LEU D 504 ? 0.7877 0.6082 0.8481 -0.0384 -0.0293 -0.0546 520 LEU A C   
12089 O O   . LEU D 504 ? 0.7914 0.6239 0.8593 -0.0239 -0.0309 -0.0612 520 LEU A O   
12090 C CB  . LEU D 504 ? 0.8632 0.6289 0.8925 -0.0602 -0.0370 -0.0564 520 LEU A CB  
12091 C CG  . LEU D 504 ? 0.8664 0.6142 0.8824 -0.0692 -0.0385 -0.0630 520 LEU A CG  
12092 C CD1 . LEU D 504 ? 0.8107 0.5726 0.8278 -0.0844 -0.0293 -0.0616 520 LEU A CD1 
12093 C CD2 . LEU D 504 ? 0.8961 0.6030 0.8916 -0.0757 -0.0485 -0.0621 520 LEU A CD2 
12094 N N   . TYR D 505 ? 0.7767 0.5974 0.8389 -0.0419 -0.0291 -0.0457 521 TYR A N   
12095 C CA  . TYR D 505 ? 0.7629 0.5979 0.8358 -0.0291 -0.0310 -0.0433 521 TYR A CA  
12096 C C   . TYR D 505 ? 0.6979 0.5680 0.7867 -0.0194 -0.0243 -0.0471 521 TYR A C   
12097 O O   . TYR D 505 ? 0.6932 0.5744 0.7897 -0.0050 -0.0274 -0.0509 521 TYR A O   
12098 C CB  . TYR D 505 ? 0.7156 0.5510 0.7897 -0.0358 -0.0298 -0.0326 521 TYR A CB  
12099 C CG  . TYR D 505 ? 0.6743 0.4762 0.7336 -0.0441 -0.0370 -0.0277 521 TYR A CG  
12100 C CD1 . TYR D 505 ? 0.7302 0.5030 0.7771 -0.0401 -0.0468 -0.0325 521 TYR A CD1 
12101 C CD2 . TYR D 505 ? 0.6831 0.4820 0.7401 -0.0556 -0.0342 -0.0182 521 TYR A CD2 
12102 C CE1 . TYR D 505 ? 0.8165 0.5572 0.8484 -0.0480 -0.0538 -0.0278 521 TYR A CE1 
12103 C CE2 . TYR D 505 ? 0.7239 0.4925 0.7671 -0.0635 -0.0408 -0.0135 521 TYR A CE2 
12104 C CZ  . TYR D 505 ? 0.7993 0.5384 0.8297 -0.0600 -0.0506 -0.0182 521 TYR A CZ  
12105 O OH  . TYR D 505 ? 0.8454 0.5524 0.8604 -0.0686 -0.0574 -0.0133 521 TYR A OH  
12106 N N   . GLN D 506 ? 0.6682 0.5568 0.7617 -0.0269 -0.0151 -0.0463 522 GLN A N   
12107 C CA  . GLN D 506 ? 0.6528 0.5752 0.7608 -0.0190 -0.0084 -0.0477 522 GLN A CA  
12108 C C   . GLN D 506 ? 0.6683 0.5982 0.7804 -0.0062 -0.0104 -0.0581 522 GLN A C   
12109 O O   . GLN D 506 ? 0.6393 0.5925 0.7628 0.0052  -0.0088 -0.0604 522 GLN A O   
12110 C CB  . GLN D 506 ? 0.6662 0.6047 0.7767 -0.0291 0.0011  -0.0450 522 GLN A CB  
12111 C CG  . GLN D 506 ? 0.6587 0.5964 0.7657 -0.0326 0.0037  -0.0525 522 GLN A CG  
12112 C CD  . GLN D 506 ? 0.7206 0.6718 0.8284 -0.0432 0.0123  -0.0494 522 GLN A CD  
12113 O OE1 . GLN D 506 ? 0.7658 0.7100 0.8689 -0.0538 0.0138  -0.0422 522 GLN A OE1 
12114 N NE2 . GLN D 506 ? 0.6994 0.6724 0.8142 -0.0392 0.0179  -0.0546 522 GLN A NE2 
12115 N N   . PHE D 507 ? 0.6979 0.6078 0.8002 -0.0082 -0.0141 -0.0646 523 PHE A N   
12116 C CA  . PHE D 507 ? 0.6874 0.6030 0.7926 0.0040  -0.0163 -0.0747 523 PHE A CA  
12117 C C   . PHE D 507 ? 0.7224 0.6250 0.8256 0.0171  -0.0260 -0.0777 523 PHE A C   
12118 O O   . PHE D 507 ? 0.7204 0.6379 0.8312 0.0310  -0.0271 -0.0844 523 PHE A O   
12119 C CB  . PHE D 507 ? 0.7388 0.6402 0.8343 -0.0031 -0.0161 -0.0809 523 PHE A CB  
12120 C CG  . PHE D 507 ? 0.7036 0.6244 0.8036 -0.0127 -0.0063 -0.0797 523 PHE A CG  
12121 C CD1 . PHE D 507 ? 0.6631 0.6144 0.7755 -0.0057 0.0004  -0.0831 523 PHE A CD1 
12122 C CD2 . PHE D 507 ? 0.7200 0.6298 0.8121 -0.0286 -0.0036 -0.0747 523 PHE A CD2 
12123 C CE1 . PHE D 507 ? 0.6334 0.6022 0.7493 -0.0137 0.0090  -0.0818 523 PHE A CE1 
12124 C CE2 . PHE D 507 ? 0.6840 0.6128 0.7803 -0.0363 0.0051  -0.0738 523 PHE A CE2 
12125 C CZ  . PHE D 507 ? 0.6303 0.5880 0.7383 -0.0285 0.0112  -0.0774 523 PHE A CZ  
12126 N N   . GLN D 508 ? 0.7531 0.6307 0.8469 0.0134  -0.0327 -0.0725 524 GLN A N   
12127 C CA  . GLN D 508 ? 0.7269 0.5975 0.8210 0.0273  -0.0415 -0.0744 524 GLN A CA  
12128 C C   . GLN D 508 ? 0.6955 0.5997 0.8065 0.0370  -0.0376 -0.0722 524 GLN A C   
12129 O O   . GLN D 508 ? 0.6963 0.6141 0.8145 0.0522  -0.0405 -0.0787 524 GLN A O   
12130 C CB  . GLN D 508 ? 0.6862 0.5245 0.7671 0.0213  -0.0493 -0.0686 524 GLN A CB  
12131 C CG  . GLN D 508 ? 0.8437 0.6487 0.9068 0.0121  -0.0538 -0.0715 524 GLN A CG  
12132 C CD  . GLN D 508 ? 0.8942 0.6644 0.9421 0.0072  -0.0627 -0.0668 524 GLN A CD  
12133 O OE1 . GLN D 508 ? 0.9139 0.6692 0.9530 -0.0087 -0.0610 -0.0604 524 GLN A OE1 
12134 N NE2 . GLN D 508 ? 0.9430 0.7004 0.9874 0.0212  -0.0726 -0.0700 524 GLN A NE2 
12135 N N   . PHE D 509 ? 0.6658 0.5843 0.7826 0.0279  -0.0311 -0.0632 525 PHE A N   
12136 C CA  . PHE D 509 ? 0.6315 0.5818 0.7629 0.0346  -0.0268 -0.0602 525 PHE A CA  
12137 C C   . PHE D 509 ? 0.6301 0.6090 0.7723 0.0435  -0.0216 -0.0677 525 PHE A C   
12138 O O   . PHE D 509 ? 0.6510 0.6484 0.8023 0.0567  -0.0233 -0.0717 525 PHE A O   
12139 C CB  . PHE D 509 ? 0.5835 0.5432 0.7173 0.0216  -0.0197 -0.0497 525 PHE A CB  
12140 C CG  . PHE D 509 ? 0.5960 0.5310 0.7206 0.0133  -0.0244 -0.0416 525 PHE A CG  
12141 C CD1 . PHE D 509 ? 0.6447 0.5556 0.7617 0.0194  -0.0347 -0.0432 525 PHE A CD1 
12142 C CD2 . PHE D 509 ? 0.5774 0.5121 0.6998 -0.0007 -0.0189 -0.0325 525 PHE A CD2 
12143 C CE1 . PHE D 509 ? 0.6849 0.5728 0.7928 0.0116  -0.0391 -0.0358 525 PHE A CE1 
12144 C CE2 . PHE D 509 ? 0.5566 0.4687 0.6702 -0.0087 -0.0231 -0.0252 525 PHE A CE2 
12145 C CZ  . PHE D 509 ? 0.6520 0.5409 0.7585 -0.0029 -0.0331 -0.0268 525 PHE A CZ  
12146 N N   . GLN D 510 ? 0.6354 0.6191 0.7767 0.0362  -0.0149 -0.0698 526 GLN A N   
12147 C CA  . GLN D 510 ? 0.6306 0.6424 0.7818 0.0430  -0.0090 -0.0759 526 GLN A CA  
12148 C C   . GLN D 510 ? 0.6572 0.6671 0.8090 0.0578  -0.0150 -0.0866 526 GLN A C   
12149 O O   . GLN D 510 ? 0.6728 0.7084 0.8354 0.0691  -0.0134 -0.0910 526 GLN A O   
12150 C CB  . GLN D 510 ? 0.5419 0.5569 0.6906 0.0324  -0.0015 -0.0763 526 GLN A CB  
12151 C CG  . GLN D 510 ? 0.5296 0.5748 0.6886 0.0387  0.0051  -0.0816 526 GLN A CG  
12152 C CD  . GLN D 510 ? 0.5703 0.6449 0.7397 0.0391  0.0115  -0.0759 526 GLN A CD  
12153 O OE1 . GLN D 510 ? 0.5517 0.6264 0.7219 0.0354  0.0111  -0.0678 526 GLN A OE1 
12154 N NE2 . GLN D 510 ? 0.5834 0.6832 0.7605 0.0446  0.0169  -0.0808 526 GLN A NE2 
12155 N N   . GLU D 511 ? 0.6172 0.5968 0.7568 0.0579  -0.0222 -0.0911 527 GLU A N   
12156 C CA  . GLU D 511 ? 0.6612 0.6364 0.7998 0.0727  -0.0288 -0.1013 527 GLU A CA  
12157 C C   . GLU D 511 ? 0.7030 0.6897 0.8491 0.0866  -0.0339 -0.1020 527 GLU A C   
12158 O O   . GLU D 511 ? 0.7721 0.7799 0.9270 0.1001  -0.0340 -0.1093 527 GLU A O   
12159 C CB  . GLU D 511 ? 0.7520 0.6882 0.8736 0.0698  -0.0370 -0.1048 527 GLU A CB  
12160 C CG  . GLU D 511 ? 0.8534 0.7824 0.9716 0.0846  -0.0438 -0.1161 527 GLU A CG  
12161 C CD  . GLU D 511 ? 1.0064 0.8939 1.1051 0.0806  -0.0524 -0.1193 527 GLU A CD  
12162 O OE1 . GLU D 511 ? 1.0653 0.9278 1.1544 0.0835  -0.0615 -0.1173 527 GLU A OE1 
12163 O OE2 . GLU D 511 ? 1.0751 0.9545 1.1673 0.0739  -0.0501 -0.1234 527 GLU A OE2 
12164 N N   . ALA D 512 ? 0.7028 0.6776 0.8458 0.0834  -0.0380 -0.0944 528 ALA A N   
12165 C CA  . ALA D 512 ? 0.6973 0.6801 0.8460 0.0969  -0.0442 -0.0955 528 ALA A CA  
12166 C C   . ALA D 512 ? 0.6544 0.6792 0.8203 0.1021  -0.0371 -0.0947 528 ALA A C   
12167 O O   . ALA D 512 ? 0.6617 0.7051 0.8355 0.1171  -0.0396 -0.1019 528 ALA A O   
12168 C CB  . ALA D 512 ? 0.7513 0.7118 0.8925 0.0909  -0.0498 -0.0871 528 ALA A CB  
12169 N N   . LEU D 513 ? 0.6446 0.6845 0.8154 0.0898  -0.0285 -0.0861 529 LEU A N   
12170 C CA  . LEU D 513 ? 0.6337 0.7122 0.8188 0.0923  -0.0212 -0.0845 529 LEU A CA  
12171 C C   . LEU D 513 ? 0.6595 0.7605 0.8516 0.1004  -0.0169 -0.0938 529 LEU A C   
12172 O O   . LEU D 513 ? 0.6620 0.7922 0.8651 0.1101  -0.0155 -0.0973 529 LEU A O   
12173 C CB  . LEU D 513 ? 0.5829 0.6681 0.7685 0.0765  -0.0129 -0.0739 529 LEU A CB  
12174 C CG  . LEU D 513 ? 0.5146 0.5800 0.6937 0.0672  -0.0159 -0.0641 529 LEU A CG  
12175 C CD1 . LEU D 513 ? 0.5172 0.5962 0.6989 0.0547  -0.0075 -0.0548 529 LEU A CD1 
12176 C CD2 . LEU D 513 ? 0.5892 0.6608 0.7731 0.0770  -0.0222 -0.0636 529 LEU A CD2 
12177 N N   . CYS D 514 ? 0.6633 0.7523 0.8491 0.0961  -0.0147 -0.0980 530 CYS A N   
12178 C CA  . CYS D 514 ? 0.6540 0.7632 0.8459 0.1036  -0.0107 -0.1069 530 CYS A CA  
12179 C C   . CYS D 514 ? 0.7149 0.8244 0.9084 0.1211  -0.0184 -0.1172 530 CYS A C   
12180 O O   . CYS D 514 ? 0.7087 0.8464 0.9121 0.1311  -0.0157 -0.1234 530 CYS A O   
12181 C CB  . CYS D 514 ? 0.6341 0.7289 0.8183 0.0950  -0.0074 -0.1091 530 CYS A CB  
12182 S SG  . CYS D 514 ? 0.7272 0.8318 0.9121 0.0772  0.0032  -0.0991 530 CYS A SG  
12183 N N   . GLN D 515 ? 0.7489 0.8265 0.9317 0.1250  -0.0282 -0.1194 531 GLN A N   
12184 C CA  . GLN D 515 ? 0.6875 0.7627 0.8705 0.1428  -0.0371 -0.1282 531 GLN A CA  
12185 C C   . GLN D 515 ? 0.6325 0.7397 0.8290 0.1517  -0.0365 -0.1273 531 GLN A C   
12186 O O   . GLN D 515 ? 0.6373 0.7686 0.8425 0.1653  -0.0366 -0.1356 531 GLN A O   
12187 C CB  . GLN D 515 ? 0.7216 0.7563 0.8897 0.1432  -0.0479 -0.1274 531 GLN A CB  
12188 C CG  . GLN D 515 ? 0.9290 0.9563 1.0945 0.1619  -0.0583 -0.1368 531 GLN A CG  
12189 C CD  . GLN D 515 ? 1.1011 1.0833 1.2484 0.1616  -0.0693 -0.1367 531 GLN A CD  
12190 O OE1 . GLN D 515 ? 1.2042 1.1582 1.3383 0.1519  -0.0701 -0.1368 531 GLN A OE1 
12191 N NE2 . GLN D 515 ? 1.1645 1.1397 1.3103 0.1725  -0.0784 -0.1372 531 GLN A NE2 
12192 N N   . ALA D 516 ? 0.7228 0.8319 0.9211 0.1434  -0.0353 -0.1171 532 ALA A N   
12193 C CA  . ALA D 516 ? 0.6827 0.8203 0.8927 0.1499  -0.0351 -0.1150 532 ALA A CA  
12194 C C   . ALA D 516 ? 0.7296 0.9077 0.9526 0.1486  -0.0250 -0.1154 532 ALA A C   
12195 O O   . ALA D 516 ? 0.7575 0.9653 0.9913 0.1579  -0.0249 -0.1183 532 ALA A O   
12196 C CB  . ALA D 516 ? 0.6884 0.8146 0.8954 0.1392  -0.0361 -0.1034 532 ALA A CB  
12197 N N   . ALA D 517 ? 0.6954 0.8757 0.9171 0.1370  -0.0167 -0.1126 533 ALA A N   
12198 C CA  . ALA D 517 ? 0.6801 0.8950 0.9115 0.1359  -0.0074 -0.1140 533 ALA A CA  
12199 C C   . ALA D 517 ? 0.7264 0.9512 0.9605 0.1479  -0.0077 -0.1263 533 ALA A C   
12200 O O   . ALA D 517 ? 0.7482 0.9960 0.9877 0.1460  0.0001  -0.1285 533 ALA A O   
12201 C CB  . ALA D 517 ? 0.6497 0.8616 0.8773 0.1188  0.0011  -0.1057 533 ALA A CB  
12202 N N   . LYS D 518 ? 0.7453 0.9515 0.9746 0.1604  -0.0169 -0.1344 534 LYS A N   
12203 C CA  . LYS D 518 ? 0.7547 0.9675 0.9856 0.1741  -0.0190 -0.1468 534 LYS A CA  
12204 C C   . LYS D 518 ? 0.7956 1.0095 1.0243 0.1665  -0.0116 -0.1488 534 LYS A C   
12205 O O   . LYS D 518 ? 0.8500 1.0901 1.0862 0.1721  -0.0067 -0.1550 534 LYS A O   
12206 C CB  . LYS D 518 ? 0.7814 1.0331 1.0257 0.1869  -0.0180 -0.1525 534 LYS A CB  
12207 C CG  . LYS D 518 ? 0.8173 1.0709 1.0645 0.1975  -0.0262 -0.1530 534 LYS A CG  
12208 C CD  . LYS D 518 ? 0.9130 1.2119 1.1751 0.2054  -0.0226 -0.1560 534 LYS A CD  
12209 C CE  . LYS D 518 ? 1.1039 1.4078 1.3698 0.2111  -0.0291 -0.1530 534 LYS A CE  
12210 N NZ  . LYS D 518 ? 1.1409 1.4130 1.3977 0.2229  -0.0415 -0.1576 534 LYS A NZ  
12211 N N   . HIS D 519 ? 0.7951 0.9817 1.0137 0.1532  -0.0106 -0.1432 535 HIS A N   
12212 C CA  . HIS D 519 ? 0.8647 1.0537 1.0815 0.1437  -0.0028 -0.1432 535 HIS A CA  
12213 C C   . HIS D 519 ? 0.9227 1.0961 1.1330 0.1506  -0.0064 -0.1536 535 HIS A C   
12214 O O   . HIS D 519 ? 0.9336 1.0733 1.1321 0.1493  -0.0132 -0.1547 535 HIS A O   
12215 C CB  . HIS D 519 ? 0.8294 0.9984 1.0383 0.1264  0.0003  -0.1333 535 HIS A CB  
12216 C CG  . HIS D 519 ? 0.8481 1.0178 1.0543 0.1177  0.0071  -0.1343 535 HIS A CG  
12217 N ND1 . HIS D 519 ? 0.8475 0.9905 1.0432 0.1140  0.0044  -0.1380 535 HIS A ND1 
12218 C CD2 . HIS D 519 ? 0.8515 1.0453 1.0634 0.1121  0.0163  -0.1323 535 HIS A CD2 
12219 C CE1 . HIS D 519 ? 0.8090 0.9612 1.0051 0.1068  0.0117  -0.1385 535 HIS A CE1 
12220 N NE2 . HIS D 519 ? 0.8460 1.0281 1.0515 0.1058  0.0189  -0.1350 535 HIS A NE2 
12221 N N   . GLU D 520 ? 0.9848 1.1816 1.2015 0.1567  -0.0017 -0.1608 536 GLU A N   
12222 C CA  . GLU D 520 ? 1.0279 1.2121 1.2387 0.1626  -0.0043 -0.1707 536 GLU A CA  
12223 C C   . GLU D 520 ? 1.0169 1.1884 1.2209 0.1484  0.0010  -0.1679 536 GLU A C   
12224 O O   . GLU D 520 ? 1.0405 1.2254 1.2480 0.1371  0.0090  -0.1607 536 GLU A O   
12225 C CB  . GLU D 520 ? 1.1598 1.3749 1.3802 0.1756  -0.0016 -0.1802 536 GLU A CB  
12226 C CG  . GLU D 520 ? 1.2459 1.4862 1.4767 0.1891  -0.0042 -0.1831 536 GLU A CG  
12227 C CD  . GLU D 520 ? 1.3769 1.5963 1.6021 0.2032  -0.0161 -0.1893 536 GLU A CD  
12228 O OE1 . GLU D 520 ? 1.2738 1.4598 1.4865 0.2044  -0.0225 -0.1933 536 GLU A OE1 
12229 O OE2 . GLU D 520 ? 1.4418 1.6782 1.6745 0.2131  -0.0193 -0.1902 536 GLU A OE2 
12230 N N   . GLY D 521 ? 0.9156 1.0609 1.1090 0.1493  -0.0038 -0.1740 537 GLY A N   
12231 C CA  . GLY D 521 ? 0.8244 0.9587 1.0112 0.1373  0.0005  -0.1734 537 GLY A CA  
12232 C C   . GLY D 521 ? 0.7741 0.8759 0.9491 0.1245  -0.0029 -0.1667 537 GLY A C   
12233 O O   . GLY D 521 ? 0.7972 0.8784 0.9664 0.1267  -0.0104 -0.1645 537 GLY A O   
12234 N N   . PRO D 522 ? 0.7500 0.8470 0.9208 0.1111  0.0025  -0.1638 538 PRO A N   
12235 C CA  . PRO D 522 ? 0.7305 0.8001 0.8905 0.0971  0.0005  -0.1571 538 PRO A CA  
12236 C C   . PRO D 522 ? 0.7324 0.8098 0.8971 0.0895  0.0039  -0.1459 538 PRO A C   
12237 O O   . PRO D 522 ? 0.7626 0.8682 0.9378 0.0899  0.0106  -0.1424 538 PRO A O   
12238 C CB  . PRO D 522 ? 0.6858 0.7552 0.8421 0.0866  0.0062  -0.1588 538 PRO A CB  
12239 C CG  . PRO D 522 ? 0.6911 0.7807 0.8537 0.0967  0.0089  -0.1678 538 PRO A CG  
12240 C CD  . PRO D 522 ? 0.7051 0.8197 0.8795 0.1089  0.0098  -0.1681 538 PRO A CD  
12241 N N   . LEU D 523 ? 0.6718 0.7222 0.8270 0.0817  -0.0011 -0.1403 539 LEU A N   
12242 C CA  . LEU D 523 ? 0.6683 0.7210 0.8261 0.0751  0.0004  -0.1298 539 LEU A CA  
12243 C C   . LEU D 523 ? 0.7029 0.7726 0.8650 0.0631  0.0099  -0.1229 539 LEU A C   
12244 O O   . LEU D 523 ? 0.6884 0.7723 0.8567 0.0610  0.0132  -0.1154 539 LEU A O   
12245 C CB  . LEU D 523 ? 0.6690 0.6868 0.8140 0.0684  -0.0071 -0.1260 539 LEU A CB  
12246 C CG  . LEU D 523 ? 0.6788 0.6898 0.8226 0.0595  -0.0071 -0.1151 539 LEU A CG  
12247 C CD1 . LEU D 523 ? 0.7097 0.7400 0.8640 0.0690  -0.0077 -0.1120 539 LEU A CD1 
12248 C CD2 . LEU D 523 ? 0.7715 0.7442 0.9001 0.0548  -0.0159 -0.1143 539 LEU A CD2 
12249 N N   . HIS D 524 ? 0.7023 0.7709 0.8606 0.0554  0.0142  -0.1255 540 HIS A N   
12250 C CA  . HIS D 524 ? 0.6334 0.7119 0.7928 0.0432  0.0218  -0.1184 540 HIS A CA  
12251 C C   . HIS D 524 ? 0.6068 0.7183 0.7772 0.0474  0.0293  -0.1177 540 HIS A C   
12252 O O   . HIS D 524 ? 0.6282 0.7499 0.7994 0.0388  0.0356  -0.1119 540 HIS A O   
12253 C CB  . HIS D 524 ? 0.6756 0.7440 0.8274 0.0332  0.0241  -0.1214 540 HIS A CB  
12254 C CG  . HIS D 524 ? 0.7012 0.7880 0.8574 0.0378  0.0287  -0.1291 540 HIS A CG  
12255 N ND1 . HIS D 524 ? 0.7098 0.7904 0.8638 0.0456  0.0249  -0.1389 540 HIS A ND1 
12256 C CD2 . HIS D 524 ? 0.6549 0.7644 0.8164 0.0350  0.0366  -0.1284 540 HIS A CD2 
12257 C CE1 . HIS D 524 ? 0.7117 0.8121 0.8705 0.0477  0.0305  -0.1437 540 HIS A CE1 
12258 N NE2 . HIS D 524 ? 0.6261 0.7440 0.7893 0.0413  0.0376  -0.1376 540 HIS A NE2 
12259 N N   . LYS D 525 ? 0.6515 0.7791 0.8291 0.0602  0.0285  -0.1239 541 LYS A N   
12260 C CA  . LYS D 525 ? 0.6966 0.8556 0.8839 0.0646  0.0350  -0.1238 541 LYS A CA  
12261 C C   . LYS D 525 ? 0.7540 0.9262 0.9481 0.0691  0.0343  -0.1183 541 LYS A C   
12262 O O   . LYS D 525 ? 0.7203 0.9186 0.9216 0.0712  0.0397  -0.1169 541 LYS A O   
12263 C CB  . LYS D 525 ? 0.6891 0.8598 0.8801 0.0752  0.0352  -0.1345 541 LYS A CB  
12264 C CG  . LYS D 525 ? 0.7569 0.9186 0.9419 0.0704  0.0367  -0.1401 541 LYS A CG  
12265 C CD  . LYS D 525 ? 0.8214 0.9855 1.0074 0.0817  0.0342  -0.1517 541 LYS A CD  
12266 C CE  . LYS D 525 ? 0.8231 1.0182 1.0191 0.0916  0.0386  -0.1562 541 LYS A CE  
12267 N NZ  . LYS D 525 ? 0.9598 1.1741 1.1582 0.0862  0.0469  -0.1553 541 LYS A NZ  
12268 N N   . CYS D 526 ? 0.8322 0.9863 1.0232 0.0697  0.0278  -0.1150 542 CYS A N   
12269 C CA  . CYS D 526 ? 0.8492 1.0148 1.0468 0.0762  0.0255  -0.1117 542 CYS A CA  
12270 C C   . CYS D 526 ? 0.8185 0.9982 1.0190 0.0678  0.0311  -0.1015 542 CYS A C   
12271 O O   . CYS D 526 ? 0.8282 0.9956 1.0228 0.0561  0.0332  -0.0944 542 CYS A O   
12272 C CB  . CYS D 526 ? 0.8397 0.9793 1.0317 0.0787  0.0164  -0.1109 542 CYS A CB  
12273 S SG  . CYS D 526 ? 0.9015 1.0508 1.0995 0.0814  0.0139  -0.1031 542 CYS A SG  
12274 N N   . ASP D 527 ? 0.6273 0.8325 0.8366 0.0739  0.0330  -0.1009 543 ASP A N   
12275 C CA  . ASP D 527 ? 0.5447 0.7644 0.7565 0.0669  0.0376  -0.0914 543 ASP A CA  
12276 C C   . ASP D 527 ? 0.6195 0.8484 0.8375 0.0742  0.0332  -0.0901 543 ASP A C   
12277 O O   . ASP D 527 ? 0.5958 0.8456 0.8216 0.0848  0.0327  -0.0964 543 ASP A O   
12278 C CB  . ASP D 527 ? 0.5471 0.7934 0.7626 0.0653  0.0457  -0.0917 543 ASP A CB  
12279 C CG  . ASP D 527 ? 0.5471 0.8077 0.7637 0.0583  0.0499  -0.0820 543 ASP A CG  
12280 O OD1 . ASP D 527 ? 0.5610 0.8085 0.7751 0.0539  0.0466  -0.0750 543 ASP A OD1 
12281 O OD2 . ASP D 527 ? 0.5252 0.8095 0.7447 0.0577  0.0557  -0.0817 543 ASP A OD2 
12282 N N   . ILE D 528 ? 0.6598 0.8750 0.8745 0.0685  0.0302  -0.0820 544 ILE A N   
12283 C CA  . ILE D 528 ? 0.5794 0.7996 0.7992 0.0758  0.0246  -0.0812 544 ILE A CA  
12284 C C   . ILE D 528 ? 0.5593 0.8082 0.7859 0.0738  0.0294  -0.0759 544 ILE A C   
12285 O O   . ILE D 528 ? 0.6261 0.8803 0.8565 0.0768  0.0257  -0.0729 544 ILE A O   
12286 C CB  . ILE D 528 ? 0.5376 0.7293 0.7505 0.0711  0.0184  -0.0752 544 ILE A CB  
12287 C CG1 . ILE D 528 ? 0.4715 0.6612 0.6807 0.0572  0.0231  -0.0635 544 ILE A CG1 
12288 C CG2 . ILE D 528 ? 0.6054 0.7668 0.8095 0.0714  0.0135  -0.0800 544 ILE A CG2 
12289 C CD1 . ILE D 528 ? 0.4287 0.5940 0.6317 0.0520  0.0177  -0.0569 544 ILE A CD1 
12290 N N   . SER D 529 ? 0.5326 0.7989 0.7598 0.0680  0.0373  -0.0741 545 SER A N   
12291 C CA  . SER D 529 ? 0.5081 0.7989 0.7393 0.0642  0.0416  -0.0681 545 SER A CA  
12292 C C   . SER D 529 ? 0.5424 0.8567 0.7836 0.0759  0.0388  -0.0741 545 SER A C   
12293 O O   . SER D 529 ? 0.5934 0.9107 0.8386 0.0873  0.0358  -0.0841 545 SER A O   
12294 C CB  . SER D 529 ? 0.5597 0.8663 0.7890 0.0575  0.0500  -0.0666 545 SER A CB  
12295 O OG  . SER D 529 ? 0.5465 0.8336 0.7667 0.0474  0.0526  -0.0615 545 SER A OG  
12296 N N   . ASN D 530 ? 0.5198 0.8498 0.7645 0.0730  0.0393  -0.0680 546 ASN A N   
12297 C CA  . ASN D 530 ? 0.5531 0.9114 0.8078 0.0826  0.0378  -0.0729 546 ASN A CA  
12298 C C   . ASN D 530 ? 0.5969 0.9467 0.8558 0.0950  0.0286  -0.0783 546 ASN A C   
12299 O O   . ASN D 530 ? 0.6187 0.9906 0.8857 0.1021  0.0262  -0.0806 546 ASN A O   
12300 C CB  . ASN D 530 ? 0.6006 0.9833 0.8605 0.0888  0.0423  -0.0817 546 ASN A CB  
12301 C CG  . ASN D 530 ? 0.6128 1.0139 0.8702 0.0782  0.0509  -0.0765 546 ASN A CG  
12302 O OD1 . ASN D 530 ? 0.5645 0.9698 0.8190 0.0683  0.0533  -0.0671 546 ASN A OD1 
12303 N ND2 . ASN D 530 ? 0.7151 1.1255 0.9725 0.0801  0.0553  -0.0824 546 ASN A ND2 
12304 N N   . SER D 531 ? 0.6139 0.9326 0.8668 0.0980  0.0231  -0.0810 547 SER A N   
12305 C CA  . SER D 531 ? 0.6413 0.9485 0.8959 0.1102  0.0136  -0.0863 547 SER A CA  
12306 C C   . SER D 531 ? 0.6415 0.9384 0.8943 0.1053  0.0094  -0.0774 547 SER A C   
12307 O O   . SER D 531 ? 0.6539 0.9201 0.8977 0.0982  0.0066  -0.0717 547 SER A O   
12308 C CB  . SER D 531 ? 0.6796 0.9550 0.9264 0.1143  0.0086  -0.0920 547 SER A CB  
12309 O OG  . SER D 531 ? 0.6683 0.9277 0.9138 0.1248  -0.0013 -0.0958 547 SER A OG  
12310 N N   . THR D 532 ? 0.6664 0.9898 0.9274 0.1086  0.0092  -0.0762 548 THR A N   
12311 C CA  . THR D 532 ? 0.6187 0.9346 0.8785 0.1043  0.0052  -0.0679 548 THR A CA  
12312 C C   . THR D 532 ? 0.6649 0.9541 0.9210 0.1139  -0.0053 -0.0714 548 THR A C   
12313 O O   . THR D 532 ? 0.7054 0.9755 0.9564 0.1083  -0.0092 -0.0639 548 THR A O   
12314 C CB  . THR D 532 ? 0.5690 0.9210 0.8386 0.1059  0.0069  -0.0666 548 THR A CB  
12315 O OG1 . THR D 532 ? 0.6103 0.9842 0.8890 0.1221  0.0034  -0.0780 548 THR A OG1 
12316 C CG2 . THR D 532 ? 0.5984 0.9730 0.8687 0.0940  0.0169  -0.0612 548 THR A CG2 
12317 N N   . GLU D 533 ? 0.7280 1.0145 0.9856 0.1281  -0.0103 -0.0826 549 GLU A N   
12318 C CA  . GLU D 533 ? 0.7315 0.9876 0.9825 0.1369  -0.0208 -0.0861 549 GLU A CA  
12319 C C   . GLU D 533 ? 0.7259 0.9425 0.9637 0.1254  -0.0215 -0.0803 549 GLU A C   
12320 O O   . GLU D 533 ? 0.7135 0.9035 0.9439 0.1238  -0.0282 -0.0760 549 GLU A O   
12321 C CB  . GLU D 533 ? 0.7620 1.0231 1.0159 0.1543  -0.0255 -0.0997 549 GLU A CB  
12322 C CG  . GLU D 533 ? 0.7963 1.1020 1.0639 0.1635  -0.0217 -0.1063 549 GLU A CG  
12323 C CD  . GLU D 533 ? 0.9705 1.2966 1.2413 0.1556  -0.0108 -0.1067 549 GLU A CD  
12324 O OE1 . GLU D 533 ? 1.0486 1.3623 1.3149 0.1570  -0.0095 -0.1122 549 GLU A OE1 
12325 O OE2 . GLU D 533 ? 0.9926 1.3464 1.2695 0.1474  -0.0036 -0.1011 549 GLU A OE2 
12326 N N   . ALA D 534 ? 0.6875 0.9008 0.9219 0.1168  -0.0144 -0.0799 550 ALA A N   
12327 C CA  . ALA D 534 ? 0.6389 0.8193 0.8615 0.1043  -0.0138 -0.0741 550 ALA A CA  
12328 C C   . ALA D 534 ? 0.6227 0.7987 0.8427 0.0907  -0.0112 -0.0616 550 ALA A C   
12329 O O   . ALA D 534 ? 0.5799 0.7258 0.7903 0.0836  -0.0149 -0.0562 550 ALA A O   
12330 C CB  . ALA D 534 ? 0.5861 0.7696 0.8071 0.0988  -0.0063 -0.0769 550 ALA A CB  
12331 N N   . GLY D 535 ? 0.6580 0.8635 0.8857 0.0867  -0.0050 -0.0569 551 GLY A N   
12332 C CA  . GLY D 535 ? 0.5981 0.8008 0.8232 0.0744  -0.0027 -0.0452 551 GLY A CA  
12333 C C   . GLY D 535 ? 0.6484 0.8370 0.8719 0.0780  -0.0113 -0.0422 551 GLY A C   
12334 O O   . GLY D 535 ? 0.6927 0.8570 0.9080 0.0687  -0.0131 -0.0344 551 GLY A O   
12335 N N   . GLN D 536 ? 0.6160 0.8205 0.8472 0.0918  -0.0168 -0.0485 552 GLN A N   
12336 C CA  . GLN D 536 ? 0.6203 0.8124 0.8502 0.0975  -0.0259 -0.0469 552 GLN A CA  
12337 C C   . GLN D 536 ? 0.5646 0.7145 0.7819 0.0970  -0.0331 -0.0472 552 GLN A C   
12338 O O   . GLN D 536 ? 0.5498 0.6782 0.7602 0.0909  -0.0372 -0.0399 552 GLN A O   
12339 C CB  . GLN D 536 ? 0.6835 0.8985 0.9232 0.1152  -0.0313 -0.0565 552 GLN A CB  
12340 C CG  . GLN D 536 ? 0.6843 0.8888 0.9228 0.1224  -0.0411 -0.0554 552 GLN A CG  
12341 C CD  . GLN D 536 ? 0.6510 0.8683 0.8926 0.1119  -0.0380 -0.0448 552 GLN A CD  
12342 O OE1 . GLN D 536 ? 0.5543 0.8069 0.8057 0.1102  -0.0321 -0.0437 552 GLN A OE1 
12343 N NE2 . GLN D 536 ? 0.6806 0.8681 0.9124 0.1021  -0.0408 -0.0360 552 GLN A NE2 
12344 N N   . LYS D 537 ? 0.6418 0.7794 0.8552 0.1033  -0.0348 -0.0558 553 LYS A N   
12345 C CA  . LYS D 537 ? 0.6526 0.7500 0.8527 0.1034  -0.0421 -0.0574 553 LYS A CA  
12346 C C   . LYS D 537 ? 0.6325 0.7063 0.8227 0.0856  -0.0386 -0.0475 553 LYS A C   
12347 O O   . LYS D 537 ? 0.6703 0.7147 0.8507 0.0820  -0.0450 -0.0434 553 LYS A O   
12348 C CB  . LYS D 537 ? 0.6176 0.7098 0.8155 0.1115  -0.0429 -0.0683 553 LYS A CB  
12349 C CG  . LYS D 537 ? 0.6555 0.7140 0.8421 0.1199  -0.0538 -0.0741 553 LYS A CG  
12350 C CD  . LYS D 537 ? 0.6861 0.7514 0.8747 0.1338  -0.0558 -0.0867 553 LYS A CD  
12351 C CE  . LYS D 537 ? 0.8068 0.8375 0.9826 0.1436  -0.0676 -0.0931 553 LYS A CE  
12352 N NZ  . LYS D 537 ? 0.8875 0.9141 1.0633 0.1508  -0.0760 -0.0903 553 LYS A NZ  
12353 N N   . LEU D 538 ? 0.6406 0.7278 0.8332 0.0745  -0.0284 -0.0436 554 LEU A N   
12354 C CA  . LEU D 538 ? 0.6245 0.6942 0.8088 0.0577  -0.0241 -0.0342 554 LEU A CA  
12355 C C   . LEU D 538 ? 0.6237 0.6921 0.8076 0.0510  -0.0251 -0.0239 554 LEU A C   
12356 O O   . LEU D 538 ? 0.6051 0.6466 0.7791 0.0420  -0.0279 -0.0176 554 LEU A O   
12357 C CB  . LEU D 538 ? 0.6152 0.7036 0.8028 0.0499  -0.0135 -0.0332 554 LEU A CB  
12358 C CG  . LEU D 538 ? 0.5435 0.6188 0.7234 0.0334  -0.0079 -0.0244 554 LEU A CG  
12359 C CD1 . LEU D 538 ? 0.5130 0.5551 0.6813 0.0290  -0.0117 -0.0265 554 LEU A CD1 
12360 C CD2 . LEU D 538 ? 0.4707 0.5684 0.6545 0.0277  0.0023  -0.0236 554 LEU A CD2 
12361 N N   . PHE D 539 ? 0.6395 0.7380 0.8338 0.0543  -0.0226 -0.0220 555 PHE A N   
12362 C CA  . PHE D 539 ? 0.5959 0.6966 0.7904 0.0476  -0.0230 -0.0121 555 PHE A CA  
12363 C C   . PHE D 539 ? 0.6025 0.6790 0.7914 0.0523  -0.0334 -0.0112 555 PHE A C   
12364 O O   . PHE D 539 ? 0.5888 0.6518 0.7724 0.0433  -0.0346 -0.0022 555 PHE A O   
12365 C CB  . PHE D 539 ? 0.5081 0.6469 0.7147 0.0515  -0.0192 -0.0119 555 PHE A CB  
12366 C CG  . PHE D 539 ? 0.5613 0.7051 0.7682 0.0438  -0.0189 -0.0018 555 PHE A CG  
12367 C CD1 . PHE D 539 ? 0.5612 0.7061 0.7642 0.0293  -0.0116 0.0074  555 PHE A CD1 
12368 C CD2 . PHE D 539 ? 0.5967 0.7445 0.8076 0.0515  -0.0262 -0.0018 555 PHE A CD2 
12369 C CE1 . PHE D 539 ? 0.5371 0.6860 0.7396 0.0219  -0.0114 0.0168  555 PHE A CE1 
12370 C CE2 . PHE D 539 ? 0.5330 0.6862 0.7442 0.0440  -0.0259 0.0076  555 PHE A CE2 
12371 C CZ  . PHE D 539 ? 0.5381 0.6914 0.7449 0.0289  -0.0184 0.0170  555 PHE A CZ  
12372 N N   . ASN D 540 ? 0.6251 0.6946 0.8141 0.0664  -0.0412 -0.0205 556 ASN A N   
12373 C CA  . ASN D 540 ? 0.6121 0.6557 0.7939 0.0719  -0.0520 -0.0204 556 ASN A CA  
12374 C C   . ASN D 540 ? 0.6484 0.6538 0.8153 0.0594  -0.0538 -0.0143 556 ASN A C   
12375 O O   . ASN D 540 ? 0.6174 0.6018 0.7773 0.0577  -0.0606 -0.0094 556 ASN A O   
12376 C CB  . ASN D 540 ? 0.6359 0.6742 0.8175 0.0892  -0.0602 -0.0321 556 ASN A CB  
12377 C CG  . ASN D 540 ? 0.7447 0.8203 0.9407 0.1033  -0.0604 -0.0385 556 ASN A CG  
12378 O OD1 . ASN D 540 ? 0.6711 0.7740 0.8765 0.1005  -0.0564 -0.0334 556 ASN A OD1 
12379 N ND2 . ASN D 540 ? 0.7922 0.8685 0.9893 0.1189  -0.0659 -0.0499 556 ASN A ND2 
12380 N N   . MET D 541 ? 0.6826 0.6787 0.8443 0.0506  -0.0480 -0.0149 557 MET A N   
12381 C CA  . MET D 541 ? 0.6545 0.6179 0.8026 0.0370  -0.0486 -0.0089 557 MET A CA  
12382 C C   . MET D 541 ? 0.6195 0.5908 0.7684 0.0226  -0.0410 0.0018  557 MET A C   
12383 O O   . MET D 541 ? 0.6133 0.5634 0.7537 0.0133  -0.0433 0.0095  557 MET A O   
12384 C CB  . MET D 541 ? 0.6482 0.5962 0.7889 0.0337  -0.0468 -0.0146 557 MET A CB  
12385 C CG  . MET D 541 ? 0.6759 0.5952 0.8034 0.0178  -0.0456 -0.0086 557 MET A CG  
12386 S SD  . MET D 541 ? 0.6712 0.6063 0.8013 0.0015  -0.0327 -0.0009 557 MET A SD  
12387 C CE  . MET D 541 ? 0.5951 0.5489 0.7315 0.0076  -0.0272 -0.0111 557 MET A CE  
12388 N N   . LEU D 542 ? 0.6183 0.6194 0.7766 0.0206  -0.0320 0.0024  558 LEU A N   
12389 C CA  . LEU D 542 ? 0.6558 0.6626 0.8130 0.0068  -0.0246 0.0122  558 LEU A CA  
12390 C C   . LEU D 542 ? 0.6194 0.6241 0.7763 0.0040  -0.0281 0.0206  558 LEU A C   
12391 O O   . LEU D 542 ? 0.6354 0.6200 0.7836 -0.0070 -0.0284 0.0283  558 LEU A O   
12392 C CB  . LEU D 542 ? 0.6111 0.6503 0.7774 0.0063  -0.0154 0.0113  558 LEU A CB  
12393 C CG  . LEU D 542 ? 0.5087 0.5514 0.6753 0.0081  -0.0112 0.0035  558 LEU A CG  
12394 C CD1 . LEU D 542 ? 0.4582 0.5323 0.6328 0.0071  -0.0026 0.0041  558 LEU A CD1 
12395 C CD2 . LEU D 542 ? 0.5200 0.5370 0.6754 -0.0034 -0.0097 0.0063  558 LEU A CD2 
12396 N N   . ARG D 543 ? 0.6517 0.6764 0.8178 0.0143  -0.0314 0.0187  559 ARG A N   
12397 C CA  . ARG D 543 ? 0.5944 0.6213 0.7615 0.0120  -0.0344 0.0265  559 ARG A CA  
12398 C C   . ARG D 543 ? 0.5793 0.5711 0.7350 0.0086  -0.0423 0.0305  559 ARG A C   
12399 O O   . ARG D 543 ? 0.6318 0.6204 0.7858 0.0033  -0.0440 0.0385  559 ARG A O   
12400 C CB  . ARG D 543 ? 0.5680 0.6222 0.7469 0.0254  -0.0379 0.0219  559 ARG A CB  
12401 C CG  . ARG D 543 ? 0.6154 0.6607 0.7949 0.0413  -0.0476 0.0121  559 ARG A CG  
12402 C CD  . ARG D 543 ? 0.6135 0.6778 0.8016 0.0523  -0.0536 0.0108  559 ARG A CD  
12403 N NE  . ARG D 543 ? 0.6479 0.7000 0.8308 0.0425  -0.0552 0.0214  559 ARG A NE  
12404 C CZ  . ARG D 543 ? 0.7066 0.7288 0.8802 0.0430  -0.0638 0.0239  559 ARG A CZ  
12405 N NH1 . ARG D 543 ? 0.7422 0.7439 0.9105 0.0542  -0.0727 0.0163  559 ARG A NH1 
12406 N NH2 . ARG D 543 ? 0.7277 0.7381 0.8957 0.0314  -0.0635 0.0343  559 ARG A NH2 
12407 N N   . LEU D 544 ? 0.6314 0.5963 0.7783 0.0106  -0.0472 0.0253  560 LEU A N   
12408 C CA  . LEU D 544 ? 0.6586 0.5899 0.7937 0.0079  -0.0556 0.0288  560 LEU A CA  
12409 C C   . LEU D 544 ? 0.6826 0.5983 0.8091 -0.0090 -0.0514 0.0390  560 LEU A C   
12410 O O   . LEU D 544 ? 0.7411 0.6427 0.8625 -0.0128 -0.0561 0.0457  560 LEU A O   
12411 C CB  . LEU D 544 ? 0.7165 0.6210 0.8422 0.0133  -0.0620 0.0209  560 LEU A CB  
12412 C CG  . LEU D 544 ? 0.6905 0.6046 0.8224 0.0318  -0.0689 0.0110  560 LEU A CG  
12413 C CD1 . LEU D 544 ? 0.7492 0.6332 0.8693 0.0366  -0.0760 0.0035  560 LEU A CD1 
12414 C CD2 . LEU D 544 ? 0.6994 0.6197 0.8354 0.0398  -0.0758 0.0135  560 LEU A CD2 
12415 N N   . GLY D 545 ? 0.7078 0.6261 0.8325 -0.0189 -0.0430 0.0403  561 GLY A N   
12416 C CA  . GLY D 545 ? 0.6988 0.5977 0.8132 -0.0343 -0.0402 0.0485  561 GLY A CA  
12417 C C   . GLY D 545 ? 0.7509 0.6149 0.8520 -0.0371 -0.0465 0.0458  561 GLY A C   
12418 O O   . GLY D 545 ? 0.7370 0.5958 0.8369 -0.0309 -0.0485 0.0372  561 GLY A O   
12419 N N   . LYS D 546 ? 0.8154 0.6547 0.9059 -0.0463 -0.0501 0.0529  562 LYS A N   
12420 C CA  . LYS D 546 ? 0.8562 0.6604 0.9325 -0.0486 -0.0577 0.0506  562 LYS A CA  
12421 C C   . LYS D 546 ? 0.8925 0.6784 0.9635 -0.0437 -0.0681 0.0535  562 LYS A C   
12422 O O   . LYS D 546 ? 0.9245 0.6789 0.9813 -0.0509 -0.0735 0.0564  562 LYS A O   
12423 C CB  . LYS D 546 ? 0.8753 0.6613 0.9403 -0.0653 -0.0534 0.0552  562 LYS A CB  
12424 C CG  . LYS D 546 ? 0.9063 0.6949 0.9702 -0.0768 -0.0489 0.0657  562 LYS A CG  
12425 C CD  . LYS D 546 ? 0.9912 0.7636 1.0440 -0.0927 -0.0443 0.0686  562 LYS A CD  
12426 C CE  . LYS D 546 ? 1.0282 0.7636 1.0648 -0.0993 -0.0523 0.0699  562 LYS A CE  
12427 N NZ  . LYS D 546 ? 1.0685 0.7899 1.0943 -0.1144 -0.0480 0.0709  562 LYS A NZ  
12428 N N   . SER D 547 ? 0.8148 0.6208 0.8967 -0.0314 -0.0710 0.0524  563 SER A N   
12429 C CA  . SER D 547 ? 0.7772 0.5711 0.8561 -0.0247 -0.0808 0.0547  563 SER A CA  
12430 C C   . SER D 547 ? 0.8466 0.6190 0.9181 -0.0127 -0.0915 0.0463  563 SER A C   
12431 O O   . SER D 547 ? 0.8479 0.5958 0.9097 -0.0102 -0.1011 0.0480  563 SER A O   
12432 C CB  . SER D 547 ? 0.7925 0.6199 0.8867 -0.0158 -0.0795 0.0558  563 SER A CB  
12433 O OG  . SER D 547 ? 0.7856 0.6359 0.8906 -0.0023 -0.0789 0.0463  563 SER A OG  
12434 N N   . GLU D 548 ? 0.8143 0.5952 0.8897 -0.0048 -0.0903 0.0373  564 GLU A N   
12435 C CA  . GLU D 548 ? 0.7992 0.5554 0.8645 0.0044  -0.0996 0.0290  564 GLU A CA  
12436 C C   . GLU D 548 ? 0.8363 0.5680 0.8884 -0.0077 -0.0973 0.0278  564 GLU A C   
12437 O O   . GLU D 548 ? 0.8193 0.5604 0.8736 -0.0205 -0.0874 0.0316  564 GLU A O   
12438 C CB  . GLU D 548 ? 0.8226 0.6039 0.9001 0.0217  -0.1003 0.0189  564 GLU A CB  
12439 C CG  . GLU D 548 ? 0.8666 0.6747 0.9575 0.0343  -0.1030 0.0189  564 GLU A CG  
12440 C CD  . GLU D 548 ? 1.0349 0.8193 1.1167 0.0432  -0.1161 0.0187  564 GLU A CD  
12441 O OE1 . GLU D 548 ? 1.0455 0.7911 1.1097 0.0394  -0.1231 0.0185  564 GLU A OE1 
12442 O OE2 . GLU D 548 ? 1.1461 0.9505 1.2378 0.0540  -0.1196 0.0186  564 GLU A OE2 
12443 N N   . PRO D 549 ? 0.9010 0.6001 0.9381 -0.0043 -0.1065 0.0226  565 PRO A N   
12444 C CA  . PRO D 549 ? 0.8912 0.5678 0.9152 -0.0154 -0.1047 0.0201  565 PRO A CA  
12445 C C   . PRO D 549 ? 0.8783 0.5804 0.9131 -0.0137 -0.0958 0.0138  565 PRO A C   
12446 O O   . PRO D 549 ? 0.8912 0.6198 0.9396 0.0003  -0.0948 0.0081  565 PRO A O   
12447 C CB  . PRO D 549 ? 0.8985 0.5402 0.9063 -0.0069 -0.1176 0.0139  565 PRO A CB  
12448 C CG  . PRO D 549 ? 0.9506 0.5871 0.9583 0.0023  -0.1262 0.0169  565 PRO A CG  
12449 C CD  . PRO D 549 ? 0.9167 0.5958 0.9462 0.0091  -0.1196 0.0191  565 PRO A CD  
12450 N N   . TRP D 550 ? 0.8689 0.5631 0.8971 -0.0277 -0.0897 0.0142  566 TRP A N   
12451 C CA  . TRP D 550 ? 0.8652 0.5829 0.9029 -0.0259 -0.0817 0.0079  566 TRP A CA  
12452 C C   . TRP D 550 ? 0.8568 0.5692 0.8928 -0.0113 -0.0881 -0.0031 566 TRP A C   
12453 O O   . TRP D 550 ? 0.8346 0.5749 0.8839 -0.0018 -0.0835 -0.0090 566 TRP A O   
12454 C CB  . TRP D 550 ? 0.8491 0.5602 0.8799 -0.0431 -0.0743 0.0096  566 TRP A CB  
12455 C CG  . TRP D 550 ? 0.8789 0.5537 0.8902 -0.0512 -0.0800 0.0064  566 TRP A CG  
12456 C CD1 . TRP D 550 ? 0.9274 0.5723 0.9225 -0.0650 -0.0834 0.0121  566 TRP A CD1 
12457 C CD2 . TRP D 550 ? 0.8493 0.5139 0.8542 -0.0473 -0.0826 -0.0031 566 TRP A CD2 
12458 N NE1 . TRP D 550 ? 0.9195 0.5366 0.8984 -0.0705 -0.0879 0.0070  566 TRP A NE1 
12459 C CE2 . TRP D 550 ? 0.8618 0.4899 0.8462 -0.0597 -0.0877 -0.0024 566 TRP A CE2 
12460 C CE3 . TRP D 550 ? 0.8779 0.5604 0.8918 -0.0350 -0.0812 -0.0121 566 TRP A CE3 
12461 C CZ2 . TRP D 550 ? 0.9091 0.5177 0.8814 -0.0603 -0.0916 -0.0102 566 TRP A CZ2 
12462 C CZ3 . TRP D 550 ? 0.8901 0.5533 0.8926 -0.0349 -0.0851 -0.0199 566 TRP A CZ3 
12463 C CH2 . TRP D 550 ? 0.9399 0.5665 0.9217 -0.0476 -0.0902 -0.0189 566 TRP A CH2 
12464 N N   . THR D 551 ? 0.8314 0.5076 0.8503 -0.0093 -0.0988 -0.0061 567 THR A N   
12465 C CA  . THR D 551 ? 0.9059 0.5742 0.9212 0.0054  -0.1059 -0.0168 567 THR A CA  
12466 C C   . THR D 551 ? 0.9354 0.6323 0.9670 0.0252  -0.1078 -0.0213 567 THR A C   
12467 O O   . THR D 551 ? 0.9352 0.6490 0.9746 0.0365  -0.1065 -0.0299 567 THR A O   
12468 C CB  . THR D 551 ? 1.0008 0.6235 0.9934 0.0051  -0.1185 -0.0181 567 THR A CB  
12469 O OG1 . THR D 551 ? 1.0512 0.6649 1.0417 0.0073  -0.1247 -0.0115 567 THR A OG1 
12470 C CG2 . THR D 551 ? 0.9892 0.5854 0.9654 -0.0150 -0.1164 -0.0149 567 THR A CG2 
12471 N N   . LEU D 552 ? 0.9540 0.6584 0.9913 0.0293  -0.1105 -0.0154 568 LEU A N   
12472 C CA  . LEU D 552 ? 0.9092 0.6445 0.9629 0.0466  -0.1116 -0.0190 568 LEU A CA  
12473 C C   . LEU D 552 ? 0.8526 0.6311 0.9258 0.0455  -0.0991 -0.0189 568 LEU A C   
12474 O O   . LEU D 552 ? 0.8439 0.6481 0.9291 0.0594  -0.0982 -0.0262 568 LEU A O   
12475 C CB  . LEU D 552 ? 0.9124 0.6453 0.9668 0.0486  -0.1170 -0.0119 568 LEU A CB  
12476 C CG  . LEU D 552 ? 0.9035 0.6715 0.9755 0.0641  -0.1174 -0.0141 568 LEU A CG  
12477 C CD1 . LEU D 552 ? 0.9005 0.6729 0.9745 0.0842  -0.1243 -0.0264 568 LEU A CD1 
12478 C CD2 . LEU D 552 ? 0.8926 0.6546 0.9633 0.0643  -0.1232 -0.0067 568 LEU A CD2 
12479 N N   . ALA D 553 ? 0.7897 0.5760 0.8653 0.0293  -0.0896 -0.0107 569 ALA A N   
12480 C CA  . ALA D 553 ? 0.7751 0.5974 0.8657 0.0264  -0.0778 -0.0104 569 ALA A CA  
12481 C C   . ALA D 553 ? 0.8166 0.6466 0.9095 0.0322  -0.0751 -0.0203 569 ALA A C   
12482 O O   . ALA D 553 ? 0.8488 0.7105 0.9557 0.0414  -0.0706 -0.0249 569 ALA A O   
12483 C CB  . ALA D 553 ? 0.7366 0.5572 0.8245 0.0076  -0.0694 -0.0012 569 ALA A CB  
12484 N N   . LEU D 554 ? 0.8214 0.6227 0.9001 0.0264  -0.0779 -0.0237 570 LEU A N   
12485 C CA  . LEU D 554 ? 0.8735 0.6803 0.9532 0.0306  -0.0754 -0.0329 570 LEU A CA  
12486 C C   . LEU D 554 ? 0.8588 0.6725 0.9430 0.0507  -0.0823 -0.0426 570 LEU A C   
12487 O O   . LEU D 554 ? 0.8296 0.6679 0.9241 0.0586  -0.0778 -0.0495 570 LEU A O   
12488 C CB  . LEU D 554 ? 0.9098 0.6821 0.9715 0.0193  -0.0779 -0.0342 570 LEU A CB  
12489 C CG  . LEU D 554 ? 0.8569 0.6262 0.9151 0.0205  -0.0764 -0.0433 570 LEU A CG  
12490 C CD1 . LEU D 554 ? 0.7957 0.6018 0.8696 0.0193  -0.0648 -0.0442 570 LEU A CD1 
12491 C CD2 . LEU D 554 ? 0.8984 0.6358 0.9389 0.0044  -0.0776 -0.0413 570 LEU A CD2 
12492 N N   . GLU D 555 ? 0.8478 0.6396 0.9235 0.0595  -0.0937 -0.0436 571 GLU A N   
12493 C CA  . GLU D 555 ? 0.8654 0.6621 0.9441 0.0799  -0.1015 -0.0533 571 GLU A CA  
12494 C C   . GLU D 555 ? 0.8361 0.6775 0.9359 0.0908  -0.0963 -0.0546 571 GLU A C   
12495 O O   . GLU D 555 ? 0.8084 0.6673 0.9156 0.1055  -0.0974 -0.0640 571 GLU A O   
12496 C CB  . GLU D 555 ? 0.9270 0.6919 0.9921 0.0873  -0.1150 -0.0532 571 GLU A CB  
12497 C CG  . GLU D 555 ? 0.9545 0.7212 1.0205 0.1093  -0.1242 -0.0639 571 GLU A CG  
12498 C CD  . GLU D 555 ? 1.0686 0.8102 1.1238 0.1186  -0.1374 -0.0634 571 GLU A CD  
12499 O OE1 . GLU D 555 ? 1.1035 0.8633 1.1688 0.1209  -0.1371 -0.0579 571 GLU A OE1 
12500 O OE2 . GLU D 555 ? 1.0947 0.7996 1.1315 0.1243  -0.1482 -0.0686 571 GLU A OE2 
12501 N N   . ASN D 556 ? 0.8146 0.6751 0.9236 0.0833  -0.0907 -0.0455 572 ASN A N   
12502 C CA  . ASN D 556 ? 0.8558 0.7592 0.9839 0.0915  -0.0853 -0.0462 572 ASN A CA  
12503 C C   . ASN D 556 ? 0.7770 0.7079 0.9152 0.0928  -0.0762 -0.0519 572 ASN A C   
12504 O O   . ASN D 556 ? 0.7645 0.7284 0.9165 0.1041  -0.0740 -0.0567 572 ASN A O   
12505 C CB  . ASN D 556 ? 0.8157 0.7320 0.9495 0.0802  -0.0799 -0.0347 572 ASN A CB  
12506 C CG  . ASN D 556 ? 0.7955 0.7043 0.9278 0.0864  -0.0887 -0.0312 572 ASN A CG  
12507 O OD1 . ASN D 556 ? 0.8416 0.7259 0.9642 0.0961  -0.0997 -0.0357 572 ASN A OD1 
12508 N ND2 . ASN D 556 ? 0.7335 0.6612 0.8739 0.0798  -0.0842 -0.0226 572 ASN A ND2 
12509 N N   . VAL D 557 ? 0.7494 0.6682 0.8810 0.0815  -0.0709 -0.0518 573 VAL A N   
12510 C CA  . VAL D 557 ? 0.7556 0.6992 0.8960 0.0818  -0.0621 -0.0568 573 VAL A CA  
12511 C C   . VAL D 557 ? 0.7972 0.7274 0.9314 0.0915  -0.0671 -0.0679 573 VAL A C   
12512 O O   . VAL D 557 ? 0.8023 0.7553 0.9458 0.1044  -0.0663 -0.0762 573 VAL A O   
12513 C CB  . VAL D 557 ? 0.7819 0.7252 0.9202 0.0637  -0.0524 -0.0501 573 VAL A CB  
12514 C CG1 . VAL D 557 ? 0.7911 0.7648 0.9402 0.0652  -0.0433 -0.0543 573 VAL A CG1 
12515 C CG2 . VAL D 557 ? 0.7626 0.7104 0.9028 0.0528  -0.0488 -0.0387 573 VAL A CG2 
12516 N N   . VAL D 558 ? 0.8318 0.7244 0.9492 0.0849  -0.0722 -0.0684 574 VAL A N   
12517 C CA  . VAL D 558 ? 0.7841 0.6622 0.8937 0.0896  -0.0750 -0.0780 574 VAL A CA  
12518 C C   . VAL D 558 ? 0.8460 0.7017 0.9462 0.1053  -0.0879 -0.0857 574 VAL A C   
12519 O O   . VAL D 558 ? 0.9119 0.7606 1.0075 0.1134  -0.0909 -0.0952 574 VAL A O   
12520 C CB  . VAL D 558 ? 0.8038 0.6550 0.8996 0.0723  -0.0726 -0.0750 574 VAL A CB  
12521 C CG1 . VAL D 558 ? 0.7770 0.6479 0.8805 0.0569  -0.0608 -0.0666 574 VAL A CG1 
12522 C CG2 . VAL D 558 ? 0.8483 0.6585 0.9260 0.0671  -0.0822 -0.0714 574 VAL A CG2 
12523 N N   . GLY D 559 ? 0.9046 0.7483 1.0011 0.1103  -0.0959 -0.0823 575 GLY A N   
12524 C CA  . GLY D 559 ? 0.9245 0.7437 1.0100 0.1253  -0.1090 -0.0894 575 GLY A CA  
12525 C C   . GLY D 559 ? 0.9209 0.6918 0.9830 0.1173  -0.1167 -0.0894 575 GLY A C   
12526 O O   . GLY D 559 ? 0.9722 0.7202 1.0223 0.1287  -0.1263 -0.0977 575 GLY A O   
12527 N N   . ALA D 560 ? 0.9600 0.7142 1.0142 0.0978  -0.1128 -0.0803 576 ALA A N   
12528 C CA  . ALA D 560 ? 1.0027 0.7105 1.0335 0.0887  -0.1204 -0.0795 576 ALA A CA  
12529 C C   . ALA D 560 ? 1.0448 0.7410 1.0707 0.0703  -0.1173 -0.0677 576 ALA A C   
12530 O O   . ALA D 560 ? 1.0261 0.7489 1.0652 0.0608  -0.1068 -0.0612 576 ALA A O   
12531 C CB  . ALA D 560 ? 1.0457 0.7423 1.0681 0.0819  -0.1175 -0.0853 576 ALA A CB  
12532 N N   . LYS D 561 ? 1.1568 0.8120 1.1624 0.0653  -0.1269 -0.0651 577 LYS A N   
12533 C CA  . LYS D 561 ? 1.1374 0.7783 1.1367 0.0497  -0.1260 -0.0541 577 LYS A CA  
12534 C C   . LYS D 561 ? 1.1955 0.8208 1.1843 0.0279  -0.1200 -0.0499 577 LYS A C   
12535 O O   . LYS D 561 ? 1.1563 0.7696 1.1392 0.0140  -0.1189 -0.0409 577 LYS A O   
12536 C CB  . LYS D 561 ? 1.1687 0.7721 1.1503 0.0548  -0.1399 -0.0529 577 LYS A CB  
12537 C CG  . LYS D 561 ? 1.2094 0.8248 1.1993 0.0757  -0.1473 -0.0561 577 LYS A CG  
12538 C CD  . LYS D 561 ? 1.2616 0.8344 1.2303 0.0798  -0.1619 -0.0554 577 LYS A CD  
12539 C CE  . LYS D 561 ? 1.3116 0.8975 1.2888 0.1009  -0.1697 -0.0584 577 LYS A CE  
12540 N NZ  . LYS D 561 ? 1.4679 1.0092 1.4220 0.1080  -0.1853 -0.0604 577 LYS A NZ  
12541 N N   . ASN D 562 ? 1.2394 0.8642 1.2251 0.0241  -0.1163 -0.0562 578 ASN A N   
12542 C CA  . ASN D 562 ? 1.2167 0.8263 1.1913 0.0031  -0.1113 -0.0526 578 ASN A CA  
12543 C C   . ASN D 562 ? 1.1621 0.7986 1.1477 -0.0013 -0.1003 -0.0567 578 ASN A C   
12544 O O   . ASN D 562 ? 1.1042 0.7611 1.1005 0.0122  -0.0989 -0.0643 578 ASN A O   
12545 C CB  . ASN D 562 ? 1.2553 0.8173 1.2032 -0.0026 -0.1218 -0.0554 578 ASN A CB  
12546 C CG  . ASN D 562 ? 1.3297 0.8703 1.2637 -0.0259 -0.1193 -0.0477 578 ASN A CG  
12547 O OD1 . ASN D 562 ? 1.2891 0.8519 1.2335 -0.0383 -0.1086 -0.0418 578 ASN A OD1 
12548 N ND2 . ASN D 562 ? 1.4735 0.9703 1.3828 -0.0319 -0.1295 -0.0478 578 ASN A ND2 
12549 N N   . MET D 563 ? 1.1340 0.7702 1.1165 -0.0204 -0.0928 -0.0516 579 MET A N   
12550 C CA  . MET D 563 ? 1.0950 0.7537 1.0855 -0.0279 -0.0823 -0.0544 579 MET A CA  
12551 C C   . MET D 563 ? 1.1008 0.7503 1.0844 -0.0221 -0.0855 -0.0650 579 MET A C   
12552 O O   . MET D 563 ? 1.1668 0.7818 1.1323 -0.0201 -0.0958 -0.0690 579 MET A O   
12553 C CB  . MET D 563 ? 1.1122 0.7607 1.0938 -0.0499 -0.0772 -0.0480 579 MET A CB  
12554 C CG  . MET D 563 ? 1.0425 0.7175 1.0335 -0.0593 -0.0654 -0.0489 579 MET A CG  
12555 S SD  . MET D 563 ? 1.0078 0.6768 0.9914 -0.0834 -0.0592 -0.0400 579 MET A SD  
12556 C CE  . MET D 563 ? 1.0468 0.6659 1.0023 -0.0950 -0.0698 -0.0409 579 MET A CE  
12557 N N   . ASN D 564 ? 1.1035 0.7828 1.1006 -0.0196 -0.0770 -0.0696 580 ASN A N   
12558 C CA  . ASN D 564 ? 1.1368 0.8120 1.1299 -0.0121 -0.0795 -0.0801 580 ASN A CA  
12559 C C   . ASN D 564 ? 1.1229 0.8255 1.1264 -0.0188 -0.0683 -0.0826 580 ASN A C   
12560 O O   . ASN D 564 ? 1.0827 0.8180 1.1030 -0.0191 -0.0591 -0.0786 580 ASN A O   
12561 C CB  . ASN D 564 ? 1.1529 0.8395 1.1550 0.0106  -0.0846 -0.0864 580 ASN A CB  
12562 C CG  . ASN D 564 ? 1.2833 0.9516 1.2744 0.0195  -0.0916 -0.0971 580 ASN A CG  
12563 O OD1 . ASN D 564 ? 1.2933 0.9741 1.2879 0.0181  -0.0863 -0.1029 580 ASN A OD1 
12564 N ND2 . ASN D 564 ? 1.3815 1.0195 1.3586 0.0293  -0.1040 -0.0999 580 ASN A ND2 
12565 N N   . VAL D 565 ? 1.1375 0.8262 1.1300 -0.0241 -0.0694 -0.0894 581 VAL A N   
12566 C CA  . VAL D 565 ? 1.0718 0.7866 1.0737 -0.0293 -0.0594 -0.0928 581 VAL A CA  
12567 C C   . VAL D 565 ? 1.0213 0.7566 1.0344 -0.0124 -0.0585 -0.1016 581 VAL A C   
12568 O O   . VAL D 565 ? 1.0197 0.7877 1.0480 -0.0113 -0.0492 -0.1025 581 VAL A O   
12569 C CB  . VAL D 565 ? 1.0151 0.7098 1.0011 -0.0464 -0.0590 -0.0951 581 VAL A CB  
12570 C CG1 . VAL D 565 ? 0.9777 0.6683 0.9593 -0.0650 -0.0549 -0.0864 581 VAL A CG1 
12571 C CG2 . VAL D 565 ? 1.1078 0.7627 1.0726 -0.0444 -0.0708 -0.1007 581 VAL A CG2 
12572 N N   . ARG D 566 ? 1.1494 0.8664 1.1549 0.0012  -0.0681 -0.1083 582 ARG A N   
12573 C CA  . ARG D 566 ? 1.2160 0.9518 1.2307 0.0164  -0.0671 -0.1176 582 ARG A CA  
12574 C C   . ARG D 566 ? 1.1770 0.9579 1.2153 0.0238  -0.0572 -0.1167 582 ARG A C   
12575 O O   . ARG D 566 ? 1.1417 0.9418 1.1875 0.0292  -0.0527 -0.1234 582 ARG A O   
12576 C CB  . ARG D 566 ? 1.3545 1.0714 1.3620 0.0341  -0.0787 -0.1238 582 ARG A CB  
12577 C CG  . ARG D 566 ? 1.4268 1.1543 1.4380 0.0480  -0.0792 -0.1351 582 ARG A CG  
12578 C CD  . ARG D 566 ? 1.7088 1.4296 1.7191 0.0699  -0.0892 -0.1415 582 ARG A CD  
12579 N NE  . ARG D 566 ? 1.8268 1.5555 1.8452 0.0782  -0.0919 -0.1359 582 ARG A NE  
12580 C CZ  . ARG D 566 ? 1.6116 1.3781 1.6509 0.0841  -0.0849 -0.1325 582 ARG A CZ  
12581 N NH1 . ARG D 566 ? 1.5257 1.3272 1.5809 0.0842  -0.0745 -0.1342 582 ARG A NH1 
12582 N NH2 . ARG D 566 ? 1.6031 1.3717 1.6467 0.0899  -0.0885 -0.1272 582 ARG A NH2 
12583 N N   . PRO D 567 ? 1.0674 0.8653 1.1169 0.0241  -0.0537 -0.1087 583 PRO A N   
12584 C CA  . PRO D 567 ? 1.0436 0.8828 1.1129 0.0271  -0.0433 -0.1070 583 PRO A CA  
12585 C C   . PRO D 567 ? 1.0029 0.8561 1.0750 0.0132  -0.0335 -0.1055 583 PRO A C   
12586 O O   . PRO D 567 ? 0.9198 0.8004 1.0032 0.0178  -0.0267 -0.1094 583 PRO A O   
12587 C CB  . PRO D 567 ? 1.0029 0.8496 1.0790 0.0276  -0.0431 -0.0979 583 PRO A CB  
12588 C CG  . PRO D 567 ? 1.0629 0.8808 1.1278 0.0345  -0.0546 -0.0988 583 PRO A CG  
12589 C CD  . PRO D 567 ? 1.1250 0.9076 1.1704 0.0258  -0.0601 -0.1022 583 PRO A CD  
12590 N N   . LEU D 568 ? 0.9254 0.7614 0.9873 -0.0035 -0.0326 -0.0999 584 LEU A N   
12591 C CA  . LEU D 568 ? 0.8418 0.6889 0.9043 -0.0169 -0.0242 -0.0995 584 LEU A CA  
12592 C C   . LEU D 568 ? 0.8122 0.6594 0.8716 -0.0147 -0.0240 -0.1094 584 LEU A C   
12593 O O   . LEU D 568 ? 0.7664 0.6406 0.8365 -0.0125 -0.0165 -0.1126 584 LEU A O   
12594 C CB  . LEU D 568 ? 0.8282 0.6517 0.8772 -0.0346 -0.0254 -0.0935 584 LEU A CB  
12595 C CG  . LEU D 568 ? 0.7670 0.6014 0.8160 -0.0500 -0.0171 -0.0916 584 LEU A CG  
12596 C CD1 . LEU D 568 ? 0.6998 0.5663 0.7641 -0.0492 -0.0082 -0.0862 584 LEU A CD1 
12597 C CD2 . LEU D 568 ? 0.8022 0.6087 0.8357 -0.0660 -0.0206 -0.0866 584 LEU A CD2 
12598 N N   . LEU D 569 ? 0.8478 0.6635 0.8913 -0.0153 -0.0325 -0.1145 585 LEU A N   
12599 C CA  . LEU D 569 ? 0.8365 0.6483 0.8748 -0.0134 -0.0334 -0.1241 585 LEU A CA  
12600 C C   . LEU D 569 ? 0.8751 0.7118 0.9271 0.0043  -0.0316 -0.1307 585 LEU A C   
12601 O O   . LEU D 569 ? 0.9329 0.7821 0.9878 0.0056  -0.0278 -0.1374 585 LEU A O   
12602 C CB  . LEU D 569 ? 0.7867 0.5574 0.8042 -0.0148 -0.0445 -0.1279 585 LEU A CB  
12603 C CG  . LEU D 569 ? 0.8648 0.6108 0.8680 -0.0333 -0.0463 -0.1210 585 LEU A CG  
12604 C CD1 . LEU D 569 ? 0.9299 0.6326 0.9097 -0.0372 -0.0573 -0.1243 585 LEU A CD1 
12605 C CD2 . LEU D 569 ? 0.8578 0.6203 0.8640 -0.0492 -0.0369 -0.1194 585 LEU A CD2 
12606 N N   . ASN D 570 ? 0.8936 0.7388 0.9541 0.0177  -0.0342 -0.1289 586 ASN A N   
12607 C CA  . ASN D 570 ? 0.8925 0.7606 0.9651 0.0348  -0.0333 -0.1355 586 ASN A CA  
12608 C C   . ASN D 570 ? 0.7700 0.6768 0.8596 0.0339  -0.0220 -0.1333 586 ASN A C   
12609 O O   . ASN D 570 ? 0.6926 0.6197 0.7902 0.0424  -0.0186 -0.1399 586 ASN A O   
12610 C CB  . ASN D 570 ? 1.0147 0.8780 1.0894 0.0487  -0.0406 -0.1345 586 ASN A CB  
12611 C CG  . ASN D 570 ? 1.0629 0.9513 1.1505 0.0668  -0.0401 -0.1411 586 ASN A CG  
12612 O OD1 . ASN D 570 ? 1.0460 0.9484 1.1376 0.0708  -0.0364 -0.1482 586 ASN A OD1 
12613 N ND2 . ASN D 570 ? 1.0332 0.9297 1.1278 0.0779  -0.0434 -0.1389 586 ASN A ND2 
12614 N N   . TYR D 571 ? 0.7890 0.7047 0.8828 0.0235  -0.0165 -0.1241 587 TYR A N   
12615 C CA  . TYR D 571 ? 0.7817 0.7307 0.8888 0.0209  -0.0061 -0.1213 587 TYR A CA  
12616 C C   . TYR D 571 ? 0.7347 0.6894 0.8397 0.0143  -0.0011 -0.1268 587 TYR A C   
12617 O O   . TYR D 571 ? 0.6762 0.6565 0.7911 0.0201  0.0046  -0.1307 587 TYR A O   
12618 C CB  . TYR D 571 ? 0.7422 0.6940 0.8508 0.0099  -0.0022 -0.1103 587 TYR A CB  
12619 C CG  . TYR D 571 ? 0.6625 0.6460 0.7828 0.0067  0.0080  -0.1060 587 TYR A CG  
12620 C CD1 . TYR D 571 ? 0.5947 0.5852 0.7136 -0.0043 0.0145  -0.1058 587 TYR A CD1 
12621 C CD2 . TYR D 571 ? 0.6580 0.6650 0.7903 0.0156  0.0108  -0.1031 587 TYR A CD2 
12622 C CE1 . TYR D 571 ? 0.5824 0.6004 0.7106 -0.0058 0.0230  -0.1022 587 TYR A CE1 
12623 C CE2 . TYR D 571 ? 0.5946 0.6282 0.7356 0.0131  0.0194  -0.0994 587 TYR A CE2 
12624 C CZ  . TYR D 571 ? 0.5715 0.6098 0.7101 0.0029  0.0252  -0.0990 587 TYR A CZ  
12625 O OH  . TYR D 571 ? 0.5234 0.5870 0.6694 0.0019  0.0330  -0.0953 587 TYR A OH  
12626 N N   . PHE D 572 ? 0.7216 0.6516 0.8130 0.0025  -0.0040 -0.1277 588 PHE A N   
12627 C CA  . PHE D 572 ? 0.6643 0.5975 0.7520 -0.0073 0.0005  -0.1316 588 PHE A CA  
12628 C C   . PHE D 572 ? 0.7448 0.6657 0.8253 -0.0022 -0.0041 -0.1418 588 PHE A C   
12629 O O   . PHE D 572 ? 0.8129 0.7305 0.8873 -0.0115 -0.0021 -0.1457 588 PHE A O   
12630 C CB  . PHE D 572 ? 0.6576 0.5721 0.7342 -0.0249 0.0003  -0.1263 588 PHE A CB  
12631 C CG  . PHE D 572 ? 0.6867 0.6180 0.7703 -0.0324 0.0071  -0.1176 588 PHE A CG  
12632 C CD1 . PHE D 572 ? 0.6488 0.6076 0.7413 -0.0350 0.0159  -0.1179 588 PHE A CD1 
12633 C CD2 . PHE D 572 ? 0.6850 0.6053 0.7667 -0.0352 0.0044  -0.1092 588 PHE A CD2 
12634 C CE1 . PHE D 572 ? 0.6239 0.5970 0.7217 -0.0409 0.0217  -0.1100 588 PHE A CE1 
12635 C CE2 . PHE D 572 ? 0.6050 0.5401 0.6926 -0.0415 0.0105  -0.1012 588 PHE A CE2 
12636 C CZ  . PHE D 572 ? 0.6014 0.5625 0.6967 -0.0443 0.0190  -0.1016 588 PHE A CZ  
12637 N N   . GLU D 573 ? 0.7829 0.6957 0.8629 0.0121  -0.0108 -0.1465 589 GLU A N   
12638 C CA  . GLU D 573 ? 0.8354 0.7318 0.9056 0.0160  -0.0161 -0.1561 589 GLU A CA  
12639 C C   . GLU D 573 ? 0.8393 0.7591 0.9168 0.0180  -0.0095 -0.1628 589 GLU A C   
12640 O O   . GLU D 573 ? 0.9133 0.8200 0.9806 0.0107  -0.0107 -0.1682 589 GLU A O   
12641 C CB  . GLU D 573 ? 0.8777 0.7605 0.9450 0.0322  -0.0250 -0.1605 589 GLU A CB  
12642 C CG  . GLU D 573 ? 0.9835 0.8592 1.0448 0.0389  -0.0283 -0.1711 589 GLU A CG  
12643 C CD  . GLU D 573 ? 1.2723 1.1149 1.3191 0.0467  -0.0399 -0.1752 589 GLU A CD  
12644 O OE1 . GLU D 573 ? 1.4154 1.2474 1.4608 0.0502  -0.0448 -0.1700 589 GLU A OE1 
12645 O OE2 . GLU D 573 ? 1.4496 1.2749 1.4850 0.0481  -0.0445 -0.1833 589 GLU A OE2 
12646 N N   . PRO D 574 ? 0.7957 0.7490 0.8894 0.0266  -0.0026 -0.1629 590 PRO A N   
12647 C CA  . PRO D 574 ? 0.8047 0.7796 0.9041 0.0260  0.0042  -0.1685 590 PRO A CA  
12648 C C   . PRO D 574 ? 0.7877 0.7587 0.8806 0.0090  0.0081  -0.1673 590 PRO A C   
12649 O O   . PRO D 574 ? 0.8033 0.7699 0.8901 0.0054  0.0080  -0.1742 590 PRO A O   
12650 C CB  . PRO D 574 ? 0.7383 0.7477 0.8544 0.0327  0.0117  -0.1646 590 PRO A CB  
12651 C CG  . PRO D 574 ? 0.7354 0.7419 0.8549 0.0416  0.0075  -0.1609 590 PRO A CG  
12652 C CD  . PRO D 574 ? 0.7348 0.7085 0.8414 0.0343  0.0002  -0.1570 590 PRO A CD  
12653 N N   . LEU D 575 ? 0.7395 0.7120 0.8329 -0.0018 0.0113  -0.1586 591 LEU A N   
12654 C CA  . LEU D 575 ? 0.7248 0.6940 0.8117 -0.0183 0.0147  -0.1573 591 LEU A CA  
12655 C C   . LEU D 575 ? 0.7729 0.7091 0.8425 -0.0272 0.0075  -0.1610 591 LEU A C   
12656 O O   . LEU D 575 ? 0.7971 0.7319 0.8606 -0.0371 0.0094  -0.1652 591 LEU A O   
12657 C CB  . LEU D 575 ? 0.6432 0.6173 0.7327 -0.0274 0.0184  -0.1473 591 LEU A CB  
12658 C CG  . LEU D 575 ? 0.6649 0.6385 0.7481 -0.0439 0.0222  -0.1467 591 LEU A CG  
12659 C CD1 . LEU D 575 ? 0.7016 0.7031 0.7931 -0.0430 0.0296  -0.1513 591 LEU A CD1 
12660 C CD2 . LEU D 575 ? 0.6940 0.6668 0.7772 -0.0528 0.0242  -0.1374 591 LEU A CD2 
12661 N N   . PHE D 576 ? 0.8004 0.7093 0.8608 -0.0239 -0.0009 -0.1597 592 PHE A N   
12662 C CA  . PHE D 576 ? 0.8384 0.7128 0.8798 -0.0329 -0.0084 -0.1628 592 PHE A CA  
12663 C C   . PHE D 576 ? 0.8552 0.7265 0.8915 -0.0296 -0.0101 -0.1731 592 PHE A C   
12664 O O   . PHE D 576 ? 0.8740 0.7346 0.8994 -0.0428 -0.0102 -0.1762 592 PHE A O   
12665 C CB  . PHE D 576 ? 0.8763 0.7208 0.9078 -0.0266 -0.0184 -0.1611 592 PHE A CB  
12666 C CG  . PHE D 576 ? 0.7852 0.5914 0.7947 -0.0392 -0.0260 -0.1621 592 PHE A CG  
12667 C CD1 . PHE D 576 ? 0.7861 0.5887 0.7880 -0.0583 -0.0226 -0.1602 592 PHE A CD1 
12668 C CD2 . PHE D 576 ? 0.8129 0.5884 0.8087 -0.0315 -0.0364 -0.1665 592 PHE A CD2 
12669 C CE1 . PHE D 576 ? 0.8099 0.5776 0.7905 -0.0714 -0.0294 -0.1611 592 PHE A CE1 
12670 C CE2 . PHE D 576 ? 0.8129 0.5512 0.7861 -0.0439 -0.0437 -0.1676 592 PHE A CE2 
12671 C CZ  . PHE D 576 ? 0.7530 0.4874 0.7185 -0.0646 -0.0401 -0.1647 592 PHE A CZ  
12672 N N   . THR D 577 ? 0.8726 0.7516 0.9154 -0.0123 -0.0120 -0.1787 593 THR A N   
12673 C CA  . THR D 577 ? 0.8857 0.7585 0.9222 -0.0082 -0.0146 -0.1888 593 THR A CA  
12674 C C   . THR D 577 ? 0.8763 0.7741 0.9196 -0.0155 -0.0060 -0.1919 593 THR A C   
12675 O O   . THR D 577 ? 0.9006 0.7873 0.9333 -0.0235 -0.0075 -0.1978 593 THR A O   
12676 C CB  . THR D 577 ? 0.8606 0.7389 0.9036 0.0127  -0.0182 -0.1944 593 THR A CB  
12677 O OG1 . THR D 577 ? 0.8178 0.7339 0.8805 0.0213  -0.0100 -0.1932 593 THR A OG1 
12678 C CG2 . THR D 577 ? 0.8505 0.7054 0.8872 0.0211  -0.0272 -0.1915 593 THR A CG2 
12679 N N   . TRP D 578 ? 0.8766 0.8074 0.9363 -0.0139 0.0027  -0.1876 594 TRP A N   
12680 C CA  . TRP D 578 ? 0.8449 0.8001 0.9109 -0.0201 0.0107  -0.1905 594 TRP A CA  
12681 C C   . TRP D 578 ? 0.8445 0.7890 0.8998 -0.0396 0.0117  -0.1889 594 TRP A C   
12682 O O   . TRP D 578 ? 0.8762 0.8221 0.9265 -0.0463 0.0129  -0.1950 594 TRP A O   
12683 C CB  . TRP D 578 ? 0.8154 0.8045 0.8986 -0.0148 0.0191  -0.1855 594 TRP A CB  
12684 C CG  . TRP D 578 ? 0.7873 0.8033 0.8776 -0.0189 0.0272  -0.1880 594 TRP A CG  
12685 C CD1 . TRP D 578 ? 0.7998 0.8357 0.8976 -0.0097 0.0305  -0.1947 594 TRP A CD1 
12686 C CD2 . TRP D 578 ? 0.7811 0.8080 0.8719 -0.0323 0.0328  -0.1841 594 TRP A CD2 
12687 N NE1 . TRP D 578 ? 0.7854 0.8429 0.8878 -0.0165 0.0376  -0.1950 594 TRP A NE1 
12688 C CE2 . TRP D 578 ? 0.7370 0.7900 0.8354 -0.0300 0.0391  -0.1888 594 TRP A CE2 
12689 C CE3 . TRP D 578 ? 0.8060 0.8235 0.8912 -0.0458 0.0330  -0.1774 594 TRP A CE3 
12690 C CZ2 . TRP D 578 ? 0.7308 0.8004 0.8313 -0.0399 0.0451  -0.1872 594 TRP A CZ2 
12691 C CZ3 . TRP D 578 ? 0.7760 0.8113 0.8638 -0.0559 0.0394  -0.1759 594 TRP A CZ3 
12692 C CH2 . TRP D 578 ? 0.7443 0.8052 0.8396 -0.0526 0.0452  -0.1809 594 TRP A CH2 
12693 N N   . LEU D 579 ? 0.8148 0.7492 0.8663 -0.0493 0.0111  -0.1808 595 LEU A N   
12694 C CA  . LEU D 579 ? 0.8391 0.7617 0.8791 -0.0686 0.0114  -0.1792 595 LEU A CA  
12695 C C   . LEU D 579 ? 0.9007 0.7940 0.9229 -0.0753 0.0042  -0.1858 595 LEU A C   
12696 O O   . LEU D 579 ? 1.0397 0.9341 1.0553 -0.0881 0.0062  -0.1897 595 LEU A O   
12697 C CB  . LEU D 579 ? 0.7977 0.7067 0.8334 -0.0769 0.0097  -0.1699 595 LEU A CB  
12698 C CG  . LEU D 579 ? 0.7980 0.7328 0.8474 -0.0766 0.0170  -0.1625 595 LEU A CG  
12699 C CD1 . LEU D 579 ? 0.7989 0.7150 0.8419 -0.0839 0.0138  -0.1540 595 LEU A CD1 
12700 C CD2 . LEU D 579 ? 0.7972 0.7543 0.8501 -0.0868 0.0244  -0.1643 595 LEU A CD2 
12701 N N   . LYS D 580 ? 0.9047 0.7695 0.9172 -0.0681 -0.0046 -0.1866 596 LYS A N   
12702 C CA  . LYS D 580 ? 0.9316 0.7645 0.9244 -0.0743 -0.0123 -0.1926 596 LYS A CA  
12703 C C   . LYS D 580 ? 1.0720 0.9184 1.0665 -0.0730 -0.0095 -0.2017 596 LYS A C   
12704 O O   . LYS D 580 ? 1.1256 0.9614 1.1077 -0.0871 -0.0103 -0.2056 596 LYS A O   
12705 C CB  . LYS D 580 ? 0.9451 0.7507 0.9299 -0.0610 -0.0220 -0.1939 596 LYS A CB  
12706 C CG  . LYS D 580 ? 0.9162 0.6868 0.8841 -0.0700 -0.0295 -0.1887 596 LYS A CG  
12707 C CD  . LYS D 580 ? 0.8909 0.6551 0.8637 -0.0538 -0.0344 -0.1851 596 LYS A CD  
12708 C CE  . LYS D 580 ? 0.8912 0.6491 0.8635 -0.0347 -0.0403 -0.1931 596 LYS A CE  
12709 N NZ  . LYS D 580 ? 0.9215 0.6798 0.9014 -0.0186 -0.0439 -0.1897 596 LYS A NZ  
12710 N N   . ASP D 581 ? 1.1460 1.0178 1.1562 -0.0569 -0.0056 -0.2050 597 ASP A N   
12711 C CA  . ASP D 581 ? 1.2028 1.0901 1.2160 -0.0545 -0.0024 -0.2135 597 ASP A CA  
12712 C C   . ASP D 581 ? 1.2710 1.1787 1.2872 -0.0698 0.0052  -0.2133 597 ASP A C   
12713 O O   . ASP D 581 ? 1.3703 1.2731 1.3775 -0.0790 0.0047  -0.2194 597 ASP A O   
12714 C CB  . ASP D 581 ? 1.2237 1.1375 1.2543 -0.0353 0.0014  -0.2158 597 ASP A CB  
12715 C CG  . ASP D 581 ? 1.4129 1.3436 1.4472 -0.0325 0.0049  -0.2242 597 ASP A CG  
12716 O OD1 . ASP D 581 ? 1.3566 1.3153 1.4008 -0.0378 0.0131  -0.2235 597 ASP A OD1 
12717 O OD2 . ASP D 581 ? 1.5818 1.4970 1.6082 -0.0248 -0.0008 -0.2316 597 ASP A OD2 
12718 N N   . GLN D 582 ? 1.0500 0.9816 1.0788 -0.0723 0.0123  -0.2065 598 GLN A N   
12719 C CA  . GLN D 582 ? 0.9503 0.9055 0.9837 -0.0842 0.0198  -0.2067 598 GLN A CA  
12720 C C   . GLN D 582 ? 1.0406 0.9764 1.0577 -0.1044 0.0171  -0.2074 598 GLN A C   
12721 O O   . GLN D 582 ? 1.1199 1.0680 1.1353 -0.1142 0.0206  -0.2122 598 GLN A O   
12722 C CB  . GLN D 582 ? 0.8584 0.8370 0.9051 -0.0838 0.0264  -0.1985 598 GLN A CB  
12723 C CG  . GLN D 582 ? 0.8971 0.9042 0.9612 -0.0672 0.0317  -0.1980 598 GLN A CG  
12724 C CD  . GLN D 582 ? 0.9016 0.9346 0.9730 -0.0639 0.0372  -0.2049 598 GLN A CD  
12725 O OE1 . GLN D 582 ? 0.9011 0.9489 0.9730 -0.0743 0.0418  -0.2061 598 GLN A OE1 
12726 N NE2 . GLN D 582 ? 0.9133 0.9518 0.9900 -0.0493 0.0363  -0.2101 598 GLN A NE2 
12727 N N   . ASN D 583 ? 1.0316 0.9372 1.0358 -0.1111 0.0108  -0.2027 599 ASN A N   
12728 C CA  . ASN D 583 ? 1.0726 0.9592 1.0602 -0.1320 0.0084  -0.2023 599 ASN A CA  
12729 C C   . ASN D 583 ? 1.0901 0.9510 1.0598 -0.1379 0.0018  -0.2102 599 ASN A C   
12730 O O   . ASN D 583 ? 1.1023 0.9415 1.0549 -0.1555 -0.0017 -0.2099 599 ASN A O   
12731 C CB  . ASN D 583 ? 1.0204 0.8826 0.9992 -0.1384 0.0039  -0.1939 599 ASN A CB  
12732 C CG  . ASN D 583 ? 0.9457 0.8306 0.9385 -0.1381 0.0105  -0.1855 599 ASN A CG  
12733 O OD1 . ASN D 583 ? 0.9341 0.8518 0.9406 -0.1377 0.0186  -0.1856 599 ASN A OD1 
12734 N ND2 . ASN D 583 ? 0.9291 0.7943 0.9165 -0.1399 0.0065  -0.1782 599 ASN A ND2 
12735 N N   . LYS D 584 ? 1.1380 1.0008 1.1105 -0.1241 0.0001  -0.2173 600 LYS A N   
12736 C CA  . LYS D 584 ? 1.0815 0.9192 1.0365 -0.1285 -0.0064 -0.2251 600 LYS A CA  
12737 C C   . LYS D 584 ? 1.1944 1.0366 1.1405 -0.1491 -0.0037 -0.2287 600 LYS A C   
12738 O O   . LYS D 584 ? 1.1656 0.9785 1.0912 -0.1605 -0.0102 -0.2324 600 LYS A O   
12739 C CB  . LYS D 584 ? 1.1377 0.9852 1.1009 -0.1096 -0.0067 -0.2322 600 LYS A CB  
12740 C CG  . LYS D 584 ? 1.1492 1.0389 1.1318 -0.1039 0.0028  -0.2353 600 LYS A CG  
12741 C CD  . LYS D 584 ? 1.2655 1.1629 1.2573 -0.0824 0.0019  -0.2405 600 LYS A CD  
12742 C CE  . LYS D 584 ? 1.2849 1.2233 1.2963 -0.0739 0.0109  -0.2428 600 LYS A CE  
12743 N NZ  . LYS D 584 ? 1.2550 1.2193 1.2811 -0.0750 0.0182  -0.2348 600 LYS A NZ  
12744 N N   . ASN D 585 ? 1.1762 1.0540 1.1363 -0.1545 0.0054  -0.2277 601 ASN A N   
12745 C CA  . ASN D 585 ? 1.1628 1.0498 1.1163 -0.1739 0.0085  -0.2314 601 ASN A CA  
12746 C C   . ASN D 585 ? 1.1333 1.0270 1.0863 -0.1898 0.0121  -0.2246 601 ASN A C   
12747 O O   . ASN D 585 ? 1.1782 1.0957 1.1348 -0.2019 0.0180  -0.2265 601 ASN A O   
12748 C CB  . ASN D 585 ? 1.2505 1.1744 1.2189 -0.1685 0.0159  -0.2375 601 ASN A CB  
12749 C CG  . ASN D 585 ? 1.2492 1.1674 1.2166 -0.1551 0.0126  -0.2453 601 ASN A CG  
12750 O OD1 . ASN D 585 ? 1.2437 1.1286 1.1941 -0.1563 0.0045  -0.2486 601 ASN A OD1 
12751 N ND2 . ASN D 585 ? 1.2776 1.2278 1.2623 -0.1425 0.0187  -0.2484 601 ASN A ND2 
12752 N N   . SER D 586 ? 1.1074 0.9815 1.0564 -0.1893 0.0086  -0.2169 602 SER A N   
12753 C CA  . SER D 586 ? 1.0212 0.9005 0.9699 -0.2031 0.0118  -0.2098 602 SER A CA  
12754 C C   . SER D 586 ? 0.9686 0.8062 0.8953 -0.2154 0.0035  -0.2063 602 SER A C   
12755 O O   . SER D 586 ? 0.9874 0.7938 0.9038 -0.2069 -0.0046 -0.2067 602 SER A O   
12756 C CB  . SER D 586 ? 1.0032 0.9029 0.9705 -0.1900 0.0167  -0.2024 602 SER A CB  
12757 O OG  . SER D 586 ? 0.9850 0.9211 0.9713 -0.1780 0.0239  -0.2052 602 SER A OG  
12758 N N   . PHE D 587 ? 0.9185 0.7551 0.8372 -0.2351 0.0052  -0.2029 603 PHE A N   
12759 C CA  . PHE D 587 ? 0.9097 0.7094 0.8097 -0.2458 -0.0019 -0.1974 603 PHE A CA  
12760 C C   . PHE D 587 ? 0.9691 0.7694 0.8796 -0.2347 -0.0013 -0.1885 603 PHE A C   
12761 O O   . PHE D 587 ? 1.0173 0.8493 0.9454 -0.2311 0.0064  -0.1848 603 PHE A O   
12762 C CB  . PHE D 587 ? 0.9076 0.7047 0.7937 -0.2720 -0.0005 -0.1971 603 PHE A CB  
12763 C CG  . PHE D 587 ? 0.9738 0.7308 0.8384 -0.2846 -0.0081 -0.1916 603 PHE A CG  
12764 C CD1 . PHE D 587 ? 0.9582 0.6744 0.8010 -0.2859 -0.0182 -0.1932 603 PHE A CD1 
12765 C CD2 . PHE D 587 ? 1.0007 0.7641 0.8675 -0.2923 -0.0053 -0.1824 603 PHE A CD2 
12766 C CE1 . PHE D 587 ? 0.9175 0.6027 0.7442 -0.2903 -0.0256 -0.1839 603 PHE A CE1 
12767 C CE2 . PHE D 587 ? 0.9485 0.6816 0.7993 -0.2971 -0.0124 -0.1733 603 PHE A CE2 
12768 C CZ  . PHE D 587 ? 0.9196 0.6142 0.7508 -0.2962 -0.0224 -0.1741 603 PHE A CZ  
12769 N N   . VAL D 588 ? 0.9799 0.7448 0.8788 -0.2287 -0.0099 -0.1853 604 VAL A N   
12770 C CA  . VAL D 588 ? 0.9455 0.7066 0.8521 -0.2182 -0.0108 -0.1770 604 VAL A CA  
12771 C C   . VAL D 588 ? 0.9712 0.7011 0.8587 -0.2348 -0.0160 -0.1711 604 VAL A C   
12772 O O   . VAL D 588 ? 0.9475 0.6384 0.8135 -0.2394 -0.0253 -0.1725 604 VAL A O   
12773 C CB  . VAL D 588 ? 0.9671 0.7141 0.8768 -0.1961 -0.0167 -0.1782 604 VAL A CB  
12774 C CG1 . VAL D 588 ? 1.0281 0.7669 0.9424 -0.1879 -0.0188 -0.1695 604 VAL A CG1 
12775 C CG2 . VAL D 588 ? 0.9744 0.7547 0.9040 -0.1801 -0.0107 -0.1834 604 VAL A CG2 
12776 N N   . GLY D 589 ? 0.9803 0.7260 0.8745 -0.2433 -0.0105 -0.1645 605 GLY A N   
12777 C CA  . GLY D 589 ? 0.9917 0.7119 0.8683 -0.2612 -0.0143 -0.1589 605 GLY A CA  
12778 C C   . GLY D 589 ? 0.9581 0.7048 0.8387 -0.2790 -0.0061 -0.1577 605 GLY A C   
12779 O O   . GLY D 589 ? 0.9591 0.7442 0.8574 -0.2750 0.0023  -0.1605 605 GLY A O   
12780 N N   . TRP D 590 ? 0.9884 0.7230 0.8570 -0.2893 -0.0089 -0.1492 606 TRP A N   
12781 C CA  . TRP D 590 ? 1.0053 0.7688 0.8782 -0.3004 -0.0018 -0.1452 606 TRP A CA  
12782 C C   . TRP D 590 ? 1.0474 0.7919 0.9020 -0.3115 -0.0064 -0.1385 606 TRP A C   
12783 O O   . TRP D 590 ? 1.0834 0.7993 0.9279 -0.3096 -0.0131 -0.1321 606 TRP A O   
12784 C CB  . TRP D 590 ? 1.0033 0.7901 0.8922 -0.2971 0.0049  -0.1395 606 TRP A CB  
12785 C CG  . TRP D 590 ? 1.0111 0.7744 0.8971 -0.2913 -0.0001 -0.1313 606 TRP A CG  
12786 C CD1 . TRP D 590 ? 1.0157 0.7651 0.8919 -0.2965 -0.0032 -0.1217 606 TRP A CD1 
12787 C CD2 . TRP D 590 ? 0.9781 0.7304 0.8712 -0.2789 -0.0021 -0.1323 606 TRP A CD2 
12788 N NE1 . TRP D 590 ? 1.0311 0.7621 0.9086 -0.2878 -0.0073 -0.1163 606 TRP A NE1 
12789 C CE2 . TRP D 590 ? 0.9796 0.7115 0.8669 -0.2771 -0.0068 -0.1225 606 TRP A CE2 
12790 C CE3 . TRP D 590 ? 0.9656 0.7309 0.8732 -0.2614 -0.0004 -0.1373 606 TRP A CE3 
12791 C CZ2 . TRP D 590 ? 0.9696 0.6872 0.8612 -0.2661 -0.0097 -0.1208 606 TRP A CZ2 
12792 C CZ3 . TRP D 590 ? 0.9240 0.6821 0.8393 -0.2438 -0.0034 -0.1325 606 TRP A CZ3 
12793 C CH2 . TRP D 590 ? 0.9593 0.6940 0.8669 -0.2462 -0.0080 -0.1246 606 TRP A CH2 
12794 N N   . SER D 591 ? 1.0543 0.8160 0.9049 -0.3230 -0.0025 -0.1401 607 SER A N   
12795 C CA  . SER D 591 ? 1.1527 0.9033 0.9879 -0.3345 -0.0045 -0.1332 607 SER A CA  
12796 C C   . SER D 591 ? 1.1707 0.9435 1.0145 -0.3368 0.0018  -0.1261 607 SER A C   
12797 O O   . SER D 591 ? 1.1585 0.9637 1.0192 -0.3336 0.0096  -0.1280 607 SER A O   
12798 C CB  . SER D 591 ? 1.2010 0.9588 1.0259 -0.3468 -0.0032 -0.1377 607 SER A CB  
12799 O OG  . SER D 591 ? 1.2317 1.0285 1.0667 -0.3531 0.0063  -0.1390 607 SER A OG  
12800 N N   . THR D 592 ? 1.1716 0.9266 1.0033 -0.3419 -0.0016 -0.1182 608 THR A N   
12801 C CA  . THR D 592 ? 1.2515 1.0200 1.0901 -0.3414 0.0025  -0.1108 608 THR A CA  
12802 C C   . THR D 592 ? 1.3082 1.1055 1.1465 -0.3522 0.0100  -0.1101 608 THR A C   
12803 O O   . THR D 592 ? 1.3164 1.1236 1.1577 -0.3526 0.0132  -0.1041 608 THR A O   
12804 C CB  . THR D 592 ? 1.2340 0.9705 1.0600 -0.3407 -0.0046 -0.1029 608 THR A CB  
12805 O OG1 . THR D 592 ? 1.2801 0.9999 1.0860 -0.3525 -0.0082 -0.1021 608 THR A OG1 
12806 C CG2 . THR D 592 ? 1.2109 0.9191 1.0368 -0.3290 -0.0122 -0.1038 608 THR A CG2 
12807 N N   . ASP D 593 ? 1.4944 1.3057 1.3288 -0.3607 0.0130  -0.1164 609 ASP A N   
12808 C CA  . ASP D 593 ? 1.5244 1.3602 1.3549 -0.3723 0.0193  -0.1162 609 ASP A CA  
12809 C C   . ASP D 593 ? 1.4470 1.3226 1.2913 -0.3726 0.0279  -0.1236 609 ASP A C   
12810 O O   . ASP D 593 ? 1.4830 1.3840 1.3281 -0.3789 0.0342  -0.1231 609 ASP A O   
12811 C CB  . ASP D 593 ? 1.5921 1.4082 1.4006 -0.3856 0.0152  -0.1160 609 ASP A CB  
12812 C CG  . ASP D 593 ? 1.7505 1.5551 1.5540 -0.3864 0.0115  -0.1229 609 ASP A CG  
12813 O OD1 . ASP D 593 ? 1.7602 1.5484 1.5690 -0.3756 0.0067  -0.1250 609 ASP A OD1 
12814 O OD2 . ASP D 593 ? 1.9318 1.7449 1.7263 -0.3976 0.0135  -0.1267 609 ASP A OD2 
12815 N N   . TRP D 594 ? 1.2420 1.1246 1.0966 -0.3657 0.0283  -0.1306 610 TRP A N   
12816 C CA  . TRP D 594 ? 1.1575 1.0801 1.0276 -0.3636 0.0367  -0.1372 610 TRP A CA  
12817 C C   . TRP D 594 ? 1.2158 1.1605 1.0994 -0.3571 0.0423  -0.1334 610 TRP A C   
12818 O O   . TRP D 594 ? 1.2888 1.2213 1.1789 -0.3479 0.0399  -0.1289 610 TRP A O   
12819 C CB  . TRP D 594 ? 1.1328 1.0594 1.0141 -0.3546 0.0363  -0.1450 610 TRP A CB  
12820 C CG  . TRP D 594 ? 1.1181 1.0876 1.0163 -0.3513 0.0450  -0.1518 610 TRP A CG  
12821 C CD1 . TRP D 594 ? 1.1244 1.1176 1.0225 -0.3577 0.0493  -0.1588 610 TRP A CD1 
12822 C CD2 . TRP D 594 ? 1.0860 1.0796 1.0028 -0.3405 0.0503  -0.1522 610 TRP A CD2 
12823 N NE1 . TRP D 594 ? 1.1252 1.1557 1.0408 -0.3508 0.0566  -0.1637 610 TRP A NE1 
12824 C CE2 . TRP D 594 ? 1.1105 1.1415 1.0377 -0.3402 0.0573  -0.1597 610 TRP A CE2 
12825 C CE3 . TRP D 594 ? 1.0952 1.0824 1.0207 -0.3310 0.0498  -0.1469 610 TRP A CE3 
12826 C CZ2 . TRP D 594 ? 1.1113 1.1724 1.0567 -0.3302 0.0633  -0.1622 610 TRP A CZ2 
12827 C CZ3 . TRP D 594 ? 1.0918 1.1087 1.0352 -0.3221 0.0560  -0.1490 610 TRP A CZ3 
12828 C CH2 . TRP D 594 ? 1.0284 1.0816 0.9814 -0.3215 0.0626  -0.1566 610 TRP A CH2 
12829 N N   . SER D 595 ? 1.1525 1.1298 1.0400 -0.3616 0.0495  -0.1354 611 SER A N   
12830 C CA  . SER D 595 ? 1.1960 1.1936 1.0957 -0.3545 0.0544  -0.1322 611 SER A CA  
12831 C C   . SER D 595 ? 1.2022 1.2414 1.1124 -0.3541 0.0625  -0.1394 611 SER A C   
12832 O O   . SER D 595 ? 1.2287 1.2798 1.1319 -0.3633 0.0646  -0.1443 611 SER A O   
12833 C CB  . SER D 595 ? 1.2157 1.2017 1.1045 -0.3600 0.0531  -0.1237 611 SER A CB  
12834 O OG  . SER D 595 ? 1.2554 1.2634 1.1380 -0.3695 0.0581  -0.1253 611 SER A OG  
12835 N N   . PRO D 596 ? 1.2906 1.3524 1.2171 -0.3434 0.0670  -0.1404 612 PRO A N   
12836 C CA  . PRO D 596 ? 1.3526 1.4542 1.2896 -0.3410 0.0741  -0.1483 612 PRO A CA  
12837 C C   . PRO D 596 ? 1.4237 1.5451 1.3521 -0.3507 0.0782  -0.1495 612 PRO A C   
12838 O O   . PRO D 596 ? 1.4612 1.6111 1.3932 -0.3523 0.0827  -0.1574 612 PRO A O   
12839 C CB  . PRO D 596 ? 1.2048 1.3211 1.1582 -0.3275 0.0770  -0.1469 612 PRO A CB  
12840 C CG  . PRO D 596 ? 1.1623 1.2469 1.1165 -0.3222 0.0714  -0.1411 612 PRO A CG  
12841 C CD  . PRO D 596 ? 1.1489 1.2014 1.0851 -0.3323 0.0657  -0.1348 612 PRO A CD  
12842 N N   . TYR D 597 ? 1.2490 1.3569 1.1659 -0.3571 0.0767  -0.1425 613 TYR A N   
12843 C CA  . TYR D 597 ? 1.2558 1.3835 1.1646 -0.3660 0.0808  -0.1439 613 TYR A CA  
12844 C C   . TYR D 597 ? 1.4470 1.5616 1.3377 -0.3813 0.0787  -0.1443 613 TYR A C   
12845 O O   . TYR D 597 ? 1.6199 1.7533 1.5031 -0.3901 0.0825  -0.1471 613 TYR A O   
12846 C CB  . TYR D 597 ? 1.1710 1.2950 1.0774 -0.3642 0.0809  -0.1366 613 TYR A CB  
12847 C CG  . TYR D 597 ? 1.1884 1.2737 1.0853 -0.3662 0.0744  -0.1273 613 TYR A CG  
12848 C CD1 . TYR D 597 ? 1.2575 1.3247 1.1365 -0.3788 0.0715  -0.1239 613 TYR A CD1 
12849 C CD2 . TYR D 597 ? 1.1469 1.2144 1.0524 -0.3554 0.0710  -0.1219 613 TYR A CD2 
12850 C CE1 . TYR D 597 ? 1.2281 1.2600 1.0978 -0.3800 0.0651  -0.1156 613 TYR A CE1 
12851 C CE2 . TYR D 597 ? 1.0913 1.1236 0.9877 -0.3567 0.0646  -0.1136 613 TYR A CE2 
12852 C CZ  . TYR D 597 ? 1.0979 1.1128 0.9765 -0.3686 0.0615  -0.1106 613 TYR A CZ  
12853 O OH  . TYR D 597 ? 1.1480 1.1290 1.0171 -0.3694 0.0549  -0.1030 613 TYR A OH  
12854 N N   . ALA D 598 ? 1.3341 1.4169 1.2168 -0.3846 0.0726  -0.1418 614 ALA A N   
12855 C CA  . ALA D 598 ? 1.2962 1.3642 1.1607 -0.3991 0.0700  -0.1420 614 ALA A CA  
12856 C C   . ALA D 598 ? 1.2481 1.3305 1.1144 -0.4023 0.0719  -0.1507 614 ALA A C   
12857 O O   . ALA D 598 ? 1.2776 1.3439 1.1469 -0.3979 0.0679  -0.1525 614 ALA A O   
12858 C CB  . ALA D 598 ? 1.2659 1.2909 1.1191 -0.4007 0.0618  -0.1352 614 ALA A CB  
# 
